data_8Z6E
# 
_entry.id   8Z6E 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8Z6E         pdb_00008z6e 10.2210/pdb8z6e/pdb 
WWPDB D_1300046809 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_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                        8Z6E 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yurong.wen@xjtu.edu.cn 
_pdbx_contact_author.name_first         Yurong 
_pdbx_contact_author.name_last          Wen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8730-5197 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'He, W.'  1 0000-0002-2109-1517 
'Wen, Y.' 2 0000-0001-8730-5197 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure of transcriptional regulator TetR' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'He, W.'  1 0000-0002-2109-1517 
primary 'Wen, Y.' 2 0000-0001-8730-5197 
# 
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 'TetR family transcriptional regulator' 23110.395 2   ? ? ? ? 
2 water   nat water                                   18.015    161 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'TetR/AcrR family transcriptional regulator,transcriptional regulator TetR2' 
# 
_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       
;MGMTNKASQPRTFTLSDEKRNHILTTALNLFDQFGFQHISIMRIITEAKIAKQSFYMAFPSKDSFIIECLDMEINRLKQS
LSNLLGQCGKDDHTSILKSFYQWHVDLAYREGYNGTLLTKAVIEYWNLPDIKMKVEDFNKWKYEIFAEYLAEEINNARLR
IIVSAMNGILLPASTYLPTWEDIESLYGEQFHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGMTNKASQPRTFTLSDEKRNHILTTALNLFDQFGFQHISIMRIITEAKIAKQSFYMAFPSKDSFIIECLDMEINRLKQS
LSNLLGQCGKDDHTSILKSFYQWHVDLAYREGYNGTLLTKAVIEYWNLPDIKMKVEDFNKWKYEIFAEYLAEEINNARLR
IIVSAMNGILLPASTYLPTWEDIESLYGEQFHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   MET n 
1 4   THR n 
1 5   ASN n 
1 6   LYS n 
1 7   ALA n 
1 8   SER n 
1 9   GLN n 
1 10  PRO n 
1 11  ARG n 
1 12  THR n 
1 13  PHE n 
1 14  THR n 
1 15  LEU n 
1 16  SER n 
1 17  ASP n 
1 18  GLU n 
1 19  LYS n 
1 20  ARG n 
1 21  ASN n 
1 22  HIS n 
1 23  ILE n 
1 24  LEU n 
1 25  THR n 
1 26  THR n 
1 27  ALA n 
1 28  LEU n 
1 29  ASN n 
1 30  LEU n 
1 31  PHE n 
1 32  ASP n 
1 33  GLN n 
1 34  PHE n 
1 35  GLY n 
1 36  PHE n 
1 37  GLN n 
1 38  HIS n 
1 39  ILE n 
1 40  SER n 
1 41  ILE n 
1 42  MET n 
1 43  ARG n 
1 44  ILE n 
1 45  ILE n 
1 46  THR n 
1 47  GLU n 
1 48  ALA n 
1 49  LYS n 
1 50  ILE n 
1 51  ALA n 
1 52  LYS n 
1 53  GLN n 
1 54  SER n 
1 55  PHE n 
1 56  TYR n 
1 57  MET n 
1 58  ALA n 
1 59  PHE n 
1 60  PRO n 
1 61  SER n 
1 62  LYS n 
1 63  ASP n 
1 64  SER n 
1 65  PHE n 
1 66  ILE n 
1 67  ILE n 
1 68  GLU n 
1 69  CYS n 
1 70  LEU n 
1 71  ASP n 
1 72  MET n 
1 73  GLU n 
1 74  ILE n 
1 75  ASN n 
1 76  ARG n 
1 77  LEU n 
1 78  LYS n 
1 79  GLN n 
1 80  SER n 
1 81  LEU n 
1 82  SER n 
1 83  ASN n 
1 84  LEU n 
1 85  LEU n 
1 86  GLY n 
1 87  GLN n 
1 88  CYS n 
1 89  GLY n 
1 90  LYS n 
1 91  ASP n 
1 92  ASP n 
1 93  HIS n 
1 94  THR n 
1 95  SER n 
1 96  ILE n 
1 97  LEU n 
1 98  LYS n 
1 99  SER n 
1 100 PHE n 
1 101 TYR n 
1 102 GLN n 
1 103 TRP n 
1 104 HIS n 
1 105 VAL n 
1 106 ASP n 
1 107 LEU n 
1 108 ALA n 
1 109 TYR n 
1 110 ARG n 
1 111 GLU n 
1 112 GLY n 
1 113 TYR n 
1 114 ASN n 
1 115 GLY n 
1 116 THR n 
1 117 LEU n 
1 118 LEU n 
1 119 THR n 
1 120 LYS n 
1 121 ALA n 
1 122 VAL n 
1 123 ILE n 
1 124 GLU n 
1 125 TYR n 
1 126 TRP n 
1 127 ASN n 
1 128 LEU n 
1 129 PRO n 
1 130 ASP n 
1 131 ILE n 
1 132 LYS n 
1 133 MET n 
1 134 LYS n 
1 135 VAL n 
1 136 GLU n 
1 137 ASP n 
1 138 PHE n 
1 139 ASN n 
1 140 LYS n 
1 141 TRP n 
1 142 LYS n 
1 143 TYR n 
1 144 GLU n 
1 145 ILE n 
1 146 PHE n 
1 147 ALA n 
1 148 GLU n 
1 149 TYR n 
1 150 LEU n 
1 151 ALA n 
1 152 GLU n 
1 153 GLU n 
1 154 ILE n 
1 155 ASN n 
1 156 ASN n 
1 157 ALA n 
1 158 ARG n 
1 159 LEU n 
1 160 ARG n 
1 161 ILE n 
1 162 ILE n 
1 163 VAL n 
1 164 SER n 
1 165 ALA n 
1 166 MET n 
1 167 ASN n 
1 168 GLY n 
1 169 ILE n 
1 170 LEU n 
1 171 LEU n 
1 172 PRO n 
1 173 ALA n 
1 174 SER n 
1 175 THR n 
1 176 TYR n 
1 177 LEU n 
1 178 PRO n 
1 179 THR n 
1 180 TRP n 
1 181 GLU n 
1 182 ASP n 
1 183 ILE n 
1 184 GLU n 
1 185 SER n 
1 186 LEU n 
1 187 TYR n 
1 188 GLY n 
1 189 GLU n 
1 190 GLN n 
1 191 PHE n 
1 192 HIS n 
1 193 HIS n 
1 194 HIS n 
1 195 HIS n 
1 196 HIS n 
1 197 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   197 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'AUO97_08420, F4T85_12235, FJU42_13590, HBK86_20440' 
_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      'Acinetobacter baumannii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     470 
_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 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -1  ?   ?   ?   A . n 
A 1 2   GLY 2   0   ?   ?   ?   A . n 
A 1 3   MET 3   1   ?   ?   ?   A . n 
A 1 4   THR 4   2   ?   ?   ?   A . n 
A 1 5   ASN 5   3   ?   ?   ?   A . n 
A 1 6   LYS 6   4   ?   ?   ?   A . n 
A 1 7   ALA 7   5   ?   ?   ?   A . n 
A 1 8   SER 8   6   ?   ?   ?   A . n 
A 1 9   GLN 9   7   ?   ?   ?   A . n 
A 1 10  PRO 10  8   ?   ?   ?   A . n 
A 1 11  ARG 11  9   ?   ?   ?   A . n 
A 1 12  THR 12  10  ?   ?   ?   A . n 
A 1 13  PHE 13  11  ?   ?   ?   A . n 
A 1 14  THR 14  12  ?   ?   ?   A . n 
A 1 15  LEU 15  13  13  LEU LEU A . n 
A 1 16  SER 16  14  14  SER SER A . n 
A 1 17  ASP 17  15  15  ASP ASP A . n 
A 1 18  GLU 18  16  16  GLU GLU A . n 
A 1 19  LYS 19  17  17  LYS LYS A . n 
A 1 20  ARG 20  18  18  ARG ARG A . n 
A 1 21  ASN 21  19  19  ASN ASN A . n 
A 1 22  HIS 22  20  20  HIS HIS A . n 
A 1 23  ILE 23  21  21  ILE ILE A . n 
A 1 24  LEU 24  22  22  LEU LEU A . n 
A 1 25  THR 25  23  23  THR THR A . n 
A 1 26  THR 26  24  24  THR THR A . n 
A 1 27  ALA 27  25  25  ALA ALA A . n 
A 1 28  LEU 28  26  26  LEU LEU A . n 
A 1 29  ASN 29  27  27  ASN ASN A . n 
A 1 30  LEU 30  28  28  LEU LEU A . n 
A 1 31  PHE 31  29  29  PHE PHE A . n 
A 1 32  ASP 32  30  30  ASP ASP A . n 
A 1 33  GLN 33  31  31  GLN GLN A . n 
A 1 34  PHE 34  32  32  PHE PHE A . n 
A 1 35  GLY 35  33  33  GLY GLY A . n 
A 1 36  PHE 36  34  34  PHE PHE A . n 
A 1 37  GLN 37  35  35  GLN GLN A . n 
A 1 38  HIS 38  36  36  HIS HIS A . n 
A 1 39  ILE 39  37  37  ILE ILE A . n 
A 1 40  SER 40  38  38  SER SER A . n 
A 1 41  ILE 41  39  39  ILE ILE A . n 
A 1 42  MET 42  40  40  MET MET A . n 
A 1 43  ARG 43  41  41  ARG ARG A . n 
A 1 44  ILE 44  42  42  ILE ILE A . n 
A 1 45  ILE 45  43  43  ILE ILE A . n 
A 1 46  THR 46  44  44  THR THR A . n 
A 1 47  GLU 47  45  45  GLU GLU A . n 
A 1 48  ALA 48  46  46  ALA ALA A . n 
A 1 49  LYS 49  47  47  LYS LYS A . n 
A 1 50  ILE 50  48  48  ILE ILE A . n 
A 1 51  ALA 51  49  49  ALA ALA A . n 
A 1 52  LYS 52  50  50  LYS LYS A . n 
A 1 53  GLN 53  51  51  GLN GLN A . n 
A 1 54  SER 54  52  52  SER SER A . n 
A 1 55  PHE 55  53  53  PHE PHE A . n 
A 1 56  TYR 56  54  54  TYR TYR A . n 
A 1 57  MET 57  55  55  MET MET A . n 
A 1 58  ALA 58  56  56  ALA ALA A . n 
A 1 59  PHE 59  57  57  PHE PHE A . n 
A 1 60  PRO 60  58  58  PRO PRO A . n 
A 1 61  SER 61  59  59  SER SER A . n 
A 1 62  LYS 62  60  60  LYS LYS A . n 
A 1 63  ASP 63  61  61  ASP ASP A . n 
A 1 64  SER 64  62  62  SER SER A . n 
A 1 65  PHE 65  63  63  PHE PHE A . n 
A 1 66  ILE 66  64  64  ILE ILE A . n 
A 1 67  ILE 67  65  65  ILE ILE A . n 
A 1 68  GLU 68  66  66  GLU GLU A . n 
A 1 69  CYS 69  67  67  CYS CYS A . n 
A 1 70  LEU 70  68  68  LEU LEU A . n 
A 1 71  ASP 71  69  69  ASP ASP A . n 
A 1 72  MET 72  70  70  MET MET A . n 
A 1 73  GLU 73  71  71  GLU GLU A . n 
A 1 74  ILE 74  72  72  ILE ILE A . n 
A 1 75  ASN 75  73  73  ASN ASN A . n 
A 1 76  ARG 76  74  74  ARG ARG A . n 
A 1 77  LEU 77  75  75  LEU LEU A . n 
A 1 78  LYS 78  76  76  LYS LYS A . n 
A 1 79  GLN 79  77  77  GLN GLN A . n 
A 1 80  SER 80  78  78  SER SER A . n 
A 1 81  LEU 81  79  79  LEU LEU A . n 
A 1 82  SER 82  80  80  SER SER A . n 
A 1 83  ASN 83  81  81  ASN ASN A . n 
A 1 84  LEU 84  82  82  LEU LEU A . n 
A 1 85  LEU 85  83  83  LEU LEU A . n 
A 1 86  GLY 86  84  84  GLY GLY A . n 
A 1 87  GLN 87  85  85  GLN GLN A . n 
A 1 88  CYS 88  86  86  CYS CYS A . n 
A 1 89  GLY 89  87  87  GLY GLY A . n 
A 1 90  LYS 90  88  88  LYS LYS A . n 
A 1 91  ASP 91  89  89  ASP ASP A . n 
A 1 92  ASP 92  90  90  ASP ASP A . n 
A 1 93  HIS 93  91  91  HIS HIS A . n 
A 1 94  THR 94  92  92  THR THR A . n 
A 1 95  SER 95  93  93  SER SER A . n 
A 1 96  ILE 96  94  94  ILE ILE A . n 
A 1 97  LEU 97  95  95  LEU LEU A . n 
A 1 98  LYS 98  96  96  LYS LYS A . n 
A 1 99  SER 99  97  97  SER SER A . n 
A 1 100 PHE 100 98  98  PHE PHE A . n 
A 1 101 TYR 101 99  99  TYR TYR A . n 
A 1 102 GLN 102 100 100 GLN GLN A . n 
A 1 103 TRP 103 101 101 TRP TRP A . n 
A 1 104 HIS 104 102 102 HIS HIS A . n 
A 1 105 VAL 105 103 103 VAL VAL A . n 
A 1 106 ASP 106 104 104 ASP ASP A . n 
A 1 107 LEU 107 105 105 LEU LEU A . n 
A 1 108 ALA 108 106 106 ALA ALA A . n 
A 1 109 TYR 109 107 107 TYR TYR A . n 
A 1 110 ARG 110 108 108 ARG ARG A . n 
A 1 111 GLU 111 109 109 GLU GLU A . n 
A 1 112 GLY 112 110 110 GLY GLY A . n 
A 1 113 TYR 113 111 111 TYR TYR A . n 
A 1 114 ASN 114 112 112 ASN ASN A . n 
A 1 115 GLY 115 113 113 GLY GLY A . n 
A 1 116 THR 116 114 114 THR THR A . n 
A 1 117 LEU 117 115 115 LEU LEU A . n 
A 1 118 LEU 118 116 116 LEU LEU A . n 
A 1 119 THR 119 117 117 THR THR A . n 
A 1 120 LYS 120 118 118 LYS LYS A . n 
A 1 121 ALA 121 119 119 ALA ALA A . n 
A 1 122 VAL 122 120 120 VAL VAL A . n 
A 1 123 ILE 123 121 121 ILE ILE A . n 
A 1 124 GLU 124 122 122 GLU GLU A . n 
A 1 125 TYR 125 123 123 TYR TYR A . n 
A 1 126 TRP 126 124 124 TRP TRP A . n 
A 1 127 ASN 127 125 125 ASN ASN A . n 
A 1 128 LEU 128 126 126 LEU LEU A . n 
A 1 129 PRO 129 127 127 PRO PRO A . n 
A 1 130 ASP 130 128 128 ASP ASP A . n 
A 1 131 ILE 131 129 129 ILE ILE A . n 
A 1 132 LYS 132 130 130 LYS LYS A . n 
A 1 133 MET 133 131 131 MET MET A . n 
A 1 134 LYS 134 132 132 LYS LYS A . n 
A 1 135 VAL 135 133 133 VAL VAL A . n 
A 1 136 GLU 136 134 134 GLU GLU A . n 
A 1 137 ASP 137 135 135 ASP ASP A . n 
A 1 138 PHE 138 136 136 PHE PHE A . n 
A 1 139 ASN 139 137 137 ASN ASN A . n 
A 1 140 LYS 140 138 138 LYS LYS A . n 
A 1 141 TRP 141 139 139 TRP TRP A . n 
A 1 142 LYS 142 140 140 LYS LYS A . n 
A 1 143 TYR 143 141 141 TYR TYR A . n 
A 1 144 GLU 144 142 142 GLU GLU A . n 
A 1 145 ILE 145 143 143 ILE ILE A . n 
A 1 146 PHE 146 144 144 PHE PHE A . n 
A 1 147 ALA 147 145 145 ALA ALA A . n 
A 1 148 GLU 148 146 146 GLU GLU A . n 
A 1 149 TYR 149 147 147 TYR TYR A . n 
A 1 150 LEU 150 148 148 LEU LEU A . n 
A 1 151 ALA 151 149 149 ALA ALA A . n 
A 1 152 GLU 152 150 150 GLU GLU A . n 
A 1 153 GLU 153 151 151 GLU GLU A . n 
A 1 154 ILE 154 152 152 ILE ILE A . n 
A 1 155 ASN 155 153 153 ASN ASN A . n 
A 1 156 ASN 156 154 154 ASN ASN A . n 
A 1 157 ALA 157 155 155 ALA ALA A . n 
A 1 158 ARG 158 156 156 ARG ARG A . n 
A 1 159 LEU 159 157 157 LEU LEU A . n 
A 1 160 ARG 160 158 158 ARG ARG A . n 
A 1 161 ILE 161 159 159 ILE ILE A . n 
A 1 162 ILE 162 160 160 ILE ILE A . n 
A 1 163 VAL 163 161 161 VAL VAL A . n 
A 1 164 SER 164 162 162 SER SER A . n 
A 1 165 ALA 165 163 163 ALA ALA A . n 
A 1 166 MET 166 164 164 MET MET A . n 
A 1 167 ASN 167 165 165 ASN ASN A . n 
A 1 168 GLY 168 166 166 GLY GLY A . n 
A 1 169 ILE 169 167 167 ILE ILE A . n 
A 1 170 LEU 170 168 168 LEU LEU A . n 
A 1 171 LEU 171 169 169 LEU LEU A . n 
A 1 172 PRO 172 170 170 PRO PRO A . n 
A 1 173 ALA 173 171 171 ALA ALA A . n 
A 1 174 SER 174 172 172 SER SER A . n 
A 1 175 THR 175 173 173 THR THR A . n 
A 1 176 TYR 176 174 174 TYR TYR A . n 
A 1 177 LEU 177 175 175 LEU LEU A . n 
A 1 178 PRO 178 176 176 PRO PRO A . n 
A 1 179 THR 179 177 177 THR THR A . n 
A 1 180 TRP 180 178 178 TRP TRP A . n 
A 1 181 GLU 181 179 179 GLU GLU A . n 
A 1 182 ASP 182 180 180 ASP ASP A . n 
A 1 183 ILE 183 181 181 ILE ILE A . n 
A 1 184 GLU 184 182 182 GLU GLU A . n 
A 1 185 SER 185 183 183 SER SER A . n 
A 1 186 LEU 186 184 184 LEU LEU A . n 
A 1 187 TYR 187 185 185 TYR TYR A . n 
A 1 188 GLY 188 186 ?   ?   ?   A . n 
A 1 189 GLU 189 187 ?   ?   ?   A . n 
A 1 190 GLN 190 188 ?   ?   ?   A . n 
A 1 191 PHE 191 189 ?   ?   ?   A . n 
A 1 192 HIS 192 190 ?   ?   ?   A . n 
A 1 193 HIS 193 191 ?   ?   ?   A . n 
A 1 194 HIS 194 192 ?   ?   ?   A . n 
A 1 195 HIS 195 193 ?   ?   ?   A . n 
A 1 196 HIS 196 194 ?   ?   ?   A . n 
A 1 197 HIS 197 195 ?   ?   ?   A . n 
B 1 1   MET 1   -1  ?   ?   ?   B . n 
B 1 2   GLY 2   0   ?   ?   ?   B . n 
B 1 3   MET 3   1   ?   ?   ?   B . n 
B 1 4   THR 4   2   ?   ?   ?   B . n 
B 1 5   ASN 5   3   ?   ?   ?   B . n 
B 1 6   LYS 6   4   ?   ?   ?   B . n 
B 1 7   ALA 7   5   ?   ?   ?   B . n 
B 1 8   SER 8   6   ?   ?   ?   B . n 
B 1 9   GLN 9   7   ?   ?   ?   B . n 
B 1 10  PRO 10  8   ?   ?   ?   B . n 
B 1 11  ARG 11  9   ?   ?   ?   B . n 
B 1 12  THR 12  10  ?   ?   ?   B . n 
B 1 13  PHE 13  11  ?   ?   ?   B . n 
B 1 14  THR 14  12  12  THR THR B . n 
B 1 15  LEU 15  13  13  LEU LEU B . n 
B 1 16  SER 16  14  14  SER SER B . n 
B 1 17  ASP 17  15  15  ASP ASP B . n 
B 1 18  GLU 18  16  16  GLU GLU B . n 
B 1 19  LYS 19  17  17  LYS LYS B . n 
B 1 20  ARG 20  18  18  ARG ARG B . n 
B 1 21  ASN 21  19  19  ASN ASN B . n 
B 1 22  HIS 22  20  20  HIS HIS B . n 
B 1 23  ILE 23  21  21  ILE ILE B . n 
B 1 24  LEU 24  22  22  LEU LEU B . n 
B 1 25  THR 25  23  23  THR THR B . n 
B 1 26  THR 26  24  24  THR THR B . n 
B 1 27  ALA 27  25  25  ALA ALA B . n 
B 1 28  LEU 28  26  26  LEU LEU B . n 
B 1 29  ASN 29  27  27  ASN ASN B . n 
B 1 30  LEU 30  28  28  LEU LEU B . n 
B 1 31  PHE 31  29  29  PHE PHE B . n 
B 1 32  ASP 32  30  30  ASP ASP B . n 
B 1 33  GLN 33  31  31  GLN GLN B . n 
B 1 34  PHE 34  32  32  PHE PHE B . n 
B 1 35  GLY 35  33  33  GLY GLY B . n 
B 1 36  PHE 36  34  34  PHE PHE B . n 
B 1 37  GLN 37  35  35  GLN GLN B . n 
B 1 38  HIS 38  36  36  HIS HIS B . n 
B 1 39  ILE 39  37  37  ILE ILE B . n 
B 1 40  SER 40  38  38  SER SER B . n 
B 1 41  ILE 41  39  39  ILE ILE B . n 
B 1 42  MET 42  40  40  MET MET B . n 
B 1 43  ARG 43  41  41  ARG ARG B . n 
B 1 44  ILE 44  42  42  ILE ILE B . n 
B 1 45  ILE 45  43  43  ILE ILE B . n 
B 1 46  THR 46  44  44  THR THR B . n 
B 1 47  GLU 47  45  45  GLU GLU B . n 
B 1 48  ALA 48  46  46  ALA ALA B . n 
B 1 49  LYS 49  47  47  LYS LYS B . n 
B 1 50  ILE 50  48  48  ILE ILE B . n 
B 1 51  ALA 51  49  49  ALA ALA B . n 
B 1 52  LYS 52  50  50  LYS LYS B . n 
B 1 53  GLN 53  51  51  GLN GLN B . n 
B 1 54  SER 54  52  52  SER SER B . n 
B 1 55  PHE 55  53  53  PHE PHE B . n 
B 1 56  TYR 56  54  54  TYR TYR B . n 
B 1 57  MET 57  55  55  MET MET B . n 
B 1 58  ALA 58  56  56  ALA ALA B . n 
B 1 59  PHE 59  57  57  PHE PHE B . n 
B 1 60  PRO 60  58  58  PRO PRO B . n 
B 1 61  SER 61  59  59  SER SER B . n 
B 1 62  LYS 62  60  60  LYS LYS B . n 
B 1 63  ASP 63  61  61  ASP ASP B . n 
B 1 64  SER 64  62  62  SER SER B . n 
B 1 65  PHE 65  63  63  PHE PHE B . n 
B 1 66  ILE 66  64  64  ILE ILE B . n 
B 1 67  ILE 67  65  65  ILE ILE B . n 
B 1 68  GLU 68  66  66  GLU GLU B . n 
B 1 69  CYS 69  67  67  CYS CYS B . n 
B 1 70  LEU 70  68  68  LEU LEU B . n 
B 1 71  ASP 71  69  69  ASP ASP B . n 
B 1 72  MET 72  70  70  MET MET B . n 
B 1 73  GLU 73  71  71  GLU GLU B . n 
B 1 74  ILE 74  72  72  ILE ILE B . n 
B 1 75  ASN 75  73  73  ASN ASN B . n 
B 1 76  ARG 76  74  74  ARG ARG B . n 
B 1 77  LEU 77  75  75  LEU LEU B . n 
B 1 78  LYS 78  76  76  LYS LYS B . n 
B 1 79  GLN 79  77  77  GLN GLN B . n 
B 1 80  SER 80  78  78  SER SER B . n 
B 1 81  LEU 81  79  79  LEU LEU B . n 
B 1 82  SER 82  80  80  SER SER B . n 
B 1 83  ASN 83  81  81  ASN ASN B . n 
B 1 84  LEU 84  82  82  LEU LEU B . n 
B 1 85  LEU 85  83  83  LEU LEU B . n 
B 1 86  GLY 86  84  84  GLY GLY B . n 
B 1 87  GLN 87  85  85  GLN GLN B . n 
B 1 88  CYS 88  86  86  CYS CYS B . n 
B 1 89  GLY 89  87  87  GLY GLY B . n 
B 1 90  LYS 90  88  88  LYS LYS B . n 
B 1 91  ASP 91  89  89  ASP ASP B . n 
B 1 92  ASP 92  90  90  ASP ASP B . n 
B 1 93  HIS 93  91  91  HIS HIS B . n 
B 1 94  THR 94  92  92  THR THR B . n 
B 1 95  SER 95  93  93  SER SER B . n 
B 1 96  ILE 96  94  94  ILE ILE B . n 
B 1 97  LEU 97  95  95  LEU LEU B . n 
B 1 98  LYS 98  96  96  LYS LYS B . n 
B 1 99  SER 99  97  97  SER SER B . n 
B 1 100 PHE 100 98  98  PHE PHE B . n 
B 1 101 TYR 101 99  99  TYR TYR B . n 
B 1 102 GLN 102 100 100 GLN GLN B . n 
B 1 103 TRP 103 101 101 TRP TRP B . n 
B 1 104 HIS 104 102 102 HIS HIS B . n 
B 1 105 VAL 105 103 103 VAL VAL B . n 
B 1 106 ASP 106 104 104 ASP ASP B . n 
B 1 107 LEU 107 105 105 LEU LEU B . n 
B 1 108 ALA 108 106 106 ALA ALA B . n 
B 1 109 TYR 109 107 107 TYR TYR B . n 
B 1 110 ARG 110 108 108 ARG ARG B . n 
B 1 111 GLU 111 109 ?   ?   ?   B . n 
B 1 112 GLY 112 110 110 GLY GLY B . n 
B 1 113 TYR 113 111 111 TYR TYR B . n 
B 1 114 ASN 114 112 112 ASN ASN B . n 
B 1 115 GLY 115 113 113 GLY GLY B . n 
B 1 116 THR 116 114 114 THR THR B . n 
B 1 117 LEU 117 115 115 LEU LEU B . n 
B 1 118 LEU 118 116 116 LEU LEU B . n 
B 1 119 THR 119 117 117 THR THR B . n 
B 1 120 LYS 120 118 118 LYS LYS B . n 
B 1 121 ALA 121 119 119 ALA ALA B . n 
B 1 122 VAL 122 120 120 VAL VAL B . n 
B 1 123 ILE 123 121 121 ILE ILE B . n 
B 1 124 GLU 124 122 122 GLU GLU B . n 
B 1 125 TYR 125 123 123 TYR TYR B . n 
B 1 126 TRP 126 124 124 TRP TRP B . n 
B 1 127 ASN 127 125 125 ASN ASN B . n 
B 1 128 LEU 128 126 126 LEU LEU B . n 
B 1 129 PRO 129 127 127 PRO PRO B . n 
B 1 130 ASP 130 128 128 ASP ASP B . n 
B 1 131 ILE 131 129 129 ILE ILE B . n 
B 1 132 LYS 132 130 130 LYS LYS B . n 
B 1 133 MET 133 131 131 MET MET B . n 
B 1 134 LYS 134 132 132 LYS LYS B . n 
B 1 135 VAL 135 133 133 VAL VAL B . n 
B 1 136 GLU 136 134 134 GLU GLU B . n 
B 1 137 ASP 137 135 135 ASP ASP B . n 
B 1 138 PHE 138 136 136 PHE PHE B . n 
B 1 139 ASN 139 137 137 ASN ASN B . n 
B 1 140 LYS 140 138 138 LYS LYS B . n 
B 1 141 TRP 141 139 139 TRP TRP B . n 
B 1 142 LYS 142 140 140 LYS LYS B . n 
B 1 143 TYR 143 141 141 TYR TYR B . n 
B 1 144 GLU 144 142 142 GLU GLU B . n 
B 1 145 ILE 145 143 143 ILE ILE B . n 
B 1 146 PHE 146 144 144 PHE PHE B . n 
B 1 147 ALA 147 145 145 ALA ALA B . n 
B 1 148 GLU 148 146 146 GLU GLU B . n 
B 1 149 TYR 149 147 147 TYR TYR B . n 
B 1 150 LEU 150 148 148 LEU LEU B . n 
B 1 151 ALA 151 149 149 ALA ALA B . n 
B 1 152 GLU 152 150 150 GLU GLU B . n 
B 1 153 GLU 153 151 151 GLU GLU B . n 
B 1 154 ILE 154 152 152 ILE ILE B . n 
B 1 155 ASN 155 153 153 ASN ASN B . n 
B 1 156 ASN 156 154 154 ASN ASN B . n 
B 1 157 ALA 157 155 155 ALA ALA B . n 
B 1 158 ARG 158 156 156 ARG ARG B . n 
B 1 159 LEU 159 157 157 LEU LEU B . n 
B 1 160 ARG 160 158 158 ARG ARG B . n 
B 1 161 ILE 161 159 159 ILE ILE B . n 
B 1 162 ILE 162 160 160 ILE ILE B . n 
B 1 163 VAL 163 161 161 VAL VAL B . n 
B 1 164 SER 164 162 162 SER SER B . n 
B 1 165 ALA 165 163 163 ALA ALA B . n 
B 1 166 MET 166 164 164 MET MET B . n 
B 1 167 ASN 167 165 165 ASN ASN B . n 
B 1 168 GLY 168 166 166 GLY GLY B . n 
B 1 169 ILE 169 167 167 ILE ILE B . n 
B 1 170 LEU 170 168 168 LEU LEU B . n 
B 1 171 LEU 171 169 169 LEU LEU B . n 
B 1 172 PRO 172 170 170 PRO PRO B . n 
B 1 173 ALA 173 171 171 ALA ALA B . n 
B 1 174 SER 174 172 172 SER SER B . n 
B 1 175 THR 175 173 173 THR THR B . n 
B 1 176 TYR 176 174 174 TYR TYR B . n 
B 1 177 LEU 177 175 175 LEU LEU B . n 
B 1 178 PRO 178 176 176 PRO PRO B . n 
B 1 179 THR 179 177 177 THR THR B . n 
B 1 180 TRP 180 178 178 TRP TRP B . n 
B 1 181 GLU 181 179 179 GLU GLU B . n 
B 1 182 ASP 182 180 180 ASP ASP B . n 
B 1 183 ILE 183 181 181 ILE ILE B . n 
B 1 184 GLU 184 182 182 GLU GLU B . n 
B 1 185 SER 185 183 183 SER SER B . n 
B 1 186 LEU 186 184 184 LEU LEU B . n 
B 1 187 TYR 187 185 185 TYR TYR B . n 
B 1 188 GLY 188 186 186 GLY GLY B . n 
B 1 189 GLU 189 187 187 GLU GLU B . n 
B 1 190 GLN 190 188 188 GLN GLN B . n 
B 1 191 PHE 191 189 189 PHE PHE B . n 
B 1 192 HIS 192 190 190 HIS HIS B . n 
B 1 193 HIS 193 191 191 HIS HIS B . n 
B 1 194 HIS 194 192 192 HIS HIS B . n 
B 1 195 HIS 195 193 193 HIS HIS B . n 
B 1 196 HIS 196 194 194 HIS HIS B . n 
B 1 197 HIS 197 195 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1  201 36  HOH HOH A . 
C 2 HOH 2  202 106 HOH HOH A . 
C 2 HOH 3  203 32  HOH HOH A . 
C 2 HOH 4  204 126 HOH HOH A . 
C 2 HOH 5  205 43  HOH HOH A . 
C 2 HOH 6  206 155 HOH HOH A . 
C 2 HOH 7  207 147 HOH HOH A . 
C 2 HOH 8  208 23  HOH HOH A . 
C 2 HOH 9  209 62  HOH HOH A . 
C 2 HOH 10 210 122 HOH HOH A . 
C 2 HOH 11 211 130 HOH HOH A . 
C 2 HOH 12 212 164 HOH HOH A . 
C 2 HOH 13 213 171 HOH HOH A . 
C 2 HOH 14 214 16  HOH HOH A . 
C 2 HOH 15 215 40  HOH HOH A . 
C 2 HOH 16 216 83  HOH HOH A . 
C 2 HOH 17 217 128 HOH HOH A . 
C 2 HOH 18 218 4   HOH HOH A . 
C 2 HOH 19 219 17  HOH HOH A . 
C 2 HOH 20 220 34  HOH HOH A . 
C 2 HOH 21 221 76  HOH HOH A . 
C 2 HOH 22 222 1   HOH HOH A . 
C 2 HOH 23 223 103 HOH HOH A . 
C 2 HOH 24 224 160 HOH HOH A . 
C 2 HOH 25 225 168 HOH HOH A . 
C 2 HOH 26 226 157 HOH HOH A . 
C 2 HOH 27 227 151 HOH HOH A . 
C 2 HOH 28 228 37  HOH HOH A . 
C 2 HOH 29 229 20  HOH HOH A . 
C 2 HOH 30 230 82  HOH HOH A . 
C 2 HOH 31 231 158 HOH HOH A . 
C 2 HOH 32 232 137 HOH HOH A . 
C 2 HOH 33 233 27  HOH HOH A . 
C 2 HOH 34 234 2   HOH HOH A . 
C 2 HOH 35 235 68  HOH HOH A . 
C 2 HOH 36 236 124 HOH HOH A . 
C 2 HOH 37 237 30  HOH HOH A . 
C 2 HOH 38 238 6   HOH HOH A . 
C 2 HOH 39 239 129 HOH HOH A . 
C 2 HOH 40 240 10  HOH HOH A . 
C 2 HOH 41 241 101 HOH HOH A . 
C 2 HOH 42 242 73  HOH HOH A . 
C 2 HOH 43 243 29  HOH HOH A . 
C 2 HOH 44 244 109 HOH HOH A . 
C 2 HOH 45 245 3   HOH HOH A . 
C 2 HOH 46 246 61  HOH HOH A . 
C 2 HOH 47 247 148 HOH HOH A . 
C 2 HOH 48 248 35  HOH HOH A . 
C 2 HOH 49 249 60  HOH HOH A . 
C 2 HOH 50 250 86  HOH HOH A . 
C 2 HOH 51 251 44  HOH HOH A . 
C 2 HOH 52 252 143 HOH HOH A . 
C 2 HOH 53 253 72  HOH HOH A . 
C 2 HOH 54 254 91  HOH HOH A . 
C 2 HOH 55 255 69  HOH HOH A . 
C 2 HOH 56 256 24  HOH HOH A . 
C 2 HOH 57 257 50  HOH HOH A . 
C 2 HOH 58 258 110 HOH HOH A . 
C 2 HOH 59 259 31  HOH HOH A . 
C 2 HOH 60 260 112 HOH HOH A . 
C 2 HOH 61 261 45  HOH HOH A . 
C 2 HOH 62 262 49  HOH HOH A . 
C 2 HOH 63 263 107 HOH HOH A . 
C 2 HOH 64 264 115 HOH HOH A . 
C 2 HOH 65 265 38  HOH HOH A . 
C 2 HOH 66 266 117 HOH HOH A . 
C 2 HOH 67 267 167 HOH HOH A . 
C 2 HOH 68 268 18  HOH HOH A . 
C 2 HOH 69 269 51  HOH HOH A . 
C 2 HOH 70 270 133 HOH HOH A . 
C 2 HOH 71 271 173 HOH HOH A . 
C 2 HOH 72 272 90  HOH HOH A . 
C 2 HOH 73 273 146 HOH HOH A . 
C 2 HOH 74 274 105 HOH HOH A . 
C 2 HOH 75 275 152 HOH HOH A . 
C 2 HOH 76 276 96  HOH HOH A . 
C 2 HOH 77 277 132 HOH HOH A . 
C 2 HOH 78 278 118 HOH HOH A . 
C 2 HOH 79 279 113 HOH HOH A . 
C 2 HOH 80 280 142 HOH HOH A . 
C 2 HOH 81 281 116 HOH HOH A . 
C 2 HOH 82 282 121 HOH HOH A . 
C 2 HOH 83 283 172 HOH HOH A . 
C 2 HOH 84 284 134 HOH HOH A . 
C 2 HOH 85 285 150 HOH HOH A . 
D 2 HOH 1  201 87  HOH HOH B . 
D 2 HOH 2  202 67  HOH HOH B . 
D 2 HOH 3  203 53  HOH HOH B . 
D 2 HOH 4  204 81  HOH HOH B . 
D 2 HOH 5  205 46  HOH HOH B . 
D 2 HOH 6  206 104 HOH HOH B . 
D 2 HOH 7  207 25  HOH HOH B . 
D 2 HOH 8  208 139 HOH HOH B . 
D 2 HOH 9  209 131 HOH HOH B . 
D 2 HOH 10 210 63  HOH HOH B . 
D 2 HOH 11 211 54  HOH HOH B . 
D 2 HOH 12 212 95  HOH HOH B . 
D 2 HOH 13 213 12  HOH HOH B . 
D 2 HOH 14 214 21  HOH HOH B . 
D 2 HOH 15 215 7   HOH HOH B . 
D 2 HOH 16 216 11  HOH HOH B . 
D 2 HOH 17 217 58  HOH HOH B . 
D 2 HOH 18 218 33  HOH HOH B . 
D 2 HOH 19 219 13  HOH HOH B . 
D 2 HOH 20 220 22  HOH HOH B . 
D 2 HOH 21 221 102 HOH HOH B . 
D 2 HOH 22 222 26  HOH HOH B . 
D 2 HOH 23 223 92  HOH HOH B . 
D 2 HOH 24 224 65  HOH HOH B . 
D 2 HOH 25 225 19  HOH HOH B . 
D 2 HOH 26 226 15  HOH HOH B . 
D 2 HOH 27 227 89  HOH HOH B . 
D 2 HOH 28 228 5   HOH HOH B . 
D 2 HOH 29 229 70  HOH HOH B . 
D 2 HOH 30 230 125 HOH HOH B . 
D 2 HOH 31 231 55  HOH HOH B . 
D 2 HOH 32 232 52  HOH HOH B . 
D 2 HOH 33 233 97  HOH HOH B . 
D 2 HOH 34 234 88  HOH HOH B . 
D 2 HOH 35 235 74  HOH HOH B . 
D 2 HOH 36 236 100 HOH HOH B . 
D 2 HOH 37 237 111 HOH HOH B . 
D 2 HOH 38 238 120 HOH HOH B . 
D 2 HOH 39 239 42  HOH HOH B . 
D 2 HOH 40 240 127 HOH HOH B . 
D 2 HOH 41 241 64  HOH HOH B . 
D 2 HOH 42 242 136 HOH HOH B . 
D 2 HOH 43 243 138 HOH HOH B . 
D 2 HOH 44 244 149 HOH HOH B . 
D 2 HOH 45 245 141 HOH HOH B . 
D 2 HOH 46 246 57  HOH HOH B . 
D 2 HOH 47 247 14  HOH HOH B . 
D 2 HOH 48 248 71  HOH HOH B . 
D 2 HOH 49 249 93  HOH HOH B . 
D 2 HOH 50 250 154 HOH HOH B . 
D 2 HOH 51 251 9   HOH HOH B . 
D 2 HOH 52 252 48  HOH HOH B . 
D 2 HOH 53 253 85  HOH HOH B . 
D 2 HOH 54 254 56  HOH HOH B . 
D 2 HOH 55 255 59  HOH HOH B . 
D 2 HOH 56 256 39  HOH HOH B . 
D 2 HOH 57 257 47  HOH HOH B . 
D 2 HOH 58 258 28  HOH HOH B . 
D 2 HOH 59 259 135 HOH HOH B . 
D 2 HOH 60 260 108 HOH HOH B . 
D 2 HOH 61 261 98  HOH HOH B . 
D 2 HOH 62 262 8   HOH HOH B . 
D 2 HOH 63 263 94  HOH HOH B . 
D 2 HOH 64 264 41  HOH HOH B . 
D 2 HOH 65 265 170 HOH HOH B . 
D 2 HOH 66 266 79  HOH HOH B . 
D 2 HOH 67 267 162 HOH HOH B . 
D 2 HOH 68 268 156 HOH HOH B . 
D 2 HOH 69 269 66  HOH HOH B . 
D 2 HOH 70 270 123 HOH HOH B . 
D 2 HOH 71 271 153 HOH HOH B . 
D 2 HOH 72 272 80  HOH HOH B . 
D 2 HOH 73 273 84  HOH HOH B . 
D 2 HOH 74 274 119 HOH HOH B . 
D 2 HOH 75 275 78  HOH HOH B . 
D 2 HOH 76 276 114 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 A LYS 88  ? CG  ? A LYS 90  CG  
2  1 Y 1 A LYS 88  ? CD  ? A LYS 90  CD  
3  1 Y 1 A LYS 88  ? CE  ? A LYS 90  CE  
4  1 Y 1 A LYS 88  ? NZ  ? A LYS 90  NZ  
5  1 Y 1 A ASP 89  ? CG  ? A ASP 91  CG  
6  1 Y 1 A ASP 89  ? OD1 ? A ASP 91  OD1 
7  1 Y 1 A ASP 89  ? OD2 ? A ASP 91  OD2 
8  1 Y 1 A LYS 96  ? CE  ? A LYS 98  CE  
9  1 Y 1 A LYS 96  ? NZ  ? A LYS 98  NZ  
10 1 Y 1 A TYR 107 ? CG  ? A TYR 109 CG  
11 1 Y 1 A TYR 107 ? CD1 ? A TYR 109 CD1 
12 1 Y 1 A TYR 107 ? CD2 ? A TYR 109 CD2 
13 1 Y 1 A TYR 107 ? CE1 ? A TYR 109 CE1 
14 1 Y 1 A TYR 107 ? CE2 ? A TYR 109 CE2 
15 1 Y 1 A TYR 107 ? CZ  ? A TYR 109 CZ  
16 1 Y 1 A TYR 107 ? OH  ? A TYR 109 OH  
17 1 Y 1 A GLU 109 ? CG  ? A GLU 111 CG  
18 1 Y 1 A GLU 109 ? CD  ? A GLU 111 CD  
19 1 Y 1 A GLU 109 ? OE1 ? A GLU 111 OE1 
20 1 Y 1 A GLU 109 ? OE2 ? A GLU 111 OE2 
21 1 Y 1 A GLU 122 ? CG  ? A GLU 124 CG  
22 1 Y 1 A GLU 122 ? CD  ? A GLU 124 CD  
23 1 Y 1 A GLU 122 ? OE1 ? A GLU 124 OE1 
24 1 Y 1 A GLU 122 ? OE2 ? A GLU 124 OE2 
25 1 Y 1 A ASP 128 ? CG  ? A ASP 130 CG  
26 1 Y 1 A ASP 128 ? OD1 ? A ASP 130 OD1 
27 1 Y 1 A ASP 128 ? OD2 ? A ASP 130 OD2 
28 1 Y 1 A LYS 138 ? CD  ? A LYS 140 CD  
29 1 Y 1 A LYS 138 ? CE  ? A LYS 140 CE  
30 1 Y 1 A LYS 138 ? NZ  ? A LYS 140 NZ  
31 1 Y 1 A GLU 150 ? CG  ? A GLU 152 CG  
32 1 Y 1 A GLU 150 ? CD  ? A GLU 152 CD  
33 1 Y 1 A GLU 150 ? OE1 ? A GLU 152 OE1 
34 1 Y 1 A GLU 150 ? OE2 ? A GLU 152 OE2 
35 1 Y 1 A GLU 151 ? CG  ? A GLU 153 CG  
36 1 Y 1 A GLU 151 ? CD  ? A GLU 153 CD  
37 1 Y 1 A GLU 151 ? OE1 ? A GLU 153 OE1 
38 1 Y 1 A GLU 151 ? OE2 ? A GLU 153 OE2 
39 1 Y 1 A GLU 179 ? CG  ? A GLU 181 CG  
40 1 Y 1 A GLU 179 ? CD  ? A GLU 181 CD  
41 1 Y 1 A GLU 179 ? OE1 ? A GLU 181 OE1 
42 1 Y 1 A GLU 179 ? OE2 ? A GLU 181 OE2 
43 1 Y 1 B LYS 88  ? CG  ? B LYS 90  CG  
44 1 Y 1 B LYS 88  ? CD  ? B LYS 90  CD  
45 1 Y 1 B LYS 88  ? CE  ? B LYS 90  CE  
46 1 Y 1 B LYS 88  ? NZ  ? B LYS 90  NZ  
47 1 Y 1 B SER 93  ? OG  ? B SER 95  OG  
48 1 Y 1 B TYR 107 ? CD1 ? B TYR 109 CD1 
49 1 Y 1 B TYR 107 ? CD2 ? B TYR 109 CD2 
50 1 Y 1 B TYR 107 ? CE1 ? B TYR 109 CE1 
51 1 Y 1 B TYR 107 ? CE2 ? B TYR 109 CE2 
52 1 Y 1 B TYR 107 ? CZ  ? B TYR 109 CZ  
53 1 Y 1 B TYR 107 ? OH  ? B TYR 109 OH  
54 1 Y 1 B ARG 108 ? CG  ? B ARG 110 CG  
55 1 Y 1 B ARG 108 ? CD  ? B ARG 110 CD  
56 1 Y 1 B ARG 108 ? NE  ? B ARG 110 NE  
57 1 Y 1 B ARG 108 ? CZ  ? B ARG 110 CZ  
58 1 Y 1 B ARG 108 ? NH1 ? B ARG 110 NH1 
59 1 Y 1 B ARG 108 ? NH2 ? B ARG 110 NH2 
60 1 Y 1 B GLU 122 ? CG  ? B GLU 124 CG  
61 1 Y 1 B GLU 122 ? CD  ? B GLU 124 CD  
62 1 Y 1 B GLU 122 ? OE1 ? B GLU 124 OE1 
63 1 Y 1 B GLU 122 ? OE2 ? B GLU 124 OE2 
64 1 Y 1 B ASP 128 ? CG  ? B ASP 130 CG  
65 1 Y 1 B ASP 128 ? OD1 ? B ASP 130 OD1 
66 1 Y 1 B ASP 128 ? OD2 ? B ASP 130 OD2 
67 1 Y 1 B GLU 187 ? CG  ? B GLU 189 CG  
68 1 Y 1 B GLU 187 ? CD  ? B GLU 189 CD  
69 1 Y 1 B GLU 187 ? OE1 ? B GLU 189 OE1 
70 1 Y 1 B GLU 187 ? OE2 ? B GLU 189 OE2 
71 1 Y 1 B PHE 189 ? CG  ? B PHE 191 CG  
72 1 Y 1 B PHE 189 ? CD1 ? B PHE 191 CD1 
73 1 Y 1 B PHE 189 ? CD2 ? B PHE 191 CD2 
74 1 Y 1 B PHE 189 ? CE1 ? B PHE 191 CE1 
75 1 Y 1 B PHE 189 ? CE2 ? B PHE 191 CE2 
76 1 Y 1 B PHE 189 ? CZ  ? B PHE 191 CZ  
77 1 Y 1 B HIS 194 ? CG  ? B HIS 196 CG  
78 1 Y 1 B HIS 194 ? ND1 ? B HIS 196 ND1 
79 1 Y 1 B HIS 194 ? CD2 ? B HIS 196 CD2 
80 1 Y 1 B HIS 194 ? CE1 ? B HIS 196 CE1 
81 1 Y 1 B HIS 194 ? NE2 ? B HIS 196 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.570 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z6E 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.999 
_cell.length_a_esd                 ? 
_cell.length_b                     47.760 
_cell.length_b_esd                 ? 
_cell.length_c                     80.451 
_cell.length_c_esd                 ? 
_cell.volume                       186168.676 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8Z6E 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Z6E 
_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             2.01 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.92 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'Potassium citrate tribasic monohydrate, PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-03-27 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.98 
_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 BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          32.17 
_reflns.entry_id                                       8Z6E 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.97 
_reflns.d_resolution_low                               34.01 
_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                                     25972 
_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                           98.24 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.36 
_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                                0.087 
_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                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.078 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.97 
_reflns_shell.d_res_low                                     2.04 
_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                             2597 
_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                                  0.792 
_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                               37.46 
_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                                 8Z6E 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.97 
_refine.ls_d_res_low                             34.01 
_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                     25731 
_refine.ls_number_reflns_R_free                  2019 
_refine.ls_number_reflns_R_work                  23712 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.26 
_refine.ls_percent_reflns_R_free                 7.85 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2043 
_refine.ls_R_factor_R_free                       0.2518 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2003 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      AlphaFold 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 26.8536 
_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                            0.2231 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.97 
_refine_hist.d_res_low                        34.01 
_refine_hist.number_atoms_solvent             161 
_refine_hist.number_atoms_total               3015 
_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        2854 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0082 ? 2921 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9760 ? 3957 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0549 ? 443  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0068 ? 494  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 5.4166 ? 379  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.97 2.02  . . 101 1755 99.84 . . . . 0.2845 . . . . . . . . . . . 0.3381 
'X-RAY DIFFRACTION' 2.02 2.08  . . 202 1658 99.89 . . . . 0.2508 . . . . . . . . . . . 0.2894 
'X-RAY DIFFRACTION' 2.08 2.14  . . 101 1761 99.84 . . . . 0.2406 . . . . . . . . . . . 0.2795 
'X-RAY DIFFRACTION' 2.14 2.21  . . 202 1614 99.89 . . . . 0.2238 . . . . . . . . . . . 0.2955 
'X-RAY DIFFRACTION' 2.21 2.29  . . 101 1508 86.23 . . . . 0.3728 . . . . . . . . . . . 0.5244 
'X-RAY DIFFRACTION' 2.29 2.38  . . 134 1725 99.84 . . . . 0.2386 . . . . . . . . . . . 0.2979 
'X-RAY DIFFRACTION' 2.38 2.49  . . 169 1679 99.95 . . . . 0.2253 . . . . . . . . . . . 0.2782 
'X-RAY DIFFRACTION' 2.49 2.62  . . 101 1765 99.95 . . . . 0.2222 . . . . . . . . . . . 0.2956 
'X-RAY DIFFRACTION' 2.62 2.78  . . 201 1663 99.73 . . . . 0.2169 . . . . . . . . . . . 0.2606 
'X-RAY DIFFRACTION' 2.78 2.99  . . 101 1772 99.84 . . . . 0.2112 . . . . . . . . . . . 0.2423 
'X-RAY DIFFRACTION' 2.99 3.30  . . 202 1665 99.57 . . . . 0.2040 . . . . . . . . . . . 0.2581 
'X-RAY DIFFRACTION' 3.30 3.77  . . 101 1639 92.65 . . . . 0.1747 . . . . . . . . . . . 0.2315 
'X-RAY DIFFRACTION' 3.77 4.75  . . 150 1734 99.58 . . . . 0.1586 . . . . . . . . . . . 0.2075 
'X-RAY DIFFRACTION' 4.75 34.01 . . 153 1774 98.87 . . . . 0.1696 . . . . . . . . . . . 0.1908 
# 
_struct.entry_id                     8Z6E 
_struct.title                        'Structure of transcriptional regulator TetR' 
_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        8Z6E 
_struct_keywords.text            'Transcriptional regulator, TetR, DNA binding protein' 
_struct_keywords.pdbx_keywords   'DNA 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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1E3M4M0_ACIBA 
_struct_ref.pdbx_db_accession          A0A1E3M4M0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTNKASQPRTFTLSDEKRNHILTTALNLFDQFGFQHISIMRIITEAKIAKQSFYMAFPSKDSFIIECLDMEINRLKQSLS
NLLGQCGKDDHTSILKSFYQWHVDLAYREGYNGTLLTKAVIEYWNLPDIKMKVEDFNKWKYEIFAEYLAEEINNARLRII
VSAMNGILLPASTYLPTWEDIESLYGEQF
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8Z6E A 3 ? 191 ? A0A1E3M4M0 1 ? 189 ? 1 189 
2 1 8Z6E B 3 ? 191 ? A0A1E3M4M0 1 ? 189 ? 1 189 
# 
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 8Z6E MET A 1   ? UNP A0A1E3M4M0 ? ? 'initiating methionine' -1  1  
1 8Z6E GLY A 2   ? UNP A0A1E3M4M0 ? ? 'expression tag'        0   2  
1 8Z6E HIS A 192 ? UNP A0A1E3M4M0 ? ? 'expression tag'        190 3  
1 8Z6E HIS A 193 ? UNP A0A1E3M4M0 ? ? 'expression tag'        191 4  
1 8Z6E HIS A 194 ? UNP A0A1E3M4M0 ? ? 'expression tag'        192 5  
1 8Z6E HIS A 195 ? UNP A0A1E3M4M0 ? ? 'expression tag'        193 6  
1 8Z6E HIS A 196 ? UNP A0A1E3M4M0 ? ? 'expression tag'        194 7  
1 8Z6E HIS A 197 ? UNP A0A1E3M4M0 ? ? 'expression tag'        195 8  
2 8Z6E MET B 1   ? UNP A0A1E3M4M0 ? ? 'initiating methionine' -1  9  
2 8Z6E GLY B 2   ? UNP A0A1E3M4M0 ? ? 'expression tag'        0   10 
2 8Z6E HIS B 192 ? UNP A0A1E3M4M0 ? ? 'expression tag'        190 11 
2 8Z6E HIS B 193 ? UNP A0A1E3M4M0 ? ? 'expression tag'        191 12 
2 8Z6E HIS B 194 ? UNP A0A1E3M4M0 ? ? 'expression tag'        192 13 
2 8Z6E HIS B 195 ? UNP A0A1E3M4M0 ? ? 'expression tag'        193 14 
2 8Z6E HIS B 196 ? UNP A0A1E3M4M0 ? ? 'expression tag'        194 15 
2 8Z6E HIS B 197 ? UNP A0A1E3M4M0 ? ? 'expression tag'        195 16 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 3650  ? 
