data_8Z7M
# 
_entry.id   8Z7M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8Z7M         pdb_00008z7m 10.2210/pdb8z7m/pdb 
WWPDB D_1300047174 ?            ?                   
# 
_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       2025-02-26 
_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                        8Z7M 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              zefangwang@tju.edu.cn 
_pdbx_contact_author.name_first         Zefang 
_pdbx_contact_author.name_last          Wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0852-6483 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xiao, Y.J.' 1 ? 
'Wang, Z.F.' 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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biochem.Biophys.Res.Commun. 
_citation.journal_id_ASTM           BBRCA9 
_citation.journal_id_CSD            0146 
_citation.journal_id_ISSN           1090-2104 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            720 
_citation.language                  ? 
_citation.page_first                150102 
_citation.page_last                 150102 
_citation.title                     'Structural insight into the subclass B1 metallo-beta-lactamase AFM-1.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bbrc.2024.150102 
_citation.pdbx_database_id_PubMed   38759302 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Niu, W.'  1 ? 
primary 'Ti, R.'   2 ? 
primary 'Li, D.'   3 ? 
primary 'Dong, R.' 4 ? 
primary 'Dong, J.' 5 ? 
primary 'Ye, Y.'   6 ? 
primary 'Xiao, Y.' 7 ? 
primary 'Wang, Z.' 8 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Metallo-beta-lactamase type 2' 25554.617 2   3.5.2.6 ? ? ? 
2 non-polymer syn 'ZINC ION'                      65.409    4   ?       ? ? ? 
3 water       nat water                           18.015    129 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'AFM-1,B2 metallo-beta-lactamase,Metallo-beta-lactamase type II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPLGSDQRFGDLVFRQLAPNVWQHTSFMDVPGFGAVSSNGLIVKDGERVLLVDTAWTDDQTSQILNWIKQEINLPVALAV
VTHAHQDKMGGMGALHAEAIPTYANALSNQLAPQEGMTAAQHSLTFAANGWVDPATAPNFGPLRVFYPGPGHTSDNITVG
IDGTDIAFGGCLIKDSKAKSLGNLGDADTERYAASARAFGAAFPKANTIAMSHSAPDSRAAITHTARMADKLRLERPHRD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPLGSDQRFGDLVFRQLAPNVWQHTSFMDVPGFGAVSSNGLIVKDGERVLLVDTAWTDDQTSQILNWIKQEINLPVALAV
VTHAHQDKMGGMGALHAEAIPTYANALSNQLAPQEGMTAAQHSLTFAANGWVDPATAPNFGPLRVFYPGPGHTSDNITVG
IDGTDIAFGGCLIKDSKAKSLGNLGDADTERYAASARAFGAAFPKANTIAMSHSAPDSRAAITHTARMADKLRLERPHRD
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION' ZN  
3 water      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   LEU n 
1 4   GLY n 
1 5   SER n 
1 6   ASP n 
1 7   GLN n 
1 8   ARG n 
1 9   PHE n 
1 10  GLY n 
1 11  ASP n 
1 12  LEU n 
1 13  VAL n 
1 14  PHE n 
1 15  ARG n 
1 16  GLN n 
1 17  LEU n 
1 18  ALA n 
1 19  PRO n 
1 20  ASN n 
1 21  VAL n 
1 22  TRP n 
1 23  GLN n 
1 24  HIS n 
1 25  THR n 
1 26  SER n 
1 27  PHE n 
1 28  MET n 
1 29  ASP n 
1 30  VAL n 
1 31  PRO n 
1 32  GLY n 
1 33  PHE n 
1 34  GLY n 
1 35  ALA n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  ASN n 
1 40  GLY n 
1 41  LEU n 
1 42  ILE n 
1 43  VAL n 
1 44  LYS n 
1 45  ASP n 
1 46  GLY n 
1 47  GLU n 
1 48  ARG n 
1 49  VAL n 
1 50  LEU n 
1 51  LEU n 
1 52  VAL n 
1 53  ASP n 
1 54  THR n 
1 55  ALA n 
1 56  TRP n 
1 57  THR n 
1 58  ASP n 
1 59  ASP n 
1 60  GLN n 
1 61  THR n 
1 62  SER n 
1 63  GLN n 
1 64  ILE n 
1 65  LEU n 
1 66  ASN n 
1 67  TRP n 
1 68  ILE n 
1 69  LYS n 
1 70  GLN n 
1 71  GLU n 
1 72  ILE n 
1 73  ASN n 
1 74  LEU n 
1 75  PRO n 
1 76  VAL n 
1 77  ALA n 
1 78  LEU n 
1 79  ALA n 
1 80  VAL n 
1 81  VAL n 
1 82  THR n 
1 83  HIS n 
1 84  ALA n 
1 85  HIS n 
1 86  GLN n 
1 87  ASP n 
1 88  LYS n 
1 89  MET n 
1 90  GLY n 
1 91  GLY n 
1 92  MET n 
1 93  GLY n 
1 94  ALA n 
1 95  LEU n 
1 96  HIS n 
1 97  ALA n 
1 98  GLU n 
1 99  ALA n 
1 100 ILE n 
1 101 PRO n 
1 102 THR n 
1 103 TYR n 
1 104 ALA n 
1 105 ASN n 
1 106 ALA n 
1 107 LEU n 
1 108 SER n 
1 109 ASN n 
1 110 GLN n 
1 111 LEU n 
1 112 ALA n 
1 113 PRO n 
1 114 GLN n 
1 115 GLU n 
1 116 GLY n 
1 117 MET n 
1 118 THR n 
1 119 ALA n 
1 120 ALA n 
1 121 GLN n 
1 122 HIS n 
1 123 SER n 
1 124 LEU n 
1 125 THR n 
1 126 PHE n 
1 127 ALA n 
1 128 ALA n 
1 129 ASN n 
1 130 GLY n 
1 131 TRP n 
1 132 VAL n 
1 133 ASP n 
1 134 PRO n 
1 135 ALA n 
1 136 THR n 
1 137 ALA n 
1 138 PRO n 
1 139 ASN n 
1 140 PHE n 
1 141 GLY n 
1 142 PRO n 
1 143 LEU n 
1 144 ARG n 
1 145 VAL n 
1 146 PHE n 
1 147 TYR n 
1 148 PRO n 
1 149 GLY n 
1 150 PRO n 
1 151 GLY n 
1 152 HIS n 
1 153 THR n 
1 154 SER n 
1 155 ASP n 
1 156 ASN n 
1 157 ILE n 
1 158 THR n 
1 159 VAL n 
1 160 GLY n 
1 161 ILE n 
1 162 ASP n 
1 163 GLY n 
1 164 THR n 
1 165 ASP n 
1 166 ILE n 
1 167 ALA n 
1 168 PHE n 
1 169 GLY n 
1 170 GLY n 
1 171 CYS n 
1 172 LEU n 
1 173 ILE n 
1 174 LYS n 
1 175 ASP n 
1 176 SER n 
1 177 LYS n 
1 178 ALA n 
1 179 LYS n 
1 180 SER n 
1 181 LEU n 
1 182 GLY n 
1 183 ASN n 
1 184 LEU n 
1 185 GLY n 
1 186 ASP n 
1 187 ALA n 
1 188 ASP n 
1 189 THR n 
1 190 GLU n 
1 191 ARG n 
1 192 TYR n 
1 193 ALA n 
1 194 ALA n 
1 195 SER n 
1 196 ALA n 
1 197 ARG n 
1 198 ALA n 
1 199 PHE n 
1 200 GLY n 
1 201 ALA n 
1 202 ALA n 
1 203 PHE n 
1 204 PRO n 
1 205 LYS n 
1 206 ALA n 
1 207 ASN n 
1 208 THR n 
1 209 ILE n 
1 210 ALA n 
1 211 MET n 
1 212 SER n 
1 213 HIS n 
1 214 SER n 
1 215 ALA n 
1 216 PRO n 
1 217 ASP n 
1 218 SER n 
1 219 ARG n 
1 220 ALA n 
1 221 ALA n 
1 222 ILE n 
1 223 THR n 
1 224 HIS n 
1 225 THR n 
1 226 ALA n 
1 227 ARG n 
1 228 MET n 
1 229 ALA n 
1 230 ASP n 
1 231 LYS n 
1 232 LEU n 
1 233 ARG n 
1 234 LEU n 
1 235 GLU n 
1 236 ARG n 
1 237 PRO n 
1 238 HIS n 
1 239 ARG n 
1 240 ASP 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                   240 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 blaAFM 
_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      'Alcaligenes faecalis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     511 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   35  ?   ?   ?   A . n 
A 1 2   PRO 2   36  ?   ?   ?   A . n 
A 1 3   LEU 3   37  ?   ?   ?   A . n 
A 1 4   GLY 4   38  ?   ?   ?   A . n 
A 1 5   SER 5   39  39  SER SER A . n 
A 1 6   ASP 6   40  40  ASP ASP A . n 
A 1 7   GLN 7   41  41  GLN GLN A . n 
A 1 8   ARG 8   42  42  ARG ARG A . n 
A 1 9   PHE 9   43  43  PHE PHE A . n 
A 1 10  GLY 10  44  44  GLY GLY A . n 
A 1 11  ASP 11  45  45  ASP ASP A . n 
A 1 12  LEU 12  46  46  LEU LEU A . n 
A 1 13  VAL 13  47  47  VAL VAL A . n 
A 1 14  PHE 14  48  48  PHE PHE A . n 
A 1 15  ARG 15  49  49  ARG ARG A . n 
A 1 16  GLN 16  50  50  GLN GLN A . n 
A 1 17  LEU 17  51  51  LEU LEU A . n 
A 1 18  ALA 18  52  52  ALA ALA A . n 
A 1 19  PRO 19  53  53  PRO PRO A . n 
A 1 20  ASN 20  54  54  ASN ASN A . n 
A 1 21  VAL 21  55  55  VAL VAL A . n 
A 1 22  TRP 22  56  56  TRP TRP A . n 
A 1 23  GLN 23  57  57  GLN GLN A . n 
A 1 24  HIS 24  58  58  HIS HIS A . n 
A 1 25  THR 25  59  59  THR THR A . n 
A 1 26  SER 26  60  60  SER SER A . n 
A 1 27  PHE 27  61  61  PHE PHE A . n 
A 1 28  MET 28  62  62  MET MET A . n 
A 1 29  ASP 29  63  63  ASP ASP A . n 
A 1 30  VAL 30  64  64  VAL VAL A . n 
A 1 31  PRO 31  65  65  PRO PRO A . n 
A 1 32  GLY 32  66  66  GLY GLY A . n 
A 1 33  PHE 33  67  67  PHE PHE A . n 
A 1 34  GLY 34  68  68  GLY GLY A . n 
A 1 35  ALA 35  69  69  ALA ALA A . n 
A 1 36  VAL 36  70  70  VAL VAL A . n 
A 1 37  SER 37  71  71  SER SER A . n 
A 1 38  SER 38  72  72  SER SER A . n 
A 1 39  ASN 39  73  73  ASN ASN A . n 
A 1 40  GLY 40  74  74  GLY GLY A . n 
A 1 41  LEU 41  75  75  LEU LEU A . n 
A 1 42  ILE 42  76  76  ILE ILE A . n 
A 1 43  VAL 43  77  77  VAL VAL A . n 
A 1 44  LYS 44  78  78  LYS LYS A . n 
A 1 45  ASP 45  79  79  ASP ASP A . n 
A 1 46  GLY 46  80  80  GLY GLY A . n 
A 1 47  GLU 47  81  81  GLU GLU A . n 
A 1 48  ARG 48  82  82  ARG ARG A . n 
A 1 49  VAL 49  83  83  VAL VAL A . n 
A 1 50  LEU 50  84  84  LEU LEU A . n 
A 1 51  LEU 51  85  85  LEU LEU A . n 
A 1 52  VAL 52  86  86  VAL VAL A . n 
A 1 53  ASP 53  87  87  ASP ASP A . n 
A 1 54  THR 54  88  88  THR THR A . n 
A 1 55  ALA 55  89  89  ALA ALA A . n 
A 1 56  TRP 56  90  90  TRP TRP A . n 
A 1 57  THR 57  91  91  THR THR A . n 
A 1 58  ASP 58  92  92  ASP ASP A . n 
A 1 59  ASP 59  93  93  ASP ASP A . n 
A 1 60  GLN 60  94  94  GLN GLN A . n 
A 1 61  THR 61  95  95  THR THR A . n 
A 1 62  SER 62  96  96  SER SER A . n 
A 1 63  GLN 63  97  97  GLN GLN A . n 
A 1 64  ILE 64  98  98  ILE ILE A . n 
A 1 65  LEU 65  99  99  LEU LEU A . n 
A 1 66  ASN 66  100 100 ASN ASN A . n 
A 1 67  TRP 67  101 101 TRP TRP A . n 
A 1 68  ILE 68  102 102 ILE ILE A . n 
A 1 69  LYS 69  103 103 LYS LYS A . n 
A 1 70  GLN 70  104 104 GLN GLN A . n 
A 1 71  GLU 71  105 105 GLU GLU A . n 
A 1 72  ILE 72  106 106 ILE ILE A . n 
A 1 73  ASN 73  107 107 ASN ASN A . n 
A 1 74  LEU 74  108 108 LEU LEU A . n 
A 1 75  PRO 75  109 109 PRO PRO A . n 
A 1 76  VAL 76  110 110 VAL VAL A . n 
A 1 77  ALA 77  111 111 ALA ALA A . n 
A 1 78  LEU 78  112 112 LEU LEU A . n 
A 1 79  ALA 79  113 113 ALA ALA A . n 
A 1 80  VAL 80  114 114 VAL VAL A . n 
A 1 81  VAL 81  115 115 VAL VAL A . n 
A 1 82  THR 82  116 116 THR THR A . n 
A 1 83  HIS 83  117 117 HIS HIS A . n 
A 1 84  ALA 84  118 118 ALA ALA A . n 
A 1 85  HIS 85  119 119 HIS HIS A . n 
A 1 86  GLN 86  120 120 GLN GLN A . n 
A 1 87  ASP 87  121 121 ASP ASP A . n 
A 1 88  LYS 88  122 122 LYS LYS A . n 
A 1 89  MET 89  123 123 MET MET A . n 
A 1 90  GLY 90  124 124 GLY GLY A . n 
A 1 91  GLY 91  125 125 GLY GLY A . n 
A 1 92  MET 92  126 126 MET MET A . n 
A 1 93  GLY 93  127 127 GLY GLY A . n 
A 1 94  ALA 94  128 128 ALA ALA A . n 
A 1 95  LEU 95  129 129 LEU LEU A . n 
A 1 96  HIS 96  130 130 HIS HIS A . n 
A 1 97  ALA 97  131 131 ALA ALA A . n 
A 1 98  GLU 98  132 132 GLU GLU A . n 
A 1 99  ALA 99  133 133 ALA ALA A . n 
A 1 100 ILE 100 134 134 ILE ILE A . n 
A 1 101 PRO 101 135 135 PRO PRO A . n 
A 1 102 THR 102 136 136 THR THR A . n 
A 1 103 TYR 103 137 137 TYR TYR A . n 
A 1 104 ALA 104 138 138 ALA ALA A . n 
A 1 105 ASN 105 139 139 ASN ASN A . n 
A 1 106 ALA 106 140 140 ALA ALA A . n 
A 1 107 LEU 107 141 141 LEU LEU A . n 
A 1 108 SER 108 142 142 SER SER A . n 
A 1 109 ASN 109 143 143 ASN ASN A . n 
A 1 110 GLN 110 144 144 GLN GLN A . n 
A 1 111 LEU 111 145 145 LEU LEU A . n 
A 1 112 ALA 112 146 146 ALA ALA A . n 
A 1 113 PRO 113 147 147 PRO PRO A . n 
A 1 114 GLN 114 148 148 GLN GLN A . n 
A 1 115 GLU 115 149 149 GLU GLU A . n 
A 1 116 GLY 116 150 150 GLY GLY A . n 
A 1 117 MET 117 151 151 MET MET A . n 
A 1 118 THR 118 152 152 THR THR A . n 
A 1 119 ALA 119 153 153 ALA ALA A . n 
A 1 120 ALA 120 154 154 ALA ALA A . n 
A 1 121 GLN 121 155 155 GLN GLN A . n 
A 1 122 HIS 122 156 156 HIS HIS A . n 
A 1 123 SER 123 157 157 SER SER A . n 
A 1 124 LEU 124 158 158 LEU LEU A . n 
A 1 125 THR 125 159 159 THR THR A . n 
A 1 126 PHE 126 160 160 PHE PHE A . n 
A 1 127 ALA 127 161 161 ALA ALA A . n 
A 1 128 ALA 128 162 162 ALA ALA A . n 
A 1 129 ASN 129 163 163 ASN ASN A . n 
A 1 130 GLY 130 164 164 GLY GLY A . n 
A 1 131 TRP 131 165 165 TRP TRP A . n 
A 1 132 VAL 132 166 166 VAL VAL A . n 
A 1 133 ASP 133 167 167 ASP ASP A . n 
A 1 134 PRO 134 168 168 PRO PRO A . n 
A 1 135 ALA 135 169 169 ALA ALA A . n 
A 1 136 THR 136 170 170 THR THR A . n 
A 1 137 ALA 137 171 171 ALA ALA A . n 
A 1 138 PRO 138 172 172 PRO PRO A . n 
A 1 139 ASN 139 173 173 ASN ASN A . n 
A 1 140 PHE 140 174 174 PHE PHE A . n 
A 1 141 GLY 141 175 175 GLY GLY A . n 
A 1 142 PRO 142 176 176 PRO PRO A . n 
A 1 143 LEU 143 177 177 LEU LEU A . n 
A 1 144 ARG 144 178 178 ARG ARG A . n 
A 1 145 VAL 145 179 179 VAL VAL A . n 
A 1 146 PHE 146 180 180 PHE PHE A . n 
A 1 147 TYR 147 181 181 TYR TYR A . n 
A 1 148 PRO 148 182 182 PRO PRO A . n 
A 1 149 GLY 149 183 183 GLY GLY A . n 
A 1 150 PRO 150 184 184 PRO PRO A . n 
A 1 151 GLY 151 185 185 GLY GLY A . n 
A 1 152 HIS 152 186 186 HIS HIS A . n 
A 1 153 THR 153 187 187 THR THR A . n 
A 1 154 SER 154 188 188 SER SER A . n 
A 1 155 ASP 155 189 189 ASP ASP A . n 
A 1 156 ASN 156 190 190 ASN ASN A . n 
A 1 157 ILE 157 191 191 ILE ILE A . n 
A 1 158 THR 158 192 192 THR THR A . n 
A 1 159 VAL 159 193 193 VAL VAL A . n 
A 1 160 GLY 160 194 194 GLY GLY A . n 
A 1 161 ILE 161 195 195 ILE ILE A . n 
A 1 162 ASP 162 196 196 ASP ASP A . n 
A 1 163 GLY 163 197 197 GLY GLY A . n 
A 1 164 THR 164 198 198 THR THR A . n 
A 1 165 ASP 165 199 199 ASP ASP A . n 
A 1 166 ILE 166 200 200 ILE ILE A . n 
A 1 167 ALA 167 201 201 ALA ALA A . n 
A 1 168 PHE 168 202 202 PHE PHE A . n 
A 1 169 GLY 169 203 203 GLY GLY A . n 
A 1 170 GLY 170 204 204 GLY GLY A . n 
A 1 171 CYS 171 205 205 CYS CYS A . n 
A 1 172 LEU 172 206 206 LEU LEU A . n 
A 1 173 ILE 173 207 207 ILE ILE A . n 
A 1 174 LYS 174 208 208 LYS LYS A . n 
A 1 175 ASP 175 209 209 ASP ASP A . n 
A 1 176 SER 176 210 210 SER SER A . n 
A 1 177 LYS 177 211 211 LYS LYS A . n 
A 1 178 ALA 178 212 212 ALA ALA A . n 
A 1 179 LYS 179 213 213 LYS LYS A . n 
A 1 180 SER 180 214 214 SER SER A . n 
A 1 181 LEU 181 215 215 LEU LEU A . n 
A 1 182 GLY 182 216 216 GLY GLY A . n 
A 1 183 ASN 183 217 217 ASN ASN A . n 
A 1 184 LEU 184 218 218 LEU LEU A . n 
A 1 185 GLY 185 219 219 GLY GLY A . n 
A 1 186 ASP 186 220 220 ASP ASP A . n 
A 1 187 ALA 187 221 221 ALA ALA A . n 
A 1 188 ASP 188 222 222 ASP ASP A . n 
A 1 189 THR 189 223 223 THR THR A . n 
A 1 190 GLU 190 224 224 GLU GLU A . n 
A 1 191 ARG 191 225 225 ARG ARG A . n 
A 1 192 TYR 192 226 226 TYR TYR A . n 
A 1 193 ALA 193 227 227 ALA ALA A . n 
A 1 194 ALA 194 228 228 ALA ALA A . n 
A 1 195 SER 195 229 229 SER SER A . n 
A 1 196 ALA 196 230 230 ALA ALA A . n 
A 1 197 ARG 197 231 231 ARG ARG A . n 
A 1 198 ALA 198 232 232 ALA ALA A . n 
A 1 199 PHE 199 233 233 PHE PHE A . n 
A 1 200 GLY 200 234 234 GLY GLY A . n 
A 1 201 ALA 201 235 235 ALA ALA A . n 
A 1 202 ALA 202 236 236 ALA ALA A . n 
A 1 203 PHE 203 237 237 PHE PHE A . n 
A 1 204 PRO 204 238 238 PRO PRO A . n 
A 1 205 LYS 205 239 239 LYS LYS A . n 
A 1 206 ALA 206 240 240 ALA ALA A . n 
A 1 207 ASN 207 241 241 ASN ASN A . n 
A 1 208 THR 208 242 242 THR THR A . n 
A 1 209 ILE 209 243 243 ILE ILE A . n 
A 1 210 ALA 210 244 244 ALA ALA A . n 
A 1 211 MET 211 245 245 MET MET A . n 
A 1 212 SER 212 246 246 SER SER A . n 
A 1 213 HIS 213 247 247 HIS HIS A . n 
A 1 214 SER 214 248 248 SER SER A . n 
A 1 215 ALA 215 249 249 ALA ALA A . n 
A 1 216 PRO 216 250 250 PRO PRO A . n 
A 1 217 ASP 217 251 251 ASP ASP A . n 
A 1 218 SER 218 252 252 SER SER A . n 
A 1 219 ARG 219 253 253 ARG ARG A . n 
A 1 220 ALA 220 254 254 ALA ALA A . n 
A 1 221 ALA 221 255 255 ALA ALA A . n 
A 1 222 ILE 222 256 256 ILE ILE A . n 
A 1 223 THR 223 257 257 THR THR A . n 
A 1 224 HIS 224 258 258 HIS HIS A . n 
A 1 225 THR 225 259 259 THR THR A . n 
A 1 226 ALA 226 260 260 ALA ALA A . n 
A 1 227 ARG 227 261 261 ARG ARG A . n 
A 1 228 MET 228 262 262 MET MET A . n 
A 1 229 ALA 229 263 263 ALA ALA A . n 
A 1 230 ASP 230 264 264 ASP ASP A . n 
A 1 231 LYS 231 265 265 LYS LYS A . n 
A 1 232 LEU 232 266 266 LEU LEU A . n 
A 1 233 ARG 233 267 267 ARG ARG A . n 
A 1 234 LEU 234 268 268 LEU LEU A . n 
A 1 235 GLU 235 269 269 GLU GLU A . n 
A 1 236 ARG 236 270 270 ARG ARG A . n 
A 1 237 PRO 237 271 ?   ?   ?   A . n 
A 1 238 HIS 238 272 ?   ?   ?   A . n 
A 1 239 ARG 239 273 ?   ?   ?   A . n 
A 1 240 ASP 240 274 ?   ?   ?   A . n 
B 1 1   GLY 1   35  ?   ?   ?   B . n 
B 1 2   PRO 2   36  ?   ?   ?   B . n 
B 1 3   LEU 3   37  ?   ?   ?   B . n 
B 1 4   GLY 4   38  ?   ?   ?   B . n 
B 1 5   SER 5   39  ?   ?   ?   B . n 
B 1 6   ASP 6   40  40  ASP ASP B . n 
B 1 7   GLN 7   41  41  GLN GLN B . n 
B 1 8   ARG 8   42  42  ARG ARG B . n 
B 1 9   PHE 9   43  43  PHE PHE B . n 
B 1 10  GLY 10  44  44  GLY GLY B . n 
B 1 11  ASP 11  45  45  ASP ASP B . n 
B 1 12  LEU 12  46  46  LEU LEU B . n 
B 1 13  VAL 13  47  47  VAL VAL B . n 
B 1 14  PHE 14  48  48  PHE PHE B . n 
B 1 15  ARG 15  49  49  ARG ARG B . n 
B 1 16  GLN 16  50  50  GLN GLN B . n 
B 1 17  LEU 17  51  51  LEU LEU B . n 
B 1 18  ALA 18  52  52  ALA ALA B . n 
B 1 19  PRO 19  53  53  PRO PRO B . n 
B 1 20  ASN 20  54  54  ASN ASN B . n 
B 1 21  VAL 21  55  55  VAL VAL B . n 
B 1 22  TRP 22  56  56  TRP TRP B . n 
B 1 23  GLN 23  57  57  GLN GLN B . n 
B 1 24  HIS 24  58  58  HIS HIS B . n 
B 1 25  THR 25  59  59  THR THR B . n 
B 1 26  SER 26  60  60  SER SER B . n 
B 1 27  PHE 27  61  61  PHE PHE B . n 
B 1 28  MET 28  62  62  MET MET B . n 
B 1 29  ASP 29  63  63  ASP ASP B . n 
B 1 30  VAL 30  64  64  VAL VAL B . n 
B 1 31  PRO 31  65  65  PRO PRO B . n 
B 1 32  GLY 32  66  66  GLY GLY B . n 
B 1 33  PHE 33  67  67  PHE PHE B . n 
B 1 34  GLY 34  68  68  GLY GLY B . n 
B 1 35  ALA 35  69  69  ALA ALA B . n 
B 1 36  VAL 36  70  70  VAL VAL B . n 
B 1 37  SER 37  71  71  SER SER B . n 
B 1 38  SER 38  72  72  SER SER B . n 
B 1 39  ASN 39  73  73  ASN ASN B . n 
B 1 40  GLY 40  74  74  GLY GLY B . n 
B 1 41  LEU 41  75  75  LEU LEU B . n 
B 1 42  ILE 42  76  76  ILE ILE B . n 
B 1 43  VAL 43  77  77  VAL VAL B . n 
B 1 44  LYS 44  78  78  LYS LYS B . n 
B 1 45  ASP 45  79  79  ASP ASP B . n 
B 1 46  GLY 46  80  80  GLY GLY B . n 
B 1 47  GLU 47  81  81  GLU GLU B . n 
B 1 48  ARG 48  82  82  ARG ARG B . n 
B 1 49  VAL 49  83  83  VAL VAL B . n 
B 1 50  LEU 50  84  84  LEU LEU B . n 
B 1 51  LEU 51  85  85  LEU LEU B . n 
B 1 52  VAL 52  86  86  VAL VAL B . n 
B 1 53  ASP 53  87  87  ASP ASP B . n 
B 1 54  THR 54  88  88  THR THR B . n 
B 1 55  ALA 55  89  89  ALA ALA B . n 
B 1 56  TRP 56  90  90  TRP TRP B . n 
B 1 57  THR 57  91  91  THR THR B . n 
B 1 58  ASP 58  92  92  ASP ASP B . n 
B 1 59  ASP 59  93  93  ASP ASP B . n 
B 1 60  GLN 60  94  94  GLN GLN B . n 
B 1 61  THR 61  95  95  THR THR B . n 
B 1 62  SER 62  96  96  SER SER B . n 
B 1 63  GLN 63  97  97  GLN GLN B . n 
B 1 64  ILE 64  98  98  ILE ILE B . n 
B 1 65  LEU 65  99  99  LEU LEU B . n 
B 1 66  ASN 66  100 100 ASN ASN B . n 
B 1 67  TRP 67  101 101 TRP TRP B . n 
B 1 68  ILE 68  102 102 ILE ILE B . n 
B 1 69  LYS 69  103 103 LYS LYS B . n 
B 1 70  GLN 70  104 104 GLN GLN B . n 
B 1 71  GLU 71  105 105 GLU GLU B . n 
B 1 72  ILE 72  106 106 ILE ILE B . n 
B 1 73  ASN 73  107 107 ASN ASN B . n 
B 1 74  LEU 74  108 108 LEU LEU B . n 
B 1 75  PRO 75  109 109 PRO PRO B . n 
B 1 76  VAL 76  110 110 VAL VAL B . n 
B 1 77  ALA 77  111 111 ALA ALA B . n 
B 1 78  LEU 78  112 112 LEU LEU B . n 
B 1 79  ALA 79  113 113 ALA ALA B . n 
B 1 80  VAL 80  114 114 VAL VAL B . n 
B 1 81  VAL 81  115 115 VAL VAL B . n 
B 1 82  THR 82  116 116 THR THR B . n 
B 1 83  HIS 83  117 117 HIS HIS B . n 
B 1 84  ALA 84  118 118 ALA ALA B . n 
B 1 85  HIS 85  119 119 HIS HIS B . n 
B 1 86  GLN 86  120 120 GLN GLN B . n 
B 1 87  ASP 87  121 121 ASP ASP B . n 
B 1 88  LYS 88  122 122 LYS LYS B . n 
B 1 89  MET 89  123 123 MET MET B . n 
B 1 90  GLY 90  124 124 GLY GLY B . n 
B 1 91  GLY 91  125 125 GLY GLY B . n 
B 1 92  MET 92  126 126 MET MET B . n 
B 1 93  GLY 93  127 127 GLY GLY B . n 
B 1 94  ALA 94  128 128 ALA ALA B . n 
B 1 95  LEU 95  129 129 LEU LEU B . n 
B 1 96  HIS 96  130 130 HIS HIS B . n 
B 1 97  ALA 97  131 131 ALA ALA B . n 
B 1 98  GLU 98  132 132 GLU GLU B . n 
B 1 99  ALA 99  133 133 ALA ALA B . n 
B 1 100 ILE 100 134 134 ILE ILE B . n 
B 1 101 PRO 101 135 135 PRO PRO B . n 
B 1 102 THR 102 136 136 THR THR B . n 
B 1 103 TYR 103 137 137 TYR TYR B . n 
B 1 104 ALA 104 138 138 ALA ALA B . n 
B 1 105 ASN 105 139 139 ASN ASN B . n 
B 1 106 ALA 106 140 140 ALA ALA B . n 
B 1 107 LEU 107 141 141 LEU LEU B . n 
B 1 108 SER 108 142 142 SER SER B . n 
B 1 109 ASN 109 143 143 ASN ASN B . n 
B 1 110 GLN 110 144 144 GLN GLN B . n 
B 1 111 LEU 111 145 145 LEU LEU B . n 
B 1 112 ALA 112 146 146 ALA ALA B . n 
B 1 113 PRO 113 147 147 PRO PRO B . n 
B 1 114 GLN 114 148 148 GLN GLN B . n 
B 1 115 GLU 115 149 149 GLU GLU B . n 
B 1 116 GLY 116 150 150 GLY GLY B . n 
B 1 117 MET 117 151 151 MET MET B . n 
B 1 118 THR 118 152 152 THR THR B . n 
B 1 119 ALA 119 153 153 ALA ALA B . n 
B 1 120 ALA 120 154 154 ALA ALA B . n 
B 1 121 GLN 121 155 155 GLN GLN B . n 
B 1 122 HIS 122 156 156 HIS HIS B . n 
B 1 123 SER 123 157 157 SER SER B . n 
B 1 124 LEU 124 158 158 LEU LEU B . n 
B 1 125 THR 125 159 159 THR THR B . n 
B 1 126 PHE 126 160 160 PHE PHE B . n 
B 1 127 ALA 127 161 161 ALA ALA B . n 
B 1 128 ALA 128 162 162 ALA ALA B . n 
B 1 129 ASN 129 163 163 ASN ASN B . n 
B 1 130 GLY 130 164 164 GLY GLY B . n 
B 1 131 TRP 131 165 165 TRP TRP B . n 
B 1 132 VAL 132 166 166 VAL VAL B . n 
B 1 133 ASP 133 167 167 ASP ASP B . n 
B 1 134 PRO 134 168 168 PRO PRO B . n 
B 1 135 ALA 135 169 169 ALA ALA B . n 
B 1 136 THR 136 170 170 THR THR B . n 
B 1 137 ALA 137 171 171 ALA ALA B . n 
B 1 138 PRO 138 172 172 PRO PRO B . n 
B 1 139 ASN 139 173 173 ASN ASN B . n 
B 1 140 PHE 140 174 174 PHE PHE B . n 
B 1 141 GLY 141 175 175 GLY GLY B . n 
B 1 142 PRO 142 176 176 PRO PRO B . n 
B 1 143 LEU 143 177 177 LEU LEU B . n 
B 1 144 ARG 144 178 178 ARG ARG B . n 
B 1 145 VAL 145 179 179 VAL VAL B . n 
B 1 146 PHE 146 180 180 PHE PHE B . n 
B 1 147 TYR 147 181 181 TYR TYR B . n 
B 1 148 PRO 148 182 182 PRO PRO B . n 
B 1 149 GLY 149 183 183 GLY GLY B . n 
B 1 150 PRO 150 184 184 PRO PRO B . n 
B 1 151 GLY 151 185 185 GLY GLY B . n 
B 1 152 HIS 152 186 186 HIS HIS B . n 
B 1 153 THR 153 187 187 THR THR B . n 
B 1 154 SER 154 188 188 SER SER B . n 
B 1 155 ASP 155 189 189 ASP ASP B . n 
B 1 156 ASN 156 190 190 ASN ASN B . n 
B 1 157 ILE 157 191 191 ILE ILE B . n 
B 1 158 THR 158 192 192 THR THR B . n 
B 1 159 VAL 159 193 193 VAL VAL B . n 
B 1 160 GLY 160 194 194 GLY GLY B . n 
B 1 161 ILE 161 195 195 ILE ILE B . n 
B 1 162 ASP 162 196 196 ASP ASP B . n 
B 1 163 GLY 163 197 197 GLY GLY B . n 
B 1 164 THR 164 198 198 THR THR B . n 
B 1 165 ASP 165 199 199 ASP ASP B . n 
B 1 166 ILE 166 200 200 ILE ILE B . n 
B 1 167 ALA 167 201 201 ALA ALA B . n 
B 1 168 PHE 168 202 202 PHE PHE B . n 
B 1 169 GLY 169 203 203 GLY GLY B . n 
B 1 170 GLY 170 204 204 GLY GLY B . n 
B 1 171 CYS 171 205 205 CYS CYS B . n 
B 1 172 LEU 172 206 206 LEU LEU B . n 
B 1 173 ILE 173 207 207 ILE ILE B . n 
B 1 174 LYS 174 208 208 LYS LYS B . n 
B 1 175 ASP 175 209 209 ASP ASP B . n 
B 1 176 SER 176 210 210 SER SER B . n 
B 1 177 LYS 177 211 211 LYS LYS B . n 
B 1 178 ALA 178 212 212 ALA ALA B . n 
B 1 179 LYS 179 213 213 LYS LYS B . n 
B 1 180 SER 180 214 214 SER SER B . n 
B 1 181 LEU 181 215 215 LEU LEU B . n 
B 1 182 GLY 182 216 216 GLY GLY B . n 
B 1 183 ASN 183 217 217 ASN ASN B . n 
B 1 184 LEU 184 218 218 LEU LEU B . n 
B 1 185 GLY 185 219 219 GLY GLY B . n 
B 1 186 ASP 186 220 220 ASP ASP B . n 
B 1 187 ALA 187 221 221 ALA ALA B . n 
B 1 188 ASP 188 222 222 ASP ASP B . n 
B 1 189 THR 189 223 223 THR THR B . n 
B 1 190 GLU 190 224 224 GLU GLU B . n 
B 1 191 ARG 191 225 225 ARG ARG B . n 
B 1 192 TYR 192 226 226 TYR TYR B . n 
B 1 193 ALA 193 227 227 ALA ALA B . n 
B 1 194 ALA 194 228 228 ALA ALA B . n 
B 1 195 SER 195 229 229 SER SER B . n 
B 1 196 ALA 196 230 230 ALA ALA B . n 
B 1 197 ARG 197 231 231 ARG ARG B . n 
B 1 198 ALA 198 232 232 ALA ALA B . n 
B 1 199 PHE 199 233 233 PHE PHE B . n 
B 1 200 GLY 200 234 234 GLY GLY B . n 
B 1 201 ALA 201 235 235 ALA ALA B . n 
B 1 202 ALA 202 236 236 ALA ALA B . n 
B 1 203 PHE 203 237 237 PHE PHE B . n 
B 1 204 PRO 204 238 238 PRO PRO B . n 
B 1 205 LYS 205 239 239 LYS LYS B . n 
B 1 206 ALA 206 240 240 ALA ALA B . n 
B 1 207 ASN 207 241 241 ASN ASN B . n 
B 1 208 THR 208 242 242 THR THR B . n 
B 1 209 ILE 209 243 243 ILE ILE B . n 
B 1 210 ALA 210 244 244 ALA ALA B . n 
B 1 211 MET 211 245 245 MET MET B . n 
B 1 212 SER 212 246 246 SER SER B . n 
B 1 213 HIS 213 247 247 HIS HIS B . n 
B 1 214 SER 214 248 248 SER SER B . n 
B 1 215 ALA 215 249 249 ALA ALA B . n 
B 1 216 PRO 216 250 250 PRO PRO B . n 
B 1 217 ASP 217 251 251 ASP ASP B . n 
B 1 218 SER 218 252 252 SER SER B . n 
B 1 219 ARG 219 253 253 ARG ARG B . n 
B 1 220 ALA 220 254 254 ALA ALA B . n 
B 1 221 ALA 221 255 255 ALA ALA B . n 
B 1 222 ILE 222 256 256 ILE ILE B . n 
B 1 223 THR 223 257 257 THR THR B . n 
B 1 224 HIS 224 258 258 HIS HIS B . n 
B 1 225 THR 225 259 259 THR THR B . n 
B 1 226 ALA 226 260 260 ALA ALA B . n 
B 1 227 ARG 227 261 261 ARG ARG B . n 
B 1 228 MET 228 262 262 MET MET B . n 
B 1 229 ALA 229 263 263 ALA ALA B . n 
B 1 230 ASP 230 264 264 ASP ASP B . n 
B 1 231 LYS 231 265 265 LYS LYS B . n 
B 1 232 LEU 232 266 266 LEU LEU B . n 
B 1 233 ARG 233 267 267 ARG ARG B . n 
B 1 234 LEU 234 268 268 LEU LEU B . n 
B 1 235 GLU 235 269 269 GLU GLU B . n 
B 1 236 ARG 236 270 ?   ?   ?   B . n 
B 1 237 PRO 237 271 ?   ?   ?   B . n 
B 1 238 HIS 238 272 ?   ?   ?   B . n 
B 1 239 ARG 239 273 ?   ?   ?   B . n 
B 1 240 ASP 240 274 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN  1  301 298 ZN  ZN  A . 
D 2 ZN  1  302 398 ZN  ZN  A . 
E 2 ZN  1  301 298 ZN  ZN  B . 
F 2 ZN  1  302 398 ZN  ZN  B . 
G 3 HOH 1  401 128 HOH HOH A . 
G 3 HOH 2  402 58  HOH HOH A . 
G 3 HOH 3  403 21  HOH HOH A . 
G 3 HOH 4  404 24  HOH HOH A . 
G 3 HOH 5  405 4   HOH HOH A . 
G 3 HOH 6  406 2   HOH HOH A . 
G 3 HOH 7  407 29  HOH HOH A . 
G 3 HOH 8  408 15  HOH HOH A . 
G 3 HOH 9  409 3   HOH HOH A . 
G 3 HOH 10 410 11  HOH HOH A . 
G 3 HOH 11 411 25  HOH HOH A . 
G 3 HOH 12 412 111 HOH HOH A . 
G 3 HOH 13 413 8   HOH HOH A . 
G 3 HOH 14 414 6   HOH HOH A . 
G 3 HOH 15 415 53  HOH HOH A . 
G 3 HOH 16 416 108 HOH HOH A . 
G 3 HOH 17 417 114 HOH HOH A . 
G 3 HOH 18 418 17  HOH HOH A . 
G 3 HOH 19 419 14  HOH HOH A . 
G 3 HOH 20 420 31  HOH HOH A . 
G 3 HOH 21 421 5   HOH HOH A . 
G 3 HOH 22 422 9   HOH HOH A . 
G 3 HOH 23 423 27  HOH HOH A . 
G 3 HOH 24 424 23  HOH HOH A . 
G 3 HOH 25 425 19  HOH HOH A . 
G 3 HOH 26 426 10  HOH HOH A . 
G 3 HOH 27 427 47  HOH HOH A . 
G 3 HOH 28 428 110 HOH HOH A . 
G 3 HOH 29 429 28  HOH HOH A . 
G 3 HOH 30 430 74  HOH HOH A . 
G 3 HOH 31 431 13  HOH HOH A . 
G 3 HOH 32 432 1   HOH HOH A . 
G 3 HOH 33 433 91  HOH HOH A . 
G 3 HOH 34 434 101 HOH HOH A . 
G 3 HOH 35 435 40  HOH HOH A . 
G 3 HOH 36 436 88  HOH HOH A . 
G 3 HOH 37 437 119 HOH HOH A . 
G 3 HOH 38 438 66  HOH HOH A . 
G 3 HOH 39 439 96  HOH HOH A . 
G 3 HOH 40 440 65  HOH HOH A . 
G 3 HOH 41 441 76  HOH HOH A . 
G 3 HOH 42 442 32  HOH HOH A . 
G 3 HOH 43 443 112 HOH HOH A . 
G 3 HOH 44 444 109 HOH HOH A . 
G 3 HOH 45 445 57  HOH HOH A . 
G 3 HOH 46 446 103 HOH HOH A . 
G 3 HOH 47 447 90  HOH HOH A . 
G 3 HOH 48 448 62  HOH HOH A . 
G 3 HOH 49 449 106 HOH HOH A . 
G 3 HOH 50 450 83  HOH HOH A . 
G 3 HOH 51 451 89  HOH HOH A . 
G 3 HOH 52 452 51  HOH HOH A . 
G 3 HOH 53 453 126 HOH HOH A . 
G 3 HOH 54 454 104 HOH HOH A . 
G 3 HOH 55 455 60  HOH HOH A . 
G 3 HOH 56 456 78  HOH HOH A . 
G 3 HOH 57 457 68  HOH HOH A . 
G 3 HOH 58 458 120 HOH HOH A . 
G 3 HOH 59 459 86  HOH HOH A . 
G 3 HOH 60 460 85  HOH HOH A . 
G 3 HOH 61 461 84  HOH HOH A . 
G 3 HOH 62 462 38  HOH HOH A . 
G 3 HOH 63 463 129 HOH HOH A . 
G 3 HOH 64 464 59  HOH HOH A . 
G 3 HOH 65 465 56  HOH HOH A . 
G 3 HOH 66 466 125 HOH HOH A . 
G 3 HOH 67 467 48  HOH HOH A . 
G 3 HOH 68 468 102 HOH HOH A . 
G 3 HOH 69 469 52  HOH HOH A . 
G 3 HOH 70 470 113 HOH HOH A . 
G 3 HOH 71 471 115 HOH HOH A . 
G 3 HOH 72 472 61  HOH HOH A . 
G 3 HOH 73 473 39  HOH HOH A . 
G 3 HOH 74 474 49  HOH HOH A . 
G 3 HOH 75 475 107 HOH HOH A . 
G 3 HOH 76 476 130 HOH HOH A . 
G 3 HOH 77 477 127 HOH HOH A . 
G 3 HOH 78 478 41  HOH HOH A . 
G 3 HOH 79 479 37  HOH HOH A . 
G 3 HOH 80 480 100 HOH HOH A . 
G 3 HOH 81 481 55  HOH HOH A . 
G 3 HOH 82 482 87  HOH HOH A . 
H 3 HOH 1  401 136 HOH HOH B . 
H 3 HOH 2  402 42  HOH HOH B . 
H 3 HOH 3  403 44  HOH HOH B . 
H 3 HOH 4  404 26  HOH HOH B . 
H 3 HOH 5  405 20  HOH HOH B . 
H 3 HOH 6  406 12  HOH HOH B . 
H 3 HOH 7  407 7   HOH HOH B . 
H 3 HOH 8  408 46  HOH HOH B . 
H 3 HOH 9  409 71  HOH HOH B . 
H 3 HOH 10 410 93  HOH HOH B . 
H 3 HOH 11 411 82  HOH HOH B . 
H 3 HOH 12 412 72  HOH HOH B . 
H 3 HOH 13 413 79  HOH HOH B . 
H 3 HOH 14 414 92  HOH HOH B . 
H 3 HOH 15 415 16  HOH HOH B . 
H 3 HOH 16 416 33  HOH HOH B . 
H 3 HOH 17 417 81  HOH HOH B . 
H 3 HOH 18 418 18  HOH HOH B . 
H 3 HOH 19 419 50  HOH HOH B . 
H 3 HOH 20 420 116 HOH HOH B . 
H 3 HOH 21 421 22  HOH HOH B . 
H 3 HOH 22 422 43  HOH HOH B . 
H 3 HOH 23 423 134 HOH HOH B . 
H 3 HOH 24 424 70  HOH HOH B . 
H 3 HOH 25 425 73  HOH HOH B . 
H 3 HOH 26 426 135 HOH HOH B . 
H 3 HOH 27 427 117 HOH HOH B . 
H 3 HOH 28 428 139 HOH HOH B . 
H 3 HOH 29 429 77  HOH HOH B . 
H 3 HOH 30 430 75  HOH HOH B . 
H 3 HOH 31 431 138 HOH HOH B . 
H 3 HOH 32 432 36  HOH HOH B . 
H 3 HOH 33 433 131 HOH HOH B . 
H 3 HOH 34 434 137 HOH HOH B . 
H 3 HOH 35 435 35  HOH HOH B . 
H 3 HOH 36 436 133 HOH HOH B . 
H 3 HOH 37 437 95  HOH HOH B . 
H 3 HOH 38 438 80  HOH HOH B . 
H 3 HOH 39 439 122 HOH HOH B . 
H 3 HOH 40 440 143 HOH HOH B . 
H 3 HOH 41 441 94  HOH HOH B . 
H 3 HOH 42 442 123 HOH HOH B . 
H 3 HOH 43 443 34  HOH HOH B . 
H 3 HOH 44 444 69  HOH HOH B . 
H 3 HOH 45 445 97  HOH HOH B . 
H 3 HOH 46 446 132 HOH HOH B . 
H 3 HOH 47 447 140 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 B GLU 81  ? CG  ? B GLU 47  CG  
2  1 Y 1 B GLU 81  ? CD  ? B GLU 47  CD  
3  1 Y 1 B GLU 81  ? OE1 ? B GLU 47  OE1 
4  1 Y 1 B GLU 81  ? OE2 ? B GLU 47  OE2 
5  1 Y 1 B ASN 107 ? CG  ? B ASN 73  CG  
6  1 Y 1 B ASN 107 ? OD1 ? B ASN 73  OD1 
7  1 Y 1 B ASN 107 ? ND2 ? B ASN 73  ND2 
8  1 Y 1 B GLN 144 ? CG  ? B GLN 110 CG  
9  1 Y 1 B GLN 144 ? CD  ? B GLN 110 CD  
10 1 Y 1 B GLN 144 ? OE1 ? B GLN 110 OE1 
11 1 Y 1 B GLN 144 ? NE2 ? B GLN 110 NE2 
12 1 Y 1 B GLU 224 ? CG  ? B GLU 190 CG  
13 1 Y 1 B GLU 224 ? CD  ? B GLU 190 CD  
14 1 Y 1 B GLU 224 ? OE1 ? B GLU 190 OE1 
15 1 Y 1 B GLU 224 ? OE2 ? B GLU 190 OE2 
16 1 Y 1 B ARG 267 ? CG  ? B ARG 233 CG  
17 1 Y 1 B ARG 267 ? CD  ? B ARG 233 CD  
18 1 Y 1 B ARG 267 ? NE  ? B ARG 233 NE  
19 1 Y 1 B ARG 267 ? CZ  ? B ARG 233 CZ  
20 1 Y 1 B ARG 267 ? NH1 ? B ARG 233 NH1 
21 1 Y 1 B ARG 267 ? NH2 ? B ARG 233 NH2 
22 1 Y 1 B GLU 269 ? CG  ? B GLU 235 CG  
23 1 Y 1 B GLU 269 ? CD  ? B GLU 235 CD  
24 1 Y 1 B GLU 269 ? OE1 ? B GLU 235 OE1 
25 1 Y 1 B GLU 269 ? OE2 ? B GLU 235 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(1.19_4092: ???)' 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .                  2 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .                  3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .                  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                     8Z7M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.960 
_cell.length_a_esd                 ? 
_cell.length_b                     105.459 
_cell.length_b_esd                 ? 
_cell.length_c                     106.359 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Z7M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 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                   8Z7M 
_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             2.69 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.21 
_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          'BATCH MODE' 
_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    '30% (w/v) PEG 8000, 100 mM imidazole/Hydrochloric acid pH 8.0, and 200 mM NaCl' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 X 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-01-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97891 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97891 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          53.26 
_reflns.entry_id                                       8Z7M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.60 
_reflns.d_resolution_low                               50.00 
_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                                     17530 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.2 
_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                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.60 
_reflns_shell.d_res_low                                     2.69 
_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                             1694 
_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                                  0.80 
_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                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Z7M 
_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                            2.60 
_refine.ls_d_res_low                             47.48 
_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                     17530 
_refine.ls_number_reflns_R_free                  1745 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.86 
_refine.ls_percent_reflns_R_free                 9.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2144 
_refine.ls_R_factor_R_free                       0.2583 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2096 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          SAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.73 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.34 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        47.48 
_refine_hist.number_atoms_solvent             129 
_refine_hist.number_atoms_total               3569 
_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        3436 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_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' ? 0.002 ? 3525 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.444 ? 4803 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.238 ? 485  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041 ? 539  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003 ? 637  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.60 2.68  . . 142 1272 99.00  . . . . 0.2674 . . . . . . . . . . . 0.3418 
'X-RAY DIFFRACTION' 2.68 2.76  . . 140 1296 100.00 . . . . 0.2707 . . . . . . . . . . . 0.3337 
'X-RAY DIFFRACTION' 2.76 2.86  . . 145 1293 100.00 . . . . 0.2793 . . . . . . . . . . . 0.3345 
'X-RAY DIFFRACTION' 2.86 2.98  . . 143 1282 100.00 . . . . 0.2664 . . . . . . . . . . . 0.3378 
'X-RAY DIFFRACTION' 2.98 3.11  . . 142 1299 100.00 . . . . 0.2428 . . . . . . . . . . . 0.3148 
'X-RAY DIFFRACTION' 3.11 3.28  . . 146 1324 100.00 . . . . 0.2213 . . . . . . . . . . . 0.2806 
'X-RAY DIFFRACTION' 3.28 3.48  . . 148 1287 100.00 . . . . 0.2259 . . . . . . . . . . . 0.2737 
'X-RAY DIFFRACTION' 3.48 3.75  . . 139 1325 100.00 . . . . 0.2035 . . . . . . . . . . . 0.2835 
'X-RAY DIFFRACTION' 3.75 4.13  . . 147 1301 100.00 . . . . 0.1840 . . . . . . . . . . . 0.2394 
'X-RAY DIFFRACTION' 4.13 4.72  . . 145 1328 100.00 . . . . 0.1768 . . . . . . . . . . . 0.2115 
'X-RAY DIFFRACTION' 4.73 5.95  . . 150 1348 100.00 . . . . 0.1961 . . . . . . . . . . . 0.2220 
'X-RAY DIFFRACTION' 5.95 47.48 . . 158 1430 100.00 . . . . 0.1991 . . . . . . . . . . . 0.2307 
# 
_struct.entry_id                     8Z7M 
_struct.title                        'The crystal structure of AFM-1' 
_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        8Z7M 
_struct_keywords.text            'AFM-1; Metallo-beta-lactamase, METAL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A3G5BD68_ALCFA 
_struct_ref.pdbx_db_accession          A0A3G5BD68 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DQRFGDLVFRQLAPNVWQHTSFMDVPGFGAVSSNGLIVKDGERVLLVDTAWTDDQTSQILNWIKQEINLPVALAVVTHAH
QDKMGGMGALHAEAIPTYANALSNQLAPQEGMTAAQHSLTFAANGWVDPATAPNFGPLRVFYPGPGHTSDNITVGIDGTD
IAFGGCLIKDSKAKSLGNLGDADTERYAASARAFGAAFPKANTIAMSHSAPDSRAAITHTARMADKLR
;
_struct_ref.pdbx_align_begin           40 
# 
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 8Z7M A 6 ? 233 ? A0A3G5BD68 40 ? 267 ? 40 267 
2 1 8Z7M B 6 ? 233 ? A0A3G5BD68 40 ? 267 ? 40 267 
# 
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 8Z7M GLY A 1   ? UNP A0A3G5BD68 ? ? 'expression tag' 35  1  
1 8Z7M PRO A 2   ? UNP A0A3G5BD68 ? ? 'expression tag' 36  2  
1 8Z7M LEU A 3   ? UNP A0A3G5BD68 ? ? 'expression tag' 37  3  
1 8Z7M GLY A 4   ? UNP A0A3G5BD68 ? ? 'expression tag' 38  4  
1 8Z7M SER A 5   ? UNP A0A3G5BD68 ? ? 'expression tag' 39  5  
1 8Z7M LEU A 234 ? UNP A0A3G5BD68 ? ? 'expression tag' 268 6  
1 8Z7M GLU A 235 ? UNP A0A3G5BD68 ? ? 'expression tag' 269 7  
1 8Z7M ARG A 236 ? UNP A0A3G5BD68 ? ? 'expression tag' 270 8  
1 8Z7M PRO A 237 ? UNP A0A3G5BD68 ? ? 'expression tag' 271 9  
1 8Z7M HIS A 238 ? UNP A0A3G5BD68 ? ? 'expression tag' 272 10 
1 8Z7M ARG A 239 ? UNP A0A3G5BD68 ? ? 'expression tag' 273 11 
1 8Z7M ASP A 240 ? UNP A0A3G5BD68 ? ? 'expression tag' 274 12 
2 8Z7M GLY B 1   ? UNP A0A3G5BD68 ? ? 'expression tag' 35  13 
2 8Z7M PRO B 2   ? UNP A0A3G5BD68 ? ? 'expression tag' 36  14 
2 8Z7M LEU B 3   ? UNP A0A3G5BD68 ? ? 'expression tag' 37  15 
2 8Z7M GLY B 4   ? UNP A0A3G5BD68 ? ? 'expression tag' 38  16 
2 8Z7M SER B 5   ? UNP A0A3G5BD68 ? ? 'expression tag' 39  17 
2 8Z7M LEU B 234 ? UNP A0A3G5BD68 ? ? 'expression tag' 268 18 
2 8Z7M GLU B 235 ? UNP A0A3G5BD68 ? ? 'expression tag' 269 19 
2 8Z7M ARG B 236 ? UNP A0A3G5BD68 ? ? 'expression tag' 270 20 
2 8Z7M PRO B 237 ? UNP A0A3G5BD68 ? ? 'expression tag' 271 21 
2 8Z7M HIS B 238 ? UNP A0A3G5BD68 ? ? 'expression tag' 272 22 
2 8Z7M ARG B 239 ? UNP A0A3G5BD68 ? ? 'expression tag' 273 23 
2 8Z7M ASP B 240 ? UNP A0A3G5BD68 ? ? 'expression tag' 274 24 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
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)' 210   ? 
1 MORE         -79   ? 
1 'SSA (A^2)'  10000 ? 
2 'ABSA (A^2)' 210   ? 
2 MORE         -79   ? 
2 'SSA (A^2)'  9610  ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 57  ? ILE A 72  ? THR A 91  ILE A 106 1 ? 16 
HELX_P HELX_P2  AA2 HIS A 85  ? GLY A 90  ? HIS A 119 GLY A 124 1 ? 6  
HELX_P HELX_P3  AA3 GLY A 91  ? GLU A 98  ? GLY A 125 GLU A 132 1 ? 8  
HELX_P HELX_P4  AA4 ALA A 106 ? ALA A 112 ? ALA A 140 ALA A 146 1 ? 7  
HELX_P HELX_P5  AA5 PRO A 113 ? GLY A 116 ? PRO A 147 GLY A 150 5 ? 4  
HELX_P HELX_P6  AA6 ARG A 191 ? PHE A 203 ? ARG A 225 PHE A 237 1 ? 13 
HELX_P HELX_P7  AA7 ARG A 219 ? GLU A 235 ? ARG A 253 GLU A 269 1 ? 17 
HELX_P HELX_P8  AA8 THR B 57  ? ILE B 72  ? THR B 91  ILE B 106 1 ? 16 
HELX_P HELX_P9  AA9 HIS B 85  ? GLY B 90  ? HIS B 119 GLY B 124 1 ? 6  
HELX_P HELX_P10 AB1 GLY B 91  ? ALA B 97  ? GLY B 125 ALA B 131 1 ? 7  
HELX_P HELX_P11 AB2 ALA B 106 ? ALA B 112 ? ALA B 140 ALA B 146 1 ? 7  
HELX_P HELX_P12 AB3 PRO B 113 ? GLY B 116 ? PRO B 147 GLY B 150 5 ? 4  
HELX_P HELX_P13 AB4 GLU B 190 ? PHE B 203 ? GLU B 224 PHE B 237 1 ? 14 
HELX_P HELX_P14 AB5 ARG B 219 ? GLU B 235 ? ARG B 253 GLU B 269 1 ? 17 
# 
_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 
metalc1  metalc ? ? A HIS 83  NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc2  metalc ? ? A HIS 85  ND1 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc3  metalc ? ? A ASP 87  OD2 ? ? ? 1_555 D ZN  . ZN ? ? A ASP 121 A ZN  302 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
metalc4  metalc ? ? A HIS 152 NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 186 A ZN  301 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc5  metalc ? ? A CYS 171 SG  ? ? ? 1_555 D ZN  . ZN ? ? A CYS 205 A ZN  302 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc6  metalc ? ? A HIS 213 NE2 ? ? ? 1_555 D ZN  . ZN ? ? A HIS 247 A ZN  302 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc7  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 G HOH . O  ? ? A ZN  301 A HOH 442 1_555 ? ? ? ? ? ? ? 2.201 ? ? 
metalc8  metalc ? ? D ZN  .   ZN  ? ? ? 1_555 G HOH . O  ? ? A ZN  302 A HOH 442 1_555 ? ? ? ? ? ? ? 2.381 ? ? 
metalc9  metalc ? ? B HIS 83  NE2 ? ? ? 1_555 F ZN  . ZN ? ? B HIS 117 B ZN  302 1_555 ? ? ? ? ? ? ? 2.294 ? ? 
metalc10 metalc ? ? B HIS 85  ND1 ? ? ? 1_555 F ZN  . ZN ? ? B HIS 119 B ZN  302 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc11 metalc ? ? B ASP 87  OD2 ? ? ? 1_555 E ZN  . ZN ? ? B ASP 121 B ZN  301 1_555 ? ? ? ? ? ? ? 2.111 ? ? 
metalc12 metalc ? ? B HIS 152 NE2 ? ? ? 1_555 F ZN  . ZN ? ? B HIS 186 B ZN  302 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc13 metalc ? ? B CYS 171 SG  ? ? ? 1_555 E ZN  . ZN ? ? B CYS 205 B ZN  301 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc14 metalc ? ? B HIS 213 NE2 ? ? ? 1_555 E ZN  . ZN ? ? B HIS 247 B ZN  301 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc15 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 H HOH . O  ? ? B ZN  301 B HOH 416 1_555 ? ? ? ? ? ? ? 2.118 ? ? 
metalc16 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 H HOH . O  ? ? B ZN  302 B HOH 416 1_555 ? ? ? ? ? ? ? 2.201 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 83  ? A HIS 117 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 85  ? A HIS 119 ? 1_555 96.0  ? 
2  NE2 ? A HIS 83  ? A HIS 117 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 152 ? A HIS 186 ? 1_555 111.2 ? 
3  ND1 ? A HIS 85  ? A HIS 119 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 152 ? A HIS 186 ? 1_555 101.9 ? 
4  NE2 ? A HIS 83  ? A HIS 117 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 O   ? G HOH .   ? A HOH 442 ? 1_555 147.3 ? 
5  ND1 ? A HIS 85  ? A HIS 119 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 O   ? G HOH .   ? A HOH 442 ? 1_555 97.7  ? 
6  NE2 ? A HIS 152 ? A HIS 186 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 O   ? G HOH .   ? A HOH 442 ? 1_555 94.8  ? 
7  OD2 ? A ASP 87  ? A ASP 121 ? 1_555 ZN ? D ZN . ? A ZN 302 ? 1_555 SG  ? A CYS 171 ? A CYS 205 ? 1_555 116.9 ? 
8  OD2 ? A ASP 87  ? A ASP 121 ? 1_555 ZN ? D ZN . ? A ZN 302 ? 1_555 NE2 ? A HIS 213 ? A HIS 247 ? 1_555 100.4 ? 
9  SG  ? A CYS 171 ? A CYS 205 ? 1_555 ZN ? D ZN . ? A ZN 302 ? 1_555 NE2 ? A HIS 213 ? A HIS 247 ? 1_555 102.0 ? 
10 OD2 ? A ASP 87  ? A ASP 121 ? 1_555 ZN ? D ZN . ? A ZN 302 ? 1_555 O   ? G HOH .   ? A HOH 442 ? 1_555 106.2 ? 
11 SG  ? A CYS 171 ? A CYS 205 ? 1_555 ZN ? D ZN . ? A ZN 302 ? 1_555 O   ? G HOH .   ? A HOH 442 ? 1_555 120.7 ? 
12 NE2 ? A HIS 213 ? A HIS 247 ? 1_555 ZN ? D ZN . ? A ZN 302 ? 1_555 O   ? G HOH .   ? A HOH 442 ? 1_555 108.4 ? 
13 NE2 ? B HIS 83  ? B HIS 117 ? 1_555 ZN ? F ZN . ? B ZN 302 ? 1_555 ND1 ? B HIS 85  ? B HIS 119 ? 1_555 113.3 ? 
14 NE2 ? B HIS 83  ? B HIS 117 ? 1_555 ZN ? F ZN . ? B ZN 302 ? 1_555 NE2 ? B HIS 152 ? B HIS 186 ? 1_555 114.7 ? 
15 ND1 ? B HIS 85  ? B HIS 119 ? 1_555 ZN ? F ZN . ? B ZN 302 ? 1_555 NE2 ? B HIS 152 ? B HIS 186 ? 1_555 101.3 ? 
16 NE2 ? B HIS 83  ? B HIS 117 ? 1_555 ZN ? F ZN . ? B ZN 302 ? 1_555 O   ? H HOH .   ? B HOH 416 ? 1_555 125.9 ? 
17 ND1 ? B HIS 85  ? B HIS 119 ? 1_555 ZN ? F ZN . ? B ZN 302 ? 1_555 O   ? H HOH .   ? B HOH 416 ? 1_555 92.0  ? 
18 NE2 ? B HIS 152 ? B HIS 186 ? 1_555 ZN ? F ZN . ? B ZN 302 ? 1_555 O   ? H HOH .   ? B HOH 416 ? 1_555 105.2 ? 
19 OD2 ? B ASP 87  ? B ASP 121 ? 1_555 ZN ? E ZN . ? B ZN 301 ? 1_555 SG  ? B CYS 171 ? B CYS 205 ? 1_555 94.2  ? 
20 OD2 ? B ASP 87  ? B ASP 121 ? 1_555 ZN ? E ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 213 ? B HIS 247 ? 1_555 106.1 ? 
21 SG  ? B CYS 171 ? B CYS 205 ? 1_555 ZN ? E ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 213 ? B HIS 247 ? 1_555 93.1  ? 
22 OD2 ? B ASP 87  ? B ASP 121 ? 1_555 ZN ? E ZN . ? B ZN 301 ? 1_555 O   ? H HOH .   ? B HOH 416 ? 1_555 94.6  ? 
23 SG  ? B CYS 171 ? B CYS 205 ? 1_555 ZN ? E ZN . ? B ZN 301 ? 1_555 O   ? H HOH .   ? B HOH 416 ? 1_555 124.5 ? 
24 NE2 ? B HIS 213 ? B HIS 247 ? 1_555 ZN ? E ZN . ? B ZN 301 ? 1_555 O   ? H HOH .   ? B HOH 416 ? 1_555 135.7 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 4 ? 
AA3 ? 8 ? 
AA4 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA3 7 8 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? 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 GLN A 7   ? PHE A 9   ? GLN A 41  PHE A 43  
AA1 2 LEU A 12  ? ALA A 18  ? LEU A 46  ALA A 52  
AA1 3 VAL A 21  ? VAL A 30  ? VAL A 55  VAL A 64  
AA1 4 GLY A 34  ? ASP A 45  ? GLY A 68  ASP A 79  
AA1 5 ARG A 48  ? LEU A 51  ? ARG A 82  LEU A 85  
AA1 6 VAL A 76  ? VAL A 80  ? VAL A 110 VAL A 114 
AA1 7 THR A 102 ? ASN A 105 ? THR A 136 ASN A 139 
AA1 8 HIS A 122 ? LEU A 124 ? HIS A 156 LEU A 158 
AA2 1 LEU A 143 ? PHE A 146 ? LEU A 177 PHE A 180 
AA2 2 THR A 158 ? ILE A 161 ? THR A 192 ILE A 195 
AA2 3 ILE A 166 ? PHE A 168 ? ILE A 200 PHE A 202 
AA2 4 THR A 208 ? ALA A 210 ? THR A 242 ALA A 244 
AA3 1 GLN B 7   ? PHE B 9   ? GLN B 41  PHE B 43  
AA3 2 LEU B 12  ? ALA B 18  ? LEU B 46  ALA B 52  
AA3 3 VAL B 21  ? VAL B 30  ? VAL B 55  VAL B 64  
AA3 4 GLY B 34  ? LYS B 44  ? GLY B 68  LYS B 78  
AA3 5 VAL B 49  ? LEU B 51  ? VAL B 83  LEU B 85  
AA3 6 VAL B 76  ? VAL B 81  ? VAL B 110 VAL B 115 
AA3 7 THR B 102 ? ASN B 105 ? THR B 136 ASN B 139 
AA3 8 HIS B 122 ? LEU B 124 ? HIS B 156 LEU B 158 
AA4 1 LEU B 143 ? PHE B 146 ? LEU B 177 PHE B 180 
AA4 2 THR B 158 ? ILE B 161 ? THR B 192 ILE B 195 
AA4 3 ILE B 166 ? GLY B 170 ? ILE B 200 GLY B 204 
AA4 4 THR B 208 ? MET B 211 ? THR B 242 MET B 245 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 7   ? N GLN A 41  O PHE A 14  ? O PHE A 48  
AA1 2 3 N ARG A 15  ? N ARG A 49  O GLN A 23  ? O GLN A 57  
AA1 3 4 N TRP A 22  ? N TRP A 56  O ILE A 42  ? O ILE A 76  
AA1 4 5 N VAL A 43  ? N VAL A 77  O LEU A 50  ? O LEU A 84  
AA1 5 6 N LEU A 51  ? N LEU A 85  O VAL A 80  ? O VAL A 114 
AA1 6 7 N ALA A 79  ? N ALA A 113 O TYR A 103 ? O TYR A 137 
AA1 7 8 N ALA A 104 ? N ALA A 138 O LEU A 124 ? O LEU A 158 
AA2 1 2 N PHE A 146 ? N PHE A 180 O THR A 158 ? O THR A 192 
AA2 2 3 N VAL A 159 ? N VAL A 193 O PHE A 168 ? O PHE A 202 
AA2 3 4 N ALA A 167 ? N ALA A 201 O ALA A 210 ? O ALA A 244 
AA3 1 2 N PHE B 9   ? N PHE B 43  O LEU B 12  ? O LEU B 46  
AA3 2 3 N VAL B 13  ? N VAL B 47  O THR B 25  ? O THR B 59  
AA3 3 4 N TRP B 22  ? N TRP B 56  O ILE B 42  ? O ILE B 76  
AA3 4 5 N VAL B 43  ? N VAL B 77  O LEU B 50  ? O LEU B 84  
AA3 5 6 N LEU B 51  ? N LEU B 85  O VAL B 80  ? O VAL B 114 
AA3 6 7 N ALA B 79  ? N ALA B 113 O TYR B 103 ? O TYR B 137 
AA3 7 8 N ALA B 104 ? N ALA B 138 O LEU B 124 ? O LEU B 158 
AA4 1 2 N ARG B 144 ? N ARG B 178 O GLY B 160 ? O GLY B 194 
AA4 2 3 N VAL B 159 ? N VAL B 193 O PHE B 168 ? O PHE B 202 
AA4 3 4 N GLY B 169 ? N GLY B 203 O ALA B 210 ? O ALA B 244 
# 
_pdbx_entry_details.entry_id                   8Z7M 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PHE A 67  ? ? -145.10 10.99  
2 1 ASP B 79  ? ? -112.09 64.85  
3 1 ALA B 171 ? ? -113.61 75.29  
4 1 LYS B 211 ? ? -95.07  58.85  
5 1 LYS B 213 ? ? -116.28 56.74  
6 1 SER B 214 ? ? -174.15 141.76 
7 1 ASP B 220 ? ? -87.81  30.19  
8 1 PHE B 237 ? ? -119.00 75.84  
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1  ? refined 25.923 2.148  12.746  0.4329 0.5525 0.5689 -0.0230 -0.0096 0.0892  2.9385 5.0725 4.7950 -0.0051 
1.9917  0.9881  -0.4755 0.1344  0.0284  -0.5007 -0.1302 0.7576  1.1099  0.4061  0.6186  
'X-RAY DIFFRACTION' 2  ? refined 26.860 3.330  3.257   0.4206 0.4433 0.4688 0.0132  -0.0022 0.0260  3.4337 4.1737 2.7944 -0.3663 
1.0996  0.5515  0.1151  -0.1518 -0.1355 0.2851  -0.6340 -0.0542 -0.2361 0.1298  0.5274  
'X-RAY DIFFRACTION' 3  ? refined 16.632 6.127  4.685   0.3783 0.3888 0.6057 -0.0933 0.0494  0.0007  4.2505 6.8460 4.7536 -2.5820 
-1.4705 1.3503  0.1274  -0.2387 -0.1728 -0.2909 -0.5405 0.0025  0.2512  0.2548  -0.0015 
'X-RAY DIFFRACTION' 4  ? refined 15.273 0.556  7.673   0.3466 0.3393 0.5179 -0.0582 0.0416  0.0320  2.4543 3.6856 3.5201 0.2871  
0.4980  -1.0709 0.0270  0.1978  -0.1711 -0.3596 -0.3292 0.3746  0.3767  0.3664  -0.1695 
'X-RAY DIFFRACTION' 5  ? refined 16.215 6.257  -7.194  0.4515 0.4234 0.5028 0.0163  -0.0565 -0.0553 1.3938 5.9485 3.3117 -0.2470 
2.1531  -1.0343 0.1367  -0.0018 -0.1343 0.3509  -0.2322 0.2594  -0.7341 0.5471  0.0143  
'X-RAY DIFFRACTION' 6  ? refined 16.015 17.684 -4.496  0.2701 0.4108 0.4664 -0.0212 0.0431  -0.0192 1.6292 3.5424 2.2345 -1.3063 
1.1883  -1.1450 -0.1020 0.0563  -0.0946 0.0793  -0.4642 0.6103  -0.3046 0.1640  -0.1856 
'X-RAY DIFFRACTION' 7  ? refined 28.306 16.371 3.979   0.3036 0.4393 0.4263 0.0284  0.0264  -0.0299 3.0528 3.7708 3.5344 0.5843  
-0.2755 -0.8407 0.4325  -0.2177 0.0559  0.1587  0.4223  -0.2574 -0.0673 -0.3812 0.1869  
'X-RAY DIFFRACTION' 8  ? refined 32.298 19.095 -8.239  0.2715 0.4625 0.5356 0.0137  0.0529  -0.0294 4.9881 4.0792 3.9868 0.6386  
0.5578  0.5887  -0.0723 0.1871  -0.0663 0.5443  0.1648  -0.1335 -0.4011 0.3122  0.2626  
'X-RAY DIFFRACTION' 9  ? refined 35.036 19.544 -0.955  0.2944 0.3816 0.5313 -0.0249 -0.0025 -0.0741 4.6134 1.6027 2.8789 -0.1632 
0.6206  1.6742  -0.0405 0.1058  -0.0566 0.0995  -0.1031 -0.2882 -0.2156 -0.1501 0.1878  
'X-RAY DIFFRACTION' 10 ? refined 23.818 26.740 -36.696 0.7491 0.8832 0.4513 -0.2540 0.0215  0.1115  2.6666 5.8032 4.7639 -1.4144 
-0.1102 0.8301  -0.0136 -0.3716 0.6862  0.2223  0.0374  -1.4972 -0.2646 -1.0251 1.1560  
'X-RAY DIFFRACTION' 11 ? refined 15.655 27.074 -31.469 0.6392 0.4714 0.4627 -0.0497 -0.0163 0.0093  3.2126 1.2443 4.6288 0.8546  
1.0798  -1.0316 -0.5077 0.0752  0.2272  0.1618  0.1233  -0.5894 -0.3570 -0.5300 0.4281  
'X-RAY DIFFRACTION' 12 ? refined 16.519 35.588 -36.310 0.9645 0.4750 0.5669 -0.1833 0.0162  0.0923  3.4381 3.0386 3.5172 -0.2877 
0.2916  -0.2768 -0.6166 0.2755  0.2998  0.5428  0.6549  -0.4146 -0.5745 -0.7461 0.1681  
'X-RAY DIFFRACTION' 13 ? refined 2.011  30.892 -28.744 0.7028 0.5967 0.6816 0.1664  -0.2220 -0.1359 2.5390 2.5637 4.2518 0.0976  
-0.3892 2.3866  -0.2716 -0.3835 0.4974  -0.3186 0.2091  0.3076  -0.3180 -1.1296 -0.9541 
'X-RAY DIFFRACTION' 14 ? refined -1.096 24.784 -42.000 0.9735 0.8066 0.5080 0.1157  -0.2910 -0.0571 5.2162 2.9369 2.4936 -1.2070 
-0.7300 1.1374  -0.2032 -0.1658 0.4698  1.4456  0.3024  0.5480  -0.9407 -1.4854 -1.3041 
'X-RAY DIFFRACTION' 15 ? refined 5.955  17.558 -33.398 0.4565 0.5041 0.4524 -0.0229 -0.0205 -0.1104 3.5275 4.0858 5.2763 0.5602  
0.8515  0.5581  -0.1425 0.0985  0.0788  -0.0138 -0.1967 0.5282  -0.2340 0.7423  -0.0028 
'X-RAY DIFFRACTION' 16 ? refined 8.063  11.571 -21.516 0.5016 0.6943 0.6138 -0.0392 -0.1210 -0.0719 6.0015 5.2562 6.9925 -0.9140 
-0.8183 0.4115  -0.2409 0.3196  -0.0078 -2.0131 1.1777  -0.1629 1.0836  0.8288  0.0082  
'X-RAY DIFFRACTION' 17 ? refined 8.018  12.085 -34.678 0.4785 0.4841 0.5127 -0.0143 0.0028  -0.0452 3.9756 5.0903 2.9757 0.8163  
2.0314  0.6185  0.4940  -0.3364 -0.1689 0.2589  -0.3819 0.2687  -0.4055 0.1288  -0.1507 
'X-RAY DIFFRACTION' 18 ? refined 6.720  4.598  -26.279 0.9369 0.6972 0.6057 -0.3163 -0.0502 -0.0690 1.9816 5.3103 1.8224 0.2850  
1.2772  -2.0757 0.6099  -0.1761 -0.1712 -0.7580 0.3080  -0.4939 0.4370  1.7910  0.5535  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1  1  A 42  A 57  '( CHAIN A AND RESID 42:57 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  A 58  A 82  '( CHAIN A AND RESID 58:82 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  A 83  A 94  '( CHAIN A AND RESID 83:94 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  A 95  A 118 '( CHAIN A AND RESID 95:118 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  A 119 A 152 '( CHAIN A AND RESID 119:152 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  A 153 A 194 '( CHAIN A AND RESID 153:194 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  A 195 A 215 '( CHAIN A AND RESID 195:215 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  A 216 A 239 '( CHAIN A AND RESID 216:239 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  A 240 A 270 '( CHAIN A AND RESID 240:270 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 B 43  B 57  '( CHAIN B AND RESID 43:57 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 B 58  B 94  '( CHAIN B AND RESID 58:94 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 B 95  B 118 '( CHAIN B AND RESID 95:118 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 13 13 B 119 B 166 '( CHAIN B AND RESID 119:166 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 14 14 B 167 B 183 '( CHAIN B AND RESID 167:183 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 15 15 B 184 B 212 '( CHAIN B AND RESID 184:212 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 16 16 B 213 B 227 '( CHAIN B AND RESID 213:227 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 17 17 B 228 B 255 '( CHAIN B AND RESID 228:255 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 18 18 B 256 B 269 '( CHAIN B AND RESID 256:269 )' ? ? ? ? ? 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       482 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.98 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 35  ? A GLY 1   
2  1 Y 1 A PRO 36  ? A PRO 2   
3  1 Y 1 A LEU 37  ? A LEU 3   
4  1 Y 1 A GLY 38  ? A GLY 4   
5  1 Y 1 A PRO 271 ? A PRO 237 
6  1 Y 1 A HIS 272 ? A HIS 238 
7  1 Y 1 A ARG 273 ? A ARG 239 
8  1 Y 1 A ASP 274 ? A ASP 240 
9  1 Y 1 B GLY 35  ? B GLY 1   
10 1 Y 1 B PRO 36  ? B PRO 2   
11 1 Y 1 B LEU 37  ? B LEU 3   
12 1 Y 1 B GLY 38  ? B GLY 4   
13 1 Y 1 B SER 39  ? B SER 5   
14 1 Y 1 B ARG 270 ? B ARG 236 
15 1 Y 1 B PRO 271 ? B PRO 237 
16 1 Y 1 B HIS 272 ? B HIS 238 
17 1 Y 1 B ARG 273 ? B ARG 239 
18 1 Y 1 B ASP 274 ? B ASP 240 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
PHE N    N  N N 250 
PHE CA   C  N S 251 
PHE C    C  N N 252 
PHE O    O  N N 253 
PHE CB   C  N N 254 
PHE CG   C  Y N 255 
PHE CD1  C  Y N 256 
PHE CD2  C  Y N 257 
PHE CE1  C  Y N 258 
PHE CE2  C  Y N 259 
PHE CZ   C  Y N 260 
PHE OXT  O  N N 261 
PHE H    H  N N 262 
PHE H2   H  N N 263 
PHE HA   H  N N 264 
PHE HB2  H  N N 265 
PHE HB3  H  N N 266 
PHE HD1  H  N N 267 
PHE HD2  H  N N 268 
PHE HE1  H  N N 269 
PHE HE2  H  N N 270 
PHE HZ   H  N N 271 
PHE HXT  H  N N 272 
PRO N    N  N N 273 
PRO CA   C  N S 274 
PRO C    C  N N 275 
PRO O    O  N N 276 
PRO CB   C  N N 277 
PRO CG   C  N N 278 
PRO CD   C  N N 279 
PRO OXT  O  N N 280 
PRO H    H  N N 281 
PRO HA   H  N N 282 
PRO HB2  H  N N 283 
PRO HB3  H  N N 284 
PRO HG2  H  N N 285 
PRO HG3  H  N N 286 
PRO HD2  H  N N 287 
PRO HD3  H  N N 288 
PRO HXT  H  N N 289 
SER N    N  N N 290 
SER CA   C  N S 291 
SER C    C  N N 292 
SER O    O  N N 293 
SER CB   C  N N 294 
SER OG   O  N N 295 
SER OXT  O  N N 296 
SER H    H  N N 297 
SER H2   H  N N 298 
SER HA   H  N N 299 
SER HB2  H  N N 300 
SER HB3  H  N N 301 
SER HG   H  N N 302 
SER HXT  H  N N 303 
THR N    N  N N 304 
THR CA   C  N S 305 
THR C    C  N N 306 
THR O    O  N N 307 
THR CB   C  N R 308 
THR OG1  O  N N 309 
THR CG2  C  N N 310 
THR OXT  O  N N 311 
THR H    H  N N 312 
THR H2   H  N N 313 
THR HA   H  N N 314 
THR HB   H  N N 315 
THR HG1  H  N N 316 
THR HG21 H  N N 317 
THR HG22 H  N N 318 
THR HG23 H  N N 319 
THR HXT  H  N N 320 
TRP N    N  N N 321 
TRP CA   C  N S 322 
TRP C    C  N N 323 
TRP O    O  N N 324 
TRP CB   C  N N 325 
TRP CG   C  Y N 326 
TRP CD1  C  Y N 327 
TRP CD2  C  Y N 328 
TRP NE1  N  Y N 329 
TRP CE2  C  Y N 330 
TRP CE3  C  Y N 331 
TRP CZ2  C  Y N 332 
TRP CZ3  C  Y N 333 
TRP CH2  C  Y N 334 
TRP OXT  O  N N 335 
TRP H    H  N N 336 
TRP H2   H  N N 337 
TRP HA   H  N N 338 
TRP HB2  H  N N 339 
TRP HB3  H  N N 340 
TRP HD1  H  N N 341 
TRP HE1  H  N N 342 
TRP HE3  H  N N 343 
TRP HZ2  H  N N 344 
TRP HZ3  H  N N 345 
TRP HH2  H  N N 346 
TRP HXT  H  N N 347 
TYR N    N  N N 348 
TYR CA   C  N S 349 
TYR C    C  N N 350 
TYR O    O  N N 351 
TYR CB   C  N N 352 
TYR CG   C  Y N 353 
TYR CD1  C  Y N 354 
TYR CD2  C  Y N 355 
TYR CE1  C  Y N 356 
TYR CE2  C  Y N 357 
TYR CZ   C  Y N 358 
TYR OH   O  N N 359 
TYR OXT  O  N N 360 
TYR H    H  N N 361 
TYR H2   H  N N 362 
TYR HA   H  N N 363 
TYR HB2  H  N N 364 
TYR HB3  H  N N 365 
TYR HD1  H  N N 366 
TYR HD2  H  N N 367 
TYR HE1  H  N N 368 
TYR HE2  H  N N 369 
TYR HH   H  N N 370 
TYR HXT  H  N N 371 
VAL N    N  N N 372 
VAL CA   C  N S 373 
VAL C    C  N N 374 
VAL O    O  N N 375 
VAL CB   C  N N 376 
VAL CG1  C  N N 377 
VAL CG2  C  N N 378 
VAL OXT  O  N N 379 
VAL H    H  N N 380 
VAL H2   H  N N 381 
VAL HA   H  N N 382 
VAL HB   H  N N 383 
VAL HG11 H  N N 384 
VAL HG12 H  N N 385 
VAL HG13 H  N N 386 
VAL HG21 H  N N 387 
VAL HG22 H  N N 388 
VAL HG23 H  N N 389 
VAL HXT  H  N N 390 
ZN  ZN   ZN N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           82170680 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8Z7M 
_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]   0.020425 
_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]   0.009482 
_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]   0.009402 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 5   ? 32.513  2.791   17.985  1.00 104.88 ? 39  SER A N   1 
ATOM   2    C  CA  . SER A 1 5   ? 31.224  3.425   17.735  1.00 98.07  ? 39  SER A CA  1 
ATOM   3    C  C   . SER A 1 5   ? 30.512  2.768   16.557  1.00 90.05  ? 39  SER A C   1 
ATOM   4    O  O   . SER A 1 5   ? 29.282  2.722   16.513  1.00 93.33  ? 39  SER A O   1 
ATOM   5    C  CB  . SER A 1 5   ? 31.402  4.922   17.477  1.00 107.10 ? 39  SER A CB  1 
ATOM   6    O  OG  . SER A 1 5   ? 31.924  5.574   18.622  1.00 120.33 ? 39  SER A OG  1 
ATOM   7    N  N   . ASP A 1 6   ? 31.294  2.263   15.603  1.00 90.52  ? 40  ASP A N   1 
ATOM   8    C  CA  . ASP A 1 6   ? 30.738  1.549   14.460  1.00 93.20  ? 40  ASP A CA  1 
ATOM   9    C  C   . ASP A 1 6   ? 30.010  0.292   14.921  1.00 89.59  ? 40  ASP A C   1 
ATOM   10   O  O   . ASP A 1 6   ? 30.638  -0.644  15.425  1.00 91.49  ? 40  ASP A O   1 
ATOM   11   C  CB  . ASP A 1 6   ? 31.836  1.178   13.459  1.00 91.16  ? 40  ASP A CB  1 
ATOM   12   C  CG  . ASP A 1 6   ? 32.522  2.390   12.864  1.00 95.98  ? 40  ASP A CG  1 
ATOM   13   O  OD1 . ASP A 1 6   ? 32.559  3.442   13.533  1.00 106.51 ? 40  ASP A OD1 1 
ATOM   14   O  OD2 . ASP A 1 6   ? 33.017  2.293   11.722  1.00 88.66  ? 40  ASP A OD2 1 
ATOM   15   N  N   . GLN A 1 7   ? 28.691  0.263   14.761  1.00 74.93  ? 41  GLN A N   1 
ATOM   16   C  CA  . GLN A 1 7   ? 27.888  -0.900  15.111  1.00 71.15  ? 41  GLN A CA  1 
ATOM   17   C  C   . GLN A 1 7   ? 27.620  -1.718  13.855  1.00 64.84  ? 41  GLN A C   1 
ATOM   18   O  O   . GLN A 1 7   ? 27.188  -1.174  12.833  1.00 60.44  ? 41  GLN A O   1 
ATOM   19   C  CB  . GLN A 1 7   ? 26.571  -0.487  15.768  1.00 74.02  ? 41  GLN A CB  1 
ATOM   20   C  CG  . GLN A 1 7   ? 25.598  -1.639  15.968  1.00 87.71  ? 41  GLN A CG  1 
ATOM   21   C  CD  . GLN A 1 7   ? 24.163  -1.176  16.127  1.00 98.60  ? 41  GLN A CD  1 
ATOM   22   O  OE1 . GLN A 1 7   ? 23.900  0.003   16.362  1.00 96.66  ? 41  GLN A OE1 1 
ATOM   23   N  NE2 . GLN A 1 7   ? 23.224  -2.108  16.002  1.00 80.85  ? 41  GLN A NE2 1 
ATOM   24   N  N   . ARG A 1 8   ? 27.878  -3.019  13.934  1.00 53.17  ? 42  ARG A N   1 
ATOM   25   C  CA  . ARG A 1 8   ? 27.734  -3.913  12.795  1.00 57.36  ? 42  ARG A CA  1 
ATOM   26   C  C   . ARG A 1 8   ? 26.378  -4.604  12.830  1.00 55.88  ? 42  ARG A C   1 
ATOM   27   O  O   . ARG A 1 8   ? 25.927  -5.064  13.883  1.00 57.94  ? 42  ARG A O   1 
ATOM   28   C  CB  . ARG A 1 8   ? 28.854  -4.956  12.776  1.00 54.14  ? 42  ARG A CB  1 
ATOM   29   C  CG  . ARG A 1 8   ? 29.990  -4.606  11.831  1.00 63.69  ? 42  ARG A CG  1 
ATOM   30   C  CD  . ARG A 1 8   ? 30.690  -5.848  11.309  1.00 71.43  ? 42  ARG A CD  1 
ATOM   31   N  NE  . ARG A 1 8   ? 31.940  -5.518  10.637  1.00 68.97  ? 42  ARG A NE  1 
ATOM   32   C  CZ  . ARG A 1 8   ? 32.730  -6.403  10.044  1.00 93.70  ? 42  ARG A CZ  1 
ATOM   33   N  NH1 . ARG A 1 8   ? 32.430  -7.692  10.023  1.00 99.61  ? 42  ARG A NH1 1 
ATOM   34   N  NH2 . ARG A 1 8   ? 33.848  -5.986  9.458   1.00 103.89 ? 42  ARG A NH2 1 
ATOM   35   N  N   . PHE A 1 9   ? 25.732  -4.670  11.666  1.00 54.94  ? 43  PHE A N   1 
ATOM   36   C  CA  . PHE A 1 9   ? 24.424  -5.310  11.538  1.00 53.17  ? 43  PHE A CA  1 
ATOM   37   C  C   . PHE A 1 9   ? 24.379  -5.953  10.155  1.00 60.13  ? 43  PHE A C   1 
ATOM   38   O  O   . PHE A 1 9   ? 24.220  -5.253  9.150   1.00 52.75  ? 43  PHE A O   1 
ATOM   39   C  CB  . PHE A 1 9   ? 23.298  -4.304  11.735  1.00 45.93  ? 43  PHE A CB  1 
ATOM   40   C  CG  . PHE A 1 9   ? 21.923  -4.876  11.528  1.00 49.63  ? 43  PHE A CG  1 
ATOM   41   C  CD1 . PHE A 1 9   ? 21.244  -5.475  12.577  1.00 50.31  ? 43  PHE A CD1 1 
ATOM   42   C  CD2 . PHE A 1 9   ? 21.306  -4.810  10.290  1.00 48.74  ? 43  PHE A CD2 1 
ATOM   43   C  CE1 . PHE A 1 9   ? 19.979  -5.999  12.393  1.00 52.69  ? 43  PHE A CE1 1 
ATOM   44   C  CE2 . PHE A 1 9   ? 20.041  -5.333  10.100  1.00 51.17  ? 43  PHE A CE2 1 
ATOM   45   C  CZ  . PHE A 1 9   ? 19.377  -5.928  11.153  1.00 52.86  ? 43  PHE A CZ  1 
ATOM   46   N  N   . GLY A 1 10  ? 24.525  -7.275  10.113  1.00 52.95  ? 44  GLY A N   1 
ATOM   47   C  CA  . GLY A 1 10  ? 24.546  -7.964  8.836   1.00 54.00  ? 44  GLY A CA  1 
ATOM   48   C  C   . GLY A 1 10  ? 25.745  -7.554  8.006   1.00 57.36  ? 44  GLY A C   1 
ATOM   49   O  O   . GLY A 1 10  ? 26.875  -7.464  8.499   1.00 57.19  ? 44  GLY A O   1 
ATOM   50   N  N   . ASP A 1 11  ? 25.499  -7.293  6.725   1.00 63.02  ? 45  ASP A N   1 
ATOM   51   C  CA  . ASP A 1 11  ? 26.543  -6.862  5.805   1.00 66.24  ? 45  ASP A CA  1 
ATOM   52   C  C   . ASP A 1 11  ? 26.781  -5.357  5.839   1.00 58.40  ? 45  ASP A C   1 
ATOM   53   O  O   . ASP A 1 11  ? 27.483  -4.838  4.965   1.00 63.35  ? 45  ASP A O   1 
ATOM   54   C  CB  . ASP A 1 11  ? 26.197  -7.294  4.376   1.00 74.49  ? 45  ASP A CB  1 
ATOM   55   C  CG  . ASP A 1 11  ? 25.756  -8.743  4.293   1.00 80.06  ? 45  ASP A CG  1 
ATOM   56   O  OD1 . ASP A 1 11  ? 26.054  -9.514  5.229   1.00 88.80  ? 45  ASP A OD1 1 
ATOM   57   O  OD2 . ASP A 1 11  ? 25.108  -9.110  3.290   1.00 78.71  ? 45  ASP A OD2 1 
ATOM   58   N  N   . LEU A 1 12  ? 26.221  -4.650  6.816   1.00 60.63  ? 46  LEU A N   1 
ATOM   59   C  CA  . LEU A 1 12  ? 26.310  -3.200  6.885   1.00 53.16  ? 46  LEU A CA  1 
ATOM   60   C  C   . LEU A 1 12  ? 26.920  -2.764  8.211   1.00 52.65  ? 46  LEU A C   1 
ATOM   61   O  O   . LEU A 1 12  ? 27.041  -3.542  9.161   1.00 50.42  ? 46  LEU A O   1 
ATOM   62   C  CB  . LEU A 1 12  ? 24.930  -2.552  6.712   1.00 52.14  ? 46  LEU A CB  1 
ATOM   63   C  CG  . LEU A 1 12  ? 23.967  -3.209  5.724   1.00 53.25  ? 46  LEU A CG  1 
ATOM   64   C  CD1 . LEU A 1 12  ? 22.551  -2.737  5.990   1.00 64.55  ? 46  LEU A CD1 1 
ATOM   65   C  CD2 . LEU A 1 12  ? 24.377  -2.911  4.293   1.00 61.90  ? 46  LEU A CD2 1 
ATOM   66   N  N   . VAL A 1 13  ? 27.305  -1.491  8.256   1.00 55.49  ? 47  VAL A N   1 
ATOM   67   C  CA  . VAL A 1 13  ? 27.833  -0.849  9.453   1.00 48.83  ? 47  VAL A CA  1 
ATOM   68   C  C   . VAL A 1 13  ? 26.980  0.377   9.745   1.00 50.36  ? 47  VAL A C   1 
ATOM   69   O  O   . VAL A 1 13  ? 26.577  1.096   8.825   1.00 50.30  ? 47  VAL A O   1 
ATOM   70   C  CB  . VAL A 1 13  ? 29.317  -0.460  9.285   1.00 45.21  ? 47  VAL A CB  1 
ATOM   71   C  CG1 . VAL A 1 13  ? 29.875  0.103   10.582  1.00 46.95  ? 47  VAL A CG1 1 
ATOM   72   C  CG2 . VAL A 1 13  ? 30.135  -1.658  8.827   1.00 40.03  ? 47  VAL A CG2 1 
ATOM   73   N  N   . PHE A 1 14  ? 26.697  0.607   11.025  1.00 47.59  ? 48  PHE A N   1 
ATOM   74   C  CA  . PHE A 1 14  ? 25.886  1.736   11.453  1.00 47.94  ? 48  PHE A CA  1 
ATOM   75   C  C   . PHE A 1 14  ? 26.639  2.536   12.505  1.00 52.32  ? 48  PHE A C   1 
ATOM   76   O  O   . PHE A 1 14  ? 27.254  1.964   13.411  1.00 55.84  ? 48  PHE A O   1 
ATOM   77   C  CB  . PHE A 1 14  ? 24.534  1.274   12.012  1.00 50.41  ? 48  PHE A CB  1 
ATOM   78   C  CG  . PHE A 1 14  ? 23.609  0.707   10.972  1.00 52.94  ? 48  PHE A CG  1 
ATOM   79   C  CD1 . PHE A 1 14  ? 23.722  -0.614  10.571  1.00 52.51  ? 48  PHE A CD1 1 
ATOM   80   C  CD2 . PHE A 1 14  ? 22.626  1.495   10.397  1.00 49.42  ? 48  PHE A CD2 1 
ATOM   81   C  CE1 . PHE A 1 14  ? 22.873  -1.138  9.613   1.00 53.82  ? 48  PHE A CE1 1 
ATOM   82   C  CE2 . PHE A 1 14  ? 21.773  0.977   9.441   1.00 44.11  ? 48  PHE A CE2 1 
ATOM   83   C  CZ  . PHE A 1 14  ? 21.898  -0.341  9.047   1.00 48.54  ? 48  PHE A CZ  1 
ATOM   84   N  N   . ARG A 1 15  ? 26.590  3.860   12.376  1.00 51.21  ? 49  ARG A N   1 
ATOM   85   C  CA  . ARG A 1 15  ? 27.224  4.763   13.324  1.00 52.58  ? 49  ARG A CA  1 
ATOM   86   C  C   . ARG A 1 15  ? 26.276  5.907   13.644  1.00 48.54  ? 49  ARG A C   1 
ATOM   87   O  O   . ARG A 1 15  ? 25.649  6.475   12.745  1.00 44.38  ? 49  ARG A O   1 
ATOM   88   C  CB  . ARG A 1 15  ? 28.544  5.325   12.783  1.00 52.86  ? 49  ARG A CB  1 
ATOM   89   C  CG  . ARG A 1 15  ? 29.364  6.075   13.824  1.00 71.76  ? 49  ARG A CG  1 
ATOM   90   C  CD  . ARG A 1 15  ? 30.848  6.019   13.512  1.00 75.54  ? 49  ARG A CD  1 
ATOM   91   N  NE  . ARG A 1 15  ? 31.343  7.265   12.940  1.00 72.22  ? 49  ARG A NE  1 
ATOM   92   C  CZ  . ARG A 1 15  ? 31.879  8.252   13.645  1.00 84.36  ? 49  ARG A CZ  1 
ATOM   93   N  NH1 . ARG A 1 15  ? 32.009  8.172   14.959  1.00 82.70  ? 49  ARG A NH1 1 
ATOM   94   N  NH2 . ARG A 1 15  ? 32.300  9.345   13.014  1.00 69.77  ? 49  ARG A NH2 1 
ATOM   95   N  N   . GLN A 1 16  ? 26.179  6.241   14.928  1.00 48.53  ? 50  GLN A N   1 
ATOM   96   C  CA  . GLN A 1 16  ? 25.351  7.357   15.372  1.00 52.50  ? 50  GLN A CA  1 
ATOM   97   C  C   . GLN A 1 16  ? 26.158  8.644   15.260  1.00 52.05  ? 50  GLN A C   1 
ATOM   98   O  O   . GLN A 1 16  ? 27.150  8.828   15.974  1.00 59.47  ? 50  GLN A O   1 
ATOM   99   C  CB  . GLN A 1 16  ? 24.869  7.132   16.803  1.00 47.09  ? 50  GLN A CB  1 
ATOM   100  C  CG  . GLN A 1 16  ? 23.904  8.195   17.302  1.00 53.76  ? 50  GLN A CG  1 
ATOM   101  C  CD  . GLN A 1 16  ? 23.069  7.725   18.476  1.00 51.70  ? 50  GLN A CD  1 
ATOM   102  O  OE1 . GLN A 1 16  ? 23.284  6.637   19.011  1.00 56.61  ? 50  GLN A OE1 1 
ATOM   103  N  NE2 . GLN A 1 16  ? 22.110  8.547   18.886  1.00 53.56  ? 50  GLN A NE2 1 
ATOM   104  N  N   . LEU A 1 17  ? 25.740  9.533   14.361  1.00 46.86  ? 51  LEU A N   1 
ATOM   105  C  CA  . LEU A 1 17  ? 26.419  10.808  14.175  1.00 53.88  ? 51  LEU A CA  1 
ATOM   106  C  C   . LEU A 1 17  ? 25.941  11.881  15.141  1.00 48.18  ? 51  LEU A C   1 
ATOM   107  O  O   . LEU A 1 17  ? 26.690  12.824  15.420  1.00 52.72  ? 51  LEU A O   1 
ATOM   108  C  CB  . LEU A 1 17  ? 26.228  11.301  12.737  1.00 48.47  ? 51  LEU A CB  1 
ATOM   109  C  CG  . LEU A 1 17  ? 26.747  10.378  11.634  1.00 46.09  ? 51  LEU A CG  1 
ATOM   110  C  CD1 . LEU A 1 17  ? 26.693  11.072  10.282  1.00 52.75  ? 51  LEU A CD1 1 
ATOM   111  C  CD2 . LEU A 1 17  ? 28.160  9.914   11.946  1.00 52.13  ? 51  LEU A CD2 1 
ATOM   112  N  N   . ALA A 1 18  ? 24.722  11.754  15.657  1.00 53.08  ? 52  ALA A N   1 
ATOM   113  C  CA  . ALA A 1 18  ? 24.112  12.723  16.555  1.00 55.45  ? 52  ALA A CA  1 
ATOM   114  C  C   . ALA A 1 18  ? 22.825  12.125  17.108  1.00 55.19  ? 52  ALA A C   1 
ATOM   115  O  O   . ALA A 1 18  ? 22.365  11.091  16.605  1.00 55.12  ? 52  ALA A O   1 
ATOM   116  C  CB  . ALA A 1 18  ? 23.831  14.038  15.822  1.00 52.13  ? 52  ALA A CB  1 
ATOM   117  N  N   . PRO A 1 19  ? 22.227  12.712  18.143  1.00 59.76  ? 53  PRO A N   1 
ATOM   118  C  CA  . PRO A 1 19  ? 20.873  12.295  18.527  1.00 61.18  ? 53  PRO A CA  1 
ATOM   119  C  C   . PRO A 1 19  ? 19.913  12.474  17.360  1.00 60.65  ? 53  PRO A C   1 
ATOM   120  O  O   . PRO A 1 19  ? 19.838  13.546  16.756  1.00 64.46  ? 53  PRO A O   1 
ATOM   121  C  CB  . PRO A 1 19  ? 20.528  13.221  19.702  1.00 59.68  ? 53  PRO A CB  1 
ATOM   122  C  CG  . PRO A 1 19  ? 21.572  14.306  19.682  1.00 65.41  ? 53  PRO A CG  1 
ATOM   123  C  CD  . PRO A 1 19  ? 22.792  13.674  19.103  1.00 57.13  ? 53  PRO A CD  1 
ATOM   124  N  N   . ASN A 1 20  ? 19.202  11.394  17.031  1.00 55.58  ? 54  ASN A N   1 
ATOM   125  C  CA  . ASN A 1 20  ? 18.213  11.288  15.954  1.00 56.41  ? 54  ASN A CA  1 
ATOM   126  C  C   . ASN A 1 20  ? 18.845  11.210  14.570  1.00 51.43  ? 54  ASN A C   1 
ATOM   127  O  O   . ASN A 1 20  ? 18.114  11.310  13.574  1.00 51.43  ? 54  ASN A O   1 
ATOM   128  C  CB  . ASN A 1 20  ? 17.205  12.443  15.959  1.00 57.98  ? 54  ASN A CB  1 
ATOM   129  C  CG  . ASN A 1 20  ? 16.514  12.609  17.296  1.00 81.82  ? 54  ASN A CG  1 
ATOM   130  O  OD1 . ASN A 1 20  ? 15.768  11.736  17.736  1.00 87.54  ? 54  ASN A OD1 1 
ATOM   131  N  ND2 . ASN A 1 20  ? 16.760  13.737  17.952  1.00 78.05  ? 54  ASN A ND2 1 
ATOM   132  N  N   . VAL A 1 21  ? 20.162  11.038  14.459  1.00 41.50  ? 55  VAL A N   1 
ATOM   133  C  CA  . VAL A 1 21  ? 20.830  10.919  13.167  1.00 44.70  ? 55  VAL A CA  1 
ATOM   134  C  C   . VAL A 1 21  ? 21.800  9.748   13.220  1.00 43.84  ? 55  VAL A C   1 
ATOM   135  O  O   . VAL A 1 21  ? 22.659  9.686   14.108  1.00 51.52  ? 55  VAL A O   1 
ATOM   136  C  CB  . VAL A 1 21  ? 21.576  12.209  12.772  1.00 45.65  ? 55  VAL A CB  1 
ATOM   137  C  CG1 . VAL A 1 21  ? 22.239  12.031  11.413  1.00 44.22  ? 55  VAL A CG1 1 
ATOM   138  C  CG2 . VAL A 1 21  ? 20.629  13.399  12.749  1.00 41.15  ? 55  VAL A CG2 1 
ATOM   139  N  N   . TRP A 1 22  ? 21.670  8.829   12.267  1.00 40.26  ? 56  TRP A N   1 
ATOM   140  C  CA  . TRP A 1 22  ? 22.574  7.698   12.133  1.00 42.52  ? 56  TRP A CA  1 
ATOM   141  C  C   . TRP A 1 22  ? 23.084  7.625   10.701  1.00 46.08  ? 56  TRP A C   1 
ATOM   142  O  O   . TRP A 1 22  ? 22.454  8.128   9.768   1.00 43.80  ? 56  TRP A O   1 
ATOM   143  C  CB  . TRP A 1 22  ? 21.894  6.374   12.510  1.00 39.25  ? 56  TRP A CB  1 
ATOM   144  C  CG  . TRP A 1 22  ? 21.487  6.294   13.945  1.00 42.94  ? 56  TRP A CG  1 
ATOM   145  C  CD1 . TRP A 1 22  ? 22.177  5.699   14.962  1.00 47.27  ? 56  TRP A CD1 1 
ATOM   146  C  CD2 . TRP A 1 22  ? 20.291  6.823   14.528  1.00 43.82  ? 56  TRP A CD2 1 
ATOM   147  N  NE1 . TRP A 1 22  ? 21.486  5.828   16.142  1.00 51.81  ? 56  TRP A NE1 1 
ATOM   148  C  CE2 . TRP A 1 22  ? 20.324  6.514   15.902  1.00 45.44  ? 56  TRP A CE2 1 
ATOM   149  C  CE3 . TRP A 1 22  ? 19.196  7.529   14.021  1.00 40.86  ? 56  TRP A CE3 1 
ATOM   150  C  CZ2 . TRP A 1 22  ? 19.304  6.886   16.775  1.00 39.51  ? 56  TRP A CZ2 1 
ATOM   151  C  CZ3 . TRP A 1 22  ? 18.185  7.897   14.888  1.00 45.43  ? 56  TRP A CZ3 1 
ATOM   152  C  CH2 . TRP A 1 22  ? 18.246  7.576   16.250  1.00 47.48  ? 56  TRP A CH2 1 
ATOM   153  N  N   . GLN A 1 23  ? 24.240  6.986   10.538  1.00 39.96  ? 57  GLN A N   1 
ATOM   154  C  CA  . GLN A 1 23  ? 24.857  6.786   9.234   1.00 41.46  ? 57  GLN A CA  1 
ATOM   155  C  C   . GLN A 1 23  ? 24.918  5.296   8.937   1.00 42.84  ? 57  GLN A C   1 
ATOM   156  O  O   . GLN A 1 23  ? 25.449  4.521   9.740   1.00 37.99  ? 57  GLN A O   1 
ATOM   157  C  CB  . GLN A 1 23  ? 26.261  7.395   9.188   1.00 41.83  ? 57  GLN A CB  1 
ATOM   158  C  CG  . GLN A 1 23  ? 26.909  7.361   7.814   1.00 45.50  ? 57  GLN A CG  1 
ATOM   159  C  CD  . GLN A 1 23  ? 28.421  7.415   7.881   1.00 45.79  ? 57  GLN A CD  1 
ATOM   160  O  OE1 . GLN A 1 23  ? 29.051  6.628   8.587   1.00 48.98  ? 57  GLN A OE1 1 
ATOM   161  N  NE2 . GLN A 1 23  ? 29.014  8.348   7.144   1.00 39.58  ? 57  GLN A NE2 1 
ATOM   162  N  N   . HIS A 1 24  ? 24.370  4.897   7.794   1.00 46.20  ? 58  HIS A N   1 
ATOM   163  C  CA  . HIS A 1 24  ? 24.397  3.509   7.357   1.00 48.97  ? 58  HIS A CA  1 
ATOM   164  C  C   . HIS A 1 24  ? 25.403  3.349   6.225   1.00 46.52  ? 58  HIS A C   1 
ATOM   165  O  O   . HIS A 1 24  ? 25.474  4.187   5.320   1.00 44.97  ? 58  HIS A O   1 
ATOM   166  C  CB  . HIS A 1 24  ? 23.006  3.033   6.916   1.00 37.32  ? 58  HIS A CB  1 
ATOM   167  C  CG  . HIS A 1 24  ? 22.490  3.700   5.678   1.00 41.63  ? 58  HIS A CG  1 
ATOM   168  N  ND1 . HIS A 1 24  ? 22.921  3.362   4.413   1.00 48.02  ? 58  HIS A ND1 1 
ATOM   169  C  CD2 . HIS A 1 24  ? 21.560  4.670   5.511   1.00 39.96  ? 58  HIS A CD2 1 
ATOM   170  C  CE1 . HIS A 1 24  ? 22.287  4.103   3.521   1.00 43.36  ? 58  HIS A CE1 1 
ATOM   171  N  NE2 . HIS A 1 24  ? 21.455  4.904   4.161   1.00 39.60  ? 58  HIS A NE2 1 
ATOM   172  N  N   . THR A 1 25  ? 26.183  2.271   6.285   1.00 36.72  ? 59  THR A N   1 
ATOM   173  C  CA  . THR A 1 25  ? 27.256  2.025   5.330   1.00 44.01  ? 59  THR A CA  1 
ATOM   174  C  C   . THR A 1 25  ? 27.069  0.649   4.710   1.00 49.41  ? 59  THR A C   1 
ATOM   175  O  O   . THR A 1 25  ? 26.977  -0.351  5.429   1.00 44.03  ? 59  THR A O   1 
ATOM   176  C  CB  . THR A 1 25  ? 28.628  2.123   6.003   1.00 46.97  ? 59  THR A CB  1 
ATOM   177  O  OG1 . THR A 1 25  ? 28.776  3.416   6.604   1.00 45.17  ? 59  THR A OG1 1 
ATOM   178  C  CG2 . THR A 1 25  ? 29.739  1.913   4.983   1.00 44.05  ? 59  THR A CG2 1 
ATOM   179  N  N   . SER A 1 26  ? 27.015  0.602   3.381   1.00 54.02  ? 60  SER A N   1 
ATOM   180  C  CA  . SER A 1 26  ? 26.951  -0.643  2.633   1.00 43.21  ? 60  SER A CA  1 
ATOM   181  C  C   . SER A 1 26  ? 28.212  -0.791  1.793   1.00 44.55  ? 60  SER A C   1 
ATOM   182  O  O   . SER A 1 26  ? 28.832  0.200   1.396   1.00 45.69  ? 60  SER A O   1 
ATOM   183  C  CB  . SER A 1 26  ? 25.711  -0.697  1.732   1.00 39.40  ? 60  SER A CB  1 
ATOM   184  O  OG  . SER A 1 26  ? 25.458  0.562   1.133   1.00 54.39  ? 60  SER A OG  1 
ATOM   185  N  N   . PHE A 1 27  ? 28.587  -2.038  1.525   1.00 49.03  ? 61  PHE A N   1 
ATOM   186  C  CA  . PHE A 1 27  ? 29.817  -2.347  0.812   1.00 49.52  ? 61  PHE A CA  1 
ATOM   187  C  C   . PHE A 1 27  ? 29.507  -3.114  -0.466  1.00 49.10  ? 61  PHE A C   1 
ATOM   188  O  O   . PHE A 1 27  ? 28.536  -3.874  -0.536  1.00 59.31  ? 61  PHE A O   1 
ATOM   189  C  CB  . PHE A 1 27  ? 30.778  -3.159  1.691   1.00 53.11  ? 61  PHE A CB  1 
ATOM   190  C  CG  . PHE A 1 27  ? 31.088  -2.508  3.010   1.00 44.29  ? 61  PHE A CG  1 
ATOM   191  C  CD1 . PHE A 1 27  ? 30.275  -2.720  4.111   1.00 48.36  ? 61  PHE A CD1 1 
ATOM   192  C  CD2 . PHE A 1 27  ? 32.191  -1.682  3.146   1.00 44.18  ? 61  PHE A CD2 1 
ATOM   193  C  CE1 . PHE A 1 27  ? 30.557  -2.120  5.323   1.00 46.01  ? 61  PHE A CE1 1 
ATOM   194  C  CE2 . PHE A 1 27  ? 32.478  -1.080  4.357   1.00 43.24  ? 61  PHE A CE2 1 
ATOM   195  C  CZ  . PHE A 1 27  ? 31.660  -1.299  5.446   1.00 45.31  ? 61  PHE A CZ  1 
ATOM   196  N  N   . MET A 1 28  ? 30.346  -2.906  -1.478  1.00 47.47  ? 62  MET A N   1 
ATOM   197  C  CA  . MET A 1 28  ? 30.182  -3.552  -2.771  1.00 55.93  ? 62  MET A CA  1 
ATOM   198  C  C   . MET A 1 28  ? 31.553  -3.732  -3.404  1.00 73.91  ? 62  MET A C   1 
ATOM   199  O  O   . MET A 1 28  ? 32.411  -2.851  -3.301  1.00 75.74  ? 62  MET A O   1 
ATOM   200  C  CB  . MET A 1 28  ? 29.269  -2.734  -3.691  1.00 58.49  ? 62  MET A CB  1 
ATOM   201  C  CG  . MET A 1 28  ? 29.183  -3.246  -5.120  1.00 65.21  ? 62  MET A CG  1 
ATOM   202  S  SD  . MET A 1 28  ? 28.216  -4.760  -5.260  1.00 71.57  ? 62  MET A SD  1 
ATOM   203  C  CE  . MET A 1 28  ? 26.663  -4.113  -5.875  1.00 60.53  ? 62  MET A CE  1 
ATOM   204  N  N   . ASP A 1 29  ? 31.751  -4.876  -4.056  1.00 80.79  ? 63  ASP A N   1 
ATOM   205  C  CA  . ASP A 1 29  ? 33.034  -5.207  -4.674  1.00 89.08  ? 63  ASP A CA  1 
ATOM   206  C  C   . ASP A 1 29  ? 33.007  -4.763  -6.131  1.00 96.54  ? 63  ASP A C   1 
ATOM   207  O  O   . ASP A 1 29  ? 32.580  -5.498  -7.022  1.00 96.53  ? 63  ASP A O   1 
ATOM   208  C  CB  . ASP A 1 29  ? 33.322  -6.698  -4.548  1.00 96.00  ? 63  ASP A CB  1 
ATOM   209  C  CG  . ASP A 1 29  ? 33.284  -7.178  -3.111  1.00 97.61  ? 63  ASP A CG  1 
ATOM   210  O  OD1 . ASP A 1 29  ? 33.940  -6.547  -2.255  1.00 96.95  ? 63  ASP A OD1 1 
ATOM   211  O  OD2 . ASP A 1 29  ? 32.600  -8.185  -2.837  1.00 99.38  ? 63  ASP A OD2 1 
ATOM   212  N  N   . VAL A 1 30  ? 33.463  -3.541  -6.373  1.00 100.41 ? 64  VAL A N   1 
ATOM   213  C  CA  . VAL A 1 30  ? 33.669  -3.086  -7.753  1.00 113.87 ? 64  VAL A CA  1 
ATOM   214  C  C   . VAL A 1 30  ? 34.861  -3.834  -8.341  1.00 121.12 ? 64  VAL A C   1 
ATOM   215  O  O   . VAL A 1 30  ? 35.910  -3.933  -7.678  1.00 118.47 ? 64  VAL A O   1 
ATOM   216  C  CB  . VAL A 1 30  ? 33.889  -1.571  -7.786  1.00 116.12 ? 64  VAL A CB  1 
ATOM   217  C  CG1 . VAL A 1 30  ? 34.127  -1.091  -9.211  1.00 124.37 ? 64  VAL A CG1 1 
ATOM   218  C  CG2 . VAL A 1 30  ? 32.697  -0.851  -7.172  1.00 95.16  ? 64  VAL A CG2 1 
ATOM   219  N  N   . PRO A 1 31  ? 34.752  -4.389  -9.554  1.00 122.41 ? 65  PRO A N   1 
ATOM   220  C  CA  . PRO A 1 31  ? 35.834  -5.258  -10.057 1.00 124.95 ? 65  PRO A CA  1 
ATOM   221  C  C   . PRO A 1 31  ? 37.203  -4.596  -10.076 1.00 130.93 ? 65  PRO A C   1 
ATOM   222  O  O   . PRO A 1 31  ? 38.175  -5.177  -9.575  1.00 124.53 ? 65  PRO A O   1 
ATOM   223  C  CB  . PRO A 1 31  ? 35.350  -5.622  -11.467 1.00 122.03 ? 65  PRO A CB  1 
ATOM   224  C  CG  . PRO A 1 31  ? 33.864  -5.516  -11.391 1.00 109.90 ? 65  PRO A CG  1 
ATOM   225  C  CD  . PRO A 1 31  ? 33.587  -4.373  -10.456 1.00 112.55 ? 65  PRO A CD  1 
ATOM   226  N  N   . GLY A 1 32  ? 37.310  -3.394  -10.633 1.00 151.70 ? 66  GLY A N   1 
ATOM   227  C  CA  . GLY A 1 32  ? 38.593  -2.724  -10.712 1.00 145.35 ? 66  GLY A CA  1 
ATOM   228  C  C   . GLY A 1 32  ? 38.809  -1.688  -9.629  1.00 150.53 ? 66  GLY A C   1 
ATOM   229  O  O   . GLY A 1 32  ? 39.588  -0.748  -9.812  1.00 144.03 ? 66  GLY A O   1 
ATOM   230  N  N   . PHE A 1 33  ? 38.129  -1.848  -8.489  1.00 137.39 ? 67  PHE A N   1 
ATOM   231  C  CA  . PHE A 1 33  ? 38.249  -0.858  -7.425  1.00 129.90 ? 67  PHE A CA  1 
ATOM   232  C  C   . PHE A 1 33  ? 38.187  -1.456  -6.023  1.00 124.32 ? 67  PHE A C   1 
ATOM   233  O  O   . PHE A 1 33  ? 38.071  -0.690  -5.057  1.00 115.87 ? 67  PHE A O   1 
ATOM   234  C  CB  . PHE A 1 33  ? 37.156  0.211   -7.576  1.00 125.69 ? 67  PHE A CB  1 
ATOM   235  C  CG  . PHE A 1 33  ? 37.567  1.384   -8.419  1.00 123.70 ? 67  PHE A CG  1 
ATOM   236  C  CD1 . PHE A 1 33  ? 38.222  2.465   -7.853  1.00 120.72 ? 67  PHE A CD1 1 
ATOM   237  C  CD2 . PHE A 1 33  ? 37.299  1.406   -9.778  1.00 122.33 ? 67  PHE A CD2 1 
ATOM   238  C  CE1 . PHE A 1 33  ? 38.601  3.546   -8.626  1.00 118.47 ? 67  PHE A CE1 1 
ATOM   239  C  CE2 . PHE A 1 33  ? 37.677  2.483   -10.557 1.00 124.36 ? 67  PHE A CE2 1 
ATOM   240  C  CZ  . PHE A 1 33  ? 38.329  3.555   -9.980  1.00 118.75 ? 67  PHE A CZ  1 
ATOM   241  N  N   . GLY A 1 34  ? 38.257  -2.776  -5.866  1.00 123.86 ? 68  GLY A N   1 
ATOM   242  C  CA  . GLY A 1 34  ? 38.256  -3.382  -4.548  1.00 113.02 ? 68  GLY A CA  1 
ATOM   243  C  C   . GLY A 1 34  ? 36.899  -3.388  -3.873  1.00 111.24 ? 68  GLY A C   1 
ATOM   244  O  O   . GLY A 1 34  ? 35.869  -3.536  -4.536  1.00 109.61 ? 68  GLY A O   1 
ATOM   245  N  N   . ALA A 1 35  ? 36.888  -3.232  -2.550  1.00 88.86  ? 69  ALA A N   1 
ATOM   246  C  CA  . ALA A 1 35  ? 35.658  -3.218  -1.759  1.00 71.87  ? 69  ALA A CA  1 
ATOM   247  C  C   . ALA A 1 35  ? 35.342  -1.771  -1.398  1.00 71.98  ? 69  ALA A C   1 
ATOM   248  O  O   . ALA A 1 35  ? 35.894  -1.222  -0.441  1.00 73.28  ? 69  ALA A O   1 
ATOM   249  C  CB  . ALA A 1 35  ? 35.801  -4.089  -0.516  1.00 67.41  ? 69  ALA A CB  1 
ATOM   250  N  N   . VAL A 1 36  ? 34.444  -1.157  -2.165  1.00 68.24  ? 70  VAL A N   1 
ATOM   251  C  CA  . VAL A 1 36  ? 34.104  0.254   -2.018  1.00 60.51  ? 70  VAL A CA  1 
ATOM   252  C  C   . VAL A 1 36  ? 32.869  0.374   -1.137  1.00 52.47  ? 70  VAL A C   1 
ATOM   253  O  O   . VAL A 1 36  ? 31.884  -0.350  -1.332  1.00 58.37  ? 70  VAL A O   1 
ATOM   254  C  CB  . VAL A 1 36  ? 33.873  0.911   -3.391  1.00 59.42  ? 70  VAL A CB  1 
ATOM   255  C  CG1 . VAL A 1 36  ? 33.054  2.187   -3.252  1.00 50.45  ? 70  VAL A CG1 1 
ATOM   256  C  CG2 . VAL A 1 36  ? 35.205  1.195   -4.072  1.00 63.43  ? 70  VAL A CG2 1 
ATOM   257  N  N   . SER A 1 37  ? 32.919  1.284   -0.169  1.00 46.83  ? 71  SER A N   1 
ATOM   258  C  CA  . SER A 1 37  ? 31.813  1.534   0.742   1.00 49.43  ? 71  SER A CA  1 
ATOM   259  C  C   . SER A 1 37  ? 31.008  2.750   0.293   1.00 48.02  ? 71  SER A C   1 
ATOM   260  O  O   . SER A 1 37  ? 31.473  3.582   -0.490  1.00 48.40  ? 71  SER A O   1 
ATOM   261  C  CB  . SER A 1 37  ? 32.325  1.746   2.168   1.00 41.53  ? 71  SER A CB  1 
ATOM   262  O  OG  . SER A 1 37  ? 33.153  2.894   2.246   1.00 47.10  ? 71  SER A OG  1 
ATOM   263  N  N   . SER A 1 38  ? 29.782  2.840   0.806   1.00 52.03  ? 72  SER A N   1 
ATOM   264  C  CA  . SER A 1 38  ? 28.890  3.949   0.502   1.00 50.36  ? 72  SER A CA  1 
ATOM   265  C  C   . SER A 1 38  ? 28.050  4.253   1.733   1.00 39.18  ? 72  SER A C   1 
ATOM   266  O  O   . SER A 1 38  ? 27.576  3.336   2.407   1.00 42.92  ? 72  SER A O   1 
ATOM   267  C  CB  . SER A 1 38  ? 27.984  3.633   -0.693  1.00 44.14  ? 72  SER A CB  1 
ATOM   268  O  OG  . SER A 1 38  ? 27.064  4.685   -0.922  1.00 45.26  ? 72  SER A OG  1 
ATOM   269  N  N   . ASN A 1 39  ? 27.862  5.539   2.015   1.00 40.37  ? 73  ASN A N   1 
ATOM   270  C  CA  . ASN A 1 39  ? 27.190  5.981   3.226   1.00 42.52  ? 73  ASN A CA  1 
ATOM   271  C  C   . ASN A 1 39  ? 25.866  6.663   2.908   1.00 44.76  ? 73  ASN A C   1 
ATOM   272  O  O   . ASN A 1 39  ? 25.705  7.303   1.865   1.00 44.35  ? 73  ASN A O   1 
ATOM   273  C  CB  . ASN A 1 39  ? 28.071  6.944   4.028   1.00 48.43  ? 73  ASN A CB  1 
ATOM   274  C  CG  . ASN A 1 39  ? 29.383  6.321   4.447   1.00 39.24  ? 73  ASN A CG  1 
ATOM   275  O  OD1 . ASN A 1 39  ? 29.425  5.177   4.898   1.00 46.90  ? 73  ASN A OD1 1 
ATOM   276  N  ND2 . ASN A 1 39  ? 30.467  7.075   4.305   1.00 45.16  ? 73  ASN A ND2 1 
ATOM   277  N  N   . GLY A 1 40  ? 24.920  6.515   3.832   1.00 42.59  ? 74  GLY A N   1 
ATOM   278  C  CA  . GLY A 1 40  ? 23.669  7.244   3.809   1.00 39.66  ? 74  GLY A CA  1 
ATOM   279  C  C   . GLY A 1 40  ? 23.317  7.701   5.209   1.00 41.41  ? 74  GLY A C   1 
ATOM   280  O  O   . GLY A 1 40  ? 24.111  7.509   6.134   1.00 45.38  ? 74  GLY A O   1 
ATOM   281  N  N   . LEU A 1 41  ? 22.142  8.297   5.394   1.00 46.19  ? 75  LEU A N   1 
ATOM   282  C  CA  . LEU A 1 41  ? 21.748  8.813   6.696   1.00 44.67  ? 75  LEU A CA  1 
ATOM   283  C  C   . LEU A 1 41  ? 20.357  8.319   7.069   1.00 41.62  ? 75  LEU A C   1 
ATOM   284  O  O   . LEU A 1 41  ? 19.510  8.078   6.205   1.00 42.84  ? 75  LEU A O   1 
ATOM   285  C  CB  . LEU A 1 41  ? 21.775  10.348  6.731   1.00 43.42  ? 75  LEU A CB  1 
ATOM   286  C  CG  . LEU A 1 41  ? 23.127  11.032  6.522   1.00 45.71  ? 75  LEU A CG  1 
ATOM   287  C  CD1 . LEU A 1 41  ? 22.986  12.539  6.664   1.00 40.27  ? 75  LEU A CD1 1 
ATOM   288  C  CD2 . LEU A 1 41  ? 24.159  10.492  7.498   1.00 44.81  ? 75  LEU A CD2 1 
ATOM   289  N  N   . ILE A 1 42  ? 20.139  8.172   8.374   1.00 39.80  ? 76  ILE A N   1 
ATOM   290  C  CA  . ILE A 1 42  ? 18.841  7.825   8.942   1.00 41.70  ? 76  ILE A CA  1 
ATOM   291  C  C   . ILE A 1 42  ? 18.507  8.877   9.989   1.00 34.71  ? 76  ILE A C   1 
ATOM   292  O  O   . ILE A 1 42  ? 19.265  9.062   10.948  1.00 43.10  ? 76  ILE A O   1 
ATOM   293  C  CB  . ILE A 1 42  ? 18.836  6.419   9.565   1.00 40.52  ? 76  ILE A CB  1 
ATOM   294  C  CG1 . ILE A 1 42  ? 19.016  5.352   8.485   1.00 38.23  ? 76  ILE A CG1 1 
ATOM   295  C  CG2 . ILE A 1 42  ? 17.551  6.187   10.344  1.00 36.95  ? 76  ILE A CG2 1 
ATOM   296  C  CD1 . ILE A 1 42  ? 19.764  4.126   8.959   1.00 39.33  ? 76  ILE A CD1 1 
ATOM   297  N  N   . VAL A 1 43  ? 17.383  9.564   9.808   1.00 41.94  ? 77  VAL A N   1 
ATOM   298  C  CA  . VAL A 1 43  ? 16.998  10.685  10.658  1.00 45.57  ? 77  VAL A CA  1 
ATOM   299  C  C   . VAL A 1 43  ? 15.699  10.332  11.367  1.00 44.38  ? 77  VAL A C   1 
ATOM   300  O  O   . VAL A 1 43  ? 14.702  9.996   10.716  1.00 43.18  ? 77  VAL A O   1 
ATOM   301  C  CB  . VAL A 1 43  ? 16.842  11.985  9.853   1.00 45.50  ? 77  VAL A CB  1 
ATOM   302  C  CG1 . VAL A 1 43  ? 16.733  13.178  10.789  1.00 48.23  ? 77  VAL A CG1 1 