1 MORE         -32   ? 
1 'SSA (A^2)'  16510 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_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 SER A 16  ? GLY A 35  ? SER A 14  GLY A 33  1 ? 20 
HELX_P HELX_P2  AA2 SER A 40  ? LYS A 49  ? SER A 38  LYS A 47  1 ? 10 
HELX_P HELX_P3  AA3 ALA A 51  ? PHE A 59  ? ALA A 49  PHE A 57  1 ? 9  
HELX_P HELX_P4  AA4 SER A 61  ? GLY A 86  ? SER A 59  GLY A 84  1 ? 26 
HELX_P HELX_P5  AA5 ASP A 92  ? TYR A 109 ? ASP A 90  TYR A 107 1 ? 18 
HELX_P HELX_P6  AA6 THR A 116 ? TYR A 125 ? THR A 114 TYR A 123 1 ? 10 
HELX_P HELX_P7  AA7 LEU A 128 ? ALA A 151 ? LEU A 126 ALA A 149 1 ? 24 
HELX_P HELX_P8  AA8 ASN A 155 ? LEU A 171 ? ASN A 153 LEU A 169 1 ? 17 
HELX_P HELX_P9  AA9 THR A 179 ? TYR A 187 ? THR A 177 TYR A 185 1 ? 9  
HELX_P HELX_P10 AB1 SER B 16  ? GLY B 35  ? SER B 14  GLY B 33  1 ? 20 
HELX_P HELX_P11 AB2 SER B 40  ? LYS B 49  ? SER B 38  LYS B 47  1 ? 10 
HELX_P HELX_P12 AB3 ALA B 51  ? PHE B 59  ? ALA B 49  PHE B 57  1 ? 9  
HELX_P HELX_P13 AB4 SER B 61  ? CYS B 88  ? SER B 59  CYS B 86  1 ? 28 
HELX_P HELX_P14 AB5 ASP B 92  ? ARG B 110 ? ASP B 90  ARG B 108 1 ? 19 
HELX_P HELX_P15 AB6 THR B 116 ? TYR B 125 ? THR B 114 TYR B 123 1 ? 10 
HELX_P HELX_P16 AB7 LEU B 128 ? ALA B 151 ? LEU B 126 ALA B 149 1 ? 24 
HELX_P HELX_P17 AB8 ASN B 155 ? LEU B 170 ? ASN B 153 LEU B 168 1 ? 16 
HELX_P HELX_P18 AB9 THR B 179 ? GLU B 189 ? THR B 177 GLU B 187 1 ? 11 
HELX_P HELX_P19 AC1 GLN B 190 ? HIS B 195 ? GLN B 188 HIS B 193 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   8Z6E 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OG 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    SER 
_pdbx_validate_symm_contact.auth_seq_id_1     62 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OD2 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    ASP 
_pdbx_validate_symm_contact.auth_seq_id_2     61 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_556 
_pdbx_validate_symm_contact.dist              2.15 
# 
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 TYR A 107 ? ? -97.17  57.24 
2 1 ASN A 112 ? ? -143.30 32.71 
3 1 TYR A 123 ? ? -111.44 57.69 
4 1 TYR B 123 ? ? -116.38 55.13 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -2.73941012783 
_pdbx_refine_tls.origin_y         -1.21126550777 
_pdbx_refine_tls.origin_z         22.1324814637 
_pdbx_refine_tls.T[1][1]          0.158719946418 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0200374425934 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.011480052925 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.152528195716 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.00606670674972 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.189913789628 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.87017369207 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0790074150847 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.126874448325 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.729560803301 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.262558130524 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.28934811335 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.00335762036708 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.110497306453 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0552873721139 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.00934866695086 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0280753402859 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0130701012423 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.037864320005 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.02494641641 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0179275829211 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     13 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   C 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    S 
_pdbx_refine_tls_group.end_auth_seq_id     173 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
_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                       285 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.14 
_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 MET -1  ? A MET 1   
2  1 Y 1 A GLY 0   ? A GLY 2   
3  1 Y 1 A MET 1   ? A MET 3   
4  1 Y 1 A THR 2   ? A THR 4   
5  1 Y 1 A ASN 3   ? A ASN 5   
6  1 Y 1 A LYS 4   ? A LYS 6   
7  1 Y 1 A ALA 5   ? A ALA 7   
8  1 Y 1 A SER 6   ? A SER 8   
9  1 Y 1 A GLN 7   ? A GLN 9   
10 1 Y 1 A PRO 8   ? A PRO 10  
11 1 Y 1 A ARG 9   ? A ARG 11  
12 1 Y 1 A THR 10  ? A THR 12  
13 1 Y 1 A PHE 11  ? A PHE 13  
14 1 Y 1 A THR 12  ? A THR 14  
15 1 Y 1 A GLY 186 ? A GLY 188 
16 1 Y 1 A GLU 187 ? A GLU 189 
17 1 Y 1 A GLN 188 ? A GLN 190 
18 1 Y 1 A PHE 189 ? A PHE 191 
19 1 Y 1 A HIS 190 ? A HIS 192 
20 1 Y 1 A HIS 191 ? A HIS 193 
21 1 Y 1 A HIS 192 ? A HIS 194 
22 1 Y 1 A HIS 193 ? A HIS 195 
23 1 Y 1 A HIS 194 ? A HIS 196 
24 1 Y 1 A HIS 195 ? A HIS 197 
25 1 Y 1 B MET -1  ? B MET 1   
26 1 Y 1 B GLY 0   ? B GLY 2   
27 1 Y 1 B MET 1   ? B MET 3   
28 1 Y 1 B THR 2   ? B THR 4   
29 1 Y 1 B ASN 3   ? B ASN 5   
30 1 Y 1 B LYS 4   ? B LYS 6   
31 1 Y 1 B ALA 5   ? B ALA 7   
32 1 Y 1 B SER 6   ? B SER 8   
33 1 Y 1 B GLN 7   ? B GLN 9   
34 1 Y 1 B PRO 8   ? B PRO 10  
35 1 Y 1 B ARG 9   ? B ARG 11  
36 1 Y 1 B THR 10  ? B THR 12  
37 1 Y 1 B PHE 11  ? B PHE 13  
38 1 Y 1 B GLU 109 ? B GLU 111 
39 1 Y 1 B HIS 195 ? B HIS 197 
# 
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 
# 
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           No.82072237 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Z6E 
_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]   0.020409 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003076 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020938 
_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]   0.012570 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . LEU A 1 15  ? 15.76612  -0.69471  53.55477  1.000 70.57393 ?  13  LEU A N   1 
ATOM   2    C CA  . LEU A 1 15  ? 15.63558  -1.47214  52.32630  1.000 63.08402 ?  13  LEU A CA  1 
ATOM   3    C C   . LEU A 1 15  ? 16.87544  -1.34001  51.44108  1.000 66.34872 ?  13  LEU A C   1 
ATOM   4    O O   . LEU A 1 15  ? 17.22243  -0.23863  51.00259  1.000 69.16147 ?  13  LEU A O   1 
ATOM   5    C CB  . LEU A 1 15  ? 14.38611  -1.04418  51.54444  1.000 63.17531 ?  13  LEU A CB  1 
ATOM   6    C CG  . LEU A 1 15  ? 14.06201  -1.85006  50.28057  1.000 59.31525 ?  13  LEU A CG  1 
ATOM   7    C CD1 . LEU A 1 15  ? 13.40936  -3.17287  50.65692  1.000 59.67474 ?  13  LEU A CD1 1 
ATOM   8    C CD2 . LEU A 1 15  ? 13.14806  -1.07764  49.32888  1.000 53.57133 ?  13  LEU A CD2 1 
ATOM   9    N N   . SER A 1 16  ? 17.52990  -2.47326  51.17437  1.000 66.07718 ?  14  SER A N   1 
ATOM   10   C CA  . SER A 1 16  ? 18.69666  -2.48930  50.29855  1.000 61.95025 ?  14  SER A CA  1 
ATOM   11   C C   . SER A 1 16  ? 18.32748  -2.01861  48.90532  1.000 63.86087 ?  14  SER A C   1 
ATOM   12   O O   . SER A 1 16  ? 17.29019  -2.40365  48.35827  1.000 61.24494 ?  14  SER A O   1 
ATOM   13   C CB  . SER A 1 16  ? 19.28392  -3.89984  50.20856  1.000 61.99219 ?  14  SER A CB  1 
ATOM   14   O OG  . SER A 1 16  ? 18.57123  -4.81392  51.02522  1.000 61.07733 ?  14  SER A OG  1 
ATOM   15   N N   . ASP A 1 17  ? 19.19388  -1.19756  48.31079  1.000 60.98387 ?  15  ASP A N   1 
ATOM   16   C CA  . ASP A 1 17  ? 18.99878  -0.89461  46.90158  1.000 60.90706 ?  15  ASP A CA  1 
ATOM   17   C C   . ASP A 1 17  ? 18.95632  -2.17109  46.06921  1.000 64.06125 ?  15  ASP A C   1 
ATOM   18   O O   . ASP A 1 17  ? 18.21582  -2.24559  45.07975  1.000 61.22718 ?  15  ASP A O   1 
ATOM   19   C CB  . ASP A 1 17  ? 20.09832  0.03525   46.39014  1.000 59.81369 ?  15  ASP A CB  1 
ATOM   20   C CG  . ASP A 1 17  ? 19.82970  0.52106   44.97551  1.000 62.23783 ?  15  ASP A CG  1 
ATOM   21   O OD1 . ASP A 1 17  ? 19.03746  1.47652   44.79705  1.000 65.00554 ?  15  ASP A OD1 1 
ATOM   22   O OD2 . ASP A 1 17  ? 20.37634  -0.09181  44.03419  1.000 59.77118 -1 15  ASP A OD2 1 
ATOM   23   N N   . GLU A 1 18  ? 19.73689  -3.18560  46.45693  1.000 64.84699 ?  16  GLU A N   1 
ATOM   24   C CA  . GLU A 1 18  ? 19.70787  -4.46316  45.74968  1.000 63.07872 ?  16  GLU A CA  1 
ATOM   25   C C   . GLU A 1 18  ? 18.37848  -5.16692  45.95261  1.000 57.89427 ?  16  GLU A C   1 
ATOM   26   O O   . GLU A 1 18  ? 17.80213  -5.71101  45.00284  1.000 57.71701 ?  16  GLU A O   1 
ATOM   27   C CB  . GLU A 1 18  ? 20.84540  -5.37249  46.21662  1.000 64.45492 ?  16  GLU A CB  1 
ATOM   28   C CG  . GLU A 1 18  ? 20.99470  -6.63131  45.35203  1.000 68.06562 ?  16  GLU A CG  1 
ATOM   29   C CD  . GLU A 1 18  ? 22.14779  -7.52589  45.79037  1.000 70.74487 ?  16  GLU A CD  1 
ATOM   30   O OE1 . GLU A 1 18  ? 23.30079  -7.26861  45.36108  1.000 68.68891 ?  16  GLU A OE1 1 
ATOM   31   O OE2 . GLU A 1 18  ? 21.89553  -8.48353  46.56252  1.000 66.92498 ?  16  GLU A OE2 1 
ATOM   32   N N   . LYS A 1 19  ? 17.88515  -5.18936  47.19189  1.000 58.86266 ?  17  LYS A N   1 
ATOM   33   C CA  . LYS A 1 19  ? 16.57370  -5.76957  47.41013  1.000 58.51442 ?  17  LYS A CA  1 
ATOM   34   C C   . LYS A 1 19  ? 15.50263  -4.96324  46.69665  1.000 53.82329 ?  17  LYS A C   1 
ATOM   35   O O   . LYS A 1 19  ? 14.47138  -5.51643  46.30843  1.000 49.13085 ?  17  LYS A O   1 
ATOM   36   C CB  . LYS A 1 19  ? 16.26113  -5.85799  48.89241  1.000 56.23292 ?  17  LYS A CB  1 
ATOM   37   C CG  . LYS A 1 19  ? 15.13096  -6.81058  49.18375  1.000 53.72605 ?  17  LYS A CG  1 
ATOM   38   C CD  . LYS A 1 19  ? 15.64522  -8.19326  49.54194  1.000 59.41851 ?  17  LYS A CD  1 
ATOM   39   C CE  . LYS A 1 19  ? 14.50638  -9.21811  49.59511  1.000 56.23860 ?  17  LYS A CE  1 
ATOM   40   N NZ  . LYS A 1 19  ? 15.02448  -10.62566 49.55983  1.000 58.49674 ?  17  LYS A NZ  1 
ATOM   41   N N   . ARG A 1 20  ? 15.74309  -3.66621  46.48423  1.000 54.00533 ?  18  ARG A N   1 
ATOM   42   C CA  . ARG A 1 20  ? 14.76259  -2.84487  45.78525  1.000 54.75635 ?  18  ARG A CA  1 
ATOM   43   C C   . ARG A 1 20  ? 14.61356  -3.30014  44.33650  1.000 46.66643 ?  18  ARG A C   1 
ATOM   44   O O   . ARG A 1 20  ? 13.49381  -3.54974  43.87458  1.000 46.90871 ?  18  ARG A O   1 
ATOM   45   C CB  . ARG A 1 20  ? 15.14896  -1.36276  45.88153  1.000 53.59091 ?  18  ARG A CB  1 
ATOM   46   C CG  . ARG A 1 20  ? 13.98433  -0.40199  45.63421  1.000 50.52800 ?  18  ARG A CG  1 
ATOM   47   C CD  . ARG A 1 20  ? 14.42978  1.03720   45.37856  1.000 45.59568 ?  18  ARG A CD  1 
ATOM   48   N NE  . ARG A 1 20  ? 13.31561  1.85786   44.90906  1.000 43.39412 ?  18  ARG A NE  1 
ATOM   49   C CZ  . ARG A 1 20  ? 13.09321  2.17093   43.63673  1.000 47.27958 ?  18  ARG A CZ  1 
ATOM   50   N NH1 . ARG A 1 20  ? 13.90428  1.76906   42.67135  1.000 45.65704 ?  18  ARG A NH1 1 
ATOM   51   N NH2 . ARG A 1 20  ? 12.01750  2.88838   43.32130  1.000 43.83398 ?  18  ARG A NH2 1 
ATOM   52   N N   . ASN A 1 21  ? 15.73276  -3.43363  43.60709  1.000 48.34151 ?  19  ASN A N   1 
ATOM   53   C CA  . ASN A 1 21  ? 15.67016  -3.98334  42.25291  1.000 48.34481 ?  19  ASN A CA  1 
ATOM   54   C C   . ASN A 1 21  ? 15.01105  -5.36361  42.26871  1.000 44.79833 ?  19  ASN A C   1 
ATOM   55   O O   . ASN A 1 21  ? 14.17296  -5.65680  41.41462  1.000 40.48390 ?  19  ASN A O   1 
ATOM   56   C CB  . ASN A 1 21  ? 17.07910  -4.01503  41.62208  1.000 45.16102 ?  19  ASN A CB  1 
ATOM   57   C CG  . ASN A 1 21  ? 17.07832  -4.30899  40.08018  1.000 46.83048 ?  19  ASN A CG  1 
ATOM   58   O OD1 . ASN A 1 21  ? 17.54776  -5.37106  39.62174  1.000 41.74597 ?  19  ASN A OD1 1 
ATOM   59   N ND2 . ASN A 1 21  ? 16.55274  -3.36477  39.29030  1.000 44.57257 ?  19  ASN A ND2 1 
ATOM   60   N N   . HIS A 1 22  ? 15.30911  -6.19172  43.28493  1.000 43.83012 ?  20  HIS A N   1 
ATOM   61   C CA  . HIS A 1 22  ? 14.75062  -7.54774  43.32461  1.000 43.58631 ?  20  HIS A CA  1 
ATOM   62   C C   . HIS A 1 22  ? 13.22639  -7.54961  43.49395  1.000 39.95894 ?  20  HIS A C   1 
ATOM   63   O O   . HIS A 1 22  ? 12.52227  -8.31490  42.81030  1.000 36.60743 ?  20  HIS A O   1 
ATOM   64   C CB  . HIS A 1 22  ? 15.40875  -8.36920  44.43423  1.000 41.58026 ?  20  HIS A CB  1 
ATOM   65   C CG  . HIS A 1 22  ? 14.81352  -9.73556  44.59504  1.000 41.93129 ?  20  HIS A CG  1 
ATOM   66   N ND1 . HIS A 1 22  ? 14.86473  -10.68819 43.60095  1.000 41.53618 ?  20  HIS A ND1 1 
ATOM   67   C CD2 . HIS A 1 22  ? 14.15756  -10.31148 45.63086  1.000 45.70101 ?  20  HIS A CD2 1 
ATOM   68   C CE1 . HIS A 1 22  ? 14.26515  -11.79011 44.01565  1.000 40.41867 ?  20  HIS A CE1 1 
ATOM   69   N NE2 . HIS A 1 22  ? 13.82736  -11.58846 45.24460  1.000 42.98465 ?  20  HIS A NE2 1 
ATOM   70   N N   . ILE A 1 23  ? 12.69268  -6.70966  44.38779  1.000 37.18180 ?  21  ILE A N   1 
ATOM   71   C CA  . ILE A 1 23  ? 11.23670  -6.64140  44.57415  1.000 39.29429 ?  21  ILE A CA  1 
ATOM   72   C C   . ILE A 1 23  ? 10.55091  -6.09789  43.32399  1.000 34.94832 ?  21  ILE A C   1 
ATOM   73   O O   . ILE A 1 23  ? 9.56770   -6.66487  42.82725  1.000 32.18273 ?  21  ILE A O   1 
ATOM   74   C CB  . ILE A 1 23  ? 10.89692  -5.78530  45.80844  1.000 37.56463 ?  21  ILE A CB  1 
ATOM   75   C CG1 . ILE A 1 23  ? 11.74518  -6.20579  46.99220  1.000 45.83780 ?  21  ILE A CG1 1 
ATOM   76   C CG2 . ILE A 1 23  ? 9.44923   -5.92144  46.16447  1.000 37.30125 ?  21  ILE A CG2 1 
ATOM   77   C CD1 . ILE A 1 23  ? 11.37968  -5.50526  48.28019  1.000 50.39458 ?  21  ILE A CD1 1 
ATOM   78   N N   . LEU A 1 24  ? 11.05256  -4.98511  42.79321  1.000 37.84879 ?  22  LEU A N   1 
ATOM   79   C CA  . LEU A 1 24  ? 10.37468  -4.36602  41.66663  1.000 33.26326 ?  22  LEU A CA  1 
ATOM   80   C C   . LEU A 1 24  ? 10.44992  -5.24077  40.42256  1.000 34.08590 ?  22  LEU A C   1 
ATOM   81   O O   . LEU A 1 24  ? 9.47755   -5.32348  39.66924  1.000 32.70367 ?  22  LEU A O   1 
ATOM   82   C CB  . LEU A 1 24  ? 10.93721  -2.97367  41.40119  1.000 35.04650 ?  22  LEU A CB  1 
ATOM   83   C CG  . LEU A 1 24  ? 10.74037  -1.92590  42.50150  1.000 42.19862 ?  22  LEU A CG  1 
ATOM   84   C CD1 . LEU A 1 24  ? 11.75095  -0.80712  42.31002  1.000 44.80732 ?  22  LEU A CD1 1 
ATOM   85   C CD2 . LEU A 1 24  ? 9.33440   -1.36181  42.52440  1.000 34.56894 ?  22  LEU A CD2 1 
ATOM   86   N N   . THR A 1 25  ? 11.57235  -5.94169  40.21056  1.000 36.42074 ?  23  THR A N   1 
ATOM   87   C CA  . THR A 1 25  ? 11.67211  -6.77678  39.01664  1.000 34.95646 ?  23  THR A CA  1 
ATOM   88   C C   . THR A 1 25  ? 10.93885  -8.10343  39.17301  1.000 31.69052 ?  23  THR A C   1 
ATOM   89   O O   . THR A 1 25  ? 10.47911  -8.67051  38.17594  1.000 33.93973 ?  23  THR A O   1 
ATOM   90   C CB  . THR A 1 25  ? 13.13828  -7.02912  38.63840  1.000 33.17436 ?  23  THR A CB  1 
ATOM   91   O OG1 . THR A 1 25  ? 13.86297  -7.53976  39.76035  1.000 34.10452 ?  23  THR A OG1 1 
ATOM   92   C CG2 . THR A 1 25  ? 13.80233  -5.73688  38.15915  1.000 36.75063 ?  23  THR A CG2 1 
ATOM   93   N N   . THR A 1 26  ? 10.82460  -8.61972  40.39163  1.000 31.94070 ?  24  THR A N   1 
ATOM   94   C CA  . THR A 1 26  ? 9.96194   -9.77317  40.61081  1.000 32.10632 ?  24  THR A CA  1 
ATOM   95   C C   . THR A 1 26  ? 8.52349   -9.43245  40.26160  1.000 32.63366 ?  24  THR A C   1 
ATOM   96   O O   . THR A 1 26  ? 7.83503   -10.20881 39.58906  1.000 32.10729 ?  24  THR A O   1 
ATOM   97   C CB  . THR A 1 26  ? 10.05969  -10.24563 42.06298  1.000 35.21268 ?  24  THR A CB  1 
ATOM   98   O OG1 . THR A 1 26  ? 11.40687  -10.64676 42.35221  1.000 39.10661 ?  24  THR A OG1 1 
ATOM   99   C CG2 . THR A 1 26  ? 9.09416   -11.40374 42.32757  1.000 37.25143 ?  24  THR A CG2 1 
ATOM   100  N N   . ALA A 1 27  ? 8.06486   -8.25766  40.68943  1.000 31.83450 ?  25  ALA A N   1 
ATOM   101  C CA  . ALA A 1 27  ? 6.69683   -7.84257  40.41936  1.000 31.80743 ?  25  ALA A CA  1 
ATOM   102  C C   . ALA A 1 27  ? 6.47528   -7.62295  38.92668  1.000 29.66688 ?  25  ALA A C   1 
ATOM   103  O O   . ALA A 1 27  ? 5.50584   -8.13163  38.35987  1.000 26.50679 ?  25  ALA A O   1 
ATOM   104  C CB  . ALA A 1 27  ? 6.36595   -6.58304  41.22451  1.000 26.37994 ?  25  ALA A CB  1 
ATOM   105  N N   . LEU A 1 28  ? 7.39082   -6.89651  38.26772  1.000 29.15970 ?  26  LEU A N   1 
ATOM   106  C CA  . LEU A 1 28  ? 7.23585   -6.60230  36.84599  1.000 31.47426 ?  26  LEU A CA  1 
ATOM   107  C C   . LEU A 1 28  ? 7.09635   -7.87010  36.01744  1.000 29.96682 ?  26  LEU A C   1 
ATOM   108  O O   . LEU A 1 28  ? 6.33240   -7.89604  35.04670  1.000 29.04179 ?  26  LEU A O   1 
ATOM   109  C CB  . LEU A 1 28  ? 8.42118   -5.76903  36.35921  1.000 32.69811 ?  26  LEU A CB  1 
ATOM   110  C CG  . LEU A 1 28  ? 8.26925   -4.28549  36.75144  1.000 33.76838 ?  26  LEU A CG  1 
ATOM   111  C CD1 . LEU A 1 28  ? 9.57374   -3.52221  36.60189  1.000 35.77710 ?  26  LEU A CD1 1 
ATOM   112  C CD2 . LEU A 1 28  ? 7.19375   -3.61125  35.95691  1.000 31.84195 ?  26  LEU A CD2 1 
ATOM   113  N N   . ASN A 1 29  ? 7.76610   -8.94093  36.41424  1.000 27.74740 ?  27  ASN A N   1 
ATOM   114  C CA  . ASN A 1 29  ? 7.73272   -10.14652 35.60499  1.000 30.73043 ?  27  ASN A CA  1 
ATOM   115  C C   . ASN A 1 29  ? 6.40973   -10.87202 35.78799  1.000 34.23773 ?  27  ASN A C   1 
ATOM   116  O O   . ASN A 1 29  ? 5.84711   -11.40022 34.82156  1.000 33.49689 ?  27  ASN A O   1 
ATOM   117  C CB  . ASN A 1 29  ? 8.90504   -11.03773 35.97775  1.000 29.27780 ?  27  ASN A CB  1 
ATOM   118  C CG  . ASN A 1 29  ? 10.17777  -10.59928 35.30428  1.000 31.41753 ?  27  ASN A CG  1 
ATOM   119  O OD1 . ASN A 1 29  ? 10.13870  -9.98528  34.24271  1.000 37.74670 ?  27  ASN A OD1 1 
ATOM   120  N ND2 . ASN A 1 29  ? 11.31440  -10.83967 35.95234  1.000 34.36724 ?  27  ASN A ND2 1 
ATOM   121  N N   . LEU A 1 30  ? 5.88515   -10.86896 37.01632  1.000 30.65376 ?  28  LEU A N   1 
ATOM   122  C CA  . LEU A 1 30  ? 4.52484   -11.34382 37.26292  1.000 32.22912 ?  28  LEU A CA  1 
ATOM   123  C C   . LEU A 1 30  ? 3.49875   -10.48586 36.53165  1.000 34.25583 ?  28  LEU A C   1 
ATOM   124  O O   . LEU A 1 30  ? 2.57233   -11.00876 35.89165  1.000 33.00602 ?  28  LEU A O   1 
ATOM   125  C CB  . LEU A 1 30  ? 4.24961   -11.35324 38.77334  1.000 32.82750 ?  28  LEU A CB  1 
ATOM   126  C CG  . LEU A 1 30  ? 5.01404   -12.40188 39.57559  1.000 36.75978 ?  28  LEU A CG  1 
ATOM   127  C CD1 . LEU A 1 30  ? 5.05874   -12.03995 41.05759  1.000 34.27542 ?  28  LEU A CD1 1 
ATOM   128  C CD2 . LEU A 1 30  ? 4.40157   -13.77699 39.35159  1.000 38.96059 ?  28  LEU A CD2 1 
ATOM   129  N N   . PHE A 1 31  ? 3.63549   -9.15974  36.61738  1.000 32.12226 ?  29  PHE A N   1 
ATOM   130  C CA  . PHE A 1 31  ? 2.70464   -8.28496  35.90109  1.000 30.88965 ?  29  PHE A CA  1 
ATOM   131  C C   . PHE A 1 31  ? 2.74615   -8.54382  34.40376  1.000 36.78094 ?  29  PHE A C   1 
ATOM   132  O O   . PHE A 1 31  ? 1.70531   -8.53245  33.71863  1.000 32.91205 ?  29  PHE A O   1 
ATOM   133  C CB  . PHE A 1 31  ? 3.03107   -6.81752  36.18079  1.000 30.05315 ?  29  PHE A CB  1 
ATOM   134  C CG  . PHE A 1 31  ? 2.77686   -6.39070  37.60337  1.000 28.98429 ?  29  PHE A CG  1 
ATOM   135  C CD1 . PHE A 1 31  ? 1.77289   -6.98335  38.36382  1.000 35.10202 ?  29  PHE A CD1 1 
ATOM   136  C CD2 . PHE A 1 31  ? 3.55017   -5.39021  38.18529  1.000 33.13395 ?  29  PHE A CD2 1 
ATOM   137  C CE1 . PHE A 1 31  ? 1.54460   -6.58590  39.69076  1.000 33.15205 ?  29  PHE A CE1 1 
ATOM   138  C CE2 . PHE A 1 31  ? 3.33635   -4.98746  39.49618  1.000 31.98074 ?  29  PHE A CE2 1 
ATOM   139  C CZ  . PHE A 1 31  ? 2.32745   -5.58714  40.25407  1.000 34.31271 ?  29  PHE A CZ  1 
ATOM   140  N N   . ASP A 1 32  ? 3.95058   -8.74320  33.87034  1.000 34.94425 ?  30  ASP A N   1 
ATOM   141  C CA  . ASP A 1 32  ? 4.10943   -8.96348  32.44058  1.000 34.87533 ?  30  ASP A CA  1 
ATOM   142  C C   . ASP A 1 32  ? 3.44761   -10.25572 31.99515  1.000 35.74739 ?  30  ASP A C   1 
ATOM   143  O O   . ASP A 1 32  ? 2.93775   -10.34006 30.87378  1.000 36.44083 ?  30  ASP A O   1 
ATOM   144  C CB  . ASP A 1 32  ? 5.59459   -8.95188  32.09150  1.000 32.46297 ?  30  ASP A CB  1 
ATOM   145  C CG  . ASP A 1 32  ? 5.84433   -8.65265  30.62753  1.000 41.67886 ?  30  ASP A CG  1 
ATOM   146  O OD1 . ASP A 1 32  ? 5.70202   -7.47989  30.20449  1.000 43.09950 ?  30  ASP A OD1 1 
ATOM   147  O OD2 . ASP A 1 32  ? 6.20004   -9.59460  29.89397  1.000 43.31334 -1 30  ASP A OD2 1 
ATOM   148  N N   . GLN A 1 33  ? 3.40124   -11.24153 32.87555  1.000 35.60085 ?  31  GLN A N   1 
ATOM   149  C CA  . GLN A 1 33  ? 2.79407   -12.54066 32.64111  1.000 38.33383 ?  31  GLN A CA  1 
ATOM   150  C C   . GLN A 1 33  ? 1.29502   -12.55499 32.92320  1.000 40.74008 ?  31  GLN A C   1 
ATOM   151  O O   . GLN A 1 33  ? 0.52775   -13.12518 32.14367  1.000 44.24964 ?  31  GLN A O   1 
ATOM   152  C CB  . GLN A 1 33  ? 3.49987   -13.56031 33.53006  1.000 42.08673 ?  31  GLN A CB  1 
ATOM   153  C CG  . GLN A 1 33  ? 3.81209   -14.89227 32.92406  1.000 41.39836 ?  31  GLN A CG  1 
ATOM   154  C CD  . GLN A 1 33  ? 4.50961   -15.78523 33.92036  1.000 43.34369 ?  31  GLN A CD  1 
ATOM   155  O OE1 . GLN A 1 33  ? 5.43682   -15.36218 34.62663  1.000 41.73832 ?  31  GLN A OE1 1 
ATOM   156  N NE2 . GLN A 1 33  ? 4.06345   -17.02536 33.99768  1.000 47.39122 ?  31  GLN A NE2 1 
ATOM   157  N N   . PHE A 1 34  ? 0.85587   -11.93852 34.02474  1.000 40.07715 ?  32  PHE A N   1 
ATOM   158  C CA  . PHE A 1 34  ? -0.50531  -12.08436 34.50941  1.000 38.51092 ?  32  PHE A CA  1 
ATOM   159  C C   . PHE A 1 34  ? -1.27545  -10.78881 34.70439  1.000 41.96891 ?  32  PHE A C   1 
ATOM   160  O O   . PHE A 1 34  ? -2.42117  -10.84766 35.15214  1.000 46.37660 ?  32  PHE A O   1 
ATOM   161  C CB  . PHE A 1 34  ? -0.52208  -12.84615 35.83347  1.000 43.44737 ?  32  PHE A CB  1 
ATOM   162  C CG  . PHE A 1 34  ? 0.18329   -14.15455 35.78150  1.000 45.72375 ?  32  PHE A CG  1 
ATOM   163  C CD1 . PHE A 1 34  ? -0.37474  -15.21919 35.09165  1.000 45.88459 ?  32  PHE A CD1 1 
ATOM   164  C CD2 . PHE A 1 34  ? 1.37937   -14.34121 36.44885  1.000 42.34473 ?  32  PHE A CD2 1 
ATOM   165  C CE1 . PHE A 1 34  ? 0.26479   -16.43068 35.04755  1.000 44.00381 ?  32  PHE A CE1 1 
ATOM   166  C CE2 . PHE A 1 34  ? 2.01848   -15.55331 36.41581  1.000 42.14991 ?  32  PHE A CE2 1 
ATOM   167  C CZ  . PHE A 1 34  ? 1.46415   -16.60063 35.71364  1.000 45.13903 ?  32  PHE A CZ  1 
ATOM   168  N N   . GLY A 1 35  ? -0.70879  -9.63452  34.39741  1.000 40.74846 ?  33  GLY A N   1 
ATOM   169  C CA  . GLY A 1 35  ? -1.43991  -8.39496  34.53342  1.000 35.80797 ?  33  GLY A CA  1 
ATOM   170  C C   . GLY A 1 35  ? -1.35101  -7.79745  35.92691  1.000 35.73873 ?  33  GLY A C   1 
ATOM   171  O O   . GLY A 1 35  ? -1.01520  -8.45527  36.90012  1.000 35.17559 ?  33  GLY A O   1 
ATOM   172  N N   . PHE A 1 36  ? -1.71503  -6.51514  36.01142  1.000 34.85635 ?  34  PHE A N   1 
ATOM   173  C CA  . PHE A 1 36  ? -1.52215  -5.74750  37.23618  1.000 40.10737 ?  34  PHE A CA  1 
ATOM   174  C C   . PHE A 1 36  ? -2.53684  -6.10606  38.32430  1.000 41.28269 ?  34  PHE A C   1 
ATOM   175  O O   . PHE A 1 36  ? -2.15529  -6.36044  39.47116  1.000 42.79916 ?  34  PHE A O   1 
ATOM   176  C CB  . PHE A 1 36  ? -1.57641  -4.25817  36.91165  1.000 36.21414 ?  34  PHE A CB  1 
ATOM   177  C CG  . PHE A 1 36  ? -0.35153  -3.75201  36.23502  1.000 35.72916 ?  34  PHE A CG  1 
ATOM   178  C CD1 . PHE A 1 36  ? 0.80164   -3.53746  36.95882  1.000 32.62345 ?  34  PHE A CD1 1 
ATOM   179  C CD2 . PHE A 1 36  ? -0.35118  -3.47139  34.89022  1.000 31.71180 ?  34  PHE A CD2 1 
ATOM   180  C CE1 . PHE A 1 36  ? 1.94252   -3.07237  36.35227  1.000 33.87914 ?  34  PHE A CE1 1 
ATOM   181  C CE2 . PHE A 1 36  ? 0.78148   -3.00112  34.27872  1.000 30.35752 ?  34  PHE A CE2 1 
ATOM   182  C CZ  . PHE A 1 36  ? 1.92662   -2.79138  35.00862  1.000 29.61539 ?  34  PHE A CZ  1 
ATOM   183  N N   . GLN A 1 37  ? -3.83958  -6.10967  38.00480  1.000 43.81125 ?  35  GLN A N   1 
ATOM   184  C CA  . GLN A 1 37  ? -4.84357  -6.35142  39.04930  1.000 44.54934 ?  35  GLN A CA  1 
ATOM   185  C C   . GLN A 1 37  ? -4.90151  -7.80893  39.49566  1.000 45.09624 ?  35  GLN A C   1 
ATOM   186  O O   . GLN A 1 37  ? -5.36269  -8.08670  40.60498  1.000 50.56950 ?  35  GLN A O   1 
ATOM   187  C CB  . GLN A 1 37  ? -6.23644  -5.90987  38.58173  1.000 49.22454 ?  35  GLN A CB  1 
ATOM   188  C CG  . GLN A 1 37  ? -6.21710  -4.71813  37.64805  1.000 49.41199 ?  35  GLN A CG  1 
ATOM   189  C CD  . GLN A 1 37  ? -6.59372  -3.42813  38.35451  1.000 48.13784 ?  35  GLN A CD  1 
ATOM   190  O OE1 . GLN A 1 37  ? -6.66383  -3.37040  39.58972  1.000 51.72056 ?  35  GLN A OE1 1 
ATOM   191  N NE2 . GLN A 1 37  ? -6.82686  -2.38042  37.57413  1.000 47.34549 ?  35  GLN A NE2 1 
ATOM   192  N N   . HIS A 1 38  ? -4.46066  -8.73714  38.65016  1.000 47.48441 ?  36  HIS A N   1 
ATOM   193  C CA  . HIS A 1 38  ? -4.40043  -10.15379 39.00190  1.000 46.72734 ?  36  HIS A CA  1 
ATOM   194  C C   . HIS A 1 38  ? -3.38495  -10.44750 40.10617  1.000 45.85276 ?  36  HIS A C   1 
ATOM   195  O O   . HIS A 1 38  ? -3.54580  -11.42231 40.84696  1.000 48.43602 ?  36  HIS A O   1 
ATOM   196  C CB  . HIS A 1 38  ? -4.03204  -10.94044 37.74684  1.000 49.83373 ?  36  HIS A CB  1 
ATOM   197  C CG  . HIS A 1 38  ? -4.58949  -12.32520 37.69109  1.000 57.54128 ?  36  HIS A CG  1 
ATOM   198  N ND1 . HIS A 1 38  ? -3.87379  -13.38722 37.17378  1.000 57.09353 ?  36  HIS A ND1 1 
ATOM   199  C CD2 . HIS A 1 38  ? -5.80536  -12.81636 38.02855  1.000 59.54160 ?  36  HIS A CD2 1 
ATOM   200  C CE1 . HIS A 1 38  ? -4.61397  -14.48107 37.23158  1.000 58.69422 ?  36  HIS A CE1 1 
ATOM   201  N NE2 . HIS A 1 38  ? -5.79062  -14.16153 37.74366  1.000 62.27812 ?  36  HIS A NE2 1 
ATOM   202  N N   . ILE A 1 39  ? -2.32214  -9.65191  40.22254  1.000 46.93243 ?  37  ILE A N   1 
ATOM   203  C CA  . ILE A 1 39  ? -1.18488  -9.97597  41.08095  1.000 43.41522 ?  37  ILE A CA  1 
ATOM   204  C C   . ILE A 1 39  ? -1.22141  -9.08848  42.32464  1.000 43.16895 ?  37  ILE A C   1 
ATOM   205  O O   . ILE A 1 39  ? -1.13900  -7.85699  42.22914  1.000 41.09862 ?  37  ILE A O   1 
ATOM   206  C CB  . ILE A 1 39  ? 0.15111   -9.82017  40.33240  1.000 38.46927 ?  37  ILE A CB  1 
ATOM   207  C CG1 . ILE A 1 39  ? 0.27274   -10.83327 39.18960  1.000 36.16404 ?  37  ILE A CG1 1 
ATOM   208  C CG2 . ILE A 1 39  ? 1.29914   -10.05021 41.28089  1.000 37.71465 ?  37  ILE A CG2 1 
ATOM   209  C CD1 . ILE A 1 39  ? 0.49247   -12.24793 39.67587  1.000 39.09134 ?  37  ILE A CD1 1 
ATOM   210  N N   . SER A 1 40  ? -1.29411  -9.71040  43.49270  1.000 45.11151 ?  38  SER A N   1 
ATOM   211  C CA  . SER A 1 40  ? -1.40475  -8.96507  44.73688  1.000 43.58527 ?  38  SER A CA  1 
ATOM   212  C C   . SER A 1 40  ? -0.03218  -8.70282  45.35779  1.000 44.06920 ?  38  SER A C   1 
ATOM   213  O O   . SER A 1 40  ? 0.95813   -9.36754  45.04191  1.000 42.87271 ?  38  SER A O   1 
ATOM   214  C CB  . SER A 1 40  ? -2.29667  -9.71838  45.72527  1.000 46.52837 ?  38  SER A CB  1 
ATOM   215  O OG  . SER A 1 40  ? -1.62880  -10.82596 46.31984  1.000 44.68535 ?  38  SER A OG  1 
ATOM   216  N N   . ILE A 1 41  ? 0.00810   -7.69889  46.24721  1.000 45.24651 ?  39  ILE A N   1 
ATOM   217  C CA  . ILE A 1 41  ? 1.16225   -7.48876  47.12755  1.000 42.77277 ?  39  ILE A CA  1 
ATOM   218  C C   . ILE A 1 41  ? 1.56117   -8.77199  47.82715  1.000 47.18694 ?  39  ILE A C   1 
ATOM   219  O O   . ILE A 1 41  ? 2.74941   -9.08366  47.94982  1.000 42.82564 ?  39  ILE A O   1 
ATOM   220  C CB  . ILE A 1 41  ? 0.87850   -6.36983  48.15220  1.000 43.80697 ?  39  ILE A CB  1 
ATOM   221  C CG1 . ILE A 1 41  ? 0.71773   -5.01785  47.46391  1.000 47.76647 ?  39  ILE A CG1 1 
ATOM   222  C CG2 . ILE A 1 41  ? 1.96143   -6.29622  49.22675  1.000 47.85780 ?  39  ILE A CG2 1 
ATOM   223  C CD1 . ILE A 1 41  ? 1.48727   -4.92655  46.15460  1.000 44.75179 ?  39  ILE A CD1 1 
ATOM   224  N N   . MET A 1 42  ? 0.58068   -9.51150  48.34819  1.000 46.28888 ?  40  MET A N   1 
ATOM   225  C CA  . MET A 1 42  ? 0.93272   -10.69759 49.11531  1.000 47.57399 ?  40  MET A CA  1 
ATOM   226  C C   . MET A 1 42  ? 1.70368   -11.68760 48.26132  1.000 45.27109 ?  40  MET A C   1 
ATOM   227  O O   . MET A 1 42  ? 2.67917   -12.30157 48.72038  1.000 46.15787 ?  40  MET A O   1 
ATOM   228  C CB  . MET A 1 42  ? -0.32532  -11.34248 49.68394  1.000 50.98192 ?  40  MET A CB  1 
ATOM   229  C CG  . MET A 1 42  ? -0.00857  -12.09644 50.91881  1.000 50.63656 ?  40  MET A CG  1 
ATOM   230  S SD  . MET A 1 42  ? 0.42708   -10.96763 52.27594  1.000 69.02067 ?  40  MET A SD  1 
ATOM   231  C CE  . MET A 1 42  ? -0.56518  -9.50783  51.84249  1.000 57.27926 ?  40  MET A CE  1 
ATOM   232  N N   . ARG A 1 43  ? 1.28301   -11.83211 47.00798  1.000 47.13078 ?  41  ARG A N   1 
ATOM   233  C CA  . ARG A 1 43  ? 1.96039   -12.71240 46.06635  1.000 48.56314 ?  41  ARG A CA  1 
ATOM   234  C C   . ARG A 1 43  ? 3.36168   -12.19861 45.74764  1.000 45.54292 ?  41  ARG A C   1 
ATOM   235  O O   . ARG A 1 43  ? 4.34314   -12.94784 45.81978  1.000 43.48721 ?  41  ARG A O   1 
ATOM   236  C CB  . ARG A 1 43  ? 1.10762   -12.82117 44.81625  1.000 41.72562 ?  41  ARG A CB  1 
ATOM   237  C CG  . ARG A 1 43  ? 1.73974   -13.48333 43.65189  1.000 50.09967 ?  41  ARG A CG  1 
ATOM   238  C CD  . ARG A 1 43  ? 1.37091   -14.94190 43.59186  1.000 52.02043 ?  41  ARG A CD  1 
ATOM   239  N NE  . ARG A 1 43  ? 1.85580   -15.53210 42.34935  1.000 50.90862 ?  41  ARG A NE  1 
ATOM   240  C CZ  . ARG A 1 43  ? 1.12246   -15.66537 41.25403  1.000 48.60047 ?  41  ARG A CZ  1 
ATOM   241  N NH1 . ARG A 1 43  ? -0.13331  -15.24990 41.20768  1.000 52.35263 ?  41  ARG A NH1 1 
ATOM   242  N NH2 . ARG A 1 43  ? 1.66367   -16.22142 40.17496  1.000 49.26521 ?  41  ARG A NH2 1 
ATOM   243  N N   . ILE A 1 44  ? 3.47955   -10.90800 45.43521  1.000 43.68556 ?  42  ILE A N   1 
ATOM   244  C CA  . ILE A 1 44  ? 4.79055   -10.32958 45.16237  1.000 42.19528 ?  42  ILE A CA  1 
ATOM   245  C C   . ILE A 1 44  ? 5.70097   -10.49312 46.36805  1.000 45.52960 ?  42  ILE A C   1 
ATOM   246  O O   . ILE A 1 44  ? 6.87232   -10.86348 46.23593  1.000 41.94936 ?  42  ILE A O   1 
ATOM   247  C CB  . ILE A 1 44  ? 4.63392   -8.85685  44.74320  1.000 41.30123 ?  42  ILE A CB  1 
ATOM   248  C CG1 . ILE A 1 44  ? 3.97605   -8.79262  43.36893  1.000 38.55428 ?  42  ILE A CG1 1 
ATOM   249  C CG2 . ILE A 1 44  ? 5.97672   -8.17293  44.67879  1.000 34.19892 ?  42  ILE A CG2 1 
ATOM   250  C CD1 . ILE A 1 44  ? 3.28275   -7.46867  43.05317  1.000 36.30690 ?  42  ILE A CD1 1 
ATOM   251  N N   . ILE A 1 45  ? 5.15396   -10.28492 47.56712  1.000 44.69960 ?  43  ILE A N   1 
ATOM   252  C CA  . ILE A 1 45  ? 5.94573   -10.30270 48.78373  1.000 47.13112 ?  43  ILE A CA  1 
ATOM   253  C C   . ILE A 1 45  ? 6.45650   -11.71038 49.07832  1.000 49.01803 ?  43  ILE A C   1 
ATOM   254  O O   . ILE A 1 45  ? 7.59349   -11.89299 49.52881  1.000 47.45408 ?  43  ILE A O   1 
ATOM   255  C CB  . ILE A 1 45  ? 5.09111   -9.74341  49.93412  1.000 49.57117 ?  43  ILE A CB  1 
ATOM   256  C CG1 . ILE A 1 45  ? 5.16339   -8.21600  49.96590  1.000 48.63330 ?  43  ILE A CG1 1 
ATOM   257  C CG2 . ILE A 1 45  ? 5.49296   -10.34622 51.24071  1.000 53.49104 ?  43  ILE A CG2 1 
ATOM   258  C CD1 . ILE A 1 45  ? 4.55219   -7.63072  51.23865  1.000 54.87479 ?  43  ILE A CD1 1 
ATOM   259  N N   . THR A 1 46  ? 5.64318   -12.73078 48.80520  1.000 45.09364 ?  44  THR A N   1 
ATOM   260  C CA  . THR A 1 46  ? 6.11866   -14.09560 48.99499  1.000 47.85964 ?  44  THR A CA  1 
ATOM   261  C C   . THR A 1 46  ? 7.10993   -14.49136 47.90353  1.000 50.53281 ?  44  THR A C   1 
ATOM   262  O O   . THR A 1 46  ? 8.18989   -15.02217 48.19969  1.000 52.78034 ?  44  THR A O   1 
ATOM   263  C CB  . THR A 1 46  ? 4.94082   -15.06419 49.03777  1.000 50.63150 ?  44  THR A CB  1 
ATOM   264  O OG1 . THR A 1 46  ? 4.01672   -14.61833 50.03656  1.000 54.82700 ?  44  THR A OG1 1 
ATOM   265  C CG2 . THR A 1 46  ? 5.43156   -16.45332 49.43525  1.000 49.16651 ?  44  THR A CG2 1 
ATOM   266  N N   . GLU A 1 47  ? 6.75915   -14.24059 46.63540  1.000 46.84019 ?  45  GLU A N   1 
ATOM   267  C CA  . GLU A 1 47  ? 7.68521   -14.51854 45.53807  1.000 48.63604 ?  45  GLU A CA  1 
ATOM   268  C C   . GLU A 1 47  ? 9.01340   -13.80780 45.75216  1.000 50.18134 ?  45  GLU A C   1 
ATOM   269  O O   . GLU A 1 47  ? 10.08145  -14.38934 45.53024  1.000 54.00668 ?  45  GLU A O   1 
ATOM   270  C CB  . GLU A 1 47  ? 7.08143   -14.09778 44.19658  1.000 48.93651 ?  45  GLU A CB  1 
ATOM   271  C CG  . GLU A 1 47  ? 5.69226   -14.64639 43.87983  1.000 51.88761 ?  45  GLU A CG  1 
ATOM   272  C CD  . GLU A 1 47  ? 5.68244   -15.78398 42.87661  1.000 55.38032 ?  45  GLU A CD  1 
ATOM   273  O OE1 . GLU A 1 47  ? 6.57111   -15.80614 41.99421  1.000 55.49140 ?  45  GLU A OE1 1 
ATOM   274  O OE2 . GLU A 1 47  ? 4.75060   -16.62294 42.93894  1.000 57.03278 -1 45  GLU A OE2 1 
ATOM   275  N N   . ALA A 1 48  ? 8.97522   -12.55635 46.20529  1.000 47.10891 ?  46  ALA A N   1 
ATOM   276  C CA  . ALA A 1 48  ? 10.21445  -11.81858 46.39748  1.000 48.08270 ?  46  ALA A CA  1 
ATOM   277  C C   . ALA A 1 48  ? 10.92243  -12.17590 47.69854  1.000 52.06023 ?  46  ALA A C   1 
ATOM   278  O O   . ALA A 1 48  ? 12.08995  -11.80686 47.85926  1.000 50.97916 ?  46  ALA A O   1 
ATOM   279  C CB  . ALA A 1 48  ? 9.94437   -10.30980 46.33193  1.000 45.69951 ?  46  ALA A CB  1 
ATOM   280  N N   . LYS A 1 49  ? 10.25261  -12.90358 48.60520  1.000 52.77647 ?  47  LYS A N   1 
ATOM   281  C CA  . LYS A 1 49  ? 10.79414  -13.31618 49.90808  1.000 51.08912 ?  47  LYS A CA  1 
ATOM   282  C C   . LYS A 1 49  ? 11.28511  -12.11968 50.72683  1.000 56.16000 ?  47  LYS A C   1 
ATOM   283  O O   . LYS A 1 49  ? 12.42096  -12.08171 51.20964  1.000 54.48640 ?  47  LYS A O   1 
ATOM   284  C CB  . LYS A 1 49  ? 11.89109  -14.37638 49.75785  1.000 57.26961 ?  47  LYS A CB  1 
ATOM   285  C CG  . LYS A 1 49  ? 11.69909  -15.34518 48.58501  1.000 58.45789 ?  47  LYS A CG  1 
ATOM   286  C CD  . LYS A 1 49  ? 12.85964  -16.34658 48.48566  1.000 63.72597 ?  47  LYS A CD  1 
ATOM   287  C CE  . LYS A 1 49  ? 12.64877  -17.56284 49.40666  1.000 63.70953 ?  47  LYS A CE  1 
ATOM   288  N NZ  . LYS A 1 49  ? 12.26620  -18.80734 48.66413  1.000 63.93096 ?  47  LYS A NZ  1 
ATOM   289  N N   . ILE A 1 50  ? 10.39151  -11.14685 50.90706  1.000 57.50608 ?  48  ILE A N   1 
ATOM   290  C CA  . ILE A 1 50  ? 10.63832  -9.95821  51.71177  1.000 58.53597 ?  48  ILE A CA  1 
ATOM   291  C C   . ILE A 1 50  ? 9.52199   -9.84211  52.74674  1.000 58.65167 ?  48  ILE A C   1 
ATOM   292  O O   . ILE A 1 50  ? 8.37514   -10.22725 52.49688  1.000 59.53819 ?  48  ILE A O   1 
ATOM   293  C CB  . ILE A 1 50  ? 10.74106  -8.68425  50.82478  1.000 57.31074 ?  48  ILE A CB  1 
ATOM   294  C CG1 . ILE A 1 50  ? 11.41937  -7.54671  51.59758  1.000 59.11592 ?  48  ILE A CG1 1 
ATOM   295  C CG2 . ILE A 1 50  ? 9.37852   -8.28069  50.26758  1.000 50.76677 ?  48  ILE A CG2 1 
ATOM   296  C CD1 . ILE A 1 50  ? 10.56787  -6.31235  51.78459  1.000 56.56485 ?  48  ILE A CD1 1 
ATOM   297  N N   . ALA A 1 51  ? 9.86753   -9.32527  53.92477  1.000 63.74380 ?  49  ALA A N   1 
ATOM   298  C CA  . ALA A 1 51  ? 8.91386   -9.26088  55.02551  1.000 59.93305 ?  49  ALA A CA  1 
ATOM   299  C C   . ALA A 1 51  ? 7.82797   -8.22905  54.75515  1.000 58.57446 ?  49  ALA A C   1 
ATOM   300  O O   . ALA A 1 51  ? 8.10383   -7.11923  54.29158  1.000 58.43075 ?  49  ALA A O   1 
ATOM   301  C CB  . ALA A 1 51  ? 9.62592   -8.92579  56.33162  1.000 62.63590 ?  49  ALA A CB  1 
ATOM   302  N N   . LYS A 1 52  ? 6.58381   -8.61687  55.05039  1.000 57.31406 ?  50  LYS A N   1 
ATOM   303  C CA  . LYS A 1 52  ? 5.43624   -7.72368  54.90729  1.000 58.50798 ?  50  LYS A CA  1 
ATOM   304  C C   . LYS A 1 52  ? 5.71922   -6.32611  55.42715  1.000 58.76509 ?  50  LYS A C   1 
ATOM   305  O O   . LYS A 1 52  ? 5.45312   -5.33270  54.74430  1.000 57.25919 ?  50  LYS A O   1 
ATOM   306  C CB  . LYS A 1 52  ? 4.22987   -8.28171  55.64956  1.000 57.35915 ?  50  LYS A CB  1 
ATOM   307  C CG  . LYS A 1 52  ? 2.92728   -7.99243  54.98674  1.000 55.08621 ?  50  LYS A CG  1 
ATOM   308  C CD  . LYS A 1 52  ? 1.78976   -8.51583  55.83066  1.000 63.53965 ?  50  LYS A CD  1 
ATOM   309  C CE  . LYS A 1 52  ? 0.64885   -8.99736  54.98650  1.000 63.00726 ?  50  LYS A CE  1 
ATOM   310  N NZ  . LYS A 1 52  ? -0.21457  -9.91671  55.75706  1.000 64.00011 ?  50  LYS A NZ  1 
ATOM   311  N N   . GLN A 1 53  ? 6.21898   -6.22718  56.65509  1.000 57.95277 ?  51  GLN A N   1 
ATOM   312  C CA  . GLN A 1 53  ? 6.28960   -4.91999  57.28757  1.000 59.64622 ?  51  GLN A CA  1 
ATOM   313  C C   . GLN A 1 53  ? 7.33482   -4.05258  56.60692  1.000 55.62357 ?  51  GLN A C   1 
ATOM   314  O O   . GLN A 1 53  ? 7.15123   -2.83673  56.47362  1.000 54.78438 ?  51  GLN A O   1 
ATOM   315  C CB  . GLN A 1 53  ? 6.58625   -5.07473  58.77326  1.000 62.93076 ?  51  GLN A CB  1 
ATOM   316  C CG  . GLN A 1 53  ? 5.33957   -5.17533  59.64123  1.000 69.10719 ?  51  GLN A CG  1 
ATOM   317  C CD  . GLN A 1 53  ? 5.65036   -5.81449  60.98112  1.000 71.64696 ?  51  GLN A CD  1 
ATOM   318  O OE1 . GLN A 1 53  ? 6.48886   -6.71840  61.06903  1.000 73.13372 ?  51  GLN A OE1 1 
ATOM   319  N NE2 . GLN A 1 53  ? 4.97663   -5.35107  62.03606  1.000 74.87767 ?  51  GLN A NE2 1 
ATOM   320  N N   . SER A 1 54  ? 8.42619   -4.66707  56.14899  1.000 54.72329 ?  52  SER A N   1 
ATOM   321  C CA  . SER A 1 54  ? 9.43526   -3.91306  55.42101  1.000 54.20995 ?  52  SER A CA  1 
ATOM   322  C C   . SER A 1 54  ? 8.87425   -3.38381  54.11531  1.000 54.79908 ?  52  SER A C   1 
ATOM   323  O O   . SER A 1 54  ? 9.10776   -2.22223  53.75791  1.000 55.08709 ?  52  SER A O   1 
ATOM   324  C CB  . SER A 1 54  ? 10.66624  -4.78183  55.15451  1.000 58.27612 ?  52  SER A CB  1 
ATOM   325  O OG  . SER A 1 54  ? 11.19350  -5.31320  56.36004  1.000 63.55208 ?  52  SER A OG  1 
ATOM   326  N N   . PHE A 1 55  ? 8.13808   -4.22683  53.38116  1.000 53.12184 ?  53  PHE A N   1 
ATOM   327  C CA  . PHE A 1 55  ? 7.61651   -3.81338  52.08582  1.000 51.68652 ?  53  PHE A CA  1 
ATOM   328  C C   . PHE A 1 55  ? 6.70215   -2.61230  52.23694  1.000 49.85754 ?  53  PHE A C   1 
ATOM   329  O O   . PHE A 1 55  ? 6.79487   -1.65030  51.46688  1.000 45.68604 ?  53  PHE A O   1 
ATOM   330  C CB  . PHE A 1 55  ? 6.86976   -4.97205  51.42162  1.000 51.42159 ?  53  PHE A CB  1 
ATOM   331  C CG  . PHE A 1 55  ? 6.18995   -4.59979  50.12970  1.000 51.30259 ?  53  PHE A CG  1 
ATOM   332  C CD1 . PHE A 1 55  ? 4.89256   -4.09979  50.12518  1.000 48.62104 ?  53  PHE A CD1 1 
ATOM   333  C CD2 . PHE A 1 55  ? 6.84346   -4.76472  48.91914  1.000 47.60037 ?  53  PHE A CD2 1 
ATOM   334  C CE1 . PHE A 1 55  ? 4.27509   -3.74855  48.94702  1.000 48.20741 ?  53  PHE A CE1 1 
ATOM   335  C CE2 . PHE A 1 55  ? 6.22879   -4.42108  47.74197  1.000 45.48851 ?  53  PHE A CE2 1 
ATOM   336  C CZ  . PHE A 1 55  ? 4.93541   -3.91594  47.74939  1.000 46.47088 ?  53  PHE A CZ  1 
ATOM   337  N N   . TYR A 1 56  ? 5.81541   -2.64787  53.23565  1.000 53.39589 ?  54  TYR A N   1 
ATOM   338  C CA  . TYR A 1 56  ? 4.89180   -1.54347  53.42976  1.000 51.37269 ?  54  TYR A CA  1 
ATOM   339  C C   . TYR A 1 56  ? 5.59370   -0.29505  53.93523  1.000 50.66619 ?  54  TYR A C   1 
ATOM   340  O O   . TYR A 1 56  ? 5.11883   0.81337   53.66423  1.000 49.61912 ?  54  TYR A O   1 
ATOM   341  C CB  . TYR A 1 56  ? 3.74725   -1.96363  54.35077  1.000 54.17404 ?  54  TYR A CB  1 
ATOM   342  C CG  . TYR A 1 56  ? 2.75236   -2.81771  53.59937  1.000 52.65592 ?  54  TYR A CG  1 
ATOM   343  C CD1 . TYR A 1 56  ? 1.93142   -2.24776  52.63325  1.000 52.75158 ?  54  TYR A CD1 1 
ATOM   344  C CD2 . TYR A 1 56  ? 2.63331   -4.18761  53.83542  1.000 56.99197 ?  54  TYR A CD2 1 
ATOM   345  C CE1 . TYR A 1 56  ? 1.02128   -3.00603  51.91475  1.000 52.97416 ?  54  TYR A CE1 1 
ATOM   346  C CE2 . TYR A 1 56  ? 1.70467   -4.96741  53.11035  1.000 54.49354 ?  54  TYR A CE2 1 
ATOM   347  C CZ  . TYR A 1 56  ? 0.90235   -4.36104  52.15588  1.000 56.33434 ?  54  TYR A CZ  1 
ATOM   348  O OH  . TYR A 1 56  ? -0.02222  -5.08856  51.41428  1.000 56.17073 ?  54  TYR A OH  1 
ATOM   349  N N   . MET A 1 57  ? 6.74022   -0.43189  54.60364  1.000 49.36058 ?  55  MET A N   1 
ATOM   350  C CA  . MET A 1 57  ? 7.50223   0.76773   54.91360  1.000 50.78871 ?  55  MET A CA  1 
ATOM   351  C C   . MET A 1 57  ? 8.03720   1.41297   53.63712  1.000 50.47593 ?  55  MET A C   1 
ATOM   352  O O   . MET A 1 57  ? 7.99854   2.64030   53.49533  1.000 51.03657 ?  55  MET A O   1 
ATOM   353  C CB  . MET A 1 57  ? 8.61848   0.43725   55.89588  1.000 53.94616 ?  55  MET A CB  1 
ATOM   354  C CG  . MET A 1 57  ? 8.84180   1.56055   56.88759  1.000 55.53317 ?  55  MET A CG  1 
ATOM   355  S SD  . MET A 1 57  ? 7.39959   1.58862   57.96594  1.000 68.66700 ?  55  MET A SD  1 
ATOM   356  C CE  . MET A 1 57  ? 7.34859   3.30295   58.49915  1.000 65.81089 ?  55  MET A CE  1 
ATOM   357  N N   . ALA A 1 58  ? 8.47922   0.60289   52.66913  1.000 48.28243 ?  56  ALA A N   1 
ATOM   358  C CA  . ALA A 1 58  ? 9.00113   1.15346   51.42303  1.000 45.22921 ?  56  ALA A CA  1 
ATOM   359  C C   . ALA A 1 58  ? 7.90123   1.56701   50.45158  1.000 45.29104 ?  56  ALA A C   1 
ATOM   360  O O   . ALA A 1 58  ? 8.08455   2.52342   49.68259  1.000 43.98679 ?  56  ALA A O   1 
ATOM   361  C CB  . ALA A 1 58  ? 9.92275   0.14299   50.73331  1.000 47.50415 ?  56  ALA A CB  1 
ATOM   362  N N   . PHE A 1 59  ? 6.78466   0.83876   50.42716  1.000 39.24266 ?  57  PHE A N   1 
ATOM   363  C CA  . PHE A 1 59  ? 5.71442   1.06690   49.45893  1.000 42.94921 ?  57  PHE A CA  1 
ATOM   364  C C   . PHE A 1 59  ? 4.41629   1.02551   50.24726  1.000 42.53845 ?  57  PHE A C   1 
ATOM   365  O O   . PHE A 1 59  ? 3.83914   -0.04395  50.45697  1.000 43.32729 ?  57  PHE A O   1 
ATOM   366  C CB  . PHE A 1 59  ? 5.72669   0.02207   48.33716  1.000 38.68177 ?  57  PHE A CB  1 
ATOM   367  C CG  . PHE A 1 59  ? 7.07092   -0.11711  47.64802  1.000 40.39889 ?  57  PHE A CG  1 
ATOM   368  C CD1 . PHE A 1 59  ? 7.51364   0.85027   46.75400  1.000 36.92770 ?  57  PHE A CD1 1 
ATOM   369  C CD2 . PHE A 1 59  ? 7.91060   -1.18919  47.94216  1.000 39.12645 ?  57  PHE A CD2 1 
ATOM   370  C CE1 . PHE A 1 59  ? 8.74890   0.72817   46.13885  1.000 40.73316 ?  57  PHE A CE1 1 
ATOM   371  C CE2 . PHE A 1 59  ? 9.13333   -1.30945  47.35094  1.000 37.84759 ?  57  PHE A CE2 1 
ATOM   372  C CZ  . PHE A 1 59  ? 9.55739   -0.35215  46.43609  1.000 41.41409 ?  57  PHE A CZ  1 
ATOM   373  N N   . PRO A 1 60  ? 3.92760   2.18237   50.70206  1.000 40.24893 ?  58  PRO A N   1 
ATOM   374  C CA  . PRO A 1 60  ? 2.80078   2.17597   51.64176  1.000 44.35109 ?  58  PRO A CA  1 
ATOM   375  C C   . PRO A 1 60  ? 1.51013   1.64504   51.04778  1.000 42.77065 ?  58  PRO A C   1 
ATOM   376  O O   . PRO A 1 60  ? 0.67684   1.14601   51.80161  1.000 45.81191 ?  58  PRO A O   1 
ATOM   377  C CB  . PRO A 1 60  ? 2.66852   3.65491   52.03927  1.000 44.69719 ?  58  PRO A CB  1 
ATOM   378  C CG  . PRO A 1 60  ? 3.96587   4.26633   51.68056  1.000 42.28738 ?  58  PRO A CG  1 
ATOM   379  C CD  . PRO A 1 60  ? 4.44666   3.53999   50.48650  1.000 42.10954 ?  58  PRO A CD  1 
ATOM   380  N N   . SER A 1 61  ? 1.30196   1.72542   49.74138  1.000 38.98529 ?  59  SER A N   1 
ATOM   381  C CA  . SER A 1 61  ? 0.10477   1.15036   49.14525  1.000 40.24106 ?  59  SER A CA  1 
ATOM   382  C C   . SER A 1 61  ? 0.49619   0.39680   47.89496  1.000 39.27073 ?  59  SER A C   1 
ATOM   383  O O   . SER A 1 61  ? 1.62117   0.53370   47.39780  1.000 37.61607 ?  59  SER A O   1 
ATOM   384  C CB  . SER A 1 61  ? -0.93386  2.21762   48.80483  1.000 40.45775 ?  59  SER A CB  1 
ATOM   385  O OG  . SER A 1 61  ? -0.46020  3.03602   47.75234  1.000 36.00012 ?  59  SER A OG  1 
ATOM   386  N N   . LYS A 1 62  ? -0.45366  -0.39246  47.36890  1.000 38.87654 ?  60  LYS A N   1 
ATOM   387  C CA  . LYS A 1 62  ? -0.27841  -0.97835  46.04182  1.000 37.86306 ?  60  LYS A CA  1 
ATOM   388  C C   . LYS A 1 62  ? -0.05018  0.08574   44.97957  1.000 39.85697 ?  60  LYS A C   1 
ATOM   389  O O   . LYS A 1 62  ? 0.86062   -0.03352  44.15100  1.000 36.68956 ?  60  LYS A O   1 
ATOM   390  C CB  . LYS A 1 62  ? -1.48233  -1.82841  45.63834  1.000 42.67235 ?  60  LYS A CB  1 
ATOM   391  C CG  . LYS A 1 62  ? -1.09861  -3.14494  44.97396  1.000 44.94989 ?  60  LYS A CG  1 
ATOM   392  C CD  . LYS A 1 62  ? -2.24405  -3.71028  44.13772  1.000 44.89814 ?  60  LYS A CD  1 
ATOM   393  C CE  . LYS A 1 62  ? -1.70764  -4.62375  43.01656  1.000 46.44226 ?  60  LYS A CE  1 
ATOM   394  N NZ  . LYS A 1 62  ? -2.79969  -5.36904  42.29739  1.000 43.88514 ?  60  LYS A NZ  1 
ATOM   395  N N   . ASP A 1 63  ? -0.93093  1.08930   44.93698  1.000 40.08025 ?  61  ASP A N   1 
ATOM   396  C CA  . ASP A 1 63  ? -0.74782  2.23389   44.04996  1.000 38.23503 ?  61  ASP A CA  1 
ATOM   397  C C   . ASP A 1 63  ? 0.65382   2.82057   44.13567  1.000 37.24299 ?  61  ASP A C   1 
ATOM   398  O O   . ASP A 1 63  ? 1.23205   3.19400   43.10721  1.000 35.53282 ?  61  ASP A O   1 
ATOM   399  C CB  . ASP A 1 63  ? -1.79105  3.29352   44.38041  1.000 41.19160 ?  61  ASP A CB  1 
ATOM   400  C CG  . ASP A 1 63  ? -3.18108  2.93260   43.86856  1.000 47.88494 ?  61  ASP A CG  1 
ATOM   401  O OD1 . ASP A 1 63  ? -3.36328  1.85173   43.23922  1.000 44.16859 ?  61  ASP A OD1 1 
ATOM   402  O OD2 . ASP A 1 63  ? -4.10998  3.70302   44.18854  1.000 51.77238 -1 61  ASP A OD2 1 
ATOM   403  N N   . SER A 1 64  ? 1.20431   2.93295   45.35020  1.000 35.91269 ?  62  SER A N   1 
ATOM   404  C CA  . SER A 1 64  ? 2.56269   3.44373   45.50785  1.000 37.31441 ?  62  SER A CA  1 
ATOM   405  C C   . SER A 1 64  ? 3.55664   2.53075   44.80993  1.000 36.53613 ?  62  SER A C   1 
ATOM   406  O O   . SER A 1 64  ? 4.46595   2.99194   44.11336  1.000 35.79224 ?  62  SER A O   1 
ATOM   407  C CB  . SER A 1 64  ? 2.92573   3.55041   46.98470  1.000 38.80808 ?  62  SER A CB  1 
ATOM   408  O OG  . SER A 1 64  ? 2.12665   4.49972   47.67117  1.000 44.97388 ?  62  SER A OG  1 
ATOM   409  N N   . PHE A 1 65  ? 3.40024   1.22318   45.02218  1.000 33.45683 ?  63  PHE A N   1 
ATOM   410  C CA  . PHE A 1 65  ? 4.27043   0.22744   44.41794  1.000 36.24575 ?  63  PHE A CA  1 
ATOM   411  C C   . PHE A 1 65  ? 4.15845   0.21702   42.89666  1.000 33.39080 ?  63  PHE A C   1 
ATOM   412  O O   . PHE A 1 65  ? 5.17203   0.08710   42.20002  1.000 29.97177 ?  63  PHE A O   1 
ATOM   413  C CB  . PHE A 1 65  ? 3.92299   -1.14524  44.98210  1.000 37.57882 ?  63  PHE A CB  1 
ATOM   414  C CG  . PHE A 1 65  ? 4.88127   -2.20333  44.57980  1.000 38.88800 ?  63  PHE A CG  1 
ATOM   415  C CD1 . PHE A 1 65  ? 6.21034   -2.12091  44.95117  1.000 36.13987 ?  63  PHE A CD1 1 
ATOM   416  C CD2 . PHE A 1 65  ? 4.46666   -3.26275  43.79955  1.000 35.39709 ?  63  PHE A CD2 1 
ATOM   417  C CE1 . PHE A 1 65  ? 7.12905   -3.09610  44.55569  1.000 35.66251 ?  63  PHE A CE1 1 
ATOM   418  C CE2 . PHE A 1 65  ? 5.36044   -4.24649  43.41485  1.000 34.48079 ?  63  PHE A CE2 1 
ATOM   419  C CZ  . PHE A 1 65  ? 6.70773   -4.16370  43.79552  1.000 32.16721 ?  63  PHE A CZ  1 
ATOM   420  N N   . ILE A 1 66  ? 2.93014   0.31318   42.36705  1.000 33.96362 ?  64  ILE A N   1 
ATOM   421  C CA  . ILE A 1 66  ? 2.69942   0.30003   40.92125  1.000 30.18610 ?  64  ILE A CA  1 
ATOM   422  C C   . ILE A 1 66  ? 3.39827   1.46379   40.24719  1.000 31.74993 ?  64  ILE A C   1 
ATOM   423  O O   . ILE A 1 66  ? 3.96897   1.32285   39.15996  1.000 31.77590 ?  64  ILE A O   1 
ATOM   424  C CB  . ILE A 1 66  ? 1.18693   0.33128   40.61884  1.000 35.19131 ?  64  ILE A CB  1 
ATOM   425  C CG1 . ILE A 1 66  ? 0.52067   -0.96804  41.04497  1.000 36.11797 ?  64  ILE A CG1 1 
ATOM   426  C CG2 . ILE A 1 66  ? 0.92938   0.61262   39.13539  1.000 30.57116 ?  64  ILE A CG2 1 
ATOM   427  C CD1 . ILE A 1 66  ? 1.19764   -2.17152  40.46294  1.000 36.80299 ?  64  ILE A CD1 1 
ATOM   428  N N   . ILE A 1 67  ? 3.31557   2.64353   40.84833  1.000 30.08396 ?  65  ILE A N   1 
ATOM   429  C CA  . ILE A 1 67  ? 3.97084   3.81748   40.29086  1.000 31.52655 ?  65  ILE A CA  1 
ATOM   430  C C   . ILE A 1 67  ? 5.48727   3.62977   40.27801  1.000 34.12687 ?  65  ILE A C   1 
ATOM   431  O O   . ILE A 1 67  ? 6.16226   4.04374   39.33169  1.000 32.32595 ?  65  ILE A O   1 
ATOM   432  C CB  . ILE A 1 67  ? 3.54870   5.07430   41.08058  1.000 35.73916 ?  65  ILE A CB  1 
ATOM   433  C CG1 . ILE A 1 67  ? 2.29581   5.69183   40.44990  1.000 39.57534 ?  65  ILE A CG1 1 
ATOM   434  C CG2 . ILE A 1 67  ? 4.68036   6.08860   41.14119  1.000 38.43724 ?  65  ILE A CG2 1 
ATOM   435  C CD1 . ILE A 1 67  ? 1.60620   6.72539   41.33192  1.000 46.12790 ?  65  ILE A CD1 1 
ATOM   436  N N   . GLU A 1 68  ? 6.04695   2.99635   41.31377  1.000 35.36792 ?  66  GLU A N   1 
ATOM   437  C CA  . GLU A 1 68  ? 7.49192   2.77089   41.32316  1.000 35.21219 ?  66  GLU A CA  1 
ATOM   438  C C   . GLU A 1 68  ? 7.88635   1.72669   40.28612  1.000 32.48433 ?  66  GLU A C   1 
ATOM   439  O O   . GLU A 1 68  ? 8.92632   1.85937   39.63252  1.000 30.61964 ?  66  GLU A O   1 
ATOM   440  C CB  . GLU A 1 68  ? 7.96062   2.32927   42.70680  1.000 36.91065 ?  66  GLU A CB  1 
ATOM   441  C CG  . GLU A 1 68  ? 7.75768   3.38035   43.77176  1.000 39.38056 ?  66  GLU A CG  1 
ATOM   442  C CD  . GLU A 1 68  ? 8.27394   4.76921   43.39952  1.000 42.61026 ?  66  GLU A CD  1 
ATOM   443  O OE1 . GLU A 1 68  ? 9.39891   4.89277   42.83778  1.000 42.37288 ?  66  GLU A OE1 1 
ATOM   444  O OE2 . GLU A 1 68  ? 7.52878   5.74673   43.69395  1.000 43.06482 -1 66  GLU A OE2 1 
ATOM   445  N N   . CYS A 1 69  ? 7.05995   0.68804   40.12122  1.000 32.13314 ?  67  CYS A N   1 
ATOM   446  C CA  . CYS A 1 69  ? 7.29672   -0.31178  39.08269  1.000 32.22656 ?  67  CYS A CA  1 
ATOM   447  C C   . CYS A 1 69  ? 7.25648   0.30540   37.69965  1.000 31.07476 ?  67  CYS A C   1 
ATOM   448  O O   . CYS A 1 69  ? 8.08023   -0.01974  36.83793  1.000 29.29436 ?  67  CYS A O   1 
ATOM   449  C CB  . CYS A 1 69  ? 6.24940   -1.41758  39.17071  1.000 29.89136 ?  67  CYS A CB  1 
ATOM   450  S SG  . CYS A 1 69  ? 6.55612   -2.48652  40.53557  1.000 34.21332 ?  67  CYS A SG  1 
ATOM   451  N N   . LEU A 1 70  ? 6.29514   1.18651   37.46478  1.000 29.20598 ?  68  LEU A N   1 
ATOM   452  C CA  . LEU A 1 70  ? 6.15479   1.77604   36.14593  1.000 32.33891 ?  68  LEU A CA  1 
ATOM   453  C C   . LEU A 1 70  ? 7.29852   2.72858   35.85359  1.000 29.63174 ?  68  LEU A C   1 
ATOM   454  O O   . LEU A 1 70  ? 7.78100   2.78428   34.71936  1.000 28.61848 ?  68  LEU A O   1 
ATOM   455  C CB  . LEU A 1 70  ? 4.82008   2.50294   36.04079  1.000 28.36734 ?  68  LEU A CB  1 
ATOM   456  C CG  . LEU A 1 70  ? 4.49340   3.06328   34.66160  1.000 34.80201 ?  68  LEU A CG  1 
ATOM   457  C CD1 . LEU A 1 70  ? 3.84327   1.97165   33.78818  1.000 32.94971 ?  68  LEU A CD1 1 
ATOM   458  C CD2 . LEU A 1 70  ? 3.57446   4.29511   34.80202  1.000 33.11607 ?  68  LEU A CD2 1 
ATOM   459  N N   . ASP A 1 71  ? 7.73250   3.49412   36.86299  1.000 31.96764 ?  69  ASP A N   1 
ATOM   460  C CA  . ASP A 1 71  ? 8.88215   4.37888   36.68879  1.000 33.09122 ?  69  ASP A CA  1 
ATOM   461  C C   . ASP A 1 71  ? 10.12609  3.59770   36.31688  1.000 30.86300 ?  69  ASP A C   1 
ATOM   462  O O   . ASP A 1 71  ? 10.90775  4.03777   35.46870  1.000 30.33767 ?  69  ASP A O   1 
ATOM   463  C CB  . ASP A 1 71  ? 9.14640   5.18423   37.95339  1.000 32.78337 ?  69  ASP A CB  1 
ATOM   464  C CG  . ASP A 1 71  ? 8.30751   6.43283   38.02199  1.000 41.63859 ?  69  ASP A CG  1 
ATOM   465  O OD1 . ASP A 1 71  ? 7.56142   6.66042   37.04688  1.000 42.75590 ?  69  ASP A OD1 1 
ATOM   466  O OD2 . ASP A 1 71  ? 8.37875   7.16358   39.03820  1.000 44.92907 -1 69  ASP A OD2 1 
ATOM   467  N N   . MET A 1 72  ? 10.32688  2.43385   36.93472  1.000 30.08485 ?  70  MET A N   1 
ATOM   468  C CA  . MET A 1 72  ? 11.51854  1.65942   36.61333  1.000 31.59591 ?  70  MET A CA  1 
ATOM   469  C C   . MET A 1 72  ? 11.43600  1.08122   35.20329  1.000 29.35215 ?  70  MET A C   1 
ATOM   470  O O   . MET A 1 72  ? 12.40180  1.16519   34.43372  1.000 32.36818 ?  70  MET A O   1 