ATOM   303  C  CG2 . VAL A 1 43  ? 18.007  12.158  8.888   1.00 35.02  ? 77  VAL A CG2 1 
ATOM   304  N  N   . LYS A 1 44  ? 15.710  10.410  12.696  1.00 45.66  ? 78  LYS A N   1 
ATOM   305  C  CA  . LYS A 1 44  ? 14.501  10.241  13.496  1.00 44.02  ? 78  LYS A CA  1 
ATOM   306  C  C   . LYS A 1 44  ? 13.856  11.609  13.675  1.00 52.62  ? 78  LYS A C   1 
ATOM   307  O  O   . LYS A 1 44  ? 14.388  12.467  14.386  1.00 59.68  ? 78  LYS A O   1 
ATOM   308  C  CB  . LYS A 1 44  ? 14.817  9.599   14.845  1.00 46.61  ? 78  LYS A CB  1 
ATOM   309  C  CG  . LYS A 1 44  ? 13.581  9.333   15.697  1.00 54.15  ? 78  LYS A CG  1 
ATOM   310  C  CD  . LYS A 1 44  ? 13.916  9.269   17.180  1.00 58.71  ? 78  LYS A CD  1 
ATOM   311  C  CE  . LYS A 1 44  ? 12.658  9.299   18.036  1.00 52.33  ? 78  LYS A CE  1 
ATOM   312  N  NZ  . LYS A 1 44  ? 12.595  10.519  18.888  1.00 65.74  ? 78  LYS A NZ  1 
ATOM   313  N  N   . ASP A 1 45  ? 12.717  11.815  13.024  1.00 51.60  ? 79  ASP A N   1 
ATOM   314  C  CA  . ASP A 1 45  ? 11.996  13.084  13.057  1.00 44.96  ? 79  ASP A CA  1 
ATOM   315  C  C   . ASP A 1 45  ? 10.719  12.868  13.867  1.00 52.45  ? 79  ASP A C   1 
ATOM   316  O  O   . ASP A 1 45  ? 9.664   12.539  13.321  1.00 51.44  ? 79  ASP A O   1 
ATOM   317  C  CB  . ASP A 1 45  ? 11.698  13.577  11.643  1.00 41.31  ? 79  ASP A CB  1 
ATOM   318  C  CG  . ASP A 1 45  ? 10.798  14.795  11.627  1.00 51.07  ? 79  ASP A CG  1 
ATOM   319  O  OD1 . ASP A 1 45  ? 11.004  15.698  12.465  1.00 55.99  ? 79  ASP A OD1 1 
ATOM   320  O  OD2 . ASP A 1 45  ? 9.884   14.847  10.777  1.00 52.57  ? 79  ASP A OD2 1 
ATOM   321  N  N   . GLY A 1 46  ? 10.824  13.052  15.181  1.00 54.98  ? 80  GLY A N   1 
ATOM   322  C  CA  . GLY A 1 46  ? 9.690   12.860  16.061  1.00 50.72  ? 80  GLY A CA  1 
ATOM   323  C  C   . GLY A 1 46  ? 9.252   11.414  16.157  1.00 56.40  ? 80  GLY A C   1 
ATOM   324  O  O   . GLY A 1 46  ? 9.950   10.585  16.749  1.00 61.83  ? 80  GLY A O   1 
ATOM   325  N  N   . GLU A 1 47  ? 8.098   11.097  15.573  1.00 57.13  ? 81  GLU A N   1 
ATOM   326  C  CA  . GLU A 1 47  ? 7.542   9.752   15.611  1.00 57.88  ? 81  GLU A CA  1 
ATOM   327  C  C   . GLU A 1 47  ? 7.707   9.008   14.292  1.00 56.11  ? 81  GLU A C   1 
ATOM   328  O  O   . GLU A 1 47  ? 7.086   7.957   14.104  1.00 61.57  ? 81  GLU A O   1 
ATOM   329  C  CB  . GLU A 1 47  ? 6.062   9.806   15.997  1.00 57.61  ? 81  GLU A CB  1 
ATOM   330  C  CG  . GLU A 1 47  ? 5.797   10.457  17.343  1.00 74.22  ? 81  GLU A CG  1 
ATOM   331  C  CD  . GLU A 1 47  ? 5.922   9.481   18.496  1.00 86.00  ? 81  GLU A CD  1 
ATOM   332  O  OE1 . GLU A 1 47  ? 5.364   8.368   18.397  1.00 97.89  ? 81  GLU A OE1 1 
ATOM   333  O  OE2 . GLU A 1 47  ? 6.579   9.827   19.500  1.00 96.38  ? 81  GLU A OE2 1 
ATOM   334  N  N   . ARG A 1 48  ? 8.523   9.524   13.378  1.00 54.23  ? 82  ARG A N   1 
ATOM   335  C  CA  . ARG A 1 48  ? 8.760   8.885   12.093  1.00 48.86  ? 82  ARG A CA  1 
ATOM   336  C  C   . ARG A 1 48  ? 10.252  8.895   11.788  1.00 51.47  ? 82  ARG A C   1 
ATOM   337  O  O   . ARG A 1 48  ? 11.048  9.544   12.472  1.00 45.31  ? 82  ARG A O   1 
ATOM   338  C  CB  . ARG A 1 48  ? 7.976   9.576   10.968  1.00 47.76  ? 82  ARG A CB  1 
ATOM   339  C  CG  . ARG A 1 48  ? 8.537   10.922  10.547  1.00 44.73  ? 82  ARG A CG  1 
ATOM   340  C  CD  . ARG A 1 48  ? 7.427   11.856  10.089  1.00 51.18  ? 82  ARG A CD  1 
ATOM   341  N  NE  . ARG A 1 48  ? 7.940   13.161  9.690   1.00 58.78  ? 82  ARG A NE  1 
ATOM   342  C  CZ  . ARG A 1 48  ? 7.831   13.668  8.470   1.00 55.79  ? 82  ARG A CZ  1 
ATOM   343  N  NH1 . ARG A 1 48  ? 7.221   13.007  7.499   1.00 50.46  ? 82  ARG A NH1 1 
ATOM   344  N  NH2 . ARG A 1 48  ? 8.346   14.868  8.217   1.00 58.26  ? 82  ARG A NH2 1 
ATOM   345  N  N   . VAL A 1 49  ? 10.624  8.159   10.745  1.00 45.83  ? 83  VAL A N   1 
ATOM   346  C  CA  . VAL A 1 49  ? 12.013  8.007   10.333  1.00 41.46  ? 83  VAL A CA  1 
ATOM   347  C  C   . VAL A 1 49  ? 12.148  8.483   8.894   1.00 43.25  ? 83  VAL A C   1 
ATOM   348  O  O   . VAL A 1 49  ? 11.297  8.184   8.049   1.00 50.65  ? 83  VAL A O   1 
ATOM   349  C  CB  . VAL A 1 49  ? 12.485  6.544   10.474  1.00 43.50  ? 83  VAL A CB  1 
ATOM   350  C  CG1 . VAL A 1 49  ? 13.908  6.389   9.968   1.00 42.05  ? 83  VAL A CG1 1 
ATOM   351  C  CG2 . VAL A 1 49  ? 12.377  6.091   11.922  1.00 47.87  ? 83  VAL A CG2 1 
ATOM   352  N  N   . LEU A 1 50  ? 13.214  9.231   8.620   1.00 39.47  ? 84  LEU A N   1 
ATOM   353  C  CA  . LEU A 1 50  ? 13.513  9.728   7.284   1.00 39.30  ? 84  LEU A CA  1 
ATOM   354  C  C   . LEU A 1 50  ? 14.830  9.129   6.814   1.00 46.97  ? 84  LEU A C   1 
ATOM   355  O  O   . LEU A 1 50  ? 15.838  9.204   7.525   1.00 45.20  ? 84  LEU A O   1 
ATOM   356  C  CB  . LEU A 1 50  ? 13.584  11.258  7.266   1.00 40.28  ? 84  LEU A CB  1 
ATOM   357  C  CG  . LEU A 1 50  ? 12.454  11.996  7.989   1.00 46.34  ? 84  LEU A CG  1 
ATOM   358  C  CD1 . LEU A 1 50  ? 12.664  13.500  7.926   1.00 36.67  ? 84  LEU A CD1 1 
ATOM   359  C  CD2 . LEU A 1 50  ? 11.100  11.616  7.406   1.00 42.56  ? 84  LEU A CD2 1 
ATOM   360  N  N   . LEU A 1 51  ? 14.820  8.538   5.623   1.00 44.41  ? 85  LEU A N   1 
ATOM   361  C  CA  . LEU A 1 51  ? 15.996  7.904   5.046   1.00 41.40  ? 85  LEU A CA  1 
ATOM   362  C  C   . LEU A 1 51  ? 16.570  8.790   3.949   1.00 43.13  ? 85  LEU A C   1 
ATOM   363  O  O   . LEU A 1 51  ? 15.827  9.337   3.127   1.00 46.81  ? 85  LEU A O   1 
ATOM   364  C  CB  . LEU A 1 51  ? 15.650  6.520   4.490   1.00 45.05  ? 85  LEU A CB  1 
ATOM   365  C  CG  . LEU A 1 51  ? 16.770  5.733   3.809   1.00 52.37  ? 85  LEU A CG  1 
ATOM   366  C  CD1 . LEU A 1 51  ? 17.767  5.234   4.841   1.00 44.21  ? 85  LEU A CD1 1 
ATOM   367  C  CD2 . LEU A 1 51  ? 16.187  4.571   3.024   1.00 42.60  ? 85  LEU A CD2 1 
ATOM   368  N  N   . VAL A 1 52  ? 17.895  8.929   3.938   1.00 47.20  ? 86  VAL A N   1 
ATOM   369  C  CA  . VAL A 1 52  ? 18.569  9.872   3.049   1.00 53.80  ? 86  VAL A CA  1 
ATOM   370  C  C   . VAL A 1 52  ? 19.270  9.184   1.882   1.00 57.67  ? 86  VAL A C   1 
ATOM   371  O  O   . VAL A 1 52  ? 19.591  9.857   0.887   1.00 68.16  ? 86  VAL A O   1 
ATOM   372  C  CB  . VAL A 1 52  ? 19.557  10.763  3.837   1.00 51.45  ? 86  VAL A CB  1 
ATOM   373  C  CG1 . VAL A 1 52  ? 20.213  11.818  2.949   1.00 43.89  ? 86  VAL A CG1 1 
ATOM   374  C  CG2 . VAL A 1 52  ? 18.837  11.432  5.002   1.00 53.15  ? 86  VAL A CG2 1 
ATOM   375  N  N   . ASP A 1 53  ? 19.489  7.874   1.947   1.00 43.20  ? 87  ASP A N   1 
ATOM   376  C  CA  . ASP A 1 53  ? 20.009  7.135   0.803   1.00 49.26  ? 87  ASP A CA  1 
ATOM   377  C  C   . ASP A 1 53  ? 19.780  5.651   1.030   1.00 51.92  ? 87  ASP A C   1 
ATOM   378  O  O   . ASP A 1 53  ? 19.630  5.190   2.166   1.00 46.17  ? 87  ASP A O   1 
ATOM   379  C  CB  . ASP A 1 53  ? 21.498  7.411   0.567   1.00 57.24  ? 87  ASP A CB  1 
ATOM   380  C  CG  . ASP A 1 53  ? 21.739  8.346   -0.604  1.00 62.41  ? 87  ASP A CG  1 
ATOM   381  O  OD1 . ASP A 1 53  ? 20.920  8.356   -1.548  1.00 65.47  ? 87  ASP A OD1 1 
ATOM   382  O  OD2 . ASP A 1 53  ? 22.739  9.093   -0.567  1.00 67.34  ? 87  ASP A OD2 1 
ATOM   383  N  N   . THR A 1 54  ? 19.762  4.914   -0.070  1.00 40.03  ? 88  THR A N   1 
ATOM   384  C  CA  . THR A 1 54  ? 19.626  3.471   -0.021  1.00 49.69  ? 88  THR A CA  1 
ATOM   385  C  C   . THR A 1 54  ? 21.019  2.844   -0.017  1.00 48.09  ? 88  THR A C   1 
ATOM   386  O  O   . THR A 1 54  ? 22.036  3.530   0.108   1.00 51.02  ? 88  THR A O   1 
ATOM   387  C  CB  . THR A 1 54  ? 18.790  2.972   -1.195  1.00 44.51  ? 88  THR A CB  1 
ATOM   388  O  OG1 . THR A 1 54  ? 19.642  2.775   -2.329  1.00 51.66  ? 88  THR A OG1 1 
ATOM   389  C  CG2 . THR A 1 54  ? 17.699  3.987   -1.556  1.00 54.20  ? 88  THR A CG2 1 
ATOM   390  N  N   . ALA A 1 55  ? 21.076  1.529   -0.161  1.00 48.21  ? 89  ALA A N   1 
ATOM   391  C  CA  . ALA A 1 55  ? 22.331  0.808   -0.214  1.00 49.41  ? 89  ALA A CA  1 
ATOM   392  C  C   . ALA A 1 55  ? 22.642  0.447   -1.663  1.00 54.26  ? 89  ALA A C   1 
ATOM   393  O  O   . ALA A 1 55  ? 21.975  0.900   -2.599  1.00 53.65  ? 89  ALA A O   1 
ATOM   394  C  CB  . ALA A 1 55  ? 22.257  -0.422  0.689   1.00 44.08  ? 89  ALA A CB  1 
ATOM   395  N  N   . TRP A 1 56  ? 23.669  -0.381  -1.858  1.00 56.35  ? 90  TRP A N   1 
ATOM   396  C  CA  . TRP A 1 56  ? 24.027  -0.805  -3.206  1.00 52.16  ? 90  TRP A CA  1 
ATOM   397  C  C   . TRP A 1 56  ? 22.944  -1.687  -3.816  1.00 49.78  ? 90  TRP A C   1 
ATOM   398  O  O   . TRP A 1 56  ? 22.647  -1.577  -5.011  1.00 49.59  ? 90  TRP A O   1 
ATOM   399  C  CB  . TRP A 1 56  ? 25.362  -1.548  -3.181  1.00 50.21  ? 90  TRP A CB  1 
ATOM   400  C  CG  . TRP A 1 56  ? 26.540  -0.695  -2.821  1.00 52.38  ? 90  TRP A CG  1 
ATOM   401  C  CD1 . TRP A 1 56  ? 27.035  -0.464  -1.570  1.00 53.21  ? 90  TRP A CD1 1 
ATOM   402  C  CD2 . TRP A 1 56  ? 27.384  0.027   -3.726  1.00 50.13  ? 90  TRP A CD2 1 
ATOM   403  N  NE1 . TRP A 1 56  ? 28.132  0.361   -1.641  1.00 50.36  ? 90  TRP A NE1 1 
ATOM   404  C  CE2 . TRP A 1 56  ? 28.368  0.674   -2.953  1.00 54.33  ? 90  TRP A CE2 1 
ATOM   405  C  CE3 . TRP A 1 56  ? 27.404  0.185   -5.115  1.00 57.71  ? 90  TRP A CE3 1 
ATOM   406  C  CZ2 . TRP A 1 56  ? 29.359  1.472   -3.523  1.00 57.53  ? 90  TRP A CZ2 1 
ATOM   407  C  CZ3 . TRP A 1 56  ? 28.389  0.977   -5.679  1.00 56.21  ? 90  TRP A CZ3 1 
ATOM   408  C  CH2 . TRP A 1 56  ? 29.352  1.610   -4.884  1.00 53.50  ? 90  TRP A CH2 1 
ATOM   409  N  N   . THR A 1 57  ? 22.347  -2.567  -3.016  1.00 50.74  ? 91  THR A N   1 
ATOM   410  C  CA  . THR A 1 57  ? 21.426  -3.580  -3.509  1.00 54.99  ? 91  THR A CA  1 
ATOM   411  C  C   . THR A 1 57  ? 20.104  -3.507  -2.755  1.00 51.75  ? 91  THR A C   1 
ATOM   412  O  O   . THR A 1 57  ? 19.981  -2.841  -1.723  1.00 53.91  ? 91  THR A O   1 
ATOM   413  C  CB  . THR A 1 57  ? 22.019  -4.990  -3.370  1.00 52.17  ? 91  THR A CB  1 
ATOM   414  O  OG1 . THR A 1 57  ? 21.923  -5.415  -2.004  1.00 59.24  ? 91  THR A OG1 1 
ATOM   415  C  CG2 . THR A 1 57  ? 23.480  -5.009  -3.799  1.00 53.61  ? 91  THR A CG2 1 
ATOM   416  N  N   . ASP A 1 58  ? 19.107  -4.213  -3.296  1.00 51.17  ? 92  ASP A N   1 
ATOM   417  C  CA  . ASP A 1 58  ? 17.830  -4.352  -2.603  1.00 53.92  ? 92  ASP A CA  1 
ATOM   418  C  C   . ASP A 1 58  ? 17.998  -5.112  -1.293  1.00 53.72  ? 92  ASP A C   1 
ATOM   419  O  O   . ASP A 1 58  ? 17.374  -4.769  -0.282  1.00 56.17  ? 92  ASP A O   1 
ATOM   420  C  CB  . ASP A 1 58  ? 16.822  -5.069  -3.502  1.00 53.00  ? 92  ASP A CB  1 
ATOM   421  C  CG  . ASP A 1 58  ? 15.929  -4.112  -4.266  1.00 51.28  ? 92  ASP A CG  1 
ATOM   422  O  OD1 . ASP A 1 58  ? 16.034  -2.889  -4.048  1.00 47.92  ? 92  ASP A OD1 1 
ATOM   423  O  OD2 . ASP A 1 58  ? 15.118  -4.587  -5.088  1.00 65.93  ? 92  ASP A OD2 1 
ATOM   424  N  N   . ASP A 1 59  ? 18.837  -6.151  -1.297  1.00 55.11  ? 93  ASP A N   1 
ATOM   425  C  CA  . ASP A 1 59  ? 19.022  -6.967  -0.101  1.00 56.73  ? 93  ASP A CA  1 
ATOM   426  C  C   . ASP A 1 59  ? 19.654  -6.162  1.027   1.00 55.72  ? 93  ASP A C   1 
ATOM   427  O  O   . ASP A 1 59  ? 19.266  -6.303  2.193   1.00 55.56  ? 93  ASP A O   1 
ATOM   428  C  CB  . ASP A 1 59  ? 19.876  -8.190  -0.432  1.00 55.19  ? 93  ASP A CB  1 
ATOM   429  C  CG  . ASP A 1 59  ? 20.197  -9.027  0.790   1.00 62.99  ? 93  ASP A CG  1 
ATOM   430  O  OD1 . ASP A 1 59  ? 19.373  -9.892  1.153   1.00 72.80  ? 93  ASP A OD1 1 
ATOM   431  O  OD2 . ASP A 1 59  ? 21.275  -8.820  1.386   1.00 67.42  ? 93  ASP A OD2 1 
ATOM   432  N  N   . GLN A 1 60  ? 20.630  -5.312  0.702   1.00 60.07  ? 94  GLN A N   1 
ATOM   433  C  CA  . GLN A 1 60  ? 21.263  -4.495  1.730   1.00 58.37  ? 94  GLN A CA  1 
ATOM   434  C  C   . GLN A 1 60  ? 20.335  -3.393  2.223   1.00 48.07  ? 94  GLN A C   1 
ATOM   435  O  O   . GLN A 1 60  ? 20.447  -2.960  3.376   1.00 47.70  ? 94  GLN A O   1 
ATOM   436  C  CB  . GLN A 1 60  ? 22.564  -3.896  1.196   1.00 48.65  ? 94  GLN A CB  1 
ATOM   437  C  CG  . GLN A 1 60  ? 23.625  -4.919  0.840   1.00 55.06  ? 94  GLN A CG  1 
ATOM   438  C  CD  . GLN A 1 60  ? 24.867  -4.280  0.252   1.00 59.45  ? 94  GLN A CD  1 
ATOM   439  O  OE1 . GLN A 1 60  ? 24.788  -3.268  -0.444  1.00 59.58  ? 94  GLN A OE1 1 
ATOM   440  N  NE2 . GLN A 1 60  ? 26.024  -4.869  0.530   1.00 61.42  ? 94  GLN A NE2 1 
ATOM   441  N  N   . THR A 1 61  ? 19.415  -2.929  1.374   1.00 47.24  ? 95  THR A N   1 
ATOM   442  C  CA  . THR A 1 61  ? 18.478  -1.892  1.795   1.00 53.04  ? 95  THR A CA  1 
ATOM   443  C  C   . THR A 1 61  ? 17.424  -2.454  2.743   1.00 46.92  ? 95  THR A C   1 
ATOM   444  O  O   . THR A 1 61  ? 17.027  -1.787  3.705   1.00 45.68  ? 95  THR A O   1 
ATOM   445  C  CB  . THR A 1 61  ? 17.822  -1.251  0.572   1.00 48.21  ? 95  THR A CB  1 
ATOM   446  O  OG1 . THR A 1 61  ? 18.829  -0.619  -0.228  1.00 44.05  ? 95  THR A OG1 1 
ATOM   447  C  CG2 . THR A 1 61  ? 16.794  -0.210  0.992   1.00 40.19  ? 95  THR A CG2 1 
ATOM   448  N  N   . SER A 1 62  ? 16.964  -3.680  2.491   1.00 46.48  ? 96  SER A N   1 
ATOM   449  C  CA  . SER A 1 62  ? 16.026  -4.312  3.412   1.00 50.37  ? 96  SER A CA  1 
ATOM   450  C  C   . SER A 1 62  ? 16.676  -4.603  4.759   1.00 50.66  ? 96  SER A C   1 
ATOM   451  O  O   . SER A 1 62  ? 15.980  -4.670  5.779   1.00 54.04  ? 96  SER A O   1 
ATOM   452  C  CB  . SER A 1 62  ? 15.466  -5.590  2.791   1.00 43.56  ? 96  SER A CB  1 
ATOM   453  O  OG  . SER A 1 62  ? 16.384  -6.657  2.923   1.00 67.96  ? 96  SER A OG  1 
ATOM   454  N  N   . GLN A 1 63  ? 17.999  -4.777  4.786   1.00 46.20  ? 97  GLN A N   1 
ATOM   455  C  CA  . GLN A 1 63  ? 18.700  -4.868  6.062   1.00 54.86  ? 97  GLN A CA  1 
ATOM   456  C  C   . GLN A 1 63  ? 18.708  -3.527  6.785   1.00 49.57  ? 97  GLN A C   1 
ATOM   457  O  O   . GLN A 1 63  ? 18.693  -3.489  8.020   1.00 42.62  ? 97  GLN A O   1 
ATOM   458  C  CB  . GLN A 1 63  ? 20.130  -5.365  5.851   1.00 52.59  ? 97  GLN A CB  1 
ATOM   459  C  CG  . GLN A 1 63  ? 20.235  -6.765  5.271   1.00 51.88  ? 97  GLN A CG  1 
ATOM   460  C  CD  . GLN A 1 63  ? 21.673  -7.199  5.060   1.00 57.41  ? 97  GLN A CD  1 
ATOM   461  O  OE1 . GLN A 1 63  ? 22.544  -6.924  5.886   1.00 64.30  ? 97  GLN A OE1 1 
ATOM   462  N  NE2 . GLN A 1 63  ? 21.930  -7.879  3.949   1.00 53.21  ? 97  GLN A NE2 1 
ATOM   463  N  N   . ILE A 1 64  ? 18.736  -2.421  6.037   1.00 49.15  ? 98  ILE A N   1 
ATOM   464  C  CA  . ILE A 1 64  ? 18.646  -1.101  6.656   1.00 46.86  ? 98  ILE A CA  1 
ATOM   465  C  C   . ILE A 1 64  ? 17.290  -0.927  7.327   1.00 47.12  ? 98  ILE A C   1 
ATOM   466  O  O   . ILE A 1 64  ? 17.198  -0.490  8.480   1.00 51.11  ? 98  ILE A O   1 
ATOM   467  C  CB  . ILE A 1 64  ? 18.905  0.003   5.614   1.00 50.25  ? 98  ILE A CB  1 
ATOM   468  C  CG1 . ILE A 1 64  ? 20.404  0.174   5.368   1.00 50.27  ? 98  ILE A CG1 1 
ATOM   469  C  CG2 . ILE A 1 64  ? 18.291  1.323   6.061   1.00 43.82  ? 98  ILE A CG2 1 
ATOM   470  C  CD1 . ILE A 1 64  ? 20.733  0.776   4.017   1.00 45.77  ? 98  ILE A CD1 1 
ATOM   471  N  N   . LEU A 1 65  ? 16.216  -1.278  6.613   1.00 44.02  ? 99  LEU A N   1 
ATOM   472  C  CA  . LEU A 1 65  ? 14.876  -1.160  7.179   1.00 48.91  ? 99  LEU A CA  1 
ATOM   473  C  C   . LEU A 1 65  ? 14.713  -2.053  8.402   1.00 47.93  ? 99  LEU A C   1 
ATOM   474  O  O   . LEU A 1 65  ? 14.087  -1.656  9.392   1.00 44.58  ? 99  LEU A O   1 
ATOM   475  C  CB  . LEU A 1 65  ? 13.828  -1.503  6.121   1.00 49.29  ? 99  LEU A CB  1 
ATOM   476  C  CG  . LEU A 1 65  ? 13.866  -0.674  4.836   1.00 54.16  ? 99  LEU A CG  1 
ATOM   477  C  CD1 . LEU A 1 65  ? 12.782  -1.129  3.873   1.00 36.12  ? 99  LEU A CD1 1 
ATOM   478  C  CD2 . LEU A 1 65  ? 13.724  0.806   5.151   1.00 42.28  ? 99  LEU A CD2 1 
ATOM   479  N  N   . ASN A 1 66  ? 15.270  -3.266  8.352   1.00 47.55  ? 100 ASN A N   1 
ATOM   480  C  CA  . ASN A 1 66  ? 15.226  -4.146  9.514   1.00 50.04  ? 100 ASN A CA  1 
ATOM   481  C  C   . ASN A 1 66  ? 15.982  -3.547  10.692  1.00 52.39  ? 100 ASN A C   1 
ATOM   482  O  O   . ASN A 1 66  ? 15.604  -3.764  11.848  1.00 51.38  ? 100 ASN A O   1 
ATOM   483  C  CB  . ASN A 1 66  ? 15.798  -5.517  9.156   1.00 51.78  ? 100 ASN A CB  1 
ATOM   484  C  CG  . ASN A 1 66  ? 14.796  -6.394  8.434   1.00 57.97  ? 100 ASN A CG  1 
ATOM   485  O  OD1 . ASN A 1 66  ? 13.601  -6.101  8.410   1.00 63.35  ? 100 ASN A OD1 1 
ATOM   486  N  ND2 . ASN A 1 66  ? 15.280  -7.478  7.839   1.00 59.93  ? 100 ASN A ND2 1 
ATOM   487  N  N   . TRP A 1 67  ? 17.046  -2.790  10.418  1.00 48.81  ? 101 TRP A N   1 
ATOM   488  C  CA  . TRP A 1 67  ? 17.766  -2.107  11.487  1.00 46.13  ? 101 TRP A CA  1 
ATOM   489  C  C   . TRP A 1 67  ? 16.934  -0.973  12.073  1.00 43.75  ? 101 TRP A C   1 
ATOM   490  O  O   . TRP A 1 67  ? 16.979  -0.722  13.283  1.00 47.22  ? 101 TRP A O   1 
ATOM   491  C  CB  . TRP A 1 67  ? 19.103  -1.586  10.959  1.00 49.51  ? 101 TRP A CB  1 
ATOM   492  C  CG  . TRP A 1 67  ? 19.968  -0.944  11.998  1.00 54.23  ? 101 TRP A CG  1 
ATOM   493  C  CD1 . TRP A 1 67  ? 20.944  -1.546  12.737  1.00 50.17  ? 101 TRP A CD1 1 
ATOM   494  C  CD2 . TRP A 1 67  ? 19.947  0.430   12.406  1.00 45.41  ? 101 TRP A CD2 1 
ATOM   495  N  NE1 . TRP A 1 67  ? 21.527  -0.635  13.584  1.00 59.56  ? 101 TRP A NE1 1 
ATOM   496  C  CE2 . TRP A 1 67  ? 20.934  0.586   13.399  1.00 55.77  ? 101 TRP A CE2 1 
ATOM   497  C  CE3 . TRP A 1 67  ? 19.188  1.542   12.028  1.00 43.20  ? 101 TRP A CE3 1 
ATOM   498  C  CZ2 . TRP A 1 67  ? 21.180  1.809   14.021  1.00 50.26  ? 101 TRP A CZ2 1 
ATOM   499  C  CZ3 . TRP A 1 67  ? 19.434  2.755   12.647  1.00 46.57  ? 101 TRP A CZ3 1 
ATOM   500  C  CH2 . TRP A 1 67  ? 20.421  2.878   13.632  1.00 46.82  ? 101 TRP A CH2 1 
ATOM   501  N  N   . ILE A 1 68  ? 16.166  -0.279  11.231  1.00 44.67  ? 102 ILE A N   1 
ATOM   502  C  CA  . ILE A 1 68  ? 15.331  0.819   11.710  1.00 48.67  ? 102 ILE A CA  1 
ATOM   503  C  C   . ILE A 1 68  ? 14.204  0.288   12.587  1.00 50.29  ? 102 ILE A C   1 
ATOM   504  O  O   . ILE A 1 68  ? 13.930  0.823   13.668  1.00 55.77  ? 102 ILE A O   1 
ATOM   505  C  CB  . ILE A 1 68  ? 14.786  1.635   10.524  1.00 45.85  ? 102 ILE A CB  1 
ATOM   506  C  CG1 . ILE A 1 68  ? 15.940  2.146   9.657   1.00 40.42  ? 102 ILE A CG1 1 
ATOM   507  C  CG2 . ILE A 1 68  ? 13.909  2.776   11.024  1.00 40.18  ? 102 ILE A CG2 1 
ATOM   508  C  CD1 . ILE A 1 68  ? 15.603  3.366   8.829   1.00 38.60  ? 102 ILE A CD1 1 
ATOM   509  N  N   . LYS A 1 69  ? 13.528  -0.770  12.130  1.00 50.59  ? 103 LYS A N   1 
ATOM   510  C  CA  . LYS A 1 69  ? 12.478  -1.384  12.937  1.00 56.75  ? 103 LYS A CA  1 
ATOM   511  C  C   . LYS A 1 69  ? 13.034  -1.944  14.239  1.00 48.05  ? 103 LYS A C   1 
ATOM   512  O  O   . LYS A 1 69  ? 12.351  -1.919  15.269  1.00 57.54  ? 103 LYS A O   1 
ATOM   513  C  CB  . LYS A 1 69  ? 11.782  -2.485  12.134  1.00 62.52  ? 103 LYS A CB  1 
ATOM   514  C  CG  . LYS A 1 69  ? 10.741  -3.279  12.911  1.00 56.20  ? 103 LYS A CG  1 
ATOM   515  C  CD  . LYS A 1 69  ? 9.334   -2.968  12.431  1.00 59.96  ? 103 LYS A CD  1 
ATOM   516  C  CE  . LYS A 1 69  ? 8.301   -3.772  13.203  1.00 64.48  ? 103 LYS A CE  1 
ATOM   517  N  NZ  . LYS A 1 69  ? 8.208   -3.338  14.624  1.00 63.72  ? 103 LYS A NZ  1 
ATOM   518  N  N   . GLN A 1 70  ? 14.272  -2.435  14.216  1.00 48.58  ? 104 GLN A N   1 
ATOM   519  C  CA  . GLN A 1 70  ? 14.871  -3.023  15.407  1.00 54.55  ? 104 GLN A CA  1 
ATOM   520  C  C   . GLN A 1 70  ? 15.307  -1.952  16.402  1.00 60.85  ? 104 GLN A C   1 
ATOM   521  O  O   . GLN A 1 70  ? 14.998  -2.041  17.595  1.00 62.75  ? 104 GLN A O   1 
ATOM   522  C  CB  . GLN A 1 70  ? 16.056  -3.906  15.008  1.00 59.47  ? 104 GLN A CB  1 
ATOM   523  C  CG  . GLN A 1 70  ? 16.801  -4.523  16.174  1.00 63.77  ? 104 GLN A CG  1 
ATOM   524  C  CD  . GLN A 1 70  ? 18.031  -5.293  15.742  1.00 58.48  ? 104 GLN A CD  1 
ATOM   525  O  OE1 . GLN A 1 70  ? 17.940  -6.262  14.988  1.00 59.50  ? 104 GLN A OE1 1 
ATOM   526  N  NE2 . GLN A 1 70  ? 19.194  -4.865  16.219  1.00 63.77  ? 104 GLN A NE2 1 
ATOM   527  N  N   . GLU A 1 71  ? 16.016  -0.928  15.928  1.00 52.86  ? 105 GLU A N   1 
ATOM   528  C  CA  . GLU A 1 71  ? 16.602  0.070   16.815  1.00 57.41  ? 105 GLU A CA  1 
ATOM   529  C  C   . GLU A 1 71  ? 15.630  1.195   17.159  1.00 57.33  ? 105 GLU A C   1 
ATOM   530  O  O   . GLU A 1 71  ? 15.510  1.578   18.327  1.00 63.84  ? 105 GLU A O   1 
ATOM   531  C  CB  . GLU A 1 71  ? 17.872  0.649   16.184  1.00 55.81  ? 105 GLU A CB  1 
ATOM   532  C  CG  . GLU A 1 71  ? 19.010  -0.350  16.051  1.00 60.74  ? 105 GLU A CG  1 
ATOM   533  C  CD  . GLU A 1 71  ? 19.365  -1.016  17.366  1.00 63.82  ? 105 GLU A CD  1 
ATOM   534  O  OE1 . GLU A 1 71  ? 19.402  -0.316  18.401  1.00 67.30  ? 105 GLU A OE1 1 
ATOM   535  O  OE2 . GLU A 1 71  ? 19.610  -2.240  17.365  1.00 63.26  ? 105 GLU A OE2 1 
ATOM   536  N  N   . ILE A 1 72  ? 14.937  1.738   16.162  1.00 57.33  ? 106 ILE A N   1 
ATOM   537  C  CA  . ILE A 1 72  ? 14.062  2.885   16.360  1.00 58.30  ? 106 ILE A CA  1 
ATOM   538  C  C   . ILE A 1 72  ? 12.605  2.465   16.516  1.00 54.71  ? 106 ILE A C   1 
ATOM   539  O  O   . ILE A 1 72  ? 11.884  3.028   17.341  1.00 56.15  ? 106 ILE A O   1 
ATOM   540  C  CB  . ILE A 1 72  ? 14.232  3.891   15.201  1.00 54.43  ? 106 ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 72  ? 15.697  4.312   15.076  1.00 52.99  ? 106 ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 72  ? 13.348  5.109   15.413  1.00 48.70  ? 106 ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 72  ? 16.272  4.117   13.691  1.00 53.66  ? 106 ILE A CD1 1 
ATOM   544  N  N   . ASN A 1 73  ? 12.163  1.480   15.731  1.00 55.05  ? 107 ASN A N   1 
ATOM   545  C  CA  . ASN A 1 73  ? 10.788  0.976   15.778  1.00 55.67  ? 107 ASN A CA  1 
ATOM   546  C  C   . ASN A 1 73  ? 9.780   2.083   15.470  1.00 58.05  ? 107 ASN A C   1 
ATOM   547  O  O   . ASN A 1 73  ? 8.835   2.326   16.224  1.00 58.80  ? 107 ASN A O   1 
ATOM   548  C  CB  . ASN A 1 73  ? 10.486  0.317   17.126  1.00 55.08  ? 107 ASN A CB  1 
ATOM   549  C  CG  . ASN A 1 73  ? 9.350   -0.682  17.042  1.00 56.96  ? 107 ASN A CG  1 
ATOM   550  O  OD1 . ASN A 1 73  ? 8.960   -1.107  15.955  1.00 56.03  ? 107 ASN A OD1 1 
ATOM   551  N  ND2 . ASN A 1 73  ? 8.805   -1.054  18.194  1.00 51.26  ? 107 ASN A ND2 1 
ATOM   552  N  N   . LEU A 1 74  ? 9.991   2.757   14.345  1.00 58.00  ? 108 LEU A N   1 
ATOM   553  C  CA  . LEU A 1 74  ? 9.108   3.803   13.857  1.00 50.98  ? 108 LEU A CA  1 
ATOM   554  C  C   . LEU A 1 74  ? 9.023   3.701   12.342  1.00 51.49  ? 108 LEU A C   1 
ATOM   555  O  O   . LEU A 1 74  ? 9.992   3.294   11.691  1.00 49.73  ? 108 LEU A O   1 
ATOM   556  C  CB  . LEU A 1 74  ? 9.601   5.203   14.258  1.00 48.65  ? 108 LEU A CB  1 
ATOM   557  C  CG  . LEU A 1 74  ? 9.486   5.566   15.740  1.00 50.67  ? 108 LEU A CG  1 
ATOM   558  C  CD1 . LEU A 1 74  ? 10.127  6.918   16.016  1.00 44.14  ? 108 LEU A CD1 1 
ATOM   559  C  CD2 . LEU A 1 74  ? 8.032   5.554   16.187  1.00 47.05  ? 108 LEU A CD2 1 
ATOM   560  N  N   . PRO A 1 75  ? 7.880   4.053   11.757  1.00 53.60  ? 109 PRO A N   1 
ATOM   561  C  CA  . PRO A 1 75  ? 7.737   3.932   10.303  1.00 48.80  ? 109 PRO A CA  1 
ATOM   562  C  C   . PRO A 1 75  ? 8.644   4.900   9.563   1.00 49.93  ? 109 PRO A C   1 
ATOM   563  O  O   . PRO A 1 75  ? 8.949   5.996   10.039  1.00 54.98  ? 109 PRO A O   1 
ATOM   564  C  CB  . PRO A 1 75  ? 6.259   4.263   10.063  1.00 48.83  ? 109 PRO A CB  1 
ATOM   565  C  CG  . PRO A 1 75  ? 5.868   5.100   11.234  1.00 48.81  ? 109 PRO A CG  1 
ATOM   566  C  CD  . PRO A 1 75  ? 6.653   4.561   12.394  1.00 50.01  ? 109 PRO A CD  1 
ATOM   567  N  N   . VAL A 1 76  ? 9.084   4.473   8.384   1.00 50.72  ? 110 VAL A N   1 
ATOM   568  C  CA  . VAL A 1 76  ? 9.891   5.309   7.503   1.00 49.56  ? 110 VAL A CA  1 
ATOM   569  C  C   . VAL A 1 76  ? 8.931   6.166   6.687   1.00 52.38  ? 110 VAL A C   1 
ATOM   570  O  O   . VAL A 1 76  ? 8.280   5.676   5.761   1.00 54.22  ? 110 VAL A O   1 
ATOM   571  C  CB  . VAL A 1 76  ? 10.800  4.466   6.600   1.00 54.70  ? 110 VAL A CB  1 
ATOM   572  C  CG1 . VAL A 1 76  ? 11.578  5.362   5.645   1.00 42.05  ? 110 VAL A CG1 1 
ATOM   573  C  CG2 . VAL A 1 76  ? 11.749  3.622   7.442   1.00 35.50  ? 110 VAL A CG2 1 
ATOM   574  N  N   . ALA A 1 77  ? 8.838   7.451   7.038   1.00 47.81  ? 111 ALA A N   1 
ATOM   575  C  CA  . ALA A 1 77  ? 7.847   8.322   6.412   1.00 43.79  ? 111 ALA A CA  1 
ATOM   576  C  C   . ALA A 1 77  ? 8.180   8.592   4.951   1.00 46.99  ? 111 ALA A C   1 
ATOM   577  O  O   . ALA A 1 77  ? 7.283   8.616   4.100   1.00 51.70  ? 111 ALA A O   1 
ATOM   578  C  CB  . ALA A 1 77  ? 7.738   9.634   7.187   1.00 43.91  ? 111 ALA A CB  1 
ATOM   579  N  N   . LEU A 1 78  ? 9.455   8.803   4.639   1.00 48.09  ? 112 LEU A N   1 
ATOM   580  C  CA  . LEU A 1 78  ? 9.859   9.090   3.270   1.00 51.03  ? 112 LEU A CA  1 
ATOM   581  C  C   . LEU A 1 78  ? 11.330  8.738   3.110   1.00 39.54  ? 112 LEU A C   1 
ATOM   582  O  O   . LEU A 1 78  ? 12.046  8.505   4.087   1.00 42.21  ? 112 LEU A O   1 
ATOM   583  C  CB  . LEU A 1 78  ? 9.603   10.556  2.904   1.00 42.61  ? 112 LEU A CB  1 
ATOM   584  C  CG  . LEU A 1 78  ? 10.335  11.603  3.746   1.00 51.67  ? 112 LEU A CG  1 
ATOM   585  C  CD1 . LEU A 1 78  ? 11.493  12.208  2.967   1.00 45.67  ? 112 LEU A CD1 1 
ATOM   586  C  CD2 . LEU A 1 78  ? 9.374   12.687  4.208   1.00 50.86  ? 112 LEU A CD2 1 
ATOM   587  N  N   . ALA A 1 79  ? 11.773  8.709   1.856   1.00 42.30  ? 113 ALA A N   1 
ATOM   588  C  CA  . ALA A 1 79  ? 13.161  8.421   1.528   1.00 43.64  ? 113 ALA A CA  1 
ATOM   589  C  C   . ALA A 1 79  ? 13.582  9.275   0.344   1.00 45.20  ? 113 ALA A C   1 
ATOM   590  O  O   . ALA A 1 79  ? 12.915  9.276   -0.694  1.00 45.46  ? 113 ALA A O   1 
ATOM   591  C  CB  . ALA A 1 79  ? 13.361  6.937   1.209   1.00 39.19  ? 113 ALA A CB  1 
ATOM   592  N  N   . VAL A 1 80  ? 14.681  10.005  0.506   1.00 41.09  ? 114 VAL A N   1 
ATOM   593  C  CA  . VAL A 1 80  ? 15.272  10.800  -0.561  1.00 46.44  ? 114 VAL A CA  1 
ATOM   594  C  C   . VAL A 1 80  ? 16.538  10.096  -1.024  1.00 42.61  ? 114 VAL A C   1 
ATOM   595  O  O   . VAL A 1 80  ? 17.238  9.473   -0.220  1.00 45.64  ? 114 VAL A O   1 
ATOM   596  C  CB  . VAL A 1 80  ? 15.580  12.237  -0.094  1.00 43.11  ? 114 VAL A CB  1 
ATOM   597  C  CG1 . VAL A 1 80  ? 15.838  13.146  -1.288  1.00 41.60  ? 114 VAL A CG1 1 
ATOM   598  C  CG2 . VAL A 1 80  ? 14.439  12.775  0.756   1.00 42.55  ? 114 VAL A CG2 1 
ATOM   599  N  N   . VAL A 1 81  ? 16.817  10.169  -2.322  1.00 40.06  ? 115 VAL A N   1 
ATOM   600  C  CA  . VAL A 1 81  ? 18.064  9.668   -2.885  1.00 41.37  ? 115 VAL A CA  1 
ATOM   601  C  C   . VAL A 1 81  ? 18.743  10.817  -3.614  1.00 50.33  ? 115 VAL A C   1 
ATOM   602  O  O   . VAL A 1 81  ? 18.075  11.661  -4.223  1.00 41.33  ? 115 VAL A O   1 
ATOM   603  C  CB  . VAL A 1 81  ? 17.842  8.457   -3.817  1.00 46.09  ? 115 VAL A CB  1 
ATOM   604  C  CG1 . VAL A 1 81  ? 17.248  7.295   -3.036  1.00 43.48  ? 115 VAL A CG1 1 
ATOM   605  C  CG2 . VAL A 1 81  ? 16.943  8.824   -4.975  1.00 46.60  ? 115 VAL A CG2 1 
ATOM   606  N  N   . THR A 1 82  ? 20.072  10.855  -3.541  1.00 44.13  ? 116 THR A N   1 
ATOM   607  C  CA  . THR A 1 82  ? 20.806  12.055  -3.922  1.00 39.40  ? 116 THR A CA  1 
ATOM   608  C  C   . THR A 1 82  ? 21.111  12.135  -5.412  1.00 46.07  ? 116 THR A C   1 
ATOM   609  O  O   . THR A 1 82  ? 21.192  13.245  -5.953  1.00 48.15  ? 116 THR A O   1 
ATOM   610  C  CB  . THR A 1 82  ? 22.105  12.149  -3.119  1.00 43.16  ? 116 THR A CB  1 
ATOM   611  O  OG1 . THR A 1 82  ? 22.656  10.840  -2.947  1.00 58.96  ? 116 THR A OG1 1 
ATOM   612  C  CG2 . THR A 1 82  ? 21.830  12.747  -1.748  1.00 41.46  ? 116 THR A CG2 1 
ATOM   613  N  N   . HIS A 1 83  ? 21.282  11.003  -6.089  1.00 35.52  ? 117 HIS A N   1 
ATOM   614  C  CA  . HIS A 1 83  ? 21.452  10.995  -7.539  1.00 42.48  ? 117 HIS A CA  1 
ATOM   615  C  C   . HIS A 1 83  ? 21.307  9.562   -8.034  1.00 44.19  ? 117 HIS A C   1 
ATOM   616  O  O   . HIS A 1 83  ? 21.229  8.615   -7.247  1.00 41.54  ? 117 HIS A O   1 
ATOM   617  C  CB  . HIS A 1 83  ? 22.797  11.586  -7.967  1.00 44.36  ? 117 HIS A CB  1 
ATOM   618  C  CG  . HIS A 1 83  ? 23.978  10.813  -7.476  1.00 45.94  ? 117 HIS A CG  1 
ATOM   619  N  ND1 . HIS A 1 83  ? 24.535  11.015  -6.232  1.00 46.95  ? 117 HIS A ND1 1 
ATOM   620  C  CD2 . HIS A 1 83  ? 24.708  9.834   -8.061  1.00 51.38  ? 117 HIS A CD2 1 
ATOM   621  C  CE1 . HIS A 1 83  ? 25.558  10.195  -6.073  1.00 52.98  ? 117 HIS A CE1 1 
ATOM   622  N  NE2 . HIS A 1 83  ? 25.683  9.467   -7.167  1.00 50.17  ? 117 HIS A NE2 1 
ATOM   623  N  N   . ALA A 1 84  ? 21.284  9.418   -9.361  1.00 42.97  ? 118 ALA A N   1 
ATOM   624  C  CA  . ALA A 1 84  ? 20.994  8.136   -10.004 1.00 47.19  ? 118 ALA A CA  1 
ATOM   625  C  C   . ALA A 1 84  ? 22.296  7.373   -10.229 1.00 47.08  ? 118 ALA A C   1 
ATOM   626  O  O   . ALA A 1 84  ? 22.861  7.342   -11.323 1.00 46.01  ? 118 ALA A O   1 
ATOM   627  C  CB  . ALA A 1 84  ? 20.235  8.352   -11.307 1.00 47.16  ? 118 ALA A CB  1 
ATOM   628  N  N   . HIS A 1 85  ? 22.774  6.742   -9.159  1.00 47.36  ? 119 HIS A N   1 
ATOM   629  C  CA  . HIS A 1 85  ? 23.905  5.828   -9.228  1.00 47.81  ? 119 HIS A CA  1 
ATOM   630  C  C   . HIS A 1 85  ? 23.619  4.644   -8.315  1.00 47.04  ? 119 HIS A C   1 
ATOM   631  O  O   . HIS A 1 85  ? 22.764  4.713   -7.429  1.00 52.09  ? 119 HIS A O   1 
ATOM   632  C  CB  . HIS A 1 85  ? 25.224  6.515   -8.843  1.00 51.66  ? 119 HIS A CB  1 
ATOM   633  C  CG  . HIS A 1 85  ? 25.976  7.077   -10.010 1.00 54.07  ? 119 HIS A CG  1 
ATOM   634  N  ND1 . HIS A 1 85  ? 27.067  7.907   -9.863  1.00 50.35  ? 119 HIS A ND1 1 
ATOM   635  C  CD2 . HIS A 1 85  ? 25.798  6.926   -11.344 1.00 52.33  ? 119 HIS A CD2 1 
ATOM   636  C  CE1 . HIS A 1 85  ? 27.526  8.245   -11.055 1.00 50.45  ? 119 HIS A CE1 1 
ATOM   637  N  NE2 . HIS A 1 85  ? 26.772  7.663   -11.971 1.00 49.02  ? 119 HIS A NE2 1 
ATOM   638  N  N   . GLN A 1 86  ? 24.353  3.549   -8.543  1.00 58.01  ? 120 GLN A N   1 
ATOM   639  C  CA  . GLN A 1 86  ? 24.030  2.282   -7.890  1.00 52.23  ? 120 GLN A CA  1 
ATOM   640  C  C   . GLN A 1 86  ? 24.065  2.400   -6.371  1.00 51.58  ? 120 GLN A C   1 
ATOM   641  O  O   . GLN A 1 86  ? 23.199  1.851   -5.679  1.00 51.96  ? 120 GLN A O   1 
ATOM   642  C  CB  . GLN A 1 86  ? 24.985  1.186   -8.359  1.00 58.09  ? 120 GLN A CB  1 
ATOM   643  C  CG  . GLN A 1 86  ? 24.385  -0.209  -8.296  1.00 61.26  ? 120 GLN A CG  1 
ATOM   644  C  CD  . GLN A 1 86  ? 25.294  -1.263  -8.893  1.00 85.24  ? 120 GLN A CD  1 
ATOM   645  O  OE1 . GLN A 1 86  ? 26.327  -0.947  -9.483  1.00 94.10  ? 120 GLN A OE1 1 
ATOM   646  N  NE2 . GLN A 1 86  ? 24.915  -2.527  -8.739  1.00 86.06  ? 120 GLN A NE2 1 
ATOM   647  N  N   . ASP A 1 87  ? 25.054  3.112   -5.831  1.00 51.10  ? 121 ASP A N   1 
ATOM   648  C  CA  . ASP A 1 87  ? 25.184  3.229   -4.385  1.00 51.75  ? 121 ASP A CA  1 
ATOM   649  C  C   . ASP A 1 87  ? 24.102  4.098   -3.758  1.00 51.27  ? 121 ASP A C   1 
ATOM   650  O  O   . ASP A 1 87  ? 24.030  4.170   -2.526  1.00 51.26  ? 121 ASP A O   1 
ATOM   651  C  CB  . ASP A 1 87  ? 26.561  3.790   -4.030  1.00 53.56  ? 121 ASP A CB  1 
ATOM   652  C  CG  . ASP A 1 87  ? 26.907  5.031   -4.829  1.00 59.76  ? 121 ASP A CG  1 
ATOM   653  O  OD1 . ASP A 1 87  ? 26.201  5.323   -5.817  1.00 60.89  ? 121 ASP A OD1 1 
ATOM   654  O  OD2 . ASP A 1 87  ? 27.885  5.717   -4.467  1.00 67.09  ? 121 ASP A OD2 1 
ATOM   655  N  N   . LYS A 1 88  ? 23.263  4.747   -4.561  1.00 48.98  ? 122 LYS A N   1 
ATOM   656  C  CA  . LYS A 1 88  ? 22.263  5.682   -4.062  1.00 49.89  ? 122 LYS A CA  1 
ATOM   657  C  C   . LYS A 1 88  ? 20.832  5.231   -4.303  1.00 50.57  ? 122 LYS A C   1 
ATOM   658  O  O   . LYS A 1 88  ? 19.981  5.410   -3.429  1.00 48.94  ? 122 LYS A O   1 
ATOM   659  C  CB  . LYS A 1 88  ? 22.474  7.059   -4.701  1.00 57.32  ? 122 LYS A CB  1 
ATOM   660  C  CG  . LYS A 1 88  ? 23.908  7.557   -4.604  1.00 53.44  ? 122 LYS A CG  1 
ATOM   661  C  CD  . LYS A 1 88  ? 24.187  8.163   -3.240  1.00 50.88  ? 122 LYS A CD  1 
ATOM   662  C  CE  . LYS A 1 88  ? 25.181  7.338   -2.442  1.00 59.91  ? 122 LYS A CE  1 
ATOM   663  N  NZ  . LYS A 1 88  ? 25.135  7.690   -0.995  1.00 42.00  ? 122 LYS A NZ  1 
ATOM   664  N  N   . MET A 1 89  ? 20.537  4.650   -5.468  1.00 44.34  ? 123 MET A N   1 
ATOM   665  C  CA  . MET A 1 89  ? 19.195  4.168   -5.779  1.00 48.87  ? 123 MET A CA  1 
ATOM   666  C  C   . MET A 1 89  ? 19.172  2.667   -6.042  1.00 51.50  ? 123 MET A C   1 
ATOM   667  O  O   . MET A 1 89  ? 18.231  2.165   -6.666  1.00 47.54  ? 123 MET A O   1 
ATOM   668  C  CB  . MET A 1 89  ? 18.611  4.925   -6.975  1.00 46.24  ? 123 MET A CB  1 
ATOM   669  C  CG  . MET A 1 89  ? 18.849  6.424   -6.945  1.00 57.26  ? 123 MET A CG  1 
ATOM   670  S  SD  . MET A 1 89  ? 17.984  7.300   -8.264  1.00 54.05  ? 123 MET A SD  1 
ATOM   671  C  CE  . MET A 1 89  ? 16.402  6.463   -8.254  1.00 58.64  ? 123 MET A CE  1 
ATOM   672  N  N   . GLY A 1 90  ? 20.191  1.939   -5.582  1.00 51.37  ? 124 GLY A N   1 
ATOM   673  C  CA  . GLY A 1 90  ? 20.237  0.505   -5.802  1.00 44.71  ? 124 GLY A CA  1 
ATOM   674  C  C   . GLY A 1 90  ? 19.194  -0.278  -5.032  1.00 48.43  ? 124 GLY A C   1 
ATOM   675  O  O   . GLY A 1 90  ? 18.862  -1.401  -5.428  1.00 57.33  ? 124 GLY A O   1 
ATOM   676  N  N   . GLY A 1 91  ? 18.668  0.284   -3.946  1.00 43.49  ? 125 GLY A N   1 
ATOM   677  C  CA  . GLY A 1 91  ? 17.677  -0.404  -3.141  1.00 45.26  ? 125 GLY A CA  1 
ATOM   678  C  C   . GLY A 1 91  ? 16.292  0.194   -3.266  1.00 52.75  ? 125 GLY A C   1 
ATOM   679  O  O   . GLY A 1 91  ? 15.528  0.223   -2.296  1.00 50.80  ? 125 GLY A O   1 
ATOM   680  N  N   . MET A 1 92  ? 15.960  0.674   -4.469  1.00 57.29  ? 126 MET A N   1 
ATOM   681  C  CA  . MET A 1 92  ? 14.678  1.338   -4.689  1.00 51.47  ? 126 MET A CA  1 
ATOM   682  C  C   . MET A 1 92  ? 13.520  0.352   -4.619  1.00 53.88  ? 126 MET A C   1 
ATOM   683  O  O   . MET A 1 92  ? 12.477  0.660   -4.032  1.00 50.55  ? 126 MET A O   1 
ATOM   684  C  CB  . MET A 1 92  ? 14.696  2.062   -6.035  1.00 51.97  ? 126 MET A CB  1 
ATOM   685  C  CG  . MET A 1 92  ? 15.128  3.548   -6.012  1.00 53.34  ? 126 MET A CG  1 
ATOM   686  S  SD  . MET A 1 92  ? 14.162  4.727   -5.030  1.00 73.93  ? 126 MET A SD  1 
ATOM   687  C  CE  . MET A 1 92  ? 14.765  4.530   -3.361  1.00 64.57  ? 126 MET A CE  1 
ATOM   688  N  N   . GLY A 1 93  ? 13.679  -0.833  -5.217  1.00 54.24  ? 127 GLY A N   1 
ATOM   689  C  CA  . GLY A 1 93  ? 12.637  -1.842  -5.133  1.00 50.64  ? 127 GLY A CA  1 
ATOM   690  C  C   . GLY A 1 93  ? 12.369  -2.303  -3.714  1.00 47.06  ? 127 GLY A C   1 
ATOM   691  O  O   . GLY A 1 93  ? 11.246  -2.693  -3.386  1.00 59.74  ? 127 GLY A O   1 
ATOM   692  N  N   . ALA A 1 94  ? 13.389  -2.265  -2.854  1.00 48.89  ? 128 ALA A N   1 
ATOM   693  C  CA  . ALA A 1 94  ? 13.191  -2.644  -1.458  1.00 46.35  ? 128 ALA A CA  1 
ATOM   694  C  C   . ALA A 1 94  ? 12.348  -1.610  -0.720  1.00 55.37  ? 128 ALA A C   1 
ATOM   695  O  O   . ALA A 1 94  ? 11.513  -1.966  0.119   1.00 57.34  ? 128 ALA A O   1 
ATOM   696  C  CB  . ALA A 1 94  ? 14.541  -2.831  -0.767  1.00 49.84  ? 128 ALA A CB  1 
ATOM   697  N  N   . LEU A 1 95  ? 12.550  -0.325  -1.019  1.00 48.98  ? 129 LEU A N   1 
ATOM   698  C  CA  . LEU A 1 95  ? 11.744  0.708   -0.381  1.00 51.53  ? 129 LEU A CA  1 
ATOM   699  C  C   . LEU A 1 95  ? 10.330  0.743   -0.946  1.00 52.38  ? 129 LEU A C   1 
ATOM   700  O  O   . LEU A 1 95  ? 9.378   1.035   -0.213  1.00 55.85  ? 129 LEU A O   1 
ATOM   701  C  CB  . LEU A 1 95  ? 12.412  2.073   -0.535  1.00 42.75  ? 129 LEU A CB  1 
ATOM   702  C  CG  . LEU A 1 95  ? 13.757  2.226   0.176   1.00 47.76  ? 129 LEU A CG  1 
ATOM   703  C  CD1 . LEU A 1 95  ? 14.265  3.653   0.053   1.00 57.51  ? 129 LEU A CD1 1 
ATOM   704  C  CD2 . LEU A 1 95  ? 13.638  1.809   1.634   1.00 41.67  ? 129 LEU A CD2 1 
ATOM   705  N  N   . HIS A 1 96  ? 10.171  0.445   -2.238  1.00 54.08  ? 130 HIS A N   1 
ATOM   706  C  CA  . HIS A 1 96  ? 8.839   0.430   -2.831  1.00 51.68  ? 130 HIS A CA  1 
ATOM   707  C  C   . HIS A 1 96  ? 8.044   -0.795  -2.399  1.00 55.16  ? 130 HIS A C   1 
ATOM   708  O  O   . HIS A 1 96  ? 6.808   -0.758  -2.391  1.00 53.43  ? 130 HIS A O   1 
ATOM   709  C  CB  . HIS A 1 96  ? 8.940   0.487   -4.354  1.00 55.30  ? 130 HIS A CB  1 
ATOM   710  C  CG  . HIS A 1 96  ? 9.457   1.791   -4.876  1.00 53.08  ? 130 HIS A CG  1 
ATOM   711  N  ND1 . HIS A 1 96  ? 10.007  1.925   -6.132  1.00 54.81  ? 130 HIS A ND1 1 
ATOM   712  C  CD2 . HIS A 1 96  ? 9.508   3.019   -4.309  1.00 42.82  ? 130 HIS A CD2 1 
ATOM   713  C  CE1 . HIS A 1 96  ? 10.373  3.181   -6.318  1.00 56.83  ? 130 HIS A CE1 1 
ATOM   714  N  NE2 . HIS A 1 96  ? 10.081  3.866   -5.227  1.00 55.41  ? 130 HIS A NE2 1 
ATOM   715  N  N   . ALA A 1 97  ? 8.728   -1.883  -2.037  1.00 56.17  ? 131 ALA A N   1 
ATOM   716  C  CA  . ALA A 1 97  ? 8.027   -3.078  -1.582  1.00 53.32  ? 131 ALA A CA  1 
ATOM   717  C  C   . ALA A 1 97  ? 7.374   -2.865  -0.223  1.00 51.03  ? 131 ALA A C   1 
ATOM   718  O  O   . ALA A 1 97  ? 6.353   -3.493  0.077   1.00 60.14  ? 131 ALA A O   1 
ATOM   719  C  CB  . ALA A 1 97  ? 8.988   -4.266  -1.530  1.00 51.40  ? 131 ALA A CB  1 
ATOM   720  N  N   . GLU A 1 98  ? 7.942   -1.990  0.606   1.00 52.43  ? 132 GLU A N   1 
ATOM   721  C  CA  . GLU A 1 98  ? 7.389   -1.675  1.915   1.00 52.50  ? 132 GLU A CA  1 
ATOM   722  C  C   . GLU A 1 98  ? 6.513   -0.428  1.894   1.00 57.76  ? 132 GLU A C   1 
ATOM   723  O  O   . GLU A 1 98  ? 6.176   0.096   2.961   1.00 55.28  ? 132 GLU A O   1 
ATOM   724  C  CB  . GLU A 1 98  ? 8.515   -1.508  2.937   1.00 51.72  ? 132 GLU A CB  1 
ATOM   725  C  CG  . GLU A 1 98  ? 9.561   -2.611  2.888   1.00 71.63  ? 132 GLU A CG  1 
ATOM   726  C  CD  . GLU A 1 98  ? 9.243   -3.760  3.825   1.00 73.78  ? 132 GLU A CD  1 
ATOM   727  O  OE1 . GLU A 1 98  ? 9.751   -4.877  3.592   1.00 84.09  ? 132 GLU A OE1 1 
ATOM   728  O  OE2 . GLU A 1 98  ? 8.486   -3.545  4.795   1.00 81.65  ? 132 GLU A OE2 1 
ATOM   729  N  N   . ALA A 1 99  ? 6.143   0.055   0.705   1.00 55.97  ? 133 ALA A N   1 
ATOM   730  C  CA  . ALA A 1 99  ? 5.265   1.217   0.546   1.00 53.36  ? 133 ALA A CA  1 
ATOM   731  C  C   . ALA A 1 99  ? 5.843   2.453   1.236   1.00 55.65  ? 133 ALA A C   1 
ATOM   732  O  O   . ALA A 1 99  ? 5.170   3.133   2.014   1.00 57.16  ? 133 ALA A O   1 
ATOM   733  C  CB  . ALA A 1 99  ? 3.852   0.913   1.051   1.00 54.13  ? 133 ALA A CB  1 
ATOM   734  N  N   . ILE A 1 100 ? 7.104   2.741   0.942   1.00 52.66  ? 134 ILE A N   1 
ATOM   735  C  CA  . ILE A 1 100 ? 7.798   3.906   1.482   1.00 53.57  ? 134 ILE A CA  1 
ATOM   736  C  C   . ILE A 1 100 ? 7.843   4.973   0.392   1.00 53.05  ? 134 ILE A C   1 
ATOM   737  O  O   . ILE A 1 100 ? 8.388   4.708   -0.690  1.00 54.76  ? 134 ILE A O   1 
ATOM   738  C  CB  . ILE A 1 100 ? 9.213   3.552   1.961   1.00 46.55  ? 134 ILE A CB  1 
ATOM   739  C  CG1 . ILE A 1 100 ? 9.150   2.622   3.174   1.00 45.69  ? 134 ILE A CG1 1 
ATOM   740  C  CG2 . ILE A 1 100 ? 9.993   4.816   2.293   1.00 40.33  ? 134 ILE A CG2 1 
ATOM   741  C  CD1 . ILE A 1 100 ? 10.507  2.166   3.665   1.00 41.14  ? 134 ILE A CD1 1 
ATOM   742  N  N   . PRO A 1 101 ? 7.285   6.162   0.620   1.00 50.45  ? 135 PRO A N   1 
ATOM   743  C  CA  . PRO A 1 101 ? 7.362   7.227   -0.393  1.00 50.50  ? 135 PRO A CA  1 
ATOM   744  C  C   . PRO A 1 101 ? 8.803   7.638   -0.651  1.00 50.42  ? 135 PRO A C   1 
ATOM   745  O  O   . PRO A 1 101 ? 9.533   8.024   0.264   1.00 51.69  ? 135 PRO A O   1 
ATOM   746  C  CB  . PRO A 1 101 ? 6.548   8.368   0.231   1.00 47.58  ? 135 PRO A CB  1 
ATOM   747  C  CG  . PRO A 1 101 ? 5.687   7.713   1.266   1.00 44.90  ? 135 PRO A CG  1 
ATOM   748  C  CD  . PRO A 1 101 ? 6.482   6.559   1.787   1.00 49.30  ? 135 PRO A CD  1 
ATOM   749  N  N   . THR A 1 102 ? 9.211   7.551   -1.914  1.00 48.75  ? 136 THR A N   1 
ATOM   750  C  CA  . THR A 1 102 ? 10.577  7.844   -2.323  1.00 50.81  ? 136 THR A CA  1 
ATOM   751  C  C   . THR A 1 102 ? 10.618  9.130   -3.137  1.00 46.00  ? 136 THR A C   1 
ATOM   752  O  O   . THR A 1 102 ? 9.753   9.370   -3.984  1.00 41.59  ? 136 THR A O   1 
ATOM   753  C  CB  . THR A 1 102 ? 11.164  6.688   -3.137  1.00 54.33  ? 136 THR A CB  1 
ATOM   754  O  OG1 . THR A 1 102 ? 10.380  6.487   -4.320  1.00 47.24  ? 136 THR A OG1 1 
ATOM   755  C  CG2 . THR A 1 102 ? 11.169  5.408   -2.313  1.00 42.94  ? 136 THR A CG2 1 
ATOM   756  N  N   . TYR A 1 103 ? 11.631  9.955   -2.876  1.00 43.14  ? 137 TYR A N   1 
ATOM   757  C  CA  . TYR A 1 103 ? 11.784  11.245  -3.532  1.00 41.52  ? 137 TYR A CA  1 
ATOM   758  C  C   . TYR A 1 103 ? 13.163  11.341  -4.165  1.00 40.16  ? 137 TYR A C   1 
ATOM   759  O  O   . TYR A 1 103 ? 14.147  10.841  -3.613  1.00 39.63  ? 137 TYR A O   1 
ATOM   760  C  CB  . TYR A 1 103 ? 11.582  12.401  -2.543  1.00 38.48  ? 137 TYR A CB  1 
ATOM   761  C  CG  . TYR A 1 103 ? 10.162  12.538  -2.045  1.00 50.37  ? 137 TYR A CG  1 
ATOM   762  C  CD1 . TYR A 1 103 ? 9.676   11.714  -1.038  1.00 45.21  ? 137 TYR A CD1 1 
ATOM   763  C  CD2 . TYR A 1 103 ? 9.306   13.491  -2.582  1.00 48.22  ? 137 TYR A CD2 1 
ATOM   764  C  CE1 . TYR A 1 103 ? 8.378   11.833  -0.582  1.00 51.28  ? 137 TYR A CE1 1 
ATOM   765  C  CE2 . TYR A 1 103 ? 8.006   13.619  -2.132  1.00 50.63  ? 137 TYR A CE2 1 
ATOM   766  C  CZ  . TYR A 1 103 ? 7.548   12.787  -1.132  1.00 57.97  ? 137 TYR A CZ  1 
ATOM   767  O  OH  . TYR A 1 103 ? 6.254   12.910  -0.679  1.00 70.47  ? 137 TYR A OH  1 
ATOM   768  N  N   . ALA A 1 104 ? 13.226  11.989  -5.325  1.00 38.94  ? 138 ALA A N   1 
ATOM   769  C  CA  . ALA A 1 104 ? 14.487  12.179  -6.027  1.00 45.01  ? 138 ALA A CA  1 
ATOM   770  C  C   . ALA A 1 104 ? 14.364  13.388  -6.938  1.00 42.39  ? 138 ALA A C   1 
ATOM   771  O  O   . ALA A 1 104 ? 13.260  13.833  -7.264  1.00 41.12  ? 138 ALA A O   1 
ATOM   772  C  CB  . ALA A 1 104 ? 14.876  10.943  -6.842  1.00 43.37  ? 138 ALA A CB  1 
ATOM   773  N  N   . ASN A 1 105 ? 15.518  13.915  -7.338  1.00 34.71  ? 139 ASN A N   1 
ATOM   774  C  CA  . ASN A 1 105 ? 15.547  14.965  -8.346  1.00 40.67  ? 139 ASN A CA  1 
ATOM   775  C  C   . ASN A 1 105 ? 14.870  14.471  -9.618  1.00 41.16  ? 139 ASN A C   1 
ATOM   776  O  O   . ASN A 1 105 ? 14.997  13.302  -9.994  1.00 45.26  ? 139 ASN A O   1 
ATOM   777  C  CB  . ASN A 1 105 ? 16.992  15.381  -8.633  1.00 42.02  ? 139 ASN A CB  1 
ATOM   778  C  CG  . ASN A 1 105 ? 17.094  16.511  -9.644  1.00 39.07  ? 139 ASN A CG  1 
ATOM   779  O  OD1 . ASN A 1 105 ? 16.093  17.120  -10.022 1.00 40.50  ? 139 ASN A OD1 1 
ATOM   780  N  ND2 . ASN A 1 105 ? 18.314  16.798  -10.085 1.00 39.82  ? 139 ASN A ND2 1 
ATOM   781  N  N   . ALA A 1 106 ? 14.128  15.369  -10.272 1.00 36.53  ? 140 ALA A N   1 
ATOM   782  C  CA  . ALA A 1 106 ? 13.444  15.000  -11.507 1.00 40.03  ? 140 ALA A CA  1 
ATOM   783  C  C   . ALA A 1 106 ? 14.421  14.487  -12.556 1.00 42.37  ? 140 ALA A C   1 
ATOM   784  O  O   . ALA A 1 106 ? 14.077  13.594  -13.339 1.00 41.23  ? 140 ALA A O   1 
ATOM   785  C  CB  . ALA A 1 106 ? 12.657  16.194  -12.049 1.00 45.39  ? 140 ALA A CB  1 
ATOM   786  N  N   . LEU A 1 107 ? 15.641  15.027  -12.582 1.00 45.66  ? 141 LEU A N   1 
ATOM   787  C  CA  . LEU A 1 107 ? 16.653  14.519  -13.501 1.00 43.97  ? 141 LEU A CA  1 
ATOM   788  C  C   . LEU A 1 107 ? 17.120  13.127  -13.092 1.00 44.84  ? 141 LEU A C   1 
ATOM   789  O  O   . LEU A 1 107 ? 17.374  12.275  -13.952 1.00 44.70  ? 141 LEU A O   1 
ATOM   790  C  CB  . LEU A 1 107 ? 17.834  15.488  -13.569 1.00 46.59  ? 141 LEU A CB  1 
ATOM   791  C  CG  . LEU A 1 107 ? 19.013  15.077  -14.454 1.00 45.46  ? 141 LEU A CG  1 
ATOM   792  C  CD1 . LEU A 1 107 ? 18.551  14.770  -15.871 1.00 45.41  ? 141 LEU A CD1 1 
ATOM   793  C  CD2 . LEU A 1 107 ? 20.082  16.157  -14.458 1.00 43.56  ? 141 LEU A CD2 1 
ATOM   794  N  N   . SER A 1 108 ? 17.236  12.876  -11.785 1.00 38.52  ? 142 SER A N   1 
ATOM   795  C  CA  . SER A 1 108 ? 17.635  11.552  -11.319 1.00 38.59  ? 142 SER A CA  1 
ATOM   796  C  C   . SER A 1 108 ? 16.631  10.487  -11.736 1.00 46.61  ? 142 SER A C   1 
ATOM   797  O  O   . SER A 1 108 ? 17.016  9.349   -12.030 1.00 40.37  ? 142 SER A O   1 
ATOM   798  C  CB  . SER A 1 108 ? 17.802  11.553  -9.799  1.00 40.99  ? 142 SER A CB  1 
ATOM   799  O  OG  . SER A 1 108 ? 18.604  12.639  -9.370  1.00 47.52  ? 142 SER A OG  1 
ATOM   800  N  N   . ASN A 1 109 ? 15.344  10.835  -11.770 1.00 45.14  ? 143 ASN A N   1 
ATOM   801  C  CA  . ASN A 1 109 ? 14.330  9.882   -12.200 1.00 40.66  ? 143 ASN A CA  1 
ATOM   802  C  C   . ASN A 1 109 ? 14.335  9.692   -13.711 1.00 45.19  ? 143 ASN A C   1 
ATOM   803  O  O   . ASN A 1 109 ? 13.969  8.615   -14.196 1.00 49.38  ? 143 ASN A O   1 
ATOM   804  C  CB  . ASN A 1 109 ? 12.952  10.337  -11.720 1.00 43.90  ? 143 ASN A CB  1 
ATOM   805  C  CG  . ASN A 1 109 ? 12.819  10.285  -10.211 1.00 44.42  ? 143 ASN A CG  1 
ATOM   806  O  OD1 . ASN A 1 109 ? 13.328  9.369   -9.565  1.00 45.69  ? 143 ASN A OD1 1 
ATOM   807  N  ND2 . ASN A 1 109 ? 12.138  11.271  -9.640  1.00 46.79  ? 143 ASN A ND2 1 
ATOM   808  N  N   . GLN A 1 110 ? 14.747  10.713  -14.466 1.00 46.16  ? 144 GLN A N   1 
ATOM   809  C  CA  . GLN A 1 110 ? 14.888  10.550  -15.909 1.00 52.74  ? 144 GLN A CA  1 
ATOM   810  C  C   . GLN A 1 110 ? 16.127  9.735   -16.262 1.00 51.30  ? 144 GLN A C   1 
ATOM   811  O  O   . GLN A 1 110 ? 16.161  9.085   -17.313 1.00 53.67  ? 144 GLN A O   1 
ATOM   812  C  CB  . GLN A 1 110 ? 14.948  11.917  -16.593 1.00 47.07  ? 144 GLN A CB  1 
ATOM   813  C  CG  . GLN A 1 110 ? 13.714  12.780  -16.389 1.00 53.01  ? 144 GLN A CG  1 
ATOM   814  C  CD  . GLN A 1 110 ? 13.811  14.111  -17.112 1.00 59.18  ? 144 GLN A CD  1 
ATOM   815  O  OE1 . GLN A 1 110 ? 14.632  14.283  -18.013 1.00 60.08  ? 144 GLN A OE1 1 
ATOM   816  N  NE2 . GLN A 1 110 ? 12.975  15.063  -16.713 1.00 54.19  ? 144 GLN A NE2 1 
ATOM   817  N  N   . LEU A 1 111 ? 17.146  9.755   -15.402 1.00 51.45  ? 145 LEU A N   1 
ATOM   818  C  CA  . LEU A 1 111 ? 18.396  9.056   -15.668 1.00 50.66  ? 145 LEU A CA  1 
ATOM   819  C  C   . LEU A 1 111 ? 18.430  7.646   -15.099 1.00 57.68  ? 145 LEU A C   1 
ATOM   820  O  O   . LEU A 1 111 ? 19.229  6.827   -15.566 1.00 56.87  ? 145 LEU A O   1 
ATOM   821  C  CB  . LEU A 1 111 ? 19.577  9.847   -15.095 1.00 46.30  ? 145 LEU A CB  1 
ATOM   822  C  CG  . LEU A 1 111 ? 20.078  11.052  -15.891 1.00 49.78  ? 145 LEU A CG  1 
ATOM   823  C  CD1 . LEU A 1 111 ? 20.914  11.957  -15.000 1.00 45.99  ? 145 LEU A CD1 1 
ATOM   824  C  CD2 . LEU A 1 111 ? 20.876  10.602  -17.105 1.00 54.01  ? 145 LEU A CD2 1 
ATOM   825  N  N   . ALA A 1 112 ? 17.592  7.348   -14.105 1.00 62.28  ? 146 ALA A N   1 
ATOM   826  C  CA  . ALA A 1 112 ? 17.638  6.038   -13.457 1.00 59.47  ? 146 ALA A CA  1 
ATOM   827  C  C   . ALA A 1 112 ? 17.399  4.881   -14.421 1.00 63.30  ? 146 ALA A C   1 
ATOM   828  O  O   . ALA A 1 112 ? 18.157  3.897   -14.361 1.00 62.15  ? 146 ALA A O   1 
ATOM   829  C  CB  . ALA A 1 112 ? 16.647  6.009   -12.288 1.00 53.33  ? 146 ALA A CB  1 
ATOM   830  N  N   . PRO A 1 113 ? 16.399  4.909   -15.311 1.00 67.16  ? 147 PRO A N   1 
ATOM   831  C  CA  . PRO A 1 113 ? 16.245  3.776   -16.238 1.00 75.26  ? 147 PRO A CA  1 
ATOM   832  C  C   . PRO A 1 113 ? 17.404  3.631   -17.209 1.00 75.10  ? 147 PRO A C   1 
ATOM   833  O  O   . PRO A 1 113 ? 17.648  2.521   -17.697 1.00 78.75  ? 147 PRO A O   1 
ATOM   834  C  CB  . PRO A 1 113 ? 14.932  4.090   -16.970 1.00 66.62  ? 147 PRO A CB  1 
ATOM   835  C  CG  . PRO A 1 113 ? 14.217  5.050   -16.086 1.00 65.23  ? 147 PRO A CG  1 
ATOM   836  C  CD  . PRO A 1 113 ? 15.294  5.874   -15.462 1.00 61.11  ? 147 PRO A CD  1 
ATOM   837  N  N   . GLN A 1 114 ? 18.129  4.714   -17.500 1.00 92.83  ? 148 GLN A N   1 
ATOM   838  C  CA  . GLN A 1 114 ? 19.265  4.626   -18.410 1.00 95.04  ? 148 GLN A CA  1 
ATOM   839  C  C   . GLN A 1 114 ? 20.430  3.849   -17.811 1.00 85.82  ? 148 GLN A C   1 
ATOM   840  O  O   . GLN A 1 114 ? 21.310  3.406   -18.556 1.00 85.12  ? 148 GLN A O   1 
ATOM   841  C  CB  . GLN A 1 114 ? 19.726  6.027   -18.816 1.00 93.08  ? 148 GLN A CB  1 
ATOM   842  C  CG  . GLN A 1 114 ? 18.629  6.884   -19.427 1.00 106.28 ? 148 GLN A CG  1 
ATOM   843  C  CD  . GLN A 1 114 ? 19.160  7.874   -20.446 1.00 107.70 ? 148 GLN A CD  1 
ATOM   844  O  OE1 . GLN A 1 114 ? 18.419  8.358   -21.302 1.00 97.35  ? 148 GLN A OE1 1 
ATOM   845  N  NE2 . GLN A 1 114 ? 20.449  8.182   -20.358 1.00 97.21  ? 148 GLN A NE2 1 
ATOM   846  N  N   . GLU A 1 115 ? 20.456  3.677   -16.489 1.00 78.42  ? 149 GLU A N   1 
ATOM   847  C  CA  . GLU A 1 115 ? 21.494  2.901   -15.818 1.00 79.70  ? 149 GLU A CA  1 
ATOM   848  C  C   . GLU A 1 115 ? 20.926  1.665   -15.131 1.00 77.44  ? 149 GLU A C   1 
ATOM   849  O  O   . GLU A 1 115 ? 21.575  1.098   -14.246 1.00 76.84  ? 149 GLU A O   1 
ATOM   850  C  CB  . GLU A 1 115 ? 22.245  3.772   -14.810 1.00 70.63  ? 149 GLU A CB  1 
ATOM   851  C  CG  . GLU A 1 115 ? 23.398  4.559   -15.409 1.00 69.82  ? 149 GLU A CG  1 
ATOM   852  C  CD  . GLU A 1 115 ? 23.481  5.968   -14.862 1.00 80.97  ? 149 GLU A CD  1 
ATOM   853  O  OE1 . GLU A 1 115 ? 24.169  6.809   -15.476 1.00 78.45  ? 149 GLU A OE1 1 
ATOM   854  O  OE2 . GLU A 1 115 ? 22.849  6.234   -13.820 1.00 81.81  ? 149 GLU A OE2 1 
ATOM   855  N  N   . GLY A 1 116 ? 19.727  1.237   -15.519 1.00 90.66  ? 150 GLY A N   1 
ATOM   856  C  CA  . GLY A 1 116 ? 19.108  0.067   -14.927 1.00 93.64  ? 150 GLY A CA  1 
ATOM   857  C  C   . GLY A 1 116 ? 18.724  0.269   -13.476 1.00 92.99  ? 150 GLY A C   1 
ATOM   858  O  O   . GLY A 1 116 ? 19.107  -0.523  -12.610 1.00 91.00  ? 150 GLY A O   1 
ATOM   859  N  N   . MET A 1 117 ? 17.970  1.329   -13.198 1.00 67.10  ? 151 MET A N   1 
ATOM   860  C  CA  . MET A 1 117 ? 17.557  1.660   -11.844 1.00 60.89  ? 151 MET A CA  1 
ATOM   861  C  C   . MET A 1 117 ? 16.057  1.906   -11.805 1.00 61.10  ? 151 MET A C   1 
ATOM   862  O  O   . MET A 1 117 ? 15.452  2.319   -12.798 1.00 58.16  ? 151 MET A O   1 
ATOM   863  C  CB  . MET A 1 117 ? 18.287  2.902   -11.315 1.00 67.81  ? 151 MET A CB  1 
ATOM   864  C  CG  . MET A 1 117 ? 19.767  2.942   -11.634 1.00 76.09  ? 151 MET A CG  1 
ATOM   865  S  SD  . MET A 1 117 ? 20.693  1.847   -10.551 1.00 78.13  ? 151 MET A SD  1 
ATOM   866  C  CE  . MET A 1 117 ? 20.717  2.840   -9.068  1.00 45.85  ? 151 MET A CE  1 
ATOM   867  N  N   . THR A 1 118 ? 15.464  1.647   -10.644 1.00 60.23  ? 152 THR A N   1 
ATOM   868  C  CA  . THR A 1 118 ? 14.068  1.989   -10.407 1.00 56.22  ? 152 THR A CA  1 
ATOM   869  C  C   . THR A 1 118 ? 13.984  3.455   -10.003 1.00 53.75  ? 152 THR A C   1 
ATOM   870  O  O   . THR A 1 118 ? 14.540  3.853   -8.976  1.00 49.13  ? 152 THR A O   1 
ATOM   871  C  CB  . THR A 1 118 ? 13.470  1.097   -9.322  1.00 55.51  ? 152 THR A CB  1 
ATOM   872  O  OG1 . THR A 1 118 ? 13.473  -0.267  -9.763  1.00 69.91  ? 152 THR A OG1 1 
ATOM   873  C  CG2 . THR A 1 118 ? 12.043  1.524   -9.008  1.00 56.02  ? 152 THR A CG2 1 
ATOM   874  N  N   . ALA A 1 119 ? 13.308  4.261   -10.815 1.00 55.19  ? 153 ALA A N   1 
ATOM   875  C  CA  . ALA A 1 119 ? 13.169  5.674   -10.500 1.00 59.34  ? 153 ALA A CA  1 
ATOM   876  C  C   . ALA A 1 119 ? 12.289  5.863   -9.270  1.00 48.96  ? 153 ALA A C   1 
ATOM   877  O  O   . ALA A 1 119 ? 11.406  5.051   -8.979  1.00 51.06  ? 153 ALA A O   1 
ATOM   878  C  CB  . ALA A 1 119 ? 12.582  6.434   -11.689 1.00 53.63  ? 153 ALA A CB  1 
ATOM   879  N  N   . ALA A 1 120 ? 12.547  6.942   -8.538  1.00 51.27  ? 154 ALA A N   1 
ATOM   880  C  CA  . ALA A 1 120 ? 11.725  7.264   -7.382  1.00 46.18  ? 154 ALA A CA  1 
ATOM   881  C  C   . ALA A 1 120 ? 10.314  7.632   -7.824  1.00 52.13  ? 154 ALA A C   1 
ATOM   882  O  O   . ALA A 1 120 ? 10.095  8.132   -8.931  1.00 54.99  ? 154 ALA A O   1 
ATOM   883  C  CB  . ALA A 1 120 ? 12.343  8.409   -6.581  1.00 43.36  ? 154 ALA A CB  1 
ATOM   884  N  N   . GLN A 1 121 ? 9.347   7.373   -6.943  1.00 52.96  ? 155 GLN A N   1 
ATOM   885  C  CA  . GLN A 1 121 ? 7.950   7.601   -7.289  1.00 56.00  ? 155 GLN A CA  1 
ATOM   886  C  C   . GLN A 1 121 ? 7.592   9.081   -7.328  1.00 55.44  ? 155 GLN A C   1 
ATOM   887  O  O   . GLN A 1 121 ? 6.586   9.444   -7.946  1.00 63.95  ? 155 GLN A O   1 
ATOM   888  C  CB  . GLN A 1 121 ? 7.044   6.853   -6.308  1.00 64.67  ? 155 GLN A CB  1 
ATOM   889  C  CG  . GLN A 1 121 ? 6.501   7.702   -5.175  1.00 68.74  ? 155 GLN A CG  1 
ATOM   890  C  CD  . GLN A 1 121 ? 5.842   6.871   -4.093  1.00 85.36  ? 155 GLN A CD  1 
ATOM   891  O  OE1 . GLN A 1 121 ? 6.502   6.097   -3.401  1.00 82.65  ? 155 GLN A OE1 1 
ATOM   892  N  NE2 . GLN A 1 121 ? 4.532   7.027   -3.943  1.00 89.28  ? 155 GLN A NE2 1 
ATOM   893  N  N   . HIS A 1 122 ? 8.388   9.940   -6.695  1.00 48.67  ? 156 HIS A N   1 
ATOM   894  C  CA  . HIS A 1 122 ? 8.165   11.377  -6.716  1.00 52.36  ? 156 HIS A CA  1 
ATOM   895  C  C   . HIS A 1 122 ? 9.406   12.087  -7.239  1.00 47.22  ? 156 HIS A C   1 
ATOM   896  O  O   . HIS A 1 122 ? 10.537  11.641  -7.020  1.00 42.53  ? 156 HIS A O   1 
ATOM   897  C  CB  . HIS A 1 122 ? 7.812   11.913  -5.323  1.00 48.97  ? 156 HIS A CB  1 
ATOM   898  C  CG  . HIS A 1 122 ? 6.595   11.282  -4.722  1.00 56.21  ? 156 HIS A CG  1 
ATOM   899  N  ND1 . HIS A 1 122 ? 5.376   11.257  -5.364  1.00 63.77  ? 156 HIS A ND1 1 
ATOM   900  C  CD2 . HIS A 1 122 ? 6.406   10.667  -3.531  1.00 53.64  ? 156 HIS A CD2 1 
ATOM   901  C  CE1 . HIS A 1 122 ? 4.490   10.644  -4.599  1.00 59.42  ? 156 HIS A CE1 1 
ATOM   902  N  NE2 . HIS A 1 122 ? 5.089   10.276  -3.481  1.00 61.07  ? 156 HIS A NE2 1 
ATOM   903  N  N   . SER A 1 123 ? 9.183   13.198  -7.934  1.00 42.74  ? 157 SER A N   1 
ATOM   904  C  CA  . SER A 1 123 ? 10.251  13.994  -8.523  1.00 40.87  ? 157 SER A CA  1 
ATOM   905  C  C   . SER A 1 123 ? 10.342  15.332  -7.805  1.00 42.34  ? 157 SER A C   1 
ATOM   906  O  O   . SER A 1 123 ? 9.330   16.017  -7.628  1.00 45.60  ? 157 SER A O   1 
ATOM   907  C  CB  . SER A 1 123 ? 10.011  14.213  -10.019 1.00 42.00  ? 157 SER A CB  1 
ATOM   908  O  OG  . SER A 1 123 ? 10.030  12.986  -10.726 1.00 55.46  ? 157 SER A OG  1 
ATOM   909  N  N   . LEU A 1 124 ? 11.552  15.699  -7.393  1.00 38.40  ? 158 LEU A N   1 
ATOM   910  C  CA  . LEU A 1 124 ? 11.786  16.972  -6.729  1.00 37.57  ? 158 LEU A CA  1 
ATOM   911  C  C   . LEU A 1 124 ? 12.164  18.037  -7.748  1.00 38.04  ? 158 LEU A C   1 
ATOM   912  O  O   . LEU A 1 124 ? 12.907  17.772  -8.697  1.00 44.77  ? 158 LEU A O   1 
ATOM   913  C  CB  . LEU A 1 124 ? 12.892  16.843  -5.681  1.00 33.92  ? 158 LEU A CB  1 
ATOM   914  C  CG  . LEU A 1 124 ? 12.691  15.829  -4.555  1.00 41.32  ? 158 LEU A CG  1 
ATOM   915  C  CD1 . LEU A 1 124 ? 13.916  15.790  -3.654  1.00 41.82  ? 158 LEU A CD1 1 
ATOM   916  C  CD2 . LEU A 1 124 ? 11.446  16.160  -3.753  1.00 45.87  ? 158 LEU A CD2 1 
ATOM   917  N  N   . THR A 1 125 ? 11.639  19.242  -7.550  1.00 38.61  ? 159 THR A N   1 
ATOM   918  C  CA  . THR A 1 125 ? 12.024  20.405  -8.331  1.00 40.46  ? 159 THR A CA  1 
ATOM   919  C  C   . THR A 1 125 ? 12.712  21.410  -7.418  1.00 41.87  ? 159 THR A C   1 
ATOM   920  O  O   . THR A 1 125 ? 12.610  21.336  -6.190  1.00 44.28  ? 159 THR A O   1 
ATOM   921  C  CB  . THR A 1 125 ? 10.817  21.053  -9.021  1.00 39.45  ? 159 THR A CB  1 
ATOM   922  O  OG1 . THR A 1 125 ? 9.890   21.518  -8.033  1.00 46.20  ? 159 THR A OG1 1 
ATOM   923  C  CG2 . THR A 1 125 ? 10.125  20.049  -9.929  1.00 36.92  ? 159 THR A CG2 1 
ATOM   924  N  N   . PHE A 1 126 ? 13.421  22.356  -8.029  1.00 41.62  ? 160 PHE A N   1 
ATOM   925  C  CA  . PHE A 1 126 ? 14.259  23.276  -7.277  1.00 39.20  ? 160 PHE A CA  1 
ATOM   926  C  C   . PHE A 1 126 ? 14.102  24.686  -7.824  1.00 37.75  ? 160 PHE A C   1 
ATOM   927  O  O   . PHE A 1 126 ? 13.845  24.886  -9.014  1.00 45.18  ? 160 PHE A O   1 
ATOM   928  C  CB  . PHE A 1 126 ? 15.731  22.843  -7.324  1.00 35.84  ? 160 PHE A CB  1 
ATOM   929  C  CG  . PHE A 1 126 ? 15.956  21.428  -6.869  1.00 43.31  ? 160 PHE A CG  1 
ATOM   930  C  CD1 . PHE A 1 126 ? 15.872  20.374  -7.766  1.00 36.68  ? 160 PHE A CD1 1 
ATOM   931  C  CD2 . PHE A 1 126 ? 16.238  21.149  -5.543  1.00 39.04  ? 160 PHE A CD2 1 
ATOM   932  C  CE1 . PHE A 1 126 ? 16.068  19.072  -7.349  1.00 31.29  ? 160 PHE A CE1 1 
ATOM   933  C  CE2 . PHE A 1 126 ? 16.437  19.848  -5.120  1.00 35.14  ? 160 PHE A CE2 1 
ATOM   934  C  CZ  . PHE A 1 126 ? 16.352  18.809  -6.024  1.00 37.14  ? 160 PHE A CZ  1 
ATOM   935  N  N   . ALA A 1 127 ? 14.256  25.663  -6.934  1.00 39.35  ? 161 ALA A N   1 
ATOM   936  C  CA  . ALA A 1 127 ? 14.187  27.065  -7.308  1.00 36.56  ? 161 ALA A CA  1 
ATOM   937  C  C   . ALA A 1 127 ? 15.530  27.522  -7.875  1.00 46.96  ? 161 ALA A C   1 
ATOM   938  O  O   . ALA A 1 127 ? 16.494  26.755  -7.963  1.00 50.76  ? 161 ALA A O   1 
ATOM   939  C  CB  . ALA A 1 127 ? 13.772  27.913  -6.108  1.00 35.67  ? 161 ALA A CB  1 
ATOM   940  N  N   . ALA A 1 128 ? 15.598  28.799  -8.258  1.00 47.06  ? 162 ALA A N   1 
ATOM   941  C  CA  . ALA A 1 128 ? 16.808  29.322  -8.886  1.00 38.18  ? 162 ALA A CA  1 
ATOM   942  C  C   . ALA A 1 128 ? 17.998  29.311  -7.934  1.00 38.22  ? 162 ALA A C   1 
ATOM   943  O  O   . ALA A 1 128 ? 19.146  29.234  -8.386  1.00 50.19  ? 162 ALA A O   1 
ATOM   944  C  CB  . ALA A 1 128 ? 16.561  30.738  -9.407  1.00 39.27  ? 162 ALA A CB  1 
ATOM   945  N  N   . ASN A 1 129 ? 17.755  29.383  -6.627  1.00 37.18  ? 163 ASN A N   1 
ATOM   946  C  CA  . ASN A 1 129 ? 18.828  29.381  -5.643  1.00 36.69  ? 163 ASN A CA  1 
ATOM   947  C  C   . ASN A 1 129 ? 19.231  27.977  -5.207  1.00 40.37  ? 163 ASN A C   1 
ATOM   948  O  O   . ASN A 1 129 ? 19.980  27.834  -4.234  1.00 49.05  ? 163 ASN A O   1 
ATOM   949  C  CB  . ASN A 1 129 ? 18.433  30.216  -4.420  1.00 31.30  ? 163 ASN A CB  1 
ATOM   950  C  CG  . ASN A 1 129 ? 17.063  29.854  -3.878  1.00 40.88  ? 163 ASN A CG  1 
ATOM   951  O  OD1 . ASN A 1 129 ? 16.487  28.827  -4.237  1.00 38.18  ? 163 ASN A OD1 1 
ATOM   952  N  ND2 . ASN A 1 129 ? 16.534  30.703  -3.004  1.00 44.87  ? 163 ASN A ND2 1 
ATOM   953  N  N   . GLY A 1 130 ? 18.755  26.942  -5.898  1.00 37.93  ? 164 GLY A N   1 
ATOM   954  C  CA  . GLY A 1 130 ? 19.153  25.580  -5.620  1.00 39.22  ? 164 GLY A CA  1 
ATOM   955  C  C   . GLY A 1 130 ? 18.363  24.877  -4.538  1.00 40.64  ? 164 GLY A C   1 
ATOM   956  O  O   . GLY A 1 130 ? 18.508  23.657  -4.383  1.00 41.33  ? 164 GLY A O   1 
ATOM   957  N  N   . TRP A 1 131 ? 17.536  25.596  -3.785  1.00 39.33  ? 165 TRP A N   1 
ATOM   958  C  CA  . TRP A 1 131 ? 16.749  24.978  -2.730  1.00 41.29  ? 165 TRP A CA  1 
ATOM   959  C  C   . TRP A 1 131 ? 15.541  24.256  -3.313  1.00 42.77  ? 165 TRP A C   1 
ATOM   960  O  O   . TRP A 1 131 ? 14.997  24.645  -4.351  1.00 45.47  ? 165 TRP A O   1 
ATOM   961  C  CB  . TRP A 1 131 ? 16.298  26.025  -1.714  1.00 39.45  ? 165 TRP A CB  1 
ATOM   962  C  CG  . TRP A 1 131 ? 17.424  26.555  -0.888  1.00 39.65  ? 165 TRP A CG  1 
ATOM   963  C  CD1 . TRP A 1 131 ? 17.983  27.797  -0.964  1.00 40.04  ? 165 TRP A CD1 1 
ATOM   964  C  CD2 . TRP A 1 131 ? 18.140  25.853  0.134   1.00 44.64  ? 165 TRP A CD2 1 
ATOM   965  N  NE1 . TRP A 1 131 ? 19.001  27.914  -0.048  1.00 47.95  ? 165 TRP A NE1 1 
ATOM   966  C  CE2 . TRP A 1 131 ? 19.118  26.734  0.638   1.00 44.56  ? 165 TRP A CE2 1 
ATOM   967  C  CE3 . TRP A 1 131 ? 18.049  24.566  0.674   1.00 31.25  ? 165 TRP A CE3 1 
ATOM   968  C  CZ2 . TRP A 1 131 ? 19.997  26.370  1.656   1.00 44.04  ? 165 TRP A CZ2 1 
ATOM   969  C  CZ3 . TRP A 1 131 ? 18.923  24.206  1.684   1.00 41.07  ? 165 TRP A CZ3 1 
ATOM   970  C  CH2 . TRP A 1 131 ? 19.884  25.105  2.164   1.00 48.43  ? 165 TRP A CH2 1 
ATOM   971  N  N   . VAL A 1 132 ? 15.122  23.190  -2.628  1.00 39.60  ? 166 VAL A N   1 
ATOM   972  C  CA  . VAL A 1 132 ? 14.021  22.373  -3.118  1.00 40.05  ? 166 VAL A CA  1 
ATOM   973  C  C   . VAL A 1 132 ? 12.717  23.163  -3.055  1.00 38.51  ? 166 VAL A C   1 
ATOM   974  O  O   . VAL A 1 132 ? 12.517  24.022  -2.185  1.00 38.25  ? 166 VAL A O   1 
ATOM   975  C  CB  . VAL A 1 132 ? 13.922  21.057  -2.322  1.00 33.40  ? 166 VAL A CB  1 
ATOM   976  C  CG1 . VAL A 1 132 ? 13.333  21.297  -0.937  1.00 30.29  ? 166 VAL A CG1 1 
ATOM   977  C  CG2 . VAL A 1 132 ? 13.107  20.025  -3.089  1.00 31.11  ? 166 VAL A CG2 1 
ATOM   978  N  N   . ASP A 1 133 ? 11.832  22.886  -4.002  1.00 43.78  ? 167 ASP A N   1 
ATOM   979  C  CA  . ASP A 1 133 ? 10.520  23.518  -4.009  1.00 44.86  ? 167 ASP A CA  1 
ATOM   980  C  C   . ASP A 1 133 ? 9.641   22.881  -2.939  1.00 45.15  ? 167 ASP A C   1 
ATOM   981  O  O   . ASP A 1 133 ? 9.491   21.655  -2.920  1.00 51.56  ? 167 ASP A O   1 
ATOM   982  C  CB  . ASP A 1 133 ? 9.867   23.379  -5.381  1.00 42.45  ? 167 ASP A CB  1 
ATOM   983  C  CG  . ASP A 1 133 ? 8.863   24.478  -5.665  1.00 50.44  ? 167 ASP A CG  1 
ATOM   984  O  OD1 . ASP A 1 133 ? 7.884   24.606  -4.900  1.00 46.01  ? 167 ASP A OD1 1 
ATOM   985  O  OD2 . ASP A 1 133 ? 9.054   25.216  -6.655  1.00 57.36  ? 167 ASP A OD2 1 
ATOM   986  N  N   . PRO A 1 134 ? 9.056   23.669  -2.034  1.00 48.14  ? 168 PRO A N   1 
ATOM   987  C  CA  . PRO A 1 134 ? 8.211   23.076  -0.984  1.00 47.84  ? 168 PRO A CA  1 
ATOM   988  C  C   . PRO A 1 134 ? 7.001   22.340  -1.528  1.00 55.66  ? 168 PRO A C   1 
ATOM   989  O  O   . PRO A 1 134 ? 6.449   21.482  -0.828  1.00 59.25  ? 168 PRO A O   1 
ATOM   990  C  CB  . PRO A 1 134 ? 7.795   24.286  -0.134  1.00 44.56  ? 168 PRO A CB  1 
ATOM   991  C  CG  . PRO A 1 134 ? 8.747   25.381  -0.501  1.00 48.04  ? 168 PRO A CG  1 
ATOM   992  C  CD  . PRO A 1 134 ? 9.144   25.133  -1.919  1.00 48.03  ? 168 PRO A CD  1 
ATOM   993  N  N   . ALA A 1 135 ? 6.571   22.646  -2.754  1.00 53.67  ? 169 ALA A N   1 
ATOM   994  C  CA  . ALA A 1 135 ? 5.449   21.928  -3.345  1.00 40.26  ? 169 ALA A CA  1 
ATOM   995  C  C   . ALA A 1 135 ? 5.820   20.492  -3.693  1.00 43.70  ? 169 ALA A C   1 
ATOM   996  O  O   . ALA A 1 135 ? 4.945   19.619  -3.727  1.00 53.43  ? 169 ALA A O   1 
ATOM   997  C  CB  . ALA A 1 135 ? 4.955   22.664  -4.589  1.00 40.69  ? 169 ALA A CB  1 
ATOM   998  N  N   . THR A 1 136 ? 7.101   20.227  -3.950  1.00 49.85  ? 170 THR A N   1 
ATOM   999  C  CA  . THR A 1 136 ? 7.564   18.893  -4.305  1.00 57.32  ? 170 THR A CA  1 
ATOM   1000 C  C   . THR A 1 136 ? 8.162   18.130  -3.131  1.00 54.82  ? 170 THR A C   1 
ATOM   1001 O  O   . THR A 1 136 ? 8.319   16.908  -3.226  1.00 54.50  ? 170 THR A O   1 
ATOM   1002 C  CB  . THR A 1 136 ? 8.601   18.970  -5.434  1.00 45.47  ? 170 THR A CB  1 
ATOM   1003 O  OG1 . THR A 1 136 ? 9.589   19.958  -5.114  1.00 47.12  ? 170 THR A OG1 1 
ATOM   1004 C  CG2 . THR A 1 136 ? 7.929   19.333  -6.749  1.00 43.83  ? 170 THR A CG2 1 
ATOM   1005 N  N   . ALA A 1 137 ? 8.495   18.810  -2.030  1.00 52.38  ? 171 ALA A N   1 
ATOM   1006 C  CA  . ALA A 1 137 ? 9.060   18.181  -0.836  1.00 51.64  ? 171 ALA A CA  1 
ATOM   1007 C  C   . ALA A 1 137 ? 8.139   18.464  0.346   1.00 59.62  ? 171 ALA A C   1 
ATOM   1008 O  O   . ALA A 1 137 ? 8.443   19.318  1.193   1.00 60.51  ? 171 ALA A O   1 
ATOM   1009 C  CB  . ALA A 1 137 ? 10.478  18.679  -0.564  1.00 41.92  ? 171 ALA A CB  1 
ATOM   1010 N  N   . PRO A 1 138 ? 7.007   17.765  0.438   1.00 55.51  ? 172 PRO A N   1 
ATOM   1011 C  CA  . PRO A 1 138 ? 6.057   18.022  1.526   1.00 57.16  ? 172 PRO A CA  1 
ATOM   1012 C  C   . PRO A 1 138 ? 6.397   17.265  2.801   1.00 64.57  ? 172 PRO A C   1 
ATOM   1013 O  O   . PRO A 1 138 ? 6.730   16.078  2.786   1.00 66.26  ? 172 PRO A O   1 
ATOM   1014 C  CB  . PRO A 1 138 ? 4.730   17.527  0.936   1.00 47.51  ? 172 PRO A CB  1 
ATOM   1015 C  CG  . PRO A 1 138 ? 5.134   16.408  0.030   1.00 55.02  ? 172 PRO A CG  1 
ATOM   1016 C  CD  . PRO A 1 138 ? 6.519   16.726  -0.487  1.00 59.63  ? 172 PRO A CD  1 
ATOM   1017 N  N   . ASN A 1 139 ? 6.303   17.981  3.923   1.00 64.44  ? 173 ASN A N   1 
ATOM   1018 C  CA  . ASN A 1 139 ? 6.491   17.406  5.256   1.00 65.92  ? 173 ASN A CA  1 
ATOM   1019 C  C   . ASN A 1 139 ? 7.858   16.737  5.391   1.00 73.10  ? 173 ASN A C   1 
ATOM   1020 O  O   . ASN A 1 139 ? 7.980   15.604  5.863   1.00 74.94  ? 173 ASN A O   1 
ATOM   1021 C  CB  . ASN A 1 139 ? 5.366   16.424  5.592   1.00 67.61  ? 173 ASN A CB  1 
ATOM   1022 C  CG  . ASN A 1 139 ? 4.698   16.736  6.915   1.00 81.79  ? 173 ASN A CG  1 
ATOM   1023 O  OD1 . ASN A 1 139 ? 4.311   17.874  7.175   1.00 89.55  ? 173 ASN A OD1 1 
ATOM   1024 N  ND2 . ASN A 1 139 ? 4.563   15.722  7.763   1.00 88.29  ? 173 ASN A ND2 1 
ATOM   1025 N  N   . PHE A 1 140 ? 8.900   17.454  4.972   1.00 63.50  ? 174 PHE A N   1 
ATOM   1026 C  CA  . PHE A 1 140 ? 10.257  16.942  5.094   1.00 52.79  ? 174 PHE A CA  1 
ATOM   1027 C  C   . PHE A 1 140 ? 10.865  17.201  6.466   1.00 53.60  ? 174 PHE A C   1 
ATOM   1028 O  O   . PHE A 1 140 ? 11.955  16.690  6.747   1.00 48.55  ? 174 PHE A O   1 
ATOM   1029 C  CB  . PHE A 1 140 ? 11.150  17.549  4.008   1.00 51.98  ? 174 PHE A CB  1 
ATOM   1030 C  CG  . PHE A 1 140 ? 11.203  16.734  2.745   1.00 48.71  ? 174 PHE A CG  1 
ATOM   1031 C  CD1 . PHE A 1 140 ? 10.067  16.106  2.262   1.00 58.53  ? 174 PHE A CD1 1 
ATOM   1032 C  CD2 . PHE A 1 140 ? 12.389  16.593  2.045   1.00 43.87  ? 174 PHE A CD2 1 
ATOM   1033 C  CE1 . PHE A 1 140 ? 10.111  15.353  1.103   1.00 56.69  ? 174 PHE A CE1 1 
ATOM   1034 C  CE2 . PHE A 1 140 ? 12.441  15.842  0.883   1.00 54.41  ? 174 PHE A CE2 1 
ATOM   1035 C  CZ  . PHE A 1 140 ? 11.300  15.222  0.412   1.00 49.49  ? 174 PHE A CZ  1 
ATOM   1036 N  N   . GLY A 1 141 ? 10.191  17.970  7.320   1.00 55.45  ? 175 GLY A N   1 
ATOM   1037 C  CA  . GLY A 1 141 ? 10.662  18.228  8.659   1.00 43.76  ? 175 GLY A CA  1 
ATOM   1038 C  C   . GLY A 1 141 ? 11.997  18.943  8.684   1.00 50.31  ? 175 GLY A C   1 
ATOM   1039 O  O   . GLY A 1 141 ? 12.154  20.042  8.143   1.00 49.42  ? 175 GLY A O   1 
ATOM   1040 N  N   . PRO A 1 142 ? 12.995  18.323  9.321   1.00 51.82  ? 176 PRO A N   1 
ATOM   1041 C  CA  . PRO A 1 142 ? 14.325  18.942  9.393   1.00 53.47  ? 176 PRO A CA  1 
ATOM   1042 C  C   . PRO A 1 142 ? 15.139  18.811  8.118   1.00 48.46  ? 176 PRO A C   1 
ATOM   1043 O  O   . PRO A 1 142 ? 16.178  19.475  8.001   1.00 56.39  ? 176 PRO A O   1 
ATOM   1044 C  CB  . PRO A 1 142 ? 14.993  18.182  10.545  1.00 48.24  ? 176 PRO A CB  1 
ATOM   1045 C  CG  . PRO A 1 142 ? 14.367  16.828  10.493  1.00 50.18  ? 176 PRO A CG  1 
ATOM   1046 C  CD  . PRO A 1 142 ? 12.943  17.031  10.027  1.00 47.10  ? 176 PRO A CD  1 
ATOM   1047 N  N   . LEU A 1 143 ? 14.707  17.987  7.167   1.00 42.75  ? 177 LEU A N   1 
ATOM   1048 C  CA  . LEU A 1 143 ? 15.477  17.764  5.950   1.00 40.83  ? 177 LEU A CA  1 
ATOM   1049 C  C   . LEU A 1 143 ? 15.472  19.017  5.084   1.00 39.26  ? 177 LEU A C   1 
ATOM   1050 O  O   . LEU A 1 143 ? 14.411  19.484  4.658   1.00 38.40  ? 177 LEU A O   1 
ATOM   1051 C  CB  . LEU A 1 143 ? 14.908  16.578  5.175   1.00 47.73  ? 177 LEU A CB  1 
ATOM   1052 C  CG  . LEU A 1 143 ? 15.202  15.180  5.724   1.00 49.97  ? 177 LEU A CG  1 
ATOM   1053 C  CD1 . LEU A 1 143 ? 15.025  14.133  4.636   1.00 49.27  ? 177 LEU A CD1 1 
ATOM   1054 C  CD2 . LEU A 1 143 ? 16.600  15.109  6.321   1.00 50.61  ? 177 LEU A CD2 1 
ATOM   1055 N  N   . ARG A 1 144 ? 16.659  19.560  4.824   1.00 40.68  ? 178 ARG A N   1 
ATOM   1056 C  CA  . ARG A 1 144 ? 16.838  20.698  3.930   1.00 39.54  ? 178 ARG A CA  1 
ATOM   1057 C  C   . ARG A 1 144 ? 17.555  20.201  2.681   1.00 34.16  ? 178 ARG A C   1 
ATOM   1058 O  O   . ARG A 1 144 ? 18.759  19.923  2.719   1.00 48.42  ? 178 ARG A O   1 
ATOM   1059 C  CB  . ARG A 1 144 ? 17.624  21.817  4.612   1.00 38.79  ? 178 ARG A CB  1 
ATOM   1060 C  CG  . ARG A 1 144 ? 16.960  22.377  5.861   1.00 30.85  ? 178 ARG A CG  1 
ATOM   1061 C  CD  . ARG A 1 144 ? 15.665  23.097  5.523   1.00 37.59  ? 178 ARG A CD  1 
ATOM   1062 N  NE  . ARG A 1 144 ? 14.837  23.318  6.703   1.00 51.28  ? 178 ARG A NE  1 
ATOM   1063 C  CZ  . ARG A 1 144 ? 13.905  22.479  7.132   1.00 51.71  ? 178 ARG A CZ  1 
ATOM   1064 N  NH1 . ARG A 1 144 ? 13.654  21.343  6.502   1.00 47.43  ? 178 ARG A NH1 1 
ATOM   1065 N  NH2 . ARG A 1 144 ? 13.206  22.787  8.221   1.00 49.79  ? 178 ARG A NH2 1 
ATOM   1066 N  N   . VAL A 1 145 ? 16.819  20.085  1.581   1.00 30.17  ? 179 VAL A N   1 
ATOM   1067 C  CA  . VAL A 1 145 ? 17.365  19.574  0.330   1.00 34.52  ? 179 VAL A CA  1 
ATOM   1068 C  C   . VAL A 1 145 ? 17.850  20.745  -0.513  1.00 36.71  ? 179 VAL A C   1 
ATOM   1069 O  O   . VAL A 1 145 ? 17.135  21.740  -0.683  1.00 38.62  ? 179 VAL A O   1 
ATOM   1070 C  CB  . VAL A 1 145 ? 16.319  18.739  -0.426  1.00 30.58  ? 179 VAL A CB  1 
ATOM   1071 C  CG1 . VAL A 1 145 ? 16.924  18.150  -1.692  1.00 32.31  ? 179 VAL A CG1 1 
ATOM   1072 C  CG2 . VAL A 1 145 ? 15.772  17.639  0.471   1.00 37.66  ? 179 VAL A CG2 1 
ATOM   1073 N  N   . PHE A 1 146 ? 19.063  20.623  -1.048  1.00 38.49  ? 180 PHE A N   1 
ATOM   1074 C  CA  . PHE A 1 146 ? 19.706  21.706  -1.780  1.00 39.18  ? 180 PHE A CA  1 
ATOM   1075 C  C   . PHE A 1 146 ? 20.372  21.151  -3.029  1.00 40.44  ? 180 PHE A C   1 
ATOM   1076 O  O   . PHE A 1 146 ? 21.086  20.146  -2.960  1.00 38.48  ? 180 PHE A O   1 
ATOM   1077 C  CB  . PHE A 1 146 ? 20.741  22.416  -0.898  1.00 39.00  ? 180 PHE A CB  1 
ATOM   1078 C  CG  . PHE A 1 146 ? 21.541  23.464  -1.616  1.00 44.12  ? 180 PHE A CG  1 
ATOM   1079 C  CD1 . PHE A 1 146 ? 20.964  24.670  -1.980  1.00 40.52  ? 180 PHE A CD1 1 
ATOM   1080 C  CD2 . PHE A 1 146 ? 22.876  23.249  -1.916  1.00 38.71  ? 180 PHE A CD2 1 
ATOM   1081 C  CE1 . PHE A 1 146 ? 21.702  25.639  -2.635  1.00 40.23  ? 180 PHE A CE1 1 
ATOM   1082 C  CE2 . PHE A 1 146 ? 23.619  24.215  -2.567  1.00 41.21  ? 180 PHE A CE2 1 
ATOM   1083 C  CZ  . PHE A 1 146 ? 23.031  25.410  -2.930  1.00 43.29  ? 180 PHE A CZ  1 
ATOM   1084 N  N   . TYR A 1 147 ? 20.136  21.805  -4.168  1.00 33.85  ? 181 TYR A N   1 
ATOM   1085 C  CA  . TYR A 1 147 ? 20.802  21.437  -5.408  1.00 43.23  ? 181 TYR A CA  1 
ATOM   1086 C  C   . TYR A 1 147 ? 21.970  22.382  -5.640  1.00 47.17  ? 181 TYR A C   1 
ATOM   1087 O  O   . TYR A 1 147 ? 21.748  23.547  -6.003  1.00 44.52  ? 181 TYR A O   1 
ATOM   1088 C  CB  . TYR A 1 147 ? 19.832  21.488  -6.586  1.00 32.49  ? 181 TYR A CB  1 
ATOM   1089 C  CG  . TYR A 1 147 ? 20.492  21.212  -7.920  1.00 39.94  ? 181 TYR A CG  1 
ATOM   1090 C  CD1 . TYR A 1 147 ? 20.893  19.928  -8.265  1.00 44.51  ? 181 TYR A CD1 1 
ATOM   1091 C  CD2 . TYR A 1 147 ? 20.721  22.237  -8.829  1.00 44.94  ? 181 TYR A CD2 1 
ATOM   1092 C  CE1 . TYR A 1 147 ? 21.500  19.671  -9.480  1.00 45.01  ? 181 TYR A CE1 1 
ATOM   1093 C  CE2 . TYR A 1 147 ? 21.325  21.989  -10.048 1.00 39.83  ? 181 TYR A CE2 1 
ATOM   1094 C  CZ  . TYR A 1 147 ? 21.714  20.705  -10.367 1.00 46.72  ? 181 TYR A CZ  1 
ATOM   1095 O  OH  . TYR A 1 147 ? 22.317  20.452  -11.579 1.00 41.72  ? 181 TYR A OH  1 
ATOM   1096 N  N   . PRO A 1 148 ? 23.218  21.941  -5.452  1.00 43.15  ? 182 PRO A N   1 
ATOM   1097 C  CA  . PRO A 1 148 ? 24.357  22.853  -5.615  1.00 37.55  ? 182 PRO A CA  1 
ATOM   1098 C  C   . PRO A 1 148 ? 24.746  23.110  -7.058  1.00 42.45  ? 182 PRO A C   1 
ATOM   1099 O  O   . PRO A 1 148 ? 25.519  24.043  -7.315  1.00 46.68  ? 182 PRO A O   1 
ATOM   1100 C  CB  . PRO A 1 148 ? 25.483  22.129  -4.869  1.00 41.76  ? 182 PRO A CB  1 
ATOM   1101 C  CG  . PRO A 1 148 ? 25.151  20.682  -5.036  1.00 41.25  ? 182 PRO A CG  1 
ATOM   1102 C  CD  . PRO A 1 148 ? 23.642  20.583  -5.070  1.00 44.27  ? 182 PRO A CD  1 
ATOM   1103 N  N   . GLY A 1 149 ? 24.237  22.325  -8.001  1.00 40.91  ? 183 GLY A N   1 
ATOM   1104 C  CA  . GLY A 1 149 ? 24.648  22.427  -9.378  1.00 42.00  ? 183 GLY A CA  1 
ATOM   1105 C  C   . GLY A 1 149 ? 25.344  21.161  -9.828  1.00 31.65  ? 183 GLY A C   1 
ATOM   1106 O  O   . GLY A 1 149 ? 25.651  20.277  -9.022  1.00 38.57  ? 183 GLY A O   1 
ATOM   1107 N  N   . PRO A 1 150 ? 25.599  21.045  -11.128 1.00 31.70  ? 184 PRO A N   1 
ATOM   1108 C  CA  . PRO A 1 150 ? 26.304  19.861  -11.635 1.00 37.58  ? 184 PRO A CA  1 
ATOM   1109 C  C   . PRO A 1 150 ? 27.709  19.772  -11.057 1.00 46.21  ? 184 PRO A C   1 
ATOM   1110 O  O   . PRO A 1 150 ? 28.448  20.758  -11.017 1.00 52.04  ? 184 PRO A O   1 
ATOM   1111 C  CB  . PRO A 1 150 ? 26.324  20.080  -13.153 1.00 49.33  ? 184 PRO A CB  1 
ATOM   1112 C  CG  . PRO A 1 150 ? 25.240  21.077  -13.420 1.00 38.41  ? 184 PRO A CG  1 
ATOM   1113 C  CD  . PRO A 1 150 ? 25.187  21.954  -12.209 1.00 37.85  ? 184 PRO A CD  1 
ATOM   1114 N  N   . GLY A 1 151 ? 28.070  18.578  -10.597 1.00 39.66  ? 185 GLY A N   1 
ATOM   1115 C  CA  . GLY A 1 151 ? 29.385  18.345  -10.036 1.00 42.25  ? 185 GLY A CA  1 
ATOM   1116 C  C   . GLY A 1 151 ? 29.829  16.910  -10.220 1.00 45.24  ? 185 GLY A C   1 
ATOM   1117 O  O   . GLY A 1 151 ? 30.389  16.560  -11.262 1.00 43.62  ? 185 GLY A O   1 
ATOM   1118 N  N   . HIS A 1 152 ? 29.590  16.071  -9.209  1.00 49.53  ? 186 HIS A N   1 
ATOM   1119 C  CA  . HIS A 1 152 ? 29.857  14.645  -9.360  1.00 47.52  ? 186 HIS A CA  1 
ATOM   1120 C  C   . HIS A 1 152 ? 29.000  14.051  -10.470 1.00 50.36  ? 186 HIS A C   1 
ATOM   1121 O  O   . HIS A 1 152 ? 29.486  13.265  -11.291 1.00 51.05  ? 186 HIS A O   1 
ATOM   1122 C  CB  . HIS A 1 152 ? 29.607  13.921  -8.037  1.00 52.52  ? 186 HIS A CB  1 
ATOM   1123 C  CG  . HIS A 1 152 ? 29.628  12.430  -8.155  1.00 53.65  ? 186 HIS A CG  1 
ATOM   1124 N  ND1 . HIS A 1 152 ? 30.792  11.716  -8.337  1.00 63.64  ? 186 HIS A ND1 1 
ATOM   1125 C  CD2 . HIS A 1 152 ? 28.628  11.518  -8.123  1.00 51.54  ? 186 HIS A CD2 1 
ATOM   1126 C  CE1 . HIS A 1 152 ? 30.510  10.428  -8.412  1.00 54.08  ? 186 HIS A CE1 1 
ATOM   1127 N  NE2 . HIS A 1 152 ? 29.203  10.281  -8.286  1.00 60.63  ? 186 HIS A NE2 1 
ATOM   1128 N  N   . THR A 1 153 ? 27.718  14.407  -10.500 1.00 54.30  ? 187 THR A N   1 
ATOM   1129 C  CA  . THR A 1 153 ? 26.865  14.158  -11.653 1.00 48.57  ? 187 THR A CA  1 
ATOM   1130 C  C   . THR A 1 153 ? 26.161  15.454  -12.029 1.00 51.86  ? 187 THR A C   1 
ATOM   1131 O  O   . THR A 1 153 ? 26.503  16.521  -11.513 1.00 50.48  ? 187 THR A O   1 
ATOM   1132 C  CB  . THR A 1 153 ? 25.845  13.049  -11.372 1.00 52.47  ? 187 THR A CB  1 
ATOM   1133 O  OG1 . THR A 1 153 ? 24.886  13.509  -10.408 1.00 49.95  ? 187 THR A OG1 1 
ATOM   1134 C  CG2 . THR A 1 153 ? 26.529  11.786  -10.862 1.00 54.32  ? 187 THR A CG2 1 
ATOM   1135 N  N   . SER A 1 154 ? 25.188  15.386  -12.928 1.00 49.59  ? 188 SER A N   1 
ATOM   1136 C  CA  . SER A 1 154 ? 24.377  16.556  -13.236 1.00 41.34  ? 188 SER A CA  1 
ATOM   1137 C  C   . SER A 1 154 ? 23.100  16.612  -12.412 1.00 44.81  ? 188 SER A C   1 
ATOM   1138 O  O   . SER A 1 154 ? 22.347  17.585  -12.524 1.00 47.15  ? 188 SER A O   1 
ATOM   1139 C  CB  . SER A 1 154 ? 24.035  16.591  -14.729 1.00 43.27  ? 188 SER A CB  1 
ATOM   1140 O  OG  . SER A 1 154 ? 25.172  16.924  -15.505 1.00 59.89  ? 188 SER A OG  1 
ATOM   1141 N  N   . ASP A 1 155 ? 22.845  15.599  -11.583 1.00 37.77  ? 189 ASP A N   1 
ATOM   1142 C  CA  . ASP A 1 155 ? 21.616  15.515  -10.803 1.00 44.13  ? 189 ASP A CA  1 
ATOM   1143 C  C   . ASP A 1 155 ? 21.868  15.355  -9.308  1.00 43.24  ? 189 ASP A C   1 
ATOM   1144 O  O   . ASP A 1 155 ? 20.913  15.125  -8.555  1.00 37.30  ? 189 ASP A O   1 
ATOM   1145 C  CB  . ASP A 1 155 ? 20.750  14.355  -11.305 1.00 45.86  ? 189 ASP A CB  1 
ATOM   1146 C  CG  . ASP A 1 155 ? 21.467  13.019  -11.231 1.00 46.15  ? 189 ASP A CG  1 
ATOM   1147 O  OD1 . ASP A 1 155 ? 22.622  12.933  -11.697 1.00 48.06  ? 189 ASP A OD1 1 
ATOM   1148 O  OD2 . ASP A 1 155 ? 20.876  12.054  -10.703 1.00 42.47  ? 189 ASP A OD2 1 
ATOM   1149 N  N   . ASN A 1 156 ? 23.116  15.462  -8.858  1.00 41.94  ? 190 ASN A N   1 
ATOM   1150 C  CA  . ASN A 1 156 ? 23.409  15.256  -7.447  1.00 39.93  ? 190 ASN A CA  1 
ATOM   1151 C  C   . ASN A 1 156 ? 22.767  16.352  -6.605  1.00 48.24  ? 190 ASN A C   1 
ATOM   1152 O  O   . ASN A 1 156 ? 22.842  17.540  -6.933  1.00 45.24  ? 190 ASN A O   1 
ATOM   1153 C  CB  . ASN A 1 156 ? 24.916  15.231  -7.193  1.00 48.42  ? 190 ASN A CB  1 
ATOM   1154 C  CG  . ASN A 1 156 ? 25.634  16.440  -7.762  1.00 52.65  ? 190 ASN A CG  1 
ATOM   1155 O  OD1 . ASN A 1 156 ? 26.137  16.407  -8.880  1.00 51.26  ? 190 ASN A OD1 1 
ATOM   1156 N  ND2 . ASN A 1 156 ? 25.679  17.521  -6.988  1.00 55.91  ? 190 ASN A ND2 1 
ATOM   1157 N  N   . ILE A 1 157 ? 22.114  15.942  -5.520  1.00 47.00  ? 191 ILE A N   1 
ATOM   1158 C  CA  . ILE A 1 157 ? 21.515  16.862  -4.566  1.00 42.26  ? 191 ILE A CA  1 
ATOM   1159 C  C   . ILE A 1 157 ? 22.140  16.608  -3.202  1.00 43.06  ? 191 ILE A C   1 
ATOM   1160 O  O   . ILE A 1 157 ? 22.747  15.563  -2.952  1.00 43.53  ? 191 ILE A O   1 
ATOM   1161 C  CB  . ILE A 1 157 ? 19.979  16.725  -4.500  1.00 40.15  ? 191 ILE A CB  1 
ATOM   1162 C  CG1 . ILE A 1 157 ? 19.585  15.400  -3.847  1.00 39.95  ? 191 ILE A CG1 1 
ATOM   1163 C  CG2 . ILE A 1 157 ? 19.372  16.833  -5.892  1.00 46.09  ? 191 ILE A CG2 1 
ATOM   1164 C  CD1 . ILE A 1 157 ? 18.089  15.186  -3.742  1.00 38.67  ? 191 ILE A CD1 1 
ATOM   1165 N  N   . THR A 1 158 ? 21.997  17.589  -2.318  1.00 42.52  ? 192 THR A N   1 
ATOM   1166 C  CA  . THR A 1 158 ? 22.540  17.513  -0.972  1.00 36.33  ? 192 THR A CA  1 
ATOM   1167 C  C   . THR A 1 158 ? 21.425  17.727  0.042   1.00 37.33  ? 192 THR A C   1 
ATOM   1168 O  O   . THR A 1 158 ? 20.397  18.342  -0.252  1.00 42.42  ? 192 THR A O   1 
ATOM   1169 C  CB  . THR A 1 158 ? 23.651  18.549  -0.757  1.00 49.08  ? 192 THR A CB  1 
ATOM   1170 O  OG1 . THR A 1 158 ? 23.114  19.869  -0.914  1.00 43.48  ? 192 THR A OG1 1 
ATOM   1171 C  CG2 . THR A 1 158 ? 24.778  18.338  -1.762  1.00 34.72  ? 192 THR A CG2 1 
ATOM   1172 N  N   . VAL A 1 159 ? 21.659  17.228  1.240   1.00 35.09  ? 193 VAL A N   1 
ATOM   1173 C  CA  . VAL A 1 159 ? 20.685  17.357  2.290   1.00 41.83  ? 193 VAL A CA  1 
ATOM   1174 C  C   . VAL A 1 159 ? 21.315  17.823  3.575   1.00 39.30  ? 193 VAL A C   1 
ATOM   1175 O  O   . VAL A 1 159 ? 22.396  17.404  3.929   1.00 42.70  ? 193 VAL A O   1 
ATOM   1176 C  CB  . VAL A 1 159 ? 19.966  16.018  2.555   1.00 44.62  ? 193 VAL A CB  1 
ATOM   1177 C  CG1 . VAL A 1 159 ? 18.894  16.183  3.615   1.00 36.55  ? 193 VAL A CG1 1 
ATOM   1178 C  CG2 . VAL A 1 159 ? 19.361  15.474  1.275   1.00 43.48  ? 193 VAL A CG2 1 
ATOM   1179 N  N   . GLY A 1 160 ? 20.631  18.699  4.277   1.00 40.48  ? 194 GLY A N   1 
ATOM   1180 C  CA  . GLY A 1 160 ? 21.098  19.149  5.555   1.00 33.93  ? 194 GLY A CA  1 
ATOM   1181 C  C   . GLY A 1 160 ? 20.037  18.838  6.564   1.00 41.57  ? 194 GLY A C   1 
ATOM   1182 O  O   . GLY A 1 160 ? 18.888  18.684  6.217   1.00 49.95  ? 194 GLY A O   1 
ATOM   1183 N  N   . ILE A 1 161 ? 20.428  18.710  7.814   1.00 38.69  ? 195 ILE A N   1 
ATOM   1184 C  CA  . ILE A 1 161 ? 19.494  18.385  8.862   1.00 36.20  ? 195 ILE A CA  1 
ATOM   1185 C  C   . ILE A 1 161 ? 19.461  19.491  9.879   1.00 38.54  ? 195 ILE A C   1 
ATOM   1186 O  O   . ILE A 1 161 ? 20.456  19.797  10.502  1.00 48.45  ? 195 ILE A O   1 
ATOM   1187 C  CB  . ILE A 1 161 ? 19.880  17.074  9.548   1.00 43.93  ? 195 ILE A CB  1 
ATOM   1188 C  CG1 . ILE A 1 161 ? 20.227  16.017  8.503   1.00 45.54  ? 195 ILE A CG1 1 
ATOM   1189 C  CG2 . ILE A 1 161 ? 18.755  16.596  10.450  1.00 41.46  ? 195 ILE A CG2 1 
ATOM   1190 C  CD1 . ILE A 1 161 ? 20.845  14.770  9.085   1.00 45.78  ? 195 ILE A CD1 1 
ATOM   1191 N  N   . ASP A 1 162 ? 18.304  20.095  10.039  1.00 45.62  ? 196 ASP A N   1 
ATOM   1192 C  CA  . ASP A 1 162 ? 18.158  21.186  10.971  1.00 46.88  ? 196 ASP A CA  1 
ATOM   1193 C  C   . ASP A 1 162 ? 18.166  20.704  12.394  1.00 51.23  ? 196 ASP A C   1 
ATOM   1194 O  O   . ASP A 1 162 ? 17.611  19.665  12.701  1.00 54.03  ? 196 ASP A O   1 
ATOM   1195 C  CB  . ASP A 1 162 ? 16.867  21.948  10.691  1.00 47.22  ? 196 ASP A CB  1 
ATOM   1196 C  CG  . ASP A 1 162 ? 17.061  23.089  9.735   1.00 58.68  ? 196 ASP A CG  1 
ATOM   1197 O  OD1 . ASP A 1 162 ? 18.180  23.258  9.219   1.00 73.65  ? 196 ASP A OD1 1 
ATOM   1198 O  OD2 . ASP A 1 162 ? 16.090  23.828  9.504   1.00 68.63  ? 196 ASP A OD2 1 
ATOM   1199 N  N   . GLY A 1 163 ? 18.803  21.468  13.263  1.00 57.53  ? 197 GLY A N   1 
ATOM   1200 C  CA  . GLY A 1 163 ? 18.882  21.106  14.653  1.00 54.14  ? 197 GLY A CA  1 
ATOM   1201 C  C   . GLY A 1 163 ? 20.108  20.305  14.872  1.00 55.77  ? 197 GLY A C   1 
ATOM   1202 O  O   . GLY A 1 163 ? 20.340  19.780  15.949  1.00 52.35  ? 197 GLY A O   1 
ATOM   1203 N  N   . THR A 1 164 ? 20.903  20.200  13.830  1.00 54.30  ? 198 THR A N   1 
ATOM   1204 C  CA  . THR A 1 164 ? 22.099  19.419  13.917  1.00 49.12  ? 198 THR A CA  1 
ATOM   1205 C  C   . THR A 1 164 ? 23.242  20.131  13.289  1.00 50.43  ? 198 THR A C   1 
ATOM   1206 O  O   . THR A 1 164 ? 23.065  21.128  12.617  1.00 50.99  ? 198 THR A O   1 
ATOM   1207 C  CB  . THR A 1 164 ? 21.952  18.056  13.194  1.00 48.09  ? 198 THR A CB  1 
ATOM   1208 O  OG1 . THR A 1 164 ? 21.844  18.267  11.784  1.00 41.55  ? 198 THR A OG1 1 
ATOM   1209 C  CG2 . THR A 1 164 ? 20.733  17.309  13.690  1.00 39.30  ? 198 THR A CG2 1 
ATOM   1210 N  N   . ASP A 1 165 ? 24.424  19.620  13.519  1.00 52.71  ? 199 ASP A N   1 
ATOM   1211 C  CA  . ASP A 1 165 ? 25.624  20.160  12.901  1.00 50.21  ? 199 ASP A CA  1 
ATOM   1212 C  C   . ASP A 1 165 ? 25.967  19.456  11.592  1.00 47.15  ? 199 ASP A C   1 
ATOM   1213 O  O   . ASP A 1 165 ? 27.085  19.608  11.086  1.00 48.84  ? 199 ASP A O   1 
ATOM   1214 C  CB  . ASP A 1 165 ? 26.797  20.058  13.881  1.00 49.80  ? 199 ASP A CB  1 
ATOM   1215 C  CG  . ASP A 1 165 ? 27.934  20.997  13.538  1.00 64.61  ? 199 ASP A CG  1 
ATOM   1216 O  OD1 . ASP A 1 165 ? 27.664  22.169  13.199  1.00 72.06  ? 199 ASP A OD1 1 
ATOM   1217 O  OD2 . ASP A 1 165 ? 29.100  20.557  13.608  1.00 66.58  ? 199 ASP A OD2 1 
ATOM   1218 N  N   . ILE A 1 166 ? 25.025  18.706  11.028  1.00 45.69  ? 200 ILE A N   1 
ATOM   1219 C  CA  . ILE A 1 166 ? 25.300  17.744  9.967   1.00 39.51  ? 200 ILE A CA  1 
ATOM   1220 C  C   . ILE A 1 166 ? 24.734  18.259  8.652   1.00 35.02  ? 200 ILE A C   1 
ATOM   1221 O  O   . ILE A 1 166 ? 23.590  18.729  8.598   1.00 34.44  ? 200 ILE A O   1 
ATOM   1222 C  CB  . ILE A 1 166 ? 24.716  16.363  10.312  1.00 38.64  ? 200 ILE A CB  1 
ATOM   1223 C  CG1 . ILE A 1 166 ? 25.301  15.864  11.634  1.00 44.81  ? 200 ILE A CG1 1 
ATOM   1224 C  CG2 . ILE A 1 166 ? 24.987  15.368  9.194   1.00 38.88  ? 200 ILE A CG2 1 
ATOM   1225 C  CD1 . ILE A 1 166 ? 24.672  14.591  12.140  1.00 37.94  ? 200 ILE A CD1 1 
ATOM   1226 N  N   . ALA A 1 167 ? 25.541  18.172  7.595   1.00 31.65  ? 201 ALA A N   1 
ATOM   1227 C  CA  . ALA A 1 167 ? 25.102  18.389  6.223   1.00 38.36  ? 201 ALA A CA  1 
ATOM   1228 C  C   . ALA A 1 167 ? 25.669  17.267  5.368   1.00 39.43  ? 201 ALA A C   1 
ATOM   1229 O  O   . ALA A 1 167 ? 26.862  16.959  5.458   1.00 42.35  ? 201 ALA A O   1 
ATOM   1230 C  CB  . ALA A 1 167 ? 25.555  19.750  5.687   1.00 33.14  ? 201 ALA A CB  1 
ATOM   1231 N  N   . PHE A 1 168 ? 24.819  16.654  4.551   1.00 40.49  ? 202 PHE A N   1 
ATOM   1232 C  CA  . PHE A 1 168 ? 25.198  15.493  3.756   1.00 40.71  ? 202 PHE A CA  1 
ATOM   1233 C  C   . PHE A 1 168 ? 25.534  15.936  2.338   1.00 45.10  ? 202 PHE A C   1 
ATOM   1234 O  O   . PHE A 1 168 ? 24.663  16.433  1.617   1.00 44.60  ? 202 PHE A O   1 
ATOM   1235 C  CB  . PHE A 1 168 ? 24.076  14.455  3.745   1.00 39.25  ? 202 PHE A CB  1 
ATOM   1236 C  CG  . PHE A 1 168 ? 24.441  13.176  3.051   1.00 33.67  ? 202 PHE A CG  1 
ATOM   1237 C  CD1 . PHE A 1 168 ? 25.409  12.339  3.581   1.00 38.77  ? 202 PHE A CD1 1 
ATOM   1238 C  CD2 . PHE A 1 168 ? 23.813  12.806  1.874   1.00 32.66  ? 202 PHE A CD2 1 
ATOM   1239 C  CE1 . PHE A 1 168 ? 25.747  11.158  2.947   1.00 40.98  ? 202 PHE A CE1 1 
ATOM   1240 C  CE2 . PHE A 1 168 ? 24.146  11.626  1.236   1.00 39.85  ? 202 PHE A CE2 1 
ATOM   1241 C  CZ  . PHE A 1 168 ? 25.114  10.802  1.773   1.00 35.84  ? 202 PHE A CZ  1 
ATOM   1242 N  N   . GLY A 1 169 ? 26.792  15.750  1.943   1.00 35.52  ? 203 GLY A N   1 
ATOM   1243 C  CA  . GLY A 1 169 ? 27.229  16.104  0.608   1.00 35.44  ? 203 GLY A CA  1 
ATOM   1244 C  C   . GLY A 1 169 ? 27.108  15.011  -0.425  1.00 44.42  ? 203 GLY A C   1 
ATOM   1245 O  O   . GLY A 1 169 ? 27.245  15.286  -1.621  1.00 50.67  ? 203 GLY A O   1 
ATOM   1246 N  N   . GLY A 1 170 ? 26.850  13.777  0.001   1.00 44.83  ? 204 GLY A N   1 
ATOM   1247 C  CA  . GLY A 1 170 ? 26.751  12.680  -0.949  1.00 39.89  ? 204 GLY A CA  1 
ATOM   1248 C  C   . GLY A 1 170 ? 28.099  12.357  -1.564  1.00 42.09  ? 204 GLY A C   1 
ATOM   1249 O  O   . GLY A 1 170 ? 29.123  12.275  -0.877  1.00 43.47  ? 204 GLY A O   1 
ATOM   1250 N  N   . CYS A 1 171 ? 28.102  12.172  -2.881  1.00 45.16  ? 205 CYS A N   1 
ATOM   1251 C  CA  . CYS A 1 171 ? 29.322  11.901  -3.628  1.00 50.21  ? 205 CYS A CA  1 
ATOM   1252 C  C   . CYS A 1 171 ? 29.963  13.163  -4.190  1.00 48.88  ? 205 CYS A C   1 
ATOM   1253 O  O   . CYS A 1 171 ? 31.053  13.084  -4.765  1.00 56.07  ? 205 CYS A O   1 
ATOM   1254 C  CB  . CYS A 1 171 ? 29.034  10.917  -4.767  1.00 51.43  ? 205 CYS A CB  1 
ATOM   1255 S  SG  . CYS A 1 171 ? 28.205  9.399   -4.248  1.00 53.58  ? 205 CYS A SG  1 
ATOM   1256 N  N   . LEU A 1 172 ? 29.315  14.319  -4.041  1.00 47.79  ? 206 LEU A N   1 
ATOM   1257 C  CA  . LEU A 1 172 ? 29.912  15.566  -4.507  1.00 50.70  ? 206 LEU A CA  1 
ATOM   1258 C  C   . LEU A 1 172 ? 31.129  15.941  -3.672  1.00 50.22  ? 206 LEU A C   1 
ATOM   1259 O  O   . LEU A 1 172 ? 32.124  16.446  -4.205  1.00 44.99  ? 206 LEU A O   1 
ATOM   1260 C  CB  . LEU A 1 172 ? 28.874  16.688  -4.472  1.00 40.26  ? 206 LEU A CB  1 
ATOM   1261 C  CG  . LEU A 1 172 ? 29.344  18.075  -4.919  1.00 43.90  ? 206 LEU A CG  1 
ATOM   1262 C  CD1 . LEU A 1 172 ? 29.350  18.180  -6.435  1.00 42.76  ? 206 LEU A CD1 1 
ATOM   1263 C  CD2 . LEU A 1 172 ? 28.475  19.164  -4.307  1.00 39.76  ? 206 LEU A CD2 1 
ATOM   1264 N  N   . ILE A 1 173 ? 31.073  15.694  -2.367  1.00 44.53  ? 207 ILE A N   1 
ATOM   1265 C  CA  . ILE A 1 173 ? 32.115  16.109  -1.437  1.00 39.27  ? 207 ILE A CA  1 
ATOM   1266 C  C   . ILE A 1 173 ? 32.942  14.894  -1.045  1.00 49.71  ? 207 ILE A C   1 
ATOM   1267 O  O   . ILE A 1 173 ? 32.392  13.845  -0.688  1.00 45.56  ? 207 ILE A O   1 
ATOM   1268 C  CB  . ILE A 1 173 ? 31.510  16.786  -0.195  1.00 38.56  ? 207 ILE A CB  1 
ATOM   1269 C  CG1 . ILE A 1 173 ? 30.652  17.986  -0.607  1.00 48.43  ? 207 ILE A CG1 1 
ATOM   1270 C  CG2 . ILE A 1 173 ? 32.604  17.208  0.774   1.00 40.00  ? 207 ILE A CG2 1 
ATOM   1271 C  CD1 . ILE A 1 173 ? 31.457  19.180  -1.081  1.00 37.24  ? 207 ILE A CD1 1 
ATOM   1272 N  N   . LYS A 1 174 ? 34.262  15.033  -1.118  1.00 44.59  ? 208 LYS A N   1 
ATOM   1273 C  CA  . LYS A 1 174 ? 35.197  14.029  -0.641  1.00 40.61  ? 208 LYS A CA  1 
ATOM   1274 C  C   . LYS A 1 174 ? 35.919  14.562  0.589   1.00 42.82  ? 208 LYS A C   1 
ATOM   1275 O  O   . LYS A 1 174 ? 35.981  15.772  0.820   1.00 39.86  ? 208 LYS A O   1 
ATOM   1276 C  CB  . LYS A 1 174 ? 36.209  13.644  -1.728  1.00 39.22  ? 208 LYS A CB  1 
ATOM   1277 C  CG  . LYS A 1 174 ? 35.688  12.642  -2.755  1.00 46.63  ? 208 LYS A CG  1 
ATOM   1278 C  CD  . LYS A 1 174 ? 34.695  13.275  -3.720  1.00 45.28  ? 208 LYS A CD  1 
ATOM   1279 C  CE  . LYS A 1 174 ? 34.150  12.258  -4.708  1.00 45.54  ? 208 LYS A CE  1 
ATOM   1280 N  NZ  . LYS A 1 174 ? 33.813  10.961  -4.058  1.00 64.12  ? 208 LYS A NZ  1 
ATOM   1281 N  N   . ASP A 1 175 ? 36.463  13.642  1.385   1.00 50.06  ? 209 ASP A N   1 
ATOM   1282 C  CA  . ASP A 1 175 ? 37.113  14.033  2.627   1.00 47.03  ? 209 ASP A CA  1 
ATOM   1283 C  C   . ASP A 1 175 ? 38.348  14.886  2.345   1.00 43.22  ? 209 ASP A C   1 
ATOM   1284 O  O   . ASP A 1 175 ? 38.877  14.918  1.230   1.00 48.27  ? 209 ASP A O   1 
ATOM   1285 C  CB  . ASP A 1 175 ? 37.491  12.800  3.451   1.00 43.80  ? 209 ASP A CB  1 
ATOM   1286 C  CG  . ASP A 1 175 ? 38.617  12.003  2.828   1.00 50.38  ? 209 ASP A CG  1 
ATOM   1287 O  OD1 . ASP A 1 175 ? 38.467  11.567  1.668   1.00 53.01  ? 209 ASP A OD1 1 
ATOM   1288 O  OD2 . ASP A 1 175 ? 39.652  11.811  3.500   1.00 53.79  ? 209 ASP A OD2 1 
ATOM   1289 N  N   . SER A 1 176 ? 38.805  15.588  3.385   1.00 47.99  ? 210 SER A N   1 
ATOM   1290 C  CA  . SER A 1 176 ? 39.904  16.537  3.235   1.00 50.55  ? 210 SER A CA  1 
ATOM   1291 C  C   . SER A 1 176 ? 41.218  15.868  2.855   1.00 49.39  ? 210 SER A C   1 
ATOM   1292 O  O   . SER A 1 176 ? 42.132  16.554  2.385   1.00 49.49  ? 210 SER A O   1 
ATOM   1293 C  CB  . SER A 1 176 ? 40.088  17.332  4.529   1.00 48.97  ? 210 SER A CB  1 
ATOM   1294 O  OG  . SER A 1 176 ? 40.357  16.470  5.621   1.00 45.11  ? 210 SER A OG  1 
ATOM   1295 N  N   . LYS A 1 177 ? 41.338  14.555  3.045   1.00 51.75  ? 211 LYS A N   1 
ATOM   1296 C  CA  . LYS A 1 177 ? 42.560  13.829  2.725   1.00 54.05  ? 211 LYS A CA  1 
ATOM   1297 C  C   . LYS A 1 177 ? 42.431  12.996  1.457   1.00 53.07  ? 211 LYS A C   1 
ATOM   1298 O  O   . LYS A 1 177 ? 43.312  12.177  1.173   1.00 53.78  ? 211 LYS A O   1 
ATOM   1299 C  CB  . LYS A 1 177 ? 42.967  12.940  3.902   1.00 47.92  ? 211 LYS A CB  1 
ATOM   1300 C  CG  . LYS A 1 177 ? 44.064  13.532  4.770   1.00 61.29  ? 211 LYS A CG  1 
ATOM   1301 C  CD  . LYS A 1 177 ? 43.483  14.295  5.950   1.00 73.86  ? 211 LYS A CD  1 
ATOM   1302 C  CE  . LYS A 1 177 ? 44.414  15.412  6.398   1.00 96.75  ? 211 LYS A CE  1 
ATOM   1303 N  NZ  . LYS A 1 177 ? 43.715  16.414  7.250   1.00 97.04  ? 211 LYS A NZ  1 
ATOM   1304 N  N   . ALA A 1 178 ? 41.362  13.185  0.687   1.00 45.89  ? 212 ALA A N   1 
ATOM   1305 C  CA  . ALA A 1 178 ? 41.177  12.426  -0.542  1.00 46.16  ? 212 ALA A CA  1 
ATOM   1306 C  C   . ALA A 1 178 ? 42.223  12.826  -1.574  1.00 53.13  ? 212 ALA A C   1 
ATOM   1307 O  O   . ALA A 1 178 ? 42.492  14.014  -1.775  1.00 50.05  ? 212 ALA A O   1 
ATOM   1308 C  CB  . ALA A 1 178 ? 39.772  12.648  -1.098  1.00 44.00  ? 212 ALA A CB  1 
ATOM   1309 N  N   . LYS A 1 179 ? 42.813  11.830  -2.229  1.00 55.47  ? 213 LYS A N   1 
ATOM   1310 C  CA  . LYS A 1 179 ? 43.822  12.061  -3.252  1.00 50.00  ? 213 LYS A CA  1 
ATOM   1311 C  C   . LYS A 1 179 ? 43.229  12.235  -4.644  1.00 56.02  ? 213 LYS A C   1 
ATOM   1312 O  O   . LYS A 1 179 ? 43.987  12.406  -5.605  1.00 61.38  ? 213 LYS A O   1 
ATOM   1313 C  CB  . LYS A 1 179 ? 44.835  10.910  -3.264  1.00 60.33  ? 213 LYS A CB  1 
ATOM   1314 C  CG  . LYS A 1 179 ? 46.054  11.148  -2.388  1.00 63.20  ? 213 LYS A CG  1 
ATOM   1315 C  CD  . LYS A 1 179 ? 46.267  10.003  -1.412  1.00 81.55  ? 213 LYS A CD  1 
ATOM   1316 C  CE  . LYS A 1 179 ? 46.971  10.477  -0.151  1.00 84.52  ? 213 LYS A CE  1 
ATOM   1317 N  NZ  . LYS A 1 179 ? 46.835  9.497   0.962   1.00 92.77  ? 213 LYS A NZ  1 
ATOM   1318 N  N   . SER A 1 180 ? 41.906  12.200  -4.777  1.00 52.44  ? 214 SER A N   1 
ATOM   1319 C  CA  . SER A 1 180 ? 41.250  12.336  -6.071  1.00 51.52  ? 214 SER A CA  1 
ATOM   1320 C  C   . SER A 1 180 ? 39.791  12.708  -5.838  1.00 50.06  ? 214 SER A C   1 
ATOM   1321 O  O   . SER A 1 180 ? 39.317  12.763  -4.700  1.00 48.57  ? 214 SER A O   1 
ATOM   1322 C  CB  . SER A 1 180 ? 41.375  11.048  -6.891  1.00 51.09  ? 214 SER A CB  1 
ATOM   1323 O  OG  . SER A 1 180 ? 40.314  10.934  -7.823  1.00 63.73  ? 214 SER A OG  1 
ATOM   1324 N  N   . LEU A 1 181 ? 39.079  12.962  -6.936  1.00 52.63  ? 215 LEU A N   1 
ATOM   1325 C  CA  . LEU A 1 181 ? 37.658  13.278  -6.900  1.00 45.40  ? 215 LEU A CA  1 
ATOM   1326 C  C   . LEU A 1 181 ? 36.785  12.055  -7.162  1.00 48.79  ? 215 LEU A C   1 
ATOM   1327 O  O   . LEU A 1 181 ? 35.609  12.203  -7.513  1.00 56.39  ? 215 LEU A O   1 
ATOM   1328 C  CB  . LEU A 1 181 ? 37.337  14.385  -7.906  1.00 47.14  ? 215 LEU A CB  1 
ATOM   1329 C  CG  . LEU A 1 181 ? 37.563  15.821  -7.427  1.00 46.75  ? 215 LEU A CG  1 
ATOM   1330 C  CD1 . LEU A 1 181 ? 37.393  16.807  -8.571  1.00 44.91  ? 215 LEU A CD1 1 
ATOM   1331 C  CD2 . LEU A 1 181 ? 36.623  16.160  -6.281  1.00 36.38  ? 215 LEU A CD2 1 
ATOM   1332 N  N   . GLY A 1 182 ? 37.341  10.854  -7.014  1.00 51.12  ? 216 GLY A N   1 
ATOM   1333 C  CA  . GLY A 1 182 ? 36.537  9.648   -7.131  1.00 51.94  ? 216 GLY A CA  1 
ATOM   1334 C  C   . GLY A 1 182 ? 36.062  9.406   -8.551  1.00 54.36  ? 216 GLY A C   1 
ATOM   1335 O  O   . GLY A 1 182 ? 36.764  9.681   -9.530  1.00 54.26  ? 216 GLY A O   1 
ATOM   1336 N  N   . ASN A 1 183 ? 34.844  8.878   -8.662  1.00 59.25  ? 217 ASN A N   1 
ATOM   1337 C  CA  . ASN A 1 183 ? 34.256  8.549   -9.957  1.00 55.19  ? 217 ASN A CA  1 
ATOM   1338 C  C   . ASN A 1 183 ? 33.925  9.832   -10.709 1.00 56.20  ? 217 ASN A C   1 
ATOM   1339 O  O   . ASN A 1 183 ? 33.022  10.577  -10.316 1.00 62.04  ? 217 ASN A O   1 
ATOM   1340 C  CB  . ASN A 1 183 ? 33.011  7.690   -9.762  1.00 68.85  ? 217 ASN A CB  1 
ATOM   1341 C  CG  . ASN A 1 183 ? 32.392  7.252   -11.075 1.00 80.33  ? 217 ASN A CG  1 
ATOM   1342 O  OD1 . ASN A 1 183 ? 33.083  7.106   -12.083 1.00 65.45  ? 217 ASN A OD1 1 
ATOM   1343 N  ND2 . ASN A 1 183 ? 31.082  7.039   -11.068 1.00 77.84  ? 217 ASN A ND2 1 
ATOM   1344 N  N   . LEU A 1 184 ? 34.655  10.091  -11.795 1.00 48.29  ? 218 LEU A N   1 
ATOM   1345 C  CA  . LEU A 1 184 ? 34.463  11.283  -12.611 1.00 50.50  ? 218 LEU A CA  1 
ATOM   1346 C  C   . LEU A 1 184 ? 33.770  10.971  -13.933 1.00 51.96  ? 218 LEU A C   1 
ATOM   1347 O  O   . LEU A 1 184 ? 33.795  11.797  -14.851 1.00 50.58  ? 218 LEU A O   1 
ATOM   1348 C  CB  . LEU A 1 184 ? 35.807  11.967  -12.871 1.00 51.47  ? 218 LEU A CB  1 
ATOM   1349 C  CG  . LEU A 1 184 ? 36.411  12.802  -11.740 1.00 44.26  ? 218 LEU A CG  1 
ATOM   1350 C  CD1 . LEU A 1 184 ? 37.740  13.401  -12.174 1.00 45.25  ? 218 LEU A CD1 1 
ATOM   1351 C  CD2 . LEU A 1 184 ? 35.451  13.891  -11.297 1.00 44.00  ? 218 LEU A CD2 1 
ATOM   1352 N  N   . GLY A 1 185 ? 33.147  9.796   -14.046 1.00 57.84  ? 219 GLY A N   1 
ATOM   1353 C  CA  . GLY A 1 185 ? 32.572  9.392   -15.320 1.00 50.80  ? 219 GLY A CA  1 
ATOM   1354 C  C   . GLY A 1 185 ? 31.396  10.250  -15.747 1.00 55.85  ? 219 GLY A C   1 
ATOM   1355 O  O   . GLY A 1 185 ? 31.274  10.610  -16.921 1.00 55.34  ? 219 GLY A O   1 
ATOM   1356 N  N   . ASP A 1 186 ? 30.514  10.587  -14.807 1.00 51.66  ? 220 ASP A N   1 
ATOM   1357 C  CA  . ASP A 1 186 ? 29.326  11.383  -15.091 1.00 50.21  ? 220 ASP A CA  1 
ATOM   1358 C  C   . ASP A 1 186 ? 29.459  12.810  -14.567 1.00 50.20  ? 220 ASP A C   1 
ATOM   1359 O  O   . ASP A 1 186 ? 28.457  13.460  -14.264 1.00 51.93  ? 220 ASP A O   1 
ATOM   1360 C  CB  . ASP A 1 186 ? 28.086  10.718  -14.497 1.00 47.69  ? 220 ASP A CB  1 
ATOM   1361 C  CG  . ASP A 1 186 ? 27.770  9.385   -15.146 1.00 56.30  ? 220 ASP A CG  1 
ATOM   1362 O  OD1 . ASP A 1 186 ? 27.979  9.253   -16.371 1.00 61.60  ? 220 ASP A OD1 1 
ATOM   1363 O  OD2 . ASP A 1 186 ? 27.312  8.469   -14.431 1.00 49.50  ? 220 ASP A OD2 1 
ATOM   1364 N  N   . ALA A 1 187 ? 30.684  13.314  -14.473 1.00 44.23  ? 221 ALA A N   1 
ATOM   1365 C  CA  . ALA A 1 187 ? 30.946  14.568  -13.783 1.00 44.07  ? 221 ALA A CA  1 
ATOM   1366 C  C   . ALA A 1 187 ? 30.913  15.758  -14.737 1.00 46.90  ? 221 ALA A C   1 
ATOM   1367 O  O   . ALA A 1 187 ? 31.130  15.634  -15.945 1.00 46.74  ? 221 ALA A O   1 
ATOM   1368 C  CB  . ALA A 1 187 ? 32.299  14.513  -13.072 1.00 50.54  ? 221 ALA A CB  1 
ATOM   1369 N  N   . ASP A 1 188 ? 30.634  16.928  -14.164 1.00 45.19  ? 222 ASP A N   1 
ATOM   1370 C  CA  . ASP A 1 188 ? 30.707  18.207  -14.866 1.00 41.96  ? 222 ASP A CA  1 
ATOM   1371 C  C   . ASP A 1 188 ? 31.990  18.890  -14.406 1.00 50.19  ? 222 ASP A C   1 
ATOM   1372 O  O   . ASP A 1 188 ? 32.036  19.487  -13.327 1.00 50.55  ? 222 ASP A O   1 
ATOM   1373 C  CB  . ASP A 1 188 ? 29.475  19.058  -14.577 1.00 49.81  ? 222 ASP A CB  1 
ATOM   1374 C  CG  . ASP A 1 188 ? 29.372  20.275  -15.483 1.00 52.50  ? 222 ASP A CG  1 
ATOM   1375 O  OD1 . ASP A 1 188 ? 30.387  20.975  -15.678 1.00 52.24  ? 222 ASP A OD1 1 
ATOM   1376 O  OD2 . ASP A 1 188 ? 28.265  20.534  -15.999 1.00 60.46  ? 222 ASP A OD2 1 
ATOM   1377 N  N   . THR A 1 189 ? 33.034  18.803  -15.233 1.00 50.23  ? 223 THR A N   1 
ATOM   1378 C  CA  . THR A 1 189 ? 34.345  19.314  -14.849 1.00 44.87  ? 223 THR A CA  1 
ATOM   1379 C  C   . THR A 1 189 ? 34.366  20.829  -14.691 1.00 54.58  ? 223 THR A C   1 
ATOM   1380 O  O   . THR A 1 189 ? 35.255  21.353  -14.011 1.00 59.01  ? 223 THR A O   1 
ATOM   1381 C  CB  . THR A 1 189 ? 35.394  18.892  -15.877 1.00 51.47  ? 223 THR A CB  1 
ATOM   1382 O  OG1 . THR A 1 189 ? 35.137  19.551  -17.122 1.00 60.37  ? 223 THR A OG1 1 
ATOM   1383 C  CG2 . THR A 1 189 ? 35.357  17.385  -16.088 1.00 47.01  ? 223 THR A CG2 1 
ATOM   1384 N  N   . GLU A 1 190 ? 33.418  21.543  -15.297 1.00 48.35  ? 224 GLU A N   1 
ATOM   1385 C  CA  . GLU A 1 190 ? 33.391  22.998  -15.201 1.00 50.65  ? 224 GLU A CA  1 
ATOM   1386 C  C   . GLU A 1 190 ? 32.680  23.479  -13.939 1.00 56.01  ? 224 GLU A C   1 
ATOM   1387 O  O   . GLU A 1 190 ? 33.210  24.321  -13.208 1.00 54.38  ? 224 GLU A O   1 
ATOM   1388 C  CB  . GLU A 1 190 ? 32.719  23.599  -16.440 1.00 59.15  ? 224 GLU A CB  1 
ATOM   1389 C  CG  . GLU A 1 190 ? 32.745  25.120  -16.472 1.00 76.68  ? 224 GLU A CG  1 
ATOM   1390 C  CD  . GLU A 1 190 ? 31.381  25.727  -16.744 1.00 91.97  ? 224 GLU A CD  1 
ATOM   1391 O  OE1 . GLU A 1 190 ? 31.000  26.679  -16.029 1.00 94.95  ? 224 GLU A OE1 1 
ATOM   1392 O  OE2 . GLU A 1 190 ? 30.691  25.255  -17.672 1.00 101.40 ? 224 GLU A OE2 1 
ATOM   1393 N  N   . ARG A 1 191 ? 31.518  22.946  -13.660 1.00 51.28  ? 225 ARG A N   1 
ATOM   1394 C  CA  . ARG A 1 191 ? 30.748  23.443  -12.552 1.00 47.10  ? 225 ARG A CA  1 
ATOM   1395 C  C   . ARG A 1 191 ? 31.071  22.804  -11.225 1.00 45.74  ? 225 ARG A C   1 
ATOM   1396 O  O   . ARG A 1 191 ? 30.633  23.288  -10.203 1.00 52.28  ? 225 ARG A O   1 
ATOM   1397 C  CB  . ARG A 1 191 ? 29.289  23.245  -12.917 1.00 46.63  ? 225 ARG A CB  1 
ATOM   1398 C  CG  . ARG A 1 191 ? 28.857  23.981  -14.168 1.00 44.96  ? 225 ARG A CG  1 
ATOM   1399 C  CD  . ARG A 1 191 ? 27.529  23.437  -14.646 1.00 63.97  ? 225 ARG A CD  1 
ATOM   1400 N  NE  . ARG A 1 191 ? 26.965  24.185  -15.761 1.00 72.85  ? 225 ARG A NE  1 
ATOM   1401 C  CZ  . ARG A 1 191 ? 26.071  25.156  -15.626 1.00 78.11  ? 225 ARG A CZ  1 
ATOM   1402 N  NH1 . ARG A 1 191 ? 25.608  25.783  -16.697 1.00 68.19  ? 225 ARG A NH1 1 
ATOM   1403 N  NH2 . ARG A 1 191 ? 25.643  25.500  -14.419 1.00 72.68  ? 225 ARG A NH2 1 
ATOM   1404 N  N   . TYR A 1 192 ? 31.852  21.740  -11.226 1.00 44.37  ? 226 TYR A N   1 
ATOM   1405 C  CA  . TYR A 1 192 ? 32.139  21.020  -9.987  1.00 44.00  ? 226 TYR A CA  1 
ATOM   1406 C  C   . TYR A 1 192 ? 32.675  21.957  -8.911  1.00 45.02  ? 226 TYR A C   1 
ATOM   1407 O  O   . TYR A 1 192 ? 32.267  21.874  -7.746  1.00 41.75  ? 226 TYR A O   1 
ATOM   1408 C  CB  . TYR A 1 192 ? 33.134  19.888  -10.257 1.00 47.33  ? 226 TYR A CB  1 
ATOM   1409 C  CG  . TYR A 1 192 ? 33.047  18.716  -9.296  1.00 42.76  ? 226 TYR A CG  1 
ATOM   1410 C  CD1 . TYR A 1 192 ? 32.942  18.916  -7.925  1.00 40.13  ? 226 TYR A CD1 1 
ATOM   1411 C  CD2 . TYR A 1 192 ? 33.085  17.409  -9.763  1.00 48.68  ? 226 TYR A CD2 1 
ATOM   1412 C  CE1 . TYR A 1 192 ? 32.868  17.850  -7.048  1.00 41.64  ? 226 TYR A CE1 1 
ATOM   1413 C  CE2 . TYR A 1 192 ? 33.010  16.335  -8.893  1.00 42.10  ? 226 TYR A CE2 1 
ATOM   1414 C  CZ  . TYR A 1 192 ? 32.902  16.562  -7.537  1.00 36.28  ? 226 TYR A CZ  1 
ATOM   1415 O  OH  . TYR A 1 192 ? 32.828  15.500  -6.666  1.00 39.72  ? 226 TYR A OH  1 
ATOM   1416 N  N   . ALA A 1 193 ? 33.585  22.860  -9.282  1.00 49.58  ? 227 ALA A N   1 
ATOM   1417 C  CA  . ALA A 1 193 ? 34.178  23.765  -8.303  1.00 46.28  ? 227 ALA A CA  1 
ATOM   1418 C  C   . ALA A 1 193 ? 33.123  24.667  -7.675  1.00 49.36  ? 227 ALA A C   1 
ATOM   1419 O  O   . ALA A 1 193 ? 33.019  24.759  -6.446  1.00 44.42  ? 227 ALA A O   1 
ATOM   1420 C  CB  . ALA A 1 193 ? 35.280  24.596  -8.959  1.00 40.22  ? 227 ALA A CB  1 
ATOM   1421 N  N   . ALA A 1 194 ? 32.324  25.341  -8.506  1.00 44.49  ? 228 ALA A N   1 
ATOM   1422 C  CA  . ALA A 1 194 ? 31.300  26.235  -7.978  1.00 39.60  ? 228 ALA A CA  1 
ATOM   1423 C  C   . ALA A 1 194 ? 30.193  25.468  -7.267  1.00 45.98  ? 228 ALA A C   1 
ATOM   1424 O  O   . ALA A 1 194 ? 29.563  26.003  -6.348  1.00 43.95  ? 228 ALA A O   1 
ATOM   1425 C  CB  . ALA A 1 194 ? 30.718  27.092  -9.102  1.00 37.51  ? 228 ALA A CB  1 
ATOM   1426 N  N   . SER A 1 195 ? 29.939  24.221  -7.673  1.00 43.39  ? 229 SER A N   1 
ATOM   1427 C  CA  . SER A 1 195 ? 28.915  23.426  -7.004  1.00 46.08  ? 229 SER A CA  1 
ATOM   1428 C  C   . SER A 1 195 ? 29.368  23.002  -5.614  1.00 41.44  ? 229 SER A C   1 
ATOM   1429 O  O   . SER A 1 195 ? 28.569  22.990  -4.671  1.00 48.96  ? 229 SER A O   1 
ATOM   1430 C  CB  . SER A 1 195 ? 28.560  22.204  -7.850  1.00 43.38  ? 229 SER A CB  1 
ATOM   1431 O  OG  . SER A 1 195 ? 28.111  22.589  -9.138  1.00 41.36  ? 229 SER A OG  1 
ATOM   1432 N  N   . ALA A 1 196 ? 30.648  22.651  -5.467  1.00 47.17  ? 230 ALA A N   1 
ATOM   1433 C  CA  . ALA A 1 196 ? 31.160  22.268  -4.156  1.00 47.62  ? 230 ALA A CA  1 
ATOM   1434 C  C   . ALA A 1 196 ? 31.131  23.442  -3.186  1.00 46.90  ? 230 ALA A C   1 
ATOM   1435 O  O   . ALA A 1 196 ? 30.853  23.263  -1.994  1.00 49.63  ? 230 ALA A O   1 
ATOM   1436 C  CB  . ALA A 1 196 ? 32.578  21.712  -4.289  1.00 42.08  ? 230 ALA A CB  1 
ATOM   1437 N  N   . ARG A 1 197 ? 31.410  24.652  -3.677  1.00 46.07  ? 231 ARG A N   1 
ATOM   1438 C  CA  . ARG A 1 197 ? 31.357  25.832  -2.822  1.00 47.17  ? 231 ARG A CA  1 
ATOM   1439 C  C   . ARG A 1 197 ? 29.926  26.277  -2.550  1.00 46.05  ? 231 ARG A C   1 
ATOM   1440 O  O   . ARG A 1 197 ? 29.652  26.851  -1.490  1.00 51.51  ? 231 ARG A O   1 
ATOM   1441 C  CB  . ARG A 1 197 ? 32.153  26.976  -3.452  1.00 43.64  ? 231 ARG A CB  1 
ATOM   1442 C  CG  . ARG A 1 197 ? 33.577  26.599  -3.807  1.00 51.78  ? 231 ARG A CG  1 
ATOM   1443 C  CD  . ARG A 1 197 ? 34.397  27.806  -4.221  1.00 39.92  ? 231 ARG A CD  1 
ATOM   1444 N  NE  . ARG A 1 197 ? 35.820  27.577  -4.007  1.00 48.77  ? 231 ARG A NE  1 
ATOM   1445 C  CZ  . ARG A 1 197 ? 36.671  27.213  -4.956  1.00 48.88  ? 231 ARG A CZ  1 
ATOM   1446 N  NH1 . ARG A 1 197 ? 36.277  27.035  -6.207  1.00 44.83  ? 231 ARG A NH1 1 
ATOM   1447 N  NH2 . ARG A 1 197 ? 37.949  27.020  -4.643  1.00 48.95  ? 231 ARG A NH2 1 
ATOM   1448 N  N   . ALA A 1 198 ? 29.007  26.029  -3.487  1.00 38.21  ? 232 ALA A N   1 
ATOM   1449 C  CA  . ALA A 1 198 ? 27.606  26.350  -3.241  1.00 40.11  ? 232 ALA A CA  1 
ATOM   1450 C  C   . ALA A 1 198 ? 27.037  25.493  -2.118  1.00 36.63  ? 232 ALA A C   1 
ATOM   1451 O  O   . ALA A 1 198 ? 26.249  25.977  -1.297  1.00 34.87  ? 232 ALA A O   1 
ATOM   1452 C  CB  . ALA A 1 198 ? 26.792  26.172  -4.522  1.00 38.07  ? 232 ALA A CB  1 
ATOM   1453 N  N   . PHE A 1 199 ? 27.431  24.218  -2.064  1.00 40.03  ? 233 PHE A N   1 
ATOM   1454 C  CA  . PHE A 1 199 ? 26.990  23.349  -0.977  1.00 38.33  ? 233 PHE A CA  1 
ATOM   1455 C  C   . PHE A 1 199 ? 27.493  23.854  0.369   1.00 40.83  ? 233 PHE A C   1 
ATOM   1456 O  O   . PHE A 1 199 ? 26.778  23.780  1.376   1.00 38.28  ? 233 PHE A O   1 
ATOM   1457 C  CB  . PHE A 1 199 ? 27.466  21.918  -1.230  1.00 41.58  ? 233 PHE A CB  1 
ATOM   1458 C  CG  . PHE A 1 199 ? 27.474  21.052  -0.002  1.00 40.65  ? 233 PHE A CG  1 
ATOM   1459 C  CD1 . PHE A 1 199 ? 26.291  20.575  0.534   1.00 38.57  ? 233 PHE A CD1 1 
ATOM   1460 C  CD2 . PHE A 1 199 ? 28.668  20.708  0.612   1.00 43.98  ? 233 PHE A CD2 1 
ATOM   1461 C  CE1 . PHE A 1 199 ? 26.296  19.774  1.662   1.00 42.95  ? 233 PHE A CE1 1 
ATOM   1462 C  CE2 . PHE A 1 199 ? 28.679  19.908  1.739   1.00 40.32  ? 233 PHE A CE2 1 
ATOM   1463 C  CZ  . PHE A 1 199 ? 27.492  19.441  2.265   1.00 34.83  ? 233 PHE A CZ  1 
ATOM   1464 N  N   . GLY A 1 200 ? 28.721  24.375  0.406   1.00 39.79  ? 234 GLY A N   1 
ATOM   1465 C  CA  . GLY A 1 200 ? 29.246  24.921  1.644   1.00 39.42  ? 234 GLY A CA  1 
ATOM   1466 C  C   . GLY A 1 200 ? 28.562  26.204  2.072   1.00 42.24  ? 234 GLY A C   1 
ATOM   1467 O  O   . GLY A 1 200 ? 28.525  26.522  3.264   1.00 39.14  ? 234 GLY A O   1 
ATOM   1468 N  N   . ALA A 1 201 ? 28.012  26.957  1.117   1.00 40.24  ? 235 ALA A N   1 
ATOM   1469 C  CA  . ALA A 1 201 ? 27.324  28.193  1.469   1.00 39.69  ? 235 ALA A CA  1 
ATOM   1470 C  C   . ALA A 1 201 ? 25.861  27.952  1.821   1.00 47.14  ? 235 ALA A C   1 
ATOM   1471 O  O   . ALA A 1 201 ? 25.266  28.746  2.559   1.00 38.94  ? 235 ALA A O   1 
ATOM   1472 C  CB  . ALA A 1 201 ? 27.436  29.202  0.324   1.00 37.34  ? 235 ALA A CB  1 
ATOM   1473 N  N   . ALA A 1 202 ? 25.269  26.870  1.311   1.00 39.93  ? 236 ALA A N   1 
ATOM   1474 C  CA  . ALA A 1 202 ? 23.879  26.568  1.636   1.00 40.35  ? 236 ALA A CA  1 
ATOM   1475 C  C   . ALA A 1 202 ? 23.718  26.150  3.091   1.00 37.91  ? 236 ALA A C   1 
ATOM   1476 O  O   . ALA A 1 202 ? 22.684  26.435  3.705   1.00 47.62  ? 236 ALA A O   1 
ATOM   1477 C  CB  . ALA A 1 202 ? 23.347  25.476  0.711   1.00 36.22  ? 236 ALA A CB  1 
ATOM   1478 N  N   . PHE A 1 203 ? 24.721  25.476  3.656   1.00 39.10  ? 237 PHE A N   1 
ATOM   1479 C  CA  . PHE A 1 203 ? 24.708  25.027  5.047   1.00 44.95  ? 237 PHE A CA  1 
ATOM   1480 C  C   . PHE A 1 203 ? 25.916  25.640  5.746   1.00 46.66  ? 237 PHE A C   1 
ATOM   1481 O  O   . PHE A 1 203 ? 26.918  24.954  6.000   1.00 40.86  ? 237 PHE A O   1 
ATOM   1482 C  CB  . PHE A 1 203 ? 24.717  23.502  5.133   1.00 38.83  ? 237 PHE A CB  1 
ATOM   1483 C  CG  . PHE A 1 203 ? 23.711  22.842  4.232   1.00 37.61  ? 237 PHE A CG  1 
ATOM   1484 C  CD1 . PHE A 1 203 ? 22.369  22.809  4.575   1.00 32.81  ? 237 PHE A CD1 1 
ATOM   1485 C  CD2 . PHE A 1 203 ? 24.106  22.261  3.038   1.00 36.97  ? 237 PHE A CD2 1 
ATOM   1486 C  CE1 . PHE A 1 203 ? 21.440  22.206  3.746   1.00 33.84  ? 237 PHE A CE1 1 
ATOM   1487 C  CE2 . PHE A 1 203 ? 23.182  21.655  2.206   1.00 38.45  ? 237 PHE A CE2 1 
ATOM   1488 C  CZ  . PHE A 1 203 ? 21.848  21.627  2.561   1.00 36.93  ? 237 PHE A CZ  1 
ATOM   1489 N  N   . PRO A 1 204 ? 25.854  26.933  6.079   1.00 48.35  ? 238 PRO A N   1 
ATOM   1490 C  CA  . PRO A 1 204 ? 27.044  27.600  6.630   1.00 42.56  ? 238 PRO A CA  1 
ATOM   1491 C  C   . PRO A 1 204 ? 27.406  27.148  8.033   1.00 47.66  ? 238 PRO A C   1 
ATOM   1492 O  O   . PRO A 1 204 ? 28.588  27.190  8.395   1.00 42.42  ? 238 PRO A O   1 
ATOM   1493 C  CB  . PRO A 1 204 ? 26.653  29.084  6.604   1.00 40.40  ? 238 PRO A CB  1 
ATOM   1494 C  CG  . PRO A 1 204 ? 25.163  29.078  6.676   1.00 42.07  ? 238 PRO A CG  1 
ATOM   1495 C  CD  . PRO A 1 204 ? 24.715  27.855  5.931   1.00 34.91  ? 238 PRO A CD  1 
ATOM   1496 N  N   . LYS A 1 205 ? 26.435  26.721  8.833   1.00 49.91  ? 239 LYS A N   1 
ATOM   1497 C  CA  . LYS A 1 205 ? 26.680  26.371  10.225  1.00 51.07  ? 239 LYS A CA  1 
ATOM   1498 C  C   . LYS A 1 205 ? 26.969  24.890  10.431  1.00 44.51  ? 239 LYS A C   1 
ATOM   1499 O  O   . LYS A 1 205 ? 27.109  24.457  11.579  1.00 47.09  ? 239 LYS A O   1 
ATOM   1500 C  CB  . LYS A 1 205 ? 25.484  26.785  11.088  1.00 56.53  ? 239 LYS A CB  1 
ATOM   1501 C  CG  . LYS A 1 205 ? 25.249  28.285  11.136  1.00 49.99  ? 239 LYS A CG  1 
ATOM   1502 C  CD  . LYS A 1 205 ? 24.947  28.750  12.549  1.00 63.93  ? 239 LYS A CD  1 
ATOM   1503 C  CE  . LYS A 1 205 ? 26.195  28.729  13.413  1.00 60.61  ? 239 LYS A CE  1 
ATOM   1504 N  NZ  . LYS A 1 205 ? 25.862  28.640  14.861  1.00 70.66  ? 239 LYS A NZ  1 
ATOM   1505 N  N   . ALA A 1 206 ? 27.066  24.108  9.360   1.00 42.15  ? 240 ALA A N   1 
ATOM   1506 C  CA  . ALA A 1 206 ? 27.294  22.671  9.465   1.00 43.84  ? 240 ALA A CA  1 
ATOM   1507 C  C   . ALA A 1 206 ? 28.794  22.403  9.458   1.00 50.67  ? 240 ALA A C   1 
ATOM   1508 O  O   . ALA A 1 206 ? 29.456  22.561  8.428   1.00 54.08  ? 240 ALA A O   1 
ATOM   1509 C  CB  . ALA A 1 206 ? 26.598  21.932  8.326   1.00 36.83  ? 240 ALA A CB  1 
ATOM   1510 N  N   . ASN A 1 207 ? 29.329  21.996  10.607  1.00 52.85  ? 241 ASN A N   1 
ATOM   1511 C  CA  . ASN A 1 207 ? 30.737  21.647  10.734  1.00 40.95  ? 241 ASN A CA  1 
ATOM   1512 C  C   . ASN A 1 207 ? 30.979  20.145  10.664  1.00 47.13  ? 241 ASN A C   1 
ATOM   1513 O  O   . ASN A 1 207 ? 32.137  19.716  10.677  1.00 50.14  ? 241 ASN A O   1 
ATOM   1514 C  CB  . ASN A 1 207 ? 31.302  22.203  12.044  1.00 45.37  ? 241 ASN A CB  1 
ATOM   1515 C  CG  . ASN A 1 207 ? 31.391  23.714  12.041  1.00 52.90  ? 241 ASN A CG  1 
ATOM   1516 O  OD1 . ASN A 1 207 ? 32.155  24.302  11.275  1.00 62.40  ? 241 ASN A OD1 1 
ATOM   1517 N  ND2 . ASN A 1 207 ? 30.603  24.354  12.897  1.00 51.33  ? 241 ASN A ND2 1 
ATOM   1518 N  N   . THR A 1 208 ? 29.922  19.342  10.596  1.00 48.73  ? 242 THR A N   1 
ATOM   1519 C  CA  . THR A 1 208 ? 30.026  17.897  10.418  1.00 43.37  ? 242 THR A CA  1 
ATOM   1520 C  C   . THR A 1 208 ? 29.546  17.584  9.005   1.00 41.14  ? 242 THR A C   1 
ATOM   1521 O  O   . THR A 1 208 ? 28.340  17.537  8.744   1.00 46.46  ? 242 THR A O   1 
ATOM   1522 C  CB  . THR A 1 208 ? 29.207  17.146  11.465  1.00 45.03  ? 242 THR A CB  1 
ATOM   1523 O  OG1 . THR A 1 208 ? 29.505  17.661  12.769  1.00 49.12  ? 242 THR A OG1 1 
ATOM   1524 C  CG2 . THR A 1 208 ? 29.531  15.661  11.426  1.00 37.27  ? 242 THR A CG2 1 
ATOM   1525 N  N   . ILE A 1 209 ? 30.490  17.379  8.094   1.00 39.28  ? 243 ILE A N   1 
ATOM   1526 C  CA  . ILE A 1 209 ? 30.189  17.124  6.691   1.00 42.80  ? 243 ILE A CA  1 
ATOM   1527 C  C   . ILE A 1 209 ? 30.246  15.618  6.469   1.00 48.71  ? 243 ILE A C   1 
ATOM   1528 O  O   . ILE A 1 209 ? 31.316  15.006  6.551   1.00 43.88  ? 243 ILE A O   1 
ATOM   1529 C  CB  . ILE A 1 209 ? 31.158  17.864  5.760   1.00 40.02  ? 243 ILE A CB  1 
ATOM   1530 C  CG1 . ILE A 1 209 ? 31.230  19.349  6.127   1.00 35.17  ? 243 ILE A CG1 1 
ATOM   1531 C  CG2 . ILE A 1 209 ? 30.735  17.695  4.308   1.00 37.55  ? 243 ILE A CG2 1 
ATOM   1532 C  CD1 . ILE A 1 209 ? 29.882  20.038  6.180   1.00 32.12  ? 243 ILE A CD1 1 
ATOM   1533 N  N   . ALA A 1 210 ? 29.093  15.017  6.195   1.00 45.65  ? 244 ALA A N   1 
ATOM   1534 C  CA  . ALA A 1 210 ? 29.007  13.605  5.863   1.00 42.16  ? 244 ALA A CA  1 
ATOM   1535 C  C   . ALA A 1 210 ? 28.972  13.431  4.350   1.00 42.16  ? 244 ALA A C   1 
ATOM   1536 O  O   . ALA A 1 210 ? 28.453  14.280  3.621   1.00 45.97  ? 244 ALA A O   1 
ATOM   1537 C  CB  . ALA A 1 210 ? 27.768  12.965  6.494   1.00 35.40  ? 244 ALA A CB  1 
ATOM   1538 N  N   . MET A 1 211 ? 29.538  12.320  3.882   1.00 41.65  ? 245 MET A N   1 
ATOM   1539 C  CA  . MET A 1 211 ? 29.619  12.033  2.458   1.00 42.86  ? 245 MET A CA  1 
ATOM   1540 C  C   . MET A 1 211 ? 29.450  10.535  2.243   1.00 43.45  ? 245 MET A C   1 
ATOM   1541 O  O   . MET A 1 211 ? 29.363  9.753   3.195   1.00 40.05  ? 245 MET A O   1 
ATOM   1542 C  CB  . MET A 1 211 ? 30.940  12.534  1.864   1.00 47.45  ? 245 MET A CB  1 
ATOM   1543 C  CG  . MET A 1 211 ? 32.163  12.166  2.679   1.00 49.52  ? 245 MET A CG  1 
ATOM   1544 S  SD  . MET A 1 211 ? 33.441  13.431  2.593   1.00 57.76  ? 245 MET A SD  1 
ATOM   1545 C  CE  . MET A 1 211 ? 33.393  14.072  4.262   1.00 48.39  ? 245 MET A CE  1 
ATOM   1546 N  N   . SER A 1 212 ? 29.416  10.134  0.972   1.00 46.11  ? 246 SER A N   1 
ATOM   1547 C  CA  . SER A 1 212 ? 29.115  8.749   0.630   1.00 46.91  ? 246 SER A CA  1 
ATOM   1548 C  C   . SER A 1 212 ? 30.329  7.844   0.812   1.00 48.75  ? 246 SER A C   1 
ATOM   1549 O  O   . SER A 1 212 ? 30.224  6.764   1.404   1.00 47.28  ? 246 SER A O   1 
ATOM   1550 C  CB  . SER A 1 212 ? 28.603  8.666   -0.808  1.00 41.93  ? 246 SER A CB  1 
ATOM   1551 O  OG  . SER A 1 212 ? 27.415  9.419   -0.974  1.00 44.40  ? 246 SER A OG  1 
ATOM   1552 N  N   . HIS A 1 213 ? 31.490  8.265   0.309   1.00 55.05  ? 247 HIS A N   1 
ATOM   1553 C  CA  . HIS A 1 213 ? 32.661  7.401   0.227   1.00 49.98  ? 247 HIS A CA  1 
ATOM   1554 C  C   . HIS A 1 213 ? 33.738  7.762   1.245   1.00 45.03  ? 247 HIS A C   1 
ATOM   1555 O  O   . HIS A 1 213 ? 34.914  7.451   1.030   1.00 49.09  ? 247 HIS A O   1 
ATOM   1556 C  CB  . HIS A 1 213 ? 33.236  7.441   -1.188  1.00 51.92  ? 247 HIS A CB  1 
ATOM   1557 C  CG  . HIS A 1 213 ? 32.231  7.127   -2.252  1.00 55.89  ? 247 HIS A CG  1 
ATOM   1558 N  ND1 . HIS A 1 213 ? 31.427  6.009   -2.209  1.00 44.46  ? 247 HIS A ND1 1 
ATOM   1559 C  CD2 . HIS A 1 213 ? 31.892  7.791   -3.383  1.00 51.35  ? 247 HIS A CD2 1 
ATOM   1560 C  CE1 . HIS A 1 213 ? 30.640  5.994   -3.270  1.00 54.41  ? 247 HIS A CE1 1 
ATOM   1561 N  NE2 . HIS A 1 213 ? 30.902  7.065   -3.998  1.00 57.84  ? 247 HIS A NE2 1 
ATOM   1562 N  N   . SER A 1 214 ? 33.367  8.408   2.347   1.00 46.54  ? 248 SER A N   1 
ATOM   1563 C  CA  . SER A 1 214 ? 34.334  8.747   3.382   1.00 46.38  ? 248 SER A CA  1 
ATOM   1564 C  C   . SER A 1 214 ? 33.613  8.894   4.712   1.00 46.92  ? 248 SER A C   1 
ATOM   1565 O  O   . SER A 1 214 ? 32.396  9.094   4.764   1.00 52.32  ? 248 SER A O   1 
ATOM   1566 C  CB  . SER A 1 214 ? 35.100  10.035  3.050   1.00 49.64  ? 248 SER A CB  1 
ATOM   1567 O  OG  . SER A 1 214 ? 35.532  10.060  1.701   1.00 59.33  ? 248 SER A OG  1 
ATOM   1568 N  N   . ALA A 1 215 ? 34.387  8.788   5.789   1.00 51.53  ? 249 ALA A N   1 
ATOM   1569 C  CA  . ALA A 1 215 ? 33.871  9.052   7.118   1.00 40.86  ? 249 ALA A CA  1 
ATOM   1570 C  C   . ALA A 1 215 ? 33.524  10.533  7.255   1.00 45.98  ? 249 ALA A C   1 
ATOM   1571 O  O   . ALA A 1 215 ? 34.009  11.365  6.484   1.00 48.03  ? 249 ALA A O   1 
ATOM   1572 C  CB  . ALA A 1 215 ? 34.898  8.643   8.172   1.00 42.58  ? 249 ALA A CB  1 
ATOM   1573 N  N   . PRO A 1 216 ? 32.667  10.886  8.215   1.00 50.96  ? 250 PRO A N   1 
ATOM   1574 C  CA  . PRO A 1 216 ? 32.345  12.303  8.422   1.00 51.32  ? 250 PRO A CA  1 
ATOM   1575 C  C   . PRO A 1 216 ? 33.596  13.122  8.706   1.00 43.37  ? 250 PRO A C   1 
ATOM   1576 O  O   . PRO A 1 216 ? 34.494  12.692  9.432   1.00 54.16  ? 250 PRO A O   1 
ATOM   1577 C  CB  . PRO A 1 216 ? 31.400  12.279  9.627   1.00 40.75  ? 250 PRO A CB  1 
ATOM   1578 C  CG  . PRO A 1 216 ? 30.773  10.932  9.577   1.00 46.68  ? 250 PRO A CG  1 
ATOM   1579 C  CD  . PRO A 1 216 ? 31.828  10.003  9.046   1.00 51.65  ? 250 PRO A CD  1 
ATOM   1580 N  N   . ASP A 1 217 ? 33.648  14.314  8.115   1.00 46.68  ? 251 ASP A N   1 
ATOM   1581 C  CA  . ASP A 1 217 ? 34.804  15.194  8.200   1.00 47.93  ? 251 ASP A CA  1 
ATOM   1582 C  C   . ASP A 1 217 ? 34.333  16.612  8.505   1.00 42.10  ? 251 ASP A C   1 
ATOM   1583 O  O   . ASP A 1 217 ? 33.132  16.896  8.560   1.00 42.81  ? 251 ASP A O   1 
ATOM   1584 C  CB  . ASP A 1 217 ? 35.618  15.152  6.900   1.00 45.71  ? 251 ASP A CB  1 
ATOM   1585 C  CG  . ASP A 1 217 ? 37.049  15.613  7.089   1.00 49.49  ? 251 ASP A CG  1 
ATOM   1586 O  OD1 . ASP A 1 217 ? 37.396  16.037  8.212   1.00 53.44  ? 251 ASP A OD1 1 
ATOM   1587 O  OD2 . ASP A 1 217 ? 37.827  15.556  6.113   1.00 51.95  ? 251 ASP A OD2 1 
ATOM   1588 N  N   . SER A 1 218 ? 35.293  17.509  8.704   1.00 52.64  ? 252 SER A N   1 
ATOM   1589 C  CA  . SER A 1 218 ? 34.999  18.911  8.964   1.00 49.70  ? 252 SER A CA  1 
ATOM   1590 C  C   . SER A 1 218 ? 34.734  19.629  7.641   1.00 41.98  ? 252 SER A C   1 
ATOM   1591 O  O   . SER A 1 218 ? 34.663  19.014  6.573   1.00 44.01  ? 252 SER A O   1 
ATOM   1592 C  CB  . SER A 1 218 ? 36.142  19.553  9.745   1.00 47.47  ? 252 SER A CB  1 
ATOM   1593 O  OG  . SER A 1 218 ? 37.275  19.753  8.917   1.00 51.31  ? 252 SER A OG  1 
ATOM   1594 N  N   . ARG A 1 219 ? 34.587  20.954  7.699   1.00 42.09  ? 253 ARG A N   1 
ATOM   1595 C  CA  . ARG A 1 219 ? 34.348  21.733  6.491   1.00 37.38  ? 253 ARG A CA  1 
ATOM   1596 C  C   . ARG A 1 219 ? 35.575  21.824  5.595   1.00 45.00  ? 253 ARG A C   1 
ATOM   1597 O  O   . ARG A 1 219 ? 35.459  22.313  4.466   1.00 44.81  ? 253 ARG A O   1 
ATOM   1598 C  CB  . ARG A 1 219 ? 33.862  23.136  6.859   1.00 32.35  ? 253 ARG A CB  1 
ATOM   1599 C  CG  . ARG A 1 219 ? 32.503  23.146  7.536   1.00 44.45  ? 253 ARG A CG  1 
ATOM   1600 C  CD  . ARG A 1 219 ? 32.071  24.552  7.919   1.00 47.28  ? 253 ARG A CD  1 
ATOM   1601 N  NE  . ARG A 1 219 ? 31.734  25.360  6.754   1.00 43.58  ? 253 ARG A NE  1 
ATOM   1602 C  CZ  . ARG A 1 219 ? 30.583  25.290  6.099   1.00 48.18  ? 253 ARG A CZ  1 
ATOM   1603 N  NH1 . ARG A 1 219 ? 29.631  24.447  6.463   1.00 43.39  ? 253 ARG A NH1 1 
ATOM   1604 N  NH2 . ARG A 1 219 ? 30.382  26.087  5.053   1.00 39.61  ? 253 ARG A NH2 1 
ATOM   1605 N  N   . ALA A 1 220 ? 36.740  21.369  6.064   1.00 42.45  ? 254 ALA A N   1 
ATOM   1606 C  CA  . ALA A 1 220 ? 37.906  21.285  5.195   1.00 37.37  ? 254 ALA A CA  1 
ATOM   1607 C  C   . ALA A 1 220 ? 37.673  20.338  4.026   1.00 46.55  ? 254 ALA A C   1 
ATOM   1608 O  O   . ALA A 1 220 ? 38.321  20.484  2.985   1.00 46.80  ? 254 ALA A O   1 
ATOM   1609 C  CB  . ALA A 1 220 ? 39.132  20.841  5.995   1.00 36.81  ? 254 ALA A CB  1 
ATOM   1610 N  N   . ALA A 1 221 ? 36.760  19.375  4.177   1.00 44.64  ? 255 ALA A N   1 
ATOM   1611 C  CA  . ALA A 1 221 ? 36.405  18.500  3.066   1.00 40.62  ? 255 ALA A CA  1 
ATOM   1612 C  C   . ALA A 1 221 ? 35.736  19.270  1.936   1.00 40.35  ? 255 ALA A C   1 
ATOM   1613 O  O   . ALA A 1 221 ? 35.871  18.893  0.766   1.00 38.32  ? 255 ALA A O   1 
ATOM   1614 C  CB  . ALA A 1 221 ? 35.490  17.378  3.555   1.00 32.95  ? 255 ALA A CB  1 
ATOM   1615 N  N   . ILE A 1 222 ? 35.013  20.343  2.260   1.00 36.60  ? 256 ILE A N   1 
ATOM   1616 C  CA  . ILE A 1 222 ? 34.359  21.139  1.226   1.00 37.97  ? 256 ILE A CA  1 
ATOM   1617 C  C   . ILE A 1 222 ? 35.392  21.928  0.433   1.00 41.45  ? 256 ILE A C   1 
ATOM   1618 O  O   . ILE A 1 222 ? 35.407  21.898  -0.803  1.00 37.35  ? 256 ILE A O   1 
ATOM   1619 C  CB  . ILE A 1 222 ? 33.301  22.065  1.851   1.00 42.04  ? 256 ILE A CB  1 
ATOM   1620 C  CG1 . ILE A 1 222 ? 32.206  21.243  2.534   1.00 44.12  ? 256 ILE A CG1 1 
ATOM   1621 C  CG2 . ILE A 1 222 ? 32.705  22.982  0.794   1.00 38.20  ? 256 ILE A CG2 1 
ATOM   1622 C  CD1 . ILE A 1 222 ? 31.128  22.083  3.180   1.00 33.90  ? 256 ILE A CD1 1 
ATOM   1623 N  N   . THR A 1 223 ? 36.276  22.643  1.134   1.00 45.42  ? 257 THR A N   1 
ATOM   1624 C  CA  . THR A 1 223 ? 37.279  23.456  0.454   1.00 41.14  ? 257 THR A CA  1 
ATOM   1625 C  C   . THR A 1 223 ? 38.283  22.587  -0.294  1.00 36.75  ? 257 THR A C   1 
ATOM   1626 O  O   . THR A 1 223 ? 38.725  22.947  -1.391  1.00 39.42  ? 257 THR A O   1 
ATOM   1627 C  CB  . THR A 1 223 ? 37.996  24.357  1.459   1.00 38.30  ? 257 THR A CB  1 
ATOM   1628 O  OG1 . THR A 1 223 ? 38.699  23.549  2.412   1.00 41.84  ? 257 THR A OG1 1 
ATOM   1629 C  CG2 . THR A 1 223 ? 36.996  25.240  2.192   1.00 34.03  ? 257 THR A CG2 1 
ATOM   1630 N  N   . HIS A 1 224 ? 38.655  21.442  0.283   1.00 39.52  ? 258 HIS A N   1 
ATOM   1631 C  CA  . HIS A 1 224 ? 39.578  20.539  -0.397  1.00 38.43  ? 258 HIS A CA  1 
ATOM   1632 C  C   . HIS A 1 224 ? 38.957  19.976  -1.668  1.00 41.24  ? 258 HIS A C   1 
ATOM   1633 O  O   . HIS A 1 224 ? 39.645  19.808  -2.682  1.00 42.79  ? 258 HIS A O   1 
ATOM   1634 C  CB  . HIS A 1 224 ? 39.998  19.410  0.544   1.00 39.24  ? 258 HIS A CB  1 
ATOM   1635 C  CG  . HIS A 1 224 ? 40.875  18.382  -0.099  1.00 42.14  ? 258 HIS A CG  1 
ATOM   1636 N  ND1 . HIS A 1 224 ? 42.130  18.675  -0.589  1.00 38.61  ? 258 HIS A ND1 1 
ATOM   1637 C  CD2 . HIS A 1 224 ? 40.680  17.062  -0.329  1.00 44.48  ? 258 HIS A CD2 1 
ATOM   1638 C  CE1 . HIS A 1 224 ? 42.669  17.580  -1.094  1.00 40.27  ? 258 HIS A CE1 1 
ATOM   1639 N  NE2 . HIS A 1 224 ? 41.810  16.587  -0.948  1.00 47.30  ? 258 HIS A NE2 1 
ATOM   1640 N  N   . THR A 1 225 ? 37.656  19.680  -1.634  1.00 42.93  ? 259 THR A N   1 
ATOM   1641 C  CA  . THR A 1 225 ? 36.969  19.229  -2.839  1.00 36.80  ? 259 THR A CA  1 
ATOM   1642 C  C   . THR A 1 225 ? 36.872  20.350  -3.866  1.00 49.41  ? 259 THR A C   1 
ATOM   1643 O  O   . THR A 1 225 ? 37.027  20.114  -5.070  1.00 50.26  ? 259 THR A O   1 
ATOM   1644 C  CB  . THR A 1 225 ? 35.577  18.703  -2.483  1.00 44.39  ? 259 THR A CB  1 
ATOM   1645 O  OG1 . THR A 1 225 ? 35.697  17.633  -1.537  1.00 40.11  ? 259 THR A OG1 1 
ATOM   1646 C  CG2 . THR A 1 225 ? 34.858  18.198  -3.724  1.00 42.01  ? 259 THR A CG2 1 
ATOM   1647 N  N   . ALA A 1 226 ? 36.628  21.580  -3.406  1.00 42.83  ? 260 ALA A N   1 
ATOM   1648 C  CA  . ALA A 1 226 ? 36.539  22.711  -4.323  1.00 40.57  ? 260 ALA A CA  1 
ATOM   1649 C  C   . ALA A 1 226 ? 37.884  23.003  -4.976  1.00 47.63  ? 260 ALA A C   1 
ATOM   1650 O  O   . ALA A 1 226 ? 37.947  23.291  -6.177  1.00 44.60  ? 260 ALA A O   1 
ATOM   1651 C  CB  . ALA A 1 226 ? 36.022  23.944  -3.584  1.00 42.11  ? 260 ALA A CB  1 
ATOM   1652 N  N   . ARG A 1 227 ? 38.970  22.935  -4.203  1.00 42.47  ? 261 ARG A N   1 
ATOM   1653 C  CA  . ARG A 1 227 ? 40.293  23.175  -4.771  1.00 47.81  ? 261 ARG A CA  1 
ATOM   1654 C  C   . ARG A 1 227 ? 40.692  22.060  -5.728  1.00 47.78  ? 261 ARG A C   1 
ATOM   1655 O  O   . ARG A 1 227 ? 41.344  22.313  -6.748  1.00 53.92  ? 261 ARG A O   1 
ATOM   1656 C  CB  . ARG A 1 227 ? 41.327  23.325  -3.655  1.00 45.92  ? 261 ARG A CB  1 
ATOM   1657 C  CG  . ARG A 1 227 ? 41.403  24.727  -3.066  1.00 51.11  ? 261 ARG A CG  1 
ATOM   1658 C  CD  . ARG A 1 227 ? 41.599  25.777  -4.152  1.00 53.83  ? 261 ARG A CD  1 
ATOM   1659 N  NE  . ARG A 1 227 ? 42.988  25.866  -4.587  1.00 51.39  ? 261 ARG A NE  1 
ATOM   1660 C  CZ  . ARG A 1 227 ? 43.393  26.509  -5.673  1.00 52.67  ? 261 ARG A CZ  1 
ATOM   1661 N  NH1 . ARG A 1 227 ? 42.538  27.133  -6.467  1.00 52.84  ? 261 ARG A NH1 1 
ATOM   1662 N  NH2 . ARG A 1 227 ? 44.690  26.527  -5.971  1.00 48.39  ? 261 ARG A NH2 1 
ATOM   1663 N  N   . MET A 1 228 ? 40.315  20.818  -5.414  1.00 46.42  ? 262 MET A N   1 
ATOM   1664 C  CA  . MET A 1 228 ? 40.543  19.722  -6.351  1.00 47.13  ? 262 MET A CA  1 
ATOM   1665 C  C   . MET A 1 228 ? 39.754  19.934  -7.635  1.00 50.77  ? 262 MET A C   1 
ATOM   1666 O  O   . MET A 1 228 ? 40.268  19.698  -8.736  1.00 48.68  ? 262 MET A O   1 
ATOM   1667 C  CB  . MET A 1 228 ? 40.163  18.389  -5.708  1.00 42.42  ? 262 MET A CB  1 
ATOM   1668 C  CG  . MET A 1 228 ? 41.187  17.844  -4.733  1.00 40.89  ? 262 MET A CG  1 
ATOM   1669 S  SD  . MET A 1 228 ? 41.139  16.047  -4.624  1.00 43.98  ? 262 MET A SD  1 
ATOM   1670 C  CE  . MET A 1 228 ? 39.769  15.817  -3.495  1.00 37.81  ? 262 MET A CE  1 
ATOM   1671 N  N   . ALA A 1 229 ? 38.502  20.383  -7.516  1.00 45.19  ? 263 ALA A N   1 
ATOM   1672 C  CA  . ALA A 1 229 ? 37.702  20.644  -8.706  1.00 44.60  ? 263 ALA A CA  1 
ATOM   1673 C  C   . ALA A 1 229 ? 38.179  21.891  -9.438  1.00 47.40  ? 263 ALA A C   1 
ATOM   1674 O  O   . ALA A 1 229 ? 37.955  22.021  -10.647 1.00 45.96  ? 263 ALA A O   1 
ATOM   1675 C  CB  . ALA A 1 229 ? 36.226  20.773  -8.329  1.00 48.38  ? 263 ALA A CB  1 
ATOM   1676 N  N   . ASP A 1 230 ? 38.828  22.817  -8.726  1.00 51.60  ? 264 ASP A N   1 
ATOM   1677 C  CA  . ASP A 1 230 ? 39.402  23.988  -9.381  1.00 49.06  ? 264 ASP A CA  1 
ATOM   1678 C  C   . ASP A 1 230 ? 40.449  23.581  -10.408 1.00 50.79  ? 264 ASP A C   1 
ATOM   1679 O  O   . ASP A 1 230 ? 40.494  24.134  -11.513 1.00 59.78  ? 264 ASP A O   1 
ATOM   1680 C  CB  . ASP A 1 230 ? 40.015  24.928  -8.342  1.00 44.63  ? 264 ASP A CB  1 
ATOM   1681 C  CG  . ASP A 1 230 ? 38.998  25.870  -7.735  1.00 53.97  ? 264 ASP A CG  1 
ATOM   1682 O  OD1 . ASP A 1 230 ? 38.054  26.265  -8.450  1.00 57.65  ? 264 ASP A OD1 1 
ATOM   1683 O  OD2 . ASP A 1 230 ? 39.148  26.220  -6.545  1.00 50.88  ? 264 ASP A OD2 1 
ATOM   1684 N  N   . LYS A 1 231 ? 41.301  22.616  -10.060 1.00 54.11  ? 265 LYS A N   1 
ATOM   1685 C  CA  . LYS A 1 231 ? 42.315  22.147  -10.996 1.00 58.00  ? 265 LYS A CA  1 
ATOM   1686 C  C   . LYS A 1 231 ? 41.716  21.234  -12.057 1.00 64.64  ? 265 LYS A C   1 
ATOM   1687 O  O   . LYS A 1 231 ? 42.235  21.166  -13.177 1.00 70.45  ? 265 LYS A O   1 
ATOM   1688 C  CB  . LYS A 1 231 ? 43.438  21.427  -10.244 1.00 52.11  ? 265 LYS A CB  1 
ATOM   1689 C  CG  . LYS A 1 231 ? 43.849  22.086  -8.924  1.00 71.26  ? 265 LYS A CG  1 
ATOM   1690 C  CD  . LYS A 1 231 ? 44.065  23.593  -9.063  1.00 76.85  ? 265 LYS A CD  1 
ATOM   1691 C  CE  . LYS A 1 231 ? 45.305  24.055  -8.317  1.00 68.78  ? 265 LYS A CE  1 
ATOM   1692 N  NZ  . LYS A 1 231 ? 45.841  25.324  -8.879  1.00 57.86  ? 265 LYS A NZ  1 
ATOM   1693 N  N   . LEU A 1 232 ? 40.631  20.530  -11.725 1.00 64.37  ? 266 LEU A N   1 
ATOM   1694 C  CA  . LEU A 1 232 ? 39.913  19.757  -12.732 1.00 66.67  ? 266 LEU A CA  1 
ATOM   1695 C  C   . LEU A 1 232 ? 39.241  20.666  -13.753 1.00 64.97  ? 266 LEU A C   1 
ATOM   1696 O  O   . LEU A 1 232 ? 39.118  20.296  -14.927 1.00 69.36  ? 266 LEU A O   1 
ATOM   1697 C  CB  . LEU A 1 232 ? 38.879  18.855  -12.058 1.00 54.68  ? 266 LEU A CB  1 
ATOM   1698 C  CG  . LEU A 1 232 ? 37.983  18.013  -12.968 1.00 61.61  ? 266 LEU A CG  1 
ATOM   1699 C  CD1 . LEU A 1 232 ? 38.780  16.893  -13.619 1.00 45.96  ? 266 LEU A CD1 1 
ATOM   1700 C  CD2 . LEU A 1 232 ? 36.795  17.458  -12.196 1.00 57.43  ? 266 LEU A CD2 1 
ATOM   1701 N  N   . ARG A 1 233 ? 38.812  21.856  -13.329 1.00 62.14  ? 267 ARG A N   1 
ATOM   1702 C  CA  . ARG A 1 233 ? 38.171  22.794  -14.245 1.00 62.50  ? 267 ARG A CA  1 
ATOM   1703 C  C   . ARG A 1 233 ? 39.148  23.280  -15.309 1.00 68.37  ? 267 ARG A C   1 
ATOM   1704 O  O   . ARG A 1 233 ? 38.851  23.228  -16.509 1.00 72.77  ? 267 ARG A O   1 
ATOM   1705 C  CB  . ARG A 1 233 ? 37.597  23.975  -13.461 1.00 59.07  ? 267 ARG A CB  1 
ATOM   1706 C  CG  . ARG A 1 233 ? 36.538  24.769  -14.205 1.00 59.76  ? 267 ARG A CG  1 
ATOM   1707 C  CD  . ARG A 1 233 ? 36.534  26.222  -13.757 1.00 62.27  ? 267 ARG A CD  1 
ATOM   1708 N  NE  . ARG A 1 233 ? 35.276  26.890  -14.067 1.00 68.97  ? 267 ARG A NE  1 
ATOM   1709 C  CZ  . ARG A 1 233 ? 35.026  27.526  -15.203 1.00 73.32  ? 267 ARG A CZ  1 
ATOM   1710 N  NH1 . ARG A 1 233 ? 35.929  27.600  -16.167 1.00 73.08  ? 267 ARG A NH1 1 
ATOM   1711 N  NH2 . ARG A 1 233 ? 33.840  28.104  -15.375 1.00 74.85  ? 267 ARG A NH2 1 
ATOM   1712 N  N   T LEU A 1 234 ? 40.382  23.537  -14.928 1.00 79.11  ? 268 LEU A N   1 
ATOM   1713 C  CA  T LEU A 1 234 ? 41.355  24.075  -15.878 1.00 86.16  ? 268 LEU A CA  1 
ATOM   1714 C  C   T LEU A 1 234 ? 42.060  22.980  -16.667 1.00 91.35  ? 268 LEU A C   1 
ATOM   1715 O  O   T LEU A 1 234 ? 42.853  23.272  -17.551 1.00 88.85  ? 268 LEU A O   1 
ATOM   1716 C  CB  T LEU A 1 234 ? 42.368  24.956  -15.156 1.00 78.28  ? 268 LEU A CB  1 
ATOM   1717 C  CG  T LEU A 1 234 ? 41.763  26.031  -14.261 1.00 85.42  ? 268 LEU A CG  1 
ATOM   1718 C  CD1 T LEU A 1 234 ? 42.809  26.631  -13.336 1.00 84.25  ? 268 LEU A CD1 1 
ATOM   1719 C  CD2 T LEU A 1 234 ? 41.088  27.101  -15.099 1.00 92.47  ? 268 LEU A CD2 1 
ATOM   1720 N  N   T GLU A 1 235 ? 41.797  21.723  -16.339 1.00 102.68 ? 269 GLU A N   1 
ATOM   1721 C  CA  T GLU A 1 235 ? 42.362  20.620  -17.092 1.00 103.47 ? 269 GLU A CA  1 
ATOM   1722 C  C   T GLU A 1 235 ? 41.377  20.170  -18.138 1.00 102.82 ? 269 GLU A C   1 
ATOM   1723 O  O   T GLU A 1 235 ? 41.483  19.063  -18.640 1.00 106.29 ? 269 GLU A O   1 
ATOM   1724 C  CB  T GLU A 1 235 ? 42.671  19.457  -16.170 1.00 97.64  ? 269 GLU A CB  1 
ATOM   1725 C  CG  T GLU A 1 235 ? 43.896  19.663  -15.299 1.00 111.96 ? 269 GLU A CG  1 
ATOM   1726 C  CD  T GLU A 1 235 ? 44.006  18.630  -14.197 1.00 122.06 ? 269 GLU A CD  1 
ATOM   1727 O  OE1 T GLU A 1 235 ? 45.089  18.527  -13.584 1.00 119.58 ? 269 GLU A OE1 1 
ATOM   1728 O  OE2 T GLU A 1 235 ? 43.009  17.922  -13.944 1.00 114.60 ? 269 GLU A OE2 1 
ATOM   1729 N  N   T ARG A 1 236 ? 40.418  21.021  -18.480 1.00 93.81  ? 270 ARG A N   1 
ATOM   1730 C  CA  T ARG A 1 236 ? 39.390  20.640  -19.422 1.00 85.13  ? 270 ARG A CA  1 
ATOM   1731 C  C   T ARG A 1 236 ? 38.697  21.872  -19.980 1.00 85.75  ? 270 ARG A C   1 
ATOM   1732 O  O   T ARG A 1 236 ? 39.254  22.963  -19.988 1.00 81.10  ? 270 ARG A O   1 
ATOM   1733 C  CB  T ARG A 1 236 ? 38.375  19.734  -18.735 1.00 30.00  ? 270 ARG A CB  1 
ATOM   1734 C  CG  T ARG A 1 236 ? 37.791  18.636  -19.600 1.00 30.00  ? 270 ARG A CG  1 
ATOM   1735 C  CD  T ARG A 1 236 ? 38.813  17.539  -19.810 1.00 30.00  ? 270 ARG A CD  1 
ATOM   1736 N  NE  T ARG A 1 236 ? 39.585  17.313  -18.595 1.00 30.00  ? 270 ARG A NE  1 
ATOM   1737 C  CZ  T ARG A 1 236 ? 39.298  16.395  -17.682 1.00 30.00  ? 270 ARG A CZ  1 
ATOM   1738 N  NH1 T ARG A 1 236 ? 38.255  15.595  -17.846 1.00 30.00  ? 270 ARG A NH1 1 
ATOM   1739 N  NH2 T ARG A 1 236 ? 40.064  16.269  -16.611 1.00 30.00  ? 270 ARG A NH2 1 
ATOM   1740 N  N   . ASP B 1 6   ? 28.238  22.764  -36.842 1.00 79.33  ? 40  ASP B N   1 
ATOM   1741 C  CA  . ASP B 1 6   ? 27.800  23.511  -35.669 1.00 90.11  ? 40  ASP B CA  1 
ATOM   1742 C  C   . ASP B 1 6   ? 28.471  24.879  -35.607 1.00 84.50  ? 40  ASP B C   1 
ATOM   1743 O  O   . ASP B 1 6   ? 29.580  25.011  -35.091 1.00 95.73  ? 40  ASP B O   1 
ATOM   1744 C  CB  . ASP B 1 6   ? 28.097  22.725  -34.390 1.00 86.22  ? 40  ASP B CB  1 
ATOM   1745 C  CG  . ASP B 1 6   ? 27.090  21.622  -34.136 1.00 94.17  ? 40  ASP B CG  1 
ATOM   1746 O  OD1 . ASP B 1 6   ? 26.117  21.516  -34.911 1.00 89.70  ? 40  ASP B OD1 1 
ATOM   1747 O  OD2 . ASP B 1 6   ? 27.268  20.862  -33.161 1.00 95.95  ? 40  ASP B OD2 1 
ATOM   1748 N  N   . GLN B 1 7   ? 27.793  25.895  -36.135 1.00 86.19  ? 41  GLN B N   1 
ATOM   1749 C  CA  . GLN B 1 7   ? 28.311  27.259  -36.131 1.00 92.21  ? 41  GLN B CA  1 
ATOM   1750 C  C   . GLN B 1 7   ? 27.798  27.976  -34.888 1.00 89.40  ? 41  GLN B C   1 
ATOM   1751 O  O   . GLN B 1 7   ? 26.596  28.233  -34.760 1.00 86.14  ? 41  GLN B O   1 
ATOM   1752 C  CB  . GLN B 1 7   ? 27.904  28.003  -37.400 1.00 91.58  ? 41  GLN B CB  1 
ATOM   1753 C  CG  . GLN B 1 7   ? 28.859  29.126  -37.782 1.00 99.43  ? 41  GLN B CG  1 
ATOM   1754 C  CD  . GLN B 1 7   ? 28.141  30.351  -38.313 1.00 98.51  ? 41  GLN B CD  1 
ATOM   1755 O  OE1 . GLN B 1 7   ? 26.949  30.541  -38.068 1.00 90.11  ? 41  GLN B OE1 1 
ATOM   1756 N  NE2 . GLN B 1 7   ? 28.866  31.195  -39.039 1.00 97.99  ? 41  GLN B NE2 1 
ATOM   1757 N  N   . ARG B 1 8   ? 28.708  28.297  -33.974 1.00 86.44  ? 42  ARG B N   1 
ATOM   1758 C  CA  . ARG B 1 8   ? 28.353  29.033  -32.770 1.00 89.38  ? 42  ARG B CA  1 
ATOM   1759 C  C   . ARG B 1 8   ? 28.170  30.509  -33.093 1.00 93.18  ? 42  ARG B C   1 
ATOM   1760 O  O   . ARG B 1 8   ? 28.960  31.101  -33.833 1.00 97.36  ? 42  ARG B O   1 
ATOM   1761 C  CB  . ARG B 1 8   ? 29.427  28.864  -31.693 1.00 88.10  ? 42  ARG B CB  1 
ATOM   1762 C  CG  . ARG B 1 8   ? 29.761  27.420  -31.328 1.00 90.19  ? 42  ARG B CG  1 
ATOM   1763 C  CD  . ARG B 1 8   ? 30.867  26.853  -32.209 1.00 101.12 ? 42  ARG B CD  1 
ATOM   1764 N  NE  . ARG B 1 8   ? 31.990  27.774  -32.340 1.00 102.03 ? 42  ARG B NE  1 
ATOM   1765 C  CZ  . ARG B 1 8   ? 32.529  28.137  -33.496 1.00 97.01  ? 42  ARG B CZ  1 
ATOM   1766 N  NH1 . ARG B 1 8   ? 32.067  27.680  -34.648 1.00 81.23  ? 42  ARG B NH1 1 
ATOM   1767 N  NH2 . ARG B 1 8   ? 33.556  28.983  -33.496 1.00 100.76 ? 42  ARG B NH2 1 
ATOM   1768 N  N   . PHE B 1 9   ? 27.114  31.102  -32.536 1.00 85.97  ? 43  PHE B N   1 
ATOM   1769 C  CA  . PHE B 1 9   ? 26.825  32.524  -32.727 1.00 77.02  ? 43  PHE B CA  1 
ATOM   1770 C  C   . PHE B 1 9   ? 26.272  33.058  -31.409 1.00 75.34  ? 43  PHE B C   1 
ATOM   1771 O  O   . PHE B 1 9   ? 25.097  32.848  -31.092 1.00 81.67  ? 43  PHE B O   1 
ATOM   1772 C  CB  . PHE B 1 9   ? 25.846  32.746  -33.873 1.00 70.73  ? 43  PHE B CB  1 
ATOM   1773 C  CG  . PHE B 1 9   ? 25.569  34.194  -34.158 1.00 83.64  ? 43  PHE B CG  1 
ATOM   1774 C  CD1 . PHE B 1 9   ? 26.582  35.034  -34.590 1.00 85.78  ? 43  PHE B CD1 1 
ATOM   1775 C  CD2 . PHE B 1 9   ? 24.296  34.715  -33.995 1.00 74.35  ? 43  PHE B CD2 1 
ATOM   1776 C  CE1 . PHE B 1 9   ? 26.332  36.367  -34.854 1.00 83.33  ? 43  PHE B CE1 1 
ATOM   1777 C  CE2 . PHE B 1 9   ? 24.039  36.048  -34.258 1.00 81.68  ? 43  PHE B CE2 1 
ATOM   1778 C  CZ  . PHE B 1 9   ? 25.059  36.874  -34.688 1.00 82.98  ? 43  PHE B CZ  1 
ATOM   1779 N  N   . GLY B 1 10  ? 27.120  33.747  -30.650 1.00 83.10  ? 44  GLY B N   1 
ATOM   1780 C  CA  . GLY B 1 10  ? 26.736  34.222  -29.336 1.00 86.51  ? 44  GLY B CA  1 
ATOM   1781 C  C   . GLY B 1 10  ? 26.571  33.082  -28.353 1.00 81.21  ? 44  GLY B C   1 
ATOM   1782 O  O   . GLY B 1 10  ? 27.522  32.341  -28.086 1.00 87.78  ? 44  GLY B O   1 
ATOM   1783 N  N   . ASP B 1 11  ? 25.364  32.927  -27.809 1.00 80.34  ? 45  ASP B N   1 
ATOM   1784 C  CA  . ASP B 1 11  ? 25.043  31.824  -26.914 1.00 77.13  ? 45  ASP B CA  1 
ATOM   1785 C  C   . ASP B 1 11  ? 24.212  30.747  -27.602 1.00 79.25  ? 45  ASP B C   1 
ATOM   1786 O  O   . ASP B 1 11  ? 23.555  29.951  -26.923 1.00 82.20  ? 45  ASP B O   1 
ATOM   1787 C  CB  . ASP B 1 11  ? 24.312  32.342  -25.675 1.00 81.48  ? 45  ASP B CB  1 
ATOM   1788 C  CG  . ASP B 1 11  ? 24.902  33.635  -25.148 1.00 91.25  ? 45  ASP B CG  1 
ATOM   1789 O  OD1 . ASP B 1 11  ? 26.054  33.613  -24.666 1.00 85.18  ? 45  ASP B OD1 1 
ATOM   1790 O  OD2 . ASP B 1 11  ? 24.211  34.674  -25.213 1.00 95.48  ? 45  ASP B OD2 1 
ATOM   1791 N  N   . LEU B 1 12  ? 24.230  30.705  -28.933 1.00 79.66  ? 46  LEU B N   1 
ATOM   1792 C  CA  . LEU B 1 12  ? 23.396  29.791  -29.696 1.00 71.23  ? 46  LEU B CA  1 
ATOM   1793 C  C   . LEU B 1 12  ? 24.253  28.975  -30.651 1.00 75.18  ? 46  LEU B C   1 
ATOM   1794 O  O   . LEU B 1 12  ? 25.276  29.447  -31.156 1.00 80.62  ? 46  LEU B O   1 
ATOM   1795 C  CB  . LEU B 1 12  ? 22.325  30.548  -30.491 1.00 73.89  ? 46  LEU B CB  1 
ATOM   1796 C  CG  . LEU B 1 12  ? 21.557  31.626  -29.727 1.00 70.46  ? 46  LEU B CG  1 
ATOM   1797 C  CD1 . LEU B 1 12  ? 20.617  32.358  -30.661 1.00 65.96  ? 46  LEU B CD1 1 
ATOM   1798 C  CD2 . LEU B 1 12  ? 20.795  31.027  -28.558 1.00 57.69  ? 46  LEU B CD2 1 
ATOM   1799 N  N   . VAL B 1 13  ? 23.818  27.742  -30.897 1.00 69.32  ? 47  VAL B N   1 
ATOM   1800 C  CA  . VAL B 1 13  ? 24.459  26.837  -31.844 1.00 71.26  ? 47  VAL B CA  1 
ATOM   1801 C  C   . VAL B 1 13  ? 23.504  26.626  -33.010 1.00 64.22  ? 47  VAL B C   1 
ATOM   1802 O  O   . VAL B 1 13  ? 22.305  26.402  -32.804 1.00 71.87  ? 47  VAL B O   1 
ATOM   1803 C  CB  . VAL B 1 13  ? 24.832  25.498  -31.183 1.00 75.47  ? 47  VAL B CB  1 
ATOM   1804 C  CG1 . VAL B 1 13  ? 25.475  24.561  -32.195 1.00 71.88  ? 47  VAL B CG1 1 
ATOM   1805 C  CG2 . VAL B 1 13  ? 25.761  25.732  -30.000 1.00 60.02  ? 47  VAL B CG2 1 
ATOM   1806 N  N   . PHE B 1 14  ? 24.031  26.702  -34.229 1.00 69.72  ? 48  PHE B N   1 
ATOM   1807 C  CA  . PHE B 1 14  ? 23.235  26.561  -35.441 1.00 68.63  ? 48  PHE B CA  1 
ATOM   1808 C  C   . PHE B 1 14  ? 23.758  25.390  -36.259 1.00 67.27  ? 48  PHE B C   1 
ATOM   1809 O  O   . PHE B 1 14  ? 24.971  25.256  -36.453 1.00 73.10  ? 48  PHE B O   1 
ATOM   1810 C  CB  . PHE B 1 14  ? 23.266  27.846  -36.273 1.00 64.60  ? 48  PHE B CB  1 
ATOM   1811 C  CG  . PHE B 1 14  ? 22.489  28.980  -35.666 1.00 66.78  ? 48  PHE B CG  1 
ATOM   1812 C  CD1 . PHE B 1 14  ? 23.039  29.751  -34.655 1.00 72.23  ? 48  PHE B CD1 1 
ATOM   1813 C  CD2 . PHE B 1 14  ? 21.209  29.273  -36.105 1.00 67.30  ? 48  PHE B CD2 1 
ATOM   1814 C  CE1 . PHE B 1 14  ? 22.326  30.794  -34.094 1.00 69.91  ? 48  PHE B CE1 1 
ATOM   1815 C  CE2 . PHE B 1 14  ? 20.492  30.314  -35.547 1.00 66.09  ? 48  PHE B CE2 1 
ATOM   1816 C  CZ  . PHE B 1 14  ? 21.051  31.075  -34.540 1.00 70.95  ? 48  PHE B CZ  1 
ATOM   1817 N  N   . ARG B 1 15  ? 22.844  24.545  -36.731 1.00 60.07  ? 49  ARG B N   1 
ATOM   1818 C  CA  . ARG B 1 15  ? 23.179  23.412  -37.582 1.00 60.24  ? 49  ARG B CA  1 
ATOM   1819 C  C   . ARG B 1 15  ? 22.249  23.401  -38.784 1.00 63.22  ? 49  ARG B C   1 
ATOM   1820 O  O   . ARG B 1 15  ? 21.026  23.469  -38.627 1.00 69.14  ? 49  ARG B O   1 
ATOM   1821 C  CB  . ARG B 1 15  ? 23.076  22.087  -36.820 1.00 69.41  ? 49  ARG B CB  1 
ATOM   1822 C  CG  . ARG B 1 15  ? 24.087  21.039  -37.262 1.00 76.72  ? 49  ARG B CG  1 
ATOM   1823 C  CD  . ARG B 1 15  ? 23.560  19.629  -37.050 1.00 78.25  ? 49  ARG B CD  1 
ATOM   1824 N  NE  . ARG B 1 15  ? 24.202  18.972  -35.917 1.00 94.05  ? 49  ARG B NE  1 
ATOM   1825 C  CZ  . ARG B 1 15  ? 25.316  18.258  -35.998 1.00 97.40  ? 49  ARG B CZ  1 
ATOM   1826 N  NH1 . ARG B 1 15  ? 25.950  18.094  -37.147 1.00 84.71  ? 49  ARG B NH1 1 
ATOM   1827 N  NH2 . ARG B 1 15  ? 25.809  17.698  -34.897 1.00 97.31  ? 49  ARG B NH2 1 
ATOM   1828 N  N   . GLN B 1 16  ? 22.829  23.314  -39.978 1.00 64.60  ? 50  GLN B N   1 
ATOM   1829 C  CA  . GLN B 1 16  ? 22.063  23.276  -41.218 1.00 62.87  ? 50  GLN B CA  1 
ATOM   1830 C  C   . GLN B 1 16  ? 21.755  21.822  -41.554 1.00 69.19  ? 50  GLN B C   1 
ATOM   1831 O  O   . GLN B 1 16  ? 22.662  21.040  -41.857 1.00 73.18  ? 50  GLN B O   1 
ATOM   1832 C  CB  . GLN B 1 16  ? 22.834  23.955  -42.347 1.00 62.03  ? 50  GLN B CB  1 
ATOM   1833 C  CG  . GLN B 1 16  ? 22.174  23.841  -43.710 1.00 68.72  ? 50  GLN B CG  1 
ATOM   1834 C  CD  . GLN B 1 16  ? 22.912  24.621  -44.780 1.00 75.26  ? 50  GLN B CD  1 
ATOM   1835 O  OE1 . GLN B 1 16  ? 24.125  24.481  -44.942 1.00 75.67  ? 50  GLN B OE1 1 
ATOM   1836 N  NE2 . GLN B 1 16  ? 22.182  25.449  -45.519 1.00 66.97  ? 50  GLN B NE2 1 
ATOM   1837 N  N   . LEU B 1 17  ? 20.474  21.458  -41.497 1.00 63.68  ? 51  LEU B N   1 
ATOM   1838 C  CA  . LEU B 1 17  ? 20.056  20.088  -41.761 1.00 65.76  ? 51  LEU B CA  1 
ATOM   1839 C  C   . LEU B 1 17  ? 19.696  19.843  -43.219 1.00 70.42  ? 51  LEU B C   1 
ATOM   1840 O  O   . LEU B 1 17  ? 19.682  18.685  -43.652 1.00 77.39  ? 51  LEU B O   1 
ATOM   1841 C  CB  . LEU B 1 17  ? 18.861  19.722  -40.875 1.00 62.13  ? 51  LEU B CB  1 
ATOM   1842 C  CG  . LEU B 1 17  ? 18.802  20.411  -39.510 1.00 61.66  ? 51  LEU B CG  1 
ATOM   1843 C  CD1 . LEU B 1 17  ? 17.443  20.198  -38.859 1.00 65.46  ? 51  LEU B CD1 1 
ATOM   1844 C  CD2 . LEU B 1 17  ? 19.918  19.912  -38.604 1.00 63.88  ? 51  LEU B CD2 1 
ATOM   1845 N  N   . ALA B 1 18  ? 19.410  20.895  -43.976 1.00 72.03  ? 52  ALA B N   1 
ATOM   1846 C  CA  . ALA B 1 18  ? 19.057  20.788  -45.384 1.00 76.63  ? 52  ALA B CA  1 
ATOM   1847 C  C   . ALA B 1 18  ? 19.104  22.186  -45.992 1.00 85.36  ? 52  ALA B C   1 
ATOM   1848 O  O   . ALA B 1 18  ? 19.007  23.178  -45.265 1.00 85.02  ? 52  ALA B O   1 
ATOM   1849 C  CB  . ALA B 1 18  ? 17.661  20.170  -45.570 1.00 72.73  ? 52  ALA B CB  1 
ATOM   1850 N  N   . PRO B 1 19  ? 19.276  22.286  -47.309 1.00 74.44  ? 53  PRO B N   1 
ATOM   1851 C  CA  . PRO B 1 19  ? 19.141  23.594  -47.964 1.00 69.17  ? 53  PRO B CA  1 
ATOM   1852 C  C   . PRO B 1 19  ? 17.786  24.210  -47.649 1.00 85.72  ? 53  PRO B C   1 
ATOM   1853 O  O   . PRO B 1 19  ? 16.747  23.554  -47.759 1.00 91.82  ? 53  PRO B O   1 
ATOM   1854 C  CB  . PRO B 1 19  ? 19.290  23.275  -49.458 1.00 67.47  ? 53  PRO B CB  1 
ATOM   1855 C  CG  . PRO B 1 19  ? 19.507  21.797  -49.569 1.00 65.75  ? 53  PRO B CG  1 
ATOM   1856 C  CD  . PRO B 1 19  ? 19.787  21.246  -48.216 1.00 69.48  ? 53  PRO B CD  1 
ATOM   1857 N  N   . ASN B 1 20  ? 17.813  25.476  -47.228 1.00 87.32  ? 54  ASN B N   1 
ATOM   1858 C  CA  . ASN B 1 20  ? 16.643  26.234  -46.787 1.00 88.60  ? 54  ASN B CA  1 
ATOM   1859 C  C   . ASN B 1 20  ? 16.057  25.710  -45.481 1.00 83.84  ? 54  ASN B C   1 
ATOM   1860 O  O   . ASN B 1 20  ? 14.891  25.980  -45.178 1.00 83.03  ? 54  ASN B O   1 
ATOM   1861 C  CB  . ASN B 1 20  ? 15.549  26.273  -47.863 1.00 84.94  ? 54  ASN B CB  1 
ATOM   1862 C  CG  . ASN B 1 20  ? 16.001  26.962  -49.133 1.00 96.15  ? 54  ASN B CG  1 
ATOM   1863 O  OD1 . ASN B 1 20  ? 17.186  26.958  -49.466 1.00 97.21  ? 54  ASN B OD1 1 
ATOM   1864 N  ND2 . ASN B 1 20  ? 15.057  27.557  -49.852 1.00 98.82  ? 54  ASN B ND2 1 
ATOM   1865 N  N   . VAL B 1 21  ? 16.833  24.963  -44.695 1.00 73.93  ? 55  VAL B N   1 
ATOM   1866 C  CA  . VAL B 1 21  ? 16.388  24.464  -43.396 1.00 71.01  ? 55  VAL B CA  1 
ATOM   1867 C  C   . VAL B 1 21  ? 17.555  24.556  -42.422 1.00 67.11  ? 55  VAL B C   1 
ATOM   1868 O  O   . VAL B 1 21  ? 18.623  23.988  -42.674 1.00 65.31  ? 55  VAL B O   1 
ATOM   1869 C  CB  . VAL B 1 21  ? 15.869  23.016  -43.459 1.00 66.20  ? 55  VAL B CB  1 
ATOM   1870 C  CG1 . VAL B 1 21  ? 15.694  22.465  -42.052 1.00 60.80  ? 55  VAL B CG1 1 
ATOM   1871 C  CG2 . VAL B 1 21  ? 14.556  22.943  -44.223 1.00 65.56  ? 55  VAL B CG2 1 
ATOM   1872 N  N   . TRP B 1 22  ? 17.353  25.259  -41.311 1.00 66.27  ? 56  TRP B N   1 
ATOM   1873 C  CA  . TRP B 1 22  ? 18.355  25.373  -40.263 1.00 62.00  ? 56  TRP B CA  1 
ATOM   1874 C  C   . TRP B 1 22  ? 17.733  25.001  -38.926 1.00 60.67  ? 56  TRP B C   1 
ATOM   1875 O  O   . TRP B 1 22  ? 16.512  25.027  -38.757 1.00 63.43  ? 56  TRP B O   1 
ATOM   1876 C  CB  . TRP B 1 22  ? 18.943  26.789  -40.194 1.00 64.09  ? 56  TRP B CB  1 
ATOM   1877 C  CG  . TRP B 1 22  ? 19.904  27.089  -41.299 1.00 65.30  ? 56  TRP B CG  1 
ATOM   1878 C  CD1 . TRP B 1 22  ? 21.249  26.862  -41.299 1.00 62.45  ? 56  TRP B CD1 1 
ATOM   1879 C  CD2 . TRP B 1 22  ? 19.594  27.670  -42.571 1.00 70.18  ? 56  TRP B CD2 1 
ATOM   1880 N  NE1 . TRP B 1 22  ? 21.797  27.267  -42.492 1.00 66.40  ? 56  TRP B NE1 1 
ATOM   1881 C  CE2 . TRP B 1 22  ? 20.802  27.767  -43.290 1.00 67.73  ? 56  TRP B CE2 1 
ATOM   1882 C  CE3 . TRP B 1 22  ? 18.414  28.118  -43.171 1.00 64.04  ? 56  TRP B CE3 1 
ATOM   1883 C  CZ2 . TRP B 1 22  ? 20.863  28.294  -44.579 1.00 71.38  ? 56  TRP B CZ2 1 
ATOM   1884 C  CZ3 . TRP B 1 22  ? 18.476  28.641  -44.450 1.00 76.64  ? 56  TRP B CZ3 1 
ATOM   1885 C  CH2 . TRP B 1 22  ? 19.692  28.724  -45.140 1.00 80.24  ? 56  TRP B CH2 1 
ATOM   1886 N  N   . GLN B 1 23  ? 18.592  24.650  -37.971 1.00 55.64  ? 57  GLN B N   1 
ATOM   1887 C  CA  . GLN B 1 23  ? 18.166  24.280  -36.625 1.00 55.23  ? 57  GLN B CA  1 
ATOM   1888 C  C   . GLN B 1 23  ? 18.924  25.140  -35.624 1.00 63.28  ? 57  GLN B C   1 
ATOM   1889 O  O   . GLN B 1 23  ? 20.149  25.029  -35.508 1.00 61.77  ? 57  GLN B O   1 
ATOM   1890 C  CB  . GLN B 1 23  ? 18.406  22.794  -36.353 1.00 55.38  ? 57  GLN B CB  1 
ATOM   1891 C  CG  . GLN B 1 23  ? 17.889  22.326  -35.000 1.00 52.20  ? 57  GLN B CG  1 
ATOM   1892 C  CD  . GLN B 1 23  ? 18.498  21.009  -34.563 1.00 56.76  ? 57  GLN B CD  1 
ATOM   1893 O  OE1 . GLN B 1 23  ? 17.790  20.024  -34.353 1.00 52.92  ? 57  GLN B OE1 1 
ATOM   1894 N  NE2 . GLN B 1 23  ? 19.818  20.986  -34.422 1.00 57.30  ? 57  GLN B NE2 1 
ATOM   1895 N  N   . HIS B 1 24  ? 18.201  25.993  -34.904 1.00 53.53  ? 58  HIS B N   1 
ATOM   1896 C  CA  . HIS B 1 24  ? 18.803  26.816  -33.867 1.00 55.65  ? 58  HIS B CA  1 
ATOM   1897 C  C   . HIS B 1 24  ? 18.663  26.133  -32.514 1.00 52.87  ? 58  HIS B C   1 
ATOM   1898 O  O   . HIS B 1 24  ? 17.604  25.593  -32.181 1.00 55.55  ? 58  HIS B O   1 
ATOM   1899 C  CB  . HIS B 1 24  ? 18.169  28.210  -33.833 1.00 55.35  ? 58  HIS B CB  1 
ATOM   1900 C  CG  . HIS B 1 24  ? 16.726  28.220  -33.432 1.00 56.83  ? 58  HIS B CG  1 
ATOM   1901 N  ND1 . HIS B 1 24  ? 16.317  28.184  -32.116 1.00 54.47  ? 58  HIS B ND1 1 
ATOM   1902 C  CD2 . HIS B 1 24  ? 15.595  28.281  -34.175 1.00 55.23  ? 58  HIS B CD2 1 
ATOM   1903 C  CE1 . HIS B 1 24  ? 14.997  28.215  -32.066 1.00 46.40  ? 58  HIS B CE1 1 
ATOM   1904 N  NE2 . HIS B 1 24  ? 14.535  28.275  -33.302 1.00 45.62  ? 58  HIS B NE2 1 
ATOM   1905 N  N   . THR B 1 25  ? 19.746  26.150  -31.741 1.00 52.47  ? 59  THR B N   1 
ATOM   1906 C  CA  . THR B 1 25  ? 19.799  25.507  -30.435 1.00 53.57  ? 59  THR B CA  1 
ATOM   1907 C  C   . THR B 1 25  ? 20.156  26.553  -29.389 1.00 65.38  ? 59  THR B C   1 
ATOM   1908 O  O   . THR B 1 25  ? 21.182  27.231  -29.510 1.00 59.38  ? 59  THR B O   1 
ATOM   1909 C  CB  . THR B 1 25  ? 20.819  24.366  -30.421 1.00 53.23  ? 59  THR B CB  1 
ATOM   1910 O  OG1 . THR B 1 25  ? 20.428  23.361  -31.365 1.00 48.02  ? 59  THR B OG1 1 
ATOM   1911 C  CG2 . THR B 1 25  ? 20.905  23.744  -29.035 1.00 51.26  ? 59  THR B CG2 1 
ATOM   1912 N  N   . SER B 1 26  ? 19.312  26.680  -28.370 1.00 57.87  ? 60  SER B N   1 
ATOM   1913 C  CA  . SER B 1 26  ? 19.535  27.605  -27.271 1.00 53.87  ? 60  SER B CA  1 
ATOM   1914 C  C   . SER B 1 26  ? 19.608  26.838  -25.957 1.00 55.88  ? 60  SER B C   1 
ATOM   1915 O  O   . SER B 1 26  ? 19.010  25.768  -25.810 1.00 56.61  ? 60  SER B O   1 
ATOM   1916 C  CB  . SER B 1 26  ? 18.433  28.667  -27.208 1.00 44.48  ? 60  SER B CB  1 
ATOM   1917 O  OG  . SER B 1 26  ? 17.211  28.111  -26.760 1.00 64.84  ? 60  SER B OG  1 
ATOM   1918 N  N   . PHE B 1 27  ? 20.350  27.396  -25.005 1.00 56.79  ? 61  PHE B N   1 
ATOM   1919 C  CA  . PHE B 1 27  ? 20.617  26.744  -23.733 1.00 58.53  ? 61  PHE B CA  1 
ATOM   1920 C  C   . PHE B 1 27  ? 20.067  27.582  -22.586 1.00 50.79  ? 61  PHE B C   1 
ATOM   1921 O  O   . PHE B 1 27  ? 19.828  28.785  -22.724 1.00 54.01  ? 61  PHE B O   1 
ATOM   1922 C  CB  . PHE B 1 27  ? 22.122  26.507  -23.540 1.00 49.53  ? 61  PHE B CB  1 
ATOM   1923 C  CG  . PHE B 1 27  ? 22.787  25.855  -24.720 1.00 52.45  ? 61  PHE B CG  1 
ATOM   1924 C  CD1 . PHE B 1 27  ? 23.326  26.621  -25.741 1.00 59.80  ? 61  PHE B CD1 1 
ATOM   1925 C  CD2 . PHE B 1 27  ? 22.869  24.475  -24.809 1.00 58.42  ? 61  PHE B CD2 1 
ATOM   1926 C  CE1 . PHE B 1 27  ? 23.936  26.023  -26.828 1.00 55.74  ? 61  PHE B CE1 1 
ATOM   1927 C  CE2 . PHE B 1 27  ? 23.478  23.871  -25.894 1.00 59.95  ? 61  PHE B CE2 1 
ATOM   1928 C  CZ  . PHE B 1 27  ? 24.011  24.646  -26.904 1.00 57.48  ? 61  PHE B CZ  1 
ATOM   1929 N  N   . MET B 1 28  ? 19.870  26.927  -21.444 1.00 45.83  ? 62  MET B N   1 
ATOM   1930 C  CA  . MET B 1 28  ? 19.311  27.585  -20.272 1.00 53.54  ? 62  MET B CA  1 
ATOM   1931 C  C   . MET B 1 28  ? 19.674  26.788  -19.029 1.00 50.38  ? 62  MET B C   1 
ATOM   1932 O  O   . MET B 1 28  ? 19.574  25.558  -19.023 1.00 44.19  ? 62  MET B O   1 
ATOM   1933 C  CB  . MET B 1 28  ? 17.788  27.726  -20.390 1.00 50.61  ? 62  MET B CB  1 
ATOM   1934 C  CG  . MET B 1 28  ? 17.061  27.882  -19.063 1.00 57.57  ? 62  MET B CG  1 
ATOM   1935 S  SD  . MET B 1 28  ? 17.298  29.507  -18.318 1.00 62.37  ? 62  MET B SD  1 
ATOM   1936 C  CE  . MET B 1 28  ? 16.275  30.518  -19.384 1.00 48.90  ? 62  MET B CE  1 
ATOM   1937 N  N   . ASP B 1 29  ? 20.095  27.497  -17.985 1.00 59.93  ? 63  ASP B N   1 
ATOM   1938 C  CA  . ASP B 1 29  ? 20.406  26.878  -16.700 1.00 56.64  ? 63  ASP B CA  1 
ATOM   1939 C  C   . ASP B 1 29  ? 19.101  26.565  -15.978 1.00 54.97  ? 63  ASP B C   1 
ATOM   1940 O  O   . ASP B 1 29  ? 18.429  27.470  -15.474 1.00 67.23  ? 63  ASP B O   1 
ATOM   1941 C  CB  . ASP B 1 29  ? 21.290  27.801  -15.867 1.00 59.88  ? 63  ASP B CB  1 
ATOM   1942 C  CG  . ASP B 1 29  ? 22.371  27.052  -15.117 1.00 64.03  ? 63  ASP B CG  1 
ATOM   1943 O  OD1 . ASP B 1 29  ? 22.228  25.825  -14.935 1.00 67.68  ? 63  ASP B OD1 1 
ATOM   1944 O  OD2 . ASP B 1 29  ? 23.364  27.690  -14.708 1.00 74.70  ? 63  ASP B OD2 1 
ATOM   1945 N  N   . VAL B 1 30  ? 18.742  25.291  -15.928 1.00 53.06  ? 64  VAL B N   1 
ATOM   1946 C  CA  . VAL B 1 30  ? 17.517  24.834  -15.276 1.00 46.32  ? 64  VAL B CA  1 
ATOM   1947 C  C   . VAL B 1 30  ? 17.889  24.240  -13.922 1.00 51.11  ? 64  VAL B C   1 
ATOM   1948 O  O   . VAL B 1 30  ? 18.785  23.386  -13.863 1.00 57.90  ? 64  VAL B O   1 
ATOM   1949 C  CB  . VAL B 1 30  ? 16.768  23.800  -16.137 1.00 51.94  ? 64  VAL B CB  1 
ATOM   1950 C  CG1 . VAL B 1 30  ? 15.621  23.182  -15.352 1.00 44.20  ? 64  VAL B CG1 1 
ATOM   1951 C  CG2 . VAL B 1 30  ? 16.258  24.447  -17.416 1.00 44.92  ? 64  VAL B CG2 1 
ATOM   1952 N  N   . PRO B 1 31  ? 17.251  24.661  -12.831 1.00 52.05  ? 65  PRO B N   1 
ATOM   1953 C  CA  . PRO B 1 31  ? 17.596  24.110  -11.514 1.00 48.09  ? 65  PRO B CA  1 
ATOM   1954 C  C   . PRO B 1 31  ? 17.329  22.613  -11.448 1.00 44.51  ? 65  PRO B C   1 
ATOM   1955 O  O   . PRO B 1 31  ? 16.283  22.129  -11.885 1.00 44.52  ? 65  PRO B O   1 
ATOM   1956 C  CB  . PRO B 1 31  ? 16.691  24.891  -10.555 1.00 45.98  ? 65  PRO B CB  1 
ATOM   1957 C  CG  . PRO B 1 31  ? 16.338  26.141  -11.293 1.00 45.95  ? 65  PRO B CG  1 
ATOM   1958 C  CD  . PRO B 1 31  ? 16.263  25.748  -12.736 1.00 44.32  ? 65  PRO B CD  1 
ATOM   1959 N  N   . GLY B 1 32  ? 18.292  21.880  -10.891 1.00 50.94  ? 66  GLY B N   1 
ATOM   1960 C  CA  . GLY B 1 32  ? 18.226  20.440  -10.805 1.00 47.99  ? 66  GLY B CA  1 
ATOM   1961 C  C   . GLY B 1 32  ? 18.798  19.705  -11.999 1.00 50.49  ? 66  GLY B C   1 
ATOM   1962 O  O   . GLY B 1 32  ? 19.131  18.520  -11.879 1.00 45.53  ? 66  GLY B O   1 
ATOM   1963 N  N   . PHE B 1 33  ? 18.932  20.375  -13.141 1.00 51.07  ? 67  PHE B N   1 
ATOM   1964 C  CA  . PHE B 1 33  ? 19.407  19.755  -14.369 1.00 52.55  ? 67  PHE B CA  1 
ATOM   1965 C  C   . PHE B 1 33  ? 20.714  20.334  -14.883 1.00 55.47  ? 67  PHE B C   1 
ATOM   1966 O  O   . PHE B 1 33  ? 21.499  19.601  -15.490 1.00 59.02  ? 67  PHE B O   1 
ATOM   1967 C  CB  . PHE B 1 33  ? 18.351  19.887  -15.480 1.00 51.56  ? 67  PHE B CB  1 
ATOM   1968 C  CG  . PHE B 1 33  ? 17.149  19.005  -15.290 1.00 53.16  ? 67  PHE B CG  1 
ATOM   1969 C  CD1 . PHE B 1 33  ? 16.250  19.241  -14.262 1.00 57.12  ? 67  PHE B CD1 1 
ATOM   1970 C  CD2 . PHE B 1 33  ? 16.910  17.947  -16.151 1.00 48.10  ? 67  PHE B CD2 1 
ATOM   1971 C  CE1 . PHE B 1 33  ? 15.142  18.433  -14.090 1.00 46.65  ? 67  PHE B CE1 1 
ATOM   1972 C  CE2 . PHE B 1 33  ? 15.803  17.135  -15.984 1.00 55.09  ? 67  PHE B CE2 1 
ATOM   1973 C  CZ  . PHE B 1 33  ? 14.919  17.379  -14.952 1.00 50.06  ? 67  PHE B CZ  1 
ATOM   1974 N  N   . GLY B 1 34  ? 20.972  21.619  -14.658 1.00 55.03  ? 68  GLY B N   1 
ATOM   1975 C  CA  . GLY B 1 34  ? 22.106  22.280  -15.269 1.00 46.95  ? 68  GLY B CA  1 
ATOM   1976 C  C   . GLY B 1 34  ? 21.718  22.936  -16.578 1.00 51.17  ? 68  GLY B C   1 
ATOM   1977 O  O   . GLY B 1 34  ? 20.584  23.400  -16.731 1.00 52.12  ? 68  GLY B O   1 
ATOM   1978 N  N   . ALA B 1 35  ? 22.643  22.976  -17.533 1.00 54.00  ? 69  ALA B N   1 
ATOM   1979 C  CA  . ALA B 1 35  ? 22.353  23.564  -18.834 1.00 51.25  ? 69  ALA B CA  1 
ATOM   1980 C  C   . ALA B 1 35  ? 21.475  22.619  -19.646 1.00 46.12  ? 69  ALA B C   1 
ATOM   1981 O  O   . ALA B 1 35  ? 21.838  21.460  -19.869 1.00 58.12  ? 69  ALA B O   1 
ATOM   1982 C  CB  . ALA B 1 35  ? 23.650  23.868  -19.579 1.00 48.07  ? 69  ALA B CB  1 
ATOM   1983 N  N   . VAL B 1 36  ? 20.319  23.112  -20.085 1.00 43.20  ? 70  VAL B N   1 
ATOM   1984 C  CA  . VAL B 1 36  ? 19.378  22.343  -20.890 1.00 49.18  ? 70  VAL B CA  1 
ATOM   1985 C  C   . VAL B 1 36  ? 19.259  23.013  -22.251 1.00 54.30  ? 70  VAL B C   1 
ATOM   1986 O  O   . VAL B 1 36  ? 19.066  24.231  -22.333 1.00 49.97  ? 70  VAL B O   1 
ATOM   1987 C  CB  . VAL B 1 36  ? 18.002  22.235  -20.207 1.00 47.52  ? 70  VAL B CB  1 
ATOM   1988 C  CG1 . VAL B 1 36  ? 17.013  21.514  -21.110 1.00 39.18  ? 70  VAL B CG1 1 
ATOM   1989 C  CG2 . VAL B 1 36  ? 18.129  21.521  -18.870 1.00 43.96  ? 70  VAL B CG2 1 
ATOM   1990 N  N   . SER B 1 37  ? 19.375  22.219  -23.311 1.00 52.99  ? 71  SER B N   1 
ATOM   1991 C  CA  . SER B 1 37  ? 19.309  22.720  -24.676 1.00 50.67  ? 71  SER B CA  1 
ATOM   1992 C  C   . SER B 1 37  ? 17.914  22.520  -25.257 1.00 51.90  ? 71  SER B C   1 
ATOM   1993 O  O   . SER B 1 37  ? 17.212  21.562  -24.924 1.00 49.83  ? 71  SER B O   1 
ATOM   1994 C  CB  . SER B 1 37  ? 20.343  22.023  -25.563 1.00 47.11  ? 71  SER B CB  1 
ATOM   1995 O  OG  . SER B 1 37  ? 19.780  20.896  -26.211 1.00 63.64  ? 71  SER B OG  1 
ATOM   1996 N  N   . SER B 1 38  ? 17.523  23.441  -26.136 1.00 58.32  ? 72  SER B N   1 
ATOM   1997 C  CA  . SER B 1 38  ? 16.234  23.387  -26.813 1.00 51.91  ? 72  SER B CA  1 
ATOM   1998 C  C   . SER B 1 38  ? 16.437  23.747  -28.277 1.00 53.04  ? 72  SER B C   1 
ATOM   1999 O  O   . SER B 1 38  ? 17.107  24.736  -28.586 1.00 55.99  ? 72  SER B O   1 
ATOM   2000 C  CB  . SER B 1 38  ? 15.223  24.338  -26.165 1.00 52.26  ? 72  SER B CB  1 
ATOM   2001 O  OG  . SER B 1 38  ? 14.020  24.395  -26.912 1.00 59.97  ? 72  SER B OG  1 
ATOM   2002 N  N   . ASN B 1 39  ? 15.856  22.950  -29.170 1.00 49.91  ? 73  ASN B N   1 
ATOM   2003 C  CA  . ASN B 1 39  ? 16.044  23.108  -30.604 1.00 53.10  ? 73  ASN B CA  1 
ATOM   2004 C  C   . ASN B 1 39  ? 14.805  23.712  -31.252 1.00 53.87  ? 73  ASN B C   1 
ATOM   2005 O  O   . ASN B 1 39  ? 13.673  23.349  -30.918 1.00 50.44  ? 73  ASN B O   1 
ATOM   2006 C  CB  . ASN B 1 39  ? 16.359  21.765  -31.274 1.00 49.41  ? 73  ASN B CB  1 
ATOM   2007 C  CG  . ASN B 1 39  ? 17.682  21.177  -30.822 1.00 54.28  ? 73  ASN B CG  1 
ATOM   2008 O  OD1 . ASN B 1 39  ? 18.706  21.859  -30.806 1.00 55.68  ? 73  ASN B OD1 1 
ATOM   2009 N  ND2 . ASN B 1 39  ? 17.668  19.899  -30.460 1.00 58.35  ? 73  ASN B ND2 1 
ATOM   2010 N  N   . GLY B 1 40  ? 15.035  24.643  -32.178 1.00 47.38  ? 74  GLY B N   1 
ATOM   2011 C  CA  . GLY B 1 40  ? 14.003  25.121  -33.074 1.00 49.51  ? 74  GLY B CA  1 
ATOM   2012 C  C   . GLY B 1 40  ? 14.489  25.030  -34.511 1.00 53.37  ? 74  GLY B C   1 
ATOM   2013 O  O   . GLY B 1 40  ? 15.578  24.525  -34.781 1.00 56.66  ? 74  GLY B O   1 
ATOM   2014 N  N   . LEU B 1 41  ? 13.664  25.538  -35.422 1.00 53.16  ? 75  LEU B N   1 
ATOM   2015 C  CA  . LEU B 1 41  ? 13.970  25.442  -36.842 1.00 52.67  ? 75  LEU B CA  1 
ATOM   2016 C  C   . LEU B 1 41  ? 13.811  26.793  -37.526 1.00 62.23  ? 75  LEU B C   1 
ATOM   2017 O  O   . LEU B 1 41  ? 12.954  27.602  -37.159 1.00 57.77  ? 75  LEU B O   1 
ATOM   2018 C  CB  . LEU B 1 41  ? 13.083  24.401  -37.539 1.00 50.09  ? 75  LEU B CB  1 
ATOM   2019 C  CG  . LEU B 1 41  ? 13.320  22.934  -37.173 1.00 55.79  ? 75  LEU B CG  1 
ATOM   2020 C  CD1 . LEU B 1 41  ? 12.472  22.023  -38.048 1.00 47.24  ? 75  LEU B CD1 1 
ATOM   2021 C  CD2 . LEU B 1 41  ? 14.793  22.576  -37.298 1.00 63.12  ? 75  LEU B CD2 1 
ATOM   2022 N  N   . ILE B 1 42  ? 14.666  27.026  -38.520 1.00 63.40  ? 76  ILE B N   1 
ATOM   2023 C  CA  . ILE B 1 42  ? 14.612  28.206  -39.375 1.00 66.53  ? 76  ILE B CA  1 
ATOM   2024 C  C   . ILE B 1 42  ? 14.584  27.720  -40.816 1.00 63.44  ? 76  ILE B C   1 
ATOM   2025 O  O   . ILE B 1 42  ? 15.529  27.062  -41.268 1.00 66.66  ? 76  ILE B O   1 
ATOM   2026 C  CB  . ILE B 1 42  ? 15.809  29.146  -39.151 1.00 73.58  ? 76  ILE B CB  1 
ATOM   2027 C  CG1 . ILE B 1 42  ? 15.975  29.466  -37.665 1.00 68.55  ? 76  ILE B CG1 1 
ATOM   2028 C  CG2 . ILE B 1 42  ? 15.638  30.423  -39.956 1.00 73.82  ? 76  ILE B CG2 1 
ATOM   2029 C  CD1 . ILE B 1 42  ? 17.415  29.479  -37.204 1.00 72.74  ? 76  ILE B CD1 1 
ATOM   2030 N  N   . VAL B 1 43  ? 13.512  28.037  -41.535 1.00 62.96  ? 77  VAL B N   1 
ATOM   2031 C  CA  . VAL B 1 43  ? 13.351  27.574  -42.906 1.00 63.54  ? 77  VAL B CA  1 
ATOM   2032 C  C   . VAL B 1 43  ? 13.266  28.779  -43.833 1.00 66.88  ? 77  VAL B C   1 
ATOM   2033 O  O   . VAL B 1 43  ? 12.872  29.878  -43.429 1.00 70.24  ? 77  VAL B O   1 
ATOM   2034 C  CB  . VAL B 1 43  ? 12.115  26.660  -43.066 1.00 70.23  ? 77  VAL B CB  1 
ATOM   2035 C  CG1 . VAL B 1 43  ? 12.041  25.671  -41.915 1.00 61.63  ? 77  VAL B CG1 1 
ATOM   2036 C  CG2 . VAL B 1 43  ? 10.839  27.475  -43.163 1.00 71.12  ? 77  VAL B CG2 1 
ATOM   2037 N  N   . LYS B 1 44  ? 13.655  28.562  -45.088 1.00 71.80  ? 78  LYS B N   1 
ATOM   2038 C  CA  . LYS B 1 44  ? 13.694  29.608  -46.102 1.00 76.13  ? 78  LYS B CA  1 
ATOM   2039 C  C   . LYS B 1 44  ? 12.701  29.265  -47.202 1.00 80.00  ? 78  LYS B C   1 
ATOM   2040 O  O   . LYS B 1 44  ? 12.762  28.174  -47.779 1.00 82.73  ? 78  LYS B O   1 
ATOM   2041 C  CB  . LYS B 1 44  ? 15.104  29.761  -46.678 1.00 81.14  ? 78  LYS B CB  1 
ATOM   2042 C  CG  . LYS B 1 44  ? 15.245  30.887  -47.692 1.00 82.24  ? 78  LYS B CG  1 
ATOM   2043 C  CD  . LYS B 1 44  ? 16.692  31.068  -48.124 1.00 82.18  ? 78  LYS B CD  1 
ATOM   2044 C  CE  . LYS B 1 44  ? 16.953  30.419  -49.474 1.00 89.54  ? 78  LYS B CE  1 
ATOM   2045 N  NZ  . LYS B 1 44  ? 18.342  29.889  -49.581 1.00 91.04  ? 78  LYS B NZ  1 
ATOM   2046 N  N   . ASP B 1 45  ? 11.792  30.191  -47.487 1.00 76.82  ? 79  ASP B N   1 
ATOM   2047 C  CA  . ASP B 1 45  ? 10.808  30.030  -48.551 1.00 80.45  ? 79  ASP B CA  1 
ATOM   2048 C  C   . ASP B 1 45  ? 11.113  31.027  -49.665 1.00 90.58  ? 79  ASP B C   1 
ATOM   2049 O  O   . ASP B 1 45  ? 10.340  31.945  -49.947 1.00 87.81  ? 79  ASP B O   1 
ATOM   2050 C  CB  . ASP B 1 45  ? 9.391   30.212  -48.002 1.00 79.08  ? 79  ASP B CB  1 
ATOM   2051 C  CG  . ASP B 1 45  ? 8.332   29.638  -48.920 1.00 88.62  ? 79  ASP B CG  1 
ATOM   2052 O  OD1 . ASP B 1 45  ? 8.700   28.960  -49.903 1.00 89.40  ? 79  ASP B OD1 1 
ATOM   2053 O  OD2 . ASP B 1 45  ? 7.132   29.863  -48.658 1.00 89.02  ? 79  ASP B OD2 1 
ATOM   2054 N  N   . GLY B 1 46  ? 12.268  30.839  -50.297 1.00 98.89  ? 80  GLY B N   1 
ATOM   2055 C  CA  . GLY B 1 46  ? 12.670  31.685  -51.403 1.00 103.03 ? 80  GLY B CA  1 
ATOM   2056 C  C   . GLY B 1 46  ? 13.113  33.071  -50.985 1.00 104.01 ? 80  GLY B C   1 
ATOM   2057 O  O   . GLY B 1 46  ? 14.313  33.334  -50.857 1.00 101.52 ? 80  GLY B O   1 
ATOM   2058 N  N   . GLU B 1 47  ? 12.152  33.970  -50.766 1.00 111.17 ? 81  GLU B N   1 
ATOM   2059 C  CA  . GLU B 1 47  ? 12.439  35.364  -50.453 1.00 113.29 ? 81  GLU B CA  1 
ATOM   2060 C  C   . GLU B 1 47  ? 12.028  35.743  -49.033 1.00 113.44 ? 81  GLU B C   1 
ATOM   2061 O  O   . GLU B 1 47  ? 11.867  36.931  -48.736 1.00 99.79  ? 81  GLU B O   1 
ATOM   2062 C  CB  . GLU B 1 47  ? 11.752  36.283  -51.465 1.00 108.74 ? 81  GLU B CB  1 
ATOM   2063 N  N   . ARG B 1 48  ? 11.772  34.736  -48.192 1.00 100.12 ? 82  ARG B N   1 
ATOM   2064 C  CA  . ARG B 1 48  ? 11.352  34.968  -46.803 1.00 89.68  ? 82  ARG B CA  1 
ATOM   2065 C  C   . ARG B 1 48  ? 11.852  33.873  -45.880 1.00 80.47  ? 82  ARG B C   1 
ATOM   2066 O  O   . ARG B 1 48  ? 12.276  32.823  -46.339 1.00 79.38  ? 82  ARG B O   1 
ATOM   2067 C  CB  . ARG B 1 48  ? 9.837   35.061  -46.690 1.00 79.43  ? 82  ARG B CB  1 
ATOM   2068 C  CG  . ARG B 1 48  ? 9.103   33.785  -47.032 1.00 79.12  ? 82  ARG B CG  1 
ATOM   2069 C  CD  . ARG B 1 48  ? 7.636   33.906  -46.673 1.00 72.31  ? 82  ARG B CD  1 
ATOM   2070 N  NE  . ARG B 1 48  ? 6.918   32.678  -46.973 1.00 80.79  ? 82  ARG B NE  1 
ATOM   2071 C  CZ  . ARG B 1 48  ? 5.642   32.470  -46.683 1.00 86.18  ? 82  ARG B CZ  1 
ATOM   2072 N  NH1 . ARG B 1 48  ? 4.933   33.409  -46.077 1.00 87.94  ? 82  ARG B NH1 1 
ATOM   2073 N  NH2 . ARG B 1 48  ? 5.077   31.317  -47.000 1.00 86.86  ? 82  ARG B NH2 1 
ATOM   2074 N  N   . VAL B 1 49  ? 11.813  34.122  -44.577 1.00 79.89  ? 83  VAL B N   1 
ATOM   2075 C  CA  . VAL B 1 49  ? 12.285  33.148  -43.599 1.00 68.88  ? 83  VAL B CA  1 
ATOM   2076 C  C   . VAL B 1 49  ? 11.240  32.865  -42.561 1.00 65.90  ? 83  VAL B C   1 
ATOM   2077 O  O   . VAL B 1 49  ? 10.617  33.770  -42.035 1.00 69.81  ? 83  VAL B O   1 
ATOM   2078 C  CB  . VAL B 1 49  ? 13.545  33.636  -42.896 1.00 81.60  ? 83  VAL B CB  1 
ATOM   2079 C  CG1 . VAL B 1 49  ? 13.804  32.832  -41.635 1.00 77.90  ? 83  VAL B CG1 1 
ATOM   2080 C  CG2 . VAL B 1 49  ? 14.735  33.576  -43.837 1.00 83.83  ? 83  VAL B CG2 1 
ATOM   2081 N  N   . LEU B 1 50  ? 11.039  31.593  -42.277 1.00 63.87  ? 84  LEU B N   1 
ATOM   2082 C  CA  . LEU B 1 50  ? 10.034  31.207  -41.319 1.00 63.29  ? 84  LEU B CA  1 
ATOM   2083 C  C   . LEU B 1 50  ? 10.671  30.607  -40.078 1.00 66.82  ? 84  LEU B C   1 
ATOM   2084 O  O   . LEU B 1 50  ? 11.678  29.919  -40.166 1.00 70.73  ? 84  LEU B O   1 
ATOM   2085 C  CB  . LEU B 1 50  ? 9.064   30.233  -41.968 1.00 59.31  ? 84  LEU B CB  1 
ATOM   2086 C  CG  . LEU B 1 50  ? 8.395   30.659  -43.280 1.00 71.03  ? 84  LEU B CG  1 
ATOM   2087 C  CD1 . LEU B 1 50  ? 9.358   30.561  -44.451 1.00 70.16  ? 84  LEU B CD1 1 
ATOM   2088 C  CD2 . LEU B 1 50  ? 7.174   29.802  -43.556 1.00 73.62  ? 84  LEU B CD2 1 
ATOM   2089 N  N   . LEU B 1 51  ? 10.101  30.888  -38.918 1.00 63.20  ? 85  LEU B N   1 
ATOM   2090 C  CA  . LEU B 1 51  ? 10.664  30.400  -37.671 1.00 64.34  ? 85  LEU B CA  1 
ATOM   2091 C  C   . LEU B 1 51  ? 9.732   29.423  -36.999 1.00 63.07  ? 85  LEU B C   1 
ATOM   2092 O  O   . LEU B 1 51  ? 8.557   29.707  -36.820 1.00 61.14  ? 85  LEU B O   1 
ATOM   2093 C  CB  . LEU B 1 51  ? 10.965  31.568  -36.737 1.00 64.86  ? 85  LEU B CB  1 
ATOM   2094 C  CG  . LEU B 1 51  ? 11.881  31.272  -35.557 1.00 69.81  ? 85  LEU B CG  1 
ATOM   2095 C  CD1 . LEU B 1 51  ? 13.249  30.867  -36.074 1.00 75.98  ? 85  LEU B CD1 1 
ATOM   2096 C  CD2 . LEU B 1 51  ? 11.989  32.487  -34.653 1.00 74.24  ? 85  LEU B CD2 1 
ATOM   2097 N  N   . VAL B 1 52  ? 10.260  28.266  -36.618 1.00 65.77  ? 86  VAL B N   1 
ATOM   2098 C  CA  . VAL B 1 52  ? 9.412   27.235  -36.044 1.00 67.27  ? 86  VAL B CA  1 
ATOM   2099 C  C   . VAL B 1 52  ? 9.394   27.300  -34.543 1.00 72.60  ? 86  VAL B C   1 
ATOM   2100 O  O   . VAL B 1 52  ? 8.487   26.778  -33.926 1.00 87.01  ? 86  VAL B O   1 
ATOM   2101 C  CB  . VAL B 1 52  ? 9.814   25.833  -36.517 1.00 64.84  ? 86  VAL B CB  1 
ATOM   2102 C  CG1 . VAL B 1 52  ? 8.967   24.766  -35.845 1.00 56.48  ? 86  VAL B CG1 1 
ATOM   2103 C  CG2 . VAL B 1 52  ? 9.688   25.738  -38.027 1.00 65.61  ? 86  VAL B CG2 1 
ATOM   2104 N  N   . ASP B 1 53  ? 10.369  27.930  -33.931 1.00 51.43  ? 87  ASP B N   1 
ATOM   2105 C  CA  . ASP B 1 53  ? 10.264  28.116  -32.491 1.00 60.53  ? 87  ASP B CA  1 
ATOM   2106 C  C   . ASP B 1 53  ? 11.150  29.229  -31.976 1.00 63.04  ? 87  ASP B C   1 
ATOM   2107 O  O   . ASP B 1 53  ? 12.064  29.655  -32.662 1.00 57.72  ? 87  ASP B O   1 
ATOM   2108 C  CB  . ASP B 1 53  ? 10.565  26.810  -31.745 1.00 64.62  ? 87  ASP B CB  1 
ATOM   2109 C  CG  . ASP B 1 53  ? 9.318   26.081  -31.309 1.00 65.22  ? 87  ASP B CG  1 
ATOM   2110 O  OD1 . ASP B 1 53  ? 8.256   26.716  -31.195 1.00 64.32  ? 87  ASP B OD1 1 
ATOM   2111 O  OD2 . ASP B 1 53  ? 9.403   24.864  -31.074 1.00 65.72  ? 87  ASP B OD2 1 
ATOM   2112 N  N   . THR B 1 54  ? 10.872  29.711  -30.778 1.00 51.03  ? 88  THR B N   1 
ATOM   2113 C  CA  . THR B 1 54  ? 11.719  30.715  -30.160 1.00 57.45  ? 88  THR B CA  1 
ATOM   2114 C  C   . THR B 1 54  ? 12.716  30.033  -29.226 1.00 66.22  ? 88  THR B C   1 
ATOM   2115 O  O   . THR B 1 54  ? 12.768  28.805  -29.116 1.00 61.17  ? 88  THR B O   1 
ATOM   2116 C  CB  . THR B 1 54  ? 10.883  31.744  -29.400 1.00 58.67  ? 88  THR B CB  1 
ATOM   2117 O  OG1 . THR B 1 54  ? 10.461  31.191  -28.147 1.00 63.60  ? 88  THR B OG1 1 
ATOM   2118 C  CG2 . THR B 1 54  ? 9.655   32.131  -30.206 1.00 65.02  ? 88  THR B CG2 1 
ATOM   2119 N  N   . ALA B 1 55  ? 13.515  30.838  -28.539 1.00 64.08  ? 89  ALA B N   1 
ATOM   2120 C  CA  . ALA B 1 55  ? 14.479  30.340  -27.576 1.00 58.09  ? 89  ALA B CA  1 
ATOM   2121 C  C   . ALA B 1 55  ? 13.901  30.458  -26.167 1.00 57.36  ? 89  ALA B C   1 
ATOM   2122 O  O   . ALA B 1 55  ? 12.715  30.745  -25.979 1.00 63.08  ? 89  ALA B O   1 
ATOM   2123 C  CB  . ALA B 1 55  ? 15.800  31.094  -27.725 1.00 64.73  ? 89  ALA B CB  1 
ATOM   2124 N  N   . TRP B 1 56  ? 14.747  30.235  -25.158 1.00 64.63  ? 90  TRP B N   1 
ATOM   2125 C  CA  . TRP B 1 56  ? 14.278  30.310  -23.778 1.00 56.48  ? 90  TRP B CA  1 
ATOM   2126 C  C   . TRP B 1 56  ? 13.942  31.743  -23.378 1.00 64.64  ? 90  TRP B C   1 
ATOM   2127 O  O   . TRP B 1 56  ? 12.984  31.975  -22.632 1.00 67.14  ? 90  TRP B O   1 
ATOM   2128 C  CB  . TRP B 1 56  ? 15.328  29.735  -22.826 1.00 53.46  ? 90  TRP B CB  1 
ATOM   2129 C  CG  . TRP B 1 56  ? 15.641  28.282  -23.028 1.00 56.18  ? 90  TRP B CG  1 
ATOM   2130 C  CD1 . TRP B 1 56  ? 16.509  27.750  -23.933 1.00 56.44  ? 90  TRP B CD1 1 
ATOM   2131 C  CD2 . TRP B 1 56  ? 15.106  27.175  -22.289 1.00 55.89  ? 90  TRP B CD2 1 
ATOM   2132 N  NE1 . TRP B 1 56  ? 16.542  26.382  -23.813 1.00 53.31  ? 90  TRP B NE1 1 
ATOM   2133 C  CE2 . TRP B 1 56  ? 15.692  26.004  -22.808 1.00 55.25  ? 90  TRP B CE2 1 
ATOM   2134 C  CE3 . TRP B 1 56  ? 14.191  27.062  -21.238 1.00 55.07  ? 90  TRP B CE3 1 
ATOM   2135 C  CZ2 . TRP B 1 56  ? 15.388  24.736  -22.318 1.00 56.13  ? 90  TRP B CZ2 1 
ATOM   2136 C  CZ3 . TRP B 1 56  ? 13.891  25.802  -20.752 1.00 54.32  ? 90  TRP B CZ3 1 
ATOM   2137 C  CH2 . TRP B 1 56  ? 14.487  24.656  -21.291 1.00 52.53  ? 90  TRP B CH2 1 
ATOM   2138 N  N   . THR B 1 57  ? 14.722  32.714  -23.850 1.00 69.18  ? 91  THR B N   1 
ATOM   2139 C  CA  . THR B 1 57  ? 14.602  34.097  -23.410 1.00 65.58  ? 91  THR B CA  1 
ATOM   2140 C  C   . THR B 1 57  ? 14.415  35.020  -24.607 1.00 63.78  ? 91  THR B C   1 
ATOM   2141 O  O   . THR B 1 57  ? 14.560  34.620  -25.766 1.00 61.78  ? 91  THR B O   1 
ATOM   2142 C  CB  . THR B 1 57  ? 15.834  34.544  -22.607 1.00 67.51  ? 91  THR B CB  1 
ATOM   2143 O  OG1 . THR B 1 57  ? 16.858  34.984  -23.506 1.00 69.46  ? 91  THR B OG1 1 
ATOM   2144 C  CG2 . THR B 1 57  ? 16.374  33.400  -21.760 1.00 60.63  ? 91  THR B CG2 1 
ATOM   2145 N  N   . ASP B 1 58  ? 14.090  36.281  -24.304 1.00 69.02  ? 92  ASP B N   1 
ATOM   2146 C  CA  . ASP B 1 58  ? 14.007  37.301  -25.344 1.00 72.16  ? 92  ASP B CA  1 
ATOM   2147 C  C   . ASP B 1 58  ? 15.383  37.611  -25.922 1.00 67.27  ? 92  ASP B C   1 
ATOM   2148 O  O   . ASP B 1 58  ? 15.522  37.819  -27.133 1.00 69.72  ? 92  ASP B O   1 
ATOM   2149 C  CB  . ASP B 1 58  ? 13.373  38.575  -24.782 1.00 74.15  ? 92  ASP B CB  1 
ATOM   2150 C  CG  . ASP B 1 58  ? 11.876  38.448  -24.582 1.00 74.75  ? 92  ASP B CG  1 
ATOM   2151 O  OD1 . ASP B 1 58  ? 11.198  37.890  -25.469 1.00 63.44  ? 92  ASP B OD1 1 
ATOM   2152 O  OD2 . ASP B 1 58  ? 11.377  38.910  -23.534 1.00 74.69  ? 92  ASP B OD2 1 
ATOM   2153 N  N   . ASP B 1 59  ? 16.410  37.647  -25.068 1.00 68.70  ? 93  ASP B N   1 
ATOM   2154 C  CA  . ASP B 1 59  ? 17.753  37.977  -25.532 1.00 73.77  ? 93  ASP B CA  1 
ATOM   2155 C  C   . ASP B 1 59  ? 18.302  36.918  -26.479 1.00 74.20  ? 93  ASP B C   1 
ATOM   2156 O  O   . ASP B 1 59  ? 19.076  37.243  -27.386 1.00 77.90  ? 93  ASP B O   1 
ATOM   2157 C  CB  . ASP B 1 59  ? 18.690  38.159  -24.338 1.00 78.94  ? 93  ASP B CB  1 
ATOM   2158 C  CG  . ASP B 1 59  ? 19.832  39.110  -24.633 1.00 86.48  ? 93  ASP B CG  1 
ATOM   2159 O  OD1 . ASP B 1 59  ? 20.718  38.747  -25.436 1.00 84.01  ? 93  ASP B OD1 1 
ATOM   2160 O  OD2 . ASP B 1 59  ? 19.844  40.221  -24.063 1.00 87.17  ? 93  ASP B OD2 1 