ATOM   471  C CB  . MET A 1 72  ? 11.73810  0.55692   37.65115  1.000 32.71410 ?  70  MET A CB  1 
ATOM   472  C CG  . MET A 1 72  ? 12.52055  -0.60743  37.09467  1.000 36.88509 ?  70  MET A CG  1 
ATOM   473  S SD  . MET A 1 72  ? 12.83964  -1.92087  38.25600  1.000 43.39065 ?  70  MET A SD  1 
ATOM   474  C CE  . MET A 1 72  ? 14.02335  -1.15510  39.35646  1.000 44.95147 ?  70  MET A CE  1 
ATOM   475  N N   . GLU A 1 73  ? 10.28602  0.51746   34.83287  1.000 31.26944 ?  71  GLU A N   1 
ATOM   476  C CA  . GLU A 1 73  ? 10.13266  -0.04835  33.49829  1.000 26.31245 ?  71  GLU A CA  1 
ATOM   477  C C   . GLU A 1 73  ? 10.34294  1.03003   32.43855  1.000 29.22014 ?  71  GLU A C   1 
ATOM   478  O O   . GLU A 1 73  ? 10.97919  0.78402   31.41139  1.000 29.09360 ?  71  GLU A O   1 
ATOM   479  C CB  . GLU A 1 73  ? 8.74235   -0.67029  33.36726  1.000 28.62404 ?  71  GLU A CB  1 
ATOM   480  C CG  . GLU A 1 73  ? 8.41209   -1.49810  32.11617  1.000 30.72065 ?  71  GLU A CG  1 
ATOM   481  C CD  . GLU A 1 73  ? 9.51983   -2.42677  31.65404  1.000 34.29198 ?  71  GLU A CD  1 
ATOM   482  O OE1 . GLU A 1 73  ? 10.28766  -2.92446  32.50438  1.000 36.84628 ?  71  GLU A OE1 1 
ATOM   483  O OE2 . GLU A 1 73  ? 9.57822   -2.72586  30.43934  1.000 36.38926 -1 71  GLU A OE2 1 
ATOM   484  N N   . ILE A 1 74  ? 9.83454   2.24167   32.68502  1.000 29.67043 ?  72  ILE A N   1 
ATOM   485  C CA  . ILE A 1 74  ? 10.02656  3.33882   31.73910  1.000 28.93946 ?  72  ILE A CA  1 
ATOM   486  C C   . ILE A 1 74  ? 11.50585  3.68360   31.62996  1.000 32.60571 ?  72  ILE A C   1 
ATOM   487  O O   . ILE A 1 74  ? 12.04689  3.84674   30.52443  1.000 27.81602 ?  72  ILE A O   1 
ATOM   488  C CB  . ILE A 1 74  ? 9.18765   4.56259   32.15398  1.000 27.64784 ?  72  ILE A CB  1 
ATOM   489  C CG1 . ILE A 1 74  ? 7.70994   4.32901   31.86143  1.000 28.18667 ?  72  ILE A CG1 1 
ATOM   490  C CG2 . ILE A 1 74  ? 9.64347   5.82215   31.40524  1.000 28.85046 ?  72  ILE A CG2 1 
ATOM   491  C CD1 . ILE A 1 74  ? 6.82315   5.34415   32.53372  1.000 28.75132 ?  72  ILE A CD1 1 
ATOM   492  N N   . ASN A 1 75  ? 12.18646  3.79290   32.77968  1.000 30.19533 ?  73  ASN A N   1 
ATOM   493  C CA  . ASN A 1 75  ? 13.62302  4.07015   32.75540  1.000 31.85936 ?  73  ASN A CA  1 
ATOM   494  C C   . ASN A 1 75  ? 14.39997  2.97284   32.04201  1.000 28.01158 ?  73  ASN A C   1 
ATOM   495  O O   . ASN A 1 75  ? 15.37272  3.25607   31.33584  1.000 28.71109 ?  73  ASN A O   1 
ATOM   496  C CB  . ASN A 1 75  ? 14.17365  4.23729   34.17168  1.000 32.64018 ?  73  ASN A CB  1 
ATOM   497  C CG  . ASN A 1 75  ? 13.72167  5.51730   34.81237  1.000 40.00014 ?  73  ASN A CG  1 
ATOM   498  O OD1 . ASN A 1 75  ? 13.46805  6.50673   34.11904  1.000 42.87760 ?  73  ASN A OD1 1 
ATOM   499  N ND2 . ASN A 1 75  ? 13.66537  5.53295   36.15029  1.000 41.44886 ?  73  ASN A ND2 1 
ATOM   500  N N   . ARG A 1 76  ? 14.02591  1.71617   32.26472  1.000 26.65919 ?  74  ARG A N   1 
ATOM   501  C CA  . ARG A 1 76  ? 14.70404  0.61189   31.60526  1.000 27.65092 ?  74  ARG A CA  1 
ATOM   502  C C   . ARG A 1 76  ? 14.49413  0.65879   30.10204  1.000 27.99164 ?  74  ARG A C   1 
ATOM   503  O O   . ARG A 1 76  ? 15.43075  0.40439   29.33403  1.000 24.31914 ?  74  ARG A O   1 
ATOM   504  C CB  . ARG A 1 76  ? 14.20168  -0.71632  32.16861  1.000 29.90030 ?  74  ARG A CB  1 
ATOM   505  C CG  . ARG A 1 76  ? 15.01345  -1.90360  31.69776  1.000 30.09920 ?  74  ARG A CG  1 
ATOM   506  C CD  . ARG A 1 76  ? 14.33761  -3.22497  32.00972  1.000 31.00602 ?  74  ARG A CD  1 
ATOM   507  N NE  . ARG A 1 76  ? 13.17371  -3.43686  31.15438  1.000 33.05748 ?  74  ARG A NE  1 
ATOM   508  C CZ  . ARG A 1 76  ? 13.22657  -3.69631  29.85417  1.000 32.22972 ?  74  ARG A CZ  1 
ATOM   509  N NH1 . ARG A 1 76  ? 14.38299  -3.84579  29.22144  1.000 29.76698 ?  74  ARG A NH1 1 
ATOM   510  N NH2 . ARG A 1 76  ? 12.09245  -3.83030  29.17277  1.000 26.32464 ?  74  ARG A NH2 1 
ATOM   511  N N   . LEU A 1 77  ? 13.25753  0.94076   29.66550  1.000 25.20069 ?  75  LEU A N   1 
ATOM   512  C CA  . LEU A 1 77  ? 12.97632  1.03269   28.24152  1.000 27.73714 ?  75  LEU A CA  1 
ATOM   513  C C   . LEU A 1 77  ? 13.72488  2.18549   27.61188  1.000 25.92146 ?  75  LEU A C   1 
ATOM   514  O O   . LEU A 1 77  ? 14.18183  2.07976   26.46777  1.000 25.60870 ?  75  LEU A O   1 
ATOM   515  C CB  . LEU A 1 77  ? 11.47626  1.20644   27.99739  1.000 25.66639 ?  75  LEU A CB  1 
ATOM   516  C CG  . LEU A 1 77  ? 10.64843  -0.02924  28.31451  1.000 28.56146 ?  75  LEU A CG  1 
ATOM   517  C CD1 . LEU A 1 77  ? 9.14882   0.37441   28.48845  1.000 28.16668 ?  75  LEU A CD1 1 
ATOM   518  C CD2 . LEU A 1 77  ? 10.84794  -1.13019  27.23766  1.000 26.51772 ?  75  LEU A CD2 1 
ATOM   519  N N   . LYS A 1 78  ? 13.80289  3.31718   28.30838  1.000 23.72818 ?  76  LYS A N   1 
ATOM   520  C CA  . LYS A 1 78  ? 14.56280  4.43996   27.77388  1.000 27.15175 ?  76  LYS A CA  1 
ATOM   521  C C   . LYS A 1 78  ? 16.03296  4.08194   27.64980  1.000 29.50833 ?  76  LYS A C   1 
ATOM   522  O O   . LYS A 1 78  ? 16.69722  4.48825   26.69546  1.000 28.89887 ?  76  LYS A O   1 
ATOM   523  C CB  . LYS A 1 78  ? 14.42262  5.66913   28.66082  1.000 30.40854 ?  76  LYS A CB  1 
ATOM   524  C CG  . LYS A 1 78  ? 13.03218  6.26158   28.76978  1.000 29.60000 ?  76  LYS A CG  1 
ATOM   525  C CD  . LYS A 1 78  ? 13.11541  7.51688   29.62484  1.000 31.11710 ?  76  LYS A CD  1 
ATOM   526  C CE  . LYS A 1 78  ? 12.07063  8.53311   29.24150  1.000 38.18898 ?  76  LYS A CE  1 
ATOM   527  N NZ  . LYS A 1 78  ? 11.91994  9.56016   30.31443  1.000 38.75420 ?  76  LYS A NZ  1 
ATOM   528  N N   . GLN A 1 79  ? 16.56093  3.31004   28.59233  1.000 28.51160 ?  77  GLN A N   1 
ATOM   529  C CA  . GLN A 1 79  ? 17.97783  2.98941   28.50338  1.000 28.74023 ?  77  GLN A CA  1 
ATOM   530  C C   . GLN A 1 79  ? 18.20795  1.89224   27.46418  1.000 27.35355 ?  77  GLN A C   1 
ATOM   531  O O   . GLN A 1 79  ? 19.18571  1.95109   26.72377  1.000 27.72378 ?  77  GLN A O   1 
ATOM   532  C CB  . GLN A 1 79  ? 18.50608  2.68659   29.92526  1.000 29.79281 ?  77  GLN A CB  1 
ATOM   533  C CG  . GLN A 1 79  ? 19.79703  1.88394   30.07633  1.000 36.39799 ?  77  GLN A CG  1 
ATOM   534  C CD  . GLN A 1 79  ? 19.87760  1.06910   31.37907  1.000 40.73304 ?  77  GLN A CD  1 
ATOM   535  O OE1 . GLN A 1 79  ? 19.17893  1.36863   32.35367  1.000 44.58153 ?  77  GLN A OE1 1 
ATOM   536  N NE2 . GLN A 1 79  ? 20.80105  0.10041   31.42935  1.000 38.09475 ?  77  GLN A NE2 1 
ATOM   537  N N   . SER A 1 80  ? 17.24249  0.98505   27.30787  1.000 27.75150 ?  78  SER A N   1 
ATOM   538  C CA  . SER A 1 80  ? 17.28502  -0.06521  26.28705  1.000 28.37833 ?  78  SER A CA  1 
ATOM   539  C C   . SER A 1 80  ? 17.30612  0.50098   24.86548  1.000 28.33900 ?  78  SER A C   1 
ATOM   540  O O   . SER A 1 80  ? 18.13791  0.10355   24.03974  1.000 30.88965 ?  78  SER A O   1 
ATOM   541  C CB  . SER A 1 80  ? 16.07550  -0.97677  26.45924  1.000 27.13902 ?  78  SER A CB  1 
ATOM   542  O OG  . SER A 1 80  ? 15.96016  -1.93356  25.41383  1.000 30.47407 ?  78  SER A OG  1 
ATOM   543  N N   . LEU A 1 81  ? 16.37898  1.40182   24.55476  1.000 26.43321 ?  79  LEU A N   1 
ATOM   544  C CA  . LEU A 1 81  ? 16.33166  2.00672   23.22249  1.000 29.41606 ?  79  LEU A CA  1 
ATOM   545  C C   . LEU A 1 81  ? 17.48015  2.99000   23.01166  1.000 30.37731 ?  79  LEU A C   1 
ATOM   546  O O   . LEU A 1 81  ? 18.10021  3.01885   21.93928  1.000 34.09084 ?  79  LEU A O   1 
ATOM   547  C CB  . LEU A 1 81  ? 14.99286  2.70522   23.03454  1.000 27.59945 ?  79  LEU A CB  1 
ATOM   548  C CG  . LEU A 1 81  ? 14.77896  3.31308   21.64558  1.000 30.66457 ?  79  LEU A CG  1 
ATOM   549  C CD1 . LEU A 1 81  ? 14.91845  2.28313   20.51827  1.000 28.14120 ?  79  LEU A CD1 1 
ATOM   550  C CD2 . LEU A 1 81  ? 13.44664  4.01226   21.58373  1.000 23.10328 ?  79  LEU A CD2 1 
ATOM   551  N N   . SER A 1 82  ? 17.78367  3.79983   24.03035  1.000 30.48601 ?  80  SER A N   1 
ATOM   552  C CA  . SER A 1 82  ? 18.87668  4.75514   23.93290  1.000 32.02663 ?  80  SER A CA  1 
ATOM   553  C C   . SER A 1 82  ? 20.20072  4.04664   23.64853  1.000 33.91377 ?  80  SER A C   1 
ATOM   554  O O   . SER A 1 82  ? 20.97223  4.47752   22.78214  1.000 34.86133 ?  80  SER A O   1 
ATOM   555  C CB  . SER A 1 82  ? 18.95235  5.56229   25.22896  1.000 31.33116 ?  80  SER A CB  1 
ATOM   556  O OG  . SER A 1 82  ? 19.89857  6.59850   25.13786  1.000 42.58550 ?  80  SER A OG  1 
ATOM   557  N N   . ASN A 1 83  ? 20.46238  2.93253   24.34586  1.000 32.30775 ?  81  ASN A N   1 
ATOM   558  C CA  . ASN A 1 83  ? 21.70454  2.18944   24.13769  1.000 32.13606 ?  81  ASN A CA  1 
ATOM   559  C C   . ASN A 1 83  ? 21.74207  1.49562   22.78178  1.000 34.30230 ?  81  ASN A C   1 
ATOM   560  O O   . ASN A 1 83  ? 22.80553  1.41306   22.15566  1.000 32.04624 ?  81  ASN A O   1 
ATOM   561  C CB  . ASN A 1 83  ? 21.90440  1.16251   25.24666  1.000 28.35570 ?  81  ASN A CB  1 
ATOM   562  C CG  . ASN A 1 83  ? 22.37279  1.79546   26.53160  1.000 33.86202 ?  81  ASN A CG  1 
ATOM   563  O OD1 . ASN A 1 83  ? 22.88201  2.91920   26.53074  1.000 34.15490 ?  81  ASN A OD1 1 
ATOM   564  N ND2 . ASN A 1 83  ? 22.22152  1.08320   27.63204  1.000 33.62676 ?  81  ASN A ND2 1 
ATOM   565  N N   . LEU A 1 84  ? 20.61178  0.95208   22.33638  1.000 29.57080 ?  82  LEU A N   1 
ATOM   566  C CA  . LEU A 1 84  ? 20.56094  0.29166   21.03907  1.000 30.37336 ?  82  LEU A CA  1 
ATOM   567  C C   . LEU A 1 84  ? 20.82635  1.28606   19.91027  1.000 33.39964 ?  82  LEU A C   1 
ATOM   568  O O   . LEU A 1 84  ? 21.64571  1.02389   19.01589  1.000 33.79708 ?  82  LEU A O   1 
ATOM   569  C CB  . LEU A 1 84  ? 19.19643  -0.39055  20.85312  1.000 29.08820 ?  82  LEU A CB  1 
ATOM   570  C CG  . LEU A 1 84  ? 19.07904  -1.26201  19.61117  1.000 27.63468 ?  82  LEU A CG  1 
ATOM   571  C CD1 . LEU A 1 84  ? 19.93920  -2.51828  19.78191  1.000 29.89565 ?  82  LEU A CD1 1 
ATOM   572  C CD2 . LEU A 1 84  ? 17.67257  -1.64943  19.31164  1.000 27.98572 ?  82  LEU A CD2 1 
ATOM   573  N N   . LEU A 1 85  ? 20.15840  2.44392   19.94909  1.000 29.84725 ?  83  LEU A N   1 
ATOM   574  C CA  . LEU A 1 85  ? 20.37903  3.47446   18.93509  1.000 32.71238 ?  83  LEU A CA  1 
ATOM   575  C C   . LEU A 1 85  ? 21.76934  4.07651   19.04009  1.000 35.77869 ?  83  LEU A C   1 
ATOM   576  O O   . LEU A 1 85  ? 22.39534  4.38200   18.01880  1.000 34.07544 ?  83  LEU A O   1 
ATOM   577  C CB  . LEU A 1 85  ? 19.33769  4.58149   19.06179  1.000 31.40156 ?  83  LEU A CB  1 
ATOM   578  C CG  . LEU A 1 85  ? 17.88772  4.14133   18.92388  1.000 30.67552 ?  83  LEU A CG  1 
ATOM   579  C CD1 . LEU A 1 85  ? 16.98977  5.35235   18.94448  1.000 31.53234 ?  83  LEU A CD1 1 
ATOM   580  C CD2 . LEU A 1 85  ? 17.72136  3.37082   17.63928  1.000 31.25561 ?  83  LEU A CD2 1 
ATOM   581  N N   . GLY A 1 86  ? 22.25418  4.28986   20.26512  1.000 36.47149 ?  84  GLY A N   1 
ATOM   582  C CA  . GLY A 1 86  ? 23.60115  4.79853   20.47200  1.000 37.17077 ?  84  GLY A CA  1 
ATOM   583  C C   . GLY A 1 86  ? 24.69777  3.93485   19.87683  1.000 37.41503 ?  84  GLY A C   1 
ATOM   584  O O   . GLY A 1 86  ? 25.83646  4.40375   19.76450  1.000 40.28112 ?  84  GLY A O   1 
ATOM   585  N N   . GLN A 1 87  ? 24.38036  2.69834   19.47944  1.000 40.17304 ?  85  GLN A N   1 
ATOM   586  C CA  . GLN A 1 87  ? 25.36181  1.77877   18.91362  1.000 40.77807 ?  85  GLN A CA  1 
ATOM   587  C C   . GLN A 1 87  ? 25.62062  1.99457   17.42764  1.000 38.98279 ?  85  GLN A C   1 
ATOM   588  O O   . GLN A 1 87  ? 26.63695  1.51270   16.92141  1.000 41.27302 ?  85  GLN A O   1 
ATOM   589  C CB  . GLN A 1 87  ? 24.90729  0.33690   19.11424  1.000 40.35745 ?  85  GLN A CB  1 
ATOM   590  C CG  . GLN A 1 87  ? 25.07048  -0.16495  20.52505  1.000 41.12130 ?  85  GLN A CG  1 
ATOM   591  C CD  . GLN A 1 87  ? 25.04199  -1.66970  20.59032  1.000 39.41945 ?  85  GLN A CD  1 
ATOM   592  O OE1 . GLN A 1 87  ? 25.91066  -2.29339  21.20286  1.000 45.12395 ?  85  GLN A OE1 1 
ATOM   593  N NE2 . GLN A 1 87  ? 24.04981  -2.26737  19.93397  1.000 39.66373 ?  85  GLN A NE2 1 
ATOM   594  N N   . CYS A 1 88  ? 24.74201  2.68165   16.71252  1.000 37.93033 ?  86  CYS A N   1 
ATOM   595  C CA  . CYS A 1 88  ? 24.94230  2.83461   15.27930  1.000 40.78215 ?  86  CYS A CA  1 
ATOM   596  C C   . CYS A 1 88  ? 25.91473  3.97327   14.97247  1.000 41.63443 ?  86  CYS A C   1 
ATOM   597  O O   . CYS A 1 88  ? 26.06195  4.91949   15.75121  1.000 41.00793 ?  86  CYS A O   1 
ATOM   598  C CB  . CYS A 1 88  ? 23.61222  3.07663   14.56483  1.000 40.54459 ?  86  CYS A CB  1 
ATOM   599  S SG  . CYS A 1 88  ? 22.33980  1.88798   14.95207  1.000 43.86510 ?  86  CYS A SG  1 
ATOM   600  N N   . GLY A 1 89  ? 26.58296  3.86794   13.81785  1.000 41.99404 ?  87  GLY A N   1 
ATOM   601  C CA  . GLY A 1 89  ? 27.48918  4.92557   13.39243  1.000 44.21538 ?  87  GLY A CA  1 
ATOM   602  C C   . GLY A 1 89  ? 26.76282  6.24135   13.17722  1.000 49.07434 ?  87  GLY A C   1 
ATOM   603  O O   . GLY A 1 89  ? 25.59056  6.27537   12.79791  1.000 46.12650 ?  87  GLY A O   1 
ATOM   604  N N   . LYS A 1 90  ? 27.48207  7.34545   13.41841  1.000 51.03455 ?  88  LYS A N   1 
ATOM   605  C CA  . LYS A 1 90  ? 26.84903  8.66400   13.40282  1.000 49.89911 ?  88  LYS A CA  1 
ATOM   606  C C   . LYS A 1 90  ? 26.12065  8.92021   12.08888  1.000 52.08503 ?  88  LYS A C   1 
ATOM   607  O O   . LYS A 1 90  ? 25.03028  9.50270   12.07219  1.000 49.29099 ?  88  LYS A O   1 
ATOM   608  C CB  . LYS A 1 90  ? 27.89436  9.75294   13.65236  1.000 50.24247 ?  88  LYS A CB  1 
ATOM   609  N N   . ASP A 1 91  ? 26.69834  8.47422   10.97773  1.000 53.84965 ?  89  ASP A N   1 
ATOM   610  C CA  . ASP A 1 91  ? 26.08974  8.70425   9.67397   1.000 53.81065 ?  89  ASP A CA  1 
ATOM   611  C C   . ASP A 1 91  ? 25.01735  7.67180   9.31810   1.000 49.83432 ?  89  ASP A C   1 
ATOM   612  O O   . ASP A 1 91  ? 24.30596  7.85368   8.31981   1.000 50.50418 ?  89  ASP A O   1 
ATOM   613  C CB  . ASP A 1 91  ? 27.19304  8.72481   8.59875   1.000 49.00077 ?  89  ASP A CB  1 
ATOM   614  N N   . ASP A 1 92  ? 24.85639  6.61596   10.11786  1.000 46.03109 ?  90  ASP A N   1 
ATOM   615  C CA  . ASP A 1 92  ? 24.24647  5.37701   9.63426   1.000 44.94630 ?  90  ASP A CA  1 
ATOM   616  C C   . ASP A 1 92  ? 22.73129  5.39554   9.82201   1.000 41.69698 ?  90  ASP A C   1 
ATOM   617  O O   . ASP A 1 92  ? 22.17045  4.74708   10.70405  1.000 37.03886 ?  90  ASP A O   1 
ATOM   618  C CB  . ASP A 1 92  ? 24.88114  4.17898   10.32818  1.000 43.23397 ?  90  ASP A CB  1 
ATOM   619  C CG  . ASP A 1 92  ? 24.65647  2.88743   9.56467   1.000 43.27714 ?  90  ASP A CG  1 
ATOM   620  O OD1 . ASP A 1 92  ? 23.68349  2.82916   8.77365   1.000 39.70378 ?  90  ASP A OD1 1 
ATOM   621  O OD2 . ASP A 1 92  ? 25.43796  1.93416   9.76879   1.000 42.91609 -1 90  ASP A OD2 1 
ATOM   622  N N   . HIS A 1 93  ? 22.05281  6.11212   8.92611   1.000 42.42278 ?  91  HIS A N   1 
ATOM   623  C CA  . HIS A 1 93  ? 20.61996  6.31786   9.09555   1.000 42.57378 ?  91  HIS A CA  1 
ATOM   624  C C   . HIS A 1 93  ? 19.83189  5.03297   8.87321   1.000 39.81469 ?  91  HIS A C   1 
ATOM   625  O O   . HIS A 1 93  ? 18.84580  4.78469   9.57588   1.000 34.38827 ?  91  HIS A O   1 
ATOM   626  C CB  . HIS A 1 93  ? 20.15407  7.43832   8.16972   1.000 46.77642 ?  91  HIS A CB  1 
ATOM   627  C CG  . HIS A 1 93  ? 20.88496  8.72241   8.40030   1.000 45.83569 ?  91  HIS A CG  1 
ATOM   628  N ND1 . HIS A 1 93  ? 20.72619  9.46671   9.54772   1.000 46.05587 ?  91  HIS A ND1 1 
ATOM   629  C CD2 . HIS A 1 93  ? 21.83677  9.35280   7.67112   1.000 51.95632 ?  91  HIS A CD2 1 
ATOM   630  C CE1 . HIS A 1 93  ? 21.51908  10.52126  9.49962   1.000 50.12854 ?  91  HIS A CE1 1 
ATOM   631  N NE2 . HIS A 1 93  ? 22.21020  10.47176  8.37567   1.000 50.16079 ?  91  HIS A NE2 1 
ATOM   632  N N   . THR A 1 94  ? 20.25252  4.19307   7.92307   1.000 36.30368 ?  92  THR A N   1 
ATOM   633  C CA  . THR A 1 94  ? 19.59339  2.89866   7.76119   1.000 38.09592 ?  92  THR A CA  1 
ATOM   634  C C   . THR A 1 94  ? 19.66246  2.08058   9.05114   1.000 38.35992 ?  92  THR A C   1 
ATOM   635  O O   . THR A 1 94  ? 18.64714  1.55024   9.52093   1.000 34.84718 ?  92  THR A O   1 
ATOM   636  C CB  . THR A 1 94  ? 20.21090  2.12841   6.59378   1.000 41.39307 ?  92  THR A CB  1 
ATOM   637  O OG1 . THR A 1 94  ? 20.34666  3.00249   5.47084   1.000 45.68602 ?  92  THR A OG1 1 
ATOM   638  C CG2 . THR A 1 94  ? 19.33864  0.94099   6.20143   1.000 36.64156 ?  92  THR A CG2 1 
ATOM   639  N N   . SER A 1 95  ? 20.84317  2.00978   9.66510   1.000 35.46874 ?  93  SER A N   1 
ATOM   640  C CA  . SER A 1 95  ? 20.99276  1.18521   10.86063  1.000 36.75775 ?  93  SER A CA  1 
ATOM   641  C C   . SER A 1 95  ? 20.18076  1.73481   12.02315  1.000 34.47414 ?  93  SER A C   1 
ATOM   642  O O   . SER A 1 95  ? 19.62261  0.96399   12.80236  1.000 31.66380 ?  93  SER A O   1 
ATOM   643  C CB  . SER A 1 95  ? 22.46164  1.08292   11.25566  1.000 37.62363 ?  93  SER A CB  1 
ATOM   644  O OG  . SER A 1 95  ? 23.13728  0.17679   10.39981  1.000 41.78316 ?  93  SER A OG  1 
ATOM   645  N N   . ILE A 1 96  ? 20.13381  3.06006   12.17700  1.000 33.94211 ?  94  ILE A N   1 
ATOM   646  C CA  . ILE A 1 96  ? 19.25714  3.66279   13.17690  1.000 34.60273 ?  94  ILE A CA  1 
ATOM   647  C C   . ILE A 1 96  ? 17.82240  3.21401   12.94419  1.000 32.54936 ?  94  ILE A C   1 
ATOM   648  O O   . ILE A 1 96  ? 17.10700  2.80755   13.86611  1.000 28.62867 ?  94  ILE A O   1 
ATOM   649  C CB  . ILE A 1 96  ? 19.38053  5.19632   13.12837  1.000 34.65030 ?  94  ILE A CB  1 
ATOM   650  C CG1 . ILE A 1 96  ? 20.71393  5.66291   13.72253  1.000 34.94171 ?  94  ILE A CG1 1 
ATOM   651  C CG2 . ILE A 1 96  ? 18.24058  5.84315   13.89778  1.000 34.57479 ?  94  ILE A CG2 1 
ATOM   652  C CD1 . ILE A 1 96  ? 20.92365  5.21203   15.12295  1.000 37.00166 ?  94  ILE A CD1 1 
ATOM   653  N N   . LEU A 1 97  ? 17.39312  3.24816   11.69219  1.000 33.59662 ?  95  LEU A N   1 
ATOM   654  C CA  . LEU A 1 97  ? 16.00597  2.96419   11.38087  1.000 30.02912 ?  95  LEU A CA  1 
ATOM   655  C C   . LEU A 1 97  ? 15.71232  1.47026   11.55554  1.000 31.10442 ?  95  LEU A C   1 
ATOM   656  O O   . LEU A 1 97  ? 14.68205  1.09134   12.13906  1.000 26.63989 ?  95  LEU A O   1 
ATOM   657  C CB  . LEU A 1 97  ? 15.74344  3.49730   9.97011   1.000 35.45342 ?  95  LEU A CB  1 
ATOM   658  C CG  . LEU A 1 97  ? 14.42568  3.55884   9.20434   1.000 37.72684 ?  95  LEU A CG  1 
ATOM   659  C CD1 . LEU A 1 97  ? 14.13969  2.27957   8.53317   1.000 39.26511 ?  95  LEU A CD1 1 
ATOM   660  C CD2 . LEU A 1 97  ? 13.30821  3.92668   10.12826  1.000 29.82566 ?  95  LEU A CD2 1 
ATOM   661  N N   . LYS A 1 98  ? 16.65046  0.60983   11.14843  1.000 30.62365 ?  96  LYS A N   1 
ATOM   662  C CA  . LYS A 1 98  ? 16.48836  -0.82940  11.35734  1.000 30.66161 ?  96  LYS A CA  1 
ATOM   663  C C   . LYS A 1 98  ? 16.44810  -1.19284  12.83303  1.000 28.20374 ?  96  LYS A C   1 
ATOM   664  O O   . LYS A 1 98  ? 15.72574  -2.11722  13.23405  1.000 29.52963 ?  96  LYS A O   1 
ATOM   665  C CB  . LYS A 1 98  ? 17.62720  -1.59459  10.69589  1.000 32.39196 ?  96  LYS A CB  1 
ATOM   666  C CG  . LYS A 1 98  ? 17.38053  -3.09785  10.60352  1.000 31.25304 ?  96  LYS A CG  1 
ATOM   667  C CD  . LYS A 1 98  ? 18.42512  -3.74082  9.71905   1.000 34.89788 ?  96  LYS A CD  1 
ATOM   668  N N   . SER A 1 99  ? 17.25196  -0.51139  13.64847  1.000 27.85274 ?  97  SER A N   1 
ATOM   669  C CA  . SER A 1 99  ? 17.27491  -0.81304  15.07266  1.000 29.11494 ?  97  SER A CA  1 
ATOM   670  C C   . SER A 1 99  ? 15.96353  -0.40348  15.73502  1.000 28.49776 ?  97  SER A C   1 
ATOM   671  O O   . SER A 1 99  ? 15.46206  -1.09817  16.62212  1.000 26.94969 ?  97  SER A O   1 
ATOM   672  C CB  . SER A 1 99  ? 18.45899  -0.09855  15.72500  1.000 29.53068 ?  97  SER A CB  1 
ATOM   673  O OG  . SER A 1 99  ? 19.67451  -0.68926  15.29137  1.000 32.51136 ?  97  SER A OG  1 
ATOM   674  N N   . PHE A 1 100 ? 15.41997  0.74555   15.34281  1.000 26.38288 ?  98  PHE A N   1 
ATOM   675  C CA  . PHE A 1 100 ? 14.16092  1.20068   15.90544  1.000 25.63087 ?  98  PHE A CA  1 
ATOM   676  C C   . PHE A 1 100 ? 13.04088  0.22926   15.56284  1.000 24.89479 ?  98  PHE A C   1 
ATOM   677  O O   . PHE A 1 100 ? 12.19329  -0.07937  16.40697  1.000 25.24788 ?  98  PHE A O   1 
ATOM   678  C CB  . PHE A 1 100 ? 13.87386  2.60311   15.38013  1.000 26.44697 ?  98  PHE A CB  1 
ATOM   679  C CG  . PHE A 1 100 ? 12.72513  3.28935   16.05060  1.000 29.01777 ?  98  PHE A CG  1 
ATOM   680  C CD1 . PHE A 1 100 ? 12.88022  3.87565   17.29555  1.000 27.80507 ?  98  PHE A CD1 1 
ATOM   681  C CD2 . PHE A 1 100 ? 11.50688  3.38241   15.41769  1.000 26.57535 ?  98  PHE A CD2 1 
ATOM   682  C CE1 . PHE A 1 100 ? 11.83673  4.52896   17.89833  1.000 25.04139 ?  98  PHE A CE1 1 
ATOM   683  C CE2 . PHE A 1 100 ? 10.44164  4.03976   16.00305  1.000 27.12745 ?  98  PHE A CE2 1 
ATOM   684  C CZ  . PHE A 1 100 ? 10.59367  4.61287   17.24983  1.000 30.92018 ?  98  PHE A CZ  1 
ATOM   685  N N   . TYR A 1 101 ? 13.04277  -0.27529  14.32885  1.000 23.35492 ?  99  TYR A N   1 
ATOM   686  C CA  . TYR A 1 101 ? 12.09849  -1.30737  13.91785  1.000 26.78174 ?  99  TYR A CA  1 
ATOM   687  C C   . TYR A 1 101 ? 12.26534  -2.56858  14.75956  1.000 24.28644 ?  99  TYR A C   1 
ATOM   688  O O   . TYR A 1 101 ? 11.29407  -3.09643  15.32420  1.000 22.17204 ?  99  TYR A O   1 
ATOM   689  C CB  . TYR A 1 101 ? 12.28802  -1.61073  12.41987  1.000 23.05987 ?  99  TYR A CB  1 
ATOM   690  C CG  . TYR A 1 101 ? 11.54646  -2.83444  11.97899  1.000 25.99983 ?  99  TYR A CG  1 
ATOM   691  C CD1 . TYR A 1 101 ? 10.18673  -2.77414  11.73944  1.000 25.77771 ?  99  TYR A CD1 1 
ATOM   692  C CD2 . TYR A 1 101 ? 12.19785  -4.05767  11.81139  1.000 27.65295 ?  99  TYR A CD2 1 
ATOM   693  C CE1 . TYR A 1 101 ? 9.47791   -3.89067  11.34860  1.000 27.94044 ?  99  TYR A CE1 1 
ATOM   694  C CE2 . TYR A 1 101 ? 11.49000  -5.19398  11.44059  1.000 27.40107 ?  99  TYR A CE2 1 
ATOM   695  C CZ  . TYR A 1 101 ? 10.12648  -5.09100  11.20821  1.000 29.25745 ?  99  TYR A CZ  1 
ATOM   696  O OH  . TYR A 1 101 ? 9.37783   -6.17142  10.82452  1.000 32.69085 ?  99  TYR A OH  1 
ATOM   697  N N   . GLN A 1 102 ? 13.50409  -3.05316  14.86774  1.000 25.69781 ?  100 GLN A N   1 
ATOM   698  C CA  . GLN A 1 102 ? 13.76300  -4.34223  15.49514  1.000 26.18892 ?  100 GLN A CA  1 
ATOM   699  C C   . GLN A 1 102 ? 13.44236  -4.30354  16.98033  1.000 23.12358 ?  100 GLN A C   1 
ATOM   700  O O   . GLN A 1 102 ? 12.97561  -5.29451  17.55421  1.000 27.47823 ?  100 GLN A O   1 
ATOM   701  C CB  . GLN A 1 102 ? 15.23105  -4.71735  15.25582  1.000 28.41468 ?  100 GLN A CB  1 
ATOM   702  C CG  . GLN A 1 102 ? 15.54889  -6.16132  15.52400  1.000 35.07739 ?  100 GLN A CG  1 
ATOM   703  C CD  . GLN A 1 102 ? 15.09067  -7.05792  14.38683  1.000 37.33111 ?  100 GLN A CD  1 
ATOM   704  O OE1 . GLN A 1 102 ? 14.11286  -7.79478  14.51053  1.000 39.91369 ?  100 GLN A OE1 1 
ATOM   705  N NE2 . GLN A 1 102 ? 15.78940  -6.97309  13.25169  1.000 48.33023 ?  100 GLN A NE2 1 
ATOM   706  N N   . TRP A 1 103 ? 13.67039  -3.16139  17.61093  1.000 23.90890 ?  101 TRP A N   1 
ATOM   707  C CA  . TRP A 1 103 ? 13.34898  -3.00434  19.02312  1.000 25.76114 ?  101 TRP A CA  1 
ATOM   708  C C   . TRP A 1 103 ? 11.86123  -3.25081  19.27233  1.000 25.96945 ?  101 TRP A C   1 
ATOM   709  O O   . TRP A 1 103 ? 11.47887  -3.93944  20.23439  1.000 24.62145 ?  101 TRP A O   1 
ATOM   710  C CB  . TRP A 1 103 ? 13.77078  -1.59857  19.44822  1.000 25.09097 ?  101 TRP A CB  1 
ATOM   711  C CG  . TRP A 1 103 ? 13.78231  -1.33190  20.90930  1.000 25.15915 ?  101 TRP A CG  1 
ATOM   712  C CD1 . TRP A 1 103 ? 14.77117  -1.64847  21.80490  1.000 27.84587 ?  101 TRP A CD1 1 
ATOM   713  C CD2 . TRP A 1 103 ? 12.77488  -0.64003  21.64497  1.000 24.76509 ?  101 TRP A CD2 1 
ATOM   714  N NE1 . TRP A 1 103 ? 14.42168  -1.20885  23.06247  1.000 27.51133 ?  101 TRP A NE1 1 
ATOM   715  C CE2 . TRP A 1 103 ? 13.19811  -0.58778  22.98558  1.000 24.55949 ?  101 TRP A CE2 1 
ATOM   716  C CE3 . TRP A 1 103 ? 11.52713  -0.08443  21.29825  1.000 27.21160 ?  101 TRP A CE3 1 
ATOM   717  C CZ2 . TRP A 1 103 ? 12.43557  0.01542   23.98197  1.000 29.87924 ?  101 TRP A CZ2 1 
ATOM   718  C CZ3 . TRP A 1 103 ? 10.77235  0.51772   22.28192  1.000 25.96279 ?  101 TRP A CZ3 1 
ATOM   719  C CH2 . TRP A 1 103 ? 11.22709  0.55987   23.61726  1.000 29.17979 ?  101 TRP A CH2 1 
ATOM   720  N N   . HIS A 1 104 ? 11.01178  -2.69570  18.40798  1.000 22.14669 ?  102 HIS A N   1 
ATOM   721  C CA  . HIS A 1 104 ? 9.57088   -2.88815  18.52346  1.000 21.49198 ?  102 HIS A CA  1 
ATOM   722  C C   . HIS A 1 104 ? 9.17214   -4.33658  18.25418  1.000 23.39476 ?  102 HIS A C   1 
ATOM   723  O O   . HIS A 1 104 ? 8.36412   -4.91237  18.98970  1.000 23.74685 ?  102 HIS A O   1 
ATOM   724  C CB  . HIS A 1 104 ? 8.84425   -1.94451  17.56302  1.000 22.28851 ?  102 HIS A CB  1 
ATOM   725  C CG  . HIS A 1 104 ? 8.84268   -0.53026  18.01683  1.000 22.15071 ?  102 HIS A CG  1 
ATOM   726  N ND1 . HIS A 1 104 ? 9.87154   0.33990   17.74189  1.000 22.84569 ?  102 HIS A ND1 1 
ATOM   727  C CD2 . HIS A 1 104 ? 7.95392   0.15915   18.76724  1.000 24.38603 ?  102 HIS A CD2 1 
ATOM   728  C CE1 . HIS A 1 104 ? 9.62142   1.50756   18.30597  1.000 23.62092 ?  102 HIS A CE1 1 
ATOM   729  N NE2 . HIS A 1 104 ? 8.45638   1.42684   18.92065  1.000 24.47804 ?  102 HIS A NE2 1 
ATOM   730  N N   . VAL A 1 105 ? 9.70531   -4.93935  17.18953  1.000 23.68438 ?  103 VAL A N   1 
ATOM   731  C CA  . VAL A 1 105 ? 9.45238   -6.35970  16.95901  1.000 25.88887 ?  103 VAL A CA  1 
ATOM   732  C C   . VAL A 1 105 ? 9.91352   -7.19258  18.16044  1.000 28.89431 ?  103 VAL A C   1 
ATOM   733  O O   . VAL A 1 105 ? 9.20570   -8.10050  18.61710  1.000 29.02849 ?  103 VAL A O   1 
ATOM   734  C CB  . VAL A 1 105 ? 10.12903  -6.81107  15.65300  1.000 28.31453 ?  103 VAL A CB  1 
ATOM   735  C CG1 . VAL A 1 105 ? 10.06814  -8.30764  15.49359  1.000 31.39231 ?  103 VAL A CG1 1 
ATOM   736  C CG2 . VAL A 1 105 ? 9.46307   -6.14507  14.44688  1.000 29.33260 ?  103 VAL A CG2 1 
ATOM   737  N N   . ASP A 1 106 ? 11.09393  -6.88140  18.69958  1.000 28.10115 ?  104 ASP A N   1 
ATOM   738  C CA  . ASP A 1 106 ? 11.63742  -7.64636  19.81890  1.000 31.05751 ?  104 ASP A CA  1 
ATOM   739  C C   . ASP A 1 106 ? 10.77463  -7.52427  21.06638  1.000 31.87105 ?  104 ASP A C   1 
ATOM   740  O O   . ASP A 1 106 ? 10.71705  -8.46347  21.86258  1.000 35.19526 ?  104 ASP A O   1 
ATOM   741  C CB  . ASP A 1 106 ? 13.06389  -7.19317  20.13950  1.000 31.59105 ?  104 ASP A CB  1 
ATOM   742  C CG  . ASP A 1 106 ? 14.08839  -7.65375  19.10300  1.000 33.83317 ?  104 ASP A CG  1 
ATOM   743  O OD1 . ASP A 1 106 ? 13.78994  -8.54871  18.27949  1.000 31.79058 ?  104 ASP A OD1 1 
ATOM   744  O OD2 . ASP A 1 106 ? 15.24350  -7.14633  19.15447  1.000 38.82464 -1 104 ASP A OD2 1 
ATOM   745  N N   . LEU A 1 107 ? 10.10517  -6.38162  21.26403  1.000 31.13721 ?  105 LEU A N   1 
ATOM   746  C CA  . LEU A 1 107 ? 9.15032   -6.26174  22.36278  1.000 29.92895 ?  105 LEU A CA  1 
ATOM   747  C C   . LEU A 1 107 ? 7.94616   -7.16917  22.16270  1.000 34.10296 ?  105 LEU A C   1 
ATOM   748  O O   . LEU A 1 107 ? 7.50151   -7.83876  23.10149  1.000 36.91971 ?  105 LEU A O   1 
ATOM   749  C CB  . LEU A 1 107 ? 8.68219   -4.82080  22.51093  1.000 28.28072 ?  105 LEU A CB  1 
ATOM   750  C CG  . LEU A 1 107 ? 9.63683   -3.86004  23.18133  1.000 27.40022 ?  105 LEU A CG  1 
ATOM   751  C CD1 . LEU A 1 107 ? 9.06318   -2.46826  23.08318  1.000 26.02849 ?  105 LEU A CD1 1 
ATOM   752  C CD2 . LEU A 1 107 ? 9.72862   -4.31104  24.62043  1.000 32.11959 ?  105 LEU A CD2 1 
ATOM   753  N N   . ALA A 1 108 ? 7.38744   -7.18628  20.95402  1.000 30.04773 ?  106 ALA A N   1 
ATOM   754  C CA  . ALA A 1 108 ? 6.09531   -7.81627  20.72948  1.000 33.45586 ?  106 ALA A CA  1 
ATOM   755  C C   . ALA A 1 108 ? 6.18235   -9.24307  20.21051  1.000 35.47286 ?  106 ALA A C   1 
ATOM   756  O O   . ALA A 1 108 ? 5.16981   -9.94892  20.22463  1.000 37.87252 ?  106 ALA A O   1 
ATOM   757  C CB  . ALA A 1 108 ? 5.26101   -6.97816  19.75024  1.000 31.50693 ?  106 ALA A CB  1 
ATOM   758  N N   . TYR A 1 109 ? 7.33443   -9.69250  19.73994  1.000 35.35439 ?  107 TYR A N   1 
ATOM   759  C CA  . TYR A 1 109 ? 7.40313   -11.00443 19.09669  1.000 38.45426 ?  107 TYR A CA  1 
ATOM   760  C C   . TYR A 1 109 ? 7.88109   -12.06455 20.08584  1.000 41.20528 ?  107 TYR A C   1 
ATOM   761  O O   . TYR A 1 109 ? 8.88148   -12.75164 19.86935  1.000 49.15662 ?  107 TYR A O   1 
ATOM   762  C CB  . TYR A 1 109 ? 8.29738   -10.94658 17.86315  1.000 39.96788 ?  107 TYR A CB  1 
ATOM   763  N N   . ARG A 1 110 ? 7.14791   -12.19162 21.18984  1.000 41.97831 ?  108 ARG A N   1 
ATOM   764  C CA  . ARG A 1 110 ? 7.41074   -13.21582 22.18838  1.000 43.52831 ?  108 ARG A CA  1 
ATOM   765  C C   . ARG A 1 110 ? 6.15180   -14.05019 22.39207  1.000 43.44537 ?  108 ARG A C   1 
ATOM   766  O O   . ARG A 1 110 ? 5.03987   -13.57274 22.17224  1.000 41.84692 ?  108 ARG A O   1 
ATOM   767  C CB  . ARG A 1 110 ? 7.85152   -12.60448 23.51790  1.000 45.79485 ?  108 ARG A CB  1 
ATOM   768  C CG  . ARG A 1 110 ? 7.15249   -11.30367 23.88486  1.000 43.67346 ?  108 ARG A CG  1 
ATOM   769  C CD  . ARG A 1 110 ? 7.72535   -10.75041 25.19300  1.000 43.63107 ?  108 ARG A CD  1 
ATOM   770  N NE  . ARG A 1 110 ? 6.73455   -10.01880 25.98270  1.000 44.74896 ?  108 ARG A NE  1 
ATOM   771  C CZ  . ARG A 1 110 ? 6.73167   -8.70550  26.18935  1.000 43.66599 ?  108 ARG A CZ  1 
ATOM   772  N NH1 . ARG A 1 110 ? 7.63933   -7.90827  25.63902  1.000 39.51946 ?  108 ARG A NH1 1 
ATOM   773  N NH2 . ARG A 1 110 ? 5.80969   -8.17835  26.99245  1.000 42.36494 ?  108 ARG A NH2 1 
ATOM   774  N N   . GLU A 1 111 ? 6.33025   -15.30820 22.79763  1.000 46.38666 ?  109 GLU A N   1 
ATOM   775  C CA  . GLU A 1 111 ? 5.18202   -16.16902 23.05542  1.000 43.42573 ?  109 GLU A CA  1 
ATOM   776  C C   . GLU A 1 111 ? 4.32278   -15.58428 24.17041  1.000 42.87034 ?  109 GLU A C   1 
ATOM   777  O O   . GLU A 1 111 ? 4.83559   -15.02346 25.14538  1.000 43.47315 ?  109 GLU A O   1 
ATOM   778  C CB  . GLU A 1 111 ? 5.63486   -17.58083 23.42837  1.000 47.20928 ?  109 GLU A CB  1 
ATOM   779  N N   . GLY A 1 112 ? 3.00503   -15.68700 24.00624  1.000 37.85690 ?  110 GLY A N   1 
ATOM   780  C CA  . GLY A 1 112 ? 2.08731   -15.20220 25.01579  1.000 40.00286 ?  110 GLY A CA  1 
ATOM   781  C C   . GLY A 1 112 ? 1.92041   -13.69908 25.08115  1.000 38.87044 ?  110 GLY A C   1 
ATOM   782  O O   . GLY A 1 112 ? 1.31805   -13.20134 26.03938  1.000 36.97770 ?  110 GLY A O   1 
ATOM   783  N N   . TYR A 1 113 ? 2.42586   -12.96282 24.09477  1.000 35.79381 ?  111 TYR A N   1 
ATOM   784  C CA  . TYR A 1 113 ? 2.30204   -11.51084 24.09226  1.000 34.72986 ?  111 TYR A CA  1 
ATOM   785  C C   . TYR A 1 113 ? 0.84183   -11.07753 24.13222  1.000 35.26627 ?  111 TYR A C   1 
ATOM   786  O O   . TYR A 1 113 ? 0.00010   -11.58045 23.37962  1.000 37.56675 ?  111 TYR A O   1 
ATOM   787  C CB  . TYR A 1 113 ? 2.98168   -10.93339 22.85551  1.000 34.31277 ?  111 TYR A CB  1 
ATOM   788  C CG  . TYR A 1 113 ? 3.03266   -9.42852  22.83019  1.000 32.19794 ?  111 TYR A CG  1 
ATOM   789  C CD1 . TYR A 1 113 ? 3.89142   -8.73401  23.67313  1.000 30.88889 ?  111 TYR A CD1 1 
ATOM   790  C CD2 . TYR A 1 113 ? 2.25432   -8.70149  21.93779  1.000 32.47573 ?  111 TYR A CD2 1 
ATOM   791  C CE1 . TYR A 1 113 ? 3.94887   -7.36961  23.65203  1.000 29.21691 ?  111 TYR A CE1 1 
ATOM   792  C CE2 . TYR A 1 113 ? 2.31973   -7.32976  21.89705  1.000 29.26537 ?  111 TYR A CE2 1 
ATOM   793  C CZ  . TYR A 1 113 ? 3.16543   -6.67009  22.76690  1.000 28.85456 ?  111 TYR A CZ  1 
ATOM   794  O OH  . TYR A 1 113 ? 3.22841   -5.29473  22.72690  1.000 24.35620 ?  111 TYR A OH  1 
ATOM   795  N N   . ASN A 1 114 ? 0.54069   -10.14385 25.03005  1.000 32.85764 ?  112 ASN A N   1 
ATOM   796  C CA  . ASN A 1 114 ? -0.78380  -9.55465  25.12050  1.000 30.50003 ?  112 ASN A CA  1 
ATOM   797  C C   . ASN A 1 114 ? -0.68260  -8.08101  25.46786  1.000 30.45737 ?  112 ASN A C   1 
ATOM   798  O O   . ASN A 1 114 ? -1.55488  -7.54464  26.15338  1.000 31.38683 ?  112 ASN A O   1 
ATOM   799  C CB  . ASN A 1 114 ? -1.66451  -10.28692 26.14654  1.000 32.23112 ?  112 ASN A CB  1 
ATOM   800  C CG  . ASN A 1 114 ? -1.09941  -10.23617 27.55000  1.000 34.66167 ?  112 ASN A CG  1 
ATOM   801  O OD1 . ASN A 1 114 ? 0.11154   -10.09682 27.74050  1.000 31.84572 ?  112 ASN A OD1 1 
ATOM   802  N ND2 . ASN A 1 114 ? -1.97415  -10.33756 28.54492  1.000 34.83127 ?  112 ASN A ND2 1 
ATOM   803  N N   . GLY A 1 115 ? 0.36941   -7.41853  25.00499  1.000 28.05906 ?  113 GLY A N   1 
ATOM   804  C CA  . GLY A 1 115 ? 0.59038   -6.00308  25.19683  1.000 26.11807 ?  113 GLY A CA  1 
ATOM   805  C C   . GLY A 1 115 ? 1.79820   -5.73253  26.08573  1.000 28.32814 ?  113 GLY A C   1 
ATOM   806  O O   . GLY A 1 115 ? 2.20294   -6.55559  26.91099  1.000 26.15774 ?  113 GLY A O   1 
ATOM   807  N N   . THR A 1 116 ? 2.37206   -4.54145  25.91735  1.000 25.57234 ?  114 THR A N   1 
ATOM   808  C CA  . THR A 1 116 ? 3.49339   -4.15508  26.76332  1.000 27.41518 ?  114 THR A CA  1 
ATOM   809  C C   . THR A 1 116 ? 3.01586   -3.72853  28.16110  1.000 26.96379 ?  114 THR A C   1 
ATOM   810  O O   . THR A 1 116 ? 1.84770   -3.39451  28.38061  1.000 22.47562 ?  114 THR A O   1 
ATOM   811  C CB  . THR A 1 116 ? 4.26545   -2.99997  26.15455  1.000 28.68606 ?  114 THR A CB  1 
ATOM   812  O OG1 . THR A 1 116 ? 3.48830   -1.82098  26.32824  1.000 26.50048 ?  114 THR A OG1 1 
ATOM   813  C CG2 . THR A 1 116 ? 4.52257   -3.22365  24.65583  1.000 25.29937 ?  114 THR A CG2 1 
ATOM   814  N N   . LEU A 1 117 ? 3.96158   -3.70077  29.10624  1.000 24.89376 ?  115 LEU A N   1 
ATOM   815  C CA  . LEU A 1 117 ? 3.62001   -3.28672  30.46425  1.000 26.23358 ?  115 LEU A CA  1 
ATOM   816  C C   . LEU A 1 117 ? 3.10449   -1.86526  30.50985  1.000 24.18109 ?  115 LEU A C   1 
ATOM   817  O O   . LEU A 1 117 ? 2.24069   -1.54284  31.32928  1.000 24.36533 ?  115 LEU A O   1 
ATOM   818  C CB  . LEU A 1 117 ? 4.80783   -3.41255  31.42286  1.000 25.69475 ?  115 LEU A CB  1 
ATOM   819  C CG  . LEU A 1 117 ? 5.06086   -4.80889  31.96592  1.000 31.11943 ?  115 LEU A CG  1 
ATOM   820  C CD1 . LEU A 1 117 ? 6.53776   -5.01553  32.36775  1.000 34.65461 ?  115 LEU A CD1 1 
ATOM   821  C CD2 . LEU A 1 117 ? 4.09547   -5.09443  33.08441  1.000 29.34606 ?  115 LEU A CD2 1 
ATOM   822  N N   . LEU A 1 118 ? 3.61099   -0.99275  29.64708  1.000 22.48539 ?  116 LEU A N   1 
ATOM   823  C CA  . LEU A 1 118 ? 3.11165   0.37590   29.67370  1.000 24.44520 ?  116 LEU A CA  1 
ATOM   824  C C   . LEU A 1 118 ? 1.67694   0.43033   29.16820  1.000 26.20921 ?  116 LEU A C   1 
ATOM   825  O O   . LEU A 1 118 ? 0.86141   1.21168   29.67015  1.000 23.63817 ?  116 LEU A O   1 
ATOM   826  C CB  . LEU A 1 118 ? 4.00971   1.29306   28.83923  1.000 23.92730 ?  116 LEU A CB  1 
ATOM   827  C CG  . LEU A 1 118 ? 5.21649   1.94298   29.55376  1.000 25.21420 ?  116 LEU A CG  1 
ATOM   828  C CD1 . LEU A 1 118 ? 5.95575   0.95186   30.37618  1.000 23.30689 ?  116 LEU A CD1 1 
ATOM   829  C CD2 . LEU A 1 118 ? 6.16211   2.56932   28.54012  1.000 28.18101 ?  116 LEU A CD2 1 
ATOM   830  N N   . THR A 1 119 ? 1.34804   -0.39530  28.17456  1.000 26.21919 ?  117 THR A N   1 
ATOM   831  C CA  . THR A 1 119 ? -0.02051  -0.37324  27.66407  1.000 26.07554 ?  117 THR A CA  1 
ATOM   832  C C   . THR A 1 119 ? -0.96328  -0.94398  28.69725  1.000 27.19387 ?  117 THR A C   1 
ATOM   833  O O   . THR A 1 119 ? -2.02844  -0.36858  28.95613  1.000 28.23810 ?  117 THR A O   1 
ATOM   834  C CB  . THR A 1 119 ? -0.12462  -1.14522  26.34540  1.000 23.54177 ?  117 THR A CB  1 
ATOM   835  O OG1 . THR A 1 119 ? 0.61485   -0.44237  25.34867  1.000 27.21355 ?  117 THR A OG1 1 
ATOM   836  C CG2 . THR A 1 119 ? -1.59499  -1.24953  25.86970  1.000 23.91837 ?  117 THR A CG2 1 
ATOM   837  N N   . LYS A 1 120 ? -0.55019  -2.04777  29.33083  1.000 25.69678 ?  118 LYS A N   1 
ATOM   838  C CA  . LYS A 1 120 ? -1.35066  -2.66543  30.37442  1.000 22.79762 ?  118 LYS A CA  1 
ATOM   839  C C   . LYS A 1 120 ? -1.60332  -1.70133  31.52007  1.000 26.21985 ?  118 LYS A C   1 
ATOM   840  O O   . LYS A 1 120 ? -2.69997  -1.69060  32.09299  1.000 26.20693 ?  118 LYS A O   1 
ATOM   841  C CB  . LYS A 1 120 ? -0.67563  -3.93589  30.88817  1.000 24.38039 ?  118 LYS A CB  1 
ATOM   842  C CG  . LYS A 1 120 ? -0.67058  -5.11045  29.92689  1.000 27.98676 ?  118 LYS A CG  1 
ATOM   843  C CD  . LYS A 1 120 ? 0.06895   -6.27996  30.59016  1.000 29.32099 ?  118 LYS A CD  1 
ATOM   844  C CE  . LYS A 1 120 ? 0.20841   -7.49126  29.67628  1.000 32.43114 ?  118 LYS A CE  1 
ATOM   845  N NZ  . LYS A 1 120 ? 1.09190   -8.53180  30.28714  1.000 32.60703 ?  118 LYS A NZ  1 
ATOM   846  N N   . ALA A 1 121 ? -0.60435  -0.88466  31.88093  1.000 23.81375 ?  119 ALA A N   1 
ATOM   847  C CA  . ALA A 1 121 ? -0.78777  0.00700   33.02603  1.000 27.96966 ?  119 ALA A CA  1 
ATOM   848  C C   . ALA A 1 121 ? -1.78451  1.11355   32.71520  1.000 28.99704 ?  119 ALA A C   1 
ATOM   849  O O   . ALA A 1 121 ? -2.60449  1.47739   33.57115  1.000 26.60950 ?  119 ALA A O   1 
ATOM   850  C CB  . ALA A 1 121 ? 0.55383   0.59289   33.47775  1.000 26.67674 ?  119 ALA A CB  1 
ATOM   851  N N   . VAL A 1 122 ? -1.74573  1.64701   31.48961  1.000 27.04282 ?  120 VAL A N   1 
ATOM   852  C CA  . VAL A 1 122 ? -2.67691  2.70894   31.10130  1.000 30.48396 ?  120 VAL A CA  1 
ATOM   853  C C   . VAL A 1 122 ? -4.11054  2.18096   31.07512  1.000 30.03373 ?  120 VAL A C   1 
ATOM   854  O O   . VAL A 1 122 ? -5.06077  2.87649   31.45655  1.000 32.68369 ?  120 VAL A O   1 
ATOM   855  C CB  . VAL A 1 122 ? -2.26529  3.29530   29.73479  1.000 29.26935 ?  120 VAL A CB  1 
ATOM   856  C CG1 . VAL A 1 122 ? -3.36552  4.18871   29.18194  1.000 31.64650 ?  120 VAL A CG1 1 
ATOM   857  C CG2 . VAL A 1 122 ? -0.94962  4.03485   29.85716  1.000 28.60042 ?  120 VAL A CG2 1 
ATOM   858  N N   . ILE A 1 123 ? -4.28449  0.94247   30.63881  1.000 28.59851 ?  121 ILE A N   1 
ATOM   859  C CA  . ILE A 1 123 ? -5.61323  0.35675   30.57161  1.000 33.67399 ?  121 ILE A CA  1 
ATOM   860  C C   . ILE A 1 123 ? -6.11129  -0.06174  31.95368  1.000 35.62378 ?  121 ILE A C   1 
ATOM   861  O O   . ILE A 1 123 ? -7.27361  0.17182   32.30320  1.000 38.48881 ?  121 ILE A O   1 
ATOM   862  C CB  . ILE A 1 123 ? -5.57632  -0.79207  29.55290  1.000 32.18739 ?  121 ILE A CB  1 
ATOM   863  C CG1 . ILE A 1 123 ? -5.59426  -0.16289  28.15162  1.000 37.13614 ?  121 ILE A CG1 1 
ATOM   864  C CG2 . ILE A 1 123 ? -6.69545  -1.80448  29.75598  1.000 33.00311 ?  121 ILE A CG2 1 
ATOM   865  C CD1 . ILE A 1 123 ? -5.29639  -1.08617  27.02080  1.000 36.18329 ?  121 ILE A CD1 1 
ATOM   866  N N   . GLU A 1 124 ? -5.24707  -0.63187  32.78879  1.000 30.10037 ?  122 GLU A N   1 
ATOM   867  C CA  . GLU A 1 124 ? -5.70141  -1.06712  34.10741  1.000 32.29018 ?  122 GLU A CA  1 
ATOM   868  C C   . GLU A 1 124 ? -5.94003  0.11411   35.04685  1.000 37.83513 ?  122 GLU A C   1 
ATOM   869  O O   . GLU A 1 124 ? -6.88078  0.09806   35.85308  1.000 30.85779 ?  122 GLU A O   1 
ATOM   870  C CB  . GLU A 1 124 ? -4.68962  -2.03887  34.71392  1.000 34.00006 ?  122 GLU A CB  1 
ATOM   871  N N   . TYR A 1 125 ? -5.12064  1.15605   34.96394  1.000 36.15603 ?  123 TYR A N   1 
ATOM   872  C CA  . TYR A 1 125 ? -5.30479  2.23415   35.92914  1.000 37.03377 ?  123 TYR A CA  1 
ATOM   873  C C   . TYR A 1 125 ? -5.82057  3.50780   35.27761  1.000 39.21392 ?  123 TYR A C   1 
ATOM   874  O O   . TYR A 1 125 ? -5.18574  4.56048   35.38801  1.000 39.03083 ?  123 TYR A O   1 
ATOM   875  C CB  . TYR A 1 125 ? -3.99558  2.48950   36.68226  1.000 36.56802 ?  123 TYR A CB  1 
ATOM   876  C CG  . TYR A 1 125 ? -3.61224  1.28140   37.49273  1.000 38.66393 ?  123 TYR A CG  1 
ATOM   877  C CD1 . TYR A 1 125 ? -4.20528  1.02637   38.73619  1.000 43.37639 ?  123 TYR A CD1 1 
ATOM   878  C CD2 . TYR A 1 125 ? -2.70721  0.36657   37.00247  1.000 37.59643 ?  123 TYR A CD2 1 
ATOM   879  C CE1 . TYR A 1 125 ? -3.86973  -0.10213  39.47011  1.000 43.71939 ?  123 TYR A CE1 1 
ATOM   880  C CE2 . TYR A 1 125 ? -2.36733  -0.75420  37.72555  1.000 38.96657 ?  123 TYR A CE2 1 
ATOM   881  C CZ  . TYR A 1 125 ? -2.94154  -0.98923  38.94369  1.000 42.56157 ?  123 TYR A CZ  1 
ATOM   882  O OH  . TYR A 1 125 ? -2.56661  -2.12116  39.63286  1.000 43.36045 ?  123 TYR A OH  1 
ATOM   883  N N   . TRP A 1 126 ? -6.97830  3.41969   34.60750  1.000 38.46573 ?  124 TRP A N   1 
ATOM   884  C CA  . TRP A 1 126 ? -7.64669  4.61035   34.08827  1.000 42.65828 ?  124 TRP A CA  1 
ATOM   885  C C   . TRP A 1 126 ? -7.96159  5.61211   35.19606  1.000 44.41566 ?  124 TRP A C   1 
ATOM   886  O O   . TRP A 1 126 ? -8.13673  6.80433   34.91113  1.000 46.39494 ?  124 TRP A O   1 
ATOM   887  C CB  . TRP A 1 126 ? -8.95330  4.21386   33.38284  1.000 44.13750 ?  124 TRP A CB  1 
ATOM   888  C CG  . TRP A 1 126 ? -9.73885  3.28621   34.24051  1.000 42.59153 ?  124 TRP A CG  1 
ATOM   889  C CD1 . TRP A 1 126 ? -9.68542  1.92942   34.22856  1.000 40.21370 ?  124 TRP A CD1 1 
ATOM   890  C CD2 . TRP A 1 126 ? -10.66539 3.64651   35.28419  1.000 40.95208 ?  124 TRP A CD2 1 
ATOM   891  N NE1 . TRP A 1 126 ? -10.51413 1.41636   35.19920  1.000 43.01238 ?  124 TRP A NE1 1 
ATOM   892  C CE2 . TRP A 1 126 ? -11.12913 2.44719   35.85908  1.000 41.04805 ?  124 TRP A CE2 1 
ATOM   893  C CE3 . TRP A 1 126 ? -11.14420 4.86168   35.78221  1.000 40.62401 ?  124 TRP A CE3 1 
ATOM   894  C CZ2 . TRP A 1 126 ? -12.05924 2.42133   36.90321  1.000 44.74584 ?  124 TRP A CZ2 1 
ATOM   895  C CZ3 . TRP A 1 126 ? -12.06984 4.83692   36.83737  1.000 45.07833 ?  124 TRP A CZ3 1 
ATOM   896  C CH2 . TRP A 1 126 ? -12.51796 3.62497   37.37830  1.000 42.34292 ?  124 TRP A CH2 1 
ATOM   897  N N   . ASN A 1 127 ? -8.04604  5.15595   36.45177  1.000 40.92675 ?  125 ASN A N   1 
ATOM   898  C CA  . ASN A 1 127 ? -8.41403  6.02942   37.55940  1.000 41.96619 ?  125 ASN A CA  1 
ATOM   899  C C   . ASN A 1 127 ? -7.23244  6.79974   38.14062  1.000 46.22196 ?  125 ASN A C   1 
ATOM   900  O O   . ASN A 1 127 ? -7.44658  7.70457   38.95850  1.000 42.49263 ?  125 ASN A O   1 
ATOM   901  C CB  . ASN A 1 127 ? -9.08932  5.20705   38.66451  1.000 43.29338 ?  125 ASN A CB  1 
ATOM   902  C CG  . ASN A 1 127 ? -8.17070  4.14369   39.25519  1.000 43.13292 ?  125 ASN A CG  1 
ATOM   903  O OD1 . ASN A 1 127 ? -7.70058  3.23981   38.54896  1.000 41.36595 ?  125 ASN A OD1 1 
ATOM   904  N ND2 . ASN A 1 127 ? -7.93908  4.22513   40.56444  1.000 44.63647 ?  125 ASN A ND2 1 
ATOM   905  N N   . LEU A 1 128 ? -5.99872  6.46617   37.74458  1.000 39.61425 ?  126 LEU A N   1 
ATOM   906  C CA  . LEU A 1 128 ? -4.79669  7.14413   38.21871  1.000 43.28760 ?  126 LEU A CA  1 
ATOM   907  C C   . LEU A 1 128 ? -4.23285  7.93357   37.04611  1.000 43.97843 ?  126 LEU A C   1 
ATOM   908  O O   . LEU A 1 128 ? -3.43901  7.39370   36.25924  1.000 42.48813 ?  126 LEU A O   1 
ATOM   909  C CB  . LEU A 1 128 ? -3.76712  6.14101   38.73511  1.000 40.34920 ?  126 LEU A CB  1 
ATOM   910  C CG  . LEU A 1 128 ? -4.10633  5.20460   39.88414  1.000 41.31495 ?  126 LEU A CG  1 
ATOM   911  C CD1 . LEU A 1 128 ? -2.85205  4.53834   40.42355  1.000 39.61995 ?  126 LEU A CD1 1 
ATOM   912  C CD2 . LEU A 1 128 ? -4.80606  5.97925   40.99710  1.000 45.46712 ?  126 LEU A CD2 1 
ATOM   913  N N   . PRO A 1 129 ? -4.62447  9.20183   36.86711  1.000 45.64485 ?  127 PRO A N   1 
ATOM   914  C CA  . PRO A 1 129 ? -4.15858  9.95745   35.68625  1.000 43.81219 ?  127 PRO A CA  1 
ATOM   915  C C   . PRO A 1 129 ? -2.65036  10.12729  35.63361  1.000 41.28274 ?  127 PRO A C   1 
ATOM   916  O O   . PRO A 1 129 ? -2.11976  10.45806  34.56378  1.000 40.90743 ?  127 PRO A O   1 
ATOM   917  C CB  . PRO A 1 129 ? -4.86280  11.31881  35.81052  1.000 47.15596 ?  127 PRO A CB  1 
ATOM   918  C CG  . PRO A 1 129 ? -5.77339  11.23364  36.98665  1.000 47.53491 ?  127 PRO A CG  1 
ATOM   919  C CD  . PRO A 1 129 ? -5.53041  9.97342   37.73906  1.000 46.36763 ?  127 PRO A CD  1 
ATOM   920  N N   . ASP A 1 130 ? -1.94840  9.90753   36.74861  1.000 41.92601 ?  128 ASP A N   1 
ATOM   921  C CA  . ASP A 1 130 ? -0.49329  9.96507   36.74196  1.000 36.28123 ?  128 ASP A CA  1 
ATOM   922  C C   . ASP A 1 130 ? 0.10009   8.89815   35.82421  1.000 38.63374 ?  128 ASP A C   1 
ATOM   923  O O   . ASP A 1 130 ? 1.12056   9.13817   35.16933  1.000 35.70819 ?  128 ASP A O   1 
ATOM   924  C CB  . ASP A 1 130 ? 0.03785   9.80230   38.16416  1.000 38.40989 ?  128 ASP A CB  1 
ATOM   925  N N   . ILE A 1 131 ? -0.50731  7.70710   35.75930  1.000 35.34471 ?  129 ILE A N   1 
ATOM   926  C CA  . ILE A 1 131 ? 0.06420   6.66993   34.90603  1.000 31.58258 ?  129 ILE A CA  1 
ATOM   927  C C   . ILE A 1 131 ? -0.06484  7.02803   33.43230  1.000 35.29983 ?  129 ILE A C   1 
ATOM   928  O O   . ILE A 1 131 ? 0.90457   6.89922   32.68134  1.000 32.93431 ?  129 ILE A O   1 
ATOM   929  C CB  . ILE A 1 131 ? -0.51203  5.27307   35.20092  1.000 33.58696 ?  129 ILE A CB  1 
ATOM   930  C CG1 . ILE A 1 131 ? -0.02063  4.74638   36.54636  1.000 37.73179 ?  129 ILE A CG1 1 
ATOM   931  C CG2 . ILE A 1 131 ? -0.19927  4.30219   34.07732  1.000 35.38437 ?  129 ILE A CG2 1 
ATOM   932  C CD1 . ILE A 1 131 ? -1.01030  4.70380   37.55793  1.000 37.15947 ?  129 ILE A CD1 1 
ATOM   933  N N   . LYS A 1 132 ? -1.25183  7.45434   32.98325  1.000 35.39908 ?  130 LYS A N   1 
ATOM   934  C CA  . LYS A 1 132 ? -1.38275  7.80916   31.57098  1.000 36.49197 ?  130 LYS A CA  1 
ATOM   935  C C   . LYS A 1 132 ? -0.38709  8.89517   31.19654  1.000 34.13186 ?  130 LYS A C   1 
ATOM   936  O O   . LYS A 1 132 ? 0.15389   8.89978   30.08815  1.000 33.35401 ?  130 LYS A O   1 
ATOM   937  C CB  . LYS A 1 132 ? -2.80097  8.27478   31.22888  1.000 38.92410 ?  130 LYS A CB  1 
ATOM   938  C CG  . LYS A 1 132 ? -2.94028  8.57063   29.72365  1.000 40.92345 ?  130 LYS A CG  1 
ATOM   939  C CD  . LYS A 1 132 ? -4.38451  8.52462   29.23686  1.000 45.45605 ?  130 LYS A CD  1 
ATOM   940  C CE  . LYS A 1 132 ? -4.65917  9.70218   28.31055  1.000 47.25356 ?  130 LYS A CE  1 
ATOM   941  N NZ  . LYS A 1 132 ? -5.31352  10.83666  29.03940  1.000 56.69401 ?  130 LYS A NZ  1 
ATOM   942  N N   . MET A 1 133 ? -0.11922  9.81443   32.11316  1.000 32.89760 ?  131 MET A N   1 
ATOM   943  C CA  . MET A 1 133 ? 0.75509   10.91140  31.75456  1.000 37.12125 ?  131 MET A CA  1 
ATOM   944  C C   . MET A 1 133 ? 2.21941   10.47929  31.72528  1.000 34.62289 ?  131 MET A C   1 
ATOM   945  O O   . MET A 1 133 ? 2.97632   10.98356  30.89581  1.000 35.87185 ?  131 MET A O   1 
ATOM   946  C CB  . MET A 1 133 ? 0.53279   12.08479  32.70363  1.000 38.48168 ?  131 MET A CB  1 
ATOM   947  C CG  . MET A 1 133 ? 1.72996   12.94209  32.93457  1.000 44.22889 ?  131 MET A CG  1 
ATOM   948  S SD  . MET A 1 133 ? 1.20585   14.38845  33.84906  1.000 69.11782 ?  131 MET A SD  1 
ATOM   949  C CE  . MET A 1 133 ? 0.21443   15.23477  32.60189  1.000 49.62066 ?  131 MET A CE  1 
ATOM   950  N N   . LYS A 1 134 ? 2.62778   9.52340   32.56904  1.000 33.01816 ?  132 LYS A N   1 
ATOM   951  C CA  . LYS A 1 134 ? 3.99429   9.00735   32.48149  1.000 32.85628 ?  132 LYS A CA  1 
ATOM   952  C C   . LYS A 1 134 ? 4.20195   8.17409   31.23115  1.000 31.30493 ?  132 LYS A C   1 
ATOM   953  O O   . LYS A 1 134 ? 5.29332   8.19961   30.64771  1.000 30.56294 ?  132 LYS A O   1 
ATOM   954  C CB  . LYS A 1 134 ? 4.34005   8.19007   33.72775  1.000 32.58766 ?  132 LYS A CB  1 
ATOM   955  C CG  . LYS A 1 134 ? 4.04814   8.93453   35.00943  1.000 39.41909 ?  132 LYS A CG  1 
ATOM   956  C CD  . LYS A 1 134 ? 3.86197   8.04016   36.22812  1.000 40.32463 ?  132 LYS A CD  1 
ATOM   957  C CE  . LYS A 1 134 ? 5.06778   7.99521   37.11636  1.000 44.87335 ?  132 LYS A CE  1 
ATOM   958  N NZ  . LYS A 1 134 ? 5.59228   9.33205   37.54844  1.000 45.08160 ?  132 LYS A NZ  1 
ATOM   959  N N   . VAL A 1 135 ? 3.17546   7.44097   30.79090  1.000 29.91035 ?  133 VAL A N   1 
ATOM   960  C CA  . VAL A 1 135 ? 3.33092   6.65341   29.57626  1.000 30.06630 ?  133 VAL A CA  1 
ATOM   961  C C   . VAL A 1 135 ? 3.32156   7.56085   28.36157  1.000 30.47663 ?  133 VAL A C   1 
ATOM   962  O O   . VAL A 1 135 ? 4.09142   7.36771   27.40956  1.000 26.28531 ?  133 VAL A O   1 
ATOM   963  C CB  . VAL A 1 135 ? 2.23726   5.58309   29.49358  1.000 27.53268 ?  133 VAL A CB  1 
ATOM   964  C CG1 . VAL A 1 135 ? 2.29166   4.89286   28.16237  1.000 24.29887 ?  133 VAL A CG1 1 
ATOM   965  C CG2 . VAL A 1 135 ? 2.42235   4.59216   30.65276  1.000 28.58808 ?  133 VAL A CG2 1 
ATOM   966  N N   . GLU A 1 136 ? 2.46496   8.57805   28.38341  1.000 30.26513 ?  134 GLU A N   1 
ATOM   967  C CA  . GLU A 1 136 ? 2.45312   9.54863   27.29904  1.000 32.96575 ?  134 GLU A CA  1 
ATOM   968  C C   . GLU A 1 136 ? 3.81066   10.23156  27.16117  1.000 32.93069 ?  134 GLU A C   1 
ATOM   969  O O   . GLU A 1 136 ? 4.32537   10.40415  26.04681  1.000 32.33775 ?  134 GLU A O   1 
ATOM   970  C CB  . GLU A 1 136 ? 1.34747   10.56838  27.55353  1.000 34.97397 ?  134 GLU A CB  1 
ATOM   971  C CG  . GLU A 1 136 ? 0.93850   11.30930  26.32703  1.000 40.58407 ?  134 GLU A CG  1 
ATOM   972  C CD  . GLU A 1 136 ? -0.22556  12.22813  26.57416  1.000 50.46909 ?  134 GLU A CD  1 
ATOM   973  O OE1 . GLU A 1 136 ? -1.32873  11.71943  26.89883  1.000 50.32133 ?  134 GLU A OE1 1 
ATOM   974  O OE2 . GLU A 1 136 ? -0.03385  13.45702  26.42371  1.000 51.33731 -1 134 GLU A OE2 1 
ATOM   975  N N   . ASP A 1 137 ? 4.40981   10.60709  28.29218  1.000 30.61456 ?  135 ASP A N   1 
ATOM   976  C CA  . ASP A 1 137 ? 5.70160   11.28310  28.28018  1.000 31.35375 ?  135 ASP A CA  1 
ATOM   977  C C   . ASP A 1 137 ? 6.79594   10.36153  27.75047  1.000 32.95312 ?  135 ASP A C   1 
ATOM   978  O O   . ASP A 1 137 ? 7.73030   10.81842  27.07556  1.000 32.48916 ?  135 ASP A O   1 
ATOM   979  C CB  . ASP A 1 137 ? 6.05382   11.75279  29.69647  1.000 34.41738 ?  135 ASP A CB  1 
ATOM   980  C CG  . ASP A 1 137 ? 5.33480   13.04225  30.09498  1.000 42.84999 ?  135 ASP A CG  1 
ATOM   981  O OD1 . ASP A 1 137 ? 4.85544   13.79390  29.20617  1.000 43.10573 ?  135 ASP A OD1 1 
ATOM   982  O OD2 . ASP A 1 137 ? 5.29468   13.32325  31.32124  1.000 46.22682 -1 135 ASP A OD2 1 
ATOM   983  N N   . PHE A 1 138 ? 6.72255   9.06624   28.07719  1.000 29.47003 ?  136 PHE A N   1 
ATOM   984  C CA  . PHE A 1 138 ? 7.63936   8.11352   27.46359  1.000 31.72359 ?  136 PHE A CA  1 
ATOM   985  C C   . PHE A 1 138 ? 7.43536   8.06645   25.95089  1.000 31.95187 ?  136 PHE A C   1 
ATOM   986  O O   . PHE A 1 138 ? 8.40548   8.04582   25.18065  1.000 28.30092 ?  136 PHE A O   1 
ATOM   987  C CB  . PHE A 1 138 ? 7.46481   6.70985   28.05637  1.000 26.60875 ?  136 PHE A CB  1 
ATOM   988  C CG  . PHE A 1 138 ? 8.23842   5.66178   27.30305  1.000 30.75683 ?  136 PHE A CG  1 
ATOM   989  C CD1 . PHE A 1 138 ? 9.61831   5.57309   27.44117  1.000 27.73588 ?  136 PHE A CD1 1 
ATOM   990  C CD2 . PHE A 1 138 ? 7.60737   4.82842   26.39306  1.000 29.94632 ?  136 PHE A CD2 1 
ATOM   991  C CE1 . PHE A 1 138 ? 10.35480  4.65295   26.71934  1.000 28.80987 ?  136 PHE A CE1 1 
ATOM   992  C CE2 . PHE A 1 138 ? 8.32809   3.90389   25.65770  1.000 28.67015 ?  136 PHE A CE2 1 
ATOM   993  C CZ  . PHE A 1 138 ? 9.71126   3.80844   25.82403  1.000 29.40650 ?  136 PHE A CZ  1 
ATOM   994  N N   . ASN A 1 139 ? 6.17721   8.05784   25.50494  1.000 27.69222 ?  137 ASN A N   1 
ATOM   995  C CA  . ASN A 1 139 ? 5.92302   7.96976   24.07510  1.000 30.92864 ?  137 ASN A CA  1 
ATOM   996  C C   . ASN A 1 139 ? 6.35674   9.22988   23.33640  1.000 30.60412 ?  137 ASN A C   1 
ATOM   997  O O   . ASN A 1 139 ? 6.85086   9.13240   22.21212  1.000 29.55525 ?  137 ASN A O   1 
ATOM   998  C CB  . ASN A 1 139 ? 4.45295   7.65909   23.82668  1.000 31.37391 ?  137 ASN A CB  1 
ATOM   999  C CG  . ASN A 1 139 ? 4.12245   6.21412   24.10926  1.000 31.47954 ?  137 ASN A CG  1 
ATOM   1000 O OD1 . ASN A 1 139 ? 4.98321   5.34885   23.99023  1.000 37.13935 ?  137 ASN A OD1 1 
ATOM   1001 N ND2 . ASN A 1 139 ? 2.87346   5.94056   24.47999  1.000 30.79479 ?  137 ASN A ND2 1 