ATOM   2161 N  N   . GLN B 1 60  ? 17.923  35.653  -26.287 1.00 67.22  ? 94  GLN B N   1 
ATOM   2162 C  CA  . GLN B 1 60  ? 18.361  34.607  -27.202 1.00 57.94  ? 94  GLN B CA  1 
ATOM   2163 C  C   . GLN B 1 60  ? 17.523  34.579  -28.473 1.00 62.21  ? 94  GLN B C   1 
ATOM   2164 O  O   . GLN B 1 60  ? 18.051  34.276  -29.549 1.00 57.88  ? 94  GLN B O   1 
ATOM   2165 C  CB  . GLN B 1 60  ? 18.314  33.245  -26.509 1.00 59.01  ? 94  GLN B CB  1 
ATOM   2166 C  CG  . GLN B 1 60  ? 18.967  33.219  -25.139 1.00 66.65  ? 94  GLN B CG  1 
ATOM   2167 C  CD  . GLN B 1 60  ? 18.799  31.883  -24.442 1.00 61.43  ? 94  GLN B CD  1 
ATOM   2168 O  OE1 . GLN B 1 60  ? 17.840  31.154  -24.694 1.00 63.19  ? 94  GLN B OE1 1 
ATOM   2169 N  NE2 . GLN B 1 60  ? 19.732  31.556  -23.555 1.00 59.40  ? 94  GLN B NE2 1 
ATOM   2170 N  N   . THR B 1 61  ? 16.227  34.885  -28.373 1.00 68.43  ? 95  THR B N   1 
ATOM   2171 C  CA  . THR B 1 61  ? 15.397  34.973  -29.569 1.00 65.01  ? 95  THR B CA  1 
ATOM   2172 C  C   . THR B 1 61  ? 15.820  36.147  -30.442 1.00 65.42  ? 95  THR B C   1 
ATOM   2173 O  O   . THR B 1 61  ? 15.851  36.035  -31.673 1.00 68.64  ? 95  THR B O   1 
ATOM   2174 C  CB  . THR B 1 61  ? 13.923  35.092  -29.181 1.00 63.45  ? 95  THR B CB  1 
ATOM   2175 O  OG1 . THR B 1 61  ? 13.552  33.968  -28.374 1.00 65.65  ? 95  THR B OG1 1 
ATOM   2176 C  CG2 . THR B 1 61  ? 13.043  35.130  -30.422 1.00 55.46  ? 95  THR B CG2 1 
ATOM   2177 N  N   . SER B 1 62  ? 16.153  37.282  -29.823 1.00 74.75  ? 96  SER B N   1 
ATOM   2178 C  CA  . SER B 1 62  ? 16.729  38.389  -30.578 1.00 71.75  ? 96  SER B CA  1 
ATOM   2179 C  C   . SER B 1 62  ? 18.088  38.014  -31.151 1.00 64.75  ? 96  SER B C   1 
ATOM   2180 O  O   . SER B 1 62  ? 18.470  38.506  -32.219 1.00 73.68  ? 96  SER B O   1 
ATOM   2181 C  CB  . SER B 1 62  ? 16.845  39.628  -29.691 1.00 61.99  ? 96  SER B CB  1 
ATOM   2182 O  OG  . SER B 1 62  ? 17.982  40.399  -30.039 1.00 86.53  ? 96  SER B OG  1 
ATOM   2183 N  N   . GLN B 1 63  ? 18.831  37.148  -30.457 1.00 70.38  ? 97  GLN B N   1 
ATOM   2184 C  CA  . GLN B 1 63  ? 20.082  36.637  -31.003 1.00 69.60  ? 97  GLN B CA  1 
ATOM   2185 C  C   . GLN B 1 63  ? 19.840  35.767  -32.230 1.00 75.13  ? 97  GLN B C   1 
ATOM   2186 O  O   . GLN B 1 63  ? 20.701  35.690  -33.114 1.00 74.78  ? 97  GLN B O   1 
ATOM   2187 C  CB  . GLN B 1 63  ? 20.836  35.848  -29.933 1.00 67.69  ? 97  GLN B CB  1 
ATOM   2188 C  CG  . GLN B 1 63  ? 21.837  36.660  -29.133 1.00 57.23  ? 97  GLN B CG  1 
ATOM   2189 C  CD  . GLN B 1 63  ? 22.834  35.783  -28.402 1.00 76.96  ? 97  GLN B CD  1 
ATOM   2190 O  OE1 . GLN B 1 63  ? 23.603  35.049  -29.022 1.00 81.83  ? 97  GLN B OE1 1 
ATOM   2191 N  NE2 . GLN B 1 63  ? 22.821  35.851  -27.076 1.00 73.19  ? 97  GLN B NE2 1 
ATOM   2192 N  N   . ILE B 1 64  ? 18.683  35.104  -32.298 1.00 72.61  ? 98  ILE B N   1 
ATOM   2193 C  CA  . ILE B 1 64  ? 18.341  34.318  -33.479 1.00 68.34  ? 98  ILE B CA  1 
ATOM   2194 C  C   . ILE B 1 64  ? 18.101  35.235  -34.672 1.00 74.88  ? 98  ILE B C   1 
ATOM   2195 O  O   . ILE B 1 64  ? 18.597  34.987  -35.778 1.00 73.25  ? 98  ILE B O   1 
ATOM   2196 C  CB  . ILE B 1 64  ? 17.117  33.428  -33.196 1.00 58.96  ? 98  ILE B CB  1 
ATOM   2197 C  CG1 . ILE B 1 64  ? 17.518  32.210  -32.362 1.00 63.45  ? 98  ILE B CG1 1 
ATOM   2198 C  CG2 . ILE B 1 64  ? 16.460  32.985  -34.493 1.00 61.91  ? 98  ILE B CG2 1 
ATOM   2199 C  CD1 . ILE B 1 64  ? 16.425  31.713  -31.441 1.00 61.30  ? 98  ILE B CD1 1 
ATOM   2200 N  N   . LEU B 1 65  ? 17.340  36.313  -34.462 1.00 72.98  ? 99  LEU B N   1 
ATOM   2201 C  CA  . LEU B 1 65  ? 17.066  37.252  -35.545 1.00 74.55  ? 99  LEU B CA  1 
ATOM   2202 C  C   . LEU B 1 65  ? 18.341  37.914  -36.050 1.00 79.88  ? 99  LEU B C   1 
ATOM   2203 O  O   . LEU B 1 65  ? 18.441  38.242  -37.238 1.00 84.59  ? 99  LEU B O   1 
ATOM   2204 C  CB  . LEU B 1 65  ? 16.062  38.308  -35.081 1.00 68.24  ? 99  LEU B CB  1 
ATOM   2205 C  CG  . LEU B 1 65  ? 14.714  37.785  -34.578 1.00 73.75  ? 99  LEU B CG  1 
ATOM   2206 C  CD1 . LEU B 1 65  ? 13.869  38.918  -34.018 1.00 75.20  ? 99  LEU B CD1 1 
ATOM   2207 C  CD2 . LEU B 1 65  ? 13.971  37.055  -35.686 1.00 68.90  ? 99  LEU B CD2 1 
ATOM   2208 N  N   . ASN B 1 66  ? 19.322  38.119  -35.168 1.00 77.72  ? 100 ASN B N   1 
ATOM   2209 C  CA  . ASN B 1 66  ? 20.605  38.657  -35.606 1.00 76.21  ? 100 ASN B CA  1 
ATOM   2210 C  C   . ASN B 1 66  ? 21.351  37.668  -36.492 1.00 76.80  ? 100 ASN B C   1 
ATOM   2211 O  O   . ASN B 1 66  ? 22.072  38.079  -37.408 1.00 80.24  ? 100 ASN B O   1 
ATOM   2212 C  CB  . ASN B 1 66  ? 21.461  39.031  -34.395 1.00 79.36  ? 100 ASN B CB  1 
ATOM   2213 C  CG  . ASN B 1 66  ? 21.011  40.321  -33.740 1.00 74.03  ? 100 ASN B CG  1 
ATOM   2214 O  OD1 . ASN B 1 66  ? 20.211  41.069  -34.300 1.00 75.66  ? 100 ASN B OD1 1 
ATOM   2215 N  ND2 . ASN B 1 66  ? 21.525  40.588  -32.544 1.00 75.54  ? 100 ASN B ND2 1 
ATOM   2216 N  N   . TRP B 1 67  ? 21.187  36.368  -36.239 1.00 76.32  ? 101 TRP B N   1 
ATOM   2217 C  CA  . TRP B 1 67  ? 21.866  35.361  -37.049 1.00 79.73  ? 101 TRP B CA  1 
ATOM   2218 C  C   . TRP B 1 67  ? 21.276  35.296  -38.452 1.00 80.56  ? 101 TRP B C   1 
ATOM   2219 O  O   . TRP B 1 67  ? 22.012  35.258  -39.445 1.00 81.35  ? 101 TRP B O   1 
ATOM   2220 C  CB  . TRP B 1 67  ? 21.782  33.998  -36.363 1.00 79.83  ? 101 TRP B CB  1 
ATOM   2221 C  CG  . TRP B 1 67  ? 22.516  32.914  -37.089 1.00 76.85  ? 101 TRP B CG  1 
ATOM   2222 C  CD1 . TRP B 1 67  ? 23.822  32.557  -36.924 1.00 72.16  ? 101 TRP B CD1 1 
ATOM   2223 C  CD2 . TRP B 1 67  ? 21.985  32.042  -38.094 1.00 72.46  ? 101 TRP B CD2 1 
ATOM   2224 N  NE1 . TRP B 1 67  ? 24.139  31.518  -37.766 1.00 76.26  ? 101 TRP B NE1 1 
ATOM   2225 C  CE2 . TRP B 1 67  ? 23.028  31.183  -38.495 1.00 77.71  ? 101 TRP B CE2 1 
ATOM   2226 C  CE3 . TRP B 1 67  ? 20.730  31.905  -38.695 1.00 72.96  ? 101 TRP B CE3 1 
ATOM   2227 C  CZ2 . TRP B 1 67  ? 22.854  30.201  -39.468 1.00 76.95  ? 101 TRP B CZ2 1 
ATOM   2228 C  CZ3 . TRP B 1 67  ? 20.559  30.930  -39.661 1.00 75.11  ? 101 TRP B CZ3 1 
ATOM   2229 C  CH2 . TRP B 1 67  ? 21.616  30.091  -40.038 1.00 69.77  ? 101 TRP B CH2 1 
ATOM   2230 N  N   . ILE B 1 68  ? 19.944  35.276  -38.552 1.00 82.18  ? 102 ILE B N   1 
ATOM   2231 C  CA  . ILE B 1 68  ? 19.297  35.253  -39.861 1.00 81.23  ? 102 ILE B CA  1 
ATOM   2232 C  C   . ILE B 1 68  ? 19.621  36.523  -40.636 1.00 81.71  ? 102 ILE B C   1 
ATOM   2233 O  O   . ILE B 1 68  ? 19.807  36.493  -41.859 1.00 89.51  ? 102 ILE B O   1 
ATOM   2234 C  CB  . ILE B 1 68  ? 17.777  35.057  -39.703 1.00 76.46  ? 102 ILE B CB  1 
ATOM   2235 C  CG1 . ILE B 1 68  ? 17.479  33.794  -38.892 1.00 70.54  ? 102 ILE B CG1 1 
ATOM   2236 C  CG2 . ILE B 1 68  ? 17.099  34.985  -41.061 1.00 80.63  ? 102 ILE B CG2 1 
ATOM   2237 C  CD1 . ILE B 1 68  ? 16.258  33.915  -38.010 1.00 65.16  ? 102 ILE B CD1 1 
ATOM   2238 N  N   . LYS B 1 69  ? 19.701  37.657  -39.937 1.00 80.28  ? 103 LYS B N   1 
ATOM   2239 C  CA  . LYS B 1 69  ? 20.043  38.913  -40.596 1.00 84.99  ? 103 LYS B CA  1 
ATOM   2240 C  C   . LYS B 1 69  ? 21.456  38.882  -41.162 1.00 86.50  ? 103 LYS B C   1 
ATOM   2241 O  O   . LYS B 1 69  ? 21.728  39.514  -42.190 1.00 92.71  ? 103 LYS B O   1 
ATOM   2242 C  CB  . LYS B 1 69  ? 19.883  40.075  -39.612 1.00 77.52  ? 103 LYS B CB  1 
ATOM   2243 C  CG  . LYS B 1 69  ? 20.233  41.441  -40.181 1.00 88.10  ? 103 LYS B CG  1 
ATOM   2244 C  CD  . LYS B 1 69  ? 20.043  42.535  -39.142 1.00 82.15  ? 103 LYS B CD  1 
ATOM   2245 C  CE  . LYS B 1 69  ? 21.330  43.312  -38.916 1.00 90.12  ? 103 LYS B CE  1 
ATOM   2246 N  NZ  . LYS B 1 69  ? 21.376  44.562  -39.724 1.00 83.16  ? 103 LYS B NZ  1 
ATOM   2247 N  N   . GLN B 1 70  ? 22.363  38.145  -40.521 1.00 90.67  ? 104 GLN B N   1 
ATOM   2248 C  CA  . GLN B 1 70  ? 23.753  38.087  -40.956 1.00 85.01  ? 104 GLN B CA  1 
ATOM   2249 C  C   . GLN B 1 70  ? 23.998  36.999  -41.995 1.00 86.05  ? 104 GLN B C   1 
ATOM   2250 O  O   . GLN B 1 70  ? 24.733  37.223  -42.963 1.00 88.30  ? 104 GLN B O   1 
ATOM   2251 C  CB  . GLN B 1 70  ? 24.669  37.871  -39.747 1.00 94.67  ? 104 GLN B CB  1 
ATOM   2252 C  CG  . GLN B 1 70  ? 26.045  37.319  -40.088 1.00 99.35  ? 104 GLN B CG  1 
ATOM   2253 C  CD  . GLN B 1 70  ? 26.903  37.087  -38.859 1.00 111.86 ? 104 GLN B CD  1 
ATOM   2254 O  OE1 . GLN B 1 70  ? 27.579  36.064  -38.744 1.00 109.98 ? 104 GLN B OE1 1 
ATOM   2255 N  NE2 . GLN B 1 70  ? 26.880  38.039  -37.933 1.00 112.19 ? 104 GLN B NE2 1 
ATOM   2256 N  N   . GLU B 1 71  ? 23.389  35.826  -41.825 1.00 82.47  ? 105 GLU B N   1 
ATOM   2257 C  CA  . GLU B 1 71  ? 23.672  34.684  -42.686 1.00 79.19  ? 105 GLU B CA  1 
ATOM   2258 C  C   . GLU B 1 71  ? 22.672  34.505  -43.820 1.00 83.76  ? 105 GLU B C   1 
ATOM   2259 O  O   . GLU B 1 71  ? 23.047  33.998  -44.882 1.00 79.95  ? 105 GLU B O   1 
ATOM   2260 C  CB  . GLU B 1 71  ? 23.726  33.397  -41.856 1.00 83.79  ? 105 GLU B CB  1 
ATOM   2261 C  CG  . GLU B 1 71  ? 24.861  33.365  -40.845 1.00 86.50  ? 105 GLU B CG  1 
ATOM   2262 C  CD  . GLU B 1 71  ? 26.149  32.819  -41.431 1.00 93.97  ? 105 GLU B CD  1 
ATOM   2263 O  OE1 . GLU B 1 71  ? 27.210  32.976  -40.789 1.00 97.63  ? 105 GLU B OE1 1 
ATOM   2264 O  OE2 . GLU B 1 71  ? 26.102  32.233  -42.533 1.00 90.69  ? 105 GLU B OE2 1 
ATOM   2265 N  N   . ILE B 1 72  ? 21.415  34.901  -43.630 1.00 83.68  ? 106 ILE B N   1 
ATOM   2266 C  CA  . ILE B 1 72  ? 20.388  34.752  -44.650 1.00 80.89  ? 106 ILE B CA  1 
ATOM   2267 C  C   . ILE B 1 72  ? 19.992  36.095  -45.251 1.00 91.05  ? 106 ILE B C   1 
ATOM   2268 O  O   . ILE B 1 72  ? 19.763  36.192  -46.460 1.00 88.55  ? 106 ILE B O   1 
ATOM   2269 C  CB  . ILE B 1 72  ? 19.153  34.016  -44.084 1.00 92.26  ? 106 ILE B CB  1 
ATOM   2270 C  CG1 . ILE B 1 72  ? 19.570  32.694  -43.437 1.00 83.42  ? 106 ILE B CG1 1 
ATOM   2271 C  CG2 . ILE B 1 72  ? 18.133  33.763  -45.183 1.00 90.88  ? 106 ILE B CG2 1 
ATOM   2272 C  CD1 . ILE B 1 72  ? 18.420  31.927  -42.818 1.00 66.12  ? 106 ILE B CD1 1 
ATOM   2273 N  N   . ASN B 1 73  ? 19.905  37.140  -44.424 1.00 103.86 ? 107 ASN B N   1 
ATOM   2274 C  CA  . ASN B 1 73  ? 19.557  38.491  -44.873 1.00 111.66 ? 107 ASN B CA  1 
ATOM   2275 C  C   . ASN B 1 73  ? 18.176  38.527  -45.527 1.00 99.91  ? 107 ASN B C   1 
ATOM   2276 O  O   . ASN B 1 73  ? 17.943  39.258  -46.491 1.00 101.62 ? 107 ASN B O   1 
ATOM   2277 C  CB  . ASN B 1 73  ? 20.621  39.058  -45.816 1.00 97.32  ? 107 ASN B CB  1 
ATOM   2278 N  N   . LEU B 1 74  ? 17.252  37.730  -44.995 1.00 92.28  ? 108 LEU B N   1 
ATOM   2279 C  CA  . LEU B 1 74  ? 15.866  37.729  -45.431 1.00 86.04  ? 108 LEU B CA  1 
ATOM   2280 C  C   . LEU B 1 74  ? 14.949  38.008  -44.246 1.00 86.20  ? 108 LEU B C   1 
ATOM   2281 O  O   . LEU B 1 74  ? 15.239  37.589  -43.121 1.00 85.93  ? 108 LEU B O   1 
ATOM   2282 C  CB  . LEU B 1 74  ? 15.480  36.389  -46.073 1.00 92.20  ? 108 LEU B CB  1 
ATOM   2283 C  CG  . LEU B 1 74  ? 15.886  36.189  -47.535 1.00 89.08  ? 108 LEU B CG  1 
ATOM   2284 C  CD1 . LEU B 1 74  ? 15.539  34.783  -48.004 1.00 87.25  ? 108 LEU B CD1 1 
ATOM   2285 C  CD2 . LEU B 1 74  ? 15.226  37.232  -48.421 1.00 85.20  ? 108 LEU B CD2 1 
ATOM   2286 N  N   . PRO B 1 75  ? 13.841  38.715  -44.462 1.00 81.21  ? 109 PRO B N   1 
ATOM   2287 C  CA  . PRO B 1 75  ? 12.950  39.036  -43.342 1.00 68.60  ? 109 PRO B CA  1 
ATOM   2288 C  C   . PRO B 1 75  ? 12.255  37.794  -42.805 1.00 75.92  ? 109 PRO B C   1 
ATOM   2289 O  O   . PRO B 1 75  ? 12.043  36.809  -43.518 1.00 77.43  ? 109 PRO B O   1 
ATOM   2290 C  CB  . PRO B 1 75  ? 11.938  40.014  -43.949 1.00 72.71  ? 109 PRO B CB  1 
ATOM   2291 C  CG  . PRO B 1 75  ? 12.020  39.827  -45.417 1.00 71.13  ? 109 PRO B CG  1 
ATOM   2292 C  CD  . PRO B 1 75  ? 13.360  39.249  -45.748 1.00 71.07  ? 109 PRO B CD  1 
ATOM   2293 N  N   . VAL B 1 76  ? 11.905  37.851  -41.523 1.00 77.59  ? 110 VAL B N   1 
ATOM   2294 C  CA  . VAL B 1 76  ? 11.171  36.777  -40.863 1.00 65.75  ? 110 VAL B CA  1 
ATOM   2295 C  C   . VAL B 1 76  ? 9.685   37.049  -41.067 1.00 70.55  ? 110 VAL B C   1 
ATOM   2296 O  O   . VAL B 1 76  ? 9.110   37.932  -40.425 1.00 79.43  ? 110 VAL B O   1 
ATOM   2297 C  CB  . VAL B 1 76  ? 11.525  36.681  -39.375 1.00 66.21  ? 110 VAL B CB  1 
ATOM   2298 C  CG1 . VAL B 1 76  ? 10.621  35.677  -38.679 1.00 54.76  ? 110 VAL B CG1 1 
ATOM   2299 C  CG2 . VAL B 1 76  ? 12.990  36.307  -39.200 1.00 73.46  ? 110 VAL B CG2 1 
ATOM   2300 N  N   . ALA B 1 77  ? 9.059   36.284  -41.964 1.00 71.71  ? 111 ALA B N   1 
ATOM   2301 C  CA  . ALA B 1 77  ? 7.679   36.556  -42.348 1.00 69.56  ? 111 ALA B CA  1 
ATOM   2302 C  C   . ALA B 1 77  ? 6.677   36.124  -41.285 1.00 75.59  ? 111 ALA B C   1 
ATOM   2303 O  O   . ALA B 1 77  ? 5.639   36.774  -41.122 1.00 72.62  ? 111 ALA B O   1 
ATOM   2304 C  CB  . ALA B 1 77  ? 7.357   35.869  -43.674 1.00 65.50  ? 111 ALA B CB  1 
ATOM   2305 N  N   . LEU B 1 78  ? 6.954   35.039  -40.567 1.00 72.20  ? 112 LEU B N   1 
ATOM   2306 C  CA  . LEU B 1 78  ? 6.028   34.545  -39.557 1.00 70.26  ? 112 LEU B CA  1 
ATOM   2307 C  C   . LEU B 1 78  ? 6.796   33.692  -38.560 1.00 65.98  ? 112 LEU B C   1 
ATOM   2308 O  O   . LEU B 1 78  ? 7.981   33.400  -38.740 1.00 67.38  ? 112 LEU B O   1 
ATOM   2309 C  CB  . LEU B 1 78  ? 4.879   33.751  -40.191 1.00 70.68  ? 112 LEU B CB  1 
ATOM   2310 C  CG  . LEU B 1 78  ? 5.183   32.334  -40.684 1.00 70.08  ? 112 LEU B CG  1 
ATOM   2311 C  CD1 . LEU B 1 78  ? 4.696   31.277  -39.699 1.00 69.47  ? 112 LEU B CD1 1 
ATOM   2312 C  CD2 . LEU B 1 78  ? 4.562   32.116  -42.053 1.00 75.46  ? 112 LEU B CD2 1 
ATOM   2313 N  N   . ALA B 1 79  ? 6.097   33.295  -37.500 1.00 60.12  ? 113 ALA B N   1 
ATOM   2314 C  CA  . ALA B 1 79  ? 6.663   32.427  -36.479 1.00 62.34  ? 113 ALA B CA  1 
ATOM   2315 C  C   . ALA B 1 79  ? 5.538   31.628  -35.841 1.00 67.47  ? 113 ALA B C   1 
ATOM   2316 O  O   . ALA B 1 79  ? 4.515   32.197  -35.452 1.00 72.68  ? 113 ALA B O   1 
ATOM   2317 C  CB  . ALA B 1 79  ? 7.415   33.233  -35.415 1.00 56.31  ? 113 ALA B CB  1 
ATOM   2318 N  N   . VAL B 1 80  ? 5.724   30.316  -35.750 1.00 56.36  ? 114 VAL B N   1 
ATOM   2319 C  CA  . VAL B 1 80  ? 4.784   29.427  -35.081 1.00 62.56  ? 114 VAL B CA  1 
ATOM   2320 C  C   . VAL B 1 80  ? 5.510   28.771  -33.915 1.00 61.11  ? 114 VAL B C   1 
ATOM   2321 O  O   . VAL B 1 80  ? 6.698   28.451  -34.018 1.00 59.29  ? 114 VAL B O   1 
ATOM   2322 C  CB  . VAL B 1 80  ? 4.205   28.374  -36.052 1.00 57.81  ? 114 VAL B CB  1 
ATOM   2323 C  CG1 . VAL B 1 80  ? 5.317   27.550  -36.687 1.00 58.78  ? 114 VAL B CG1 1 
ATOM   2324 C  CG2 . VAL B 1 80  ? 3.198   27.476  -35.343 1.00 53.04  ? 114 VAL B CG2 1 
ATOM   2325 N  N   . VAL B 1 81  ? 4.810   28.609  -32.795 1.00 55.65  ? 115 VAL B N   1 
ATOM   2326 C  CA  . VAL B 1 81  ? 5.368   27.942  -31.626 1.00 53.74  ? 115 VAL B CA  1 
ATOM   2327 C  C   . VAL B 1 81  ? 4.555   26.684  -31.355 1.00 55.66  ? 115 VAL B C   1 
ATOM   2328 O  O   . VAL B 1 81  ? 3.342   26.642  -31.580 1.00 56.32  ? 115 VAL B O   1 
ATOM   2329 C  CB  . VAL B 1 81  ? 5.402   28.863  -30.387 1.00 57.62  ? 115 VAL B CB  1 
ATOM   2330 C  CG1 . VAL B 1 81  ? 6.403   29.990  -30.596 1.00 55.17  ? 115 VAL B CG1 1 
ATOM   2331 C  CG2 . VAL B 1 81  ? 4.027   29.425  -30.102 1.00 55.74  ? 115 VAL B CG2 1 
ATOM   2332 N  N   . THR B 1 82  ? 5.239   25.648  -30.870 1.00 55.87  ? 116 THR B N   1 
ATOM   2333 C  CA  . THR B 1 82  ? 4.644   24.320  -30.798 1.00 52.81  ? 116 THR B CA  1 
ATOM   2334 C  C   . THR B 1 82  ? 3.843   24.080  -29.525 1.00 58.70  ? 116 THR B C   1 
ATOM   2335 O  O   . THR B 1 82  ? 2.919   23.258  -29.536 1.00 66.84  ? 116 THR B O   1 
ATOM   2336 C  CB  . THR B 1 82  ? 5.730   23.250  -30.938 1.00 62.77  ? 116 THR B CB  1 
ATOM   2337 O  OG1 . THR B 1 82  ? 6.751   23.467  -29.958 1.00 71.75  ? 116 THR B OG1 1 
ATOM   2338 C  CG2 . THR B 1 82  ? 6.347   23.309  -32.329 1.00 51.20  ? 116 THR B CG2 1 
ATOM   2339 N  N   . HIS B 1 83  ? 4.172   24.767  -28.434 1.00 54.49  ? 117 HIS B N   1 
ATOM   2340 C  CA  . HIS B 1 83  ? 3.378   24.720  -27.210 1.00 58.46  ? 117 HIS B CA  1 
ATOM   2341 C  C   . HIS B 1 83  ? 3.892   25.803  -26.273 1.00 62.42  ? 117 HIS B C   1 
ATOM   2342 O  O   . HIS B 1 83  ? 4.937   26.415  -26.512 1.00 61.66  ? 117 HIS B O   1 
ATOM   2343 C  CB  . HIS B 1 83  ? 3.423   23.345  -26.536 1.00 59.23  ? 117 HIS B CB  1 
ATOM   2344 C  CG  . HIS B 1 83  ? 4.803   22.880  -26.200 1.00 55.12  ? 117 HIS B CG  1 
ATOM   2345 N  ND1 . HIS B 1 83  ? 5.677   22.399  -27.151 1.00 61.84  ? 117 HIS B ND1 1 
ATOM   2346 C  CD2 . HIS B 1 83  ? 5.461   22.818  -25.019 1.00 57.17  ? 117 HIS B CD2 1 
ATOM   2347 C  CE1 . HIS B 1 83  ? 6.814   22.063  -26.571 1.00 59.75  ? 117 HIS B CE1 1 
ATOM   2348 N  NE2 . HIS B 1 83  ? 6.710   22.308  -25.277 1.00 57.35  ? 117 HIS B NE2 1 
ATOM   2349 N  N   . ALA B 1 84  ? 3.144   26.029  -25.194 1.00 59.94  ? 118 ALA B N   1 
ATOM   2350 C  CA  . ALA B 1 84  ? 3.433   27.126  -24.274 1.00 63.24  ? 118 ALA B CA  1 
ATOM   2351 C  C   . ALA B 1 84  ? 4.258   26.623  -23.091 1.00 58.15  ? 118 ALA B C   1 
ATOM   2352 O  O   . ALA B 1 84  ? 3.797   26.524  -21.953 1.00 64.16  ? 118 ALA B O   1 
ATOM   2353 C  CB  . ALA B 1 84  ? 2.137   27.790  -23.818 1.00 57.96  ? 118 ALA B CB  1 
ATOM   2354 N  N   . HIS B 1 85  ? 5.510   26.296  -23.392 1.00 64.01  ? 119 HIS B N   1 
ATOM   2355 C  CA  . HIS B 1 85  ? 6.533   26.078  -22.384 1.00 62.20  ? 119 HIS B CA  1 
ATOM   2356 C  C   . HIS B 1 85  ? 7.666   27.067  -22.627 1.00 53.91  ? 119 HIS B C   1 
ATOM   2357 O  O   . HIS B 1 85  ? 7.767   27.671  -23.699 1.00 59.33  ? 119 HIS B O   1 
ATOM   2358 C  CB  . HIS B 1 85  ? 7.051   24.631  -22.399 1.00 55.39  ? 119 HIS B CB  1 
ATOM   2359 C  CG  . HIS B 1 85  ? 6.334   23.724  -21.446 1.00 51.89  ? 119 HIS B CG  1 
ATOM   2360 N  ND1 . HIS B 1 85  ? 6.496   22.355  -21.453 1.00 53.29  ? 119 HIS B ND1 1 
ATOM   2361 C  CD2 . HIS B 1 85  ? 5.449   23.991  -20.456 1.00 65.40  ? 119 HIS B CD2 1 
ATOM   2362 C  CE1 . HIS B 1 85  ? 5.744   21.818  -20.509 1.00 61.07  ? 119 HIS B CE1 1 
ATOM   2363 N  NE2 . HIS B 1 85  ? 5.098   22.789  -19.889 1.00 75.61  ? 119 HIS B NE2 1 
ATOM   2364 N  N   . GLN B 1 86  ? 8.517   27.236  -21.611 1.00 62.69  ? 120 GLN B N   1 
ATOM   2365 C  CA  . GLN B 1 86  ? 9.509   28.308  -21.648 1.00 56.99  ? 120 GLN B CA  1 
ATOM   2366 C  C   . GLN B 1 86  ? 10.465  28.153  -22.826 1.00 56.40  ? 120 GLN B C   1 
ATOM   2367 O  O   . GLN B 1 86  ? 10.846  29.145  -23.460 1.00 59.67  ? 120 GLN B O   1 
ATOM   2368 C  CB  . GLN B 1 86  ? 10.281  28.353  -20.329 1.00 51.66  ? 120 GLN B CB  1 
ATOM   2369 C  CG  . GLN B 1 86  ? 11.565  29.166  -20.393 1.00 66.63  ? 120 GLN B CG  1 
ATOM   2370 C  CD  . GLN B 1 86  ? 11.484  30.449  -19.595 1.00 64.97  ? 120 GLN B CD  1 
ATOM   2371 O  OE1 . GLN B 1 86  ? 10.451  30.763  -19.004 1.00 75.41  ? 120 GLN B OE1 1 
ATOM   2372 N  NE2 . GLN B 1 86  ? 12.576  31.205  -19.578 1.00 58.27  ? 120 GLN B NE2 1 
ATOM   2373 N  N   . ASP B 1 87  ? 10.851  26.918  -23.148 1.00 58.54  ? 121 ASP B N   1 
ATOM   2374 C  CA  . ASP B 1 87  ? 11.801  26.687  -24.230 1.00 60.66  ? 121 ASP B CA  1 
ATOM   2375 C  C   . ASP B 1 87  ? 11.223  26.987  -25.607 1.00 61.68  ? 121 ASP B C   1 
ATOM   2376 O  O   . ASP B 1 87  ? 11.971  26.956  -26.591 1.00 60.70  ? 121 ASP B O   1 
ATOM   2377 C  CB  . ASP B 1 87  ? 12.301  25.242  -24.189 1.00 60.78  ? 121 ASP B CB  1 
ATOM   2378 C  CG  . ASP B 1 87  ? 11.176  24.240  -24.026 1.00 59.17  ? 121 ASP B CG  1 
ATOM   2379 O  OD1 . ASP B 1 87  ? 10.228  24.525  -23.264 1.00 56.39  ? 121 ASP B OD1 1 
ATOM   2380 O  OD2 . ASP B 1 87  ? 11.241  23.167  -24.661 1.00 58.24  ? 121 ASP B OD2 1 
ATOM   2381 N  N   . LYS B 1 88  ? 9.929   27.276  -25.706 1.00 60.59  ? 122 LYS B N   1 
ATOM   2382 C  CA  . LYS B 1 88  ? 9.286   27.543  -26.987 1.00 64.49  ? 122 LYS B CA  1 
ATOM   2383 C  C   . LYS B 1 88  ? 8.676   28.931  -27.081 1.00 62.65  ? 122 LYS B C   1 
ATOM   2384 O  O   . LYS B 1 88  ? 8.720   29.543  -28.151 1.00 67.93  ? 122 LYS B O   1 
ATOM   2385 C  CB  . LYS B 1 88  ? 8.199   26.492  -27.259 1.00 61.89  ? 122 LYS B CB  1 
ATOM   2386 C  CG  . LYS B 1 88  ? 8.569   25.085  -26.817 1.00 59.65  ? 122 LYS B CG  1 
ATOM   2387 C  CD  . LYS B 1 88  ? 9.104   24.262  -27.976 1.00 53.07  ? 122 LYS B CD  1 
ATOM   2388 C  CE  . LYS B 1 88  ? 10.616  24.362  -28.090 1.00 56.25  ? 122 LYS B CE  1 
ATOM   2389 N  NZ  . LYS B 1 88  ? 11.112  23.721  -29.339 1.00 57.34  ? 122 LYS B NZ  1 
ATOM   2390 N  N   . MET B 1 89  ? 8.106   29.449  -25.991 1.00 63.48  ? 123 MET B N   1 
ATOM   2391 C  CA  . MET B 1 89  ? 7.467   30.761  -25.994 1.00 69.36  ? 123 MET B CA  1 
ATOM   2392 C  C   . MET B 1 89  ? 8.121   31.726  -25.013 1.00 72.75  ? 123 MET B C   1 
ATOM   2393 O  O   . MET B 1 89  ? 7.486   32.696  -24.586 1.00 77.51  ? 123 MET B O   1 
ATOM   2394 C  CB  . MET B 1 89  ? 5.973   30.632  -25.690 1.00 63.15  ? 123 MET B CB  1 
ATOM   2395 C  CG  . MET B 1 89  ? 5.228   29.689  -26.617 1.00 67.96  ? 123 MET B CG  1 
ATOM   2396 S  SD  . MET B 1 89  ? 3.440   29.900  -26.523 1.00 65.68  ? 123 MET B SD  1 
ATOM   2397 C  CE  . MET B 1 89  ? 3.260   31.559  -27.173 1.00 71.90  ? 123 MET B CE  1 
ATOM   2398 N  N   . GLY B 1 90  ? 9.382   31.484  -24.644 1.00 65.27  ? 124 GLY B N   1 
ATOM   2399 C  CA  . GLY B 1 90  ? 10.064  32.380  -23.729 1.00 68.01  ? 124 GLY B CA  1 
ATOM   2400 C  C   . GLY B 1 90  ? 10.583  33.651  -24.361 1.00 70.69  ? 124 GLY B C   1 
ATOM   2401 O  O   . GLY B 1 90  ? 10.839  34.626  -23.647 1.00 71.44  ? 124 GLY B O   1 
ATOM   2402 N  N   . GLY B 1 91  ? 10.742  33.667  -25.682 1.00 71.29  ? 125 GLY B N   1 
ATOM   2403 C  CA  . GLY B 1 91  ? 11.232  34.843  -26.370 1.00 66.10  ? 125 GLY B CA  1 
ATOM   2404 C  C   . GLY B 1 91  ? 10.208  35.462  -27.298 1.00 69.86  ? 125 GLY B C   1 
ATOM   2405 O  O   . GLY B 1 91  ? 10.549  35.934  -28.386 1.00 69.37  ? 125 GLY B O   1 
ATOM   2406 N  N   . MET B 1 92  ? 8.941   35.464  -26.875 1.00 68.21  ? 126 MET B N   1 
ATOM   2407 C  CA  . MET B 1 92  ? 7.888   36.042  -27.701 1.00 68.64  ? 126 MET B CA  1 
ATOM   2408 C  C   . MET B 1 92  ? 8.014   37.556  -27.799 1.00 78.17  ? 126 MET B C   1 
ATOM   2409 O  O   . MET B 1 92  ? 7.631   38.144  -28.817 1.00 74.57  ? 126 MET B O   1 
ATOM   2410 C  CB  . MET B 1 92  ? 6.516   35.661  -27.145 1.00 70.51  ? 126 MET B CB  1 
ATOM   2411 C  CG  . MET B 1 92  ? 6.197   34.179  -27.235 1.00 73.63  ? 126 MET B CG  1 
ATOM   2412 S  SD  . MET B 1 92  ? 5.963   33.628  -28.934 1.00 85.99  ? 126 MET B SD  1 
ATOM   2413 C  CE  . MET B 1 92  ? 4.564   34.635  -29.412 1.00 69.00  ? 126 MET B CE  1 
ATOM   2414 N  N   . GLY B 1 93  ? 8.545   38.202  -26.758 1.00 73.61  ? 127 GLY B N   1 
ATOM   2415 C  CA  . GLY B 1 93  ? 8.696   39.647  -26.797 1.00 69.52  ? 127 GLY B CA  1 
ATOM   2416 C  C   . GLY B 1 93  ? 9.689   40.106  -27.846 1.00 77.42  ? 127 GLY B C   1 
ATOM   2417 O  O   . GLY B 1 93  ? 9.503   41.152  -28.474 1.00 79.75  ? 127 GLY B O   1 
ATOM   2418 N  N   . ALA B 1 94  ? 10.757  39.331  -28.054 1.00 86.30  ? 128 ALA B N   1 
ATOM   2419 C  CA  . ALA B 1 94  ? 11.730  39.679  -29.084 1.00 80.79  ? 128 ALA B CA  1 
ATOM   2420 C  C   . ALA B 1 94  ? 11.128  39.581  -30.479 1.00 87.94  ? 128 ALA B C   1 
ATOM   2421 O  O   . ALA B 1 94  ? 11.576  40.280  -31.396 1.00 99.06  ? 128 ALA B O   1 
ATOM   2422 C  CB  . ALA B 1 94  ? 12.960  38.779  -28.972 1.00 75.00  ? 128 ALA B CB  1 
ATOM   2423 N  N   . LEU B 1 95  ? 10.119  38.728  -30.660 1.00 81.39  ? 129 LEU B N   1 
ATOM   2424 C  CA  . LEU B 1 95  ? 9.463   38.619  -31.957 1.00 77.27  ? 129 LEU B CA  1 
ATOM   2425 C  C   . LEU B 1 95  ? 8.449   39.736  -32.165 1.00 84.51  ? 129 LEU B C   1 
ATOM   2426 O  O   . LEU B 1 95  ? 8.330   40.272  -33.272 1.00 87.81  ? 129 LEU B O   1 
ATOM   2427 C  CB  . LEU B 1 95  ? 8.784   37.257  -32.090 1.00 65.86  ? 129 LEU B CB  1 
ATOM   2428 C  CG  . LEU B 1 95  ? 9.714   36.049  -32.180 1.00 71.62  ? 129 LEU B CG  1 
ATOM   2429 C  CD1 . LEU B 1 95  ? 8.914   34.804  -32.509 1.00 57.40  ? 129 LEU B CD1 1 
ATOM   2430 C  CD2 . LEU B 1 95  ? 10.806  36.281  -33.213 1.00 73.23  ? 129 LEU B CD2 1 
ATOM   2431 N  N   . HIS B 1 96  ? 7.709   40.097  -31.114 1.00 84.12  ? 130 HIS B N   1 
ATOM   2432 C  CA  . HIS B 1 96  ? 6.739   41.180  -31.234 1.00 82.74  ? 130 HIS B CA  1 
ATOM   2433 C  C   . HIS B 1 96  ? 7.422   42.538  -31.324 1.00 81.92  ? 130 HIS B C   1 
ATOM   2434 O  O   . HIS B 1 96  ? 6.871   43.468  -31.922 1.00 81.48  ? 130 HIS B O   1 
ATOM   2435 C  CB  . HIS B 1 96  ? 5.766   41.147  -30.056 1.00 72.62  ? 130 HIS B CB  1 
ATOM   2436 C  CG  . HIS B 1 96  ? 4.962   39.887  -29.973 1.00 70.97  ? 130 HIS B CG  1 
ATOM   2437 N  ND1 . HIS B 1 96  ? 4.243   39.535  -28.852 1.00 74.90  ? 130 HIS B ND1 1 
ATOM   2438 C  CD2 . HIS B 1 96  ? 4.764   38.896  -30.874 1.00 77.05  ? 130 HIS B CD2 1 
ATOM   2439 C  CE1 . HIS B 1 96  ? 3.636   38.381  -29.065 1.00 73.33  ? 130 HIS B CE1 1 
ATOM   2440 N  NE2 . HIS B 1 96  ? 3.936   37.972  -30.284 1.00 74.76  ? 130 HIS B NE2 1 
ATOM   2441 N  N   . ALA B 1 97  ? 8.617   42.671  -30.743 1.00 83.79  ? 131 ALA B N   1 
ATOM   2442 C  CA  . ALA B 1 97  ? 9.376   43.910  -30.862 1.00 86.39  ? 131 ALA B CA  1 
ATOM   2443 C  C   . ALA B 1 97  ? 9.933   44.123  -32.262 1.00 91.43  ? 131 ALA B C   1 
ATOM   2444 O  O   . ALA B 1 97  ? 10.481  45.196  -32.535 1.00 93.07  ? 131 ALA B O   1 
ATOM   2445 C  CB  . ALA B 1 97  ? 10.518  43.929  -29.844 1.00 83.83  ? 131 ALA B CB  1 
ATOM   2446 N  N   . GLU B 1 98  ? 9.811   43.133  -33.147 1.00 83.80  ? 132 GLU B N   1 
ATOM   2447 C  CA  . GLU B 1 98  ? 10.256  43.253  -34.530 1.00 84.93  ? 132 GLU B CA  1 
ATOM   2448 C  C   . GLU B 1 98  ? 9.101   43.160  -35.519 1.00 93.39  ? 132 GLU B C   1 
ATOM   2449 O  O   . GLU B 1 98  ? 9.343   43.018  -36.724 1.00 97.47  ? 132 GLU B O   1 
ATOM   2450 C  CB  . GLU B 1 98  ? 11.304  42.181  -34.846 1.00 84.89  ? 132 GLU B CB  1 
ATOM   2451 C  CG  . GLU B 1 98  ? 12.526  42.708  -35.581 1.00 95.57  ? 132 GLU B CG  1 
ATOM   2452 C  CD  . GLU B 1 98  ? 13.481  43.453  -34.668 1.00 106.26 ? 132 GLU B CD  1 
ATOM   2453 O  OE1 . GLU B 1 98  ? 13.344  43.331  -33.432 1.00 103.48 ? 132 GLU B OE1 1 
ATOM   2454 O  OE2 . GLU B 1 98  ? 14.368  44.162  -35.187 1.00 110.26 ? 132 GLU B OE2 1 
ATOM   2455 N  N   . ALA B 1 99  ? 7.856   43.235  -35.040 1.00 92.96  ? 133 ALA B N   1 
ATOM   2456 C  CA  . ALA B 1 99  ? 6.663   43.170  -35.886 1.00 92.75  ? 133 ALA B CA  1 
ATOM   2457 C  C   . ALA B 1 99  ? 6.638   41.883  -36.712 1.00 93.80  ? 133 ALA B C   1 
ATOM   2458 O  O   . ALA B 1 99  ? 6.451   41.900  -37.931 1.00 95.57  ? 133 ALA B O   1 
ATOM   2459 C  CB  . ALA B 1 99  ? 6.555   44.404  -36.785 1.00 97.79  ? 133 ALA B CB  1 
ATOM   2460 N  N   . ILE B 1 100 ? 6.827   40.760  -36.034 1.00 89.80  ? 134 ILE B N   1 
ATOM   2461 C  CA  . ILE B 1 100 ? 6.820   39.438  -36.650 1.00 79.10  ? 134 ILE B CA  1 
ATOM   2462 C  C   . ILE B 1 100 ? 5.515   38.748  -36.270 1.00 89.72  ? 134 ILE B C   1 
ATOM   2463 O  O   . ILE B 1 100 ? 5.251   38.553  -35.076 1.00 89.99  ? 134 ILE B O   1 
ATOM   2464 C  CB  . ILE B 1 100 ? 8.033   38.600  -36.213 1.00 75.53  ? 134 ILE B CB  1 
ATOM   2465 C  CG1 . ILE B 1 100 ? 9.333   39.264  -36.672 1.00 73.55  ? 134 ILE B CG1 1 
ATOM   2466 C  CG2 . ILE B 1 100 ? 7.923   37.183  -36.754 1.00 77.27  ? 134 ILE B CG2 1 
ATOM   2467 C  CD1 . ILE B 1 100 ? 10.577  38.665  -36.054 1.00 71.37  ? 134 ILE B CD1 1 
ATOM   2468 N  N   . PRO B 1 101 ? 4.672   38.375  -37.232 1.00 89.45  ? 135 PRO B N   1 
ATOM   2469 C  CA  . PRO B 1 101 ? 3.425   37.678  -36.892 1.00 81.30  ? 135 PRO B CA  1 
ATOM   2470 C  C   . PRO B 1 101 ? 3.709   36.325  -36.259 1.00 73.04  ? 135 PRO B C   1 
ATOM   2471 O  O   . PRO B 1 101 ? 4.446   35.503  -36.810 1.00 72.42  ? 135 PRO B O   1 
ATOM   2472 C  CB  . PRO B 1 101 ? 2.714   37.535  -38.244 1.00 78.93  ? 135 PRO B CB  1 
ATOM   2473 C  CG  . PRO B 1 101 ? 3.374   38.532  -39.146 1.00 82.23  ? 135 PRO B CG  1 
ATOM   2474 C  CD  . PRO B 1 101 ? 4.787   38.641  -38.675 1.00 81.58  ? 135 PRO B CD  1 
ATOM   2475 N  N   . THR B 1 102 ? 3.119   36.099  -35.090 1.00 77.47  ? 136 THR B N   1 
ATOM   2476 C  CA  . THR B 1 102 ? 3.320   34.876  -34.326 1.00 69.74  ? 136 THR B CA  1 
ATOM   2477 C  C   . THR B 1 102 ? 2.028   34.073  -34.290 1.00 68.40  ? 136 THR B C   1 
ATOM   2478 O  O   . THR B 1 102 ? 0.964   34.614  -33.972 1.00 72.94  ? 136 THR B O   1 
ATOM   2479 C  CB  . THR B 1 102 ? 3.789   35.188  -32.904 1.00 70.37  ? 136 THR B CB  1 
ATOM   2480 O  OG1 . THR B 1 102 ? 2.753   35.880  -32.197 1.00 81.95  ? 136 THR B OG1 1 
ATOM   2481 C  CG2 . THR B 1 102 ? 5.043   36.048  -32.934 1.00 73.86  ? 136 THR B CG2 1 
ATOM   2482 N  N   . TYR B 1 103 ? 2.128   32.787  -34.613 1.00 64.39  ? 137 TYR B N   1 
ATOM   2483 C  CA  . TYR B 1 103 ? 0.993   31.879  -34.604 1.00 63.13  ? 137 TYR B CA  1 
ATOM   2484 C  C   . TYR B 1 103 ? 1.231   30.776  -33.582 1.00 63.59  ? 137 TYR B C   1 
ATOM   2485 O  O   . TYR B 1 103 ? 2.375   30.454  -33.247 1.00 57.17  ? 137 TYR B O   1 
ATOM   2486 C  CB  . TYR B 1 103 ? 0.753   31.267  -35.991 1.00 70.58  ? 137 TYR B CB  1 
ATOM   2487 C  CG  . TYR B 1 103 ? 0.484   32.290  -37.073 1.00 71.80  ? 137 TYR B CG  1 
ATOM   2488 C  CD1 . TYR B 1 103 ? 1.529   32.956  -37.702 1.00 66.77  ? 137 TYR B CD1 1 
ATOM   2489 C  CD2 . TYR B 1 103 ? -0.814  32.591  -37.463 1.00 75.78  ? 137 TYR B CD2 1 
ATOM   2490 C  CE1 . TYR B 1 103 ? 1.288   33.892  -38.689 1.00 74.58  ? 137 TYR B CE1 1 
ATOM   2491 C  CE2 . TYR B 1 103 ? -1.065  33.527  -38.449 1.00 80.08  ? 137 TYR B CE2 1 
ATOM   2492 C  CZ  . TYR B 1 103 ? -0.010  34.174  -39.058 1.00 83.81  ? 137 TYR B CZ  1 
ATOM   2493 O  OH  . TYR B 1 103 ? -0.253  35.106  -40.041 1.00 86.53  ? 137 TYR B OH  1 
ATOM   2494 N  N   . ALA B 1 104 ? 0.138   30.201  -33.088 1.00 63.28  ? 138 ALA B N   1 
ATOM   2495 C  CA  . ALA B 1 104 ? 0.226   29.151  -32.084 1.00 61.61  ? 138 ALA B CA  1 
ATOM   2496 C  C   . ALA B 1 104 ? -1.092  28.396  -32.042 1.00 75.00  ? 138 ALA B C   1 
ATOM   2497 O  O   . ALA B 1 104 ? -2.119  28.874  -32.533 1.00 74.12  ? 138 ALA B O   1 
ATOM   2498 C  CB  . ALA B 1 104 ? 0.556   29.720  -30.701 1.00 58.74  ? 138 ALA B CB  1 
ATOM   2499 N  N   . ASN B 1 105 ? -1.044  27.203  -31.454 1.00 70.66  ? 139 ASN B N   1 
ATOM   2500 C  CA  . ASN B 1 105 ? -2.267  26.477  -31.154 1.00 64.61  ? 139 ASN B CA  1 
ATOM   2501 C  C   . ASN B 1 105 ? -3.163  27.335  -30.273 1.00 72.27  ? 139 ASN B C   1 
ATOM   2502 O  O   . ASN B 1 105 ? -2.690  28.016  -29.358 1.00 67.28  ? 139 ASN B O   1 
ATOM   2503 C  CB  . ASN B 1 105 ? -1.943  25.154  -30.457 1.00 60.95  ? 139 ASN B CB  1 
ATOM   2504 C  CG  . ASN B 1 105 ? -3.137  24.220  -30.381 1.00 63.77  ? 139 ASN B CG  1 
ATOM   2505 O  OD1 . ASN B 1 105 ? -4.253  24.583  -30.754 1.00 72.98  ? 139 ASN B OD1 1 
ATOM   2506 N  ND2 . ASN B 1 105 ? -2.906  23.007  -29.892 1.00 60.76  ? 139 ASN B ND2 1 
ATOM   2507 N  N   . ALA B 1 106 ? -4.465  27.322  -30.573 1.00 72.03  ? 140 ALA B N   1 
ATOM   2508 C  CA  . ALA B 1 106 ? -5.408  28.107  -29.784 1.00 68.52  ? 140 ALA B CA  1 
ATOM   2509 C  C   . ALA B 1 106 ? -5.298  27.765  -28.305 1.00 69.68  ? 140 ALA B C   1 
ATOM   2510 O  O   . ALA B 1 106 ? -5.302  28.660  -27.453 1.00 70.15  ? 140 ALA B O   1 
ATOM   2511 C  CB  . ALA B 1 106 ? -6.833  27.883  -30.286 1.00 71.76  ? 140 ALA B CB  1 
ATOM   2512 N  N   . LEU B 1 107 ? -5.173  26.475  -27.984 1.00 68.33  ? 141 LEU B N   1 
ATOM   2513 C  CA  . LEU B 1 107 ? -4.987  26.072  -26.594 1.00 64.62  ? 141 LEU B CA  1 
ATOM   2514 C  C   . LEU B 1 107 ? -3.697  26.645  -26.020 1.00 72.12  ? 141 LEU B C   1 
ATOM   2515 O  O   . LEU B 1 107 ? -3.666  27.083  -24.864 1.00 72.02  ? 141 LEU B O   1 
ATOM   2516 C  CB  . LEU B 1 107 ? -4.992  24.547  -26.489 1.00 61.22  ? 141 LEU B CB  1 
ATOM   2517 C  CG  . LEU B 1 107 ? -4.894  23.950  -25.084 1.00 61.14  ? 141 LEU B CG  1 
ATOM   2518 C  CD1 . LEU B 1 107 ? -5.863  24.636  -24.130 1.00 67.81  ? 141 LEU B CD1 1 
ATOM   2519 C  CD2 . LEU B 1 107 ? -5.136  22.449  -25.115 1.00 60.87  ? 141 LEU B CD2 1 
ATOM   2520 N  N   . SER B 1 108 ? -2.624  26.657  -26.818 1.00 69.49  ? 142 SER B N   1 
ATOM   2521 C  CA  . SER B 1 108 ? -1.349  27.187  -26.342 1.00 64.22  ? 142 SER B CA  1 
ATOM   2522 C  C   . SER B 1 108 ? -1.476  28.645  -25.922 1.00 70.68  ? 142 SER B C   1 
ATOM   2523 O  O   . SER B 1 108 ? -0.948  29.045  -24.878 1.00 74.22  ? 142 SER B O   1 
ATOM   2524 C  CB  . SER B 1 108 ? -0.279  27.035  -27.423 1.00 62.98  ? 142 SER B CB  1 
ATOM   2525 O  OG  . SER B 1 108 ? -0.085  25.674  -27.764 1.00 66.38  ? 142 SER B OG  1 
ATOM   2526 N  N   . ASN B 1 109 ? -2.180  29.452  -26.715 1.00 66.92  ? 143 ASN B N   1 
ATOM   2527 C  CA  . ASN B 1 109 ? -2.365  30.857  -26.374 1.00 70.99  ? 143 ASN B CA  1 
ATOM   2528 C  C   . ASN B 1 109 ? -3.325  31.062  -25.209 1.00 77.34  ? 143 ASN B C   1 
ATOM   2529 O  O   . ASN B 1 109 ? -3.385  32.173  -24.671 1.00 74.84  ? 143 ASN B O   1 
ATOM   2530 C  CB  . ASN B 1 109 ? -2.856  31.629  -27.600 1.00 69.77  ? 143 ASN B CB  1 
ATOM   2531 C  CG  . ASN B 1 109 ? -1.719  32.072  -28.503 1.00 71.62  ? 143 ASN B CG  1 
ATOM   2532 O  OD1 . ASN B 1 109 ? -0.569  32.161  -28.072 1.00 70.95  ? 143 ASN B OD1 1 
ATOM   2533 N  ND2 . ASN B 1 109 ? -2.035  32.349  -29.763 1.00 72.29  ? 143 ASN B ND2 1 
ATOM   2534 N  N   . GLN B 1 110 ? -4.071  30.031  -24.808 1.00 80.78  ? 144 GLN B N   1 
ATOM   2535 C  CA  . GLN B 1 110 ? -4.998  30.136  -23.688 1.00 75.14  ? 144 GLN B CA  1 
ATOM   2536 C  C   . GLN B 1 110 ? -4.424  29.618  -22.378 1.00 81.83  ? 144 GLN B C   1 
ATOM   2537 O  O   . GLN B 1 110 ? -4.739  30.170  -21.320 1.00 88.66  ? 144 GLN B O   1 
ATOM   2538 C  CB  . GLN B 1 110 ? -6.302  29.392  -24.000 1.00 79.08  ? 144 GLN B CB  1 
ATOM   2539 N  N   . LEU B 1 111 ? -3.589  28.582  -22.413 1.00 75.66  ? 145 LEU B N   1 
ATOM   2540 C  CA  . LEU B 1 111 ? -2.898  28.138  -21.213 1.00 74.68  ? 145 LEU B CA  1 
ATOM   2541 C  C   . LEU B 1 111 ? -1.557  28.833  -21.016 1.00 72.44  ? 145 LEU B C   1 
ATOM   2542 O  O   . LEU B 1 111 ? -0.864  28.534  -20.038 1.00 71.88  ? 145 LEU B O   1 
ATOM   2543 C  CB  . LEU B 1 111 ? -2.708  26.611  -21.234 1.00 66.82  ? 145 LEU B CB  1 
ATOM   2544 C  CG  . LEU B 1 111 ? -2.071  25.880  -22.421 1.00 69.72  ? 145 LEU B CG  1 
ATOM   2545 C  CD1 . LEU B 1 111 ? -0.557  25.995  -22.424 1.00 74.20  ? 145 LEU B CD1 1 
ATOM   2546 C  CD2 . LEU B 1 111 ? -2.492  24.417  -22.432 1.00 68.24  ? 145 LEU B CD2 1 
ATOM   2547 N  N   . ALA B 1 112 ? -1.168  29.747  -21.915 1.00 70.02  ? 146 ALA B N   1 
ATOM   2548 C  CA  . ALA B 1 112 ? 0.093   30.459  -21.708 1.00 67.98  ? 146 ALA B CA  1 
ATOM   2549 C  C   . ALA B 1 112 ? 0.022   31.463  -20.562 1.00 73.78  ? 146 ALA B C   1 
ATOM   2550 O  O   . ALA B 1 112 ? 0.986   31.527  -19.775 1.00 76.71  ? 146 ALA B O   1 
ATOM   2551 C  CB  . ALA B 1 112 ? 0.553   31.112  -23.014 1.00 69.08  ? 146 ALA B CB  1 
ATOM   2552 N  N   . PRO B 1 113 ? -1.044  32.266  -20.389 1.00 78.28  ? 147 PRO B N   1 
ATOM   2553 C  CA  . PRO B 1 113 ? -1.052  33.193  -19.241 1.00 63.53  ? 147 PRO B CA  1 
ATOM   2554 C  C   . PRO B 1 113 ? -0.939  32.493  -17.899 1.00 62.11  ? 147 PRO B C   1 
ATOM   2555 O  O   . PRO B 1 113 ? -0.362  33.064  -16.966 1.00 62.66  ? 147 PRO B O   1 
ATOM   2556 C  CB  . PRO B 1 113 ? -2.387  33.942  -19.364 1.00 66.32  ? 147 PRO B CB  1 
ATOM   2557 C  CG  . PRO B 1 113 ? -3.060  33.443  -20.558 1.00 75.10  ? 147 PRO B CG  1 
ATOM   2558 C  CD  . PRO B 1 113 ? -2.198  32.477  -21.287 1.00 73.95  ? 147 PRO B CD  1 
ATOM   2559 N  N   . GLN B 1 114 ? -1.468  31.274  -17.770 1.00 69.44  ? 148 GLN B N   1 
ATOM   2560 C  CA  . GLN B 1 114 ? -1.328  30.539  -16.517 1.00 65.72  ? 148 GLN B CA  1 
ATOM   2561 C  C   . GLN B 1 114 ? 0.108   30.086  -16.289 1.00 66.62  ? 148 GLN B C   1 
ATOM   2562 O  O   . GLN B 1 114 ? 0.522   29.887  -15.141 1.00 67.16  ? 148 GLN B O   1 
ATOM   2563 C  CB  . GLN B 1 114 ? -2.274  29.338  -16.505 1.00 72.82  ? 148 GLN B CB  1 
ATOM   2564 C  CG  . GLN B 1 114 ? -3.631  29.613  -17.133 1.00 77.32  ? 148 GLN B CG  1 
ATOM   2565 C  CD  . GLN B 1 114 ? -4.361  28.343  -17.519 1.00 89.04  ? 148 GLN B CD  1 
ATOM   2566 O  OE1 . GLN B 1 114 ? -3.952  27.243  -17.147 1.00 84.03  ? 148 GLN B OE1 1 
ATOM   2567 N  NE2 . GLN B 1 114 ? -5.452  28.487  -18.264 1.00 85.84  ? 148 GLN B NE2 1 
ATOM   2568 N  N   . GLU B 1 115 ? 0.880   29.921  -17.362 1.00 74.97  ? 149 GLU B N   1 
ATOM   2569 C  CA  . GLU B 1 115 ? 2.269   29.495  -17.273 1.00 66.99  ? 149 GLU B CA  1 
ATOM   2570 C  C   . GLU B 1 115 ? 3.249   30.652  -17.422 1.00 67.04  ? 149 GLU B C   1 
ATOM   2571 O  O   . GLU B 1 115 ? 4.444   30.417  -17.625 1.00 75.09  ? 149 GLU B O   1 
ATOM   2572 C  CB  . GLU B 1 115 ? 2.555   28.420  -18.323 1.00 66.78  ? 149 GLU B CB  1 
ATOM   2573 C  CG  . GLU B 1 115 ? 2.012   27.048  -17.960 1.00 68.68  ? 149 GLU B CG  1 
ATOM   2574 C  CD  . GLU B 1 115 ? 2.903   25.920  -18.438 1.00 95.22  ? 149 GLU B CD  1 
ATOM   2575 O  OE1 . GLU B 1 115 ? 2.616   25.349  -19.512 1.00 96.72  ? 149 GLU B OE1 1 
ATOM   2576 O  OE2 . GLU B 1 115 ? 3.890   25.603  -17.741 1.00 96.43  ? 149 GLU B OE2 1 
ATOM   2577 N  N   . GLY B 1 116 ? 2.772   31.893  -17.328 1.00 70.65  ? 150 GLY B N   1 
ATOM   2578 C  CA  . GLY B 1 116 ? 3.631   33.057  -17.367 1.00 65.00  ? 150 GLY B CA  1 
ATOM   2579 C  C   . GLY B 1 116 ? 4.106   33.478  -18.740 1.00 70.34  ? 150 GLY B C   1 
ATOM   2580 O  O   . GLY B 1 116 ? 4.890   34.430  -18.837 1.00 66.14  ? 150 GLY B O   1 
ATOM   2581 N  N   . MET B 1 117 ? 3.662   32.812  -19.802 1.00 70.99  ? 151 MET B N   1 
ATOM   2582 C  CA  . MET B 1 117 ? 4.101   33.133  -21.152 1.00 71.60  ? 151 MET B CA  1 
ATOM   2583 C  C   . MET B 1 117 ? 3.200   34.193  -21.771 1.00 79.41  ? 151 MET B C   1 
ATOM   2584 O  O   . MET B 1 117 ? 1.990   34.217  -21.528 1.00 75.65  ? 151 MET B O   1 
ATOM   2585 C  CB  . MET B 1 117 ? 4.101   31.882  -22.032 1.00 74.91  ? 151 MET B CB  1 
ATOM   2586 C  CG  . MET B 1 117 ? 4.800   30.682  -21.417 1.00 73.49  ? 151 MET B CG  1 
ATOM   2587 S  SD  . MET B 1 117 ? 6.552   30.617  -21.834 1.00 61.78  ? 151 MET B SD  1 
ATOM   2588 C  CE  . MET B 1 117 ? 7.289   31.058  -20.263 1.00 64.41  ? 151 MET B CE  1 
ATOM   2589 N  N   . THR B 1 118 ? 3.800   35.070  -22.571 1.00 85.95  ? 152 THR B N   1 
ATOM   2590 C  CA  . THR B 1 118 ? 3.037   36.032  -23.355 1.00 73.99  ? 152 THR B CA  1 
ATOM   2591 C  C   . THR B 1 118 ? 2.533   35.343  -24.618 1.00 81.26  ? 152 THR B C   1 
ATOM   2592 O  O   . THR B 1 118 ? 3.332   34.882  -25.441 1.00 85.22  ? 152 THR B O   1 
ATOM   2593 C  CB  . THR B 1 118 ? 3.891   37.251  -23.700 1.00 77.21  ? 152 THR B CB  1 
ATOM   2594 O  OG1 . THR B 1 118 ? 4.664   36.980  -24.875 1.00 93.14  ? 152 THR B OG1 1 
ATOM   2595 C  CG2 . THR B 1 118 ? 4.829   37.587  -22.549 1.00 83.27  ? 152 THR B CG2 1 
ATOM   2596 N  N   . ALA B 1 119 ? 1.213   35.269  -24.767 1.00 78.22  ? 153 ALA B N   1 
ATOM   2597 C  CA  . ALA B 1 119 ? 0.607   34.497  -25.841 1.00 73.79  ? 153 ALA B CA  1 
ATOM   2598 C  C   . ALA B 1 119 ? 0.933   35.104  -27.205 1.00 70.09  ? 153 ALA B C   1 
ATOM   2599 O  O   . ALA B 1 119 ? 1.420   36.233  -27.323 1.00 79.58  ? 153 ALA B O   1 
ATOM   2600 C  CB  . ALA B 1 119 ? -0.906  34.409  -25.648 1.00 71.92  ? 153 ALA B CB  1 
ATOM   2601 N  N   . ALA B 1 120 ? 0.652   34.329  -28.250 1.00 69.18  ? 154 ALA B N   1 
ATOM   2602 C  CA  . ALA B 1 120 ? 0.916   34.753  -29.614 1.00 71.01  ? 154 ALA B CA  1 
ATOM   2603 C  C   . ALA B 1 120 ? -0.220  35.631  -30.133 1.00 74.38  ? 154 ALA B C   1 
ATOM   2604 O  O   . ALA B 1 120 ? -1.286  35.751  -29.522 1.00 81.40  ? 154 ALA B O   1 
ATOM   2605 C  CB  . ALA B 1 120 ? 1.113   33.541  -30.523 1.00 67.95  ? 154 ALA B CB  1 
ATOM   2606 N  N   . GLN B 1 121 ? 0.022   36.251  -31.290 1.00 79.38  ? 155 GLN B N   1 
ATOM   2607 C  CA  . GLN B 1 121 ? -0.964  37.160  -31.867 1.00 81.40  ? 155 GLN B CA  1 
ATOM   2608 C  C   . GLN B 1 121 ? -2.177  36.400  -32.389 1.00 78.43  ? 155 GLN B C   1 
ATOM   2609 O  O   . GLN B 1 121 ? -3.320  36.725  -32.048 1.00 83.46  ? 155 GLN B O   1 
ATOM   2610 C  CB  . GLN B 1 121 ? -0.322  37.986  -32.982 1.00 87.64  ? 155 GLN B CB  1 
ATOM   2611 C  CG  . GLN B 1 121 ? 0.844   38.848  -32.525 1.00 93.37  ? 155 GLN B CG  1 
ATOM   2612 C  CD  . GLN B 1 121 ? 1.433   39.676  -33.651 1.00 102.30 ? 155 GLN B CD  1 
ATOM   2613 O  OE1 . GLN B 1 121 ? 1.104   39.479  -34.820 1.00 97.84  ? 155 GLN B OE1 1 
ATOM   2614 N  NE2 . GLN B 1 121 ? 2.310   40.611  -33.301 1.00 95.66  ? 155 GLN B NE2 1 
ATOM   2615 N  N   . HIS B 1 122 ? -1.950  35.386  -33.217 1.00 83.04  ? 156 HIS B N   1 
ATOM   2616 C  CA  . HIS B 1 122 ? -3.021  34.612  -33.824 1.00 80.94  ? 156 HIS B CA  1 
ATOM   2617 C  C   . HIS B 1 122 ? -3.067  33.210  -33.230 1.00 74.01  ? 156 HIS B C   1 
ATOM   2618 O  O   . HIS B 1 122 ? -2.101  32.731  -32.629 1.00 77.49  ? 156 HIS B O   1 
ATOM   2619 C  CB  . HIS B 1 122 ? -2.845  34.537  -35.344 1.00 78.26  ? 156 HIS B CB  1 
ATOM   2620 C  CG  . HIS B 1 122 ? -2.492  35.849  -35.974 1.00 85.67  ? 156 HIS B CG  1 
ATOM   2621 N  ND1 . HIS B 1 122 ? -1.197  36.315  -36.047 1.00 85.22  ? 156 HIS B ND1 1 
ATOM   2622 C  CD2 . HIS B 1 122 ? -3.267  36.797  -36.552 1.00 81.79  ? 156 HIS B CD2 1 
ATOM   2623 C  CE1 . HIS B 1 122 ? -1.189  37.492  -36.647 1.00 86.53  ? 156 HIS B CE1 1 
ATOM   2624 N  NE2 . HIS B 1 122 ? -2.432  37.808  -36.963 1.00 86.11  ? 156 HIS B NE2 1 
ATOM   2625 N  N   . SER B 1 123 ? -4.212  32.556  -33.406 1.00 82.40  ? 157 SER B N   1 
ATOM   2626 C  CA  . SER B 1 123 ? -4.462  31.233  -32.849 1.00 85.76  ? 157 SER B CA  1 
ATOM   2627 C  C   . SER B 1 123 ? -4.803  30.264  -33.971 1.00 90.19  ? 157 SER B C   1 
ATOM   2628 O  O   . SER B 1 123 ? -5.661  30.555  -34.811 1.00 88.19  ? 157 SER B O   1 
ATOM   2629 C  CB  . SER B 1 123 ? -5.599  31.275  -31.824 1.00 78.79  ? 157 SER B CB  1 
ATOM   2630 O  OG  . SER B 1 123 ? -5.187  31.915  -30.629 1.00 91.45  ? 157 SER B OG  1 
ATOM   2631 N  N   . LEU B 1 124 ? -4.133  29.116  -33.979 1.00 74.02  ? 158 LEU B N   1 
ATOM   2632 C  CA  . LEU B 1 124 ? -4.396  28.071  -34.955 1.00 75.43  ? 158 LEU B CA  1 
ATOM   2633 C  C   . LEU B 1 124 ? -5.474  27.124  -34.441 1.00 77.64  ? 158 LEU B C   1 
ATOM   2634 O  O   . LEU B 1 124 ? -5.578  26.861  -33.240 1.00 77.52  ? 158 LEU B O   1 
ATOM   2635 C  CB  . LEU B 1 124 ? -3.122  27.281  -35.265 1.00 72.69  ? 158 LEU B CB  1 
ATOM   2636 C  CG  . LEU B 1 124 ? -1.915  28.052  -35.802 1.00 67.22  ? 158 LEU B CG  1 
ATOM   2637 C  CD1 . LEU B 1 124 ? -0.650  27.220  -35.669 1.00 69.58  ? 158 LEU B CD1 1 
ATOM   2638 C  CD2 . LEU B 1 124 ? -2.139  28.452  -37.248 1.00 69.31  ? 158 LEU B CD2 1 
ATOM   2639 N  N   . THR B 1 125 ? -6.280  26.616  -35.367 1.00 74.50  ? 159 THR B N   1 
ATOM   2640 C  CA  . THR B 1 125 ? -7.293  25.618  -35.064 1.00 72.68  ? 159 THR B CA  1 
ATOM   2641 C  C   . THR B 1 125 ? -7.055  24.380  -35.918 1.00 76.50  ? 159 THR B C   1 
ATOM   2642 O  O   . THR B 1 125 ? -6.420  24.439  -36.975 1.00 73.00  ? 159 THR B O   1 
ATOM   2643 C  CB  . THR B 1 125 ? -8.710  26.157  -35.301 1.00 76.50  ? 159 THR B CB  1 
ATOM   2644 O  OG1 . THR B 1 125 ? -8.753  26.873  -36.541 1.00 80.00  ? 159 THR B OG1 1 
ATOM   2645 C  CG2 . THR B 1 125 ? -9.118  27.088  -34.169 1.00 68.64  ? 159 THR B CG2 1 
ATOM   2646 N  N   . PHE B 1 126 ? -7.572  23.248  -35.446 1.00 75.96  ? 160 PHE B N   1 
ATOM   2647 C  CA  . PHE B 1 126 ? -7.328  21.966  -36.087 1.00 71.70  ? 160 PHE B CA  1 
ATOM   2648 C  C   . PHE B 1 126 ? -8.630  21.189  -36.192 1.00 80.62  ? 160 PHE B C   1 
ATOM   2649 O  O   . PHE B 1 126 ? -9.518  21.314  -35.345 1.00 90.06  ? 160 PHE B O   1 
ATOM   2650 C  CB  . PHE B 1 126 ? -6.281  21.149  -35.317 1.00 65.06  ? 160 PHE B CB  1 
ATOM   2651 C  CG  . PHE B 1 126 ? -4.969  21.860  -35.145 1.00 71.12  ? 160 PHE B CG  1 
ATOM   2652 C  CD1 . PHE B 1 126 ? -4.767  22.725  -34.082 1.00 69.58  ? 160 PHE B CD1 1 
ATOM   2653 C  CD2 . PHE B 1 126 ? -3.940  21.668  -36.049 1.00 67.74  ? 160 PHE B CD2 1 
ATOM   2654 C  CE1 . PHE B 1 126 ? -3.562  23.384  -33.926 1.00 65.80  ? 160 PHE B CE1 1 
ATOM   2655 C  CE2 . PHE B 1 126 ? -2.733  22.322  -35.899 1.00 61.90  ? 160 PHE B CE2 1 
ATOM   2656 C  CZ  . PHE B 1 126 ? -2.544  23.182  -34.837 1.00 62.65  ? 160 PHE B CZ  1 
ATOM   2657 N  N   . ALA B 1 127 ? -8.733  20.383  -37.245 1.00 83.44  ? 161 ALA B N   1 
ATOM   2658 C  CA  . ALA B 1 127 ? -9.910  19.556  -37.471 1.00 82.18  ? 161 ALA B CA  1 
ATOM   2659 C  C   . ALA B 1 127 ? -9.780  18.259  -36.675 1.00 83.91  ? 161 ALA B C   1 
ATOM   2660 O  O   . ALA B 1 127 ? -8.915  18.115  -35.806 1.00 90.89  ? 161 ALA B O   1 
ATOM   2661 C  CB  . ALA B 1 127 ? -10.097 19.299  -38.964 1.00 89.31  ? 161 ALA B CB  1 
ATOM   2662 N  N   . ALA B 1 128 ? -10.649 17.290  -36.967 1.00 90.86  ? 162 ALA B N   1 
ATOM   2663 C  CA  . ALA B 1 128 ? -10.604 16.020  -36.251 1.00 89.56  ? 162 ALA B CA  1 
ATOM   2664 C  C   . ALA B 1 128 ? -9.423  15.169  -36.704 1.00 81.95  ? 162 ALA B C   1 
ATOM   2665 O  O   . ALA B 1 128 ? -8.821  14.454  -35.895 1.00 85.82  ? 162 ALA B O   1 
ATOM   2666 C  CB  . ALA B 1 128 ? -11.917 15.262  -36.440 1.00 94.91  ? 162 ALA B CB  1 
ATOM   2667 N  N   . ASN B 1 129 ? -9.075  15.234  -37.992 1.00 80.83  ? 163 ASN B N   1 
ATOM   2668 C  CA  . ASN B 1 129 ? -7.946  14.461  -38.493 1.00 75.59  ? 163 ASN B CA  1 
ATOM   2669 C  C   . ASN B 1 129 ? -6.614  14.970  -37.958 1.00 79.44  ? 163 ASN B C   1 
ATOM   2670 O  O   . ASN B 1 129 ? -5.620  14.238  -38.008 1.00 83.34  ? 163 ASN B O   1 
ATOM   2671 C  CB  . ASN B 1 129 ? -7.938  14.467  -40.023 1.00 72.00  ? 163 ASN B CB  1 
ATOM   2672 C  CG  . ASN B 1 129 ? -7.866  15.865  -40.603 1.00 73.28  ? 163 ASN B CG  1 
ATOM   2673 O  OD1 . ASN B 1 129 ? -8.016  16.856  -39.889 1.00 81.21  ? 163 ASN B OD1 1 
ATOM   2674 N  ND2 . ASN B 1 129 ? -7.638  15.952  -41.909 1.00 71.21  ? 163 ASN B ND2 1 
ATOM   2675 N  N   . GLY B 1 130 ? -6.570  16.201  -37.449 1.00 81.93  ? 164 GLY B N   1 
ATOM   2676 C  CA  . GLY B 1 130 ? -5.393  16.751  -36.812 1.00 73.42  ? 164 GLY B CA  1 
ATOM   2677 C  C   . GLY B 1 130 ? -4.726  17.877  -37.571 1.00 72.19  ? 164 GLY B C   1 
ATOM   2678 O  O   . GLY B 1 130 ? -3.984  18.659  -36.963 1.00 72.67  ? 164 GLY B O   1 
ATOM   2679 N  N   . TRP B 1 131 ? -4.965  17.988  -38.875 1.00 65.58  ? 165 TRP B N   1 
ATOM   2680 C  CA  . TRP B 1 131 ? -4.293  19.007  -39.667 1.00 59.80  ? 165 TRP B CA  1 
ATOM   2681 C  C   . TRP B 1 131 ? -4.857  20.392  -39.365 1.00 70.88  ? 165 TRP B C   1 
ATOM   2682 O  O   . TRP B 1 131 ? -6.010  20.545  -38.953 1.00 72.12  ? 165 TRP B O   1 
ATOM   2683 C  CB  . TRP B 1 131 ? -4.422  18.697  -41.158 1.00 63.78  ? 165 TRP B CB  1 
ATOM   2684 C  CG  . TRP B 1 131 ? -3.645  17.486  -41.576 1.00 66.86  ? 165 TRP B CG  1 
ATOM   2685 C  CD1 . TRP B 1 131 ? -4.139  16.236  -41.813 1.00 63.43  ? 165 TRP B CD1 1 
ATOM   2686 C  CD2 . TRP B 1 131 ? -2.231  17.406  -41.791 1.00 62.10  ? 165 TRP B CD2 1 
ATOM   2687 N  NE1 . TRP B 1 131 ? -3.121  15.385  -42.170 1.00 58.32  ? 165 TRP B NE1 1 
ATOM   2688 C  CE2 . TRP B 1 131 ? -1.939  16.079  -42.164 1.00 63.92  ? 165 TRP B CE2 1 
ATOM   2689 C  CE3 . TRP B 1 131 ? -1.183  18.329  -41.709 1.00 58.63  ? 165 TRP B CE3 1 
ATOM   2690 C  CZ2 . TRP B 1 131 ? -0.645  15.651  -42.453 1.00 60.45  ? 165 TRP B CZ2 1 
ATOM   2691 C  CZ3 . TRP B 1 131 ? 0.101   17.902  -41.996 1.00 63.30  ? 165 TRP B CZ3 1 
ATOM   2692 C  CH2 . TRP B 1 131 ? 0.359   16.576  -42.363 1.00 59.60  ? 165 TRP B CH2 1 
ATOM   2693 N  N   . VAL B 1 132 ? -4.020  21.409  -39.577 1.00 67.99  ? 166 VAL B N   1 
ATOM   2694 C  CA  . VAL B 1 132 ? -4.401  22.774  -39.243 1.00 74.26  ? 166 VAL B CA  1 
ATOM   2695 C  C   . VAL B 1 132 ? -5.431  23.290  -40.243 1.00 74.83  ? 166 VAL B C   1 
ATOM   2696 O  O   . VAL B 1 132 ? -5.443  22.906  -41.421 1.00 75.02  ? 166 VAL B O   1 
ATOM   2697 C  CB  . VAL B 1 132 ? -3.158  23.684  -39.194 1.00 71.78  ? 166 VAL B CB  1 
ATOM   2698 C  CG1 . VAL B 1 132 ? -2.611  23.939  -40.593 1.00 60.83  ? 166 VAL B CG1 1 
ATOM   2699 C  CG2 . VAL B 1 132 ? -3.473  24.995  -38.482 1.00 71.53  ? 166 VAL B CG2 1 
ATOM   2700 N  N   . ASP B 1 133 ? -6.320  24.147  -39.761 1.00 68.89  ? 167 ASP B N   1 
ATOM   2701 C  CA  . ASP B 1 133 ? -7.272  24.813  -40.638 1.00 80.00  ? 167 ASP B CA  1 
ATOM   2702 C  C   . ASP B 1 133 ? -6.518  25.766  -41.555 1.00 80.17  ? 167 ASP B C   1 
ATOM   2703 O  O   . ASP B 1 133 ? -5.808  26.651  -41.060 1.00 75.69  ? 167 ASP B O   1 
ATOM   2704 C  CB  . ASP B 1 133 ? -8.316  25.570  -39.821 1.00 89.75  ? 167 ASP B CB  1 
ATOM   2705 C  CG  . ASP B 1 133 ? -9.438  24.674  -39.334 1.00 92.39  ? 167 ASP B CG  1 
ATOM   2706 O  OD1 . ASP B 1 133 ? -10.078 24.009  -40.176 1.00 91.60  ? 167 ASP B OD1 1 
ATOM   2707 O  OD2 . ASP B 1 133 ? -9.681  24.636  -38.109 1.00 85.16  ? 167 ASP B OD2 1 
ATOM   2708 N  N   . PRO B 1 134 ? -6.626  25.623  -42.878 1.00 77.75  ? 168 PRO B N   1 
ATOM   2709 C  CA  . PRO B 1 134 ? -5.895  26.534  -43.776 1.00 77.02  ? 168 PRO B CA  1 
ATOM   2710 C  C   . PRO B 1 134 ? -6.279  27.992  -43.603 1.00 87.19  ? 168 PRO B C   1 
ATOM   2711 O  O   . PRO B 1 134 ? -5.491  28.871  -43.973 1.00 82.80  ? 168 PRO B O   1 
ATOM   2712 C  CB  . PRO B 1 134 ? -6.259  26.019  -45.176 1.00 84.43  ? 168 PRO B CB  1 
ATOM   2713 C  CG  . PRO B 1 134 ? -6.730  24.613  -44.965 1.00 86.26  ? 168 PRO B CG  1 
ATOM   2714 C  CD  . PRO B 1 134 ? -7.376  24.594  -43.616 1.00 78.15  ? 168 PRO B CD  1 
ATOM   2715 N  N   . ALA B 1 135 ? -7.458  28.278  -43.049 1.00 93.30  ? 169 ALA B N   1 
ATOM   2716 C  CA  . ALA B 1 135 ? -7.865  29.651  -42.776 1.00 92.25  ? 169 ALA B CA  1 
ATOM   2717 C  C   . ALA B 1 135 ? -7.136  30.259  -41.585 1.00 96.27  ? 169 ALA B C   1 
ATOM   2718 O  O   . ALA B 1 135 ? -7.353  31.439  -41.289 1.00 104.50 ? 169 ALA B O   1 
ATOM   2719 C  CB  . ALA B 1 135 ? -9.376  29.714  -42.546 1.00 92.82  ? 169 ALA B CB  1 
ATOM   2720 N  N   . THR B 1 136 ? -6.291  29.492  -40.895 1.00 86.57  ? 170 THR B N   1 
ATOM   2721 C  CA  . THR B 1 136 ? -5.496  30.005  -39.791 1.00 80.57  ? 170 THR B CA  1 
ATOM   2722 C  C   . THR B 1 136 ? -4.001  29.999  -40.074 1.00 82.86  ? 170 THR B C   1 
ATOM   2723 O  O   . THR B 1 136 ? -3.243  30.609  -39.312 1.00 83.41  ? 170 THR B O   1 
ATOM   2724 C  CB  . THR B 1 136 ? -5.768  29.196  -38.513 1.00 81.72  ? 170 THR B CB  1 
ATOM   2725 O  OG1 . THR B 1 136 ? -5.349  27.838  -38.704 1.00 82.85  ? 170 THR B OG1 1 
ATOM   2726 C  CG2 . THR B 1 136 ? -7.249  29.224  -38.175 1.00 84.45  ? 170 THR B CG2 1 
ATOM   2727 N  N   . ALA B 1 137 ? -3.561  29.335  -41.140 1.00 85.20  ? 171 ALA B N   1 
ATOM   2728 C  CA  . ALA B 1 137 ? -2.158  29.310  -41.530 1.00 75.89  ? 171 ALA B CA  1 
ATOM   2729 C  C   . ALA B 1 137 ? -1.988  30.036  -42.859 1.00 81.73  ? 171 ALA B C   1 
ATOM   2730 O  O   . ALA B 1 137 ? -1.803  29.392  -43.900 1.00 89.44  ? 171 ALA B O   1 
ATOM   2731 C  CB  . ALA B 1 137 ? -1.651  27.871  -41.631 1.00 68.73  ? 171 ALA B CB  1 
ATOM   2732 N  N   . PRO B 1 138 ? -2.038  31.371  -42.868 1.00 85.85  ? 172 PRO B N   1 
ATOM   2733 C  CA  . PRO B 1 138 ? -2.041  32.113  -44.137 1.00 91.14  ? 172 PRO B CA  1 
ATOM   2734 C  C   . PRO B 1 138 ? -0.645  32.170  -44.740 1.00 94.34  ? 172 PRO B C   1 
ATOM   2735 O  O   . PRO B 1 138 ? 0.292   32.674  -44.117 1.00 96.29  ? 172 PRO B O   1 
ATOM   2736 C  CB  . PRO B 1 138 ? -2.536  33.505  -43.728 1.00 85.83  ? 172 PRO B CB  1 
ATOM   2737 C  CG  . PRO B 1 138 ? -2.084  33.653  -42.312 1.00 81.95  ? 172 PRO B CG  1 
ATOM   2738 C  CD  . PRO B 1 138 ? -2.040  32.271  -41.700 1.00 86.26  ? 172 PRO B CD  1 
ATOM   2739 N  N   . ASN B 1 139 ? -0.515  31.649  -45.960 1.00 100.96 ? 173 ASN B N   1 
ATOM   2740 C  CA  . ASN B 1 139 ? 0.747   31.659  -46.698 1.00 107.29 ? 173 ASN B CA  1 
ATOM   2741 C  C   . ASN B 1 139 ? 1.874   31.056  -45.864 1.00 97.98  ? 173 ASN B C   1 
ATOM   2742 O  O   . ASN B 1 139 ? 2.975   31.600  -45.771 1.00 97.96  ? 173 ASN B O   1 
ATOM   2743 C  CB  . ASN B 1 139 ? 1.100   33.075  -47.160 1.00 114.97 ? 173 ASN B CB  1 
ATOM   2744 C  CG  . ASN B 1 139 ? 2.075   33.083  -48.321 1.00 115.70 ? 173 ASN B CG  1 
ATOM   2745 O  OD1 . ASN B 1 139 ? 2.505   32.032  -48.797 1.00 104.67 ? 173 ASN B OD1 1 
ATOM   2746 N  ND2 . ASN B 1 139 ? 2.430   34.276  -48.784 1.00 115.99 ? 173 ASN B ND2 1 
ATOM   2747 N  N   . PHE B 1 140 ? 1.584   29.915  -45.239 1.00 90.21  ? 174 PHE B N   1 
ATOM   2748 C  CA  . PHE B 1 140 ? 2.578   29.251  -44.406 1.00 81.25  ? 174 PHE B CA  1 
ATOM   2749 C  C   . PHE B 1 140 ? 3.677   28.577  -45.217 1.00 81.87  ? 174 PHE B C   1 
ATOM   2750 O  O   . PHE B 1 140 ? 4.611   28.031  -44.619 1.00 73.98  ? 174 PHE B O   1 
ATOM   2751 C  CB  . PHE B 1 140 ? 1.902   28.226  -43.495 1.00 76.72  ? 174 PHE B CB  1 
ATOM   2752 C  CG  . PHE B 1 140 ? 1.717   28.703  -42.082 1.00 72.06  ? 174 PHE B CG  1 
ATOM   2753 C  CD1 . PHE B 1 140 ? 1.465   30.038  -41.816 1.00 79.94  ? 174 PHE B CD1 1 
ATOM   2754 C  CD2 . PHE B 1 140 ? 1.807   27.818  -41.021 1.00 63.49  ? 174 PHE B CD2 1 
ATOM   2755 C  CE1 . PHE B 1 140 ? 1.297   30.481  -40.517 1.00 72.89  ? 174 PHE B CE1 1 
ATOM   2756 C  CE2 . PHE B 1 140 ? 1.640   28.254  -39.720 1.00 70.45  ? 174 PHE B CE2 1 
ATOM   2757 C  CZ  . PHE B 1 140 ? 1.385   29.588  -39.468 1.00 70.00  ? 174 PHE B CZ  1 
ATOM   2758 N  N   . GLY B 1 141 ? 3.591   28.602  -46.545 1.00 87.09  ? 175 GLY B N   1 
ATOM   2759 C  CA  . GLY B 1 141 ? 4.623   28.056  -47.391 1.00 91.76  ? 175 GLY B CA  1 
ATOM   2760 C  C   . GLY B 1 141 ? 4.797   26.562  -47.219 1.00 92.95  ? 175 GLY B C   1 
ATOM   2761 O  O   . GLY B 1 141 ? 3.832   25.791  -47.237 1.00 91.89  ? 175 GLY B O   1 
ATOM   2762 N  N   . PRO B 1 142 ? 6.047   26.123  -47.044 1.00 77.16  ? 176 PRO B N   1 
ATOM   2763 C  CA  . PRO B 1 142 ? 6.309   24.682  -46.904 1.00 69.72  ? 176 PRO B CA  1 
ATOM   2764 C  C   . PRO B 1 142 ? 5.895   24.107  -45.560 1.00 66.77  ? 176 PRO B C   1 
ATOM   2765 O  O   . PRO B 1 142 ? 5.896   22.879  -45.411 1.00 65.15  ? 176 PRO B O   1 
ATOM   2766 C  CB  . PRO B 1 142 ? 7.827   24.586  -47.100 1.00 75.65  ? 176 PRO B CB  1 
ATOM   2767 C  CG  . PRO B 1 142 ? 8.338   25.908  -46.630 1.00 76.75  ? 176 PRO B CG  1 
ATOM   2768 C  CD  . PRO B 1 142 ? 7.286   26.920  -47.002 1.00 72.90  ? 176 PRO B CD  1 
ATOM   2769 N  N   . LEU B 1 143 ? 5.541   24.942  -44.586 1.00 69.21  ? 177 LEU B N   1 
ATOM   2770 C  CA  . LEU B 1 143 ? 5.199   24.451  -43.257 1.00 65.91  ? 177 LEU B CA  1 
ATOM   2771 C  C   . LEU B 1 143 ? 3.835   23.771  -43.280 1.00 70.88  ? 177 LEU B C   1 
ATOM   2772 O  O   . LEU B 1 143 ? 2.825   24.396  -43.621 1.00 72.74  ? 177 LEU B O   1 
ATOM   2773 C  CB  . LEU B 1 143 ? 5.209   25.598  -42.250 1.00 61.48  ? 177 LEU B CB  1 
ATOM   2774 C  CG  . LEU B 1 143 ? 6.512   26.389  -42.107 1.00 68.66  ? 177 LEU B CG  1 
ATOM   2775 C  CD1 . LEU B 1 143 ? 6.483   27.237  -40.845 1.00 60.03  ? 177 LEU B CD1 1 
ATOM   2776 C  CD2 . LEU B 1 143 ? 7.718   25.461  -42.104 1.00 58.42  ? 177 LEU B CD2 1 
ATOM   2777 N  N   . ARG B 1 144 ? 3.826   22.501  -42.879 1.00 65.17  ? 178 ARG B N   1 
ATOM   2778 C  CA  . ARG B 1 144 ? 2.595   21.746  -42.786 1.00 64.84  ? 178 ARG B CA  1 
ATOM   2779 C  C   . ARG B 1 144 ? 2.380   21.473  -41.320 1.00 64.32  ? 178 ARG B C   1 
ATOM   2780 O  O   . ARG B 1 144 ? 2.937   20.541  -40.769 1.00 55.96  ? 178 ARG B O   1 
ATOM   2781 C  CB  . ARG B 1 144 ? 2.696   20.449  -43.571 1.00 58.59  ? 178 ARG B CB  1 
ATOM   2782 C  CG  . ARG B 1 144 ? 3.072   20.632  -45.025 1.00 69.30  ? 178 ARG B CG  1 
ATOM   2783 C  CD  . ARG B 1 144 ? 2.103   21.565  -45.722 1.00 77.65  ? 178 ARG B CD  1 
ATOM   2784 N  NE  . ARG B 1 144 ? 2.551   21.885  -47.070 1.00 97.46  ? 178 ARG B NE  1 
ATOM   2785 C  CZ  . ARG B 1 144 ? 1.979   22.793  -47.850 1.00 97.04  ? 178 ARG B CZ  1 
ATOM   2786 N  NH1 . ARG B 1 144 ? 0.935   23.482  -47.413 1.00 88.29  ? 178 ARG B NH1 1 
ATOM   2787 N  NH2 . ARG B 1 144 ? 2.455   23.017  -49.065 1.00 89.30  ? 178 ARG B NH2 1 
ATOM   2788 N  N   . VAL B 1 145 ? 1.563   22.282  -40.685 1.00 66.10  ? 179 VAL B N   1 
ATOM   2789 C  CA  . VAL B 1 145 ? 1.322   22.175  -39.250 1.00 52.96  ? 179 VAL B CA  1 
ATOM   2790 C  C   . VAL B 1 145 ? 0.289   21.085  -38.996 1.00 63.30  ? 179 VAL B C   1 
ATOM   2791 O  O   . VAL B 1 145 ? -0.749  21.025  -39.666 1.00 62.56  ? 179 VAL B O   1 
ATOM   2792 C  CB  . VAL B 1 145 ? 0.864   23.524  -38.676 1.00 51.53  ? 179 VAL B CB  1 
ATOM   2793 C  CG1 . VAL B 1 145 ? 0.652   23.418  -37.172 1.00 55.56  ? 179 VAL B CG1 1 
ATOM   2794 C  CG2 . VAL B 1 145 ? 1.877   24.609  -39.004 1.00 49.38  ? 179 VAL B CG2 1 
ATOM   2795 N  N   . PHE B 1 146 ? 0.570   20.224  -38.019 1.00 57.37  ? 180 PHE B N   1 
ATOM   2796 C  CA  . PHE B 1 146 ? -0.300  19.107  -37.683 1.00 55.37  ? 180 PHE B CA  1 
ATOM   2797 C  C   . PHE B 1 146 ? -0.370  18.961  -36.171 1.00 58.29  ? 180 PHE B C   1 
ATOM   2798 O  O   . PHE B 1 146 ? 0.637   19.131  -35.477 1.00 59.01  ? 180 PHE B O   1 
ATOM   2799 C  CB  . PHE B 1 146 ? 0.203   17.804  -38.323 1.00 60.23  ? 180 PHE B CB  1 
ATOM   2800 C  CG  . PHE B 1 146 ? -0.522  16.575  -37.855 1.00 56.31  ? 180 PHE B CG  1 
ATOM   2801 C  CD1 . PHE B 1 146 ? -1.768  16.253  -38.366 1.00 61.38  ? 180 PHE B CD1 1 
ATOM   2802 C  CD2 . PHE B 1 146 ? 0.046   15.737  -36.910 1.00 48.83  ? 180 PHE B CD2 1 
ATOM   2803 C  CE1 . PHE B 1 146 ? -2.437  15.120  -37.940 1.00 64.53  ? 180 PHE B CE1 1 
ATOM   2804 C  CE2 . PHE B 1 146 ? -0.617  14.604  -36.481 1.00 56.72  ? 180 PHE B CE2 1 
ATOM   2805 C  CZ  . PHE B 1 146 ? -1.860  14.295  -36.995 1.00 60.51  ? 180 PHE B CZ  1 
ATOM   2806 N  N   . TYR B 1 147 ? -1.561  18.647  -35.666 1.00 65.61  ? 181 TYR B N   1 
ATOM   2807 C  CA  . TYR B 1 147 ? -1.770  18.448  -34.236 1.00 67.05  ? 181 TYR B CA  1 
ATOM   2808 C  C   . TYR B 1 147 ? -2.098  16.986  -33.969 1.00 63.83  ? 181 TYR B C   1 
ATOM   2809 O  O   . TYR B 1 147 ? -3.186  16.523  -34.346 1.00 68.28  ? 181 TYR B O   1 
ATOM   2810 C  CB  . TYR B 1 147 ? -2.892  19.350  -33.721 1.00 70.20  ? 181 TYR B CB  1 
ATOM   2811 C  CG  . TYR B 1 147 ? -3.281  19.094  -32.282 1.00 72.79  ? 181 TYR B CG  1 
ATOM   2812 C  CD1 . TYR B 1 147 ? -2.367  19.275  -31.253 1.00 70.46  ? 181 TYR B CD1 1 
ATOM   2813 C  CD2 . TYR B 1 147 ? -4.563  18.676  -31.952 1.00 66.28  ? 181 TYR B CD2 1 
ATOM   2814 C  CE1 . TYR B 1 147 ? -2.717  19.045  -29.937 1.00 67.89  ? 181 TYR B CE1 1 
ATOM   2815 C  CE2 . TYR B 1 147 ? -4.923  18.443  -30.638 1.00 67.37  ? 181 TYR B CE2 1 
ATOM   2816 C  CZ  . TYR B 1 147 ? -3.996  18.629  -29.635 1.00 67.22  ? 181 TYR B CZ  1 
ATOM   2817 O  OH  . TYR B 1 147 ? -4.348  18.398  -28.325 1.00 71.06  ? 181 TYR B OH  1 
ATOM   2818 N  N   . PRO B 1 148 ? -1.208  16.226  -33.334 1.00 66.37  ? 182 PRO B N   1 
ATOM   2819 C  CA  . PRO B 1 148 ? -1.459  14.796  -33.099 1.00 65.28  ? 182 PRO B CA  1 
ATOM   2820 C  C   . PRO B 1 148 ? -2.214  14.472  -31.818 1.00 66.45  ? 182 PRO B C   1 
ATOM   2821 O  O   . PRO B 1 148 ? -2.350  13.288  -31.495 1.00 55.91  ? 182 PRO B O   1 
ATOM   2822 C  CB  . PRO B 1 148 ? -0.035  14.230  -33.033 1.00 56.49  ? 182 PRO B CB  1 
ATOM   2823 C  CG  . PRO B 1 148 ? 0.767   15.339  -32.433 1.00 51.96  ? 182 PRO B CG  1 
ATOM   2824 C  CD  . PRO B 1 148 ? 0.124   16.640  -32.860 1.00 57.19  ? 182 PRO B CD  1 
ATOM   2825 N  N   . GLY B 1 149 ? -2.705  15.470  -31.090 1.00 65.73  ? 183 GLY B N   1 
ATOM   2826 C  CA  . GLY B 1 149 ? -3.377  15.234  -29.836 1.00 62.00  ? 183 GLY B CA  1 
ATOM   2827 C  C   . GLY B 1 149 ? -2.461  15.473  -28.654 1.00 67.08  ? 183 GLY B C   1 
ATOM   2828 O  O   . GLY B 1 149 ? -1.267  15.750  -28.811 1.00 58.57  ? 183 GLY B O   1 
ATOM   2829 N  N   . PRO B 1 150 ? -3.006  15.376  -27.443 1.00 67.20  ? 184 PRO B N   1 
ATOM   2830 C  CA  . PRO B 1 150 ? -2.183  15.608  -26.248 1.00 66.11  ? 184 PRO B CA  1 
ATOM   2831 C  C   . PRO B 1 150 ? -1.098  14.551  -26.103 1.00 65.40  ? 184 PRO B C   1 
ATOM   2832 O  O   . PRO B 1 150 ? -1.334  13.356  -26.301 1.00 64.73  ? 184 PRO B O   1 
ATOM   2833 C  CB  . PRO B 1 150 ? -3.183  15.537  -25.086 1.00 61.11  ? 184 PRO B CB  1 
ATOM   2834 C  CG  . PRO B 1 150 ? -4.499  15.187  -25.660 1.00 78.73  ? 184 PRO B CG  1 
ATOM   2835 C  CD  . PRO B 1 150 ? -4.432  15.164  -27.144 1.00 72.35  ? 184 PRO B CD  1 
ATOM   2836 N  N   . GLY B 1 151 ? 0.102   15.008  -25.754 1.00 64.24  ? 185 GLY B N   1 
ATOM   2837 C  CA  . GLY B 1 151 ? 1.230   14.122  -25.536 1.00 63.10  ? 185 GLY B CA  1 
ATOM   2838 C  C   . GLY B 1 151 ? 2.166   14.646  -24.467 1.00 60.74  ? 185 GLY B C   1 
ATOM   2839 O  O   . GLY B 1 151 ? 1.875   14.536  -23.272 1.00 63.72  ? 185 GLY B O   1 
ATOM   2840 N  N   . HIS B 1 152 ? 3.301   15.214  -24.886 1.00 51.53  ? 186 HIS B N   1 
ATOM   2841 C  CA  . HIS B 1 152 ? 4.182   15.891  -23.939 1.00 54.81  ? 186 HIS B CA  1 
ATOM   2842 C  C   . HIS B 1 152 ? 3.451   17.030  -23.239 1.00 59.21  ? 186 HIS B C   1 
ATOM   2843 O  O   . HIS B 1 152 ? 3.665   17.280  -22.047 1.00 57.92  ? 186 HIS B O   1 
ATOM   2844 C  CB  . HIS B 1 152 ? 5.429   16.406  -24.658 1.00 51.10  ? 186 HIS B CB  1 
ATOM   2845 C  CG  . HIS B 1 152 ? 6.202   17.422  -23.877 1.00 50.00  ? 186 HIS B CG  1 
ATOM   2846 N  ND1 . HIS B 1 152 ? 7.108   17.076  -22.898 1.00 59.35  ? 186 HIS B ND1 1 
ATOM   2847 C  CD2 . HIS B 1 152 ? 6.206   18.775  -23.932 1.00 54.16  ? 186 HIS B CD2 1 
ATOM   2848 C  CE1 . HIS B 1 152 ? 7.636   18.172  -22.382 1.00 60.03  ? 186 HIS B CE1 1 
ATOM   2849 N  NE2 . HIS B 1 152 ? 7.105   19.216  -22.992 1.00 54.56  ? 186 HIS B NE2 1 
ATOM   2850 N  N   . THR B 1 153 ? 2.596   17.739  -23.971 1.00 53.10  ? 187 THR B N   1 
ATOM   2851 C  CA  . THR B 1 153 ? 1.622   18.661  -23.409 1.00 54.33  ? 187 THR B CA  1 
ATOM   2852 C  C   . THR B 1 153 ? 0.281   18.403  -24.082 1.00 62.56  ? 187 THR B C   1 
ATOM   2853 O  O   . THR B 1 153 ? 0.177   17.615  -25.026 1.00 60.82  ? 187 THR B O   1 
ATOM   2854 C  CB  . THR B 1 153 ? 2.035   20.130  -23.593 1.00 55.60  ? 187 THR B CB  1 
ATOM   2855 O  OG1 . THR B 1 153 ? 2.239   20.404  -24.984 1.00 60.69  ? 187 THR B OG1 1 
ATOM   2856 C  CG2 . THR B 1 153 ? 3.308   20.440  -22.817 1.00 59.58  ? 187 THR B CG2 1 
ATOM   2857 N  N   . SER B 1 154 ? -0.755  19.073  -23.586 1.00 55.02  ? 188 SER B N   1 
ATOM   2858 C  CA  . SER B 1 154 ? -2.079  18.947  -24.182 1.00 58.67  ? 188 SER B CA  1 
ATOM   2859 C  C   . SER B 1 154 ? -2.261  19.831  -25.407 1.00 60.32  ? 188 SER B C   1 
ATOM   2860 O  O   . SER B 1 154 ? -3.313  19.761  -26.051 1.00 64.81  ? 188 SER B O   1 
ATOM   2861 C  CB  . SER B 1 154 ? -3.156  19.272  -23.144 1.00 62.03  ? 188 SER B CB  1 
ATOM   2862 O  OG  . SER B 1 154 ? -3.312  18.203  -22.226 1.00 75.34  ? 188 SER B OG  1 
ATOM   2863 N  N   . ASP B 1 155 ? -1.264  20.649  -25.749 1.00 55.61  ? 189 ASP B N   1 
ATOM   2864 C  CA  . ASP B 1 155 ? -1.363  21.579  -26.865 1.00 59.56  ? 189 ASP B CA  1 
ATOM   2865 C  C   . ASP B 1 155 ? -0.200  21.450  -27.841 1.00 58.04  ? 189 ASP B C   1 
ATOM   2866 O  O   . ASP B 1 155 ? -0.068  22.290  -28.739 1.00 60.93  ? 189 ASP B O   1 
ATOM   2867 C  CB  . ASP B 1 155 ? -1.440  23.020  -26.350 1.00 58.98  ? 189 ASP B CB  1 
ATOM   2868 C  CG  . ASP B 1 155 ? -0.264  23.381  -25.462 1.00 64.37  ? 189 ASP B CG  1 
ATOM   2869 O  OD1 . ASP B 1 155 ? 0.052   22.596  -24.545 1.00 67.75  ? 189 ASP B OD1 1 
ATOM   2870 O  OD2 . ASP B 1 155 ? 0.351   24.444  -25.685 1.00 69.29  ? 189 ASP B OD2 1 
ATOM   2871 N  N   . ASN B 1 156 ? 0.643   20.430  -27.692 1.00 62.99  ? 190 ASN B N   1 
ATOM   2872 C  CA  . ASN B 1 156 ? 1.828   20.304  -28.530 1.00 62.61  ? 190 ASN B CA  1 
ATOM   2873 C  C   . ASN B 1 156 ? 1.435   20.048  -29.979 1.00 58.18  ? 190 ASN B C   1 
ATOM   2874 O  O   . ASN B 1 156 ? 0.609   19.176  -30.267 1.00 58.62  ? 190 ASN B O   1 
ATOM   2875 C  CB  . ASN B 1 156 ? 2.724   19.177  -28.018 1.00 52.06  ? 190 ASN B CB  1 
ATOM   2876 C  CG  . ASN B 1 156 ? 1.943   17.926  -27.662 1.00 60.86  ? 190 ASN B CG  1 
ATOM   2877 O  OD1 . ASN B 1 156 ? 0.727   17.862  -27.840 1.00 59.12  ? 190 ASN B OD1 1 
ATOM   2878 N  ND2 . ASN B 1 156 ? 2.646   16.917  -27.163 1.00 53.90  ? 190 ASN B ND2 1 
ATOM   2879 N  N   . ILE B 1 157 ? 2.029   20.811  -30.892 1.00 49.39  ? 191 ILE B N   1 
ATOM   2880 C  CA  . ILE B 1 157 ? 1.779   20.656  -32.317 1.00 56.82  ? 191 ILE B CA  1 
ATOM   2881 C  C   . ILE B 1 157 ? 3.106   20.400  -33.016 1.00 59.39  ? 191 ILE B C   1 
ATOM   2882 O  O   . ILE B 1 157 ? 4.164   20.864  -32.578 1.00 57.87  ? 191 ILE B O   1 
ATOM   2883 C  CB  . ILE B 1 157 ? 1.068   21.885  -32.923 1.00 52.86  ? 191 ILE B CB  1 
ATOM   2884 C  CG1 . ILE B 1 157 ? 1.811   23.169  -32.560 1.00 59.09  ? 191 ILE B CG1 1 
ATOM   2885 C  CG2 . ILE B 1 157 ? -0.362  21.963  -32.427 1.00 59.51  ? 191 ILE B CG2 1 
ATOM   2886 C  CD1 . ILE B 1 157 ? 1.283   24.404  -33.259 1.00 65.82  ? 191 ILE B CD1 1 
ATOM   2887 N  N   . THR B 1 158 ? 3.043   19.644  -34.106 1.00 55.70  ? 192 THR B N   1 
ATOM   2888 C  CA  . THR B 1 158 ? 4.213   19.292  -34.892 1.00 50.20  ? 192 THR B CA  1 
ATOM   2889 C  C   . THR B 1 158 ? 4.118   19.928  -36.273 1.00 54.67  ? 192 THR B C   1 
ATOM   2890 O  O   . THR B 1 158 ? 3.024   20.151  -36.798 1.00 53.73  ? 192 THR B O   1 
ATOM   2891 C  CB  . THR B 1 158 ? 4.349   17.774  -35.023 1.00 53.23  ? 192 THR B CB  1 
ATOM   2892 O  OG1 . THR B 1 158 ? 3.400   17.288  -35.981 1.00 50.64  ? 192 THR B OG1 1 
ATOM   2893 C  CG2 . THR B 1 158 ? 4.096   17.100  -33.682 1.00 44.43  ? 192 THR B CG2 1 
ATOM   2894 N  N   . VAL B 1 159 ? 5.277   20.222  -36.857 1.00 43.99  ? 193 VAL B N   1 
ATOM   2895 C  CA  . VAL B 1 159 ? 5.359   20.905  -38.143 1.00 50.29  ? 193 VAL B CA  1 
ATOM   2896 C  C   . VAL B 1 159 ? 6.201   20.066  -39.093 1.00 53.91  ? 193 VAL B C   1 
ATOM   2897 O  O   . VAL B 1 159 ? 7.298   19.625  -38.734 1.00 54.49  ? 193 VAL B O   1 
ATOM   2898 C  CB  . VAL B 1 159 ? 5.954   22.320  -38.007 1.00 51.73  ? 193 VAL B CB  1 
ATOM   2899 C  CG1 . VAL B 1 159 ? 5.824   23.076  -39.320 1.00 53.23  ? 193 VAL B CG1 1 
ATOM   2900 C  CG2 . VAL B 1 159 ? 5.274   23.082  -36.880 1.00 47.48  ? 193 VAL B CG2 1 
ATOM   2901 N  N   . GLY B 1 160 ? 5.688   19.851  -40.299 1.00 52.57  ? 194 GLY B N   1 
ATOM   2902 C  CA  . GLY B 1 160 ? 6.425   19.191  -41.366 1.00 47.81  ? 194 GLY B CA  1 
ATOM   2903 C  C   . GLY B 1 160 ? 6.719   20.185  -42.476 1.00 55.19  ? 194 GLY B C   1 
ATOM   2904 O  O   . GLY B 1 160 ? 5.856   20.985  -42.848 1.00 65.00  ? 194 GLY B O   1 
ATOM   2905 N  N   . ILE B 1 161 ? 7.941   20.133  -42.994 1.00 46.25  ? 195 ILE B N   1 
ATOM   2906 C  CA  . ILE B 1 161 ? 8.408   21.071  -44.007 1.00 52.32  ? 195 ILE B CA  1 
ATOM   2907 C  C   . ILE B 1 161 ? 8.244   20.417  -45.372 1.00 59.22  ? 195 ILE B C   1 
ATOM   2908 O  O   . ILE B 1 161 ? 8.799   19.340  -45.625 1.00 66.97  ? 195 ILE B O   1 
ATOM   2909 C  CB  . ILE B 1 161 ? 9.869   21.472  -43.761 1.00 55.47  ? 195 ILE B CB  1 
ATOM   2910 C  CG1 . ILE B 1 161 ? 10.122  21.648  -42.263 1.00 43.37  ? 195 ILE B CG1 1 
ATOM   2911 C  CG2 . ILE B 1 161 ? 10.207  22.742  -44.531 1.00 60.68  ? 195 ILE B CG2 1 
ATOM   2912 C  CD1 . ILE B 1 161 ? 11.488  22.189  -41.935 1.00 52.74  ? 195 ILE B CD1 1 
ATOM   2913 N  N   . ASP B 1 162 ? 7.486   21.065  -46.251 1.00 64.38  ? 196 ASP B N   1 
ATOM   2914 C  CA  . ASP B 1 162 ? 7.260   20.528  -47.584 1.00 62.96  ? 196 ASP B CA  1 
ATOM   2915 C  C   . ASP B 1 162 ? 8.541   20.573  -48.409 1.00 68.65  ? 196 ASP B C   1 
ATOM   2916 O  O   . ASP B 1 162 ? 9.363   21.483  -48.279 1.00 66.88  ? 196 ASP B O   1 
ATOM   2917 C  CB  . ASP B 1 162 ? 6.155   21.309  -48.294 1.00 61.78  ? 196 ASP B CB  1 
ATOM   2918 C  CG  . ASP B 1 162 ? 4.871   20.515  -48.424 1.00 85.70  ? 196 ASP B CG  1 
ATOM   2919 O  OD1 . ASP B 1 162 ? 4.646   19.607  -47.596 1.00 88.01  ? 196 ASP B OD1 1 
ATOM   2920 O  OD2 . ASP B 1 162 ? 4.086   20.799  -49.353 1.00 94.57  ? 196 ASP B OD2 1 
ATOM   2921 N  N   . GLY B 1 163 ? 8.703   19.569  -49.266 1.00 74.72  ? 197 GLY B N   1 
ATOM   2922 C  CA  . GLY B 1 163 ? 9.854   19.517  -50.146 1.00 66.78  ? 197 GLY B CA  1 
ATOM   2923 C  C   . GLY B 1 163 ? 11.168  19.226  -49.458 1.00 76.65  ? 197 GLY B C   1 
ATOM   2924 O  O   . GLY B 1 163 ? 12.222  19.634  -49.956 1.00 81.30  ? 197 GLY B O   1 
ATOM   2925 N  N   . THR B 1 164 ? 11.139  18.530  -48.324 1.00 74.22  ? 198 THR B N   1 
ATOM   2926 C  CA  . THR B 1 164 ? 12.361  18.177  -47.615 1.00 67.28  ? 198 THR B CA  1 
ATOM   2927 C  C   . THR B 1 164 ? 12.147  16.855  -46.889 1.00 62.28  ? 198 THR B C   1 
ATOM   2928 O  O   . THR B 1 164 ? 11.054  16.280  -46.903 1.00 67.49  ? 198 THR B O   1 
ATOM   2929 C  CB  . THR B 1 164 ? 12.785  19.289  -46.648 1.00 71.23  ? 198 THR B CB  1 
ATOM   2930 O  OG1 . THR B 1 164 ? 14.188  19.177  -46.374 1.00 79.53  ? 198 THR B OG1 1 
ATOM   2931 C  CG2 . THR B 1 164 ? 12.017  19.188  -45.345 1.00 63.05  ? 198 THR B CG2 1 
ATOM   2932 N  N   . ASP B 1 165 ? 13.212  16.377  -46.251 1.00 68.80  ? 199 ASP B N   1 
ATOM   2933 C  CA  . ASP B 1 165 ? 13.239  15.093  -45.565 1.00 65.43  ? 199 ASP B CA  1 
ATOM   2934 C  C   . ASP B 1 165 ? 12.827  15.183  -44.101 1.00 65.19  ? 199 ASP B C   1 
ATOM   2935 O  O   . ASP B 1 165 ? 12.768  14.150  -43.426 1.00 62.95  ? 199 ASP B O   1 
ATOM   2936 C  CB  . ASP B 1 165 ? 14.650  14.500  -45.658 1.00 65.60  ? 199 ASP B CB  1 
ATOM   2937 C  CG  . ASP B 1 165 ? 14.650  13.041  -46.051 1.00 83.90  ? 199 ASP B CG  1 
ATOM   2938 O  OD1 . ASP B 1 165 ? 13.660  12.584  -46.660 1.00 95.20  ? 199 ASP B OD1 1 
ATOM   2939 O  OD2 . ASP B 1 165 ? 15.653  12.355  -45.763 1.00 95.45  ? 199 ASP B OD2 1 
ATOM   2940 N  N   . ILE B 1 166 ? 12.531  16.379  -43.598 1.00 55.91  ? 200 ILE B N   1 
ATOM   2941 C  CA  . ILE B 1 166 ? 12.483  16.644  -42.165 1.00 55.54  ? 200 ILE B CA  1 
ATOM   2942 C  C   . ILE B 1 166 ? 11.046  16.859  -41.713 1.00 56.31  ? 200 ILE B C   1 
ATOM   2943 O  O   . ILE B 1 166 ? 10.245  17.489  -42.414 1.00 59.24  ? 200 ILE B O   1 
ATOM   2944 C  CB  . ILE B 1 166 ? 13.354  17.864  -41.808 1.00 58.69  ? 200 ILE B CB  1 
ATOM   2945 C  CG1 . ILE B 1 166 ? 14.693  17.782  -42.542 1.00 59.49  ? 200 ILE B CG1 1 
ATOM   2946 C  CG2 . ILE B 1 166 ? 13.565  17.951  -40.304 1.00 55.98  ? 200 ILE B CG2 1 
ATOM   2947 C  CD1 . ILE B 1 166 ? 15.139  19.090  -43.139 1.00 58.65  ? 200 ILE B CD1 1 
ATOM   2948 N  N   . ALA B 1 167 ? 10.729  16.332  -40.532 1.00 48.61  ? 201 ALA B N   1 
ATOM   2949 C  CA  . ALA B 1 167 ? 9.493   16.628  -39.821 1.00 49.03  ? 201 ALA B CA  1 
ATOM   2950 C  C   . ALA B 1 167 ? 9.851   16.964  -38.381 1.00 51.48  ? 201 ALA B C   1 
ATOM   2951 O  O   . ALA B 1 167 ? 10.608  16.227  -37.741 1.00 47.98  ? 201 ALA B O   1 
ATOM   2952 C  CB  . ALA B 1 167 ? 8.515   15.450  -39.872 1.00 42.75  ? 201 ALA B CB  1 
ATOM   2953 N  N   . PHE B 1 168 ? 9.318   18.075  -37.878 1.00 49.84  ? 202 PHE B N   1 
ATOM   2954 C  CA  . PHE B 1 168 ? 9.659   18.567  -36.547 1.00 51.38  ? 202 PHE B CA  1 
ATOM   2955 C  C   . PHE B 1 168 ? 8.645   18.035  -35.541 1.00 47.94  ? 202 PHE B C   1 
ATOM   2956 O  O   . PHE B 1 168 ? 7.463   18.388  -35.593 1.00 56.75  ? 202 PHE B O   1 
ATOM   2957 C  CB  . PHE B 1 168 ? 9.697   20.092  -36.529 1.00 45.84  ? 202 PHE B CB  1 
ATOM   2958 C  CG  . PHE B 1 168 ? 10.254  20.669  -35.258 1.00 43.78  ? 202 PHE B CG  1 
ATOM   2959 C  CD1 . PHE B 1 168 ? 11.565  20.423  -34.887 1.00 47.49  ? 202 PHE B CD1 1 
ATOM   2960 C  CD2 . PHE B 1 168 ? 9.466   21.456  -34.435 1.00 38.31  ? 202 PHE B CD2 1 
ATOM   2961 C  CE1 . PHE B 1 168 ? 12.082  20.951  -33.720 1.00 50.51  ? 202 PHE B CE1 1 
ATOM   2962 C  CE2 . PHE B 1 168 ? 9.978   21.988  -33.265 1.00 56.94  ? 202 PHE B CE2 1 
ATOM   2963 C  CZ  . PHE B 1 168 ? 11.287  21.735  -32.907 1.00 48.45  ? 202 PHE B CZ  1 
ATOM   2964 N  N   . GLY B 1 169 ? 9.110   17.191  -34.620 1.00 43.63  ? 203 GLY B N   1 
ATOM   2965 C  CA  . GLY B 1 169 ? 8.259   16.649  -33.581 1.00 48.60  ? 203 GLY B CA  1 
ATOM   2966 C  C   . GLY B 1 169 ? 8.186   17.463  -32.311 1.00 52.98  ? 203 GLY B C   1 
ATOM   2967 O  O   . GLY B 1 169 ? 7.392   17.137  -31.424 1.00 58.38  ? 203 GLY B O   1 
ATOM   2968 N  N   . GLY B 1 170 ? 8.993   18.515  -32.200 1.00 49.81  ? 204 GLY B N   1 
ATOM   2969 C  CA  . GLY B 1 170 ? 8.988   19.341  -31.010 1.00 49.47  ? 204 GLY B CA  1 
ATOM   2970 C  C   . GLY B 1 170 ? 9.467   18.574  -29.793 1.00 52.61  ? 204 GLY B C   1 
ATOM   2971 O  O   . GLY B 1 170 ? 10.327  17.690  -29.872 1.00 55.08  ? 204 GLY B O   1 
ATOM   2972 N  N   . CYS B 1 171 ? 8.898   18.920  -28.640 1.00 44.67  ? 205 CYS B N   1 
ATOM   2973 C  CA  . CYS B 1 171 ? 9.202   18.223  -27.397 1.00 50.50  ? 205 CYS B CA  1 
ATOM   2974 C  C   . CYS B 1 171 ? 8.423   16.925  -27.242 1.00 47.10  ? 205 CYS B C   1 
ATOM   2975 O  O   . CYS B 1 171 ? 8.605   16.228  -26.238 1.00 48.03  ? 205 CYS B O   1 
ATOM   2976 C  CB  . CYS B 1 171 ? 8.922   19.134  -26.199 1.00 52.19  ? 205 CYS B CB  1 
ATOM   2977 S  SG  . CYS B 1 171 ? 9.875   20.667  -26.194 1.00 59.05  ? 205 CYS B SG  1 
ATOM   2978 N  N   . LEU B 1 172 ? 7.566   16.584  -28.206 1.00 52.51  ? 206 LEU B N   1 
ATOM   2979 C  CA  . LEU B 1 172 ? 6.783   15.357  -28.104 1.00 52.91  ? 206 LEU B CA  1 
ATOM   2980 C  C   . LEU B 1 172 ? 7.642   14.127  -28.371 1.00 51.77  ? 206 LEU B C   1 
ATOM   2981 O  O   . LEU B 1 172 ? 7.473   13.091  -27.718 1.00 54.01  ? 206 LEU B O   1 
ATOM   2982 C  CB  . LEU B 1 172 ? 5.603   15.412  -29.074 1.00 46.55  ? 206 LEU B CB  1 
ATOM   2983 C  CG  . LEU B 1 172 ? 4.868   14.101  -29.360 1.00 51.28  ? 206 LEU B CG  1 
ATOM   2984 C  CD1 . LEU B 1 172 ? 3.763   13.871  -28.340 1.00 53.96  ? 206 LEU B CD1 1 
ATOM   2985 C  CD2 . LEU B 1 172 ? 4.309   14.099  -30.775 1.00 52.75  ? 206 LEU B CD2 1 
ATOM   2986 N  N   . ILE B 1 173 ? 8.572   14.224  -29.316 1.00 54.92  ? 207 ILE B N   1 
ATOM   2987 C  CA  . ILE B 1 173 ? 9.384   13.092  -29.745 1.00 51.58  ? 207 ILE B CA  1 
ATOM   2988 C  C   . ILE B 1 173 ? 10.770  13.202  -29.128 1.00 52.89  ? 207 ILE B C   1 
ATOM   2989 O  O   . ILE B 1 173 ? 11.371  14.283  -29.101 1.00 61.92  ? 207 ILE B O   1 
ATOM   2990 C  CB  . ILE B 1 173 ? 9.469   13.027  -31.283 1.00 51.64  ? 207 ILE B CB  1 
ATOM   2991 C  CG1 . ILE B 1 173 ? 8.066   13.031  -31.893 1.00 52.27  ? 207 ILE B CG1 1 
ATOM   2992 C  CG2 . ILE B 1 173 ? 10.244  11.795  -31.728 1.00 43.84  ? 207 ILE B CG2 1 
ATOM   2993 C  CD1 . ILE B 1 173 ? 7.203   11.870  -31.448 1.00 51.97  ? 207 ILE B CD1 1 
ATOM   2994 N  N   . LYS B 1 174 ? 11.276  12.080  -28.624 1.00 58.96  ? 208 LYS B N   1 
ATOM   2995 C  CA  . LYS B 1 174 ? 12.648  11.957  -28.161 1.00 53.76  ? 208 LYS B CA  1 
ATOM   2996 C  C   . LYS B 1 174 ? 13.398  10.975  -29.052 1.00 60.23  ? 208 LYS B C   1 
ATOM   2997 O  O   . LYS B 1 174 ? 12.799  10.124  -29.716 1.00 61.24  ? 208 LYS B O   1 
ATOM   2998 C  CB  . LYS B 1 174 ? 12.701  11.499  -26.699 1.00 54.29  ? 208 LYS B CB  1 
ATOM   2999 C  CG  . LYS B 1 174 ? 11.607  12.092  -25.824 1.00 63.32  ? 208 LYS B CG  1 
ATOM   3000 C  CD  . LYS B 1 174 ? 11.967  13.497  -25.362 1.00 72.35  ? 208 LYS B CD  1 
ATOM   3001 C  CE  . LYS B 1 174 ? 10.741  14.242  -24.859 1.00 58.46  ? 208 LYS B CE  1 
ATOM   3002 N  NZ  . LYS B 1 174 ? 11.091  15.551  -24.240 1.00 59.97  ? 208 LYS B NZ  1 
ATOM   3003 N  N   . ASP B 1 175 ? 14.723  11.102  -29.066 1.00 62.84  ? 209 ASP B N   1 
ATOM   3004 C  CA  . ASP B 1 175 ? 15.533  10.283  -29.954 1.00 64.75  ? 209 ASP B CA  1 
ATOM   3005 C  C   . ASP B 1 175 ? 15.565  8.832   -29.469 1.00 68.63  ? 209 ASP B C   1 
ATOM   3006 O  O   . ASP B 1 175 ? 15.189  8.512   -28.337 1.00 67.02  ? 209 ASP B O   1 
ATOM   3007 C  CB  . ASP B 1 175 ? 16.947  10.853  -30.074 1.00 71.70  ? 209 ASP B CB  1 
ATOM   3008 C  CG  . ASP B 1 175 ? 17.836  10.474  -28.907 1.00 71.93  ? 209 ASP B CG  1 
ATOM   3009 O  OD1 . ASP B 1 175 ? 17.385  10.585  -27.748 1.00 72.53  ? 209 ASP B OD1 1 
ATOM   3010 O  OD2 . ASP B 1 175 ? 18.990  10.065  -29.151 1.00 75.74  ? 209 ASP B OD2 1 
ATOM   3011 N  N   . SER B 1 176 ? 16.026  7.945   -30.356 1.00 70.55  ? 210 SER B N   1 
ATOM   3012 C  CA  . SER B 1 176 ? 15.971  6.513   -30.076 1.00 70.01  ? 210 SER B CA  1 
ATOM   3013 C  C   . SER B 1 176 ? 16.911  6.111   -28.946 1.00 66.47  ? 210 SER B C   1 
ATOM   3014 O  O   . SER B 1 176 ? 16.654  5.118   -28.256 1.00 73.58  ? 210 SER B O   1 
ATOM   3015 C  CB  . SER B 1 176 ? 16.295  5.720   -31.342 1.00 59.68  ? 210 SER B CB  1 
ATOM   3016 O  OG  . SER B 1 176 ? 17.353  6.325   -32.066 1.00 66.12  ? 210 SER B OG  1 
ATOM   3017 N  N   . LYS B 1 177 ? 17.993  6.854   -28.741 1.00 73.37  ? 211 LYS B N   1 
ATOM   3018 C  CA  . LYS B 1 177 ? 18.959  6.542   -27.687 1.00 76.44  ? 211 LYS B CA  1 
ATOM   3019 C  C   . LYS B 1 177 ? 18.651  7.342   -26.422 1.00 80.14  ? 211 LYS B C   1 
ATOM   3020 O  O   . LYS B 1 177 ? 19.467  8.115   -25.920 1.00 93.10  ? 211 LYS B O   1 
ATOM   3021 C  CB  . LYS B 1 177 ? 20.380  6.802   -28.178 1.00 79.58  ? 211 LYS B CB  1 
ATOM   3022 C  CG  . LYS B 1 177 ? 20.640  6.346   -29.604 1.00 81.30  ? 211 LYS B CG  1 
ATOM   3023 C  CD  . LYS B 1 177 ? 21.911  6.969   -30.160 1.00 78.15  ? 211 LYS B CD  1 
ATOM   3024 C  CE  . LYS B 1 177 ? 21.754  8.469   -30.351 1.00 82.23  ? 211 LYS B CE  1 
ATOM   3025 N  NZ  . LYS B 1 177 ? 21.049  8.798   -31.621 1.00 78.18  ? 211 LYS B NZ  1 
ATOM   3026 N  N   . ALA B 1 178 ? 17.441  7.141   -25.906 1.00 77.58  ? 212 ALA B N   1 
ATOM   3027 C  CA  . ALA B 1 178 ? 17.000  7.817   -24.695 1.00 76.45  ? 212 ALA B CA  1 
ATOM   3028 C  C   . ALA B 1 178 ? 15.952  6.961   -24.001 1.00 80.87  ? 212 ALA B C   1 
ATOM   3029 O  O   . ALA B 1 178 ? 15.051  6.424   -24.649 1.00 79.26  ? 212 ALA B O   1 
ATOM   3030 C  CB  . ALA B 1 178 ? 16.430  9.206   -25.000 1.00 71.99  ? 212 ALA B CB  1 
ATOM   3031 N  N   . LYS B 1 179 ? 16.076  6.842   -22.680 1.00 88.72  ? 213 LYS B N   1 
ATOM   3032 C  CA  . LYS B 1 179 ? 15.132  6.049   -21.904 1.00 92.94  ? 213 LYS B CA  1 
ATOM   3033 C  C   . LYS B 1 179 ? 14.370  6.942   -20.931 1.00 91.66  ? 213 LYS B C   1 
ATOM   3034 O  O   . LYS B 1 179 ? 14.388  6.715   -19.716 1.00 94.15  ? 213 LYS B O   1 
ATOM   3035 C  CB  . LYS B 1 179 ? 15.867  4.919   -21.173 1.00 96.44  ? 213 LYS B CB  1 
ATOM   3036 C  CG  . LYS B 1 179 ? 14.964  3.870   -20.536 1.00 101.64 ? 213 LYS B CG  1 
ATOM   3037 C  CD  . LYS B 1 179 ? 13.872  3.418   -21.486 1.00 99.27  ? 213 LYS B CD  1 
ATOM   3038 C  CE  . LYS B 1 179 ? 12.656  2.928   -20.719 1.00 90.81  ? 213 LYS B CE  1 
ATOM   3039 N  NZ  . LYS B 1 179 ? 11.974  4.033   -19.988 1.00 95.87  ? 213 LYS B NZ  1 
ATOM   3040 N  N   . SER B 1 180 ? 13.704  7.967   -21.464 1.00 82.52  ? 214 SER B N   1 
ATOM   3041 C  CA  . SER B 1 180 ? 12.892  8.889   -20.681 1.00 70.30  ? 214 SER B CA  1 
ATOM   3042 C  C   . SER B 1 180 ? 12.171  9.834   -21.630 1.00 65.18  ? 214 SER B C   1 
ATOM   3043 O  O   . SER B 1 180 ? 12.743  10.259  -22.637 1.00 65.65  ? 214 SER B O   1 
ATOM   3044 C  CB  . SER B 1 180 ? 13.744  9.694   -19.689 1.00 70.92  ? 214 SER B CB  1 
ATOM   3045 O  OG  . SER B 1 180 ? 12.948  10.617  -18.967 1.00 71.68  ? 214 SER B OG  1 
ATOM   3046 N  N   . LEU B 1 181 ? 10.923  10.159  -21.304 1.00 59.58  ? 215 LEU B N   1 
ATOM   3047 C  CA  . LEU B 1 181 ? 10.155  11.132  -22.067 1.00 68.96  ? 215 LEU B CA  1 
ATOM   3048 C  C   . LEU B 1 181 ? 10.361  12.559  -21.572 1.00 60.04  ? 215 LEU B C   1 
ATOM   3049 O  O   . LEU B 1 181 ? 9.594   13.452  -21.947 1.00 63.65  ? 215 LEU B O   1 
ATOM   3050 C  CB  . LEU B 1 181 ? 8.667   10.773  -22.037 1.00 67.47  ? 215 LEU B CB  1 
ATOM   3051 C  CG  . LEU B 1 181 ? 8.282   9.466   -22.732 1.00 61.36  ? 215 LEU B CG  1 
ATOM   3052 C  CD1 . LEU B 1 181 ? 6.990   8.910   -22.158 1.00 67.41  ? 215 LEU B CD1 1 
ATOM   3053 C  CD2 . LEU B 1 181 ? 8.157   9.678   -24.233 1.00 54.88  ? 215 LEU B CD2 1 
ATOM   3054 N  N   . GLY B 1 182 ? 11.370  12.788  -20.735 1.00 60.05  ? 216 GLY B N   1 
ATOM   3055 C  CA  . GLY B 1 182 ? 11.706  14.124  -20.286 1.00 66.05  ? 216 GLY B CA  1 
ATOM   3056 C  C   . GLY B 1 182 ? 10.724  14.721  -19.301 1.00 63.46  ? 216 GLY B C   1 
ATOM   3057 O  O   . GLY B 1 182 ? 10.467  14.148  -18.237 1.00 63.26  ? 216 GLY B O   1 
ATOM   3058 N  N   . ASN B 1 183 ? 10.170  15.880  -19.649 1.00 66.22  ? 217 ASN B N   1 
ATOM   3059 C  CA  . ASN B 1 183 ? 9.275   16.616  -18.762 1.00 62.15  ? 217 ASN B CA  1 
ATOM   3060 C  C   . ASN B 1 183 ? 7.870   16.037  -18.874 1.00 70.25  ? 217 ASN B C   1 
ATOM   3061 O  O   . ASN B 1 183 ? 7.177   16.254  -19.873 1.00 65.22  ? 217 ASN B O   1 
ATOM   3062 C  CB  . ASN B 1 183 ? 9.290   18.100  -19.114 1.00 68.20  ? 217 ASN B CB  1 
ATOM   3063 C  CG  . ASN B 1 183 ? 8.706   18.965  -18.017 1.00 82.63  ? 217 ASN B CG  1 
ATOM   3064 O  OD1 . ASN B 1 183 ? 8.474   18.500  -16.901 1.00 78.73  ? 217 ASN B OD1 1 
ATOM   3065 N  ND2 . ASN B 1 183 ? 8.467   20.234  -18.329 1.00 85.10  ? 217 ASN B ND2 1 
ATOM   3066 N  N   . LEU B 1 184 ? 7.445   15.301  -17.847 1.00 69.51  ? 218 LEU B N   1 
ATOM   3067 C  CA  . LEU B 1 184 ? 6.123   14.691  -17.806 1.00 66.44  ? 218 LEU B CA  1 
ATOM   3068 C  C   . LEU B 1 184 ? 5.148   15.468  -16.927 1.00 75.71  ? 218 LEU B C   1 
ATOM   3069 O  O   . LEU B 1 184 ? 4.111   14.923  -16.532 1.00 72.20  ? 218 LEU B O   1 
ATOM   3070 C  CB  . LEU B 1 184 ? 6.224   13.242  -17.326 1.00 70.67  ? 218 LEU B CB  1 
ATOM   3071 C  CG  . LEU B 1 184 ? 6.949   12.262  -18.251 1.00 61.68  ? 218 LEU B CG  1 
ATOM   3072 C  CD1 . LEU B 1 184 ? 6.865   10.846  -17.702 1.00 59.54  ? 218 LEU B CD1 1 
ATOM   3073 C  CD2 . LEU B 1 184 ? 6.372   12.330  -19.655 1.00 59.79  ? 218 LEU B CD2 1 
ATOM   3074 N  N   . GLY B 1 185 ? 5.457   16.725  -16.616 1.00 84.24  ? 219 GLY B N   1 
ATOM   3075 C  CA  . GLY B 1 185 ? 4.597   17.539  -15.779 1.00 75.65  ? 219 GLY B CA  1 
ATOM   3076 C  C   . GLY B 1 185 ? 3.228   17.780  -16.380 1.00 83.31  ? 219 GLY B C   1 
ATOM   3077 O  O   . GLY B 1 185 ? 2.224   17.262  -15.883 1.00 90.07  ? 219 GLY B O   1 
ATOM   3078 N  N   . ASP B 1 186 ? 3.175   18.568  -17.456 1.00 79.73  ? 220 ASP B N   1 
ATOM   3079 C  CA  . ASP B 1 186 ? 1.933   18.843  -18.169 1.00 71.02  ? 220 ASP B CA  1 
ATOM   3080 C  C   . ASP B 1 186 ? 1.637   17.808  -19.247 1.00 63.57  ? 220 ASP B C   1 
ATOM   3081 O  O   . ASP B 1 186 ? 1.005   18.136  -20.260 1.00 64.34  ? 220 ASP B O   1 
ATOM   3082 C  CB  . ASP B 1 186 ? 1.978   20.245  -18.779 1.00 72.83  ? 220 ASP B CB  1 
ATOM   3083 C  CG  . ASP B 1 186 ? 2.243   21.322  -17.746 1.00 86.24  ? 220 ASP B CG  1 
ATOM   3084 O  OD1 . ASP B 1 186 ? 2.066   21.049  -16.541 1.00 93.08  ? 220 ASP B OD1 1 
ATOM   3085 O  OD2 . ASP B 1 186 ? 2.629   22.442  -18.141 1.00 96.63  ? 220 ASP B OD2 1 
ATOM   3086 N  N   . ALA B 1 187 ? 2.072   16.567  -19.056 1.00 68.10  ? 221 ALA B N   1 
ATOM   3087 C  CA  . ALA B 1 187 ? 1.933   15.536  -20.073 1.00 63.65  ? 221 ALA B CA  1 
ATOM   3088 C  C   . ALA B 1 187 ? 0.664   14.722  -19.862 1.00 68.94  ? 221 ALA B C   1 
ATOM   3089 O  O   . ALA B 1 187 ? 0.154   14.599  -18.745 1.00 66.20  ? 221 ALA B O   1 
ATOM   3090 C  CB  . ALA B 1 187 ? 3.149   14.609  -20.070 1.00 60.60  ? 221 ALA B CB  1 
ATOM   3091 N  N   . ASP B 1 188 ? 0.156   14.166  -20.960 1.00 74.28  ? 222 ASP B N   1 
ATOM   3092 C  CA  . ASP B 1 188 ? -0.997  13.273  -20.942 1.00 67.03  ? 222 ASP B CA  1 
ATOM   3093 C  C   . ASP B 1 188 ? -0.475  11.841  -20.980 1.00 65.25  ? 222 ASP B C   1 
ATOM   3094 O  O   . ASP B 1 188 ? 0.007   11.378  -22.017 1.00 72.21  ? 222 ASP B O   1 
ATOM   3095 C  CB  . ASP B 1 188 ? -1.924  13.558  -22.122 1.00 68.58  ? 222 ASP B CB  1 
ATOM   3096 C  CG  . ASP B 1 188 ? -3.314  12.981  -21.929 1.00 73.69  ? 222 ASP B CG  1 
ATOM   3097 O  OD1 . ASP B 1 188 ? -3.427  11.820  -21.481 1.00 76.69  ? 222 ASP B OD1 1 
ATOM   3098 O  OD2 . ASP B 1 188 ? -4.296  13.690  -22.230 1.00 72.63  ? 222 ASP B OD2 1 
ATOM   3099 N  N   . THR B 1 189 ? -0.572  11.143  -19.846 1.00 72.13  ? 223 THR B N   1 
ATOM   3100 C  CA  . THR B 1 189 ? -0.014  9.798   -19.753 1.00 75.91  ? 223 THR B CA  1 
ATOM   3101 C  C   . THR B 1 189 ? -0.731  8.815   -20.670 1.00 79.30  ? 223 THR B C   1 
ATOM   3102 O  O   . THR B 1 189 ? -0.123  7.839   -21.124 1.00 80.95  ? 223 THR B O   1 
ATOM   3103 C  CB  . THR B 1 189 ? -0.071  9.304   -18.307 1.00 81.98  ? 223 THR B CB  1 
ATOM   3104 O  OG1 . THR B 1 189 ? -1.419  9.378   -17.827 1.00 85.22  ? 223 THR B OG1 1 
ATOM   3105 C  CG2 . THR B 1 189 ? 0.824   10.155  -17.418 1.00 76.45  ? 223 THR B CG2 1 
ATOM   3106 N  N   . GLU B 1 190 ? -2.011  9.053   -20.959 1.00 81.56  ? 224 GLU B N   1 
ATOM   3107 C  CA  . GLU B 1 190 ? -2.776  8.118   -21.778 1.00 81.72  ? 224 GLU B CA  1 
ATOM   3108 C  C   . GLU B 1 190 ? -2.572  8.382   -23.266 1.00 82.40  ? 224 GLU B C   1 
ATOM   3109 O  O   . GLU B 1 190 ? -2.190  7.482   -24.022 1.00 83.26  ? 224 GLU B O   1 
ATOM   3110 C  CB  . GLU B 1 190 ? -4.262  8.199   -21.415 1.00 81.88  ? 224 GLU B CB  1 
ATOM   3111 N  N   . ARG B 1 191 ? -2.820  9.615   -23.703 1.00 79.92  ? 225 ARG B N   1 
ATOM   3112 C  CA  . ARG B 1 191 ? -2.778  9.953   -25.121 1.00 73.41  ? 225 ARG B CA  1 
ATOM   3113 C  C   . ARG B 1 191 ? -1.366  10.158  -25.657 1.00 67.47  ? 225 ARG B C   1 
ATOM   3114 O  O   . ARG B 1 191 ? -1.219  10.445  -26.849 1.00 70.22  ? 225 ARG B O   1 
ATOM   3115 C  CB  . ARG B 1 191 ? -3.613  11.209  -25.386 1.00 73.65  ? 225 ARG B CB  1 
ATOM   3116 C  CG  . ARG B 1 191 ? -5.077  11.083  -24.992 1.00 73.04  ? 225 ARG B CG  1 
ATOM   3117 C  CD  . ARG B 1 191 ? -5.982  11.747  -26.021 1.00 79.08  ? 225 ARG B CD  1 
ATOM   3118 N  NE  . ARG B 1 191 ? -6.814  12.788  -25.430 1.00 90.89  ? 225 ARG B NE  1 
ATOM   3119 C  CZ  . ARG B 1 191 ? -7.644  13.564  -26.115 1.00 99.30  ? 225 ARG B CZ  1 
ATOM   3120 N  NH1 . ARG B 1 191 ? -7.779  13.443  -27.425 1.00 95.55  ? 225 ARG B NH1 1 
ATOM   3121 N  NH2 . ARG B 1 191 ? -8.354  14.485  -25.469 1.00 94.28  ? 225 ARG B NH2 1 
ATOM   3122 N  N   . TYR B 1 192 ? -0.332  10.021  -24.822 1.00 72.21  ? 226 TYR B N   1 
ATOM   3123 C  CA  . TYR B 1 192 ? 1.035   10.210  -25.303 1.00 66.83  ? 226 TYR B CA  1 
ATOM   3124 C  C   . TYR B 1 192 ? 1.396   9.159   -26.347 1.00 66.31  ? 226 TYR B C   1 
ATOM   3125 O  O   . TYR B 1 192 ? 1.942   9.484   -27.408 1.00 59.90  ? 226 TYR B O   1 
ATOM   3126 C  CB  . TYR B 1 192 ? 2.018   10.166  -24.129 1.00 62.02  ? 226 TYR B CB  1 
ATOM   3127 C  CG  . TYR B 1 192 ? 3.323   10.910  -24.359 1.00 63.33  ? 226 TYR B CG  1 
ATOM   3128 C  CD1 . TYR B 1 192 ? 3.962   10.879  -25.592 1.00 59.12  ? 226 TYR B CD1 1 
ATOM   3129 C  CD2 . TYR B 1 192 ? 3.916   11.641  -23.337 1.00 53.05  ? 226 TYR B CD2 1 
ATOM   3130 C  CE1 . TYR B 1 192 ? 5.149   11.552  -25.804 1.00 54.67  ? 226 TYR B CE1 1 
ATOM   3131 C  CE2 . TYR B 1 192 ? 5.106   12.320  -23.540 1.00 57.90  ? 226 TYR B CE2 1 
ATOM   3132 C  CZ  . TYR B 1 192 ? 5.717   12.271  -24.777 1.00 58.40  ? 226 TYR B CZ  1 
ATOM   3133 O  OH  . TYR B 1 192 ? 6.900   12.943  -24.988 1.00 52.33  ? 226 TYR B OH  1 
ATOM   3134 N  N   . ALA B 1 193 ? 1.096   7.890   -26.061 1.00 72.96  ? 227 ALA B N   1 
ATOM   3135 C  CA  . ALA B 1 193 ? 1.442   6.821   -26.993 1.00 62.20  ? 227 ALA B CA  1 
ATOM   3136 C  C   . ALA B 1 193 ? 0.754   7.013   -28.338 1.00 62.19  ? 227 ALA B C   1 
ATOM   3137 O  O   . ALA B 1 193 ? 1.374   6.833   -29.392 1.00 65.19  ? 227 ALA B O   1 
ATOM   3138 C  CB  . ALA B 1 193 ? 1.077   5.465   -26.391 1.00 67.84  ? 227 ALA B CB  1 
ATOM   3139 N  N   . ALA B 1 194 ? -0.526  7.391   -28.322 1.00 66.08  ? 228 ALA B N   1 
ATOM   3140 C  CA  . ALA B 1 194 ? -1.256  7.574   -29.572 1.00 63.00  ? 228 ALA B CA  1 
ATOM   3141 C  C   . ALA B 1 194 ? -0.806  8.834   -30.301 1.00 66.75  ? 228 ALA B C   1 
ATOM   3142 O  O   . ALA B 1 194 ? -0.675  8.831   -31.531 1.00 64.22  ? 228 ALA B O   1 
ATOM   3143 C  CB  . ALA B 1 194 ? -2.759  7.620   -29.299 1.00 64.41  ? 228 ALA B CB  1 
ATOM   3144 N  N   . SER B 1 195 ? -0.566  9.921   -29.563 1.00 66.99  ? 229 SER B N   1 
ATOM   3145 C  CA  . SER B 1 195 ? -0.172  11.174  -30.201 1.00 56.26  ? 229 SER B CA  1 
ATOM   3146 C  C   . SER B 1 195 ? 1.188   11.051  -30.874 1.00 57.42  ? 229 SER B C   1 
ATOM   3147 O  O   . SER B 1 195 ? 1.404   11.610  -31.956 1.00 50.66  ? 229 SER B O   1 
ATOM   3148 C  CB  . SER B 1 195 ? -0.162  12.308  -29.177 1.00 56.72  ? 229 SER B CB  1 
ATOM   3149 O  OG  . SER B 1 195 ? -1.441  12.476  -28.591 1.00 65.56  ? 229 SER B OG  1 
ATOM   3150 N  N   . ALA B 1 196 ? 2.119   10.325  -30.251 1.00 56.18  ? 230 ALA B N   1 
ATOM   3151 C  CA  . ALA B 1 196 ? 3.419   10.109  -30.876 1.00 47.92  ? 230 ALA B CA  1 
ATOM   3152 C  C   . ALA B 1 196 ? 3.278   9.335   -32.180 1.00 56.20  ? 230 ALA B C   1 
ATOM   3153 O  O   . ALA B 1 196 ? 3.959   9.637   -33.167 1.00 55.05  ? 230 ALA B O   1 
ATOM   3154 C  CB  . ALA B 1 196 ? 4.352   9.377   -29.912 1.00 51.25  ? 230 ALA B CB  1 
ATOM   3155 N  N   . ARG B 1 197 ? 2.388   8.339   -32.208 1.00 54.12  ? 231 ARG B N   1 
ATOM   3156 C  CA  . ARG B 1 197 ? 2.184   7.567   -33.428 1.00 51.69  ? 231 ARG B CA  1 
ATOM   3157 C  C   . ARG B 1 197 ? 1.425   8.365   -34.480 1.00 52.64  ? 231 ARG B C   1 
ATOM   3158 O  O   . ARG B 1 197 ? 1.667   8.192   -35.680 1.00 54.65  ? 231 ARG B O   1 
ATOM   3159 C  CB  . ARG B 1 197 ? 1.446   6.268   -33.110 1.00 60.29  ? 231 ARG B CB  1 
ATOM   3160 C  CG  . ARG B 1 197 ? 2.188   5.358   -32.147 1.00 52.46  ? 231 ARG B CG  1 
ATOM   3161 C  CD  . ARG B 1 197 ? 1.438   4.055   -31.929 1.00 60.88  ? 231 ARG B CD  1 
ATOM   3162 N  NE  . ARG B 1 197 ? 1.801   3.426   -30.665 1.00 70.09  ? 231 ARG B NE  1 
ATOM   3163 C  CZ  . ARG B 1 197 ? 2.752   2.512   -30.530 1.00 75.48  ? 231 ARG B CZ  1 
ATOM   3164 N  NH1 . ARG B 1 197 ? 3.460   2.093   -31.565 1.00 72.38  ? 231 ARG B NH1 1 
ATOM   3165 N  NH2 . ARG B 1 197 ? 2.999   2.007   -29.324 1.00 76.93  ? 231 ARG B NH2 1 
ATOM   3166 N  N   . ALA B 1 198 ? 0.505   9.236   -34.056 1.00 48.59  ? 232 ALA B N   1 
ATOM   3167 C  CA  . ALA B 1 198 ? -0.202  10.083  -35.011 1.00 47.43  ? 232 ALA B CA  1 
ATOM   3168 C  C   . ALA B 1 198 ? 0.747   11.051  -35.704 1.00 59.61  ? 232 ALA B C   1 
ATOM   3169 O  O   . ALA B 1 198 ? 0.498   11.455  -36.846 1.00 58.11  ? 232 ALA B O   1 
ATOM   3170 C  CB  . ALA B 1 198 ? -1.324  10.848  -34.309 1.00 48.49  ? 232 ALA B CB  1 
ATOM   3171 N  N   . PHE B 1 199 ? 1.835   11.435  -35.032 1.00 54.17  ? 233 PHE B N   1 
ATOM   3172 C  CA  . PHE B 1 199 ? 2.832   12.294  -35.662 1.00 50.84  ? 233 PHE B CA  1 
ATOM   3173 C  C   . PHE B 1 199 ? 3.539   11.572  -36.802 1.00 54.02  ? 233 PHE B C   1 
ATOM   3174 O  O   . PHE B 1 199 ? 3.768   12.156  -37.868 1.00 50.76  ? 233 PHE B O   1 
ATOM   3175 C  CB  . PHE B 1 199 ? 3.842   12.774  -34.620 1.00 48.01  ? 233 PHE B CB  1 
ATOM   3176 C  CG  . PHE B 1 199 ? 5.106   13.330  -35.210 1.00 50.19  ? 233 PHE B CG  1 
ATOM   3177 C  CD1 . PHE B 1 199 ? 5.085   14.496  -35.955 1.00 48.57  ? 233 PHE B CD1 1 
ATOM   3178 C  CD2 . PHE B 1 199 ? 6.318   12.687  -35.017 1.00 48.99  ? 233 PHE B CD2 1 
ATOM   3179 C  CE1 . PHE B 1 199 ? 6.248   15.012  -36.497 1.00 45.20  ? 233 PHE B CE1 1 
ATOM   3180 C  CE2 . PHE B 1 199 ? 7.484   13.197  -35.556 1.00 52.11  ? 233 PHE B CE2 1 
ATOM   3181 C  CZ  . PHE B 1 199 ? 7.448   14.361  -36.298 1.00 42.79  ? 233 PHE B CZ  1 
ATOM   3182 N  N   . GLY B 1 200 ? 3.893   10.301  -36.597 1.00 51.63  ? 234 GLY B N   1 
ATOM   3183 C  CA  . GLY B 1 200 ? 4.541   9.544   -37.652 1.00 47.52  ? 234 GLY B CA  1 
ATOM   3184 C  C   . GLY B 1 200 ? 3.615   9.212   -38.804 1.00 52.82  ? 234 GLY B C   1 
ATOM   3185 O  O   . GLY B 1 200 ? 4.054   9.143   -39.956 1.00 56.40  ? 234 GLY B O   1 
ATOM   3186 N  N   . ALA B 1 201 ? 2.327   9.006   -38.518 1.00 52.83  ? 235 ALA B N   1 
ATOM   3187 C  CA  . ALA B 1 201 ? 1.379   8.686   -39.578 1.00 53.20  ? 235 ALA B CA  1 
ATOM   3188 C  C   . ALA B 1 201 ? 1.027   9.911   -40.411 1.00 50.23  ? 235 ALA B C   1 
ATOM   3189 O  O   . ALA B 1 201 ? 0.699   9.780   -41.596 1.00 53.00  ? 235 ALA B O   1 
ATOM   3190 C  CB  . ALA B 1 201 ? 0.114   8.066   -38.985 1.00 50.98  ? 235 ALA B CB  1 
ATOM   3191 N  N   . ALA B 1 202 ? 1.088   11.105  -39.816 1.00 53.02  ? 236 ALA B N   1 
ATOM   3192 C  CA  . ALA B 1 202 ? 0.761   12.316  -40.561 1.00 60.77  ? 236 ALA B CA  1 
ATOM   3193 C  C   . ALA B 1 202 ? 1.869   12.698  -41.532 1.00 54.98  ? 236 ALA B C   1 
ATOM   3194 O  O   . ALA B 1 202 ? 1.594   13.289  -42.583 1.00 51.40  ? 236 ALA B O   1 
ATOM   3195 C  CB  . ALA B 1 202 ? 0.483   13.469  -39.599 1.00 50.94  ? 236 ALA B CB  1 
ATOM   3196 N  N   . PHE B 1 203 ? 3.122   12.377  -41.202 1.00 54.64  ? 237 PHE B N   1 
ATOM   3197 C  CA  . PHE B 1 203 ? 4.275   12.638  -42.061 1.00 52.48  ? 237 PHE B CA  1 
ATOM   3198 C  C   . PHE B 1 203 ? 4.921   11.300  -42.398 1.00 57.38  ? 237 PHE B C   1 
ATOM   3199 O  O   . PHE B 1 203 ? 5.976   10.949  -41.846 1.00 51.63  ? 237 PHE B O   1 
ATOM   3200 C  CB  . PHE B 1 203 ? 5.270   13.583  -41.390 1.00 46.72  ? 237 PHE B CB  1 
ATOM   3201 C  CG  . PHE B 1 203 ? 4.634   14.804  -40.789 1.00 53.64  ? 237 PHE B CG  1 
ATOM   3202 C  CD1 . PHE B 1 203 ? 4.286   15.883  -41.585 1.00 48.89  ? 237 PHE B CD1 1 
ATOM   3203 C  CD2 . PHE B 1 203 ? 4.386   14.874  -39.428 1.00 44.45  ? 237 PHE B CD2 1 
ATOM   3204 C  CE1 . PHE B 1 203 ? 3.701   17.008  -41.035 1.00 47.25  ? 237 PHE B CE1 1 
ATOM   3205 C  CE2 . PHE B 1 203 ? 3.801   15.996  -38.873 1.00 46.07  ? 237 PHE B CE2 1 
ATOM   3206 C  CZ  . PHE B 1 203 ? 3.459   17.064  -39.677 1.00 51.65  ? 237 PHE B CZ  1 
ATOM   3207 N  N   . PRO B 1 204 ? 4.318   10.523  -43.304 1.00 57.73  ? 238 PRO B N   1 
ATOM   3208 C  CA  . PRO B 1 204 ? 4.868   9.194   -43.608 1.00 54.11  ? 238 PRO B CA  1 
ATOM   3209 C  C   . PRO B 1 204 ? 6.134   9.235   -44.443 1.00 60.30  ? 238 PRO B C   1 
ATOM   3210 O  O   . PRO B 1 204 ? 6.882   8.250   -44.447 1.00 64.49  ? 238 PRO B O   1 
ATOM   3211 C  CB  . PRO B 1 204 ? 3.725   8.515   -44.371 1.00 55.96  ? 238 PRO B CB  1 
ATOM   3212 C  CG  . PRO B 1 204 ? 3.035   9.647   -45.054 1.00 55.89  ? 238 PRO B CG  1 
ATOM   3213 C  CD  . PRO B 1 204 ? 3.122   10.823  -44.110 1.00 53.47  ? 238 PRO B CD  1 
ATOM   3214 N  N   . LYS B 1 205 ? 6.399   10.335  -45.147 1.00 58.55  ? 239 LYS B N   1 
ATOM   3215 C  CA  . LYS B 1 205 ? 7.544   10.425  -46.041 1.00 62.34  ? 239 LYS B CA  1 
ATOM   3216 C  C   . LYS B 1 205 ? 8.787   11.001  -45.376 1.00 68.94  ? 239 LYS B C   1 
ATOM   3217 O  O   . LYS B 1 205 ? 9.857   10.995  -45.994 1.00 72.50  ? 239 LYS B O   1 
ATOM   3218 C  CB  . LYS B 1 205 ? 7.190   11.272  -47.269 1.00 64.35  ? 239 LYS B CB  1 
ATOM   3219 C  CG  . LYS B 1 205 ? 6.676   10.463  -48.445 1.00 72.42  ? 239 LYS B CG  1 
ATOM   3220 C  CD  . LYS B 1 205 ? 7.668   9.383   -48.837 1.00 77.41  ? 239 LYS B CD  1 
ATOM   3221 C  CE  . LYS B 1 205 ? 8.981   9.971   -49.334 1.00 82.77  ? 239 LYS B CE  1 
ATOM   3222 N  NZ  . LYS B 1 205 ? 9.051   9.991   -50.821 1.00 77.01  ? 239 LYS B NZ  1 
ATOM   3223 N  N   . ALA B 1 206 ? 8.676   11.497  -44.148 1.00 61.45  ? 240 ALA B N   1 
ATOM   3224 C  CA  . ALA B 1 206 ? 9.829   12.070  -43.470 1.00 59.60  ? 240 ALA B CA  1 
ATOM   3225 C  C   . ALA B 1 206 ? 10.821  10.981  -43.084 1.00 65.28  ? 240 ALA B C   1 
ATOM   3226 O  O   . ALA B 1 206 ? 10.439  9.913   -42.597 1.00 62.15  ? 240 ALA B O   1 
ATOM   3227 C  CB  . ALA B 1 206 ? 9.386   12.842  -42.229 1.00 52.10  ? 240 ALA B CB  1 
ATOM   3228 N  N   . ASN B 1 207 ? 12.104  11.254  -43.307 1.00 62.86  ? 241 ASN B N   1 
ATOM   3229 C  CA  . ASN B 1 207 ? 13.178  10.335  -42.949 1.00 64.94  ? 241 ASN B CA  1 
ATOM   3230 C  C   . ASN B 1 207 ? 13.970  10.783  -41.733 1.00 65.16  ? 241 ASN B C   1 
ATOM   3231 O  O   . ASN B 1 207 ? 14.382  9.944   -40.929 1.00 72.11  ? 241 ASN B O   1 
ATOM   3232 C  CB  . ASN B 1 207 ? 14.136  10.152  -44.131 1.00 66.61  ? 241 ASN B CB  1 
ATOM   3233 C  CG  . ASN B 1 207 ? 13.624  9.152   -45.148 1.00 73.05  ? 241 ASN B CG  1 
ATOM   3234 O  OD1 . ASN B 1 207 ? 12.775  8.315   -44.840 1.00 73.03  ? 241 ASN B OD1 1 
ATOM   3235 N  ND2 . ASN B 1 207 ? 14.138  9.235   -46.369 1.00 81.52  ? 241 ASN B ND2 1 
ATOM   3236 N  N   . THR B 1 208 ? 14.196  12.084  -41.578 1.00 65.10  ? 242 THR B N   1 
ATOM   3237 C  CA  . THR B 1 208 ? 14.890  12.636  -40.424 1.00 57.35  ? 242 THR B CA  1 
ATOM   3238 C  C   . THR B 1 208 ? 13.889  13.377  -39.549 1.00 55.36  ? 242 THR B C   1 
ATOM   3239 O  O   . THR B 1 208 ? 13.179  14.267  -40.028 1.00 57.23  ? 242 THR B O   1 
ATOM   3240 C  CB  . THR B 1 208 ? 16.019  13.579  -40.852 1.00 56.05  ? 242 THR B CB  1 
ATOM   3241 O  OG1 . THR B 1 208 ? 15.462  14.764  -41.433 1.00 63.60  ? 242 THR B OG1 1 
ATOM   3242 C  CG2 . THR B 1 208 ? 16.925  12.899  -41.868 1.00 50.38  ? 242 THR B CG2 1 
ATOM   3243 N  N   . ILE B 1 209 ? 13.831  13.005  -38.274 1.00 54.27  ? 243 ILE B N   1 
ATOM   3244 C  CA  . ILE B 1 209 ? 12.924  13.619  -37.313 1.00 47.10  ? 243 ILE B CA  1 
ATOM   3245 C  C   . ILE B 1 209 ? 13.707  14.630  -36.489 1.00 46.56  ? 243 ILE B C   1 
ATOM   3246 O  O   . ILE B 1 209 ? 14.748  14.298  -35.909 1.00 56.70  ? 243 ILE B O   1 
ATOM   3247 C  CB  . ILE B 1 209 ? 12.269  12.561  -36.409 1.00 52.55  ? 243 ILE B CB  1 
ATOM   3248 C  CG1 . ILE B 1 209 ? 11.420  11.601  -37.243 1.00 48.26  ? 243 ILE B CG1 1 
ATOM   3249 C  CG2 . ILE B 1 209 ? 11.418  13.227  -35.339 1.00 44.62  ? 243 ILE B CG2 1 
ATOM   3250 C  CD1 . ILE B 1 209 ? 10.293  12.278  -37.989 1.00 53.13  ? 243 ILE B CD1 1 
ATOM   3251 N  N   . ALA B 1 210 ? 13.214  15.863  -36.442 1.00 52.79  ? 244 ALA B N   1 
ATOM   3252 C  CA  . ALA B 1 210 ? 13.822  16.918  -35.645 1.00 45.05  ? 244 ALA B CA  1 
ATOM   3253 C  C   . ALA B 1 210 ? 13.010  17.134  -34.376 1.00 48.21  ? 244 ALA B C   1 
ATOM   3254 O  O   . ALA B 1 210 ? 11.777  17.185  -34.416 1.00 48.26  ? 244 ALA B O   1 
ATOM   3255 C  CB  . ALA B 1 210 ? 13.914  18.222  -36.439 1.00 42.89  ? 244 ALA B CB  1 
ATOM   3256 N  N   . MET B 1 211 ? 13.708  17.253  -33.249 1.00 49.72  ? 245 MET B N   1 
ATOM   3257 C  CA  . MET B 1 211 ? 13.066  17.443  -31.958 1.00 48.68  ? 245 MET B CA  1 
ATOM   3258 C  C   . MET B 1 211 ? 13.813  18.520  -31.184 1.00 50.04  ? 245 MET B C   1 
ATOM   3259 O  O   . MET B 1 211 ? 14.870  18.998  -31.603 1.00 59.88  ? 245 MET B O   1 
ATOM   3260 C  CB  . MET B 1 211 ? 13.011  16.137  -31.158 1.00 47.44  ? 245 MET B CB  1 
ATOM   3261 C  CG  . MET B 1 211 ? 14.276  15.305  -31.240 1.00 60.06  ? 245 MET B CG  1 
ATOM   3262 S  SD  . MET B 1 211 ? 13.928  13.538  -31.256 1.00 55.05  ? 245 MET B SD  1 
ATOM   3263 C  CE  . MET B 1 211 ? 14.230  13.143  -32.975 1.00 57.26  ? 245 MET B CE  1 
ATOM   3264 N  N   . SER B 1 212 ? 13.253  18.890  -30.031 1.00 48.61  ? 246 SER B N   1 
ATOM   3265 C  CA  . SER B 1 212 ? 13.770  20.032  -29.284 1.00 55.93  ? 246 SER B CA  1 
ATOM   3266 C  C   . SER B 1 212 ? 14.966  19.663  -28.413 1.00 51.34  ? 246 SER B C   1 
ATOM   3267 O  O   . SER B 1 212 ? 15.889  20.469  -28.256 1.00 49.96  ? 246 SER B O   1 
ATOM   3268 C  CB  . SER B 1 212 ? 12.660  20.638  -28.424 1.00 55.86  ? 246 SER B CB  1 
ATOM   3269 O  OG  . SER B 1 212 ? 11.490  20.876  -29.188 1.00 56.34  ? 246 SER B OG  1 
ATOM   3270 N  N   . HIS B 1 213 ? 14.973  18.463  -27.838 1.00 51.19  ? 247 HIS B N   1 
ATOM   3271 C  CA  . HIS B 1 213 ? 15.976  18.074  -26.853 1.00 56.71  ? 247 HIS B CA  1 
ATOM   3272 C  C   . HIS B 1 213 ? 16.820  16.901  -27.337 1.00 57.24  ? 247 HIS B C   1 
ATOM   3273 O  O   . HIS B 1 213 ? 17.215  16.035  -26.554 1.00 63.12  ? 247 HIS B O   1 
ATOM   3274 C  CB  . HIS B 1 213 ? 15.318  17.738  -25.518 1.00 50.41  ? 247 HIS B CB  1 
ATOM   3275 C  CG  . HIS B 1 213 ? 14.332  18.764  -25.058 1.00 61.09  ? 247 HIS B CG  1 
ATOM   3276 N  ND1 . HIS B 1 213 ? 14.681  20.077  -24.823 1.00 59.81  ? 247 HIS B ND1 1 
ATOM   3277 C  CD2 . HIS B 1 213 ? 13.009  18.673  -24.789 1.00 55.23  ? 247 HIS B CD2 1 
ATOM   3278 C  CE1 . HIS B 1 213 ? 13.614  20.750  -24.429 1.00 56.09  ? 247 HIS B CE1 1 
ATOM   3279 N  NE2 . HIS B 1 213 ? 12.587  19.920  -24.400 1.00 65.20  ? 247 HIS B NE2 1 
ATOM   3280 N  N   . SER B 1 214 ? 17.117  16.866  -28.634 1.00 57.08  ? 248 SER B N   1 
ATOM   3281 C  CA  . SER B 1 214 ? 17.943  15.805  -29.194 1.00 57.01  ? 248 SER B CA  1 
ATOM   3282 C  C   . SER B 1 214 ? 18.372  16.202  -30.597 1.00 54.75  ? 248 SER B C   1 
ATOM   3283 O  O   . SER B 1 214 ? 17.670  16.949  -31.285 1.00 59.76  ? 248 SER B O   1 
ATOM   3284 C  CB  . SER B 1 214 ? 17.197  14.464  -29.233 1.00 54.57  ? 248 SER B CB  1 
ATOM   3285 O  OG  . SER B 1 214 ? 17.250  13.811  -27.978 1.00 60.88  ? 248 SER B OG  1 
ATOM   3286 N  N   . ALA B 1 215 ? 19.532  15.697  -31.006 1.00 56.45  ? 249 ALA B N   1 
ATOM   3287 C  CA  . ALA B 1 215 ? 19.948  15.835  -32.390 1.00 56.22  ? 249 ALA B CA  1 
ATOM   3288 C  C   . ALA B 1 215 ? 18.976  15.071  -33.289 1.00 53.44  ? 249 ALA B C   1 
ATOM   3289 O  O   . ALA B 1 215 ? 18.313  14.133  -32.836 1.00 54.45  ? 249 ALA B O   1 
ATOM   3290 C  CB  . ALA B 1 215 ? 21.371  15.310  -32.575 1.00 47.81  ? 249 ALA B CB  1 
ATOM   3291 N  N   . PRO B 1 216 ? 18.855  15.464  -34.558 1.00 56.33  ? 250 PRO B N   1 
ATOM   3292 C  CA  . PRO B 1 216 ? 17.931  14.767  -35.462 1.00 56.80  ? 250 PRO B CA  1 
ATOM   3293 C  C   . PRO B 1 216 ? 18.205  13.269  -35.509 1.00 49.80  ? 250 PRO B C   1 
ATOM   3294 O  O   . PRO B 1 216 ? 19.355  12.825  -35.509 1.00 56.30  ? 250 PRO B O   1 
ATOM   3295 C  CB  . PRO B 1 216 ? 18.196  15.434  -36.814 1.00 61.70  ? 250 PRO B CB  1 
ATOM   3296 C  CG  . PRO B 1 216 ? 18.654  16.805  -36.459 1.00 54.58  ? 250 PRO B CG  1 
ATOM   3297 C  CD  . PRO B 1 216 ? 19.451  16.654  -35.191 1.00 55.93  ? 250 PRO B CD  1 
ATOM   3298 N  N   . ASP B 1 217 ? 17.127  12.489  -35.543 1.00 51.96  ? 251 ASP B N   1 
ATOM   3299 C  CA  . ASP B 1 217 ? 17.189  11.036  -35.481 1.00 57.05  ? 251 ASP B CA  1 
ATOM   3300 C  C   . ASP B 1 217 ? 16.329  10.448  -36.596 1.00 58.27  ? 251 ASP B C   1 
ATOM   3301 O  O   . ASP B 1 217 ? 15.650  11.167  -37.334 1.00 59.12  ? 251 ASP B O   1 
ATOM   3302 C  CB  . ASP B 1 217 ? 16.733  10.530  -34.105 1.00 60.83  ? 251 ASP B CB  1 
ATOM   3303 C  CG  . ASP B 1 217 ? 17.244  9.137   -33.794 1.00 60.27  ? 251 ASP B CG  1 
ATOM   3304 O  OD1 . ASP B 1 217 ? 17.999  8.582   -34.619 1.00 67.84  ? 251 ASP B OD1 1 
ATOM   3305 O  OD2 . ASP B 1 217 ? 16.890  8.600   -32.725 1.00 64.48  ? 251 ASP B OD2 1 
ATOM   3306 N  N   . SER B 1 218 ? 16.360  9.122   -36.713 1.00 59.76  ? 252 SER B N   1 
ATOM   3307 C  CA  . SER B 1 218 ? 15.607  8.421   -37.739 1.00 57.78  ? 252 SER B CA  1 
ATOM   3308 C  C   . SER B 1 218 ? 14.149  8.251   -37.311 1.00 58.37  ? 252 SER B C   1 
ATOM   3309 O  O   . SER B 1 218 ? 13.712  8.748   -36.270 1.00 61.62  ? 252 SER B O   1 
ATOM   3310 C  CB  . SER B 1 218 ? 16.251  7.069   -38.037 1.00 54.61  ? 252 SER B CB  1 
ATOM   3311 O  OG  . SER B 1 218 ? 15.774  6.072   -37.151 1.00 55.80  ? 252 SER B OG  1 
ATOM   3312 N  N   . ARG B 1 219 ? 13.385  7.527   -38.133 1.00 62.91  ? 253 ARG B N   1 
ATOM   3313 C  CA  . ARG B 1 219 ? 11.971  7.308   -37.848 1.00 64.45  ? 253 ARG B CA  1 
ATOM   3314 C  C   . ARG B 1 219 ? 11.748  6.381   -36.662 1.00 65.68  ? 253 ARG B C   1 
ATOM   3315 O  O   . ARG B 1 219 ? 10.650  6.374   -36.097 1.00 66.08  ? 253 ARG B O   1 
ATOM   3316 C  CB  . ARG B 1 219 ? 11.265  6.737   -39.078 1.00 61.08  ? 253 ARG B CB  1 
ATOM   3317 C  CG  . ARG B 1 219 ? 10.850  7.776   -40.099 1.00 55.83  ? 253 ARG B CG  1 
ATOM   3318 C  CD  . ARG B 1 219 ? 9.815   7.208   -41.053 1.00 55.28  ? 253 ARG B CD  1 
ATOM   3319 N  NE  . ARG B 1 219 ? 8.458   7.379   -40.550 1.00 55.10  ? 253 ARG B NE  1 
ATOM   3320 C  CZ  . ARG B 1 219 ? 7.696   8.437   -40.794 1.00 55.98  ? 253 ARG B CZ  1 
ATOM   3321 N  NH1 . ARG B 1 219 ? 8.127   9.443   -41.538 1.00 50.92  ? 253 ARG B NH1 1 
ATOM   3322 N  NH2 . ARG B 1 219 ? 6.471   8.487   -40.279 1.00 50.66  ? 253 ARG B NH2 1 
ATOM   3323 N  N   . ALA B 1 220 ? 12.753  5.591   -36.278 1.00 62.04  ? 254 ALA B N   1 
ATOM   3324 C  CA  . ALA B 1 220 ? 12.598  4.705   -35.131 1.00 66.93  ? 254 ALA B CA  1 
ATOM   3325 C  C   . ALA B 1 220 ? 12.437  5.473   -33.827 1.00 66.00  ? 254 ALA B C   1 
ATOM   3326 O  O   . ALA B 1 220 ? 11.898  4.923   -32.861 1.00 60.95  ? 254 ALA B O   1 
ATOM   3327 C  CB  . ALA B 1 220 ? 13.789  3.753   -35.034 1.00 66.19  ? 254 ALA B CB  1 
ATOM   3328 N  N   . ALA B 1 221 ? 12.889  6.729   -33.780 1.00 64.05  ? 255 ALA B N   1 
ATOM   3329 C  CA  . ALA B 1 221 ? 12.712  7.547   -32.587 1.00 61.37  ? 255 ALA B CA  1 
ATOM   3330 C  C   . ALA B 1 221 ? 11.247  7.849   -32.304 1.00 63.05  ? 255 ALA B C   1 
ATOM   3331 O  O   . ALA B 1 221 ? 10.900  8.149   -31.157 1.00 65.79  ? 255 ALA B O   1 
ATOM   3332 C  CB  . ALA B 1 221 ? 13.494  8.853   -32.724 1.00 64.52  ? 255 ALA B CB  1 
ATOM   3333 N  N   . ILE B 1 222 ? 10.401  7.754   -33.308 1.00 65.75  ? 256 ILE B N   1 
ATOM   3334 C  CA  . ILE B 1 222 ? 8.994   7.987   -33.097 1.00 65.07  ? 256 ILE B CA  1 
ATOM   3335 C  C   . ILE B 1 222 ? 8.377   6.885   -32.274 1.00 66.67  ? 256 ILE B C   1 
ATOM   3336 O  O   . ILE B 1 222 ? 7.582   7.145   -31.387 1.00 67.50  ? 256 ILE B O   1 
ATOM   3337 C  CB  . ILE B 1 222 ? 8.246   8.071   -34.429 1.00 70.34  ? 256 ILE B CB  1 
ATOM   3338 C  CG1 . ILE B 1 222 ? 8.848   9.168   -35.306 1.00 72.93  ? 256 ILE B CG1 1 
ATOM   3339 C  CG2 . ILE B 1 222 ? 6.767   8.324   -34.191 1.00 65.70  ? 256 ILE B CG2 1 
ATOM   3340 C  CD1 . ILE B 1 222 ? 8.218   9.266   -36.676 1.00 65.49  ? 256 ILE B CD1 1 
ATOM   3341 N  N   . THR B 1 223 ? 8.746   5.650   -32.559 1.00 67.70  ? 257 THR B N   1 
ATOM   3342 C  CA  . THR B 1 223 ? 8.130   4.529   -31.873 1.00 68.41  ? 257 THR B CA  1 
ATOM   3343 C  C   . THR B 1 223 ? 8.789   4.303   -30.549 1.00 66.18  ? 257 THR B C   1 
ATOM   3344 O  O   . THR B 1 223 ? 8.140   3.903   -29.605 1.00 71.00  ? 257 THR B O   1 
ATOM   3345 C  CB  . THR B 1 223 ? 8.174   3.249   -32.726 1.00 71.14  ? 257 THR B CB  1 
ATOM   3346 O  OG1 . THR B 1 223 ? 9.525   2.979   -33.109 1.00 72.62  ? 257 THR B OG1 1 
ATOM   3347 C  CG2 . THR B 1 223 ? 7.333   3.419   -33.968 1.00 74.18  ? 257 THR B CG2 1 
ATOM   3348 N  N   . HIS B 1 224 ? 10.076  4.576   -30.462 1.00 66.61  ? 258 HIS B N   1 
ATOM   3349 C  CA  . HIS B 1 224 ? 10.731  4.473   -29.181 1.00 69.34  ? 258 HIS B CA  1 
ATOM   3350 C  C   . HIS B 1 224 ? 10.015  5.397   -28.238 1.00 69.48  ? 258 HIS B C   1 
ATOM   3351 O  O   . HIS B 1 224 ? 9.692   5.041   -27.118 1.00 69.88  ? 258 HIS B O   1 
ATOM   3352 C  CB  . HIS B 1 224 ? 12.190  4.860   -29.279 1.00 63.37  ? 258 HIS B CB  1 
ATOM   3353 C  CG  . HIS B 1 224 ? 12.949  4.658   -28.010 1.00 65.49  ? 258 HIS B CG  1 
ATOM   3354 N  ND1 . HIS B 1 224 ? 13.074  3.425   -27.410 1.00 71.91  ? 258 HIS B ND1 1 
ATOM   3355 C  CD2 . HIS B 1 224 ? 13.630  5.527   -27.230 1.00 76.03  ? 258 HIS B CD2 1 
ATOM   3356 C  CE1 . HIS B 1 224 ? 13.795  3.544   -26.311 1.00 79.03  ? 258 HIS B CE1 1 
ATOM   3357 N  NE2 . HIS B 1 224 ? 14.146  4.809   -26.180 1.00 77.47  ? 258 HIS B NE2 1 
ATOM   3358 N  N   . THR B 1 225 ? 9.753   6.598   -28.709 1.00 66.89  ? 259 THR B N   1 
ATOM   3359 C  CA  . THR B 1 225 ? 8.999   7.525   -27.873 1.00 65.04  ? 259 THR B CA  1 
ATOM   3360 C  C   . THR B 1 225 ? 7.641   6.939   -27.506 1.00 66.96  ? 259 THR B C   1 
ATOM   3361 O  O   . THR B 1 225 ? 7.184   7.071   -26.364 1.00 68.96  ? 259 THR B O   1 
ATOM   3362 C  CB  . THR B 1 225 ? 8.840   8.865   -28.595 1.00 57.93  ? 259 THR B CB  1 
ATOM   3363 O  OG1 . THR B 1 225 ? 10.106  9.535   -28.647 1.00 57.22  ? 259 THR B OG1 1 
ATOM   3364 C  CG2 . THR B 1 225 ? 7.833   9.755   -27.879 1.00 52.00  ? 259 THR B CG2 1 
ATOM   3365 N  N   . ALA B 1 226 ? 6.990   6.267   -28.460 1.00 67.90  ? 260 ALA B N   1 
ATOM   3366 C  CA  . ALA B 1 226 ? 5.702   5.642   -28.179 1.00 66.49  ? 260 ALA B CA  1 
ATOM   3367 C  C   . ALA B 1 226 ? 5.856   4.386   -27.330 1.00 72.24  ? 260 ALA B C   1 
ATOM   3368 O  O   . ALA B 1 226 ? 4.964   4.069   -26.534 1.00 77.36  ? 260 ALA B O   1 
ATOM   3369 C  CB  . ALA B 1 226 ? 4.981   5.313   -29.486 1.00 60.71  ? 260 ALA B CB  1 
ATOM   3370 N  N   . ARG B 1 227 ? 6.964   3.656   -27.487 1.00 79.63  ? 261 ARG B N   1 
ATOM   3371 C  CA  . ARG B 1 227 ? 7.201   2.489   -26.641 1.00 75.84  ? 261 ARG B CA  1 
ATOM   3372 C  C   . ARG B 1 227 ? 7.325   2.890   -25.177 1.00 77.83  ? 261 ARG B C   1 
ATOM   3373 O  O   . ARG B 1 227 ? 6.779   2.219   -24.293 1.00 78.20  ? 261 ARG B O   1 
ATOM   3374 C  CB  . ARG B 1 227 ? 8.456   1.743   -27.098 1.00 77.42  ? 261 ARG B CB  1 
ATOM   3375 C  CG  . ARG B 1 227 ? 8.387   1.172   -28.507 1.00 76.07  ? 261 ARG B CG  1 
ATOM   3376 C  CD  . ARG B 1 227 ? 7.959   -0.285  -28.511 1.00 90.48  ? 261 ARG B CD  1 
ATOM   3377 N  NE  . ARG B 1 227 ? 6.989   -0.563  -29.563 1.00 101.45 ? 261 ARG B NE  1 
ATOM   3378 C  CZ  . ARG B 1 227 ? 7.303   -0.765  -30.836 1.00 103.53 ? 261 ARG B CZ  1 
ATOM   3379 N  NH1 . ARG B 1 227 ? 8.559   -0.726  -31.253 1.00 95.55  ? 261 ARG B NH1 1 
ATOM   3380 N  NH2 . ARG B 1 227 ? 6.334   -1.005  -31.713 1.00 102.35 ? 261 ARG B NH2 1 
ATOM   3381 N  N   . MET B 1 228 ? 7.982   4.002   -24.909 1.00 75.84  ? 262 MET B N   1 
ATOM   3382 C  CA  . MET B 1 228 ? 8.146   4.431   -23.543 1.00 72.23  ? 262 MET B CA  1 
ATOM   3383 C  C   . MET B 1 228 ? 6.827   4.924   -23.021 1.00 77.72  ? 262 MET B C   1 
ATOM   3384 O  O   . MET B 1 228 ? 6.505   4.739   -21.857 1.00 82.56  ? 262 MET B O   1 
ATOM   3385 C  CB  . MET B 1 228 ? 9.198   5.519   -23.454 1.00 76.21  ? 262 MET B CB  1 
ATOM   3386 C  CG  . MET B 1 228 ? 10.603  5.075   -23.819 1.00 71.11  ? 262 MET B CG  1 
ATOM   3387 S  SD  . MET B 1 228 ? 11.808  6.384   -23.560 1.00 66.21  ? 262 MET B SD  1 
ATOM   3388 C  CE  . MET B 1 228 ? 11.255  7.599   -24.742 1.00 72.37  ? 262 MET B CE  1 
ATOM   3389 N  N   . ALA B 1 229 ? 6.049   5.534   -23.886 1.00 73.24  ? 263 ALA B N   1 
ATOM   3390 C  CA  . ALA B 1 229 ? 4.773   6.068   -23.469 1.00 76.57  ? 263 ALA B CA  1 
ATOM   3391 C  C   . ALA B 1 229 ? 3.771   4.972   -23.221 1.00 74.17  ? 263 ALA B C   1 
ATOM   3392 O  O   . ALA B 1 229 ? 2.832   5.143   -22.457 1.00 81.06  ? 263 ALA B O   1 
ATOM   3393 C  CB  . ALA B 1 229 ? 4.258   7.031   -24.513 1.00 75.14  ? 263 ALA B CB  1 
ATOM   3394 N  N   . ASP B 1 230 ? 3.956   3.844   -23.873 1.00 75.93  ? 264 ASP B N   1 
ATOM   3395 C  CA  . ASP B 1 230 ? 3.083   2.735   -23.621 1.00 75.23  ? 264 ASP B CA  1 
ATOM   3396 C  C   . ASP B 1 230 ? 3.328   2.315   -22.203 1.00 84.64  ? 264 ASP B C   1 
ATOM   3397 O  O   . ASP B 1 230 ? 2.409   2.223   -21.400 1.00 92.99  ? 264 ASP B O   1 
ATOM   3398 C  CB  . ASP B 1 230 ? 3.398   1.589   -24.565 1.00 70.88  ? 264 ASP B CB  1 
ATOM   3399 C  CG  . ASP B 1 230 ? 2.808   1.783   -25.940 1.00 76.79  ? 264 ASP B CG  1 
ATOM   3400 O  OD1 . ASP B 1 230 ? 1.786   2.484   -26.057 1.00 82.09  ? 264 ASP B OD1 1 
ATOM   3401 O  OD2 . ASP B 1 230 ? 3.358   1.217   -26.905 1.00 72.44  ? 264 ASP B OD2 1 
ATOM   3402 N  N   . LYS B 1 231 ? 4.584   2.096   -21.877 1.00 83.40  ? 265 LYS B N   1 
ATOM   3403 C  CA  . LYS B 1 231 ? 4.927   1.680   -20.546 1.00 81.26  ? 265 LYS B CA  1 
ATOM   3404 C  C   . LYS B 1 231 ? 4.432   2.699   -19.550 1.00 89.35  ? 265 LYS B C   1 
ATOM   3405 O  O   . LYS B 1 231 ? 3.936   2.351   -18.484 1.00 95.55  ? 265 LYS B O   1 
ATOM   3406 C  CB  . LYS B 1 231 ? 6.428   1.505   -20.468 1.00 76.43  ? 265 LYS B CB  1 
ATOM   3407 C  CG  . LYS B 1 231 ? 6.936   0.413   -21.392 1.00 83.90  ? 265 LYS B CG  1 
ATOM   3408 C  CD  . LYS B 1 231 ? 8.425   0.154   -21.233 1.00 86.51  ? 265 LYS B CD  1 
ATOM   3409 C  CE  . LYS B 1 231 ? 9.255   1.169   -22.000 1.00 95.89  ? 265 LYS B CE  1 
ATOM   3410 N  NZ  . LYS B 1 231 ? 10.692  0.782   -22.044 1.00 94.29  ? 265 LYS B NZ  1 
ATOM   3411 N  N   . LEU B 1 232 ? 4.530   3.964   -19.903 1.00 85.59  ? 266 LEU B N   1 
ATOM   3412 C  CA  . LEU B 1 232 ? 4.059   5.002   -19.020 1.00 84.23  ? 266 LEU B CA  1 
ATOM   3413 C  C   . LEU B 1 232 ? 2.583   4.864   -18.753 1.00 100.71 ? 266 LEU B C   1 
ATOM   3414 O  O   . LEU B 1 232 ? 2.160   4.881   -17.604 1.00 107.94 ? 266 LEU B O   1 
ATOM   3415 C  CB  . LEU B 1 232 ? 4.326   6.368   -19.637 1.00 79.59  ? 266 LEU B CB  1 
ATOM   3416 C  CG  . LEU B 1 232 ? 3.610   7.572   -19.034 1.00 82.60  ? 266 LEU B CG  1 
ATOM   3417 C  CD1 . LEU B 1 232 ? 4.168   7.873   -17.657 1.00 93.47  ? 266 LEU B CD1 1 
ATOM   3418 C  CD2 . LEU B 1 232 ? 3.764   8.776   -19.946 1.00 74.44  ? 266 LEU B CD2 1 
ATOM   3419 N  N   . ARG B 1 233 ? 1.788   4.715   -19.802 1.00 98.89  ? 267 ARG B N   1 
ATOM   3420 C  CA  . ARG B 1 233 ? 0.345   4.652   -19.634 1.00 95.23  ? 267 ARG B CA  1 
ATOM   3421 C  C   . ARG B 1 233 ? -0.009  3.555   -18.689 1.00 105.08 ? 267 ARG B C   1 
ATOM   3422 O  O   . ARG B 1 233 ? -0.916  3.692   -17.878 1.00 111.16 ? 267 ARG B O   1 
ATOM   3423 C  CB  . ARG B 1 233 ? -0.333  4.372   -20.965 1.00 87.42  ? 267 ARG B CB  1 
ATOM   3424 N  N   T LEU B 1 234 ? 0.700   2.447   -18.794 1.00 105.20 ? 268 LEU B N   1 
ATOM   3425 C  CA  T LEU B 1 234 ? 0.369   1.309   -17.975 1.00 107.52 ? 268 LEU B CA  1 
ATOM   3426 C  C   T LEU B 1 234 ? 0.420   1.682   -16.507 1.00 114.27 ? 268 LEU B C   1 
ATOM   3427 O  O   T LEU B 1 234 ? -0.462  1.300   -15.746 1.00 114.81 ? 268 LEU B O   1 
ATOM   3428 C  CB  T LEU B 1 234 ? 1.318   0.161   -18.295 1.00 95.72  ? 268 LEU B CB  1 
ATOM   3429 C  CG  T LEU B 1 234 ? 0.920   -0.762  -19.446 1.00 106.03 ? 268 LEU B CG  1 
ATOM   3430 C  CD1 T LEU B 1 234 ? 0.368   0.009   -20.634 1.00 97.62  ? 268 LEU B CD1 1 
ATOM   3431 C  CD2 T LEU B 1 234 ? 2.091   -1.640  -19.856 1.00 107.42 ? 268 LEU B CD2 1 
ATOM   3432 N  N   . GLU B 1 235 ? 1.411   2.468   -16.109 1.00 115.48 ? 269 GLU B N   1 
ATOM   3433 C  CA  . GLU B 1 235 ? 1.477   2.927   -14.728 1.00 117.60 ? 269 GLU B CA  1 
ATOM   3434 C  C   . GLU B 1 235 ? 0.256   3.756   -14.372 1.00 123.53 ? 269 GLU B C   1 
ATOM   3435 O  O   . GLU B 1 235 ? 0.220   4.959   -14.608 1.00 126.80 ? 269 GLU B O   1 
ATOM   3436 C  CB  . GLU B 1 235 ? 2.738   3.749   -14.491 1.00 119.16 ? 269 GLU B CB  1 
HETATM 3437 ZN ZN  . ZN  C 2 .   ? 27.719  8.611   -7.777  1.00 50.20  ? 301 ZN  A ZN  1 
HETATM 3438 ZN ZN  . ZN  D 2 .   ? 28.901  7.373   -5.089  1.00 66.67  ? 302 ZN  A ZN  1 
HETATM 3439 ZN ZN  . ZN  E 2 .   ? 10.703  21.200  -24.114 1.00 74.63  ? 301 ZN  B ZN  1 
HETATM 3440 ZN ZN  . ZN  F 2 .   ? 7.508   21.455  -23.303 1.00 55.76  ? 302 ZN  B ZN  1 
HETATM 3441 O  O   . HOH G 3 .   ? 33.420  25.712  -11.242 1.00 30.00  ? 401 HOH A O   1 
HETATM 3442 O  O   . HOH G 3 .   ? 35.421  22.318  -11.640 1.00 52.39  ? 402 HOH A O   1 
HETATM 3443 O  O   . HOH G 3 .   ? 23.880  9.075   -14.276 1.00 46.63  ? 403 HOH A O   1 
HETATM 3444 O  O   . HOH G 3 .   ? 13.521  1.687   20.073  1.00 66.89  ? 404 HOH A O   1 
HETATM 3445 O  O   . HOH G 3 .   ? 28.072  3.798   9.139   1.00 39.50  ? 405 HOH A O   1 
HETATM 3446 O  O   . HOH G 3 .   ? 30.181  10.464  6.033   1.00 42.48  ? 406 HOH A O   1 
HETATM 3447 O  O   . HOH G 3 .   ? 26.083  -4.413  -10.210 1.00 70.70  ? 407 HOH A O   1 
HETATM 3448 O  O   . HOH G 3 .   ? 18.120  12.934  -6.759  1.00 32.31  ? 408 HOH A O   1 
HETATM 3449 O  O   . HOH G 3 .   ? 25.430  15.036  -3.582  1.00 42.47  ? 409 HOH A O   1 
HETATM 3450 O  O   . HOH G 3 .   ? 7.885   11.321  -11.090 1.00 44.66  ? 410 HOH A O   1 
HETATM 3451 O  O   . HOH G 3 .   ? 23.511  10.449  -12.498 1.00 51.20  ? 411 HOH A O   1 
HETATM 3452 O  O   . HOH G 3 .   ? 11.734  -4.673  1.681   1.00 30.00  ? 412 HOH A O   1 
HETATM 3453 O  O   . HOH G 3 .   ? 25.279  12.162  -3.797  1.00 45.46  ? 413 HOH A O   1 
HETATM 3454 O  O   . HOH G 3 .   ? 10.229  0.522   11.418  1.00 46.81  ? 414 HOH A O   1 
HETATM 3455 O  O   . HOH G 3 .   ? 21.666  29.525  -2.730  1.00 55.56  ? 415 HOH A O   1 
HETATM 3456 O  O   . HOH G 3 .   ? 8.103   3.048   18.856  1.00 30.00  ? 416 HOH A O   1 
HETATM 3457 O  O   . HOH G 3 .   ? 29.344  -6.570  -0.809  1.00 30.00  ? 417 HOH A O   1 
HETATM 3458 O  O   . HOH G 3 .   ? 15.931  -1.550  -6.817  1.00 50.43  ? 418 HOH A O   1 
HETATM 3459 O  O   . HOH G 3 .   ? 9.109   9.053   -11.474 1.00 53.23  ? 419 HOH A O   1 
HETATM 3460 O  O   . HOH G 3 .   ? 36.786  13.137  -17.484 1.00 58.09  ? 420 HOH A O   1 
HETATM 3461 O  O   . HOH G 3 .   ? 11.837  3.510   -13.199 1.00 58.57  ? 421 HOH A O   1 
HETATM 3462 O  O   . HOH G 3 .   ? 34.229  28.539  -7.609  1.00 46.45  ? 422 HOH A O   1 
HETATM 3463 O  O   . HOH G 3 .   ? 31.904  11.053  -1.358  1.00 47.80  ? 423 HOH A O   1 
HETATM 3464 O  O   . HOH G 3 .   ? 16.950  0.257   -8.463  1.00 53.15  ? 424 HOH A O   1 
HETATM 3465 O  O   . HOH G 3 .   ? 26.597  26.439  -8.602  1.00 48.11  ? 425 HOH A O   1 
HETATM 3466 O  O   . HOH G 3 .   ? 27.710  25.177  -10.473 1.00 46.18  ? 426 HOH A O   1 
HETATM 3467 O  O   . HOH G 3 .   ? 22.446  26.132  -7.228  1.00 41.57  ? 427 HOH A O   1 
HETATM 3468 O  O   . HOH G 3 .   ? 11.998  -5.433  5.454   1.00 30.00  ? 428 HOH A O   1 
HETATM 3469 O  O   . HOH G 3 .   ? 18.057  33.249  -3.161  1.00 42.88  ? 429 HOH A O   1 
HETATM 3470 O  O   . HOH G 3 .   ? 25.122  -11.705 7.020   1.00 61.18  ? 430 HOH A O   1 
HETATM 3471 O  O   . HOH G 3 .   ? 48.129  27.115  -8.114  1.00 51.27  ? 431 HOH A O   1 
HETATM 3472 O  O   . HOH G 3 .   ? 32.853  8.719   -6.407  1.00 42.37  ? 432 HOH A O   1 
HETATM 3473 O  O   . HOH G 3 .   ? 32.763  5.258   5.398   1.00 43.81  ? 433 HOH A O   1 
HETATM 3474 O  O   . HOH G 3 .   ? 28.415  15.988  -17.552 1.00 30.00  ? 434 HOH A O   1 
HETATM 3475 O  O   . HOH G 3 .   ? 41.270  9.466   2.088   1.00 53.06  ? 435 HOH A O   1 
HETATM 3476 O  O   . HOH G 3 .   ? 19.459  -4.847  -6.443  1.00 62.61  ? 436 HOH A O   1 
HETATM 3477 O  O   . HOH G 3 .   ? 3.303   13.569  -1.826  1.00 30.00  ? 437 HOH A O   1 
HETATM 3478 O  O   . HOH G 3 .   ? 10.634  21.351  2.437   1.00 61.79  ? 438 HOH A O   1 
HETATM 3479 O  O   . HOH G 3 .   ? 6.086   13.860  -8.667  1.00 30.00  ? 439 HOH A O   1 
HETATM 3480 O  O   . HOH G 3 .   ? 22.948  21.904  8.877   1.00 44.51  ? 440 HOH A O   1 
HETATM 3481 O  O   . HOH G 3 .   ? 10.752  14.227  -14.482 1.00 61.57  ? 441 HOH A O   1 
HETATM 3482 O  O   . HOH G 3 .   ? 29.268  7.087   -7.424  1.00 61.93  ? 442 HOH A O   1 
HETATM 3483 O  O   . HOH G 3 .   ? 27.719  -7.718  0.540   1.00 30.00  ? 443 HOH A O   1 
HETATM 3484 O  O   . HOH G 3 .   ? 8.521   1.349   7.408   1.00 30.00  ? 444 HOH A O   1 
HETATM 3485 O  O   . HOH G 3 .   ? 31.629  27.687  -12.907 1.00 59.55  ? 445 HOH A O   1 
HETATM 3486 O  O   . HOH G 3 .   ? 37.317  8.691   -13.279 1.00 30.00  ? 446 HOH A O   1 
HETATM 3487 O  O   . HOH G 3 .   ? 27.032  3.470   -10.563 1.00 63.44  ? 447 HOH A O   1 
HETATM 3488 O  O   . HOH G 3 .   ? 34.113  17.941  12.750  1.00 57.51  ? 448 HOH A O   1 
HETATM 3489 O  O   . HOH G 3 .   ? 37.403  11.356  6.589   1.00 30.00  ? 449 HOH A O   1 
HETATM 3490 O  O   . HOH G 3 .   ? 10.780  -4.168  8.655   1.00 70.05  ? 450 HOH A O   1 
HETATM 3491 O  O   . HOH G 3 .   ? 21.716  -2.624  -11.879 1.00 65.93  ? 451 HOH A O   1 
HETATM 3492 O  O   . HOH G 3 .   ? 21.234  29.667  1.884   1.00 56.64  ? 452 HOH A O   1 
HETATM 3493 O  O   . HOH G 3 .   ? 15.219  15.229  20.756  1.00 30.00  ? 453 HOH A O   1 
HETATM 3494 O  O   . HOH G 3 .   ? 33.217  6.444   -6.653  1.00 30.00  ? 454 HOH A O   1 
HETATM 3495 O  O   . HOH G 3 .   ? 36.800  15.522  11.677  1.00 57.92  ? 455 HOH A O   1 
HETATM 3496 O  O   . HOH G 3 .   ? 3.662   11.813  -8.442  1.00 56.98  ? 456 HOH A O   1 
HETATM 3497 O  O   . HOH G 3 .   ? 7.124   19.682  8.417   1.00 69.10  ? 457 HOH A O   1 
HETATM 3498 O  O   . HOH G 3 .   ? 5.434   12.743  3.192   1.00 30.00  ? 458 HOH A O   1 
HETATM 3499 O  O   . HOH G 3 .   ? 15.099  -8.144  -5.728  1.00 79.59  ? 459 HOH A O   1 
HETATM 3500 O  O   . HOH G 3 .   ? 12.938  -6.713  -3.046  1.00 63.98  ? 460 HOH A O   1 
HETATM 3501 O  O   . HOH G 3 .   ? 10.403  -1.310  -8.013  1.00 69.06  ? 461 HOH A O   1 
HETATM 3502 O  O   . HOH G 3 .   ? 30.053  5.071   -8.104  1.00 65.36  ? 462 HOH A O   1 
HETATM 3503 O  O   . HOH G 3 .   ? 6.825   0.531   12.742  1.00 30.00  ? 463 HOH A O   1 
HETATM 3504 O  O   . HOH G 3 .   ? 42.384  16.847  -10.110 1.00 57.85  ? 464 HOH A O   1 
HETATM 3505 O  O   . HOH G 3 .   ? 34.693  27.764  -10.394 1.00 52.56  ? 465 HOH A O   1 
HETATM 3506 O  O   . HOH G 3 .   ? 12.979  15.456  17.270  1.00 30.00  ? 466 HOH A O   1 
HETATM 3507 O  O   . HOH G 3 .   ? 22.925  28.467  -6.650  1.00 52.95  ? 467 HOH A O   1 
HETATM 3508 O  O   . HOH G 3 .   ? 32.150  10.184  -20.745 1.00 30.00  ? 468 HOH A O   1 
HETATM 3509 O  O   . HOH G 3 .   ? 22.942  29.322  -0.742  1.00 53.51  ? 469 HOH A O   1 
HETATM 3510 O  O   . HOH G 3 .   ? 27.256  -7.492  -2.173  1.00 30.00  ? 470 HOH A O   1 
HETATM 3511 O  O   . HOH G 3 .   ? 31.058  -6.620  4.548   1.00 30.00  ? 471 HOH A O   1 
HETATM 3512 O  O   . HOH G 3 .   ? 34.300  15.649  12.241  1.00 61.43  ? 472 HOH A O   1 
HETATM 3513 O  O   . HOH G 3 .   ? 34.711  6.066   -5.015  1.00 58.01  ? 473 HOH A O   1 
HETATM 3514 O  O   . HOH G 3 .   ? 21.549  25.840  -9.624  1.00 49.46  ? 474 HOH A O   1 
HETATM 3515 O  O   . HOH G 3 .   ? 16.649  5.254   20.362  1.00 30.00  ? 475 HOH A O   1 
HETATM 3516 O  O   . HOH G 3 .   ? 10.292  -0.079  7.948   1.00 30.00  ? 476 HOH A O   1 
HETATM 3517 O  O   . HOH G 3 .   ? 18.171  10.267  21.173  1.00 30.00  ? 477 HOH A O   1 
HETATM 3518 O  O   . HOH G 3 .   ? 38.809  11.653  8.456   1.00 55.18  ? 478 HOH A O   1 
HETATM 3519 O  O   . HOH G 3 .   ? 24.827  11.438  -18.919 1.00 58.26  ? 479 HOH A O   1 
HETATM 3520 O  O   . HOH G 3 .   ? 46.989  15.068  1.300   1.00 30.00  ? 480 HOH A O   1 
HETATM 3521 O  O   . HOH G 3 .   ? 31.742  30.158  -7.812  1.00 51.79  ? 481 HOH A O   1 
HETATM 3522 O  O   . HOH G 3 .   ? 16.363  -10.961 -7.649  1.00 71.64  ? 482 HOH A O   1 
HETATM 3523 O  O   . HOH H 3 .   ? -0.100  29.136  -46.698 1.00 30.00  ? 401 HOH B O   1 
HETATM 3524 O  O   . HOH H 3 .   ? 7.459   14.762  -22.531 1.00 57.57  ? 402 HOH B O   1 
HETATM 3525 O  O   . HOH H 3 .   ? 1.277   23.538  -20.261 1.00 58.58  ? 403 HOH B O   1 
HETATM 3526 O  O   . HOH H 3 .   ? 20.755  11.148  -32.179 1.00 60.64  ? 404 HOH B O   1 
HETATM 3527 O  O   . HOH H 3 .   ? 13.716  26.012  -28.824 1.00 52.03  ? 405 HOH B O   1 
HETATM 3528 O  O   . HOH H 3 .   ? 16.562  17.833  -33.405 1.00 51.22  ? 406 HOH B O   1 
HETATM 3529 O  O   . HOH H 3 .   ? 1.105   26.281  -30.386 1.00 56.61  ? 407 HOH B O   1 
HETATM 3530 O  O   . HOH H 3 .   ? 13.742  21.766  -11.290 1.00 55.20  ? 408 HOH B O   1 
HETATM 3531 O  O   . HOH H 3 .   ? 6.595   34.834  -23.281 1.00 73.99  ? 409 HOH B O   1 
HETATM 3532 O  O   . HOH H 3 .   ? 16.434  27.441  -29.458 1.00 56.84  ? 410 HOH B O   1 
HETATM 3533 O  O   . HOH H 3 .   ? 14.388  7.187   -41.497 1.00 54.49  ? 411 HOH B O   1 
HETATM 3534 O  O   . HOH H 3 .   ? 8.770   38.017  -22.915 1.00 62.79  ? 412 HOH B O   1 
HETATM 3535 O  O   . HOH H 3 .   ? 9.478   5.388   -19.877 1.00 72.68  ? 413 HOH B O   1 
HETATM 3536 O  O   . HOH H 3 .   ? 5.183   30.320  -50.685 1.00 84.46  ? 414 HOH B O   1 
HETATM 3537 O  O   . HOH H 3 .   ? 11.001  17.561  -22.154 1.00 48.30  ? 415 HOH B O   1 
HETATM 3538 O  O   . HOH H 3 .   ? 9.515   21.800  -22.467 1.00 60.22  ? 416 HOH B O   1 
HETATM 3539 O  O   . HOH H 3 .   ? 21.961  23.324  -33.876 1.00 63.09  ? 417 HOH B O   1 
HETATM 3540 O  O   . HOH H 3 .   ? -5.209  14.354  -34.082 1.00 64.53  ? 418 HOH B O   1 
HETATM 3541 O  O   . HOH H 3 .   ? 21.412  25.215  -12.119 1.00 53.02  ? 419 HOH B O   1 
HETATM 3542 O  O   . HOH H 3 .   ? -1.926  -1.331  -15.502 1.00 30.00  ? 420 HOH B O   1 
HETATM 3543 O  O   . HOH H 3 .   ? 22.180  13.899  -35.807 1.00 45.77  ? 421 HOH B O   1 
HETATM 3544 O  O   . HOH H 3 .   ? 10.478  21.071  -20.560 1.00 68.78  ? 422 HOH B O   1 
HETATM 3545 O  O   . HOH H 3 .   ? 6.566   17.194  -45.187 1.00 30.00  ? 423 HOH B O   1 
HETATM 3546 O  O   . HOH H 3 .   ? 21.136  30.433  -18.356 1.00 53.03  ? 424 HOH B O   1 
HETATM 3547 O  O   . HOH H 3 .   ? 0.723   26.752  -46.912 1.00 67.90  ? 425 HOH B O   1 
HETATM 3548 O  O   . HOH H 3 .   ? -1.026  26.383  -45.046 1.00 30.00  ? 426 HOH B O   1 
HETATM 3549 O  O   . HOH H 3 .   ? -1.661  0.777   -12.615 1.00 30.00  ? 427 HOH B O   1 
HETATM 3550 O  O   . HOH H 3 .   ? -3.455  12.034  -41.356 1.00 30.00  ? 428 HOH B O   1 
HETATM 3551 O  O   . HOH H 3 .   ? 8.099   14.400  -14.526 1.00 55.23  ? 429 HOH B O   1 
HETATM 3552 O  O   . HOH H 3 .   ? 8.008   15.497  -45.318 1.00 63.88  ? 430 HOH B O   1 
HETATM 3553 O  O   . HOH H 3 .   ? -1.517  11.639  -43.809 1.00 30.00  ? 431 HOH B O   1 
HETATM 3554 O  O   . HOH H 3 .   ? 18.992  18.573  -23.339 1.00 66.04  ? 432 HOH B O   1 
HETATM 3555 O  O   . HOH H 3 .   ? 27.826  36.449  -26.262 1.00 30.00  ? 433 HOH B O   1 
HETATM 3556 O  O   . HOH H 3 .   ? -1.388  22.507  -44.574 1.00 30.00  ? 434 HOH B O   1 
HETATM 3557 O  O   . HOH H 3 .   ? 20.381  17.797  -18.641 1.00 55.94  ? 435 HOH B O   1 
HETATM 3558 O  O   . HOH H 3 .   ? 24.477  36.185  -47.697 1.00 30.00  ? 436 HOH B O   1 
HETATM 3559 O  O   . HOH H 3 .   ? 8.340   17.058  -13.244 1.00 30.00  ? 437 HOH B O   1 
HETATM 3560 O  O   . HOH H 3 .   ? -6.927  21.728  -30.052 1.00 69.11  ? 438 HOH B O   1 
HETATM 3561 O  O   . HOH H 3 .   ? 7.405   20.512  -13.455 1.00 30.00  ? 439 HOH B O   1 
HETATM 3562 O  O   . HOH H 3 .   ? 11.373  27.000  -17.457 1.00 30.00  ? 440 HOH B O   1 
HETATM 3563 O  O   . HOH H 3 .   ? 14.920  13.846  -23.694 1.00 30.00  ? 441 HOH B O   1 
HETATM 3564 O  O   . HOH H 3 .   ? 12.203  22.572  -12.954 1.00 30.00  ? 442 HOH B O   1 
HETATM 3565 O  O   . HOH H 3 .   ? 14.329  17.301  -21.494 1.00 59.43  ? 443 HOH B O   1 
HETATM 3566 O  O   . HOH H 3 .   ? 14.118  27.513  -15.688 1.00 50.92  ? 444 HOH B O   1 
HETATM 3567 O  O   . HOH H 3 .   ? 10.320  11.024  -15.182 1.00 30.00  ? 445 HOH B O   1 
HETATM 3568 O  O   . HOH H 3 .   ? 23.862  39.353  -47.678 1.00 30.00  ? 446 HOH B O   1 
HETATM 3569 O  O   . HOH H 3 .   ? -11.341 19.186  -43.900 1.00 30.00  ? 447 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 5   ? 1.3429 1.5077 1.1344 0.0788  -0.1294 0.1058  39  SER A N   
2    C CA  . SER A 5   ? 1.2543 1.3947 1.0771 0.0558  -0.1043 0.0985  39  SER A CA  
3    C C   . SER A 5   ? 1.1299 1.2773 1.0142 0.0459  -0.0833 0.1023  39  SER A C   
4    O O   . SER A 5   ? 1.1766 1.2895 1.0800 0.0370  -0.0522 0.1007  39  SER A O   
5    C CB  . SER A 5   ? 1.3494 1.5205 1.1993 0.0298  -0.1328 0.0839  39  SER A CB  
6    O OG  . SER A 5   ? 1.5420 1.6972 1.3326 0.0379  -0.1524 0.0779  39  SER A OG  
7    N N   . ASP A 6   ? 1.1093 1.3042 1.0259 0.0481  -0.1010 0.1055  40  ASP A N   
8    C CA  . ASP A 6   ? 1.1249 1.3244 1.0919 0.0419  -0.0854 0.1079  40  ASP A CA  
9    C C   . ASP A 6   ? 1.1086 1.2470 1.0485 0.0604  -0.0516 0.1191  40  ASP A C   
10   O O   . ASP A 6   ? 1.1532 1.2747 1.0482 0.0876  -0.0539 0.1288  40  ASP A O   
11   C CB  . ASP A 6   ? 1.0688 1.3310 1.0637 0.0462  -0.1096 0.1073  40  ASP A CB  
12   C CG  . ASP A 6   ? 1.0982 1.4238 1.1247 0.0203  -0.1400 0.0990  40  ASP A CG  
13   O OD1 . ASP A 6   ? 1.2390 1.5593 1.2483 0.0081  -0.1526 0.0947  40  ASP A OD1 
14   O OD2 . ASP A 6   ? 0.9749 1.3531 1.0405 0.0110  -0.1511 0.0969  40  ASP A OD2 
15   N N   . GLN A 7   ? 0.9249 1.0291 0.8928 0.0454  -0.0220 0.1182  41  GLN A N   
16   C CA  . GLN A 7   ? 0.9019 0.9489 0.8527 0.0548  0.0125  0.1300  41  GLN A CA  
17   C C   . GLN A 7   ? 0.8022 0.8567 0.8046 0.0501  0.0134  0.1307  41  GLN A C   
18   O O   . GLN A 7   ? 0.7164 0.8003 0.7797 0.0287  0.0063  0.1203  41  GLN A O   
19   C CB  . GLN A 7   ? 0.9496 0.9590 0.9039 0.0404  0.0477  0.1274  41  GLN A CB  
20   C CG  . GLN A 7   ? 1.1413 1.0981 1.0933 0.0403  0.0866  0.1401  41  GLN A CG  
21   C CD  . GLN A 7   ? 1.2695 1.2135 1.2632 0.0192  0.1209  0.1323  41  GLN A CD  
22   O OE1 . GLN A 7   ? 1.2338 1.1974 1.2415 0.0111  0.1178  0.1173  41  GLN A OE1 
23   N NE2 . GLN A 7   ? 1.0479 0.9593 1.0646 0.0106  0.1525  0.1413  41  GLN A NE2 
24   N N   . ARG A 8   ? 0.6747 0.6972 0.6482 0.0710  0.0191  0.1424  42  ARG A N   
25   C CA  . ARG A 8   ? 0.7149 0.7375 0.7269 0.0717  0.0167  0.1415  42  ARG A CA  
26   C C   . ARG A 8   ? 0.7093 0.6746 0.7393 0.0581  0.0503  0.1487  42  ARG A C   
27   O O   . ARG A 8   ? 0.7679 0.6794 0.7540 0.0620  0.0766  0.1622  42  ARG A O   
28   C CB  . ARG A 8   ? 0.6878 0.7079 0.6613 0.1051  -0.0017 0.1470  42  ARG A CB  
29   C CG  . ARG A 8   ? 0.7742 0.8705 0.7752 0.1117  -0.0344 0.1337  42  ARG A CG  
30   C CD  . ARG A 8   ? 0.8765 0.9699 0.8677 0.1424  -0.0466 0.1328  42  ARG A CD  
31   N NE  . ARG A 8   ? 0.8117 0.9867 0.8220 0.1533  -0.0747 0.1198  42  ARG A NE  
32   C CZ  . ARG A 8   ? 1.1180 1.3132 1.1290 0.1823  -0.0888 0.1125  42  ARG A CZ  
33   N NH1 . ARG A 8   ? 1.2210 1.3528 1.2109 0.2048  -0.0820 0.1170  42  ARG A NH1 
34   N NH2 . ARG A 8   ? 1.2106 1.4918 1.2449 0.1885  -0.1099 0.0995  42  ARG A NH2 
35   N N   . PHE A 9   ? 0.6721 0.6495 0.7658 0.0404  0.0489  0.1399  43  PHE A N   
36   C CA  . PHE A 9   ? 0.6542 0.5857 0.7801 0.0237  0.0766  0.1443  43  PHE A CA  
37   C C   . PHE A 9   ? 0.7263 0.6639 0.8945 0.0216  0.0593  0.1367  43  PHE A C   
38   O O   . PHE A 9   ? 0.6022 0.5811 0.8210 0.0061  0.0424  0.1226  43  PHE A O   
39   C CB  . PHE A 9   ? 0.5437 0.4859 0.7157 -0.0027 0.0956  0.1362  43  PHE A CB  
40   C CG  . PHE A 9   ? 0.5851 0.4943 0.8063 -0.0229 0.1229  0.1380  43  PHE A CG  
41   C CD1 . PHE A 9   ? 0.6185 0.4796 0.8133 -0.0268 0.1617  0.1525  43  PHE A CD1 
42   C CD2 . PHE A 9   ? 0.5441 0.4706 0.8371 -0.0399 0.1093  0.1256  43  PHE A CD2 
43   C CE1 . PHE A 9   ? 0.6392 0.4762 0.8864 -0.0493 0.1881  0.1544  43  PHE A CE1 
44   C CE2 . PHE A 9   ? 0.5663 0.4664 0.9114 -0.0597 0.1312  0.1259  43  PHE A CE2 
45   C CZ  . PHE A 9   ? 0.6078 0.4663 0.9343 -0.0655 0.1715  0.1402  43  PHE A CZ  
46   N N   . GLY A 10  ? 0.6598 0.5508 0.8012 0.0377  0.0614  0.1458  44  GLY A N   
47   C CA  . GLY A 10  ? 0.6632 0.5536 0.8351 0.0401  0.0433  0.1362  44  GLY A CA  
48   C C   . GLY A 10  ? 0.6850 0.6387 0.8558 0.0557  0.0115  0.1225  44  GLY A C   
49   O O   . GLY A 10  ? 0.6887 0.6670 0.8173 0.0792  0.0002  0.1247  44  GLY A O   
50   N N   . ASP A 11  ? 0.7314 0.7137 0.9491 0.0413  -0.0033 0.1080  45  ASP A N   
51   C CA  . ASP A 11  ? 0.7503 0.7967 0.9700 0.0497  -0.0293 0.0950  45  ASP A CA  
52   C C   . ASP A 11  ? 0.6262 0.7310 0.8617 0.0297  -0.0376 0.0917  45  ASP A C   
53   O O   . ASP A 11  ? 0.6675 0.8276 0.9118 0.0260  -0.0573 0.0823  45  ASP A O   
54   C CB  . ASP A 11  ? 0.8449 0.8893 1.0961 0.0429  -0.0424 0.0814  45  ASP A CB  
55   C CG  . ASP A 11  ? 0.9419 0.9173 1.1829 0.0571  -0.0366 0.0833  45  ASP A CG  
56   O OD1 . ASP A 11  ? 1.0794 1.0150 1.2795 0.0790  -0.0269 0.0952  45  ASP A OD1 
57   O OD2 . ASP A 11  ? 0.9213 0.8772 1.1921 0.0457  -0.0446 0.0733  45  ASP A OD2 
58   N N   . LEU A 12  ? 0.6584 0.7504 0.8947 0.0163  -0.0228 0.0989  46  LEU A N   
59   C CA  . LEU A 12  ? 0.5447 0.6793 0.7960 -0.0035 -0.0328 0.0947  46  LEU A CA  
60   C C   . LEU A 12  ? 0.5511 0.6908 0.7587 0.0081  -0.0280 0.1023  46  LEU A C   
61   O O   . LEU A 12  ? 0.5488 0.6515 0.7154 0.0287  -0.0129 0.1124  46  LEU A O   
62   C CB  . LEU A 12  ? 0.5218 0.6370 0.8225 -0.0313 -0.0244 0.0902  46  LEU A CB  
63   C CG  . LEU A 12  ? 0.5302 0.6186 0.8746 -0.0421 -0.0237 0.0846  46  LEU A CG  
64   C CD1 . LEU A 12  ? 0.6645 0.7301 1.0580 -0.0632 -0.0087 0.0814  46  LEU A CD1 
65   C CD2 . LEU A 12  ? 0.6227 0.7465 0.9830 -0.0508 -0.0527 0.0744  46  LEU A CD2 
66   N N   . VAL A 13  ? 0.5716 0.7527 0.7842 -0.0063 -0.0438 0.0976  47  VAL A N   
67   C CA  . VAL A 13  ? 0.4981 0.6852 0.6721 0.0003  -0.0448 0.1015  47  VAL A CA  
68   C C   . VAL A 13  ? 0.5126 0.6920 0.7091 -0.0233 -0.0420 0.0955  47  VAL A C   
69   O O   . VAL A 13  ? 0.4917 0.6886 0.7310 -0.0460 -0.0560 0.0877  47  VAL A O   
70   C CB  . VAL A 13  ? 0.4377 0.6861 0.5939 0.0072  -0.0726 0.0995  47  VAL A CB  
71   C CG1 . VAL A 13  ? 0.4741 0.7228 0.5870 0.0160  -0.0773 0.1029  47  VAL A CG1 
72   C CG2 . VAL A 13  ? 0.3709 0.6347 0.5152 0.0337  -0.0769 0.1004  47  VAL A CG2 
73   N N   . PHE A 14  ? 0.4981 0.6479 0.6621 -0.0163 -0.0251 0.0983  48  PHE A N   
74   C CA  . PHE A 14  ? 0.5005 0.6399 0.6813 -0.0323 -0.0202 0.0893  48  PHE A CA  
75   C C   . PHE A 14  ? 0.5702 0.7166 0.7010 -0.0252 -0.0319 0.0880  48  PHE A C   
76   O O   . PHE A 14  ? 0.6379 0.7706 0.7132 -0.0040 -0.0254 0.0966  48  PHE A O   
77   C CB  . PHE A 14  ? 0.5424 0.6358 0.7373 -0.0323 0.0184  0.0898  48  PHE A CB  
78   C CG  . PHE A 14  ? 0.5564 0.6427 0.8123 -0.0448 0.0257  0.0876  48  PHE A CG  
79   C CD1 . PHE A 14  ? 0.5580 0.6279 0.8094 -0.0357 0.0335  0.0973  48  PHE A CD1 
80   C CD2 . PHE A 14  ? 0.4895 0.5818 0.8064 -0.0642 0.0210  0.0744  48  PHE A CD2 
81   C CE1 . PHE A 14  ? 0.5598 0.6196 0.8656 -0.0480 0.0366  0.0939  48  PHE A CE1 
82   C CE2 . PHE A 14  ? 0.4055 0.4910 0.7794 -0.0756 0.0232  0.0713  48  PHE A CE2 
83   C CZ  . PHE A 14  ? 0.4690 0.5383 0.8368 -0.0686 0.0312  0.0810  48  PHE A CZ  
84   N N   . ARG A 15  ? 0.5453 0.7076 0.6929 -0.0428 -0.0528 0.0770  49  ARG A N   
85   C CA  . ARG A 15  ? 0.5765 0.7412 0.6801 -0.0397 -0.0687 0.0726  49  ARG A CA  
86   C C   . ARG A 15  ? 0.5270 0.6691 0.6481 -0.0513 -0.0667 0.0575  49  ARG A C   
87   O O   . ARG A 15  ? 0.4546 0.6024 0.6291 -0.0700 -0.0776 0.0497  49  ARG A O   
88   C CB  . ARG A 15  ? 0.5639 0.7796 0.6648 -0.0504 -0.1089 0.0739  49  ARG A CB  
89   C CG  . ARG A 15  ? 0.8188 1.0376 0.8703 -0.0456 -0.1289 0.0706  49  ARG A CG  
90   C CD  . ARG A 15  ? 0.8506 1.1255 0.8939 -0.0467 -0.1592 0.0765  49  ARG A CD  
91   N NE  . ARG A 15  ? 0.7898 1.0989 0.8555 -0.0774 -0.1941 0.0716  49  ARG A NE  
92   C CZ  . ARG A 15  ? 0.9526 1.2619 0.9910 -0.0853 -0.2200 0.0659  49  ARG A CZ  
93   N NH1 . ARG A 15  ? 0.9595 1.2385 0.9442 -0.0628 -0.2159 0.0627  49  ARG A NH1 
94   N NH2 . ARG A 15  ? 0.7589 1.0752 0.8170 -0.1093 -0.2381 0.0580  49  ARG A NH2 
95   N N   . GLN A 16  ? 0.5524 0.6664 0.6253 -0.0381 -0.0547 0.0520  50  GLN A N   
96   C CA  . GLN A 16  ? 0.6069 0.6986 0.6893 -0.0432 -0.0530 0.0335  50  GLN A CA  
97   C C   . GLN A 16  ? 0.5999 0.7067 0.6712 -0.0569 -0.0995 0.0253  50  GLN A C   
98   O O   . GLN A 16  ? 0.7107 0.8213 0.7276 -0.0498 -0.1166 0.0278  50  GLN A O   
99   C CB  . GLN A 16  ? 0.5689 0.6222 0.5981 -0.0225 -0.0166 0.0295  50  GLN A CB  
100  C CG  . GLN A 16  ? 0.6565 0.6882 0.6978 -0.0223 -0.0081 0.0062  50  GLN A CG  
101  C CD  . GLN A 16  ? 0.6528 0.6522 0.6595 -0.0047 0.0436  0.0026  50  GLN A CD  
102  O OE1 . GLN A 16  ? 0.7346 0.7198 0.6965 0.0059  0.0702  0.0203  50  GLN A OE1 
103  N NE2 . GLN A 16  ? 0.6745 0.6609 0.6997 -0.0013 0.0582  -0.0208 50  GLN A NE2 
104  N N   . LEU A 17  ? 0.5155 0.6277 0.6373 -0.0778 -0.1230 0.0162  51  LEU A N   
105  C CA  . LEU A 17  ? 0.6051 0.7239 0.7183 -0.0964 -0.1690 0.0101  51  LEU A CA  
106  C C   . LEU A 17  ? 0.5545 0.6335 0.6427 -0.0886 -0.1745 -0.0111 51  LEU A C   
107  O O   . LEU A 17  ? 0.6234 0.6985 0.6810 -0.0984 -0.2111 -0.0160 51  LEU A O   
108  C CB  . LEU A 17  ? 0.5128 0.6467 0.6820 -0.1239 -0.1960 0.0121  51  LEU A CB  
109  C CG  . LEU A 17  ? 0.4616 0.6362 0.6536 -0.1336 -0.1951 0.0299  51  LEU A CG  
110  C CD1 . LEU A 17  ? 0.5388 0.7123 0.7532 -0.1520 -0.2105 0.0281  51  LEU A CD1 
111  C CD2 . LEU A 17  ? 0.5390 0.7513 0.6906 -0.1292 -0.2027 0.0422  51  LEU A CD2 
112  N N   . ALA A 18  ? 0.6216 0.6724 0.7228 -0.0715 -0.1388 -0.0249 52  ALA A N   
113  C CA  . ALA A 18  ? 0.6703 0.6843 0.7521 -0.0591 -0.1378 -0.0497 52  ALA A CA  
114  C C   . ALA A 18  ? 0.6655 0.6657 0.7658 -0.0388 -0.0829 -0.0598 52  ALA A C   
115  O O   . ALA A 18  ? 0.6463 0.6632 0.7850 -0.0404 -0.0540 -0.0470 52  ALA A O   
116  C CB  . ALA A 18  ? 0.6196 0.6208 0.7404 -0.0769 -0.1812 -0.0644 52  ALA A CB  
117  N N   . PRO A 19  ? 0.7419 0.7132 0.8155 -0.0202 -0.0659 -0.0830 53  PRO A N   
118  C CA  . PRO A 19  ? 0.7497 0.7171 0.8578 -0.0051 -0.0128 -0.0957 53  PRO A CA  
119  C C   . PRO A 19  ? 0.7047 0.6883 0.9115 -0.0168 -0.0199 -0.1033 53  PRO A C   
120  O O   . PRO A 19  ? 0.7454 0.7209 0.9830 -0.0248 -0.0632 -0.1173 53  PRO A O   
121  C CB  . PRO A 19  ? 0.7562 0.6922 0.8191 0.0160  -0.0054 -0.1251 53  PRO A CB  
122  C CG  . PRO A 19  ? 0.8485 0.7669 0.8699 0.0081  -0.0659 -0.1302 53  PRO A CG  
123  C CD  . PRO A 19  ? 0.7411 0.6836 0.7462 -0.0108 -0.0899 -0.0987 53  PRO A CD  
124  N N   . ASN A 20  ? 0.6186 0.6210 0.8721 -0.0187 0.0194  -0.0928 54  ASN A N   
125  C CA  . ASN A 20  ? 0.5911 0.6114 0.9410 -0.0289 0.0182  -0.0980 54  ASN A CA  
126  C C   . ASN A 20  ? 0.5151 0.5483 0.8906 -0.0518 -0.0267 -0.0801 54  ASN A C   
127  O O   . ASN A 20  ? 0.4878 0.5295 0.9366 -0.0613 -0.0404 -0.0856 54  ASN A O   
128  C CB  . ASN A 20  ? 0.5961 0.6085 0.9985 -0.0190 0.0070  -0.1318 54  ASN A CB  
129  C CG  . ASN A 20  ? 0.9079 0.9125 1.2885 0.0056  0.0539  -0.1547 54  ASN A CG  
130  O OD1 . ASN A 20  ? 0.9682 0.9888 1.3691 0.0106  0.1096  -0.1527 54  ASN A OD1 
131  N ND2 . ASN A 20  ? 0.8837 0.8621 1.2199 0.0197  0.0318  -0.1769 54  ASN A ND2 
132  N N   . VAL A 21  ? 0.5681 0.5219 0.4868 -0.0508 0.0273  0.0595  55  VAL A N   
133  C CA  . VAL A 21  ? 0.6038 0.5580 0.5363 -0.0514 0.0146  0.0601  55  VAL A CA  
134  C C   . VAL A 21  ? 0.5894 0.5506 0.5258 -0.0520 0.0140  0.0751  55  VAL A C   
135  O O   . VAL A 21  ? 0.6929 0.6563 0.6085 -0.0540 0.0112  0.0849  55  VAL A O   
136  C CB  . VAL A 21  ? 0.6243 0.5720 0.5383 -0.0549 -0.0006 0.0549  55  VAL A CB  
137  C CG1 . VAL A 21  ? 0.6012 0.5521 0.5269 -0.0562 -0.0092 0.0572  55  VAL A CG1 
138  C CG2 . VAL A 21  ? 0.5726 0.5081 0.4827 -0.0522 -0.0030 0.0397  55  VAL A CG2 
139  N N   . TRP A 22  ? 0.5344 0.4979 0.4974 -0.0490 0.0144  0.0753  56  TRP A N   
140  C CA  . TRP A 22  ? 0.5583 0.5269 0.5304 -0.0467 0.0122  0.0862  56  TRP A CA  
141  C C   . TRP A 22  ? 0.5975 0.5709 0.5826 -0.0435 0.0044  0.0792  56  TRP A C   
142  O O   . TRP A 22  ? 0.5683 0.5376 0.5584 -0.0428 0.0018  0.0676  56  TRP A O   
143  C CB  . TRP A 22  ? 0.5121 0.4754 0.5039 -0.0450 0.0224  0.0936  56  TRP A CB  
144  C CG  . TRP A 22  ? 0.5659 0.5253 0.5401 -0.0487 0.0335  0.1044  56  TRP A CG  
145  C CD1 . TRP A 22  ? 0.6280 0.5842 0.5837 -0.0489 0.0335  0.1216  56  TRP A CD1 
146  C CD2 . TRP A 22  ? 0.5784 0.5372 0.5493 -0.0518 0.0466  0.0986  56  TRP A CD2 
147  N NE1 . TRP A 22  ? 0.6938 0.6459 0.6287 -0.0528 0.0470  0.1280  56  TRP A NE1 
148  C CE2 . TRP A 22  ? 0.6083 0.5641 0.5542 -0.0546 0.0570  0.1132  56  TRP A CE2 
149  C CE3 . TRP A 22  ? 0.5345 0.4961 0.5218 -0.0513 0.0503  0.0821  56  TRP A CE3 
150  C CZ2 . TRP A 22  ? 0.5359 0.4937 0.4715 -0.0574 0.0745  0.1109  56  TRP A CZ2 
151  C CZ3 . TRP A 22  ? 0.5924 0.5574 0.5763 -0.0529 0.0660  0.0787  56  TRP A CZ3 
152  C CH2 . TRP A 22  ? 0.6272 0.5916 0.5851 -0.0562 0.0798  0.0926  56  TRP A CH2 
153  N N   . GLN A 23  ? 0.5153 0.4981 0.5049 -0.0405 0.0003  0.0860  57  GLN A N   
154  C CA  . GLN A 23  ? 0.5279 0.5193 0.5281 -0.0362 -0.0036 0.0795  57  GLN A CA  
155  C C   . GLN A 23  ? 0.5379 0.5278 0.5620 -0.0270 -0.0020 0.0799  57  GLN A C   
156  O O   . GLN A 23  ? 0.4744 0.4651 0.5039 -0.0239 -0.0025 0.0910  57  GLN A O   
157  C CB  . GLN A 23  ? 0.5300 0.5387 0.5209 -0.0397 -0.0088 0.0842  57  GLN A CB  
158  C CG  . GLN A 23  ? 0.5698 0.5913 0.5676 -0.0366 -0.0085 0.0774  57  GLN A CG  
159  C CD  . GLN A 23  ? 0.5630 0.6096 0.5673 -0.0379 -0.0103 0.0838  57  GLN A CD  
160  O OE1 . GLN A 23  ? 0.5959 0.6513 0.6137 -0.0321 -0.0129 0.0905  57  GLN A OE1 
161  N NE2 . GLN A 23  ? 0.4830 0.5415 0.4795 -0.0457 -0.0096 0.0826  57  GLN A NE2 
162  N N   . HIS A 24  ? 0.5779 0.5626 0.6149 -0.0218 -0.0025 0.0673  58  HIS A N   
163  C CA  . HIS A 24  ? 0.6069 0.5864 0.6675 -0.0123 -0.0033 0.0633  58  HIS A CA  
164  C C   . HIS A 24  ? 0.5710 0.5646 0.6320 -0.0038 -0.0055 0.0542  58  HIS A C   
165  O O   . HIS A 24  ? 0.5546 0.5546 0.5995 -0.0058 -0.0057 0.0463  58  HIS A O   
166  C CB  . HIS A 24  ? 0.4590 0.4218 0.5370 -0.0120 -0.0037 0.0529  58  HIS A CB  
167  C CG  . HIS A 24  ? 0.5166 0.4786 0.5867 -0.0108 -0.0089 0.0367  58  HIS A CG  
168  N ND1 . HIS A 24  ? 0.5975 0.5618 0.6652 -0.0019 -0.0137 0.0238  58  HIS A ND1 
169  C CD2 . HIS A 24  ? 0.4996 0.4571 0.5617 -0.0160 -0.0113 0.0312  58  HIS A CD2 
170  C CE1 . HIS A 24  ? 0.5445 0.5042 0.5985 -0.0026 -0.0195 0.0129  58  HIS A CE1 
171  N NE2 . HIS A 24  ? 0.4989 0.4540 0.5518 -0.0107 -0.0194 0.0173  58  HIS A NE2 
172  N N   . THR A 25  ? 0.4395 0.4374 0.5182 0.0063  -0.0066 0.0557  59  THR A N   
173  C CA  . THR A 25  ? 0.5241 0.5408 0.6071 0.0167  -0.0057 0.0463  59  THR A CA  
174  C C   . THR A 25  ? 0.5895 0.5933 0.6945 0.0311  -0.0088 0.0332  59  THR A C   
175  O O   . THR A 25  ? 0.5197 0.5087 0.6446 0.0355  -0.0128 0.0403  59  THR A O   
176  C CB  . THR A 25  ? 0.5520 0.5924 0.6404 0.0179  -0.0058 0.0579  59  THR A CB  
177  O OG1 . THR A 25  ? 0.5329 0.5819 0.6014 0.0035  -0.0055 0.0682  59  THR A OG1 
178  C CG2 . THR A 25  ? 0.5030 0.5698 0.6011 0.0286  -0.0013 0.0467  59  THR A CG2 
179  N N   . SER A 26  ? 0.6491 0.6556 0.7479 0.0384  -0.0079 0.0145  60  SER A N   
180  C CA  . SER A 26  ? 0.5102 0.5050 0.6266 0.0541  -0.0122 -0.0031 60  SER A CA  
181  C C   . SER A 26  ? 0.5188 0.5402 0.6337 0.0677  -0.0056 -0.0145 60  SER A C   
182  O O   . SER A 26  ? 0.5315 0.5781 0.6262 0.0622  0.0031  -0.0121 60  SER A O   
183  C CB  . SER A 26  ? 0.4714 0.4449 0.5806 0.0535  -0.0185 -0.0200 60  SER A CB  
184  O OG  . SER A 26  ? 0.6689 0.6510 0.7467 0.0451  -0.0161 -0.0214 60  SER A OG  
185  N N   . PHE A 27  ? 0.5697 0.5853 0.7079 0.0855  -0.0092 -0.0272 61  PHE A N   
186  C CA  . PHE A 27  ? 0.5645 0.6083 0.7088 0.1020  -0.0014 -0.0404 61  PHE A CA  
187  C C   . PHE A 27  ? 0.5651 0.5958 0.7046 0.1183  -0.0035 -0.0695 61  PHE A C   
188  O O   . PHE A 27  ? 0.7030 0.6988 0.8517 0.1210  -0.0159 -0.0787 61  PHE A O   
189  C CB  . PHE A 27  ? 0.5955 0.6477 0.7747 0.1134  -0.0051 -0.0318 61  PHE A CB  
190  C CG  . PHE A 27  ? 0.4799 0.5418 0.6610 0.0990  -0.0069 -0.0046 61  PHE A CG  
191  C CD1 . PHE A 27  ? 0.5410 0.5726 0.7238 0.0891  -0.0161 0.0128  61  PHE A CD1 
192  C CD2 . PHE A 27  ? 0.4654 0.5671 0.6462 0.0948  0.0008  0.0031  61  PHE A CD2 
193  C CE1 . PHE A 27  ? 0.5106 0.5496 0.6881 0.0773  -0.0181 0.0358  61  PHE A CE1 
194  C CE2 . PHE A 27  ? 0.4512 0.5597 0.6319 0.0821  -0.0041 0.0255  61  PHE A CE2 
195  C CZ  . PHE A 27  ? 0.4899 0.5661 0.6657 0.0743  -0.0139 0.0411  61  PHE A CZ  
196  N N   . MET A 28  ? 0.5396 0.5994 0.6646 0.1287  0.0092  -0.0843 62  MET A N   
197  C CA  . MET A 28  ? 0.6540 0.7052 0.7658 0.1462  0.0089  -0.1147 62  MET A CA  
198  C C   . MET A 28  ? 0.8669 0.9584 0.9830 0.1636  0.0260  -0.1279 62  MET A C   
199  O O   . MET A 28  ? 0.8788 1.0089 0.9901 0.1547  0.0416  -0.1141 62  MET A O   
200  C CB  . MET A 28  ? 0.7055 0.7451 0.7718 0.1360  0.0078  -0.1212 62  MET A CB  
201  C CG  . MET A 28  ? 0.8013 0.8348 0.8417 0.1540  0.0079  -0.1533 62  MET A CG  
202  S SD  . MET A 28  ? 0.8889 0.8749 0.9554 0.1690  -0.0164 -0.1788 62  MET A SD  
203  C CE  . MET A 28  ? 0.7706 0.7272 0.8020 0.1550  -0.0327 -0.1836 62  MET A CE  
204  N N   . ASP A 29  ? 0.9527 1.0359 1.0810 0.1881  0.0232  -0.1559 63  ASP A N   
205  C CA  . ASP A 29  ? 1.0410 1.1640 1.1794 0.2091  0.0405  -0.1734 63  ASP A CA  
206  C C   . ASP A 29  ? 1.1481 1.2840 1.2361 0.2133  0.0556  -0.1940 63  ASP A C   
207  O O   . ASP A 29  ? 1.1611 1.2742 1.2324 0.2306  0.0491  -0.2236 63  ASP A O   
208  C CB  . ASP A 29  ? 1.1207 1.2265 1.3003 0.2362  0.0289  -0.1940 63  ASP A CB  
209  C CG  . ASP A 29  ? 1.1334 1.2195 1.3560 0.2317  0.0122  -0.1706 63  ASP A CG  
210  O OD1 . ASP A 29  ? 1.1107 1.2256 1.3474 0.2204  0.0178  -0.1453 63  ASP A OD1 
211  O OD2 . ASP A 29  ? 1.1649 1.2053 1.4057 0.2386  -0.0074 -0.1770 63  ASP A OD2 
212  N N   . VAL A 30  ? 1.1945 1.3649 1.2556 0.1967  0.0748  -0.1777 64  VAL A N   
213  C CA  . VAL A 30  ? 1.3759 1.5647 1.3859 0.2008  0.0938  -0.1933 64  VAL A CA  
214  C C   . VAL A 30  ? 1.4483 1.6761 1.4775 0.2274  0.1139  -0.2182 64  VAL A C   
215  O O   . VAL A 30  ? 1.3860 1.6519 1.4633 0.2308  0.1238  -0.2092 64  VAL A O   
216  C CB  . VAL A 30  ? 1.4064 1.6194 1.3860 0.1737  0.1094  -0.1653 64  VAL A CB  
217  C CG1 . VAL A 30  ? 1.5246 1.7548 1.4462 0.1764  0.1306  -0.1772 64  VAL A CG1 
218  C CG2 . VAL A 30  ? 1.1591 1.3331 1.1236 0.1508  0.0886  -0.1437 64  VAL A CG2 
219  N N   . PRO A 31  ? 1.4783 1.6994 1.4734 0.2481  0.1192  -0.2512 65  PRO A N   
220  C CA  . PRO A 31  ? 1.4908 1.7468 1.5100 0.2782  0.1372  -0.2802 65  PRO A CA  
221  C C   . PRO A 31  ? 1.5376 1.8629 1.5744 0.2736  0.1709  -0.2675 65  PRO A C   
222  O O   . PRO A 31  ? 1.4255 1.7841 1.5218 0.2894  0.1770  -0.2729 65  PRO A O   
223  C CB  . PRO A 31  ? 1.4804 1.7163 1.4398 0.2955  0.1391  -0.3150 65  PRO A CB  
224  C CG  . PRO A 31  ? 1.3564 1.5320 1.2873 0.2816  0.1078  -0.3101 65  PRO A CG  
225  C CD  . PRO A 31  ? 1.3871 1.5650 1.3244 0.2482  0.1049  -0.2671 65  PRO A CD  
226  N N   . GLY A 32  ? 1.8087 2.1566 1.7986 0.2517  0.1920  -0.2502 66  GLY A N   
227  C CA  . GLY A 32  ? 1.6997 2.1150 1.7081 0.2436  0.2258  -0.2372 66  GLY A CA  
228  C C   . GLY A 32  ? 1.7512 2.1807 1.7877 0.2118  0.2224  -0.1968 66  GLY A C   
229  O O   . GLY A 32  ? 1.6541 2.1296 1.6888 0.1936  0.2483  -0.1788 66  GLY A O   
230  N N   . PHE A 33  ? 1.5893 1.9793 1.6518 0.2043  0.1910  -0.1824 67  PHE A N   
231  C CA  . PHE A 33  ? 1.4848 1.8827 1.5679 0.1752  0.1849  -0.1466 67  PHE A CA  
232  C C   . PHE A 33  ? 1.4014 1.7824 1.5397 0.1791  0.1586  -0.1377 67  PHE A C   
233  O O   . PHE A 33  ? 1.2928 1.6692 1.4406 0.1560  0.1482  -0.1099 67  PHE A O   
234  C CB  . PHE A 33  ? 1.4641 1.8223 1.4891 0.1487  0.1756  -0.1270 67  PHE A CB  
235  C CG  . PHE A 33  ? 1.4439 1.8298 1.4265 0.1293  0.2020  -0.1137 67  PHE A CG  
236  C CD1 . PHE A 33  ? 1.3897 1.8058 1.3914 0.1028  0.2115  -0.0848 67  PHE A CD1 
237  C CD2 . PHE A 33  ? 1.4490 1.8283 1.3705 0.1369  0.2161  -0.1296 67  PHE A CD2 
238  C CE1 . PHE A 33  ? 1.3664 1.8046 1.3305 0.0825  0.2358  -0.0699 67  PHE A CE1 
239  C CE2 . PHE A 33  ? 1.4819 1.8835 1.3597 0.1178  0.2412  -0.1138 67  PHE A CE2 
240  C CZ  . PHE A 33  ? 1.3934 1.8240 1.2943 0.0896  0.2517  -0.0828 67  PHE A CZ  
241  N N   . GLY A 34  ? 1.3885 1.7573 1.5602 0.2075  0.1469  -0.1596 68  GLY A N   
242  C CA  . GLY A 34  ? 1.2409 1.5920 1.4614 0.2117  0.1223  -0.1486 68  GLY A CA  
243  C C   . GLY A 34  ? 1.2458 1.5349 1.4457 0.1981  0.0960  -0.1350 68  GLY A C   
244  O O   . GLY A 34  ? 1.2508 1.5018 1.4119 0.1987  0.0900  -0.1473 68  GLY A O   
245  N N   . ALA A 35  ? 0.9565 1.2371 1.1827 0.1861  0.0800  -0.1102 69  ALA A N   
246  C CA  . ALA A 35  ? 0.7638 0.9916 0.9755 0.1722  0.0583  -0.0949 69  ALA A CA  
247  C C   . ALA A 35  ? 0.7732 1.0055 0.9561 0.1416  0.0618  -0.0700 69  ALA A C   
248  O O   . ALA A 35  ? 0.7771 1.0285 0.9788 0.1294  0.0591  -0.0492 69  ALA A O   
249  C CB  . ALA A 35  ? 0.6992 0.9093 0.9527 0.1811  0.0383  -0.0844 69  ALA A CB  
250  N N   . VAL A 36  ? 0.7479 0.9601 0.8850 0.1305  0.0652  -0.0733 70  VAL A N   
251  C CA  . VAL A 36  ? 0.6601 0.8727 0.7663 0.1036  0.0683  -0.0528 70  VAL A CA  
252  C C   . VAL A 36  ? 0.5755 0.7439 0.6743 0.0917  0.0489  -0.0402 70  VAL A C   
253  O O   . VAL A 36  ? 0.6637 0.7963 0.7578 0.0997  0.0376  -0.0521 70  VAL A O   
254  C CB  . VAL A 36  ? 0.6612 0.8769 0.7195 0.0993  0.0824  -0.0621 70  VAL A CB  
255  C CG1 . VAL A 36  ? 0.5668 0.7609 0.5892 0.0746  0.0767  -0.0434 70  VAL A CG1 
256  C CG2 . VAL A 36  ? 0.6926 0.9613 0.7562 0.1021  0.1077  -0.0655 70  VAL A CG2 
257  N N   . SER A 37  ? 0.5025 0.6746 0.6020 0.0725  0.0454  -0.0175 71  SER A N   
258  C CA  . SER A 37  ? 0.5499 0.6865 0.6416 0.0604  0.0309  -0.0049 71  SER A CA  
259  C C   . SER A 37  ? 0.5497 0.6724 0.6023 0.0433  0.0318  -0.0002 71  SER A C   
260  O O   . SER A 37  ? 0.5556 0.6969 0.5863 0.0362  0.0430  0.0007  71  SER A O   
261  C CB  . SER A 37  ? 0.4398 0.5854 0.5528 0.0523  0.0243  0.0150  71  SER A CB  
262  O OG  . SER A 37  ? 0.5018 0.6778 0.6098 0.0378  0.0316  0.0260  71  SER A OG  
263  N N   . SER A 38  ? 0.6141 0.7034 0.6595 0.0369  0.0202  0.0037  72  SER A N   
264  C CA  . SER A 38  ? 0.6091 0.6813 0.6229 0.0232  0.0170  0.0074  72  SER A CA  
265  C C   . SER A 38  ? 0.4721 0.5241 0.4925 0.0131  0.0078  0.0194  72  SER A C   
266  O O   . SER A 38  ? 0.5169 0.5549 0.5590 0.0187  0.0024  0.0190  72  SER A O   
267  C CB  . SER A 38  ? 0.5439 0.5954 0.5377 0.0317  0.0124  -0.0109 72  SER A CB  
268  O OG  . SER A 38  ? 0.5734 0.6063 0.5400 0.0204  0.0056  -0.0067 72  SER A OG  
269  N N   . ASN A 39  ? 0.4945 0.5440 0.4953 -0.0019 0.0068  0.0301  73  ASN A N   
270  C CA  . ASN A 39  ? 0.5257 0.5606 0.5292 -0.0110 0.0006  0.0403  73  ASN A CA  
271  C C   . ASN A 39  ? 0.5677 0.5785 0.5546 -0.0156 -0.0060 0.0353  73  ASN A C   
272  O O   . ASN A 39  ? 0.5717 0.5778 0.5357 -0.0169 -0.0077 0.0304  73  ASN A O   
273  C CB  . ASN A 39  ? 0.5971 0.6474 0.5958 -0.0234 0.0019  0.0547  73  ASN A CB  
274  C CG  . ASN A 39  ? 0.4642 0.5415 0.4852 -0.0187 0.0052  0.0597  73  ASN A CG  
275  O OD1 . ASN A 39  ? 0.5548 0.6305 0.5965 -0.0076 0.0033  0.0586  73  ASN A OD1 
276  N ND2 . ASN A 39  ? 0.5314 0.6333 0.5513 -0.0274 0.0091  0.0659  73  ASN A ND2 
277  N N   . GLY A 40  ? 0.5411 0.5374 0.5399 -0.0174 -0.0096 0.0373  74  GLY A N   
278  C CA  . GLY A 40  ? 0.5125 0.4907 0.5038 -0.0215 -0.0157 0.0331  74  GLY A CA  
279  C C   . GLY A 40  ? 0.5346 0.5095 0.5294 -0.0288 -0.0138 0.0422  74  GLY A C   
280  O O   . GLY A 40  ? 0.5806 0.5658 0.5777 -0.0314 -0.0096 0.0528  74  GLY A O   
281  N N   . LEU A 41  ? 0.5994 0.5613 0.5945 -0.0308 -0.0174 0.0373  75  LEU A N   
282  C CA  . LEU A 41  ? 0.5810 0.5406 0.5755 -0.0363 -0.0135 0.0430  75  LEU A CA  
283  C C   . LEU A 41  ? 0.5363 0.4899 0.5551 -0.0337 -0.0102 0.0365  75  LEU A C   
284  O O   . LEU A 41  ? 0.5486 0.4965 0.5826 -0.0291 -0.0162 0.0251  75  LEU A O   
285  C CB  . LEU A 41  ? 0.5755 0.5278 0.5465 -0.0421 -0.0196 0.0428  75  LEU A CB  
286  C CG  . LEU A 41  ? 0.6092 0.5681 0.5594 -0.0493 -0.0221 0.0512  75  LEU A CG  
287  C CD1 . LEU A 41  ? 0.5517 0.4963 0.4820 -0.0562 -0.0299 0.0509  75  LEU A CD1 
288  C CD2 . LEU A 41  ? 0.5913 0.5659 0.5456 -0.0518 -0.0168 0.0615  75  LEU A CD2 
289  N N   . ILE A 42  ? 0.5113 0.4674 0.5335 -0.0372 -0.0005 0.0440  76  ILE A N   
290  C CA  . ILE A 42  ? 0.5278 0.4829 0.5737 -0.0376 0.0078  0.0404  76  ILE A CA  
291  C C   . ILE A 42  ? 0.4446 0.4003 0.4741 -0.0405 0.0138  0.0406  76  ILE A C   
292  O O   . ILE A 42  ? 0.5580 0.5155 0.5639 -0.0439 0.0181  0.0508  76  ILE A O   
293  C CB  . ILE A 42  ? 0.5062 0.4626 0.5710 -0.0392 0.0178  0.0509  76  ILE A CB  
294  C CG1 . ILE A 42  ? 0.4717 0.4239 0.5568 -0.0343 0.0102  0.0460  76  ILE A CG1 
295  C CG2 . ILE A 42  ? 0.4526 0.4112 0.5400 -0.0432 0.0311  0.0507  76  ILE A CG2 
296  C CD1 . ILE A 42  ? 0.4847 0.4343 0.5755 -0.0336 0.0140  0.0591  76  ILE A CD1 
297  N N   . VAL A 43  ? 0.5324 0.4866 0.5746 -0.0378 0.0125  0.0277  77  VAL A N   
298  C CA  . VAL A 43  ? 0.5835 0.5368 0.6112 -0.0374 0.0166  0.0226  77  VAL A CA  
299  C C   . VAL A 43  ? 0.5552 0.5194 0.6118 -0.0366 0.0329  0.0175  77  VAL A C   
300  O O   . VAL A 43  ? 0.5259 0.4951 0.6196 -0.0338 0.0310  0.0078  77  VAL A O   
301  C CB  . VAL A 43  ? 0.5898 0.5313 0.6078 -0.0331 0.0001  0.0108  77  VAL A CB  
302  C CG1 . VAL A 43  ? 0.6330 0.5690 0.6306 -0.0322 0.0019  0.0053  77  VAL A CG1 
303  C CG2 . VAL A 43  ? 0.4670 0.4004 0.4632 -0.0359 -0.0133 0.0173  77  VAL A CG2 
304  N N   . LYS A 44  ? 0.5752 0.5446 0.6149 -0.0393 0.0489  0.0235  78  LYS A N   
305  C CA  . LYS A 44  ? 0.5422 0.5255 0.6047 -0.0392 0.0693  0.0189  78  LYS A CA  
306  C C   . LYS A 44  ? 0.6521 0.6359 0.7111 -0.0310 0.0673  0.0001  78  LYS A C   
307  O O   . LYS A 44  ? 0.7569 0.7329 0.7777 -0.0294 0.0664  -0.0016 78  LYS A O   
308  C CB  . LYS A 44  ? 0.5815 0.5687 0.6209 -0.0456 0.0893  0.0357  78  LYS A CB  
309  C CG  . LYS A 44  ? 0.6638 0.6683 0.7255 -0.0476 0.1158  0.0338  78  LYS A CG  
310  C CD  . LYS A 44  ? 0.7360 0.7409 0.7540 -0.0511 0.1346  0.0467  78  LYS A CD  
311  C CE  . LYS A 44  ? 0.6428 0.6682 0.6773 -0.0519 0.1643  0.0414  78  LYS A CE  
312  N NZ  . LYS A 44  ? 0.8247 0.8519 0.8212 -0.0433 0.1705  0.0266  78  LYS A NZ  
313  N N   . ASP A 45  ? 0.6227 0.6146 0.7233 -0.0250 0.0640  -0.0153 79  ASP A N   
314  C CA  . ASP A 45  ? 0.5369 0.5285 0.6431 -0.0142 0.0589  -0.0354 79  ASP A CA  
315  C C   . ASP A 45  ? 0.6106 0.6290 0.7533 -0.0118 0.0844  -0.0443 79  ASP A C   
316  O O   . ASP A 45  ? 0.5747 0.6091 0.7706 -0.0093 0.0847  -0.0538 79  ASP A O   
317  C CB  . ASP A 45  ? 0.4879 0.4681 0.6137 -0.0069 0.0322  -0.0465 79  ASP A CB  
318  C CG  . ASP A 45  ? 0.6070 0.5859 0.7477 0.0065  0.0246  -0.0676 79  ASP A CG  
319  O OD1 . ASP A 45  ? 0.6810 0.6529 0.7936 0.0106  0.0294  -0.0735 79  ASP A OD1 
320  O OD2 . ASP A 45  ? 0.6109 0.5947 0.7920 0.0141  0.0119  -0.0796 79  ASP A OD2 
321  N N   . GLY A 46  ? 0.7360 0.7204 0.6326 -0.0987 0.1522  -0.0130 80  GLY A N   
322  C CA  . GLY A 46  ? 0.6908 0.6713 0.5650 -0.0940 0.1878  -0.0045 80  GLY A CA  
323  C C   . GLY A 46  ? 0.7542 0.7364 0.6523 -0.1012 0.2091  0.0201  80  GLY A C   
324  O O   . GLY A 46  ? 0.8426 0.8026 0.7043 -0.0996 0.2030  0.0398  80  GLY A O   
325  N N   . GLU A 47  ? 0.7339 0.7413 0.6956 -0.1085 0.2336  0.0181  81  GLU A N   
326  C CA  . GLU A 47  ? 0.7308 0.7390 0.7292 -0.1204 0.2591  0.0374  81  GLU A CA  
327  C C   . GLU A 47  ? 0.6786 0.7048 0.7485 -0.1321 0.2400  0.0325  81  GLU A C   
328  O O   . GLU A 47  ? 0.7300 0.7609 0.8486 -0.1455 0.2605  0.0407  81  GLU A O   
329  C CB  . GLU A 47  ? 0.7106 0.7382 0.7402 -0.1233 0.3040  0.0358  81  GLU A CB  
330  C CG  . GLU A 47  ? 0.9538 0.9593 0.9071 -0.1092 0.3307  0.0416  81  GLU A CG  
331  C CD  . GLU A 47  ? 1.1360 1.1006 1.0311 -0.1086 0.3602  0.0738  81  GLU A CD  
332  O OE1 . GLU A 47  ? 1.2705 1.2352 1.2137 -0.1238 0.3900  0.0907  81  GLU A OE1 
333  O OE2 . GLU A 47  ? 1.3113 1.2404 1.1103 -0.0919 0.3535  0.0815  81  GLU A OE2 
334  N N   . ARG A 48  ? 0.6502 0.6833 0.7270 -0.1277 0.2039  0.0184  82  ARG A N   
335  C CA  . ARG A 48  ? 0.5597 0.6053 0.6916 -0.1341 0.1851  0.0121  82  ARG A CA  
336  C C   . ARG A 48  ? 0.6073 0.6361 0.7122 -0.1292 0.1537  0.0160  82  ARG A C   
337  O O   . ARG A 48  ? 0.5508 0.5660 0.6050 -0.1223 0.1424  0.0182  82  ARG A O   
338  C CB  . ARG A 48  ? 0.5178 0.5973 0.6994 -0.1296 0.1781  -0.0131 82  ARG A CB  
339  C CG  . ARG A 48  ? 0.4901 0.5668 0.6425 -0.1155 0.1577  -0.0264 82  ARG A CG  
340  C CD  . ARG A 48  ? 0.5551 0.6575 0.7321 -0.1036 0.1640  -0.0458 82  ARG A CD  
341  N NE  . ARG A 48  ? 0.6668 0.7551 0.8114 -0.0892 0.1498  -0.0559 82  ARG A NE  
342  C CZ  . ARG A 48  ? 0.6208 0.7162 0.7827 -0.0755 0.1355  -0.0685 82  ARG A CZ  
343  N NH1 . ARG A 48  ? 0.5286 0.6503 0.7385 -0.0725 0.1273  -0.0768 82  ARG A NH1 
344  N NH2 . ARG A 48  ? 0.6716 0.7433 0.7986 -0.0637 0.1296  -0.0737 82  ARG A NH2 
345  N N   . VAL A 49  ? 0.5219 0.5539 0.6654 -0.1326 0.1397  0.0142  83  VAL A N   
346  C CA  . VAL A 49  ? 0.4740 0.4952 0.6061 -0.1277 0.1145  0.0181  83  VAL A CA  
347  C C   . VAL A 49  ? 0.4815 0.5173 0.6446 -0.1230 0.0996  -0.0005 83  VAL A C   
348  O O   . VAL A 49  ? 0.5579 0.6073 0.7593 -0.1241 0.1029  -0.0122 83  VAL A O   
349  C CB  . VAL A 49  ? 0.5046 0.5057 0.6427 -0.1308 0.1155  0.0373  83  VAL A CB  
350  C CG1 . VAL A 49  ? 0.4883 0.4854 0.6242 -0.1227 0.0903  0.0394  83  VAL A CG1 
351  C CG2 . VAL A 49  ? 0.5827 0.5601 0.6759 -0.1300 0.1329  0.0602  83  VAL A CG2 
352  N N   . LEU A 50  ? 0.4404 0.4728 0.5866 -0.1170 0.0839  -0.0041 84  LEU A N   
353  C CA  . LEU A 50  ? 0.4311 0.4678 0.5943 -0.1096 0.0750  -0.0168 84  LEU A CA  
354  C C   . LEU A 50  ? 0.5277 0.5578 0.6993 -0.1079 0.0631  -0.0096 84  LEU A C   
355  O O   . LEU A 50  ? 0.5104 0.5382 0.6687 -0.1099 0.0550  -0.0017 84  LEU A O   
356  C CB  . LEU A 50  ? 0.4517 0.4855 0.5933 -0.1045 0.0757  -0.0274 84  LEU A CB  
357  C CG  . LEU A 50  ? 0.5322 0.5701 0.6583 -0.1031 0.0884  -0.0339 84  LEU A CG  
358  C CD1 . LEU A 50  ? 0.4221 0.4468 0.5242 -0.0968 0.0894  -0.0446 84  LEU A CD1 
359  C CD2 . LEU A 50  ? 0.4674 0.5244 0.6250 -0.0982 0.0960  -0.0418 84  LEU A CD2 
360  N N   . LEU A 51  ? 0.4878 0.5171 0.6822 -0.1020 0.0607  -0.0147 85  LEU A N   
361  C CA  . LEU A 51  ? 0.4482 0.4712 0.6536 -0.0970 0.0537  -0.0091 85  LEU A CA  
362  C C   . LEU A 51  ? 0.4715 0.4924 0.6748 -0.0872 0.0550  -0.0176 85  LEU A C   
363  O O   . LEU A 51  ? 0.5216 0.5396 0.7173 -0.0784 0.0587  -0.0288 85  LEU A O   
364  C CB  . LEU A 51  ? 0.4901 0.5051 0.7166 -0.0957 0.0534  -0.0094 85  LEU A CB  
365  C CG  . LEU A 51  ? 0.5823 0.5875 0.8200 -0.0866 0.0487  -0.0050 85  LEU A CG  
366  C CD1 . LEU A 51  ? 0.4802 0.4837 0.7159 -0.0877 0.0439  0.0136  85  LEU A CD1 
367  C CD2 . LEU A 51  ? 0.4573 0.4490 0.7123 -0.0844 0.0487  -0.0141 85  LEU A CD2 
368  N N   . VAL A 52  ? 0.5201 0.5423 0.7308 -0.0870 0.0532  -0.0116 86  VAL A N   
369  C CA  . VAL A 52  ? 0.6056 0.6221 0.8163 -0.0811 0.0626  -0.0163 86  VAL A CA  
370  C C   . VAL A 52  ? 0.6524 0.6628 0.8761 -0.0683 0.0683  -0.0147 86  VAL A C   
371  O O   . VAL A 52  ? 0.7924 0.7901 1.0074 -0.0587 0.0827  -0.0173 86  VAL A O   
372  C CB  . VAL A 52  ? 0.5699 0.5955 0.7894 -0.0931 0.0613  -0.0155 86  VAL A CB  
373  C CG1 . VAL A 52  ? 0.4762 0.4903 0.7012 -0.0914 0.0789  -0.0194 86  VAL A CG1 
374  C CG2 . VAL A 52  ? 0.5988 0.6250 0.7957 -0.1027 0.0559  -0.0197 86  VAL A CG2 
375  N N   . ASP A 53  ? 0.4634 0.4760 0.7020 -0.0655 0.0608  -0.0098 87  ASP A N   
376  C CA  . ASP A 53  ? 0.5414 0.5435 0.7869 -0.0502 0.0670  -0.0112 87  ASP A CA  
377  C C   . ASP A 53  ? 0.5737 0.5693 0.8295 -0.0488 0.0574  -0.0087 87  ASP A C   
378  O O   . ASP A 53  ? 0.4974 0.4978 0.7589 -0.0590 0.0490  0.0005  87  ASP A O   
379  C CB  . ASP A 53  ? 0.6311 0.6432 0.9007 -0.0469 0.0775  -0.0049 87  ASP A CB  
380  C CG  . ASP A 53  ? 0.7065 0.7038 0.9612 -0.0370 0.0998  -0.0086 87  ASP A CG  
381  O OD1 . ASP A 53  ? 0.7644 0.7392 0.9841 -0.0224 0.1038  -0.0160 87  ASP A OD1 
382  O OD2 . ASP A 53  ? 0.7579 0.7651 1.0358 -0.0433 0.1138  -0.0046 87  ASP A OD2 
383  N N   . THR A 54  ? 0.4299 0.4084 0.6826 -0.0345 0.0607  -0.0170 88  THR A N   
384  C CA  . THR A 54  ? 0.5536 0.5167 0.8177 -0.0325 0.0548  -0.0171 88  THR A CA  
385  C C   . THR A 54  ? 0.5268 0.4903 0.8102 -0.0210 0.0588  -0.0054 88  THR A C   
386  O O   . THR A 54  ? 0.5525 0.5368 0.8493 -0.0188 0.0643  0.0021  88  THR A O   
387  C CB  . THR A 54  ? 0.4991 0.4421 0.7500 -0.0227 0.0523  -0.0385 88  THR A CB  
388  O OG1 . THR A 54  ? 0.5978 0.5270 0.8379 -0.0011 0.0614  -0.0431 88  THR A OG1 
389  C CG2 . THR A 54  ? 0.6254 0.5774 0.8566 -0.0235 0.0484  -0.0523 88  THR A CG2 
390  N N   . ALA A 55  ? 0.5334 0.4745 0.8239 -0.0135 0.0569  -0.0054 89  ALA A N   
391  C CA  . ALA A 55  ? 0.5426 0.4822 0.8526 0.0028  0.0607  0.0048  89  ALA A CA  
392  C C   . ALA A 55  ? 0.6134 0.5334 0.9149 0.0231  0.0728  -0.0099 89  ALA A C   
393  O O   . ALA A 55  ? 0.6178 0.5277 0.8928 0.0260  0.0762  -0.0267 89  ALA A O   
394  C CB  . ALA A 55  ? 0.4797 0.3985 0.7966 0.0020  0.0531  0.0179  89  ALA A CB  
395  N N   . TRP A 56  ? 0.6360 0.5495 0.9556 0.0416  0.0791  -0.0037 90  TRP A N   
396  C CA  . TRP A 56  ? 0.5950 0.4856 0.9013 0.0645  0.0938  -0.0178 90  TRP A CA  
397  C C   . TRP A 56  ? 0.5882 0.4358 0.8676 0.0653  0.0859  -0.0393 90  TRP A C   
398  O O   . TRP A 56  ? 0.6023 0.4319 0.8499 0.0788  0.0909  -0.0599 90  TRP A O   
399  C CB  . TRP A 56  ? 0.5584 0.4536 0.8957 0.0860  0.1032  -0.0067 90  TRP A CB  
400  C CG  . TRP A 56  ? 0.5564 0.5010 0.9327 0.0872  0.1116  0.0072  90  TRP A CG  
401  C CD1 . TRP A 56  ? 0.5433 0.5244 0.9539 0.0776  0.0962  0.0227  90  TRP A CD1 
402  C CD2 . TRP A 56  ? 0.5180 0.4808 0.9059 0.0985  0.1381  0.0046  90  TRP A CD2 
403  N NE1 . TRP A 56  ? 0.4782 0.5046 0.9305 0.0793  0.1077  0.0259  90  TRP A NE1 
404  C CE2 . TRP A 56  ? 0.5356 0.5506 0.9779 0.0906  0.1373  0.0166  90  TRP A CE2 
405  C CE3 . TRP A 56  ? 0.6333 0.5711 0.9885 0.1158  0.1639  -0.0072 90  TRP A CE3 
406  C CZ2 . TRP A 56  ? 0.5547 0.5995 1.0316 0.0943  0.1651  0.0173  90  TRP A CZ2 
407  C CZ3 . TRP A 56  ? 0.5990 0.5603 0.9765 0.1232  0.1950  -0.0021 90  TRP A CZ3 
408  C CH2 . TRP A 56  ? 0.5246 0.5399 0.9684 0.1101  0.1973  0.0100  90  TRP A CH2 
409  N N   . THR A 57  ? 0.6028 0.4316 0.8937 0.0516  0.0741  -0.0361 91  THR A N   
410  C CA  . THR A 57  ? 0.6739 0.4604 0.9552 0.0485  0.0677  -0.0587 91  THR A CA  
411  C C   . THR A 57  ? 0.6288 0.4183 0.9191 0.0187  0.0565  -0.0618 91  THR A C   
412  O O   . THR A 57  ? 0.6443 0.4614 0.9425 0.0035  0.0552  -0.0424 91  THR A O   
413  C CB  . THR A 57  ? 0.6472 0.3939 0.9413 0.0616  0.0731  -0.0528 91  THR A CB  
414  O OG1 . THR A 57  ? 0.7319 0.4742 1.0447 0.0471  0.0703  -0.0277 91  THR A OG1 
415  C CG2 . THR A 57  ? 0.6605 0.4170 0.9592 0.0919  0.0869  -0.0427 91  THR A CG2 
416  N N   . ASP A 58  ? 0.6671 0.5076 0.7695 -0.0498 -0.0220 -0.0701 92  ASP A N   
417  C CA  . ASP A 58  ? 0.6981 0.5357 0.8150 -0.0666 -0.0296 -0.0549 92  ASP A CA  
418  C C   . ASP A 58  ? 0.6968 0.5239 0.8203 -0.0591 -0.0278 -0.0441 92  ASP A C   
419  O O   . ASP A 58  ? 0.7162 0.5612 0.8568 -0.0659 -0.0258 -0.0292 92  ASP A O   
420  C CB  . ASP A 58  ? 0.7019 0.5063 0.8054 -0.0847 -0.0434 -0.0574 92  ASP A CB  
421  C CG  . ASP A 58  ? 0.6705 0.4964 0.7817 -0.1016 -0.0499 -0.0548 92  ASP A CG  
422  O OD1 . ASP A 58  ? 0.6097 0.4736 0.7374 -0.0987 -0.0426 -0.0505 92  ASP A OD1 
423  O OD2 . ASP A 58  ? 0.8674 0.6700 0.9675 -0.1183 -0.0642 -0.0567 92  ASP A OD2 
424  N N   . ASP A 59  ? 0.7296 0.5265 0.8379 -0.0439 -0.0278 -0.0510 93  ASP A N   
425  C CA  . ASP A 59  ? 0.7543 0.5357 0.8655 -0.0363 -0.0285 -0.0390 93  ASP A CA  
426  C C   . ASP A 59  ? 0.7236 0.5438 0.8497 -0.0259 -0.0208 -0.0304 93  ASP A C   
427  O O   . ASP A 59  ? 0.7191 0.5413 0.8506 -0.0297 -0.0209 -0.0148 93  ASP A O   
428  C CB  . ASP A 59  ? 0.7550 0.4946 0.8474 -0.0185 -0.0305 -0.0491 93  ASP A CB  
429  C CG  . ASP A 59  ? 0.8589 0.5811 0.9534 -0.0081 -0.0326 -0.0352 93  ASP A CG  
430  O OD1 . ASP A 59  ? 0.9966 0.6841 1.0853 -0.0211 -0.0405 -0.0244 93  ASP A OD1 
431  O OD2 . ASP A 59  ? 0.9053 0.6489 1.0075 0.0118  -0.0276 -0.0337 93  ASP A OD2 
432  N N   . GLN A 60  ? 0.7671 0.6175 0.8978 -0.0143 -0.0144 -0.0400 94  GLN A N   
433  C CA  . GLN A 60  ? 0.7299 0.6153 0.8726 -0.0070 -0.0102 -0.0331 94  GLN A CA  
434  C C   . GLN A 60  ? 0.5884 0.4979 0.7399 -0.0227 -0.0076 -0.0250 94  GLN A C   
435  O O   . GLN A 60  ? 0.5776 0.5028 0.7319 -0.0209 -0.0056 -0.0160 94  GLN A O   
436  C CB  . GLN A 60  ? 0.5960 0.5081 0.7444 0.0068  -0.0051 -0.0443 94  GLN A CB  
437  C CG  . GLN A 60  ? 0.6840 0.5795 0.8287 0.0279  -0.0043 -0.0516 94  GLN A CG  
438  C CD  . GLN A 60  ? 0.7244 0.6541 0.8803 0.0403  0.0034  -0.0611 94  GLN A CD  
439  O OE1 . GLN A 60  ? 0.7180 0.6702 0.8757 0.0303  0.0083  -0.0668 94  GLN A OE1 
440  N NE2 . GLN A 60  ? 0.7443 0.6796 0.9098 0.0622  0.0046  -0.0611 94  GLN A NE2 
441  N N   . THR A 61  ? 0.5763 0.4879 0.7308 -0.0370 -0.0080 -0.0281 95  THR A N   
442  C CA  . THR A 61  ? 0.6383 0.5722 0.8046 -0.0488 -0.0046 -0.0203 95  THR A CA  
443  C C   . THR A 61  ? 0.5627 0.4868 0.7333 -0.0575 -0.0040 -0.0048 95  THR A C   
444  O O   . THR A 61  ? 0.5390 0.4814 0.7152 -0.0590 0.0030  0.0038  95  THR A O   
445  C CB  . THR A 61  ? 0.5734 0.5139 0.7445 -0.0600 -0.0071 -0.0260 95  THR A CB  
446  O OG1 . THR A 61  ? 0.5185 0.4711 0.6841 -0.0529 -0.0051 -0.0381 95  THR A OG1 
447  C CG2 . THR A 61  ? 0.4590 0.4218 0.6465 -0.0692 -0.0033 -0.0169 95  THR A CG2 
448  N N   . SER A 62  ? 0.5688 0.4626 0.7349 -0.0639 -0.0106 -0.0010 96  SER A N   
449  C CA  . SER A 62  ? 0.6195 0.5039 0.7904 -0.0740 -0.0096 0.0164  96  SER A CA  
450  C C   . SER A 62  ? 0.6275 0.5096 0.7877 -0.0626 -0.0051 0.0253  96  SER A C   
451  O O   . SER A 62  ? 0.6681 0.5549 0.8302 -0.0692 0.0011  0.0408  96  SER A O   
452  C CB  . SER A 62  ? 0.5471 0.3943 0.7138 -0.0857 -0.0202 0.0184  96  SER A CB  
453  O OG  . SER A 62  ? 0.8737 0.6868 1.0218 -0.0731 -0.0248 0.0149  96  SER A OG  
454  N N   . GLN A 63  ? 0.5765 0.4533 0.7255 -0.0454 -0.0080 0.0168  97  GLN A N   
455  C CA  . GLN A 63  ? 0.6885 0.5686 0.8275 -0.0343 -0.0067 0.0255  97  GLN A CA  
456  C C   . GLN A 63  ? 0.6099 0.5237 0.7498 -0.0345 0.0011  0.0259  97  GLN A C   
457  O O   . GLN A 63  ? 0.5251 0.4412 0.6529 -0.0330 0.0042  0.0370  97  GLN A O   
458  C CB  . GLN A 63  ? 0.6643 0.5358 0.7978 -0.0150 -0.0133 0.0174  97  GLN A CB  
459  C CG  . GLN A 63  ? 0.6713 0.5014 0.7985 -0.0103 -0.0202 0.0159  97  GLN A CG  
460  C CD  . GLN A 63  ? 0.7430 0.5690 0.8692 0.0131  -0.0240 0.0077  97  GLN A CD  
461  O OE1 . GLN A 63  ? 0.8229 0.6687 0.9513 0.0251  -0.0257 0.0129  97  GLN A OE1 
462  N NE2 . GLN A 63  ? 0.6995 0.5002 0.8222 0.0202  -0.0255 -0.0053 97  GLN A NE2 
463  N N   . ILE A 64  ? 0.5938 0.5299 0.7438 -0.0363 0.0039  0.0140  98  ILE A N   
464  C CA  . ILE A 64  ? 0.5568 0.5178 0.7059 -0.0373 0.0109  0.0130  98  ILE A CA  
465  C C   . ILE A 64  ? 0.5583 0.5222 0.7099 -0.0472 0.0211  0.0249  98  ILE A C   
466  O O   . ILE A 64  ? 0.6112 0.5813 0.7494 -0.0451 0.0283  0.0307  98  ILE A O   
467  C CB  . ILE A 64  ? 0.5901 0.5693 0.7499 -0.0384 0.0110  -0.0007 98  ILE A CB  
468  C CG1 . ILE A 64  ? 0.5882 0.5762 0.7456 -0.0278 0.0051  -0.0101 98  ILE A CG1 
469  C CG2 . ILE A 64  ? 0.5024 0.4985 0.6640 -0.0428 0.0191  -0.0005 98  ILE A CG2 
470  C CD1 . ILE A 64  ? 0.5243 0.5233 0.6914 -0.0296 0.0047  -0.0219 98  ILE A CD1 
471  N N   . LEU A 65  ? 0.5146 0.4749 0.6829 -0.0584 0.0218  0.0290  99  LEU A N   
472  C CA  . LEU A 65  ? 0.5698 0.5396 0.7489 -0.0680 0.0327  0.0424  99  LEU A CA  
473  C C   . LEU A 65  ? 0.5668 0.5233 0.7311 -0.0691 0.0374  0.0584  99  LEU A C   
474  O O   . LEU A 65  ? 0.5216 0.4903 0.6817 -0.0702 0.0513  0.0681  99  LEU A O   
475  C CB  . LEU A 65  ? 0.5664 0.5363 0.7700 -0.0818 0.0281  0.0456  99  LEU A CB  
476  C CG  . LEU A 65  ? 0.6204 0.6014 0.8360 -0.0826 0.0220  0.0325  99  LEU A CG  
477  C CD1 . LEU A 65  ? 0.3855 0.3648 0.6221 -0.0983 0.0139  0.0378  99  LEU A CD1 