ATOM   1002 N N   . LYS A 1 140 ? 6.22618   10.40969  23.94388  1.000 28.00854 ?  138 LYS A N   1 
ATOM   1003 C CA  . LYS A 1 140 ? 6.83970   11.59060  23.33667  1.000 30.80017 ?  138 LYS A CA  1 
ATOM   1004 C C   . LYS A 1 140 ? 8.35510   11.45899  23.31989  1.000 34.06276 ?  138 LYS A C   1 
ATOM   1005 O O   . LYS A 1 140 ? 9.01262   11.82479  22.33603  1.000 29.78622 ?  138 LYS A O   1 
ATOM   1006 C CB  . LYS A 1 140 ? 6.44052   12.87570  24.07851  1.000 32.96340 ?  138 LYS A CB  1 
ATOM   1007 C CG  . LYS A 1 140 ? 5.02733   13.38169  23.81260  1.000 33.02679 ?  138 LYS A CG  1 
ATOM   1008 N N   . TRP A 1 141 ? 8.92838   10.94173  24.40057  1.000 32.09905 ?  139 TRP A N   1 
ATOM   1009 C CA  . TRP A 1 141 ? 10.36536  10.72228  24.42502  1.000 31.32613 ?  139 TRP A CA  1 
ATOM   1010 C C   . TRP A 1 141 ? 10.79666  9.81452   23.27831  1.000 28.22420 ?  139 TRP A C   1 
ATOM   1011 O O   . TRP A 1 141 ? 11.78541  10.08808  22.59546  1.000 28.61502 ?  139 TRP A O   1 
ATOM   1012 C CB  . TRP A 1 141 ? 10.78304  10.13469  25.77558  1.000 31.72308 ?  139 TRP A CB  1 
ATOM   1013 C CG  . TRP A 1 141 ? 12.25165  9.85381   25.87615  1.000 29.11231 ?  139 TRP A CG  1 
ATOM   1014 C CD1 . TRP A 1 141 ? 13.21517  10.71320  26.30942  1.000 33.22906 ?  139 TRP A CD1 1 
ATOM   1015 C CD2 . TRP A 1 141 ? 12.91925  8.62673   25.56243  1.000 28.77430 ?  139 TRP A CD2 1 
ATOM   1016 N NE1 . TRP A 1 141 ? 14.44662  10.10601  26.26912  1.000 31.06600 ?  139 TRP A NE1 1 
ATOM   1017 C CE2 . TRP A 1 141 ? 14.29164  8.82329   25.81403  1.000 30.20562 ?  139 TRP A CE2 1 
ATOM   1018 C CE3 . TRP A 1 141 ? 12.49092  7.38543   25.09006  1.000 27.86111 ?  139 TRP A CE3 1 
ATOM   1019 C CZ2 . TRP A 1 141 ? 15.24442  7.82867   25.59468  1.000 33.17685 ?  139 TRP A CZ2 1 
ATOM   1020 C CZ3 . TRP A 1 141 ? 13.43369  6.39413   24.88139  1.000 30.40504 ?  139 TRP A CZ3 1 
ATOM   1021 C CH2 . TRP A 1 141 ? 14.79582  6.62165   25.12947  1.000 28.50265 ?  139 TRP A CH2 1 
ATOM   1022 N N   . LYS A 1 142 ? 10.07392  8.72353   23.05776  1.000 30.59225 ?  140 LYS A N   1 
ATOM   1023 C CA  . LYS A 1 142 ? 10.48731  7.77359   22.03265  1.000 31.99583 ?  140 LYS A CA  1 
ATOM   1024 C C   . LYS A 1 142 ? 10.45006  8.39667   20.64162  1.000 31.89687 ?  140 LYS A C   1 
ATOM   1025 O O   . LYS A 1 142 ? 11.38248  8.21773   19.85065  1.000 28.78249 ?  140 LYS A O   1 
ATOM   1026 C CB  . LYS A 1 142 ? 9.61611   6.52991   22.07597  1.000 27.96115 ?  140 LYS A CB  1 
ATOM   1027 C CG  . LYS A 1 142 ? 10.00857  5.54641   21.00944  1.000 27.74080 ?  140 LYS A CG  1 
ATOM   1028 C CD  . LYS A 1 142 ? 9.37482   4.21850   21.27026  1.000 31.08932 ?  140 LYS A CD  1 
ATOM   1029 C CE  . LYS A 1 142 ? 7.88411   4.37238   21.17123  1.000 28.78179 ?  140 LYS A CE  1 
ATOM   1030 N NZ  . LYS A 1 142 ? 7.23414   3.06934   21.12806  1.000 29.09048 ?  140 LYS A NZ  1 
ATOM   1031 N N   . TYR A 1 143 ? 9.37256   9.12403   20.31668  1.000 31.44568 ?  141 TYR A N   1 
ATOM   1032 C CA  . TYR A 1 143 ? 9.34631   9.84906   19.04896  1.000 30.60503 ?  141 TYR A CA  1 
ATOM   1033 C C   . TYR A 1 143 ? 10.52142  10.80993  18.95068  1.000 31.78027 ?  141 TYR A C   1 
ATOM   1034 O O   . TYR A 1 143 ? 11.15565  10.93091  17.89574  1.000 31.09689 ?  141 TYR A O   1 
ATOM   1035 C CB  . TYR A 1 143 ? 8.02000   10.60520  18.87356  1.000 32.25595 ?  141 TYR A CB  1 
ATOM   1036 C CG  . TYR A 1 143 ? 7.98656   11.46950  17.61427  1.000 31.11101 ?  141 TYR A CG  1 
ATOM   1037 C CD1 . TYR A 1 143 ? 8.52523   12.75097  17.61954  1.000 32.04379 ?  141 TYR A CD1 1 
ATOM   1038 C CD2 . TYR A 1 143 ? 7.43228   11.00015  16.42166  1.000 30.25328 ?  141 TYR A CD2 1 
ATOM   1039 C CE1 . TYR A 1 143 ? 8.53037   13.54401  16.48311  1.000 34.37751 ?  141 TYR A CE1 1 
ATOM   1040 C CE2 . TYR A 1 143 ? 7.42598   11.80114  15.27198  1.000 31.41640 ?  141 TYR A CE2 1 
ATOM   1041 C CZ  . TYR A 1 143 ? 7.98563   13.06730  15.32229  1.000 32.42503 ?  141 TYR A CZ  1 
ATOM   1042 O OH  . TYR A 1 143 ? 7.99596   13.89582  14.23062  1.000 36.30213 ?  141 TYR A OH  1 
ATOM   1043 N N   . GLU A 1 144 ? 10.83813  11.49457  20.03842  1.000 33.08285 ?  142 GLU A N   1 
ATOM   1044 C CA  . GLU A 1 144 ? 11.77749  12.59857  19.92981  1.000 31.86279 ?  142 GLU A CA  1 
ATOM   1045 C C   . GLU A 1 144 ? 13.22050  12.11722  19.78339  1.000 33.86012 ?  142 GLU A C   1 
ATOM   1046 O O   . GLU A 1 144 ? 14.01053  12.76701  19.08860  1.000 35.55822 ?  142 GLU A O   1 
ATOM   1047 C CB  . GLU A 1 144 ? 11.61125  13.51929  21.13803  1.000 32.94733 ?  142 GLU A CB  1 
ATOM   1048 C CG  . GLU A 1 144 ? 10.33518  14.31269  21.03115  1.000 36.46188 ?  142 GLU A CG  1 
ATOM   1049 C CD  . GLU A 1 144 ? 9.79743   14.83915  22.36978  1.000 43.60108 ?  142 GLU A CD  1 
ATOM   1050 O OE1 . GLU A 1 144 ? 10.19347  14.32787  23.44122  1.000 42.77449 ?  142 GLU A OE1 1 
ATOM   1051 O OE2 . GLU A 1 144 ? 8.87331   15.69171  22.33964  1.000 45.55033 -1 142 GLU A OE2 1 
ATOM   1052 N N   . ILE A 1 145 ? 13.58430  10.99157  20.40836  1.000 29.99206 ?  143 ILE A N   1 
ATOM   1053 C CA  . ILE A 1 145 ? 14.94637  10.48859  20.26105  1.000 31.74029 ?  143 ILE A CA  1 
ATOM   1054 C C   . ILE A 1 145 ? 15.15114  9.92829   18.85721  1.000 34.87309 ?  143 ILE A C   1 
ATOM   1055 O O   . ILE A 1 145 ? 16.21249  10.11213  18.24286  1.000 32.46850 ?  143 ILE A O   1 
ATOM   1056 C CB  . ILE A 1 145 ? 15.26652  9.45068   21.35836  1.000 31.35953 ?  143 ILE A CB  1 
ATOM   1057 C CG1 . ILE A 1 145 ? 16.76727  9.13859   21.37651  1.000 32.56185 ?  143 ILE A CG1 1 
ATOM   1058 C CG2 . ILE A 1 145 ? 14.45382  8.16360   21.19984  1.000 31.05267 ?  143 ILE A CG2 1 
ATOM   1059 C CD1 . ILE A 1 145 ? 17.16026  8.08777   22.40053  1.000 33.63341 ?  143 ILE A CD1 1 
ATOM   1060 N N   . PHE A 1 146 ? 14.13212  9.24982   18.32831  1.000 31.56641 ?  144 PHE A N   1 
ATOM   1061 C CA  . PHE A 1 146 ? 14.14950  8.79966   16.94269  1.000 35.58270 ?  144 PHE A CA  1 
ATOM   1062 C C   . PHE A 1 146 ? 14.27950  9.98245   15.99397  1.000 34.65175 ?  144 PHE A C   1 
ATOM   1063 O O   . PHE A 1 146 ? 15.11514  9.97540   15.08355  1.000 36.30201 ?  144 PHE A O   1 
ATOM   1064 C CB  . PHE A 1 146 ? 12.87052  8.00204   16.65861  1.000 30.65082 ?  144 PHE A CB  1 
ATOM   1065 C CG  . PHE A 1 146 ? 12.85869  7.33837   15.32347  1.000 32.12082 ?  144 PHE A CG  1 
ATOM   1066 C CD1 . PHE A 1 146 ? 13.82619  6.41700   14.98713  1.000 31.64460 ?  144 PHE A CD1 1 
ATOM   1067 C CD2 . PHE A 1 146 ? 11.87954  7.64353   14.40366  1.000 33.45877 ?  144 PHE A CD2 1 
ATOM   1068 C CE1 . PHE A 1 146 ? 13.80991  5.80169   13.75578  1.000 34.73781 ?  144 PHE A CE1 1 
ATOM   1069 C CE2 . PHE A 1 146 ? 11.86157  7.03473   13.15797  1.000 33.95173 ?  144 PHE A CE2 1 
ATOM   1070 C CZ  . PHE A 1 146 ? 12.82224  6.11616   12.83629  1.000 34.63550 ?  144 PHE A CZ  1 
ATOM   1071 N N   . ALA A 1 147 ? 13.48328  11.03179  16.22427  1.000 33.33936 ?  145 ALA A N   1 
ATOM   1072 C CA  . ALA A 1 147 ? 13.53960  12.22020  15.37513  1.000 36.84005 ?  145 ALA A CA  1 
ATOM   1073 C C   . ALA A 1 147 ? 14.88996  12.90564  15.46002  1.000 39.31091 ?  145 ALA A C   1 
ATOM   1074 O O   . ALA A 1 147 ? 15.44929  13.31129  14.43727  1.000 44.34719 ?  145 ALA A O   1 
ATOM   1075 C CB  . ALA A 1 147 ? 12.43633  13.19960  15.75863  1.000 36.50869 ?  145 ALA A CB  1 
ATOM   1076 N N   . GLU A 1 148 ? 15.42678  13.05390  16.67025  1.000 39.87163 ?  146 GLU A N   1 
ATOM   1077 C CA  . GLU A 1 148 ? 16.72948  13.68411  16.81973  1.000 40.57466 ?  146 GLU A CA  1 
ATOM   1078 C C   . GLU A 1 148 ? 17.79851  12.94029  16.03299  1.000 40.93639 ?  146 GLU A C   1 
ATOM   1079 O O   . GLU A 1 148 ? 18.76832  13.54962  15.57613  1.000 43.11994 ?  146 GLU A O   1 
ATOM   1080 C CB  . GLU A 1 148 ? 17.10769  13.77500  18.29676  1.000 42.22609 ?  146 GLU A CB  1 
ATOM   1081 C CG  . GLU A 1 148 ? 18.29782  14.70760  18.56445  1.000 48.14135 ?  146 GLU A CG  1 
ATOM   1082 C CD  . GLU A 1 148 ? 19.04485  14.35061  19.83100  1.000 56.38168 ?  146 GLU A CD  1 
ATOM   1083 O OE1 . GLU A 1 148 ? 18.39600  13.84470  20.77737  1.000 57.15429 ?  146 GLU A OE1 1 
ATOM   1084 O OE2 . GLU A 1 148 ? 20.27450  14.59719  19.89316  1.000 62.08800 -1 146 GLU A OE2 1 
ATOM   1085 N N   . TYR A 1 149 ? 17.64201  11.63247  15.84648  1.000 40.59990 ?  147 TYR A N   1 
ATOM   1086 C CA  . TYR A 1 149 ? 18.59291  10.92875  14.99580  1.000 40.97151 ?  147 TYR A CA  1 
ATOM   1087 C C   . TYR A 1 149 ? 18.33451  11.22005  13.52719  1.000 42.64576 ?  147 TYR A C   1 
ATOM   1088 O O   . TYR A 1 149 ? 19.27298  11.45794  12.76342  1.000 43.62061 ?  147 TYR A O   1 
ATOM   1089 C CB  . TYR A 1 149 ? 18.54964  9.42489   15.26011  1.000 39.79977 ?  147 TYR A CB  1 
ATOM   1090 C CG  . TYR A 1 149 ? 19.45140  8.99405   16.39056  1.000 36.95025 ?  147 TYR A CG  1 
ATOM   1091 C CD1 . TYR A 1 149 ? 20.82823  8.92291   16.21133  1.000 38.20772 ?  147 TYR A CD1 1 
ATOM   1092 C CD2 . TYR A 1 149 ? 18.93370  8.66722   17.63625  1.000 35.15146 ?  147 TYR A CD2 1 
ATOM   1093 C CE1 . TYR A 1 149 ? 21.66834  8.53531   17.25432  1.000 34.30706 ?  147 TYR A CE1 1 
ATOM   1094 C CE2 . TYR A 1 149 ? 19.75316  8.28421   18.67513  1.000 35.16363 ?  147 TYR A CE2 1 
ATOM   1095 C CZ  . TYR A 1 149 ? 21.12149  8.21052   18.47593  1.000 36.95879 ?  147 TYR A CZ  1 
ATOM   1096 O OH  . TYR A 1 149 ? 21.94168  7.82114   19.51072  1.000 32.67147 ?  147 TYR A OH  1 
ATOM   1097 N N   . LEU A 1 150 ? 17.07355  11.24047  13.11363  1.000 41.08004 ?  148 LEU A N   1 
ATOM   1098 C CA  . LEU A 1 150 ? 16.74864  11.20021  11.69686  1.000 43.80248 ?  148 LEU A CA  1 
ATOM   1099 C C   . LEU A 1 150 ? 16.10327  12.48306  11.18240  1.000 50.19912 ?  148 LEU A C   1 
ATOM   1100 O O   . LEU A 1 150 ? 15.55128  12.48289  10.07526  1.000 50.55009 ?  148 LEU A O   1 
ATOM   1101 C CB  . LEU A 1 150 ? 15.83721  10.00421  11.42962  1.000 40.23616 ?  148 LEU A CB  1 
ATOM   1102 C CG  . LEU A 1 150 ? 16.48295  8.64010   11.66719  1.000 35.67687 ?  148 LEU A CG  1 
ATOM   1103 C CD1 . LEU A 1 150 ? 15.52043  7.58532   11.20270  1.000 37.29005 ?  148 LEU A CD1 1 
ATOM   1104 C CD2 . LEU A 1 150 ? 17.81355  8.51551   10.93248  1.000 40.95259 ?  148 LEU A CD2 1 
ATOM   1105 N N   . ALA A 1 151 ? 16.16771  13.58256  11.93910  1.000 50.96814 ?  149 ALA A N   1 
ATOM   1106 C CA  . ALA A 1 151 ? 15.39560  14.76102  11.55043  1.000 52.77251 ?  149 ALA A CA  1 
ATOM   1107 C C   . ALA A 1 151 ? 15.99196  15.43228  10.32120  1.000 55.77376 ?  149 ALA A C   1 
ATOM   1108 O O   . ALA A 1 151 ? 15.25463  15.93096  9.46015   1.000 57.76454 ?  149 ALA A O   1 
ATOM   1109 C CB  . ALA A 1 151 ? 15.29524  15.75212  12.71274  1.000 51.61901 ?  149 ALA A CB  1 
ATOM   1110 N N   . GLU A 1 152 ? 17.31750  15.44943  10.20473  1.000 55.71063 ?  150 GLU A N   1 
ATOM   1111 C CA  . GLU A 1 152 ? 17.86418  16.03078  8.99271   1.000 56.10213 ?  150 GLU A CA  1 
ATOM   1112 C C   . GLU A 1 152 ? 17.65075  15.14200  7.77241   1.000 52.46381 ?  150 GLU A C   1 
ATOM   1113 O O   . GLU A 1 152 ? 17.88441  15.60619  6.65107   1.000 53.23259 ?  150 GLU A O   1 
ATOM   1114 C CB  . GLU A 1 152 ? 19.35470  16.33649  9.17380   1.000 56.89166 ?  150 GLU A CB  1 
ATOM   1115 N N   . GLU A 1 153 ? 17.18690  13.90255  7.95431   1.000 51.09584 ?  151 GLU A N   1 
ATOM   1116 C CA  . GLU A 1 153 ? 17.17841  12.89614  6.89591   1.000 47.12128 ?  151 GLU A CA  1 
ATOM   1117 C C   . GLU A 1 153 ? 15.79385  12.48997  6.40690   1.000 50.22890 ?  151 GLU A C   1 
ATOM   1118 O O   . GLU A 1 153 ? 15.65648  12.11635  5.23962   1.000 49.35981 ?  151 GLU A O   1 
ATOM   1119 C CB  . GLU A 1 153 ? 17.91449  11.63445  7.36962   1.000 46.64710 ?  151 GLU A CB  1 
ATOM   1120 N N   . ILE A 1 154 ? 14.77562  12.53959  7.26638   1.000 47.09234 ?  152 ILE A N   1 
ATOM   1121 C CA  . ILE A 1 154 ? 13.43470  12.04915  6.97001   1.000 44.45387 ?  152 ILE A CA  1 
ATOM   1122 C C   . ILE A 1 154 ? 12.45766  13.11640  7.45297   1.000 44.02988 ?  152 ILE A C   1 
ATOM   1123 O O   . ILE A 1 154 ? 12.63924  13.67560  8.53866   1.000 45.56572 ?  152 ILE A O   1 
ATOM   1124 C CB  . ILE A 1 154 ? 13.19209  10.69368  7.67185   1.000 43.22596 ?  152 ILE A CB  1 
ATOM   1125 C CG1 . ILE A 1 154 ? 13.70449  9.54575   6.80662   1.000 46.11926 ?  152 ILE A CG1 1 
ATOM   1126 C CG2 . ILE A 1 154 ? 11.71422  10.45764  7.94243   1.000 38.81620 ?  152 ILE A CG2 1 
ATOM   1127 C CD1 . ILE A 1 154 ? 13.61150  8.20043   7.48655   1.000 45.82386 ?  152 ILE A CD1 1 
ATOM   1128 N N   . ASN A 1 155 ? 11.43809  13.42738  6.65274   1.000 42.90546 ?  153 ASN A N   1 
ATOM   1129 C CA  . ASN A 1 155 ? 10.62296  14.58289  7.01840   1.000 43.33258 ?  153 ASN A CA  1 
ATOM   1130 C C   . ASN A 1 155 ? 9.62150   14.22685  8.12178   1.000 37.75665 ?  153 ASN A C   1 
ATOM   1131 O O   . ASN A 1 155 ? 9.41891   13.06030  8.47454   1.000 34.45456 ?  153 ASN A O   1 
ATOM   1132 C CB  . ASN A 1 155 ? 9.91329   15.18480  5.78880   1.000 43.69273 ?  153 ASN A CB  1 
ATOM   1133 C CG  . ASN A 1 155 ? 8.91548   14.23499  5.12975   1.000 42.49241 ?  153 ASN A CG  1 
ATOM   1134 O OD1 . ASN A 1 155 ? 8.28704   13.39592  5.77741   1.000 41.33041 ?  153 ASN A OD1 1 
ATOM   1135 N ND2 . ASN A 1 155 ? 8.75882   14.38262  3.82527   1.000 46.28977 ?  153 ASN A ND2 1 
ATOM   1136 N N   . ASN A 1 156 ? 8.99222   15.26690  8.67483   1.000 39.32328 ?  154 ASN A N   1 
ATOM   1137 C CA  . ASN A 1 156 ? 8.10528   15.07477  9.81783   1.000 39.15232 ?  154 ASN A CA  1 
ATOM   1138 C C   . ASN A 1 156 ? 6.97226   14.11021  9.49347   1.000 35.28068 ?  154 ASN A C   1 
ATOM   1139 O O   . ASN A 1 156 ? 6.60338   13.27544  10.32359  1.000 35.55058 ?  154 ASN A O   1 
ATOM   1140 C CB  . ASN A 1 156 ? 7.54626   16.41711  10.27787  1.000 40.95008 ?  154 ASN A CB  1 
ATOM   1141 C CG  . ASN A 1 156 ? 8.54030   17.21114  11.10729  1.000 42.00791 ?  154 ASN A CG  1 
ATOM   1142 O OD1 . ASN A 1 156 ? 9.60190   16.70775  11.47593  1.000 43.20319 ?  154 ASN A OD1 1 
ATOM   1143 N ND2 . ASN A 1 156 ? 8.19087   18.44754  11.41914  1.000 40.91098 ?  154 ASN A ND2 1 
ATOM   1144 N N   . ALA A 1 157 ? 6.41846   14.19942  8.28692   1.000 36.04725 ?  155 ALA A N   1 
ATOM   1145 C CA  . ALA A 1 157 ? 5.32177   13.31686  7.90765   1.000 35.84362 ?  155 ALA A CA  1 
ATOM   1146 C C   . ALA A 1 157 ? 5.74797   11.85395  7.93914   1.000 32.80733 ?  155 ALA A C   1 
ATOM   1147 O O   . ALA A 1 157 ? 5.01998   10.99792  8.45102   1.000 31.31220 ?  155 ALA A O   1 
ATOM   1148 C CB  . ALA A 1 157 ? 4.79912   13.70114  6.52117   1.000 36.14520 ?  155 ALA A CB  1 
ATOM   1149 N N   . ARG A 1 158 ? 6.92298   11.54082  7.39905   1.000 31.75721 ?  156 ARG A N   1 
ATOM   1150 C CA  . ARG A 1 158 ? 7.37100   10.15292  7.42868   1.000 35.14365 ?  156 ARG A CA  1 
ATOM   1151 C C   . ARG A 1 158 ? 7.75655   9.72744   8.83719   1.000 30.00644 ?  156 ARG A C   1 
ATOM   1152 O O   . ARG A 1 158 ? 7.55132   8.57010   9.20768   1.000 33.19654 ?  156 ARG A O   1 
ATOM   1153 C CB  . ARG A 1 158 ? 8.55432   9.94247   6.47872   1.000 34.84891 ?  156 ARG A CB  1 
ATOM   1154 C CG  . ARG A 1 158 ? 8.12903   9.56489   5.08213   1.000 41.71220 ?  156 ARG A CG  1 
ATOM   1155 C CD  . ARG A 1 158 ? 9.33223   9.24003   4.20169   1.000 41.48972 ?  156 ARG A CD  1 
ATOM   1156 N NE  . ARG A 1 158 ? 9.23628   9.91849   2.91830   1.000 46.34069 ?  156 ARG A NE  1 
ATOM   1157 C CZ  . ARG A 1 158 ? 9.90259   11.02865  2.62877   1.000 53.01722 ?  156 ARG A CZ  1 
ATOM   1158 N NH1 . ARG A 1 158 ? 10.73540  11.58437  3.50741   1.000 51.66284 ?  156 ARG A NH1 1 
ATOM   1159 N NH2 . ARG A 1 158 ? 9.75666   11.57897  1.42325   1.000 49.48800 ?  156 ARG A NH2 1 
ATOM   1160 N N   . LEU A 1 159 ? 8.29980   10.64226  9.63592   1.000 31.05963 ?  157 LEU A N   1 
ATOM   1161 C CA  . LEU A 1 159 ? 8.60900   10.32270  11.02670  1.000 33.71840 ?  157 LEU A CA  1 
ATOM   1162 C C   . LEU A 1 159 ? 7.35154   9.90432   11.78635  1.000 28.26174 ?  157 LEU A C   1 
ATOM   1163 O O   . LEU A 1 159 ? 7.30266   8.81879   12.37303  1.000 27.10734 ?  157 LEU A O   1 
ATOM   1164 C CB  . LEU A 1 159 ? 9.27699   11.52187  11.69889  1.000 34.81533 ?  157 LEU A CB  1 
ATOM   1165 C CG  . LEU A 1 159 ? 10.72815  11.75064  11.29048  1.000 38.91222 ?  157 LEU A CG  1 
ATOM   1166 C CD1 . LEU A 1 159 ? 11.26229  13.03705  11.91018  1.000 42.80552 ?  157 LEU A CD1 1 
ATOM   1167 C CD2 . LEU A 1 159 ? 11.56364  10.56461  11.71094  1.000 38.37022 ?  157 LEU A CD2 1 
ATOM   1168 N N   . ARG A 1 160 ? 6.31060   10.73882  11.75561  1.000 28.45767 ?  158 ARG A N   1 
ATOM   1169 C CA  . ARG A 1 160 ? 5.08229   10.41107  12.48107  1.000 30.00558 ?  158 ARG A CA  1 
ATOM   1170 C C   . ARG A 1 160 ? 4.47003   9.10114   11.99897  1.000 26.28118 ?  158 ARG A C   1 
ATOM   1171 O O   . ARG A 1 160 ? 3.95146   8.32120   12.80443  1.000 25.54587 ?  158 ARG A O   1 
ATOM   1172 C CB  . ARG A 1 160 ? 4.08430   11.54970  12.34983  1.000 28.76540 ?  158 ARG A CB  1 
ATOM   1173 C CG  . ARG A 1 160 ? 4.42718   12.77107  13.20363  1.000 32.08131 ?  158 ARG A CG  1 
ATOM   1174 C CD  . ARG A 1 160 ? 3.31236   13.83683  13.13850  1.000 36.03362 ?  158 ARG A CD  1 
ATOM   1175 N NE  . ARG A 1 160 ? 3.09708   14.36590  11.79199  1.000 37.41395 ?  158 ARG A NE  1 
ATOM   1176 C CZ  . ARG A 1 160 ? 3.62391   15.48886  11.31911  1.000 36.87216 ?  158 ARG A CZ  1 
ATOM   1177 N NH1 . ARG A 1 160 ? 4.44424   16.23259  12.04511  1.000 37.35277 ?  158 ARG A NH1 1 
ATOM   1178 N NH2 . ARG A 1 160 ? 3.32342   15.87319  10.08221  1.000 39.78605 ?  158 ARG A NH2 1 
ATOM   1179 N N   . ILE A 1 161 ? 4.52173   8.83634   10.69467  1.000 25.69310 ?  159 ILE A N   1 
ATOM   1180 C CA  . ILE A 1 161 ? 3.93486   7.61116   10.16025  1.000 24.90614 ?  159 ILE A CA  1 
ATOM   1181 C C   . ILE A 1 161 ? 4.72812   6.39053   10.61430  1.000 23.08027 ?  159 ILE A C   1 
ATOM   1182 O O   . ILE A 1 161 ? 4.15048   5.38550   11.04308  1.000 21.29294 ?  159 ILE A O   1 
ATOM   1183 C CB  . ILE A 1 161 ? 3.84663   7.68951   8.62616   1.000 28.30937 ?  159 ILE A CB  1 
ATOM   1184 C CG1 . ILE A 1 161 ? 2.66566   8.56041   8.20544   1.000 27.49407 ?  159 ILE A CG1 1 
ATOM   1185 C CG2 . ILE A 1 161 ? 3.75486   6.29353   8.00552   1.000 25.14969 ?  159 ILE A CG2 1 
ATOM   1186 C CD1 . ILE A 1 161 ? 2.75260   9.00307   6.77037   1.000 34.42657 ?  159 ILE A CD1 1 
ATOM   1187 N N   . ILE A 1 162 ? 6.06146   6.45699   10.53319  1.000 23.46210 ?  160 ILE A N   1 
ATOM   1188 C CA  . ILE A 1 162 ? 6.88827   5.31342   10.92420  1.000 23.16505 ?  160 ILE A CA  1 
ATOM   1189 C C   . ILE A 1 162 ? 6.71475   4.99717   12.40347  1.000 22.00212 ?  160 ILE A C   1 
ATOM   1190 O O   . ILE A 1 162 ? 6.53201   3.83317   12.79623  1.000 23.79657 ?  160 ILE A O   1 
ATOM   1191 C CB  . ILE A 1 162 ? 8.36776   5.58510   10.57608  1.000 23.83986 ?  160 ILE A CB  1 
ATOM   1192 C CG1 . ILE A 1 162 ? 8.56207   5.56628   9.08500   1.000 25.53243 ?  160 ILE A CG1 1 
ATOM   1193 C CG2 . ILE A 1 162 ? 9.25211   4.50007   11.17730  1.000 23.70651 ?  160 ILE A CG2 1 
ATOM   1194 C CD1 . ILE A 1 162 ? 9.94987   6.11532   8.64820   1.000 25.98564 ?  160 ILE A CD1 1 
ATOM   1195 N N   . VAL A 1 163 ? 6.74578   6.02002   13.25194  1.000 22.56296 ?  161 VAL A N   1 
ATOM   1196 C CA  . VAL A 1 163 ? 6.61017   5.76930   14.68369  1.000 24.20578 ?  161 VAL A CA  1 
ATOM   1197 C C   . VAL A 1 163 ? 5.21921   5.22268   15.00309  1.000 23.34674 ?  161 VAL A C   1 
ATOM   1198 O O   . VAL A 1 163 ? 5.07347   4.27843   15.79177  1.000 23.03964 ?  161 VAL A O   1 
ATOM   1199 C CB  . VAL A 1 163 ? 6.94970   7.04655   15.48063  1.000 26.99628 ?  161 VAL A CB  1 
ATOM   1200 C CG1 . VAL A 1 163 ? 6.69362   6.84935   16.96580  1.000 24.30228 ?  161 VAL A CG1 1 
ATOM   1201 C CG2 . VAL A 1 163 ? 8.42922   7.37325   15.30262  1.000 22.99752 ?  161 VAL A CG2 1 
ATOM   1202 N N   . SER A 1 164 ? 4.18358   5.73639   14.33261  1.000 21.09615 ?  162 SER A N   1 
ATOM   1203 C CA  . SER A 1 164 ? 2.85293   5.18825   14.55254  1.000 22.61414 ?  162 SER A CA  1 
ATOM   1204 C C   . SER A 1 164 ? 2.76707   3.73769   14.08346  1.000 23.43458 ?  162 SER A C   1 
ATOM   1205 O O   . SER A 1 164 ? 2.14452   2.89618   14.74960  1.000 21.90017 ?  162 SER A O   1 
ATOM   1206 C CB  . SER A 1 164 ? 1.80222   6.05402   13.85330  1.000 24.03452 ?  162 SER A CB  1 
ATOM   1207 O OG  . SER A 1 164 ? 0.51485   5.78213   14.39750  1.000 26.41604 ?  162 SER A OG  1 
ATOM   1208 N N   . ALA A 1 165 ? 3.38726   3.42657   12.93838  1.000 22.94393 ?  163 ALA A N   1 
ATOM   1209 C CA  . ALA A 1 165 ? 3.44372   2.04275   12.46790  1.000 23.61904 ?  163 ALA A CA  1 
ATOM   1210 C C   . ALA A 1 165 ? 4.13416   1.12862   13.47983  1.000 23.13101 ?  163 ALA A C   1 
ATOM   1211 O O   . ALA A 1 165 ? 3.73046   -0.03156  13.65430  1.000 21.93161 ?  163 ALA A O   1 
ATOM   1212 C CB  . ALA A 1 165 ? 4.15466   1.98365   11.10981  1.000 23.38519 ?  163 ALA A CB  1 
ATOM   1213 N N   . MET A 1 166 ? 5.17323   1.62133   14.16878  1.000 23.32937 ?  164 MET A N   1 
ATOM   1214 C CA  . MET A 1 166 ? 5.85605   0.73158   15.10499  1.000 22.82671 ?  164 MET A CA  1 
ATOM   1215 C C   . MET A 1 166 ? 5.03301   0.52178   16.36546  1.000 23.92261 ?  164 MET A C   1 
ATOM   1216 O O   . MET A 1 166 ? 5.02826   -0.57678  16.93130  1.000 24.37427 ?  164 MET A O   1 
ATOM   1217 C CB  . MET A 1 166 ? 7.24493   1.25463   15.47790  1.000 25.27161 ?  164 MET A CB  1 
ATOM   1218 C CG  . MET A 1 166 ? 8.09549   1.54639   14.27959  1.000 25.87413 ?  164 MET A CG  1 
ATOM   1219 S SD  . MET A 1 166 ? 8.67087   0.06587   13.45225  1.000 27.57550 ?  164 MET A SD  1 
ATOM   1220 C CE  . MET A 1 166 ? 7.36629   -0.21677  12.26505  1.000 25.90756 ?  164 MET A CE  1 
ATOM   1221 N N   . ASN A 1 167 ? 4.33010   1.56321   16.81374  1.000 23.15252 ?  165 ASN A N   1 
ATOM   1222 C CA  . ASN A 1 167 ? 3.36930   1.40482   17.89143  1.000 25.39556 ?  165 ASN A CA  1 
ATOM   1223 C C   . ASN A 1 167 ? 2.26000   0.42390   17.52220  1.000 25.20143 ?  165 ASN A C   1 
ATOM   1224 O O   . ASN A 1 167 ? 1.72602   -0.25285  18.40200  1.000 25.51354 ?  165 ASN A O   1 
ATOM   1225 C CB  . ASN A 1 167 ? 2.79316   2.77204   18.27472  1.000 27.50855 ?  165 ASN A CB  1 
ATOM   1226 C CG  . ASN A 1 167 ? 3.79267   3.63163   19.04663  1.000 29.99621 ?  165 ASN A CG  1 
ATOM   1227 O OD1 . ASN A 1 167 ? 4.60419   3.11393   19.82446  1.000 30.75870 ?  165 ASN A OD1 1 
ATOM   1228 N ND2 . ASN A 1 167 ? 3.74847   4.94700   18.82389  1.000 30.75660 ?  165 ASN A ND2 1 
ATOM   1229 N N   . GLY A 1 168 ? 1.91758   0.30244   16.23384  1.000 24.47520 ?  166 GLY A N   1 
ATOM   1230 C CA  . GLY A 1 168 ? 0.93410   -0.69476  15.83736  1.000 23.28411 ?  166 GLY A CA  1 
ATOM   1231 C C   . GLY A 1 168 ? 1.43756   -2.12419  15.94608  1.000 23.04581 ?  166 GLY A C   1 
ATOM   1232 O O   . GLY A 1 168 ? 0.65494   -3.04559  16.19423  1.000 22.66354 ?  166 GLY A O   1 
ATOM   1233 N N   . ILE A 1 169 ? 2.74621   -2.33142  15.78376  1.000 20.54687 ?  167 ILE A N   1 
ATOM   1234 C CA  . ILE A 1 169 ? 3.34784   -3.63705  16.06118  1.000 20.19476 ?  167 ILE A CA  1 
ATOM   1235 C C   . ILE A 1 169 ? 3.14394   -4.02339  17.52893  1.000 22.08997 ?  167 ILE A C   1 
ATOM   1236 O O   . ILE A 1 169 ? 3.08650   -5.21152  17.86948  1.000 23.29831 ?  167 ILE A O   1 
ATOM   1237 C CB  . ILE A 1 169 ? 4.84679   -3.58987  15.67281  1.000 23.53634 ?  167 ILE A CB  1 
ATOM   1238 C CG1 . ILE A 1 169 ? 4.99260   -3.49512  14.15329  1.000 21.70643 ?  167 ILE A CG1 1 
ATOM   1239 C CG2 . ILE A 1 169 ? 5.61977   -4.78565  16.22318  1.000 24.26038 ?  167 ILE A CG2 1 
ATOM   1240 C CD1 . ILE A 1 169 ? 6.45931   -3.36589  13.68929  1.000 27.55934 ?  167 ILE A CD1 1 
ATOM   1241 N N   . LEU A 1 170 ? 3.02247   -3.03434  18.40887  1.000 18.64724 ?  168 LEU A N   1 
ATOM   1242 C CA  . LEU A 1 170 ? 2.85618   -3.25643  19.84581  1.000 21.99130 ?  168 LEU A CA  1 
ATOM   1243 C C   . LEU A 1 170 ? 1.40510   -3.50131  20.25943  1.000 24.91510 ?  168 LEU A C   1 
ATOM   1244 O O   . LEU A 1 170 ? 1.16446   -3.98676  21.36776  1.000 25.19780 ?  168 LEU A O   1 
ATOM   1245 C CB  . LEU A 1 170 ? 3.38560   -2.05765  20.63022  1.000 21.41208 ?  168 LEU A CB  1 
ATOM   1246 C CG  . LEU A 1 170 ? 4.85128   -1.65158  20.39085  1.000 22.82012 ?  168 LEU A CG  1 
ATOM   1247 C CD1 . LEU A 1 170 ? 5.19349   -0.51278  21.29631  1.000 21.20854 ?  168 LEU A CD1 1 
ATOM   1248 C CD2 . LEU A 1 170 ? 5.77776   -2.81111  20.60527  1.000 19.60295 ?  168 LEU A CD2 1 
ATOM   1249 N N   . LEU A 1 171 ? 0.44934   -3.17280  19.42659  1.000 25.48089 ?  169 LEU A N   1 
ATOM   1250 C CA  . LEU A 1 171 ? -0.93811  -3.47786  19.74146  1.000 25.54320 ?  169 LEU A CA  1 
ATOM   1251 C C   . LEU A 1 171 ? -1.13440  -4.98949  19.77464  1.000 28.64660 ?  169 LEU A C   1 
ATOM   1252 O O   . LEU A 1 171 ? -0.77445  -5.67838  18.82533  1.000 28.03404 ?  169 LEU A O   1 
ATOM   1253 C CB  . LEU A 1 171 ? -1.84692  -2.83352  18.71257  1.000 28.93836 ?  169 LEU A CB  1 
ATOM   1254 C CG  . LEU A 1 171 ? -3.30840  -2.65929  19.11962  1.000 29.71843 ?  169 LEU A CG  1 
ATOM   1255 C CD1 . LEU A 1 171 ? -3.52573  -1.36100  19.92068  1.000 31.23697 ?  169 LEU A CD1 1 
ATOM   1256 C CD2 . LEU A 1 171 ? -4.14831  -2.68062  17.88410  1.000 31.55220 ?  169 LEU A CD2 1 
ATOM   1257 N N   . PRO A 1 172 ? -1.66497  -5.55207  20.85250  1.000 29.29071 ?  170 PRO A N   1 
ATOM   1258 C CA  . PRO A 1 172 ? -1.81951  -7.00526  20.89503  1.000 31.44608 ?  170 PRO A CA  1 
ATOM   1259 C C   . PRO A 1 172 ? -2.87252  -7.44171  19.88924  1.000 29.45029 ?  170 PRO A C   1 
ATOM   1260 O O   . PRO A 1 172 ? -3.72374  -6.65595  19.47063  1.000 32.04533 ?  170 PRO A O   1 
ATOM   1261 C CB  . PRO A 1 172 ? -2.24364  -7.27494  22.34807  1.000 32.47562 ?  170 PRO A CB  1 
ATOM   1262 C CG  . PRO A 1 172 ? -2.88247  -6.01106  22.78094  1.000 28.93462 ?  170 PRO A CG  1 
ATOM   1263 C CD  . PRO A 1 172 ? -2.12618  -4.90764  22.09032  1.000 30.14120 ?  170 PRO A CD  1 
ATOM   1264 N N   . ALA A 1 173 ? -2.76059  -8.69677  19.46123  1.000 30.20793 ?  171 ALA A N   1 
ATOM   1265 C CA  . ALA A 1 173 ? -3.64520  -9.31330  18.46853  1.000 35.43288 ?  171 ALA A CA  1 
ATOM   1266 C C   . ALA A 1 173 ? -3.56301  -8.62844  17.11652  1.000 35.29617 ?  171 ALA A C   1 
ATOM   1267 O O   . ALA A 1 173 ? -4.45684  -8.78008  16.27993  1.000 36.82770 ?  171 ALA A O   1 
ATOM   1268 C CB  . ALA A 1 173 ? -5.10339  -9.35392  18.94395  1.000 35.54420 ?  171 ALA A CB  1 
ATOM   1269 N N   . SER A 1 174 ? -2.49573  -7.87699  16.88218  1.000 36.08425 ?  172 SER A N   1 
ATOM   1270 C CA  . SER A 1 174 ? -2.31917  -7.21469  15.61022  1.000 34.66766 ?  172 SER A CA  1 
ATOM   1271 C C   . SER A 1 174 ? -1.75397  -8.19084  14.58469  1.000 35.67881 ?  172 SER A C   1 
ATOM   1272 O O   . SER A 1 174 ? -1.11252  -9.18837  14.92202  1.000 34.54232 ?  172 SER A O   1 
ATOM   1273 C CB  . SER A 1 174 ? -1.43267  -5.98242  15.77773  1.000 35.65495 ?  172 SER A CB  1 
ATOM   1274 O OG  . SER A 1 174 ? -0.09442  -6.29713  15.46959  1.000 40.57523 ?  172 SER A OG  1 
ATOM   1275 N N   . THR A 1 175 ? -2.06798  -7.92508  13.32015  1.000 33.93920 ?  173 THR A N   1 
ATOM   1276 C CA  . THR A 1 175 ? -1.81578  -8.83193  12.20773  1.000 36.65292 ?  173 THR A CA  1 
ATOM   1277 C C   . THR A 1 175 ? -1.27594  -8.03291  11.02641  1.000 30.04338 ?  173 THR A C   1 
ATOM   1278 O O   . THR A 1 175 ? -1.31047  -6.80333  11.02252  1.000 32.31393 ?  173 THR A O   1 
ATOM   1279 C CB  . THR A 1 175 ? -3.10531  -9.56946  11.80152  1.000 37.82448 ?  173 THR A CB  1 
ATOM   1280 O OG1 . THR A 1 175 ? -3.94523  -8.67115  11.06901  1.000 37.29956 ?  173 THR A OG1 1 
ATOM   1281 C CG2 . THR A 1 175 ? -3.87185  -10.06152 12.99964  1.000 38.06750 ?  173 THR A CG2 1 
ATOM   1282 N N   . TYR A 1 176 ? -0.79753  -8.74111  10.00572  1.000 33.89135 ?  174 TYR A N   1 
ATOM   1283 C CA  . TYR A 1 176 ? -0.28813  -8.10952  8.77769   1.000 32.92160 ?  174 TYR A CA  1 
ATOM   1284 C C   . TYR A 1 176 ? 0.74784   -7.02436  9.08350   1.000 31.34359 ?  174 TYR A C   1 
ATOM   1285 O O   . TYR A 1 176 ? 0.69935   -5.92597  8.52515   1.000 28.52983 ?  174 TYR A O   1 
ATOM   1286 C CB  . TYR A 1 176 ? -1.43733  -7.51866  7.95508   1.000 30.97348 ?  174 TYR A CB  1 
ATOM   1287 C CG  . TYR A 1 176 ? -2.24827  -8.50472  7.15388   1.000 34.47867 ?  174 TYR A CG  1 
ATOM   1288 C CD1 . TYR A 1 176 ? -1.72039  -9.10272  6.02730   1.000 33.32871 ?  174 TYR A CD1 1 
ATOM   1289 C CD2 . TYR A 1 176 ? -3.56074  -8.81369  7.50560   1.000 32.10477 ?  174 TYR A CD2 1 
ATOM   1290 C CE1 . TYR A 1 176 ? -2.44967  -9.98921  5.27502   1.000 34.37319 ?  174 TYR A CE1 1 
ATOM   1291 C CE2 . TYR A 1 176 ? -4.31163  -9.70590  6.74124   1.000 32.88500 ?  174 TYR A CE2 1 
ATOM   1292 C CZ  . TYR A 1 176 ? -3.73959  -10.28961 5.62484   1.000 35.30590 ?  174 TYR A CZ  1 
ATOM   1293 O OH  . TYR A 1 176 ? -4.43937  -11.19374 4.85146   1.000 33.95073 ?  174 TYR A OH  1 
ATOM   1294 N N   . LEU A 1 177 ? 1.66976   -7.31829  10.00958  1.000 29.49630 ?  175 LEU A N   1 
ATOM   1295 C CA  . LEU A 1 177 ? 2.61016   -6.30750  10.48895  1.000 27.85359 ?  175 LEU A CA  1 
ATOM   1296 C C   . LEU A 1 177 ? 3.59494   -5.89632  9.39464   1.000 27.82330 ?  175 LEU A C   1 
ATOM   1297 O O   . LEU A 1 177 ? 4.02820   -6.72851  8.60329   1.000 27.98411 ?  175 LEU A O   1 
ATOM   1298 C CB  . LEU A 1 177 ? 3.39667   -6.83469  11.68556  1.000 29.67147 ?  175 LEU A CB  1 
ATOM   1299 C CG  . LEU A 1 177 ? 2.62995   -7.04245  12.98618  1.000 33.58553 ?  175 LEU A CG  1 
ATOM   1300 C CD1 . LEU A 1 177 ? 3.60240   -7.50011  14.08576  1.000 33.32985 ?  175 LEU A CD1 1 
ATOM   1301 C CD2 . LEU A 1 177 ? 1.90931   -5.73320  13.36295  1.000 33.25867 ?  175 LEU A CD2 1 
ATOM   1302 N N   . PRO A 1 178 ? 3.96431   -4.62261  9.33367   1.000 26.72751 ?  176 PRO A N   1 
ATOM   1303 C CA  . PRO A 1 178 ? 5.00782   -4.19925  8.39372   1.000 30.04490 ?  176 PRO A CA  1 
ATOM   1304 C C   . PRO A 1 178 ? 6.33674   -4.89767  8.68351   1.000 29.46851 ?  176 PRO A C   1 
ATOM   1305 O O   . PRO A 1 178 ? 6.71112   -5.10777  9.83857   1.000 28.33318 ?  176 PRO A O   1 
ATOM   1306 C CB  . PRO A 1 178 ? 5.09263   -2.67998  8.61903   1.000 29.11815 ?  176 PRO A CB  1 
ATOM   1307 C CG  . PRO A 1 178 ? 4.42323   -2.42297  9.96195   1.000 29.38912 ?  176 PRO A CG  1 
ATOM   1308 C CD  . PRO A 1 178 ? 3.42273   -3.51454  10.14204  1.000 26.85691 ?  176 PRO A CD  1 
ATOM   1309 N N   . THR A 1 179 ? 7.02706   -5.28546  7.61367   1.000 29.30829 ?  177 THR A N   1 
ATOM   1310 C CA  . THR A 1 179 ? 8.31313   -5.96875  7.66949   1.000 28.94072 ?  177 THR A CA  1 
ATOM   1311 C C   . THR A 1 179 ? 9.44241   -4.94907  7.53482   1.000 29.35809 ?  177 THR A C   1 
ATOM   1312 O O   . THR A 1 179 ? 9.23160   -3.78660  7.17619   1.000 27.17001 ?  177 THR A O   1 
ATOM   1313 C CB  . THR A 1 179 ? 8.41357   -7.04918  6.56585   1.000 34.51185 ?  177 THR A CB  1 
ATOM   1314 O OG1 . THR A 1 179 ? 8.62951   -6.44499  5.28479   1.000 28.03532 ?  177 THR A OG1 1 
ATOM   1315 C CG2 . THR A 1 179 ? 7.12934   -7.87771  6.48073   1.000 32.42776 ?  177 THR A CG2 1 
ATOM   1316 N N   . TRP A 1 180 ? 10.66408  -5.38853  7.85135   1.000 30.54735 ?  178 TRP A N   1 
ATOM   1317 C CA  . TRP A 1 180 ? 11.80635  -4.50975  7.66530   1.000 29.27014 ?  178 TRP A CA  1 
ATOM   1318 C C   . TRP A 1 180 ? 11.88523  -4.02348  6.22039   1.000 30.52091 ?  178 TRP A C   1 
ATOM   1319 O O   . TRP A 1 180 ? 12.06646  -2.82587  5.97037   1.000 31.55969 ?  178 TRP A O   1 
ATOM   1320 C CB  . TRP A 1 180 ? 13.10939  -5.20784  8.06421   1.000 30.34710 ?  178 TRP A CB  1 
ATOM   1321 C CG  . TRP A 1 180 ? 14.29704  -4.50278  7.45536   1.000 32.33459 ?  178 TRP A CG  1 
ATOM   1322 C CD1 . TRP A 1 180 ? 15.19798  -5.00433  6.57568   1.000 35.93762 ?  178 TRP A CD1 1 
ATOM   1323 C CD2 . TRP A 1 180 ? 14.66911  -3.14596  7.68355   1.000 33.87573 ?  178 TRP A CD2 1 
ATOM   1324 N NE1 . TRP A 1 180 ? 16.12143  -4.03883  6.23385   1.000 34.28688 ?  178 TRP A NE1 1 
ATOM   1325 C CE2 . TRP A 1 180 ? 15.81571  -2.88956  6.91483   1.000 32.25449 ?  178 TRP A CE2 1 
ATOM   1326 C CE3 . TRP A 1 180 ? 14.14816  -2.12238  8.48993   1.000 30.67856 ?  178 TRP A CE3 1 
ATOM   1327 C CZ2 . TRP A 1 180 ? 16.43881  -1.64620  6.90088   1.000 32.56526 ?  178 TRP A CZ2 1 
ATOM   1328 C CZ3 . TRP A 1 180 ? 14.76586  -0.89870  8.47567   1.000 31.20606 ?  178 TRP A CZ3 1 
ATOM   1329 C CH2 . TRP A 1 180 ? 15.89782  -0.66355  7.68200   1.000 33.47010 ?  178 TRP A CH2 1 
ATOM   1330 N N   . GLU A 1 181 ? 11.70335  -4.92275  5.25882   1.000 30.24005 ?  179 GLU A N   1 
ATOM   1331 C CA  . GLU A 1 181 ? 11.77622  -4.50399  3.86159   1.000 33.80025 ?  179 GLU A CA  1 
ATOM   1332 C C   . GLU A 1 181 ? 10.67911  -3.49778  3.50638   1.000 35.36259 ?  179 GLU A C   1 
ATOM   1333 O O   . GLU A 1 181 ? 10.91784  -2.60526  2.68948   1.000 37.48687 ?  179 GLU A O   1 
ATOM   1334 C CB  . GLU A 1 181 ? 11.72572  -5.72451  2.94320   1.000 36.09062 ?  179 GLU A CB  1 
ATOM   1335 N N   . ASP A 1 182 ? 9.48632   -3.60519  4.10668   1.000 32.15505 ?  180 ASP A N   1 
ATOM   1336 C CA  . ASP A 1 182 ? 8.48366   -2.54860  3.94755   1.000 32.90238 ?  180 ASP A CA  1 
ATOM   1337 C C   . ASP A 1 182 ? 9.03643   -1.20530  4.40442   1.000 36.10118 ?  180 ASP A C   1 
ATOM   1338 O O   . ASP A 1 182 ? 8.96432   -0.20524  3.68077   1.000 34.34696 ?  180 ASP A O   1 
ATOM   1339 C CB  . ASP A 1 182 ? 7.21853   -2.84795  4.76113   1.000 31.77488 ?  180 ASP A CB  1 
ATOM   1340 C CG  . ASP A 1 182 ? 6.49653   -4.11118  4.32885   1.000 32.15455 ?  180 ASP A CG  1 
ATOM   1341 O OD1 . ASP A 1 182 ? 6.69429   -4.60252  3.19763   1.000 34.38124 ?  180 ASP A OD1 1 
ATOM   1342 O OD2 . ASP A 1 182 ? 5.74018   -4.64098  5.16459   1.000 32.70570 -1 180 ASP A OD2 1 
ATOM   1343 N N   . ILE A 1 183 ? 9.54314   -1.15918  5.63708   1.000 30.42813 ?  181 ILE A N   1 
ATOM   1344 C CA  . ILE A 1 183 ? 10.06550  0.08270   6.20204   1.000 35.63351 ?  181 ILE A CA  1 
ATOM   1345 C C   . ILE A 1 183 ? 11.24600  0.58860   5.39170   1.000 36.79013 ?  181 ILE A C   1 
ATOM   1346 O O   . ILE A 1 183 ? 11.38876  1.79615   5.15937   1.000 39.58193 ?  181 ILE A O   1 
ATOM   1347 C CB  . ILE A 1 183 ? 10.46330  -0.11901  7.67593   1.000 32.34576 ?  181 ILE A CB  1 
ATOM   1348 C CG1 . ILE A 1 183 ? 9.28766   -0.64138  8.49446   1.000 31.12434 ?  181 ILE A CG1 1 
ATOM   1349 C CG2 . ILE A 1 183 ? 10.97979  1.17014   8.25290   1.000 33.85905 ?  181 ILE A CG2 1 
ATOM   1350 C CD1 . ILE A 1 183 ? 8.07995   0.30464   8.49277   1.000 34.57225 ?  181 ILE A CD1 1 
ATOM   1351 N N   . GLU A 1 184 ? 12.13033  -0.32031  4.97844   1.000 36.53790 ?  182 GLU A N   1 
ATOM   1352 C CA  . GLU A 1 184 ? 13.28624  0.08176   4.18821   1.000 38.42231 ?  182 GLU A CA  1 
ATOM   1353 C C   . GLU A 1 184 ? 12.86307  0.65970   2.84245   1.000 42.48857 ?  182 GLU A C   1 
ATOM   1354 O O   . GLU A 1 184 ? 13.51448  1.58142   2.33330   1.000 41.31824 ?  182 GLU A O   1 
ATOM   1355 C CB  . GLU A 1 184 ? 14.23426  -1.10996  4.01383   1.000 37.51494 ?  182 GLU A CB  1 
ATOM   1356 C CG  . GLU A 1 184 ? 15.34296  -0.89455  2.98569   1.000 44.08057 ?  182 GLU A CG  1 
ATOM   1357 C CD  . GLU A 1 184 ? 16.48377  -1.89978  3.09746   1.000 47.94886 ?  182 GLU A CD  1 
ATOM   1358 O OE1 . GLU A 1 184 ? 16.25492  -3.09593  2.79849   1.000 50.00417 ?  182 GLU A OE1 1 
ATOM   1359 O OE2 . GLU A 1 184 ? 17.61656  -1.49024  3.46043   1.000 45.98507 -1 182 GLU A OE2 1 
ATOM   1360 N N   . SER A 1 185 ? 11.76095  0.15489   2.26817   1.000 42.92769 ?  183 SER A N   1 
ATOM   1361 C CA  . SER A 1 185 ? 11.24487  0.69851   1.01033   1.000 43.10658 ?  183 SER A CA  1 
ATOM   1362 C C   . SER A 1 185 ? 10.70166  2.10763   1.19224   1.000 44.79040 ?  183 SER A C   1 
ATOM   1363 O O   . SER A 1 185 ? 10.75468  2.92052   0.26513   1.000 46.72146 ?  183 SER A O   1 
ATOM   1364 C CB  . SER A 1 185 ? 10.14648  -0.20809  0.45500   1.000 44.59240 ?  183 SER A CB  1 
ATOM   1365 O OG  . SER A 1 185 ? 10.68220  -1.46288  0.06657   1.000 48.18291 ?  183 SER A OG  1 
ATOM   1366 N N   . LEU A 1 186 ? 10.18275  2.41306   2.37750   1.000 44.44840 ?  184 LEU A N   1 
ATOM   1367 C CA  . LEU A 1 186 ? 9.63883   3.73651   2.63755   1.000 45.93567 ?  184 LEU A CA  1 
ATOM   1368 C C   . LEU A 1 186 ? 10.72372  4.78424   2.85768   1.000 46.45727 ?  184 LEU A C   1 
ATOM   1369 O O   . LEU A 1 186 ? 10.48050  5.96698   2.59919   1.000 46.42189 ?  184 LEU A O   1 
ATOM   1370 C CB  . LEU A 1 186 ? 8.68365   3.65521   3.82835   1.000 44.65481 ?  184 LEU A CB  1 
ATOM   1371 C CG  . LEU A 1 186 ? 8.13675   4.95338   4.39618   1.000 42.96988 ?  184 LEU A CG  1 
ATOM   1372 C CD1 . LEU A 1 186 ? 6.85424   5.28420   3.69839   1.000 47.49723 ?  184 LEU A CD1 1 
ATOM   1373 C CD2 . LEU A 1 186 ? 7.86760   4.74685   5.84830   1.000 38.79130 ?  184 LEU A CD2 1 
ATOM   1374 N N   . TYR A 1 187 ? 11.91708  4.38182   3.28831   1.000 47.53036 ?  185 TYR A N   1 
ATOM   1375 C CA  . TYR A 1 187 ? 13.02517  5.32146   3.46594   1.000 50.55944 ?  185 TYR A CA  1 
ATOM   1376 C C   . TYR A 1 187 ? 13.80110  5.61686   2.17509   1.000 47.94976 ?  185 TYR A C   1 
ATOM   1377 O O   . TYR A 1 187 ? 13.83179  4.82560   1.22911   1.000 45.82545 ?  185 TYR A O   1 
ATOM   1378 C CB  . TYR A 1 187 ? 13.98338  4.80073   4.55302   1.000 52.24873 ?  185 TYR A CB  1 
ATOM   1379 C CG  . TYR A 1 187 ? 15.28690  5.57209   4.66571   1.000 55.14675 ?  185 TYR A CG  1 
ATOM   1380 C CD1 . TYR A 1 187 ? 15.29636  6.96007   4.75303   1.000 56.85191 ?  185 TYR A CD1 1 
ATOM   1381 C CD2 . TYR A 1 187 ? 16.50680  4.90989   4.72295   1.000 56.48488 ?  185 TYR A CD2 1 
ATOM   1382 C CE1 . TYR A 1 187 ? 16.48935  7.66882   4.85715   1.000 57.97581 ?  185 TYR A CE1 1 
ATOM   1383 C CE2 . TYR A 1 187 ? 17.70460  5.60823   4.84051   1.000 55.16017 ?  185 TYR A CE2 1 
ATOM   1384 C CZ  . TYR A 1 187 ? 17.69131  6.98616   4.90653   1.000 58.83204 ?  185 TYR A CZ  1 
ATOM   1385 O OH  . TYR A 1 187 ? 18.88288  7.68173   5.01429   1.000 57.92006 ?  185 TYR A OH  1 
ATOM   1386 N N   . THR B 1 14  ? -39.97057 -16.37629 29.97685  1.000 63.62372 ?  12  THR B N   1 
ATOM   1387 C CA  . THR B 1 14  ? -38.64921 -16.25276 29.36904  1.000 65.63291 ?  12  THR B CA  1 
ATOM   1388 C C   . THR B 1 14  ? -38.28581 -14.81016 29.01110  1.000 60.43714 ?  12  THR B C   1 
ATOM   1389 O O   . THR B 1 14  ? -39.06337 -13.87747 29.22497  1.000 65.04155 ?  12  THR B O   1 
ATOM   1390 C CB  . THR B 1 14  ? -38.52278 -17.11705 28.09271  1.000 64.89875 ?  12  THR B CB  1 
ATOM   1391 O OG1 . THR B 1 14  ? -37.14946 -17.15585 27.66740  1.000 57.07907 ?  12  THR B OG1 1 
ATOM   1392 C CG2 . THR B 1 14  ? -39.41103 -16.56426 26.97415  1.000 69.22771 ?  12  THR B CG2 1 
ATOM   1393 N N   . LEU B 1 15  ? -37.10534 -14.65919 28.42697  1.000 60.57530 ?  13  LEU B N   1 
ATOM   1394 C CA  . LEU B 1 15  ? -36.44625 -13.37346 28.26139  1.000 53.86807 ?  13  LEU B CA  1 
ATOM   1395 C C   . LEU B 1 15  ? -36.64224 -12.83898 26.84571  1.000 48.58563 ?  13  LEU B C   1 
ATOM   1396 O O   . LEU B 1 15  ? -36.32622 -13.53282 25.87393  1.000 49.36411 ?  13  LEU B O   1 
ATOM   1397 C CB  . LEU B 1 15  ? -34.95672 -13.53254 28.52913  1.000 50.87765 ?  13  LEU B CB  1 
ATOM   1398 C CG  . LEU B 1 15  ? -34.22342 -12.25818 28.89987  1.000 45.18613 ?  13  LEU B CG  1 
ATOM   1399 C CD1 . LEU B 1 15  ? -34.94283 -11.62179 30.10077  1.000 49.58220 ?  13  LEU B CD1 1 
ATOM   1400 C CD2 . LEU B 1 15  ? -32.78763 -12.56137 29.17645  1.000 44.25342 ?  13  LEU B CD2 1 
ATOM   1401 N N   . SER B 1 16  ? -37.10117 -11.59395 26.72592  1.000 43.03311 ?  14  SER B N   1 
ATOM   1402 C CA  . SER B 1 16  ? -37.19297 -11.01238 25.38931  1.000 43.65382 ?  14  SER B CA  1 
ATOM   1403 C C   . SER B 1 16  ? -35.79971 -10.83155 24.80489  1.000 41.17807 ?  14  SER B C   1 
ATOM   1404 O O   . SER B 1 16  ? -34.80361 -10.72068 25.52350  1.000 39.19122 ?  14  SER B O   1 
ATOM   1405 C CB  . SER B 1 16  ? -37.88055 -9.64607  25.40253  1.000 43.34990 ?  14  SER B CB  1 
ATOM   1406 O OG  . SER B 1 16  ? -37.19673 -8.73526  26.24981  1.000 40.23773 ?  14  SER B OG  1 
ATOM   1407 N N   . ASP B 1 17  ? -35.73000 -10.76891 23.47815  1.000 40.87158 ?  15  ASP B N   1 
ATOM   1408 C CA  . ASP B 1 17  ? -34.44343 -10.45994 22.87757  1.000 39.17071 ?  15  ASP B CA  1 
ATOM   1409 C C   . ASP B 1 17  ? -34.05719 -9.01394  23.12102  1.000 34.98581 ?  15  ASP B C   1 
ATOM   1410 O O   . ASP B 1 17  ? -32.86998 -8.68726  23.09282  1.000 35.67230 ?  15  ASP B O   1 
ATOM   1411 C CB  . ASP B 1 17  ? -34.43637 -10.75780 21.37717  1.000 41.73091 ?  15  ASP B CB  1 
ATOM   1412 C CG  . ASP B 1 17  ? -34.71178 -12.21699 21.07522  1.000 45.47978 ?  15  ASP B CG  1 
ATOM   1413 O OD1 . ASP B 1 17  ? -33.98113 -13.07949 21.59729  1.000 52.59366 ?  15  ASP B OD1 1 
ATOM   1414 O OD2 . ASP B 1 17  ? -35.63265 -12.50193 20.29711  1.000 47.23665 -1 15  ASP B OD2 1 
ATOM   1415 N N   . GLU B 1 18  ? -35.03277 -8.12996  23.32666  1.000 35.10981 ?  16  GLU B N   1 
ATOM   1416 C CA  . GLU B 1 18  ? -34.66451 -6.75787  23.63992  1.000 36.10245 ?  16  GLU B CA  1 
ATOM   1417 C C   . GLU B 1 18  ? -33.90383 -6.71390  24.95236  1.000 33.23128 ?  16  GLU B C   1 
ATOM   1418 O O   . GLU B 1 18  ? -32.93027 -5.97142  25.08463  1.000 30.74936 ?  16  GLU B O   1 
ATOM   1419 C CB  . GLU B 1 18  ? -35.90016 -5.85780  23.70770  1.000 34.02297 ?  16  GLU B CB  1 
ATOM   1420 C CG  . GLU B 1 18  ? -35.60652 -4.41507  24.17483  1.000 31.27179 ?  16  GLU B CG  1 
ATOM   1421 C CD  . GLU B 1 18  ? -35.60311 -4.28945  25.71161  1.000 31.92733 ?  16  GLU B CD  1 
ATOM   1422 O OE1 . GLU B 1 18  ? -36.42855 -4.95145  26.36851  1.000 32.79405 ?  16  GLU B OE1 1 
ATOM   1423 O OE2 . GLU B 1 18  ? -34.73503 -3.56957  26.27468  1.000 31.17668 -1 16  GLU B OE2 1 
ATOM   1424 N N   . LYS B 1 19  ? -34.32944 -7.51737  25.93067  1.000 33.38435 ?  17  LYS B N   1 
ATOM   1425 C CA  . LYS B 1 19  ? -33.68166 -7.46891  27.23000  1.000 33.42078 ?  17  LYS B CA  1 
ATOM   1426 C C   . LYS B 1 19  ? -32.32661 -8.17625  27.19272  1.000 33.89303 ?  17  LYS B C   1 
ATOM   1427 O O   . LYS B 1 19  ? -31.35337 -7.68302  27.77268  1.000 31.10885 ?  17  LYS B O   1 
ATOM   1428 C CB  . LYS B 1 19  ? -34.61860 -8.04446  28.29148  1.000 35.54052 ?  17  LYS B CB  1 
ATOM   1429 C CG  . LYS B 1 19  ? -34.38497 -7.45963  29.68254  1.000 38.21592 ?  17  LYS B CG  1 
ATOM   1430 C CD  . LYS B 1 19  ? -35.31219 -8.08321  30.72658  1.000 41.18123 ?  17  LYS B CD  1 
ATOM   1431 C CE  . LYS B 1 19  ? -36.61210 -7.31060  30.90451  1.000 36.08844 ?  17  LYS B CE  1 
ATOM   1432 N NZ  . LYS B 1 19  ? -37.54760 -8.04377  31.80848  1.000 40.19161 ?  17  LYS B NZ  1 
ATOM   1433 N N   . ARG B 1 20  ? -32.22617 -9.30281  26.47798  1.000 34.05064 ?  18  ARG B N   1 
ATOM   1434 C CA  . ARG B 1 20  ? -30.92498 -9.95305  26.30310  1.000 33.82304 ?  18  ARG B CA  1 
ATOM   1435 C C   . ARG B 1 20  ? -29.90579 -9.00017  25.69664  1.000 29.37741 ?  18  ARG B C   1 
ATOM   1436 O O   . ARG B 1 20  ? -28.78105 -8.86043  26.19597  1.000 26.48567 ?  18  ARG B O   1 
ATOM   1437 C CB  . ARG B 1 20  ? -31.06940 -11.18560 25.41578  1.000 38.42135 ?  18  ARG B CB  1 
ATOM   1438 C CG  . ARG B 1 20  ? -29.95812 -12.19893 25.54931  1.000 39.43412 ?  18  ARG B CG  1 
ATOM   1439 C CD  . ARG B 1 20  ? -30.42584 -13.53869 24.98101  1.000 42.84927 ?  18  ARG B CD  1 
ATOM   1440 N NE  . ARG B 1 20  ? -29.45485 -14.61292 25.16940  1.000 45.47565 ?  18  ARG B NE  1 
ATOM   1441 C CZ  . ARG B 1 20  ? -28.21037 -14.61757 24.70924  1.000 39.45807 ?  18  ARG B CZ  1 
ATOM   1442 N NH1 . ARG B 1 20  ? -27.74248 -13.63490 23.95780  1.000 37.29489 ?  18  ARG B NH1 1 
ATOM   1443 N NH2 . ARG B 1 20  ? -27.41404 -15.64309 25.00958  1.000 39.48824 ?  18  ARG B NH2 1 
ATOM   1444 N N   . ASN B 1 21  ? -30.27417 -8.34496  24.59846  1.000 30.61881 ?  19  ASN B N   1 
ATOM   1445 C CA  . ASN B 1 21  ? -29.34493 -7.42417  23.96015  1.000 30.53084 ?  19  ASN B CA  1 
ATOM   1446 C C   . ASN B 1 21  ? -29.04617 -6.23112  24.85055  1.000 28.64050 ?  19  ASN B C   1 
ATOM   1447 O O   . ASN B 1 21  ? -27.97649 -5.63132  24.73624  1.000 29.98676 ?  19  ASN B O   1 
ATOM   1448 C CB  . ASN B 1 21  ? -29.91686 -6.97964  22.61503  1.000 33.51314 ?  19  ASN B CB  1 
ATOM   1449 C CG  . ASN B 1 21  ? -29.79248 -8.06191  21.57684  1.000 35.87267 ?  19  ASN B CG  1 
ATOM   1450 O OD1 . ASN B 1 21  ? -28.81106 -8.80450  21.58270  1.000 38.57326 ?  19  ASN B OD1 1 
ATOM   1451 N ND2 . ASN B 1 21  ? -30.82259 -8.23087  20.74826  1.000 37.87092 ?  19  ASN B ND2 1 
ATOM   1452 N N   . HIS B 1 22  ? -29.97661 -5.88412  25.73793  1.000 29.29097 ?  20  HIS B N   1 
ATOM   1453 C CA  . HIS B 1 22  ? -29.77392 -4.76080  26.63988  1.000 29.95375 ?  20  HIS B CA  1 
ATOM   1454 C C   . HIS B 1 22  ? -28.73697 -5.09698  27.70898  1.000 28.37460 ?  20  HIS B C   1 
ATOM   1455 O O   . HIS B 1 22  ? -27.93610 -4.23880  28.09192  1.000 27.95032 ?  20  HIS B O   1 
ATOM   1456 C CB  . HIS B 1 22  ? -31.11110 -4.37775  27.25596  1.000 28.07783 ?  20  HIS B CB  1 
ATOM   1457 C CG  . HIS B 1 22  ? -31.00732 -3.65719  28.56310  1.000 28.21129 ?  20  HIS B CG  1 
ATOM   1458 N ND1 . HIS B 1 22  ? -30.68596 -2.31915  28.65416  1.000 27.98360 ?  20  HIS B ND1 1 
ATOM   1459 C CD2 . HIS B 1 22  ? -31.17153 -4.09405  29.83362  1.000 29.30114 ?  20  HIS B CD2 1 
ATOM   1460 C CE1 . HIS B 1 22  ? -30.67830 -1.95793  29.92542  1.000 29.68622 ?  20  HIS B CE1 1 
ATOM   1461 N NE2 . HIS B 1 22  ? -30.96914 -3.01635  30.66074  1.000 29.55894 ?  20  HIS B NE2 1 
ATOM   1462 N N   . ILE B 1 23  ? -28.74817 -6.33348  28.21096  1.000 27.24289 ?  21  ILE B N   1 
ATOM   1463 C CA  . ILE B 1 23  ? -27.69861 -6.77067  29.13787  1.000 28.39727 ?  21  ILE B CA  1 
ATOM   1464 C C   . ILE B 1 23  ? -26.34387 -6.67046  28.47040  1.000 29.96379 ?  21  ILE B C   1 
ATOM   1465 O O   . ILE B 1 23  ? -25.36365 -6.21711  29.07954  1.000 27.48580 ?  21  ILE B O   1 
ATOM   1466 C CB  . ILE B 1 23  ? -27.96961 -8.20768  29.62268  1.000 27.38786 ?  21  ILE B CB  1 
ATOM   1467 C CG1 . ILE B 1 23  ? -29.38042 -8.32795  30.20443  1.000 30.13248 ?  21  ILE B CG1 1 
ATOM   1468 C CG2 . ILE B 1 23  ? -26.95440 -8.64474  30.68662  1.000 30.93107 ?  21  ILE B CG2 1 
ATOM   1469 C CD1 . ILE B 1 23  ? -29.84780 -9.77995  30.30628  1.000 30.68176 ?  21  ILE B CD1 1 
ATOM   1470 N N   . LEU B 1 24  ? -26.26520 -7.10286  27.20385  1.000 28.31142 ?  22  LEU B N   1 
ATOM   1471 C CA  . LEU B 1 24  ? -24.99313 -7.09255  26.48194  1.000 26.62121 ?  22  LEU B CA  1 
ATOM   1472 C C   . LEU B 1 24  ? -24.48409 -5.67602  26.28805  1.000 27.74069 ?  22  LEU B C   1 
ATOM   1473 O O   . LEU B 1 24  ? -23.29948 -5.39188  26.52437  1.000 28.47018 ?  22  LEU B O   1 
ATOM   1474 C CB  . LEU B 1 24  ? -25.14172 -7.80123  25.13087  1.000 27.00853 ?  22  LEU B CB  1 
ATOM   1475 C CG  . LEU B 1 24  ? -25.26654 -9.33459  25.18390  1.000 30.02823 ?  22  LEU B CG  1 
ATOM   1476 C CD1 . LEU B 1 24  ? -25.64544 -9.87031  23.82959  1.000 27.63954 ?  22  LEU B CD1 1 
ATOM   1477 C CD2 . LEU B 1 24  ? -23.94599 -9.99917  25.66044  1.000 27.84030 ?  22  LEU B CD2 1 
ATOM   1478 N N   . THR B 1 25  ? -25.36715 -4.76894  25.86388  1.000 28.95433 ?  23  THR B N   1 
ATOM   1479 C CA  . THR B 1 25  ? -24.93981 -3.40310  25.57165  1.000 31.22758 ?  23  THR B CA  1 
ATOM   1480 C C   . THR B 1 25  ? -24.66896 -2.60451  26.83928  1.000 29.44269 ?  23  THR B C   1 
ATOM   1481 O O   . THR B 1 25  ? -23.82919 -1.69995  26.81445  1.000 29.33694 ?  23  THR B O   1 
ATOM   1482 C CB  . THR B 1 25  ? -25.97764 -2.66568  24.71165  1.000 28.62178 ?  23  THR B CB  1 
ATOM   1483 O OG1 . THR B 1 25  ? -27.22842 -2.57976  25.40201  1.000 29.72244 ?  23  THR B OG1 1 
ATOM   1484 C CG2 . THR B 1 25  ? -26.18163 -3.34926  23.36090  1.000 30.52716 ?  23  THR B CG2 1 
ATOM   1485 N N   . THR B 1 26  ? -25.36413 -2.92102  27.93898  1.000 30.64542 ?  24  THR B N   1 
ATOM   1486 C CA  . THR B 1 26  ? -25.06580 -2.30550  29.23102  1.000 30.26499 ?  24  THR B CA  1 
ATOM   1487 C C   . THR B 1 26  ? -23.67234 -2.70158  29.70153  1.000 31.11739 ?  24  THR B C   1 
ATOM   1488 O O   . THR B 1 26  ? -22.87452 -1.85506  30.12629  1.000 30.12170 ?  24  THR B O   1 
ATOM   1489 C CB  . THR B 1 26  ? -26.11534 -2.71835  30.27025  1.000 31.25877 ?  24  THR B CB  1 
ATOM   1490 O OG1 . THR B 1 26  ? -27.34241 -2.02287  30.02733  1.000 30.48068 ?  24  THR B OG1 1 
ATOM   1491 C CG2 . THR B 1 26  ? -25.65995 -2.39071  31.68705  1.000 31.42272 ?  24  THR B CG2 1 
ATOM   1492 N N   . ALA B 1 27  ? -23.37343 -3.99752  29.64344  1.000 25.75984 ?  25  ALA B N   1 
ATOM   1493 C CA  . ALA B 1 27  ? -22.06804 -4.47552  30.05209  1.000 31.33488 ?  25  ALA B CA  1 
ATOM   1494 C C   . ALA B 1 27  ? -20.97386 -3.84873  29.20201  1.000 30.27212 ?  25  ALA B C   1 
ATOM   1495 O O   . ALA B 1 27  ? -19.96179 -3.37464  29.73510  1.000 31.04532 ?  25  ALA B O   1 
ATOM   1496 C CB  . ALA B 1 27  ? -22.02972 -5.99929  29.96702  1.000 28.55740 ?  25  ALA B CB  1 
ATOM   1497 N N   . LEU B 1 28  ? -21.18244 -3.78947  27.88202  1.000 28.72172 ?  26  LEU B N   1 
ATOM   1498 C CA  . LEU B 1 28  ? -20.18285 -3.19989  26.99583  1.000 32.31630 ?  26  LEU B CA  1 
ATOM   1499 C C   . LEU B 1 28  ? -19.86149 -1.76816  27.40550  1.000 32.91763 ?  26  LEU B C   1 
ATOM   1500 O O   . LEU B 1 28  ? -18.69057 -1.39312  27.50029  1.000 31.27887 ?  26  LEU B O   1 
ATOM   1501 C CB  . LEU B 1 28  ? -20.64836 -3.26198  25.53765  1.000 30.81470 ?  26  LEU B CB  1 
ATOM   1502 C CG  . LEU B 1 28  ? -20.38895 -4.59175  24.82933  1.000 30.62322 ?  26  LEU B CG  1 
ATOM   1503 C CD1 . LEU B 1 28  ? -20.92065 -4.55683  23.41842  1.000 33.01306 ?  26  LEU B CD1 1 
ATOM   1504 C CD2 . LEU B 1 28  ? -18.91903 -4.92753  24.79792  1.000 30.13370 ?  26  LEU B CD2 1 
ATOM   1505 N N   . ASN B 1 29  ? -20.89109 -0.96654  27.69379  1.000 31.12862 ?  27  ASN B N   1 
ATOM   1506 C CA  . ASN B 1 29  ? -20.65563 0.37653   28.21289  1.000 33.95522 ?  27  ASN B CA  1 
ATOM   1507 C C   . ASN B 1 29  ? -19.89748 0.33931   29.53786  1.000 35.37901 ?  27  ASN B C   1 
ATOM   1508 O O   . ASN B 1 29  ? -18.95992 1.12012   29.73586  1.000 37.56590 ?  27  ASN B O   1 
ATOM   1509 C CB  . ASN B 1 29  ? -21.98103 1.12721   28.34286  1.000 35.88487 ?  27  ASN B CB  1 
ATOM   1510 C CG  . ASN B 1 29  ? -22.17347 2.16577   27.23760  1.000 46.14685 ?  27  ASN B CG  1 
ATOM   1511 O OD1 . ASN B 1 29  ? -21.89314 1.89996   26.06246  1.000 46.29246 ?  27  ASN B OD1 1 
ATOM   1512 N ND2 . ASN B 1 29  ? -22.68513 3.34231   27.60505  1.000 49.94929 ?  27  ASN B ND2 1 
ATOM   1513 N N   . LEU B 1 30  ? -20.25252 -0.58582  30.44044  1.000 33.40876 ?  28  LEU B N   1 
ATOM   1514 C CA  . LEU B 1 30  ? -19.49669 -0.73911  31.68676  1.000 30.93206 ?  28  LEU B CA  1 
ATOM   1515 C C   . LEU B 1 30  ? -18.03208 -1.05609  31.41218  1.000 38.00733 ?  28  LEU B C   1 
ATOM   1516 O O   . LEU B 1 30  ? -17.12921 -0.42031  31.97648  1.000 36.14757 ?  28  LEU B O   1 
ATOM   1517 C CB  . LEU B 1 30  ? -20.10059 -1.84449  32.55322  1.000 30.98239 ?  28  LEU B CB  1 
ATOM   1518 C CG  . LEU B 1 30  ? -21.40657 -1.54696  33.28165  1.000 31.57243 ?  28  LEU B CG  1 
ATOM   1519 C CD1 . LEU B 1 30  ? -21.92860 -2.77255  33.99804  1.000 31.51415 ?  28  LEU B CD1 1 
ATOM   1520 C CD2 . LEU B 1 30  ? -21.24077 -0.38963  34.25049  1.000 36.48280 ?  28  LEU B CD2 1 
ATOM   1521 N N   . PHE B 1 31  ? -17.78295 -2.06976  30.57130  1.000 32.83333 ?  29  PHE B N   1 
ATOM   1522 C CA  . PHE B 1 31  ? -16.42446 -2.51632  30.29996  1.000 37.40756 ?  29  PHE B CA  1 
ATOM   1523 C C   . PHE B 1 31  ? -15.61244 -1.41493  29.63912  1.000 39.48562 ?  29  PHE B C   1 
ATOM   1524 O O   . PHE B 1 31  ? -14.43217 -1.23554  29.94754  1.000 38.34497 ?  29  PHE B O   1 
ATOM   1525 C CB  . PHE B 1 31  ? -16.44195 -3.74728  29.39075  1.000 36.55634 ?  29  PHE B CB  1 
ATOM   1526 C CG  . PHE B 1 31  ? -17.12310 -4.95061  29.98822  1.000 34.95923 ?  29  PHE B CG  1 
ATOM   1527 C CD1 . PHE B 1 31  ? -17.08828 -5.17976  31.34573  1.000 32.87470 ?  29  PHE B CD1 1 
ATOM   1528 C CD2 . PHE B 1 31  ? -17.80398 -5.84859  29.16762  1.000 30.76491 ?  29  PHE B CD2 1 
ATOM   1529 C CE1 . PHE B 1 31  ? -17.68245 -6.29173  31.88568  1.000 35.24396 ?  29  PHE B CE1 1 
ATOM   1530 C CE2 . PHE B 1 31  ? -18.41466 -6.96524  29.70526  1.000 31.63144 ?  29  PHE B CE2 1 
ATOM   1531 C CZ  . PHE B 1 31  ? -18.36359 -7.18078  31.06024  1.000 34.50841 ?  29  PHE B CZ  1 