478  C CD2 . LEU A 65  ? 0.4597 0.4657 0.6809 -0.0764 0.0321  0.0289  99  LEU A CD2 
479  N N   . ASN A 66  ? 0.5744 0.5038 0.7284 -0.0679 0.0268  0.0619  100 ASN A N   
480  C CA  . ASN A 66  ? 0.6175 0.5300 0.7538 -0.0687 0.0292  0.0789  100 ASN A CA  
481  C C   . ASN A 66  ? 0.6531 0.5739 0.7636 -0.0571 0.0336  0.0791  100 ASN A C   
482  O O   . ASN A 66  ? 0.6471 0.5651 0.7402 -0.0596 0.0423  0.0941  100 ASN A O   
483  C CB  . ASN A 66  ? 0.6538 0.5305 0.7832 -0.0668 0.0150  0.0812  100 ASN A CB  
484  C CG  . ASN A 66  ? 0.7330 0.5911 0.8784 -0.0838 0.0107  0.0880  100 ASN A CG  
485  O OD1 . ASN A 66  ? 0.7890 0.6649 0.9533 -0.0987 0.0188  0.0965  100 ASN A OD1 
486  N ND2 . ASN A 66  ? 0.7723 0.5938 0.9108 -0.0816 -0.0025 0.0843  100 ASN A ND2 
487  N N   . TRP A 67  ? 0.6059 0.5368 0.7121 -0.0459 0.0272  0.0631  101 TRP A N   
488  C CA  . TRP A 67  ? 0.5774 0.5165 0.6587 -0.0376 0.0280  0.0617  101 TRP A CA  
489  C C   . TRP A 67  ? 0.5437 0.4998 0.6189 -0.0414 0.0444  0.0608  101 TRP A C   
490  O O   . TRP A 67  ? 0.5979 0.5522 0.6440 -0.0390 0.0506  0.0665  101 TRP A O   
491  C CB  . TRP A 67  ? 0.6162 0.5645 0.7004 -0.0276 0.0158  0.0460  101 TRP A CB  
492  C CG  . TRP A 67  ? 0.6818 0.6372 0.7414 -0.0214 0.0110  0.0444  101 TRP A CG  
493  C CD1 . TRP A 67  ? 0.6386 0.5863 0.6814 -0.0135 -0.0017 0.0516  101 TRP A CD1 
494  C CD2 . TRP A 67  ? 0.5695 0.5388 0.6172 -0.0232 0.0166  0.0349  101 TRP A CD2 
495  N NE1 . TRP A 67  ? 0.7616 0.7193 0.7820 -0.0123 -0.0060 0.0474  101 TRP A NE1 
496  C CE2 . TRP A 67  ? 0.7098 0.6782 0.7310 -0.0184 0.0056  0.0361  101 TRP A CE2 
497  C CE3 . TRP A 67  ? 0.5350 0.5149 0.5913 -0.0280 0.0285  0.0258  101 TRP A CE3 
498  C CZ2 . TRP A 67  ? 0.6454 0.6195 0.6446 -0.0203 0.0058  0.0269  101 TRP A CZ2 
499  C CZ3 . TRP A 67  ? 0.5833 0.5673 0.6190 -0.0273 0.0305  0.0168  101 TRP A CZ3 
500  C CH2 . TRP A 67  ? 0.5979 0.5773 0.6036 -0.0245 0.0190  0.0165  101 TRP A CH2 
501  N N   . ILE A 68  ? 0.5419 0.5129 0.6423 -0.0462 0.0517  0.0538  102 ILE A N   
502  C CA  . ILE A 68  ? 0.5879 0.5744 0.6868 -0.0464 0.0686  0.0524  102 ILE A CA  
503  C C   . ILE A 68  ? 0.6095 0.5967 0.7048 -0.0521 0.0853  0.0708  102 ILE A C   
504  O O   . ILE A 68  ? 0.6859 0.6762 0.7570 -0.0480 0.1001  0.0733  102 ILE A O   
505  C CB  . ILE A 68  ? 0.5365 0.5387 0.6670 -0.0489 0.0700  0.0428  102 ILE A CB  
506  C CG1 . ILE A 68  ? 0.4674 0.4692 0.5991 -0.0448 0.0553  0.0266  102 ILE A CG1 
507  C CG2 . ILE A 68  ? 0.4596 0.4758 0.5912 -0.0455 0.0883  0.0416  102 ILE A CG2 
508  C CD1 . ILE A 68  ? 0.4342 0.4491 0.5834 -0.0451 0.0577  0.0164  102 ILE A CD1 
509  N N   . LYS A 69  ? 0.6069 0.5905 0.7248 -0.0626 0.0836  0.0839  103 LYS A N   
510  C CA  . LYS A 69  ? 0.6838 0.6702 0.8021 -0.0711 0.0992  0.1048  103 LYS A CA  
511  C C   . LYS A 69  ? 0.5939 0.5617 0.6699 -0.0678 0.1006  0.1154  103 LYS A C   
512  O O   . LYS A 69  ? 0.7174 0.6912 0.7777 -0.0700 0.1196  0.1288  103 LYS A O   
513  C CB  . LYS A 69  ? 0.7482 0.7293 0.8979 -0.0863 0.0918  0.1169  103 LYS A CB  
514  C CG  . LYS A 69  ? 0.6658 0.6495 0.8202 -0.0992 0.1058  0.1419  103 LYS A CG  
515  C CD  . LYS A 69  ? 0.6877 0.7033 0.8871 -0.1102 0.1178  0.1500  103 LYS A CD  
516  C CE  . LYS A 69  ? 0.7393 0.7625 0.9480 -0.1252 0.1331  0.1773  103 LYS A CE  
517  N NZ  . LYS A 69  ? 0.7372 0.7695 0.9142 -0.1160 0.1579  0.1849  103 LYS A NZ  
518  N N   . GLN A 70  ? 0.6141 0.5608 0.6710 -0.0617 0.0811  0.1106  104 GLN A N   
519  C CA  . GLN A 70  ? 0.7093 0.6370 0.7262 -0.0583 0.0778  0.1226  104 GLN A CA  
520  C C   . GLN A 70  ? 0.7994 0.7335 0.7790 -0.0494 0.0843  0.1140  104 GLN A C   
521  O O   . GLN A 70  ? 0.8367 0.7655 0.7819 -0.0505 0.0965  0.1265  104 GLN A O   
522  C CB  . GLN A 70  ? 0.7799 0.6853 0.7945 -0.0523 0.0536  0.1210  104 GLN A CB  
523  C CG  . GLN A 70  ? 0.8538 0.7395 0.8295 -0.0469 0.0451  0.1345  104 GLN A CG  
524  C CD  . GLN A 70  ? 0.7916 0.6595 0.7711 -0.0366 0.0215  0.1320  104 GLN A CD  
525  O OE1 . GLN A 70  ? 0.8037 0.6535 0.8037 -0.0386 0.0146  0.1357  104 GLN A OE1 
526  N NE2 . GLN A 70  ? 0.8632 0.7360 0.8236 -0.0252 0.0087  0.1256  104 GLN A NE2 
527  N N   . GLU A 71  ? 0.6942 0.6374 0.6769 -0.0419 0.0763  0.0930  105 GLU A N   
528  C CA  . GLU A 71  ? 0.7648 0.7075 0.7090 -0.0351 0.0767  0.0827  105 GLU A CA  
529  C C   . GLU A 71  ? 0.7622 0.7163 0.6999 -0.0340 0.1007  0.0757  105 GLU A C   
530  O O   . GLU A 71  ? 0.8614 0.8080 0.7561 -0.0313 0.1121  0.0772  105 GLU A O   
531  C CB  . GLU A 71  ? 0.7410 0.6873 0.6923 -0.0296 0.0558  0.0647  105 GLU A CB  
532  C CG  . GLU A 71  ? 0.8058 0.7431 0.7591 -0.0259 0.0330  0.0707  105 GLU A CG  
533  C CD  . GLU A 71  ? 0.8641 0.7848 0.7761 -0.0243 0.0270  0.0867  105 GLU A CD  
534  O OE1 . GLU A 71  ? 0.9226 0.8404 0.7942 -0.0245 0.0313  0.0846  105 GLU A OE1 
535  O OE2 . GLU A 71  ? 0.8600 0.7671 0.7765 -0.0229 0.0174  0.1015  105 GLU A OE2 
536  N N   . ILE A 72  ? 0.7432 0.7139 0.7212 -0.0350 0.1085  0.0681  106 ILE A N   
537  C CA  . ILE A 72  ? 0.7515 0.7335 0.7300 -0.0302 0.1303  0.0603  106 ILE A CA  
538  C C   . ILE A 72  ? 0.6931 0.6913 0.6944 -0.0344 0.1544  0.0774  106 ILE A C   
539  O O   . ILE A 72  ? 0.7154 0.7192 0.6990 -0.0286 0.1787  0.0788  106 ILE A O   
540  C CB  . ILE A 72  ? 0.6895 0.6806 0.6981 -0.0274 0.1228  0.0424  106 ILE A CB  
541  C CG1 . ILE A 72  ? 0.6816 0.6609 0.6707 -0.0256 0.1000  0.0276  106 ILE A CG1 
542  C CG2 . ILE A 72  ? 0.6142 0.6127 0.6235 -0.0196 0.1444  0.0343  106 ILE A CG2 
543  C CD1 . ILE A 72  ? 0.6755 0.6624 0.7010 -0.0290 0.0821  0.0222  106 ILE A CD1 
544  N N   . ASN A 73  ? 0.6817 0.6878 0.7223 -0.0446 0.1484  0.0904  107 ASN A N   
545  C CA  . ASN A 73  ? 0.6730 0.6984 0.7439 -0.0528 0.1676  0.1096  107 ASN A CA  
546  C C   . ASN A 73  ? 0.6840 0.7365 0.7852 -0.0461 0.1869  0.1037  107 ASN A C   
547  O O   . ASN A 73  ? 0.6881 0.7570 0.7891 -0.0426 0.2140  0.1132  107 ASN A O   
548  C CB  . ASN A 73  ? 0.6794 0.6980 0.7154 -0.0560 0.1841  0.1285  107 ASN A CB  
549  C CG  . ASN A 73  ? 0.6866 0.7204 0.7572 -0.0710 0.1950  0.1537  107 ASN A CG  
550  O OD1 . ASN A 73  ? 0.6564 0.6992 0.7733 -0.0811 0.1836  0.1569  107 ASN A OD1 
551  N ND2 . ASN A 73  ? 0.6215 0.6580 0.6681 -0.0742 0.2170  0.1722  107 ASN A ND2 
552  N N   . LEU A 74  ? 0.6729 0.7302 0.8007 -0.0433 0.1735  0.0888  108 LEU A N   
553  C CA  . LEU A 74  ? 0.5649 0.6455 0.7265 -0.0360 0.1863  0.0837  108 LEU A CA  
554  C C   . LEU A 74  ? 0.5537 0.6433 0.7595 -0.0440 0.1660  0.0814  108 LEU A C   
555  O O   . LEU A 74  ? 0.5402 0.6119 0.7375 -0.0492 0.1430  0.0737  108 LEU A O   
556  C CB  . LEU A 74  ? 0.5500 0.6183 0.6800 -0.0198 0.1923  0.0629  108 LEU A CB  
557  C CG  . LEU A 74  ? 0.5946 0.6533 0.6772 -0.0096 0.2160  0.0618  108 LEU A CG  
558  C CD1 . LEU A 74  ? 0.5311 0.5680 0.5778 0.0037  0.2153  0.0382  108 LEU A CD1 
559  C CD2 . LEU A 74  ? 0.5305 0.6182 0.6391 -0.0053 0.2478  0.0774  108 LEU A CD2 
560  N N   . PRO A 75  ? 0.5553 0.6731 0.8080 -0.0447 0.1740  0.0887  109 PRO A N   
561  C CA  . PRO A 75  ? 0.4795 0.6047 0.7701 -0.0541 0.1528  0.0878  109 PRO A CA  
562  C C   . PRO A 75  ? 0.5030 0.6134 0.7807 -0.0462 0.1380  0.0672  109 PRO A C   
563  O O   . PRO A 75  ? 0.5763 0.6798 0.8329 -0.0323 0.1472  0.0550  109 PRO A O   
564  C CB  . PRO A 75  ? 0.4497 0.6128 0.7927 -0.0540 0.1666  0.1019  109 PRO A CB  
565  C CG  . PRO A 75  ? 0.4513 0.6233 0.7800 -0.0362 0.1965  0.1007  109 PRO A CG  
566  C CD  . PRO A 75  ? 0.4933 0.6396 0.7674 -0.0362 0.2029  0.0989  109 PRO A CD  
567  N N   . VAL A 76  ? 0.5121 0.6151 0.8000 -0.0563 0.1149  0.0635  110 VAL A N   
568  C CA  . VAL A 76  ? 0.5033 0.5959 0.7836 -0.0521 0.1006  0.0472  110 VAL A CA  
569  C C   . VAL A 76  ? 0.5196 0.6329 0.8378 -0.0499 0.1009  0.0503  110 VAL A C   
570  O O   . VAL A 76  ? 0.5281 0.6542 0.8777 -0.0612 0.0894  0.0595  110 VAL A O   
571  C CB  . VAL A 76  ? 0.5772 0.6529 0.8482 -0.0620 0.0788  0.0417  110 VAL A CB  
572  C CG1 . VAL A 76  ? 0.4209 0.4906 0.6862 -0.0589 0.0668  0.0272  110 VAL A CG1 
573  C CG2 . VAL A 76  ? 0.3516 0.4080 0.5892 -0.0611 0.0779  0.0404  110 VAL A CG2 
574  N N   . ALA A 77  ? 0.4628 0.5771 0.7768 -0.0353 0.1124  0.0430  111 ALA A N   
575  C CA  . ALA A 77  ? 0.3925 0.5267 0.7446 -0.0293 0.1146  0.0482  111 ALA A CA  
576  C C   . ALA A 77  ? 0.4314 0.5609 0.7932 -0.0371 0.0910  0.0441  111 ALA A C   
577  O O   . ALA A 77  ? 0.4718 0.6212 0.8714 -0.0419 0.0828  0.0549  111 ALA A O   
578  C CB  . ALA A 77  ? 0.4003 0.5283 0.7400 -0.0095 0.1332  0.0396  111 ALA A CB  
579  N N   . LEU A 78  ? 0.4646 0.5699 0.7929 -0.0390 0.0796  0.0298  112 LEU A N   
580  C CA  . LEU A 78  ? 0.5026 0.6025 0.8338 -0.0463 0.0599  0.0258  112 LEU A CA  
581  C C   . LEU A 78  ? 0.3757 0.4551 0.6716 -0.0516 0.0506  0.0132  112 LEU A C   
582  O O   . LEU A 78  ? 0.4212 0.4905 0.6920 -0.0477 0.0576  0.0071  112 LEU A O   
583  C CB  . LEU A 78  ? 0.3934 0.4920 0.7337 -0.0363 0.0605  0.0236  112 LEU A CB  
584  C CG  . LEU A 78  ? 0.5252 0.6027 0.8354 -0.0246 0.0707  0.0103  112 LEU A CG  
585  C CD1 . LEU A 78  ? 0.4627 0.5214 0.7510 -0.0308 0.0559  0.0003  112 LEU A CD1 
586  C CD2 . LEU A 78  ? 0.5079 0.5890 0.8355 -0.0077 0.0854  0.0132  112 LEU A CD2 
587  N N   . ALA A 79  ? 0.4126 0.4877 0.7069 -0.0600 0.0346  0.0101  113 ALA A N   
588  C CA  . ALA A 79  ? 0.4433 0.5046 0.7102 -0.0638 0.0271  -0.0009 113 ALA A CA  
589  C C   . ALA A 79  ? 0.4653 0.5232 0.7289 -0.0677 0.0169  -0.0048 113 ALA A C   
590  O O   . ALA A 79  ? 0.4622 0.5252 0.7398 -0.0740 0.0074  0.0016  113 ALA A O   
591  C CB  . ALA A 79  ? 0.3897 0.4469 0.6523 -0.0717 0.0203  0.0002  113 ALA A CB  
592  N N   . VAL A 80  ? 0.4224 0.4720 0.6669 -0.0656 0.0178  -0.0138 114 VAL A N   
593  C CA  . VAL A 80  ? 0.4936 0.5394 0.7314 -0.0712 0.0095  -0.0165 114 VAL A CA  
594  C C   . VAL A 80  ? 0.4508 0.4965 0.6717 -0.0764 0.0057  -0.0237 114 VAL A C   
595  O O   . VAL A 80  ? 0.4918 0.5379 0.7043 -0.0727 0.0098  -0.0286 114 VAL A O   
596  C CB  . VAL A 80  ? 0.4569 0.4930 0.6882 -0.0670 0.0130  -0.0200 114 VAL A CB  
597  C CG1 . VAL A 80  ? 0.4400 0.4712 0.6693 -0.0742 0.0041  -0.0176 114 VAL A CG1 
598  C CG2 . VAL A 80  ? 0.4459 0.4801 0.6905 -0.0560 0.0224  -0.0159 114 VAL A CG2 
599  N N   . VAL A 81  ? 0.4201 0.4660 0.6358 -0.0839 -0.0016 -0.0236 115 VAL A N   
600  C CA  . VAL A 81  ? 0.4411 0.4894 0.6416 -0.0869 -0.0019 -0.0307 115 VAL A CA  
601  C C   . VAL A 81  ? 0.5563 0.6062 0.7497 -0.0934 -0.0036 -0.0304 115 VAL A C   
602  O O   . VAL A 81  ? 0.4432 0.4879 0.6394 -0.0978 -0.0088 -0.0236 115 VAL A O   
603  C CB  . VAL A 81  ? 0.5044 0.5487 0.6981 -0.0901 -0.0066 -0.0320 115 VAL A CB  
604  C CG1 . VAL A 81  ? 0.4705 0.5102 0.6713 -0.0859 -0.0056 -0.0310 115 VAL A CG1 
605  C CG2 . VAL A 81  ? 0.5122 0.5527 0.7059 -0.0986 -0.0160 -0.0255 115 VAL A CG2 
606  N N   . THR A 82  ? 0.4924 0.5489 0.6354 0.0328  -0.0150 -0.0132 116 THR A N   
607  C CA  . THR A 82  ? 0.4264 0.4959 0.5749 0.0324  -0.0145 -0.0023 116 THR A CA  
608  C C   . THR A 82  ? 0.5136 0.5908 0.6460 0.0326  -0.0062 -0.0022 116 THR A C   
609  O O   . THR A 82  ? 0.5390 0.6234 0.6672 0.0278  -0.0088 0.0074  116 THR A O   
610  C CB  . THR A 82  ? 0.4659 0.5381 0.6357 0.0356  -0.0137 0.0053  116 THR A CB  
611  O OG1 . THR A 82  ? 0.6662 0.7331 0.8408 0.0421  -0.0072 -0.0029 116 THR A OG1 
612  C CG2 . THR A 82  ? 0.4482 0.5054 0.6216 0.0341  -0.0263 0.0100  116 THR A CG2 
613  N N   . HIS A 83  ? 0.3872 0.4578 0.5046 0.0383  0.0030  -0.0124 117 HIS A N   
614  C CA  . HIS A 83  ? 0.4857 0.5543 0.5739 0.0404  0.0123  -0.0141 117 HIS A CA  
615  C C   . HIS A 83  ? 0.5225 0.5703 0.5861 0.0487  0.0161  -0.0296 117 HIS A C   
616  O O   . HIS A 83  ? 0.4883 0.5271 0.5629 0.0518  0.0118  -0.0370 117 HIS A O   
617  C CB  . HIS A 83  ? 0.4987 0.5888 0.5979 0.0432  0.0294  -0.0023 117 HIS A CB  
618  C CG  . HIS A 83  ? 0.5055 0.6078 0.6324 0.0541  0.0426  -0.0037 117 HIS A CG  
619  N ND1 . HIS A 83  ? 0.5017 0.6138 0.6683 0.0528  0.0348  0.0036  117 HIS A ND1 
620  C CD2 . HIS A 83  ? 0.5764 0.6796 0.6963 0.0683  0.0609  -0.0122 117 HIS A CD2 
621  C CE1 . HIS A 83  ? 0.5679 0.6888 0.7562 0.0644  0.0458  0.0006  117 HIS A CE1 
622  N NE2 . HIS A 83  ? 0.5420 0.6598 0.7044 0.0751  0.0633  -0.0094 117 HIS A NE2 
623  N N   . ALA A 84  ? 0.5251 0.5589 0.5487 0.0523  0.0224  -0.0342 118 ALA A N   
624  C CA  . ALA A 84  ? 0.6016 0.6036 0.5880 0.0606  0.0205  -0.0500 118 ALA A CA  
625  C C   . ALA A 84  ? 0.6001 0.6053 0.5836 0.0789  0.0437  -0.0560 118 ALA A C   
626  O O   . ALA A 84  ? 0.5998 0.5989 0.5494 0.0892  0.0621  -0.0583 118 ALA A O   
627  C CB  . ALA A 84  ? 0.6273 0.6017 0.5626 0.0564  0.0114  -0.0530 118 ALA A CB  
628  N N   . HIS A 85  ? 0.5891 0.6025 0.6079 0.0841  0.0432  -0.0586 119 HIS A N   
629  C CA  . HIS A 85  ? 0.5930 0.6070 0.6164 0.1039  0.0599  -0.0668 119 HIS A CA  
630  C C   . HIS A 85  ? 0.5888 0.5793 0.6192 0.1061  0.0426  -0.0777 119 HIS A C   
631  O O   . HIS A 85  ? 0.6502 0.6352 0.6937 0.0907  0.0234  -0.0741 119 HIS A O   
632  C CB  . HIS A 85  ? 0.6109 0.6679 0.6840 0.1085  0.0788  -0.0530 119 HIS A CB  
633  C CG  . HIS A 85  ? 0.6392 0.7158 0.6995 0.1158  0.1067  -0.0461 119 HIS A CG  
634  N ND1 . HIS A 85  ? 0.5620 0.6820 0.6692 0.1147  0.1237  -0.0284 119 HIS A ND1 
635  C CD2 . HIS A 85  ? 0.6430 0.6991 0.6462 0.1232  0.1206  -0.0530 119 HIS A CD2 
636  C CE1 . HIS A 85  ? 0.5680 0.6984 0.6505 0.1203  0.1504  -0.0235 119 HIS A CE1 
637  N NE2 . HIS A 85  ? 0.5862 0.6754 0.6009 0.1265  0.1497  -0.0391 119 HIS A NE2 
638  N N   . GLN A 86  ? 0.7363 0.7115 0.7564 0.1262  0.0506  -0.0906 120 GLN A N   
639  C CA  . GLN A 86  ? 0.6768 0.6178 0.6900 0.1285  0.0307  -0.1025 120 GLN A CA  
640  C C   . GLN A 86  ? 0.6497 0.6025 0.7078 0.1167  0.0178  -0.0934 120 GLN A C   
641  O O   . GLN A 86  ? 0.6650 0.5932 0.7159 0.1039  -0.0028 -0.0952 120 GLN A O   
642  C CB  . GLN A 86  ? 0.7621 0.6853 0.7599 0.1562  0.0417  -0.1182 120 GLN A CB  
643  C CG  . GLN A 86  ? 0.8331 0.7016 0.7930 0.1595  0.0175  -0.1343 120 GLN A CG  
644  C CD  . GLN A 86  ? 1.1530 0.9973 1.0886 0.1913  0.0279  -0.1524 120 GLN A CD  
645  O OE1 . GLN A 86  ? 1.2524 1.1246 1.1984 0.2122  0.0581  -0.1531 120 GLN A OE1 
646  N NE2 . GLN A 86  ? 1.1912 0.9833 1.0953 0.1957  0.0031  -0.1666 120 GLN A NE2 
647  N N   . ASP A 87  ? 0.6171 0.6047 0.7196 0.1198  0.0288  -0.0823 121 ASP A N   
648  C CA  . ASP A 87  ? 0.6136 0.6030 0.7498 0.1104  0.0143  -0.0741 121 ASP A CA  
649  C C   . ASP A 87  ? 0.6073 0.5986 0.7422 0.0885  0.0036  -0.0634 121 ASP A C   
650  O O   . ASP A 87  ? 0.6048 0.5884 0.7544 0.0804  -0.0082 -0.0574 121 ASP A O   
651  C CB  . ASP A 87  ? 0.6094 0.6315 0.7943 0.1191  0.0240  -0.0638 121 ASP A CB  
652  C CG  . ASP A 87  ? 0.6710 0.7311 0.8686 0.1167  0.0429  -0.0513 121 ASP A CG  
653  O OD1 . ASP A 87  ? 0.6980 0.7553 0.8601 0.1129  0.0508  -0.0539 121 ASP A OD1 
654  O OD2 . ASP A 87  ? 0.7389 0.8287 0.9816 0.1172  0.0470  -0.0377 121 ASP A OD2 
655  N N   . LYS A 88  ? 0.5826 0.5807 0.6980 0.0804  0.0071  -0.0613 122 LYS A N   
656  C CA  . LYS A 88  ? 0.5904 0.5954 0.7098 0.0637  -0.0009 -0.0516 122 LYS A CA  
657  C C   . LYS A 88  ? 0.6129 0.5993 0.7092 0.0529  -0.0123 -0.0568 122 LYS A C   
658  O O   . LYS A 88  ? 0.5896 0.5748 0.6951 0.0411  -0.0202 -0.0514 122 LYS A O   
659  C CB  . LYS A 88  ? 0.6732 0.7054 0.7994 0.0616  0.0083  -0.0413 122 LYS A CB  
660  C CG  . LYS A 88  ? 0.6064 0.6620 0.7622 0.0695  0.0193  -0.0325 122 LYS A CG  
661  C CD  . LYS A 88  ? 0.5640 0.6218 0.7476 0.0632  0.0077  -0.0217 122 LYS A CD  
662  C CE  . LYS A 88  ? 0.6735 0.7235 0.8795 0.0720  0.0036  -0.0240 122 LYS A CE  
663  N NZ  . LYS A 88  ? 0.4492 0.4826 0.6640 0.0645  -0.0136 -0.0166 122 LYS A NZ  
664  N N   . MET A 89  ? 0.5493 0.5198 0.6157 0.0568  -0.0138 -0.0663 123 MET A N   
665  C CA  . MET A 89  ? 0.6192 0.5697 0.6677 0.0450  -0.0302 -0.0697 123 MET A CA  
666  C C   . MET A 89  ? 0.6743 0.5866 0.6958 0.0497  -0.0414 -0.0822 123 MET A C   
667  O O   . MET A 89  ? 0.6396 0.5282 0.6384 0.0419  -0.0579 -0.0862 123 MET A O   
668  C CB  . MET A 89  ? 0.5912 0.5451 0.6207 0.0418  -0.0322 -0.0684 123 MET A CB  
669  C CG  . MET A 89  ? 0.7139 0.6996 0.7621 0.0402  -0.0222 -0.0570 123 MET A CG  
670  S SD  . MET A 89  ? 0.6828 0.6648 0.7061 0.0336  -0.0315 -0.0546 123 MET A SD  
671  C CE  . MET A 89  ? 0.7482 0.7088 0.7711 0.0206  -0.0576 -0.0587 123 MET A CE  
672  N N   . GLY A 90  ? 0.6751 0.5775 0.6991 0.0624  -0.0367 -0.0883 124 GLY A N   
673  C CA  . GLY A 90  ? 0.6143 0.4749 0.6097 0.0692  -0.0499 -0.1014 124 GLY A CA  
674  C C   . GLY A 90  ? 0.6687 0.5060 0.6653 0.0498  -0.0720 -0.0980 124 GLY A C   
675  O O   . GLY A 90  ? 0.8051 0.6016 0.7718 0.0496  -0.0904 -0.1069 124 GLY A O   
676  N N   . GLY A 91  ? 0.5884 0.4480 0.6160 0.0337  -0.0705 -0.0845 125 GLY A N   
677  C CA  . GLY A 91  ? 0.6146 0.4580 0.6470 0.0136  -0.0858 -0.0778 125 GLY A CA  
678  C C   . GLY A 91  ? 0.6964 0.5612 0.7466 -0.0050 -0.0892 -0.0670 125 GLY A C   
679  O O   . GLY A 91  ? 0.6609 0.5362 0.7330 -0.0213 -0.0886 -0.0552 125 GLY A O   
680  N N   . MET A 92  ? 0.7554 0.6258 0.7957 -0.0020 -0.0924 -0.0704 126 MET A N   
681  C CA  . MET A 92  ? 0.6667 0.5594 0.7297 -0.0172 -0.0986 -0.0605 126 MET A CA  
682  C C   . MET A 92  ? 0.7013 0.5751 0.7708 -0.0375 -0.1216 -0.0551 126 MET A C   
683  O O   . MET A 92  ? 0.6373 0.5380 0.7452 -0.0539 -0.1210 -0.0416 126 MET A O   
684  C CB  . MET A 92  ? 0.6787 0.5733 0.7228 -0.0089 -0.1006 -0.0657 126 MET A CB  
685  C CG  . MET A 92  ? 0.6787 0.6097 0.7382 -0.0008 -0.0811 -0.0609 126 MET A CG  
686  S SD  . MET A 92  ? 0.9087 0.8826 1.0176 -0.0118 -0.0745 -0.0460 126 MET A SD  
687  C CE  . MET A 92  ? 0.7833 0.7629 0.9070 -0.0104 -0.0581 -0.0415 126 MET A CE  
688  N N   . GLY A 93  ? 0.7332 0.5606 0.7669 -0.0364 -0.1422 -0.0647 127 GLY A N   
689  C CA  . GLY A 93  ? 0.6935 0.4975 0.7330 -0.0584 -0.1690 -0.0576 127 GLY A CA  
690  C C   . GLY A 93  ? 0.6359 0.4494 0.7029 -0.0743 -0.1626 -0.0448 127 GLY A C   
691  O O   . GLY A 93  ? 0.7849 0.6046 0.8803 -0.0983 -0.1751 -0.0303 127 GLY A O   
692  N N   . ALA A 94  ? 0.6616 0.4754 0.7208 -0.0623 -0.1437 -0.0484 128 ALA A N   
693  C CA  . ALA A 94  ? 0.6235 0.4392 0.6982 -0.0769 -0.1367 -0.0361 128 ALA A CA  
694  C C   . ALA A 94  ? 0.7069 0.5726 0.8243 -0.0874 -0.1151 -0.0201 128 ALA A C   
695  O O   . ALA A 94  ? 0.7224 0.5956 0.8607 -0.1078 -0.1124 -0.0047 128 ALA A O   
696  C CB  . ALA A 94  ? 0.6815 0.4781 0.7339 -0.0601 -0.1270 -0.0446 128 ALA A CB  
697  N N   . LEU A 95  ? 0.6108 0.5099 0.7403 -0.0730 -0.0987 -0.0231 129 LEU A N   
698  C CA  . LEU A 95  ? 0.6158 0.5591 0.7829 -0.0782 -0.0792 -0.0104 129 LEU A CA  
699  C C   . LEU A 95  ? 0.6060 0.5732 0.8109 -0.0944 -0.0907 -0.0005 129 LEU A C   
700  O O   . LEU A 95  ? 0.6263 0.6260 0.8698 -0.1058 -0.0772 0.0141  129 LEU A O   
701  C CB  . LEU A 95  ? 0.4977 0.4630 0.6636 -0.0581 -0.0635 -0.0164 129 LEU A CB  
702  C CG  . LEU A 95  ? 0.5748 0.5239 0.7162 -0.0437 -0.0525 -0.0221 129 LEU A CG  
703  C CD1 . LEU A 95  ? 0.6887 0.6614 0.8352 -0.0283 -0.0401 -0.0238 129 LEU A CD1 
704  C CD2 . LEU A 95  ? 0.5029 0.4398 0.6406 -0.0528 -0.0431 -0.0128 129 LEU A CD2 
705  N N   . HIS A 96  ? 0.6367 0.5870 0.8312 -0.0950 -0.1159 -0.0078 130 HIS A N   
706  C CA  . HIS A 96  ? 0.5878 0.5555 0.8204 -0.1117 -0.1345 0.0023  130 HIS A CA  
707  C C   . HIS A 96  ? 0.6299 0.5852 0.8808 -0.1378 -0.1502 0.0160  130 HIS A C   
708  O O   . HIS A 96  ? 0.5803 0.5659 0.8838 -0.1561 -0.1572 0.0319  130 HIS A O   
709  C CB  . HIS A 96  ? 0.6513 0.5934 0.8563 -0.1046 -0.1606 -0.0096 130 HIS A CB  
710  C CG  . HIS A 96  ? 0.6206 0.5804 0.8158 -0.0846 -0.1472 -0.0178 130 HIS A CG  
711  N ND1 . HIS A 96  ? 0.6671 0.5973 0.8180 -0.0725 -0.1603 -0.0309 130 HIS A ND1 
712  C CD2 . HIS A 96  ? 0.4691 0.4689 0.6889 -0.0752 -0.1227 -0.0141 130 HIS A CD2 
713  C CE1 . HIS A 96  ? 0.6843 0.6385 0.8365 -0.0591 -0.1444 -0.0330 130 HIS A CE1 
714  N NE2 . HIS A 96  ? 0.6388 0.6339 0.8328 -0.0602 -0.1237 -0.0234 130 HIS A NE2 
715  N N   . ALA A 97  ? 0.6702 0.5818 0.8823 -0.1405 -0.1572 0.0115  131 ALA A N   
716  C CA  . ALA A 97  ? 0.6357 0.5296 0.8604 -0.1678 -0.1743 0.0262  131 ALA A CA  
717  C C   . ALA A 97  ? 0.5790 0.5139 0.8459 -0.1827 -0.1450 0.0467  131 ALA A C   
718  O O   . ALA A 97  ? 0.6785 0.6241 0.9823 -0.2100 -0.1536 0.0665  131 ALA A O   
719  C CB  . ALA A 97  ? 0.6517 0.4825 0.8187 -0.1643 -0.1913 0.0147  131 ALA A CB  
720  N N   . GLU A 98  ? 0.5920 0.5477 0.8523 -0.1656 -0.1107 0.0435  132 GLU A N   
721  C CA  . GLU A 98  ? 0.5728 0.5617 0.8604 -0.1745 -0.0782 0.0607  132 GLU A CA  
722  C C   . GLU A 98  ? 0.6011 0.6512 0.9425 -0.1679 -0.0568 0.0677  132 GLU A C   
723  O O   . GLU A 98  ? 0.5549 0.6334 0.9119 -0.1661 -0.0233 0.0779  132 GLU A O   
724  C CB  . GLU A 98  ? 0.5872 0.5509 0.8272 -0.1594 -0.0573 0.0532  132 GLU A CB  
725  C CG  . GLU A 98  ? 0.8771 0.7798 1.0648 -0.1588 -0.0801 0.0423  132 GLU A CG  
726  C CD  . GLU A 98  ? 0.9176 0.7918 1.0938 -0.1839 -0.0838 0.0579  132 GLU A CD  
727  O OE1 . GLU A 98  ? 1.0764 0.8995 1.2193 -0.1894 -0.1119 0.0518  132 GLU A OE1 
728  O OE2 . GLU A 98  ? 1.0013 0.9019 1.1991 -0.1976 -0.0579 0.0765  132 GLU A OE2 
729  N N   . ALA A 99  ? 0.5650 0.6313 0.9303 -0.1628 -0.0763 0.0618  133 ALA A N   
730  C CA  . ALA A 99  ? 0.4952 0.6168 0.9153 -0.1558 -0.0632 0.0675  133 ALA A CA  
731  C C   . ALA A 99  ? 0.5247 0.6618 0.9280 -0.1301 -0.0304 0.0596  133 ALA A C   
732  O O   . ALA A 99  ? 0.5189 0.6959 0.9569 -0.1259 -0.0020 0.0694  133 ALA A O   
733  C CB  . ALA A 99  ? 0.4665 0.6330 0.9571 -0.1787 -0.0545 0.0919  133 ALA A CB  
734  N N   . ILE A 100 ? 0.5158 0.6195 0.8656 -0.1122 -0.0348 0.0421  134 ILE A N   
735  C CA  . ILE A 100 ? 0.5326 0.6415 0.8612 -0.0891 -0.0122 0.0344  134 ILE A CA  
736  C C   . ILE A 100 ? 0.5185 0.6418 0.8555 -0.0746 -0.0242 0.0250  134 ILE A C   
737  O O   . ILE A 100 ? 0.5562 0.6554 0.8692 -0.0734 -0.0471 0.0151  134 ILE A O   
738  C CB  . ILE A 100 ? 0.4778 0.5425 0.7485 -0.0809 -0.0104 0.0247  134 ILE A CB  
739  C CG1 . ILE A 100 ? 0.4780 0.5233 0.7346 -0.0948 0.0015  0.0349  134 ILE A CG1 
740  C CG2 . ILE A 100 ? 0.4051 0.4714 0.6559 -0.0583 0.0037  0.0171  134 ILE A CG2 
741  C CD1 . ILE A 100 ? 0.4539 0.4518 0.6573 -0.0877 -0.0026 0.0260  134 ILE A CD1 
742  N N   . PRO A 101 ? 0.4644 0.6222 0.8302 -0.0626 -0.0098 0.0277  135 PRO A N   
743  C CA  . PRO A 101 ? 0.4615 0.6272 0.8302 -0.0495 -0.0239 0.0195  135 PRO A CA  
744  C C   . PRO A 101 ? 0.4889 0.6229 0.8038 -0.0359 -0.0262 0.0072  135 PRO A C   
745  O O   . PRO A 101 ? 0.5166 0.6404 0.8072 -0.0255 -0.0090 0.0057  135 PRO A O   
746  C CB  . PRO A 101 ? 0.3991 0.6033 0.8053 -0.0369 -0.0044 0.0249  135 PRO A CB  
747  C CG  . PRO A 101 ? 0.3465 0.5736 0.7858 -0.0481 0.0177  0.0386  135 PRO A CG  
748  C CD  . PRO A 101 ? 0.4291 0.6186 0.8253 -0.0601 0.0199  0.0388  135 PRO A CD  
749  N N   . THR A 102 ? 0.4797 0.5967 0.7757 -0.0363 -0.0480 -0.0004 136 THR A N   
750  C CA  . THR A 102 ? 0.5289 0.6211 0.7804 -0.0252 -0.0488 -0.0099 136 THR A CA  
751  C C   . THR A 102 ? 0.4656 0.5667 0.7155 -0.0154 -0.0563 -0.0122 136 THR A C   
752  O O   . THR A 102 ? 0.4007 0.5107 0.6690 -0.0198 -0.0732 -0.0110 136 THR A O   
753  C CB  . THR A 102 ? 0.5944 0.6547 0.8150 -0.0308 -0.0633 -0.0171 136 THR A CB  
754  O OG1 . THR A 102 ? 0.5041 0.5603 0.7305 -0.0387 -0.0865 -0.0179 136 THR A OG1 
755  C CG2 . THR A 102 ? 0.4559 0.5011 0.6745 -0.0410 -0.0600 -0.0146 136 THR A CG2 
756  N N   . TYR A 103 ? 0.4386 0.5340 0.6664 -0.0036 -0.0471 -0.0143 137 TYR A N   
757  C CA  . TYR A 103 ? 0.4186 0.5183 0.6406 0.0043  -0.0544 -0.0145 137 TYR A CA  
758  C C   . TYR A 103 ? 0.4198 0.5007 0.6053 0.0079  -0.0543 -0.0179 137 TYR A C   
759  O O   . TYR A 103 ? 0.4207 0.4916 0.5933 0.0104  -0.0437 -0.0192 137 TYR A O   
760  C CB  . TYR A 103 ? 0.3713 0.4842 0.6067 0.0152  -0.0446 -0.0105 137 TYR A CB  
761  C CG  . TYR A 103 ? 0.4997 0.6383 0.7760 0.0159  -0.0409 -0.0067 137 TYR A CG  
762  C CD1 . TYR A 103 ? 0.4258 0.5731 0.7189 0.0112  -0.0245 -0.0030 137 TYR A CD1 
763  C CD2 . TYR A 103 ? 0.4589 0.6138 0.7594 0.0213  -0.0532 -0.0058 137 TYR A CD2 
764  C CE1 . TYR A 103 ? 0.4778 0.6554 0.8150 0.0120  -0.0161 0.0027  137 TYR A CE1 
765  C CE2 . TYR A 103 ? 0.4637 0.6485 0.8114 0.0243  -0.0479 -0.0018 137 TYR A CE2 
766  C CZ  . TYR A 103 ? 0.5452 0.7443 0.9133 0.0196  -0.0271 0.0030  137 TYR A CZ  
767  O OH  . TYR A 103 ? 0.6736 0.9090 1.0949 0.0227  -0.0169 0.0092  137 TYR A OH  
768  N N   . ALA A 104 ? 0.4108 0.4873 0.5815 0.0081  -0.0660 -0.0183 138 ALA A N   
769  C CA  . ALA A 104 ? 0.5027 0.5664 0.6412 0.0111  -0.0620 -0.0189 138 ALA A CA  
770  C C   . ALA A 104 ? 0.4740 0.5361 0.6003 0.0109  -0.0738 -0.0146 138 ALA A C   
771  O O   . ALA A 104 ? 0.4529 0.5179 0.5917 0.0085  -0.0897 -0.0141 138 ALA A O   
772  C CB  . ALA A 104 ? 0.4971 0.5415 0.6093 0.0091  -0.0616 -0.0263 138 ALA A CB  
773  N N   . ASN A 105 ? 0.3855 0.4432 0.4901 0.0127  -0.0667 -0.0103 139 ASN A N   
774  C CA  . ASN A 105 ? 0.4707 0.5206 0.5538 0.0097  -0.0776 -0.0046 139 ASN A CA  
775  C C   . ASN A 105 ? 0.4929 0.5224 0.5486 0.0048  -0.0910 -0.0102 139 ASN A C   
776  O O   . ASN A 105 ? 0.5547 0.5715 0.5933 0.0049  -0.0860 -0.0178 139 ASN A O   
777  C CB  . ASN A 105 ? 0.4933 0.5440 0.5591 0.0097  -0.0637 0.0034  139 ASN A CB  
778  C CG  . ASN A 105 ? 0.4682 0.5085 0.5077 0.0036  -0.0738 0.0125  139 ASN A CG  
779  O OD1 . ASN A 105 ? 0.4912 0.5214 0.5263 0.0009  -0.0947 0.0122  139 ASN A OD1 
780  N ND2 . ASN A 105 ? 0.4816 0.5251 0.5062 0.0009  -0.0593 0.0219  139 ASN A ND2 
781  N N   . ALA A 106 ? 0.4397 0.4600 0.4882 0.0010  -0.1120 -0.0068 140 ALA A N   
782  C CA  . ALA A 106 ? 0.5036 0.4962 0.5212 -0.0046 -0.1314 -0.0112 140 ALA A CA  
783  C C   . ALA A 106 ? 0.5609 0.5275 0.5213 -0.0048 -0.1187 -0.0132 140 ALA A C   
784  O O   . ALA A 106 ? 0.5669 0.5047 0.4952 -0.0061 -0.1277 -0.0210 140 ALA A O   
785  C CB  . ALA A 106 ? 0.5752 0.5583 0.5912 -0.0081 -0.1583 -0.0059 140 ALA A CB  
786  N N   . LEU A 107 ? 0.6042 0.5794 0.5512 -0.0030 -0.0976 -0.0055 141 LEU A N   
787  C CA  . LEU A 107 ? 0.6048 0.5629 0.5031 -0.0003 -0.0773 -0.0065 141 LEU A CA  
788  C C   . LEU A 107 ? 0.6122 0.5743 0.5171 0.0089  -0.0593 -0.0173 141 LEU A C   
789  O O   . LEU A 107 ? 0.6350 0.5693 0.4940 0.0144  -0.0524 -0.0257 141 LEU A O   
790  C CB  . LEU A 107 ? 0.6335 0.6080 0.5289 -0.0025 -0.0584 0.0080  141 LEU A CB  
791  C CG  . LEU A 107 ? 0.6351 0.6029 0.4892 0.0018  -0.0289 0.0101  141 LEU A CG  
792  C CD1 . LEU A 107 ? 0.6743 0.5949 0.4564 0.0010  -0.0370 0.0039  141 LEU A CD1 
793  C CD2 . LEU A 107 ? 0.6000 0.5909 0.4643 -0.0046 -0.0130 0.0293  141 LEU A CD2 
794  N N   . SER A 108 ? 0.5060 0.4963 0.4615 0.0118  -0.0529 -0.0178 142 SER A N   
795  C CA  . SER A 108 ? 0.5046 0.4947 0.4669 0.0197  -0.0404 -0.0276 142 SER A CA  
796  C C   . SER A 108 ? 0.6228 0.5830 0.5653 0.0180  -0.0591 -0.0393 142 SER A C   
797  O O   . SER A 108 ? 0.5590 0.4987 0.4761 0.0255  -0.0524 -0.0494 142 SER A O   
798  C CB  . SER A 108 ? 0.5084 0.5263 0.5227 0.0207  -0.0354 -0.0247 142 SER A CB  
799  O OG  . SER A 108 ? 0.5777 0.6172 0.6108 0.0203  -0.0266 -0.0125 142 SER A OG  
800  N N   . ASN A 109 ? 0.6009 0.5571 0.5570 0.0085  -0.0848 -0.0376 143 ASN A N   
801  C CA  . ASN A 109 ? 0.5578 0.4856 0.5015 0.0034  -0.1084 -0.0454 143 ASN A CA  
802  C C   . ASN A 109 ? 0.6540 0.5341 0.5288 0.0044  -0.1201 -0.0509 143 ASN A C   
803  O O   . ASN A 109 ? 0.7293 0.5726 0.5741 0.0044  -0.1351 -0.0601 143 ASN A O   
804  C CB  . ASN A 109 ? 0.5770 0.5223 0.5688 -0.0067 -0.1316 -0.0398 143 ASN A CB  
805  C CG  . ASN A 109 ? 0.5516 0.5351 0.6011 -0.0066 -0.1186 -0.0360 143 ASN A CG  
806  O OD1 . ASN A 109 ? 0.5659 0.5506 0.6194 -0.0038 -0.1049 -0.0398 143 ASN A OD1 
807  N ND2 . ASN A 109 ? 0.5591 0.5697 0.6490 -0.0081 -0.1233 -0.0288 143 ASN A ND2 
808  N N   . GLN A 110 ? 0.6788 0.5529 0.5220 0.0047  -0.1150 -0.0448 144 GLN A N   
809  C CA  . GLN A 110 ? 0.8054 0.6283 0.5701 0.0069  -0.1211 -0.0494 144 GLN A CA  
810  C C   . GLN A 110 ? 0.8059 0.6154 0.5277 0.0221  -0.0891 -0.0574 144 GLN A C   
811  O O   . GLN A 110 ? 0.8767 0.6344 0.5281 0.0285  -0.0937 -0.0669 144 GLN A O   
812  C CB  . GLN A 110 ? 0.7432 0.5614 0.4839 0.0007  -0.1248 -0.0383 144 GLN A CB  
813  C CG  . GLN A 110 ? 0.8031 0.6290 0.5818 -0.0107 -0.1592 -0.0318 144 GLN A CG  
814  C CD  . GLN A 110 ? 0.8959 0.7089 0.6437 -0.0168 -0.1669 -0.0211 144 GLN A CD  
815  O OE1 . GLN A 110 ? 0.9372 0.7242 0.6215 -0.0154 -0.1505 -0.0183 144 GLN A OE1 
816  N NE2 . GLN A 110 ? 0.8125 0.6426 0.6041 -0.0229 -0.1908 -0.0146 144 GLN A NE2 
817  N N   . LEU A 111 ? 0.7802 0.6327 0.5421 0.0295  -0.0582 -0.0542 145 LEU A N   
818  C CA  . LEU A 111 ? 0.7801 0.6296 0.5151 0.0464  -0.0255 -0.0606 145 LEU A CA  
819  C C   . LEU A 111 ? 0.8686 0.7085 0.6144 0.0561  -0.0270 -0.0745 145 LEU A C   
820  O O   . LEU A 111 ? 0.8776 0.6975 0.5858 0.0735  -0.0078 -0.0849 145 LEU A O   
821  C CB  . LEU A 111 ? 0.6937 0.5946 0.4711 0.0489  0.0058  -0.0477 145 LEU A CB  
822  C CG  . LEU A 111 ? 0.7445 0.6507 0.4963 0.0433  0.0194  -0.0331 145 LEU A CG  
823  C CD1 . LEU A 111 ? 0.6579 0.6176 0.4719 0.0386  0.0354  -0.0168 145 LEU A CD1 
824  C CD2 . LEU A 111 ? 0.8299 0.7088 0.5133 0.0569  0.0471  -0.0378 145 LEU A CD2 
825  N N   . ALA A 112 ? 0.9063 0.7589 0.7012 0.0460  -0.0484 -0.0744 146 ALA A N   
826  C CA  . ALA A 112 ? 0.8698 0.7128 0.6770 0.0521  -0.0516 -0.0848 146 ALA A CA  
827  C C   . ALA A 112 ? 0.9610 0.7426 0.7016 0.0602  -0.0666 -0.1000 146 ALA A C   
828  O O   . ALA A 112 ? 0.9572 0.7236 0.6805 0.0767  -0.0535 -0.1113 146 ALA A O   
829  C CB  . ALA A 112 ? 0.7648 0.6302 0.6314 0.0364  -0.0713 -0.0789 146 ALA A CB  
830  N N   . PRO A 113 ? 1.0376 0.7770 0.7370 0.0509  -0.0966 -0.1016 147 PRO A N   
831  C CA  . PRO A 113 ? 1.1878 0.8578 0.8138 0.0601  -0.1141 -0.1168 147 PRO A CA  
832  C C   . PRO A 113 ? 1.2187 0.8614 0.7735 0.0842  -0.0830 -0.1266 147 PRO A C   
833  O O   . PRO A 113 ? 1.3011 0.8917 0.7993 0.1005  -0.0866 -0.1425 147 PRO A O   
834  C CB  . PRO A 113 ? 1.0983 0.7319 0.7011 0.0425  -0.1558 -0.1128 147 PRO A CB  
835  C CG  . PRO A 113 ? 1.0339 0.7256 0.7189 0.0240  -0.1628 -0.0972 147 PRO A CG  
836  C CD  . PRO A 113 ? 0.9518 0.6991 0.6710 0.0321  -0.1218 -0.0905 147 PRO A CD  
837  N N   . GLN A 114 ? 1.4322 1.1074 0.9874 0.0875  -0.0521 -0.1170 148 GLN A N   
838  C CA  . GLN A 114 ? 1.4866 1.1443 0.9800 0.1102  -0.0155 -0.1234 148 GLN A CA  
839  C C   . GLN A 114 ? 1.3517 1.0359 0.8732 0.1324  0.0165  -0.1314 148 GLN A C   
840  O O   . GLN A 114 ? 1.3678 1.0301 0.8362 0.1570  0.0455  -0.1414 148 GLN A O   
841  C CB  . GLN A 114 ? 1.4503 1.1409 0.9453 0.1036  0.0087  -0.1067 148 GLN A CB  
842  C CG  . GLN A 114 ? 1.6361 1.2989 1.1032 0.0828  -0.0247 -0.0984 148 GLN A CG  
843  C CD  . GLN A 114 ? 1.6750 1.3291 1.0881 0.0827  -0.0020 -0.0881 148 GLN A CD  
844  O OE1 . GLN A 114 ? 1.5776 1.1858 0.9355 0.0716  -0.0280 -0.0853 148 GLN A OE1 
845  N NE2 . GLN A 114 ? 1.5219 1.2196 0.9522 0.0938  0.0451  -0.0808 148 GLN A NE2 
846  N N   . GLU A 115 ? 1.2164 0.9449 0.8182 0.1256  0.0122  -0.1274 149 GLU A N   
847  C CA  . GLU A 115 ? 1.2148 0.9648 0.8486 0.1452  0.0347  -0.1348 149 GLU A CA  
848  C C   . GLU A 115 ? 1.1933 0.9134 0.8356 0.1438  0.0041  -0.1464 149 GLU A C   
849  O O   . GLU A 115 ? 1.1645 0.9059 0.8491 0.1532  0.0128  -0.1496 149 GLU A O   
850  C CB  . GLU A 115 ? 1.0475 0.8713 0.7647 0.1393  0.0569  -0.1184 149 GLU A CB  
851  C CG  . GLU A 115 ? 1.0265 0.8837 0.7425 0.1503  0.0981  -0.1089 149 GLU A CG  
852  C CD  . GLU A 115 ? 1.1309 1.0415 0.9041 0.1298  0.1019  -0.0866 149 GLU A CD  
853  O OE1 . GLU A 115 ? 1.0936 1.0268 0.8604 0.1306  0.1286  -0.0743 149 GLU A OE1 
854  O OE2 . GLU A 115 ? 1.1200 1.0471 0.9412 0.1131  0.0780  -0.0807 149 GLU A OE2 
855  N N   . GLY A 116 ? 1.3400 0.9334 1.1712 0.0755  -0.1168 -0.2230 150 GLY A N   
856  C CA  . GLY A 116 ? 1.3749 0.9397 1.2431 0.0599  -0.1378 -0.2234 150 GLY A CA  
857  C C   . GLY A 116 ? 1.3254 0.9383 1.2693 0.0346  -0.1226 -0.1990 150 GLY A C   
858  O O   . GLY A 116 ? 1.2940 0.9043 1.2593 0.0330  -0.1121 -0.1911 150 GLY A O   
859  N N   . MET A 117 ? 0.9707 0.6262 0.9526 0.0167  -0.1210 -0.1868 151 MET A N   
860  C CA  . MET A 117 ? 0.8541 0.5568 0.9025 -0.0041 -0.1047 -0.1632 151 MET A CA  
861  C C   . MET A 117 ? 0.8371 0.5489 0.9356 -0.0288 -0.1293 -0.1576 151 MET A C   
862  O O   . MET A 117 ? 0.8102 0.5083 0.8916 -0.0294 -0.1530 -0.1696 151 MET A O   
863  C CB  . MET A 117 ? 0.9240 0.6803 0.9723 0.0018  -0.0702 -0.1496 151 MET A CB  
864  C CG  . MET A 117 ? 1.0466 0.8004 1.0443 0.0274  -0.0474 -0.1548 151 MET A CG  
865  S SD  . MET A 117 ? 1.0699 0.8185 1.0801 0.0338  -0.0283 -0.1466 151 MET A SD  
866  C CE  . MET A 117 ? 0.6236 0.4340 0.6844 0.0194  -0.0016 -0.1203 151 MET A CE  
867  N N   . THR A 118 ? 0.7971 0.5331 0.9582 -0.0482 -0.1231 -0.1381 152 THR A N   
868  C CA  . THR A 118 ? 0.7192 0.4777 0.9391 -0.0713 -0.1389 -0.1267 152 THR A CA  
869  C C   . THR A 118 ? 0.6652 0.4788 0.8980 -0.0715 -0.1163 -0.1146 152 THR A C   
870  O O   . THR A 118 ? 0.5920 0.4394 0.8354 -0.0684 -0.0850 -0.0996 152 THR A O   
871  C CB  . THR A 118 ? 0.6880 0.4511 0.9700 -0.0903 -0.1385 -0.1079 152 THR A CB  
872  O OG1 . THR A 118 ? 0.8931 0.5993 1.1637 -0.0916 -0.1649 -0.1197 152 THR A OG1 
873  C CG2 . THR A 118 ? 0.6612 0.4569 1.0106 -0.1128 -0.1497 -0.0920 152 THR A CG2 
874  N N   . ALA A 119 ? 0.6830 0.5023 0.9118 -0.0740 -0.1341 -0.1217 153 ALA A N   
875  C CA  . ALA A 119 ? 0.7163 0.5831 0.9554 -0.0736 -0.1163 -0.1113 153 ALA A CA  
876  C C   . ALA A 119 ? 0.5476 0.4560 0.8567 -0.0900 -0.1047 -0.0879 153 ALA A C   
877  O O   . ALA A 119 ? 0.5599 0.4625 0.9177 -0.1060 -0.1195 -0.0800 153 ALA A O   
878  C CB  . ALA A 119 ? 0.6532 0.5126 0.8719 -0.0724 -0.1409 -0.1243 153 ALA A CB  
879  N N   . ALA A 120 ? 0.5618 0.5114 0.8750 -0.0851 -0.0779 -0.0756 154 ALA A N   
880  C CA  . ALA A 120 ? 0.4643 0.4543 0.8360 -0.0958 -0.0638 -0.0535 154 ALA A CA  
881  C C   . ALA A 120 ? 0.5208 0.5245 0.9353 -0.1084 -0.0871 -0.0511 154 ALA A C   
882  O O   . ALA A 120 ? 0.5692 0.5604 0.9598 -0.1058 -0.1090 -0.0660 154 ALA A O   
883  C CB  . ALA A 120 ? 0.4221 0.4461 0.7793 -0.0846 -0.0337 -0.0439 154 ALA A CB  
884  N N   . GLN A 121 ? 0.5007 0.5313 0.9801 -0.1214 -0.0820 -0.0307 155 GLN A N   
885  C CA  . GLN A 121 ? 0.5160 0.5638 1.0481 -0.1346 -0.1043 -0.0251 155 GLN A CA  
886  C C   . GLN A 121 ? 0.4976 0.5804 1.0283 -0.1266 -0.0972 -0.0231 155 GLN A C   
887  O O   . GLN A 121 ? 0.5929 0.6844 1.1524 -0.1336 -0.1207 -0.0247 155 GLN A O   
888  C CB  . GLN A 121 ? 0.5934 0.6635 1.2004 -0.1504 -0.0977 -0.0002 155 GLN A CB  
889  C CG  . GLN A 121 ? 0.6139 0.7379 1.2599 -0.1469 -0.0679 0.0232  155 GLN A CG  
890  C CD  . GLN A 121 ? 0.7958 0.9405 1.5070 -0.1592 -0.0534 0.0507  155 GLN A CD  
891  O OE1 . GLN A 121 ? 0.7699 0.9004 1.4701 -0.1584 -0.0367 0.0573  155 GLN A OE1 
892  N NE2 . GLN A 121 ? 0.8124 0.9906 1.5893 -0.1691 -0.0589 0.0681  155 GLN A NE2 
893  N N   . HIS A 122 ? 0.4169 0.5174 0.9151 -0.1122 -0.0681 -0.0198 156 HIS A N   
894  C CA  . HIS A 122 ? 0.4574 0.5850 0.9469 -0.1030 -0.0621 -0.0189 156 HIS A CA  
895  C C   . HIS A 122 ? 0.4219 0.5320 0.8404 -0.0888 -0.0568 -0.0342 156 HIS A C   
896  O O   . HIS A 122 ? 0.3797 0.4726 0.7636 -0.0827 -0.0431 -0.0376 156 HIS A O   
897  C CB  . HIS A 122 ? 0.3896 0.5584 0.9124 -0.0983 -0.0323 0.0032  156 HIS A CB  
898  C CG  . HIS A 122 ? 0.4485 0.6418 1.0453 -0.1108 -0.0317 0.0231  156 HIS A CG  
899  N ND1 . HIS A 122 ? 0.5245 0.7284 1.1698 -0.1223 -0.0572 0.0246  156 HIS A ND1 
900  C CD2 . HIS A 122 ? 0.3982 0.6088 1.0310 -0.1135 -0.0083 0.0443  156 HIS A CD2 
901  C CE1 . HIS A 122 ? 0.4385 0.6680 1.1512 -0.1327 -0.0490 0.0472  156 HIS A CE1 
902  N NE2 . HIS A 122 ? 0.4607 0.6944 1.1654 -0.1272 -0.0183 0.0598  156 HIS A NE2 
903  N N   . SER A 123 ? 0.3695 0.4852 0.7694 -0.0836 -0.0678 -0.0416 157 SER A N   
904  C CA  . SER A 123 ? 0.3712 0.4731 0.7085 -0.0715 -0.0643 -0.0532 157 SER A CA  
905  C C   . SER A 123 ? 0.3814 0.5121 0.7151 -0.0627 -0.0463 -0.0435 157 SER A C   
906  O O   . SER A 123 ? 0.4045 0.5584 0.7698 -0.0635 -0.0511 -0.0370 157 SER A O   
907  C CB  . SER A 123 ? 0.4032 0.4806 0.7120 -0.0716 -0.0938 -0.0702 157 SER A CB  
908  O OG  . SER A 123 ? 0.5876 0.6305 0.8890 -0.0769 -0.1127 -0.0818 157 SER A OG  
909  N N   . LEU A 124 ? 0.3450 0.4731 0.6411 -0.0535 -0.0272 -0.0425 158 LEU A N   
910  C CA  . LEU A 124 ? 0.3316 0.4791 0.6169 -0.0446 -0.0134 -0.0347 158 LEU A CA  
911  C C   . LEU A 124 ? 0.3544 0.4921 0.5988 -0.0397 -0.0256 -0.0441 158 LEU A C   
912  O O   . LEU A 124 ? 0.4592 0.5746 0.6675 -0.0389 -0.0323 -0.0543 158 LEU A O   
913  C CB  . LEU A 124 ? 0.2902 0.4390 0.5595 -0.0383 0.0104  -0.0270 158 LEU A CB  
914  C CG  . LEU A 124 ? 0.3706 0.5267 0.6727 -0.0411 0.0259  -0.0157 158 LEU A CG  
915  C CD1 . LEU A 124 ? 0.3862 0.5389 0.6637 -0.0334 0.0456  -0.0101 158 LEU A CD1 
916  C CD2 . LEU A 124 ? 0.4049 0.5879 0.7502 -0.0409 0.0315  -0.0027 158 LEU A CD2 
917  N N   . THR A 125 ? 0.3549 0.5084 0.6037 -0.0352 -0.0278 -0.0397 159 THR A N   
918  C CA  . THR A 125 ? 0.3938 0.5392 0.6044 -0.0303 -0.0373 -0.0451 159 THR A CA  
919  C C   . THR A 125 ? 0.4142 0.5683 0.6086 -0.0222 -0.0221 -0.0362 159 THR A C   
920  O O   . THR A 125 ? 0.4336 0.6013 0.6476 -0.0185 -0.0068 -0.0269 159 THR A O   
921  C CB  . THR A 125 ? 0.3744 0.5248 0.5997 -0.0313 -0.0588 -0.0490 159 THR A CB  
922  O OG1 . THR A 125 ? 0.4382 0.6148 0.7023 -0.0276 -0.0522 -0.0387 159 THR A OG1 
923  C CG2 . THR A 125 ? 0.3410 0.4791 0.5827 -0.0400 -0.0788 -0.0582 159 THR A CG2 
924  N N   . PHE A 126 ? 0.4269 0.5707 0.5836 -0.0192 -0.0274 -0.0384 160 PHE A N   
925  C CA  . PHE A 126 ? 0.4019 0.5477 0.5397 -0.0134 -0.0173 -0.0304 160 PHE A CA  
926  C C   . PHE A 126 ? 0.3921 0.5334 0.5089 -0.0103 -0.0313 -0.0307 160 PHE A C   
927  O O   . PHE A 126 ? 0.4938 0.6259 0.5967 -0.0130 -0.0461 -0.0372 160 PHE A O   
928  C CB  . PHE A 126 ? 0.3704 0.5071 0.4842 -0.0145 -0.0061 -0.0285 160 PHE A CB  
929  C CG  . PHE A 126 ? 0.4593 0.5964 0.5898 -0.0167 0.0062  -0.0290 160 PHE A CG  
930  C CD1 . PHE A 126 ? 0.3794 0.5054 0.5088 -0.0208 0.0010  -0.0379 160 PHE A CD1 
931  C CD2 . PHE A 126 ? 0.3982 0.5431 0.5422 -0.0136 0.0212  -0.0207 160 PHE A CD2 
932  C CE1 . PHE A 126 ? 0.3074 0.4301 0.4514 -0.0226 0.0104  -0.0384 160 PHE A CE1 
933  C CE2 . PHE A 126 ? 0.3445 0.4878 0.5031 -0.0156 0.0319  -0.0202 160 PHE A CE2 
934  C CZ  . PHE A 126 ? 0.3729 0.5053 0.5329 -0.0206 0.0263  -0.0289 160 PHE A CZ  
935  N N   . ALA A 127 ? 0.4129 0.5573 0.5248 -0.0037 -0.0279 -0.0236 161 ALA A N   
936  C CA  . ALA A 127 ? 0.3873 0.5239 0.4780 -0.0003 -0.0417 -0.0227 161 ALA A CA  
937  C C   . ALA A 127 ? 0.5346 0.6578 0.5917 -0.0049 -0.0428 -0.0187 161 ALA A C   
938  O O   . ALA A 127 ? 0.5848 0.7074 0.6365 -0.0090 -0.0317 -0.0169 161 ALA A O   
939  C CB  . ALA A 127 ? 0.3727 0.5134 0.4691 0.0105  -0.0396 -0.0175 161 ALA A CB  
940  N N   . ALA A 128 ? 0.5461 0.6594 0.5825 -0.0037 -0.0561 -0.0157 162 ALA A N   
941  C CA  . ALA A 128 ? 0.4464 0.5493 0.4551 -0.0093 -0.0577 -0.0085 162 ALA A CA  
942  C C   . ALA A 128 ? 0.4466 0.5506 0.4551 -0.0104 -0.0467 0.0009  162 ALA A C   
943  O O   . ALA A 128 ? 0.6023 0.7054 0.5993 -0.0162 -0.0414 0.0083  162 ALA A O   
944  C CB  . ALA A 128 ? 0.4710 0.5611 0.4599 -0.0085 -0.0758 -0.0055 162 ALA A CB  
945  N N   . ASN A 129 ? 0.4287 0.5347 0.4494 -0.0040 -0.0433 0.0017  163 ASN A N   
946  C CA  . ASN A 129 ? 0.4238 0.5275 0.4429 -0.0040 -0.0365 0.0098  163 ASN A CA  
947  C C   . ASN A 129 ? 0.4615 0.5761 0.4964 -0.0048 -0.0185 0.0088  163 ASN A C   
948  O O   . ASN A 129 ? 0.5714 0.6845 0.6077 -0.0030 -0.0128 0.0145  163 ASN A O   
949  C CB  . ASN A 129 ? 0.3602 0.4539 0.3753 0.0062  -0.0436 0.0108  163 ASN A CB  
950  C CG  . ASN A 129 ? 0.4732 0.5756 0.5046 0.0169  -0.0379 0.0035  163 ASN A CG  
951  O OD1 . ASN A 129 ? 0.4273 0.5443 0.4790 0.0144  -0.0285 -0.0013 163 ASN A OD1 
952  N ND2 . ASN A 129 ? 0.5296 0.6226 0.5528 0.0296  -0.0441 0.0034  163 ASN A ND2 
953  N N   . GLY A 130 ? 0.4245 0.5469 0.4700 -0.0071 -0.0117 0.0015  164 GLY A N   
954  C CA  . GLY A 130 ? 0.4342 0.5633 0.4927 -0.0081 0.0035  0.0002  164 GLY A CA  
955  C C   . GLY A 130 ? 0.4428 0.5780 0.5234 -0.0029 0.0121  -0.0018 164 GLY A C   
956  O O   . GLY A 130 ? 0.4460 0.5849 0.5393 -0.0044 0.0234  -0.0034 164 GLY A O   
957  N N   . TRP A 131 ? 0.4246 0.5604 0.5093 0.0044  0.0080  -0.0008 165 TRP A N   
958  C CA  . TRP A 131 ? 0.4396 0.5837 0.5454 0.0112  0.0193  0.0003  165 TRP A CA  
959  C C   . TRP A 131 ? 0.4454 0.6011 0.5784 0.0077  0.0191  -0.0051 165 TRP A C   
960  O O   . TRP A 131 ? 0.4800 0.6354 0.6124 0.0041  0.0059  -0.0109 165 TRP A O   
961  C CB  . TRP A 131 ? 0.4206 0.5606 0.5177 0.0239  0.0166  0.0039  165 TRP A CB  
962  C CG  . TRP A 131 ? 0.4363 0.5612 0.5092 0.0280  0.0150  0.0094  165 TRP A CG  
963  C CD1 . TRP A 131 ? 0.4544 0.5638 0.5031 0.0289  -0.0006 0.0111  165 TRP A CD1 
964  C CD2 . TRP A 131 ? 0.5009 0.6227 0.5724 0.0311  0.0267  0.0144  165 TRP A CD2 
965  N NE1 . TRP A 131 ? 0.5635 0.6604 0.5979 0.0317  -0.0010 0.0167  165 TRP A NE1 
966  C CE2 . TRP A 131 ? 0.5140 0.6183 0.5607 0.0338  0.0158  0.0185  165 TRP A CE2 
967  C CE3 . TRP A 131 ? 0.3228 0.4529 0.4118 0.0315  0.0437  0.0165  165 TRP A CE3 
968  C CZ2 . TRP A 131 ? 0.5132 0.6086 0.5517 0.0376  0.0203  0.0237  165 TRP A CZ2 
969  C CZ3 . TRP A 131 ? 0.4535 0.5748 0.5323 0.0359  0.0501  0.0220  165 TRP A CZ3 
970  C CH2 . TRP A 131 ? 0.5608 0.6650 0.6142 0.0393  0.0380  0.0251  165 TRP A CH2 
971  N N   . VAL A 132 ? 0.3940 0.5586 0.5519 0.0083  0.0325  -0.0022 166 VAL A N   
972  C CA  . VAL A 132 ? 0.3853 0.5607 0.5758 0.0025  0.0307  -0.0053 166 VAL A CA  
973  C C   . VAL A 132 ? 0.3554 0.5439 0.5640 0.0087  0.0242  -0.0041 166 VAL A C   
974  O O   . VAL A 132 ? 0.3536 0.5450 0.5548 0.0210  0.0288  0.0011  166 VAL A O   
975  C CB  . VAL A 132 ? 0.2908 0.4721 0.5063 0.0007  0.0467  0.0006  166 VAL A CB  
976  C CG1 . VAL A 132 ? 0.2431 0.4364 0.4715 0.0123  0.0612  0.0115  166 VAL A CG1 
977  C CG2 . VAL A 132 ? 0.2499 0.4354 0.4969 -0.0100 0.0400  -0.0036 166 VAL A CG2 
978  N N   . ASP A 133 ? 0.4127 0.6072 0.6434 0.0016  0.0117  -0.0095 167 ASP A N   
979  C CA  . ASP A 133 ? 0.4126 0.6234 0.6686 0.0072  0.0046  -0.0076 167 ASP A CA  
980  C C   . ASP A 133 ? 0.3945 0.6279 0.6930 0.0116  0.0216  0.0039  167 ASP A C   
981  O O   . ASP A 133 ? 0.4651 0.7031 0.7909 0.0018  0.0268  0.0067  167 ASP A O   
982  C CB  . ASP A 133 ? 0.3787 0.5877 0.6465 -0.0024 -0.0171 -0.0165 167 ASP A CB  
983  C CG  . ASP A 133 ? 0.4735 0.6923 0.7506 0.0049  -0.0306 -0.0171 167 ASP A CG  
984  O OD1 . ASP A 133 ? 0.3981 0.6398 0.7103 0.0130  -0.0225 -0.0086 167 ASP A OD1 
985  O OD2 . ASP A 133 ? 0.5753 0.7794 0.8245 0.0037  -0.0484 -0.0250 167 ASP A OD2 
986  N N   . PRO A 134 ? 0.4263 0.6729 0.7300 0.0271  0.0310  0.0116  168 PRO A N   
987  C CA  . PRO A 134 ? 0.4011 0.6719 0.7448 0.0336  0.0513  0.0257  168 PRO A CA  
988  C C   . PRO A 134 ? 0.4728 0.7670 0.8750 0.0227  0.0449  0.0299  168 PRO A C   
989  O O   . PRO A 134 ? 0.4984 0.8120 0.9407 0.0212  0.0613  0.0433  168 PRO A O   
990  C CB  . PRO A 134 ? 0.3620 0.6392 0.6917 0.0561  0.0592  0.0307  168 PRO A CB  
991  C CG  . PRO A 134 ? 0.4335 0.6827 0.7093 0.0596  0.0443  0.0196  168 PRO A CG  
992  C CD  . PRO A 134 ? 0.4384 0.6765 0.7099 0.0410  0.0240  0.0087  168 PRO A CD  
993  N N   . ALA A 135 ? 0.4459 0.7380 0.8551 0.0146  0.0204  0.0199  169 ALA A N   
994  C CA  . ALA A 135 ? 0.2510 0.5619 0.7169 0.0025  0.0085  0.0231  169 ALA A CA  
995  C C   . ALA A 135 ? 0.2946 0.5931 0.7729 -0.0157 0.0052  0.0211  169 ALA A C   
996  O O   . ALA A 135 ? 0.3940 0.7092 0.9268 -0.0262 0.0021  0.0294  169 ALA A O   
997  C CB  . ALA A 135 ? 0.2591 0.5652 0.7218 0.0000  -0.0203 0.0115  169 ALA A CB  
998  N N   . THR A 136 ? 0.3980 0.6674 0.8286 -0.0192 0.0052  0.0111  170 THR A N   
999  C CA  . THR A 136 ? 0.4971 0.7496 0.9313 -0.0333 0.0017  0.0073  170 THR A CA  
1000 C C   . THR A 136 ? 0.4651 0.7181 0.8999 -0.0314 0.0272  0.0181  170 THR A C   
1001 O O   . THR A 136 ? 0.4594 0.7023 0.9089 -0.0426 0.0263  0.0186  170 THR A O   
1002 C CB  . THR A 136 ? 0.3751 0.5954 0.7572 -0.0369 -0.0140 -0.0101 170 THR A CB  
1003 O OG1 . THR A 136 ? 0.4140 0.6270 0.7494 -0.0257 -0.0041 -0.0117 170 THR A OG1 
1004 C CG2 . THR A 136 ? 0.3558 0.5698 0.7397 -0.0418 -0.0427 -0.0211 170 THR A CG2 
1005 N N   . ALA A 137 ? 0.4376 0.6984 0.8541 -0.0166 0.0478  0.0264  171 ALA A N   
1006 C CA  . ALA A 137 ? 0.4303 0.6898 0.8421 -0.0122 0.0716  0.0373  171 ALA A CA  
1007 C C   . ALA A 137 ? 0.5121 0.7995 0.9535 0.0003  0.0923  0.0553  171 ALA A C   
1008 O O   . ALA A 137 ? 0.5337 0.8206 0.9448 0.0178  0.1053  0.0586  171 ALA A O   
1009 C CB  . ALA A 137 ? 0.3335 0.5709 0.6882 -0.0041 0.0764  0.0305  171 ALA A CB  
1010 N N   . PRO A 138 ? 0.4326 0.7439 0.9329 -0.0073 0.0956  0.0681  172 PRO A N   
1011 C CA  . PRO A 138 ? 0.4322 0.7749 0.9649 0.0064  0.1184  0.0881  172 PRO A CA  
1012 C C   . PRO A 138 ? 0.5285 0.8691 1.0559 0.0118  0.1452  0.1035  172 PRO A C   
1013 O O   . PRO A 138 ? 0.5505 0.8790 1.0882 -0.0026 0.1452  0.1062  172 PRO A O   
1014 C CB  . PRO A 138 ? 0.2771 0.6472 0.8808 -0.0074 0.1072  0.0965  172 PRO A CB  
1015 C CG  . PRO A 138 ? 0.3779 0.7246 0.9880 -0.0302 0.0867  0.0865  172 PRO A CG  
1016 C CD  . PRO A 138 ? 0.4716 0.7815 1.0126 -0.0283 0.0768  0.0655  172 PRO A CD  
1017 N N   . ASN A 139 ? 0.5364 0.8788 1.0331 0.0338  0.1638  0.1110  173 ASN A N   
1018 C CA  . ASN A 139 ? 0.5660 0.8977 1.0408 0.0423  0.1855  0.1242  173 ASN A CA  
1019 C C   . ASN A 139 ? 0.6761 0.9809 1.1203 0.0365  0.1868  0.1186  173 ASN A C   
1020 O O   . ASN A 139 ? 0.6997 0.9960 1.1516 0.0286  0.1945  0.1279  173 ASN A O   
1021 C CB  . ASN A 139 ? 0.5670 0.9145 1.0876 0.0331  0.1925  0.1419  173 ASN A CB  
1022 C CG  . ASN A 139 ? 0.7476 1.1035 1.2564 0.0535  0.2153  0.1583  173 ASN A CG  
1023 O OD1 . ASN A 139 ? 0.8483 1.2130 1.3410 0.0723  0.2196  0.1567  173 ASN A OD1 
1024 N ND2 . ASN A 139 ? 0.8289 1.1808 1.3449 0.0511  0.2300  0.1746  173 ASN A ND2 
1025 N N   . PHE A 140 ? 0.5700 0.8618 0.9808 0.0410  0.1792  0.1044  174 PHE A N   
1026 C CA  . PHE A 140 ? 0.4565 0.7193 0.8301 0.0368  0.1772  0.0971  174 PHE A CA  
1027 C C   . PHE A 140 ? 0.4848 0.7348 0.8171 0.0567  0.1958  0.1051  174 PHE A C   
1028 O O   . PHE A 140 ? 0.4374 0.6649 0.7424 0.0544  0.1957  0.1022  174 PHE A O   
1029 C CB  . PHE A 140 ? 0.4638 0.7068 0.8044 0.0303  0.1530  0.0759  174 PHE A CB  
1030 C CG  . PHE A 140 ? 0.4168 0.6548 0.7792 0.0094  0.1355  0.0660  174 PHE A CG  
1031 C CD1 . PHE A 140 ? 0.5178 0.7735 0.9326 -0.0027 0.1309  0.0715  174 PHE A CD1 
1032 C CD2 . PHE A 140 ? 0.3739 0.5887 0.7044 0.0030  0.1229  0.0519  174 PHE A CD2 
1033 C CE1 . PHE A 140 ? 0.4936 0.7381 0.9225 -0.0203 0.1114  0.0608  174 PHE A CE1 
1034 C CE2 . PHE A 140 ? 0.5060 0.7120 0.8491 -0.0124 0.1073  0.0419  174 PHE A CE2 
1035 C CZ  . PHE A 140 ? 0.4244 0.6423 0.8137 -0.0237 0.1001  0.0452  174 PHE A CZ  
1036 N N   . GLY A 141 ? 0.5114 0.7669 0.8287 0.0758  0.2055  0.1123  175 GLY A N   
1037 C CA  . GLY A 141 ? 0.3855 0.6215 0.6557 0.0959  0.2184  0.1183  175 GLY A CA  
1038 C C   . GLY A 141 ? 0.4919 0.7050 0.7149 0.1048  0.2106  0.1067  175 GLY A C   
1039 O O   . GLY A 141 ? 0.4895 0.6959 0.6924 0.1079  0.1930  0.0937  175 GLY A O   
1040 N N   . PRO A 142 ? 0.5269 0.7183 0.7239 0.1054  0.2146  0.1089  176 PRO A N   
1041 C CA  . PRO A 142 ? 0.5742 0.7356 0.7218 0.1091  0.1973  0.0963  176 PRO A CA  
1042 C C   . PRO A 142 ? 0.5096 0.6667 0.6651 0.0878  0.1760  0.0820  176 PRO A C   
1043 O O   . PRO A 142 ? 0.6274 0.7653 0.7499 0.0889  0.1600  0.0727  176 PRO A O   
1044 C CB  . PRO A 142 ? 0.5219 0.6650 0.6460 0.1175  0.2102  0.1061  176 PRO A CB  
1045 C CG  . PRO A 142 ? 0.5258 0.6861 0.6949 0.1045  0.2257  0.1184  176 PRO A CG  
1046 C CD  . PRO A 142 ? 0.4654 0.6518 0.6725 0.1000  0.2270  0.1216  176 PRO A CD  
1047 N N   . LEU A 143 ? 0.4180 0.5910 0.6153 0.0693  0.1747  0.0807  177 LEU A N   
1048 C CA  . LEU A 143 ? 0.3948 0.5617 0.5948 0.0521  0.1570  0.0675  177 LEU A CA  
1049 C C   . LEU A 143 ? 0.3790 0.5466 0.5662 0.0515  0.1389  0.0559  177 LEU A C   
1050 O O   . LEU A 143 ? 0.3563 0.5395 0.5632 0.0517  0.1365  0.0553  177 LEU A O   
1051 C CB  . LEU A 143 ? 0.4641 0.6424 0.7070 0.0350  0.1580  0.0683  177 LEU A CB  
1052 C CG  . LEU A 143 ? 0.4908 0.6620 0.7457 0.0304  0.1702  0.0773  177 LEU A CG  
1053 C CD1 . LEU A 143 ? 0.4716 0.6429 0.7575 0.0119  0.1611  0.0713  177 LEU A CD1 
1054 C CD2 . LEU A 143 ? 0.5187 0.6684 0.7357 0.0373  0.1704  0.0756  177 LEU A CD2 
1055 N N   . ARG A 144 ? 0.4125 0.5639 0.5694 0.0504  0.1258  0.0483  178 ARG A N   
1056 C CA  . ARG A 144 ? 0.4032 0.5523 0.5467 0.0475  0.1077  0.0388  178 ARG A CA  
1057 C C   . ARG A 144 ? 0.3334 0.4816 0.4831 0.0317  0.0984  0.0310  178 ARG A C   
1058 O O   . ARG A 144 ? 0.5219 0.6602 0.6577 0.0293  0.0970  0.0308  178 ARG A O   
1059 C CB  . ARG A 144 ? 0.4129 0.5434 0.5176 0.0589  0.0987  0.0388  178 ARG A CB  
1060 C CG  . ARG A 144 ? 0.3197 0.4447 0.4076 0.0792  0.1069  0.0449  178 ARG A CG  
1061 C CD  . ARG A 144 ? 0.3962 0.5353 0.4969 0.0851  0.1062  0.0434  178 ARG A CD  
1062 N NE  . ARG A 144 ? 0.5719 0.7123 0.6643 0.1065  0.1215  0.0516  178 ARG A NE  
1063 C CZ  . ARG A 144 ? 0.5605 0.7213 0.6829 0.1098  0.1428  0.0620  178 ARG A CZ  
1064 N NH1 . ARG A 144 ? 0.4868 0.6652 0.6501 0.0919  0.1484  0.0646  178 ARG A NH1 
1065 N NH2 . ARG A 144 ? 0.5397 0.7019 0.6502 0.1325  0.1587  0.0710  178 ARG A NH2 
1066 N N   . VAL A 145 ? 0.2727 0.4310 0.4425 0.0226  0.0920  0.0249  179 VAL A N   
1067 C CA  . VAL A 145 ? 0.3286 0.4835 0.4995 0.0107  0.0839  0.0167  179 VAL A CA  
1068 C C   . VAL A 145 ? 0.3654 0.5159 0.5137 0.0093  0.0693  0.0112  179 VAL A C   
1069 O O   . VAL A 145 ? 0.3891 0.5431 0.5351 0.0125  0.0609  0.0098  179 VAL A O   
1070 C CB  . VAL A 145 ? 0.2660 0.4286 0.4674 0.0018  0.0817  0.0127  179 VAL A CB  
1071 C CG1 . VAL A 145 ? 0.2937 0.4464 0.4874 -0.0069 0.0731  0.0028  179 VAL A CG1 
1072 C CG2 . VAL A 145 ? 0.3449 0.5127 0.5733 0.0018  0.0962  0.0216  179 VAL A CG2 
1073 N N   . PHE A 146 ? 0.3953 0.5391 0.5282 0.0052  0.0668  0.0095  180 PHE A N   
1074 C CA  . PHE A 146 ? 0.4120 0.5523 0.5244 0.0032  0.0550  0.0084  180 PHE A CA  
1075 C C   . PHE A 146 ? 0.4301 0.5693 0.5373 -0.0033 0.0544  0.0037  180 PHE A C   
1076 O O   . PHE A 146 ? 0.4047 0.5425 0.5149 -0.0034 0.0636  0.0042  180 PHE A O   
1077 C CB  . PHE A 146 ? 0.4172 0.5510 0.5135 0.0078  0.0533  0.0163  180 PHE A CB  
1078 C CG  . PHE A 146 ? 0.4885 0.6192 0.5688 0.0033  0.0412  0.0187  180 PHE A CG  
1079 C CD1 . PHE A 146 ? 0.4475 0.5744 0.5178 0.0035  0.0280  0.0173  180 PHE A CD1 
1080 C CD2 . PHE A 146 ? 0.4202 0.5529 0.4977 -0.0007 0.0433  0.0242  180 PHE A CD2 
1081 C CE1 . PHE A 146 ? 0.4496 0.5726 0.5063 -0.0018 0.0166  0.0219  180 PHE A CE1 
1082 C CE2 . PHE A 146 ? 0.4551 0.5879 0.5228 -0.0058 0.0336  0.0301  180 PHE A CE2 
1083 C CZ  . PHE A 146 ? 0.4870 0.6139 0.5438 -0.0071 0.0199  0.0293  180 PHE A CZ  
1084 N N   . TYR A 147 ? 0.3505 0.4888 0.4470 -0.0067 0.0438  -0.0007 181 TYR A N   
1085 C CA  . TYR A 147 ? 0.4748 0.6099 0.5580 -0.0095 0.0438  -0.0044 181 TYR A CA  
1086 C C   . TYR A 147 ? 0.5294 0.6665 0.5962 -0.0102 0.0422  0.0048  181 TYR A C   
1087 O O   . TYR A 147 ? 0.5000 0.6353 0.5563 -0.0121 0.0310  0.0071  181 TYR A O   
1088 C CB  . TYR A 147 ? 0.3419 0.4721 0.4203 -0.0120 0.0327  -0.0141 181 TYR A CB  
1089 C CG  . TYR A 147 ? 0.4465 0.5694 0.5018 -0.0115 0.0326  -0.0181 181 TYR A CG  
1090 C CD1 . TYR A 147 ? 0.5074 0.6234 0.5602 -0.0088 0.0406  -0.0238 181 TYR A CD1 
1091 C CD2 . TYR A 147 ? 0.5179 0.6387 0.5508 -0.0121 0.0251  -0.0155 181 TYR A CD2 
1092 C CE1 . TYR A 147 ? 0.5256 0.6329 0.5517 -0.0044 0.0422  -0.0276 181 TYR A CE1 
1093 C CE2 . TYR A 147 ? 0.4640 0.5779 0.4716 -0.0091 0.0277  -0.0175 181 TYR A CE2 
1094 C CZ  . TYR A 147 ? 0.5549 0.6622 0.5580 -0.0041 0.0369  -0.0240 181 TYR A CZ  
1095 O OH  . TYR A 147 ? 0.5046 0.6033 0.4773 0.0028  0.0411  -0.0263 181 TYR A OH  
1096 N N   . PRO A 148 ? 0.4771 0.6183 0.5441 -0.0090 0.0520  0.0116  182 PRO A N   
1097 C CA  . PRO A 148 ? 0.4067 0.5535 0.4665 -0.0114 0.0498  0.0238  182 PRO A CA  
1098 C C   . PRO A 148 ? 0.4735 0.6225 0.5169 -0.0126 0.0507  0.0255  182 PRO A C   
1099 O O   . PRO A 148 ? 0.5266 0.6812 0.5659 -0.0163 0.0475  0.0379  182 PRO A O   
1100 C CB  . PRO A 148 ? 0.4540 0.6071 0.5257 -0.0087 0.0606  0.0309  182 PRO A CB  
1101 C CG  . PRO A 148 ? 0.4473 0.5970 0.5229 -0.0042 0.0713  0.0207  182 PRO A CG  
1102 C CD  . PRO A 148 ? 0.4879 0.6293 0.5649 -0.0056 0.0646  0.0096  182 PRO A CD  
1103 N N   . GLY A 149 ? 0.4596 0.6025 0.4923 -0.0092 0.0539  0.0142  183 GLY A N   
1104 C CA  . GLY A 149 ? 0.4813 0.6230 0.4914 -0.0067 0.0570  0.0153  183 GLY A CA  
1105 C C   . GLY A 149 ? 0.3523 0.4939 0.3565 0.0019  0.0723  0.0118  183 GLY A C   
1106 O O   . GLY A 149 ? 0.4336 0.5776 0.4542 0.0044  0.0800  0.0105  183 GLY A O   
1107 N N   . PRO A 150 ? 0.3636 0.5001 0.3407 0.0085  0.0768  0.0100  184 PRO A N   
1108 C CA  . PRO A 150 ? 0.4430 0.5765 0.4084 0.0206  0.0920  0.0060  184 PRO A CA  
1109 C C   . PRO A 150 ? 0.5385 0.6940 0.5234 0.0232  0.1081  0.0222  184 PRO A C   
1110 O O   . PRO A 150 ? 0.6035 0.7767 0.5970 0.0183  0.1105  0.0399  184 PRO A O   
1111 C CB  . PRO A 150 ? 0.6081 0.7315 0.5345 0.0288  0.0933  0.0039  184 PRO A CB  
1112 C CG  . PRO A 150 ? 0.4752 0.5898 0.3943 0.0197  0.0741  0.0003  184 PRO A CG  
1113 C CD  . PRO A 150 ? 0.4524 0.5818 0.4039 0.0073  0.0678  0.0105  184 PRO A CD  
1114 N N   . GLY A 151 ? 0.4531 0.6066 0.4473 0.0305  0.1173  0.0169  185 GLY A N   
1115 C CA  . GLY A 151 ? 0.4721 0.6461 0.4870 0.0346  0.1316  0.0312  185 GLY A CA  
1116 C C   . GLY A 151 ? 0.5148 0.6811 0.5229 0.0495  0.1446  0.0228  185 GLY A C   
1117 O O   . GLY A 151 ? 0.5020 0.6681 0.4871 0.0635  0.1574  0.0229  185 GLY A O   
1118 N N   . HIS A 152 ? 0.5661 0.7243 0.5917 0.0482  0.1419  0.0159  186 HIS A N   
1119 C CA  . HIS A 152 ? 0.5480 0.6922 0.5653 0.0620  0.1508  0.0057  186 HIS A CA  
1120 C C   . HIS A 152 ? 0.6053 0.7201 0.5879 0.0689  0.1446  -0.0132 186 HIS A C   
1121 O O   . HIS A 152 ? 0.6263 0.7296 0.5838 0.0860  0.1542  -0.0196 186 HIS A O   
1122 C CB  . HIS A 152 ? 0.6054 0.7430 0.6472 0.0572  0.1466  0.0028  186 HIS A CB  
1123 C CG  . HIS A 152 ? 0.6300 0.7459 0.6626 0.0690  0.1511  -0.0096 186 HIS A CG  
1124 N ND1 . HIS A 152 ? 0.7554 0.8770 0.7856 0.0852  0.1661  -0.0059 186 HIS A ND1 
1125 C CD2 . HIS A 152 ? 0.6147 0.7022 0.6413 0.0671  0.1412  -0.0250 186 HIS A CD2 
1126 C CE1 . HIS A 152 ? 0.6473 0.7413 0.6662 0.0937  0.1647  -0.0200 186 HIS A CE1 
1127 N NE2 . HIS A 152 ? 0.7379 0.8103 0.7553 0.0819  0.1489  -0.0313 186 HIS A NE2 
1128 N N   . THR A 153 ? 0.6606 0.7616 0.6408 0.0572  0.1273  -0.0225 187 THR A N   
1129 C CA  . THR A 153 ? 0.6079 0.6823 0.5553 0.0613  0.1162  -0.0385 187 THR A CA  
1130 C C   . THR A 153 ? 0.6492 0.7294 0.5918 0.0505  0.1044  -0.0354 187 THR A C   
1131 O O   . THR A 153 ? 0.6179 0.7217 0.5783 0.0422  0.1070  -0.0204 187 THR A O   
1132 C CB  . THR A 153 ? 0.6646 0.7113 0.6178 0.0579  0.1024  -0.0549 187 THR A CB  
1133 O OG1 . THR A 153 ? 0.6191 0.6741 0.6047 0.0407  0.0914  -0.0519 187 THR A OG1 
1134 C CG2 . THR A 153 ? 0.6883 0.7273 0.6483 0.0675  0.1127  -0.0568 187 THR A CG2 
1135 N N   . SER A 154 ? 0.6365 0.6931 0.5547 0.0510  0.0891  -0.0495 188 SER A N   
1136 C CA  . SER A 154 ? 0.5319 0.5915 0.4474 0.0408  0.0751  -0.0480 188 SER A CA  
1137 C C   . SER A 154 ? 0.5659 0.6238 0.5127 0.0265  0.0585  -0.0533 188 SER A C   
1138 O O   . SER A 154 ? 0.5932 0.6552 0.5430 0.0185  0.0462  -0.0520 188 SER A O   
1139 C CB  . SER A 154 ? 0.5797 0.6153 0.4492 0.0502  0.0662  -0.0587 188 SER A CB  
1140 O OG  . SER A 154 ? 0.7971 0.8408 0.6375 0.0633  0.0841  -0.0484 188 SER A OG  
1141 N N   . ASP A 155 ? 0.4704 0.5235 0.4414 0.0239  0.0590  -0.0577 189 ASP A N   
1142 C CA  . ASP A 155 ? 0.5400 0.5934 0.5435 0.0118  0.0465  -0.0605 189 ASP A CA  
1143 C C   . ASP A 155 ? 0.5119 0.5822 0.5491 0.0071  0.0576  -0.0498 189 ASP A C   
1144 O O   . ASP A 155 ? 0.4266 0.4985 0.4920 -0.0009 0.0518  -0.0500 189 ASP A O   
1145 C CB  . ASP A 155 ? 0.5716 0.5973 0.5733 0.0114  0.0315  -0.0762 189 ASP A CB  
1146 C CG  . ASP A 155 ? 0.5832 0.5926 0.5776 0.0202  0.0404  -0.0811 189 ASP A CG  
1147 O OD1 . ASP A 155 ? 0.6168 0.6255 0.5837 0.0334  0.0542  -0.0795 189 ASP A OD1 
1148 O OD2 . ASP A 155 ? 0.5327 0.5304 0.5505 0.0145  0.0340  -0.0852 189 ASP A OD2 
1149 N N   . ASN A 156 ? 0.4916 0.5748 0.5272 0.0125  0.0734  -0.0395 190 ASN A N   
1150 C CA  . ASN A 156 ? 0.4534 0.5481 0.5155 0.0098  0.0820  -0.0301 190 ASN A CA  
1151 C C   . ASN A 156 ? 0.5486 0.6569 0.6276 0.0019  0.0767  -0.0225 190 ASN A C   
1152 O O   . ASN A 156 ? 0.5110 0.6275 0.5803 0.0001  0.0719  -0.0181 190 ASN A O   
1153 C CB  . ASN A 156 ? 0.5584 0.6646 0.6167 0.0174  0.0967  -0.0201 190 ASN A CB  
1154 C CG  . ASN A 156 ? 0.6113 0.7325 0.6567 0.0181  0.0985  -0.0107 190 ASN A CG  
1155 O OD1 . ASN A 156 ? 0.6020 0.7210 0.6248 0.0255  0.1030  -0.0124 190 ASN A OD1 
1156 N ND2 . ASN A 156 ? 0.6438 0.7785 0.7020 0.0111  0.0947  0.0000  190 ASN A ND2 
1157 N N   . ILE A 157 ? 0.5248 0.6339 0.6273 -0.0017 0.0777  -0.0203 191 ILE A N   
1158 C CA  . ILE A 157 ? 0.4565 0.5767 0.5724 -0.0051 0.0754  -0.0129 191 ILE A CA  
1159 C C   . ILE A 157 ? 0.4623 0.5864 0.5874 -0.0017 0.0861  -0.0031 191 ILE A C   
1160 O O   . ILE A 157 ? 0.4692 0.5875 0.5972 0.0013  0.0942  -0.0027 191 ILE A O   
1161 C CB  . ILE A 157 ? 0.4235 0.5431 0.5591 -0.0104 0.0676  -0.0172 191 ILE A CB  
1162 C CG1 . ILE A 157 ? 0.4153 0.5292 0.5733 -0.0122 0.0739  -0.0165 191 ILE A CG1 
1163 C CG2 . ILE A 157 ? 0.5046 0.6163 0.6303 -0.0134 0.0535  -0.0281 191 ILE A CG2 
1164 C CD1 . ILE A 157 ? 0.3885 0.5060 0.5749 -0.0187 0.0672  -0.0170 191 ILE A CD1 
1165 N N   . THR A 158 ? 0.4714 0.6130 0.5310 0.1295  0.0162  0.0446  192 THR A N   
1166 C CA  . THR A 158 ? 0.3896 0.5251 0.4657 0.1151  0.0228  0.0289  192 THR A CA  
1167 C C   . THR A 158 ? 0.3948 0.5330 0.4907 0.1152  0.0218  0.0252  192 THR A C   
1168 O O   . THR A 158 ? 0.4554 0.5959 0.5604 0.1283  0.0228  0.0374  192 THR A O   
1169 C CB  . THR A 158 ? 0.5570 0.6708 0.6372 0.1082  0.0427  0.0307  192 THR A CB  
1170 O OG1 . THR A 158 ? 0.4904 0.5849 0.5769 0.1173  0.0553  0.0444  192 THR A OG1 
1171 C CG2 . THR A 158 ? 0.3795 0.4956 0.4440 0.1080  0.0471  0.0356  192 THR A CG2 
1172 N N   . VAL A 159 ? 0.3635 0.5031 0.4667 0.1012  0.0204  0.0094  193 VAL A N   
1173 C CA  . VAL A 159 ? 0.4424 0.5860 0.5610 0.0990  0.0220  0.0037  193 VAL A CA  
1174 C C   . VAL A 159 ? 0.4164 0.5399 0.5368 0.0848  0.0356  -0.0090 193 VAL A C   
1175 O O   . VAL A 159 ? 0.4629 0.5839 0.5758 0.0709  0.0319  -0.0179 193 VAL A O   
1176 C CB  . VAL A 159 ? 0.4695 0.6369 0.5889 0.0933  0.0035  -0.0027 193 VAL A CB  
1177 C CG1 . VAL A 159 ? 0.3582 0.5345 0.4959 0.0926  0.0083  -0.0051 193 VAL A CG1 
1178 C CG2 . VAL A 159 ? 0.4522 0.6365 0.5632 0.1027  -0.0133 0.0066  193 VAL A CG2 
1179 N N   . GLY A 160 ? 0.4329 0.5420 0.5632 0.0887  0.0509  -0.0099 194 GLY A N   
1180 C CA  . GLY A 160 ? 0.3580 0.4467 0.4845 0.0736  0.0626  -0.0250 194 GLY A CA  
1181 C C   . GLY A 160 ? 0.4493 0.5487 0.5816 0.0721  0.0647  -0.0329 194 GLY A C   
1182 O O   . GLY A 160 ? 0.5435 0.6629 0.6913 0.0863  0.0626  -0.0240 194 GLY A O   
1183 N N   . ILE A 161 ? 0.4203 0.5091 0.5405 0.0542  0.0684  -0.0484 195 ILE A N   
1184 C CA  . ILE A 161 ? 0.3855 0.4841 0.5059 0.0498  0.0725  -0.0563 195 ILE A CA  
1185 C C   . ILE A 161 ? 0.4286 0.4953 0.5404 0.0467  0.0964  -0.0688 195 ILE A C   
1186 O O   . ILE A 161 ? 0.5691 0.6115 0.6602 0.0288  0.0988  -0.0811 195 ILE A O   
1187 C CB  . ILE A 161 ? 0.4836 0.5960 0.5896 0.0305  0.0553  -0.0633 195 ILE A CB  
1188 C CG1 . ILE A 161 ? 0.4953 0.6291 0.6060 0.0337  0.0331  -0.0537 195 ILE A CG1 
1189 C CG2 . ILE A 161 ? 0.4477 0.5735 0.5541 0.0261  0.0603  -0.0676 195 ILE A CG2 
1190 C CD1 . ILE A 161 ? 0.5002 0.6411 0.5981 0.0171  0.0157  -0.0588 195 ILE A CD1 
1191 N N   . ASP A 162 ? 0.5129 0.5796 0.6410 0.0640  0.1140  -0.0659 196 ASP A N   
1192 C CA  . ASP A 162 ? 0.5434 0.5758 0.6620 0.0642  0.1404  -0.0798 196 ASP A CA  
1193 C C   . ASP A 162 ? 0.6084 0.6377 0.7005 0.0423  0.1433  -0.0978 196 ASP A C   
1194 O O   . ASP A 162 ? 0.6332 0.6938 0.7257 0.0352  0.1313  -0.0956 196 ASP A O   
1195 C CB  . ASP A 162 ? 0.5357 0.5751 0.6834 0.0911  0.1593  -0.0714 196 ASP A CB  
1196 C CG  . ASP A 162 ? 0.6904 0.6932 0.8459 0.1084  0.1756  -0.0659 196 ASP A CG  
1197 O OD1 . ASP A 162 ? 0.8769 0.8706 1.0509 0.1293  0.1977  -0.0645 196 ASP A OD1 
1198 O OD2 . ASP A 162 ? 0.8266 0.8094 0.9715 0.1017  0.1673  -0.0619 196 ASP A OD2 
1199 N N   . GLY A 163 ? 0.7106 0.6990 0.7761 0.0300  0.1587  -0.1156 197 GLY A N   
1200 C CA  . GLY A 163 ? 0.6819 0.6619 0.7132 0.0071  0.1610  -0.1334 197 GLY A CA  
1201 C C   . GLY A 163 ? 0.7078 0.6938 0.7176 -0.0187 0.1344  -0.1356 197 GLY A C   
1202 O O   . GLY A 163 ? 0.6772 0.6567 0.6550 -0.0396 0.1323  -0.1483 197 GLY A O   
1203 N N   . THR A 164 ? 0.6792 0.6786 0.7055 -0.0171 0.1146  -0.1229 198 THR A N   
1204 C CA  . THR A 164 ? 0.6147 0.6228 0.6289 -0.0377 0.0902  -0.1230 198 THR A CA  
1205 C C   . THR A 164 ? 0.6349 0.6256 0.6557 -0.0415 0.0879  -0.1214 198 THR A C   
1206 O O   . THR A 164 ? 0.6445 0.6154 0.6775 -0.0279 0.1036  -0.1180 198 THR A O   
1207 C CB  . THR A 164 ? 0.5833 0.6304 0.6134 -0.0326 0.0680  -0.1084 198 THR A CB  
1208 O OG1 . THR A 164 ? 0.4884 0.5462 0.5442 -0.0148 0.0640  -0.0947 198 THR A OG1 
1209 C CG2 . THR A 164 ? 0.4647 0.5314 0.4973 -0.0266 0.0724  -0.1060 198 THR A CG2 
1210 N N   . ASP A 165 ? 0.6628 0.6624 0.6776 -0.0604 0.0679  -0.1219 199 ASP A N   
1211 C CA  . ASP A 165 ? 0.6296 0.6225 0.6556 -0.0673 0.0633  -0.1183 199 ASP A CA  
1212 C C   . ASP A 165 ? 0.5719 0.5950 0.6248 -0.0525 0.0516  -0.1006 199 ASP A C   
1213 O O   . ASP A 165 ? 0.5876 0.6157 0.6525 -0.0591 0.0456  -0.0956 199 ASP A O   
1214 C CB  . ASP A 165 ? 0.6309 0.6213 0.6399 -0.0967 0.0481  -0.1283 199 ASP A CB  
1215 C CG  . ASP A 165 ? 0.8205 0.7956 0.8390 -0.1099 0.0495  -0.1291 199 ASP A CG  
1216 O OD1 . ASP A 165 ? 0.9256 0.8679 0.9444 -0.1050 0.0698  -0.1322 199 ASP A OD1 
1217 O OD2 . ASP A 165 ? 0.8350 0.8316 0.8633 -0.1252 0.0304  -0.1255 199 ASP A OD2 
1218 N N   . ILE A 166 ? 0.5435 0.5868 0.6055 -0.0334 0.0492  -0.0916 200 ILE A N   
1219 C CA  . ILE A 166 ? 0.4507 0.5221 0.5286 -0.0221 0.0349  -0.0786 200 ILE A CA  
1220 C C   . ILE A 166 ? 0.3898 0.4600 0.4810 -0.0001 0.0454  -0.0666 200 ILE A C   
1221 O O   . ILE A 166 ? 0.3841 0.4470 0.4773 0.0125  0.0571  -0.0650 200 ILE A O   
1222 C CB  . ILE A 166 ? 0.4335 0.5270 0.5076 -0.0209 0.0198  -0.0775 200 ILE A CB  
1223 C CG1 . ILE A 166 ? 0.5173 0.6105 0.5747 -0.0427 0.0081  -0.0862 200 ILE A CG1 
1224 C CG2 . ILE A 166 ? 0.4251 0.5405 0.5116 -0.0090 0.0060  -0.0670 200 ILE A CG2 
1225 C CD1 . ILE A 166 ? 0.4277 0.5360 0.4777 -0.0442 -0.0045 -0.0841 200 ILE A CD1 
1226 N N   . ALA A 167 ? 0.3409 0.4200 0.4416 0.0049  0.0415  -0.0572 201 ALA A N   
1227 C CA  . ALA A 167 ? 0.4224 0.5052 0.5299 0.0252  0.0465  -0.0433 201 ALA A CA  
1228 C C   . ALA A 167 ? 0.4273 0.5344 0.5367 0.0303  0.0323  -0.0376 201 ALA A C   
1229 O O   . ALA A 167 ? 0.4603 0.5746 0.5740 0.0203  0.0276  -0.0398 201 ALA A O   
1230 C CB  . ALA A 167 ? 0.3632 0.4220 0.4741 0.0265  0.0635  -0.0368 201 ALA A CB  
1231 N N   . PHE A 168 ? 0.4372 0.5571 0.5442 0.0457  0.0255  -0.0308 202 PHE A N   
1232 C CA  . PHE A 168 ? 0.4355 0.5729 0.5383 0.0513  0.0125  -0.0287 202 PHE A CA  
1233 C C   . PHE A 168 ? 0.4929 0.6295 0.5912 0.0639  0.0202  -0.0171 202 PHE A C   
1234 O O   . PHE A 168 ? 0.4892 0.6225 0.5827 0.0763  0.0236  -0.0074 202 PHE A O   
1235 C CB  . PHE A 168 ? 0.4145 0.5641 0.5128 0.0564  -0.0019 -0.0300 202 PHE A CB  
1236 C CG  . PHE A 168 ? 0.3431 0.5031 0.4331 0.0604  -0.0159 -0.0314 202 PHE A CG  
1237 C CD1 . PHE A 168 ? 0.4062 0.5688 0.4982 0.0523  -0.0234 -0.0384 202 PHE A CD1 
1238 C CD2 . PHE A 168 ? 0.3321 0.4975 0.4111 0.0727  -0.0222 -0.0260 202 PHE A CD2 
1239 C CE1 . PHE A 168 ? 0.4351 0.6021 0.5198 0.0585  -0.0340 -0.0408 202 PHE A CE1 
1240 C CE2 . PHE A 168 ? 0.4264 0.5949 0.4928 0.0761  -0.0337 -0.0303 202 PHE A CE2 
1241 C CZ  . PHE A 168 ? 0.3748 0.5423 0.4446 0.0700  -0.0382 -0.0383 202 PHE A CZ  
1242 N N   . GLY A 169 ? 0.3692 0.5108 0.4695 0.0610  0.0233  -0.0168 203 GLY A N   
1243 C CA  . GLY A 169 ? 0.3708 0.5126 0.4633 0.0713  0.0332  -0.0058 203 GLY A CA  
1244 C C   . GLY A 169 ? 0.4864 0.6396 0.5616 0.0837  0.0242  -0.0057 203 GLY A C   
1245 O O   . GLY A 169 ? 0.5711 0.7232 0.6311 0.0937  0.0322  0.0039  203 GLY A O   
1246 N N   . GLY A 170 ? 0.4898 0.6505 0.5630 0.0825  0.0081  -0.0162 204 GLY A N   
1247 C CA  . GLY A 170 ? 0.4324 0.5974 0.4858 0.0927  -0.0008 -0.0193 204 GLY A CA  
1248 C C   . GLY A 170 ? 0.4587 0.6290 0.5116 0.0972  0.0095  -0.0207 204 GLY A C   
1249 O O   . GLY A 170 ? 0.4663 0.6441 0.5414 0.0902  0.0133  -0.0242 204 GLY A O   
1250 N N   . CYS A 171 ? 0.5068 0.6752 0.5339 0.1092  0.0144  -0.0176 205 CYS A N   
1251 C CA  . CYS A 171 ? 0.5700 0.7443 0.5936 0.1163  0.0291  -0.0185 205 CYS A CA  
1252 C C   . CYS A 171 ? 0.5510 0.7279 0.5783 0.1157  0.0513  -0.0041 205 CYS A C   
1253 O O   . CYS A 171 ? 0.6381 0.8244 0.6680 0.1199  0.0677  -0.0027 205 CYS A O   
1254 C CB  . CYS A 171 ? 0.6002 0.7674 0.5865 0.1289  0.0243  -0.0255 205 CYS A CB  
1255 S SG  . CYS A 171 ? 0.6334 0.7911 0.6114 0.1273  -0.0023 -0.0418 205 CYS A SG  
1256 N N   . LEU A 172 ? 0.5397 0.7076 0.5687 0.1109  0.0536  0.0073  206 LEU A N   
1257 C CA  . LEU A 172 ? 0.5763 0.7408 0.6094 0.1081  0.0746  0.0225  206 LEU A CA  
1258 C C   . LEU A 172 ? 0.5544 0.7290 0.6246 0.0940  0.0850  0.0207  206 LEU A C   
1259 O O   . LEU A 172 ? 0.4832 0.6651 0.5612 0.0915  0.1043  0.0295  206 LEU A O   
1260 C CB  . LEU A 172 ? 0.4514 0.5988 0.4795 0.1080  0.0737  0.0350  206 LEU A CB  
1261 C CG  . LEU A 172 ? 0.5007 0.6359 0.5313 0.1045  0.0946  0.0530  206 LEU A CG  
1262 C CD1 . LEU A 172 ? 0.4986 0.6320 0.4940 0.1168  0.1038  0.0676  206 LEU A CD1 
1263 C CD2 . LEU A 172 ? 0.4519 0.5663 0.4924 0.1018  0.0934  0.0602  206 LEU A CD2 
1264 N N   . ILE A 173 ? 0.4742 0.6510 0.5668 0.0832  0.0720  0.0101  207 ILE A N   
1265 C CA  . ILE A 173 ? 0.3931 0.5794 0.5195 0.0664  0.0765  0.0083  207 ILE A CA  
1266 C C   . ILE A 173 ? 0.5116 0.7209 0.6561 0.0676  0.0678  -0.0017 207 ILE A C   
1267 O O   . ILE A 173 ? 0.4624 0.6705 0.5982 0.0735  0.0508  -0.0115 207 ILE A O   
1268 C CB  . ILE A 173 ? 0.3868 0.5569 0.5213 0.0521  0.0684  0.0039  207 ILE A CB  
1269 C CG1 . ILE A 173 ? 0.5253 0.6700 0.6449 0.0551  0.0783  0.0146  207 ILE A CG1 
1270 C CG2 . ILE A 173 ? 0.3922 0.5710 0.5567 0.0315  0.0698  0.0007  207 ILE A CG2 
1271 C CD1 . ILE A 173 ? 0.3835 0.5197 0.5117 0.0469  0.0988  0.0275  207 ILE A CD1 
1272 N N   . LYS A 174 ? 0.4305 0.6611 0.6028 0.0621  0.0795  0.0023  208 LYS A N   
1273 C CA  . LYS A 174 ? 0.3622 0.6185 0.5621 0.0634  0.0719  -0.0042 208 LYS A CA  
1274 C C   . LYS A 174 ? 0.3741 0.6433 0.6094 0.0410  0.0647  -0.0038 208 LYS A C   
1275 O O   . LYS A 174 ? 0.3381 0.5978 0.5784 0.0244  0.0723  0.0015  208 LYS A O   
1276 C CB  . LYS A 174 ? 0.3341 0.6125 0.5435 0.0771  0.0913  0.0003  208 LYS A CB  
1277 C CG  . LYS A 174 ? 0.4436 0.7112 0.6169 0.1001  0.0930  -0.0061 208 LYS A CG  
1278 C CD  . LYS A 174 ? 0.4490 0.6924 0.5789 0.1047  0.1002  -0.0002 208 LYS A CD  
1279 C CE  . LYS A 174 ? 0.4698 0.7013 0.5590 0.1240  0.0981  -0.0085 208 LYS A CE  
1280 N NZ  . LYS A 174 ? 0.7065 0.9331 0.7967 0.1289  0.0766  -0.0234 208 LYS A NZ  
1281 N N   . ASP A 175 ? 0.4519 0.7404 0.7099 0.0401  0.0487  -0.0094 209 ASP A N   
1282 C CA  . ASP A 175 ? 0.3992 0.7014 0.6865 0.0174  0.0364  -0.0094 209 ASP A CA  
1283 C C   . ASP A 175 ? 0.3302 0.6581 0.6538 0.0046  0.0521  0.0004  209 ASP A C   
1284 O O   . ASP A 175 ? 0.3866 0.7288 0.7186 0.0163  0.0730  0.0079  209 ASP A O   
1285 C CB  . ASP A 175 ? 0.3466 0.6667 0.6509 0.0213  0.0146  -0.0137 209 ASP A CB  
1286 C CG  . ASP A 175 ? 0.4075 0.7614 0.7452 0.0380  0.0220  -0.0088 209 ASP A CG  
1287 O OD1 . ASP A 175 ? 0.4476 0.7964 0.7701 0.0594  0.0379  -0.0096 209 ASP A OD1 
1288 O OD2 . ASP A 175 ? 0.4263 0.8124 0.8052 0.0301  0.0120  -0.0041 209 ASP A OD2 
1289 N N   . SER A 176 ? 0.3823 0.7155 0.7257 -0.0218 0.0420  0.0002  210 SER A N   
1290 C CA  . SER A 176 ? 0.3957 0.7506 0.7744 -0.0408 0.0547  0.0095  210 SER A CA  
1291 C C   . SER A 176 ? 0.3475 0.7540 0.7749 -0.0327 0.0594  0.0178  210 SER A C   
1292 O O   . SER A 176 ? 0.3302 0.7605 0.7896 -0.0436 0.0765  0.0282  210 SER A O   
1293 C CB  . SER A 176 ? 0.3758 0.7231 0.7617 -0.0733 0.0385  0.0046  210 SER A CB  
1294 O OG  . SER A 176 ? 0.3164 0.6831 0.7146 -0.0776 0.0113  -0.0006 210 SER A OG  
1295 N N   . LYS A 177 ? 0.3687 0.7928 0.8048 -0.0135 0.0460  0.0144  211 LYS A N   
1296 C CA  . LYS A 177 ? 0.3647 0.8381 0.8508 -0.0009 0.0510  0.0220  211 LYS A CA  
1297 C C   . LYS A 177 ? 0.3577 0.8294 0.8294 0.0327  0.0718  0.0209  211 LYS A C   
1298 O O   . LYS A 177 ? 0.3426 0.8497 0.8510 0.0502  0.0773  0.0244  211 LYS A O   
1299 C CB  . LYS A 177 ? 0.2709 0.7667 0.7832 -0.0026 0.0205  0.0207  211 LYS A CB  
1300 C CG  . LYS A 177 ? 0.4103 0.9458 0.9728 -0.0311 0.0067  0.0289  211 LYS A CG  
1301 C CD  . LYS A 177 ? 0.5890 1.0947 1.1226 -0.0623 -0.0147 0.0214  211 LYS A CD  
1302 C CE  . LYS A 177 ? 0.8585 1.3892 1.4282 -0.0973 -0.0175 0.0273  211 LYS A CE  
1303 N NZ  . LYS A 177 ? 0.8903 1.3773 1.4194 -0.1269 -0.0277 0.0165  211 LYS A NZ  
1304 N N   . ALA A 178 ? 0.2977 0.7291 0.7167 0.0423  0.0833  0.0160  212 ALA A N   
1305 C CA  . ALA A 178 ? 0.3111 0.7359 0.7067 0.0714  0.1016  0.0129  212 ALA A CA  
1306 C C   . ALA A 178 ? 0.3799 0.8365 0.8022 0.0762  0.1336  0.0236  212 ALA A C   
1307 O O   . ALA A 178 ? 0.3367 0.7975 0.7673 0.0569  0.1475  0.0339  212 ALA A O   
1308 C CB  . ALA A 178 ? 0.3202 0.6980 0.6536 0.0766  0.1030  0.0071  212 ALA A CB  
1309 N N   . LYS A 179 ? 0.4958 0.7170 0.8947 0.2211  -0.0026 -0.1252 213 LYS A N   
1310 C CA  . LYS A 179 ? 0.3967 0.6677 0.8353 0.2292  0.0155  -0.1443 213 LYS A CA  
1311 C C   . LYS A 179 ? 0.4808 0.7486 0.8990 0.2124  0.0409  -0.1515 213 LYS A C   
1312 O O   . LYS A 179 ? 0.5271 0.8355 0.9694 0.2158  0.0603  -0.1668 213 LYS A O   
1313 C CB  . LYS A 179 ? 0.5227 0.7898 0.9797 0.2613  0.0084  -0.1549 213 LYS A CB  
1314 C CG  . LYS A 179 ? 0.5359 0.8398 1.0256 0.2710  -0.0073 -0.1493 213 LYS A CG  
1315 C CD  . LYS A 179 ? 0.7821 1.0490 1.2674 0.2995  -0.0353 -0.1421 213 LYS A CD  
1316 C CE  . LYS A 179 ? 0.8029 1.1005 1.3080 0.3025  -0.0598 -0.1310 213 LYS A CE  
1317 N NZ  . LYS A 179 ? 0.9282 1.1816 1.4150 0.3258  -0.0916 -0.1165 213 LYS A NZ  
1318 N N   . SER A 180 ? 0.4647 0.6891 0.8387 0.1933  0.0410  -0.1405 214 SER A N   
1319 C CA  . SER A 180 ? 0.4627 0.6825 0.8123 0.1768  0.0599  -0.1456 214 SER A CA  
1320 C C   . SER A 180 ? 0.4670 0.6537 0.7814 0.1523  0.0541  -0.1278 214 SER A C   
1321 O O   . SER A 180 ? 0.4569 0.6236 0.7649 0.1491  0.0391  -0.1142 214 SER A O   
1322 C CB  . SER A 180 ? 0.4706 0.6642 0.8063 0.1948  0.0659  -0.1658 214 SER A CB  
1323 O OG  . SER A 180 ? 0.6526 0.8209 0.9481 0.1761  0.0741  -0.1671 214 SER A OG  
1324 N N   . LEU A 181 ? 0.5078 0.6924 0.7994 0.1350  0.0664  -0.1285 215 LEU A N   
1325 C CA  . LEU A 181 ? 0.4339 0.5930 0.6980 0.1131  0.0612  -0.1139 215 LEU A CA  
1326 C C   . LEU A 181 ? 0.5042 0.6144 0.7353 0.1130  0.0550  -0.1195 215 LEU A C   
1327 O O   . LEU A 181 ? 0.6125 0.7083 0.8220 0.0938  0.0531  -0.1121 215 LEU A O   
1328 C CB  . LEU A 181 ? 0.4478 0.6347 0.7084 0.0931  0.0735  -0.1075 215 LEU A CB  
1329 C CG  . LEU A 181 ? 0.4234 0.6413 0.7116 0.0822  0.0747  -0.0936 215 LEU A CG  
1330 C CD1 . LEU A 181 ? 0.3941 0.6346 0.6777 0.0644  0.0869  -0.0851 215 LEU A CD1 
1331 C CD2 . LEU A 181 ? 0.2994 0.4966 0.5861 0.0748  0.0610  -0.0808 215 LEU A CD2 
1332 N N   . GLY A 182 ? 0.5425 0.6269 0.7730 0.1340  0.0506  -0.1328 216 GLY A N   
1333 C CA  . GLY A 182 ? 0.5806 0.6104 0.7825 0.1325  0.0428  -0.1378 216 GLY A CA  
1334 C C   . GLY A 182 ? 0.6206 0.6468 0.7979 0.1217  0.0523  -0.1539 216 GLY A C   
1335 O O   . GLY A 182 ? 0.6073 0.6664 0.7878 0.1271  0.0671  -0.1689 216 GLY A O   
1336 N N   . ASN A 183 ? 0.7039 0.6921 0.8552 0.1046  0.0439  -0.1510 217 ASN A N   
1337 C CA  . ASN A 183 ? 0.6644 0.6450 0.7875 0.0919  0.0479  -0.1673 217 ASN A CA  
1338 C C   . ASN A 183 ? 0.6630 0.6906 0.7818 0.0741  0.0553  -0.1574 217 ASN A C   
1339 O O   . ASN A 183 ? 0.7329 0.7686 0.8556 0.0566  0.0484  -0.1364 217 ASN A O   
1340 C CB  . ASN A 183 ? 0.8608 0.7915 0.9638 0.0751  0.0341  -0.1651 217 ASN A CB  
1341 C CG  . ASN A 183 ? 1.0194 0.9404 1.0923 0.0611  0.0342  -0.1855 217 ASN A CG  
1342 O OD1 . ASN A 183 ? 0.8305 0.7651 0.8912 0.0713  0.0451  -0.2086 217 ASN A OD1 
1343 N ND2 . ASN A 183 ? 0.9986 0.8997 1.0594 0.0365  0.0223  -0.1783 217 ASN A ND2 
1344 N N   . LEU A 184 ? 0.5552 0.6135 0.6662 0.0789  0.0701  -0.1720 218 LEU A N   
1345 C CA  . LEU A 184 ? 0.5722 0.6721 0.6746 0.0624  0.0774  -0.1599 218 LEU A CA  
1346 C C   . LEU A 184 ? 0.6064 0.7017 0.6661 0.0477  0.0765  -0.1722 218 LEU A C   
1347 O O   . LEU A 184 ? 0.5832 0.7122 0.6265 0.0365  0.0840  -0.1651 218 LEU A O   
1348 C CB  . LEU A 184 ? 0.5627 0.7078 0.6853 0.0734  0.0965  -0.1620 218 LEU A CB  
1349 C CG  . LEU A 184 ? 0.4500 0.6163 0.6153 0.0793  0.0960  -0.1445 218 LEU A CG  
1350 C CD1 . LEU A 184 ? 0.4392 0.6539 0.6263 0.0862  0.1158  -0.1496 218 LEU A CD1 
1351 C CD2 . LEU A 184 ? 0.4441 0.6133 0.6145 0.0599  0.0857  -0.1172 218 LEU A CD2 
1352 N N   . GLY A 185 ? 0.7017 0.7544 0.7414 0.0459  0.0660  -0.1899 219 GLY A N   
1353 C CA  . GLY A 185 ? 0.6284 0.6765 0.6252 0.0324  0.0634  -0.2078 219 GLY A CA  
1354 C C   . GLY A 185 ? 0.6906 0.7576 0.6737 0.0071  0.0501  -0.1854 219 GLY A C   
1355 O O   . GLY A 185 ? 0.6876 0.7782 0.6367 -0.0034 0.0523  -0.1885 219 GLY A O   
1356 N N   . ASP A 186 ? 0.6318 0.6905 0.6405 -0.0020 0.0361  -0.1625 220 ASP A N   
1357 C CA  . ASP A 186 ? 0.6078 0.6853 0.6146 -0.0225 0.0213  -0.1413 220 ASP A CA  
1358 C C   . ASP A 186 ? 0.5869 0.6961 0.6242 -0.0211 0.0250  -0.1112 220 ASP A C   
1359 O O   . ASP A 186 ? 0.6000 0.7182 0.6547 -0.0321 0.0122  -0.0914 220 ASP A O   
1360 C CB  . ASP A 186 ? 0.5818 0.6311 0.5990 -0.0360 0.0036  -0.1404 220 ASP A CB  
1361 C CG  . ASP A 186 ? 0.7125 0.7277 0.6990 -0.0434 -0.0039 -0.1699 220 ASP A CG  
1362 O OD1 . ASP A 186 ? 0.7889 0.8138 0.7379 -0.0462 -0.0026 -0.1876 220 ASP A OD1 
1363 O OD2 . ASP A 186 ? 0.6352 0.6124 0.6331 -0.0479 -0.0107 -0.1756 220 ASP A OD2 
1364 N N   . ALA A 187 ? 0.5019 0.6291 0.5494 -0.0078 0.0423  -0.1095 221 ALA A N   
1365 C CA  . ALA A 187 ? 0.4811 0.6304 0.5629 -0.0058 0.0462  -0.0853 221 ALA A CA  
1366 C C   . ALA A 187 ? 0.5107 0.6903 0.5811 -0.0165 0.0478  -0.0658 221 ALA A C   
1367 O O   . ALA A 187 ? 0.5174 0.7085 0.5501 -0.0220 0.0528  -0.0723 221 ALA A O   
1368 C CB  . ALA A 187 ? 0.5535 0.7076 0.6590 0.0120  0.0615  -0.0926 221 ALA A CB  
1369 N N   . ASP A 188 ? 0.4750 0.6653 0.5767 -0.0195 0.0435  -0.0416 222 ASP A N   
1370 C CA  . ASP A 188 ? 0.4274 0.6400 0.5269 -0.0283 0.0447  -0.0175 222 ASP A CA  
1371 C C   . ASP A 188 ? 0.5178 0.7450 0.6440 -0.0219 0.0628  -0.0135 222 ASP A C   
1372 O O   . ASP A 188 ? 0.5103 0.7345 0.6758 -0.0176 0.0611  -0.0064 222 ASP A O   
1373 C CB  . ASP A 188 ? 0.5199 0.7311 0.6415 -0.0349 0.0257  0.0051  222 ASP A CB  
1374 C CG  . ASP A 188 ? 0.5519 0.7781 0.6647 -0.0441 0.0213  0.0331  222 ASP A CG  
1375 O OD1 . ASP A 188 ? 0.5442 0.7809 0.6598 -0.0453 0.0366  0.0427  222 ASP A OD1 
1376 O OD2 . ASP A 188 ? 0.6549 0.8826 0.7597 -0.0510 0.0013  0.0470  222 ASP A OD2 
1377 N N   . THR A 189 ? 0.5191 0.7651 0.6245 -0.0225 0.0809  -0.0201 223 THR A N   
1378 C CA  . THR A 189 ? 0.4346 0.7009 0.5695 -0.0178 0.0994  -0.0202 223 THR A CA  
1379 C C   . THR A 189 ? 0.5459 0.8206 0.7073 -0.0290 0.0982  0.0090  223 THR A C   
1380 O O   . THR A 189 ? 0.5859 0.8722 0.7843 -0.0266 0.1077  0.0092  223 THR A O   
1381 C CB  . THR A 189 ? 0.5185 0.8102 0.6270 -0.0177 0.1218  -0.0344 223 THR A CB  
1382 O OG1 . THR A 189 ? 0.6394 0.9443 0.7100 -0.0353 0.1245  -0.0144 223 THR A OG1 
1383 C CG2 . THR A 189 ? 0.4753 0.7528 0.5581 -0.0050 0.1223  -0.0668 223 THR A CG2 
1384 N N   . GLU A 190 ? 0.4746 0.7424 0.6201 -0.0408 0.0849  0.0333  224 GLU A N   
1385 C CA  . GLU A 190 ? 0.4953 0.7628 0.6665 -0.0504 0.0820  0.0623  224 GLU A CA  
1386 C C   . GLU A 190 ? 0.5549 0.8032 0.7700 -0.0431 0.0670  0.0645  224 GLU A C   
1387 O O   . GLU A 190 ? 0.5216 0.7696 0.7749 -0.0436 0.0715  0.0690  224 GLU A O   
1388 C CB  . GLU A 190 ? 0.6151 0.8821 0.7502 -0.0641 0.0723  0.0905  224 GLU A CB  
1389 C CG  . GLU A 190 ? 0.8312 1.0915 0.9907 -0.0743 0.0689  0.1243  224 GLU A CG  
1390 C CD  . GLU A 190 ? 1.0315 1.2736 1.1894 -0.0751 0.0420  0.1490  224 GLU A CD  
1391 O OE1 . GLU A 190 ? 1.0602 1.2852 1.2623 -0.0715 0.0320  0.1617  224 GLU A OE1 
1392 O OE2 . GLU A 190 ? 1.1640 1.4102 1.2783 -0.0785 0.0298  0.1538  224 GLU A OE2 
1393 N N   . ARG A 191 ? 0.5009 0.7355 0.7118 -0.0377 0.0501  0.0593  225 ARG A N   
1394 C CA  . ARG A 191 ? 0.4394 0.6608 0.6893 -0.0317 0.0379  0.0611  225 ARG A CA  
1395 C C   . ARG A 191 ? 0.4171 0.6339 0.6868 -0.0209 0.0431  0.0372  225 ARG A C   
1396 O O   . ARG A 191 ? 0.4926 0.7016 0.7922 -0.0163 0.0368  0.0357  225 ARG A O   
1397 C CB  . ARG A 191 ? 0.4379 0.6538 0.6799 -0.0326 0.0179  0.0681  225 ARG A CB  
1398 C CG  . ARG A 191 ? 0.4232 0.6435 0.6415 -0.0420 0.0066  0.0943  225 ARG A CG  
1399 C CD  . ARG A 191 ? 0.6592 0.8777 0.8936 -0.0397 -0.0171 0.1045  225 ARG A CD  
1400 N NE  . ARG A 191 ? 0.7752 0.9954 0.9975 -0.0456 -0.0326 0.1357  225 ARG A NE  
1401 C CZ  . ARG A 191 ? 0.8505 1.0800 1.0374 -0.0518 -0.0500 0.1442  225 ARG A CZ  
1402 N NH1 . ARG A 191 ? 0.7308 0.9675 0.8926 -0.0545 -0.0534 0.1214  225 ARG A NH1 
1403 N NH2 . ARG A 191 ? 0.7856 1.0150 0.9609 -0.0562 -0.0662 0.1769  225 ARG A NH2 
1404 N N   . TYR A 192 ? 0.4038 0.6253 0.6569 -0.0158 0.0541  0.0187  226 TYR A N   
1405 C CA  . TYR A 192 ? 0.3968 0.6111 0.6640 -0.0047 0.0556  -0.0001 226 TYR A CA  
1406 C C   . TYR A 192 ? 0.3956 0.6144 0.7007 -0.0022 0.0580  0.0008  226 TYR A C   
1407 O O   . TYR A 192 ? 0.3523 0.5620 0.6720 0.0033  0.0525  -0.0063 226 TYR A O   
1408 C CB  . TYR A 192 ? 0.4439 0.6625 0.6920 0.0033  0.0658  -0.0183 226 TYR A CB  
1409 C CG  . TYR A 192 ? 0.3928 0.5930 0.6388 0.0148  0.0613  -0.0348 226 TYR A CG  
1410 C CD1 . TYR A 192 ? 0.3541 0.5478 0.6230 0.0196  0.0562  -0.0353 226 TYR A CD1 
1411 C CD2 . TYR A 192 ? 0.4815 0.6682 0.7000 0.0202  0.0620  -0.0496 226 TYR A CD2 
1412 C CE1 . TYR A 192 ? 0.3819 0.5567 0.6434 0.0283  0.0517  -0.0454 226 TYR A CE1 
1413 C CE2 . TYR A 192 ? 0.4068 0.5698 0.6229 0.0298  0.0566  -0.0607 226 TYR A CE2 
1414 C CZ  . TYR A 192 ? 0.3283 0.4857 0.5646 0.0333  0.0514  -0.0562 226 TYR A CZ  
1415 O OH  . TYR A 192 ? 0.3829 0.5147 0.6115 0.0412  0.0456  -0.0624 226 TYR A OH  
1416 N N   . ALA A 193 ? 0.4436 0.6768 0.7635 -0.0083 0.0665  0.0089  227 ALA A N   
1417 C CA  . ALA A 193 ? 0.3880 0.6252 0.7452 -0.0085 0.0676  0.0066  227 ALA A CA  
1418 C C   . ALA A 193 ? 0.4256 0.6462 0.8035 -0.0098 0.0571  0.0136  227 ALA A C   
1419 O O   . ALA A 193 ? 0.3588 0.5749 0.7542 -0.0039 0.0536  0.0009  227 ALA A O   
1420 C CB  . ALA A 193 ? 0.3005 0.5559 0.6718 -0.0196 0.0792  0.0160  227 ALA A CB  
1421 N N   . ALA A 194 ? 0.3674 0.5801 0.7430 -0.0165 0.0514  0.0332  228 ALA A N   
1422 C CA  . ALA A 194 ? 0.3014 0.4998 0.7035 -0.0144 0.0413  0.0387  228 ALA A CA  
1423 C C   . ALA A 194 ? 0.3844 0.5799 0.7826 -0.0058 0.0351  0.0266  228 ALA A C   
1424 O O   . ALA A 194 ? 0.3518 0.5421 0.7761 -0.0008 0.0319  0.0198  228 ALA A O   
1425 C CB  . ALA A 194 ? 0.2775 0.4681 0.6794 -0.0212 0.0336  0.0656  228 ALA A CB  
1426 N N   . SER A 195 ? 0.3611 0.5599 0.7277 -0.0052 0.0345  0.0224  229 SER A N   
1427 C CA  . SER A 195 ? 0.3972 0.5931 0.7606 -0.0014 0.0300  0.0126  229 SER A CA  
1428 C C   . SER A 195 ? 0.3379 0.5316 0.7050 0.0046  0.0361  -0.0049 229 SER A C   
1429 O O   . SER A 195 ? 0.4297 0.6226 0.8080 0.0068  0.0354  -0.0116 229 SER A O   
1430 C CB  . SER A 195 ? 0.3748 0.5696 0.7037 -0.0051 0.0264  0.0121  229 SER A CB  
1431 O OG  . SER A 195 ? 0.3510 0.5504 0.6702 -0.0115 0.0183  0.0283  229 SER A OG  
1432 N N   . ALA A 196 ? 0.4128 0.6087 0.7707 0.0074  0.0419  -0.0122 230 ALA A N   
1433 C CA  . ALA A 196 ? 0.4185 0.6134 0.7773 0.0139  0.0437  -0.0264 230 ALA A CA  
1434 C C   . ALA A 196 ? 0.3989 0.5969 0.7862 0.0141  0.0437  -0.0321 230 ALA A C   
1435 O O   . ALA A 196 ? 0.4346 0.6311 0.8198 0.0175  0.0436  -0.0428 230 ALA A O   
1436 C CB  . ALA A 196 ? 0.3488 0.5506 0.6993 0.0191  0.0472  -0.0327 230 ALA A CB  
1437 N N   . ARG A 197 ? 0.3794 0.5797 0.7913 0.0096  0.0440  -0.0253 231 ARG A N   
1438 C CA  . ARG A 197 ? 0.3843 0.5819 0.8260 0.0095  0.0433  -0.0337 231 ARG A CA  
1439 C C   . ARG A 197 ? 0.3674 0.5588 0.8234 0.0125  0.0413  -0.0336 231 ARG A C   
1440 O O   . ARG A 197 ? 0.4314 0.6218 0.9040 0.0160  0.0429  -0.0489 231 ARG A O   
1441 C CB  . ARG A 197 ? 0.3319 0.5282 0.7980 0.0017  0.0440  -0.0252 231 ARG A CB  
1442 C CG  . ARG A 197 ? 0.4320 0.6434 0.8920 -0.0025 0.0487  -0.0257 231 ARG A CG  
1443 C CD  . ARG A 197 ? 0.2717 0.4841 0.7608 -0.0145 0.0514  -0.0185 231 ARG A CD  
1444 N NE  . ARG A 197 ? 0.3735 0.6085 0.8709 -0.0178 0.0556  -0.0283 231 ARG A NE  
1445 C CZ  . ARG A 197 ? 0.3705 0.6245 0.8623 -0.0229 0.0644  -0.0198 231 ARG A CZ  
1446 N NH1 . ARG A 197 ? 0.3274 0.5781 0.7979 -0.0268 0.0699  -0.0012 231 ARG A NH1 
1447 N NH2 . ARG A 197 ? 0.3570 0.6376 0.8653 -0.0240 0.0676  -0.0317 231 ARG A NH2 
1448 N N   . ALA A 198 ? 0.2698 0.4606 0.7213 0.0116  0.0375  -0.0188 232 ALA A N   
1449 C CA  . ALA A 198 ? 0.2866 0.4793 0.7582 0.0159  0.0349  -0.0195 232 ALA A CA  
1450 C C   . ALA A 198 ? 0.2438 0.4450 0.7031 0.0179  0.0412  -0.0349 232 ALA A C   
1451 O O   . ALA A 198 ? 0.2121 0.4196 0.6931 0.0224  0.0454  -0.0465 232 ALA A O   
1452 C CB  . ALA A 198 ? 0.2608 0.4561 0.7295 0.0135  0.0260  0.0002  232 ALA A CB  
1453 N N   . PHE A 199 ? 0.2987 0.4991 0.7230 0.0145  0.0428  -0.0352 233 PHE A N   
1454 C CA  . PHE A 199 ? 0.2821 0.4855 0.6888 0.0136  0.0488  -0.0452 233 PHE A CA  
1455 C C   . PHE A 199 ? 0.3125 0.5180 0.7210 0.0176  0.0542  -0.0619 233 PHE A C   
1456 O O   . PHE A 199 ? 0.2781 0.4916 0.6849 0.0172  0.0617  -0.0720 233 PHE A O   
1457 C CB  . PHE A 199 ? 0.3390 0.5323 0.7085 0.0104  0.0470  -0.0404 233 PHE A CB  
1458 C CG  . PHE A 199 ? 0.3370 0.5256 0.6817 0.0096  0.0516  -0.0470 233 PHE A CG  
1459 C CD1 . PHE A 199 ? 0.3103 0.5035 0.6518 0.0025  0.0576  -0.0468 233 PHE A CD1 
1460 C CD2 . PHE A 199 ? 0.3881 0.5697 0.7132 0.0151  0.0493  -0.0517 233 PHE A CD2 
1461 C CE1 . PHE A 199 ? 0.3773 0.5641 0.6904 -0.0009 0.0627  -0.0487 233 PHE A CE1 