ATOM   1532 N N   . ASP B 1 32  ? -16.23125 -0.67165  28.71960  1.000 37.35915 ?  30  ASP B N   1 
ATOM   1533 C CA  . ASP B 1 32  ? -15.49095 0.34421   27.98590  1.000 42.44607 ?  30  ASP B CA  1 
ATOM   1534 C C   . ASP B 1 32  ? -14.90175 1.37917   28.93041  1.000 43.47056 ?  30  ASP B C   1 
ATOM   1535 O O   . ASP B 1 32  ? -13.80535 1.89925   28.68505  1.000 43.85172 ?  30  ASP B O   1 
ATOM   1536 C CB  . ASP B 1 32  ? -16.40034 1.00470   26.95534  1.000 40.87832 ?  30  ASP B CB  1 
ATOM   1537 C CG  . ASP B 1 32  ? -15.64393 1.90872   25.99452  1.000 47.92166 ?  30  ASP B CG  1 
ATOM   1538 O OD1 . ASP B 1 32  ? -14.82201 1.38759   25.19735  1.000 45.05315 ?  30  ASP B OD1 1 
ATOM   1539 O OD2 . ASP B 1 32  ? -15.89231 3.13642   26.01903  1.000 49.92862 -1 30  ASP B OD2 1 
ATOM   1540 N N   . GLN B 1 33  ? -15.57700 1.63925   30.04251  1.000 42.11531 ?  31  GLN B N   1 
ATOM   1541 C CA  . GLN B 1 33  ? -15.17417 2.72020   30.91932  1.000 45.65652 ?  31  GLN B CA  1 
ATOM   1542 C C   . GLN B 1 33  ? -14.50711 2.26181   32.21317  1.000 45.62487 ?  31  GLN B C   1 
ATOM   1543 O O   . GLN B 1 33  ? -13.71686 3.02624   32.77745  1.000 46.29227 ?  31  GLN B O   1 
ATOM   1544 C CB  . GLN B 1 33  ? -16.39689 3.61309   31.18024  1.000 48.19190 ?  31  GLN B CB  1 
ATOM   1545 C CG  . GLN B 1 33  ? -16.59067 4.23172   32.53045  1.000 48.95178 ?  31  GLN B CG  1 
ATOM   1546 C CD  . GLN B 1 33  ? -18.04226 4.63129   32.70842  1.000 53.51539 ?  31  GLN B CD  1 
ATOM   1547 O OE1 . GLN B 1 33  ? -18.89273 4.31010   31.87083  1.000 55.23000 ?  31  GLN B OE1 1 
ATOM   1548 N NE2 . GLN B 1 33  ? -18.32740 5.38229   33.76298  1.000 55.32015 ?  31  GLN B NE2 1 
ATOM   1549 N N   . PHE B 1 34  ? -14.72596 1.01870   32.65756  1.000 42.58763 ?  32  PHE B N   1 
ATOM   1550 C CA  . PHE B 1 34  ? -14.01207 0.49361   33.81978  1.000 44.46908 ?  32  PHE B CA  1 
ATOM   1551 C C   . PHE B 1 34  ? -13.16826 -0.75204  33.57479  1.000 44.19045 ?  32  PHE B C   1 
ATOM   1552 O O   . PHE B 1 34  ? -12.46299 -1.17681  34.49607  1.000 44.95349 ?  32  PHE B O   1 
ATOM   1553 C CB  . PHE B 1 34  ? -14.96334 0.17706   34.98948  1.000 42.90485 ?  32  PHE B CB  1 
ATOM   1554 C CG  . PHE B 1 34  ? -15.90737 1.27647   35.33941  1.000 44.38312 ?  32  PHE B CG  1 
ATOM   1555 C CD1 . PHE B 1 34  ? -17.12585 1.40982   34.70748  1.000 46.35600 ?  32  PHE B CD1 1 
ATOM   1556 C CD2 . PHE B 1 34  ? -15.53949 2.22404   36.27826  1.000 46.22812 ?  32  PHE B CD2 1 
ATOM   1557 C CE1 . PHE B 1 34  ? -17.98483 2.42698   35.05499  1.000 47.05784 ?  32  PHE B CE1 1 
ATOM   1558 C CE2 . PHE B 1 34  ? -16.37972 3.25850   36.60964  1.000 47.02691 ?  32  PHE B CE2 1 
ATOM   1559 C CZ  . PHE B 1 34  ? -17.60714 3.36241   35.99513  1.000 51.39338 ?  32  PHE B CZ  1 
ATOM   1560 N N   . GLY B 1 35  ? -13.22102 -1.36024  32.39516  1.000 40.47483 ?  33  GLY B N   1 
ATOM   1561 C CA  . GLY B 1 35  ? -12.48893 -2.58427  32.14590  1.000 41.17682 ?  33  GLY B CA  1 
ATOM   1562 C C   . GLY B 1 35  ? -13.22800 -3.80469  32.65222  1.000 39.58305 ?  33  GLY B C   1 
ATOM   1563 O O   . GLY B 1 35  ? -14.19977 -3.71657  33.39926  1.000 39.64279 ?  33  GLY B O   1 
ATOM   1564 N N   . PHE B 1 36  ? -12.74598 -4.98380  32.23803  1.000 38.97750 ?  34  PHE B N   1 
ATOM   1565 C CA  . PHE B 1 36  ? -13.50242 -6.20470  32.50911  1.000 40.39133 ?  34  PHE B CA  1 
ATOM   1566 C C   . PHE B 1 36  ? -13.36837 -6.65261  33.95688  1.000 46.65731 ?  34  PHE B C   1 
ATOM   1567 O O   . PHE B 1 36  ? -14.34711 -7.11753  34.55523  1.000 48.02099 ?  34  PHE B O   1 
ATOM   1568 C CB  . PHE B 1 36  ? -13.08250 -7.34093  31.57232  1.000 41.41679 ?  34  PHE B CB  1 
ATOM   1569 C CG  . PHE B 1 36  ? -13.40013 -7.09545  30.10448  1.000 38.81205 ?  34  PHE B CG  1 
ATOM   1570 C CD1 . PHE B 1 36  ? -12.47148 -6.49504  29.25919  1.000 35.97462 ?  34  PHE B CD1 1 
ATOM   1571 C CD2 . PHE B 1 36  ? -14.65024 -7.42652  29.58707  1.000 35.19004 ?  34  PHE B CD2 1 
ATOM   1572 C CE1 . PHE B 1 36  ? -12.74906 -6.27753  27.91899  1.000 33.45560 ?  34  PHE B CE1 1 
ATOM   1573 C CE2 . PHE B 1 36  ? -14.95179 -7.20748  28.24295  1.000 34.57775 ?  34  PHE B CE2 1 
ATOM   1574 C CZ  . PHE B 1 36  ? -14.00009 -6.61899  27.40016  1.000 35.74248 ?  34  PHE B CZ  1 
ATOM   1575 N N   . GLN B 1 37  ? -12.17573 -6.49242  34.53637  1.000 48.51871 ?  35  GLN B N   1 
ATOM   1576 C CA  . GLN B 1 37  ? -11.88519 -7.02260  35.86661  1.000 51.32633 ?  35  GLN B CA  1 
ATOM   1577 C C   . GLN B 1 37  ? -12.78860 -6.40798  36.92527  1.000 45.98640 ?  35  GLN B C   1 
ATOM   1578 O O   . GLN B 1 37  ? -13.36253 -7.11367  37.75661  1.000 44.14414 ?  35  GLN B O   1 
ATOM   1579 C CB  . GLN B 1 37  ? -10.40854 -6.76512  36.18664  1.000 53.61012 ?  35  GLN B CB  1 
ATOM   1580 C CG  . GLN B 1 37  ? -9.46263  -7.53185  35.25634  1.000 56.37803 ?  35  GLN B CG  1 
ATOM   1581 C CD  . GLN B 1 37  ? -8.92254  -6.69701  34.08921  1.000 57.56861 ?  35  GLN B CD  1 
ATOM   1582 O OE1 . GLN B 1 37  ? -9.69223  -6.18775  33.24862  1.000 48.33090 ?  35  GLN B OE1 1 
ATOM   1583 N NE2 . GLN B 1 37  ? -7.59171  -6.57394  34.01957  1.000 50.79324 ?  35  GLN B NE2 1 
ATOM   1584 N N   . HIS B 1 38  ? -12.91900 -5.08734  36.90080  1.000 45.39847 ?  36  HIS B N   1 
ATOM   1585 C CA  . HIS B 1 38  ? -13.65176 -4.34266  37.90996  1.000 45.62634 ?  36  HIS B CA  1 
ATOM   1586 C C   . HIS B 1 38  ? -15.13475 -4.73331  38.01513  1.000 43.64913 ?  36  HIS B C   1 
ATOM   1587 O O   . HIS B 1 38  ? -15.75353 -4.46582  39.05000  1.000 42.92373 ?  36  HIS B O   1 
ATOM   1588 C CB  . HIS B 1 38  ? -13.49579 -2.85094  37.56923  1.000 48.26611 ?  36  HIS B CB  1 
ATOM   1589 C CG  . HIS B 1 38  ? -13.69537 -1.92294  38.73086  1.000 58.63559 ?  36  HIS B CG  1 
ATOM   1590 N ND1 . HIS B 1 38  ? -13.69617 -0.54886  38.59046  1.000 57.67441 ?  36  HIS B ND1 1 
ATOM   1591 C CD2 . HIS B 1 38  ? -13.90362 -2.16671  40.04838  1.000 61.25881 ?  36  HIS B CD2 1 
ATOM   1592 C CE1 . HIS B 1 38  ? -13.89854 0.01195   39.77120  1.000 62.25298 ?  36  HIS B CE1 1 
ATOM   1593 N NE2 . HIS B 1 38  ? -14.02686 -0.94707  40.67243  1.000 64.77653 ?  36  HIS B NE2 1 
ATOM   1594 N N   . ILE B 1 39  ? -15.71714 -5.35919  36.98896  1.000 42.76924 ?  37  ILE B N   1 
ATOM   1595 C CA  . ILE B 1 39  ? -17.17163 -5.42262  36.80900  1.000 35.99571 ?  37  ILE B CA  1 
ATOM   1596 C C   . ILE B 1 39  ? -17.67304 -6.85208  36.98037  1.000 39.02736 ?  37  ILE B C   1 
ATOM   1597 O O   . ILE B 1 39  ? -17.40458 -7.71307  36.13458  1.000 39.30582 ?  37  ILE B O   1 
ATOM   1598 C CB  . ILE B 1 39  ? -17.59194 -4.89389  35.43215  1.000 35.09599 ?  37  ILE B CB  1 
ATOM   1599 C CG1 . ILE B 1 39  ? -17.09695 -3.46453  35.22761  1.000 36.08563 ?  37  ILE B CG1 1 
ATOM   1600 C CG2 . ILE B 1 39  ? -19.12842 -5.01330  35.24333  1.000 36.13182 ?  37  ILE B CG2 1 
ATOM   1601 C CD1 . ILE B 1 39  ? -17.74286 -2.47404  36.16222  1.000 36.47827 ?  37  ILE B CD1 1 
ATOM   1602 N N   . SER B 1 40  ? -18.49705 -7.07991  38.00183  1.000 33.76158 ?  38  SER B N   1 
ATOM   1603 C CA  . SER B 1 40  ? -19.03799 -8.40952  38.25389  1.000 35.19415 ?  38  SER B CA  1 
ATOM   1604 C C   . SER B 1 40  ? -20.38185 -8.61269  37.54479  1.000 36.85742 ?  38  SER B C   1 
ATOM   1605 O O   . SER B 1 40  ? -20.93723 -7.70657  36.92435  1.000 34.99412 ?  38  SER B O   1 
ATOM   1606 C CB  . SER B 1 40  ? -19.19736 -8.65025  39.75123  1.000 34.63704 ?  38  SER B CB  1 
ATOM   1607 O OG  . SER B 1 40  ? -20.18866 -7.79777  40.30080  1.000 33.81604 ?  38  SER B OG  1 
ATOM   1608 N N   . ILE B 1 41  ? -20.88509 -9.84578  37.62720  1.000 37.55220 ?  39  ILE B N   1 
ATOM   1609 C CA  . ILE B 1 41  ? -22.23154 -10.14875 37.15451  1.000 41.38852 ?  39  ILE B CA  1 
ATOM   1610 C C   . ILE B 1 41  ? -23.25028 -9.31746  37.92397  1.000 38.09221 ?  39  ILE B C   1 
ATOM   1611 O O   . ILE B 1 41  ? -24.15104 -8.71228  37.33735  1.000 38.36864 ?  39  ILE B O   1 
ATOM   1612 C CB  . ILE B 1 41  ? -22.52709 -11.65280 37.30140  1.000 40.96131 ?  39  ILE B CB  1 
ATOM   1613 C CG1 . ILE B 1 41  ? -21.70691 -12.49089 36.30948  1.000 44.09061 ?  39  ILE B CG1 1 
ATOM   1614 C CG2 . ILE B 1 41  ? -23.95787 -11.90412 36.99805  1.000 38.35553 ?  39  ILE B CG2 1 
ATOM   1615 C CD1 . ILE B 1 41  ? -21.96513 -14.01576 36.44899  1.000 38.23428 ?  39  ILE B CD1 1 
ATOM   1616 N N   . MET B 1 42  ? -23.10645 -9.25609  39.25273  1.000 34.98835 ?  40  MET B N   1 
ATOM   1617 C CA  . MET B 1 42  ? -24.07240 -8.49899  40.05241  1.000 39.75680 ?  40  MET B CA  1 
ATOM   1618 C C   . MET B 1 42  ? -24.05227 -7.01168  39.74690  1.000 35.83217 ?  40  MET B C   1 
ATOM   1619 O O   . MET B 1 42  ? -25.09218 -6.34846  39.82716  1.000 34.23857 ?  40  MET B O   1 
ATOM   1620 C CB  . MET B 1 42  ? -23.84280 -8.72360  41.54593  1.000 44.07385 ?  40  MET B CB  1 
ATOM   1621 C CG  . MET B 1 42  ? -24.10998 -10.14387 42.02587  1.000 46.98477 ?  40  MET B CG  1 
ATOM   1622 S SD  . MET B 1 42  ? -25.90370 -10.46194 42.02763  1.000 65.66021 ?  40  MET B SD  1 
ATOM   1623 C CE  . MET B 1 42  ? -26.56584 -8.86019  42.52879  1.000 55.93753 ?  40  MET B CE  1 
ATOM   1624 N N   . ARG B 1 43  ? -22.88395 -6.46151  39.44954  1.000 34.31655 ?  41  ARG B N   1 
ATOM   1625 C CA  . ARG B 1 43  ? -22.82403 -5.07927  38.99951  1.000 35.37287 ?  41  ARG B CA  1 
ATOM   1626 C C   . ARG B 1 43  ? -23.55476 -4.91018  37.66893  1.000 35.64881 ?  41  ARG B C   1 
ATOM   1627 O O   . ARG B 1 43  ? -24.31879 -3.95296  37.48896  1.000 29.31630 ?  41  ARG B O   1 
ATOM   1628 C CB  . ARG B 1 43  ? -21.36296 -4.65849  38.88221  1.000 34.01921 ?  41  ARG B CB  1 
ATOM   1629 C CG  . ARG B 1 43  ? -21.11542 -3.31024  38.24573  1.000 35.61547 ?  41  ARG B CG  1 
ATOM   1630 C CD  . ARG B 1 43  ? -21.79606 -2.17869  38.98401  1.000 33.95070 ?  41  ARG B CD  1 
ATOM   1631 N NE  . ARG B 1 43  ? -21.26855 -0.87589  38.59035  1.000 42.69288 ?  41  ARG B NE  1 
ATOM   1632 C CZ  . ARG B 1 43  ? -20.02145 -0.47031  38.80568  1.000 40.74259 ?  41  ARG B CZ  1 
ATOM   1633 N NH1 . ARG B 1 43  ? -19.14039 -1.24036  39.41961  1.000 43.73054 ?  41  ARG B NH1 1 
ATOM   1634 N NH2 . ARG B 1 43  ? -19.65391 0.74420   38.40416  1.000 43.70218 ?  41  ARG B NH2 1 
ATOM   1635 N N   . ILE B 1 44  ? -23.33201 -5.84199  36.73621  1.000 32.54901 ?  42  ILE B N   1 
ATOM   1636 C CA  . ILE B 1 44  ? -23.98941 -5.80339  35.43220  1.000 34.45710 ?  42  ILE B CA  1 
ATOM   1637 C C   . ILE B 1 44  ? -25.50099 -5.89643  35.59664  1.000 34.35356 ?  42  ILE B C   1 
ATOM   1638 O O   . ILE B 1 44  ? -26.25745 -5.18333  34.92984  1.000 32.70306 ?  42  ILE B O   1 
ATOM   1639 C CB  . ILE B 1 44  ? -23.45961 -6.94383  34.54675  1.000 32.95772 ?  42  ILE B CB  1 
ATOM   1640 C CG1 . ILE B 1 44  ? -22.03897 -6.65892  34.08972  1.000 35.82921 ?  42  ILE B CG1 1 
ATOM   1641 C CG2 . ILE B 1 44  ? -24.37614 -7.16728  33.35938  1.000 34.05878 ?  42  ILE B CG2 1 
ATOM   1642 C CD1 . ILE B 1 44  ? -21.35506 -7.87852  33.54834  1.000 38.03085 ?  42  ILE B CD1 1 
ATOM   1643 N N   . ILE B 1 45  ? -25.95101 -6.78536  36.49181  1.000 32.81993 ?  43  ILE B N   1 
ATOM   1644 C CA  . ILE B 1 45  ? -27.36691 -7.01596  36.75466  1.000 35.44060 ?  43  ILE B CA  1 
ATOM   1645 C C   . ILE B 1 45  ? -28.00582 -5.77269  37.34612  1.000 36.64826 ?  43  ILE B C   1 
ATOM   1646 O O   . ILE B 1 45  ? -29.13094 -5.39939  36.99255  1.000 34.31028 ?  43  ILE B O   1 
ATOM   1647 C CB  . ILE B 1 45  ? -27.50871 -8.21874  37.70789  1.000 38.76258 ?  43  ILE B CB  1 
ATOM   1648 C CG1 . ILE B 1 45  ? -27.53984 -9.53455  36.93254  1.000 38.58946 ?  43  ILE B CG1 1 
ATOM   1649 C CG2 . ILE B 1 45  ? -28.69212 -8.06449  38.67293  1.000 43.09688 ?  43  ILE B CG2 1 
ATOM   1650 C CD1 . ILE B 1 45  ? -27.23366 -10.71022 37.82933  1.000 43.66640 ?  43  ILE B CD1 1 
ATOM   1651 N N   . THR B 1 46  ? -27.30654 -5.12610  38.28147  1.000 35.35467 ?  44  THR B N   1 
ATOM   1652 C CA  . THR B 1 46  ? -27.84378 -3.91355  38.87932  1.000 36.98248 ?  44  THR B CA  1 
ATOM   1653 C C   . THR B 1 46  ? -27.85190 -2.76135  37.87941  1.000 36.56949 ?  44  THR B C   1 
ATOM   1654 O O   . THR B 1 46  ? -28.83650 -2.02408  37.79313  1.000 34.81128 ?  44  THR B O   1 
ATOM   1655 C CB  . THR B 1 46  ? -27.04817 -3.53739  40.11967  1.000 37.67711 ?  44  THR B CB  1 
ATOM   1656 O OG1 . THR B 1 46  ? -26.86690 -4.71041  40.91537  1.000 43.56421 ?  44  THR B OG1 1 
ATOM   1657 C CG2 . THR B 1 46  ? -27.85133 -2.52482  40.92849  1.000 40.86829 ?  44  THR B CG2 1 
ATOM   1658 N N   . GLU B 1 47  ? -26.77657 -2.58622  37.10580  1.000 34.85247 ?  45  GLU B N   1 
ATOM   1659 C CA  . GLU B 1 47  ? -26.80939 -1.53510  36.08814  1.000 34.92333 ?  45  GLU B CA  1 
ATOM   1660 C C   . GLU B 1 47  ? -27.90382 -1.77615  35.04547  1.000 34.75841 ?  45  GLU B C   1 
ATOM   1661 O O   . GLU B 1 47  ? -28.61798 -0.84237  34.66587  1.000 34.09802 ?  45  GLU B O   1 
ATOM   1662 C CB  . GLU B 1 47  ? -25.45718 -1.37904  35.40699  1.000 31.31969 ?  45  GLU B CB  1 
ATOM   1663 C CG  . GLU B 1 47  ? -24.28987 -1.16673  36.37946  1.000 43.02465 ?  45  GLU B CG  1 
ATOM   1664 C CD  . GLU B 1 47  ? -24.08826 0.31539   36.69507  1.000 46.34328 ?  45  GLU B CD  1 
ATOM   1665 O OE1 . GLU B 1 47  ? -24.63983 1.16041   35.93209  1.000 48.15263 ?  45  GLU B OE1 1 
ATOM   1666 O OE2 . GLU B 1 47  ? -23.36061 0.62662   37.66528  1.000 46.90990 -1 45  GLU B OE2 1 
ATOM   1667 N N   . ALA B 1 48  ? -28.05155 -3.01117  34.56827  1.000 32.63606 ?  46  ALA B N   1 
ATOM   1668 C CA  . ALA B 1 48  ? -29.03804 -3.28367  33.53046  1.000 33.54360 ?  46  ALA B CA  1 
ATOM   1669 C C   . ALA B 1 48  ? -30.46315 -3.36500  34.06297  1.000 34.80668 ?  46  ALA B C   1 
ATOM   1670 O O   . ALA B 1 48  ? -31.39168 -3.51846  33.25756  1.000 31.31369 ?  46  ALA B O   1 
ATOM   1671 C CB  . ALA B 1 48  ? -28.68246 -4.57889  32.80199  1.000 32.63934 ?  46  ALA B CB  1 
ATOM   1672 N N   . LYS B 1 49  ? -30.65614 -3.27373  35.38428  1.000 35.26056 ?  47  LYS B N   1 
ATOM   1673 C CA  . LYS B 1 49  ? -31.97334 -3.33519  36.02494  1.000 36.60822 ?  47  LYS B CA  1 
ATOM   1674 C C   . LYS B 1 49  ? -32.76037 -4.58067  35.62506  1.000 37.11167 ?  47  LYS B C   1 
ATOM   1675 O O   . LYS B 1 49  ? -33.94690 -4.51880  35.27295  1.000 36.79857 ?  47  LYS B O   1 
ATOM   1676 C CB  . LYS B 1 49  ? -32.78429 -2.06972  35.75297  1.000 37.21132 ?  47  LYS B CB  1 
ATOM   1677 C CG  . LYS B 1 49  ? -31.97964 -0.81109  35.76257  1.000 37.67467 ?  47  LYS B CG  1 
ATOM   1678 C CD  . LYS B 1 49  ? -32.89505 0.39298   35.74334  1.000 38.53317 ?  47  LYS B CD  1 
ATOM   1679 C CE  . LYS B 1 49  ? -32.08367 1.68482   35.73633  1.000 44.52672 ?  47  LYS B CE  1 
ATOM   1680 N NZ  . LYS B 1 49  ? -30.72771 1.53910   35.11054  1.000 47.03067 ?  47  LYS B NZ  1 
ATOM   1681 N N   . ILE B 1 50  ? -32.08843 -5.72886  35.67771  1.000 35.24122 ?  48  ILE B N   1 
ATOM   1682 C CA  . ILE B 1 50  ? -32.73886 -7.00370  35.40871  1.000 36.92272 ?  48  ILE B CA  1 
ATOM   1683 C C   . ILE B 1 50  ? -32.65492 -7.86852  36.65834  1.000 39.12905 ?  48  ILE B C   1 
ATOM   1684 O O   . ILE B 1 50  ? -31.84521 -7.63138  37.56156  1.000 39.11356 ?  48  ILE B O   1 
ATOM   1685 C CB  . ILE B 1 50  ? -32.12526 -7.74426  34.20253  1.000 36.44510 ?  48  ILE B CB  1 
ATOM   1686 C CG1 . ILE B 1 50  ? -30.61953 -7.91948  34.40554  1.000 39.75648 ?  48  ILE B CG1 1 
ATOM   1687 C CG2 . ILE B 1 50  ? -32.41745 -6.97877  32.90725  1.000 41.07116 ?  48  ILE B CG2 1 
ATOM   1688 C CD1 . ILE B 1 50  ? -30.05715 -9.14143  33.71947  1.000 37.19149 ?  48  ILE B CD1 1 
ATOM   1689 N N   . ALA B 1 51  ? -33.53332 -8.86718  36.71062  1.000 35.63319 ?  49  ALA B N   1 
ATOM   1690 C CA  . ALA B 1 51  ? -33.45944 -9.87694  37.75125  1.000 36.56586 ?  49  ALA B CA  1 
ATOM   1691 C C   . ALA B 1 51  ? -32.21335 -10.73564 37.56141  1.000 39.81488 ?  49  ALA B C   1 
ATOM   1692 O O   . ALA B 1 51  ? -31.82586 -11.05962 36.43056  1.000 36.30106 ?  49  ALA B O   1 
ATOM   1693 C CB  . ALA B 1 51  ? -34.71505 -10.74956 37.74198  1.000 38.10771 ?  49  ALA B CB  1 
ATOM   1694 N N   . LYS B 1 52  ? -31.57459 -11.08719 38.68410  1.000 38.26582 ?  50  LYS B N   1 
ATOM   1695 C CA  . LYS B 1 52  ? -30.40812 -11.96004 38.62953  1.000 39.33753 ?  50  LYS B CA  1 
ATOM   1696 C C   . LYS B 1 52  ? -30.72721 -13.22640 37.86142  1.000 39.65082 ?  50  LYS B C   1 
ATOM   1697 O O   . LYS B 1 52  ? -29.91635 -13.70068 37.06267  1.000 41.54359 ?  50  LYS B O   1 
ATOM   1698 C CB  . LYS B 1 52  ? -29.92748 -12.31947 40.04308  1.000 40.69260 ?  50  LYS B CB  1 
ATOM   1699 C CG  . LYS B 1 52  ? -28.66233 -13.17656 40.04547  1.000 44.27420 ?  50  LYS B CG  1 
ATOM   1700 C CD  . LYS B 1 52  ? -28.05007 -13.34340 41.43995  1.000 50.03865 ?  50  LYS B CD  1 
ATOM   1701 C CE  . LYS B 1 52  ? -27.95644 -14.80584 41.82307  1.000 47.72099 ?  50  LYS B CE  1 
ATOM   1702 N NZ  . LYS B 1 52  ? -27.24171 -14.98711 43.10346  1.000 51.55035 ?  50  LYS B NZ  1 
ATOM   1703 N N   . GLN B 1 53  ? -31.92397 -13.76937 38.07427  1.000 39.68043 ?  51  GLN B N   1 
ATOM   1704 C CA  . GLN B 1 53  ? -32.30236 -15.01924 37.43529  1.000 42.78299 ?  51  GLN B CA  1 
ATOM   1705 C C   . GLN B 1 53  ? -32.42671 -14.85300 35.92438  1.000 43.14086 ?  51  GLN B C   1 
ATOM   1706 O O   . GLN B 1 53  ? -32.16740 -15.80246 35.17840  1.000 45.34008 ?  51  GLN B O   1 
ATOM   1707 C CB  . GLN B 1 53  ? -33.59608 -15.53312 38.09061  1.000 54.05944 ?  51  GLN B CB  1 
ATOM   1708 C CG  . GLN B 1 53  ? -34.49291 -16.41324 37.24015  1.000 54.84907 ?  51  GLN B CG  1 
ATOM   1709 C CD  . GLN B 1 53  ? -35.12586 -17.57399 38.01797  1.000 66.60950 ?  51  GLN B CD  1 
ATOM   1710 O OE1 . GLN B 1 53  ? -35.27776 -17.52499 39.24782  1.000 66.42668 ?  51  GLN B OE1 1 
ATOM   1711 N NE2 . GLN B 1 53  ? -35.51713 -18.61834 37.29161  1.000 68.21783 ?  51  GLN B NE2 1 
ATOM   1712 N N   . SER B 1 54  ? -32.75726 -13.64579 35.44912  1.000 42.47505 ?  52  SER B N   1 
ATOM   1713 C CA  . SER B 1 54  ? -32.79768 -13.41658 34.00907  1.000 42.80840 ?  52  SER B CA  1 
ATOM   1714 C C   . SER B 1 54  ? -31.41885 -13.50635 33.38086  1.000 40.47729 ?  52  SER B C   1 
ATOM   1715 O O   . SER B 1 54  ? -31.30594 -13.90212 32.21164  1.000 38.03950 ?  52  SER B O   1 
ATOM   1716 C CB  . SER B 1 54  ? -33.40455 -12.05126 33.66606  1.000 41.99168 ?  52  SER B CB  1 
ATOM   1717 O OG  . SER B 1 54  ? -34.65427 -11.82787 34.29769  1.000 39.80579 ?  52  SER B OG  1 
ATOM   1718 N N   . PHE B 1 55  ? -30.36789 -13.08859 34.10053  1.000 40.49504 ?  53  PHE B N   1 
ATOM   1719 C CA  . PHE B 1 55  ? -29.02672 -13.19845 33.54246  1.000 35.63119 ?  53  PHE B CA  1 
ATOM   1720 C C   . PHE B 1 55  ? -28.68429 -14.65346 33.28104  1.000 37.11250 ?  53  PHE B C   1 
ATOM   1721 O O   . PHE B 1 55  ? -28.16338 -14.99962 32.21362  1.000 40.85037 ?  53  PHE B O   1 
ATOM   1722 C CB  . PHE B 1 55  ? -27.98088 -12.54990 34.46285  1.000 34.97680 ?  53  PHE B CB  1 
ATOM   1723 C CG  . PHE B 1 55  ? -26.56186 -12.68974 33.95806  1.000 39.54674 ?  53  PHE B CG  1 
ATOM   1724 C CD1 . PHE B 1 55  ? -25.80848 -13.81244 34.25837  1.000 40.92449 ?  53  PHE B CD1 1 
ATOM   1725 C CD2 . PHE B 1 55  ? -25.99562 -11.71082 33.15276  1.000 36.70885 ?  53  PHE B CD2 1 
ATOM   1726 C CE1 . PHE B 1 55  ? -24.53781 -13.95491 33.79156  1.000 37.47749 ?  53  PHE B CE1 1 
ATOM   1727 C CE2 . PHE B 1 55  ? -24.69545 -11.84658 32.66635  1.000 36.42561 ?  53  PHE B CE2 1 
ATOM   1728 C CZ  . PHE B 1 55  ? -23.96931 -12.96989 32.98085  1.000 37.38915 ?  53  PHE B CZ  1 
ATOM   1729 N N   . TYR B 1 56  ? -28.95135 -15.52157 34.24830  1.000 37.45033 ?  54  TYR B N   1 
ATOM   1730 C CA  . TYR B 1 56  ? -28.51841 -16.90397 34.10330  1.000 41.70610 ?  54  TYR B CA  1 
ATOM   1731 C C   . TYR B 1 56  ? -29.44030 -17.71559 33.21288  1.000 44.04410 ?  54  TYR B C   1 
ATOM   1732 O O   . TYR B 1 56  ? -29.02201 -18.76783 32.72016  1.000 45.21478 ?  54  TYR B O   1 
ATOM   1733 C CB  . TYR B 1 56  ? -28.34497 -17.56786 35.47338  1.000 40.34987 ?  54  TYR B CB  1 
ATOM   1734 C CG  . TYR B 1 56  ? -27.20232 -16.95970 36.26264  1.000 41.82417 ?  54  TYR B CG  1 
ATOM   1735 C CD1 . TYR B 1 56  ? -25.87871 -17.30206 35.97963  1.000 42.84114 ?  54  TYR B CD1 1 
ATOM   1736 C CD2 . TYR B 1 56  ? -27.43306 -16.03728 37.27204  1.000 43.93472 ?  54  TYR B CD2 1 
ATOM   1737 C CE1 . TYR B 1 56  ? -24.82248 -16.74180 36.68295  1.000 45.55249 ?  54  TYR B CE1 1 
ATOM   1738 C CE2 . TYR B 1 56  ? -26.37804 -15.47293 37.98643  1.000 41.32462 ?  54  TYR B CE2 1 
ATOM   1739 C CZ  . TYR B 1 56  ? -25.07865 -15.82875 37.69104  1.000 46.31804 ?  54  TYR B CZ  1 
ATOM   1740 O OH  . TYR B 1 56  ? -24.03344 -15.26195 38.40625  1.000 46.79302 ?  54  TYR B OH  1 
ATOM   1741 N N   . MET B 1 57  ? -30.65920 -17.23541 32.95207  1.000 40.25019 ?  55  MET B N   1 
ATOM   1742 C CA  . MET B 1 57  ? -31.46350 -17.85250 31.90704  1.000 45.46243 ?  55  MET B CA  1 
ATOM   1743 C C   . MET B 1 57  ? -30.80886 -17.66614 30.54480  1.000 43.25985 ?  55  MET B C   1 
ATOM   1744 O O   . MET B 1 57  ? -30.86322 -18.55816 29.69144  1.000 44.01536 ?  55  MET B O   1 
ATOM   1745 C CB  . MET B 1 57  ? -32.87398 -17.26171 31.89965  1.000 47.62220 ?  55  MET B CB  1 
ATOM   1746 C CG  . MET B 1 57  ? -33.87352 -18.02113 32.73141  1.000 50.55016 ?  55  MET B CG  1 
ATOM   1747 S SD  . MET B 1 57  ? -35.28968 -16.98644 33.18517  1.000 66.91328 ?  55  MET B SD  1 
ATOM   1748 C CE  . MET B 1 57  ? -35.69792 -16.24829 31.60331  1.000 59.95491 ?  55  MET B CE  1 
ATOM   1749 N N   . ALA B 1 58  ? -30.18367 -16.50710 30.32442  1.000 40.66291 ?  56  ALA B N   1 
ATOM   1750 C CA  . ALA B 1 58  ? -29.59482 -16.16196 29.04386  1.000 39.65997 ?  56  ALA B CA  1 
ATOM   1751 C C   . ALA B 1 58  ? -28.14748 -16.61128 28.89153  1.000 40.41367 ?  56  ALA B C   1 
ATOM   1752 O O   . ALA B 1 58  ? -27.73517 -16.92447 27.77080  1.000 37.34925 ?  56  ALA B O   1 
ATOM   1753 C CB  . ALA B 1 58  ? -29.65996 -14.64551 28.83228  1.000 41.58137 ?  56  ALA B CB  1 
ATOM   1754 N N   . PHE B 1 59  ? -27.35511 -16.62691 29.97837  1.000 38.78710 ?  57  PHE B N   1 
ATOM   1755 C CA  . PHE B 1 59  ? -25.89810 -16.76943 29.89691  1.000 38.42404 ?  57  PHE B CA  1 
ATOM   1756 C C   . PHE B 1 59  ? -25.40791 -17.79692 30.91446  1.000 39.33253 ?  57  PHE B C   1 
ATOM   1757 O O   . PHE B 1 59  ? -25.71896 -17.67220 32.11415  1.000 41.95015 ?  57  PHE B O   1 
ATOM   1758 C CB  . PHE B 1 59  ? -25.20551 -15.41721 30.13691  1.000 36.29595 ?  57  PHE B CB  1 
ATOM   1759 C CG  . PHE B 1 59  ? -25.70379 -14.32582 29.23208  1.000 35.66362 ?  57  PHE B CG  1 
ATOM   1760 C CD1 . PHE B 1 59  ? -25.41132 -14.35100 27.87563  1.000 37.85181 ?  57  PHE B CD1 1 
ATOM   1761 C CD2 . PHE B 1 59  ? -26.48515 -13.28933 29.73499  1.000 36.27588 ?  57  PHE B CD2 1 
ATOM   1762 C CE1 . PHE B 1 59  ? -25.88870 -13.36379 27.01546  1.000 35.50056 ?  57  PHE B CE1 1 
ATOM   1763 C CE2 . PHE B 1 59  ? -26.97351 -12.29674 28.88715  1.000 35.88923 ?  57  PHE B CE2 1 
ATOM   1764 C CZ  . PHE B 1 59  ? -26.66708 -12.33342 27.52500  1.000 35.67968 ?  57  PHE B CZ  1 
ATOM   1765 N N   . PRO B 1 60  ? -24.65821 -18.82366 30.48656  1.000 36.93949 ?  58  PRO B N   1 
ATOM   1766 C CA  . PRO B 1 60  ? -24.35066 -19.93195 31.41398  1.000 40.68484 ?  58  PRO B CA  1 
ATOM   1767 C C   . PRO B 1 60  ? -23.21824 -19.63609 32.38147  1.000 37.89308 ?  58  PRO B C   1 
ATOM   1768 O O   . PRO B 1 60  ? -23.09359 -20.33784 33.38861  1.000 40.74921 ?  58  PRO B O   1 
ATOM   1769 C CB  . PRO B 1 60  ? -23.95537 -21.09049 30.47045  1.000 44.37605 ?  58  PRO B CB  1 
ATOM   1770 C CG  . PRO B 1 60  ? -24.37359 -20.65932 29.09926  1.000 41.87529 ?  58  PRO B CG  1 
ATOM   1771 C CD  . PRO B 1 60  ? -24.27311 -19.16200 29.10535  1.000 39.77613 ?  58  PRO B CD  1 
ATOM   1772 N N   . SER B 1 61  ? -22.39119 -18.63840 32.09947  1.000 35.58972 ?  59  SER B N   1 
ATOM   1773 C CA  . SER B 1 61  ? -21.20174 -18.30669 32.86311  1.000 37.30724 ?  59  SER B CA  1 
ATOM   1774 C C   . SER B 1 61  ? -20.83822 -16.87499 32.51582  1.000 35.25797 ?  59  SER B C   1 
ATOM   1775 O O   . SER B 1 61  ? -21.26854 -16.34664 31.48522  1.000 35.86508 ?  59  SER B O   1 
ATOM   1776 C CB  . SER B 1 61  ? -20.03633 -19.24632 32.54120  1.000 34.46375 ?  59  SER B CB  1 
ATOM   1777 O OG  . SER B 1 61  ? -19.56470 -19.04015 31.22260  1.000 35.72364 ?  59  SER B OG  1 
ATOM   1778 N N   . LYS B 1 62  ? -20.05217 -16.24517 33.38235  1.000 31.04872 ?  60  LYS B N   1 
ATOM   1779 C CA  . LYS B 1 62  ? -19.58972 -14.88917 33.08527  1.000 35.49881 ?  60  LYS B CA  1 
ATOM   1780 C C   . LYS B 1 62  ? -18.67389 -14.85700 31.86395  1.000 33.80843 ?  60  LYS B C   1 
ATOM   1781 O O   . LYS B 1 62  ? -18.67664 -13.88167 31.09892  1.000 31.86491 ?  60  LYS B O   1 
ATOM   1782 C CB  . LYS B 1 62  ? -18.86652 -14.28529 34.28063  1.000 35.60094 ?  60  LYS B CB  1 
ATOM   1783 C CG  . LYS B 1 62  ? -18.77903 -12.77015 34.16584  1.000 38.98349 ?  60  LYS B CG  1 
ATOM   1784 C CD  . LYS B 1 62  ? -17.40931 -12.25455 34.46159  1.000 42.22504 ?  60  LYS B CD  1 
ATOM   1785 C CE  . LYS B 1 62  ? -17.38959 -10.73767 34.56950  1.000 43.54826 ?  60  LYS B CE  1 
ATOM   1786 N NZ  . LYS B 1 62  ? -16.00905 -10.27834 34.94701  1.000 41.62246 ?  60  LYS B NZ  1 
ATOM   1787 N N   . ASP B 1 63  ? -17.87117 -15.90108 31.67114  1.000 30.24958 ?  61  ASP B N   1 
ATOM   1788 C CA  . ASP B 1 63  ? -16.95925 -15.91974 30.53647  1.000 36.69132 ?  61  ASP B CA  1 
ATOM   1789 C C   . ASP B 1 63  ? -17.68214 -16.20750 29.22619  1.000 32.33538 ?  61  ASP B C   1 
ATOM   1790 O O   . ASP B 1 63  ? -17.22922 -15.76835 28.16853  1.000 33.05328 ?  61  ASP B O   1 
ATOM   1791 C CB  . ASP B 1 63  ? -15.84104 -16.92676 30.79361  1.000 36.39337 ?  61  ASP B CB  1 
ATOM   1792 C CG  . ASP B 1 63  ? -14.91335 -16.47742 31.91943  1.000 41.67299 ?  61  ASP B CG  1 
ATOM   1793 O OD1 . ASP B 1 63  ? -15.04695 -15.31461 32.37454  1.000 41.42148 ?  61  ASP B OD1 1 
ATOM   1794 O OD2 . ASP B 1 63  ? -14.06432 -17.28244 32.36685  1.000 40.49545 -1 61  ASP B OD2 1 
ATOM   1795 N N   . SER B 1 64  ? -18.80468 -16.91963 29.28047  1.000 33.80121 ?  62  SER B N   1 
ATOM   1796 C CA  . SER B 1 64  ? -19.64524 -17.08280 28.10281  1.000 34.63644 ?  62  SER B CA  1 
ATOM   1797 C C   . SER B 1 64  ? -20.27547 -15.75584 27.70418  1.000 34.33431 ?  62  SER B C   1 
ATOM   1798 O O   . SER B 1 64  ? -20.30512 -15.39960 26.52187  1.000 33.48666 ?  62  SER B O   1 
ATOM   1799 C CB  . SER B 1 64  ? -20.71581 -18.13542 28.37764  1.000 36.47892 ?  62  SER B CB  1 
ATOM   1800 O OG  . SER B 1 64  ? -21.14399 -18.73805 27.16680  1.000 41.90309 ?  62  SER B OG  1 
ATOM   1801 N N   . PHE B 1 65  ? -20.80085 -15.02406 28.68673  1.000 33.16795 ?  63  PHE B N   1 
ATOM   1802 C CA  . PHE B 1 65  ? -21.30707 -13.67072 28.47317  1.000 30.43902 ?  63  PHE B CA  1 
ATOM   1803 C C   . PHE B 1 65  ? -20.25502 -12.75986 27.84230  1.000 32.46892 ?  63  PHE B C   1 
ATOM   1804 O O   . PHE B 1 65  ? -20.51916 -12.05520 26.85491  1.000 28.84747 ?  63  PHE B O   1 
ATOM   1805 C CB  . PHE B 1 65  ? -21.76997 -13.12044 29.82271  1.000 33.98930 ?  63  PHE B CB  1 
ATOM   1806 C CG  . PHE B 1 65  ? -22.27076 -11.71901 29.77354  1.000 31.53491 ?  63  PHE B CG  1 
ATOM   1807 C CD1 . PHE B 1 65  ? -23.50509 -11.43532 29.24808  1.000 31.21580 ?  63  PHE B CD1 1 
ATOM   1808 C CD2 . PHE B 1 65  ? -21.49187 -10.68401 30.23312  1.000 28.44538 ?  63  PHE B CD2 1 
ATOM   1809 C CE1 . PHE B 1 65  ? -23.96029 -10.13997 29.19172  1.000 29.80063 ?  63  PHE B CE1 1 
ATOM   1810 C CE2 . PHE B 1 65  ? -21.94182 -9.39939  30.19215  1.000 31.78619 ?  63  PHE B CE2 1 
ATOM   1811 C CZ  . PHE B 1 65  ? -23.19426 -9.12295  29.64786  1.000 27.13489 ?  63  PHE B CZ  1 
ATOM   1812 N N   . ILE B 1 66  ? -19.05092 -12.74574 28.40451  1.000 29.51221 ?  64  ILE B N   1 
ATOM   1813 C CA  . ILE B 1 66  ? -18.04063 -11.83488 27.88412  1.000 28.50488 ?  64  ILE B CA  1 
ATOM   1814 C C   . ILE B 1 66  ? -17.65582 -12.19698 26.45439  1.000 30.14778 ?  64  ILE B C   1 
ATOM   1815 O O   . ILE B 1 66  ? -17.42698 -11.30307 25.62798  1.000 31.55130 ?  64  ILE B O   1 
ATOM   1816 C CB  . ILE B 1 66  ? -16.84999 -11.79854 28.85598  1.000 31.41016 ?  64  ILE B CB  1 
ATOM   1817 C CG1 . ILE B 1 66  ? -17.19993 -10.78779 29.94204  1.000 35.32350 ?  64  ILE B CG1 1 
ATOM   1818 C CG2 . ILE B 1 66  ? -15.55264 -11.42283 28.16829  1.000 34.73702 ?  64  ILE B CG2 1 
ATOM   1819 C CD1 . ILE B 1 66  ? -16.33735 -10.82736 31.07572  1.000 40.78198 ?  64  ILE B CD1 1 
ATOM   1820 N N   . ILE B 1 67  ? -17.66262 -13.48267 26.09823  1.000 27.82632 ?  65  ILE B N   1 
ATOM   1821 C CA  . ILE B 1 67  ? -17.40121 -13.83085 24.70376  1.000 30.37263 ?  65  ILE B CA  1 
ATOM   1822 C C   . ILE B 1 67  ? -18.53011 -13.31735 23.81500  1.000 29.77897 ?  65  ILE B C   1 
ATOM   1823 O O   . ILE B 1 67  ? -18.29837 -12.85942 22.69424  1.000 28.99983 ?  65  ILE B O   1 
ATOM   1824 C CB  . ILE B 1 67  ? -17.19863 -15.34940 24.55852  1.000 33.73489 ?  65  ILE B CB  1 
ATOM   1825 C CG1 . ILE B 1 67  ? -15.74758 -15.72090 24.83505  1.000 36.89416 ?  65  ILE B CG1 1 
ATOM   1826 C CG2 . ILE B 1 67  ? -17.49146 -15.81338 23.14267  1.000 36.19976 ?  65  ILE B CG2 1 
ATOM   1827 C CD1 . ILE B 1 67  ? -15.51306 -17.21102 24.81796  1.000 42.28256 ?  65  ILE B CD1 1 
ATOM   1828 N N   . GLU B 1 68  ? -19.76749 -13.36471 24.31119  1.000 32.05627 ?  66  GLU B N   1 
ATOM   1829 C CA  . GLU B 1 68  ? -20.87995 -12.79485 23.56132  1.000 31.58757 ?  66  GLU B CA  1 
ATOM   1830 C C   . GLU B 1 68  ? -20.74510 -11.28569 23.42617  1.000 27.59501 ?  66  GLU B C   1 
ATOM   1831 O O   . GLU B 1 68  ? -21.07612 -10.72621 22.37713  1.000 31.46407 ?  66  GLU B O   1 
ATOM   1832 C CB  . GLU B 1 68  ? -22.20524 -13.15578 24.23692  1.000 29.60367 ?  66  GLU B CB  1 
ATOM   1833 C CG  . GLU B 1 68  ? -22.64830 -14.53149 23.88329  1.000 32.01337 ?  66  GLU B CG  1 
ATOM   1834 C CD  . GLU B 1 68  ? -24.15559 -14.69439 23.95546  1.000 37.87734 ?  66  GLU B CD  1 
ATOM   1835 O OE1 . GLU B 1 68  ? -24.85650 -14.13879 23.07785  1.000 38.54687 ?  66  GLU B OE1 1 
ATOM   1836 O OE2 . GLU B 1 68  ? -24.63402 -15.42441 24.84733  1.000 40.29320 -1 66  GLU B OE2 1 
ATOM   1837 N N   . CYS B 1 69  ? -20.27612 -10.60372 24.47309  1.000 23.96070 ?  67  CYS B N   1 
ATOM   1838 C CA  . CYS B 1 69  ? -20.04689 -9.16694  24.35976  1.000 27.25864 ?  67  CYS B CA  1 
ATOM   1839 C C   . CYS B 1 69  ? -18.97164 -8.86629  23.32987  1.000 28.18092 ?  67  CYS B C   1 
ATOM   1840 O O   . CYS B 1 69  ? -19.11785 -7.95378  22.51224  1.000 25.81988 ?  67  CYS B O   1 
ATOM   1841 C CB  . CYS B 1 69  ? -19.63900 -8.57415  25.70624  1.000 29.74558 ?  67  CYS B CB  1 
ATOM   1842 S SG  . CYS B 1 69  ? -20.85145 -8.65916  27.00031  1.000 32.78434 ?  67  CYS B SG  1 
ATOM   1843 N N   . LEU B 1 70  ? -17.85721 -9.60601  23.37843  1.000 30.82106 ?  68  LEU B N   1 
ATOM   1844 C CA  . LEU B 1 70  ? -16.78024 -9.35795  22.42956  1.000 30.28608 ?  68  LEU B CA  1 
ATOM   1845 C C   . LEU B 1 70  ? -17.27242 -9.56240  21.00737  1.000 31.51108 ?  68  LEU B C   1 
ATOM   1846 O O   . LEU B 1 70  ? -16.88855 -8.82639  20.09443  1.000 30.97863 ?  68  LEU B O   1 
ATOM   1847 C CB  . LEU B 1 70  ? -15.58713 -10.27948 22.71847  1.000 31.74065 ?  68  LEU B CB  1 
ATOM   1848 C CG  . LEU B 1 70  ? -14.33733 -9.95981  21.89265  1.000 34.49592 ?  68  LEU B CG  1 
ATOM   1849 C CD1 . LEU B 1 70  ? -13.81534 -8.59910  22.28725  1.000 33.80496 ?  68  LEU B CD1 1 
ATOM   1850 C CD2 . LEU B 1 70  ? -13.25675 -11.02646 22.03895  1.000 35.71822 ?  68  LEU B CD2 1 
ATOM   1851 N N   . ASP B 1 71  ? -18.17076 -10.52131 20.81824  1.000 31.79338 ?  69  ASP B N   1 
ATOM   1852 C CA  . ASP B 1 71  ? -18.62919 -10.83031 19.47769  1.000 33.26607 ?  69  ASP B CA  1 
ATOM   1853 C C   . ASP B 1 71  ? -19.56166 -9.72748  18.97331  1.000 32.82448 ?  69  ASP B C   1 
ATOM   1854 O O   . ASP B 1 71  ? -19.59296 -9.42236  17.76663  1.000 28.38793 ?  69  ASP B O   1 
ATOM   1855 C CB  . ASP B 1 71  ? -19.33133 -12.18406 19.52242  1.000 36.03364 ?  69  ASP B CB  1 
ATOM   1856 C CG  . ASP B 1 71  ? -18.44678 -13.32148 19.03212  1.000 40.21051 ?  69  ASP B CG  1 
ATOM   1857 O OD1 . ASP B 1 71  ? -17.50100 -13.08238 18.24105  1.000 42.46972 ?  69  ASP B OD1 1 
ATOM   1858 O OD2 . ASP B 1 71  ? -18.69545 -14.46905 19.47216  1.000 41.95689 -1 69  ASP B OD2 1 
ATOM   1859 N N   . MET B 1 72  ? -20.28139 -9.06744  19.88917  1.000 30.29357 ?  70  MET B N   1 
ATOM   1860 C CA  . MET B 1 72  ? -21.16892 -7.99702  19.44982  1.000 32.54479 ?  70  MET B CA  1 
ATOM   1861 C C   . MET B 1 72  ? -20.39839 -6.70195  19.24055  1.000 29.51234 ?  70  MET B C   1 
ATOM   1862 O O   . MET B 1 72  ? -20.73279 -5.91576  18.34445  1.000 25.33889 ?  70  MET B O   1 
ATOM   1863 C CB  . MET B 1 72  ? -22.32568 -7.79758  20.43924  1.000 33.80765 ?  70  MET B CB  1 
ATOM   1864 C CG  . MET B 1 72  ? -22.75498 -6.33969  20.66909  1.000 36.55111 ?  70  MET B CG  1 
ATOM   1865 S SD  . MET B 1 72  ? -23.93702 -6.09846  22.01344  1.000 31.55421 ?  70  MET B SD  1 
ATOM   1866 C CE  . MET B 1 72  ? -25.47331 -6.71778  21.32164  1.000 35.78280 ?  70  MET B CE  1 
ATOM   1867 N N   . GLU B 1 73  ? -19.35151 -6.48014  20.03166  1.000 29.98440 ?  71  GLU B N   1 
ATOM   1868 C CA  . GLU B 1 73  ? -18.45425 -5.37327  19.75610  1.000 30.08219 ?  71  GLU B CA  1 
ATOM   1869 C C   . GLU B 1 73  ? -17.76531 -5.54639  18.40859  1.000 30.31350 ?  71  GLU B C   1 
ATOM   1870 O O   . GLU B 1 73  ? -17.65508 -4.58510  17.63479  1.000 30.81666 ?  71  GLU B O   1 
ATOM   1871 C CB  . GLU B 1 73  ? -17.42478 -5.23977  20.88717  1.000 30.04805 ?  71  GLU B CB  1 
ATOM   1872 C CG  . GLU B 1 73  ? -16.35203 -4.23185  20.60662  1.000 31.82838 ?  71  GLU B CG  1 
ATOM   1873 C CD  . GLU B 1 73  ? -16.82013 -2.79185  20.75233  1.000 37.27520 ?  71  GLU B CD  1 
ATOM   1874 O OE1 . GLU B 1 73  ? -18.04219 -2.55292  20.88200  1.000 38.13774 ?  71  GLU B OE1 1 
ATOM   1875 O OE2 . GLU B 1 73  ? -15.94795 -1.89132  20.68735  1.000 38.53213 -1 71  GLU B OE2 1 
ATOM   1876 N N   . ILE B 1 74  ? -17.30268 -6.76019  18.09480  1.000 27.66084 ?  72  ILE B N   1 
ATOM   1877 C CA  . ILE B 1 74  ? -16.64099 -6.95719  16.80147  1.000 30.85053 ?  72  ILE B CA  1 
ATOM   1878 C C   . ILE B 1 74  ? -17.61260 -6.70567  15.64791  1.000 29.78276 ?  72  ILE B C   1 
ATOM   1879 O O   . ILE B 1 74  ? -17.28401 -6.00422  14.67821  1.000 28.65461 ?  72  ILE B O   1 
ATOM   1880 C CB  . ILE B 1 74  ? -16.00009 -8.35775  16.72805  1.000 31.43802 ?  72  ILE B CB  1 
ATOM   1881 C CG1 . ILE B 1 74  ? -14.75903 -8.40914  17.61774  1.000 28.95132 ?  72  ILE B CG1 1 
ATOM   1882 C CG2 . ILE B 1 74  ? -15.57917 -8.69626  15.29733  1.000 27.30544 ?  72  ILE B CG2 1 
ATOM   1883 C CD1 . ILE B 1 74  ? -14.24325 -9.82312  17.90042  1.000 29.08234 ?  72  ILE B CD1 1 
ATOM   1884 N N   . ASN B 1 75  ? -18.84058 -7.22463  15.75108  1.000 28.77955 ?  73  ASN B N   1 
ATOM   1885 C CA  . ASN B 1 75  ? -19.81841 -7.02018  14.68711  1.000 28.70169 ?  73  ASN B CA  1 
ATOM   1886 C C   . ASN B 1 75  ? -20.12440 -5.54427  14.50281  1.000 27.11971 ?  73  ASN B C   1 
ATOM   1887 O O   . ASN B 1 75  ? -20.27990 -5.06669  13.37233  1.000 27.05524 ?  73  ASN B O   1 
ATOM   1888 C CB  . ASN B 1 75  ? -21.10195 -7.78118  14.99343  1.000 31.79186 ?  73  ASN B CB  1 
ATOM   1889 C CG  . ASN B 1 75  ? -20.92427 -9.27591  14.88986  1.000 35.90609 ?  73  ASN B CG  1 
ATOM   1890 O OD1 . ASN B 1 75  ? -20.24355 -9.77218  13.99574  1.000 41.59328 ?  73  ASN B OD1 1 
ATOM   1891 N ND2 . ASN B 1 75  ? -21.59682 -10.01228 15.77135  1.000 38.17065 ?  73  ASN B ND2 1 
ATOM   1892 N N   . ARG B 1 76  ? -20.17621 -4.80028  15.59918  1.000 26.95226 ?  74  ARG B N   1 
ATOM   1893 C CA  . ARG B 1 76  ? -20.50773 -3.38562  15.52468  1.000 28.29801 ?  74  ARG B CA  1 
ATOM   1894 C C   . ARG B 1 76  ? -19.39804 -2.58370  14.85260  1.000 29.06865 ?  74  ARG B C   1 
ATOM   1895 O O   . ARG B 1 76  ? -19.67508 -1.67060  14.06532  1.000 27.78744 ?  74  ARG B O   1 
ATOM   1896 C CB  . ARG B 1 76  ? -20.79792 -2.84688  16.92539  1.000 31.73417 ?  74  ARG B CB  1 
ATOM   1897 C CG  . ARG B 1 76  ? -20.72236 -1.32385  17.04818  1.000 38.41039 ?  74  ARG B CG  1 
ATOM   1898 C CD  . ARG B 1 76  ? -20.61923 -0.81350  18.48969  1.000 38.72102 ?  74  ARG B CD  1 
ATOM   1899 N NE  . ARG B 1 76  ? -19.26511 -0.74137  19.01224  1.000 41.33758 ?  74  ARG B NE  1 
ATOM   1900 C CZ  . ARG B 1 76  ? -18.43346 0.26280   18.77569  1.000 42.83022 ?  74  ARG B CZ  1 
ATOM   1901 N NH1 . ARG B 1 76  ? -18.78184 1.28591   18.00703  1.000 46.70409 ?  74  ARG B NH1 1 
ATOM   1902 N NH2 . ARG B 1 76  ? -17.22650 0.24886   19.33163  1.000 46.82060 ?  74  ARG B NH2 1 
ATOM   1903 N N   . LEU B 1 77  ? -18.13688 -2.90270  15.15767  1.000 28.35241 ?  75  LEU B N   1 
ATOM   1904 C CA  . LEU B 1 77  ? -17.02712 -2.24522  14.48217  1.000 27.67940 ?  75  LEU B CA  1 
ATOM   1905 C C   . LEU B 1 77  ? -16.97331 -2.62723  13.00978  1.000 28.21862 ?  75  LEU B C   1 
ATOM   1906 O O   . LEU B 1 77  ? -16.66446 -1.78400  12.16476  1.000 28.53592 ?  75  LEU B O   1 
ATOM   1907 C CB  . LEU B 1 77  ? -15.70896 -2.60060  15.16964  1.000 28.95814 ?  75  LEU B CB  1 
ATOM   1908 C CG  . LEU B 1 77  ? -15.47568 -2.05302  16.58251  1.000 29.17275 ?  75  LEU B CG  1 
ATOM   1909 C CD1 . LEU B 1 77  ? -14.28261 -2.77528  17.18102  1.000 31.03156 ?  75  LEU B CD1 1 
ATOM   1910 C CD2 . LEU B 1 77  ? -15.27457 -0.54584  16.64633  1.000 29.00996 ?  75  LEU B CD2 1 
ATOM   1911 N N   . LYS B 1 78  ? -17.23237 -3.90032  12.68322  1.000 25.89767 ?  76  LYS B N   1 
ATOM   1912 C CA  . LYS B 1 78  ? -17.27237 -4.29975  11.28082  1.000 26.98880 ?  76  LYS B CA  1 
ATOM   1913 C C   . LYS B 1 78  ? -18.36619 -3.56071  10.53352  1.000 29.58650 ?  76  LYS B C   1 
ATOM   1914 O O   . LYS B 1 78  ? -18.19152 -3.17644  9.37051   1.000 28.47057 ?  76  LYS B O   1 
ATOM   1915 C CB  . LYS B 1 78  ? -17.51032 -5.80527  11.15346  1.000 29.11150 ?  76  LYS B CB  1 
ATOM   1916 C CG  . LYS B 1 78  ? -16.34281 -6.67864  11.54681  1.000 27.32040 ?  76  LYS B CG  1 
ATOM   1917 C CD  . LYS B 1 78  ? -16.61934 -8.09780  11.08103  1.000 28.92157 ?  76  LYS B CD  1 
ATOM   1918 C CE  . LYS B 1 78  ? -15.51272 -9.01639  11.49257  1.000 30.82197 ?  76  LYS B CE  1 
ATOM   1919 N NZ  . LYS B 1 78  ? -15.79855 -10.40638 11.09394  1.000 34.09191 ?  76  LYS B NZ  1 
ATOM   1920 N N   . GLN B 1 79  ? -19.51706 -3.37214  11.17626  1.000 30.92075 ?  77  GLN B N   1 
ATOM   1921 C CA  . GLN B 1 79  ? -20.61790 -2.76233  10.46320  1.000 31.91655 ?  77  GLN B CA  1 
ATOM   1922 C C   . GLN B 1 79  ? -20.37907 -1.27320  10.32216  1.000 31.47757 ?  77  GLN B C   1 
ATOM   1923 O O   . GLN B 1 79  ? -20.68788 -0.68775  9.28388   1.000 32.06508 ?  77  GLN B O   1 
ATOM   1924 C CB  . GLN B 1 79  ? -21.95581 -3.06364  11.16453  1.000 32.05464 ?  77  GLN B CB  1 
ATOM   1925 C CG  . GLN B 1 79  ? -23.06802 -2.07925  10.80135  1.000 35.67286 ?  77  GLN B CG  1 
ATOM   1926 C CD  . GLN B 1 79  ? -24.11829 -1.87402  11.90527  1.000 45.70955 ?  77  GLN B CD  1 
ATOM   1927 O OE1 . GLN B 1 79  ? -23.99642 -0.96298  12.74130  1.000 45.64433 ?  77  GLN B OE1 1 
ATOM   1928 N NE2 . GLN B 1 79  ? -25.20348 -2.65699  11.84772  1.000 43.68397 ?  77  GLN B NE2 1 
ATOM   1929 N N   . SER B 1 80  ? -19.79958 -0.65645  11.34251  1.000 26.98700 ?  78  SER B N   1 
ATOM   1930 C CA  . SER B 1 80  ? -19.47655 0.76218   11.25738  1.000 29.53447 ?  78  SER B CA  1 
ATOM   1931 C C   . SER B 1 80  ? -18.48978 1.04464   10.11930  1.000 31.34924 ?  78  SER B C   1 
ATOM   1932 O O   . SER B 1 80  ? -18.68637 1.98564   9.33721   1.000 30.17052 ?  78  SER B O   1 
ATOM   1933 C CB  . SER B 1 80  ? -18.89891 1.22329   12.59048  1.000 33.62319 ?  78  SER B CB  1 
ATOM   1934 O OG  . SER B 1 80  ? -18.67146 2.61214   12.57575  1.000 38.68965 ?  78  SER B OG  1 
ATOM   1935 N N   . LEU B 1 81  ? -17.43511 0.22749   10.00037  1.000 29.23860 ?  79  LEU B N   1 
ATOM   1936 C CA  . LEU B 1 81  ? -16.39013 0.47763   8.99931   1.000 29.89587 ?  79  LEU B CA  1 
ATOM   1937 C C   . LEU B 1 81  ? -16.85223 0.10023   7.59848   1.000 28.96225 ?  79  LEU B C   1 
ATOM   1938 O O   . LEU B 1 81  ? -16.64458 0.86628   6.64955   1.000 30.07215 ?  79  LEU B O   1 
ATOM   1939 C CB  . LEU B 1 81  ? -15.10108 -0.27527  9.35180   1.000 28.31297 ?  79  LEU B CB  1 
ATOM   1940 C CG  . LEU B 1 81  ? -13.88037 -0.09789  8.41298   1.000 27.01595 ?  79  LEU B CG  1 
ATOM   1941 C CD1 . LEU B 1 81  ? -13.48991 1.35545   8.23712   1.000 26.28320 ?  79  LEU B CD1 1 
ATOM   1942 C CD2 . LEU B 1 81  ? -12.66403 -0.89038  8.91337   1.000 26.87137 ?  79  LEU B CD2 1 
ATOM   1943 N N   . SER B 1 82  ? -17.46440 -1.08330  7.45574   1.000 27.35696 ?  80  SER B N   1 
ATOM   1944 C CA  . SER B 1 82  ? -18.11221 -1.49645  6.20380   1.000 33.61648 ?  80  SER B CA  1 
ATOM   1945 C C   . SER B 1 82  ? -18.99447 -0.40092  5.62375   1.000 33.62294 ?  80  SER B C   1 
ATOM   1946 O O   . SER B 1 82  ? -18.97948 -0.13037  4.41091   1.000 31.90030 ?  80  SER B O   1 
ATOM   1947 C CB  . SER B 1 82  ? -18.99008 -2.72243  6.45546   1.000 33.35927 ?  80  SER B CB  1 
ATOM   1948 O OG  . SER B 1 82  ? -18.20577 -3.84280  6.78785   1.000 38.51897 ?  80  SER B OG  1 
ATOM   1949 N N   . ASN B 1 83  ? -19.85245 0.17153   6.46635   1.000 34.67705 ?  81  ASN B N   1 
ATOM   1950 C CA  . ASN B 1 83  ? -20.75739 1.21490   5.99822   1.000 36.53624 ?  81  ASN B CA  1 
ATOM   1951 C C   . ASN B 1 83  ? -20.01037 2.48867   5.62335   1.000 35.89141 ?  81  ASN B C   1 
ATOM   1952 O O   . ASN B 1 83  ? -20.35610 3.14944   4.63557   1.000 34.32779 ?  81  ASN B O   1 
ATOM   1953 C CB  . ASN B 1 83  ? -21.81012 1.52072   7.06330   1.000 37.03366 ?  81  ASN B CB  1 
ATOM   1954 C CG  . ASN B 1 83  ? -22.45914 2.88821   6.85135   1.000 41.99082 ?  81  ASN B CG  1 
ATOM   1955 O OD1 . ASN B 1 83  ? -22.00465 3.89441   7.41322   1.000 43.19550 ?  81  ASN B OD1 1 
ATOM   1956 N ND2 . ASN B 1 83  ? -23.47607 2.94447   5.99428   1.000 44.43926 ?  81  ASN B ND2 1 
ATOM   1957 N N   . LEU B 1 84  ? -19.02079 2.87821   6.42637   1.000 34.39595 ?  82  LEU B N   1 
ATOM   1958 C CA  . LEU B 1 84  ? -18.26602 4.09033   6.12976   1.000 36.67464 ?  82  LEU B CA  1 
ATOM   1959 C C   . LEU B 1 84  ? -17.53579 3.97177   4.79386   1.000 35.31186 ?  82  LEU B C   1 
ATOM   1960 O O   . LEU B 1 84  ? -17.60979 4.87429   3.95126   1.000 38.83589 ?  82  LEU B O   1 
ATOM   1961 C CB  . LEU B 1 84  ? -17.28289 4.38408   7.26658   1.000 34.74534 ?  82  LEU B CB  1 
ATOM   1962 C CG  . LEU B 1 84  ? -16.69882 5.79420   7.21041   1.000 33.55214 ?  82  LEU B CG  1 
ATOM   1963 C CD1 . LEU B 1 84  ? -17.77247 6.82349   7.50403   1.000 35.98741 ?  82  LEU B CD1 1 
ATOM   1964 C CD2 . LEU B 1 84  ? -15.56090 5.92336   8.19102   1.000 31.77004 ?  82  LEU B CD2 1 
ATOM   1965 N N   . LEU B 1 85  ? -16.83776 2.85736   4.56824   1.000 32.51469 ?  83  LEU B N   1 
ATOM   1966 C CA  . LEU B 1 85  ? -16.14075 2.68594   3.28785   1.000 37.00045 ?  83  LEU B CA  1 
ATOM   1967 C C   . LEU B 1 85  ? -17.12770 2.55615   2.12429   1.000 37.62505 ?  83  LEU B C   1 
ATOM   1968 O O   . LEU B 1 85  ? -16.83085 2.97189   0.99499   1.000 37.19273 ?  83  LEU B O   1 
ATOM   1969 C CB  . LEU B 1 85  ? -15.22533 1.46146   3.35472   1.000 30.82745 ?  83  LEU B CB  1 
ATOM   1970 C CG  . LEU B 1 85  ? -14.22395 1.45403   4.52438   1.000 30.41895 ?  83  LEU B CG  1 
ATOM   1971 C CD1 . LEU B 1 85  ? -13.30290 0.23048   4.50346   1.000 30.07181 ?  83  LEU B CD1 1 
ATOM   1972 C CD2 . LEU B 1 85  ? -13.40925 2.74369   4.58301   1.000 31.73502 ?  83  LEU B CD2 1 
ATOM   1973 N N   . GLY B 1 86  ? -18.30787 1.99821   2.38136   1.000 34.71993 ?  84  GLY B N   1 
ATOM   1974 C CA  . GLY B 1 86  ? -19.30357 1.81758   1.33880   1.000 39.23908 ?  84  GLY B CA  1 
ATOM   1975 C C   . GLY B 1 86  ? -20.03955 3.08090   0.95067   1.000 36.76760 ?  84  GLY B C   1 
ATOM   1976 O O   . GLY B 1 86  ? -20.69626 3.10745   -0.09018  1.000 40.22324 ?  84  GLY B O   1 
ATOM   1977 N N   . GLN B 1 87  ? -19.95933 4.12213   1.76585   1.000 37.66597 ?  85  GLN B N   1 
ATOM   1978 C CA  . GLN B 1 87  ? -20.58255 5.38592   1.41151   1.000 39.46170 ?  85  GLN B CA  1 
ATOM   1979 C C   . GLN B 1 87  ? -19.75953 6.14132   0.38108   1.000 40.06807 ?  85  GLN B C   1 
ATOM   1980 O O   . GLN B 1 87  ? -20.30274 6.97644   -0.34267  1.000 38.17663 ?  85  GLN B O   1 
ATOM   1981 C CB  . GLN B 1 87  ? -20.76813 6.23374   2.67552   1.000 44.54166 ?  85  GLN B CB  1 
ATOM   1982 C CG  . GLN B 1 87  ? -22.17717 6.16118   3.26024   1.000 46.72960 ?  85  GLN B CG  1 
ATOM   1983 C CD  . GLN B 1 87  ? -22.47690 7.29184   4.23720   1.000 55.84722 ?  85  GLN B CD  1 
ATOM   1984 O OE1 . GLN B 1 87  ? -23.36868 8.11812   4.00143   1.000 61.19829 ?  85  GLN B OE1 1 
ATOM   1985 N NE2 . GLN B 1 87  ? -21.72958 7.32711   5.35296   1.000 54.44807 ?  85  GLN B NE2 1 
ATOM   1986 N N   . CYS B 1 88  ? -18.46694 5.84377   0.28284   1.000 41.33326 ?  86  CYS B N   1 
ATOM   1987 C CA  . CYS B 1 88  ? -17.61845 6.50069   -0.69520  1.000 40.70273 ?  86  CYS B CA  1 
ATOM   1988 C C   . CYS B 1 88  ? -18.03790 6.12128   -2.11156  1.000 42.98307 ?  86  CYS B C   1 
ATOM   1989 O O   . CYS B 1 88  ? -18.63908 5.07386   -2.35718  1.000 40.90585 ?  86  CYS B O   1 
ATOM   1990 C CB  . CYS B 1 88  ? -16.15372 6.13116   -0.45961  1.000 39.70370 ?  86  CYS B CB  1 
ATOM   1991 S SG  . CYS B 1 88  ? -15.52677 6.64271   1.17820   1.000 40.85214 ?  86  CYS B SG  1 
ATOM   1992 N N   . GLY B 1 89  ? -17.71044 6.99923   -3.05187  1.000 44.28313 ?  87  GLY B N   1 
ATOM   1993 C CA  . GLY B 1 89  ? -17.99230 6.72150   -4.44152  1.000 45.71868 ?  87  GLY B CA  1 
ATOM   1994 C C   . GLY B 1 89  ? -17.13596 5.59598   -4.98992  1.000 49.07011 ?  87  GLY B C   1 
ATOM   1995 O O   . GLY B 1 89  ? -16.06448 5.26867   -4.47315  1.000 46.58099 ?  87  GLY B O   1 
ATOM   1996 N N   . LYS B 1 90  ? -17.63757 4.98709   -6.06216  1.000 51.48618 ?  88  LYS B N   1 
ATOM   1997 C CA  . LYS B 1 90  ? -16.88978 3.94381   -6.74835  1.000 54.08730 ?  88  LYS B CA  1 
ATOM   1998 C C   . LYS B 1 90  ? -15.54161 4.48415   -7.21145  1.000 53.81310 ?  88  LYS B C   1 
ATOM   1999 O O   . LYS B 1 90  ? -15.47038 5.50266   -7.91396  1.000 47.11716 ?  88  LYS B O   1 
ATOM   2000 C CB  . LYS B 1 90  ? -17.69437 3.41367   -7.93512  1.000 54.96418 ?  88  LYS B CB  1 
ATOM   2001 N N   . ASP B 1 91  ? -14.47116 3.81656   -6.78904  1.000 52.52194 ?  89  ASP B N   1 
ATOM   2002 C CA  . ASP B 1 91  ? -13.11528 4.15161   -7.21484  1.000 51.11536 ?  89  ASP B CA  1 
ATOM   2003 C C   . ASP B 1 91  ? -12.69375 5.55424   -6.78499  1.000 47.59445 ?  89  ASP B C   1 
ATOM   2004 O O   . ASP B 1 91  ? -11.80187 6.14664   -7.39432  1.000 43.99251 ?  89  ASP B O   1 
ATOM   2005 C CB  . ASP B 1 91  ? -12.96193 4.00598   -8.73473  1.000 55.17193 ?  89  ASP B CB  1 
ATOM   2006 C CG  . ASP B 1 91  ? -13.26200 2.60086   -9.21813  1.000 59.59470 ?  89  ASP B CG  1 
ATOM   2007 O OD1 . ASP B 1 91  ? -13.27463 1.67551   -8.37502  1.000 62.76119 ?  89  ASP B OD1 1 
ATOM   2008 O OD2 . ASP B 1 91  ? -13.50881 2.42869   -10.43406 1.000 63.92902 -1 89  ASP B OD2 1 
ATOM   2009 N N   . ASP B 1 92  ? -13.32187 6.12047   -5.75044  1.000 49.30633 ?  90  ASP B N   1 
ATOM   2010 C CA  . ASP B 1 92  ? -12.80411 7.34638   -5.14179  1.000 45.12730 ?  90  ASP B CA  1 
ATOM   2011 C C   . ASP B 1 92  ? -11.84785 6.92305   -4.03757  1.000 40.35970 ?  90  ASP B C   1 
ATOM   2012 O O   . ASP B 1 92  ? -12.17014 6.93686   -2.84935  1.000 36.81876 ?  90  ASP B O   1 
ATOM   2013 C CB  . ASP B 1 92  ? -13.92557 8.23688   -4.62228  1.000 42.53441 ?  90  ASP B CB  1 
ATOM   2014 C CG  . ASP B 1 92  ? -13.41768 9.58941   -4.14480  1.000 43.67794 ?  90  ASP B CG  1 
ATOM   2015 O OD1 . ASP B 1 92  ? -12.17620 9.75637   -3.95121  1.000 40.38303 ?  90  ASP B OD1 1 
ATOM   2016 O OD2 . ASP B 1 92  ? -14.25905 10.49471  -3.95746  1.000 48.47655 -1 90  ASP B OD2 1 
ATOM   2017 N N   . HIS B 1 93  ? -10.63520 6.55147   -4.45655  1.000 34.75637 ?  91  HIS B N   1 
ATOM   2018 C CA  . HIS B 1 93  ? -9.71178  5.90887   -3.53687  1.000 40.79726 ?  91  HIS B CA  1 
ATOM   2019 C C   . HIS B 1 93  ? -9.22564  6.86899   -2.46569  1.000 36.30315 ?  91  HIS B C   1 
ATOM   2020 O O   . HIS B 1 93  ? -8.99939  6.44197   -1.33951  1.000 31.82956 ?  91  HIS B O   1 
ATOM   2021 C CB  . HIS B 1 93  ? -8.54459  5.30241   -4.32058  1.000 42.07799 ?  91  HIS B CB  1 
ATOM   2022 C CG  . HIS B 1 93  ? -8.99103  4.30738   -5.33993  1.000 44.26762 ?  91  HIS B CG  1 
ATOM   2023 N ND1 . HIS B 1 93  ? -8.77357  4.47511   -6.68947  1.000 45.44993 ?  91  HIS B ND1 1 
ATOM   2024 C CD2 . HIS B 1 93  ? -9.68341  3.15208   -5.20981  1.000 43.66444 ?  91  HIS B CD2 1 
ATOM   2025 C CE1 . HIS B 1 93  ? -9.30773  3.46178   -7.34676  1.000 47.96889 ?  91  HIS B CE1 1 
ATOM   2026 N NE2 . HIS B 1 93  ? -9.85750  2.64075   -6.47100  1.000 45.72193 ?  91  HIS B NE2 1 
ATOM   2027 N N   . THR B 1 94  ? -9.09028  8.16135   -2.78059  1.000 33.39713 ?  92  THR B N   1 
ATOM   2028 C CA  . THR B 1 94  ? -8.73052  9.13087   -1.75065  1.000 34.35104 ?  92  THR B CA  1 
ATOM   2029 C C   . THR B 1 94  ? -9.79230  9.18165   -0.65580  1.000 35.39227 ?  92  THR B C   1 
ATOM   2030 O O   . THR B 1 94  ? -9.46864  9.20950   0.53714   1.000 31.70370 ?  92  THR B O   1 
ATOM   2031 C CB  . THR B 1 94  ? -8.54799  10.51706  -2.36126  1.000 36.48731 ?  92  THR B CB  1 
ATOM   2032 O OG1 . THR B 1 94  ? -7.43894  10.49663  -3.25881  1.000 45.48610 ?  92  THR B OG1 1 
ATOM   2033 C CG2 . THR B 1 94  ? -8.27132  11.54870  -1.27790  1.000 37.24225 ?  92  THR B CG2 1 
ATOM   2034 N N   . SER B 1 95  ? -11.07272 9.21849   -1.04748  1.000 31.61479 ?  93  SER B N   1 
ATOM   2035 C CA  . SER B 1 95  ? -12.14155 9.28658   -0.05592  1.000 34.50821 ?  93  SER B CA  1 
ATOM   2036 C C   . SER B 1 95  ? -12.20071 8.02269   0.78129   1.000 32.80638 ?  93  SER B C   1 
ATOM   2037 O O   . SER B 1 95  ? -12.51947 8.08181   1.97382   1.000 31.26455 ?  93  SER B O   1 
ATOM   2038 C CB  . SER B 1 95  ? -13.48999 9.53898   -0.73268  1.000 36.31832 ?  93  SER B CB  1 
ATOM   2039 N N   . ILE B 1 96  ? -11.89236 6.87459   0.18593   1.000 32.03755 ?  94  ILE B N   1 
ATOM   2040 C CA  . ILE B 1 96  ? -11.87267 5.64428   0.95818   1.000 31.98555 ?  94  ILE B CA  1 
ATOM   2041 C C   . ILE B 1 96  ? -10.73087 5.67002   1.95896   1.000 34.55850 ?  94  ILE B C   1 
ATOM   2042 O O   . ILE B 1 96  ? -10.89201 5.27397   3.11948   1.000 26.69458 ?  94  ILE B O   1 
ATOM   2043 C CB  . ILE B 1 96  ? -11.76789 4.43544   0.02069   1.000 31.83347 ?  94  ILE B CB  1 
ATOM   2044 C CG1 . ILE B 1 96  ? -13.02833 4.32665   -0.82027  1.000 36.86615 ?  94  ILE B CG1 1 
ATOM   2045 C CG2 . ILE B 1 96  ? -11.59122 3.18489   0.83750   1.000 33.76101 ?  94  ILE B CG2 1 
ATOM   2046 C CD1 . ILE B 1 96  ? -12.91579 3.29605   -1.91841  1.000 40.85528 ?  94  ILE B CD1 1 
ATOM   2047 N N   . LEU B 1 97  ? -9.55553  6.12514   1.52101   1.000 32.01584 ?  95  LEU B N   1 
ATOM   2048 C CA  . LEU B 1 97  ? -8.39848  6.17140   2.40701   1.000 30.83834 ?  95  LEU B CA  1 
ATOM   2049 C C   . LEU B 1 97  ? -8.60623  7.18091   3.52672   1.000 28.37825 ?  95  LEU B C   1 
ATOM   2050 O O   . LEU B 1 97  ? -8.15673  6.96795   4.65681   1.000 25.62458 ?  95  LEU B O   1 
ATOM   2051 C CB  . LEU B 1 97  ? -7.14845  6.52429   1.60007   1.000 29.50978 ?  95  LEU B CB  1 
ATOM   2052 C CG  . LEU B 1 97  ? -5.88643  6.72463   2.40610   1.000 30.87860 ?  95  LEU B CG  1 
ATOM   2053 C CD1 . LEU B 1 97  ? -5.27295  5.37604   2.64197   1.000 31.23714 ?  95  LEU B CD1 1 
ATOM   2054 C CD2 . LEU B 1 97  ? -4.93628  7.62130   1.64488   1.000 33.10616 ?  95  LEU B CD2 1 
ATOM   2055 N N   . LYS B 1 98  ? -9.26179  8.29749   3.22028   1.000 27.20531 ?  96  LYS B N   1 
ATOM   2056 C CA  . LYS B 1 98  ? -9.52681  9.30550   4.23667   1.000 28.49243 ?  96  LYS B CA  1 
ATOM   2057 C C   . LYS B 1 98  ? -10.58325 8.82352   5.22856   1.000 27.35183 ?  96  LYS B C   1 
ATOM   2058 O O   . LYS B 1 98  ? -10.48456 9.11179   6.42882   1.000 27.90226 ?  96  LYS B O   1 
ATOM   2059 C CB  . LYS B 1 98  ? -9.93351  10.60170  3.55197   1.000 30.53154 ?  96  LYS B CB  1 
ATOM   2060 C CG  . LYS B 1 98  ? -10.02085 11.82617  4.42313   1.000 30.79038 ?  96  LYS B CG  1 
ATOM   2061 C CD  . LYS B 1 98  ? -10.85370 12.85976  3.67254   1.000 35.24796 ?  96  LYS B CD  1 