1462 C CE2 . PHE A 199 ? 0.3534 0.5280 0.6506 0.0145  0.0507  -0.0535 233 PHE A CE2 
1463 C CZ  . PHE A 199 ? 0.2867 0.4618 0.5748 0.0056  0.0582  -0.0507 233 PHE A CZ  
1464 N N   . GLY A 200 ? 0.2995 0.5013 0.7111 0.0197  0.0508  -0.0661 234 GLY A N   
1465 C CA  . GLY A 200 ? 0.2932 0.4983 0.7065 0.0221  0.0526  -0.0844 234 GLY A CA  
1466 C C   . GLY A 200 ? 0.3171 0.5242 0.7638 0.0245  0.0568  -0.0977 234 GLY A C   
1467 O O   . GLY A 200 ? 0.2774 0.4895 0.7202 0.0262  0.0614  -0.1176 234 GLY A O   
1468 N N   . ALA A 201 ? 0.2829 0.4850 0.7613 0.0259  0.0545  -0.0876 235 ALA A N   
1469 C CA  . ALA A 201 ? 0.2640 0.4637 0.7804 0.0318  0.0572  -0.1004 235 ALA A CA  
1470 C C   . ALA A 201 ? 0.3499 0.5651 0.8760 0.0366  0.0652  -0.1053 235 ALA A C   
1471 O O   . ALA A 201 ? 0.2358 0.4559 0.7877 0.0438  0.0723  -0.1252 235 ALA A O   
1472 C CB  . ALA A 201 ? 0.2285 0.4124 0.7777 0.0323  0.0488  -0.0845 235 ALA A CB  
1473 N N   . ALA A 202 ? 0.2611 0.4860 0.7700 0.0322  0.0650  -0.0900 236 ALA A N   
1474 C CA  . ALA A 202 ? 0.2549 0.5008 0.7773 0.0333  0.0734  -0.0941 236 ALA A CA  
1475 C C   . ALA A 202 ? 0.2273 0.4861 0.7269 0.0306  0.0887  -0.1136 236 ALA A C   
1476 O O   . ALA A 202 ? 0.3363 0.6159 0.8573 0.0339  0.1010  -0.1273 236 ALA A O   
1477 C CB  . ALA A 202 ? 0.2052 0.4567 0.7142 0.0253  0.0676  -0.0737 236 ALA A CB  
1478 N N   . PHE A 203 ? 0.3844 0.5194 0.5818 0.0301  -0.0780 -0.1266 237 PHE A N   
1479 C CA  . PHE A 203 ? 0.4426 0.6148 0.6506 0.0256  -0.0751 -0.1312 237 PHE A CA  
1480 C C   . PHE A 203 ? 0.4625 0.6315 0.6787 0.0237  -0.0755 -0.1316 237 PHE A C   
1481 O O   . PHE A 203 ? 0.3883 0.5583 0.6061 0.0157  -0.0680 -0.1200 237 PHE A O   
1482 C CB  . PHE A 203 ? 0.3611 0.5466 0.5678 0.0149  -0.0646 -0.1183 237 PHE A CB  
1483 C CG  . PHE A 203 ? 0.3477 0.5317 0.5496 0.0146  -0.0631 -0.1188 237 PHE A CG  
1484 C CD1 . PHE A 203 ? 0.2757 0.4895 0.4813 0.0172  -0.0664 -0.1322 237 PHE A CD1 
1485 C CD2 . PHE A 203 ? 0.3504 0.5084 0.5460 0.0117  -0.0583 -0.1092 237 PHE A CD2 
1486 C CE1 . PHE A 203 ? 0.2884 0.5047 0.4928 0.0166  -0.0654 -0.1360 237 PHE A CE1 
1487 C CE2 . PHE A 203 ? 0.3691 0.5298 0.5623 0.0119  -0.0578 -0.1133 237 PHE A CE2 
1488 C CZ  . PHE A 203 ? 0.3386 0.5277 0.5368 0.0143  -0.0615 -0.1267 237 PHE A CZ  
1489 N N   . PRO A 204 ? 0.4824 0.6480 0.7066 0.0318  -0.0852 -0.1469 238 PRO A N   
1490 C CA  . PRO A 204 ? 0.4070 0.5675 0.6427 0.0290  -0.0858 -0.1502 238 PRO A CA  
1491 C C   . PRO A 204 ? 0.4543 0.6581 0.6984 0.0260  -0.0836 -0.1553 238 PRO A C   
1492 O O   . PRO A 204 ? 0.3856 0.5894 0.6369 0.0212  -0.0808 -0.1528 238 PRO A O   
1493 C CB  . PRO A 204 ? 0.3817 0.5264 0.6270 0.0394  -0.0986 -0.1681 238 PRO A CB  
1494 C CG  . PRO A 204 ? 0.3968 0.5621 0.6395 0.0500  -0.1060 -0.1804 238 PRO A CG  
1495 C CD  . PRO A 204 ? 0.3114 0.4769 0.5381 0.0447  -0.0974 -0.1639 238 PRO A CD  
1496 N N   . LYS A 205 ? 0.4699 0.7138 0.7126 0.0284  -0.0846 -0.1623 239 LYS A N   
1497 C CA  . LYS A 205 ? 0.4679 0.7580 0.7144 0.0262  -0.0833 -0.1662 239 LYS A CA  
1498 C C   . LYS A 205 ? 0.3852 0.6854 0.6208 0.0167  -0.0734 -0.1426 239 LYS A C   
1499 O O   . LYS A 205 ? 0.4056 0.7443 0.6394 0.0147  -0.0723 -0.1404 239 LYS A O   
1500 C CB  . LYS A 205 ? 0.5207 0.8556 0.7716 0.0329  -0.0893 -0.1878 239 LYS A CB  
1501 C CG  . LYS A 205 ? 0.4341 0.7639 0.7013 0.0449  -0.1020 -0.2156 239 LYS A CG  
1502 C CD  . LYS A 205 ? 0.5874 0.9754 0.8661 0.0504  -0.1075 -0.2411 239 LYS A CD  
1503 C CE  . LYS A 205 ? 0.5379 0.9438 0.8213 0.0465  -0.1060 -0.2403 239 LYS A CE  
1504 N NZ  . LYS A 205 ? 0.6439 1.1154 0.9254 0.0485  -0.1059 -0.2547 239 LYS A NZ  
1505 N N   . ALA A 206 ? 0.3686 0.6356 0.5971 0.0115  -0.0671 -0.1252 240 ALA A N   
1506 C CA  . ALA A 206 ? 0.3913 0.6609 0.6134 0.0034  -0.0592 -0.1038 240 ALA A CA  
1507 C C   . ALA A 206 ? 0.4813 0.7362 0.7075 0.0022  -0.0576 -0.0936 240 ALA A C   
1508 O O   . ALA A 206 ? 0.5347 0.7563 0.7637 0.0016  -0.0556 -0.0916 240 ALA A O   
1509 C CB  . ALA A 206 ? 0.3122 0.5578 0.5293 -0.0007 -0.0542 -0.0955 240 ALA A CB  
1510 N N   . ASN A 207 ? 0.4994 0.7829 0.7256 0.0022  -0.0586 -0.0878 241 ASN A N   
1511 C CA  . ASN A 207 ? 0.3489 0.6260 0.5808 0.0031  -0.0587 -0.0798 241 ASN A CA  
1512 C C   . ASN A 207 ? 0.4320 0.6994 0.6595 -0.0004 -0.0546 -0.0564 241 ASN A C   
1513 O O   . ASN A 207 ? 0.4702 0.7308 0.7040 0.0022  -0.0558 -0.0498 241 ASN A O   
1514 C CB  . ASN A 207 ? 0.3906 0.7067 0.6266 0.0083  -0.0652 -0.0901 241 ASN A CB  
1515 C CG  . ASN A 207 ? 0.4810 0.7996 0.7292 0.0120  -0.0704 -0.1161 241 ASN A CG  
1516 O OD1 . ASN A 207 ? 0.6073 0.8975 0.8662 0.0108  -0.0698 -0.1221 241 ASN A OD1 
1517 N ND2 . ASN A 207 ? 0.4497 0.8029 0.6978 0.0159  -0.0754 -0.1323 241 ASN A ND2 
1518 N N   . THR A 208 ? 0.4550 0.7218 0.6746 -0.0062 -0.0505 -0.0454 242 THR A N   
1519 C CA  . THR A 208 ? 0.3931 0.6429 0.6120 -0.0107 -0.0469 -0.0237 242 THR A CA  
1520 C C   . THR A 208 ? 0.3744 0.5910 0.5978 -0.0147 -0.0417 -0.0264 242 THR A C   
1521 O O   . THR A 208 ? 0.4419 0.6618 0.6618 -0.0199 -0.0386 -0.0299 242 THR A O   
1522 C CB  . THR A 208 ? 0.4092 0.6843 0.6174 -0.0172 -0.0451 -0.0078 242 THR A CB  
1523 O OG1 . THR A 208 ? 0.4501 0.7653 0.6508 -0.0125 -0.0502 -0.0097 242 THR A OG1 
1524 C CG2 . THR A 208 ? 0.3179 0.5702 0.5280 -0.0211 -0.0435 0.0174  242 THR A CG2 
1525 N N   . ILE A 209 ? 0.3567 0.5468 0.5888 -0.0120 -0.0409 -0.0271 243 ILE A N   
1526 C CA  . ILE A 209 ? 0.4092 0.5725 0.6446 -0.0145 -0.0364 -0.0320 243 ILE A CA  
1527 C C   . ILE A 209 ? 0.4865 0.6338 0.7304 -0.0179 -0.0341 -0.0187 243 ILE A C   
1528 O O   . ILE A 209 ? 0.4252 0.5638 0.6784 -0.0138 -0.0362 -0.0120 243 ILE A O   
1529 C CB  . ILE A 209 ? 0.3776 0.5258 0.6169 -0.0110 -0.0356 -0.0427 243 ILE A CB  
1530 C CG1 . ILE A 209 ? 0.3140 0.4735 0.5490 -0.0084 -0.0390 -0.0543 243 ILE A CG1 
1531 C CG2 . ILE A 209 ? 0.3539 0.4812 0.5917 -0.0131 -0.0310 -0.0482 243 ILE A CG2 
1532 C CD1 . ILE A 209 ? 0.2758 0.4428 0.5018 -0.0081 -0.0412 -0.0622 243 ILE A CD1 
1533 N N   . ALA A 210 ? 0.4490 0.5929 0.6927 -0.0250 -0.0306 -0.0167 244 ALA A N   
1534 C CA  . ALA A 210 ? 0.4072 0.5314 0.6633 -0.0299 -0.0284 -0.0070 244 ALA A CA  
1535 C C   . ALA A 210 ? 0.4107 0.5161 0.6752 -0.0291 -0.0255 -0.0217 244 ALA A C   
1536 O O   . ALA A 210 ? 0.4602 0.5701 0.7163 -0.0280 -0.0243 -0.0356 244 ALA A O   
1537 C CB  . ALA A 210 ? 0.3188 0.4528 0.5732 -0.0413 -0.0251 0.0032  244 ALA A CB  
1538 N N   . MET A 211 ? 0.4054 0.4906 0.6865 -0.0283 -0.0256 -0.0190 245 MET A N   
1539 C CA  . MET A 211 ? 0.4217 0.4943 0.7125 -0.0267 -0.0229 -0.0352 245 MET A CA  
1540 C C   . MET A 211 ? 0.4280 0.4817 0.7412 -0.0307 -0.0231 -0.0324 245 MET A C   
1541 O O   . MET A 211 ? 0.3854 0.4310 0.7051 -0.0349 -0.0253 -0.0144 245 MET A O   
1542 C CB  . MET A 211 ? 0.4798 0.5514 0.7717 -0.0184 -0.0232 -0.0438 245 MET A CB  
1543 C CG  . MET A 211 ? 0.5033 0.5733 0.8050 -0.0122 -0.0279 -0.0338 245 MET A CG  
1544 S SD  . MET A 211 ? 0.6051 0.6893 0.9004 -0.0065 -0.0273 -0.0423 245 MET A SD  
1545 C CE  . MET A 211 ? 0.4845 0.5860 0.7682 -0.0056 -0.0328 -0.0285 245 MET A CE  
1546 N N   . SER A 212 ? 0.4601 0.5067 0.7854 -0.0295 -0.0210 -0.0503 246 SER A N   
1547 C CA  . SER A 212 ? 0.4676 0.4959 0.8187 -0.0339 -0.0215 -0.0536 246 SER A CA  
1548 C C   . SER A 212 ? 0.4902 0.4993 0.8626 -0.0260 -0.0269 -0.0487 246 SER A C   
1549 O O   . SER A 212 ? 0.4731 0.4610 0.8625 -0.0295 -0.0305 -0.0350 246 SER A O   
1550 C CB  . SER A 212 ? 0.4006 0.4345 0.7581 -0.0341 -0.0183 -0.0791 246 SER A CB  
1551 O OG  . SER A 212 ? 0.4319 0.4833 0.7719 -0.0393 -0.0156 -0.0843 246 SER A OG  
1552 N N   . HIS A 213 ? 0.5677 0.5839 0.9402 -0.0154 -0.0279 -0.0595 247 HIS A N   
1553 C CA  . HIS A 213 ? 0.4994 0.5028 0.8969 -0.0052 -0.0338 -0.0631 247 HIS A CA  
1554 C C   . HIS A 213 ? 0.4371 0.4453 0.8286 0.0032  -0.0393 -0.0482 247 HIS A C   
1555 O O   . HIS A 213 ? 0.4826 0.4914 0.8912 0.0144  -0.0438 -0.0572 247 HIS A O   
1556 C CB  . HIS A 213 ? 0.5165 0.5315 0.9246 0.0006  -0.0303 -0.0917 247 HIS A CB  
1557 C CG  . HIS A 213 ? 0.5646 0.5815 0.9777 -0.0057 -0.0259 -0.1099 247 HIS A CG  
1558 N ND1 . HIS A 213 ? 0.4189 0.4161 0.8543 -0.0115 -0.0284 -0.1106 247 HIS A ND1 
1559 C CD2 . HIS A 213 ? 0.5050 0.5425 0.9037 -0.0071 -0.0196 -0.1281 247 HIS A CD2 
1560 C CE1 . HIS A 213 ? 0.5405 0.5495 0.9773 -0.0157 -0.0242 -0.1319 247 HIS A CE1 
1561 N NE2 . HIS A 213 ? 0.5836 0.6177 0.9964 -0.0121 -0.0193 -0.1419 247 HIS A NE2 
1562 N N   . SER A 214 ? 0.4609 0.4771 0.8302 -0.0011 -0.0397 -0.0285 248 SER A N   
1563 C CA  . SER A 214 ? 0.4576 0.4833 0.8213 0.0073  -0.0460 -0.0159 248 SER A CA  
1564 C C   . SER A 214 ? 0.4694 0.4993 0.8140 0.0010  -0.0478 0.0089  248 SER A C   
1565 O O   . SER A 214 ? 0.5407 0.5737 0.8735 -0.0107 -0.0420 0.0123  248 SER A O   
1566 C CB  . SER A 214 ? 0.4944 0.5446 0.8473 0.0106  -0.0422 -0.0303 248 SER A CB  
1567 O OG  . SER A 214 ? 0.6126 0.6651 0.9764 0.0121  -0.0369 -0.0530 248 SER A OG  
1568 N N   . ALA A 215 ? 0.5270 0.5619 0.8691 0.0095  -0.0561 0.0245  249 ALA A N   
1569 C CA  . ALA A 215 ? 0.3943 0.4432 0.7149 0.0049  -0.0578 0.0468  249 ALA A CA  
1570 C C   . ALA A 215 ? 0.4558 0.5354 0.7559 0.0007  -0.0521 0.0355  249 ALA A C   
1571 O O   . ALA A 215 ? 0.4784 0.5657 0.7809 0.0036  -0.0490 0.0150  249 ALA A O   
1572 C CB  . ALA A 215 ? 0.4149 0.4665 0.7363 0.0179  -0.0698 0.0639  249 ALA A CB  
1573 N N   . PRO A 216 ? 0.5192 0.6169 0.8002 -0.0068 -0.0505 0.0481  250 PRO A N   
1574 C CA  . PRO A 216 ? 0.5193 0.6461 0.7847 -0.0086 -0.0472 0.0349  250 PRO A CA  
1575 C C   . PRO A 216 ? 0.4125 0.5563 0.6793 0.0023  -0.0525 0.0250  250 PRO A C   
1576 O O   . PRO A 216 ? 0.5461 0.6953 0.8164 0.0113  -0.0605 0.0351  250 PRO A O   
1577 C CB  . PRO A 216 ? 0.3839 0.5324 0.6320 -0.0163 -0.0465 0.0514  250 PRO A CB  
1578 C CG  . PRO A 216 ? 0.4650 0.5892 0.7195 -0.0253 -0.0442 0.0700  250 PRO A CG  
1579 C CD  . PRO A 216 ? 0.5319 0.6244 0.8062 -0.0159 -0.0502 0.0731  250 PRO A CD  
1580 N N   . ASP A 217 ? 0.4523 0.6041 0.7174 0.0014  -0.0486 0.0049  251 ASP A N   
1581 C CA  . ASP A 217 ? 0.4616 0.6276 0.7321 0.0080  -0.0514 -0.0083 251 ASP A CA  
1582 C C   . ASP A 217 ? 0.3847 0.5702 0.6447 0.0047  -0.0500 -0.0207 251 ASP A C   
1583 O O   . ASP A 217 ? 0.3965 0.5848 0.6454 -0.0008 -0.0474 -0.0205 251 ASP A O   
1584 C CB  . ASP A 217 ? 0.4342 0.5831 0.7197 0.0092  -0.0472 -0.0218 251 ASP A CB  
1585 C CG  . ASP A 217 ? 0.4726 0.6372 0.7706 0.0157  -0.0504 -0.0324 251 ASP A CG  
1586 O OD1 . ASP A 217 ? 0.5157 0.7041 0.8109 0.0202  -0.0568 -0.0311 251 ASP A OD1 
1587 O OD2 . ASP A 217 ? 0.5016 0.6592 0.8131 0.0159  -0.0462 -0.0441 251 ASP A OD2 
1588 N N   . SER A 218 ? 0.5112 0.7109 0.7780 0.0084  -0.0523 -0.0337 252 SER A N   
1589 C CA  . SER A 218 ? 0.4706 0.6847 0.7332 0.0061  -0.0524 -0.0484 252 SER A CA  
1590 C C   . SER A 218 ? 0.3812 0.5703 0.6437 0.0001  -0.0457 -0.0586 252 SER A C   
1591 O O   . SER A 218 ? 0.4141 0.5810 0.6772 -0.0025 -0.0404 -0.0547 252 SER A O   
1592 C CB  . SER A 218 ? 0.4303 0.6698 0.7036 0.0112  -0.0580 -0.0595 252 SER A CB  
1593 O OG  . SER A 218 ? 0.4775 0.7057 0.7664 0.0099  -0.0543 -0.0692 252 SER A OG  
1594 N N   . ARG A 219 ? 0.3814 0.5744 0.6435 -0.0016 -0.0465 -0.0720 253 ARG A N   
1595 C CA  . ARG A 219 ? 0.3314 0.4984 0.5903 -0.0067 -0.0416 -0.0781 253 ARG A CA  
1596 C C   . ARG A 219 ? 0.4290 0.5832 0.6978 -0.0114 -0.0353 -0.0811 253 ARG A C   
1597 O O   . ARG A 219 ? 0.4358 0.5681 0.6985 -0.0168 -0.0297 -0.0819 253 ARG A O   
1598 C CB  . ARG A 219 ? 0.2669 0.4372 0.5249 -0.0063 -0.0462 -0.0908 253 ARG A CB  
1599 C CG  . ARG A 219 ? 0.4182 0.6040 0.6668 -0.0020 -0.0513 -0.0919 253 ARG A CG  
1600 C CD  . ARG A 219 ? 0.4511 0.6418 0.7037 0.0011  -0.0578 -0.1091 253 ARG A CD  
1601 N NE  . ARG A 219 ? 0.4171 0.5732 0.6654 -0.0003 -0.0572 -0.1112 253 ARG A NE  
1602 C CZ  . ARG A 219 ? 0.4837 0.6274 0.7197 0.0025  -0.0583 -0.1085 253 ARG A CZ  
1603 N NH1 . ARG A 219 ? 0.4185 0.5819 0.6481 0.0046  -0.0584 -0.1052 253 ARG A NH1 
1604 N NH2 . ARG A 219 ? 0.3876 0.4996 0.6177 0.0029  -0.0594 -0.1087 253 ARG A NH2 
1605 N N   . ALA A 220 ? 0.3863 0.5569 0.6696 -0.0092 -0.0362 -0.0829 254 ALA A N   
1606 C CA  . ALA A 220 ? 0.3197 0.4850 0.6150 -0.0139 -0.0291 -0.0878 254 ALA A CA  
1607 C C   . ALA A 220 ? 0.4437 0.5916 0.7335 -0.0148 -0.0230 -0.0810 254 ALA A C   
1608 O O   . ALA A 220 ? 0.4477 0.5893 0.7413 -0.0212 -0.0147 -0.0860 254 ALA A O   
1609 C CB  . ALA A 220 ? 0.2977 0.4891 0.6119 -0.0082 -0.0335 -0.0932 254 ALA A CB  
1610 N N   . ALA A 221 ? 0.4238 0.5665 0.7059 -0.0098 -0.0264 -0.0711 255 ALA A N   
1611 C CA  . ALA A 221 ? 0.3789 0.5060 0.6583 -0.0107 -0.0215 -0.0684 255 ALA A CA  
1612 C C   . ALA A 221 ? 0.3861 0.4975 0.6496 -0.0170 -0.0156 -0.0708 255 ALA A C   
1613 O O   . ALA A 221 ? 0.3633 0.4676 0.6253 -0.0194 -0.0093 -0.0736 255 ALA A O   
1614 C CB  . ALA A 221 ? 0.2837 0.4075 0.5608 -0.0064 -0.0263 -0.0578 255 ALA A CB  
1615 N N   . ILE A 222 ? 0.3439 0.4513 0.5956 -0.0183 -0.0187 -0.0705 256 ILE A N   
1616 C CA  . ILE A 222 ? 0.3726 0.4625 0.6077 -0.0217 -0.0158 -0.0707 256 ILE A CA  
1617 C C   . ILE A 222 ? 0.4188 0.5016 0.6543 -0.0299 -0.0082 -0.0732 256 ILE A C   
1618 O O   . ILE A 222 ? 0.3737 0.4472 0.5981 -0.0339 -0.0015 -0.0713 256 ILE A O   
1619 C CB  . ILE A 222 ? 0.4279 0.5153 0.6540 -0.0184 -0.0235 -0.0716 256 ILE A CB  
1620 C CG1 . ILE A 222 ? 0.4508 0.5501 0.6755 -0.0132 -0.0285 -0.0693 256 ILE A CG1 
1621 C CG2 . ILE A 222 ? 0.3923 0.4581 0.6012 -0.0193 -0.0232 -0.0706 256 ILE A CG2 
1622 C CD1 . ILE A 222 ? 0.3215 0.4267 0.5400 -0.0091 -0.0358 -0.0742 256 ILE A CD1 
1623 N N   . THR A 223 ? 0.4624 0.5525 0.7108 -0.0336 -0.0085 -0.0780 257 THR A N   
1624 C CA  . THR A 223 ? 0.4090 0.4934 0.6606 -0.0449 0.0003  -0.0803 257 THR A CA  
1625 C C   . THR A 223 ? 0.3459 0.4439 0.6064 -0.0489 0.0098  -0.0838 257 THR A C   
1626 O O   . THR A 223 ? 0.3839 0.4767 0.6370 -0.0589 0.0201  -0.0824 257 THR A O   
1627 C CB  . THR A 223 ? 0.3643 0.4573 0.6336 -0.0486 -0.0026 -0.0887 257 THR A CB  
1628 O OG1 . THR A 223 ? 0.3934 0.5144 0.6818 -0.0425 -0.0062 -0.0957 257 THR A OG1 
1629 C CG2 . THR A 223 ? 0.3155 0.3984 0.5791 -0.0434 -0.0129 -0.0898 257 THR A CG2 
1630 N N   . HIS A 224 ? 0.3695 0.4860 0.6460 -0.0406 0.0062  -0.0883 258 HIS A N   
1631 C CA  . HIS A 224 ? 0.3465 0.4777 0.6360 -0.0412 0.0130  -0.0956 258 HIS A CA  
1632 C C   . HIS A 224 ? 0.3900 0.5123 0.6644 -0.0413 0.0182  -0.0933 258 HIS A C   
1633 O O   . HIS A 224 ? 0.4055 0.5384 0.6821 -0.0473 0.0281  -0.1001 258 HIS A O   
1634 C CB  . HIS A 224 ? 0.3446 0.4917 0.6546 -0.0292 0.0046  -0.0993 258 HIS A CB  
1635 C CG  . HIS A 224 ? 0.3706 0.5321 0.6983 -0.0258 0.0085  -0.1096 258 HIS A CG  
1636 N ND1 . HIS A 224 ? 0.3141 0.4961 0.6568 -0.0330 0.0174  -0.1227 258 HIS A ND1 
1637 C CD2 . HIS A 224 ? 0.3981 0.5578 0.7341 -0.0161 0.0045  -0.1111 258 HIS A CD2 
1638 C CE1 . HIS A 224 ? 0.3251 0.5205 0.6844 -0.0261 0.0182  -0.1335 258 HIS A CE1 
1639 N NE2 . HIS A 224 ? 0.4204 0.6001 0.7767 -0.0153 0.0098  -0.1267 258 HIS A NE2 
1640 N N   . THR A 225 ? 0.4210 0.5289 0.6811 -0.0351 0.0119  -0.0862 259 THR A N   
1641 C CA  . THR A 225 ? 0.3501 0.4524 0.5958 -0.0348 0.0155  -0.0865 259 THR A CA  
1642 C C   . THR A 225 ? 0.5208 0.6138 0.7428 -0.0438 0.0227  -0.0813 259 THR A C   
1643 O O   . THR A 225 ? 0.5323 0.6323 0.7448 -0.0473 0.0306  -0.0846 259 THR A O   
1644 C CB  . THR A 225 ? 0.4517 0.5441 0.6907 -0.0271 0.0068  -0.0820 259 THR A CB  
1645 O OG1 . THR A 225 ? 0.3890 0.4870 0.6481 -0.0207 0.0009  -0.0825 259 THR A OG1 
1646 C CG2 . THR A 225 ? 0.4260 0.5170 0.6533 -0.0260 0.0095  -0.0862 259 THR A CG2 
1647 N N   . ALA A 226 ? 0.4458 0.5233 0.6581 -0.0475 0.0197  -0.0732 260 ALA A N   
1648 C CA  . ALA A 226 ? 0.4303 0.4918 0.6195 -0.0560 0.0250  -0.0642 260 ALA A CA  
1649 C C   . ALA A 226 ? 0.5143 0.5873 0.7082 -0.0703 0.0390  -0.0660 260 ALA A C   
1650 O O   . ALA A 226 ? 0.4833 0.5547 0.6565 -0.0778 0.0476  -0.0597 260 ALA A O   
1651 C CB  . ALA A 226 ? 0.4588 0.4981 0.6429 -0.0556 0.0167  -0.0575 260 ALA A CB  
1652 N N   . ARG A 227 ? 0.4348 0.5236 0.6555 -0.0744 0.0415  -0.0751 261 ARG A N   
1653 C CA  . ARG A 227 ? 0.4932 0.5999 0.7234 -0.0892 0.0557  -0.0804 261 ARG A CA  
1654 C C   . ARG A 227 ? 0.4832 0.6163 0.7159 -0.0875 0.0637  -0.0907 261 ARG A C   
1655 O O   . ARG A 227 ? 0.5590 0.7060 0.7838 -0.1006 0.0776  -0.0912 261 ARG A O   
1656 C CB  . ARG A 227 ? 0.4535 0.5761 0.7153 -0.0918 0.0546  -0.0917 261 ARG A CB  
1657 C CG  . ARG A 227 ? 0.5251 0.6284 0.7884 -0.1016 0.0532  -0.0864 261 ARG A CG  
1658 C CD  . ARG A 227 ? 0.5720 0.6573 0.8161 -0.1205 0.0657  -0.0739 261 ARG A CD  
1659 N NE  . ARG A 227 ? 0.5268 0.6383 0.7877 -0.1382 0.0817  -0.0825 261 ARG A NE  
1660 C CZ  . ARG A 227 ? 0.5498 0.6566 0.7948 -0.1579 0.0971  -0.0720 261 ARG A CZ  
1661 N NH1 . ARG A 227 ? 0.5747 0.6486 0.7846 -0.1609 0.0971  -0.0504 261 ARG A NH1 
1662 N NH2 . ARG A 227 ? 0.4787 0.6169 0.7432 -0.1751 0.1126  -0.0830 261 ARG A NH2 
1663 N N   . MET A 228 ? 0.4591 0.6005 0.7040 -0.0723 0.0552  -0.0995 262 MET A N   
1664 C CA  . MET A 228 ? 0.4589 0.6230 0.7088 -0.0684 0.0605  -0.1124 262 MET A CA  
1665 C C   . MET A 228 ? 0.5177 0.6763 0.7350 -0.0716 0.0654  -0.1054 262 MET A C   
1666 O O   . MET A 228 ? 0.4848 0.6676 0.6971 -0.0777 0.0767  -0.1136 262 MET A O   
1667 C CB  . MET A 228 ? 0.3921 0.5572 0.6626 -0.0517 0.0485  -0.1210 262 MET A CB  
1668 C CG  . MET A 228 ? 0.3565 0.5367 0.6605 -0.0458 0.0440  -0.1314 262 MET A CG  
1669 S SD  . MET A 228 ? 0.3846 0.5711 0.7152 -0.0284 0.0345  -0.1450 262 MET A SD  
1670 C CE  . MET A 228 ? 0.3200 0.4751 0.6415 -0.0201 0.0202  -0.1268 262 MET A CE  
1671 N N   . ALA A 229 ? 0.4636 0.5950 0.6586 -0.0665 0.0566  -0.0916 263 ALA A N   
1672 C CA  . ALA A 229 ? 0.4685 0.5954 0.6306 -0.0670 0.0588  -0.0842 263 ALA A CA  
1673 C C   . ALA A 229 ? 0.5144 0.6351 0.6514 -0.0827 0.0697  -0.0691 263 ALA A C   
1674 O O   . ALA A 229 ? 0.5028 0.6314 0.6121 -0.0860 0.0758  -0.0638 263 ALA A O   
1675 C CB  . ALA A 229 ? 0.5291 0.6316 0.6775 -0.0556 0.0448  -0.0761 263 ALA A CB  
1676 N N   . ASP A 230 ? 0.5690 0.6763 0.7152 -0.0931 0.0722  -0.0616 264 ASP A N   
1677 C CA  . ASP A 230 ? 0.5461 0.6448 0.6731 -0.1117 0.0842  -0.0462 264 ASP A CA  
1678 C C   . ASP A 230 ? 0.5552 0.6922 0.6823 -0.1245 0.1021  -0.0549 264 ASP A C   
1679 O O   . ASP A 230 ? 0.6790 0.8174 0.7751 -0.1362 0.1125  -0.0410 264 ASP A O   
1680 C CB  . ASP A 230 ? 0.4892 0.5706 0.6359 -0.1215 0.0838  -0.0428 264 ASP A CB  
1681 C CG  . ASP A 230 ? 0.6253 0.6651 0.7603 -0.1148 0.0697  -0.0289 264 ASP A CG  
1682 O OD1 . ASP A 230 ? 0.6896 0.7080 0.7926 -0.1100 0.0648  -0.0139 264 ASP A OD1 
1683 O OD2 . ASP A 230 ? 0.5811 0.6126 0.7395 -0.1131 0.0626  -0.0347 264 ASP A OD2 
1684 N N   . LYS A 231 ? 0.5747 0.7452 0.7361 -0.1218 0.1055  -0.0781 265 LYS A N   
1685 C CA  . LYS A 231 ? 0.6074 0.8219 0.7744 -0.1320 0.1219  -0.0925 265 LYS A CA  
1686 C C   . LYS A 231 ? 0.6898 0.9256 0.8406 -0.1214 0.1216  -0.1017 265 LYS A C   
1687 O O   . LYS A 231 ? 0.7565 1.0261 0.8943 -0.1317 0.1361  -0.1068 265 LYS A O   
1688 C CB  . LYS A 231 ? 0.5075 0.7519 0.7204 -0.1295 0.1230  -0.1172 265 LYS A CB  
1689 C CG  . LYS A 231 ? 0.7488 0.9747 0.9839 -0.1328 0.1173  -0.1138 265 LYS A CG  
1690 C CD  . LYS A 231 ? 0.8328 1.0367 1.0503 -0.1549 0.1269  -0.0936 265 LYS A CD  
1691 C CE  . LYS A 231 ? 0.7139 0.9340 0.9654 -0.1681 0.1334  -0.1048 265 LYS A CE  
1692 N NZ  . LYS A 231 ? 0.5826 0.7946 0.8210 -0.1964 0.1501  -0.0898 265 LYS A NZ  
1693 N N   . LEU A 232 ? 0.6911 0.9111 0.8434 -0.1021 0.1057  -0.1055 266 LEU A N   
1694 C CA  . LEU A 232 ? 0.7195 0.9570 0.8565 -0.0922 0.1039  -0.1151 266 LEU A CA  
1695 C C   . LEU A 232 ? 0.7177 0.9450 0.8059 -0.0984 0.1073  -0.0931 266 LEU A C   
1696 O O   . LEU A 232 ? 0.7696 1.0270 0.8386 -0.0978 0.1133  -0.1005 266 LEU A O   
1697 C CB  . LEU A 232 ? 0.5680 0.7886 0.7210 -0.0729 0.0865  -0.1235 266 LEU A CB  
1698 C CG  . LEU A 232 ? 0.6539 0.8898 0.7970 -0.0617 0.0820  -0.1366 266 LEU A CG  
1699 C CD1 . LEU A 232 ? 0.4328 0.7124 0.6010 -0.0595 0.0892  -0.1666 266 LEU A CD1 
1700 C CD2 . LEU A 232 ? 0.6059 0.8162 0.7600 -0.0475 0.0655  -0.1375 266 LEU A CD2 
1701 N N   . ARG A 233 ? 0.7022 0.8886 0.7703 -0.1032 0.1026  -0.0668 267 ARG A N   
1702 C CA  . ARG A 233 ? 0.7280 0.8979 0.7488 -0.1073 0.1032  -0.0421 267 ARG A CA  
1703 C C   . ARG A 233 ? 0.8011 0.9966 0.8002 -0.1280 0.1234  -0.0332 267 ARG A C   
1704 O O   . ARG A 233 ? 0.8612 1.0777 0.8260 -0.1281 0.1281  -0.0284 267 ARG A O   
1705 C CB  . ARG A 233 ? 0.7052 0.8228 0.7164 -0.1071 0.0924  -0.0183 267 ARG A CB  
1706 C CG  . ARG A 233 ? 0.7376 0.8295 0.7037 -0.1012 0.0840  0.0052  267 ARG A CG  
1707 C CD  . ARG A 233 ? 0.7892 0.8326 0.7443 -0.1100 0.0807  0.0318  267 ARG A CD  
1708 N NE  . ARG A 233 ? 0.8959 0.9064 0.8182 -0.0959 0.0645  0.0501  267 ARG A NE  
1709 C CZ  . ARG A 233 ? 0.9688 0.9706 0.8464 -0.0987 0.0661  0.0739  267 ARG A CZ  
1710 N NH1 . ARG A 233 ? 0.9646 0.9900 0.8223 -0.1174 0.0850  0.0836  267 ARG A NH1 
1711 N NH2 . ARG A 233 ? 1.0069 0.9783 0.8586 -0.0819 0.0479  0.0883  267 ARG A NH2 
1712 N N   T LEU A 234 ? 0.9296 1.1280 0.9483 -0.1466 0.1362  -0.0317 268 LEU A N   
1713 C CA  T LEU A 234 ? 1.0160 1.2407 1.0167 -0.1707 0.1579  -0.0226 268 LEU A CA  
1714 C C   T LEU A 234 ? 1.0570 1.3466 1.0671 -0.1711 0.1704  -0.0508 268 LEU A C   
1715 O O   T LEU A 234 ? 1.0213 1.3433 1.0114 -0.1905 0.1897  -0.0450 268 LEU A O   
1716 C CB  T LEU A 234 ? 0.9117 1.1248 0.9377 -0.1915 0.1680  -0.0176 268 LEU A CB  
1717 C CG  T LEU A 234 ? 1.0246 1.1757 1.0453 -0.1937 0.1571  0.0075  268 LEU A CG  
1718 C CD1 T LEU A 234 ? 0.9984 1.1463 1.0565 -0.2109 0.1648  0.0014  268 LEU A CD1 
1719 C CD2 T LEU A 234 ? 1.1416 1.2605 1.1114 -0.2040 0.1598  0.0440  268 LEU A CD2 
1720 N N   T GLU A 235 ? 1.1836 1.4935 1.2245 -0.1509 0.1602  -0.0813 269 GLU A N   
1721 C CA  T GLU A 235 ? 1.1690 1.5394 1.2231 -0.1478 0.1692  -0.1127 269 GLU A CA  
1722 C C   T GLU A 235 ? 1.1666 1.5583 1.1817 -0.1402 0.1682  -0.1121 269 GLU A C   
1723 O O   T GLU A 235 ? 1.1899 1.6374 1.2111 -0.1389 0.1769  -0.1389 269 GLU A O   
1724 C CB  T GLU A 235 ? 1.0752 1.4541 1.1807 -0.1286 0.1570  -0.1455 269 GLU A CB  
1725 C CG  T GLU A 235 ? 1.2348 1.6350 1.3842 -0.1360 0.1646  -0.1635 269 GLU A CG  
1726 C CD  T GLU A 235 ? 1.3531 1.7376 1.5470 -0.1162 0.1474  -0.1814 269 GLU A CD  
1727 O OE1 T GLU A 235 ? 1.2999 1.7100 1.5335 -0.1156 0.1502  -0.2032 269 GLU A OE1 
1728 O OE2 T GLU A 235 ? 1.2724 1.6204 1.4613 -0.1012 0.1309  -0.1733 269 GLU A OE2 
1729 N N   T ARG A 236 ? 1.0784 1.4308 1.0552 -0.1339 0.1569  -0.0851 270 ARG A N   
1730 C CA  T ARG A 236 ? 0.9747 1.3480 0.9119 -0.1248 0.1537  -0.0838 270 ARG A CA  
1731 C C   T ARG A 236 ? 1.0060 1.3662 0.8857 -0.1401 0.1621  -0.0443 270 ARG A C   
1732 O O   T ARG A 236 ? 0.9730 1.2803 0.8281 -0.1361 0.1501  -0.0143 270 ARG A O   
1740 N N   . ASP B 6   ? 0.8251 1.2853 0.9036 -0.2266 0.0704  0.1501  40  ASP B N   
1741 C CA  . ASP B 6   ? 0.9894 1.4068 1.0273 -0.2463 0.0268  0.1483  40  ASP B CA  
1742 C C   . ASP B 6   ? 0.9169 1.3316 0.9619 -0.2921 0.0174  0.1593  40  ASP B C   
1743 O O   . ASP B 6   ? 1.0152 1.4867 1.1352 -0.3142 0.0007  0.1701  40  ASP B O   
1744 C CB  . ASP B 6   ? 0.9165 1.3644 0.9952 -0.2339 -0.0083 0.1502  40  ASP B CB  
1745 C CG  . ASP B 6   ? 1.0390 1.4573 1.0818 -0.1956 -0.0072 0.1381  40  ASP B CG  
1746 O OD1 . ASP B 6   ? 1.0136 1.3907 1.0037 -0.1807 0.0165  0.1253  40  ASP B OD1 
1747 O OD2 . ASP B 6   ? 1.0482 1.4827 1.1149 -0.1806 -0.0306 0.1413  40  ASP B OD2 
1748 N N   . GLN B 7   ? 0.9866 1.3337 0.9546 -0.3060 0.0265  0.1559  41  GLN B N   
1749 C CA  . GLN B 7   ? 1.0719 1.3985 1.0333 -0.3510 0.0199  0.1660  41  GLN B CA  
1750 C C   . GLN B 7   ? 1.0712 1.3436 0.9821 -0.3654 -0.0283 0.1586  41  GLN B C   
1751 O O   . GLN B 7   ? 1.0822 1.2841 0.9066 -0.3491 -0.0362 0.1460  41  GLN B O   
1752 C CB  . GLN B 7   ? 1.1029 1.3765 1.0001 -0.3561 0.0568  0.1684  41  GLN B CB  
1753 C CG  . GLN B 7   ? 1.1933 1.4697 1.1149 -0.4038 0.0706  0.1857  41  GLN B CG  
1754 C CD  . GLN B 7   ? 1.2482 1.4275 1.0674 -0.4172 0.0779  0.1862  41  GLN B CD  
1755 O OE1 . GLN B 7   ? 1.1927 1.3038 0.9273 -0.3955 0.0587  0.1718  41  GLN B OE1 
1756 N NE2 . GLN B 7   ? 1.2413 1.4132 1.0689 -0.4525 0.1068  0.2034  41  GLN B NE2 
1757 N N   . ARG B 8   ? 1.0040 1.3109 0.9695 -0.3946 -0.0612 0.1649  42  ARG B N   
1758 C CA  . ARG B 8   ? 1.0754 1.3295 0.9910 -0.4102 -0.1086 0.1572  42  ARG B CA  
1759 C C   . ARG B 8   ? 1.1675 1.3501 1.0229 -0.4451 -0.1077 0.1582  42  ARG B C   
1760 O O   . ARG B 8   ? 1.2021 1.4022 1.0949 -0.4776 -0.0850 0.1706  42  ARG B O   
1761 C CB  . ARG B 8   ? 1.0135 1.3279 1.0059 -0.4282 -0.1491 0.1615  42  ARG B CB  
1762 C CG  . ARG B 8   ? 0.9956 1.3802 1.0510 -0.3931 -0.1529 0.1634  42  ARG B CG  
1763 C CD  . ARG B 8   ? 1.0681 1.5445 1.2294 -0.3949 -0.1199 0.1755  42  ARG B CD  
1764 N NE  . ARG B 8   ? 1.0447 1.5599 1.2719 -0.4435 -0.1245 0.1845  42  ARG B NE  
1765 C CZ  . ARG B 8   ? 0.9591 1.5012 1.2255 -0.4644 -0.0797 0.1947  42  ARG B CZ  
1766 N NH1 . ARG B 8   ? 0.7715 1.3035 1.0113 -0.4386 -0.0292 0.1965  42  ARG B NH1 
1767 N NH2 . ARG B 8   ? 0.9728 1.5506 1.3049 -0.5131 -0.0852 0.2028  42  ARG B NH2 
1768 N N   . PHE B 9   ? 1.1356 1.2346 0.8961 -0.4375 -0.1301 0.1454  43  PHE B N   
1769 C CA  . PHE B 9   ? 1.0733 1.0896 0.7633 -0.4655 -0.1340 0.1444  43  PHE B CA  
1770 C C   . PHE B 9   ? 1.0928 1.0496 0.7202 -0.4667 -0.1813 0.1302  43  PHE B C   
1771 O O   . PHE B 9   ? 1.2113 1.1228 0.7691 -0.4323 -0.1857 0.1169  43  PHE B O   
1772 C CB  . PHE B 9   ? 1.0369 0.9971 0.6533 -0.4425 -0.0978 0.1421  43  PHE B CB  
1773 C CG  . PHE B 9   ? 1.2564 1.1257 0.7958 -0.4672 -0.0994 0.1434  43  PHE B CG  
1774 C CD1 . PHE B 9   ? 1.2734 1.1417 0.8439 -0.5144 -0.0882 0.1595  43  PHE B CD1 
1775 C CD2 . PHE B 9   ? 1.2008 0.9850 0.6391 -0.4431 -0.1108 0.1288  43  PHE B CD2 
1776 C CE1 . PHE B 9   ? 1.2990 1.0735 0.7934 -0.5378 -0.0886 0.1621  43  PHE B CE1 
1777 C CE2 . PHE B 9   ? 1.3489 1.0427 0.7118 -0.4620 -0.1132 0.1302  43  PHE B CE2 
1778 C CZ  . PHE B 9   ? 1.3605 1.0448 0.7477 -0.5098 -0.1023 0.1475  43  PHE B CZ  
1779 N N   . GLY B 10  ? 1.1820 1.1399 0.8356 -0.5064 -0.2160 0.1318  44  GLY B N   
1780 C CA  . GLY B 10  ? 1.2628 1.1665 0.8577 -0.5079 -0.2637 0.1174  44  GLY B CA  
1781 C C   . GLY B 10  ? 1.1765 1.1216 0.7874 -0.4747 -0.2855 0.1117  44  GLY B C   
1782 O O   . GLY B 10  ? 1.2038 1.2298 0.9014 -0.4788 -0.2962 0.1195  44  GLY B O   
1783 N N   . ASP B 11  ? 1.2117 1.1012 0.7396 -0.4403 -0.2909 0.0987  45  ASP B N   
1784 C CA  . ASP B 11  ? 1.1621 1.0775 0.6909 -0.4061 -0.3040 0.0949  45  ASP B CA  
1785 C C   . ASP B 11  ? 1.1807 1.1174 0.7129 -0.3657 -0.2633 0.0951  45  ASP B C   
1786 O O   . ASP B 11  ? 1.2264 1.1590 0.7378 -0.3327 -0.2641 0.0896  45  ASP B O   
1787 C CB  . ASP B 11  ? 1.2615 1.1043 0.7301 -0.3783 -0.3151 0.0805  45  ASP B CB  
1788 C CG  . ASP B 11  ? 1.4051 1.2049 0.8570 -0.4104 -0.3444 0.0770  45  ASP B CG  
1789 O OD1 . ASP B 11  ? 1.2968 1.1390 0.8006 -0.4360 -0.3764 0.0818  45  ASP B OD1 
1790 O OD2 . ASP B 11  ? 1.5035 1.2287 0.8955 -0.4075 -0.3355 0.0687  45  ASP B OD2 
1791 N N   . LEU B 12  ? 1.1704 1.1264 0.7298 -0.3665 -0.2250 0.1008  46  LEU B N   
1792 C CA  . LEU B 12  ? 1.0602 1.0290 0.6172 -0.3302 -0.1886 0.0972  46  LEU B CA  
1793 C C   . LEU B 12  ? 1.0556 1.1014 0.6995 -0.3301 -0.1600 0.1098  46  LEU B C   
1794 O O   . LEU B 12  ? 1.0985 1.1741 0.7906 -0.3603 -0.1548 0.1214  46  LEU B O   
1795 C CB  . LEU B 12  ? 1.1400 1.0436 0.6239 -0.3212 -0.1688 0.0870  46  LEU B CB  
1796 C CG  . LEU B 12  ? 1.1481 0.9711 0.5581 -0.3189 -0.1890 0.0736  46  LEU B CG  
1797 C CD1 . LEU B 12  ? 1.1212 0.8922 0.4929 -0.3001 -0.1635 0.0639  46  LEU B CD1 
1798 C CD2 . LEU B 12  ? 0.9837 0.8035 0.4049 -0.2787 -0.1901 0.0607  46  LEU B CD2 
1799 N N   . VAL B 13  ? 0.9645 1.0407 0.6286 -0.2962 -0.1394 0.1069  47  VAL B N   
1800 C CA  . VAL B 13  ? 0.9430 1.0852 0.6795 -0.2869 -0.1087 0.1154  47  VAL B CA  
1801 C C   . VAL B 13  ? 0.8741 0.9920 0.5738 -0.2636 -0.0732 0.1054  47  VAL B C   
1802 O O   . VAL B 13  ? 1.0015 1.0801 0.6492 -0.2401 -0.0737 0.0907  47  VAL B O   
1803 C CB  . VAL B 13  ? 0.9604 1.1552 0.7519 -0.2650 -0.1164 0.1194  47  VAL B CB  
1804 C CG1 . VAL B 13  ? 0.8696 1.1285 0.7330 -0.2516 -0.0830 0.1262  47  VAL B CG1 
1805 C CG2 . VAL B 13  ? 0.7472 0.9643 0.5691 -0.2846 -0.1580 0.1279  47  VAL B CG2 
1806 N N   . PHE B 14  ? 0.9268 1.0688 0.6534 -0.2697 -0.0426 0.1124  48  PHE B N   
1807 C CA  . PHE B 14  ? 0.9343 1.0519 0.6215 -0.2474 -0.0113 0.1027  48  PHE B CA  
1808 C C   . PHE B 14  ? 0.8768 1.0544 0.6247 -0.2284 0.0196  0.1057  48  PHE B C   
1809 O O   . PHE B 14  ? 0.9099 1.1426 0.7250 -0.2436 0.0301  0.1207  48  PHE B O   
1810 C CB  . PHE B 14  ? 0.9149 0.9865 0.5531 -0.2682 0.0003  0.1079  48  PHE B CB  
1811 C CG  . PHE B 14  ? 0.9929 0.9901 0.5545 -0.2775 -0.0263 0.1004  48  PHE B CG  
1812 C CD1 . PHE B 14  ? 1.0647 1.0494 0.6302 -0.3090 -0.0565 0.1072  48  PHE B CD1 
1813 C CD2 . PHE B 14  ? 1.0436 0.9836 0.5299 -0.2528 -0.0230 0.0845  48  PHE B CD2 
1814 C CE1 . PHE B 14  ? 1.0852 0.9959 0.5753 -0.3150 -0.0802 0.0986  48  PHE B CE1 
1815 C CE2 . PHE B 14  ? 1.0743 0.9461 0.4909 -0.2571 -0.0463 0.0766  48  PHE B CE2 
1816 C CZ  . PHE B 14  ? 1.1419 0.9962 0.5576 -0.2878 -0.0736 0.0838  48  PHE B CZ  
1817 N N   . ARG B 15  ? 0.7958 0.9635 0.5229 -0.1952 0.0338  0.0898  49  ARG B N   
1818 C CA  . ARG B 15  ? 0.7688 0.9803 0.5398 -0.1726 0.0635  0.0880  49  ARG B CA  
1819 C C   . ARG B 15  ? 0.8381 1.0123 0.5517 -0.1506 0.0850  0.0714  49  ARG B C   
1820 O O   . ARG B 15  ? 0.9444 1.0758 0.6069 -0.1365 0.0723  0.0535  49  ARG B O   
1821 C CB  . ARG B 15  ? 0.8613 1.1015 0.6744 -0.1511 0.0549  0.0830  49  ARG B CB  
1822 C CG  . ARG B 15  ? 0.9087 1.2111 0.7954 -0.1380 0.0768  0.0908  49  ARG B CG  
1823 C CD  . ARG B 15  ? 0.9222 1.2277 0.8232 -0.1064 0.0800  0.0786  49  ARG B CD  
1824 N NE  . ARG B 15  ? 1.0945 1.4323 1.0467 -0.1041 0.0604  0.0908  49  ARG B NE  
1825 C CZ  . ARG B 15  ? 1.0946 1.4892 1.1171 -0.0949 0.0691  0.1022  49  ARG B CZ  
1826 N NH1 . ARG B 15  ? 0.9121 1.3408 0.9656 -0.0884 0.1012  0.1032  49  ARG B NH1 
1827 N NH2 . ARG B 15  ? 1.0735 1.4903 1.1334 -0.0894 0.0455  0.1129  49  ARG B NH2 
1828 N N   . GLN B 16  ? 0.8468 1.0388 0.5689 -0.1465 0.1172  0.0764  50  GLN B N   
1829 C CA  . GLN B 16  ? 0.8565 1.0130 0.5194 -0.1230 0.1369  0.0608  50  GLN B CA  
1830 C C   . GLN B 16  ? 0.9192 1.1002 0.6094 -0.0903 0.1485  0.0432  50  GLN B C   
1831 O O   . GLN B 16  ? 0.9354 1.1639 0.6811 -0.0836 0.1703  0.0505  50  GLN B O   
1832 C CB  . GLN B 16  ? 0.8527 1.0064 0.4979 -0.1342 0.1684  0.0759  50  GLN B CB  
1833 C CG  . GLN B 16  ? 0.9719 1.0889 0.5502 -0.1057 0.1897  0.0608  50  GLN B CG  
1834 C CD  . GLN B 16  ? 1.0701 1.1729 0.6166 -0.1179 0.2237  0.0793  50  GLN B CD  
1835 O OE1 . GLN B 16  ? 1.0391 1.1913 0.6446 -0.1333 0.2506  0.0982  50  GLN B OE1 
1836 N NE2 . GLN B 16  ? 1.0186 1.0538 0.4720 -0.1098 0.2237  0.0745  50  GLN B NE2 
1837 N N   . LEU B 17  ? 0.8721 1.0209 0.5266 -0.0701 0.1344  0.0191  51  LEU B N   
1838 C CA  . LEU B 17  ? 0.8858 1.0488 0.5639 -0.0424 0.1424  -0.0006 51  LEU B CA  
1839 C C   . LEU B 17  ? 0.9651 1.1096 0.6010 -0.0180 0.1628  -0.0188 51  LEU B C   
1840 O O   . LEU B 17  ? 1.0403 1.2002 0.7000 0.0039  0.1759  -0.0331 51  LEU B O   
1841 C CB  . LEU B 17  ? 0.8484 0.9912 0.5208 -0.0363 0.1179  -0.0186 51  LEU B CB  
1842 C CG  . LEU B 17  ? 0.8449 0.9797 0.5184 -0.0586 0.0927  -0.0054 51  LEU B CG  
1843 C CD1 . LEU B 17  ? 0.9083 1.0166 0.5622 -0.0499 0.0757  -0.0257 51  LEU B CD1 
1844 C CD2 . LEU B 17  ? 0.8381 1.0144 0.5745 -0.0702 0.0904  0.0163  51  LEU B CD2 
1845 N N   . ALA B 18  ? 1.0206 1.1270 0.5893 -0.0196 0.1647  -0.0188 52  ALA B N   
1846 C CA  . ALA B 18  ? 1.1061 1.1866 0.6190 0.0057  0.1810  -0.0353 52  ALA B CA  
1847 C C   . ALA B 18  ? 1.2522 1.2917 0.6995 -0.0023 0.1824  -0.0213 52  ALA B C   
1848 O O   . ALA B 18  ? 1.2577 1.2778 0.6947 -0.0236 0.1640  -0.0085 52  ALA B O   
1849 C CB  . ALA B 18  ? 1.0715 1.1246 0.5674 0.0287  0.1590  -0.0705 52  ALA B CB  
1850 N N   . PRO B 19  ? 1.1249 1.1573 0.5463 0.0107  0.1972  -0.0238 53  PRO B N   
1851 C CA  . PRO B 19  ? 1.0870 1.0817 0.4596 0.0067  0.1902  -0.0124 53  PRO B CA  
1852 C C   . PRO B 19  ? 1.3108 1.2775 0.6687 0.0127  0.1479  -0.0297 53  PRO B C   
1853 O O   . PRO B 19  ? 1.3822 1.3516 0.7550 0.0258  0.1279  -0.0587 53  PRO B O   
1854 C CB  . PRO B 19  ? 1.0768 1.0636 0.4233 0.0239  0.2090  -0.0212 53  PRO B CB  
1855 C CG  . PRO B 19  ? 1.0319 1.0499 0.4166 0.0375  0.2246  -0.0389 53  PRO B CG  
1856 C CD  . PRO B 19  ? 1.0510 1.1021 0.4869 0.0266  0.2259  -0.0332 53  PRO B CD  
1857 N N   . ASN B 20  ? 1.3488 1.2853 0.6835 -0.0009 0.1374  -0.0117 54  ASN B N   
1858 C CA  . ASN B 20  ? 1.3750 1.2879 0.7037 0.0037  0.1019  -0.0238 54  ASN B CA  
1859 C C   . ASN B 20  ? 1.2916 1.2289 0.6651 0.0016  0.0815  -0.0365 54  ASN B C   
1860 O O   . ASN B 20  ? 1.2785 1.2122 0.6640 0.0085  0.0563  -0.0536 54  ASN B O   
1861 C CB  . ASN B 20  ? 1.3404 1.2366 0.6504 0.0248  0.0871  -0.0464 54  ASN B CB  
1862 C CG  . ASN B 20  ? 1.5134 1.3727 0.7672 0.0308  0.1037  -0.0328 54  ASN B CG  
1863 O OD1 . ASN B 20  ? 1.5310 1.3922 0.7703 0.0206  0.1349  -0.0117 54  ASN B OD1 
1864 N ND2 . ASN B 20  ? 1.5693 1.3937 0.7917 0.0473  0.0856  -0.0432 54  ASN B ND2 
1865 N N   . VAL B 21  ? 1.0960 0.9880 0.7249 -0.2073 0.1742  0.0074  55  VAL B N   
1866 C CA  . VAL B 21  ? 1.0579 0.9307 0.7097 -0.1796 0.1636  -0.0010 55  VAL B CA  
1867 C C   . VAL B 21  ? 0.9843 0.8813 0.6844 -0.1687 0.1640  0.0048  55  VAL B C   
1868 O O   . VAL B 21  ? 0.9421 0.8739 0.6656 -0.1660 0.1895  0.0005  55  VAL B O   
1869 C CB  . VAL B 21  ? 1.0027 0.8657 0.6471 -0.1627 0.1835  -0.0235 55  VAL B CB  
1870 C CG1 . VAL B 21  ? 0.9272 0.7800 0.6029 -0.1360 0.1744  -0.0286 55  VAL B CG1 
1871 C CG2 . VAL B 21  ? 1.0187 0.8569 0.6152 -0.1742 0.1772  -0.0278 55  VAL B CG2 
1872 N N   . TRP B 22  ? 0.9739 0.8553 0.6888 -0.1617 0.1362  0.0140  56  TRP B N   
1873 C CA  . TRP B 22  ? 0.8980 0.8009 0.6568 -0.1527 0.1323  0.0202  56  TRP B CA  
1874 C C   . TRP B 22  ? 0.8822 0.7669 0.6562 -0.1277 0.1172  0.0133  56  TRP B C   
1875 O O   . TRP B 22  ? 0.9353 0.7902 0.6845 -0.1209 0.1030  0.0080  56  TRP B O   
1876 C CB  . TRP B 22  ? 0.9231 0.8283 0.6836 -0.1754 0.1104  0.0410  56  TRP B CB  
1877 C CG  . TRP B 22  ? 0.9277 0.8671 0.6862 -0.2013 0.1268  0.0520  56  TRP B CG  
1878 C CD1 . TRP B 22  ? 0.8632 0.8528 0.6568 -0.2054 0.1449  0.0579  56  TRP B CD1 
1879 C CD2 . TRP B 22  ? 1.0047 0.9373 0.7244 -0.2273 0.1267  0.0602  56  TRP B CD2 
1880 N NE1 . TRP B 22  ? 0.9090 0.9262 0.6877 -0.2328 0.1569  0.0686  56  TRP B NE1 
1881 C CE2 . TRP B 22  ? 0.9532 0.9346 0.6855 -0.2477 0.1457  0.0705  56  TRP B CE2 
1882 C CE3 . TRP B 22  ? 0.9541 0.8487 0.6304 -0.2356 0.1119  0.0615  56  TRP B CE3 
1883 C CZ2 . TRP B 22  ? 1.0062 0.9985 0.7074 -0.2779 0.1502  0.0819  56  TRP B CZ2 
1884 C CZ3 . TRP B 22  ? 1.1211 1.0237 0.7672 -0.2648 0.1155  0.0736  56  TRP B CZ3 
1885 C CH2 . TRP B 22  ? 1.1468 1.0974 0.8044 -0.2866 0.1345  0.0836  56  TRP B CH2 
1886 N N   . GLN B 23  ? 0.7966 0.7052 0.6124 -0.1147 0.1203  0.0148  57  GLN B N   
1887 C CA  . GLN B 23  ? 0.7882 0.6878 0.6224 -0.0927 0.1065  0.0104  57  GLN B CA  
1888 C C   . GLN B 23  ? 0.8770 0.7896 0.7376 -0.0964 0.0865  0.0231  57  GLN B C   
1889 O O   . GLN B 23  ? 0.8348 0.7835 0.7286 -0.0999 0.0974  0.0308  57  GLN B O   
1890 C CB  . GLN B 23  ? 0.7771 0.6911 0.6360 -0.0713 0.1295  -0.0005 57  GLN B CB  
1891 C CG  . GLN B 23  ? 0.7338 0.6405 0.6091 -0.0511 0.1151  -0.0029 57  GLN B CG  
1892 C CD  . GLN B 23  ? 0.7737 0.6988 0.6840 -0.0314 0.1343  -0.0072 57  GLN B CD  
1893 O OE1 . GLN B 23  ? 0.7332 0.6407 0.6369 -0.0184 0.1384  -0.0161 57  GLN B OE1 
1894 N NE2 . GLN B 23  ? 0.7561 0.7172 0.7040 -0.0295 0.1450  0.0008  57  GLN B NE2 
1895 N N   . HIS B 24  ? 0.7680 0.6528 0.6130 -0.0953 0.0574  0.0248  58  HIS B N   
1896 C CA  . HIS B 24  ? 0.7871 0.6767 0.6507 -0.0990 0.0355  0.0337  58  HIS B CA  
1897 C C   . HIS B 24  ? 0.7396 0.6406 0.6288 -0.0761 0.0307  0.0278  58  HIS B C   
1898 O O   . HIS B 24  ? 0.7824 0.6691 0.6592 -0.0592 0.0284  0.0177  58  HIS B O   
1899 C CB  . HIS B 24  ? 0.8083 0.6570 0.6378 -0.1100 0.0053  0.0373  58  HIS B CB  
1900 C CG  . HIS B 24  ? 0.8456 0.6641 0.6496 -0.0909 -0.0088 0.0259  58  HIS B CG  
1901 N ND1 . HIS B 24  ? 0.8133 0.6303 0.6261 -0.0719 -0.0244 0.0190  58  HIS B ND1 
1902 C CD2 . HIS B 24  ? 0.8445 0.6393 0.6145 -0.0886 -0.0100 0.0214  58  HIS B CD2 
1903 C CE1 . HIS B 24  ? 0.7267 0.5230 0.5132 -0.0576 -0.0335 0.0104  58  HIS B CE1 
1904 N NE2 . HIS B 24  ? 0.7298 0.5124 0.4910 -0.0673 -0.0255 0.0123  58  HIS B NE2 
1905 N N   . THR B 25  ? 0.7123 0.6439 0.6374 -0.0776 0.0285  0.0363  59  THR B N   
1906 C CA  . THR B 25  ? 0.7107 0.6605 0.6640 -0.0588 0.0238  0.0345  59  THR B CA  
1907 C C   . THR B 25  ? 0.8595 0.8081 0.8167 -0.0674 -0.0043 0.0405  59  THR B C   
1908 O O   . THR B 25  ? 0.7747 0.7380 0.7436 -0.0876 -0.0089 0.0524  59  THR B O   
1909 C CB  . THR B 25  ? 0.6777 0.6704 0.6745 -0.0497 0.0487  0.0396  59  THR B CB  
1910 O OG1 . THR B 25  ? 0.6170 0.6025 0.6048 -0.0403 0.0740  0.0302  59  THR B OG1 
1911 C CG2 . THR B 25  ? 0.6363 0.6486 0.6630 -0.0322 0.0409  0.0416  59  THR B CG2 
1912 N N   . SER B 26  ? 0.7733 0.7063 0.7191 -0.0535 -0.0231 0.0322  60  SER B N   
1913 C CA  . SER B 26  ? 0.7247 0.6529 0.6692 -0.0587 -0.0504 0.0335  60  SER B CA  
1914 C C   . SER B 26  ? 0.7303 0.6901 0.7028 -0.0423 -0.0528 0.0330  60  SER B C   
1915 O O   . SER B 26  ? 0.7338 0.7036 0.7136 -0.0239 -0.0405 0.0287  60  SER B O   
1916 C CB  . SER B 26  ? 0.6371 0.5165 0.5366 -0.0564 -0.0739 0.0223  60  SER B CB  
1917 O OG  . SER B 26  ? 0.9001 0.7758 0.7877 -0.0326 -0.0744 0.0103  60  SER B OG  
1918 N N   . PHE B 27  ? 0.7321 0.7073 0.7185 -0.0516 -0.0703 0.0389  61  PHE B N   
1919 C CA  . PHE B 27  ? 0.7321 0.7440 0.7478 -0.0406 -0.0743 0.0424  61  PHE B CA  
1920 C C   . PHE B 27  ? 0.6478 0.6429 0.6389 -0.0384 -0.1030 0.0318  61  PHE B C   
1921 O O   . PHE B 27  ? 0.7132 0.6686 0.6704 -0.0486 -0.1215 0.0240  61  PHE B O   
1922 C CB  . PHE B 27  ? 0.5877 0.6464 0.6477 -0.0534 -0.0678 0.0607  61  PHE B CB  
1923 C CG  . PHE B 27  ? 0.6108 0.6885 0.6935 -0.0553 -0.0394 0.0695  61  PHE B CG  
1924 C CD1 . PHE B 27  ? 0.7102 0.7795 0.7825 -0.0773 -0.0363 0.0749  61  PHE B CD1 
1925 C CD2 . PHE B 27  ? 0.6681 0.7712 0.7805 -0.0351 -0.0163 0.0723  61  PHE B CD2 
1926 C CE1 . PHE B 27  ? 0.6445 0.7373 0.7360 -0.0782 -0.0087 0.0815  61  PHE B CE1 
1927 C CE2 . PHE B 27  ? 0.6760 0.7953 0.8066 -0.0337 0.0110  0.0769  61  PHE B CE2 
1928 C CZ  . PHE B 27  ? 0.6487 0.7663 0.7690 -0.0548 0.0157  0.0808  61  PHE B CZ  
1929 N N   . MET B 28  ? 0.5699 0.5945 0.5770 -0.0246 -0.1070 0.0315  62  MET B N   
1930 C CA  . MET B 28  ? 0.6780 0.6947 0.6617 -0.0196 -0.1318 0.0193  62  MET B CA  
1931 C C   . MET B 28  ? 0.6105 0.6776 0.6260 -0.0137 -0.1341 0.0280  62  MET B C   
1932 O O   . MET B 28  ? 0.5142 0.6089 0.5560 -0.0014 -0.1173 0.0367  62  MET B O   
1933 C CB  . MET B 28  ? 0.6635 0.6503 0.6094 -0.0005 -0.1353 0.0016  62  MET B CB  
1934 C CG  . MET B 28  ? 0.7526 0.7517 0.6833 0.0137  -0.1530 -0.0106 62  MET B CG  
1935 S SD  . MET B 28  ? 0.8354 0.8016 0.7327 0.0038  -0.1843 -0.0254 62  MET B SD  
1936 C CE  . MET B 28  ? 0.7024 0.6028 0.5527 0.0121  -0.1899 -0.0410 62  MET B CE  
1937 N N   . ASP B 29  ? 0.7300 0.8062 0.7408 -0.0236 -0.1562 0.0260  63  ASP B N   
1938 C CA  . ASP B 29  ? 0.6634 0.7890 0.6995 -0.0203 -0.1625 0.0345  63  ASP B CA  
1939 C C   . ASP B 29  ? 0.6486 0.7774 0.6626 0.0005  -0.1677 0.0208  63  ASP B C   
1940 O O   . ASP B 29  ? 0.8242 0.9303 0.7997 0.0045  -0.1856 0.0015  63  ASP B O   
1941 C CB  . ASP B 29  ? 0.7024 0.8366 0.7361 -0.0415 -0.1855 0.0361  63  ASP B CB  
1942 C CG  . ASP B 29  ? 0.7183 0.9145 0.8000 -0.0493 -0.1840 0.0590  63  ASP B CG  
1943 O OD1 . ASP B 29  ? 0.7431 0.9734 0.8549 -0.0334 -0.1694 0.0706  63  ASP B OD1 
1944 O OD2 . ASP B 29  ? 0.8463 1.0566 0.9354 -0.0721 -0.1987 0.0668  63  ASP B OD2 
1945 N N   . VAL B 30  ? 0.6075 0.7643 0.6444 0.0139  -0.1524 0.0309  64  VAL B N   
1946 C CA  . VAL B 30  ? 0.5234 0.6932 0.5435 0.0308  -0.1557 0.0228  64  VAL B CA  
1947 C C   . VAL B 30  ? 0.5580 0.7813 0.6026 0.0295  -0.1648 0.0359  64  VAL B C   
1948 O O   . VAL B 30  ? 0.6203 0.8725 0.7071 0.0250  -0.1560 0.0577  64  VAL B O   
1949 C CB  . VAL B 30  ? 0.5959 0.7576 0.6200 0.0426  -0.1353 0.0268  64  VAL B CB  
1950 C CG1 . VAL B 30  ? 0.4928 0.6805 0.5061 0.0554  -0.1396 0.0247  64  VAL B CG1 
1951 C CG2 . VAL B 30  ? 0.5333 0.6456 0.5279 0.0434  -0.1286 0.0134  64  VAL B CG2 
1952 N N   . PRO B 31  ? 0.5726 0.8126 0.5924 0.0341  -0.1822 0.0237  65  PRO B N   
1953 C CA  . PRO B 31  ? 0.4969 0.7922 0.5379 0.0304  -0.1920 0.0374  65  PRO B CA  
1954 C C   . PRO B 31  ? 0.4311 0.7575 0.5024 0.0382  -0.1788 0.0586  65  PRO B C   
1955 O O   . PRO B 31  ? 0.4397 0.7550 0.4970 0.0496  -0.1696 0.0542  65  PRO B O   
1956 C CB  . PRO B 31  ? 0.4821 0.7841 0.4809 0.0374  -0.2101 0.0145  65  PRO B CB  
1957 C CG  . PRO B 31  ? 0.5143 0.7576 0.4741 0.0407  -0.2145 -0.0105 65  PRO B CG  
1958 C CD  . PRO B 31  ? 0.5012 0.7112 0.4718 0.0433  -0.1946 -0.0038 65  PRO B CD  
1959 N N   . GLY B 32  ? 0.4859 0.8509 0.5986 0.0310  -0.1793 0.0832  66  GLY B N   
1960 C CA  . GLY B 32  ? 0.4301 0.8187 0.5748 0.0375  -0.1689 0.1066  66  GLY B CA  
1961 C C   . GLY B 32  ? 0.4606 0.8232 0.6348 0.0420  -0.1472 0.1180  66  GLY B C   
1962 O O   . GLY B 32  ? 0.3802 0.7605 0.5891 0.0469  -0.1400 0.1404  66  GLY B O   
1963 N N   . PHE B 33  ? 0.4865 0.8073 0.6468 0.0408  -0.1371 0.1033  67  PHE B N   
1964 C CA  . PHE B 33  ? 0.5061 0.8024 0.6881 0.0456  -0.1146 0.1098  67  PHE B CA  
1965 C C   . PHE B 33  ? 0.5354 0.8329 0.7392 0.0360  -0.1099 0.1142  67  PHE B C   
1966 O O   . PHE B 33  ? 0.5670 0.8697 0.8057 0.0412  -0.0928 0.1278  67  PHE B O   
1967 C CB  . PHE B 33  ? 0.5213 0.7703 0.6674 0.0512  -0.1032 0.0910  67  PHE B CB  
1968 C CG  . PHE B 33  ? 0.5464 0.7949 0.6786 0.0597  -0.1018 0.0918  67  PHE B CG  
1969 C CD1 . PHE B 33  ? 0.5959 0.8686 0.7058 0.0604  -0.1187 0.0870  67  PHE B CD1 
1970 C CD2 . PHE B 33  ? 0.4878 0.7127 0.6271 0.0658  -0.0838 0.0970  67  PHE B CD2 
1971 C CE1 . PHE B 33  ? 0.4652 0.7445 0.5629 0.0650  -0.1181 0.0905  67  PHE B CE1 
1972 C CE2 . PHE B 33  ? 0.5817 0.8052 0.7062 0.0691  -0.0845 0.0996  67  PHE B CE2 
1973 C CZ  . PHE B 33  ? 0.5145 0.7680 0.6195 0.0677  -0.1019 0.0979  67  PHE B CZ  
1974 N N   . GLY B 34  ? 0.5382 0.8314 0.7214 0.0220  -0.1250 0.1033  68  GLY B N   
1975 C CA  . GLY B 34  ? 0.4318 0.7231 0.6292 0.0082  -0.1218 0.1073  68  GLY B CA  
1976 C C   . GLY B 34  ? 0.5122 0.7530 0.6790 0.0057  -0.1118 0.0905  68  GLY B C   
1977 O O   . GLY B 34  ? 0.5497 0.7556 0.6749 0.0105  -0.1173 0.0716  68  GLY B O   
1978 N N   . ALA B 35  ? 0.5412 0.7820 0.7287 -0.0015 -0.0972 0.0985  69  ALA B N   
1979 C CA  . ALA B 35  ? 0.5301 0.7272 0.6900 -0.0064 -0.0872 0.0858  69  ALA B CA  
1980 C C   . ALA B 35  ? 0.4757 0.6492 0.6273 0.0113  -0.0667 0.0792  69  ALA B C   
1981 O O   . ALA B 35  ? 0.6110 0.8024 0.7948 0.0231  -0.0486 0.0901  69  ALA B O   
1982 C CB  . ALA B 35  ? 0.4759 0.6897 0.6610 -0.0218 -0.0775 0.0982  69  ALA B CB  
1983 N N   . VAL B 36  ? 0.4670 0.5994 0.5748 0.0134  -0.0706 0.0614  70  VAL B N   
1984 C CA  . VAL B 36  ? 0.5559 0.6640 0.6488 0.0257  -0.0541 0.0542  70  VAL B CA  
1985 C C   . VAL B 36  ? 0.6415 0.7132 0.7084 0.0169  -0.0452 0.0450  70  VAL B C   
1986 O O   . VAL B 36  ? 0.6037 0.6526 0.6422 0.0066  -0.0606 0.0369  70  VAL B O   
1987 C CB  . VAL B 36  ? 0.5466 0.6477 0.6114 0.0361  -0.0665 0.0443  70  VAL B CB  
1988 C CG1 . VAL B 36  ? 0.4554 0.5316 0.5016 0.0441  -0.0513 0.0379  70  VAL B CG1 
1989 C CG2 . VAL B 36  ? 0.4795 0.6210 0.5696 0.0424  -0.0752 0.0560  70  VAL B CG2 
1990 N N   . SER B 37  ? 0.6248 0.6890 0.6995 0.0208  -0.0213 0.0463  71  SER B N   
1991 C CA  . SER B 37  ? 0.6127 0.6484 0.6641 0.0111  -0.0103 0.0396  71  SER B CA  
1992 C C   . SER B 37  ? 0.6520 0.6542 0.6656 0.0174  -0.0077 0.0268  71  SER B C   
1993 O O   . SER B 37  ? 0.6250 0.6293 0.6390 0.0296  -0.0040 0.0253  71  SER B O   
1994 C CB  . SER B 37  ? 0.5524 0.6048 0.6328 0.0106  0.0158  0.0471  71  SER B CB  
1995 O OG  . SER B 37  ? 0.7689 0.8057 0.8436 0.0231  0.0355  0.0407  71  SER B OG  
1996 N N   . SER B 38  ? 0.7542 0.7269 0.7347 0.0071  -0.0109 0.0197  72  SER B N   
1997 C CA  . SER B 38  ? 0.6949 0.6390 0.6385 0.0108  -0.0094 0.0094  72  SER B CA  
1998 C C   . SER B 38  ? 0.7218 0.6454 0.6480 -0.0028 0.0038  0.0083  72  SER B C   
1999 O O   . SER B 38  ? 0.7617 0.6802 0.6855 -0.0172 -0.0026 0.0128  72  SER B O   
2000 C CB  . SER B 38  ? 0.7139 0.6436 0.6281 0.0157  -0.0344 0.0015  72  SER B CB  
2001 O OG  . SER B 38  ? 0.8304 0.7375 0.7105 0.0186  -0.0335 -0.0059 72  SER B OG  
2002 N N   . ASN B 39  ? 0.6909 0.6029 0.6027 -0.0008 0.0210  0.0031  73  ASN B N   
2003 C CA  . ASN B 39  ? 0.7418 0.6394 0.6362 -0.0141 0.0366  0.0017  73  ASN B CA  
2004 C C   . ASN B 39  ? 0.7757 0.6446 0.6265 -0.0187 0.0266  -0.0041 73  ASN B C   
2005 O O   . ASN B 39  ? 0.7393 0.6027 0.5746 -0.0087 0.0198  -0.0093 73  ASN B O   
2006 C CB  . ASN B 39  ? 0.6890 0.5928 0.5954 -0.0097 0.0648  -0.0017 73  ASN B CB  
2007 C CG  . ASN B 39  ? 0.7252 0.6598 0.6772 -0.0027 0.0773  0.0054  73  ASN B CG  
2008 O OD1 . ASN B 39  ? 0.7301 0.6848 0.7007 -0.0116 0.0759  0.0138  73  ASN B OD1 
2009 N ND2 . ASN B 39  ? 0.7692 0.7081 0.7396 0.0127  0.0885  0.0036  73  ASN B ND2 
2010 N N   . GLY B 40  ? 0.7046 0.5589 0.5366 -0.0348 0.0249  -0.0008 74  GLY B N   
2011 C CA  . GLY B 40  ? 0.7533 0.5824 0.5453 -0.0411 0.0195  -0.0035 74  GLY B CA  
2012 C C   . GLY B 40  ? 0.8067 0.6339 0.5873 -0.0594 0.0394  -0.0011 74  GLY B C   
2013 O O   . GLY B 40  ? 0.8336 0.6812 0.6381 -0.0640 0.0590  0.0006  74  GLY B O   
2014 N N   . LEU B 41  ? 0.8230 0.6296 0.5672 -0.0688 0.0340  -0.0006 75  LEU B N   
2015 C CA  . LEU B 41  ? 0.8225 0.6292 0.5495 -0.0879 0.0524  0.0013  75  LEU B CA  
2016 C C   . LEU B 41  ? 0.9592 0.7461 0.6593 -0.1054 0.0351  0.0125  75  LEU B C   
2017 O O   . LEU B 41  ? 0.9160 0.6804 0.5985 -0.0988 0.0105  0.0150  75  LEU B O   
2018 C CB  . LEU B 41  ? 0.7987 0.6014 0.5032 -0.0865 0.0678  -0.0087 75  LEU B CB  
2019 C CG  . LEU B 41  ? 0.8599 0.6743 0.5855 -0.0737 0.0882  -0.0194 75  LEU B CG  
2020 C CD1 . LEU B 41  ? 0.7657 0.5685 0.4606 -0.0790 0.1017  -0.0292 75  LEU B CD1 
2021 C CD2 . LEU B 41  ? 0.9350 0.7710 0.6922 -0.0747 0.1092  -0.0191 75  LEU B CD2 
2022 N N   . ILE B 42  ? 0.9717 0.7684 0.6689 -0.1270 0.0483  0.0200  76  ILE B N   
2023 C CA  . ILE B 42  ? 1.0263 0.8055 0.6961 -0.1491 0.0344  0.0339  76  ILE B CA  
2024 C C   . ILE B 42  ? 0.9907 0.7819 0.6378 -0.1666 0.0573  0.0332  76  ILE B C   
2025 O O   . ILE B 42  ? 1.0166 0.8371 0.6790 -0.1735 0.0835  0.0298  76  ILE B O   
2026 C CB  . ILE B 42  ? 1.1082 0.8921 0.7953 -0.1654 0.0245  0.0480  76  ILE B CB  
2027 C CG1 . ILE B 42  ? 1.0392 0.8155 0.7501 -0.1489 0.0049  0.0457  76  ILE B CG1 
2028 C CG2 . ILE B 42  ? 1.1306 0.8879 0.7862 -0.1889 0.0048  0.0648  76  ILE B CG2 
2029 C CD1 . ILE B 42  ? 1.0704 0.8765 0.8171 -0.1582 0.0112  0.0527  76  ILE B CD1 
2030 N N   . VAL B 43  ? 1.0034 0.7750 0.6138 -0.1729 0.0477  0.0362  77  VAL B N   
2031 C CA  . VAL B 43  ? 1.0163 0.7988 0.5993 -0.1911 0.0676  0.0347  77  VAL B CA  
2032 C C   . VAL B 43  ? 1.0721 0.8423 0.6265 -0.2164 0.0517  0.0546  77  VAL B C   
2033 O O   . VAL B 43  ? 1.1263 0.8683 0.6741 -0.2143 0.0219  0.0670  77  VAL B O   
2034 C CB  . VAL B 43  ? 1.1101 0.8861 0.6720 -0.1802 0.0729  0.0214  77  VAL B CB  
2035 C CG1 . VAL B 43  ? 0.9906 0.7706 0.5804 -0.1546 0.0789  0.0066  77  VAL B CG1 
2036 C CG2 . VAL B 43  ? 1.1383 0.8918 0.6721 -0.1792 0.0454  0.0315  77  VAL B CG2 
2037 N N   . LYS B 44  ? 1.1339 0.9244 0.6699 -0.2402 0.0715  0.0576  78  LYS B N   
2038 C CA  . LYS B 44  ? 1.1996 0.9851 0.7078 -0.2693 0.0594  0.0791  78  LYS B CA  
2039 C C   . LYS B 44  ? 1.2621 1.0475 0.7301 -0.2800 0.0651  0.0774  78  LYS B C   
2040 O O   . LYS B 44  ? 1.2921 1.0994 0.7519 -0.2826 0.0935  0.0609  78  LYS B O   
2041 C CB  . LYS B 44  ? 1.2476 1.0674 0.7679 -0.2936 0.0769  0.0880  78  LYS B CB  
2042 C CG  . LYS B 44  ? 1.2718 1.0888 0.7642 -0.3282 0.0626  0.1142  78  LYS B CG  
2043 C CD  . LYS B 44  ? 1.2516 1.1105 0.7602 -0.3531 0.0786  0.1252  78  LYS B CD  
2044 C CE  . LYS B 44  ? 1.3380 1.2392 0.8248 -0.3728 0.1102  0.1204  78  LYS B CE  
2045 N NZ  . LYS B 44  ? 1.3287 1.2854 0.8449 -0.3774 0.1407  0.1150  78  LYS B NZ  
2046 N N   . ASP B 45  ? 1.2391 0.9987 0.6811 -0.2859 0.0374  0.0942  79  ASP B N   
2047 C CA  . ASP B 45  ? 1.2974 1.0592 0.7001 -0.2991 0.0378  0.0978  79  ASP B CA  
2048 C C   . ASP B 45  ? 1.4335 1.1972 0.8108 -0.3328 0.0282  0.1238  79  ASP B C   
2049 O O   . ASP B 45  ? 1.4135 1.1534 0.7694 -0.3377 0.0004  0.1437  79  ASP B O   
2050 C CB  . ASP B 45  ? 1.2910 1.0288 0.6849 -0.2764 0.0134  0.0983  79  ASP B CB  
2051 C CG  . ASP B 45  ? 1.4195 1.1690 0.7785 -0.2863 0.0192  0.0962  79  ASP B CG  
2052 O OD1 . ASP B 45  ? 1.4280 1.2002 0.7686 -0.3086 0.0444  0.0892  79  ASP B OD1 
2053 O OD2 . ASP B 45  ? 1.4316 1.1701 0.7806 -0.2718 -0.0014 0.1011  79  ASP B OD2 
2054 N N   . GLY B 46  ? 1.5272 1.3222 0.9079 -0.3557 0.0512  0.1247  80  GLY B N   
2055 C CA  . GLY B 46  ? 1.5840 1.3899 0.9407 -0.3923 0.0453  0.1503  80  GLY B CA  
2056 C C   . GLY B 46  ? 1.6023 1.3803 0.9693 -0.4013 0.0139  0.1769  80  GLY B C   
2057 O O   . GLY B 46  ? 1.5580 1.3541 0.9453 -0.4154 0.0203  0.1837  80  GLY B O   
2058 N N   . GLU B 47  ? 1.7128 1.4463 1.0650 -0.3930 -0.0211 0.1922  81  GLU B N   
2059 C CA  . GLU B 47  ? 1.7523 1.4462 1.1058 -0.4022 -0.0554 0.2179  81  GLU B CA  
2060 C C   . GLU B 47  ? 1.7621 1.4114 1.1367 -0.3657 -0.0791 0.2084  81  GLU B C   
2061 O O   . GLU B 47  ? 1.6076 1.2091 0.9749 -0.3655 -0.1133 0.2265  81  GLU B O   
2062 C CB  . GLU B 47  ? 1.7097 1.3874 1.0345 -0.4197 -0.0802 0.2429  81  GLU B CB  
2063 N N   . ARG B 48  ? 1.5810 1.2434 0.9797 -0.3351 -0.0622 0.1802  82  ARG B N   
2064 C CA  . ARG B 48  ? 1.4539 1.0819 0.8716 -0.3003 -0.0822 0.1693  82  ARG B CA  
2065 C C   . ARG B 48  ? 1.3165 0.9732 0.7680 -0.2801 -0.0568 0.1427  82  ARG B C   
2066 O O   . ARG B 48  ? 1.2876 0.9844 0.7442 -0.2867 -0.0247 0.1304  82  ARG B O   
2067 C CB  . ARG B 48  ? 1.3386 0.9419 0.7375 -0.2750 -0.1022 0.1686  82  ARG B CB  
2068 C CG  . ARG B 48  ? 1.3259 0.9646 0.7158 -0.2682 -0.0793 0.1538  82  ARG B CG  
2069 C CD  . ARG B 48  ? 1.2499 0.8725 0.6252 -0.2429 -0.1006 0.1554  82  ARG B CD  
2070 N NE  . ARG B 48  ? 1.3465 1.0022 0.7209 -0.2318 -0.0803 0.1372  82  ARG B NE  
2071 C CZ  . ARG B 48  ? 1.4148 1.0716 0.7880 -0.2045 -0.0921 0.1315  82  ARG B CZ  
2072 N NH1 . ARG B 48  ? 1.4468 1.0744 0.8202 -0.1803 -0.1223 0.1402  82  ARG B NH1 
2073 N NH2 . ARG B 48  ? 1.4138 1.1018 0.7846 -0.2013 -0.0733 0.1167  82  ARG B NH2 
2074 N N   . VAL B 49  ? 1.3096 0.9432 0.7827 -0.2548 -0.0723 0.1337  83  VAL B N   
2075 C CA  . VAL B 49  ? 1.1509 0.8080 0.6583 -0.2350 -0.0538 0.1122  83  VAL B CA  
2076 C C   . VAL B 49  ? 1.1167 0.7597 0.6274 -0.1985 -0.0650 0.0968  83  VAL B C   
2077 O O   . VAL B 49  ? 1.1824 0.7888 0.6812 -0.1840 -0.0941 0.1021  83  VAL B O   
2078 C CB  . VAL B 49  ? 1.3046 0.9581 0.8378 -0.2433 -0.0608 0.1173  83  VAL B CB  
2079 C CG1 . VAL B 49  ? 1.2455 0.9042 0.8100 -0.2139 -0.0589 0.0981  83  VAL B CG1 
2080 C CG2 . VAL B 49  ? 1.3152 1.0107 0.8593 -0.2732 -0.0355 0.1249  83  VAL B CG2 
2081 N N   . LEU B 50  ? 1.0762 0.7486 0.6021 -0.1834 -0.0422 0.0782  84  LEU B N   
2082 C CA  . LEU B 50  ? 1.0678 0.7383 0.5988 -0.1518 -0.0494 0.0644  84  LEU B CA  
2083 C C   . LEU B 50  ? 1.0956 0.7807 0.6626 -0.1356 -0.0407 0.0502  84  LEU B C   
2084 O O   . LEU B 50  ? 1.1302 0.8400 0.7173 -0.1453 -0.0170 0.0457  84  LEU B O   
2085 C CB  . LEU B 50  ? 1.0162 0.7075 0.5300 -0.1507 -0.0340 0.0574  84  LEU B CB  
2086 C CG  . LEU B 50  ? 1.1783 0.8650 0.6556 -0.1688 -0.0393 0.0712  84  LEU B CG  
2087 C CD1 . LEU B 50  ? 1.1660 0.8671 0.6327 -0.2017 -0.0183 0.0774  84  LEU B CD1 
2088 C CD2 . LEU B 50  ? 1.2107 0.9136 0.6728 -0.1589 -0.0355 0.0639  84  LEU B CD2 
2089 N N   . LEU B 51  ? 1.0513 0.7240 0.6262 -0.1096 -0.0597 0.0435  85  LEU B N   
2090 C CA  . LEU B 51  ? 1.0503 0.7369 0.6573 -0.0938 -0.0560 0.0319  85  LEU B CA  
2091 C C   . LEU B 51  ? 1.0255 0.7335 0.6374 -0.0718 -0.0490 0.0191  85  LEU B C   
2092 O O   . LEU B 51  ? 1.0090 0.7122 0.6019 -0.0580 -0.0622 0.0185  85  LEU B O   
2093 C CB  . LEU B 51  ? 1.0653 0.7232 0.6758 -0.0835 -0.0838 0.0331  85  LEU B CB  
2094 C CG  . LEU B 51  ? 1.1140 0.7826 0.7558 -0.0874 -0.0807 0.0308  85  LEU B CG  
2095 C CD1 . LEU B 51  ? 1.1864 0.8648 0.8358 -0.1184 -0.0672 0.0434  85  LEU B CD1 
2096 C CD2 . LEU B 51  ? 1.1820 0.8184 0.8205 -0.0758 -0.1104 0.0283  85  LEU B CD2 
2097 N N   . VAL B 52  ? 1.0425 0.7759 0.6807 -0.0688 -0.0290 0.0106  86  VAL B N   
2098 C CA  . VAL B 52  ? 1.0530 0.8066 0.6963 -0.0531 -0.0217 0.0009  86  VAL B CA  
2099 C C   . VAL B 52  ? 1.1094 0.8731 0.7759 -0.0313 -0.0333 -0.0053 86  VAL B C   
2100 O O   . VAL B 52  ? 1.2858 1.0668 0.9532 -0.0170 -0.0343 -0.0108 86  VAL B O   
2101 C CB  . VAL B 52  ? 1.0139 0.7840 0.6657 -0.0640 0.0079  -0.0043 86  VAL B CB  
2102 C CG1 . VAL B 52  ? 0.9039 0.6878 0.5545 -0.0531 0.0134  -0.0121 86  VAL B CG1 
2103 C CG2 . VAL B 52  ? 1.0346 0.7976 0.6606 -0.0869 0.0201  0.0002  86  VAL B CG2 
2104 N N   . ASP B 53  ? 0.8384 0.5941 0.5217 -0.0306 -0.0434 -0.0036 87  ASP B N   
2105 C CA  . ASP B 53  ? 0.9449 0.7096 0.6454 -0.0113 -0.0570 -0.0099 87  ASP B CA  
2106 C C   . ASP B 53  ? 0.9819 0.7257 0.6875 -0.0166 -0.0736 -0.0068 87  ASP B C   
2107 O O   . ASP B 53  ? 0.9181 0.6504 0.6245 -0.0378 -0.0694 0.0020  87  ASP B O   
2108 C CB  . ASP B 53  ? 0.9760 0.7721 0.7072 -0.0066 -0.0402 -0.0135 87  ASP B CB  
2109 C CG  . ASP B 53  ? 0.9786 0.7944 0.7052 0.0086  -0.0404 -0.0187 87  ASP B CG  
2110 O OD1 . ASP B 53  ? 0.9742 0.7882 0.6816 0.0220  -0.0576 -0.0214 87  ASP B OD1 
2111 O OD2 . ASP B 53  ? 0.9739 0.8074 0.7158 0.0072  -0.0238 -0.0193 87  ASP B OD2 
2112 N N   . THR B 54  ? 0.8304 0.5709 0.5376 0.0012  -0.0931 -0.0141 88  THR B N   
2113 C CA  . THR B 54  ? 0.9174 0.6369 0.6285 -0.0042 -0.1107 -0.0136 88  THR B CA  
2114 C C   . THR B 54  ? 1.0057 0.7576 0.7526 -0.0065 -0.1022 -0.0138 88  THR B C   
2115 O O   . THR B 54  ? 0.9233 0.7091 0.6919 -0.0029 -0.0827 -0.0136 88  THR B O   
2116 C CB  . THR B 54  ? 0.9494 0.6424 0.6373 0.0172  -0.1379 -0.0239 88  THR B CB  
2117 O OG1 . THR B 54  ? 0.9970 0.7216 0.6978 0.0386  -0.1391 -0.0350 88  THR B OG1 
2118 C CG2 . THR B 54  ? 1.0462 0.7204 0.7040 0.0278  -0.1440 -0.0234 88  THR B CG2 
2119 N N   . ALA B 55  ? 0.9811 0.7204 0.7332 -0.0135 -0.1184 -0.0133 89  ALA B N   
2120 C CA  . ALA B 55  ? 0.8832 0.6550 0.6688 -0.0165 -0.1145 -0.0116 89  ALA B CA  
2121 C C   . ALA B 55  ? 0.8725 0.6519 0.6553 0.0051  -0.1310 -0.0244 89  ALA B C   
2122 O O   . ALA B 55  ? 0.9572 0.7242 0.7155 0.0250  -0.1410 -0.0352 89  ALA B O   
2123 C CB  . ALA B 55  ? 0.9681 0.7294 0.7621 -0.0426 -0.1217 -0.0009 89  ALA B CB  
2124 N N   . TRP B 56  ? 0.9473 0.7526 0.7557 0.0014  -0.1338 -0.0227 90  TRP B N   
2125 C CA  . TRP B 56  ? 0.8406 0.6595 0.6461 0.0195  -0.1487 -0.0347 90  TRP B CA  
2126 C C   . TRP B 56  ? 0.9708 0.7442 0.7409 0.0246  -0.1764 -0.0479 90  TRP B C   
2127 O O   . TRP B 56  ? 1.0088 0.7820 0.7602 0.0481  -0.1878 -0.0631 90  TRP B O   
2128 C CB  . TRP B 56  ? 0.7768 0.6361 0.6181 0.0117  -0.1459 -0.0273 90  TRP B CB  
2129 C CG  . TRP B 56  ? 0.7853 0.6868 0.6624 0.0122  -0.1208 -0.0155 90  TRP B CG  
2130 C CD1 . TRP B 56  ? 0.7778 0.6886 0.6782 -0.0019 -0.1010 -0.0025 90  TRP B CD1 
2131 C CD2 . TRP B 56  ? 0.7642 0.7025 0.6569 0.0281  -0.1137 -0.0157 90  TRP B CD2 
2132 N NE1 . TRP B 56  ? 0.7174 0.6622 0.6458 0.0069  -0.0821 0.0034  90  TRP B NE1 
2133 C CE2 . TRP B 56  ? 0.7382 0.6987 0.6624 0.0235  -0.0905 -0.0030 90  TRP B CE2 
2134 C CE3 . TRP B 56  ? 0.7514 0.7073 0.6336 0.0455  -0.1248 -0.0249 90  TRP B CE3 
2135 C CZ2 . TRP B 56  ? 0.7323 0.7238 0.6766 0.0344  -0.0804 0.0019  90  TRP B CZ2 
2136 C CZ3 . TRP B 56  ? 0.7222 0.7165 0.6253 0.0536  -0.1143 -0.0182 90  TRP B CZ3 
2137 C CH2 . TRP B 56  ? 0.6849 0.6928 0.6182 0.0475  -0.0933 -0.0043 90  TRP B CH2 
2138 N N   . THR B 57  ? 1.0448 0.7794 0.8042 0.0030  -0.1880 -0.0423 91  THR B N   
2139 C CA  . THR B 57  ? 1.0280 0.7104 0.7533 0.0044  -0.2170 -0.0544 91  THR B CA  
2140 C C   . THR B 57  ? 1.0335 0.6596 0.7305 -0.0055 -0.2253 -0.0491 91  THR B C   
2141 O O   . THR B 57  ? 1.0029 0.6359 0.7086 -0.0186 -0.2082 -0.0345 91  THR B O   
2142 C CB  . THR B 57  ? 1.0490 0.7318 0.7844 -0.0180 -0.2311 -0.0514 91  THR B CB  
2143 O OG1 . THR B 57  ? 1.0784 0.7424 0.8185 -0.0511 -0.2313 -0.0335 91  THR B OG1 
2144 C CG2 . THR B 57  ? 0.9261 0.6758 0.7018 -0.0177 -0.2168 -0.0458 91  THR B CG2 
2145 N N   . ASP B 58  ? 1.1426 0.6612 0.8187 0.0509  -0.0802 -0.0469 92  ASP B N   
2146 C CA  . ASP B 58  ? 1.1958 0.6791 0.8669 0.0343  -0.0930 -0.0368 92  ASP B CA  
2147 C C   . ASP B 58  ? 1.1332 0.6046 0.8183 0.0021  -0.0952 -0.0296 92  ASP B C   
2148 O O   . ASP B 58  ? 1.1681 0.6290 0.8520 -0.0216 -0.0910 -0.0134 92  ASP B O   
2149 C CB  . ASP B 58  ? 1.2385 0.6833 0.8955 0.0563  -0.1181 -0.0477 92  ASP B CB  
2150 C CG  . ASP B 58  ? 1.2458 0.7027 0.8916 0.0853  -0.1151 -0.0497 92  ASP B CG  
2151 O OD1 . ASP B 58  ? 1.0959 0.5723 0.7423 0.0786  -0.1023 -0.0357 92  ASP B OD1 
2152 O OD2 . ASP B 58  ? 1.2509 0.6997 0.8875 0.1148  -0.1257 -0.0661 92  ASP B OD2 
2153 N N   . ASP B 59  ? 1.1453 0.6212 0.8440 0.0006  -0.1019 -0.0410 93  ASP B N   
2154 C CA  . ASP B 59  ? 1.2046 0.6750 0.9233 -0.0303 -0.1046 -0.0346 93  ASP B CA  
2155 C C   . ASP B 59  ? 1.1937 0.6989 0.9265 -0.0517 -0.0770 -0.0202 93  ASP B C   
2156 O O   . ASP B 59  ? 1.2389 0.7384 0.9825 -0.0806 -0.0734 -0.0076 93  ASP B O   
2157 C CB  . ASP B 59  ? 1.2637 0.7389 0.9967 -0.0255 -0.1194 -0.0513 93  ASP B CB  
2158 C CG  . ASP B 59  ? 1.3605 0.8129 1.1125 -0.0551 -0.1354 -0.0485 93  ASP B CG  
2159 O OD1 . ASP B 59  ? 1.3146 0.7883 1.0890 -0.0825 -0.1204 -0.0346 93  ASP B OD1 
2160 O OD2 . ASP B 59  ? 1.3845 0.7977 1.1299 -0.0512 -0.1624 -0.0607 93  ASP B OD2 
2161 N N   . GLN B 60  ? 1.0940 0.6339 0.8262 -0.0381 -0.0564 -0.0218 94  GLN B N   
2162 C CA  . GLN B 60  ? 0.9636 0.5318 0.7059 -0.0556 -0.0295 -0.0110 94  GLN B CA  
2163 C C   . GLN B 60  ? 1.0275 0.5863 0.7500 -0.0663 -0.0201 0.0019  94  GLN B C   
2164 O O   . GLN B 60  ? 0.9690 0.5361 0.6943 -0.0896 -0.0042 0.0128  94  GLN B O   
2165 C CB  . GLN B 60  ? 0.9632 0.5662 0.7127 -0.0378 -0.0119 -0.0175 94  GLN B CB  
2166 C CG  . GLN B 60  ? 1.0518 0.6660 0.8146 -0.0217 -0.0234 -0.0297 94  GLN B CG  
2167 C CD  . GLN B 60  ? 0.9749 0.6191 0.7401 -0.0021 -0.0065 -0.0325 94  GLN B CD  
2168 O OE1 . GLN B 60  ? 0.9995 0.6493 0.7520 0.0057  0.0086  -0.0287 94  GLN B OE1 
2169 N NE2 . GLN B 60  ? 0.9371 0.6004 0.7196 0.0054  -0.0102 -0.0380 94  GLN B NE2 
2170 N N   . THR B 61  ? 1.1178 0.6623 0.8201 -0.0488 -0.0298 0.0007  95  THR B N   
2171 C CA  . THR B 61  ? 1.0836 0.6195 0.7668 -0.0584 -0.0262 0.0133  95  THR B CA  
2172 C C   . THR B 61  ? 1.1022 0.6051 0.7783 -0.0804 -0.0391 0.0267  95  THR B C   
2173 O O   . THR B 61  ? 1.1468 0.6500 0.8112 -0.1010 -0.0288 0.0409  95  THR B O   
2174 C CB  . THR B 61  ? 1.0694 0.6026 0.7388 -0.0327 -0.0358 0.0092  95  THR B CB  
2175 O OG1 . THR B 61  ? 1.0844 0.6491 0.7609 -0.0151 -0.0216 -0.0005 95  THR B OG1 
2176 C CG2 . THR B 61  ? 0.9753 0.5050 0.6268 -0.0422 -0.0345 0.0225  95  THR B CG2 
2177 N N   . SER B 62  ? 1.2290 0.7012 0.9099 -0.0769 -0.0617 0.0224  96  SER B N   
2178 C CA  . SER B 62  ? 1.2033 0.6412 0.8816 -0.1014 -0.0732 0.0367  96  SER B CA  
2179 C C   . SER B 62  ? 1.1016 0.5599 0.7986 -0.1318 -0.0553 0.0448  96  SER B C   
2180 O O   . SER B 62  ? 1.2217 0.6658 0.9119 -0.1578 -0.0522 0.0630  96  SER B O   
2181 C CB  . SER B 62  ? 1.0919 0.4895 0.7738 -0.0917 -0.1018 0.0272  96  SER B CB  
2182 O OG  . SER B 62  ? 1.4054 0.7818 1.1006 -0.1210 -0.1087 0.0363  96  SER B OG  
2183 N N   . GLN B 63  ? 1.1534 0.6467 0.8739 -0.1280 -0.0429 0.0329  97  GLN B N   
2184 C CA  . GLN B 63  ? 1.1268 0.6484 0.8692 -0.1528 -0.0224 0.0396  97  GLN B CA  
2185 C C   . GLN B 63  ? 1.1957 0.7369 0.9222 -0.1638 0.0044  0.0502  97  GLN B C   
2186 O O   . GLN B 63  ? 1.1848 0.7383 0.9182 -0.1889 0.0209  0.0615  97  GLN B O   
2187 C CB  . GLN B 63  ? 1.0816 0.6374 0.8530 -0.1408 -0.0167 0.0244  97  GLN B CB  
2188 C CG  . GLN B 63  ? 0.9425 0.4915 0.7405 -0.1480 -0.0369 0.0180  97  GLN B CG  
2189 C CD  . GLN B 63  ? 1.1670 0.7594 0.9977 -0.1429 -0.0274 0.0085  97  GLN B CD  
2190 O OE1 . GLN B 63  ? 1.2111 0.8368 1.0612 -0.1564 -0.0036 0.0155  97  GLN B OE1 
2191 N NE2 . GLN B 63  ? 1.1175 0.7105 0.9531 -0.1213 -0.0460 -0.0077 97  GLN B NE2 
2192 N N   . ILE B 64  ? 1.1692 0.7150 0.8745 -0.1459 0.0092  0.0459  98  ILE B N   
2193 C CA  . ILE B 64  ? 1.1170 0.6770 0.8024 -0.1568 0.0309  0.0534  98  ILE B CA  
2194 C C   . ILE B 64  ? 1.2176 0.7510 0.8767 -0.1768 0.0238  0.0726  98  ILE B C   
2195 O O   . ILE B 64  ? 1.1971 0.7402 0.8457 -0.1990 0.0424  0.0834  98  ILE B O   
2196 C CB  . ILE B 64  ? 0.9988 0.5699 0.6713 -0.1347 0.0344  0.0437  98  ILE B CB  
2197 C CG1 . ILE B 64  ? 1.0383 0.6394 0.7330 -0.1214 0.0509  0.0297  98  ILE B CG1 
2198 C CG2 . ILE B 64  ? 1.0448 0.6187 0.6887 -0.1468 0.0459  0.0518  98  ILE B CG2 
2199 C CD1 . ILE B 64  ? 1.0103 0.6167 0.7023 -0.0948 0.0456  0.0197  98  ILE B CD1 
2200 N N   . LEU B 65  ? 1.2094 0.7080 0.8557 -0.1677 -0.0026 0.0776  99  LEU B N   
2201 C CA  . LEU B 65  ? 1.2481 0.7165 0.8680 -0.1842 -0.0124 0.0987  99  LEU B CA  
2202 C C   . LEU B 65  ? 1.3155 0.7740 0.9456 -0.2143 -0.0076 0.1134  99  LEU B C   
2203 O O   . LEU B 65  ? 1.3861 0.8350 0.9930 -0.2360 -0.0013 0.1338  99  LEU B O   
2204 C CB  . LEU B 65  ? 1.1843 0.6147 0.7939 -0.1644 -0.0430 0.1000  99  LEU B CB  
2205 C CG  . LEU B 65  ? 1.2520 0.6952 0.8548 -0.1341 -0.0486 0.0875  99  LEU B CG  
2206 C CD1 . LEU B 65  ? 1.2842 0.6910 0.8822 -0.1117 -0.0779 0.0870  99  LEU B CD1 
2207 C CD2 . LEU B 65  ? 1.1923 0.6552 0.7705 -0.1404 -0.0368 0.0956  99  LEU B CD2 
2208 N N   . ASN B 66  ? 1.2752 0.7382 0.9397 -0.2169 -0.0106 0.1044  100 ASN B N   
2209 C CA  . ASN B 66  ? 1.2502 0.7126 0.9327 -0.2480 -0.0039 0.1180  100 ASN B CA  
2210 C C   . ASN B 66  ? 1.2425 0.7476 0.9279 -0.2659 0.0309  0.1230  100 ASN B C   
2211 O O   . ASN B 66  ? 1.2869 0.7920 0.9698 -0.2944 0.0424  0.1421  100 ASN B O   
2212 C CB  . ASN B 66  ? 1.2767 0.7398 0.9989 -0.2460 -0.0174 0.1045  100 ASN B CB  
2213 C CG  . ASN B 66  ? 1.2281 0.6389 0.9457 -0.2377 -0.0520 0.1028  100 ASN B CG  
2214 O OD1 . ASN B 66  ? 1.2716 0.6430 0.9601 -0.2371 -0.0651 0.1163  100 ASN B OD1 
2215 N ND2 . ASN B 66  ? 1.2386 0.6477 0.9837 -0.2300 -0.0678 0.0853  100 ASN B ND2 
2216 N N   . TRP B 67  ? 1.2233 0.7636 0.9129 -0.2492 0.0488  0.1063  101 TRP B N   
2217 C CA  . TRP B 67  ? 1.2532 0.8315 0.9446 -0.2620 0.0827  0.1072  101 TRP B CA  
2218 C C   . TRP B 67  ? 1.2817 0.8519 0.9273 -0.2749 0.0938  0.1215  101 TRP B C   
2219 O O   . TRP B 67  ? 1.2894 0.8736 0.9278 -0.2983 0.1155  0.1341  101 TRP B O   
2220 C CB  . TRP B 67  ? 1.2389 0.8487 0.9455 -0.2390 0.0967  0.0854  101 TRP B CB  
2221 C CG  . TRP B 67  ? 1.1875 0.8335 0.8990 -0.2478 0.1316  0.0826  101 TRP B CG  
2222 C CD1 . TRP B 67  ? 1.1040 0.7835 0.8541 -0.2548 0.1496  0.0800  101 TRP B CD1 
2223 C CD2 . TRP B 67  ? 1.1412 0.7938 0.8182 -0.2494 0.1522  0.0804  101 TRP B CD2 
2224 N NE1 . TRP B 67  ? 1.1502 0.8556 0.8916 -0.2583 0.1821  0.0760  101 TRP B NE1 
2225 C CE2 . TRP B 67  ? 1.1903 0.8775 0.8848 -0.2559 0.1840  0.0752  101 TRP B CE2 
2226 C CE3 . TRP B 67  ? 1.1681 0.8021 0.8020 -0.2457 0.1459  0.0813  101 TRP B CE3 
2227 C CZ2 . TRP B 67  ? 1.1864 0.8848 0.8527 -0.2585 0.2100  0.0689  101 TRP B CZ2 
2228 C CZ3 . TRP B 67  ? 1.2000 0.8472 0.8067 -0.2507 0.1697  0.0757  101 TRP B CZ3 
2229 C CH2 . TRP B 67  ? 1.1178 0.7944 0.7388 -0.2569 0.2017  0.0686  101 TRP B CH2 
2230 N N   . ILE B 68  ? 1.3193 0.8699 0.9332 -0.2596 0.0792  0.1198  102 ILE B N   
2231 C CA  . ILE B 68  ? 1.3253 0.8682 0.8928 -0.2707 0.0845  0.1331  102 ILE B CA  
2232 C C   . ILE B 68  ? 1.3466 0.8610 0.8970 -0.2945 0.0755  0.1607  102 ILE B C   
2233 O O   . ILE B 68  ? 1.4546 0.9732 0.9732 -0.3145 0.0912  0.1761  102 ILE B O   
2234 C CB  . ILE B 68  ? 1.2764 0.8076 0.8210 -0.2487 0.0661  0.1261  102 ILE B CB  
2235 C CG1 . ILE B 68  ? 1.1861 0.7441 0.7498 -0.2277 0.0763  0.1012  102 ILE B CG1 
2236 C CG2 . ILE B 68  ? 1.3467 0.8738 0.8430 -0.2602 0.0688  0.1388  102 ILE B CG2 
2237 C CD1 . ILE B 68  ? 1.1205 0.6681 0.6873 -0.2014 0.0529  0.0926  102 ILE B CD1 
2238 N N   . LYS B 69  ? 1.3330 0.8155 0.9017 -0.2929 0.0502  0.1673  103 LYS B N   
2239 C CA  . LYS B 69  ? 1.4083 0.8569 0.9639 -0.3166 0.0403  0.1952  103 LYS B CA  
2240 C C   . LYS B 69  ? 1.4140 0.8866 0.9861 -0.3476 0.0670  0.2070  103 LYS B C   
2241 O O   . LYS B 69  ? 1.5054 0.9639 1.0531 -0.3725 0.0727  0.2336  103 LYS B O   
2242 C CB  . LYS B 69  ? 1.3213 0.7274 0.8969 -0.3073 0.0074  0.1952  103 LYS B CB  
2243 C CG  . LYS B 69  ? 1.4733 0.8352 1.0389 -0.3319 -0.0059 0.2243  103 LYS B CG  
2244 C CD  . LYS B 69  ? 1.4072 0.7220 0.9922 -0.3201 -0.0394 0.2192  103 LYS B CD  
2245 C CE  . LYS B 69  ? 1.5012 0.8032 1.1199 -0.3491 -0.0409 0.2282  103 LYS B CE  
2246 N NZ  . LYS B 69  ? 1.4270 0.6968 1.0360 -0.3630 -0.0514 0.2546  103 LYS B NZ  
2247 N N   . GLN B 70  ? 1.4398 0.9513 1.0537 -0.3458 0.0844  0.1890  104 GLN B N   
2248 C CA  . GLN B 70  ? 1.3493 0.8920 0.9887 -0.3728 0.1107  0.1985  104 GLN B CA  
2249 C C   . GLN B 70  ? 1.3567 0.9388 0.9739 -0.3789 0.1478  0.1970  104 GLN B C   
2250 O O   . GLN B 70  ? 1.3823 0.9797 0.9929 -0.4033 0.1688  0.2153  104 GLN B O   
2251 C CB  . GLN B 70  ? 1.4432 1.0116 1.1423 -0.3668 0.1093  0.1805  104 GLN B CB  
2252 C CG  . GLN B 70  ? 1.4735 1.0940 1.2072 -0.3852 0.1424  0.1819  104 GLN B CG  
2253 C CD  . GLN B 70  ? 1.6025 1.2514 1.3964 -0.3768 0.1371  0.1643  104 GLN B CD  
2254 O OE1 . GLN B 70  ? 1.5536 1.2505 1.3746 -0.3695 0.1613  0.1517  104 GLN B OE1 
2255 N NE2 . GLN B 70  ? 1.6102 1.2285 1.4241 -0.3766 0.1042  0.1629  104 GLN B NE2 
2256 N N   . GLU B 71  ? 1.3091 0.9088 0.9156 -0.3553 0.1561  0.1743  105 GLU B N   
2257 C CA  . GLU B 71  ? 1.2617 0.8968 0.8503 -0.3582 0.1914  0.1665  105 GLU B CA  
2258 C C   . GLU B 71  ? 1.3461 0.9657 0.8707 -0.3605 0.1929  0.1731  105 GLU B C   
2259 O O   . GLU B 71  ? 1.2962 0.9413 0.8003 -0.3686 0.2186  0.1737  105 GLU B O   
2260 C CB  . GLU B 71  ? 1.3012 0.9643 0.9183 -0.3330 0.2021  0.1370  105 GLU B CB  
2261 C CG  . GLU B 71  ? 1.3059 0.9951 0.9855 -0.3302 0.2051  0.1296  105 GLU B CG  
2262 C CD  . GLU B 71  ? 1.3780 1.1123 1.0803 -0.3440 0.2421  0.1306  105 GLU B CD  
2263 O OE1 . GLU B 71  ? 1.3977 1.1582 1.1535 -0.3478 0.2446  0.1301  105 GLU B OE1 
2264 O OE2 . GLU B 71  ? 1.3446 1.0900 1.0113 -0.3504 0.2685  0.1309  105 GLU B OE2 
2265 N N   . ILE B 72  ? 1.3645 0.9508 0.8643 -0.3472 0.1628  0.1747  106 ILE B N   
2266 C CA  . ILE B 72  ? 1.3526 0.9267 0.7942 -0.3482 0.1588  0.1807  106 ILE B CA  
2267 C C   . ILE B 72  ? 1.5010 1.0418 0.9165 -0.3585 0.1349  0.2098  106 ILE B C   
2268 O O   . ILE B 72  ? 1.4798 1.0265 0.8583 -0.3650 0.1384  0.2209  106 ILE B O   
2269 C CB  . ILE B 72  ? 1.4988 1.0708 0.9360 -0.3215 0.1432  0.1585  106 ILE B CB  
2270 C CG1 . ILE B 72  ? 1.3657 0.9692 0.8349 -0.3079 0.1651  0.1302  106 ILE B CG1 
2271 C CG2 . ILE B 72  ? 1.5023 1.0687 0.8822 -0.3244 0.1389  0.1626  106 ILE B CG2 
2272 C CD1 . ILE B 72  ? 1.1467 0.7494 0.6163 -0.2843 0.1524  0.1100  106 ILE B CD1 
2273 N N   . ASN B 73  ? 1.6679 1.1739 1.1046 -0.3567 0.1088  0.2206  107 ASN B N   
2274 C CA  . ASN B 73  ? 1.7834 1.2543 1.2048 -0.3616 0.0834  0.2467  107 ASN B CA  
2275 C C   . ASN B 73  ? 1.6568 1.1108 1.0285 -0.3500 0.0645  0.2532  107 ASN B C   
2276 O O   . ASN B 73  ? 1.6915 1.1337 1.0358 -0.3565 0.0555  0.2753  107 ASN B O   
2277 C CB  . ASN B 73  ? 1.5946 1.0813 1.0218 -0.3836 0.1003  0.2668  107 ASN B CB  
2278 N N   . LEU B 74  ? 1.5605 1.0191 0.9265 -0.3305 0.0576  0.2330  108 LEU B N   
2279 C CA  . LEU B 74  ? 1.4970 0.9458 0.8266 -0.3165 0.0358  0.2359  108 LEU B CA  
2280 C C   . LEU B 74  ? 1.4937 0.9283 0.8530 -0.2867 0.0074  0.2231  108 LEU B C   
2281 O O   . LEU B 74  ? 1.4722 0.9194 0.8735 -0.2737 0.0122  0.2011  108 LEU B O   
2282 C CB  . LEU B 74  ? 1.5719 1.0563 0.8749 -0.3164 0.0544  0.2176  108 LEU B CB  
2283 C CG  . LEU B 74  ? 1.5407 1.0417 0.8023 -0.3367 0.0737  0.2282  108 LEU B CG  
2284 C CD1 . LEU B 74  ? 1.5149 1.0467 0.7536 -0.3352 0.0915  0.2034  108 LEU B CD1 
2285 C CD2 . LEU B 74  ? 1.5101 0.9895 0.7376 -0.3380 0.0486  0.2555  108 LEU B CD2 
2286 N N   . PRO B 75  ? 1.4459 0.8560 0.7838 -0.2738 -0.0220 0.2367  109 PRO B N   
2287 C CA  . PRO B 75  ? 1.2805 0.6791 0.6470 -0.2432 -0.0474 0.2244  109 PRO B CA  
2288 C C   . PRO B 75  ? 1.3550 0.7927 0.7368 -0.2252 -0.0404 0.1958  109 PRO B C   
2289 O O   . PRO B 75  ? 1.3718 0.8382 0.7319 -0.2339 -0.0257 0.1887  109 PRO B O   
2290 C CB  . PRO B 75  ? 1.3529 0.7209 0.6888 -0.2347 -0.0779 0.2486  109 PRO B CB  
2291 C CG  . PRO B 75  ? 1.3471 0.7225 0.6329 -0.2581 -0.0684 0.2683  109 PRO B CG  
2292 C CD  . PRO B 75  ? 1.3401 0.7340 0.6262 -0.2852 -0.0331 0.2647  109 PRO B CD  
2293 N N   . VAL B 76  ? 1.3642 0.8013 0.7827 -0.2005 -0.0509 0.1792  110 VAL B N   
2294 C CA  . VAL B 76  ? 1.1966 0.6680 0.6336 -0.1819 -0.0460 0.1549  110 VAL B CA  
2295 C C   . VAL B 76  ? 1.2608 0.7338 0.6859 -0.1633 -0.0711 0.1602  110 VAL B C   
2296 O O   . VAL B 76  ? 1.3756 0.8282 0.8144 -0.1411 -0.0939 0.1636  110 VAL B O   
2297 C CB  . VAL B 76  ? 1.1876 0.6614 0.6668 -0.1641 -0.0434 0.1358  110 VAL B CB  
2298 C CG1 . VAL B 76  ? 1.0259 0.5324 0.5221 -0.1438 -0.0401 0.1154  110 VAL B CG1 
2299 C CG2 . VAL B 76  ? 1.2720 0.7522 0.7668 -0.1820 -0.0193 0.1302  110 VAL B CG2 
2300 N N   . ALA B 77  ? 1.2753 0.7738 0.6758 -0.1717 -0.0676 0.1597  111 ALA B N   
2301 C CA  . ALA B 77  ? 1.2497 0.7551 0.6381 -0.1577 -0.0931 0.1677  111 ALA B CA  
2302 C C   . ALA B 77  ? 1.3052 0.8367 0.7300 -0.1307 -0.1001 0.1492  111 ALA B C   
2303 O O   . ALA B 77  ? 1.2658 0.7961 0.6973 -0.1091 -0.1248 0.1563  111 ALA B O   
2304 C CB  . ALA B 77  ? 1.2046 0.7308 0.5533 -0.1778 -0.0891 0.1718  111 ALA B CB  
2305 N N   . LEU B 78  ? 1.2461 0.8024 0.6949 -0.1306 -0.0780 0.1270  112 LEU B N   
2306 C CA  . LEU B 78  ? 1.2011 0.7851 0.6834 -0.1075 -0.0809 0.1113  112 LEU B CA  
2307 C C   . LEU B 78  ? 1.1351 0.7290 0.6430 -0.1069 -0.0558 0.0922  112 LEU B C   
2308 O O   . LEU B 78  ? 1.1584 0.7422 0.6597 -0.1243 -0.0369 0.0900  112 LEU B O   
2309 C CB  . LEU B 78  ? 1.1965 0.8165 0.6725 -0.1115 -0.0862 0.1078  112 LEU B CB  
2310 C CG  . LEU B 78  ? 1.1851 0.8265 0.6512 -0.1350 -0.0626 0.0934  112 LEU B CG  
2311 C CD1 . LEU B 78  ? 1.1554 0.8268 0.6573 -0.1251 -0.0500 0.0742  112 LEU B CD1 
2312 C CD2 . LEU B 78  ? 1.2612 0.9143 0.6918 -0.1524 -0.0739 0.1002  112 LEU B CD2 
2313 N N   . ALA B 79  ? 1.0435 0.6595 0.5813 -0.0856 -0.0555 0.0796  113 ALA B N   
2314 C CA  . ALA B 79  ? 1.0598 0.6876 0.6213 -0.0817 -0.0336 0.0633  113 ALA B CA  
2315 C C   . ALA B 79  ? 1.1052 0.7686 0.6897 -0.0676 -0.0312 0.0533  113 ALA B C   
2316 O O   . ALA B 79  ? 1.1636 0.8375 0.7604 -0.0466 -0.0483 0.0564  113 ALA B O   
2317 C CB  . ALA B 79  ? 0.9864 0.5906 0.5624 -0.0663 -0.0367 0.0612  113 ALA B CB  
2318 N N   . VAL B 80  ? 0.9561 0.6379 0.5476 -0.0792 -0.0093 0.0421  114 VAL B N   
2319 C CA  . VAL B 80  ? 1.0156 0.7300 0.6316 -0.0700 -0.0028 0.0337  114 VAL B CA  
2320 C C   . VAL B 80  ? 0.9910 0.7053 0.6255 -0.0617 0.0179  0.0240  114 VAL B C   
2321 O O   . VAL B 80  ? 0.9760 0.6735 0.6032 -0.0729 0.0323  0.0207  114 VAL B O   
2322 C CB  . VAL B 80  ? 0.9517 0.6858 0.5590 -0.0928 0.0025  0.0298  114 VAL B CB  
2323 C CG1 . VAL B 80  ? 0.9759 0.6936 0.5639 -0.1162 0.0235  0.0227  114 VAL B CG1 
2324 C CG2 . VAL B 80  ? 0.8701 0.6382 0.5070 -0.0862 0.0089  0.0231  114 VAL B CG2 
2325 N N   . VAL B 81  ? 0.9070 0.6421 0.5654 -0.0408 0.0191  0.0207  115 VAL B N   
2326 C CA  . VAL B 81  ? 0.8767 0.6147 0.5503 -0.0309 0.0375  0.0137  115 VAL B CA  
2327 C C   . VAL B 81  ? 0.8856 0.6527 0.5765 -0.0351 0.0520  0.0106  115 VAL B C   
2328 O O   . VAL B 81  ? 0.8821 0.6748 0.5830 -0.0346 0.0438  0.0133  115 VAL B O   
2329 C CB  . VAL B 81  ? 0.9244 0.6580 0.6068 -0.0015 0.0284  0.0127  115 VAL B CB  
2330 C CG1 . VAL B 81  ? 0.9099 0.6088 0.5773 -0.0019 0.0158  0.0146  115 VAL B CG1 
2331 C CG2 . VAL B 81  ? 0.8894 0.6454 0.5829 0.0182  0.0144  0.0155  115 VAL B CG2 
2332 N N   . THR B 82  ? 0.6960 0.6343 0.7924 0.0351  -0.1341 -0.0549 116 THR B N   
2333 C CA  . THR B 82  ? 0.6254 0.6165 0.7645 0.0259  -0.1150 -0.0577 116 THR B CA  
2334 C C   . THR B 82  ? 0.6796 0.7154 0.8353 0.0329  -0.1082 -0.0671 116 THR B C   
2335 O O   . THR B 82  ? 0.7580 0.8393 0.9424 0.0307  -0.0952 -0.0786 116 THR B O   
2336 C CB  . THR B 82  ? 0.7450 0.7323 0.9076 -0.0011 -0.0964 -0.0379 116 THR B CB  
2337 O OG1 . THR B 82  ? 0.8664 0.8376 1.0221 -0.0080 -0.0964 -0.0236 116 THR B OG1 
2338 C CG2 . THR B 82  ? 0.6129 0.5674 0.7651 -0.0106 -0.0987 -0.0333 116 THR B CG2 
2339 N N   . HIS B 83  ? 0.6358 0.6610 0.7736 0.0391  -0.1151 -0.0641 117 HIS B N   
2340 C CA  . HIS B 83  ? 0.6699 0.7356 0.8158 0.0472  -0.1099 -0.0754 117 HIS B CA  
2341 C C   . HIS B 83  ? 0.7383 0.7789 0.8545 0.0569  -0.1239 -0.0741 117 HIS B C   
2342 O O   . HIS B 83  ? 0.7512 0.7459 0.8457 0.0526  -0.1339 -0.0629 117 HIS B O   
2343 C CB  . HIS B 83  ? 0.6589 0.7577 0.8339 0.0265  -0.0842 -0.0636 117 HIS B CB  
2344 C CG  . HIS B 83  ? 0.6161 0.6885 0.7898 0.0094  -0.0781 -0.0371 117 HIS B CG  
2345 N ND1 . HIS B 83  ? 0.7062 0.7540 0.8892 -0.0043 -0.0748 -0.0235 117 HIS B ND1 
2346 C CD2 . HIS B 83  ? 0.6456 0.7160 0.8105 0.0053  -0.0757 -0.0238 117 HIS B CD2 
2347 C CE1 . HIS B 83  ? 0.6844 0.7182 0.8676 -0.0149 -0.0712 -0.0043 117 HIS B CE1 
2348 N NE2 . HIS B 83  ? 0.6538 0.7004 0.8250 -0.0087 -0.0727 -0.0034 117 HIS B NE2 
2349 N N   . ALA B 84  ? 0.6958 0.7694 0.8121 0.0679  -0.1229 -0.0881 118 ALA B N   
2350 C CA  . ALA B 84  ? 0.7529 0.8085 0.8415 0.0799  -0.1369 -0.0931 118 ALA B CA  
2351 C C   . ALA B 84  ? 0.6854 0.7490 0.7749 0.0636  -0.1256 -0.0756 118 ALA B C   
2352 O O   . ALA B 84  ? 0.7507 0.8471 0.8399 0.0663  -0.1188 -0.0821 118 ALA B O   
2353 C CB  . ALA B 84  ? 0.6766 0.7634 0.7622 0.1047  -0.1448 -0.1225 118 ALA B CB  
2354 N N   . HIS B 85  ? 0.7694 0.8039 0.8590 0.0470  -0.1241 -0.0539 119 HIS B N   
2355 C CA  . HIS B 85  ? 0.7486 0.7815 0.8331 0.0362  -0.1214 -0.0381 119 HIS B CA  
2356 C C   . HIS B 85  ? 0.6651 0.6538 0.7293 0.0341  -0.1376 -0.0360 119 HIS B C   
2357 O O   . HIS B 85  ? 0.7486 0.7025 0.8031 0.0358  -0.1463 -0.0405 119 HIS B O   
2358 C CB  . HIS B 85  ? 0.6502 0.6958 0.7585 0.0180  -0.1032 -0.0159 119 HIS B CB  
2359 C CG  . HIS B 85  ? 0.5908 0.6743 0.7064 0.0153  -0.0855 -0.0128 119 HIS B CG  
2360 N ND1 . HIS B 85  ? 0.5998 0.6915 0.7336 0.0008  -0.0665 0.0053  119 HIS B ND1 
2361 C CD2 . HIS B 85  ? 0.7560 0.8684 0.8606 0.0237  -0.0824 -0.0261 119 HIS B CD2 
2362 C CE1 . HIS B 85  ? 0.6901 0.8100 0.8201 -0.0013 -0.0514 0.0048  119 HIS B CE1 
2363 N NE2 . HIS B 85  ? 0.8744 1.0106 0.9877 0.0118  -0.0602 -0.0149 119 HIS B NE2 
2364 N N   . GLN B 86  ? 0.7788 0.7690 0.8342 0.0295  -0.1412 -0.0301 120 GLN B N   
2365 C CA  . GLN B 86  ? 0.7254 0.6789 0.7610 0.0262  -0.1559 -0.0343 120 GLN B CA  
2366 C C   . GLN B 86  ? 0.7254 0.6481 0.7694 0.0098  -0.1545 -0.0242 120 GLN B C   
2367 O O   . GLN B 86  ? 0.7876 0.6681 0.8113 0.0070  -0.1640 -0.0317 120 GLN B O   
2368 C CB  . GLN B 86  ? 0.6541 0.6248 0.6839 0.0229  -0.1594 -0.0312 120 GLN B CB  
2369 C CG  . GLN B 86  ? 0.8570 0.7981 0.8766 0.0120  -0.1706 -0.0345 120 GLN B CG  
2370 C CD  . GLN B 86  ? 0.8491 0.7783 0.8409 0.0209  -0.1840 -0.0541 120 GLN B CD  
2371 O OE1 . GLN B 86  ? 0.9805 0.9241 0.9607 0.0374  -0.1858 -0.0660 120 GLN B OE1 
2372 N NE2 . GLN B 86  ? 0.7757 0.6800 0.7581 0.0087  -0.1924 -0.0604 120 GLN B NE2 
2373 N N   . ASP B 87  ? 0.7373 0.6778 0.8090 -0.0018 -0.1416 -0.0079 121 ASP B N   
2374 C CA  . ASP B 87  ? 0.7678 0.6858 0.8512 -0.0183 -0.1384 -0.0003 121 ASP B CA  
2375 C C   . ASP B 87  ? 0.7928 0.6827 0.8679 -0.0176 -0.1382 -0.0057 121 ASP B C   
2376 O O   . ASP B 87  ? 0.7873 0.6537 0.8653 -0.0325 -0.1352 -0.0016 121 ASP B O   
2377 C CB  . ASP B 87  ? 0.7496 0.6941 0.8658 -0.0276 -0.1249 0.0166  121 ASP B CB  
2378 C CG  . ASP B 87  ? 0.7157 0.6874 0.8452 -0.0208 -0.1120 0.0217  121 ASP B CG  
2379 O OD1 . ASP B 87  ? 0.6795 0.6672 0.7959 -0.0086 -0.1134 0.0139  121 ASP B OD1 
2380 O OD2 . ASP B 87  ? 0.6937 0.6715 0.8476 -0.0292 -0.0991 0.0315  121 ASP B OD2 
2381 N N   . LYS B 88  ? 0.7812 0.6754 0.8455 -0.0002 -0.1417 -0.0163 122 LYS B N   
2382 C CA  . LYS B 88  ? 0.8418 0.7130 0.8955 0.0053  -0.1446 -0.0225 122 LYS B CA  
2383 C C   . LYS B 88  ? 0.8429 0.6795 0.8581 0.0244  -0.1622 -0.0381 122 LYS B C   
2384 O O   . LYS B 88  ? 0.9328 0.7254 0.9227 0.0252  -0.1693 -0.0399 122 LYS B O   
2385 C CB  . LYS B 88  ? 0.7866 0.6981 0.8669 0.0109  -0.1334 -0.0240 122 LYS B CB  
2386 C CG  . LYS B 88  ? 0.7350 0.6810 0.8504 -0.0036 -0.1153 -0.0095 122 LYS B CG  
2387 C CD  . LYS B 88  ? 0.6475 0.5858 0.7829 -0.0199 -0.1047 -0.0001 122 LYS B CD  
2388 C CE  . LYS B 88  ? 0.6955 0.6106 0.8313 -0.0359 -0.1055 0.0103  122 LYS B CE  
2389 N NZ  . LYS B 88  ? 0.7067 0.6127 0.8592 -0.0512 -0.0957 0.0152  122 LYS B NZ  
2390 N N   . MET B 89  ? 0.8508 0.7034 0.8578 0.0407  -0.1695 -0.0498 123 MET B N   
2391 C CA  . MET B 89  ? 0.9479 0.7679 0.9197 0.0630  -0.1871 -0.0671 123 MET B CA  
2392 C C   . MET B 89  ? 1.0055 0.8032 0.9554 0.0618  -0.1955 -0.0729 123 MET B C   
2393 O O   . MET B 89  ? 1.0783 0.8619 1.0049 0.0828  -0.2085 -0.0899 123 MET B O   
2394 C CB  . MET B 89  ? 0.8517 0.7136 0.8340 0.0880  -0.1897 -0.0841 123 MET B CB  
2395 C CG  . MET B 89  ? 0.8948 0.7857 0.9016 0.0890  -0.1814 -0.0835 123 MET B CG  
2396 S SD  . MET B 89  ? 0.8493 0.7829 0.8633 0.1217  -0.1896 -0.1121 123 MET B SD  
2397 C CE  . MET B 89  ? 0.9686 0.8329 0.9304 0.1500  -0.2183 -0.1247 123 MET B CE  
2398 N N   . GLY B 90  ? 0.9083 0.7050 0.8668 0.0385  -0.1890 -0.0615 124 GLY B N   
2399 C CA  . GLY B 90  ? 0.9548 0.7346 0.8949 0.0348  -0.1968 -0.0696 124 GLY B CA  
2400 C C   . GLY B 90  ? 1.0253 0.7339 0.9265 0.0295  -0.2064 -0.0763 124 GLY B C   
2401 O O   . GLY B 90  ? 1.0494 0.7363 0.9289 0.0316  -0.2150 -0.0892 124 GLY B O   
2402 N N   . GLY B 91  ? 1.0502 0.7193 0.9391 0.0213  -0.2041 -0.0683 125 GLY B N   
2403 C CA  . GLY B 91  ? 1.0249 0.6174 0.8694 0.0132  -0.2105 -0.0721 125 GLY B CA  
2404 C C   . GLY B 91  ? 1.1006 0.6459 0.9079 0.0374  -0.2221 -0.0760 125 GLY B C   
2405 O O   . GLY B 91  ? 1.1266 0.6101 0.8992 0.0276  -0.2223 -0.0699 125 GLY B O   
2406 N N   . MET B 92  ? 1.0680 0.6430 0.8806 0.0695  -0.2318 -0.0874 126 MET B N   
2407 C CA  . MET B 92  ? 1.0967 0.6346 0.8767 0.0989  -0.2466 -0.0945 126 MET B CA  
2408 C C   . MET B 92  ? 1.2655 0.7173 0.9871 0.1087  -0.2613 -0.1032 126 MET B C   
2409 O O   . MET B 92  ? 1.2546 0.6456 0.9331 0.1235  -0.2724 -0.1015 126 MET B O   
2410 C CB  . MET B 92  ? 1.0905 0.6915 0.8972 0.1303  -0.2527 -0.1096 126 MET B CB  
2411 C CG  . MET B 92  ? 1.0880 0.7639 0.9456 0.1218  -0.2374 -0.1018 126 MET B CG  
2412 S SD  . MET B 92  ? 1.2514 0.9112 1.1046 0.1200  -0.2361 -0.0910 126 MET B SD  
2413 C CE  . MET B 92  ? 1.0574 0.6901 0.8743 0.1664  -0.2621 -0.1120 126 MET B CE  
2414 N N   . GLY B 93  ? 1.2127 0.6551 0.9291 0.1012  -0.2620 -0.1129 127 GLY B N   
2415 C CA  . GLY B 93  ? 1.2084 0.5641 0.8689 0.1082  -0.2741 -0.1227 127 GLY B CA  
2416 C C   . GLY B 93  ? 1.3492 0.6241 0.9684 0.0791  -0.2673 -0.1087 127 GLY B C   
2417 O O   . GLY B 93  ? 1.4279 0.6146 0.9878 0.0906  -0.2781 -0.1101 127 GLY B O   
2418 N N   . ALA B 94  ? 1.4431 0.7450 1.0907 0.0413  -0.2487 -0.0955 128 ALA B N   
2419 C CA  . ALA B 94  ? 1.4080 0.6414 1.0202 0.0091  -0.2383 -0.0839 128 ALA B CA  
2420 C C   . ALA B 94  ? 1.5230 0.7162 1.1019 0.0224  -0.2429 -0.0712 128 ALA B C   
2421 O O   . ALA B 94  ? 1.7107 0.8190 1.2341 0.0074  -0.2402 -0.0637 128 ALA B O   
2422 C CB  . ALA B 94  ? 1.3022 0.5868 0.9607 -0.0311 -0.2180 -0.0765 128 ALA B CB  
2423 N N   . LEU B 95  ? 1.4102 0.6626 1.0197 0.0489  -0.2489 -0.0697 129 LEU B N   
2424 C CA  . LEU B 95  ? 1.3781 0.6004 0.9574 0.0651  -0.2560 -0.0608 129 LEU B CA  
2425 C C   . LEU B 95  ? 1.5102 0.6680 1.0327 0.1069  -0.2808 -0.0700 129 LEU B C   
2426 O O   . LEU B 95  ? 1.5971 0.6791 1.0603 0.1138  -0.2884 -0.0610 129 LEU B O   
2427 C CB  . LEU B 95  ? 1.1841 0.4976 0.8208 0.0753  -0.2522 -0.0590 129 LEU B CB  
2428 C CG  . LEU B 95  ? 1.2220 0.5899 0.9093 0.0382  -0.2290 -0.0473 129 LEU B CG  
2429 C CD1 . LEU B 95  ? 1.0028 0.4431 0.7350 0.0503  -0.2259 -0.0460 129 LEU B CD1 
2430 C CD2 . LEU B 95  ? 1.2739 0.5811 0.9272 0.0038  -0.2165 -0.0345 129 LEU B CD2 
2431 N N   . HIS B 96  ? 1.4910 0.6768 1.0284 0.1367  -0.2940 -0.0885 130 HIS B N   
2432 C CA  . HIS B 96  ? 1.5099 0.6371 0.9969 0.1807  -0.3192 -0.1009 130 HIS B CA  
2433 C C   . HIS B 96  ? 1.5579 0.5768 0.9776 0.1693  -0.3210 -0.0983 130 HIS B C   
2434 O O   . HIS B 96  ? 1.5859 0.5554 0.9545 0.1933  -0.3337 -0.0961 130 HIS B O   
2435 C CB  . HIS B 96  ? 1.3451 0.5417 0.8723 0.2138  -0.3302 -0.1246 130 HIS B CB  
2436 C CG  . HIS B 96  ? 1.2678 0.5709 0.8579 0.2247  -0.3264 -0.1290 130 HIS B CG  
2437 N ND1 . HIS B 96  ? 1.2743 0.6589 0.9125 0.2415  -0.3270 -0.1483 130 HIS B ND1 
2438 C CD2 . HIS B 96  ? 1.3255 0.6654 0.9366 0.2187  -0.3200 -0.1178 130 HIS B CD2 
2439 C CE1 . HIS B 96  ? 1.2121 0.6765 0.8976 0.2439  -0.3201 -0.1484 130 HIS B CE1 
2440 N NE2 . HIS B 96  ? 1.2430 0.6827 0.9147 0.2308  -0.3163 -0.1307 130 HIS B NE2 
2441 N N   . ALA B 97  ? 1.5810 0.5922 1.0104 0.1278  -0.3027 -0.0967 131 ALA B N   
2442 C CA  . ALA B 97  ? 1.6522 0.5959 1.0344 0.1056  -0.2929 -0.0916 131 ALA B CA  
2443 C C   . ALA B 97  ? 1.7476 0.6408 1.0856 0.0813  -0.2794 -0.0691 131 ALA B C   
2444 O O   . ALA B 97  ? 1.8046 0.6352 1.0965 0.0649  -0.2707 -0.0642 131 ALA B O   
2445 C CB  . ALA B 97  ? 1.6039 0.5653 1.0158 0.0673  -0.2766 -0.1002 131 ALA B CB  
2446 N N   . GLU B 98  ? 1.6383 0.5570 0.9888 0.0780  -0.2765 -0.0568 132 GLU B N   
2447 C CA  . GLU B 98  ? 1.6815 0.5570 0.9886 0.0573  -0.2644 -0.0375 132 GLU B CA  
2448 C C   . GLU B 98  ? 1.8051 0.6651 1.0782 0.0969  -0.2852 -0.0322 132 GLU B C   
2449 O O   . GLU B 98  ? 1.8769 0.7098 1.1168 0.0830  -0.2776 -0.0170 132 GLU B O   
2450 C CB  . GLU B 98  ? 1.6528 0.5710 1.0016 0.0125  -0.2394 -0.0284 132 GLU B CB  
2451 C CG  . GLU B 98  ? 1.8118 0.6900 1.1296 -0.0318 -0.2135 -0.0174 132 GLU B CG  
2452 C CD  . GLU B 98  ? 1.9468 0.8167 1.2741 -0.0591 -0.1996 -0.0276 132 GLU B CD  