ATOM   2062 C CE  . LYS B 1 98  ? -10.97778 14.13965  4.45020   1.000 40.59819 ?  96  LYS B CE  1 
ATOM   2063 N NZ  . LYS B 1 98  ? -9.86809  14.26939  5.42415   1.000 43.80555 ?  96  LYS B NZ  1 
ATOM   2064 N N   . SER B 1 99  ? -11.54503 8.03440   4.75297   1.000 26.36096 ?  97  SER B N   1 
ATOM   2065 C CA  . SER B 1 99  ? -12.53959 7.41646   5.62916   1.000 29.91121 ?  97  SER B CA  1 
ATOM   2066 C C   . SER B 1 99  ? -11.89806 6.43552   6.59638   1.000 29.69173 ?  97  SER B C   1 
ATOM   2067 O O   . SER B 1 99  ? -12.28637 6.35446   7.76255   1.000 27.20681 ?  97  SER B O   1 
ATOM   2068 C CB  . SER B 1 99  ? -13.57091 6.68413   4.77677   1.000 31.50100 ?  97  SER B CB  1 
ATOM   2069 O OG  . SER B 1 99  ? -14.58424 7.57267   4.36405   1.000 38.18579 ?  97  SER B OG  1 
ATOM   2070 N N   . PHE B 1 100 ? -10.94421 5.64102   6.10644   1.000 27.55221 ?  98  PHE B N   1 
ATOM   2071 C CA  . PHE B 1 100 ? -10.27628 4.64233   6.93077   1.000 25.82334 ?  98  PHE B CA  1 
ATOM   2072 C C   . PHE B 1 100 ? -9.44676  5.30377   8.02369   1.000 26.93527 ?  98  PHE B C   1 
ATOM   2073 O O   . PHE B 1 100 ? -9.41425  4.83466   9.16962   1.000 25.40263 ?  98  PHE B O   1 
ATOM   2074 C CB  . PHE B 1 100 ? -9.40112  3.77505   6.02302   1.000 26.92870 ?  98  PHE B CB  1 
ATOM   2075 C CG  . PHE B 1 100 ? -8.83502  2.55201   6.67604   1.000 27.39012 ?  98  PHE B CG  1 
ATOM   2076 C CD1 . PHE B 1 100 ? -9.62060  1.42370   6.88146   1.000 24.35737 ?  98  PHE B CD1 1 
ATOM   2077 C CD2 . PHE B 1 100 ? -7.50788  2.52611   7.08443   1.000 25.28951 ?  98  PHE B CD2 1 
ATOM   2078 C CE1 . PHE B 1 100 ? -9.08121  0.30215   7.46640   1.000 24.85746 ?  98  PHE B CE1 1 
ATOM   2079 C CE2 . PHE B 1 100 ? -6.96827  1.38650   7.65914   1.000 25.11374 ?  98  PHE B CE2 1 
ATOM   2080 C CZ  . PHE B 1 100 ? -7.75656  0.28761   7.86198   1.000 23.97320 ?  98  PHE B CZ  1 
ATOM   2081 N N   . TYR B 1 101 ? -8.78123  6.39943   7.67835   1.000 24.92726 ?  99  TYR B N   1 
ATOM   2082 C CA  . TYR B 1 101 ? -8.03393  7.18562   8.64745   1.000 25.98762 ?  99  TYR B CA  1 
ATOM   2083 C C   . TYR B 1 101 ? -8.95939  7.76267   9.70272   1.000 29.01288 ?  99  TYR B C   1 
ATOM   2084 O O   . TYR B 1 101 ? -8.72633  7.61242   10.91183  1.000 26.57667 ?  99  TYR B O   1 
ATOM   2085 C CB  . TYR B 1 101 ? -7.29310  8.31009   7.92567   1.000 24.80450 ?  99  TYR B CB  1 
ATOM   2086 C CG  . TYR B 1 101 ? -6.71430  9.35194   8.83697   1.000 30.01267 ?  99  TYR B CG  1 
ATOM   2087 C CD1 . TYR B 1 101 ? -5.50441  9.12826   9.49909   1.000 29.17512 ?  99  TYR B CD1 1 
ATOM   2088 C CD2 . TYR B 1 101 ? -7.35299  10.57019  9.02371   1.000 30.12032 ?  99  TYR B CD2 1 
ATOM   2089 C CE1 . TYR B 1 101 ? -4.97710  10.06985  10.34163  1.000 31.96059 ?  99  TYR B CE1 1 
ATOM   2090 C CE2 . TYR B 1 101 ? -6.81634  11.51765  9.86543   1.000 31.63547 ?  99  TYR B CE2 1 
ATOM   2091 C CZ  . TYR B 1 101 ? -5.64060  11.26528  10.51522  1.000 32.13077 ?  99  TYR B CZ  1 
ATOM   2092 O OH  . TYR B 1 101 ? -5.11073  12.21479  11.35918  1.000 39.41421 ?  99  TYR B OH  1 
ATOM   2093 N N   . GLN B 1 102 ? -9.99868  8.46150   9.25443   1.000 29.06501 ?  100 GLN B N   1 
ATOM   2094 C CA  . GLN B 1 102 ? -10.88988 9.13105   10.18266  1.000 31.22243 ?  100 GLN B CA  1 
ATOM   2095 C C   . GLN B 1 102 ? -11.59441 8.13641   11.09244  1.000 31.74758 ?  100 GLN B C   1 
ATOM   2096 O O   . GLN B 1 102 ? -11.88816 8.45963   12.25023  1.000 33.15188 ?  100 GLN B O   1 
ATOM   2097 C CB  . GLN B 1 102 ? -11.90214 9.97338   9.41238   1.000 30.21470 ?  100 GLN B CB  1 
ATOM   2098 C CG  . GLN B 1 102 ? -12.61725 10.98824  10.27116  1.000 39.18349 ?  100 GLN B CG  1 
ATOM   2099 C CD  . GLN B 1 102 ? -11.66919 12.01175  10.85524  1.000 40.40724 ?  100 GLN B CD  1 
ATOM   2100 O OE1 . GLN B 1 102 ? -10.74256 12.45865  10.18606  1.000 43.21672 ?  100 GLN B OE1 1 
ATOM   2101 N NE2 . GLN B 1 102 ? -11.90096 12.39713  12.10428  1.000 43.35364 ?  100 GLN B NE2 1 
ATOM   2102 N N   . TRP B 1 103 ? -11.88464 6.93555   10.58840  1.000 27.41299 ?  101 TRP B N   1 
ATOM   2103 C CA  . TRP B 1 103 ? -12.53044 5.93174   11.42557  1.000 29.44155 ?  101 TRP B CA  1 
ATOM   2104 C C   . TRP B 1 103 ? -11.64822 5.57017   12.62039  1.000 29.56222 ?  101 TRP B C   1 
ATOM   2105 O O   . TRP B 1 103 ? -12.14631 5.36926   13.73442  1.000 27.53353 ?  101 TRP B O   1 
ATOM   2106 C CB  . TRP B 1 103 ? -12.86535 4.70111   10.57804  1.000 27.34699 ?  101 TRP B CB  1 
ATOM   2107 C CG  . TRP B 1 103 ? -13.61724 3.58251   11.31213  1.000 28.64042 ?  101 TRP B CG  1 
ATOM   2108 C CD1 . TRP B 1 103 ? -14.98081 3.38967   11.35930  1.000 27.42384 ?  101 TRP B CD1 1 
ATOM   2109 C CD2 . TRP B 1 103 ? -13.03669 2.48674   12.02760  1.000 26.34164 ?  101 TRP B CD2 1 
ATOM   2110 N NE1 . TRP B 1 103 ? -15.27194 2.25974   12.09395  1.000 27.96049 ?  101 TRP B NE1 1 
ATOM   2111 C CE2 . TRP B 1 103 ? -14.09737 1.68561   12.50940  1.000 27.81028 ?  101 TRP B CE2 1 
ATOM   2112 C CE3 . TRP B 1 103 ? -11.72440 2.10561   12.31124  1.000 27.22666 ?  101 TRP B CE3 1 
ATOM   2113 C CZ2 . TRP B 1 103 ? -13.87717 0.52876   13.25823  1.000 26.69786 ?  101 TRP B CZ2 1 
ATOM   2114 C CZ3 . TRP B 1 103 ? -11.50709 0.96407   13.06979  1.000 27.42675 ?  101 TRP B CZ3 1 
ATOM   2115 C CH2 . TRP B 1 103 ? -12.58215 0.18795   13.52909  1.000 31.03403 ?  101 TRP B CH2 1 
ATOM   2116 N N   . HIS B 1 104 ? -10.33483 5.49752   12.40966  1.000 25.29191 ?  102 HIS B N   1 
ATOM   2117 C CA  . HIS B 1 104 ? -9.41348  5.20982   13.50333  1.000 26.31492 ?  102 HIS B CA  1 
ATOM   2118 C C   . HIS B 1 104 ? -9.24500  6.40625   14.43000  1.000 26.85877 ?  102 HIS B C   1 
ATOM   2119 O O   . HIS B 1 104 ? -9.25063  6.25319   15.65739  1.000 28.96941 ?  102 HIS B O   1 
ATOM   2120 C CB  . HIS B 1 104 ? -8.06479  4.77750   12.94251  1.000 25.33954 ?  102 HIS B CB  1 
ATOM   2121 C CG  . HIS B 1 104 ? -8.06867  3.39480   12.37810  1.000 23.71534 ?  102 HIS B CG  1 
ATOM   2122 N ND1 . HIS B 1 104 ? -8.45394  3.12558   11.07920  1.000 25.00832 ?  102 HIS B ND1 1 
ATOM   2123 C CD2 . HIS B 1 104 ? -7.73197  2.20527   12.92650  1.000 25.02266 ?  102 HIS B CD2 1 
ATOM   2124 C CE1 . HIS B 1 104 ? -8.37628  1.82448   10.86158  1.000 23.95300 ?  102 HIS B CE1 1 
ATOM   2125 N NE2 . HIS B 1 104 ? -7.93673  1.24403   11.96484  1.000 24.10327 ?  102 HIS B NE2 1 
ATOM   2126 N N   . VAL B 1 105 ? -9.07719  7.60753   13.87185  1.000 28.22761 ?  103 VAL B N   1 
ATOM   2127 C CA  . VAL B 1 105 ? -8.98087  8.79908   14.71930  1.000 30.43127 ?  103 VAL B CA  1 
ATOM   2128 C C   . VAL B 1 105 ? -10.22601 8.93834   15.59568  1.000 34.77557 ?  103 VAL B C   1 
ATOM   2129 O O   . VAL B 1 105 ? -10.13933 9.26616   16.78785  1.000 33.01005 ?  103 VAL B O   1 
ATOM   2130 C CB  . VAL B 1 105 ? -8.76091  10.05541  13.85656  1.000 32.60870 ?  103 VAL B CB  1 
ATOM   2131 C CG1 . VAL B 1 105 ? -8.89121  11.30453  14.70095  1.000 32.91877 ?  103 VAL B CG1 1 
ATOM   2132 C CG2 . VAL B 1 105 ? -7.39451  10.01051  13.18317  1.000 31.10390 ?  103 VAL B CG2 1 
ATOM   2133 N N   . ASP B 1 106 ? -11.39982 8.67964   15.02193  1.000 31.17718 ?  104 ASP B N   1 
ATOM   2134 C CA  . ASP B 1 106 ? -12.64056 8.88429   15.75814  1.000 31.82826 ?  104 ASP B CA  1 
ATOM   2135 C C   . ASP B 1 106 ? -12.78123 7.85497   16.86188  1.000 32.58181 ?  104 ASP B C   1 
ATOM   2136 O O   . ASP B 1 106 ? -13.27336 8.16442   17.95082  1.000 34.90542 ?  104 ASP B O   1 
ATOM   2137 C CB  . ASP B 1 106 ? -13.83385 8.81543   14.80088  1.000 33.50094 ?  104 ASP B CB  1 
ATOM   2138 C CG  . ASP B 1 106 ? -14.06423 10.13062  14.04338  1.000 41.46959 ?  104 ASP B CG  1 
ATOM   2139 O OD1 . ASP B 1 106 ? -13.52203 11.18466  14.45817  1.000 45.83321 ?  104 ASP B OD1 1 
ATOM   2140 O OD2 . ASP B 1 106 ? -14.75799 10.10781  12.99997  1.000 43.53447 -1 104 ASP B OD2 1 
ATOM   2141 N N   . LEU B 1 107 ? -12.34750 6.62713   16.59796  1.000 30.14061 ?  105 LEU B N   1 
ATOM   2142 C CA  . LEU B 1 107 ? -12.40548 5.58991   17.60977  1.000 30.66473 ?  105 LEU B CA  1 
ATOM   2143 C C   . LEU B 1 107 ? -11.46509 5.91642   18.75661  1.000 36.04053 ?  105 LEU B C   1 
ATOM   2144 O O   . LEU B 1 107 ? -11.81417 5.73379   19.92833  1.000 36.40795 ?  105 LEU B O   1 
ATOM   2145 C CB  . LEU B 1 107 ? -12.06747 4.25010   16.95956  1.000 30.16541 ?  105 LEU B CB  1 
ATOM   2146 C CG  . LEU B 1 107 ? -12.36476 2.92184   17.62776  1.000 34.51432 ?  105 LEU B CG  1 
ATOM   2147 C CD1 . LEU B 1 107 ? -13.88331 2.81031   17.83582  1.000 31.68140 ?  105 LEU B CD1 1 
ATOM   2148 C CD2 . LEU B 1 107 ? -11.85775 1.78875   16.73849  1.000 29.25833 ?  105 LEU B CD2 1 
ATOM   2149 N N   . ALA B 1 108 ? -10.28373 6.45236   18.43596  1.000 32.16233 ?  106 ALA B N   1 
ATOM   2150 C CA  . ALA B 1 108 ? -9.31279  6.78462   19.46435  1.000 35.21572 ?  106 ALA B CA  1 
ATOM   2151 C C   . ALA B 1 108 ? -9.70689  8.04303   20.22010  1.000 38.96539 ?  106 ALA B C   1 
ATOM   2152 O O   . ALA B 1 108 ? -9.50467  8.12347   21.43247  1.000 41.48470 ?  106 ALA B O   1 
ATOM   2153 C CB  . ALA B 1 108 ? -7.91987  6.94512   18.84710  1.000 33.14614 ?  106 ALA B CB  1 
ATOM   2154 N N   . TYR B 1 109 ? -10.26303 9.04042   19.53428  1.000 39.82385 ?  107 TYR B N   1 
ATOM   2155 C CA  . TYR B 1 109 ? -10.67240 10.23811  20.25043  1.000 40.73384 ?  107 TYR B CA  1 
ATOM   2156 C C   . TYR B 1 109 ? -11.94664 10.03804  21.05179  1.000 42.12386 ?  107 TYR B C   1 
ATOM   2157 O O   . TYR B 1 109 ? -12.20613 10.83190  21.95840  1.000 44.97677 ?  107 TYR B O   1 
ATOM   2158 C CB  . TYR B 1 109 ? -10.85112 11.41708  19.29401  1.000 41.04202 ?  107 TYR B CB  1 
ATOM   2159 C CG  . TYR B 1 109 ? -10.49152 12.75403  19.92226  1.000 41.62625 ?  107 TYR B CG  1 
ATOM   2160 N N   . ARG B 1 110 ? -12.74465 9.01307   20.74490  1.000 41.72110 ?  108 ARG B N   1 
ATOM   2161 C CA  . ARG B 1 110 ? -13.99816 8.78584   21.46887  1.000 42.59830 ?  108 ARG B CA  1 
ATOM   2162 C C   . ARG B 1 110 ? -13.74419 8.02217   22.76151  1.000 48.55215 ?  108 ARG B C   1 
ATOM   2163 O O   . ARG B 1 110 ? -13.03606 8.51270   23.65544  1.000 52.53171 ?  108 ARG B O   1 
ATOM   2164 C CB  . ARG B 1 110 ? -15.01617 8.02616   20.60760  1.000 41.27291 ?  108 ARG B CB  1 
ATOM   2165 N N   . GLY B 1 112 ? -13.66496 8.82271   26.63567  1.000 42.84654 ?  110 GLY B N   1 
ATOM   2166 C CA  . GLY B 1 112 ? -12.80295 8.59070   27.78607  1.000 50.38397 ?  110 GLY B CA  1 
ATOM   2167 C C   . GLY B 1 112 ? -11.69303 7.59888   27.48820  1.000 51.73847 ?  110 GLY B C   1 
ATOM   2168 O O   . GLY B 1 112 ? -11.29803 6.77948   28.33047  1.000 51.06150 ?  110 GLY B O   1 
ATOM   2169 N N   . TYR B 1 113 ? -11.16216 7.70525   26.27618  1.000 49.08771 ?  111 TYR B N   1 
ATOM   2170 C CA  . TYR B 1 113 ? -10.43996 6.60251   25.65553  1.000 46.24121 ?  111 TYR B CA  1 
ATOM   2171 C C   . TYR B 1 113 ? -9.11041  6.29396   26.33149  1.000 48.29958 ?  111 TYR B C   1 
ATOM   2172 O O   . TYR B 1 113 ? -8.15529  7.07896   26.25887  1.000 48.81052 ?  111 TYR B O   1 
ATOM   2173 C CB  . TYR B 1 113 ? -10.22967 6.91987   24.19010  1.000 44.52493 ?  111 TYR B CB  1 
ATOM   2174 C CG  . TYR B 1 113 ? -9.57927  5.82199   23.41884  1.000 44.17278 ?  111 TYR B CG  1 
ATOM   2175 C CD1 . TYR B 1 113 ? -10.31907 4.78245   22.85561  1.000 41.62465 ?  111 TYR B CD1 1 
ATOM   2176 C CD2 . TYR B 1 113 ? -8.20358  5.85145   23.21301  1.000 42.57739 ?  111 TYR B CD2 1 
ATOM   2177 C CE1 . TYR B 1 113 ? -9.66941  3.77878   22.11285  1.000 40.68712 ?  111 TYR B CE1 1 
ATOM   2178 C CE2 . TYR B 1 113 ? -7.56247  4.88471   22.49470  1.000 39.60450 ?  111 TYR B CE2 1 
ATOM   2179 C CZ  . TYR B 1 113 ? -8.28082  3.85059   21.94016  1.000 40.30379 ?  111 TYR B CZ  1 
ATOM   2180 O OH  . TYR B 1 113 ? -7.56454  2.90283   21.21330  1.000 39.32948 ?  111 TYR B OH  1 
ATOM   2181 N N   . ASN B 1 114 ? -9.04345  5.11364   26.93247  1.000 47.81564 ?  112 ASN B N   1 
ATOM   2182 C CA  . ASN B 1 114 ? -7.82074  4.49550   27.41115  1.000 44.75724 ?  112 ASN B CA  1 
ATOM   2183 C C   . ASN B 1 114 ? -7.56245  3.19458   26.66471  1.000 42.68732 ?  112 ASN B C   1 
ATOM   2184 O O   . ASN B 1 114 ? -7.09934  2.21218   27.23416  1.000 44.48314 ?  112 ASN B O   1 
ATOM   2185 C CB  . ASN B 1 114 ? -7.89612  4.26167   28.91708  1.000 45.76271 ?  112 ASN B CB  1 
ATOM   2186 C CG  . ASN B 1 114 ? -8.84072  3.12261   29.28883  1.000 45.08964 ?  112 ASN B CG  1 
ATOM   2187 O OD1 . ASN B 1 114 ? -9.87254  2.91339   28.62984  1.000 44.67205 ?  112 ASN B OD1 1 
ATOM   2188 N ND2 . ASN B 1 114 ? -8.52504  2.41771   30.38146  1.000 41.59286 ?  112 ASN B ND2 1 
ATOM   2189 N N   . GLY B 1 115 ? -7.85667  3.16270   25.38442  1.000 42.17657 ?  113 GLY B N   1 
ATOM   2190 C CA  . GLY B 1 115 ? -7.65708  1.90439   24.69987  1.000 38.98153 ?  113 GLY B CA  1 
ATOM   2191 C C   . GLY B 1 115 ? -8.97858  1.25664   24.33096  1.000 38.07842 ?  113 GLY B C   1 
ATOM   2192 O O   . GLY B 1 115 ? -9.99306  1.40189   25.02750  1.000 37.51619 ?  113 GLY B O   1 
ATOM   2193 N N   . THR B 1 116 ? -8.96761  0.51954   23.22475  1.000 35.59495 ?  114 THR B N   1 
ATOM   2194 C CA  . THR B 1 116 ? -10.20369 -0.05336  22.72617  1.000 36.64655 ?  114 THR B CA  1 
ATOM   2195 C C   . THR B 1 116 ? -10.64464 -1.23285  23.57965  1.000 33.17557 ?  114 THR B C   1 
ATOM   2196 O O   . THR B 1 116 ? -9.86665  -1.82326  24.33353  1.000 31.09492 ?  114 THR B O   1 
ATOM   2197 C CB  . THR B 1 116 ? -10.05625 -0.48442  21.27582  1.000 35.46760 ?  114 THR B CB  1 
ATOM   2198 O OG1 . THR B 1 116 ? -9.29492  -1.69886  21.22171  1.000 30.66596 ?  114 THR B OG1 1 
ATOM   2199 C CG2 . THR B 1 116 ? -9.41984  0.59089   20.44308  1.000 36.62064 ?  114 THR B CG2 1 
ATOM   2200 N N   . LEU B 1 117 ? -11.92893 -1.54915  23.46065  1.000 31.44813 ?  115 LEU B N   1 
ATOM   2201 C CA  . LEU B 1 117 ? -12.49219 -2.67052  24.19293  1.000 30.42731 ?  115 LEU B CA  1 
ATOM   2202 C C   . LEU B 1 117 ? -11.85300 -3.97907  23.76548  1.000 30.26814 ?  115 LEU B C   1 
ATOM   2203 O O   . LEU B 1 117 ? -11.64869 -4.87497  24.58885  1.000 29.07171 ?  115 LEU B O   1 
ATOM   2204 C CB  . LEU B 1 117 ? -14.00600 -2.70026  23.97730  1.000 34.43512 ?  115 LEU B CB  1 
ATOM   2205 C CG  . LEU B 1 117 ? -14.95126 -3.09297  25.11126  1.000 37.13525 ?  115 LEU B CG  1 
ATOM   2206 C CD1 . LEU B 1 117 ? -14.42333 -2.73673  26.50578  1.000 36.58016 ?  115 LEU B CD1 1 
ATOM   2207 C CD2 . LEU B 1 117 ? -16.28287 -2.39215  24.87956  1.000 40.62569 ?  115 LEU B CD2 1 
ATOM   2208 N N   . LEU B 1 118 ? -11.52218 -4.11485  22.48119  1.000 27.04450 ?  116 LEU B N   1 
ATOM   2209 C CA  . LEU B 1 118 ? -10.87827 -5.34711  22.03765  1.000 29.28915 ?  116 LEU B CA  1 
ATOM   2210 C C   . LEU B 1 118 ? -9.48065  -5.48845  22.63326  1.000 29.02124 ?  116 LEU B C   1 
ATOM   2211 O O   . LEU B 1 118 ? -9.08508  -6.58561  23.04322  1.000 30.18534 ?  116 LEU B O   1 
ATOM   2212 C CB  . LEU B 1 118 ? -10.80193 -5.39308  20.51642  1.000 27.51337 ?  116 LEU B CB  1 
ATOM   2213 C CG  . LEU B 1 118 ? -12.06842 -5.17264  19.70983  1.000 30.02561 ?  116 LEU B CG  1 
ATOM   2214 C CD1 . LEU B 1 118 ? -11.83552 -5.63797  18.28421  1.000 31.47056 ?  116 LEU B CD1 1 
ATOM   2215 C CD2 . LEU B 1 118 ? -13.23117 -5.90049  20.31071  1.000 31.57802 ?  116 LEU B CD2 1 
ATOM   2216 N N   . THR B 1 119 ? -8.72425  -4.39251  22.69332  1.000 27.31901 ?  117 THR B N   1 
ATOM   2217 C CA  . THR B 1 119 ? -7.40489  -4.44250  23.32886  1.000 31.15291 ?  117 THR B CA  1 
ATOM   2218 C C   . THR B 1 119 ? -7.52210  -4.78717  24.80850  1.000 28.15572 ?  117 THR B C   1 
ATOM   2219 O O   . THR B 1 119 ? -6.73562  -5.58479  25.32460  1.000 30.32323 ?  117 THR B O   1 
ATOM   2220 C CB  . THR B 1 119 ? -6.67682  -3.10595  23.16624  1.000 30.27473 ?  117 THR B CB  1 
ATOM   2221 O OG1 . THR B 1 119 ? -6.44631  -2.86303  21.77946  1.000 31.18810 ?  117 THR B OG1 1 
ATOM   2222 C CG2 . THR B 1 119 ? -5.32043  -3.10842  23.90255  1.000 27.76687 ?  117 THR B CG2 1 
ATOM   2223 N N   . LYS B 1 120 ? -8.49463  -4.19231  25.50383  1.000 30.57783 ?  118 LYS B N   1 
ATOM   2224 C CA  . LYS B 1 120 ? -8.71794  -4.54380  26.90202  1.000 27.94363 ?  118 LYS B CA  1 
ATOM   2225 C C   . LYS B 1 120 ? -8.98271  -6.02868  27.05635  1.000 29.77801 ?  118 LYS B C   1 
ATOM   2226 O O   . LYS B 1 120 ? -8.51002  -6.65929  28.01148  1.000 29.62735 ?  118 LYS B O   1 
ATOM   2227 C CB  . LYS B 1 120 ? -9.87416  -3.74016  27.47004  1.000 32.83100 ?  118 LYS B CB  1 
ATOM   2228 C CG  . LYS B 1 120 ? -9.55529  -2.27133  27.64423  1.000 34.47832 ?  118 LYS B CG  1 
ATOM   2229 C CD  . LYS B 1 120 ? -10.71444 -1.53039  28.26575  1.000 34.98380 ?  118 LYS B CD  1 
ATOM   2230 C CE  . LYS B 1 120 ? -10.44450 -0.04660  28.25692  1.000 40.12419 ?  118 LYS B CE  1 
ATOM   2231 N NZ  . LYS B 1 120 ? -11.57501 0.75450   28.76021  1.000 42.55940 ?  118 LYS B NZ  1 
ATOM   2232 N N   . ALA B 1 121 ? -9.75357  -6.60658  26.14073  1.000 27.06532 ?  119 ALA B N   1 
ATOM   2233 C CA  . ALA B 1 121 ? -10.08928 -8.01829  26.27960  1.000 31.46276 ?  119 ALA B CA  1 
ATOM   2234 C C   . ALA B 1 121 ? -8.85764  -8.89919  26.10149  1.000 31.80840 ?  119 ALA B C   1 
ATOM   2235 O O   . ALA B 1 121 ? -8.69961  -9.89884  26.81150  1.000 31.36526 ?  119 ALA B O   1 
ATOM   2236 C CB  . ALA B 1 121 ? -11.17291 -8.40772  25.27280  1.000 30.65579 ?  119 ALA B CB  1 
ATOM   2237 N N   . VAL B 1 122 ? -7.99392  -8.56284  25.13764  1.000 28.56528 ?  120 VAL B N   1 
ATOM   2238 C CA  . VAL B 1 122 ? -6.78941  -9.35882  24.90361  1.000 30.48672 ?  120 VAL B CA  1 
ATOM   2239 C C   . VAL B 1 122 ? -5.84529  -9.26871  26.10348  1.000 29.23490 ?  120 VAL B C   1 
ATOM   2240 O O   . VAL B 1 122 ? -5.24142  -10.26744 26.51812  1.000 31.13642 ?  120 VAL B O   1 
ATOM   2241 C CB  . VAL B 1 122 ? -6.10186  -8.91567  23.59731  1.000 31.19477 ?  120 VAL B CB  1 
ATOM   2242 C CG1 . VAL B 1 122 ? -4.76276  -9.63302  23.41254  1.000 28.41975 ?  120 VAL B CG1 1 
ATOM   2243 C CG2 . VAL B 1 122 ? -6.99539  -9.18865  22.42283  1.000 29.82430 ?  120 VAL B CG2 1 
ATOM   2244 N N   . ILE B 1 123 ? -5.71423  -8.07821  26.68092  1.000 26.45280 ?  121 ILE B N   1 
ATOM   2245 C CA  . ILE B 1 123 ? -4.90273  -7.90345  27.88105  1.000 29.02806 ?  121 ILE B CA  1 
ATOM   2246 C C   . ILE B 1 123 ? -5.48687  -8.69919  29.03595  1.000 32.31897 ?  121 ILE B C   1 
ATOM   2247 O O   . ILE B 1 123 ? -4.77567  -9.42471  29.73979  1.000 29.03788 ?  121 ILE B O   1 
ATOM   2248 C CB  . ILE B 1 123 ? -4.81587  -6.41452  28.24159  1.000 30.45732 ?  121 ILE B CB  1 
ATOM   2249 C CG1 . ILE B 1 123 ? -3.89631  -5.69831  27.27305  1.000 28.62120 ?  121 ILE B CG1 1 
ATOM   2250 C CG2 . ILE B 1 123 ? -4.40186  -6.23542  29.69736  1.000 33.59171 ?  121 ILE B CG2 1 
ATOM   2251 C CD1 . ILE B 1 123 ? -4.04884  -4.24210  27.35074  1.000 29.56737 ?  121 ILE B CD1 1 
ATOM   2252 N N   . GLU B 1 124 ? -6.79349  -8.56818  29.25504  1.000 28.38770 ?  122 GLU B N   1 
ATOM   2253 C CA  . GLU B 1 124 ? -7.39397  -9.15296  30.44977  1.000 33.73843 ?  122 GLU B CA  1 
ATOM   2254 C C   . GLU B 1 124 ? -7.52966  -10.66835 30.34480  1.000 35.72139 ?  122 GLU B C   1 
ATOM   2255 O O   . GLU B 1 124 ? -7.46962  -11.36023 31.36657  1.000 33.32860 ?  122 GLU B O   1 
ATOM   2256 C CB  . GLU B 1 124 ? -8.76131  -8.51204  30.71679  1.000 31.61042 ?  122 GLU B CB  1 
ATOM   2257 N N   . TYR B 1 125 ? -7.69329  -11.21726 29.13794  1.000 35.62377 ?  123 TYR B N   1 
ATOM   2258 C CA  . TYR B 1 125 ? -8.03902  -12.63224 29.07487  1.000 35.34661 ?  123 TYR B CA  1 
ATOM   2259 C C   . TYR B 1 125 ? -6.95969  -13.45760 28.39525  1.000 39.19258 ?  123 TYR B C   1 
ATOM   2260 O O   . TYR B 1 125 ? -7.24672  -14.20139 27.45180  1.000 40.42241 ?  123 TYR B O   1 
ATOM   2261 C CB  . TYR B 1 125 ? -9.38539  -12.81503 28.36750  1.000 37.26791 ?  123 TYR B CB  1 
ATOM   2262 C CG  . TYR B 1 125 ? -10.49917 -12.32645 29.25314  1.000 38.18973 ?  123 TYR B CG  1 
ATOM   2263 C CD1 . TYR B 1 125 ? -11.01558 -13.11992 30.27716  1.000 43.00374 ?  123 TYR B CD1 1 
ATOM   2264 C CD2 . TYR B 1 125 ? -11.01539 -11.05047 29.08387  1.000 35.30629 ?  123 TYR B CD2 1 
ATOM   2265 C CE1 . TYR B 1 125 ? -12.02623 -12.63938 31.10755  1.000 40.92475 ?  123 TYR B CE1 1 
ATOM   2266 C CE2 . TYR B 1 125 ? -12.00257 -10.56756 29.88843  1.000 39.14563 ?  123 TYR B CE2 1 
ATOM   2267 C CZ  . TYR B 1 125 ? -12.51567 -11.36230 30.89841  1.000 39.95907 ?  123 TYR B CZ  1 
ATOM   2268 O OH  . TYR B 1 125 ? -13.50578 -10.85504 31.69571  1.000 40.26793 ?  123 TYR B OH  1 
ATOM   2269 N N   . TRP B 1 126 ? -5.72097  -13.36845 28.89639  1.000 39.90505 ?  124 TRP B N   1 
ATOM   2270 C CA  . TRP B 1 126 ? -4.65397  -14.23882 28.40436  1.000 42.86421 ?  124 TRP B CA  1 
ATOM   2271 C C   . TRP B 1 126 ? -5.01492  -15.70442 28.57151  1.000 44.98594 ?  124 TRP B C   1 
ATOM   2272 O O   . TRP B 1 126 ? -4.48066  -16.55495 27.84883  1.000 44.34480 ?  124 TRP B O   1 
ATOM   2273 C CB  . TRP B 1 126 ? -3.33266  -13.95313 29.14302  1.000 40.55470 ?  124 TRP B CB  1 
ATOM   2274 C CG  . TRP B 1 126 ? -3.51005  -13.97993 30.62861  1.000 41.00355 ?  124 TRP B CG  1 
ATOM   2275 C CD1 . TRP B 1 126 ? -3.89093  -12.93622 31.42982  1.000 38.98233 ?  124 TRP B CD1 1 
ATOM   2276 C CD2 . TRP B 1 126 ? -3.37225  -15.11607 31.48969  1.000 42.54386 ?  124 TRP B CD2 1 
ATOM   2277 N NE1 . TRP B 1 126 ? -3.99888  -13.35762 32.73605  1.000 39.70593 ?  124 TRP B NE1 1 
ATOM   2278 C CE2 . TRP B 1 126 ? -3.68032  -14.68769 32.80171  1.000 42.78355 ?  124 TRP B CE2 1 
ATOM   2279 C CE3 . TRP B 1 126 ? -3.02092  -16.45433 31.28201  1.000 44.32749 ?  124 TRP B CE3 1 
ATOM   2280 C CZ2 . TRP B 1 126 ? -3.63012  -15.54496 33.90088  1.000 44.24585 ?  124 TRP B CZ2 1 
ATOM   2281 C CZ3 . TRP B 1 126 ? -2.97555  -17.30764 32.37791  1.000 43.05004 ?  124 TRP B CZ3 1 
ATOM   2282 C CH2 . TRP B 1 126 ? -3.27948  -16.84808 33.66999  1.000 44.15909 ?  124 TRP B CH2 1 
ATOM   2283 N N   . ASN B 1 127 ? -5.92131  -16.00464 29.49788  1.000 43.59802 ?  125 ASN B N   1 
ATOM   2284 C CA  . ASN B 1 127 ? -6.29403  -17.36022 29.87346  1.000 46.60843 ?  125 ASN B CA  1 
ATOM   2285 C C   . ASN B 1 127 ? -7.41507  -17.93892 29.01945  1.000 47.42419 ?  125 ASN B C   1 
ATOM   2286 O O   . ASN B 1 127 ? -7.80670  -19.09196 29.24391  1.000 49.34920 ?  125 ASN B O   1 
ATOM   2287 C CB  . ASN B 1 127 ? -6.73866  -17.39048 31.33960  1.000 46.30620 ?  125 ASN B CB  1 
ATOM   2288 C CG  . ASN B 1 127 ? -7.77811  -16.31745 31.65898  1.000 47.70801 ?  125 ASN B CG  1 
ATOM   2289 O OD1 . ASN B 1 127 ? -7.44864  -15.14068 31.82931  1.000 47.09639 ?  125 ASN B OD1 1 
ATOM   2290 N ND2 . ASN B 1 127 ? -9.04564  -16.72786 31.75902  1.000 47.91848 ?  125 ASN B ND2 1 
ATOM   2291 N N   . LEU B 1 128 ? -7.98516  -17.15898 28.09780  1.000 46.74589 ?  126 LEU B N   1 
ATOM   2292 C CA  . LEU B 1 128 ? -9.04461  -17.62961 27.20432  1.000 44.53978 ?  126 LEU B CA  1 
ATOM   2293 C C   . LEU B 1 128 ? -8.55544  -17.41591 25.77949  1.000 44.05256 ?  126 LEU B C   1 
ATOM   2294 O O   . LEU B 1 128 ? -8.77890  -16.34630 25.19397  1.000 43.12573 ?  126 LEU B O   1 
ATOM   2295 C CB  . LEU B 1 128 ? -10.36575 -16.90111 27.45024  1.000 44.29596 ?  126 LEU B CB  1 
ATOM   2296 C CG  . LEU B 1 128 ? -10.99308 -16.89458 28.84893  1.000 46.42601 ?  126 LEU B CG  1 
ATOM   2297 C CD1 . LEU B 1 128 ? -12.25323 -16.01782 28.87390  1.000 44.05678 ?  126 LEU B CD1 1 
ATOM   2298 C CD2 . LEU B 1 128 ? -11.29662 -18.29406 29.37035  1.000 44.45723 ?  126 LEU B CD2 1 
ATOM   2299 N N   . PRO B 1 129 ? -7.87999  -18.40560 25.18477  1.000 45.49435 ?  127 PRO B N   1 
ATOM   2300 C CA  . PRO B 1 129 ? -7.18325  -18.17061 23.90811  1.000 45.18144 ?  127 PRO B CA  1 
ATOM   2301 C C   . PRO B 1 129 ? -8.09950  -17.90862 22.72493  1.000 44.38328 ?  127 PRO B C   1 
ATOM   2302 O O   . PRO B 1 129 ? -7.59953  -17.49873 21.66814  1.000 39.18778 ?  127 PRO B O   1 
ATOM   2303 C CB  . PRO B 1 129 ? -6.37933  -19.46377 23.70624  1.000 46.92264 ?  127 PRO B CB  1 
ATOM   2304 C CG  . PRO B 1 129 ? -6.22393  -20.02964 25.10006  1.000 47.53475 ?  127 PRO B CG  1 
ATOM   2305 C CD  . PRO B 1 129 ? -7.53137  -19.70939 25.77044  1.000 46.02475 ?  127 PRO B CD  1 
ATOM   2306 N N   . ASP B 1 130 ? -9.40836  -18.13123 22.85709  1.000 42.73803 ?  128 ASP B N   1 
ATOM   2307 C CA  . ASP B 1 130 ? -10.32174 -17.78355 21.77736  1.000 41.98289 ?  128 ASP B CA  1 
ATOM   2308 C C   . ASP B 1 130 ? -10.52986 -16.27717 21.66805  1.000 41.71778 ?  128 ASP B C   1 
ATOM   2309 O O   . ASP B 1 130 ? -10.92173 -15.79398 20.60242  1.000 38.97916 ?  128 ASP B O   1 
ATOM   2310 C CB  . ASP B 1 130 ? -11.66315 -18.48921 21.97828  1.000 46.74380 ?  128 ASP B CB  1 
ATOM   2311 N N   . ILE B 1 131 ? -10.26205 -15.51828 22.73388  1.000 42.00014 ?  129 ILE B N   1 
ATOM   2312 C CA  . ILE B 1 131 ? -10.48798 -14.07748 22.68305  1.000 37.42671 ?  129 ILE B CA  1 
ATOM   2313 C C   . ILE B 1 131 ? -9.43036  -13.40988 21.81362  1.000 37.14972 ?  129 ILE B C   1 
ATOM   2314 O O   . ILE B 1 131 ? -9.74045  -12.60818 20.92047  1.000 30.75948 ?  129 ILE B O   1 
ATOM   2315 C CB  . ILE B 1 131 ? -10.52046 -13.50068 24.10725  1.000 36.42540 ?  129 ILE B CB  1 
ATOM   2316 C CG1 . ILE B 1 131 ? -11.77276 -14.01511 24.82361  1.000 38.15515 ?  129 ILE B CG1 1 
ATOM   2317 C CG2 . ILE B 1 131 ? -10.42280 -11.97710 24.10620  1.000 30.48587 ?  129 ILE B CG2 1 
ATOM   2318 C CD1 . ILE B 1 131 ? -12.25670 -13.12215 25.91073  1.000 38.21222 ?  129 ILE B CD1 1 
ATOM   2319 N N   . LYS B 1 132 ? -8.16578  -13.74448 22.05582  1.000 35.79256 ?  130 LYS B N   1 
ATOM   2320 C CA  . LYS B 1 132 ? -7.09223  -13.24645 21.21233  1.000 35.28691 ?  130 LYS B CA  1 
ATOM   2321 C C   . LYS B 1 132 ? -7.30408  -13.65444 19.75760  1.000 37.16119 ?  130 LYS B C   1 
ATOM   2322 O O   . LYS B 1 132 ? -7.02459  -12.87634 18.83838  1.000 35.49128 ?  130 LYS B O   1 
ATOM   2323 C CB  . LYS B 1 132 ? -5.75778  -13.75577 21.74220  1.000 35.71187 ?  130 LYS B CB  1 
ATOM   2324 C CG  . LYS B 1 132 ? -4.55266  -13.34565 20.93530  1.000 39.39683 ?  130 LYS B CG  1 
ATOM   2325 C CD  . LYS B 1 132 ? -3.37582  -14.26044 21.26326  1.000 43.22019 ?  130 LYS B CD  1 
ATOM   2326 C CE  . LYS B 1 132 ? -2.17331  -13.44852 21.68841  1.000 45.78007 ?  130 LYS B CE  1 
ATOM   2327 N NZ  . LYS B 1 132 ? -2.08380  -12.20084 20.88872  1.000 43.19159 ?  130 LYS B NZ  1 
ATOM   2328 N N   . MET B 1 133 ? -7.83294  -14.85477 19.52460  1.000 38.04752 ?  131 MET B N   1 
ATOM   2329 C CA  . MET B 1 133 ? -8.01888  -15.28795 18.14770  1.000 38.99686 ?  131 MET B CA  1 
ATOM   2330 C C   . MET B 1 133 ? -9.16697  -14.53635 17.48067  1.000 34.44485 ?  131 MET B C   1 
ATOM   2331 O O   . MET B 1 133 ? -9.07784  -14.18458 16.30161  1.000 34.63906 ?  131 MET B O   1 
ATOM   2332 C CB  . MET B 1 133 ? -8.24737  -16.79350 18.09552  1.000 43.37766 ?  131 MET B CB  1 
ATOM   2333 C CG  . MET B 1 133 ? -6.99409  -17.57488 17.72534  1.000 47.05056 ?  131 MET B CG  1 
ATOM   2334 S SD  . MET B 1 133 ? -7.14650  -19.31376 18.14242  1.000 62.68295 ?  131 MET B SD  1 
ATOM   2335 C CE  . MET B 1 133 ? -8.87401  -19.57906 17.69706  1.000 49.59582 ?  131 MET B CE  1 
ATOM   2336 N N   . LYS B 1 134 ? -10.24066 -14.26725 18.22143  1.000 34.26859 ?  132 LYS B N   1 
ATOM   2337 C CA  . LYS B 1 134 ? -11.31302 -13.43694 17.68875  1.000 35.09468 ?  132 LYS B CA  1 
ATOM   2338 C C   . LYS B 1 134 ? -10.81570 -12.03820 17.35620  1.000 33.59164 ?  132 LYS B C   1 
ATOM   2339 O O   . LYS B 1 134 ? -11.23102 -11.45156 16.34958  1.000 27.60496 ?  132 LYS B O   1 
ATOM   2340 C CB  . LYS B 1 134 ? -12.47867 -13.35773 18.67822  1.000 31.22081 ?  132 LYS B CB  1 
ATOM   2341 C CG  . LYS B 1 134 ? -13.36788 -14.57716 18.67675  1.000 38.07362 ?  132 LYS B CG  1 
ATOM   2342 C CD  . LYS B 1 134 ? -14.39908 -14.51512 19.80618  1.000 38.64035 ?  132 LYS B CD  1 
ATOM   2343 C CE  . LYS B 1 134 ? -15.13764 -15.83990 19.93138  1.000 40.88836 ?  132 LYS B CE  1 
ATOM   2344 N NZ  . LYS B 1 134 ? -16.18225 -15.98702 18.87132  1.000 42.70513 ?  132 LYS B NZ  1 
ATOM   2345 N N   . VAL B 1 135 ? -9.94805  -11.47069 18.20010  1.000 27.88588 ?  133 VAL B N   1 
ATOM   2346 C CA  . VAL B 1 135 ? -9.50269  -10.10539 17.93833  1.000 29.64172 ?  133 VAL B CA  1 
ATOM   2347 C C   . VAL B 1 135 ? -8.50676  -10.08314 16.78154  1.000 31.26282 ?  133 VAL B C   1 
ATOM   2348 O O   . VAL B 1 135 ? -8.52725  -9.16598  15.94852  1.000 27.54385 ?  133 VAL B O   1 
ATOM   2349 C CB  . VAL B 1 135 ? -8.94291  -9.45845  19.21568  1.000 28.73203 ?  133 VAL B CB  1 
ATOM   2350 C CG1 . VAL B 1 135 ? -8.37368  -8.06914  18.91403  1.000 28.27739 ?  133 VAL B CG1 1 
ATOM   2351 C CG2 . VAL B 1 135 ? -10.05240 -9.31327  20.24158  1.000 29.16022 ?  133 VAL B CG2 1 
ATOM   2352 N N   . GLU B 1 136 ? -7.63824  -11.10043 16.70225  1.000 29.01545 ?  134 GLU B N   1 
ATOM   2353 C CA  . GLU B 1 136 ? -6.76491  -11.26902 15.54657  1.000 32.80468 ?  134 GLU B CA  1 
ATOM   2354 C C   . GLU B 1 136 ? -7.58691  -11.41327 14.27524  1.000 32.14025 ?  134 GLU B C   1 
ATOM   2355 O O   . GLU B 1 136 ? -7.23411  -10.85869 13.22591  1.000 31.13971 ?  134 GLU B O   1 
ATOM   2356 C CB  . GLU B 1 136 ? -5.87740  -12.50847 15.72721  1.000 35.05423 ?  134 GLU B CB  1 
ATOM   2357 C CG  . GLU B 1 136 ? -4.67356  -12.33588 16.65731  1.000 39.93054 ?  134 GLU B CG  1 
ATOM   2358 C CD  . GLU B 1 136 ? -3.95680  -13.65440 16.96618  1.000 46.57512 ?  134 GLU B CD  1 
ATOM   2359 O OE1 . GLU B 1 136 ? -4.62388  -14.72049 17.02654  1.000 46.51529 ?  134 GLU B OE1 1 
ATOM   2360 O OE2 . GLU B 1 136 ? -2.71429  -13.62360 17.14592  1.000 50.62641 -1 134 GLU B OE2 1 
ATOM   2361 N N   . ASP B 1 137 ? -8.67773  -12.17950 14.34781  1.000 33.53032 ?  135 ASP B N   1 
ATOM   2362 C CA  . ASP B 1 137 ? -9.50733  -12.37232 13.17042  1.000 33.72625 ?  135 ASP B CA  1 
ATOM   2363 C C   . ASP B 1 137 ? -10.11231 -11.05686 12.70977  1.000 31.43114 ?  135 ASP B C   1 
ATOM   2364 O O   . ASP B 1 137 ? -10.23689 -10.81932 11.50233  1.000 32.70991 ?  135 ASP B O   1 
ATOM   2365 C CB  . ASP B 1 137 ? -10.58890 -13.40922 13.45285  1.000 34.42698 ?  135 ASP B CB  1 
ATOM   2366 C CG  . ASP B 1 137 ? -10.08878 -14.82841 13.27494  1.000 41.16734 ?  135 ASP B CG  1 
ATOM   2367 O OD1 . ASP B 1 137 ? -10.84307 -15.77750 13.59597  1.000 46.67030 ?  135 ASP B OD1 1 
ATOM   2368 O OD2 . ASP B 1 137 ? -8.93807  -14.99642 12.79225  1.000 42.63037 -1 135 ASP B OD2 1 
ATOM   2369 N N   . PHE B 1 138 ? -10.48766 -10.18839 13.65340  1.000 28.52244 ?  136 PHE B N   1 
ATOM   2370 C CA  . PHE B 1 138 ? -11.05180 -8.89759  13.27582  1.000 30.06275 ?  136 PHE B CA  1 
ATOM   2371 C C   . PHE B 1 138 ? -10.00140 -7.98095  12.65678  1.000 29.34374 ?  136 PHE B C   1 
ATOM   2372 O O   . PHE B 1 138 ? -10.30035 -7.23141  11.72003  1.000 28.52397 ?  136 PHE B O   1 
ATOM   2373 C CB  . PHE B 1 138 ? -11.66061 -8.20339  14.48408  1.000 28.53837 ?  136 PHE B CB  1 
ATOM   2374 C CG  . PHE B 1 138 ? -11.88249 -6.72485  14.25947  1.000 30.41446 ?  136 PHE B CG  1 
ATOM   2375 C CD1 . PHE B 1 138 ? -12.90120 -6.29006  13.44245  1.000 28.50273 ?  136 PHE B CD1 1 
ATOM   2376 C CD2 . PHE B 1 138 ? -11.02882 -5.77722  14.82369  1.000 31.07251 ?  136 PHE B CD2 1 
ATOM   2377 C CE1 . PHE B 1 138 ? -13.10364 -4.94794  13.22397  1.000 28.20705 ?  136 PHE B CE1 1 
ATOM   2378 C CE2 . PHE B 1 138 ? -11.21459 -4.42792  14.59259  1.000 25.94549 ?  136 PHE B CE2 1 
ATOM   2379 C CZ  . PHE B 1 138 ? -12.26297 -4.01234  13.81716  1.000 24.68229 ?  136 PHE B CZ  1 
ATOM   2380 N N   . ASN B 1 139 ? -8.79122  -7.96581  13.21226  1.000 26.94762 ?  137 ASN B N   1 
ATOM   2381 C CA  . ASN B 1 139 ? -7.73234  -7.14028  12.62904  1.000 29.03215 ?  137 ASN B CA  1 
ATOM   2382 C C   . ASN B 1 139 ? -7.35884  -7.62662  11.24439  1.000 29.35809 ?  137 ASN B C   1 
ATOM   2383 O O   . ASN B 1 139 ? -7.01010  -6.82379  10.37335  1.000 26.52481 ?  137 ASN B O   1 
ATOM   2384 C CB  . ASN B 1 139 ? -6.50217  -7.14019  13.52196  1.000 28.84449 ?  137 ASN B CB  1 
ATOM   2385 C CG  . ASN B 1 139 ? -6.66591  -6.24283  14.71360  1.000 31.91362 ?  137 ASN B CG  1 
ATOM   2386 O OD1 . ASN B 1 139 ? -7.21775  -5.14582  14.60003  1.000 28.78904 ?  137 ASN B OD1 1 
ATOM   2387 N ND2 . ASN B 1 139 ? -6.21932  -6.70776  15.87589  1.000 33.33883 ?  137 ASN B ND2 1 
ATOM   2388 N N   . LYS B 1 140 ? -7.39232  -8.94231  11.03865  1.000 26.63638 ?  138 LYS B N   1 
ATOM   2389 C CA  . LYS B 1 140 ? -7.17209  -9.48990  9.70946   1.000 31.78603 ?  138 LYS B CA  1 
ATOM   2390 C C   . LYS B 1 140 ? -8.27225  -9.04400  8.75477   1.000 30.75381 ?  138 LYS B C   1 
ATOM   2391 O O   . LYS B 1 140 ? -8.00221  -8.62112  7.62381   1.000 29.08883 ?  138 LYS B O   1 
ATOM   2392 C CB  . LYS B 1 140 ? -7.08916  -11.01163 9.81718   1.000 31.71081 ?  138 LYS B CB  1 
ATOM   2393 C CG  . LYS B 1 140 ? -7.32154  -11.75819 8.52587   1.000 35.92273 ?  138 LYS B CG  1 
ATOM   2394 C CD  . LYS B 1 140 ? -7.62416  -13.21387 8.82910   1.000 39.14267 ?  138 LYS B CD  1 
ATOM   2395 C CE  . LYS B 1 140 ? -6.78580  -14.14838 7.96697   1.000 43.79807 ?  138 LYS B CE  1 
ATOM   2396 N NZ  . LYS B 1 140 ? -7.44162  -14.41583 6.65341   1.000 40.64389 ?  138 LYS B NZ  1 
ATOM   2397 N N   . TRP B 1 141 ? -9.52164  -9.09477  9.21764   1.000 30.68724 ?  139 TRP B N   1 
ATOM   2398 C CA  . TRP B 1 141 ? -10.64432 -8.59338  8.44025   1.000 28.18855 ?  139 TRP B CA  1 
ATOM   2399 C C   . TRP B 1 141 ? -10.47551 -7.11320  8.10691   1.000 26.89994 ?  139 TRP B C   1 
ATOM   2400 O O   . TRP B 1 141 ? -10.79027 -6.67710  6.99498   1.000 25.31801 ?  139 TRP B O   1 
ATOM   2401 C CB  . TRP B 1 141 ? -11.94236 -8.83720  9.22335   1.000 28.73032 ?  139 TRP B CB  1 
ATOM   2402 C CG  . TRP B 1 141 ? -13.15752 -8.28473  8.56500   1.000 25.94030 ?  139 TRP B CG  1 
ATOM   2403 C CD1 . TRP B 1 141 ? -14.01061 -8.94785  7.73188   1.000 28.59769 ?  139 TRP B CD1 1 
ATOM   2404 C CD2 . TRP B 1 141 ? -13.67967 -6.95193  8.69696   1.000 26.68590 ?  139 TRP B CD2 1 
ATOM   2405 N NE1 . TRP B 1 141 ? -15.00515 -8.10431  7.31178   1.000 21.50218 ?  139 TRP B NE1 1 
ATOM   2406 C CE2 . TRP B 1 141 ? -14.82293 -6.87235  7.88258   1.000 24.82063 ?  139 TRP B CE2 1 
ATOM   2407 C CE3 . TRP B 1 141 ? -13.27795 -5.81696  9.41124   1.000 26.15795 ?  139 TRP B CE3 1 
ATOM   2408 C CZ2 . TRP B 1 141 ? -15.57813 -5.70733  7.76601   1.000 28.25455 ?  139 TRP B CZ2 1 
ATOM   2409 C CZ3 . TRP B 1 141 ? -14.01938 -4.65784  9.28287   1.000 26.56278 ?  139 TRP B CZ3 1 
ATOM   2410 C CH2 . TRP B 1 141 ? -15.15376 -4.60977  8.46046   1.000 25.47915 ?  139 TRP B CH2 1 
ATOM   2411 N N   . LYS B 1 142 ? -9.95934  -6.32851  9.04639   1.000 26.44340 ?  140 LYS B N   1 
ATOM   2412 C CA  . LYS B 1 142 ? -9.89941  -4.88950  8.83250   1.000 26.23318 ?  140 LYS B CA  1 
ATOM   2413 C C   . LYS B 1 142 ? -8.82162  -4.53067  7.82211   1.000 28.53838 ?  140 LYS B C   1 
ATOM   2414 O O   . LYS B 1 142 ? -9.02109  -3.64054  6.98774   1.000 25.13558 ?  140 LYS B O   1 
ATOM   2415 C CB  . LYS B 1 142 ? -9.65307  -4.17654  10.15631  1.000 24.04948 ?  140 LYS B CB  1 
ATOM   2416 C CG  . LYS B 1 142 ? -9.48351  -2.69359  10.00453  1.000 25.34038 ?  140 LYS B CG  1 
ATOM   2417 C CD  . LYS B 1 142 ? -9.47025  -2.02515  11.35419  1.000 27.66428 ?  140 LYS B CD  1 
ATOM   2418 C CE  . LYS B 1 142 ? -8.27399  -2.46845  12.17435  1.000 25.00452 ?  140 LYS B CE  1 
ATOM   2419 N NZ  . LYS B 1 142 ? -8.00211  -1.36421  13.09725  1.000 26.33787 ?  140 LYS B NZ  1 
ATOM   2420 N N   . TYR B 1 143 ? -7.66906  -5.20785  7.88161   1.000 26.54206 ?  141 TYR B N   1 
ATOM   2421 C CA  . TYR B 1 143 ? -6.69478  -5.08112  6.80000   1.000 27.22212 ?  141 TYR B CA  1 
ATOM   2422 C C   . TYR B 1 143 ? -7.33283  -5.44116  5.45384   1.000 27.45401 ?  141 TYR B C   1 
ATOM   2423 O O   . TYR B 1 143 ? -7.20636  -4.70518  4.46575   1.000 24.04991 ?  141 TYR B O   1 
ATOM   2424 C CB  . TYR B 1 143 ? -5.47361  -5.96911  7.08153   1.000 24.87141 ?  141 TYR B CB  1 
ATOM   2425 C CG  . TYR B 1 143 ? -4.44685  -5.92868  5.95630   1.000 25.74620 ?  141 TYR B CG  1 
ATOM   2426 C CD1 . TYR B 1 143 ? -4.58249  -6.73653  4.81897   1.000 29.17421 ?  141 TYR B CD1 1 
ATOM   2427 C CD2 . TYR B 1 143 ? -3.35404  -5.07569  6.01855   1.000 27.01467 ?  141 TYR B CD2 1 
ATOM   2428 C CE1 . TYR B 1 143 ? -3.66384  -6.68322  3.76600   1.000 28.65256 ?  141 TYR B CE1 1 
ATOM   2429 C CE2 . TYR B 1 143 ? -2.41778  -5.02311  4.96715   1.000 28.55416 ?  141 TYR B CE2 1 
ATOM   2430 C CZ  . TYR B 1 143 ? -2.57662  -5.82222  3.86092   1.000 29.90617 ?  141 TYR B CZ  1 
ATOM   2431 O OH  . TYR B 1 143 ? -1.64934  -5.74785  2.83228   1.000 31.59814 ?  141 TYR B OH  1 
ATOM   2432 N N   . GLU B 1 144 ? -8.05456  -6.55364  5.40465   1.000 27.62890 ?  142 GLU B N   1 
ATOM   2433 C CA  . GLU B 1 144 ? -8.47348  -7.10231  4.11628   1.000 27.83011 ?  142 GLU B CA  1 
ATOM   2434 C C   . GLU B 1 144 ? -9.56136  -6.27044  3.44549   1.000 30.81919 ?  142 GLU B C   1 
ATOM   2435 O O   . GLU B 1 144 ? -9.54412  -6.11004  2.21430   1.000 32.42244 ?  142 GLU B O   1 
ATOM   2436 C CB  . GLU B 1 144 ? -8.91289  -8.55149  4.29274   1.000 29.40204 ?  142 GLU B CB  1 
ATOM   2437 C CG  . GLU B 1 144 ? -7.71594  -9.45021  4.51793   1.000 33.94650 ?  142 GLU B CG  1 
ATOM   2438 C CD  . GLU B 1 144 ? -8.09589  -10.88949 4.78514   1.000 41.39185 ?  142 GLU B CD  1 
ATOM   2439 O OE1 . GLU B 1 144 ? -9.30630  -11.15981 4.96737   1.000 42.22992 ?  142 GLU B OE1 1 
ATOM   2440 O OE2 . GLU B 1 144 ? -7.17083  -11.73399 4.86666   1.000 40.08257 -1 142 GLU B OE2 1 
ATOM   2441 N N   . ILE B 1 145 ? -10.50983 -5.72536  4.21245   1.000 29.26296 ?  143 ILE B N   1 
ATOM   2442 C CA  . ILE B 1 145 ? -11.51044 -4.85222  3.59882   1.000 27.59389 ?  143 ILE B CA  1 
ATOM   2443 C C   . ILE B 1 145 ? -10.84132 -3.60583  3.02283   1.000 30.03158 ?  143 ILE B C   1 
ATOM   2444 O O   . ILE B 1 145 ? -11.25012 -3.09355  1.97361   1.000 27.47631 ?  143 ILE B O   1 
ATOM   2445 C CB  . ILE B 1 145 ? -12.62542 -4.49700  4.59997   1.000 28.08004 ?  143 ILE B CB  1 
ATOM   2446 C CG1 . ILE B 1 145 ? -13.78457 -3.80962  3.87108   1.000 30.85312 ?  143 ILE B CG1 1 
ATOM   2447 C CG2 . ILE B 1 145 ? -12.10699 -3.61904  5.73475   1.000 30.43024 ?  143 ILE B CG2 1 
ATOM   2448 C CD1 . ILE B 1 145 ? -15.06109 -3.70089  4.68397   1.000 33.75188 ?  143 ILE B CD1 1 
ATOM   2449 N N   . PHE B 1 146 ? -9.80545  -3.10566  3.70330   1.000 27.77503 ?  144 PHE B N   1 
ATOM   2450 C CA  . PHE B 1 146 ? -9.01065  -1.98506  3.20048   1.000 29.58331 ?  144 PHE B CA  1 
ATOM   2451 C C   . PHE B 1 146 ? -8.28680  -2.36941  1.91711   1.000 31.23945 ?  144 PHE B C   1 
ATOM   2452 O O   . PHE B 1 146 ? -8.36653  -1.66076  0.90404   1.000 28.59865 ?  144 PHE B O   1 
ATOM   2453 C CB  . PHE B 1 146 ? -8.01868  -1.55943  4.29189   1.000 29.00218 ?  144 PHE B CB  1 
ATOM   2454 C CG  . PHE B 1 146 ? -7.26792  -0.28657  4.00269   1.000 27.31610 ?  144 PHE B CG  1 
ATOM   2455 C CD1 . PHE B 1 146 ? -7.93572  0.91484   3.84142   1.000 30.79517 ?  144 PHE B CD1 1 
ATOM   2456 C CD2 . PHE B 1 146 ? -5.88525  -0.29421  3.92715   1.000 29.06932 ?  144 PHE B CD2 1 
ATOM   2457 C CE1 . PHE B 1 146 ? -7.23989  2.08588   3.58797   1.000 29.77622 ?  144 PHE B CE1 1 
ATOM   2458 C CE2 . PHE B 1 146 ? -5.17052  0.87184   3.65935   1.000 31.72725 ?  144 PHE B CE2 1 
ATOM   2459 C CZ  . PHE B 1 146 ? -5.84502  2.06116   3.50638   1.000 32.38448 ?  144 PHE B CZ  1 
ATOM   2460 N N   . ALA B 1 147 ? -7.59128  -3.51219  1.93934   1.000 29.60587 ?  145 ALA B N   1 
ATOM   2461 C CA  . ALA B 1 147 ? -6.94565  -4.03427  0.73643   1.000 32.81753 ?  145 ALA B CA  1 
ATOM   2462 C C   . ALA B 1 147 ? -7.95067  -4.27141  -0.39510  1.000 35.15301 ?  145 ALA B C   1 
ATOM   2463 O O   . ALA B 1 147 ? -7.63645  -4.06268  -1.58007  1.000 33.20423 ?  145 ALA B O   1 
ATOM   2464 C CB  . ALA B 1 147 ? -6.20912  -5.33020  1.08848   1.000 33.20062 ?  145 ALA B CB  1 
ATOM   2465 N N   . GLU B 1 148 ? -9.16972  -4.70421  -0.06274  1.000 31.86285 ?  146 GLU B N   1 
ATOM   2466 C CA  . GLU B 1 148 ? -10.15126 -4.92786  -1.11839  1.000 32.45334 ?  146 GLU B CA  1 
ATOM   2467 C C   . GLU B 1 148 ? -10.49342 -3.63769  -1.85184  1.000 33.56020 ?  146 GLU B C   1 
ATOM   2468 O O   . GLU B 1 148 ? -10.62728 -3.63009  -3.08323  1.000 32.67969 ?  146 GLU B O   1 
ATOM   2469 C CB  . GLU B 1 148 ? -11.41742 -5.58937  -0.57544  1.000 35.27958 ?  146 GLU B CB  1 
ATOM   2470 C CG  . GLU B 1 148 ? -12.12304 -6.41570  -1.66652  1.000 41.52878 ?  146 GLU B CG  1 
ATOM   2471 C CD  . GLU B 1 148 ? -11.49911 -7.79817  -1.91755  1.000 48.04949 ?  146 GLU B CD  1 
ATOM   2472 O OE1 . GLU B 1 148 ? -10.25049 -7.93491  -1.84802  1.000 46.23486 ?  146 GLU B OE1 1 
ATOM   2473 O OE2 . GLU B 1 148 ? -12.25591 -8.72298  -2.30545  1.000 52.25315 -1 146 GLU B OE2 1 
ATOM   2474 N N   . TYR B 1 149 ? -10.63879 -2.53749  -1.12150  1.000 32.90177 ?  147 TYR B N   1 
ATOM   2475 C CA  . TYR B 1 149 ? -10.93094 -1.28035  -1.78651  1.000 36.06938 ?  147 TYR B CA  1 
ATOM   2476 C C   . TYR B 1 149 ? -9.69568  -0.71435  -2.46674  1.000 36.48028 ?  147 TYR B C   1 
ATOM   2477 O O   . TYR B 1 149 ? -9.83050  0.01528   -3.45257  1.000 38.32704 ?  147 TYR B O   1 
ATOM   2478 C CB  . TYR B 1 149 ? -11.52076 -0.26058  -0.79848  1.000 36.42654 ?  147 TYR B CB  1 
ATOM   2479 C CG  . TYR B 1 149 ? -12.99322 -0.46898  -0.48195  1.000 34.05620 ?  147 TYR B CG  1 
ATOM   2480 C CD1 . TYR B 1 149 ? -13.98587 -0.17489  -1.42613  1.000 39.52858 ?  147 TYR B CD1 1 
ATOM   2481 C CD2 . TYR B 1 149 ? -13.39837 -0.95906  0.74760   1.000 34.21792 ?  147 TYR B CD2 1 
ATOM   2482 C CE1 . TYR B 1 149 ? -15.32540 -0.37753  -1.14953  1.000 35.10165 ?  147 TYR B CE1 1 
ATOM   2483 C CE2 . TYR B 1 149 ? -14.73911 -1.15757  1.03510   1.000 32.60527 ?  147 TYR B CE2 1 
ATOM   2484 C CZ  . TYR B 1 149 ? -15.69607 -0.86353  0.08325   1.000 36.43628 ?  147 TYR B CZ  1 
ATOM   2485 O OH  . TYR B 1 149 ? -17.02717 -1.06689  0.37836   1.000 35.40752 ?  147 TYR B OH  1 
ATOM   2486 N N   . LEU B 1 150 ? -8.48533  -1.06534  -2.00760  1.000 35.71082 ?  148 LEU B N   1 
ATOM   2487 C CA  . LEU B 1 150 ? -7.29760  -0.32113  -2.43077  1.000 38.56343 ?  148 LEU B CA  1 
ATOM   2488 C C   . LEU B 1 150 ? -6.10634  -1.12338  -2.96573  1.000 41.80481 ?  148 LEU B C   1 
ATOM   2489 O O   . LEU B 1 150 ? -5.11064  -0.50265  -3.36700  1.000 39.48803 ?  148 LEU B O   1 
ATOM   2490 C CB  . LEU B 1 150 ? -6.80954  0.54953   -1.26859  1.000 34.72876 ?  148 LEU B CB  1 
ATOM   2491 C CG  . LEU B 1 150 ? -7.30468  1.99427   -1.17372  1.000 38.45207 ?  148 LEU B CG  1 
ATOM   2492 C CD1 . LEU B 1 150 ? -8.78725  2.11092   -1.16186  1.000 43.17915 ?  148 LEU B CD1 1 
ATOM   2493 C CD2 . LEU B 1 150 ? -6.79980  2.56729   0.11468   1.000 34.80128 ?  148 LEU B CD2 1 
ATOM   2494 N N   . ALA B 1 151 ? -6.16441  -2.46290  -3.01499  1.000 42.39019 ?  149 ALA B N   1 
ATOM   2495 C CA  . ALA B 1 151 ? -4.93866  -3.21127  -3.31896  1.000 42.73338 ?  149 ALA B CA  1 
ATOM   2496 C C   . ALA B 1 151 ? -4.49359  -3.08541  -4.77463  1.000 45.36765 ?  149 ALA B C   1 
ATOM   2497 O O   . ALA B 1 151 ? -3.37814  -3.50727  -5.10178  1.000 44.67759 ?  149 ALA B O   1 
ATOM   2498 C CB  . ALA B 1 151 ? -5.08654  -4.69144  -2.93500  1.000 38.91890 ?  149 ALA B CB  1 
ATOM   2499 N N   . GLU B 1 152 ? -5.29398  -2.48945  -5.64981  1.000 42.86040 ?  150 GLU B N   1 
ATOM   2500 C CA  . GLU B 1 152 ? -4.78765  -2.20510  -6.98516  1.000 45.78950 ?  150 GLU B CA  1 
ATOM   2501 C C   . GLU B 1 152 ? -4.19154  -0.81337  -7.10913  1.000 43.98725 ?  150 GLU B C   1 
ATOM   2502 O O   . GLU B 1 152 ? -3.46559  -0.55518  -8.07464  1.000 48.46146 ?  150 GLU B O   1 
ATOM   2503 C CB  . GLU B 1 152 ? -5.87554  -2.39629  -8.04382  1.000 47.71067 ?  150 GLU B CB  1 
ATOM   2504 C CG  . GLU B 1 152 ? -6.51002  -3.77227  -8.04883  1.000 49.33458 ?  150 GLU B CG  1 
ATOM   2505 C CD  . GLU B 1 152 ? -5.71383  -4.72913  -8.91790  1.000 50.12408 ?  150 GLU B CD  1 
ATOM   2506 O OE1 . GLU B 1 152 ? -4.68935  -5.26370  -8.43810  1.000 49.01632 ?  150 GLU B OE1 1 
ATOM   2507 O OE2 . GLU B 1 152 ? -6.07433  -4.91690  -10.09619 1.000 52.40652 -1 150 GLU B OE2 1 
ATOM   2508 N N   . GLU B 1 153 ? -4.46154  0.07108   -6.15139  1.000 42.54342 ?  151 GLU B N   1 
ATOM   2509 C CA  . GLU B 1 153 ? -3.88622  1.40923   -6.11063  1.000 43.08877 ?  151 GLU B CA  1 
ATOM   2510 C C   . GLU B 1 153 ? -2.71859  1.53499   -5.14071  1.000 43.45988 ?  151 GLU B C   1 
ATOM   2511 O O   . GLU B 1 153 ? -1.94834  2.49320   -5.24854  1.000 42.80234 ?  151 GLU B O   1 
ATOM   2512 C CB  . GLU B 1 153 ? -4.95672  2.43296   -5.70951  1.000 42.81171 ?  151 GLU B CB  1 
ATOM   2513 C CG  . GLU B 1 153 ? -5.98137  2.75214   -6.77079  1.000 48.83805 ?  151 GLU B CG  1 
ATOM   2514 C CD  . GLU B 1 153 ? -5.36719  3.43521   -7.98734  1.000 51.02230 ?  151 GLU B CD  1 
ATOM   2515 O OE1 . GLU B 1 153 ? -4.84323  2.72183   -8.86961  1.000 52.09943 ?  151 GLU B OE1 1 
ATOM   2516 O OE2 . GLU B 1 153 ? -5.41051  4.68554   -8.05996  1.000 54.59312 -1 151 GLU B OE2 1 
ATOM   2517 N N   . ILE B 1 154 ? -2.57600  0.60970   -4.19394  1.000 39.78761 ?  152 ILE B N   1 
ATOM   2518 C CA  . ILE B 1 154 ? -1.55636  0.71316   -3.15620  1.000 37.94638 ?  152 ILE B CA  1 
ATOM   2519 C C   . ILE B 1 154 ? -0.87526  -0.64004  -3.04513  1.000 37.14910 ?  152 ILE B C   1 
ATOM   2520 O O   . ILE B 1 154 ? -1.54713  -1.64406  -2.79429  1.000 38.13165 ?  152 ILE B O   1 
ATOM   2521 C CB  . ILE B 1 154 ? -2.14993  1.10226   -1.79843  1.000 39.74985 ?  152 ILE B CB  1 
ATOM   2522 C CG1 . ILE B 1 154 ? -2.50787  2.56945   -1.76188  1.000 41.10875 ?  152 ILE B CG1 1 
ATOM   2523 C CG2 . ILE B 1 154 ? -1.10783  0.96411   -0.70001  1.000 35.15144 ?  152 ILE B CG2 1 
ATOM   2524 C CD1 . ILE B 1 154 ? -3.52670  2.86660   -0.73138  1.000 42.08934 ?  152 ILE B CD1 1 
ATOM   2525 N N   . ASN B 1 155 ? 0.44652   -0.67490  -3.20988  1.000 35.61784 ?  153 ASN B N   1 
ATOM   2526 C CA  . ASN B 1 155 ? 1.16050   -1.93759  -3.09036  1.000 34.22603 ?  153 ASN B CA  1 
ATOM   2527 C C   . ASN B 1 155 ? 1.12571   -2.46366  -1.65600  1.000 35.39685 ?  153 ASN B C   1 
ATOM   2528 O O   . ASN B 1 155 ? 0.81432   -1.74215  -0.70550  1.000 33.15206 ?  153 ASN B O   1 
ATOM   2529 C CB  . ASN B 1 155 ? 2.60504   -1.80529  -3.59759  1.000 35.03581 ?  153 ASN B CB  1 
ATOM   2530 C CG  . ASN B 1 155 ? 3.44643   -0.79163  -2.83037  1.000 36.02751 ?  153 ASN B CG  1 
ATOM   2531 O OD1 . ASN B 1 155 ? 3.07075   -0.30124  -1.77914  1.000 38.66636 ?  153 ASN B OD1 1 
ATOM   2532 N ND2 . ASN B 1 155 ? 4.59976   -0.45924  -3.39002  1.000 41.90731 ?  153 ASN B ND2 1 
ATOM   2533 N N   . ASN B 1 156 ? 1.44971   -3.75589  -1.51640  1.000 31.66973 ?  154 ASN B N   1 
ATOM   2534 C CA  . ASN B 1 156 ? 1.30894   -4.44039  -0.23452  1.000 33.35807 ?  154 ASN B CA  1 
ATOM   2535 C C   . ASN B 1 156 ? 2.11195   -3.75543  0.86694   1.000 32.45808 ?  154 ASN B C   1 
ATOM   2536 O O   . ASN B 1 156 ? 1.64950   -3.66854  2.00511   1.000 28.23170 ?  154 ASN B O   1 
ATOM   2537 C CB  . ASN B 1 156 ? 1.73971   -5.90549  -0.34895  1.000 33.67837 ?  154 ASN B CB  1 
ATOM   2538 C CG  . ASN B 1 156 ? 0.79605   -6.73858  -1.18789  1.000 36.41036 ?  154 ASN B CG  1 
ATOM   2539 O OD1 . ASN B 1 156 ? -0.37981  -6.42697  -1.30128  1.000 41.26866 ?  154 ASN B OD1 1 
ATOM   2540 N ND2 . ASN B 1 156 ? 1.31380   -7.81477  -1.78301  1.000 36.08858 ?  154 ASN B ND2 1 
ATOM   2541 N N   . ALA B 1 157 ? 3.30997   -3.25845  0.55215   1.000 31.31903 ?  155 ALA B N   1 
ATOM   2542 C CA  . ALA B 1 157 ? 4.15958   -2.70392  1.60576   1.000 28.30055 ?  155 ALA B CA  1 
ATOM   2543 C C   . ALA B 1 157 ? 3.51952   -1.48381  2.24255   1.000 29.32574 ?  155 ALA B C   1 
ATOM   2544 O O   . ALA B 1 157 ? 3.51204   -1.33873  3.47571   1.000 26.91089 ?  155 ALA B O   1 
ATOM   2545 C CB  . ALA B 1 157 ? 5.53781   -2.35193  1.04055   1.000 32.02672 ?  155 ALA B CB  1 
ATOM   2546 N N   . ARG B 1 158 ? 2.98658   -0.59779  1.41352   1.000 26.34504 ?  156 ARG B N   1 
ATOM   2547 C CA  . ARG B 1 158 ? 2.34441   0.61443   1.89826   1.000 30.33517 ?  156 ARG B CA  1 
ATOM   2548 C C   . ARG B 1 158 ? 1.03474   0.30457   2.59303   1.000 27.35482 ?  156 ARG B C   1 
ATOM   2549 O O   . ARG B 1 158 ? 0.71432   0.92922   3.61055   1.000 26.00376 ?  156 ARG B O   1 
ATOM   2550 C CB  . ARG B 1 158 ? 2.16549   1.58743   0.72633   1.000 29.65644 ?  156 ARG B CB  1 
ATOM   2551 C CG  . ARG B 1 158 ? 3.40543   2.46171   0.65828   1.000 36.46738 ?  156 ARG B CG  1 
ATOM   2552 C CD  . ARG B 1 158 ? 3.55230   3.47040   -0.47030  1.000 41.52376 ?  156 ARG B CD  1 
ATOM   2553 N NE  . ARG B 1 158 ? 4.21390   2.85281   -1.61377  1.000 49.03759 ?  156 ARG B NE  1 
ATOM   2554 C CZ  . ARG B 1 158 ? 4.99899   3.50687   -2.45485  1.000 47.55143 ?  156 ARG B CZ  1 
ATOM   2555 N NH1 . ARG B 1 158 ? 5.28965   4.78522   -2.27056  1.000 53.72548 ?  156 ARG B NH1 1 
ATOM   2556 N NH2 . ARG B 1 158 ? 5.52318   2.85949   -3.49409  1.000 49.95157 ?  156 ARG B NH2 1 
ATOM   2557 N N   . LEU B 1 159 ? 0.29069   -0.69050  2.10106   1.000 26.41592 ?  157 LEU B N   1 
ATOM   2558 C CA  . LEU B 1 159 ? -0.89468  -1.15462  2.83249   1.000 27.73181 ?  157 LEU B CA  1 
ATOM   2559 C C   . LEU B 1 159 ? -0.53292  -1.57884  4.25252   1.000 26.90555 ?  157 LEU B C   1 
ATOM   2560 O O   . LEU B 1 159 ? -1.21556  -1.21519  5.22839   1.000 23.06668 ?  157 LEU B O   1 
ATOM   2561 C CB  . LEU B 1 159 ? -1.53759  -2.32424  2.09204   1.000 29.36130 ?  157 LEU B CB  1 
ATOM   2562 C CG  . LEU B 1 159 ? -2.38196  -2.06322  0.84912   1.000 30.38381 ?  157 LEU B CG  1 
ATOM   2563 C CD1 . LEU B 1 159 ? -2.92214  -3.37968  0.30416   1.000 34.48771 ?  157 LEU B CD1 1 
ATOM   2564 C CD2 . LEU B 1 159 ? -3.52156  -1.11077  1.13294   1.000 30.77424 ?  157 LEU B CD2 1 
ATOM   2565 N N   . ARG B 1 160 ? 0.53122   -2.37554  4.38778   1.000 26.14032 ?  158 ARG B N   1 
ATOM   2566 C CA  . ARG B 1 160 ? 0.92406   -2.84839  5.71218   1.000 26.55269 ?  158 ARG B CA  1 
ATOM   2567 C C   . ARG B 1 160 ? 1.34865   -1.68966  6.60695   1.000 25.05887 ?  158 ARG B C   1 
ATOM   2568 O O   . ARG B 1 160 ? 0.98173   -1.64570  7.79172   1.000 24.04730 ?  158 ARG B O   1 
ATOM   2569 C CB  . ARG B 1 160 ? 2.02775   -3.89024  5.58567   1.000 25.97615 ?  158 ARG B CB  1 
ATOM   2570 C CG  . ARG B 1 160 ? 1.50248   -5.26413  5.20704   1.000 27.75033 ?  158 ARG B CG  1 
ATOM   2571 C CD  . ARG B 1 160 ? 2.57609   -6.35051  5.18234   1.000 29.68378 ?  158 ARG B CD  1 
ATOM   2572 N NE  . ARG B 1 160 ? 3.62151   -6.10581  4.19115   1.000 33.82115 ?  158 ARG B NE  1 
ATOM   2573 C CZ  . ARG B 1 160 ? 3.72580   -6.74040  3.02519   1.000 34.65384 ?  158 ARG B CZ  1 
ATOM   2574 N NH1 . ARG B 1 160 ? 2.85945   -7.66985  2.66580   1.000 35.55102 ?  158 ARG B NH1 1 
ATOM   2575 N NH2 . ARG B 1 160 ? 4.73874   -6.44414  2.20301   1.000 31.65061 ?  158 ARG B NH2 1 
ATOM   2576 N N   . ILE B 1 161 ? 2.08503   -0.72626  6.05471   1.000 25.94740 ?  159 ILE B N   1 
ATOM   2577 C CA  . ILE B 1 161 ? 2.51526   0.42478   6.84770   1.000 24.19091 ?  159 ILE B CA  1 
ATOM   2578 C C   . ILE B 1 161 ? 1.31215   1.25768   7.27741   1.000 24.92084 ?  159 ILE B C   1 
ATOM   2579 O O   . ILE B 1 161 ? 1.20074   1.65895   8.44063   1.000 27.09319 ?  159 ILE B O   1 
ATOM   2580 C CB  . ILE B 1 161 ? 3.53187   1.26309   6.06382   1.000 23.18632 ?  159 ILE B CB  1 
ATOM   2581 C CG1 . ILE B 1 161 ? 4.87465   0.56169   6.06492   1.000 29.87240 ?  159 ILE B CG1 1 
ATOM   2582 C CG2 . ILE B 1 161 ? 3.72466   2.66625   6.66611   1.000 24.39514 ?  159 ILE B CG2 1 
ATOM   2583 C CD1 . ILE B 1 161 ? 5.74344   1.01036   4.91698   1.000 31.96382 ?  159 ILE B CD1 1 
ATOM   2584 N N   . ILE B 1 162 ? 0.39380   1.53043   6.35233   1.000 24.04745 ?  160 ILE B N   1 
ATOM   2585 C CA  . ILE B 1 162 ? -0.72952  2.41647   6.66864   1.000 23.15039 ?  160 ILE B CA  1 
ATOM   2586 C C   . ILE B 1 162 ? -1.63407  1.78214   7.71647   1.000 24.09013 ?  160 ILE B C   1 
ATOM   2587 O O   . ILE B 1 162 ? -2.08814  2.45190   8.66093   1.000 21.80047 ?  160 ILE B O   1 
ATOM   2588 C CB  . ILE B 1 162 ? -1.51009  2.76548   5.38124   1.000 26.06502 ?  160 ILE B CB  1 
ATOM   2589 C CG1 . ILE B 1 162 ? -0.73259  3.72823   4.50383   1.000 25.34403 ?  160 ILE B CG1 1 
ATOM   2590 C CG2 . ILE B 1 162 ? -2.89803  3.36760   5.71064   1.000 26.06961 ?  160 ILE B CG2 1 
ATOM   2591 C CD1 . ILE B 1 162 ? -1.27868  3.82447   3.07165   1.000 31.02610 ?  160 ILE B CD1 1 
ATOM   2592 N N   . VAL B 1 163 ? -1.93659  0.48617   7.56419   1.000 23.45727 ?  161 VAL B N   1 