2453 O OE1 . GLU B 98  ? 1.8870 0.7920 1.2529 -0.0498 -0.2079 -0.0424 132 GLU B OE1 
2454 O OE2 . GLU B 98  ? 2.0218 0.8503 1.3172 -0.0901 -0.1805 -0.0226 132 GLU B OE2 
2455 N N   . ALA B 99  ? 1.7894 0.6710 1.0716 0.1461  -0.3114 -0.0471 133 ALA B N   
2456 C CA  . ALA B 99  ? 1.7962 0.6752 1.0527 0.1892  -0.3346 -0.0480 133 ALA B CA  
2457 C C   . ALA B 99  ? 1.7872 0.7065 1.0702 0.1801  -0.3289 -0.0389 133 ALA B C   
2458 O O   . ALA B 99  ? 1.8347 0.7222 1.0742 0.1846  -0.3331 -0.0277 133 ALA B O   
2459 C CB  . ALA B 99  ? 1.9173 0.7094 1.0890 0.1989  -0.3425 -0.0387 133 ALA B CB  
2460 N N   . ILE B 100 ? 1.6905 0.6780 1.0434 0.1675  -0.3199 -0.0445 134 ILE B N   
2461 C CA  . ILE B 100 ? 1.5206 0.5693 0.9158 0.1546  -0.3098 -0.0379 134 ILE B CA  
2462 C C   . ILE B 100 ? 1.6049 0.7484 1.0555 0.1934  -0.3239 -0.0559 134 ILE B C   
2463 O O   . ILE B 100 ? 1.5708 0.7758 1.0725 0.2000  -0.3224 -0.0703 134 ILE B O   
2464 C CB  . ILE B 100 ? 1.4401 0.5387 0.8909 0.1030  -0.2792 -0.0310 134 ILE B CB  
2465 C CG1 . ILE B 100 ? 1.4612 0.4729 0.8604 0.0614  -0.2632 -0.0174 134 ILE B CG1 
2466 C CG2 . ILE B 100 ? 1.4170 0.5969 0.9222 0.0918  -0.2668 -0.0267 134 ILE B CG2 
2467 C CD1 . ILE B 100 ? 1.3999 0.4585 0.8532 0.0147  -0.2367 -0.0163 134 ILE B CD1 
2468 N N   . PRO B 101 ? 1.5990 0.7589 1.0409 0.2183  -0.3370 -0.0573 135 PRO B N   
2469 C CA  . PRO B 101 ? 1.4440 0.7014 0.9437 0.2513  -0.3479 -0.0784 135 PRO B CA  
2470 C C   . PRO B 101 ? 1.2770 0.6358 0.8623 0.2200  -0.3219 -0.0799 135 PRO B C   
2471 O O   . PRO B 101 ? 1.2587 0.6313 0.8615 0.1846  -0.3015 -0.0654 135 PRO B O   
2472 C CB  . PRO B 101 ? 1.4283 0.6752 0.8954 0.2756  -0.3646 -0.0777 135 PRO B CB  
2473 C CG  . PRO B 101 ? 1.5426 0.6658 0.9161 0.2695  -0.3707 -0.0573 135 PRO B CG  
2474 C CD  . PRO B 101 ? 1.5458 0.6340 0.9199 0.2184  -0.3433 -0.0419 135 PRO B CD  
2475 N N   . THR B 102 ? 1.2935 0.7206 0.9295 0.2338  -0.3223 -0.0978 136 THR B N   
2476 C CA  . THR B 102 ? 1.1409 0.6574 0.8516 0.2075  -0.2985 -0.0988 136 THR B CA  
2477 C C   . THR B 102 ? 1.0778 0.6834 0.8376 0.2309  -0.3024 -0.1194 136 THR B C   
2478 O O   . THR B 102 ? 1.1309 0.7530 0.8875 0.2698  -0.3222 -0.1416 136 THR B O   
2479 C CB  . THR B 102 ? 1.1401 0.6653 0.8684 0.1974  -0.2910 -0.1020 136 THR B CB  
2480 O OG1 . THR B 102 ? 1.2834 0.8220 1.0085 0.2367  -0.3100 -0.1252 136 THR B OG1 
2481 C CG2 . THR B 102 ? 1.2285 0.6679 0.9098 0.1732  -0.2873 -0.0865 136 THR B CG2 
2482 N N   . TYR B 103 ? 0.9921 0.6557 0.7986 0.2067  -0.2828 -0.1144 137 TYR B N   
2483 C CA  . TYR B 103 ? 0.9297 0.6812 0.7878 0.2197  -0.2806 -0.1344 137 TYR B CA  
2484 C C   . TYR B 103 ? 0.8923 0.7115 0.8124 0.1912  -0.2533 -0.1325 137 TYR B C   
2485 O O   . TYR B 103 ? 0.8150 0.6163 0.7410 0.1589  -0.2359 -0.1121 137 TYR B O   
2486 C CB  . TYR B 103 ? 1.0221 0.7817 0.8780 0.2176  -0.2815 -0.1331 137 TYR B CB  
2487 C CG  . TYR B 103 ? 1.0833 0.7739 0.8709 0.2474  -0.3094 -0.1330 137 TYR B CG  
2488 C CD1 . TYR B 103 ? 1.0708 0.6686 0.7974 0.2320  -0.3103 -0.1091 137 TYR B CD1 
2489 C CD2 . TYR B 103 ? 1.1267 0.8442 0.9085 0.2911  -0.3348 -0.1578 137 TYR B CD2 
2490 C CE1 . TYR B 103 ? 1.2178 0.7431 0.8727 0.2587  -0.3350 -0.1062 137 TYR B CE1 
2491 C CE2 . TYR B 103 ? 1.2269 0.8761 0.9397 0.3223  -0.3630 -0.1561 137 TYR B CE2 
2492 C CZ  . TYR B 103 ? 1.3298 0.8786 0.9759 0.3057  -0.3626 -0.1285 137 TYR B CZ  
2493 O OH  . TYR B 103 ? 1.4158 0.8874 0.9844 0.3361  -0.3896 -0.1242 137 TYR B OH  
2494 N N   . ALA B 104 ? 0.8475 0.7446 0.8124 0.2037  -0.2498 -0.1549 138 ALA B N   
2495 C CA  . ALA B 104 ? 0.7886 0.7464 0.8059 0.1785  -0.2236 -0.1534 138 ALA B CA  
2496 C C   . ALA B 104 ? 0.9153 0.9563 0.9782 0.1886  -0.2180 -0.1802 138 ALA B C   
2497 O O   . ALA B 104 ? 0.9005 0.9588 0.9570 0.2209  -0.2381 -0.2046 138 ALA B O   
2498 C CB  . ALA B 104 ? 0.7568 0.7068 0.7683 0.1789  -0.2224 -0.1521 138 ALA B CB  
2499 N N   . ASN B 105 ? 0.8282 0.9200 0.9365 0.1606  -0.1902 -0.1765 139 ASN B N   
2500 C CA  . ASN B 105 ? 0.7093 0.8825 0.8630 0.1636  -0.1790 -0.2036 139 ASN B CA  
2501 C C   . ASN B 105 ? 0.7982 0.9987 0.9491 0.1934  -0.1926 -0.2300 139 ASN B C   
2502 O O   . ASN B 105 ? 0.7520 0.9233 0.8812 0.1968  -0.1963 -0.2218 139 ASN B O   
2503 C CB  . ASN B 105 ? 0.6388 0.8461 0.8311 0.1265  -0.1450 -0.1909 139 ASN B CB  
2504 C CG  . ASN B 105 ? 0.6324 0.9190 0.8718 0.1203  -0.1275 -0.2177 139 ASN B CG  
2505 O OD1 . ASN B 105 ? 0.7321 1.0594 0.9813 0.1452  -0.1416 -0.2497 139 ASN B OD1 
2506 N ND2 . ASN B 105 ? 0.5773 0.8857 0.8457 0.0871  -0.0965 -0.2060 139 ASN B ND2 
2507 N N   . ALA B 106 ? 0.7676 1.0274 0.9419 0.2160  -0.2008 -0.2647 140 ALA B N   
2508 C CA  . ALA B 106 ? 0.7104 1.0053 0.8878 0.2468  -0.2137 -0.2956 140 ALA B CA  
2509 C C   . ALA B 106 ? 0.7093 1.0334 0.9049 0.2258  -0.1894 -0.2932 140 ALA B C   
2510 O O   . ALA B 106 ? 0.7263 1.0368 0.9023 0.2432  -0.1998 -0.2997 140 ALA B O   
2511 C CB  . ALA B 106 ? 0.7138 1.0861 0.9267 0.2685  -0.2208 -0.3371 140 ALA B CB  
2512 N N   . LEU B 107 ? 0.6691 1.0287 0.8982 0.1884  -0.1568 -0.2832 141 LEU B N   
2513 C CA  . LEU B 107 ? 0.6126 0.9921 0.8507 0.1664  -0.1326 -0.2759 141 LEU B CA  
2514 C C   . LEU B 107 ? 0.7437 1.0540 0.9424 0.1614  -0.1388 -0.2438 141 LEU B C   
2515 O O   . LEU B 107 ? 0.7443 1.0598 0.9325 0.1646  -0.1369 -0.2470 141 LEU B O   
2516 C CB  . LEU B 107 ? 0.5464 0.9606 0.8191 0.1270  -0.0972 -0.2661 141 LEU B CB  
2517 C CG  . LEU B 107 ? 0.5364 0.9717 0.8148 0.1020  -0.0689 -0.2573 141 LEU B CG  
2518 C CD1 . LEU B 107 ? 0.6035 1.0877 0.8855 0.1211  -0.0718 -0.2904 141 LEU B CD1 
2519 C CD2 . LEU B 107 ? 0.5110 0.9795 0.8223 0.0659  -0.0340 -0.2531 141 LEU B CD2 
2520 N N   . SER B 108 ? 0.7381 0.9868 0.9155 0.1525  -0.1458 -0.2153 142 SER B N   
2521 C CA  . SER B 108 ? 0.7029 0.8901 0.8469 0.1452  -0.1511 -0.1880 142 SER B CA  
2522 C C   . SER B 108 ? 0.8052 0.9642 0.9159 0.1755  -0.1761 -0.2021 142 SER B C   
2523 O O   . SER B 108 ? 0.8599 1.0048 0.9554 0.1715  -0.1747 -0.1952 142 SER B O   
2524 C CB  . SER B 108 ? 0.7110 0.8420 0.8400 0.1317  -0.1549 -0.1618 142 SER B CB  
2525 O OG  . SER B 108 ? 0.7361 0.8899 0.8963 0.1039  -0.1314 -0.1491 142 SER B OG  
2526 N N   . ASN B 109 ? 0.7654 0.9145 0.8628 0.2074  -0.1999 -0.2228 143 ASN B N   
2527 C CA  . ASN B 109 ? 0.8392 0.9551 0.9028 0.2396  -0.2248 -0.2379 143 ASN B CA  
2528 C C   . ASN B 109 ? 0.8929 1.0695 0.9761 0.2546  -0.2213 -0.2681 143 ASN B C   
2529 O O   . ASN B 109 ? 0.8782 1.0297 0.9359 0.2781  -0.2384 -0.2808 143 ASN B O   
2530 C CB  . ASN B 109 ? 0.8434 0.9256 0.8820 0.2729  -0.2530 -0.2500 143 ASN B CB  
2531 C CG  . ASN B 109 ? 0.9111 0.9045 0.9055 0.2642  -0.2629 -0.2208 143 ASN B CG  
2532 O OD1 . ASN B 109 ? 0.9217 0.8737 0.9002 0.2400  -0.2541 -0.1973 143 ASN B OD1 
2533 N ND2 . ASN B 109 ? 0.9360 0.9018 0.9091 0.2833  -0.2808 -0.2236 143 ASN B ND2 
2534 N N   . GLN B 110 ? 0.8962 1.1502 1.0227 0.2401  -0.1983 -0.2813 144 GLN B N   
2535 C CA  . GLN B 110 ? 0.7967 1.1150 0.9434 0.2492  -0.1901 -0.3117 144 GLN B CA  
2536 C C   . GLN B 110 ? 0.8775 1.2071 1.0245 0.2190  -0.1651 -0.2947 144 GLN B C   
2537 O O   . GLN B 110 ? 0.9591 1.3095 1.1001 0.2293  -0.1654 -0.3124 144 GLN B O   
2538 C CB  . GLN B 110 ? 0.8032 1.2053 0.9962 0.2514  -0.1785 -0.3430 144 GLN B CB  
2539 N N   . LEU B 111 ? 0.8024 1.1183 0.9541 0.1840  -0.1445 -0.2618 145 LEU B N   
2540 C CA  . LEU B 111 ? 0.7930 1.1083 0.9361 0.1590  -0.1253 -0.2412 145 LEU B CA  
2541 C C   . LEU B 111 ? 0.7998 1.0464 0.9063 0.1580  -0.1401 -0.2160 145 LEU B C   
2542 O O   . LEU B 111 ? 0.7972 1.0405 0.8933 0.1401  -0.1286 -0.1984 145 LEU B O   
2543 C CB  . LEU B 111 ? 0.6788 1.0151 0.8450 0.1237  -0.0951 -0.2198 145 LEU B CB  
2544 C CG  . LEU B 111 ? 0.7231 1.0277 0.8983 0.1084  -0.0926 -0.1959 145 LEU B CG  
2545 C CD1 . LEU B 111 ? 0.8095 1.0508 0.9590 0.0976  -0.0994 -0.1611 145 LEU B CD1 
2546 C CD2 . LEU B 111 ? 0.6803 1.0252 0.8872 0.0803  -0.0613 -0.1920 145 LEU B CD2 
2547 N N   . ALA B 112 ? 0.7949 0.9861 0.8796 0.1757  -0.1650 -0.2145 146 ALA B N   
2548 C CA  . ALA B 112 ? 0.8014 0.9291 0.8524 0.1713  -0.1768 -0.1948 146 ALA B CA  
2549 C C   . ALA B 112 ? 0.8822 1.0088 0.9123 0.1863  -0.1863 -0.2118 146 ALA B C   
2550 O O   . ALA B 112 ? 0.9303 1.0390 0.9453 0.1708  -0.1829 -0.1961 146 ALA B O   
2551 C CB  . ALA B 112 ? 0.8441 0.9075 0.8729 0.1809  -0.1966 -0.1872 146 ALA B CB  
2552 N N   . PRO B 113 ? 0.9328 1.0797 0.9617 0.2167  -0.1989 -0.2453 147 PRO B N   
2553 C CA  . PRO B 113 ? 0.7528 0.8987 0.7623 0.2293  -0.2063 -0.2627 147 PRO B CA  
2554 C C   . PRO B 113 ? 0.7155 0.9102 0.7340 0.2074  -0.1837 -0.2580 147 PRO B C   
2555 O O   . PRO B 113 ? 0.7350 0.9147 0.7313 0.2056  -0.1877 -0.2581 147 PRO B O   
2556 C CB  . PRO B 113 ? 0.7770 0.9497 0.7930 0.2670  -0.2210 -0.3027 147 PRO B CB  
2557 C CG  . PRO B 113 ? 0.8756 1.0646 0.9132 0.2750  -0.2231 -0.3065 147 PRO B CG  
2558 C CD  . PRO B 113 ? 0.8670 1.0333 0.9095 0.2440  -0.2107 -0.2704 147 PRO B CD  
2559 N N   . GLN B 114 ? 0.7803 1.0306 0.8275 0.1898  -0.1596 -0.2542 148 GLN B N   
2560 C CA  . GLN B 114 ? 0.7206 1.0086 0.7678 0.1674  -0.1366 -0.2452 148 GLN B CA  
2561 C C   . GLN B 114 ? 0.7510 0.9993 0.7810 0.1436  -0.1333 -0.2071 148 GLN B C   
2562 O O   . GLN B 114 ? 0.7587 1.0196 0.7734 0.1320  -0.1244 -0.1988 148 GLN B O   
2563 C CB  . GLN B 114 ? 0.7796 1.1289 0.8582 0.1522  -0.1095 -0.2506 148 GLN B CB  
2564 C CG  . GLN B 114 ? 0.8135 1.2047 0.9195 0.1745  -0.1142 -0.2879 148 GLN B CG  
2565 C CD  . GLN B 114 ? 0.9337 1.3745 1.0748 0.1543  -0.0883 -0.2897 148 GLN B CD  
2566 O OE1 . GLN B 114 ? 0.8690 1.3130 1.0108 0.1232  -0.0637 -0.2638 148 GLN B OE1 
2567 N NE2 . GLN B 114 ? 0.8711 1.3498 1.0405 0.1727  -0.0942 -0.3215 148 GLN B NE2 
2568 N N   . GLU B 115 ? 0.8712 1.0744 0.9029 0.1370  -0.1409 -0.1854 149 GLU B N   
2569 C CA  . GLU B 115 ? 0.7849 0.9542 0.8061 0.1163  -0.1392 -0.1529 149 GLU B CA  
2570 C C   . GLU B 115 ? 0.8124 0.9265 0.8084 0.1230  -0.1617 -0.1520 149 GLU B C   
2571 O O   . GLU B 115 ? 0.9258 1.0097 0.9174 0.1070  -0.1632 -0.1290 149 GLU B O   
2572 C CB  . GLU B 115 ? 0.7780 0.9383 0.8208 0.0999  -0.1285 -0.1303 149 GLU B CB  
2573 C CG  . GLU B 115 ? 0.7805 0.9853 0.8437 0.0828  -0.1014 -0.1218 149 GLU B CG  
2574 C CD  . GLU B 115 ? 1.1196 1.3048 1.1935 0.0613  -0.0903 -0.0898 149 GLU B CD  
2575 O OE1 . GLU B 115 ? 1.1313 1.3158 1.2277 0.0561  -0.0841 -0.0879 149 GLU B OE1 
2576 O OE2 . GLU B 115 ? 1.1438 1.3159 1.2041 0.0510  -0.0888 -0.0684 149 GLU B OE2 
2577 N N   . GLY B 116 ? 0.8682 0.9681 0.8481 0.1459  -0.1785 -0.1784 150 GLY B N   
2578 C CA  . GLY B 116 ? 0.8245 0.8685 0.7767 0.1504  -0.1975 -0.1809 150 GLY B CA  
2579 C C   . GLY B 116 ? 0.9154 0.8987 0.8587 0.1508  -0.2094 -0.1720 150 GLY B C   
2580 O O   . GLY B 116 ? 0.8884 0.8186 0.8061 0.1497  -0.2224 -0.1730 150 GLY B O   
2581 N N   . MET B 117 ? 0.9159 0.9045 0.8770 0.1506  -0.2042 -0.1645 151 MET B N   
2582 C CA  . MET B 117 ? 0.9465 0.8784 0.8953 0.1495  -0.2138 -0.1546 151 MET B CA  
2583 C C   . MET B 117 ? 1.0625 0.9644 0.9905 0.1811  -0.2330 -0.1772 151 MET B C   
2584 O O   . MET B 117 ? 0.9966 0.9406 0.9373 0.2037  -0.2351 -0.1997 151 MET B O   
2585 C CB  . MET B 117 ? 0.9729 0.9244 0.9492 0.1340  -0.1995 -0.1362 151 MET B CB  
2586 C CG  . MET B 117 ? 0.9364 0.9207 0.9352 0.1078  -0.1802 -0.1147 151 MET B CG  
2587 S SD  . MET B 117 ? 0.8059 0.7439 0.7975 0.0821  -0.1807 -0.0897 151 MET B SD  
2588 C CE  . MET B 117 ? 0.8403 0.7885 0.8187 0.0777  -0.1842 -0.0922 151 MET B CE  
2589 N N   . THR B 118 ? 1.1811 1.0092 1.0755 0.1828  -0.2469 -0.1721 152 THR B N   
2590 C CA  . THR B 118 ? 1.0531 0.8384 0.9198 0.2143  -0.2671 -0.1882 152 THR B CA  
2591 C C   . THR B 118 ? 1.1380 0.9324 1.0170 0.2181  -0.2661 -0.1809 152 THR B C   
2592 O O   . THR B 118 ? 1.1980 0.9657 1.0744 0.1948  -0.2588 -0.1582 152 THR B O   
2593 C CB  . THR B 118 ? 1.1408 0.8343 0.9587 0.2123  -0.2803 -0.1841 152 THR B CB  
2594 O OG1 . THR B 118 ? 1.3615 1.0107 1.1668 0.1913  -0.2762 -0.1607 152 THR B OG1 
2595 C CG2 . THR B 118 ? 1.2198 0.9099 1.0340 0.1925  -0.2748 -0.1842 152 THR B CG2 
2596 N N   . ALA B 119 ? 1.0803 0.9170 0.9748 0.2470  -0.2732 -0.2028 153 ALA B N   
2597 C CA  . ALA B 119 ? 1.0089 0.8718 0.9228 0.2506  -0.2712 -0.2010 153 ALA B CA  
2598 C C   . ALA B 119 ? 1.0021 0.7875 0.8736 0.2587  -0.2876 -0.1899 153 ALA B C   
2599 O O   . ALA B 119 ? 1.1635 0.8724 0.9878 0.2668  -0.3021 -0.1873 153 ALA B O   
2600 C CB  . ALA B 119 ? 0.9541 0.8839 0.8947 0.2816  -0.2771 -0.2333 153 ALA B CB  
2601 N N   . ALA B 120 ? 0.9795 0.7835 0.8657 0.2549  -0.2839 -0.1836 154 ALA B N   
2602 C CA  . ALA B 120 ? 1.0389 0.7753 0.8836 0.2606  -0.2974 -0.1718 154 ALA B CA  
2603 C C   . ALA B 120 ? 1.0968 0.8158 0.9135 0.3087  -0.3262 -0.1948 154 ALA B C   
2604 O O   . ALA B 120 ? 1.1597 0.9331 1.0002 0.3369  -0.3341 -0.2229 154 ALA B O   
2605 C CB  . ALA B 120 ? 0.9817 0.7470 0.8530 0.2364  -0.2817 -0.1570 154 ALA B CB  
2606 N N   . GLN B 121 ? 1.2037 0.8452 0.9672 0.3188  -0.3421 -0.1834 155 GLN B N   
2607 C CA  . GLN B 121 ? 1.2520 0.8627 0.9781 0.3685  -0.3734 -0.2021 155 GLN B CA  
2608 C C   . GLN B 121 ? 1.1737 0.8667 0.9396 0.3908  -0.3796 -0.2232 155 GLN B C   
2609 O O   . GLN B 121 ? 1.2176 0.9544 0.9992 0.4302  -0.3966 -0.2545 155 GLN B O   
2610 C CB  . GLN B 121 ? 1.3940 0.8920 1.0440 0.3705  -0.3872 -0.1806 155 GLN B CB  
2611 C CG  . GLN B 121 ? 1.5095 0.9215 1.1168 0.3477  -0.3811 -0.1640 155 GLN B CG  
2612 C CD  . GLN B 121 ? 1.6879 0.9839 1.2149 0.3467  -0.3917 -0.1435 155 GLN B CD  
2613 O OE1 . GLN B 121 ? 1.6443 0.9256 1.1474 0.3584  -0.4014 -0.1371 155 GLN B OE1 
2614 N NE2 . GLN B 121 ? 1.6465 0.8588 1.1291 0.3312  -0.3890 -0.1341 155 GLN B NE2 
2615 N N   . HIS B 122 ? 1.2172 0.9354 1.0024 0.3658  -0.3657 -0.2096 156 HIS B N   
2616 C CA  . HIS B 122 ? 1.1525 0.9476 0.9754 0.3818  -0.3699 -0.2301 156 HIS B CA  
2617 C C   . HIS B 122 ? 1.0091 0.8976 0.9052 0.3463  -0.3378 -0.2331 156 HIS B C   
2618 O O   . HIS B 122 ? 1.0504 0.9332 0.9608 0.3075  -0.3132 -0.2119 156 HIS B O   
2619 C CB  . HIS B 122 ? 1.1462 0.8970 0.9302 0.3835  -0.3804 -0.2156 156 HIS B CB  
2620 C CG  . HIS B 122 ? 1.3062 0.9436 1.0052 0.4072  -0.4058 -0.2021 156 HIS B CG  
2621 N ND1 . HIS B 122 ? 1.3461 0.8935 0.9985 0.3770  -0.3954 -0.1717 156 HIS B ND1 
2622 C CD2 . HIS B 122 ? 1.2872 0.8837 0.9369 0.4581  -0.4409 -0.2156 156 HIS B CD2 
2623 C CE1 . HIS B 122 ? 1.4205 0.8716 0.9957 0.4049  -0.4205 -0.1656 156 HIS B CE1 
2624 N NE2 . HIS B 122 ? 1.4088 0.8844 0.9786 0.4563  -0.4496 -0.1906 156 HIS B NE2 
2625 N N   . SER B 123 ? 1.0717 1.0457 1.0133 0.3607  -0.3386 -0.2610 157 SER B N   
2626 C CA  . SER B 123 ? 1.0621 1.1252 1.0714 0.3296  -0.3079 -0.2685 157 SER B CA  
2627 C C   . SER B 123 ? 1.0972 1.1992 1.1305 0.3197  -0.3023 -0.2726 157 SER B C   
2628 O O   . SER B 123 ? 1.0695 1.1871 1.0940 0.3531  -0.3261 -0.2943 157 SER B O   
2629 C CB  . SER B 123 ? 0.9338 1.0762 0.9839 0.3496  -0.3075 -0.3049 157 SER B CB  
2630 O OG  . SER B 123 ? 1.1067 1.2242 1.1437 0.3486  -0.3045 -0.3001 157 SER B OG  
2631 N N   . LEU B 124 ? 0.8771 0.9951 0.9401 0.2755  -0.2720 -0.2533 158 LEU B N   
2632 C CA  . LEU B 124 ? 0.8722 1.0302 0.9636 0.2602  -0.2618 -0.2581 158 LEU B CA  
2633 C C   . LEU B 124 ? 0.8440 1.1044 1.0015 0.2534  -0.2437 -0.2893 158 LEU B C   
2634 O O   . LEU B 124 ? 0.8223 1.1158 1.0074 0.2402  -0.2250 -0.2931 158 LEU B O   
2635 C CB  . LEU B 124 ? 0.8498 0.9712 0.9410 0.2165  -0.2376 -0.2237 158 LEU B CB  
2636 C CG  . LEU B 124 ? 0.8328 0.8574 0.8640 0.2122  -0.2478 -0.1927 158 LEU B CG  
2637 C CD1 . LEU B 124 ? 0.8639 0.8700 0.9098 0.1676  -0.2195 -0.1639 158 LEU B CD1 
2638 C CD2 . LEU B 124 ? 0.8836 0.8755 0.8743 0.2322  -0.2701 -0.1953 158 LEU B CD2 
2639 N N   . THR B 125 ? 0.7798 1.0905 0.9605 0.2610  -0.2486 -0.3127 159 THR B N   
2640 C CA  . THR B 125 ? 0.7022 1.1117 0.9476 0.2485  -0.2283 -0.3450 159 THR B CA  
2641 C C   . THR B 125 ? 0.7357 1.1634 1.0077 0.2145  -0.2070 -0.3388 159 THR B C   
2642 O O   . THR B 125 ? 0.7187 1.0963 0.9588 0.2130  -0.2168 -0.3200 159 THR B O   
2643 C CB  . THR B 125 ? 0.7245 1.1978 0.9843 0.2922  -0.2546 -0.3915 159 THR B CB  
2644 O OG1 . THR B 125 ? 0.7978 1.2296 1.0123 0.3264  -0.2899 -0.3913 159 THR B OG1 
2645 C CG2 . THR B 125 ? 0.6248 1.1046 0.8787 0.3189  -0.2655 -0.4060 159 THR B CG2 
2646 N N   . PHE B 126 ? 0.6863 1.1845 1.0155 0.1856  -0.1760 -0.3558 160 PHE B N   
2647 C CA  . PHE B 126 ? 0.6168 1.1315 0.9759 0.1488  -0.1505 -0.3507 160 PHE B CA  
2648 C C   . PHE B 126 ? 0.6775 1.2910 1.0945 0.1429  -0.1377 -0.3958 160 PHE B C   
2649 O O   . PHE B 126 ? 0.7686 1.4404 1.2129 0.1507  -0.1329 -0.4239 160 PHE B O   
2650 C CB  . PHE B 126 ? 0.5418 1.0218 0.9084 0.1066  -0.1164 -0.3155 160 PHE B CB  
2651 C CG  . PHE B 126 ? 0.6646 1.0566 0.9812 0.1089  -0.1267 -0.2751 160 PHE B CG  
2652 C CD1 . PHE B 126 ? 0.6607 1.0287 0.9543 0.1231  -0.1350 -0.2665 160 PHE B CD1 
2653 C CD2 . PHE B 126 ? 0.6475 0.9845 0.9417 0.0954  -0.1270 -0.2489 160 PHE B CD2 
2654 C CE1 . PHE B 126 ? 0.6530 0.9438 0.9033 0.1228  -0.1436 -0.2330 160 PHE B CE1 
2655 C CE2 . PHE B 126 ? 0.6128 0.8745 0.8645 0.0945  -0.1346 -0.2157 160 PHE B CE2 
2656 C CZ  . PHE B 126 ? 0.6372 0.8759 0.8673 0.1078  -0.1430 -0.2081 160 PHE B CZ  
2657 N N   . ALA B 127 ? 0.6996 1.3343 1.1363 0.1273  -0.1308 -0.4049 161 ALA B N   
2658 C CA  . ALA B 127 ? 0.6328 1.3623 1.1272 0.1164  -0.1165 -0.4499 161 ALA B CA  
2659 C C   . ALA B 127 ? 0.6342 1.3835 1.1705 0.0653  -0.0686 -0.4439 161 ALA B C   
2660 O O   . ALA B 127 ? 0.7455 1.4424 1.2657 0.0460  -0.0507 -0.4080 161 ALA B O   
2661 C CB  . ALA B 127 ? 0.7183 1.4621 1.2129 0.1231  -0.1317 -0.4648 161 ALA B CB  
2662 N N   . ALA B 128 ? 0.6911 1.4968 1.2643 0.0424  -0.0461 -0.4747 162 ALA B N   
2663 C CA  . ALA B 128 ? 0.6699 1.4703 1.2625 -0.0065 0.0004  -0.4647 162 ALA B CA  
2664 C C   . ALA B 128 ? 0.5903 1.3388 1.1844 -0.0367 0.0185  -0.4305 162 ALA B C   
2665 O O   . ALA B 128 ? 0.6496 1.3646 1.2465 -0.0678 0.0488  -0.4035 162 ALA B O   
2666 C CB  . ALA B 128 ? 0.7173 1.5644 1.3245 -0.0223 0.0177  -0.5028 162 ALA B CB  
2667 N N   . ASN B 129 ? 0.5813 1.3199 1.1701 -0.0271 -0.0002 -0.4311 163 ASN B N   
2668 C CA  . ASN B 129 ? 0.5313 1.2202 1.1205 -0.0548 0.0161  -0.4013 163 ASN B CA  
2669 C C   . ASN B 129 ? 0.6231 1.2269 1.1685 -0.0507 0.0104  -0.3515 163 ASN B C   
2670 O O   . ASN B 129 ? 0.6892 1.2447 1.2327 -0.0764 0.0299  -0.3224 163 ASN B O   
2671 C CB  . ASN B 129 ? 0.4854 1.1807 1.0697 -0.0446 -0.0034 -0.4148 163 ASN B CB  
2672 C CG  . ASN B 129 ? 0.5260 1.1975 1.0608 0.0017  -0.0490 -0.4110 163 ASN B CG  
2673 O OD1 . ASN B 129 ? 0.6375 1.2992 1.1490 0.0289  -0.0675 -0.4064 163 ASN B OD1 
2674 N ND2 . ASN B 129 ? 0.5110 1.1691 1.0255 0.0108  -0.0667 -0.4128 163 ASN B ND2 
2675 N N   . GLY B 130 ? 0.8344 1.2245 1.0542 0.0372  -0.1824 -0.2984 164 GLY B N   
2676 C CA  . GLY B 130 ? 0.7766 1.0752 0.9378 0.0329  -0.1702 -0.2669 164 GLY B CA  
2677 C C   . GLY B 130 ? 0.8134 1.0508 0.8789 0.0449  -0.1944 -0.2442 164 GLY B C   
2678 O O   . GLY B 130 ? 0.8616 1.0225 0.8771 0.0522  -0.1903 -0.2176 164 GLY B O   
2679 N N   . TRP B 131 ? 0.7277 0.9971 0.7669 0.0475  -0.2188 -0.2540 165 TRP B N   
2680 C CA  . TRP B 131 ? 0.7049 0.9154 0.6518 0.0570  -0.2381 -0.2285 165 TRP B CA  
2681 C C   . TRP B 131 ? 0.8728 1.0468 0.7736 0.1041  -0.2606 -0.2035 165 TRP B C   
2682 O O   . TRP B 131 ? 0.8613 1.0796 0.7994 0.1339  -0.2709 -0.2129 165 TRP B O   
2683 C CB  . TRP B 131 ? 0.7446 1.0058 0.6730 0.0490  -0.2572 -0.2453 165 TRP B CB  
2684 C CG  . TRP B 131 ? 0.7662 1.0481 0.7260 0.0022  -0.2356 -0.2683 165 TRP B CG  
2685 C CD1 . TRP B 131 ? 0.6704 1.0306 0.7089 -0.0193 -0.2266 -0.3071 165 TRP B CD1 
2686 C CD2 . TRP B 131 ? 0.7394 0.9615 0.6584 -0.0288 -0.2182 -0.2547 165 TRP B CD2 
2687 N NE1 . TRP B 131 ? 0.6106 0.9489 0.6562 -0.0581 -0.1984 -0.3074 165 TRP B NE1 
2688 C CE2 . TRP B 131 ? 0.7293 0.9955 0.7037 -0.0660 -0.1987 -0.2845 165 TRP B CE2 
2689 C CE3 . TRP B 131 ? 0.7494 0.8831 0.5952 -0.0288 -0.2150 -0.2194 165 TRP B CE3 
2690 C CZ2 . TRP B 131 ? 0.7060 0.9282 0.6628 -0.0988 -0.1751 -0.2748 165 TRP B CZ2 
2691 C CZ3 . TRP B 131 ? 0.8249 0.9252 0.6552 -0.0657 -0.1949 -0.2182 165 TRP B CZ3 
2692 C CH2 . TRP B 131 ? 0.7430 0.8941 0.6275 -0.1008 -0.1784 -0.2513 165 TRP B CH2 
2693 N N   . VAL B 132 ? 0.8896 0.9812 0.7124 0.1103  -0.2669 -0.1719 166 VAL B N   
2694 C CA  . VAL B 132 ? 1.0005 1.0422 0.7790 0.1533  -0.2855 -0.1463 166 VAL B CA  
2695 C C   . VAL B 132 ? 1.0004 1.0867 0.7560 0.1894  -0.3200 -0.1455 166 VAL B C   
2696 O O   . VAL B 132 ? 0.9944 1.1225 0.7333 0.1793  -0.3318 -0.1538 166 VAL B O   
2697 C CB  . VAL B 132 ? 1.0270 0.9645 0.7357 0.1458  -0.2797 -0.1138 166 VAL B CB  
2698 C CG1 . VAL B 132 ? 0.9147 0.8365 0.5602 0.1359  -0.2911 -0.0984 166 VAL B CG1 
2699 C CG2 . VAL B 132 ? 1.0530 0.9310 0.7339 0.1863  -0.2915 -0.0925 166 VAL B CG2 
2700 N N   . ASP B 133 ? 0.9266 1.0087 0.6824 0.2337  -0.3368 -0.1374 167 ASP B N   
2701 C CA  . ASP B 133 ? 1.0653 1.1805 0.7937 0.2753  -0.3723 -0.1313 167 ASP B CA  
2702 C C   . ASP B 133 ? 1.1229 1.1649 0.7584 0.2821  -0.3853 -0.0941 167 ASP B C   
2703 O O   . ASP B 133 ? 1.1109 1.0591 0.7059 0.2860  -0.3770 -0.0658 167 ASP B O   
2704 C CB  . ASP B 133 ? 1.1798 1.2990 0.9314 0.3224  -0.3850 -0.1299 167 ASP B CB  
2705 C CG  . ASP B 133 ? 1.1496 1.3687 0.9920 0.3255  -0.3811 -0.1675 167 ASP B CG  
2706 O OD1 . ASP B 133 ? 1.1013 1.4060 0.9732 0.3227  -0.3956 -0.1913 167 ASP B OD1 
2707 O OD2 . ASP B 133 ? 1.0454 1.2596 0.9309 0.3306  -0.3628 -0.1741 167 ASP B OD2 
2708 N N   . PRO B 134 ? 1.0908 1.1724 0.6908 0.2832  -0.4041 -0.0931 168 PRO B N   
2709 C CA  . PRO B 134 ? 1.1359 1.1470 0.6436 0.2900  -0.4130 -0.0527 168 PRO B CA  
2710 C C   . PRO B 134 ? 1.2975 1.2437 0.7715 0.3328  -0.4235 -0.0164 168 PRO B C   
2711 O O   . PRO B 134 ? 1.2913 1.1537 0.7011 0.3324  -0.4188 0.0216  168 PRO B O   
2712 C CB  . PRO B 134 ? 1.2063 1.2948 0.7067 0.2825  -0.4220 -0.0629 168 PRO B CB  
2713 C CG  . PRO B 134 ? 1.1700 1.3545 0.7531 0.2579  -0.4155 -0.1137 168 PRO B CG  
2714 C CD  . PRO B 134 ? 1.0437 1.2361 0.6895 0.2749  -0.4137 -0.1293 168 PRO B CD  
2715 N N   . ALA B 135 ? 1.3474 1.3297 0.8680 0.3676  -0.4344 -0.0283 169 ALA B N   
2716 C CA  . ALA B 135 ? 1.3615 1.2832 0.8603 0.4069  -0.4414 0.0003  169 ALA B CA  
2717 C C   . ALA B 135 ? 1.4461 1.2732 0.9383 0.4049  -0.4259 0.0120  169 ALA B C   
2718 O O   . ALA B 135 ? 1.5746 1.3435 1.0523 0.4326  -0.4275 0.0330  169 ALA B O   
2719 C CB  . ALA B 135 ? 1.3259 1.3208 0.8798 0.4427  -0.4561 -0.0208 169 ALA B CB  
2720 N N   . THR B 136 ? 1.3239 1.1361 0.8293 0.3722  -0.4107 -0.0030 170 THR B N   
2721 C CA  . THR B 136 ? 1.2781 1.0028 0.7803 0.3633  -0.3917 0.0055  170 THR B CA  
2722 C C   . THR B 136 ? 1.3447 0.9985 0.8052 0.3197  -0.3703 0.0238  170 THR B C   
2723 O O   . THR B 136 ? 1.3820 0.9544 0.8327 0.3124  -0.3561 0.0341  170 THR B O   
2724 C CB  . THR B 136 ? 1.2531 1.0222 0.8295 0.3506  -0.3724 -0.0292 170 THR B CB  
2725 O OG1 . THR B 136 ? 1.2377 1.0629 0.8473 0.3044  -0.3534 -0.0513 170 THR B OG1 
2726 C CG2 . THR B 136 ? 1.2482 1.0890 0.8714 0.3930  -0.3901 -0.0481 170 THR B CG2 
2727 N N   . ALA B 137 ? 1.3713 1.0565 0.8096 0.2909  -0.3676 0.0251  171 ALA B N   
2728 C CA  . ALA B 137 ? 1.2865 0.9116 0.6855 0.2496  -0.3466 0.0422  171 ALA B CA  
2729 C C   . ALA B 137 ? 1.3963 0.9901 0.7191 0.2629  -0.3609 0.0793  171 ALA B C   
2730 O O   . ALA B 137 ? 1.4852 1.1262 0.7868 0.2439  -0.3612 0.0766  171 ALA B O   
2731 C CB  . ALA B 137 ? 1.1629 0.8484 0.6002 0.2016  -0.3262 0.0122  171 ALA B CB  
2732 N N   . PRO B 138 ? 1.4853 1.0042 0.7723 0.2929  -0.3677 0.1131  172 PRO B N   
2733 C CA  . PRO B 138 ? 1.5732 1.0798 0.8101 0.3041  -0.3709 0.1487  172 PRO B CA  
2734 C C   . PRO B 138 ? 1.6502 1.0968 0.8374 0.2651  -0.3491 0.1730  172 PRO B C   
2735 O O   . PRO B 138 ? 1.7038 1.0660 0.8886 0.2458  -0.3299 0.1837  172 PRO B O   
2736 C CB  . PRO B 138 ? 1.5223 0.9741 0.7648 0.3404  -0.3746 0.1696  172 PRO B CB  
2737 C CG  . PRO B 138 ? 1.4803 0.8767 0.7567 0.3305  -0.3614 0.1530  172 PRO B CG  
2738 C CD  . PRO B 138 ? 1.5052 0.9570 0.8152 0.3094  -0.3615 0.1157  172 PRO B CD  
2739 N N   . ASN B 139 ? 1.7292 1.2253 0.8817 0.2524  -0.3504 0.1788  173 ASN B N   
2740 C CA  . ASN B 139 ? 1.8401 1.2925 0.9439 0.2159  -0.3278 0.2019  173 ASN B CA  
2741 C C   . ASN B 139 ? 1.7323 1.1398 0.8505 0.1712  -0.3066 0.1843  173 ASN B C   
2742 O O   . ASN B 139 ? 1.7645 1.0923 0.8653 0.1463  -0.2832 0.2058  173 ASN B O   
2743 C CB  . ASN B 139 ? 1.9749 1.3505 1.0430 0.2294  -0.3175 0.2502  173 ASN B CB  
2744 C CG  . ASN B 139 ? 2.0065 1.3683 1.0214 0.2018  -0.2977 0.2779  173 ASN B CG  
2745 O OD1 . ASN B 139 ? 1.8550 1.2646 0.8573 0.1721  -0.2915 0.2592  173 ASN B OD1 
2746 N ND2 . ASN B 139 ? 2.0399 1.3396 1.0276 0.2107  -0.2860 0.3216  173 ASN B ND2 
2747 N N   . PHE B 140 ? 1.5886 1.0681 0.7710 0.1550  -0.3048 0.1385  174 PHE B N   
2748 C CA  . PHE B 140 ? 1.4647 0.9290 0.6934 0.1095  -0.2764 0.1146  174 PHE B CA  
2749 C C   . PHE B 140 ? 1.4759 0.9500 0.6847 0.0637  -0.2536 0.1133  174 PHE B C   
2750 O O   . PHE B 140 ? 1.3688 0.8288 0.6134 0.0251  -0.2296 0.0955  174 PHE B O   
2751 C CB  . PHE B 140 ? 1.3570 0.8952 0.6627 0.1079  -0.2784 0.0701  174 PHE B CB  
2752 C CG  . PHE B 140 ? 1.2989 0.7962 0.6427 0.1235  -0.2772 0.0639  174 PHE B CG  
2753 C CD1 . PHE B 140 ? 1.4326 0.8583 0.7464 0.1588  -0.2897 0.0914  174 PHE B CD1 
2754 C CD2 . PHE B 140 ? 1.1580 0.6877 0.5666 0.1041  -0.2629 0.0307  174 PHE B CD2 
2755 C CE1 . PHE B 140 ? 1.3434 0.7346 0.6915 0.1741  -0.2888 0.0814  174 PHE B CE1 
2756 C CE2 . PHE B 140 ? 1.2472 0.7440 0.6854 0.1204  -0.2615 0.0244  174 PHE B CE2 
2757 C CZ  . PHE B 140 ? 1.2743 0.7034 0.6821 0.1552  -0.2749 0.0475  174 PHE B CZ  
2758 N N   . GLY B 141 ? 1.5521 1.0524 0.7044 0.0686  -0.2608 0.1308  175 GLY B N   
2759 C CA  . GLY B 141 ? 1.6170 1.1260 0.7435 0.0281  -0.2385 0.1312  175 GLY B CA  
2760 C C   . GLY B 141 ? 1.5856 1.1729 0.7731 -0.0066 -0.2267 0.0820  175 GLY B C   
2761 O O   . GLY B 141 ? 1.5321 1.2025 0.7568 0.0060  -0.2433 0.0503  175 GLY B O   
2762 N N   . PRO B 142 ? 1.3888 0.9505 0.5924 -0.0512 -0.1969 0.0742  176 PRO B N   
2763 C CA  . PRO B 142 ? 1.2519 0.8820 0.5152 -0.0851 -0.1833 0.0291  176 PRO B CA  
2764 C C   . PRO B 142 ? 1.1818 0.8306 0.5245 -0.0842 -0.1837 -0.0007 176 PRO B C   
2765 O O   . PRO B 142 ? 1.1223 0.8323 0.5207 -0.1065 -0.1747 -0.0374 176 PRO B O   
2766 C CB  . PRO B 142 ? 1.3455 0.9314 0.5973 -0.1286 -0.1516 0.0361  176 PRO B CB  
2767 C CG  . PRO B 142 ? 1.4031 0.8885 0.6243 -0.1205 -0.1467 0.0749  176 PRO B CG  
2768 C CD  . PRO B 142 ? 1.3761 0.8462 0.5478 -0.0728 -0.1740 0.1055  176 PRO B CD  
2769 N N   . LEU B 143 ? 1.2271 0.8256 0.5771 -0.0586 -0.1925 0.0140  177 LEU B N   
2770 C CA  . LEU B 143 ? 1.1570 0.7708 0.5764 -0.0566 -0.1902 -0.0111 177 LEU B CA  
2771 C C   . LEU B 143 ? 1.1781 0.8787 0.6364 -0.0341 -0.2085 -0.0369 177 LEU B C   
2772 O O   . LEU B 143 ? 1.2056 0.9197 0.6386 0.0039  -0.2333 -0.0254 177 LEU B O   
2773 C CB  . LEU B 143 ? 1.1291 0.6662 0.5408 -0.0338 -0.1946 0.0096  177 LEU B CB  
2774 C CG  . LEU B 143 ? 1.2600 0.7069 0.6419 -0.0546 -0.1776 0.0328  177 LEU B CG  
2775 C CD1 . LEU B 143 ? 1.1659 0.5522 0.5628 -0.0354 -0.1812 0.0377  177 LEU B CD1 
2776 C CD2 . LEU B 143 ? 1.1181 0.5748 0.5267 -0.1023 -0.1511 0.0150  177 LEU B CD2 
2777 N N   . ARG B 144 ? 1.0646 0.8237 0.5880 -0.0574 -0.1959 -0.0718 178 ARG B N   
2778 C CA  . ARG B 144 ? 1.0143 0.8577 0.5915 -0.0428 -0.2079 -0.1011 178 ARG B CA  
2779 C C   . ARG B 144 ? 0.9889 0.8274 0.6276 -0.0394 -0.1972 -0.1119 178 ARG B C   
2780 O O   . ARG B 144 ? 0.8617 0.7136 0.5508 -0.0685 -0.1751 -0.1305 178 ARG B O   
2781 C CB  . ARG B 144 ? 0.9004 0.8174 0.5084 -0.0724 -0.1999 -0.1337 178 ARG B CB  
2782 C CG  . ARG B 144 ? 1.0491 0.9888 0.5953 -0.0702 -0.2133 -0.1277 178 ARG B CG  
2783 C CD  . ARG B 144 ? 1.1668 1.1152 0.6684 -0.0234 -0.2456 -0.1083 178 ARG B CD  
2784 N NE  . ARG B 144 ? 1.3710 1.4032 0.9287 -0.0034 -0.2635 -0.1391 178 ARG B NE  
2785 C CZ  . ARG B 144 ? 1.3605 1.3959 0.9307 0.0350  -0.2821 -0.1319 178 ARG B CZ  
2786 N NH1 . ARG B 144 ? 1.2890 1.2466 0.8191 0.0595  -0.2867 -0.0961 178 ARG B NH1 
2787 N NH2 . ARG B 144 ? 1.2149 1.3345 0.8437 0.0489  -0.2958 -0.1637 178 ARG B NH2 
2788 N N   . VAL B 145 ? 1.0196 0.8393 0.6525 -0.0017 -0.2127 -0.0994 179 VAL B N   
2789 C CA  . VAL B 145 ? 0.8398 0.6520 0.5205 0.0069  -0.2030 -0.1065 179 VAL B CA  
2790 C C   . VAL B 145 ? 0.9173 0.8175 0.6701 0.0087  -0.2010 -0.1367 179 VAL B C   
2791 O O   . VAL B 145 ? 0.8864 0.8448 0.6460 0.0279  -0.2203 -0.1471 179 VAL B O   
2792 C CB  . VAL B 145 ? 0.8499 0.6099 0.4982 0.0475  -0.2193 -0.0846 179 VAL B CB  
2793 C CG1 . VAL B 145 ? 0.8875 0.6429 0.5805 0.0572  -0.2081 -0.0939 179 VAL B CG1 
2794 C CG2 . VAL B 145 ? 0.8746 0.5450 0.4568 0.0435  -0.2198 -0.0549 179 VAL B CG2 
2795 N N   . PHE B 146 ? 0.8199 0.7310 0.6288 -0.0108 -0.1773 -0.1505 180 PHE B N   
2796 C CA  . PHE B 146 ? 0.7433 0.7318 0.6289 -0.0144 -0.1684 -0.1772 180 PHE B CA  
2797 C C   . PHE B 146 ? 0.7717 0.7474 0.6956 -0.0071 -0.1504 -0.1749 180 PHE B C   
2798 O O   . PHE B 146 ? 0.8052 0.7245 0.7124 -0.0184 -0.1366 -0.1624 180 PHE B O   
2799 C CB  . PHE B 146 ? 0.7786 0.8076 0.7025 -0.0552 -0.1520 -0.2000 180 PHE B CB  
2800 C CG  . PHE B 146 ? 0.6764 0.7744 0.6887 -0.0650 -0.1362 -0.2266 180 PHE B CG  
2801 C CD1 . PHE B 146 ? 0.7026 0.8762 0.7532 -0.0521 -0.1504 -0.2491 180 PHE B CD1 
2802 C CD2 . PHE B 146 ? 0.5692 0.6571 0.6289 -0.0869 -0.1069 -0.2287 180 PHE B CD2 
2803 C CE1 . PHE B 146 ? 0.6923 0.9281 0.8314 -0.0638 -0.1331 -0.2740 180 PHE B CE1 
2804 C CE2 . PHE B 146 ? 0.6218 0.7684 0.7650 -0.0965 -0.0891 -0.2493 180 PHE B CE2 
2805 C CZ  . PHE B 146 ? 0.6314 0.8510 0.8168 -0.0865 -0.1010 -0.2724 180 PHE B CZ  
2806 N N   . TYR B 147 ? 0.7186 0.8539 0.9205 -0.1152 -0.0990 -0.1175 181 TYR B N   
2807 C CA  . TYR B 147 ? 0.7230 0.8782 0.9465 -0.1146 -0.0722 -0.1162 181 TYR B CA  
2808 C C   . TYR B 147 ? 0.6959 0.8259 0.9034 -0.1363 -0.0617 -0.1140 181 TYR B C   
2809 O O   . TYR B 147 ? 0.7387 0.8805 0.9751 -0.1590 -0.0725 -0.1161 181 TYR B O   
2810 C CB  . TYR B 147 ? 0.7216 0.9327 1.0129 -0.1130 -0.0726 -0.1199 181 TYR B CB  
2811 C CG  . TYR B 147 ? 0.7385 0.9755 1.0518 -0.1165 -0.0428 -0.1200 181 TYR B CG  
2812 C CD1 . TYR B 147 ? 0.7216 0.9494 1.0062 -0.1015 -0.0206 -0.1181 181 TYR B CD1 
2813 C CD2 . TYR B 147 ? 0.6275 0.9015 0.9894 -0.1367 -0.0369 -0.1219 181 TYR B CD2 
2814 C CE1 . TYR B 147 ? 0.6779 0.9275 0.9740 -0.1057 0.0066  -0.1174 181 TYR B CE1 
2815 C CE2 . TYR B 147 ? 0.6277 0.9272 1.0050 -0.1425 -0.0064 -0.1212 181 TYR B CE2 
2816 C CZ  . TYR B 147 ? 0.6429 0.9275 0.9834 -0.1265 0.0153  -0.1186 181 TYR B CZ  
2817 O OH  . TYR B 147 ? 0.6816 0.9896 1.0290 -0.1333 0.0456  -0.1172 181 TYR B OH  
2818 N N   . PRO B 148 ? 0.7549 0.8492 0.9177 -0.1310 -0.0431 -0.1093 182 PRO B N   
2819 C CA  . PRO B 148 ? 0.7615 0.8178 0.9009 -0.1514 -0.0349 -0.1052 182 PRO B CA  
2820 C C   . PRO B 148 ? 0.7603 0.8390 0.9255 -0.1667 -0.0122 -0.0983 182 PRO B C   
2821 O O   . PRO B 148 ? 0.6479 0.6886 0.7879 -0.1851 -0.0034 -0.0915 182 PRO B O   
2822 C CB  . PRO B 148 ? 0.6877 0.6935 0.7651 -0.1319 -0.0277 -0.1027 182 PRO B CB  
2823 C CG  . PRO B 148 ? 0.6187 0.6547 0.7009 -0.1062 -0.0190 -0.1018 182 PRO B CG  
2824 C CD  . PRO B 148 ? 0.6532 0.7370 0.7830 -0.1055 -0.0318 -0.1072 182 PRO B CD  
2825 N N   . GLY B 149 ? 0.7169 0.8526 0.9281 -0.1601 -0.0018 -0.1001 183 GLY B N   
2826 C CA  . GLY B 149 ? 0.6536 0.8163 0.8859 -0.1738 0.0241  -0.0947 183 GLY B CA  
2827 C C   . GLY B 149 ? 0.7314 0.8873 0.9300 -0.1535 0.0455  -0.0893 183 GLY B C   
2828 O O   . GLY B 149 ? 0.6444 0.7749 0.8062 -0.1296 0.0394  -0.0896 183 GLY B O   
2829 N N   . PRO B 150 ? 0.7202 0.9024 0.9306 -0.1640 0.0712  -0.0847 184 PRO B N   
2830 C CA  . PRO B 150 ? 0.7204 0.8973 0.8942 -0.1461 0.0903  -0.0798 184 PRO B CA  
2831 C C   . PRO B 150 ? 0.7572 0.8663 0.8616 -0.1414 0.0893  -0.0661 184 PRO B C   
2832 O O   . PRO B 150 ? 0.7706 0.8366 0.8523 -0.1620 0.0888  -0.0560 184 PRO B O   
2833 C CB  . PRO B 150 ? 0.6355 0.8532 0.8331 -0.1652 0.1192  -0.0770 184 PRO B CB  
2834 C CG  . PRO B 150 ? 0.8315 1.0779 1.0820 -0.1945 0.1162  -0.0796 184 PRO B CG  
2835 C CD  . PRO B 150 ? 0.7534 0.9803 1.0152 -0.1929 0.0836  -0.0854 184 PRO B CD  
2836 N N   . GLY B 151 ? 0.7563 0.8558 0.8287 -0.1133 0.0876  -0.0666 185 GLY B N   
2837 C CA  . GLY B 151 ? 0.7808 0.8243 0.7924 -0.1012 0.0852  -0.0550 185 GLY B CA  
2838 C C   . GLY B 151 ? 0.7562 0.8107 0.7410 -0.0784 0.0932  -0.0529 185 GLY B C   
2839 O O   . GLY B 151 ? 0.7961 0.8591 0.7660 -0.0856 0.1120  -0.0449 185 GLY B O   
2840 N N   . HIS B 152 ? 0.6418 0.6978 0.6183 -0.0530 0.0791  -0.0601 186 HIS B N   
2841 C CA  . HIS B 152 ? 0.6829 0.7580 0.6416 -0.0331 0.0829  -0.0616 186 HIS B CA  
2842 C C   . HIS B 152 ? 0.7108 0.8363 0.7027 -0.0381 0.0955  -0.0724 186 HIS B C   
2843 O O   . HIS B 152 ? 0.6976 0.8353 0.6680 -0.0331 0.1076  -0.0710 186 HIS B O   
2844 C CB  . HIS B 152 ? 0.6359 0.7136 0.5919 -0.0104 0.0654  -0.0695 186 HIS B CB  
2845 C CG  . HIS B 152 ? 0.6124 0.7218 0.5657 0.0050  0.0656  -0.0762 186 HIS B CG  
2846 N ND1 . HIS B 152 ? 0.7467 0.8476 0.6607 0.0190  0.0665  -0.0682 186 HIS B ND1 
2847 C CD2 . HIS B 152 ? 0.6428 0.7889 0.6261 0.0078  0.0625  -0.0904 186 HIS B CD2 
2848 C CE1 . HIS B 152 ? 0.7418 0.8764 0.6626 0.0278  0.0641  -0.0787 186 HIS B CE1 
2849 N NE2 . HIS B 152 ? 0.6506 0.8101 0.6125 0.0208  0.0624  -0.0924 186 HIS B NE2 
2850 N N   . THR B 153 ? 0.6070 0.7611 0.6494 -0.0459 0.0917  -0.0842 187 THR B N   
2851 C CA  . THR B 153 ? 0.5938 0.7943 0.6761 -0.0508 0.1049  -0.0959 187 THR B CA  
2852 C C   . THR B 153 ? 0.6772 0.8938 0.8058 -0.0712 0.1056  -0.0975 187 THR B C   
2853 O O   . THR B 153 ? 0.6651 0.8542 0.7916 -0.0821 0.0932  -0.0907 187 THR B O   
2854 C CB  . THR B 153 ? 0.5939 0.8196 0.6991 -0.0325 0.0942  -0.1126 187 THR B CB  
2855 O OG1 . THR B 153 ? 0.6554 0.8714 0.7793 -0.0297 0.0717  -0.1149 187 THR B OG1 
2856 C CG2 . THR B 153 ? 0.6607 0.8786 0.7246 -0.0162 0.0935  -0.1130 187 THR B CG2 
2857 N N   . SER B 154 ? 0.5515 0.8154 0.7236 -0.0759 0.1198  -0.1082 188 SER B N   
2858 C CA  . SER B 154 ? 0.5695 0.8626 0.7970 -0.0940 0.1191  -0.1117 188 SER B CA  
2859 C C   . SER B 154 ? 0.5719 0.8779 0.8422 -0.0830 0.0925  -0.1228 188 SER B C   
2860 O O   . SER B 154 ? 0.6043 0.9354 0.9227 -0.0957 0.0850  -0.1258 188 SER B O   
2861 C CB  . SER B 154 ? 0.5826 0.9295 0.8450 -0.1019 0.1471  -0.1200 188 SER B CB  
2862 O OG  . SER B 154 ? 0.7674 1.1016 0.9935 -0.1234 0.1715  -0.1050 188 SER B OG  
2863 N N   . ASP B 155 ? 0.5235 0.8132 0.7764 -0.0615 0.0770  -0.1275 189 ASP B N   
2864 C CA  . ASP B 155 ? 0.5610 0.8566 0.8456 -0.0513 0.0516  -0.1351 189 ASP B CA  
2865 C C   . ASP B 155 ? 0.5689 0.8224 0.8140 -0.0461 0.0312  -0.1282 189 ASP B C   
2866 O O   . ASP B 155 ? 0.6015 0.8534 0.8601 -0.0381 0.0105  -0.1319 189 ASP B O   
2867 C CB  . ASP B 155 ? 0.5358 0.8583 0.8469 -0.0312 0.0533  -0.1506 189 ASP B CB  
2868 C CG  . ASP B 155 ? 0.6245 0.9306 0.8906 -0.0188 0.0627  -0.1527 189 ASP B CG  
2869 O OD1 . ASP B 155 ? 0.6813 0.9808 0.9119 -0.0248 0.0816  -0.1461 189 ASP B OD1 
2870 O OD2 . ASP B 155 ? 0.6901 0.9881 0.9545 -0.0044 0.0493  -0.1601 189 ASP B OD2 
2871 N N   . ASN B 156 ? 0.6592 0.8790 0.8553 -0.0495 0.0369  -0.1180 190 ASN B N   
2872 C CA  . ASN B 156 ? 0.6771 0.8646 0.8373 -0.0415 0.0220  -0.1141 190 ASN B CA  
2873 C C   . ASN B 156 ? 0.6225 0.7965 0.7914 -0.0513 0.0016  -0.1132 190 ASN B C   
2874 O O   . ASN B 156 ? 0.6274 0.7951 0.8049 -0.0682 0.0008  -0.1104 190 ASN B O   
2875 C CB  . ASN B 156 ? 0.5705 0.7266 0.6811 -0.0393 0.0322  -0.1047 190 ASN B CB  
2876 C CG  . ASN B 156 ? 0.6895 0.8294 0.7934 -0.0573 0.0435  -0.0963 190 ASN B CG  
2877 O OD1 . ASN B 156 ? 0.6492 0.8075 0.7893 -0.0745 0.0446  -0.0983 190 ASN B OD1 
2878 N ND2 . ASN B 156 ? 0.6282 0.7331 0.6867 -0.0542 0.0508  -0.0863 190 ASN B ND2 
2879 N N   . ILE B 157 ? 0.5148 0.6834 0.6784 -0.0432 -0.0153 -0.1153 191 ILE B N   
2880 C CA  . ILE B 157 ? 0.6146 0.7682 0.7761 -0.0516 -0.0362 -0.1142 191 ILE B CA  
2881 C C   . ILE B 157 ? 0.6720 0.7979 0.7865 -0.0450 -0.0398 -0.1119 191 ILE B C   
2882 O O   . ILE B 157 ? 0.6567 0.7865 0.7556 -0.0327 -0.0326 -0.1120 191 ILE B O   
2883 C CB  . ILE B 157 ? 0.5447 0.7192 0.7444 -0.0499 -0.0554 -0.1173 191 ILE B CB  
2884 C CG1 . ILE B 157 ? 0.6217 0.8026 0.8210 -0.0349 -0.0549 -0.1196 191 ILE B CG1 
2885 C CG2 . ILE B 157 ? 0.5999 0.8081 0.8532 -0.0558 -0.0531 -0.1218 191 ILE B CG2 
2886 C CD1 . ILE B 157 ? 0.6956 0.8827 0.9226 -0.0310 -0.0772 -0.1203 191 ILE B CD1 
2887 N N   . THR B 158 ? 0.6409 0.7418 0.7337 -0.0539 -0.0507 -0.1117 192 THR B N   
2888 C CA  . THR B 158 ? 0.5939 0.6712 0.6423 -0.0474 -0.0520 -0.1124 192 THR B CA  
2889 C C   . THR B 158 ? 0.6538 0.7281 0.6953 -0.0540 -0.0721 -0.1126 192 THR B C   
2890 O O   . THR B 158 ? 0.6330 0.7116 0.6969 -0.0654 -0.0892 -0.1122 192 THR B O   
2891 C CB  . THR B 158 ? 0.6549 0.6964 0.6711 -0.0501 -0.0461 -0.1142 192 THR B CB  
2892 O OG1 . THR B 158 ? 0.6276 0.6523 0.6442 -0.0678 -0.0618 -0.1174 192 THR B OG1 
2893 C CG2 . THR B 158 ? 0.5423 0.5808 0.5653 -0.0495 -0.0297 -0.1099 192 THR B CG2 
2894 N N   . VAL B 159 ? 0.5305 0.6003 0.5408 -0.0473 -0.0704 -0.1125 193 VAL B N   
2895 C CA  . VAL B 159 ? 0.6173 0.6825 0.6109 -0.0547 -0.0870 -0.1100 193 VAL B CA  
2896 C C   . VAL B 159 ? 0.6869 0.7306 0.6308 -0.0540 -0.0824 -0.1156 193 VAL B C   
2897 O O   . VAL B 159 ? 0.6992 0.7453 0.6260 -0.0413 -0.0645 -0.1195 193 VAL B O   
2898 C CB  . VAL B 159 ? 0.6263 0.7099 0.6293 -0.0514 -0.0881 -0.1038 193 VAL B CB  
2899 C CG1 . VAL B 159 ? 0.6551 0.7281 0.6394 -0.0624 -0.1081 -0.0969 193 VAL B CG1 
2900 C CG2 . VAL B 159 ? 0.5507 0.6533 0.6000 -0.0467 -0.0881 -0.1031 193 VAL B CG2 
2901 N N   . GLY B 160 ? 0.6839 0.7086 0.6050 -0.0662 -0.0991 -0.1173 194 GLY B N   
2902 C CA  . GLY B 160 ? 0.6481 0.6519 0.5165 -0.0664 -0.0954 -0.1251 194 GLY B CA  
2903 C C   . GLY B 160 ? 0.7484 0.7569 0.5918 -0.0757 -0.1065 -0.1181 194 GLY B C   
2904 O O   . GLY B 160 ? 0.8676 0.8768 0.7252 -0.0867 -0.1290 -0.1087 194 GLY B O   
2905 N N   . ILE B 161 ? 0.6460 0.6587 0.4526 -0.0710 -0.0906 -0.1219 195 ILE B N   
2906 C CA  . ILE B 161 ? 0.7312 0.7494 0.5073 -0.0828 -0.0954 -0.1132 195 ILE B CA  
2907 C C   . ILE B 161 ? 0.8462 0.8376 0.5664 -0.0920 -0.1036 -0.1215 195 ILE B C   
2908 O O   . ILE B 161 ? 0.9576 0.9385 0.6484 -0.0827 -0.0878 -0.1381 195 ILE B O   
2909 C CB  . ILE B 161 ? 0.7626 0.8106 0.5345 -0.0760 -0.0706 -0.1126 195 ILE B CB  
2910 C CG1 . ILE B 161 ? 0.5851 0.6562 0.4065 -0.0625 -0.0602 -0.1117 195 ILE B CG1 
2911 C CG2 . ILE B 161 ? 0.8329 0.8878 0.5850 -0.0940 -0.0768 -0.0974 195 ILE B CG2 
2912 C CD1 . ILE B 161 ? 0.6904 0.7970 0.5166 -0.0588 -0.0408 -0.1103 195 ILE B CD1 
2913 N N   . ASP B 162 ? 0.9217 0.8996 0.6248 -0.1089 -0.1296 -0.1108 196 ASP B N   
2914 C CA  . ASP B 162 ? 0.9323 0.8837 0.5762 -0.1202 -0.1414 -0.1183 196 ASP B CA  
2915 C C   . ASP B 162 ? 1.0207 0.9789 0.6087 -0.1217 -0.1186 -0.1223 196 ASP B C   
2916 O O   . ASP B 162 ? 0.9885 0.9715 0.5811 -0.1242 -0.1051 -0.1101 196 ASP B O   
2917 C CB  . ASP B 162 ? 0.9234 0.8616 0.5625 -0.1369 -0.1785 -0.1029 196 ASP B CB  
2918 C CG  . ASP B 162 ? 1.2281 1.1484 0.8795 -0.1422 -0.2037 -0.1122 196 ASP B CG  
2919 O OD1 . ASP B 162 ? 1.2469 1.1672 0.9301 -0.1340 -0.1930 -0.1250 196 ASP B OD1 
2920 O OD2 . ASP B 162 ? 1.3530 1.2592 0.9812 -0.1562 -0.2354 -0.1057 196 ASP B OD2 
2921 N N   . GLY B 163 ? 1.1223 1.0591 0.6574 -0.1215 -0.1134 -0.1410 197 GLY B N   
2922 C CA  . GLY B 163 ? 1.0374 0.9838 0.5159 -0.1225 -0.0893 -0.1486 197 GLY B CA  
2923 C C   . GLY B 163 ? 1.1439 1.1250 0.6435 -0.1020 -0.0523 -0.1588 197 GLY B C   
2924 O O   . GLY B 163 ? 1.2020 1.2113 0.6759 -0.1056 -0.0299 -0.1578 197 GLY B O   
2925 N N   . THR B 164 ? 1.0973 1.0795 0.6433 -0.0815 -0.0456 -0.1677 198 THR B N   
2926 C CA  . THR B 164 ? 0.9909 1.0062 0.5594 -0.0584 -0.0150 -0.1775 198 THR B CA  
2927 C C   . THR B 164 ? 0.9313 0.9199 0.5151 -0.0353 -0.0126 -0.1946 198 THR B C   
2928 O O   . THR B 164 ? 1.0124 0.9594 0.5923 -0.0416 -0.0329 -0.1977 198 THR B O   
2929 C CB  . THR B 164 ? 1.0097 1.0664 0.6306 -0.0604 -0.0104 -0.1585 198 THR B CB  
2930 O OG1 . THR B 164 ? 1.0967 1.1976 0.7274 -0.0445 0.0192  -0.1669 198 THR B OG1 
2931 C CG2 . THR B 164 ? 0.8913 0.9388 0.5657 -0.0522 -0.0234 -0.1527 198 THR B CG2 
2932 N N   . ASP B 165 ? 0.9997 1.0127 0.6017 -0.0094 0.0114  -0.2046 199 ASP B N   
2933 C CA  . ASP B 165 ? 0.9639 0.9482 0.5741 0.0164  0.0159  -0.2196 199 ASP B CA  
2934 C C   . ASP B 165 ? 0.9420 0.9290 0.6060 0.0217  0.0083  -0.2053 199 ASP B C   
2935 O O   . ASP B 165 ? 0.9215 0.8794 0.5910 0.0404  0.0099  -0.2128 199 ASP B O   
2936 C CB  . ASP B 165 ? 0.9603 0.9708 0.5614 0.0467  0.0441  -0.2383 199 ASP B CB  
2937 C CG  . ASP B 165 ? 1.2222 1.1805 0.7853 0.0682  0.0478  -0.2643 199 ASP B CG  
2938 O OD1 . ASP B 165 ? 1.3949 1.2994 0.9230 0.0522  0.0304  -0.2704 199 ASP B OD1 
2939 O OD2 . ASP B 165 ? 1.3625 1.3332 0.9310 0.1017  0.0667  -0.2795 199 ASP B OD2 
2940 N N   . ILE B 166 ? 0.8028 0.8195 0.5020 0.0057  0.0000  -0.1851 200 ILE B N   
2941 C CA  . ILE B 166 ? 0.7760 0.8100 0.5243 0.0135  -0.0003 -0.1737 200 ILE B CA  
2942 C C   . ILE B 166 ? 0.7864 0.7966 0.5564 -0.0037 -0.0211 -0.1624 200 ILE B C   
2943 O O   . ILE B 166 ? 0.8278 0.8313 0.5918 -0.0251 -0.0377 -0.1559 200 ILE B O   
2944 C CB  . ILE B 166 ? 0.7885 0.8778 0.5635 0.0106  0.0086  -0.1630 200 ILE B CB  
2945 C CG1 . ILE B 166 ? 0.7945 0.9172 0.5485 0.0203  0.0296  -0.1741 200 ILE B CG1 
2946 C CG2 . ILE B 166 ? 0.7338 0.8422 0.5512 0.0240  0.0111  -0.1566 200 ILE B CG2 
2947 C CD1 . ILE B 166 ? 0.7724 0.9316 0.5244 -0.0027 0.0328  -0.1629 200 ILE B CD1 
2948 N N   . ALA B 167 ? 0.6839 0.6838 0.4794 0.0061  -0.0203 -0.1598 201 ALA B N   
2949 C CA  . ALA B 167 ? 0.6808 0.6740 0.5083 -0.0082 -0.0337 -0.1489 201 ALA B CA  
2950 C C   . ALA B 167 ? 0.6916 0.7110 0.5533 0.0035  -0.0244 -0.1408 201 ALA B C   
2951 O O   . ALA B 167 ? 0.6502 0.6665 0.5061 0.0238  -0.0126 -0.1444 201 ALA B O   
2952 C CB  . ALA B 167 ? 0.6207 0.5670 0.4366 -0.0148 -0.0420 -0.1546 201 ALA B CB  
2953 N N   . PHE B 168 ? 0.6518 0.6952 0.5466 -0.0076 -0.0311 -0.1307 202 PHE B N   
2954 C CA  . PHE B 168 ? 0.6531 0.7230 0.5761 0.0014  -0.0233 -0.1249 202 PHE B CA  
2955 C C   . PHE B 168 ? 0.6089 0.6632 0.5492 -0.0011 -0.0236 -0.1212 202 PHE B C   
2956 O O   . PHE B 168 ? 0.7140 0.7669 0.6754 -0.0164 -0.0334 -0.1183 202 PHE B O   
2957 C CB  . PHE B 168 ? 0.5655 0.6653 0.5110 -0.0085 -0.0291 -0.1187 202 PHE B CB  
2958 C CG  . PHE B 168 ? 0.5228 0.6502 0.4905 0.0002  -0.0215 -0.1165 202 PHE B CG  
2959 C CD1 . PHE B 168 ? 0.5653 0.7137 0.5253 0.0149  -0.0104 -0.1196 202 PHE B CD1 
2960 C CD2 . PHE B 168 ? 0.4412 0.5763 0.4380 -0.0054 -0.0262 -0.1131 202 PHE B CD2 
2961 C CE1 . PHE B 168 ? 0.5888 0.7635 0.5668 0.0212  -0.0067 -0.1183 202 PHE B CE1 
2962 C CE2 . PHE B 168 ? 0.6650 0.8226 0.6760 0.0016  -0.0199 -0.1135 202 PHE B CE2 
2963 C CZ  . PHE B 168 ? 0.5548 0.7313 0.5548 0.0136  -0.0114 -0.1156 202 PHE B CZ  
2964 N N   . GLY B 169 ? 0.5604 0.6053 0.4921 0.0139  -0.0130 -0.1207 203 GLY B N   
2965 C CA  . GLY B 169 ? 0.6251 0.6549 0.5667 0.0095  -0.0098 -0.1147 203 GLY B CA  
2966 C C   . GLY B 169 ? 0.6619 0.7228 0.6285 0.0111  -0.0041 -0.1092 203 GLY B C   
2967 O O   . GLY B 169 ? 0.7296 0.7839 0.7047 0.0046  0.0011  -0.1041 203 GLY B O   
2968 N N   . GLY B 170 ? 0.6073 0.7014 0.5838 0.0175  -0.0042 -0.1109 204 GLY B N   
2969 C CA  . GLY B 170 ? 0.5877 0.7083 0.5835 0.0192  -0.0001 -0.1091 204 GLY B CA  
2970 C C   . GLY B 170 ? 0.6350 0.7504 0.6136 0.0330  0.0090  -0.1046 204 GLY B C   
2971 O O   . GLY B 170 ? 0.6787 0.7806 0.6336 0.0483  0.0104  -0.1035 204 GLY B O   
2972 N N   . CYS B 171 ? 0.5275 0.6533 0.5164 0.0291  0.0148  -0.1022 205 CYS B N   
2973 C CA  . CYS B 171 ? 0.6115 0.7293 0.5779 0.0392  0.0226  -0.0953 205 CYS B CA  
2974 C C   . CYS B 171 ? 0.5880 0.6657 0.5360 0.0325  0.0285  -0.0862 205 CYS B C   
2975 O O   . CYS B 171 ? 0.6138 0.6753 0.5359 0.0391  0.0344  -0.0767 205 CYS B O   
2976 C CB  . CYS B 171 ? 0.6204 0.7650 0.5978 0.0361  0.0284  -0.0978 205 CYS B CB  
2977 S SG  . CYS B 171 ? 0.6885 0.8720 0.6831 0.0405  0.0200  -0.1089 205 CYS B SG  
2978 N N   . LEU B 172 ? 0.6593 0.7185 0.6174 0.0178  0.0253  -0.0879 206 LEU B N   
2979 C CA  . LEU B 172 ? 0.6832 0.7019 0.6252 0.0059  0.0299  -0.0798 206 LEU B CA  
2980 C C   . LEU B 172 ? 0.6971 0.6703 0.5995 0.0219  0.0264  -0.0760 206 LEU B C   
2981 O O   . LEU B 172 ? 0.7477 0.6816 0.6227 0.0207  0.0312  -0.0647 206 LEU B O   
2982 C CB  . LEU B 172 ? 0.5947 0.6114 0.5625 -0.0165 0.0242  -0.0848 206 LEU B CB  
2983 C CG  . LEU B 172 ? 0.6753 0.6459 0.6272 -0.0334 0.0242  -0.0797 206 LEU B CG  
2984 C CD1 . LEU B 172 ? 0.7027 0.6797 0.6679 -0.0543 0.0377  -0.0707 206 LEU B CD1 
2985 C CD2 . LEU B 172 ? 0.6917 0.6557 0.6569 -0.0468 0.0099  -0.0890 206 LEU B CD2 
2986 N N   . ILE B 173 ? 0.7375 0.7140 0.6352 0.0375  0.0187  -0.0851 207 ILE B N   
2987 C CA  . ILE B 173 ? 0.7198 0.6556 0.5844 0.0569  0.0156  -0.0864 207 ILE B CA  
2988 C C   . ILE B 173 ? 0.7320 0.6899 0.5879 0.0865  0.0155  -0.0852 207 ILE B C   
2989 O O   . ILE B 173 ? 0.8218 0.8311 0.6996 0.0908  0.0147  -0.0905 207 ILE B O   
2990 C CB  . ILE B 173 ? 0.7239 0.6511 0.5871 0.0549  0.0092  -0.1001 207 ILE B CB  
2991 C CG1 . ILE B 173 ? 0.7324 0.6454 0.6082 0.0243  0.0047  -0.1016 207 ILE B CG1 
2992 C CG2 . ILE B 173 ? 0.6523 0.5334 0.4799 0.0774  0.0078  -0.1054 207 ILE B CG2 
2993 C CD1 . ILE B 173 ? 0.7513 0.6131 0.6104 0.0095  0.0066  -0.0933 207 ILE B CD1 
2994 N N   . LYS B 174 ? 0.8327 0.7505 0.6571 0.1063  0.0143  -0.0777 208 LYS B N   
2995 C CA  . LYS B 174 ? 0.7635 0.6995 0.5799 0.1395  0.0102  -0.0773 208 LYS B CA  
2996 C C   . LYS B 174 ? 0.8622 0.7658 0.6604 0.1651  0.0067  -0.0869 208 LYS B C   
2997 O O   . LYS B 174 ? 0.9002 0.7482 0.6784 0.1575  0.0066  -0.0900 208 LYS B O   
2998 C CB  . LYS B 174 ? 0.7845 0.7017 0.5767 0.1475  0.0089  -0.0594 208 LYS B CB  
2999 C CG  . LYS B 174 ? 0.8930 0.8213 0.6914 0.1183  0.0169  -0.0501 208 LYS B CG  
3000 C CD  . LYS B 174 ? 0.9755 0.9713 0.8019 0.1165  0.0172  -0.0568 208 LYS B CD  
3001 C CE  . LYS B 174 ? 0.7894 0.8004 0.6313 0.0875  0.0273  -0.0555 208 LYS B CE  
3002 N NZ  . LYS B 174 ? 0.7840 0.8494 0.6454 0.0875  0.0270  -0.0628 208 LYS B NZ  
3003 N N   . ASP B 175 ? 0.8800 0.8212 0.6866 0.1956  0.0038  -0.0936 209 ASP B N   
3004 C CA  . ASP B 175 ? 0.9141 0.8368 0.7095 0.2244  0.0031  -0.1071 209 ASP B CA  
3005 C C   . ASP B 175 ? 1.0014 0.8482 0.7582 0.2474  -0.0035 -0.0981 209 ASP B C   
3006 O O   . ASP B 175 ? 0.9969 0.8144 0.7353 0.2435  -0.0081 -0.0787 209 ASP B O   
3007 C CB  . ASP B 175 ? 0.9688 0.9639 0.7917 0.2501  0.0034  -0.1173 209 ASP B CB  
3008 C CG  . ASP B 175 ? 0.9688 0.9749 0.7892 0.2822  -0.0067 -0.1071 209 ASP B CG  
3009 O OD1 . ASP B 175 ? 0.9840 0.9783 0.7933 0.2720  -0.0123 -0.0898 209 ASP B OD1 
3010 O OD2 . ASP B 175 ? 1.0064 1.0356 0.8356 0.3185  -0.0092 -0.1170 209 ASP B OD2 
3011 N N   . SER B 176 ? 0.8591 0.7601 1.0614 0.0565  -0.1327 0.1421  210 SER B N   
3012 C CA  . SER B 176 ? 0.9088 0.7522 0.9992 0.0785  -0.1342 0.1686  210 SER B CA  
3013 C C   . SER B 176 ? 0.8546 0.7439 0.9269 0.1168  -0.1564 0.1575  210 SER B C   
3014 O O   . SER B 176 ? 0.9893 0.8400 0.9663 0.1327  -0.1620 0.1748  210 SER B O   
3015 C CB  . SER B 176 ? 0.8126 0.6052 0.8496 0.0851  -0.1010 0.1784  210 SER B CB  
3016 O OG  . SER B 176 ? 0.8558 0.6854 0.9712 0.0952  -0.0984 0.1739  210 SER B OG  
3017 N N   . LYS B 177 ? 0.8847 0.8566 1.0463 0.1313  -0.1698 0.1303  211 LYS B N   
3018 C CA  . LYS B 177 ? 0.9061 0.9381 1.0602 0.1700  -0.1968 0.1167  211 LYS B CA  
3019 C C   . LYS B 177 ? 0.9226 1.0223 1.1002 0.1570  -0.2191 0.0775  211 LYS B C   
3020 O O   . LYS B 177 ? 1.0308 1.2187 1.2879 0.1625  -0.2401 0.0404  211 LYS B O   
3021 C CB  . LYS B 177 ? 0.8965 0.9904 1.1369 0.1938  -0.2006 0.1073  211 LYS B CB  
3022 C CG  . LYS B 177 ? 0.9383 0.9745 1.1762 0.1993  -0.1714 0.1381  211 LYS B CG  
3023 C CD  . LYS B 177 ? 0.8348 0.9485 1.1859 0.2089  -0.1674 0.1237  211 LYS B CD  
3024 C CE  . LYS B 177 ? 0.8328 0.9961 1.2952 0.1631  -0.1629 0.0942  211 LYS B CE  
3025 N NZ  . LYS B 177 ? 0.8031 0.8990 1.2683 0.1319  -0.1303 0.1161  211 LYS B NZ  
3026 N N   . ALA B 178 ? 0.9272 0.9862 1.0342 0.1380  -0.2131 0.0840  212 ALA B N   
3027 C CA  . ALA B 178 ? 0.8927 1.0074 1.0048 0.1273  -0.2289 0.0476  212 ALA B CA  
3028 C C   . ALA B 178 ? 1.0052 1.0680 0.9994 0.1252  -0.2211 0.0720  212 ALA B C   
3029 O O   . ALA B 178 ? 1.0253 1.0124 0.9738 0.1046  -0.1970 0.1042  212 ALA B O   
3030 C CB  . ALA B 178 ? 0.7954 0.9365 1.0033 0.0880  -0.2193 0.0138  212 ALA B CB  
3031 N N   . LYS B 179 ? 1.1065 1.2131 1.0513 0.1446  -0.2416 0.0564  213 LYS B N   
3032 C CA  . LYS B 179 ? 1.2129 1.2760 1.0426 0.1424  -0.2314 0.0813  213 LYS B CA  
3033 C C   . LYS B 179 ? 1.1738 1.2937 1.0153 0.1219  -0.2323 0.0411  213 LYS B C   
3034 O O   . LYS B 179 ? 1.2177 1.3693 0.9901 0.1406  -0.2457 0.0332  213 LYS B O   
3035 C CB  . LYS B 179 ? 1.2940 1.3439 1.0262 0.1896  -0.2498 0.1092  213 LYS B CB  
3036 C CG  . LYS B 179 ? 1.4271 1.4075 1.0274 0.1876  -0.2331 0.1497  213 LYS B CG  
3037 C CD  . LYS B 179 ? 1.4337 1.3235 1.0144 0.1473  -0.1974 0.1815  213 LYS B CD  
3038 C CE  . LYS B 179 ? 1.3684 1.2243 0.8576 0.1232  -0.1759 0.2023  213 LYS B CE  
3039 N NZ  . LYS B 179 ? 1.3907 1.3282 0.9237 0.1005  -0.1738 0.1592  213 LYS B NZ  
3040 N N   . SER B 180 ? 1.0260 1.1580 0.9515 0.0869  -0.2173 0.0157  214 SER B N   
3041 C CA  . SER B 180 ? 0.8484 1.0279 0.7949 0.0681  -0.2128 -0.0251 214 SER B CA  
3042 C C   . SER B 180 ? 0.7557 0.9249 0.7961 0.0345  -0.1929 -0.0377 214 SER B C   
3043 O O   . SER B 180 ? 0.7383 0.8990 0.8571 0.0302  -0.1949 -0.0377 214 SER B O   
3044 C CB  . SER B 180 ? 0.8155 1.0811 0.7979 0.0870  -0.2444 -0.0810 214 SER B CB  
3045 O OG  . SER B 180 ? 0.8058 1.1109 0.8069 0.0705  -0.2375 -0.1256 214 SER B OG  
3046 N N   . LEU B 181 ? 0.6863 0.8593 0.7180 0.0133  -0.1726 -0.0462 215 LEU B N   
3047 C CA  . LEU B 181 ? 0.7763 0.9475 0.8965 -0.0124 -0.1560 -0.0602 215 LEU B CA  
3048 C C   . LEU B 181 ? 0.6153 0.8446 0.8213 -0.0114 -0.1663 -0.1226 215 LEU B C   
3049 O O   . LEU B 181 ? 0.6383 0.8689 0.9111 -0.0275 -0.1515 -0.1392 215 LEU B O   
3050 C CB  . LEU B 181 ? 0.7773 0.9297 0.8566 -0.0344 -0.1282 -0.0380 215 LEU B CB  
3051 C CG  . LEU B 181 ? 0.7462 0.8301 0.7550 -0.0469 -0.1149 0.0210  215 LEU B CG  
3052 C CD1 . LEU B 181 ? 0.8445 0.9273 0.7895 -0.0669 -0.0908 0.0381  215 LEU B CD1 
3053 C CD2 . LEU B 181 ? 0.6563 0.7013 0.7276 -0.0630 -0.1098 0.0405  215 LEU B CD2 
3054 N N   . GLY B 182 ? 0.6001 0.8761 0.8054 0.0078  -0.1927 -0.1586 216 GLY B N   
3055 C CA  . GLY B 182 ? 0.6320 0.9573 0.9201 0.0056  -0.2059 -0.2232 216 GLY B CA  
3056 C C   . GLY B 182 ? 0.5947 0.9509 0.8658 0.0031  -0.1944 -0.2640 216 GLY B C   
3057 O O   . GLY B 182 ? 0.6149 0.9959 0.7929 0.0160  -0.1956 -0.2665 216 GLY B O   
3058 N N   . ASN B 183 ? 0.6015 0.9547 0.9599 -0.0109 -0.1811 -0.2950 217 ASN B N   
3059 C CA  . ASN B 183 ? 0.5398 0.9240 0.8976 -0.0094 -0.1681 -0.3422 217 ASN B CA  
3060 C C   . ASN B 183 ? 0.6635 1.0329 0.9728 -0.0160 -0.1351 -0.3030 217 ASN B C   
3061 O O   . ASN B 183 ? 0.5923 0.9303 0.9553 -0.0291 -0.1170 -0.2768 217 ASN B O   
3062 C CB  . ASN B 183 ? 0.5794 0.9584 1.0537 -0.0178 -0.1670 -0.3909 217 ASN B CB  
3063 C CG  . ASN B 183 ? 0.7498 1.1649 1.2249 -0.0096 -0.1606 -0.4573 217 ASN B CG  
3064 O OD1 . ASN B 183 ? 0.7166 1.1715 1.1032 0.0031  -0.1611 -0.4728 217 ASN B OD1 
3065 N ND2 . ASN B 183 ? 0.7551 1.1523 1.3260 -0.0147 -0.1528 -0.4963 217 ASN B ND2 
3066 N N   . LEU B 184 ? 0.6790 1.0750 0.8872 -0.0078 -0.1273 -0.2980 218 LEU B N   
3067 C CA  . LEU B 184 ? 0.6573 1.0498 0.8173 -0.0184 -0.0937 -0.2625 218 LEU B CA  
3068 C C   . LEU B 184 ? 0.7555 1.1973 0.9240 -0.0131 -0.0711 -0.3101 218 LEU B C   
3069 O O   . LEU B 184 ? 0.7230 1.1826 0.8376 -0.0195 -0.0419 -0.2884 218 LEU B O   
3070 C CB  . LEU B 184 ? 0.7562 1.1358 0.7930 -0.0163 -0.0922 -0.2143 218 LEU B CB  
3071 C CG  . LEU B 184 ? 0.6689 0.9900 0.6846 -0.0198 -0.1059 -0.1587 218 LEU B CG  
3072 C CD1 . LEU B 184 ? 0.6919 0.9893 0.5809 -0.0167 -0.0988 -0.1106 218 LEU B CD1 
3073 C CD2 . LEU B 184 ? 0.6363 0.9152 0.7202 -0.0426 -0.0918 -0.1268 218 LEU B CD2 
3074 N N   . GLY B 185 ? 0.8337 1.2971 1.0700 -0.0023 -0.0819 -0.3757 219 GLY B N   
3075 C CA  . GLY B 185 ? 0.7073 1.2136 0.9536 0.0082  -0.0601 -0.4288 219 GLY B CA  
3076 C C   . GLY B 185 ? 0.7862 1.2930 1.0863 0.0005  -0.0250 -0.4089 219 GLY B C   
3077 O O   . GLY B 185 ? 0.8778 1.4187 1.1258 -0.0018 0.0050  -0.3925 219 GLY B O   
3078 N N   . ASP B 186 ? 0.7168 1.1898 1.1229 -0.0033 -0.0281 -0.4081 220 ASP B N   
3079 C CA  . ASP B 186 ? 0.5851 1.0608 1.0527 -0.0067 -0.0015 -0.3860 220 ASP B CA  
3080 C C   . ASP B 186 ? 0.5047 0.9521 0.9587 -0.0294 0.0005  -0.3100 220 ASP B C   
3081 O O   . ASP B 186 ? 0.4954 0.9290 1.0203 -0.0339 0.0072  -0.2867 220 ASP B O   
3082 C CB  . ASP B 186 ? 0.5786 1.0273 1.1613 0.0049  -0.0061 -0.4209 220 ASP B CB  
3083 C CG  . ASP B 186 ? 0.7367 1.2033 1.3366 0.0251  -0.0078 -0.5027 220 ASP B CG  
3084 O OD1 . ASP B 186 ? 0.8325 1.3469 1.3572 0.0339  0.0014  -0.5338 220 ASP B OD1 
3085 O OD2 . ASP B 186 ? 0.8526 1.2815 1.5373 0.0312  -0.0174 -0.5364 220 ASP B OD2 
3086 N N   . ALA B 187 ? 0.5967 1.0324 0.9584 -0.0419 -0.0062 -0.2718 221 ALA B N   
3087 C CA  . ALA B 187 ? 0.5604 0.9569 0.9009 -0.0644 -0.0069 -0.2050 221 ALA B CA  
3088 C C   . ALA B 187 ? 0.6320 1.0587 0.9289 -0.0829 0.0230  -0.1724 221 ALA B C   
3089 O O   . ALA B 187 ? 0.5975 1.0721 0.8459 -0.0786 0.0442  -0.1914 221 ALA B O   
3090 C CB  . ALA B 187 ? 0.5596 0.9156 0.8273 -0.0661 -0.0302 -0.1796 221 ALA B CB  
3091 N N   . ASP B 188 ? 0.7024 1.1030 1.0169 -0.1056 0.0254  -0.1237 222 ASP B N   
3092 C CA  . ASP B 188 ? 0.6142 1.0386 0.8941 -0.1328 0.0507  -0.0874 222 ASP B CA  
3093 C C   . ASP B 188 ? 0.6445 1.0129 0.8218 -0.1531 0.0452  -0.0407 222 ASP B C   
3094 O O   . ASP B 188 ? 0.7529 1.0616 0.9291 -0.1633 0.0270  -0.0087 222 ASP B O   
3095 C CB  . ASP B 188 ? 0.6024 1.0368 0.9664 -0.1464 0.0531  -0.0669 222 ASP B CB  
3096 C CG  . ASP B 188 ? 0.6501 1.1406 1.0092 -0.1730 0.0825  -0.0464 222 ASP B CG  
3097 O OD1 . ASP B 188 ? 0.7208 1.1994 0.9936 -0.1990 0.0958  -0.0173 222 ASP B OD1 
3098 O OD2 . ASP B 188 ? 0.5892 1.1364 1.0340 -0.1678 0.0929  -0.0581 222 ASP B OD2 
3099 N N   . THR B 189 ? 0.7567 1.1404 0.8434 -0.1564 0.0626  -0.0362 223 THR B N   
3100 C CA  . THR B 189 ? 0.8605 1.1819 0.8417 -0.1691 0.0580  0.0082  223 THR B CA  
3101 C C   . THR B 189 ? 0.9201 1.2024 0.8906 -0.2095 0.0682  0.0592  223 THR B C   
3102 O O   . THR B 189 ? 0.9868 1.1930 0.8957 -0.2183 0.0561  0.0956  223 THR B O   
3103 C CB  . THR B 189 ? 0.9621 1.3085 0.8442 -0.1630 0.0775  0.0060  223 THR B CB  
3104 O OG1 . THR B 189 ? 0.9771 1.3882 0.8725 -0.1828 0.1161  0.0033  223 THR B OG1 
3105 C CG2 . THR B 189 ? 0.8832 1.2607 0.7608 -0.1230 0.0592  -0.0464 223 THR B CG2 
3106 N N   . GLU B 190 ? 0.9110 1.2456 0.9423 -0.2334 0.0892  0.0602  224 GLU B N   
3107 C CA  . GLU B 190 ? 0.9244 1.2321 0.9485 -0.2776 0.0974  0.1036  224 GLU B CA  
3108 C C   . GLU B 190 ? 0.9238 1.1951 1.0118 -0.2801 0.0696  0.1120  224 GLU B C   
3109 O O   . GLU B 190 ? 0.9756 1.1708 1.0170 -0.2983 0.0571  0.1450  224 GLU B O   
3110 C CB  . GLU B 190 ? 0.8842 1.2777 0.9491 -0.3046 0.1315  0.1017  224 GLU B CB  
3111 N N   . ARG B 191 ? 0.8150 1.1197 1.1017 -0.2976 0.1284  -0.0193 225 ARG B N   
3112 C CA  . ARG B 191 ? 0.7287 1.0209 1.0396 -0.2583 0.1034  -0.0335 225 ARG B CA  
3113 C C   . ARG B 191 ? 0.6870 0.9265 0.9499 -0.2345 0.0848  -0.0284 225 ARG B C   
3114 O O   . ARG B 191 ? 0.7236 0.9492 0.9954 -0.2034 0.0656  -0.0383 225 ARG B O   
3115 C CB  . ARG B 191 ? 0.7047 1.0383 1.0552 -0.2335 0.1211  -0.0597 225 ARG B CB  
3116 C CG  . ARG B 191 ? 0.6554 1.0509 1.0689 -0.2519 0.1402  -0.0700 225 ARG B CG  
3117 C CD  . ARG B 191 ? 0.7022 1.1252 1.1775 -0.2197 0.1285  -0.0933 225 ARG B CD  
3118 N NE  . ARG B 191 ? 0.8209 1.2972 1.3352 -0.2135 0.1612  -0.1165 225 ARG B NE  
3119 C CZ  . ARG B 191 ? 0.8985 1.4031 1.4713 -0.1844 0.1543  -0.1395 225 ARG B CZ  
3120 N NH1 . ARG B 191 ? 0.8510 1.3351 1.4443 -0.1605 0.1153  -0.1407 225 ARG B NH1 
3121 N NH2 . ARG B 191 ? 0.8061 1.3596 1.4167 -0.1785 0.1857  -0.1631 225 ARG B NH2 
3122 N N   . TYR B 192 ? 0.7732 0.9844 0.9860 -0.2492 0.0896  -0.0132 226 TYR B N   
3123 C CA  . TYR B 192 ? 0.7319 0.8993 0.9081 -0.2277 0.0734  -0.0090 226 TYR B CA  
3124 C C   . TYR B 192 ? 0.7327 0.8701 0.9169 -0.2179 0.0395  -0.0040 226 TYR B C   
3125 O O   . TYR B 192 ? 0.6588 0.7788 0.8382 -0.1877 0.0269  -0.0127 226 TYR B O   
3126 C CB  . TYR B 192 ? 0.6947 0.8394 0.8225 -0.2483 0.0810  0.0069  226 TYR B CB  
3127 C CG  . TYR B 192 ? 0.7312 0.8470 0.8281 -0.2256 0.0769  0.0055  226 TYR B CG  
3128 C CD1 . TYR B 192 ? 0.6828 0.7779 0.7857 -0.1970 0.0574  0.0013  226 TYR B CD1 
3129 C CD2 . TYR B 192 ? 0.6148 0.7250 0.6758 -0.2346 0.0930  0.0081  226 TYR B CD2 
3130 C CE1 . TYR B 192 ? 0.6413 0.7151 0.7209 -0.1794 0.0564  0.0014  226 TYR B CE1 
3131 C CE2 . TYR B 192 ? 0.6917 0.7773 0.7309 -0.2164 0.0878  0.0078  226 TYR B CE2 
3132 C CZ  . TYR B 192 ? 0.6993 0.7689 0.7507 -0.1896 0.0707  0.0053  226 TYR B CZ  
3133 O OH  . TYR B 192 ? 0.6347 0.6847 0.6691 -0.1744 0.0683  0.0062  226 TYR B OH  
3134 N N   . ALA B 193 ? 0.8160 0.9457 1.0106 -0.2442 0.0246  0.0096  227 ALA B N   
3135 C CA  . ALA B 193 ? 0.6879 0.7850 0.8905 -0.2349 -0.0099 0.0114  227 ALA B CA  
3136 C C   . ALA B 193 ? 0.6733 0.7825 0.9070 -0.2078 -0.0221 -0.0081 227 ALA B C   
3137 O O   . ALA B 193 ? 0.7236 0.8061 0.9470 -0.1820 -0.0421 -0.0162 227 ALA B O   
3138 C CB  . ALA B 193 ? 0.7596 0.8455 0.9726 -0.2709 -0.0257 0.0300  227 ALA B CB  
3139 N N   . ALA B 194 ? 0.6962 0.8466 0.9680 -0.2131 -0.0106 -0.0170 228 ALA B N   
3140 C CA  . ALA B 194 ? 0.6433 0.8041 0.9462 -0.1886 -0.0272 -0.0347 228 ALA B CA  
3141 C C   . ALA B 194 ? 0.6991 0.8559 0.9814 -0.1530 -0.0209 -0.0475 228 ALA B C   
3142 O O   . ALA B 194 ? 0.6752 0.8135 0.9513 -0.1276 -0.0424 -0.0571 228 ALA B O   
3143 C CB  . ALA B 194 ? 0.6261 0.8360 0.9853 -0.2048 -0.0184 -0.0406 228 ALA B CB  
3144 N N   . SER B 195 ? 0.7022 0.8732 0.9701 -0.1519 0.0073  -0.0475 229 SER B N   
3145 C CA  . SER B 195 ? 0.5742 0.7388 0.8245 -0.1212 0.0122  -0.0572 229 SER B CA  
3146 C C   . SER B 195 ? 0.6173 0.7407 0.8238 -0.1048 0.0005  -0.0519 229 SER B C   
3147 O O   . SER B 195 ? 0.5403 0.6512 0.7336 -0.0788 -0.0086 -0.0590 229 SER B O   
3148 C CB  . SER B 195 ? 0.5753 0.7595 0.8203 -0.1254 0.0429  -0.0594 229 SER B CB  
3149 O OG  . SER B 195 ? 0.6576 0.8864 0.9472 -0.1380 0.0579  -0.0687 229 SER B OG  
3150 N N   . ALA B 196 ? 0.6158 0.7186 0.7999 -0.1204 0.0004  -0.0392 230 ALA B N   
3151 C CA  . ALA B 196 ? 0.5327 0.6026 0.6855 -0.1047 -0.0099 -0.0367 230 ALA B CA  
3152 C C   . ALA B 196 ? 0.6415 0.6959 0.7981 -0.0882 -0.0359 -0.0465 230 ALA B C   
3153 O O   . ALA B 196 ? 0.6401 0.6787 0.7728 -0.0648 -0.0400 -0.0528 230 ALA B O   
3154 C CB  . ALA B 196 ? 0.5858 0.6375 0.7238 -0.1247 -0.0104 -0.0222 230 ALA B CB  
3155 N N   . ARG B 197 ? 0.6043 0.6629 0.7893 -0.1016 -0.0535 -0.0484 231 ARG B N   
3156 C CA  . ARG B 197 ? 0.5784 0.6195 0.7662 -0.0866 -0.0818 -0.0605 231 ARG B CA  
3157 C C   . ARG B 197 ? 0.5855 0.6382 0.7762 -0.0647 -0.0874 -0.0737 231 ARG B C   
3158 O O   . ARG B 197 ? 0.6250 0.6575 0.7937 -0.0434 -0.1048 -0.0847 231 ARG B O   
3159 C CB  . ARG B 197 ? 0.6771 0.7161 0.8975 -0.1100 -0.1026 -0.0575 231 ARG B CB  
3160 C CG  . ARG B 197 ? 0.5867 0.6052 0.8015 -0.1322 -0.1051 -0.0421 231 ARG B CG  
3161 C CD  . ARG B 197 ? 0.6855 0.6959 0.9317 -0.1569 -0.1296 -0.0369 231 ARG B CD  
3162 N NE  . ARG B 197 ? 0.8067 0.8060 1.0504 -0.1882 -0.1271 -0.0150 231 ARG B NE  
3163 C CZ  . ARG B 197 ? 0.8923 0.8521 1.1234 -0.1901 -0.1471 -0.0086 231 ARG B CZ  
3164 N NH1 . ARG B 197 ? 0.8654 0.7969 1.0879 -0.1616 -0.1675 -0.0254 231 ARG B NH1 
3165 N NH2 . ARG B 197 ? 0.9163 0.8644 1.1424 -0.2211 -0.1473 0.0145  231 ARG B NH2 
3166 N N   . ALA B 198 ? 0.5151 0.5994 0.7318 -0.0692 -0.0741 -0.0737 232 ALA B N   
3167 C CA  . ALA B 198 ? 0.4958 0.5883 0.7179 -0.0472 -0.0832 -0.0847 232 ALA B CA  
3168 C C   . ALA B 198 ? 0.6730 0.7447 0.8473 -0.0235 -0.0758 -0.0841 232 ALA B C   
3169 O O   . ALA B 198 ? 0.6629 0.7237 0.8211 -0.0030 -0.0921 -0.0912 232 ALA B O   
3170 C CB  . ALA B 198 ? 0.4806 0.6135 0.7482 -0.0554 -0.0692 -0.0870 232 ALA B CB  
3171 N N   . PHE B 199 ? 0.6144 0.6793 0.7645 -0.0279 -0.0529 -0.0742 233 PHE B N   
3172 C CA  . PHE B 199 ? 0.5925 0.6389 0.7002 -0.0096 -0.0444 -0.0712 233 PHE B CA  
3173 C C   . PHE B 199 ? 0.6524 0.6734 0.7265 0.0043  -0.0589 -0.0769 233 PHE B C   
3174 O O   . PHE B 199 ? 0.6267 0.6347 0.6672 0.0227  -0.0626 -0.0793 233 PHE B O   
3175 C CB  . PHE B 199 ? 0.5603 0.6070 0.6570 -0.0201 -0.0191 -0.0599 233 PHE B CB  
3176 C CG  . PHE B 199 ? 0.6072 0.6350 0.6649 -0.0068 -0.0104 -0.0548 233 PHE B CG  
3177 C CD1 . PHE B 199 ? 0.5956 0.6171 0.6328 0.0088  -0.0081 -0.0533 233 PHE B CD1 
3178 C CD2 . PHE B 199 ? 0.5998 0.6168 0.6446 -0.0108 -0.0054 -0.0508 233 PHE B CD2 
3179 C CE1 . PHE B 199 ? 0.5696 0.5763 0.5716 0.0170  0.0024  -0.0461 233 PHE B CE1 
3180 C CE2 . PHE B 199 ? 0.6522 0.6590 0.6687 0.0000  0.0057  -0.0468 233 PHE B CE2 
3181 C CZ  . PHE B 199 ? 0.5431 0.5458 0.5368 0.0123  0.0112  -0.0436 233 PHE B CZ  
3182 N N   . GLY B 200 ? 0.6229 0.6352 0.7037 -0.0044 -0.0677 -0.0797 234 GLY B N   
3183 C CA  . GLY B 200 ? 0.5879 0.5773 0.6405 0.0107  -0.0812 -0.0907 234 GLY B CA  
3184 C C   . GLY B 200 ? 0.6598 0.6408 0.7065 0.0231  -0.1084 -0.1050 234 GLY B C   
3185 O O   . GLY B 200 ? 0.7245 0.6876 0.7310 0.0416  -0.1152 -0.1153 234 GLY B O   
3186 N N   . ALA B 201 ? 0.6420 0.6372 0.7283 0.0123  -0.1240 -0.1066 235 ALA B N   
3187 C CA  . ALA B 201 ? 0.6490 0.6365 0.7358 0.0228  -0.1551 -0.1203 235 ALA B CA  
3188 C C   . ALA B 201 ? 0.6200 0.6072 0.6812 0.0407  -0.1574 -0.1199 235 ALA B C   
3189 O O   . ALA B 201 ? 0.6704 0.6396 0.7038 0.0556  -0.1823 -0.1309 235 ALA B O   
3190 C CB  . ALA B 201 ? 0.5944 0.6016 0.7410 0.0035  -0.1716 -0.1213 235 ALA B CB  
3191 N N   . ALA B 202 ? 0.6481 0.6510 0.7155 0.0391  -0.1348 -0.1075 236 ALA B N   
3192 C CA  . ALA B 202 ? 0.7555 0.7528 0.8007 0.0554  -0.1404 -0.1047 236 ALA B CA  
3193 C C   . ALA B 202 ? 0.7145 0.6844 0.6901 0.0699  -0.1333 -0.1011 236 ALA B C   
3194 O O   . ALA B 202 ? 0.6868 0.6396 0.6265 0.0841  -0.1495 -0.1009 236 ALA B O   
3195 C CB  . ALA B 202 ? 0.6132 0.6325 0.6899 0.0499  -0.1203 -0.0949 236 ALA B CB  
3196 N N   . PHE B 203 ? 0.7178 0.6840 0.6741 0.0655  -0.1095 -0.0978 237 PHE B N   
3197 C CA  . PHE B 203 ? 0.7164 0.6645 0.6130 0.0767  -0.0965 -0.0957 237 PHE B CA  
3198 C C   . PHE B 203 ? 0.7853 0.7248 0.6699 0.0798  -0.0998 -0.1115 237 PHE B C   
3199 O O   . PHE B 203 ? 0.7087 0.6534 0.5997 0.0749  -0.0793 -0.1100 237 PHE B O   
3200 C CB  . PHE B 203 ? 0.6425 0.5978 0.5350 0.0705  -0.0644 -0.0789 237 PHE B CB  
3201 C CG  . PHE B 203 ? 0.7196 0.6831 0.6354 0.0665  -0.0614 -0.0667 237 PHE B CG  
3202 C CD1 . PHE B 203 ? 0.6741 0.6226 0.5611 0.0770  -0.0709 -0.0589 237 PHE B CD1 
3203 C CD2 . PHE B 203 ? 0.5803 0.5641 0.5445 0.0523  -0.0503 -0.0640 237 PHE B CD2 
3204 C CE1 . PHE B 203 ? 0.6428 0.5961 0.5564 0.0761  -0.0710 -0.0507 237 PHE B CE1 
3205 C CE2 . PHE B 203 ? 0.5905 0.5826 0.5773 0.0510  -0.0464 -0.0579 237 PHE B CE2 
3206 C CZ  . PHE B 203 ? 0.6735 0.6502 0.6386 0.0642  -0.0575 -0.0523 237 PHE B CZ  
3207 N N   . PRO B 204 ? 0.7999 0.7243 0.6692 0.0889  -0.1282 -0.1286 238 PRO B N   
3208 C CA  . PRO B 204 ? 0.7603 0.6730 0.6226 0.0936  -0.1349 -0.1481 238 PRO B CA  
3209 C C   . PRO B 204 ? 0.8601 0.7640 0.6668 0.1076  -0.1144 -0.1555 238 PRO B C   
3210 O O   . PRO B 204 ? 0.9131 0.8132 0.7240 0.1122  -0.1109 -0.1713 238 PRO B O   
3211 C CB  . PRO B 204 ? 0.7893 0.6866 0.6502 0.0991  -0.1746 -0.1648 238 PRO B CB  
3212 C CG  . PRO B 204 ? 0.7992 0.6930 0.6316 0.1061  -0.1842 -0.1558 238 PRO B CG  
3213 C CD  . PRO B 204 ? 0.7526 0.6674 0.6115 0.0964  -0.1590 -0.1326 238 PRO B CD  
3214 N N   . LYS B 205 ? 0.8556 0.7565 0.6127 0.1139  -0.1008 -0.1446 239 LYS B N   
3215 C CA  . LYS B 205 ? 0.9239 0.8207 0.6240 0.1248  -0.0780 -0.1509 239 LYS B CA  
3216 C C   . LYS B 205 ? 0.9963 0.9133 0.7099 0.1175  -0.0395 -0.1357 239 LYS B C   
3217 O O   . LYS B 205 ? 1.0511 0.9732 0.7302 0.1246  -0.0154 -0.1418 239 LYS B O   
3218 C CB  . LYS B 205 ? 0.9787 0.8577 0.6085 0.1324  -0.0853 -0.1449 239 LYS B CB  
3219 C CG  . LYS B 205 ? 1.1043 0.9597 0.6876 0.1461  -0.1141 -0.1699 239 LYS B CG  
3220 C CD  . LYS B 205 ? 1.1728 1.0293 0.7392 0.1569  -0.0993 -0.1974 239 LYS B CD  
3221 C CE  . LYS B 205 ? 1.2524 1.1214 0.7711 0.1596  -0.0568 -0.1919 239 LYS B CE  
3222 N NZ  . LYS B 205 ? 1.2163 1.0662 0.6434 0.1714  -0.0583 -0.2056 239 LYS B NZ  
3223 N N   . ALA B 206 ? 0.8804 0.8109 0.6435 0.1032  -0.0329 -0.1175 240 ALA B N   
3224 C CA  . ALA B 206 ? 0.8463 0.7938 0.6245 0.0950  -0.0011 -0.1029 240 ALA B CA  
3225 C C   . ALA B 206 ? 0.9053 0.8629 0.7120 0.0974  0.0081  -0.1179 240 ALA B C   
3226 O O   . ALA B 206 ? 0.8560 0.8085 0.6969 0.0964  -0.0118 -0.1302 240 ALA B O   
3227 C CB  . ALA B 206 ? 0.7347 0.6903 0.5545 0.0796  0.0001  -0.0832 240 ALA B CB  
3228 N N   . ASN B 207 ? 0.8735 0.8452 0.6695 0.1001  0.0372  -0.1164 241 ASN B N   
3229 C CA  . ASN B 207 ? 0.8842 0.8689 0.7144 0.1046  0.0468  -0.1308 241 ASN B CA  
3230 C C   . ASN B 207 ? 0.8663 0.8677 0.7419 0.0903  0.0619  -0.1125 241 ASN B C   
3231 O O   . ASN B 207 ? 0.9385 0.9426 0.8588 0.0884  0.0537  -0.1188 241 ASN B O   
3232 C CB  . ASN B 207 ? 0.9141 0.9091 0.7075 0.1203  0.0694  -0.1487 241 ASN B CB  
3233 C CG  . ASN B 207 ? 1.0127 0.9897 0.7732 0.1379  0.0502  -0.1786 241 ASN B CG  
3234 O OD1 . ASN B 207 ? 1.0116 0.9701 0.7933 0.1389  0.0182  -0.1889 241 ASN B OD1 
3235 N ND2 . ASN B 207 ? 1.1364 1.1184 0.8427 0.1503  0.0698  -0.1929 241 ASN B ND2 
3236 N N   . THR B 208 ? 0.8669 0.8758 0.7308 0.0797  0.0802  -0.0897 242 THR B N   
3237 C CA  . THR B 208 ? 0.7517 0.7732 0.6543 0.0648  0.0917  -0.0721 242 THR B CA  
3238 C C   . THR B 208 ? 0.7278 0.7381 0.6375 0.0508  0.0794  -0.0548 242 THR B C   
3239 O O   . THR B 208 ? 0.7649 0.7657 0.6440 0.0508  0.0781  -0.0456 242 THR B O   
3240 C CB  . THR B 208 ? 0.7335 0.7728 0.6234 0.0617  0.1226  -0.0604 242 THR B CB  
3241 O OG1 . THR B 208 ? 0.8478 0.8753 0.6934 0.0573  0.1270  -0.0435 242 THR B OG1 
3242 C CG2 . THR B 208 ? 0.6596 0.7160 0.5385 0.0769  0.1401  -0.0809 242 THR B CG2 
3243 N N   . ILE B 209 ? 0.7006 0.7114 0.6499 0.0392  0.0696  -0.0511 243 ILE B N   
3244 C CA  . ILE B 209 ? 0.6084 0.6134 0.5677 0.0254  0.0616  -0.0387 243 ILE B CA  
3245 C C   . ILE B 209 ? 0.5957 0.6069 0.5665 0.0127  0.0770  -0.0221 243 ILE B C   
3246 O O   . ILE B 209 ? 0.7134 0.7325 0.7084 0.0073  0.0817  -0.0204 243 ILE B O   
3247 C CB  . ILE B 209 ? 0.6695 0.6700 0.6572 0.0171  0.0416  -0.0443 243 ILE B CB  
3248 C CG1 . ILE B 209 ? 0.6209 0.6126 0.6002 0.0282  0.0227  -0.0607 243 ILE B CG1 
3249 C CG2 . ILE B 209 ? 0.5653 0.5664 0.5636 0.0014  0.0399  -0.0332 243 ILE B CG2 
3250 C CD1 . ILE B 209 ? 0.6922 0.6797 0.6470 0.0344  0.0171  -0.0611 243 ILE B CD1 
3251 N N   . ALA B 210 ? 0.6813 0.6868 0.6375 0.0084  0.0817  -0.0108 244 ALA B N   
3252 C CA  . ALA B 210 ? 0.5800 0.5861 0.5455 -0.0041 0.0926  0.0036  244 ALA B CA  
3253 C C   . ALA B 210 ? 0.6163 0.6180 0.5976 -0.0158 0.0839  0.0047  244 ALA B C   
3254 O O   . ALA B 210 ? 0.6190 0.6176 0.5972 -0.0126 0.0749  -0.0008 244 ALA B O   
3255 C CB  . ALA B 210 ? 0.5644 0.5626 0.5026 -0.0016 0.1030  0.0156  244 ALA B CB  
3256 N N   . MET B 211 ? 0.6291 0.6324 0.6277 -0.0297 0.0867  0.0106  245 MET B N   
3257 C CA  . MET B 211 ? 0.6142 0.6143 0.6210 -0.0431 0.0818  0.0106  245 MET B CA  
3258 C C   . MET B 211 ? 0.6330 0.6271 0.6411 -0.0541 0.0889  0.0198  245 MET B C   
3259 O O   . MET B 211 ? 0.7572 0.7515 0.7667 -0.0535 0.0963  0.0279  245 MET B O   
3260 C CB  . MET B 211 ? 0.5929 0.5955 0.6140 -0.0527 0.0706  0.0071  245 MET B CB  
3261 C CG  . MET B 211 ? 0.7475 0.7518 0.7828 -0.0519 0.0666  0.0089  245 MET B CG  
3262 S SD  . MET B 211 ? 0.6807 0.6818 0.7292 -0.0506 0.0474  0.0004  245 MET B SD  
3263 C CE  . MET B 211 ? 0.7083 0.7152 0.7520 -0.0258 0.0513  -0.0124 245 MET B CE  
3264 N N   . SER B 212 ? 0.6164 0.6061 0.6244 -0.0655 0.0872  0.0175  246 SER B N   
3265 C CA  . SER B 212 ? 0.7136 0.6928 0.7188 -0.0749 0.0912  0.0225  246 SER B CA  
3266 C C   . SER B 212 ? 0.6530 0.6306 0.6669 -0.0895 0.0862  0.0293  246 SER B C   
3267 O O   . SER B 212 ? 0.6364 0.6073 0.6546 -0.0949 0.0879  0.0366  246 SER B O   
3268 C CB  . SER B 212 ? 0.7159 0.6917 0.7149 -0.0792 0.0927  0.0126  246 SER B CB  
3269 O OG  . SER B 212 ? 0.7201 0.7003 0.7203 -0.0647 0.0934  0.0049  246 SER B OG  
3270 N N   . HIS B 213 ? 0.6483 0.6296 0.6669 -0.0969 0.0769  0.0283  247 HIS B N   
3271 C CA  . HIS B 213 ? 0.7179 0.6933 0.7434 -0.1118 0.0658  0.0352  247 HIS B CA  
3272 C C   . HIS B 213 ? 0.7144 0.6972 0.7632 -0.1060 0.0565  0.0379  247 HIS B C   
3273 O O   . HIS B 213 ? 0.7887 0.7650 0.8443 -0.1164 0.0402  0.0418  247 HIS B O   
3274 C CB  . HIS B 213 ? 0.6473 0.6143 0.6539 -0.1294 0.0589  0.0336  247 HIS B CB  
3275 C CG  . HIS B 213 ? 0.7897 0.7546 0.7769 -0.1320 0.0707  0.0247  247 HIS B CG  
3276 N ND1 . HIS B 213 ? 0.7788 0.7335 0.7603 -0.1324 0.0753  0.0230  247 HIS B ND1 
3277 C CD2 . HIS B 213 ? 0.7160 0.6891 0.6936 -0.1336 0.0784  0.0151  247 HIS B CD2 
3278 C CE1 . HIS B 213 ? 0.7361 0.6908 0.7042 -0.1318 0.0848  0.0106  247 HIS B CE1 
3279 N NE2 . HIS B 213 ? 0.8470 0.8160 0.8144 -0.1324 0.0884  0.0054  247 HIS B NE2 
3280 N N   . SER B 214 ? 0.7046 0.6995 0.7646 -0.0892 0.0658  0.0351  248 SER B N   
3281 C CA  . SER B 214 ? 0.6919 0.6969 0.7774 -0.0798 0.0601  0.0323  248 SER B CA  
3282 C C   . SER B 214 ? 0.6568 0.6775 0.7459 -0.0638 0.0782  0.0293  248 SER B C   
3283 O O   . SER B 214 ? 0.7289 0.7477 0.7942 -0.0580 0.0898  0.0292  248 SER B O   
3284 C CB  . SER B 214 ? 0.6629 0.6630 0.7475 -0.0761 0.0467  0.0249  248 SER B CB  
3285 O OG  . SER B 214 ? 0.7466 0.7328 0.8337 -0.0929 0.0273  0.0313  248 SER B OG  
3286 N N   . ALA B 215 ? 0.6631 0.6996 0.7823 -0.0570 0.0801  0.0268  249 ALA B N   
3287 C CA  . ALA B 215 ? 0.6539 0.7092 0.7732 -0.0422 0.1001  0.0215  249 ALA B CA  
3288 C C   . ALA B 215 ? 0.6277 0.6790 0.7236 -0.0267 0.0989  0.0082  249 ALA B C   
3289 O O   . ALA B 215 ? 0.6443 0.6834 0.7412 -0.0265 0.0805  0.0017  249 ALA B O   
3290 C CB  . ALA B 215 ? 0.5244 0.6035 0.6886 -0.0370 0.1036  0.0169  249 ALA B CB  
3291 N N   . PRO B 216 ? 0.6698 0.7288 0.7416 -0.0155 0.1164  0.0051  250 PRO B N   
3292 C CA  . PRO B 216 ? 0.6865 0.7392 0.7325 -0.0006 0.1118  -0.0088 250 PRO B CA  
3293 C C   . PRO B 216 ? 0.5887 0.6445 0.6590 0.0104  0.0987  -0.0266 250 PRO B C   
3294 O O   . PRO B 216 ? 0.6544 0.7267 0.7580 0.0152  0.1032  -0.0326 250 PRO B O   
3295 C CB  . PRO B 216 ? 0.7552 0.8177 0.7713 0.0078  0.1343  -0.0077 250 PRO B CB  
3296 C CG  . PRO B 216 ? 0.6647 0.7279 0.6813 -0.0073 0.1463  0.0127  250 PRO B CG  
3297 C CD  . PRO B 216 ? 0.6649 0.7341 0.7259 -0.0191 0.1387  0.0168  250 PRO B CD  
3298 N N   . ASP B 217 ? 0.6255 0.6650 0.6840 0.0145  0.0805  -0.0356 251 ASP B N   
3299 C CA  . ASP B 217 ? 0.6846 0.7176 0.7655 0.0229  0.0611  -0.0513 251 ASP B CA  
3300 C C   . ASP B 217 ? 0.7120 0.7365 0.7656 0.0382  0.0553  -0.0686 251 ASP B C   
3301 O O   . ASP B 217 ? 0.7353 0.7586 0.7524 0.0412  0.0641  -0.0665 251 ASP B O   
3302 C CB  . ASP B 217 ? 0.7323 0.7480 0.8309 0.0055  0.0374  -0.0416 251 ASP B CB  
3303 C CG  . ASP B 217 ? 0.7172 0.7234 0.8493 0.0102  0.0149  -0.0515 251 ASP B CG  
3304 O OD1 . ASP B 217 ? 0.8046 0.8206 0.9524 0.0297  0.0187  -0.0695 251 ASP B OD1 
3305 O OD2 . ASP B 217 ? 0.7732 0.7615 0.9152 -0.0057 -0.0068 -0.0416 251 ASP B OD2 
3306 N N   . SER B 218 ? 0.7279 0.7429 0.7999 0.0480  0.0363  -0.0860 252 SER B N   
3307 C CA  . SER B 218 ? 0.7144 0.7178 0.7633 0.0629  0.0257  -0.1059 252 SER B CA  
3308 C C   . SER B 218 ? 0.7307 0.7155 0.7715 0.0503  0.0042  -0.0988 252 SER B C   
3309 O O   . SER B 218 ? 0.7694 0.7536 0.8183 0.0309  0.0026  -0.0796 252 SER B O   
3310 C CB  . SER B 218 ? 0.6670 0.6650 0.7429 0.0795  0.0120  -0.1301 252 SER B CB  
3311 O OG  . SER B 218 ? 0.6809 0.6550 0.7840 0.0695  -0.0200 -0.1276 252 SER B OG  
3312 N N   . ARG B 219 ? 0.8011 0.7232 0.8657 0.0397  0.1636  -0.0242 253 ARG B N   
3313 C CA  . ARG B 219 ? 0.8617 0.7256 0.8617 -0.0130 0.1425  -0.0297 253 ARG B CA  
3314 C C   . ARG B 219 ? 0.9144 0.7339 0.8474 -0.0225 0.1094  -0.0333 253 ARG B C   
3315 O O   . ARG B 219 ? 0.9353 0.7337 0.8418 -0.0706 0.0921  -0.0378 253 ARG B O   
3316 C CB  . ARG B 219 ? 0.8864 0.6475 0.7871 -0.0128 0.1482  -0.0206 253 ARG B CB  
3317 C CG  . ARG B 219 ? 0.7904 0.5844 0.7464 -0.0332 0.1716  -0.0179 253 ARG B CG  
3318 C CD  . ARG B 219 ? 0.8565 0.5387 0.7053 -0.0516 0.1640  -0.0096 253 ARG B CD  
3319 N NE  . ARG B 219 ? 0.8600 0.5281 0.7054 -0.1132 0.1408  -0.0113 253 ARG B NE  
3320 C CZ  . ARG B 219 ? 0.8302 0.5469 0.7498 -0.1569 0.1474  -0.0117 253 ARG B CZ  
3321 N NH1 . ARG B 219 ? 0.7175 0.4990 0.7183 -0.1490 0.1737  -0.0108 253 ARG B NH1 
3322 N NH2 . ARG B 219 ? 0.7695 0.4702 0.6853 -0.2095 0.1276  -0.0113 253 ARG B NH2 
3323 N N   . ALA B 220 ? 0.8820 0.6866 0.7888 0.0221  0.1006  -0.0294 254 ALA B N   
3324 C CA  . ALA B 220 ? 0.9790 0.7418 0.8222 0.0132  0.0669  -0.0311 254 ALA B CA  
3325 C C   . ALA B 220 ? 0.9167 0.7595 0.8316 -0.0255 0.0530  -0.0429 254 ALA B C   
3326 O O   . ALA B 220 ? 0.8836 0.6906 0.7416 -0.0513 0.0268  -0.0453 254 ALA B O   
3327 C CB  . ALA B 220 ? 0.9899 0.7243 0.8008 0.0716  0.0602  -0.0231 254 ALA B CB  
3328 N N   . ALA B 221 ? 0.8176 0.7640 0.8520 -0.0303 0.0696  -0.0498 255 ALA B N   
3329 C CA  . ALA B 221 ? 0.7384 0.7558 0.8374 -0.0676 0.0572  -0.0636 255 ALA B CA  
3330 C C   . ALA B 221 ? 0.7745 0.7726 0.8485 -0.1252 0.0554  -0.0719 255 ALA B C   
3331 O O   . ALA B 221 ? 0.7967 0.8214 0.8818 -0.1572 0.0418  -0.0831 255 ALA B O   
3332 C CB  . ALA B 221 ? 0.6971 0.8240 0.9304 -0.0599 0.0742  -0.0681 255 ALA B CB  
3333 N N   . ILE B 222 ? 0.8354 0.7865 0.8762 -0.1391 0.0690  -0.0654 256 ILE B N   
3334 C CA  . ILE B 222 ? 0.8401 0.7702 0.8622 -0.1933 0.0669  -0.0686 256 ILE B CA  
3335 C C   . ILE B 222 ? 0.9210 0.7740 0.8382 -0.2087 0.0407  -0.0636 256 ILE B C   
3336 O O   . ILE B 222 ? 0.9253 0.7939 0.8454 -0.2477 0.0339  -0.0706 256 ILE B O   
3337 C CB  . ILE B 222 ? 0.9213 0.8159 0.9352 -0.2041 0.0828  -0.0592 256 ILE B CB  
3338 C CG1 . ILE B 222 ? 0.9072 0.8612 1.0026 -0.1750 0.1080  -0.0588 256 ILE B CG1 
3339 C CG2 . ILE B 222 ? 0.8488 0.7559 0.8915 -0.2616 0.0857  -0.0624 256 ILE B CG2 
3340 C CD1 . ILE B 222 ? 0.8194 0.7500 0.9189 -0.1921 0.1235  -0.0506 256 ILE B CD1 
3341 N N   . THR B 223 ? 0.9946 0.7615 0.8163 -0.1777 0.0266  -0.0507 257 THR B N   
3342 C CA  . THR B 223 ? 1.0635 0.7522 0.7834 -0.1921 -0.0012 -0.0430 257 THR B CA  
3343 C C   . THR B 223 ? 1.0231 0.7448 0.7468 -0.1869 -0.0190 -0.0503 257 THR B C   
3344 O O   . THR B 223 ? 1.1039 0.8069 0.7867 -0.2207 -0.0344 -0.0502 257 THR B O   
3345 C CB  . THR B 223 ? 1.1682 0.7509 0.7838 -0.1585 -0.0141 -0.0281 257 THR B CB  
3346 O OG1 . THR B 223 ? 1.1869 0.7568 0.8156 -0.1424 0.0073  -0.0246 257 THR B OG1 
3347 C CG2 . THR B 223 ? 1.2699 0.7614 0.7871 -0.1923 -0.0388 -0.0154 257 THR B CG2 
3348 N N   . HIS B 224 ? 0.9963 0.7660 0.7686 -0.1455 -0.0178 -0.0546 258 HIS B N   
3349 C CA  . HIS B 224 ? 1.0169 0.8193 0.7982 -0.1416 -0.0391 -0.0603 258 HIS B CA  
3350 C C   . HIS B 224 ? 0.9813 0.8459 0.8125 -0.1890 -0.0360 -0.0758 258 HIS B C   
3351 O O   . HIS B 224 ? 1.0028 0.8580 0.7944 -0.2075 -0.0566 -0.0790 258 HIS B O   
3352 C CB  . HIS B 224 ? 0.9003 0.7572 0.7504 -0.0925 -0.0366 -0.0600 258 HIS B CB  
3353 C CG  . HIS B 224 ? 0.9076 0.8026 0.7781 -0.0901 -0.0623 -0.0646 258 HIS B CG  
3354 N ND1 . HIS B 224 ? 1.0376 0.8726 0.8219 -0.0885 -0.0943 -0.0576 258 HIS B ND1 
3355 C CD2 . HIS B 224 ? 0.9804 0.9632 0.9452 -0.0910 -0.0644 -0.0743 258 HIS B CD2 
3356 C CE1 . HIS B 224 ? 1.0990 0.9825 0.9213 -0.0886 -0.1149 -0.0628 258 HIS B CE1 
3357 N NE2 . HIS B 224 ? 1.0135 0.9854 0.9445 -0.0901 -0.0982 -0.0732 258 HIS B NE2 
3358 N N   . THR B 225 ? 0.9003 0.8257 0.8156 -0.2086 -0.0099 -0.0856 259 THR B N   
3359 C CA  . THR B 225 ? 0.8471 0.8208 0.8034 -0.2549 -0.0026 -0.1010 259 THR B CA  
3360 C C   . THR B 225 ? 0.9186 0.8297 0.7960 -0.2950 -0.0059 -0.0945 259 THR B C   
3361 O O   . THR B 225 ? 0.9467 0.8666 0.8067 -0.3252 -0.0110 -0.1027 259 THR B O   
3362 C CB  . THR B 225 ? 0.6973 0.7426 0.7610 -0.2657 0.0256  -0.1107 259 THR B CB  
3363 O OG1 . THR B 225 ? 0.6369 0.7528 0.7844 -0.2349 0.0262  -0.1167 259 THR B OG1 
3364 C CG2 . THR B 225 ? 0.5986 0.6800 0.6974 -0.3149 0.0372  -0.1258 259 THR B CG2 
3365 N N   . ALA B 226 ? 0.9698 0.8140 0.7959 -0.2958 -0.0038 -0.0782 260 ALA B N   
3366 C CA  . ALA B 226 ? 0.9964 0.7782 0.7516 -0.3339 -0.0101 -0.0664 260 ALA B CA  
3367 C C   . ALA B 226 ? 1.1248 0.8417 0.7783 -0.3276 -0.0400 -0.0562 260 ALA B C   
3368 O O   . ALA B 226 ? 1.2133 0.9047 0.8215 -0.3634 -0.0457 -0.0505 260 ALA B O   
3369 C CB  . ALA B 226 ? 0.9501 0.6750 0.6816 -0.3382 -0.0049 -0.0501 260 ALA B CB  
3370 N N   . ARG B 227 ? 1.2392 0.9286 0.8580 -0.2824 -0.0585 -0.0519 261 ARG B N   
3371 C CA  . ARG B 227 ? 1.2412 0.8716 0.7689 -0.2750 -0.0899 -0.0421 261 ARG B CA  
3372 C C   . ARG B 227 ? 1.2472 0.9240 0.7858 -0.2967 -0.0972 -0.0540 261 ARG B C   
3373 O O   . ARG B 227 ? 1.2909 0.9245 0.7560 -0.3209 -0.1138 -0.0457 261 ARG B O   
3374 C CB  . ARG B 227 ? 1.2790 0.8797 0.7831 -0.2187 -0.1059 -0.0362 261 ARG B CB  
3375 C CG  . ARG B 227 ? 1.2950 0.8316 0.7639 -0.1925 -0.1004 -0.0246 261 ARG B CG  
3376 C CD  . ARG B 227 ? 1.5545 0.9794 0.9038 -0.1909 -0.1294 -0.0062 261 ARG B CD  
3377 N NE  . ARG B 227 ? 1.7290 1.0886 1.0371 -0.2060 -0.1246 0.0049  261 ARG B NE  
3378 C CZ  . ARG B 227 ? 1.7736 1.0931 1.0670 -0.1726 -0.1159 0.0078  261 ARG B CZ  
3379 N NH1 . ARG B 227 ? 1.6558 0.9977 0.9771 -0.1198 -0.1061 0.0014  261 ARG B NH1 
3380 N NH2 . ARG B 227 ? 1.7950 1.0491 1.0446 -0.1930 -0.1168 0.0188  261 ARG B NH2 
3381 N N   . MET B 228 ? 1.1646 0.9258 0.7910 -0.2891 -0.0860 -0.0728 262 MET B N   
3382 C CA  . MET B 228 ? 1.1031 0.9046 0.7368 -0.3114 -0.0933 -0.0868 262 MET B CA  
3383 C C   . MET B 228 ? 1.1702 0.9811 0.8019 -0.3626 -0.0719 -0.0930 262 MET B C   
3384 O O   . MET B 228 ? 1.2531 1.0509 0.8329 -0.3878 -0.0804 -0.0950 262 MET B O   
3385 C CB  . MET B 228 ? 1.0925 0.9786 0.8244 -0.2919 -0.0895 -0.1043 262 MET B CB  
3386 C CG  . MET B 228 ? 1.0247 0.9104 0.7668 -0.2416 -0.1118 -0.0961 262 MET B CG  
3387 S SD  . MET B 228 ? 0.8847 0.8747 0.7563 -0.2220 -0.1083 -0.1115 262 MET B SD  
3388 C CE  . MET B 228 ? 0.9171 0.9570 0.8757 -0.2377 -0.0649 -0.1208 262 MET B CE  
3389 N N   . ALA B 229 ? 1.0871 0.9202 0.7756 -0.3783 -0.0432 -0.0947 263 ALA B N   
3390 C CA  . ALA B 229 ? 1.1233 0.9661 0.8198 -0.4252 -0.0201 -0.0975 263 ALA B CA  
3391 C C   . ALA B 229 ? 1.1508 0.9150 0.7523 -0.4482 -0.0305 -0.0739 263 ALA B C   
3392 O O   . ALA B 229 ? 1.2429 1.0085 0.8284 -0.4859 -0.0170 -0.0731 263 ALA B O   
3393 C CB  . ALA B 229 ? 1.0619 0.9453 0.8479 -0.4353 0.0093  -0.1017 263 ALA B CB  
3394 N N   . ASP B 230 ? 1.2174 0.9114 0.7561 -0.4258 -0.0535 -0.0537 264 ASP B N   
3395 C CA  . ASP B 230 ? 1.2671 0.8810 0.7104 -0.4457 -0.0712 -0.0291 264 ASP B CA  
3396 C C   . ASP B 230 ? 1.4121 1.0138 0.7902 -0.4541 -0.0892 -0.0296 264 ASP B C   
3397 O O   . ASP B 230 ? 1.5365 1.1212 0.8754 -0.4913 -0.0833 -0.0198 264 ASP B O   
3398 C CB  . ASP B 230 ? 1.2571 0.7933 0.6426 -0.4150 -0.0959 -0.0105 264 ASP B CB  
3399 C CG  . ASP B 230 ? 1.3296 0.8456 0.7426 -0.4226 -0.0826 -0.0006 264 ASP B CG  
3400 O OD1 . ASP B 230 ? 1.3722 0.9182 0.8287 -0.4543 -0.0608 0.0038  264 ASP B OD1 
3401 O OD2 . ASP B 230 ? 1.2941 0.7700 0.6884 -0.3883 -0.0927 0.0042  264 ASP B OD2 
3402 N N   . LYS B 231 ? 1.3971 1.0075 0.7644 -0.4201 -0.1113 -0.0389 265 LYS B N   
3403 C CA  . LYS B 231 ? 1.3944 0.9931 0.6998 -0.4277 -0.1326 -0.0397 265 LYS B CA  
3404 C C   . LYS B 231 ? 1.4676 1.1238 0.8034 -0.4616 -0.1081 -0.0591 265 LYS B C   
3405 O O   . LYS B 231 ? 1.5755 1.2103 0.8447 -0.4848 -0.1157 -0.0554 265 LYS B O   
3406 C CB  . LYS B 231 ? 1.3310 0.9356 0.6376 -0.3839 -0.1618 -0.0454 265 LYS B CB  
3407 C CG  . LYS B 231 ? 1.4508 1.0022 0.7348 -0.3432 -0.1802 -0.0296 265 LYS B CG  
3408 C CD  . LYS B 231 ? 1.4829 1.0375 0.7665 -0.3004 -0.2097 -0.0309 265 LYS B CD  
3409 C CE  . LYS B 231 ? 1.5420 1.1697 0.9316 -0.2683 -0.1935 -0.0466 265 LYS B CE  
3410 N NZ  . LYS B 231 ? 1.5218 1.1435 0.9171 -0.2194 -0.2201 -0.0403 265 LYS B NZ  
3411 N N   . LEU B 232 ? 1.3646 1.0905 0.7970 -0.4646 -0.0784 -0.0799 266 LEU B N   
3412 C CA  . LEU B 232 ? 1.3201 1.0969 0.7833 -0.4953 -0.0522 -0.1007 266 LEU B CA  
3413 C C   . LEU B 232 ? 1.5445 1.3001 0.9818 -0.5373 -0.0256 -0.0877 266 LEU B C   
3414 O O   . LEU B 232 ? 1.6514 1.4050 1.0448 -0.5637 -0.0156 -0.0917 266 LEU B O   
3415 C CB  . LEU B 232 ? 1.1974 1.0514 0.7754 -0.4863 -0.0295 -0.1247 266 LEU B CB  
3416 C CG  . LEU B 232 ? 1.2017 1.1086 0.8281 -0.5174 0.0044  -0.1476 266 LEU B CG  
3417 C CD1 . LEU B 232 ? 1.3620 1.2638 0.9257 -0.5300 -0.0059 -0.1616 266 LEU B CD1 
3418 C CD2 . LEU B 232 ? 1.0344 1.0147 0.7794 -0.4912 0.0212  -0.1634 266 LEU B CD2 
3419 N N   . ARG B 233 ? 1.5185 1.2566 0.9823 -0.5442 -0.0138 -0.0702 267 ARG B N   
3420 C CA  . ARG B 233 ? 1.4737 1.2083 0.9363 -0.5603 0.0128  -0.0492 267 ARG B CA  
3421 C C   . ARG B 233 ? 1.6597 1.3225 1.0104 -0.5913 -0.0068 -0.0271 267 ARG B C   
3422 O O   . ARG B 233 ? 1.7396 1.4103 1.0737 -0.6128 0.0155  -0.0203 267 ARG B O   
3423 C CB  . ARG B 233 ? 1.3563 1.0925 0.8726 -0.5327 0.0184  -0.0314 267 ARG B CB  
3424 N N   T LEU B 234 ? 1.7069 1.3059 0.9844 -0.5765 -0.0484 -0.0142 268 LEU B N   
3425 C CA  T LEU B 234 ? 1.7926 1.3268 0.9658 -0.5912 -0.0714 0.0104  268 LEU B CA  
3426 C C   T LEU B 234 ? 1.8857 1.4396 1.0165 -0.6042 -0.0671 -0.0040 268 LEU B C   
3427 O O   T LEU B 234 ? 1.9194 1.4497 0.9932 -0.6360 -0.0578 0.0121  268 LEU B O   
3428 C CB  T LEU B 234 ? 1.6851 1.1543 0.7974 -0.5573 -0.1174 0.0253  268 LEU B CB  
3429 C CG  T LEU B 234 ? 1.8459 1.2484 0.9344 -0.5570 -0.1327 0.0541  268 LEU B CG  
3430 C CD1 T LEU B 234 ? 1.6995 1.1337 0.8759 -0.5579 -0.1070 0.0484  268 LEU B CD1 
3431 C CD2 T LEU B 234 ? 1.9045 1.2444 0.9325 -0.5168 -0.1760 0.0623  268 LEU B CD2 
3432 N N   . GLU B 235 ? 1.8789 1.4739 1.0351 -0.5807 -0.0744 -0.0326 269 GLU B N   
3433 C CA  . GLU B 235 ? 1.9114 1.5259 1.0309 -0.5935 -0.0709 -0.0509 269 GLU B CA  
3434 C C   . GLU B 235 ? 1.9419 1.6200 1.1317 -0.6158 -0.0223 -0.0752 269 GLU B C   
3435 O O   . GLU B 235 ? 1.9482 1.6779 1.1919 -0.6043 -0.0160 -0.1056 269 GLU B O   
3436 C CB  . GLU B 235 ? 1.9298 1.5534 1.0444 -0.5597 -0.1076 -0.0672 269 GLU B CB  
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