ATOM   2593 C CA  . VAL B 1 163 ? -2.83469  -0.16506  8.51206   1.000 23.19642 ?  161 VAL B CA  1 
ATOM   2594 C C   . VAL B 1 163 ? -2.18722  -0.24643  9.88661   1.000 25.13593 ?  161 VAL B C   1 
ATOM   2595 O O   . VAL B 1 163 ? -2.84777  -0.07461  10.91964  1.000 24.78300 ?  161 VAL B O   1 
ATOM   2596 C CB  . VAL B 1 163 ? -3.24864  -1.56039  8.00199   1.000 23.00386 ?  161 VAL B CB  1 
ATOM   2597 C CG1 . VAL B 1 163 ? -3.97168  -2.31084  9.08750   1.000 25.68319 ?  161 VAL B CG1 1 
ATOM   2598 C CG2 . VAL B 1 163 ? -4.17323  -1.44426  6.78320   1.000 24.49851 ?  161 VAL B CG2 1 
ATOM   2599 N N   . SER B 1 164 ? -0.88206  -0.49673  9.92848   1.000 22.62865 ?  162 SER B N   1 
ATOM   2600 C CA  . SER B 1 164 ? -0.21137  -0.53398  11.22174  1.000 21.55992 ?  162 SER B CA  1 
ATOM   2601 C C   . SER B 1 164 ? -0.09270  0.86131   11.81881  1.000 22.91746 ?  162 SER B C   1 
ATOM   2602 O O   . SER B 1 164 ? -0.18947  1.01788   13.03859  1.000 21.90053 ?  162 SER B O   1 
ATOM   2603 C CB  . SER B 1 164 ? 1.15286   -1.20261  11.07610  1.000 23.80512 ?  162 SER B CB  1 
ATOM   2604 O OG  . SER B 1 164 ? 1.81700   -1.37701  12.32538  1.000 25.22121 ?  162 SER B OG  1 
ATOM   2605 N N   . ALA B 1 165 ? 0.07554   1.89039   10.98642  1.000 22.57104 ?  163 ALA B N   1 
ATOM   2606 C CA  . ALA B 1 165 ? 0.06667   3.24900   11.52002  1.000 21.05422 ?  163 ALA B CA  1 
ATOM   2607 C C   . ALA B 1 165 ? -1.30858  3.62084   12.06538  1.000 24.06384 ?  163 ALA B C   1 
ATOM   2608 O O   . ALA B 1 165 ? -1.41179  4.32343   13.07881  1.000 22.61234 ?  163 ALA B O   1 
ATOM   2609 C CB  . ALA B 1 165 ? 0.49160   4.24385   10.44793  1.000 19.10770 ?  163 ALA B CB  1 
ATOM   2610 N N   . MET B 1 166 ? -2.38531  3.19218   11.39600  1.000 23.99664 ?  164 MET B N   1 
ATOM   2611 C CA  . MET B 1 166 ? -3.69725  3.39677   12.00156  1.000 22.73041 ?  164 MET B CA  1 
ATOM   2612 C C   . MET B 1 166 ? -3.88899  2.58624   13.26569  1.000 23.73308 ?  164 MET B C   1 
ATOM   2613 O O   . MET B 1 166 ? -4.55111  3.05267   14.20135  1.000 23.53052 ?  164 MET B O   1 
ATOM   2614 C CB  . MET B 1 166 ? -4.84626  3.13152   11.03703  1.000 21.25791 ?  164 MET B CB  1 
ATOM   2615 C CG  . MET B 1 166 ? -4.80340  3.72119   9.67801   1.000 25.68642 ?  164 MET B CG  1 
ATOM   2616 S SD  . MET B 1 166 ? -4.97455  5.53567   9.84475   1.000 28.36669 ?  164 MET B SD  1 
ATOM   2617 C CE  . MET B 1 166 ? -3.29279  6.15009   10.12694  1.000 27.20902 ?  164 MET B CE  1 
ATOM   2618 N N   . ASN B 1 167 ? -3.34904  1.37128   13.33189  1.000 23.94638 ?  165 ASN B N   1 
ATOM   2619 C CA  . ASN B 1 167 ? -3.45932  0.66785   14.60990  1.000 25.21064 ?  165 ASN B CA  1 
ATOM   2620 C C   . ASN B 1 167 ? -2.63556  1.34252   15.70836  1.000 24.53878 ?  165 ASN B C   1 
ATOM   2621 O O   . ASN B 1 167 ? -2.98929  1.23762   16.88188  1.000 25.02578 ?  165 ASN B O   1 
ATOM   2622 C CB  . ASN B 1 167 ? -3.07382  -0.80246  14.45545  1.000 23.31226 ?  165 ASN B CB  1 
ATOM   2623 C CG  . ASN B 1 167 ? -4.20962  -1.62517  13.90150  1.000 27.73360 ?  165 ASN B CG  1 
ATOM   2624 O OD1 . ASN B 1 167 ? -5.38684  -1.35418  14.18572  1.000 30.26186 ?  165 ASN B OD1 1 
ATOM   2625 N ND2 . ASN B 1 167 ? -3.88150  -2.62244  13.09809  1.000 28.10975 ?  165 ASN B ND2 1 
ATOM   2626 N N   . GLY B 1 168 ? -1.56577  2.06103   15.36569  1.000 26.26478 ?  166 GLY B N   1 
ATOM   2627 C CA  . GLY B 1 168 ? -0.81667  2.76336   16.40236  1.000 24.47187 ?  166 GLY B CA  1 
ATOM   2628 C C   . GLY B 1 168 ? -1.59101  3.91816   16.99562  1.000 27.93414 ?  166 GLY B C   1 
ATOM   2629 O O   . GLY B 1 168 ? -1.45137  4.22767   18.18353  1.000 28.15385 ?  166 GLY B O   1 
ATOM   2630 N N   . ILE B 1 169 ? -2.42465  4.56537   16.18677  1.000 25.15632 ?  167 ILE B N   1 
ATOM   2631 C CA  . ILE B 1 169 ? -3.33877  5.57761   16.70388  1.000 25.75935 ?  167 ILE B CA  1 
ATOM   2632 C C   . ILE B 1 169 ? -4.20759  5.02064   17.83360  1.000 28.02535 ?  167 ILE B C   1 
ATOM   2633 O O   . ILE B 1 169 ? -4.59610  5.75508   18.75256  1.000 25.91870 ?  167 ILE B O   1 
ATOM   2634 C CB  . ILE B 1 169 ? -4.17134  6.13107   15.52858  1.000 27.58249 ?  167 ILE B CB  1 
ATOM   2635 C CG1 . ILE B 1 169 ? -3.25768  6.94087   14.59134  1.000 23.81249 ?  167 ILE B CG1 1 
ATOM   2636 C CG2 . ILE B 1 169 ? -5.33537  6.99114   15.98993  1.000 29.19606 ?  167 ILE B CG2 1 
ATOM   2637 C CD1 . ILE B 1 169 ? -4.00282  7.55941   13.45490  1.000 27.27872 ?  167 ILE B CD1 1 
ATOM   2638 N N   . LEU B 1 170 ? -4.52251  3.72706   17.79629  1.000 24.67468 ?  168 LEU B N   1 
ATOM   2639 C CA  . LEU B 1 170 ? -5.38050  3.13690   18.82381  1.000 28.44098 ?  168 LEU B CA  1 
ATOM   2640 C C   . LEU B 1 170 ? -4.62097  2.71971   20.08175  1.000 29.20310 ?  168 LEU B C   1 
ATOM   2641 O O   . LEU B 1 170 ? -5.25092  2.33416   21.06793  1.000 28.06042 ?  168 LEU B O   1 
ATOM   2642 C CB  . LEU B 1 170 ? -6.13163  1.92375   18.27277  1.000 25.71548 ?  168 LEU B CB  1 
ATOM   2643 C CG  . LEU B 1 170 ? -6.99123  2.09826   17.01294  1.000 27.14183 ?  168 LEU B CG  1 
ATOM   2644 C CD1 . LEU B 1 170 ? -7.46121  0.74309   16.53152  1.000 23.90839 ?  168 LEU B CD1 1 
ATOM   2645 C CD2 . LEU B 1 170 ? -8.17740  2.98099   17.29407  1.000 30.33539 ?  168 LEU B CD2 1 
ATOM   2646 N N   . LEU B 1 171 ? -3.29944  2.74736   20.07516  1.000 30.40502 ?  169 LEU B N   1 
ATOM   2647 C CA  . LEU B 1 171 ? -2.56874  2.46785   21.29931  1.000 30.07853 ?  169 LEU B CA  1 
ATOM   2648 C C   . LEU B 1 171 ? -2.91469  3.54463   22.32015  1.000 31.61267 ?  169 LEU B C   1 
ATOM   2649 O O   . LEU B 1 171 ? -3.03076  4.72535   21.95588  1.000 32.38207 ?  169 LEU B O   1 
ATOM   2650 C CB  . LEU B 1 171 ? -1.06623  2.41797   21.02024  1.000 31.65074 ?  169 LEU B CB  1 
ATOM   2651 C CG  . LEU B 1 171 ? -0.17485  1.62032   21.98102  1.000 34.55730 ?  169 LEU B CG  1 
ATOM   2652 C CD1 . LEU B 1 171 ? -0.46699  0.11184   21.91785  1.000 32.23443 ?  169 LEU B CD1 1 
ATOM   2653 C CD2 . LEU B 1 171 ? 1.29355   1.92168   21.68692  1.000 30.47774 ?  169 LEU B CD2 1 
ATOM   2654 N N   . PRO B 1 172 ? -3.21890  3.17793   23.55693  1.000 32.41965 ?  170 PRO B N   1 
ATOM   2655 C CA  . PRO B 1 172 ? -3.51040  4.20919   24.55375  1.000 34.20861 ?  170 PRO B CA  1 
ATOM   2656 C C   . PRO B 1 172 ? -2.26904  5.04408   24.81589  1.000 29.06631 ?  170 PRO B C   1 
ATOM   2657 O O   . PRO B 1 172 ? -1.13477  4.57883   24.66447  1.000 34.86028 ?  170 PRO B O   1 
ATOM   2658 C CB  . PRO B 1 172 ? -3.95033  3.41138   25.79069  1.000 34.20702 ?  170 PRO B CB  1 
ATOM   2659 C CG  . PRO B 1 172 ? -3.43560  2.01672   25.56798  1.000 35.35432 ?  170 PRO B CG  1 
ATOM   2660 C CD  . PRO B 1 172 ? -3.43646  1.81592   24.07123  1.000 30.90894 ?  170 PRO B CD  1 
ATOM   2661 N N   . ALA B 1 173 ? -2.50748  6.31469   25.14226  1.000 26.00919 ?  171 ALA B N   1 
ATOM   2662 C CA  . ALA B 1 173 ? -1.47575  7.32784   25.34202  1.000 36.45077 ?  171 ALA B CA  1 
ATOM   2663 C C   . ALA B 1 173 ? -0.59560  7.52911   24.09843  1.000 32.64220 ?  171 ALA B C   1 
ATOM   2664 O O   . ALA B 1 173 ? 0.51715   8.02887   24.20947  1.000 29.86541 ?  171 ALA B O   1 
ATOM   2665 C CB  . ALA B 1 173 ? -0.62546  7.00380   26.57739  1.000 29.02065 ?  171 ALA B CB  1 
ATOM   2666 N N   . SER B 1 174 ? -1.08557  7.16325   22.90519  1.000 34.58806 ?  172 SER B N   1 
ATOM   2667 C CA  . SER B 1 174 ? -0.35345  7.44572   21.67334  1.000 34.10614 ?  172 SER B CA  1 
ATOM   2668 C C   . SER B 1 174 ? -0.24191  8.95189   21.47978  1.000 36.17817 ?  172 SER B C   1 
ATOM   2669 O O   . SER B 1 174 ? -1.15710  9.70825   21.82425  1.000 37.22740 ?  172 SER B O   1 
ATOM   2670 C CB  . SER B 1 174 ? -1.05808  6.81058   20.45941  1.000 35.33240 ?  172 SER B CB  1 
ATOM   2671 O OG  . SER B 1 174 ? -2.41738  7.27710   20.32192  1.000 38.10430 ?  172 SER B OG  1 
ATOM   2672 N N   . THR B 1 175 ? 0.87844   9.39455   20.91855  1.000 35.08617 ?  173 THR B N   1 
ATOM   2673 C CA  . THR B 1 175 ? 1.10393   10.82083  20.71902  1.000 36.02081 ?  173 THR B CA  1 
ATOM   2674 C C   . THR B 1 175 ? 1.79049   11.01602  19.36358  1.000 33.17398 ?  173 THR B C   1 
ATOM   2675 O O   . THR B 1 175 ? 2.12772   10.05191  18.67616  1.000 29.37433 ?  173 THR B O   1 
ATOM   2676 C CB  . THR B 1 175 ? 1.92338   11.39214  21.88550  1.000 35.90814 ?  173 THR B CB  1 
ATOM   2677 O OG1 . THR B 1 175 ? 2.09513   12.80665  21.71005  1.000 43.89622 ?  173 THR B OG1 1 
ATOM   2678 C CG2 . THR B 1 175 ? 3.30127   10.71441  21.92871  1.000 34.19399 ?  173 THR B CG2 1 
ATOM   2679 N N   . TYR B 1 176 ? 1.98560   12.27315  18.97241  1.000 32.07385 ?  174 TYR B N   1 
ATOM   2680 C CA  . TYR B 1 176 ? 2.58056   12.61740  17.68089  1.000 32.62015 ?  174 TYR B CA  1 
ATOM   2681 C C   . TYR B 1 176 ? 1.88052   11.88321  16.53650  1.000 32.84151 ?  174 TYR B C   1 
ATOM   2682 O O   . TYR B 1 176 ? 2.51082   11.29564  15.64837  1.000 30.86242 ?  174 TYR B O   1 
ATOM   2683 C CB  . TYR B 1 176 ? 4.07733   12.33035  17.66930  1.000 34.11213 ?  174 TYR B CB  1 
ATOM   2684 C CG  . TYR B 1 176 ? 4.90302   13.35531  18.37227  1.000 35.28866 ?  174 TYR B CG  1 
ATOM   2685 C CD1 . TYR B 1 176 ? 5.12072   14.61078  17.80607  1.000 36.75594 ?  174 TYR B CD1 1 
ATOM   2686 C CD2 . TYR B 1 176 ? 5.49612   13.07057  19.59685  1.000 33.62280 ?  174 TYR B CD2 1 
ATOM   2687 C CE1 . TYR B 1 176 ? 5.90169   15.55717  18.45026  1.000 35.83873 ?  174 TYR B CE1 1 
ATOM   2688 C CE2 . TYR B 1 176 ? 6.27639   14.00405  20.24018  1.000 33.37340 ?  174 TYR B CE2 1 
ATOM   2689 C CZ  . TYR B 1 176 ? 6.47959   15.24061  19.67122  1.000 35.80991 ?  174 TYR B CZ  1 
ATOM   2690 O OH  . TYR B 1 176 ? 7.25451   16.16957  20.33775  1.000 41.70787 ?  174 TYR B OH  1 
ATOM   2691 N N   . LEU B 1 177 ? 0.55561   11.93802  16.55840  1.000 29.94393 ?  175 LEU B N   1 
ATOM   2692 C CA  . LEU B 1 177 ? -0.23446  11.13313  15.63660  1.000 32.28732 ?  175 LEU B CA  1 
ATOM   2693 C C   . LEU B 1 177 ? -0.04140  11.56697  14.18515  1.000 26.95730 ?  175 LEU B C   1 
ATOM   2694 O O   . LEU B 1 177 ? -0.01095  12.76226  13.88553  1.000 28.07728 ?  175 LEU B O   1 
ATOM   2695 C CB  . LEU B 1 177 ? -1.70993  11.22220  15.99469  1.000 30.78351 ?  175 LEU B CB  1 
ATOM   2696 C CG  . LEU B 1 177 ? -2.01572  10.49233  17.30493  1.000 34.45700 ?  175 LEU B CG  1 
ATOM   2697 C CD1 . LEU B 1 177 ? -3.53869  10.40232  17.52382  1.000 37.14904 ?  175 LEU B CD1 1 
ATOM   2698 C CD2 . LEU B 1 177 ? -1.36983  9.12702   17.32608  1.000 31.02771 ?  175 LEU B CD2 1 
ATOM   2699 N N   . PRO B 1 178 ? 0.04609   10.62121  13.26046  1.000 26.12468 ?  176 PRO B N   1 
ATOM   2700 C CA  . PRO B 1 178 ? 0.04402   10.99067  11.84309  1.000 31.80258 ?  176 PRO B CA  1 
ATOM   2701 C C   . PRO B 1 178 ? -1.25802  11.69327  11.48597  1.000 31.15226 ?  176 PRO B C   1 
ATOM   2702 O O   . PRO B 1 178 ? -2.32474  11.35074  11.99895  1.000 33.24411 ?  176 PRO B O   1 
ATOM   2703 C CB  . PRO B 1 178 ? 0.18676   9.64401   11.12382  1.000 31.69459 ?  176 PRO B CB  1 
ATOM   2704 C CG  . PRO B 1 178 ? -0.29236  8.63523   12.08859  1.000 30.63351 ?  176 PRO B CG  1 
ATOM   2705 C CD  . PRO B 1 178 ? -0.04471  9.16838   13.46536  1.000 27.84893 ?  176 PRO B CD  1 
ATOM   2706 N N   . THR B 1 179 ? -1.15216  12.72554  10.65247  1.000 32.96346 ?  177 THR B N   1 
ATOM   2707 C CA  . THR B 1 179 ? -2.29492  13.50500  10.21079  1.000 35.45718 ?  177 THR B CA  1 
ATOM   2708 C C   . THR B 1 179 ? -2.79689  12.95080  8.89606   1.000 33.85252 ?  177 THR B C   1 
ATOM   2709 O O   . THR B 1 179 ? -2.13742  12.14815  8.23229   1.000 31.95446 ?  177 THR B O   1 
ATOM   2710 C CB  . THR B 1 179 ? -1.93788  14.96996  9.98512   1.000 37.11301 ?  177 THR B CB  1 
ATOM   2711 O OG1 . THR B 1 179 ? -0.87985  15.03954  9.02734   1.000 36.13442 ?  177 THR B OG1 1 
ATOM   2712 C CG2 . THR B 1 179 ? -1.46330  15.59242  11.27579  1.000 38.89727 ?  177 THR B CG2 1 
ATOM   2713 N N   . TRP B 1 180 ? -3.97424  13.42430  8.50066   1.000 34.62720 ?  178 TRP B N   1 
ATOM   2714 C CA  . TRP B 1 180 ? -4.47625  13.05573  7.18922   1.000 33.14488 ?  178 TRP B CA  1 
ATOM   2715 C C   . TRP B 1 180 ? -3.50896  13.50518  6.09795   1.000 33.08851 ?  178 TRP B C   1 
ATOM   2716 O O   . TRP B 1 180 ? -3.21200  12.74723  5.16892   1.000 30.30075 ?  178 TRP B O   1 
ATOM   2717 C CB  . TRP B 1 180 ? -5.85441  13.65746  6.95241   1.000 32.42308 ?  178 TRP B CB  1 
ATOM   2718 C CG  . TRP B 1 180 ? -6.17580  13.69206  5.51020   1.000 30.22769 ?  178 TRP B CG  1 
ATOM   2719 C CD1 . TRP B 1 180 ? -6.39719  14.79485  4.74121   1.000 34.15649 ?  178 TRP B CD1 1 
ATOM   2720 C CD2 . TRP B 1 180 ? -6.29888  12.55863  4.63695   1.000 31.78933 ?  178 TRP B CD2 1 
ATOM   2721 N NE1 . TRP B 1 180 ? -6.66775  14.42066  3.44436   1.000 31.49696 ?  178 TRP B NE1 1 
ATOM   2722 C CE2 . TRP B 1 180 ? -6.61045  13.05106  3.35632   1.000 33.46248 ?  178 TRP B CE2 1 
ATOM   2723 C CE3 . TRP B 1 180 ? -6.17997  11.17600  4.81799   1.000 31.41036 ?  178 TRP B CE3 1 
ATOM   2724 C CZ2 . TRP B 1 180 ? -6.79315  12.20863  2.25212   1.000 31.78687 ?  178 TRP B CZ2 1 
ATOM   2725 C CZ3 . TRP B 1 180 ? -6.36108  10.34213  3.71365   1.000 32.20390 ?  178 TRP B CZ3 1 
ATOM   2726 C CH2 . TRP B 1 180 ? -6.67152  10.86374  2.45762   1.000 30.68248 ?  178 TRP B CH2 1 
ATOM   2727 N N   . GLU B 1 181 ? -2.98281  14.72213  6.21010   1.000 34.05310 ?  179 GLU B N   1 
ATOM   2728 C CA  . GLU B 1 181 ? -2.03795  15.18729  5.19793   1.000 38.54967 ?  179 GLU B CA  1 
ATOM   2729 C C   . GLU B 1 181 ? -0.80970  14.28670  5.11568   1.000 38.12788 ?  179 GLU B C   1 
ATOM   2730 O O   . GLU B 1 181 ? -0.28653  14.05026  4.01455   1.000 36.83660 ?  179 GLU B O   1 
ATOM   2731 C CB  . GLU B 1 181 ? -1.64442  16.63572  5.46250   1.000 39.61521 ?  179 GLU B CB  1 
ATOM   2732 C CG  . GLU B 1 181 ? -2.83925  17.56244  5.52386   1.000 39.42717 ?  179 GLU B CG  1 
ATOM   2733 C CD  . GLU B 1 181 ? -2.75100  18.64072  4.47726   1.000 40.97203 ?  179 GLU B CD  1 
ATOM   2734 O OE1 . GLU B 1 181 ? -1.61965  18.91619  4.01453   1.000 39.83168 ?  179 GLU B OE1 1 
ATOM   2735 O OE2 . GLU B 1 181 ? -3.80132  19.20724  4.09148   1.000 39.88114 -1 179 GLU B OE2 1 
ATOM   2736 N N   . ASP B 1 182 ? -0.36434  13.74291  6.25986   1.000 34.33219 ?  180 ASP B N   1 
ATOM   2737 C CA  . ASP B 1 182 ? 0.74341   12.79295  6.25896   1.000 37.35951 ?  180 ASP B CA  1 
ATOM   2738 C C   . ASP B 1 182 ? 0.41207   11.56680  5.42569   1.000 36.13365 ?  180 ASP B C   1 
ATOM   2739 O O   . ASP B 1 182 ? 1.23563   11.09898  4.62975   1.000 32.77845 ?  180 ASP B O   1 
ATOM   2740 C CB  . ASP B 1 182 ? 1.08254   12.36156  7.68818   1.000 34.20569 ?  180 ASP B CB  1 
ATOM   2741 C CG  . ASP B 1 182 ? 1.59768   13.49864  8.53047   1.000 37.32820 ?  180 ASP B CG  1 
ATOM   2742 O OD1 . ASP B 1 182 ? 2.04047   14.49879  7.93929   1.000 41.14308 ?  180 ASP B OD1 1 
ATOM   2743 O OD2 . ASP B 1 182 ? 1.55943   13.39718  9.77582   1.000 36.36264 -1 180 ASP B OD2 1 
ATOM   2744 N N   . ILE B 1 183 ? -0.78920  11.02418  5.61844   1.000 29.11382 ?  181 ILE B N   1 
ATOM   2745 C CA  . ILE B 1 183 ? -1.18020  9.77164   4.98617   1.000 31.10120 ?  181 ILE B CA  1 
ATOM   2746 C C   . ILE B 1 183 ? -1.45664  9.97141   3.49942   1.000 36.15676 ?  181 ILE B C   1 
ATOM   2747 O O   . ILE B 1 183 ? -1.18372  9.08268   2.68263   1.000 37.30292 ?  181 ILE B O   1 
ATOM   2748 C CB  . ILE B 1 183 ? -2.40064  9.19336   5.72426   1.000 33.17354 ?  181 ILE B CB  1 
ATOM   2749 C CG1 . ILE B 1 183 ? -1.97351  8.65859   7.08984   1.000 30.70253 ?  181 ILE B CG1 1 
ATOM   2750 C CG2 . ILE B 1 183 ? -3.05386  8.07673   4.91561   1.000 31.19231 ?  181 ILE B CG2 1 
ATOM   2751 C CD1 . ILE B 1 183 ? -1.13529  7.40881   6.97937   1.000 28.52967 ?  181 ILE B CD1 1 
ATOM   2752 N N   . GLU B 1 184 ? -2.00666  11.13228  3.12116   1.000 35.00478 ?  182 GLU B N   1 
ATOM   2753 C CA  . GLU B 1 184 ? -2.26829  11.40340  1.70854   1.000 35.23828 ?  182 GLU B CA  1 
ATOM   2754 C C   . GLU B 1 184 ? -0.97430  11.48077  0.90876   1.000 36.92383 ?  182 GLU B C   1 
ATOM   2755 O O   . GLU B 1 184 ? -0.96302  11.15996  -0.28868  1.000 37.91907 ?  182 GLU B O   1 
ATOM   2756 C CB  . GLU B 1 184 ? -3.05561  12.70135  1.54507   1.000 31.95740 ?  182 GLU B CB  1 
ATOM   2757 C CG  . GLU B 1 184 ? -3.57812  12.90170  0.11354   1.000 36.62584 ?  182 GLU B CG  1 
ATOM   2758 C CD  . GLU B 1 184 ? -4.17984  14.27783  -0.13543  1.000 37.98039 ?  182 GLU B CD  1 
ATOM   2759 O OE1 . GLU B 1 184 ? -4.02672  15.18310  0.71689   1.000 41.49957 ?  182 GLU B OE1 1 
ATOM   2760 O OE2 . GLU B 1 184 ? -4.82208  14.45842  -1.19349  1.000 47.24463 -1 182 GLU B OE2 1 
ATOM   2761 N N   . SER B 1 185 ? 0.11633   11.89687  1.55940   1.000 40.46847 ?  183 SER B N   1 
ATOM   2762 C CA  . SER B 1 185 ? 1.43632   11.92281  0.92746   1.000 41.35589 ?  183 SER B CA  1 
ATOM   2763 C C   . SER B 1 185 ? 1.97142   10.51413  0.68190   1.000 41.77175 ?  183 SER B C   1 
ATOM   2764 O O   . SER B 1 185 ? 2.46050   10.21075  -0.41200  1.000 44.05840 ?  183 SER B O   1 
ATOM   2765 C CB  . SER B 1 185 ? 2.41136   12.71725  1.79760   1.000 40.29225 ?  183 SER B CB  1 
ATOM   2766 O OG  . SER B 1 185 ? 1.97540   14.06181  1.92351   1.000 43.21533 ?  183 SER B OG  1 
ATOM   2767 N N   . LEU B 1 186 ? 1.94314   9.65899   1.70410   1.000 39.35496 ?  184 LEU B N   1 
ATOM   2768 C CA  . LEU B 1 186 ? 2.21539   8.24086   1.49840   1.000 40.71126 ?  184 LEU B CA  1 
ATOM   2769 C C   . LEU B 1 186 ? 1.48806   7.68606   0.28357   1.000 41.41719 ?  184 LEU B C   1 
ATOM   2770 O O   . LEU B 1 186 ? 2.08460   7.01332   -0.56272  1.000 42.48761 ?  184 LEU B O   1 
ATOM   2771 C CB  . LEU B 1 186 ? 1.80982   7.44071   2.73576   1.000 39.68969 ?  184 LEU B CB  1 
ATOM   2772 C CG  . LEU B 1 186 ? 2.53581   6.10543   2.86877   1.000 43.81373 ?  184 LEU B CG  1 
ATOM   2773 C CD1 . LEU B 1 186 ? 3.91450   6.21727   2.23616   1.000 42.98006 ?  184 LEU B CD1 1 
ATOM   2774 C CD2 . LEU B 1 186 ? 2.62446   5.67251   4.31473   1.000 35.36007 ?  184 LEU B CD2 1 
ATOM   2775 N N   . TYR B 1 187 ? 0.18153   7.93830   0.20667   1.000 38.90427 ?  185 TYR B N   1 
ATOM   2776 C CA  . TYR B 1 187 ? -0.61646  7.47650   -0.92380  1.000 42.17975 ?  185 TYR B CA  1 
ATOM   2777 C C   . TYR B 1 187 ? -0.13528  8.05871   -2.24489  1.000 41.21228 ?  185 TYR B C   1 
ATOM   2778 O O   . TYR B 1 187 ? 0.19072   7.31862   -3.18008  1.000 45.09410 ?  185 TYR B O   1 
ATOM   2779 C CB  . TYR B 1 187 ? -2.08249  7.82312   -0.69534  1.000 41.61049 ?  185 TYR B CB  1 
ATOM   2780 C CG  . TYR B 1 187 ? -2.98311  7.32293   -1.78935  1.000 44.35692 ?  185 TYR B CG  1 
ATOM   2781 C CD1 . TYR B 1 187 ? -3.18873  5.96814   -1.99154  1.000 46.04241 ?  185 TYR B CD1 1 
ATOM   2782 C CD2 . TYR B 1 187 ? -3.63621  8.21565   -2.62076  1.000 45.86994 ?  185 TYR B CD2 1 
ATOM   2783 C CE1 . TYR B 1 187 ? -4.02483  5.51683   -2.99925  1.000 48.37853 ?  185 TYR B CE1 1 
ATOM   2784 C CE2 . TYR B 1 187 ? -4.46474  7.78175   -3.62863  1.000 47.65789 ?  185 TYR B CE2 1 
ATOM   2785 C CZ  . TYR B 1 187 ? -4.66312  6.43633   -3.81612  1.000 48.81669 ?  185 TYR B CZ  1 
ATOM   2786 O OH  . TYR B 1 187 ? -5.49894  6.02289   -4.83802  1.000 52.32025 ?  185 TYR B OH  1 
ATOM   2787 N N   . GLY B 1 188 ? -0.12345  9.38746   -2.35986  1.000 41.45876 ?  186 GLY B N   1 
ATOM   2788 C CA  . GLY B 1 188 ? 0.06111   10.00642  -3.66453  1.000 38.88893 ?  186 GLY B CA  1 
ATOM   2789 C C   . GLY B 1 188 ? 1.46619   9.89073   -4.23867  1.000 42.88487 ?  186 GLY B C   1 
ATOM   2790 O O   . GLY B 1 188 ? 1.64367   10.09480  -5.44133  1.000 38.62572 ?  186 GLY B O   1 
ATOM   2791 N N   . GLU B 1 189 ? 2.46905   9.59207   -3.40741  1.000 39.00229 ?  187 GLU B N   1 
ATOM   2792 C CA  . GLU B 1 189 ? 3.85599   9.52018   -3.87976  1.000 43.00773 ?  187 GLU B CA  1 
ATOM   2793 C C   . GLU B 1 189 ? 4.12051   8.30301   -4.75150  1.000 44.77558 ?  187 GLU B C   1 
ATOM   2794 O O   . GLU B 1 189 ? 5.18694   8.22133   -5.37630  1.000 44.17710 ?  187 GLU B O   1 
ATOM   2795 C CB  . GLU B 1 189 ? 4.81721   9.49759   -2.69226  1.000 40.79681 ?  187 GLU B CB  1 
ATOM   2796 N N   . GLN B 1 190 ? 3.15412   7.39396   -4.82878  1.000 46.21941 ?  188 GLN B N   1 
ATOM   2797 C CA  . GLN B 1 190 ? 3.33544   6.06487   -5.39211  1.000 46.92255 ?  188 GLN B CA  1 
ATOM   2798 C C   . GLN B 1 190 ? 3.55280   6.19335   -6.89913  1.000 49.87175 ?  188 GLN B C   1 
ATOM   2799 O O   . GLN B 1 190 ? 2.76213   6.85104   -7.58494  1.000 50.83283 ?  188 GLN B O   1 
ATOM   2800 C CB  . GLN B 1 190 ? 2.07567   5.26975   -5.05866  1.000 48.44259 ?  188 GLN B CB  1 
ATOM   2801 C CG  . GLN B 1 190 ? 2.26546   4.27152   -3.94189  1.000 45.35823 ?  188 GLN B CG  1 
ATOM   2802 C CD  . GLN B 1 190 ? 1.20726   3.20663   -3.91377  1.000 45.33020 ?  188 GLN B CD  1 
ATOM   2803 O OE1 . GLN B 1 190 ? 1.42994   2.06364   -4.30691  1.000 45.21467 ?  188 GLN B OE1 1 
ATOM   2804 N NE2 . GLN B 1 190 ? 0.01395   3.59841   -3.48277  1.000 45.72498 ?  188 GLN B NE2 1 
ATOM   2805 N N   . PHE B 1 191 ? 4.64009   5.59373   -7.41610  1.000 48.60204 ?  189 PHE B N   1 
ATOM   2806 C CA  . PHE B 1 191 ? 5.09394   5.92327   -8.77540  1.000 52.55040 ?  189 PHE B CA  1 
ATOM   2807 C C   . PHE B 1 191 ? 4.00854   5.67512   -9.82252  1.000 53.73540 ?  189 PHE B C   1 
ATOM   2808 O O   . PHE B 1 191 ? 3.87258   6.44657   -10.78168 1.000 54.39659 ?  189 PHE B O   1 
ATOM   2809 C CB  . PHE B 1 191 ? 6.36511   5.14210   -9.13053  1.000 51.75131 ?  189 PHE B CB  1 
ATOM   2810 N N   . HIS B 1 192 ? 3.21457   4.61267   -9.65711  1.000 55.29387 ?  190 HIS B N   1 
ATOM   2811 C CA  . HIS B 1 192 ? 2.18091   4.31883   -10.64768 1.000 54.93286 ?  190 HIS B CA  1 
ATOM   2812 C C   . HIS B 1 192 ? 1.12236   5.42148   -10.72569 1.000 53.25646 ?  190 HIS B C   1 
ATOM   2813 O O   . HIS B 1 192 ? 0.38341   5.49605   -11.71593 1.000 49.63491 ?  190 HIS B O   1 
ATOM   2814 C CB  . HIS B 1 192 ? 1.56503   2.95448   -10.32532 1.000 57.06959 ?  190 HIS B CB  1 
ATOM   2815 C CG  . HIS B 1 192 ? 0.34189   3.02628   -9.46525  1.000 57.41099 ?  190 HIS B CG  1 
ATOM   2816 N ND1 . HIS B 1 192 ? -0.90699  3.34008   -9.96189  1.000 58.51658 ?  190 HIS B ND1 1 
ATOM   2817 C CD2 . HIS B 1 192 ? 0.18186   2.84003   -8.13390  1.000 53.14868 ?  190 HIS B CD2 1 
ATOM   2818 C CE1 . HIS B 1 192 ? -1.78478  3.33014   -8.97444  1.000 52.99095 ?  190 HIS B CE1 1 
ATOM   2819 N NE2 . HIS B 1 192 ? -1.14905  3.03332   -7.85473  1.000 53.17279 ?  190 HIS B NE2 1 
ATOM   2820 N N   . HIS B 1 193 ? 1.03419   6.27603   -9.69749  1.000 54.02234 ?  191 HIS B N   1 
ATOM   2821 C CA  . HIS B 1 193 ? 0.15893   7.44500   -9.73035  1.000 51.71794 ?  191 HIS B CA  1 
ATOM   2822 C C   . HIS B 1 193 ? 0.67549   8.51703   -10.67441 1.000 50.45851 ?  191 HIS B C   1 
ATOM   2823 O O   . HIS B 1 193 ? -0.06475  9.45197   -11.00670 1.000 53.68677 ?  191 HIS B O   1 
ATOM   2824 C CB  . HIS B 1 193 ? 0.02122   8.03451   -8.32442  1.000 50.14176 ?  191 HIS B CB  1 
ATOM   2825 C CG  . HIS B 1 193 ? -0.96320  7.31667   -7.46073  1.000 49.63929 ?  191 HIS B CG  1 
ATOM   2826 N ND1 . HIS B 1 193 ? -2.08985  6.70150   -7.96631  1.000 52.35045 ?  191 HIS B ND1 1 
ATOM   2827 C CD2 . HIS B 1 193 ? -0.97601  7.09068   -6.12661  1.000 49.06717 ?  191 HIS B CD2 1 
ATOM   2828 C CE1 . HIS B 1 193 ? -2.76158  6.13905   -6.97581  1.000 52.64115 ?  191 HIS B CE1 1 
ATOM   2829 N NE2 . HIS B 1 193 ? -2.10784  6.36295   -5.84759  1.000 48.37126 ?  191 HIS B NE2 1 
ATOM   2830 N N   . HIS B 1 194 ? 1.92301   8.40021   -11.11867 1.000 48.80611 ?  192 HIS B N   1 
ATOM   2831 C CA  . HIS B 1 194 ? 2.57086   9.45259   -11.89107 1.000 52.50759 ?  192 HIS B CA  1 
ATOM   2832 C C   . HIS B 1 194 ? 2.94209   9.00595   -13.29390 1.000 50.10299 ?  192 HIS B C   1 
ATOM   2833 O O   . HIS B 1 194 ? 3.61937   9.75270   -14.00933 1.000 50.82350 ?  192 HIS B O   1 
ATOM   2834 C CB  . HIS B 1 194 ? 3.80152   9.95446   -11.13430 1.000 47.08451 ?  192 HIS B CB  1 
ATOM   2835 C CG  . HIS B 1 194 ? 3.47104   10.45931  -9.76891  1.000 44.81797 ?  192 HIS B CG  1 
ATOM   2836 N ND1 . HIS B 1 194 ? 2.84674   11.67023  -9.56085  1.000 43.64663 ?  192 HIS B ND1 1 
ATOM   2837 C CD2 . HIS B 1 194 ? 3.57003   9.87374   -8.55440  1.000 46.17250 ?  192 HIS B CD2 1 
ATOM   2838 C CE1 . HIS B 1 194 ? 2.63556   11.83813  -8.26848  1.000 41.06719 ?  192 HIS B CE1 1 
ATOM   2839 N NE2 . HIS B 1 194 ? 3.06136   10.75929  -7.63377  1.000 43.75894 ?  192 HIS B NE2 1 
ATOM   2840 N N   . HIS B 1 195 ? 2.49276   7.82841   -13.72157 1.000 51.26259 ?  193 HIS B N   1 
ATOM   2841 C CA  . HIS B 1 195 ? 2.73908   7.34471   -15.07686 1.000 52.88363 ?  193 HIS B CA  1 
ATOM   2842 C C   . HIS B 1 195 ? 1.38740   7.06016   -15.71763 1.000 55.66031 ?  193 HIS B C   1 
ATOM   2843 O O   . HIS B 1 195 ? 0.70228   6.10509   -15.33796 1.000 58.54922 ?  193 HIS B O   1 
ATOM   2844 C CB  . HIS B 1 195 ? 3.63902   6.10945   -15.05121 1.000 52.80391 ?  193 HIS B CB  1 
ATOM   2845 C CG  . HIS B 1 195 ? 5.02132   6.38686   -14.53161 1.000 54.68997 ?  193 HIS B CG  1 
ATOM   2846 N ND1 . HIS B 1 195 ? 5.80305   7.42693   -14.99657 1.000 50.02731 ?  193 HIS B ND1 1 
ATOM   2847 C CD2 . HIS B 1 195 ? 5.73196   5.79703   -13.53978 1.000 52.24845 ?  193 HIS B CD2 1 
ATOM   2848 C CE1 . HIS B 1 195 ? 6.94765   7.44139   -14.33657 1.000 46.33178 ?  193 HIS B CE1 1 
ATOM   2849 N NE2 . HIS B 1 195 ? 6.92936   6.46430   -13.44772 1.000 50.68083 ?  193 HIS B NE2 1 
ATOM   2850 N N   . HIS B 1 196 ? 1.00526   7.89608   -16.67691 1.000 59.58210 ?  194 HIS B N   1 
ATOM   2851 C CA  . HIS B 1 196 ? -0.30218  7.80675   -17.29967 1.000 58.08413 ?  194 HIS B CA  1 
ATOM   2852 C C   . HIS B 1 196 ? -0.21114  8.17982   -18.76701 1.000 57.72985 ?  194 HIS B C   1 
ATOM   2853 O O   . HIS B 1 196 ? 0.32293   7.42737   -19.59439 1.000 62.17759 ?  194 HIS B O   1 
ATOM   2854 C CB  . HIS B 1 196 ? -1.29681  8.71698   -16.57093 1.000 58.48699 ?  194 HIS B CB  1 
HETATM 2855 O O   . HOH C 2 .   ? -3.89613  -2.97439  41.18609  1.000 44.48609 ?  201 HOH A O   1 
HETATM 2856 O O   . HOH C 2 .   ? 5.73455   15.68777  13.89557  1.000 41.07813 ?  202 HOH A O   1 
HETATM 2857 O O   . HOH C 2 .   ? 4.06733   -8.95195  7.82087   1.000 37.47594 ?  203 HOH A O   1 
HETATM 2858 O O   . HOH C 2 .   ? -4.42502  -8.09542  36.38179  1.000 47.04544 ?  204 HOH A O   1 
HETATM 2859 O O   . HOH C 2 .   ? 9.58441   15.60419  13.88647  1.000 40.57435 ?  205 HOH A O   1 
HETATM 2860 O O   . HOH C 2 .   ? 8.64497   13.00955  27.37759  1.000 40.77479 ?  206 HOH A O   1 
HETATM 2861 O O   . HOH C 2 .   ? 12.99033  12.35169  3.17369   1.000 52.61698 ?  207 HOH A O   1 
HETATM 2862 O O   . HOH C 2 .   ? 24.36905  6.00152   17.08445  1.000 37.68972 ?  208 HOH A O   1 
HETATM 2863 O O   . HOH C 2 .   ? -0.06627  -14.27763 27.70848  1.000 44.57614 ?  209 HOH A O   1 
HETATM 2864 O O   . HOH C 2 .   ? 8.58821   -7.67897  3.12211   1.000 40.68064 ?  210 HOH A O   1 
HETATM 2865 O O   . HOH C 2 .   ? -5.42646  5.33206   31.71613  1.000 42.14472 ?  211 HOH A O   1 
HETATM 2866 O O   . HOH C 2 .   ? 18.63951  14.04704  11.83316  1.000 50.07695 ?  212 HOH A O   1 
HETATM 2867 O O   . HOH C 2 .   ? 8.52562   -14.76497 40.78816  1.000 47.25568 ?  213 HOH A O   1 
HETATM 2868 O O   . HOH C 2 .   ? 3.33157   -6.90029  29.53136  1.000 30.99383 ?  214 HOH A O   1 
HETATM 2869 O O   . HOH C 2 .   ? 26.23787  1.40797   12.12619  1.000 37.37749 ?  215 HOH A O   1 
HETATM 2870 O O   . HOH C 2 .   ? -9.34450  9.39794   39.02626  1.000 48.52025 ?  216 HOH A O   1 
HETATM 2871 O O   . HOH C 2 .   ? 10.61428  -5.32616  33.29192  1.000 37.11779 ?  217 HOH A O   1 
HETATM 2872 O O   . HOH C 2 .   ? -0.54458  -3.73236  8.93149   1.000 26.82226 ?  218 HOH A O   1 
HETATM 2873 O O   . HOH C 2 .   ? 0.92267   2.08441   25.60836  1.000 32.74556 ?  219 HOH A O   1 
HETATM 2874 O O   . HOH C 2 .   ? 10.69795  -11.02716 22.00569  1.000 42.53993 ?  220 HOH A O   1 
HETATM 2875 O O   . HOH C 2 .   ? -0.60535  -9.94179  20.11290  1.000 40.64894 ?  221 HOH A O   1 
HETATM 2876 O O   . HOH C 2 .   ? 2.07805   -11.55431 28.59970  1.000 29.49651 ?  222 HOH A O   1 
HETATM 2877 O O   . HOH C 2 .   ? 12.26260  15.94262  9.75134   1.000 43.72289 ?  223 HOH A O   1 
HETATM 2878 O O   . HOH C 2 .   ? 16.41129  5.62209   31.70248  1.000 38.83664 ?  224 HOH A O   1 
HETATM 2879 O O   . HOH C 2 .   ? 17.21977  -0.94732  40.04007  1.000 52.91800 ?  225 HOH A O   1 
HETATM 2880 O O   . HOH C 2 .   ? 11.96264  8.27590   32.88811  1.000 41.23901 ?  226 HOH A O   1 
HETATM 2881 O O   . HOH C 2 .   ? 9.48440   10.55693  29.92328  1.000 39.67590 ?  227 HOH A O   1 
HETATM 2882 O O   . HOH C 2 .   ? 21.04974  7.17757   21.93581  1.000 36.69125 ?  228 HOH A O   1 
HETATM 2883 O O   . HOH C 2 .   ? 16.64978  -5.34095  20.55149  1.000 34.30263 ?  229 HOH A O   1 
HETATM 2884 O O   . HOH C 2 .   ? 11.11586  3.24048   40.34582  1.000 39.23935 ?  230 HOH A O   1 
HETATM 2885 O O   . HOH C 2 .   ? -9.10311  -1.41658  35.62515  1.000 43.74159 ?  231 HOH A O   1 
HETATM 2886 O O   . HOH C 2 .   ? -4.36400  6.41653   33.56872  1.000 41.28773 ?  232 HOH A O   1 
HETATM 2887 O O   . HOH C 2 .   ? -3.24724  -5.45792  13.24111  1.000 38.69480 ?  233 HOH A O   1 
HETATM 2888 O O   . HOH C 2 .   ? 2.61872   -9.30363  26.94409  1.000 32.81626 ?  234 HOH A O   1 
HETATM 2889 O O   . HOH C 2 .   ? -1.30687  -10.54553 31.20363  1.000 39.93873 ?  235 HOH A O   1 
HETATM 2890 O O   . HOH C 2 .   ? 4.97140   -12.11877 26.39604  1.000 44.66007 ?  236 HOH A O   1 
HETATM 2891 O O   . HOH C 2 .   ? 25.19377  2.20580   23.33217  1.000 42.57059 ?  237 HOH A O   1 
HETATM 2892 O O   . HOH C 2 .   ? 1.19103   -2.76837  23.91921  1.000 24.70691 ?  238 HOH A O   1 
HETATM 2893 O O   . HOH C 2 .   ? -9.54937  -1.45510  32.30212  1.000 38.56156 ?  239 HOH A O   1 
HETATM 2894 O O   . HOH C 2 .   ? 5.03578   6.10149   44.92146  1.000 40.50053 ?  240 HOH A O   1 
HETATM 2895 O O   . HOH C 2 .   ? -6.58336  8.36412   33.17576  1.000 47.12195 ?  241 HOH A O   1 
HETATM 2896 O O   . HOH C 2 .   ? -9.97820  8.89986   34.58349  1.000 40.16768 ?  242 HOH A O   1 
HETATM 2897 O O   . HOH C 2 .   ? 9.64828   17.83822  7.73736   1.000 46.52137 ?  243 HOH A O   1 
HETATM 2898 O O   . HOH C 2 .   ? -2.79942  -0.79800  48.88538  1.000 44.37976 ?  244 HOH A O   1 
HETATM 2899 O O   . HOH C 2 .   ? 8.73051   -12.83459 38.94133  1.000 33.60477 ?  245 HOH A O   1 
HETATM 2900 O O   . HOH C 2 .   ? 13.60274  15.55429  18.56040  1.000 39.42565 ?  246 HOH A O   1 
HETATM 2901 O O   . HOH C 2 .   ? 11.94547  -7.77994  5.61870   1.000 33.54059 ?  247 HOH A O   1 
HETATM 2902 O O   . HOH C 2 .   ? 5.58140   7.25717   20.39124  1.000 33.43593 ?  248 HOH A O   1 
HETATM 2903 O O   . HOH C 2 .   ? 9.21708   -7.53526  32.97009  1.000 38.96656 ?  249 HOH A O   1 
HETATM 2904 O O   . HOH C 2 .   ? 16.61778  -4.46611  53.16045  1.000 57.91723 ?  250 HOH A O   1 
HETATM 2905 O O   . HOH C 2 .   ? -1.54578  -3.94230  11.53484  1.000 36.47116 ?  251 HOH A O   1 
HETATM 2906 O O   . HOH C 2 .   ? 13.79200  12.05546  23.48249  1.000 34.98583 ?  252 HOH A O   1 
HETATM 2907 O O   . HOH C 2 .   ? 1.09467   6.00497   17.98472  1.000 36.26923 ?  253 HOH A O   1 
HETATM 2908 O O   . HOH C 2 .   ? 7.77418   9.55205   31.59732  1.000 37.29274 ?  254 HOH A O   1 
HETATM 2909 O O   . HOH C 2 .   ? 7.18395   -2.95111  28.67609  1.000 34.27740 ?  255 HOH A O   1 
HETATM 2910 O O   . HOH C 2 .   ? 11.33688  -8.17354  8.76495   1.000 33.77648 ?  256 HOH A O   1 
HETATM 2911 O O   . HOH C 2 .   ? 19.13761  -6.40351  42.38366  1.000 55.00245 ?  257 HOH A O   1 
HETATM 2912 O O   . HOH C 2 .   ? 23.80985  2.17819   29.97828  1.000 44.10148 ?  258 HOH A O   1 
HETATM 2913 O O   . HOH C 2 .   ? -2.10490  -8.30696  49.16526  1.000 44.88363 ?  259 HOH A O   1 
HETATM 2914 O O   . HOH C 2 .   ? 5.04651   0.54646   25.17541  1.000 31.40360 ?  260 HOH A O   1 
HETATM 2915 O O   . HOH C 2 .   ? 6.15889   4.77388   54.70077  1.000 49.81388 ?  261 HOH A O   1 
HETATM 2916 O O   . HOH C 2 .   ? -3.52182  -10.70763 1.96746   1.000 38.61635 ?  262 HOH A O   1 
HETATM 2917 O O   . HOH C 2 .   ? 12.62653  -8.57387  55.07199  1.000 64.34488 ?  263 HOH A O   1 
HETATM 2918 O O   . HOH C 2 .   ? -3.47476  1.27337   46.67080  1.000 41.84733 ?  264 HOH A O   1 
HETATM 2919 O O   . HOH C 2 .   ? 11.34057  -12.87948 38.26923  1.000 35.07746 ?  265 HOH A O   1 
HETATM 2920 O O   . HOH C 2 .   ? 13.32485  -2.97911  0.78185   1.000 46.34663 ?  266 HOH A O   1 
HETATM 2921 O O   . HOH C 2 .   ? 2.21571   -8.21248  17.89350  1.000 42.82246 ?  267 HOH A O   1 
HETATM 2922 O O   . HOH C 2 .   ? 6.56464   -5.20830  28.13373  1.000 28.35771 ?  268 HOH A O   1 
HETATM 2923 O O   . HOH C 2 .   ? -2.68710  -6.52554  47.46408  1.000 46.21329 ?  269 HOH A O   1 
HETATM 2924 O O   . HOH C 2 .   ? 7.62518   16.61903  25.12272  1.000 46.06029 ?  270 HOH A O   1 
HETATM 2925 O O   . HOH C 2 .   ? 7.78654   -14.86877 37.06309  1.000 38.94707 ?  271 HOH A O   1 
HETATM 2926 O O   . HOH C 2 .   ? 14.72644  16.46621  16.04952  1.000 47.34915 ?  272 HOH A O   1 
HETATM 2927 O O   . HOH C 2 .   ? 7.23004   0.92386   24.11451  1.000 37.75742 ?  273 HOH A O   1 
HETATM 2928 O O   . HOH C 2 .   ? 4.52394   3.59849   55.99366  1.000 56.59333 ?  274 HOH A O   1 
HETATM 2929 O O   . HOH C 2 .   ? -4.11428  -6.96571  45.43554  1.000 51.39887 ?  275 HOH A O   1 
HETATM 2930 O O   . HOH C 2 .   ? 25.84833  -0.33281  24.44870  1.000 40.07109 ?  276 HOH A O   1 
HETATM 2931 O O   . HOH C 2 .   ? -8.94587  10.41883  30.24053  1.000 53.31851 ?  277 HOH A O   1 
HETATM 2932 O O   . HOH C 2 .   ? -7.19240  6.53134   31.13789  1.000 43.47791 ?  278 HOH A O   1 
HETATM 2933 O O   . HOH C 2 .   ? 21.75457  4.59034   30.04127  1.000 49.29191 ?  279 HOH A O   1 
HETATM 2934 O O   . HOH C 2 .   ? 12.37768  -5.81309  34.65487  1.000 39.20792 ?  280 HOH A O   1 
HETATM 2935 O O   . HOH C 2 .   ? 11.47178  16.55989  15.36937  1.000 49.84241 ?  281 HOH A O   1 
HETATM 2936 O O   . HOH C 2 .   ? 25.10142  1.12994   31.48617  1.000 39.66398 ?  282 HOH A O   1 
HETATM 2937 O O   . HOH C 2 .   ? -9.88868  11.11055  36.15425  1.000 43.69390 ?  283 HOH A O   1 
HETATM 2938 O O   . HOH C 2 .   ? 17.13014  11.06490  0.60592   1.000 45.65663 ?  284 HOH A O   1 
HETATM 2939 O O   . HOH C 2 .   ? 12.98194  5.91604   -4.75014  1.000 64.72142 ?  285 HOH A O   1 
HETATM 2940 O O   . HOH D 2 .   ? -16.30459 -12.61193 16.36929  1.000 39.52670 ?  201 HOH B O   1 
HETATM 2941 O O   . HOH D 2 .   ? -11.72261 12.01806  -3.36649  1.000 40.98799 ?  202 HOH B O   1 
HETATM 2942 O O   . HOH D 2 .   ? -22.07139 -0.21971  13.98521  1.000 36.79487 ?  203 HOH B O   1 
HETATM 2943 O O   . HOH D 2 .   ? 4.36537   9.12673   18.63651  1.000 38.61238 ?  204 HOH B O   1 
HETATM 2944 O O   . HOH D 2 .   ? -17.70226 -1.71151  2.63354   1.000 34.35009 ?  205 HOH B O   1 
HETATM 2945 O O   . HOH D 2 .   ? 2.44156   16.38204  6.39297   1.000 45.66750 ?  206 HOH B O   1 
HETATM 2946 O O   . HOH D 2 .   ? -7.50849  -2.94564  15.79316  1.000 35.02113 ?  207 HOH B O   1 
HETATM 2947 O O   . HOH D 2 .   ? -2.21049  -7.04043  0.72662   1.000 39.96464 ?  208 HOH B O   1 
HETATM 2948 O O   . HOH D 2 .   ? -31.53980 -12.34241 21.32306  1.000 46.11159 ?  209 HOH B O   1 
HETATM 2949 O O   . HOH D 2 .   ? -34.10842 -13.44435 24.58434  1.000 47.25106 ?  210 HOH B O   1 
HETATM 2950 O O   . HOH D 2 .   ? -22.53378 2.79304   3.30855   1.000 40.38461 ?  211 HOH B O   1 
HETATM 2951 O O   . HOH D 2 .   ? -13.71775 -11.47089 12.18509  1.000 36.28685 ?  212 HOH B O   1 
HETATM 2952 O O   . HOH D 2 .   ? 2.51812   7.43181   20.51249  1.000 39.37607 ?  213 HOH B O   1 
HETATM 2953 O O   . HOH D 2 .   ? -4.99692  -12.47630 25.18836  1.000 35.71270 ?  214 HOH B O   1 
HETATM 2954 O O   . HOH D 2 .   ? -12.32526 4.01501   28.30466  1.000 33.98071 ?  215 HOH B O   1 
HETATM 2955 O O   . HOH D 2 .   ? 3.83086   9.04689   15.47994  1.000 29.57258 ?  216 HOH B O   1 
HETATM 2956 O O   . HOH D 2 .   ? -23.51340 -17.37439 26.25178  1.000 39.28877 ?  217 HOH B O   1 
HETATM 2957 O O   . HOH D 2 .   ? -31.91512 -4.22619  23.35018  1.000 32.54575 ?  218 HOH B O   1 
HETATM 2958 O O   . HOH D 2 .   ? -10.96667 -12.46699 9.53827   1.000 33.81506 ?  219 HOH B O   1 
HETATM 2959 O O   . HOH D 2 .   ? -32.25053 -10.46971 41.19043  1.000 41.48565 ?  220 HOH B O   1 
HETATM 2960 O O   . HOH D 2 .   ? -26.60230 -18.45477 25.89731  1.000 42.83217 ?  221 HOH B O   1 
HETATM 2961 O O   . HOH D 2 .   ? -4.86323  6.63205   21.26769  1.000 36.30319 ?  222 HOH B O   1 
HETATM 2962 O O   . HOH D 2 .   ? -0.60492  12.97222  18.93693  1.000 38.32811 ?  223 HOH B O   1 
HETATM 2963 O O   . HOH D 2 .   ? -6.41199  -0.19508  22.21447  1.000 34.18149 ?  224 HOH B O   1 
HETATM 2964 O O   . HOH D 2 .   ? -13.62841 -12.03681 15.22621  1.000 34.23295 ?  225 HOH B O   1 
HETATM 2965 O O   . HOH D 2 .   ? -38.67046 -6.52869  26.89940  1.000 38.43313 ?  226 HOH B O   1 
HETATM 2966 O O   . HOH D 2 .   ? -20.61433 4.35032   9.72163   1.000 40.18880 ?  227 HOH B O   1 
HETATM 2967 O O   . HOH D 2 .   ? -28.17061 -0.92974  27.36984  1.000 31.34734 ?  228 HOH B O   1 
HETATM 2968 O O   . HOH D 2 .   ? -0.46705  11.30578  -6.70056  1.000 44.51791 ?  229 HOH B O   1 
HETATM 2969 O O   . HOH D 2 .   ? -5.77572  17.29425  0.73638   1.000 38.14706 ?  230 HOH B O   1 
HETATM 2970 O O   . HOH D 2 .   ? -13.30651 -15.08335 14.58520  1.000 40.01780 ?  231 HOH B O   1 
HETATM 2971 O O   . HOH D 2 .   ? -17.14058 2.84032   -1.72935  1.000 41.35668 ?  232 HOH B O   1 
HETATM 2972 O O   . HOH D 2 .   ? -30.46205 -17.11559 25.71012  1.000 47.72693 ?  233 HOH B O   1 
HETATM 2973 O O   . HOH D 2 .   ? -3.55360  -9.03466  32.17700  1.000 37.02420 ?  234 HOH B O   1 
HETATM 2974 O O   . HOH D 2 .   ? -6.74468  -14.61268 24.49931  1.000 38.08693 ?  235 HOH B O   1 
HETATM 2975 O O   . HOH D 2 .   ? -17.30578 7.60436   3.66385   1.000 42.98622 ?  236 HOH B O   1 
HETATM 2976 O O   . HOH D 2 .   ? -5.90660  -4.37998  11.04432  1.000 34.17099 ?  237 HOH B O   1 
HETATM 2977 O O   . HOH D 2 .   ? -16.50543 4.85204   28.11863  1.000 44.62869 ?  238 HOH B O   1 
HETATM 2978 O O   . HOH D 2 .   ? -22.90292 -11.39619 20.37887  1.000 33.15315 ?  239 HOH B O   1 
HETATM 2979 O O   . HOH D 2 .   ? -4.67721  -15.85939 25.15193  1.000 41.13015 ?  240 HOH B O   1 
HETATM 2980 O O   . HOH D 2 .   ? -29.72865 -2.51304  24.14158  1.000 34.19941 ?  241 HOH B O   1 
HETATM 2981 O O   . HOH D 2 .   ? -14.46035 -12.99154 33.86934  1.000 47.74039 ?  242 HOH B O   1 
HETATM 2982 O O   . HOH D 2 .   ? -7.96042  9.82351   25.59581  1.000 41.37212 ?  243 HOH B O   1 
HETATM 2983 O O   . HOH D 2 .   ? -2.22390  10.48204  24.33536  1.000 43.91237 ?  244 HOH B O   1 
HETATM 2984 O O   . HOH D 2 .   ? -35.42341 -9.09150  34.23116  1.000 35.98792 ?  245 HOH B O   1 
HETATM 2985 O O   . HOH D 2 .   ? -10.52578 0.47431   31.39689  1.000 43.24970 ?  246 HOH B O   1 
HETATM 2986 O O   . HOH D 2 .   ? 4.77214   -3.94625  -1.79844  1.000 35.84166 ?  247 HOH B O   1 
HETATM 2987 O O   . HOH D 2 .   ? -8.61832  -8.37186  0.70586   1.000 35.87302 ?  248 HOH B O   1 
HETATM 2988 O O   . HOH D 2 .   ? -18.40994 -4.24107  40.18833  1.000 40.61984 ?  249 HOH B O   1 
HETATM 2989 O O   . HOH D 2 .   ? -13.41569 0.36884   21.85817  1.000 42.05394 ?  250 HOH B O   1 
HETATM 2990 O O   . HOH D 2 .   ? -1.18184  -4.50614  -3.33547  1.000 39.41653 ?  251 HOH B O   1 
HETATM 2991 O O   . HOH D 2 .   ? -21.33688 -11.02630 40.74442  1.000 43.02714 ?  252 HOH B O   1 
HETATM 2992 O O   . HOH D 2 .   ? -10.60446 -4.32766  38.51946  1.000 52.95854 ?  253 HOH B O   1 
HETATM 2993 O O   . HOH D 2 .   ? -0.41497  13.79848  22.92065  1.000 48.97155 ?  254 HOH B O   1 
HETATM 2994 O O   . HOH D 2 .   ? -15.02326 -16.28804 35.17055  1.000 38.68511 ?  255 HOH B O   1 
HETATM 2995 O O   . HOH D 2 .   ? -33.75428 -12.88353 40.23700  1.000 43.72235 ?  256 HOH B O   1 
HETATM 2996 O O   . HOH D 2 .   ? -18.89352 -11.89095 38.44735  1.000 41.84429 ?  257 HOH B O   1 
HETATM 2997 O O   . HOH D 2 .   ? -5.69820  15.35251  10.04932  1.000 37.74796 ?  258 HOH B O   1 
HETATM 2998 O O   . HOH D 2 .   ? 2.91869   15.44624  20.46669  1.000 41.85646 ?  259 HOH B O   1 
HETATM 2999 O O   . HOH D 2 .   ? -1.02070  -11.10182 17.42502  1.000 41.95929 ?  260 HOH B O   1 
HETATM 3000 O O   . HOH D 2 .   ? -12.91517 -2.18690  20.52044  1.000 36.22762 ?  261 HOH B O   1 
HETATM 3001 O O   . HOH D 2 .   ? -15.06001 4.93335   14.63137  1.000 30.36181 ?  262 HOH B O   1 
HETATM 3002 O O   . HOH D 2 .   ? -6.85076  18.74235  4.71300   1.000 44.43189 ?  263 HOH B O   1 
HETATM 3003 O O   . HOH D 2 .   ? -0.59152  12.34973  -9.60860  1.000 43.92484 ?  264 HOH B O   1 
HETATM 3004 O O   . HOH D 2 .   ? -7.17600  8.55145   -6.25150  1.000 51.92391 ?  265 HOH B O   1 
HETATM 3005 O O   . HOH D 2 .   ? -4.58482  16.99645  8.48097   1.000 39.05302 ?  266 HOH B O   1 
HETATM 3006 O O   . HOH D 2 .   ? -8.94635  17.25036  7.29399   1.000 53.36670 ?  267 HOH B O   1 
HETATM 3007 O O   . HOH D 2 .   ? 7.31702   -2.51923  -1.96927  1.000 44.98864 ?  268 HOH B O   1 
HETATM 3008 O O   . HOH D 2 .   ? -7.60590  -4.08866  18.12316  1.000 38.75027 ?  269 HOH B O   1 
HETATM 3009 O O   . HOH D 2 .   ? -4.62415  15.94271  12.71655  1.000 46.21128 ?  270 HOH B O   1 
HETATM 3010 O O   . HOH D 2 .   ? -1.23296  13.67811  -3.76469  1.000 48.84516 ?  271 HOH B O   1 
HETATM 3011 O O   . HOH D 2 .   ? -6.56831  17.98607  7.27980   1.000 43.38896 ?  272 HOH B O   1 
HETATM 3012 O O   . HOH D 2 .   ? -24.67412 -9.45334  19.36530  1.000 37.79665 ?  273 HOH B O   1 
HETATM 3013 O O   . HOH D 2 .   ? -13.84045 12.34355  1.19422   1.000 45.97559 ?  274 HOH B O   1 
HETATM 3014 O O   . HOH D 2 .   ? -1.99588  13.98236  -10.85506 1.000 43.07724 ?  275 HOH B O   1 
HETATM 3015 O O   . HOH D 2 .   ? -1.39439  14.06882  -6.03207  1.000 46.74238 ?  276 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   . LEU A 15  ? 0.75632 1.25365 0.67152 -0.04436 -0.10747 -0.01973 13  LEU A N   
2    C CA  . LEU A 15  ? 0.66144 1.14387 0.59160 -0.03806 -0.10499 -0.00627 13  LEU A CA  
3    C C   . LEU A 15  ? 0.69782 1.17603 0.64710 -0.04045 -0.11011 -0.00496 13  LEU A C   
4    O O   . LEU A 15  ? 0.73576 1.20439 0.68767 -0.04711 -0.11201 -0.02228 13  LEU A O   
5    C CB  . LEU A 15  ? 0.67161 1.13176 0.59700 -0.03570 -0.09817 -0.01680 13  LEU A CB  
6    C CG  . LEU A 15  ? 0.62340 1.06785 0.56245 -0.02891 -0.09512 -0.00359 13  LEU A CG  
7    C CD1 . LEU A 15  ? 0.62658 1.07730 0.56349 -0.02166 -0.09163 0.01763  13  LEU A CD1 
8    C CD2 . LEU A 15  ? 0.56044 0.97615 0.49888 -0.02854 -0.08819 -0.01861 13  LEU A CD2 
9    N N   . SER A 16  ? 0.68744 1.17210 0.65109 -0.03483 -0.11183 0.01588  14  SER A N   
10   C CA  . SER A 16  ? 0.62921 1.11157 0.61305 -0.03544 -0.11550 0.01935  14  SER A CA  
11   C C   . SER A 16  ? 0.65798 1.11746 0.65099 -0.03520 -0.11191 0.01079  14  SER A C   
12   O O   . SER A 16  ? 0.63020 1.07568 0.62115 -0.02957 -0.10644 0.01403  14  SER A O   
13   C CB  . SER A 16  ? 0.62251 1.11255 0.62036 -0.02701 -0.11623 0.04359  14  SER A CB  
14   O OG  . SER A 16  ? 0.61201 1.10882 0.59983 -0.02193 -0.11381 0.05691  14  SER A OG  
15   N N   . ASP A 17  ? 0.61888 1.07522 0.62301 -0.04168 -0.11501 0.00061  15  ASP A N   
16   C CA  . ASP A 17  ? 0.62126 1.05518 0.63775 -0.04083 -0.11053 -0.00406 15  ASP A CA  
17   C C   . ASP A 17  ? 0.66005 1.08350 0.69049 -0.02962 -0.10513 0.01513  15  ASP A C   
18   O O   . ASP A 17  ? 0.63286 1.02742 0.66607 -0.02521 -0.09647 0.01385  15  ASP A O   
19   C CB  . ASP A 17  ? 0.60279 1.03757 0.63228 -0.04969 -0.11459 -0.01400 15  ASP A CB  
20   C CG  . ASP A 17  ? 0.64126 1.04269 0.68081 -0.04921 -0.10627 -0.02013 15  ASP A CG  
21   O OD1 . ASP A 17  ? 0.68656 1.06668 0.71667 -0.05322 -0.10232 -0.03582 15  ASP A OD1 
22   O OD2 . ASP A 17  ? 0.60582 1.00263 0.66259 -0.04399 -0.10337 -0.00871 15  ASP A OD2 
23   N N   . GLU A 18  ? 0.65941 1.10563 0.69885 -0.02471 -0.11031 0.03275  16  GLU A N   
24   C CA  . GLU A 18  ? 0.63588 1.07209 0.68873 -0.01338 -0.10569 0.05072  16  GLU A CA  
25   C C   . GLU A 18  ? 0.57867 1.00131 0.61974 -0.00729 -0.09997 0.05734  16  GLU A C   
26   O O   . GLU A 18  ? 0.58282 0.98002 0.63014 -0.00079 -0.09233 0.06172  16  GLU A O   
27   C CB  . GLU A 18  ? 0.64331 1.09829 0.70739 -0.00880 -0.11010 0.06710  16  GLU A CB  
28   C CG  . GLU A 18  ? 0.68676 1.13116 0.76826 0.00317  -0.10600 0.08382  16  GLU A CG  
29   C CD  . GLU A 18  ? 0.71204 1.17081 0.80513 0.00845  -0.10920 0.09884  16  GLU A CD  
30   O OE1 . GLU A 18  ? 0.67857 1.14512 0.78618 0.00732  -0.11111 0.09723  16  GLU A OE1 
31   O OE2 . GLU A 18  ? 0.66402 1.12666 0.75217 0.01353  -0.10961 0.11252  16  GLU A OE2 
32   N N   . LYS A 19  ? 0.59072 1.03108 0.61471 -0.00965 -0.10346 0.05842  17  LYS A N   
33   C CA  . LYS A 19  ? 0.59359 1.02339 0.60631 -0.00514 -0.09786 0.06436  17  LYS A CA  
34   C C   . LYS A 19  ? 0.54628 0.94685 0.55191 -0.00722 -0.08942 0.04792  17  LYS A C   
35   O O   . LYS A 19  ? 0.49358 0.87585 0.49732 -0.00221 -0.08260 0.05318  17  LYS A O   
36   C CB  . LYS A 19  ? 0.56404 1.01342 0.55913 -0.00791 -0.09996 0.06684  17  LYS A CB  
37   C CG  . LYS A 19  ? 0.53619 0.98069 0.52446 -0.00237 -0.09508 0.08021  17  LYS A CG  
38   C CD  . LYS A 19  ? 0.60283 1.05341 0.60139 0.00379  -0.09628 0.10320  17  LYS A CD  
39   C CE  . LYS A 19  ? 0.56680 1.00730 0.56271 0.00894  -0.09103 0.11766  17  LYS A CE  
40   N NZ  . LYS A 19  ? 0.59130 1.02890 0.60242 0.01598  -0.09170 0.13953  17  LYS A NZ  
41   N N   . ARG A 20  ? 0.55116 0.94661 0.55418 -0.01465 -0.09004 0.02860  18  ARG A N   
42   C CA  . ARG A 20  ? 0.57177 0.93927 0.56945 -0.01610 -0.08241 0.01350  18  ARG A CA  
43   C C   . ARG A 20  ? 0.47363 0.81347 0.48601 -0.01040 -0.07555 0.01893  18  ARG A C   
44   O O   . ARG A 20  ? 0.48448 0.80465 0.49319 -0.00644 -0.06854 0.01957  18  ARG A O   
45   C CB  . ARG A 20  ? 0.55852 0.92568 0.55201 -0.02545 -0.08536 -0.00741 18  ARG A CB  
46   C CG  . ARG A 20  ? 0.53082 0.87539 0.51363 -0.02708 -0.07885 -0.02420 18  ARG A CG  
47   C CD  . ARG A 20  ? 0.47096 0.80643 0.45504 -0.03565 -0.08091 -0.04376 18  ARG A CD  
48   N NE  . ARG A 20  ? 0.45382 0.76321 0.43174 -0.03512 -0.07384 -0.05726 18  ARG A NE  
49   C CZ  . ARG A 20  ? 0.50866 0.79085 0.49690 -0.03374 -0.06822 -0.05905 18  ARG A CZ  
50   N NH1 . ARG A 20  ? 0.48443 0.76139 0.48894 -0.03301 -0.06819 -0.04954 18  ARG A NH1 
51   N NH2 . ARG A 20  ? 0.47411 0.73515 0.45623 -0.03252 -0.06230 -0.07022 18  ARG A NH2 
52   N N   . ASN A 21  ? 0.48929 0.82907 0.51840 -0.00990 -0.07745 0.02292  19  ASN A N   
53   C CA  . ASN A 21  ? 0.49256 0.80921 0.53512 -0.00378 -0.07102 0.02872  19  ASN A CA  
54   C C   . ASN A 21  ? 0.44908 0.76076 0.49230 0.00492  -0.06798 0.04474  19  ASN A C   
55   O O   . ASN A 21  ? 0.40202 0.68990 0.44628 0.00869  -0.06110 0.04497  19  ASN A O   
56   C CB  . ASN A 21  ? 0.44384 0.76767 0.50441 -0.00391 -0.07379 0.03197  19  ASN A CB  
57   C CG  . ASN A 21  ? 0.46879 0.76832 0.54224 0.00120  -0.06638 0.03360  19  ASN A CG  
58   O OD1 . ASN A 21  ? 0.40005 0.70019 0.48592 0.00901  -0.06527 0.04603  19  ASN A OD1 
59   N ND2 . ASN A 21  ? 0.44822 0.72682 0.51852 -0.00291 -0.06140 0.02093  19  ASN A ND2 
60   N N   . HIS A 22  ? 0.42978 0.76395 0.47161 0.00748  -0.07341 0.05828  20  HIS A N   
61   C CA  . HIS A 22  ? 0.42763 0.75649 0.47196 0.01523  -0.07115 0.07519  20  HIS A CA  
62   C C   . HIS A 22  ? 0.39065 0.70648 0.42112 0.01470  -0.06566 0.07265  20  HIS A C   
63   O O   . HIS A 22  ? 0.35340 0.64914 0.38837 0.01958  -0.06034 0.07933  20  HIS A O   
64   C CB  . HIS A 22  ? 0.39230 0.74935 0.43821 0.01767  -0.07869 0.09150  20  HIS A CB  
65   C CG  . HIS A 22  ? 0.39771 0.74940 0.44608 0.02474  -0.07703 0.10996  20  HIS A CG  
66   N ND1 . HIS A 22  ? 0.39469 0.72542 0.45807 0.03240  -0.07309 0.11861  20  HIS A ND1 
67   C CD2 . HIS A 22  ? 0.44466 0.80907 0.48270 0.02488  -0.07880 0.12151  20  HIS A CD2 
68   C CE1 . HIS A 22  ? 0.38131 0.71011 0.44430 0.03662  -0.07289 0.13456  20  HIS A CE1 
69   N NE2 . HIS A 22  ? 0.41187 0.76152 0.45983 0.03202  -0.07623 0.13753  20  HIS A NE2 
70   N N   . ILE A 23  ? 0.35707 0.68459 0.37108 0.00886  -0.06678 0.06259  21  ILE A N   
71   C CA  . ILE A 23  ? 0.39116 0.70923 0.39260 0.00864  -0.06109 0.05953  21  ILE A CA  
72   C C   . ILE A 23  ? 0.34505 0.63322 0.34961 0.00892  -0.05382 0.04805  21  ILE A C   
73   O O   . ILE A 23  ? 0.31522 0.58708 0.32050 0.01220  -0.04837 0.05309  21  ILE A O   
74   C CB  . ILE A 23  ? 0.36839 0.70736 0.35153 0.00302  -0.06358 0.04927  21  ILE A CB  
75   C CG1 . ILE A 23  ? 0.46352 0.83467 0.44344 0.00187  -0.07188 0.05961  21  ILE A CG1 
76   C CG2 . ILE A 23  ? 0.37012 0.70584 0.34131 0.00396  -0.05786 0.04980  21  ILE A CG2 
77   C CD1 . ILE A 23  ? 0.52003 0.91464 0.48009 -0.00333 -0.07439 0.05042  21  ILE A CD1 
78   N N   . LEU A 24  ? 0.38338 0.66448 0.39022 0.00498  -0.05398 0.03305  22  LEU A N   
79   C CA  . LEU A 24  ? 0.33355 0.58810 0.34221 0.00491  -0.04750 0.02251  22  LEU A CA  
80   C C   . LEU A 24  ? 0.34579 0.58127 0.36805 0.01028  -0.04380 0.03155  22  LEU A C   
81   O O   . LEU A 24  ? 0.33502 0.55080 0.35678 0.01220  -0.03804 0.02992  22  LEU A O   
82   C CB  . LEU A 24  ? 0.35720 0.60835 0.36605 -0.00106 -0.04892 0.00585  22  LEU A CB  
83   C CG  . LEU A 24  ? 0.44803 0.71268 0.44264 -0.00673 -0.05185 -0.00770 22  LEU A CG  
84   C CD1 . LEU A 24  ? 0.47940 0.74442 0.47866 -0.01346 -0.05586 -0.02026 22  LEU A CD1 
85   C CD2 . LEU A 24  ? 0.35921 0.61120 0.34305 -0.00592 -0.04590 -0.01732 22  LEU A CD2 
86   N N   . THR A 25  ? 0.36906 0.61118 0.40359 0.01316  -0.04708 0.04113  23  THR A N   
87   C CA  . THR A 25  ? 0.35240 0.57632 0.39947 0.01890  -0.04321 0.04800  23  THR A CA  
88   C C   . THR A 25  ? 0.31258 0.53136 0.36016 0.02420  -0.04167 0.06202  23  THR A C   
89   O O   . THR A 25  ? 0.34601 0.54424 0.39930 0.02780  -0.03708 0.06410  23  THR A O   
90   C CB  . THR A 25  ? 0.32224 0.55444 0.38380 0.02112  -0.04634 0.05220  23  THR A CB  
91   O OG1 . THR A 25  ? 0.32526 0.58244 0.38812 0.02205  -0.05306 0.06241  23  THR A OG1 
92   C CG2 . THR A 25  ? 0.36679 0.59900 0.43057 0.01514  -0.04663 0.03865  23  THR A CG2 
93   N N   . THR A 26  ? 0.31152 0.54874 0.35334 0.02427  -0.04561 0.07196  24  THR A N   
94   C CA  . THR A 26  ? 0.31562 0.54736 0.35691 0.02766  -0.04396 0.08539  24  THR A CA  
95   C C   . THR A 26  ? 0.33035 0.54658 0.36300 0.02533  -0.03805 0.07831  24  THR A C   
96   O O   . THR A 26  ? 0.32805 0.52643 0.36545 0.02791  -0.03445 0.08388  24  THR A O   
97   C CB  . THR A 26  ? 0.34853 0.60589 0.38351 0.02707  -0.04928 0.09768  24  THR A CB  
98   O OG1 . THR A 26  ? 0.38947 0.66211 0.43429 0.03001  -0.05527 0.10600  24  THR A OG1 
99   C CG2 . THR A 26  ? 0.37633 0.62814 0.41091 0.02935  -0.04743 0.11275  24  THR A CG2 
100  N N   . ALA A 27  ? 0.32205 0.54480 0.34272 0.02053  -0.03715 0.06537  25  ALA A N   
101  C CA  . ALA A 27  ? 0.32821 0.53902 0.34131 0.01899  -0.03159 0.05832  25  ALA A CA  
102  C C   . ALA A 27  ? 0.30724 0.49222 0.32775 0.02025  -0.02708 0.05118  25  ALA A C   
103  O O   . ALA A 27  ? 0.27155 0.44222 0.29337 0.02151  -0.02318 0.05445  25  ALA A O   
104  C CB  . ALA A 27  ? 0.25968 0.48337 0.25927 0.01473  -0.03170 0.04483  25  ALA A CB  
105  N N   . LEU A 28  ? 0.30070 0.48081 0.32643 0.01946  -0.02784 0.04217  26  LEU A N   
106  C CA  . LEU A 28  ? 0.33539 0.49342 0.36708 0.02028  -0.02361 0.03554  26  LEU A CA  
107  C C   . LEU A 28  ? 0.31802 0.46195 0.35863 0.02484  -0.02162 0.04548  26  LEU A C   
108  O O   . LEU A 28  ? 0.31196 0.43820 0.35330 0.02531  -0.01747 0.04224  26  LEU A O   
109  C CB  . LEU A 28  ? 0.34874 0.50755 0.38609 0.01838  -0.02522 0.02747  26  LEU A CB  
110  C CG  . LEU A 28  ? 0.36389 0.52622 0.39293 0.01298  -0.02571 0.01347  26  LEU A CG  
111  C CD1 . LEU A 28  ? 0.38532 0.55377 0.42028 0.00943  -0.02900 0.00745  26  LEU A CD1 
112  C CD2 . LEU A 28  ? 0.34680 0.49055 0.37250 0.01251  -0.02058 0.00525  26  LEU A CD2 
113  N N   . ASN A 29  ? 0.28519 0.43662 0.33247 0.02828  -0.02476 0.05757  27  ASN A N   
114  C CA  . ASN A 29  ? 0.32492 0.46091 0.38178 0.03306  -0.02307 0.06565  27  ASN A CA  
115  C C   . ASN A 29  ? 0.37324 0.50143 0.42622 0.03241  -0.02122 0.07240  27  ASN A C   
116  O O   . ASN A 29  ? 0.36885 0.47812 0.42577 0.03366  -0.01815 0.07222  27  ASN A O   
117  C CB  . ASN A 29  ? 0.29989 0.44570 0.36683 0.03783  -0.02713 0.07660  27  ASN A CB  
118  C CG  . ASN A 29  ? 0.32347 0.47137 0.39888 0.03971  -0.02741 0.07063  27  ASN A CG  
119  O OD1 . ASN A 29  ? 0.40752 0.54317 0.48352 0.03862  -0.02361 0.06049  27  ASN A OD1 
120  N ND2 . ASN A 29  ? 0.35266 0.51857 0.43457 0.04201  -0.03209 0.07726  27  ASN A ND2 
121  N N   . LEU A 30  ? 0.32528 0.46923 0.37019 0.02986  -0.02304 0.07796  28  LEU A N   
122  C CA  . LEU A 30  ? 0.34802 0.48816 0.38838 0.02781  -0.02076 0.08354  28  LEU A CA  
123  C C   . LEU A 30  ? 0.37923 0.50806 0.41427 0.02516  -0.01612 0.07130  28  LEU A C   
124  O O   . LEU A 30  ? 0.36731 0.48207 0.40470 0.02464  -0.01348 0.07346  28  LEU A O   
125  C CB  . LEU A 30  ? 0.35066 0.51441 0.38223 0.02548  -0.02317 0.09111  28  LEU A CB  
126  C CG  . LEU A 30  ? 0.39469 0.57042 0.43160 0.02800  -0.02806 0.10745  28  LEU A CG  
127  C CD1 . LEU A 30  ? 0.35744 0.56158 0.38329 0.02537  -0.03111 0.11127  28  LEU A CD1 
128  C CD2 . LEU A 30  ? 0.42441 0.58678 0.46914 0.02920  -0.02743 0.12180  28  LEU A CD2 
129  N N   . PHE A 31  ? 0.35246 0.48715 0.38089 0.02333  -0.01543 0.05852  29  PHE A N   
130  C CA  . PHE A 31  ? 0.34180 0.46546 0.36641 0.02172  -0.01127 0.04744  29  PHE A CA  
131  C C   . PHE A 31  ? 0.42098 0.52325 0.45328 0.02326  -0.00914 0.04491  29  PHE A C   
132  O O   . PHE A 31  ? 0.37592 0.46694 0.40765 0.02242  -0.00612 0.04266  29  PHE A O   
133  C CB  . PHE A 31  ? 0.33101 0.46161 0.34927 0.01992  -0.01141 0.03410  29  PHE A CB  
134  C CG  . PHE A 31  ? 0.31393 0.46530 0.32205 0.01816  -0.01273 0.03294  29  PHE A CG  
135  C CD1 . PHE A 31  ? 0.38979 0.55098 0.39294 0.01786  -0.01137 0.04100  29  PHE A CD1 
136  C CD2 . PHE A 31  ? 0.36447 0.52662 0.36784 0.01632  -0.01534 0.02350  29  PHE A CD2 
137  C CE1 . PHE A 31  ? 0.36141 0.54431 0.35390 0.01646  -0.01209 0.03956  29  PHE A CE1 
138  C CE2 . PHE A 31  ? 0.34678 0.52891 0.33943 0.01469  -0.01664 0.02082  29  PHE A CE2 
139  C CZ  . PHE A 31  ? 0.37462 0.56786 0.36124 0.01512  -0.01474 0.02880  29  PHE A CZ  
140  N N   . ASP A 32  ? 0.39667 0.49495 0.43610 0.02555  -0.01066 0.04486  30  ASP A N   
141  C CA  . ASP A 32  ? 0.39969 0.47997 0.44544 0.02735  -0.00833 0.04155  30  ASP A CA  
142  C C   . ASP A 32  ? 0.41343 0.48132 0.46349 0.02873  -0.00753 0.04934  30  ASP A C   
143  O O   . ASP A 32  ? 0.42680 0.47971 0.47807 0.02857  -0.00502 0.04510  30  ASP A O   
144  C CB  . ASP A 32  ? 0.36597 0.44854 0.41894 0.02996  -0.00977 0.04055  30  ASP A CB  
145  C CG  . ASP A 32  ? 0.48616 0.55461 0.54284 0.03086  -0.00659 0.03337  30  ASP A CG  
146  O OD1 . ASP A 32  ? 0.50608 0.57261 0.55890 0.02797  -0.00497 0.02458  30  ASP A OD1 
147  O OD2 . ASP A 32  ? 0.50762 0.56695 0.57114 0.03466  -0.00567 0.03661  30  ASP A OD2 
148  N N   . GLN A 33  ? 0.40878 0.48298 0.46091 0.02948  -0.00992 0.06086  31  GLN A N   
149  C CA  . GLN A 33  ? 0.44559 0.50805 0.50288 0.02993  -0.00997 0.06979  31  GLN A CA  
150  C C   . GLN A 33  ? 0.47768 0.54063 0.52963 0.02531  -0.00849 0.07199  31  GLN A C   
151  O O   . GLN A 33  ? 0.52600 0.57441 0.58087 0.02383  -0.00722 0.07232  31  GLN A O   
152  C CB  . GLN A 33  ? 0.48865 0.55857 0.55188 0.03280  -0.01363 0.08303  31  GLN A CB  
153  C CG  . GLN A 33  ? 0.48186 0.53515 0.55594 0.03671  -0.01434 0.08965  31  GLN A CG  
154  C CD  . GLN A 33  ? 0.50133 0.56377 0.58176 0.04004  -0.01834 0.10403  31  GLN A CD  
155  O OE1 . GLN A 33  ? 0.47538 0.55527 0.55522 0.04201  -0.02075 0.10569  31  GLN A OE1 
156  N NE2 . GLN A 33  ? 0.55420 0.60526 0.64119 0.04032  -0.01953 0.11509  31  GLN A NE2 
157  N N   . PHE A 34  ? 0.46592 0.54665 0.51018 0.02291  -0.00858 0.07308  32  PHE A N   
158  C CA  . PHE A 34  ? 0.44559 0.53174 0.48591 0.01906  -0.00704 0.07769  32  PHE A CA  
159  C C   . PHE A 34  ? 0.48921 0.58456 0.52086 0.01737  -0.00413 0.06759  32  PHE A C   
160  O O   . PHE A 34  ? 0.54348 0.64642 0.57220 0.01472  -0.00231 0.07112  32  PHE A O   
161  C CB  . PHE A 34  ? 0.50314 0.60485 0.54281 0.01805  -0.00938 0.09205  32  PHE A CB  
162  C CG  . PHE A 34  ? 0.53168 0.62461 0.58101 0.02031  -0.01255 0.10386  32  PHE A CG  
163  C CD1 . PHE A 34  ? 0.53718 0.61180 0.59443 0.01899  -0.01243 0.10958  32  PHE A CD1 
164  C CD2 . PHE A 34  ? 0.48487 0.58801 0.53602 0.02378  -0.01597 0.10942  32  PHE A CD2 
165  C CE1 . PHE A 34  ? 0.51352 0.57782 0.58060 0.02175  -0.01530 0.11992  32  PHE A CE1 
166  C CE2 . PHE A 34  ? 0.48173 0.57661 0.54317 0.02702  -0.01887 0.12094  32  PHE A CE2 
167  C CZ  . PHE A 34  ? 0.52373 0.59806 0.59329 0.02633  -0.01837 0.12599  32  PHE A CZ  
168  N N   . GLY A 35  ? 0.47492 0.57002 0.50331 0.01887  -0.00352 0.05559  33  GLY A N   
169  C CA  . GLY A 35  ? 0.41272 0.51360 0.43422 0.01809  -0.00079 0.04554  33  GLY A CA  
170  C C   . GLY A 35  ? 0.40763 0.52953 0.42074 0.01779  -0.00128 0.04406  33  GLY A C   
171  O O   . GLY A 35  ? 0.39660 0.53173 0.40818 0.01733  -0.00357 0.05338  33  GLY A O   
172  N N   . PHE A 36  ? 0.39734 0.52230 0.40474 0.01818  0.00092  0.03198  34  PHE A N   
173  C CA  . PHE A 36  ? 0.46075 0.60398 0.45917 0.01810  0.00045  0.02636  34  PHE A CA  
174  C C   . PHE A 36  ? 0.47143 0.63339 0.46373 0.01741  0.00251  0.03276  34  PHE A C   
175  O O   . PHE A 36  ? 0.48650 0.66681 0.47287 0.01661  0.00052  0.03761  34  PHE A O   
176  C CB  . PHE A 36  ? 0.41440 0.55170 0.40987 0.01907  0.00218  0.01052  34  PHE A CB  
177  C CG  . PHE A 36  ? 0.41065 0.53667 0.41023 0.01861  -0.00040 0.00447  34  PHE A CG  
178  C CD1 . PHE A 36  ? 0.36868 0.50514 0.36572 0.01723  -0.00424 0.00245  34  PHE A CD1 
179  C CD2 . PHE A 36  ? 0.36394 0.47107 0.36989 0.01913  0.00089  0.00119  34  PHE A CD2 
180  C CE1 . PHE A 36  ? 0.38565 0.51392 0.38769 0.01614  -0.00656 -0.00242 34  PHE A CE1 
181  C CE2 . PHE A 36  ? 0.34816 0.44713 0.35816 0.01826  -0.00103 -0.00342 34  PHE A CE2 
182  C CZ  . PHE A 36  ? 0.33572 0.44521 0.34433 0.01664  -0.00463 -0.00525 34  PHE A CZ  
183  N N   . GLN A 37  ? 0.50367 0.66369 0.49727 0.01755  0.00650  0.03326  35  GLN A N   
184  C CA  . GLN A 37  ? 0.50798 0.68864 0.49605 0.01682  0.00929  0.03891  35  GLN A CA  
185  C C   . GLN A 37  ? 0.51148 0.69925 0.50272 0.01384  0.00747  0.05718  35  GLN A C   
186  O O   . GLN A 37  ? 0.57561 0.78483 0.56096 0.01258  0.00872  0.06422  35  GLN A O   
187  C CB  . GLN A 37  ? 0.56710 0.74593 0.55727 0.01798  0.01416  0.03460  35  GLN A CB  
188  C CG  . GLN A 37  ? 0.57420 0.73702 0.56622 0.02095  0.01530  0.02007  35  GLN A CG  
189  C CD  . GLN A 37  ? 0.55691 0.73079 0.54132 0.02444  0.01848  0.00661  35  GLN A CD  
190  O OE1 . GLN A 37  ? 0.59823 0.79277 0.57415 0.02463  0.01951  0.00625  35  GLN A OE1 
191  N NE2 . GLN A 37  ? 0.55049 0.71065 0.53777 0.02744  0.02001  -0.00466 35  GLN A NE2 
192  N N   . HIS A 38  ? 0.54450 0.71466 0.54503 0.01278  0.00473  0.06497  36  HIS A N   
193  C CA  . HIS A 38  ? 0.53250 0.70499 0.53793 0.01022  0.00234  0.08249  36  HIS A CA  
194  C C   . HIS A 38  ? 0.51775 0.70588 0.51856 0.01070  -0.00136 0.08955  36  HIS A C   
195  O O   . HIS A 38  ? 0.54656 0.74558 0.54821 0.00855  -0.00266 0.10518  36  HIS A O   
196  C CB  . HIS A 38  ? 0.57663 0.72379 0.59304 0.01016  0.00025  0.08550  36  HIS A CB  
197  C CG  . HIS A 38  ? 0.67338 0.81540 0.69753 0.00667  -0.00070 0.10094  36  HIS A CG  
198  N ND1 . HIS A 38  ? 0.67031 0.79562 0.70336 0.00715  -0.00413 0.10851  36  HIS A ND1 
199  C CD2 . HIS A 38  ? 0.69555 0.84573 0.72103 0.00244  0.00137  0.10985  36  HIS A CD2 
200  C CE1 . HIS A 38  ? 0.68966 0.81148 0.72898 0.00305  -0.00454 0.12139  36  HIS A CE1 
201  N NE2 . HIS A 38  ? 0.73129 0.86867 0.76633 -0.00041 -0.00133 0.12295  36  HIS A NE2 
202  N N   . ILE A 39  ? 0.53221 0.72212 0.52888 0.01301  -0.00355 0.07942  37  ILE A N   
203  C CA  . ILE A 39  ? 0.48405 0.68717 0.47836 0.01352  -0.00828 0.08611  37  ILE A CA  
204  C C   . ILE A 39  ? 0.47700 0.70564 0.45758 0.01297  -0.00790 0.07931  37  ILE A C   
205  O O   . ILE A 39  ? 0.45283 0.68096 0.42777 0.01383  -0.00654 0.06254  37  ILE A O   
206  C CB  . ILE A 39  ? 0.42392 0.61298 0.42475 0.01590  -0.01175 0.08054  37  ILE A CB  
207  C CG1 . ILE A 39  ? 0.39819 0.56402 0.41186 0.01714  -0.01213 0.08760  37  ILE A CG1 
208  C CG2 . ILE A 39  ? 0.40934 0.61564 0.40801 0.01649  -0.01695 0.08699  37  ILE A CG2 
209  C CD1 . ILE A 39  ? 0.43223 0.60099 0.45207 0.01731  -0.01522 0.10644  37  ILE A CD1 
210  N N   . SER A 40  ? 0.49604 0.74681 0.47118 0.01146  -0.00936 0.09224  38  SER A N   
211  C CA  . SER A 40  ? 0.47259 0.75038 0.43307 0.01076  -0.00877 0.08616  38  SER A CA  
212  C C   . SER A 40  ? 0.47625 0.76599 0.43219 0.01096  -0.01488 0.08391  38  SER A C   
213  O O   . SER A 40  ? 0.46064 0.74279 0.42554 0.01183  -0.01966 0.09257  38  SER A O   
214  C CB  . SER A 40  ? 0.50427 0.80398 0.45962 0.00847  -0.00665 0.10163  38  SER A CB  
215  O OG  . SER A 40  ? 0.47682 0.78612 0.43490 0.00736  -0.01173 0.12093  38  SER A OG  
216  N N   . ILE A 41  ? 0.48925 0.79851 0.43140 0.01029  -0.01468 0.07128  39  ILE A N   
217  C CA  . ILE A 41  ? 0.45389 0.78229 0.38899 0.00916  -0.02094 0.07033  39  ILE A CA  
218  C C   . ILE A 41  ? 0.50384 0.84813 0.44092 0.00853  -0.02534 0.09331  39  ILE A C   
219  O O   . ILE A 41  ? 0.44588 0.79396 0.38734 0.00889  -0.03177 0.09908  39  ILE A O   
220  C CB  . ILE A 41  ? 0.46543 0.81588 0.38316 0.00799  -0.01948 0.05450  39  ILE A CB  
221  C CG1 . ILE A 41  ? 0.52170 0.85411 0.43910 0.00899  -0.01644 0.03113  39  ILE A CG1 
222  C CG2 . ILE A 41  ? 0.51140 0.88696 0.42002 0.00579  -0.02654 0.05566  39  ILE A CG2 
223  C CD1 . ILE A 41  ? 0.48814 0.79219 0.42004 0.00951  -0.01869 0.02813  39  ILE A CD1 
224  N N   . MET A 42  ? 0.48961 0.84530 0.42386 0.00752  -0.02209 0.10746  40  MET A N   
225  C CA  . MET A 42  ? 0.49991 0.87214 0.43555 0.00663  -0.02649 0.13075  40  MET A CA  
226  C C   . MET A 42  ? 0.47228 0.82205 0.42577 0.00886  -0.03057 0.14335  40  MET A C   
227  O O   . MET A 42  ? 0.47903 0.83888 0.43587 0.00988  -0.03690 0.15615  40  MET A O   
228  C CB  . MET A 42  ? 0.53993 0.92551 0.47164 0.00438  -0.02170 0.14480  40  MET A CB  
229  C CG  . MET A 42  ? 0.52833 0.93630 0.45933 0.00228  -0.02451 0.16032  40  MET A CG  
230  S SD  . MET A 42  ? 0.75662 1.19546 0.67039 0.00100  -0.02537 0.14346  40  MET A SD  
231  C CE  . MET A 42  ? 0.61318 1.04887 0.51430 0.00223  -0.01842 0.11776  40  MET A CE  
232  N N   . ARG A 43  ? 0.50191 0.82189 0.46695 0.01008  -0.02704 0.13927  41  ARG A N   
233  C CA  . ARG A 43  ? 0.52242 0.81855 0.50421 0.01286  -0.02991 0.14789  41  ARG A CA  
234  C C   . ARG A 43  ? 0.48395 0.77710 0.46938 0.01553  -0.03458 0.13838  41  ARG A C   
235  O O   . ARG A 43  ? 0.45457 0.74887 0.44888 0.01822  -0.03979 0.15040  41  ARG A O   
236  C CB  . ARG A 43  ? 0.44243 0.71017 0.43278 0.01289  -0.02476 0.14248  41  ARG A CB  
237  C CG  . ARG A 43  ? 0.55237 0.79294 0.55825 0.01607  -0.02647 0.14496  41  ARG A CG  
238  C CD  . ARG A 43  ? 0.57638 0.80744 0.59272 0.01576  -0.02733 0.16507  41  ARG A CD  
239  N NE  . ARG A 43  ? 0.56710 0.76929 0.59790 0.01925  -0.02800 0.16413  41  ARG A NE  
240  C CZ  . ARG A 43  ? 0.54380 0.72268 0.58012 0.01822  -0.02431 0.15806  41  ARG A CZ  
241  N NH1 . ARG A 43  ? 0.59280 0.77337 0.62298 0.01395  -0.01986 0.15308  41  ARG A NH1 
242  N NH2 . ARG A 43  ? 0.55629 0.71099 0.60458 0.02179  -0.02511 0.15661  41  ARG A NH2 
243  N N   . ILE A 44  ? 0.46332 0.75388 0.44265 0.01478  -0.03289 0.11739  42  ILE A N   
244  C CA  . ILE A 44  ? 0.44352 0.73325 0.42646 0.01594  -0.03726 0.10804  42  ILE A CA  
245  C C   . ILE A 44  ? 0.47794 0.79644 0.45554 0.01529  -0.04407 0.11642  42  ILE A C   
246  O O   . ILE A 44  ? 0.42895 0.74884 0.41610 0.01764  -0.04932 0.12235  42  ILE A O   
247  C CB  . ILE A 44  ? 0.43664 0.71952 0.41310 0.01406  -0.03429 0.08473  42  ILE A CB  
248  C CG1 . ILE A 44  ? 0.40892 0.66230 0.39367 0.01546  -0.02881 0.07867  42  ILE A CG1 
249  C CG2 . ILE A 44  ? 0.34450 0.63159 0.32331 0.01343  -0.03931 0.07545  42  ILE A CG2 
250  C CD1 . ILE A 44  ? 0.38519 0.63168 0.36263 0.01394  -0.02429 0.05932  42  ILE A CD1 
251  N N   . ILE A 45  ? 0.46405 0.80769 0.42664 0.01241  -0.04404 0.11814  43  ILE A N   
252  C CA  . ILE A 45  ? 0.48726 0.86183 0.44168 0.01100  -0.05072 0.12433  43  ILE A CA  
253  C C   . ILE A 45  ? 0.50571 0.88641 0.47034 0.01387  -0.05550 0.14987  43  ILE A C   
254  O O   . ILE A 45  ? 0.48055 0.87293 0.44955 0.01448  -0.06108 0.15442  43  ILE A O   
255  C CB  . ILE A 45  ? 0.51640 0.91614 0.45094 0.00746  -0.04833 0.11904  43  ILE A CB  
256  C CG1 . ILE A 45  ? 0.50758 0.90882 0.43145 0.00500  -0.04724 0.09252  43  ILE A CG1 
257  C CG2 . ILE A 45  ? 0.55887 0.98338 0.49016 0.00574  -0.05133 0.13220  43  ILE A CG2 
258  C CD1 . ILE A 45  ? 0.58401 1.01310 0.48788 0.00215  -0.04553 0.08519  43  ILE A CD1 
259  N N   . THR A 46  ? 0.45800 0.82585 0.42950 0.01516  -0.05202 0.16500  44  THR A N   
260  C CA  . THR A 46  ? 0.48978 0.85341 0.47526 0.01760  -0.05446 0.18594  44  THR A CA  
261  C C   . THR A 46  ? 0.52460 0.86810 0.52732 0.02343  -0.05799 0.18811  44  THR A C   
262  O O   . THR A 46  ? 0.54843 0.89665 0.56033 0.02603  -0.06216 0.19607  44  THR A O   
263  C CB  . THR A 46  ? 0.52684 0.88100 0.51593 0.01606  -0.04970 0.20012  44  THR A CB  
264  O OG1 . THR A 46  ? 0.57789 0.95339 0.55190 0.01107  -0.04574 0.19680  44  THR A OG1 
265  C CG2 . THR A 46  ? 0.50467 0.85576 0.50767 0.01768  -0.05222 0.22054  44  THR A CG2 
266  N N   . GLU A 47  ? 0.48491 0.80062 0.49419 0.02473  -0.05349 0.17658  45  GLU A N   
267  C CA  . GLU A 47  ? 0.50918 0.80385 0.53491 0.02994  -0.05459 0.17405  45  GLU A CA  
268  C C   . GLU A 47  ? 0.52320 0.83414 0.54931 0.03076  -0.05983 0.16611  45  GLU A C   
269  O O   . GLU A 47  ? 0.56722 0.87786 0.60693 0.03594  -0.06396 0.17445  45  GLU A O   
270  C CB  . GLU A 47  ? 0.52167 0.78680 0.55090 0.02971  -0.04805 0.15846  45  GLU A CB  
271  C CG  . GLU A 47  ? 0.56453 0.81365 0.59331 0.02770  -0.04281 0.16326  45  GLU A CG  
272  C CD  . GLU A 47  ? 0.61265 0.83399 0.65756 0.03170  -0.04180 0.17161  45  GLU A CD  
273  O OE1 . GLU A 47  ? 0.61519 0.82280 0.67043 0.03631  -0.04241 0.16561  45  GLU A OE1 
274  O OE2 . GLU A 47  ? 0.63557 0.84868 0.68273 0.02985  -0.04009 0.18313  45  GLU A OE2 
275  N N   . ALA A 48  ? 0.48399 0.80988 0.49605 0.02570  -0.05992 0.15000  46  ALA A N   
276  C CA  . ALA A 48  ? 0.49100 0.83222 0.50370 0.02488  -0.06530 0.14134  46  ALA A CA  
277  C C   . ALA A 48  ? 0.53174 0.90592 0.54040 0.02457  -0.07317 0.15497  46  ALA A C   
278  O O   . ALA A 48  ? 0.51281 0.89846 0.52570 0.02406  -0.07780 0.15050  46  ALA A O   
279  C CB  . ALA A 48  ? 0.46478 0.80644 0.46515 0.01914  -0.06284 0.11767  46  ALA A CB  
280  N N   . LYS A 49  ? 0.54067 0.92145 0.54315 0.02323  -0.07106 0.16768  47  LYS A N   
281  C CA  . LYS A 49  ? 0.51295 0.91608 0.51212 0.02133  -0.07407 0.17753  47  LYS A CA  
282  C C   . LYS A 49  ? 0.57381 1.00107 0.55894 0.01568  -0.07729 0.16204  47  LYS A C   
283  O O   . LYS A 49  ? 0.54661 0.98837 0.53525 0.01524  -0.08242 0.16343  47  LYS A O   
284  C CB  . LYS A 49  ? 0.58669 0.98520 0.60409 0.02701  -0.07761 0.19267  47  LYS A CB  
285  C CG  . LYS A 49  ? 0.60598 0.97478 0.64037 0.03362  -0.07501 0.20167  47  LYS A CG  
286  C CD  . LYS A 49  ? 0.66801 1.03294 0.72035 0.04006  -0.07825 0.21453  47  LYS A CD  
287  C CE  . LYS A 49  ? 0.66547 1.03465 0.72056 0.04043  -0.07844 0.23440  47  LYS A CE  
288  N NZ  . LYS A 49  ? 0.67279 1.01337 0.74292 0.04577  -0.07566 0.24619  47  LYS A NZ  
289  N N   . ILE A 50  ? 0.59487 1.02604 0.56405 0.01130  -0.07405 0.14680  48  ILE A N   
290  C CA  . ILE A 50  ? 0.60632 1.05730 0.56048 0.00551  -0.07605 0.12942  48  ILE A CA  
291  C C   . ILE A 50  ? 0.60856 1.07352 0.54642 0.00232  -0.07130 0.12837  48  ILE A C   
292  O O   . ILE A 50  ? 0.62352 1.07876 0.55990 0.00366  -0.06562 0.13359  48  ILE A O   
293  C CB  . ILE A 50  ? 0.59510 1.03540 0.54705 0.00357  -0.07660 0.10713  48  ILE A CB  
294  C CG1 . ILE A 50  ? 0.61547 1.07370 0.55696 -0.00262 -0.08061 0.08985  48  ILE A CG1 
295  C CG2 . ILE A 50  ? 0.51956 0.94577 0.46357 0.00390  -0.07027 0.09849  48  ILE A CG2 
296  C CD1 . ILE A 50  ? 0.58881 1.04662 0.51377 -0.00675 -0.07702 0.06779  48  ILE A CD1 
297  N N   . ALA A 51  ? 0.66889 1.15778 0.59531 -0.00198 -0.07354 0.12179  49  ALA A N   
298  C CA  . ALA A 51  ? 0.61957 1.12584 0.53177 -0.00458 -0.06910 0.12147  49  ALA A CA  
299  C C   . ALA A 51  ? 0.60876 1.10790 0.50890 -0.00580 -0.06328 0.10172  49  ALA A C   
300  O O   . ALA A 51  ? 0.61076 1.10238 0.50696 -0.00738 -0.06461 0.08151  49  ALA A O   
301  C CB  . ALA A 51  ? 0.64749 1.18164 0.55075 -0.00863 -0.07334 0.11822  49  ALA A CB  
302  N N   . LYS A 52  ? 0.59356 1.09505 0.48906 -0.00509 -0.05671 0.10801  50  LYS A N   
303  C CA  . LYS A 52  ? 0.61381 1.11089 0.49834 -0.00535 -0.05014 0.09077  50  LYS A CA  
304  C C   . LYS A 52  ? 0.61833 1.12470 0.48978 -0.00837 -0.05127 0.06567  50  LYS A C   
305  O O   . LYS A 52  ? 0.60543 1.09675 0.47341 -0.00808 -0.04934 0.04647  50  LYS A O   
306  C CB  . LYS A 52  ? 0.59644 1.10643 0.47652 -0.00539 -0.04374 0.10100  50  LYS A CB  
307  C CG  . LYS A 52  ? 0.57287 1.06918 0.45097 -0.00350 -0.03627 0.09430  50  LYS A CG  
308  C CD  . LYS A 52  ? 0.67542 1.18850 0.55029 -0.00419 -0.03035 0.10436  50  LYS A CD  
309  C CE  . LYS A 52  ? 0.67185 1.16845 0.55369 -0.00245 -0.02446 0.11198  50  LYS A CE  
310  N NZ  . LYS A 52  ? 0.67826 1.19066 0.56279 -0.00409 -0.02081 0.12955  50  LYS A NZ  
311  N N   . GLN A 53  ? 0.60238 1.13297 0.46659 -0.01140 -0.05426 0.06524  51  GLN A N   
312  C CA  . GLN A 53  ? 0.62528 1.16497 0.47604 -0.01444 -0.05443 0.04095  51  GLN A CA  
313  C C   . GLN A 53  ? 0.57783 1.10368 0.43194 -0.01674 -0.06030 0.02534  51  GLN A C   
314  O O   . GLN A 53  ? 0.57238 1.08987 0.41931 -0.01827 -0.05896 0.00197  51  GLN A O   
315  C CB  . GLN A 53  ? 0.65959 1.22975 0.50174 -0.01738 -0.05660 0.04511  51  GLN A CB  
316  C CG  . GLN A 53  ? 0.73551 1.32206 0.56819 -0.01641 -0.04945 0.04628  51  GLN A CG  
317  C CD  . GLN A 53  ? 0.75880 1.37620 0.58725 -0.01877 -0.05196 0.06010  51  GLN A CD  
318  O OE1 . GLN A 53  ? 0.77292 1.39573 0.61010 -0.01940 -0.05726 0.07891  51  GLN A OE1 
319  N NE2 . GLN A 53  ? 0.79711 1.43532 0.61258 -0.01970 -0.04812 0.05096  51  GLN A NE2 
320  N N   . SER A 54  ? 0.56343 1.08587 0.42994 -0.01687 -0.06666 0.03814  52  SER A N   
321  C CA  . SER A 54  ? 0.55905 1.06911 0.43157 -0.01938 -0.07230 0.02518  52  SER A CA  
322  C C   . SER A 54  ? 0.57413 1.05740 0.45058 -0.01733 -0.06877 0.01409  52  SER A C   
323  O O   . SER A 54  ? 0.58204 1.05487 0.45615 -0.02044 -0.07003 -0.00701 52  SER A O   
324  C CB  . SER A 54  ? 0.60467 1.11756 0.49200 -0.01873 -0.07906 0.04302  52  SER A CB  
325  O OG  . SER A 54  ? 0.66414 1.20226 0.54830 -0.02035 -0.08242 0.05442  52  SER A OG  
326  N N   . PHE A 55  ? 0.55470 1.02589 0.43779 -0.01245 -0.06452 0.02829  53  PHE A N   
327  C CA  . PHE A 55  ? 0.54327 0.98999 0.43060 -0.01023 -0.06148 0.01958  53  PHE A CA  
328  C C   . PHE A 55  ? 0.52614 0.96764 0.40058 -0.01113 -0.05586 -0.00355 53  PHE A C   
329  O O   . PHE A 55  ? 0.47863 0.90249 0.35474 -0.01229 -0.05596 -0.02113 53  PHE A O   
330  C CB  . PHE A 55  ? 0.54068 0.97722 0.43588 -0.00510 -0.05756 0.03947  53  PHE A CB  
331  C CG  . PHE A 55  ? 0.54737 0.95001 0.45189 -0.00262 -0.05058 0.03050  53  PHE A CG  
332  C CD1 . PHE A 55  ? 0.51823 0.91459 0.41456 -0.00132 -0.04272 0.02047  53  PHE A CD1 
333  C CD2 . PHE A 55  ? 0.50280 0.88081 0.42499 -0.00125 -0.05149 0.03254  53  PHE A CD2 
334  C CE1 . PHE A 55  ? 0.51995 0.88614 0.42557 0.00102  -0.03670 0.01302  53  PHE A CE1 
335  C CE2 . PHE A 55  ? 0.48333 0.83152 0.41350 0.00074  -0.04521 0.02483  53  PHE A CE2 
336  C CZ  . PHE A 55  ? 0.50054 0.84256 0.42258 0.00180  -0.03810 0.01547  53  PHE A CZ  
337  N N   . TYR A 56  ? 0.56985 1.02573 0.43322 -0.01033 -0.05050 -0.00377 54  TYR A N   
338  C CA  . TYR A 56  ? 0.54935 1.00043 0.40214 -0.00968 -0.04434 -0.02535 54  TYR A CA  
339  C C   . TYR A 56  ? 0.54194 0.99463 0.38851 -0.01423 -0.04824 -0.04786 54  TYR A C   
340  O O   . TYR A 56  ? 0.53488 0.97290 0.37753 -0.01373 -0.04473 -0.06890 54  TYR A O   
341  C CB  . TYR A 56  ? 0.58187 1.04974 0.42675 -0.00722 -0.03745 -0.01850 54  TYR A CB  
342  C CG  . TYR A 56  ? 0.56378 1.02196 0.41495 -0.00307 -0.03174 -0.00322 54  TYR A CG  
343  C CD1 . TYR A 56  ? 0.57150 1.00924 0.42359 0.00014  -0.02614 -0.01450 54  TYR A CD1 
344  C CD2 . TYR A 56  ? 0.61338 1.08152 0.47054 -0.00258 -0.03195 0.02254  54  TYR A CD2 
345  C CE1 . TYR A 56  ? 0.57532 1.00422 0.43323 0.00338  -0.02100 -0.00079 54  TYR A CE1 
346  C CE2 . TYR A 56  ? 0.58314 1.04027 0.44710 0.00033  -0.02693 0.03645  54  TYR A CE2 
347  C CZ  . TYR A 56  ? 0.61276 1.05114 0.47655 0.00311  -0.02152 0.02454  54  TYR A CZ  
348  O OH  . TYR A 56  ? 0.61207 1.03805 0.48412 0.00537  -0.01635 0.03743  54  TYR A OH  
349  N N   . MET A 57  ? 0.52013 0.98825 0.36710 -0.01870 -0.05557 -0.04391 55  MET A N   
350  C CA  . MET A 57  ? 0.54015 1.00636 0.38324 -0.02407 -0.06016 -0.06516 55  MET A CA  
351  C C   . MET A 57  ? 0.54116 0.98200 0.39470 -0.02605 -0.06308 -0.07555 55  MET A C   
352  O O   . MET A 57  ? 0.55397 0.98039 0.40480 -0.02856 -0.06257 -0.09771 55  MET A O   
353  C CB  . MET A 57  ? 0.57273 1.06252 0.41445 -0.02866 -0.06751 -0.05751 55  MET A CB  
354  C CG  . MET A 57  ? 0.59389 1.09227 0.42384 -0.03333 -0.06931 -0.07862 55  MET A CG  
355  S SD  . MET A 57  ? 0.76027 1.27373 0.57503 -0.02892 -0.06044 -0.08232 55  MET A SD  
356  C CE  . MET A 57  ? 0.73036 1.23603 0.53412 -0.03221 -0.06030 -0.11532 55  MET A CE  
357  N N   . ALA A 58  ? 0.51137 0.94525 0.37789 -0.02464 -0.06576 -0.05967 56  ALA A N   
358  C CA  . ALA A 58  ? 0.47614 0.88829 0.35407 -0.02673 -0.06857 -0.06813 56  ALA A CA  
359  C C   . ALA A 58  ? 0.48534 0.86889 0.36662 -0.02222 -0.05994 -0.07593 56  ALA A C   
360  O O   . ALA A 58  ? 0.47435 0.83379 0.36316 -0.02439 -0.05921 -0.09033 56  ALA A O   
361  C CB  . ALA A 58  ? 0.49925 0.91217 0.39352 -0.02594 -0.07347 -0.04781 56  ALA A CB  
362  N N   . PHE A 59  ? 0.40968 0.79289 0.28847 -0.01609 -0.05287 -0.06465 57  PHE A N   
363  C CA  . PHE A 59  ? 0.46371 0.81913 0.34903 -0.01117 -0.04411 -0.06806 57  PHE A CA  
364  C C   . PHE A 59  ? 0.45870 0.82811 0.32946 -0.00726 -0.03760 -0.07037 57  PHE A C   
365  O O   . PHE A 59  ? 0.46521 0.84576 0.33526 -0.00421 -0.03475 -0.05230 57  PHE A O   
366  C CB  . PHE A 59  ? 0.40973 0.74799 0.31201 -0.00777 -0.04208 -0.04847 57  PHE A CB  
367  C CG  . PHE A 59  ? 0.42937 0.75965 0.34596 -0.01080 -0.04819 -0.04361 57  PHE A CG  
368  C CD1 . PHE A 59  ? 0.38997 0.69774 0.31538 -0.01345 -0.04843 -0.05686 57  PHE A CD1 
369  C CD2 . PHE A 59  ? 0.40598 0.75312 0.32753 -0.01092 -0.05375 -0.02546 57  PHE A CD2 
370  C CE1 . PHE A 59  ? 0.43511 0.73861 0.37396 -0.01642 -0.05350 -0.05203 57  PHE A CE1 
371  C CE2 . PHE A 59  ? 0.38671 0.72939 0.32194 -0.01291 -0.05888 -0.02131 57  PHE A CE2 
372  C CZ  . PHE A 59  ? 0.43605 0.75757 0.37993 -0.01584 -0.05853 -0.03471 57  PHE A CZ  
373  N N   . PRO A 60  ? 0.43346 0.80280 0.29301 -0.00723 -0.03494 -0.09254 58  PRO A N   
374  C CA  . PRO A 60  ? 0.48402 0.87104 0.33008 -0.00344 -0.02856 -0.09519 58  PRO A CA  
375  C C   . PRO A 60  ? 0.46532 0.84430 0.31547 0.00281  -0.01996 -0.08557 58  PRO A C   
376  O O   . PRO A 60  ? 0.49980 0.89781 0.34304 0.00531  -0.01528 -0.07770 58  PRO A O   
377  C CB  . PRO A 60  ? 0.49336 0.87066 0.33426 -0.00398 -0.02697 -0.12160 58  PRO A CB  
378  C CG  . PRO A 60  ? 0.46474 0.83102 0.31097 -0.01051 -0.03519 -0.13085 58  PRO A CG  
379  C CD  . PRO A 60  ? 0.46214 0.81547 0.32236 -0.01094 -0.03769 -0.11560 58  PRO A CD  
380  N N   . SER A 61  ? 0.42234 0.77053 0.28839 0.00499  -0.01719 -0.08383 59  SER A N   
381  C CA  . SER A 61  ? 0.43885 0.77844 0.31169 0.01013  -0.00963 -0.07289 59  SER A CA  
382  C C   . SER A 61  ? 0.42812 0.74540 0.31859 0.00965  -0.01131 -0.05756 59  SER A C   
383  O O   . SER A 61  ? 0.40846 0.71435 0.30643 0.00632  -0.01707 -0.05848 59  SER A O   
384  C CB  . SER A 61  ? 0.44662 0.77139 0.31920 0.01510  -0.00248 -0.09052 59  SER A CB  
385  O OG  . SER A 61  ? 0.39653 0.69101 0.28031 0.01437  -0.00424 -0.10088 59  SER A OG  
386  N N   . LYS A 62  ? 0.42273 0.73435 0.32005 0.01285  -0.00610 -0.04400 60  LYS A N   
387  C CA  . LYS A 62  ? 0.41268 0.69960 0.32634 0.01316  -0.00648 -0.03310 60  LYS A CA  
388  C C   . LYS A 62  ? 0.44445 0.70383 0.36610 0.01366  -0.00609 -0.04778 60  LYS A C   
389  O O   . LYS A 62  ? 0.40611 0.65006 0.33787 0.01158  -0.00990 -0.04457 60  LYS A O   
390  C CB  . LYS A 62  ? 0.47265 0.75700 0.39170 0.01592  -0.00078 -0.01964 60  LYS A CB  
391  C CG  . LYS A 62  ? 0.50054 0.77606 0.43129 0.01463  -0.00347 0.00027  60  LYS A CG  
392  C CD  . LYS A 62  ? 0.50129 0.76387 0.44077 0.01653  0.00172  0.00862  60  LYS A CD  
393  C CE  . LYS A 62  ? 0.52312 0.76502 0.47646 0.01574  -0.00106 0.02048  60  LYS A CE  
394  N NZ  . LYS A 62  ? 0.49147 0.72318 0.45278 0.01630  0.00288  0.03029  60  LYS A NZ  
395  N N   . ASP A 63  ? 0.45053 0.70344 0.36889 0.01693  -0.00101 -0.06265 61  ASP A N   
396  C CA  . ASP A 63  ? 0.43334 0.66090 0.35851 0.01742  -0.00080 -0.07708 61  ASP A CA  
397  C C   . ASP A 63  ? 0.42191 0.64587 0.34728 0.01205  -0.00766 -0.08549 61  ASP A C   
398  O O   . ASP A 63  ? 0.40384 0.60633 0.33992 0.01029  -0.00945 -0.08716 61  ASP A O   
399  C CB  . ASP A 63  ? 0.47304 0.69984 0.39222 0.02217  0.00484  -0.09345 61  ASP A CB  
400  C CG  . ASP A 63  ? 0.55719 0.78066 0.48156 0.02766  0.01178  -0.08622 61  ASP A CG  
401  O OD1 . ASP A 63  ? 0.50851 0.72904 0.44066 0.02694  0.01198  -0.06896 61  ASP A OD1 
402  O OD2 . ASP A 63  ? 0.60691 0.83297 0.52723 0.03273  0.01699  -0.09815 61  ASP A OD2 
403  N N   . SER A 64  ? 0.40156 0.64778 0.31517 0.00898  -0.01163 -0.09083 62  SER A N   
404  C CA  . SER A 64  ? 0.41914 0.66536 0.33327 0.00283  -0.01899 -0.09829 62  SER A CA  
405  C C   . SER A 64  ? 0.40659 0.64898 0.33263 0.00018  -0.02338 -0.08179 62  SER A C   
406  O O   . SER A 64  ? 0.39881 0.62705 0.33408 -0.00345 -0.02687 -0.08552 62  SER A O   
407  C CB  . SER A 64  ? 0.43369 0.70872 0.33213 -0.00015 -0.02296 -0.10487 62  SER A CB  
408  O OG  . SER A 64  ? 0.51438 0.79341 0.40102 0.00240  -0.01901 -0.12334 62  SER A OG  
409  N N   . PHE A 65  ? 0.36305 0.61880 0.28935 0.00203  -0.02315 -0.06328 63  PHE A N   
410  C CA  . PHE A 65  ? 0.39549 0.64836 0.33333 0.00109  -0.02676 -0.04699 63  PHE A CA  
411  C C   . PHE A 65  ? 0.36405 0.58871 0.31594 0.00294  -0.02358 -0.04448 63  PHE A C   
412  O O   . PHE A 65  ? 0.32001 0.53657 0.28221 0.00097  -0.02687 -0.04084 63  PHE A O   
413  C CB  . PHE A 65  ? 0.40739 0.67773 0.34270 0.00334  -0.02645 -0.02801 63  PHE A CB  
414  C CG  . PHE A 65  ? 0.42031 0.69053 0.36673 0.00318  -0.03075 -0.01168 63  PHE A CG  
415  C CD1 . PHE A 65  ? 0.38093 0.66319 0.32904 -0.00022 -0.03787 -0.01175 63  PHE A CD1 
416  C CD2 . PHE A 65  ? 0.37702 0.63481 0.33310 0.00657  -0.02780 0.00300  63  PHE A CD2 
417  C CE1 . PHE A 65  ? 0.37075 0.65347 0.33080 0.00087  -0.04157 0.00331  63  PHE A CE1 
418  C CE2 . PHE A 65  ? 0.36224 0.61857 0.32930 0.00751  -0.03144 0.01703  63  PHE A CE2 
419  C CZ  . PHE A 65  ? 0.32786 0.59706 0.29729 0.00521  -0.03815 0.01744  63  PHE A CZ  
420  N N   . ILE A 66  ? 0.37542 0.58710 0.32794 0.00682  -0.01718 -0.04566 64  ILE A N   
421  C CA  . ILE A 66  ? 0.33200 0.51862 0.29632 0.00861  -0.01413 -0.04316 64  ILE A CA  
422  C C   . ILE A 66  ? 0.35543 0.52579 0.32513 0.00572  -0.01579 -0.05564 64  ILE A C   
423  O O   . ILE A 66  ? 0.35700 0.51301 0.33733 0.00493  -0.01632 -0.05114 64  ILE A O   
424  C CB  . ILE A 66  ? 0.39824 0.57762 0.36125 0.01295  -0.00754 -0.04353 64  ILE A CB  
425  C CG1 . ILE A 66  ? 0.40617 0.59887 0.36728 0.01469  -0.00587 -0.02805 64  ILE A CG1 
426  C CG2 . ILE A 66  ? 0.34467 0.49865 0.31824 0.01436  -0.00490 -0.04420 64  ILE A CG2 
427  C CD1 . ILE A 66  ? 0.41333 0.60137 0.38365 0.01402  -0.00861 -0.01267 64  ILE A CD1 
428  N N   . ILE A 67  ? 0.33622 0.50793 0.29890 0.00411  -0.01625 -0.07168 65  ILE A N   
429  C CA  . ILE A 67  ? 0.35803 0.51360 0.32624 0.00035  -0.01825 -0.08365 65  ILE A CA  
430  C C   . ILE A 67  ? 0.38682 0.54917 0.36068 -0.00545 -0.02466 -0.07999 65  ILE A C   
431  O O   . ILE A 67  ? 0.36543 0.51326 0.34954 -0.00837 -0.02569 -0.08066 65  ILE A O   
432  C CB  . ILE A 67  ? 0.41434 0.57013 0.37345 -0.00008 -0.01777 -0.10256 65  ILE A CB  
433  C CG1 . ILE A 67  ? 0.46834 0.60574 0.42961 0.00555  -0.01138 -0.10814 65  ILE A CG1 
434  C CG2 . ILE A 67  ? 0.44943 0.59979 0.41121 -0.00715 -0.02332 -0.11448 65  ILE A CG2 
435  C CD1 . ILE A 67  ? 0.55374 0.69352 0.50539 0.00795  -0.00930 -0.12586 65  ILE A CD1 
436  N N   . GLU A 68  ? 0.39662 0.58272 0.36447 -0.00715 -0.02905 -0.07510 66  GLU A N   
437  C CA  . GLU A 68  ? 0.38932 0.58468 0.36390 -0.01208 -0.03541 -0.07056 66  GLU A CA  
438  C C   . GLU A 68  ? 0.35284 0.54148 0.33994 -0.00931 -0.03425 -0.05455 66  GLU A C   
439  O O   . GLU A 68  ? 0.32707 0.51165 0.32469 -0.01243 -0.03677 -0.05305 66  GLU A O   
440  C CB  . GLU A 68  ? 0.40435 0.62868 0.36940 -0.01406 -0.04083 -0.06819 66  GLU A CB  
441  C CG  . GLU A 68  ? 0.43705 0.67041 0.38882 -0.01756 -0.04279 -0.08594 66  GLU A CG  
442  C CD  . GLU A 68  ? 0.48179 0.69936 0.43784 -0.02354 -0.04499 -0.10284 66  GLU A CD  
443  O OE1 . GLU A 68  ? 0.47605 0.69039 0.44353 -0.02860 -0.04917 -0.10031 66  GLU A OE1 
444  O OE2 . GLU A 68  ? 0.49306 0.70175 0.44145 -0.02305 -0.04235 -0.11870 66  GLU A OE2 
445  N N   . CYS A 69  ? 0.34895 0.53661 0.33535 -0.00362 -0.03030 -0.04294 67  CYS A N   
446  C CA  . CYS A 69  ? 0.34951 0.52778 0.34717 -0.00038 -0.02861 -0.02959 67  CYS A CA  
447  C C   . CYS A 69  ? 0.33991 0.49487 0.34592 -0.00069 -0.02519 -0.03435 67  CYS A C   
448  O O   . CYS A 69  ? 0.31561 0.46540 0.33205 -0.00084 -0.02569 -0.02882 67  CYS A O   
449  C CB  . CYS A 69  ? 0.32069 0.49953 0.31552 0.00471  -0.02499 -0.01831 67  CYS A CB  
450  S SG  . CYS A 69  ? 0.36828 0.57417 0.35750 0.00535  -0.02937 -0.00599 67  CYS A SG  
451  N N   . LEU A 70  ? 0.32204 0.46384 0.32381 -0.00030 -0.02150 -0.04405 68  LEU A N   
452  C CA  . LEU A 70  ? 0.36645 0.48665 0.37563 -0.00036 -0.01831 -0.04704 68  LEU A CA  
453  C C   . LEU A 70  ? 0.33121 0.44806 0.34660 -0.00634 -0.02161 -0.05405 68  LEU A C   
454  O O   . LEU A 70  ? 0.31890 0.42489 0.34358 -0.00724 -0.02038 -0.05060 68  LEU A O   
455  C CB  . LEU A 70  ? 0.32184 0.43018 0.32581 0.00219  -0.01398 -0.05486 68  LEU A CB  
456  C CG  . LEU A 70  ? 0.40820 0.49482 0.41930 0.00289  -0.01063 -0.05602 68  LEU A CG  
457  C CD1 . LEU A 70  ? 0.38557 0.46658 0.39979 0.00727  -0.00714 -0.04453 68  LEU A CD1 
458  C CD2 . LEU A 70  ? 0.39159 0.46780 0.39887 0.00399  -0.00838 -0.06802 68  LEU A CD2 
459  N N   . ASP A 71  ? 0.35918 0.48603 0.36942 -0.01099 -0.02583 -0.06410 69  ASP A N   
460  C CA  . ASP A 71  ? 0.37162 0.49712 0.38858 -0.01822 -0.02990 -0.07057 69  ASP A CA  
461  C C   . ASP A 71  ? 0.33645 0.47286 0.36334 -0.01969 -0.03262 -0.05972 69  ASP A C   
462  O O   . ASP A 71  ? 0.32867 0.45830 0.36572 -0.02365 -0.03294 -0.05947 69  ASP A O   
463  C CB  . ASP A 71  ? 0.36664 0.50350 0.37547 -0.02336 -0.03482 -0.08350 69  ASP A CB  
464  C CG  . ASP A 71  ? 0.48596 0.60623 0.48989 -0.02380 -0.03259 -0.09827 69  ASP A CG  
465  O OD1 . ASP A 71  ? 0.50525 0.60605 0.51323 -0.02011 -0.02750 -0.09670 69  ASP A OD1 
466  O OD2 . ASP A 71  ? 0.52803 0.65494 0.52414 -0.02740 -0.03596 -0.11142 69  ASP A OD2 
467  N N   . MET A 72  ? 0.32143 0.47535 0.34631 -0.01625 -0.03441 -0.05001 70  MET A N   
468  C CA  . MET A 72  ? 0.33329 0.49833 0.36888 -0.01622 -0.03690 -0.03959 70  MET A CA  
469  C C   . MET A 72  ? 0.30682 0.45703 0.35140 -0.01170 -0.03159 -0.03145 70  MET A C   
470  O O   . MET A 72  ? 0.34137 0.49164 0.39684 -0.01373 -0.03176 -0.02892 70  MET A O   
471  C CB  . MET A 72  ? 0.34142 0.52822 0.37335 -0.01301 -0.04048 -0.03026 70  MET A CB  
472  C CG  . MET A 72  ? 0.38852 0.58084 0.43210 -0.00849 -0.04049 -0.01640 70  MET A CG  
473  S SD  . MET A 72  ? 0.46347 0.67997 0.50521 -0.00417 -0.04515 -0.00306 70  MET A SD  
474  C CE  . MET A 72  ? 0.47499 0.71715 0.51581 -0.01213 -0.05391 -0.00933 70  MET A CE  
475  N N   . GLU A 73  ? 0.33648 0.47500 0.37661 -0.00596 -0.02680 -0.02774 71  GLU A N   
476  C CA  . GLU A 73  ? 0.27605 0.40066 0.32305 -0.00191 -0.02202 -0.02132 71  GLU A CA  
477  C C   . GLU A 73  ? 0.31584 0.42645 0.36794 -0.00594 -0.01985 -0.02748 71  GLU A C   
478  O O   . GLU A 73  ? 0.31237 0.41988 0.37318 -0.00536 -0.01784 -0.02288 71  GLU A O   
479  C CB  . GLU A 73  ? 0.31082 0.42549 0.35127 0.00329  -0.01804 -0.01810 71  GLU A CB  
480  C CG  . GLU A 73  ? 0.34008 0.44161 0.38555 0.00786  -0.01364 -0.01129 71  GLU A CG  
481  C CD  . GLU A 73  ? 0.38012 0.48747 0.43535 0.01052  -0.01423 -0.00336 71  GLU A CD  
482  O OE1 . GLU A 73  ? 0.40629 0.52969 0.46401 0.01106  -0.01818 0.00131  71  GLU A OE1 
483  O OE2 . GLU A 73  ? 0.40857 0.50518 0.46888 0.01279  -0.01061 -0.00147 71  GLU A OE2 
484  N N   . ILE A 74  ? 0.32594 0.42840 0.37300 -0.00992 -0.02013 -0.03774 72  ILE A N   
485  C CA  . ILE A 74  ? 0.31958 0.40791 0.37208 -0.01430 -0.01858 -0.04255 72  ILE A CA  
486  C C   . ILE A 74  ? 0.35940 0.45780 0.42167 -0.02062 -0.02199 -0.04210 72  ILE A C   
487  O O   . ILE A 74  ? 0.29760 0.39086 0.36843 -0.02228 -0.01966 -0.03836 72  ILE A O   
488  C CB  . ILE A 74  ? 0.30919 0.38608 0.35523 -0.01662 -0.01867 -0.05391 72  ILE A CB  
489  C CG1 . ILE A 74  ? 0.32196 0.38728 0.36172 -0.01018 -0.01408 -0.05306 72  ILE A CG1 
490  C CG2 . ILE A 74  ? 0.32635 0.39024 0.37960 -0.02294 -0.01882 -0.05875 72  ILE A CG2 
491  C CD1 . ILE A 74  ? 0.33372 0.39208 0.36662 -0.01027 -0.01403 -0.06427 72  ILE A CD1 
492  N N   . ASN A 75  ? 0.32372 0.43870 0.38487 -0.02452 -0.02762 -0.04557 73  ASN A N   
493  C CA  . ASN A 75  ? 0.33698 0.46499 0.40854 -0.03104 -0.03157 -0.04460 73  ASN A CA  
494  C C   . ASN A 75  ? 0.28179 0.41946 0.36306 -0.02654 -0.02958 -0.03276 73  ASN A C   
495  O O   . ASN A 75  ? 0.28566 0.42726 0.37797 -0.03050 -0.02930 -0.03030 73  ASN A O   
496  C CB  . ASN A 75  ? 0.34176 0.48882 0.40960 -0.03559 -0.03867 -0.04980 73  ASN A CB  
497  C CG  . ASN A 75  ? 0.44034 0.57869 0.50079 -0.04172 -0.04116 -0.06407 73  ASN A CG  
498  O OD1 . ASN A 75  ? 0.48209 0.60161 0.54545 -0.04529 -0.03899 -0.06964 73  ASN A OD1 
499  N ND2 . ASN A 75  ? 0.45710 0.60957 0.50820 -0.04310 -0.04596 -0.07024 73  ASN A ND2 
500  N N   . ARG A 76  ? 0.26413 0.40668 0.34212 -0.01840 -0.02830 -0.02537 74  ARG A N   
501  C CA  . ARG A 76  ? 0.27120 0.42088 0.35853 -0.01270 -0.02613 -0.01509 74  ARG A CA  
502  C C   . ARG A 76  ? 0.27939 0.41340 0.37076 -0.01076 -0.01971 -0.01343 74  ARG A C   
503  O O   . ARG A 76  ? 0.22717 0.36783 0.32902 -0.01011 -0.01784 -0.00881 74  ARG A O   
504  C CB  . ARG A 76  ? 0.29975 0.45383 0.38250 -0.00456 -0.02621 -0.00777 74  ARG A CB  
505  C CG  . ARG A 76  ? 0.29587 0.45846 0.38930 0.00204  -0.02500 0.00227  74  ARG A CG  
506  C CD  . ARG A 76  ? 0.30951 0.46941 0.39917 0.01019  -0.02411 0.00994  74  ARG A CD  
507  N NE  . ARG A 76  ? 0.34449 0.48303 0.42851 0.01319  -0.01856 0.00864  74  ARG A NE  
508  C CZ  . ARG A 76  ? 0.33606 0.46350 0.42502 0.01619  -0.01353 0.00932  74  ARG A CZ  
509  N NH1 . ARG A 76  ? 0.29847 0.43399 0.39856 0.01754  -0.01241 0.01166  74  ARG A NH1 
510  N NH2 . ARG A 76  ? 0.26934 0.37896 0.35192 0.01796  -0.00949 0.00763  74  ARG A NH2 
511  N N   . LEU A 77  ? 0.25313 0.36817 0.33621 -0.00936 -0.01615 -0.01676 75  LEU A N   
512  C CA  . LEU A 77  ? 0.28916 0.39025 0.37448 -0.00792 -0.01053 -0.01515 75  LEU A CA  
513  C C   . LEU A 77  ? 0.26403 0.36435 0.35653 -0.01554 -0.01034 -0.01767 75  LEU A C   
514  O O   . LEU A 77  ? 0.25821 0.35785 0.35695 -0.01497 -0.00635 -0.01350 75  LEU A O   
515  C CB  . LEU A 77  ? 0.27223 0.35531 0.34767 -0.00553 -0.00780 -0.01807 75  LEU A CB  
516  C CG  . LEU A 77  ? 0.31117 0.39318 0.38086 0.00162  -0.00684 -0.01387 75  LEU A CG  
517  C CD1 . LEU A 77  ? 0.31371 0.38277 0.37373 0.00233  -0.00559 -0.01810 75  LEU A CD1 
518  C CD2 . LEU A 77  ? 0.28466 0.36402 0.35888 0.00730  -0.00293 -0.00743 75  LEU A CD2 
519  N N   . LYS A 78  ? 0.23687 0.33643 0.32827 -0.02296 -0.01436 -0.02469 76  LYS A N   
520  C CA  . LYS A 78  ? 0.27788 0.37621 0.37755 -0.03159 -0.01486 -0.02644 76  LYS A CA  
521  C C   . LYS A 78  ? 0.29683 0.41568 0.40867 -0.03395 -0.01609 -0.02102 76  LYS A C   
522  O O   . LYS A 78  ? 0.28572 0.40599 0.40632 -0.03792 -0.01346 -0.01756 76  LYS A O   
523  C CB  . LYS A 78  ? 0.32181 0.41494 0.41864 -0.03936 -0.01974 -0.03622 76  LYS A CB  
524  C CG  . LYS A 78  ? 0.32160 0.39461 0.40846 -0.03730 -0.01833 -0.04270 76  LYS A CG  
525  C CD  . LYS A 78  ? 0.34263 0.41111 0.42856 -0.04521 -0.02323 -0.05368 76  LYS A CD  
526  C CE  . LYS A 78  ? 0.44119 0.48615 0.52367 -0.04525 -0.02104 -0.05918 76  LYS A CE  
527  N NZ  . LYS A 78  ? 0.45130 0.49106 0.53012 -0.05029 -0.02563 -0.07227 76  LYS A NZ  
528  N N   . GLN A 79  ? 0.27789 0.41441 0.39101 -0.03133 -0.01993 -0.01928 77  GLN A N   
529  C CA  . GLN A 79  ? 0.26919 0.42732 0.39549 -0.03301 -0.02136 -0.01378 77  GLN A CA  
530  C C   . GLN A 79  ? 0.24896 0.40988 0.38047 -0.02404 -0.01516 -0.00563 77  GLN A C   
531  O O   . GLN A 79  ? 0.24622 0.41806 0.38910 -0.02579 -0.01276 -0.00152 77  GLN A O   
532  C CB  . GLN A 79  ? 0.27601 0.45352 0.40247 -0.03408 -0.02865 -0.01470 77  GLN A CB  
533  C CG  . GLN A 79  ? 0.34685 0.55005 0.48606 -0.03143 -0.03064 -0.00685 77  GLN A CG  
534  C CD  . GLN A 79  ? 0.39773 0.61655 0.53339 -0.02707 -0.03638 -0.00430 77  GLN A CD  
535  O OE1 . GLN A 79  ? 0.45170 0.66661 0.57558 -0.02934 -0.04025 -0.01012 77  GLN A OE1 
536  N NE2 . GLN A 79  ? 0.35408 0.59269 0.50066 -0.02109 -0.03719 0.00458  77  GLN A NE2 
537  N N   . SER A 80  ? 0.26061 0.41018 0.38364 -0.01509 -0.01203 -0.00406 78  SER A N   
538  C CA  . SER A 80  ? 0.26807 0.41608 0.39409 -0.00632 -0.00603 0.00151  78  SER A CA  
539  C C   . SER A 80  ? 0.26964 0.40944 0.39767 -0.00883 -0.00016 0.00164  78  SER A C   
540  O O   . SER A 80  ? 0.29557 0.44574 0.43235 -0.00610 0.00389  0.00577  78  SER A O   
541  C CB  . SER A 80  ? 0.26047 0.39475 0.37595 0.00142  -0.00477 0.00183  78  SER A CB  
542  O OG  . SER A 80  ? 0.30412 0.43284 0.42092 0.00921  0.00088  0.00520  78  SER A OG  
543  N N   . LEU A 81  ? 0.25406 0.37622 0.37407 -0.01335 0.00062  -0.00239 79  LEU A N   
544  C CA  . LEU A 81  ? 0.29402 0.40855 0.41511 -0.01623 0.00570  -0.00093 79  LEU A CA  
545  C C   . LEU A 81  ? 0.29851 0.42478 0.43090 -0.02567 0.00481  0.00066  79  LEU A C   
546  O O   . LEU A 81  ? 0.34109 0.47435 0.47986 -0.02633 0.00963  0.00527  79  LEU A O   
547  C CB  . LEU A 81  ? 0.28176 0.37467 0.39222 -0.01792 0.00601  -0.00462 79  LEU A CB  
548  C CG  . LEU A 81  ? 0.32363 0.40776 0.43372 -0.02038 0.01085  -0.00181 79  LEU A CG  
549  C CD1 . LEU A 81  ? 0.29028 0.37902 0.39994 -0.01323 0.01682  0.00233  79  LEU A CD1 
550  C CD2 . LEU A 81  ? 0.23764 0.30159 0.33859 -0.02130 0.01028  -0.00488 79  LEU A CD2 
551  N N   . SER A 82  ? 0.29793 0.42747 0.43293 -0.03353 -0.00136 -0.00329 80  SER A N   
552  C CA  . SER A 82  ? 0.30984 0.45041 0.45661 -0.04409 -0.00326 -0.00206 80  SER A CA  
553  C C   . SER A 82  ? 0.32102 0.48692 0.48063 -0.04190 -0.00142 0.00424  80  SER A C   
554  O O   . SER A 82  ? 0.32685 0.50169 0.49603 -0.04688 0.00195  0.00893  80  SER A O   
555  C CB  . SER A 82  ? 0.30120 0.44169 0.44755 -0.05215 -0.01111 -0.00913 80  SER A CB  
556  O OG  . SER A 82  ? 0.43753 0.58533 0.59520 -0.06406 -0.01365 -0.00880 80  SER A OG  
557  N N   . ASN A 83  ? 0.29623 0.47457 0.45674 -0.03391 -0.00324 0.00521  81  ASN A N   
558  C CA  . ASN A 83  ? 0.28135 0.48441 0.45526 -0.02994 -0.00155 0.01121  81  ASN A CA  
559  C C   . ASN A 83  ? 0.30847 0.51125 0.48362 -0.02185 0.00726  0.01541  81  ASN A C   
560  O O   . ASN A 83  ? 0.26948 0.49120 0.45693 -0.02206 0.01086  0.02007  81  ASN A O   
561  C CB  . ASN A 83  ? 0.22929 0.44410 0.40400 -0.02257 -0.00610 0.01211  81  ASN A CB  
562  C CG  . ASN A 83  ? 0.29414 0.52071 0.47175 -0.03128 -0.01493 0.00923  81  ASN A CG  
563  O OD1 . ASN A 83  ? 0.29454 0.52521 0.47798 -0.04302 -0.01753 0.00707  81  ASN A OD1 
564  N ND2 . ASN A 83  ? 0.29048 0.52304 0.46415 -0.02616 -0.01983 0.00936  81  ASN A ND2 
565  N N   . LEU A 84  ? 0.25915 0.44252 0.42188 -0.01455 0.01078  0.01348  82  LEU A N   
566  C CA  . LEU A 84  ? 0.27012 0.45207 0.43186 -0.00711 0.01883  0.01572  82  LEU A CA  
567  C C   . LEU A 84  ? 0.30727 0.49028 0.47149 -0.01493 0.02332  0.01814  82  LEU A C   
568  O O   . LEU A 84  ? 0.30453 0.50306 0.47655 -0.01265 0.02917  0.02197  82  LEU A O   
569  C CB  . LEU A 84  ? 0.26601 0.42591 0.41329 0.00029  0.02040  0.01248  82  LEU A CB  
570  C CG  . LEU A 84  ? 0.24918 0.40692 0.39389 0.00890  0.02791  0.01299  82  LEU A CG  
571  C CD1 . LEU A 84  ? 0.26959 0.44243 0.42388 0.01908  0.02945  0.01478  82  LEU A CD1 
572  C CD2 . LEU A 84  ? 0.26584 0.40124 0.39625 0.01278  0.02882  0.00958  82  LEU A CD2 
573  N N   . LEU A 85  ? 0.26948 0.43687 0.42771 -0.02400 0.02079  0.01640  83  LEU A N   
574  C CA  . LEU A 85  ? 0.30491 0.47197 0.46603 -0.03241 0.02428  0.02037  83  LEU A CA  
575  C C   . LEU A 85  ? 0.33096 0.52024 0.50823 -0.04125 0.02316  0.02468  83  LEU A C   
576  O O   . LEU A 85  ? 0.30340 0.50411 0.48721 -0.04464 0.02858  0.03054  83  LEU A O   
577  C CB  . LEU A 85  ? 0.29893 0.44262 0.45157 -0.03944 0.02105  0.01781  83  LEU A CB  
578  C CG  . LEU A 85  ? 0.30177 0.42441 0.43935 -0.03201 0.02193  0.01419  83  LEU A CG  
579  C CD1 . LEU A 85  ? 0.32121 0.42353 0.45334 -0.03877 0.01933  0.01272  83  LEU A CD1 
580  C CD2 . LEU A 85  ? 0.30998 0.43471 0.44288 -0.02471 0.02918  0.01720  83  LEU A CD2 
581  N N   . GLY A 86  ? 0.33503 0.53192 0.51880 -0.04586 0.01599  0.02210  84  GLY A N   
582  C CA  . GLY A 86  ? 0.33060 0.55084 0.53088 -0.05479 0.01382  0.02592  84  GLY A CA  
583  C C   . GLY A 86  ? 0.32074 0.56810 0.53276 -0.04817 0.01955  0.03169  84  GLY A C   
584  O O   . GLY A 86  ? 0.34473 0.61396 0.57181 -0.05596 0.01944  0.03652  84  GLY A O   
585  N N   . GLN A 87  ? 0.35790 0.60436 0.56413 -0.03410 0.02464  0.03106  85  GLN A N   
586  C CA  . GLN A 87  ? 0.35388 0.62457 0.57093 -0.02539 0.03072  0.03509  85  GLN A CA  
587  C C   . GLN A 87  ? 0.32849 0.60596 0.54672 -0.02604 0.04000  0.03938  85  GLN A C   
588  O O   . GLN A 87  ? 0.34525 0.64764 0.57529 -0.02144 0.04547  0.04316  85  GLN A O   
589  C CB  . GLN A 87  ? 0.35267 0.61735 0.56338 -0.00975 0.03217  0.03183  85  GLN A CB  
590  C CG  . GLN A 87  ? 0.35954 0.62898 0.57390 -0.00675 0.02430  0.03070  85  GLN A CG  
591  C CD  . GLN A 87  ? 0.33743 0.60828 0.55205 0.00903  0.02674  0.03051  85  GLN A CD  
592  O OE1 . GLN A 87  ? 0.39897 0.68950 0.62604 0.01445  0.02434  0.03376  85  GLN A OE1 
593  N NE2 . GLN A 87  ? 0.35180 0.60177 0.55346 0.01646  0.03132  0.02697  85  GLN A NE2 
594  N N   . CYS A 88  ? 0.32560 0.58343 0.53215 -0.03103 0.04210  0.03931  86  CYS A N   
595  C CA  . CYS A 88  ? 0.35935 0.62499 0.56520 -0.03127 0.05097  0.04408  86  CYS A CA  
596  C C   . CYS A 88  ? 0.35955 0.64313 0.57925 -0.04518 0.05150  0.05206  86  CYS A C   
597  O O   . CYS A 88  ? 0.35095 0.63053 0.57664 -0.05697 0.04425  0.05276  86  CYS A O   
598  C CB  . CYS A 88  ? 0.37100 0.61055 0.55896 -0.03072 0.05289  0.04228  86  CYS A CB  
599  S SG  . CYS A 88  ? 0.42606 0.64254 0.59807 -0.01735 0.05126  0.03343  86  CYS A SG  
600  N N   . GLY A 89  ? 0.35560 0.65956 0.58042 -0.04398 0.06031  0.05786  87  GLY A N   
601  C CA  . GLY A 89  ? 0.37309 0.69554 0.61136 -0.05770 0.06183  0.06713  87  GLY A CA  
602  C C   . GLY A 89  ? 0.44434 0.74414 0.67613 -0.07086 0.05849  0.07079  87  GLY A C   
603  O O   . GLY A 89  ? 0.42060 0.69589 0.63611 -0.06750 0.05898  0.06823  87  GLY A O   
604  N N   . LYS A 90  ? 0.46161 0.76997 0.70749 -0.08620 0.05481  0.07718  88  LYS A N   
605  C CA  . LYS A 90  ? 0.45641 0.74066 0.69887 -0.09927 0.05017  0.08026  88  LYS A CA  
606  C C   . LYS A 90  ? 0.49163 0.76544 0.72192 -0.09815 0.05687  0.08640  88  LYS A C   
607  O O   . LYS A 90  ? 0.46948 0.71466 0.68870 -0.10028 0.05356  0.08525  88  LYS A O   
608  C CB  . LYS A 90  ? 0.44963 0.74810 0.71125 -0.11655 0.04649  0.08750  88  LYS A CB  
609  N N   . ASP A 91  ? 0.50532 0.80344 0.73728 -0.09421 0.06639  0.09287  89  ASP A N   
610  C CA  . ASP A 91  ? 0.51063 0.80338 0.73055 -0.09359 0.07291  0.09952  89  ASP A CA  
611  C C   . ASP A 91  ? 0.47157 0.75022 0.67168 -0.07821 0.07578  0.09103  89  ASP A C   
612  O O   . ASP A 91  ? 0.48692 0.75762 0.67438 -0.07731 0.07965  0.09518  89  ASP A O   
613  C CB  . ASP A 91  ? 0.43490 0.76247 0.66444 -0.09686 0.08234  0.11026  89  ASP A CB  
614  N N   . ASP A 92  ? 0.42556 0.70059 0.62283 -0.06681 0.07342  0.07985  90  ASP A N   
615  C CA  . ASP A 92  ? 0.41770 0.68950 0.60055 -0.05158 0.07827  0.07233  90  ASP A CA  
616  C C   . ASP A 92  ? 0.39313 0.63209 0.55908 -0.04848 0.07349  0.06678  90  ASP A C   
617  O O   . ASP A 92  ? 0.34049 0.56497 0.50185 -0.04140 0.06876  0.05782  90  ASP A O   
618  C CB  . ASP A 92  ? 0.38916 0.67442 0.57911 -0.04056 0.07859  0.06465  90  ASP A CB  
619  C CG  . ASP A 92  ? 0.39163 0.68150 0.57121 -0.02553 0.08599  0.05834  90  ASP A CG  
620  O OD1 . ASP A 92  ? 0.35668 0.63198 0.51991 -0.02307 0.08832  0.05690  90  ASP A OD1 
621  O OD2 . ASP A 92  ? 0.37830 0.68590 0.56641 -0.01613 0.08909  0.05453  90  ASP A OD2 
622  N N   . HIS A 93  ? 0.40872 0.63773 0.56542 -0.05346 0.07511  0.07310  91  HIS A N   
623  C CA  . HIS A 93  ? 0.42512 0.62444 0.56805 -0.05188 0.07013  0.06950  91  HIS A CA  
624  C C   . HIS A 93  ? 0.39721 0.58989 0.52568 -0.03828 0.07225  0.06005  91  HIS A C   
625  O O   . HIS A 93  ? 0.33804 0.50925 0.45931 -0.03436 0.06678  0.05323  91  HIS A O   
626  C CB  . HIS A 93  ? 0.48217 0.67443 0.62069 -0.06055 0.07103  0.08031  91  HIS A CB  
627  C CG  . HIS A 93  ? 0.46413 0.65965 0.61777 -0.07482 0.06840  0.08987  91  HIS A CG  
628  N ND1 . HIS A 93  ? 0.47047 0.64791 0.63153 -0.08152 0.06011  0.08703  91  HIS A ND1 
629  C CD2 . HIS A 93  ? 0.53155 0.74746 0.69510 -0.08402 0.07296  0.10169  91  HIS A CD2 
630  C CE1 . HIS A 93  ? 0.51516 0.69939 0.69011 -0.09466 0.05915  0.09627  91  HIS A CE1 
631  N NE2 . HIS A 93  ? 0.50687 0.71483 0.68417 -0.09671 0.06687  0.10604  91  HIS A NE2 
632  N N   . THR A 94  ? 0.34797 0.55901 0.47239 -0.03110 0.08018  0.05900  92  THR A N   
633  C CA  . THR A 94  ? 0.37708 0.58116 0.48923 -0.01845 0.08185  0.04866  92  THR A CA  
634  C C   . THR A 94  ? 0.38084 0.57791 0.49875 -0.01182 0.07712  0.04003  92  THR A C   
635  O O   . THR A 94  ? 0.34601 0.52312 0.45491 -0.00661 0.07296  0.03328  92  THR A O   
636  C CB  . THR A 94  ? 0.41250 0.63915 0.52110 -0.01160 0.09146  0.04741  92  THR A CB  
637  O OG1 . THR A 94  ? 0.46412 0.70233 0.56941 -0.01936 0.09595  0.05774  92  THR A OG1 
638  C CG2 . THR A 94  ? 0.36111 0.57668 0.45442 -0.00032 0.09288  0.03670  92  THR A CG2 
639  N N   . SER A 95  ? 0.33326 0.54763 0.46676 -0.01260 0.07727  0.04124  93  SER A N   
640  C CA  . SER A 95  ? 0.34879 0.55971 0.48812 -0.00583 0.07285  0.03452  93  SER A CA  
641  C C   . SER A 95  ? 0.32795 0.51672 0.46518 -0.01097 0.06367  0.03290  93  SER A C   
642  O O   . SER A 95  ? 0.29776 0.47435 0.43096 -0.00421 0.05987  0.02655  93  SER A O   
643  C CB  . SER A 95  ? 0.34501 0.58199 0.50253 -0.00618 0.07442  0.03743  93  SER A CB  
644  O OG  . SER A 95  ? 0.39054 0.64704 0.54999 0.00334  0.08303  0.03565  93  SER A OG  
645  N N   . ILE A 96  ? 0.32178 0.50554 0.46233 -0.02287 0.06014  0.03859  94  ILE A N   
646  C CA  . ILE A 96  ? 0.33874 0.50027 0.47574 -0.02726 0.05216  0.03587  94  ILE A CA  
647  C C   . ILE A 96  ? 0.32509 0.46550 0.44614 -0.02090 0.05155  0.03127  94  ILE A C   
648  O O   . ILE A 96  ? 0.28145 0.40818 0.39813 -0.01700 0.04676  0.02543  94  ILE A O   
649  C CB  . ILE A 96  ? 0.33889 0.49614 0.48153 -0.04065 0.04948  0.04257  94  ILE A CB  
650  C CG1 . ILE A 96  ? 0.33075 0.50642 0.49046 -0.04857 0.04751  0.04559  94  ILE A CG1 
651  C CG2 . ILE A 96  ? 0.34876 0.48007 0.48485 -0.04346 0.04265  0.03880  94  ILE A CG2 
652  C CD1 . ILE A 96  ? 0.35513 0.53133 0.51944 -0.04600 0.04136  0.03882  94  ILE A CD1 
653  N N   . LEU A 97  ? 0.34156 0.48122 0.45374 -0.01993 0.05645  0.03421  95  LEU A N   
654  C CA  . LEU A 97  ? 0.30741 0.42848 0.40508 -0.01557 0.05532  0.03084  95  LEU A CA  
655  C C   . LEU A 97  ? 0.32349 0.44283 0.41551 -0.00440 0.05636  0.02257  95  LEU A C   
656  O O   . LEU A 97  ? 0.27474 0.37749 0.35997 -0.00108 0.05219  0.01783  95  LEU A O   
657  C CB  . LEU A 97  ? 0.37753 0.50154 0.46799 -0.01877 0.05979  0.03746  95  LEU A CB  
658  C CG  . LEU A 97  ? 0.41570 0.52605 0.49170 -0.01714 0.05941  0.03791  95  LEU A CG  
659  C CD1 . LEU A 97  ? 0.43729 0.55160 0.50300 -0.00813 0.06332  0.03136  95  LEU A CD1 
660  C CD2 . LEU A 97  ? 0.32377 0.41220 0.39727 -0.01774 0.05246  0.03511  95  LEU A CD2 
661  N N   . LYS A 98  ? 0.31022 0.44673 0.40661 0.00148  0.06173  0.02086  96  LYS A N   
662  C CA  . LYS A 98  ? 0.31266 0.44631 0.40603 0.01232  0.06257  0.01309  96  LYS A CA  
663  C C   . LYS A 98  ? 0.28181 0.40845 0.38135 0.01431  0.05636  0.01045  96  LYS A C   
664  O O   . LYS A 98  ? 0.30459 0.41881 0.39859 0.02068  0.05420  0.00533  96  LYS A O   
665  C CB  . LYS A 98  ? 0.32569 0.48003 0.42503 0.01885  0.06976  0.01171  96  LYS A CB  
666  C CG  . LYS A 98  ? 0.31461 0.46339 0.40948 0.03070  0.07166  0.00309  96  LYS A CG  
667  C CD  . LYS A 98  ? 0.35256 0.52159 0.45181 0.03768  0.08000  0.00083  96  LYS A CD  
668  N N   . SER A 99  ? 0.27043 0.40626 0.38159 0.00858  0.05335  0.01416  97  SER A N   
669  C CA  . SER A 99  ? 0.28589 0.41816 0.40219 0.00997  0.04719  0.01208  97  SER A CA  
670  C C   . SER A 99  ? 0.28823 0.39934 0.39521 0.00697  0.04153  0.00994  97  SER A C   
671  O O   . SER A 99  ? 0.27201 0.37529 0.37666 0.01149  0.03786  0.00678  97  SER A O   
672  C CB  . SER A 99  ? 0.28088 0.42986 0.41129 0.00333  0.04490  0.01608  97  SER A CB  
673  O OG  . SER A 99  ? 0.30787 0.47874 0.44868 0.00810  0.04994  0.01785  97  SER A OG  
674  N N   . PHE A 100 ? 0.26572 0.36841 0.36830 -0.00055 0.04081  0.01233  98  PHE A N   
675  C CA  . PHE A 100 ? 0.26514 0.34890 0.35981 -0.00260 0.03610  0.01016  98  PHE A CA  
676  C C   . PHE A 100 ? 0.26335 0.33554 0.34701 0.00459  0.03700  0.00665  98  PHE A C   
677  O O   . PHE A 100 ? 0.27276 0.33423 0.35231 0.00668  0.03309  0.00364  98  PHE A O   
678  C CB  . PHE A 100 ? 0.27792 0.35529 0.37166 -0.01099 0.03583  0.01428  98  PHE A CB  
679  C CG  . PHE A 100 ? 0.31819 0.37762 0.40673 -0.01332 0.03096  0.01202  98  PHE A CG  
680  C CD1 . PHE A 100 ? 0.30204 0.35885 0.39558 -0.01740 0.02587  0.00918  98  PHE A CD1 
681  C CD2 . PHE A 100 ? 0.29473 0.34139 0.37363 -0.01139 0.03152  0.01246  98  PHE A CD2 
682  C CE1 . PHE A 100 ? 0.27379 0.31500 0.36267 -0.01872 0.02213  0.00611  98  PHE A CE1 
683  C CE2 . PHE A 100 ? 0.30792 0.33952 0.38328 -0.01262 0.02757  0.01054  98  PHE A CE2 
684  C CZ  . PHE A 100 ? 0.35538 0.38382 0.43563 -0.01588 0.02320  0.00698  98  PHE A CZ  
685  N N   . TYR A 101 ? 0.24434 0.31985 0.32319 0.00803  0.04216  0.00681  99  TYR A N   
686  C CA  . TYR A 101 ? 0.29421 0.36007 0.36331 0.01440  0.04296  0.00254  99  TYR A CA  
687  C C   . TYR A 101 ? 0.26169 0.32692 0.33416 0.02141  0.04149  -0.00130 99  TYR A C   
688  O O   . TYR A 101 ? 0.24063 0.29362 0.30818 0.02362  0.03814  -0.00367 99  TYR A O   
689  C CB  . TYR A 101 ? 0.24664 0.31933 0.31020 0.01651  0.04900  0.00234  99  TYR A CB  
690  C CG  . TYR A 101 ? 0.28951 0.35406 0.34431 0.02318  0.04991  -0.00376 99  TYR A CG  
691  C CD1 . TYR A 101 ? 0.29454 0.34566 0.33923 0.02182  0.04715  -0.00484 99  TYR A CD1 
692  C CD2 . TYR A 101 ? 0.30767 0.37774 0.36527 0.03087  0.05327  -0.00863 99  TYR A CD2 
693  C CE1 . TYR A 101 ? 0.32702 0.37039 0.36419 0.02659  0.04725  -0.01071 99  TYR A CE1 
694  C CE2 . TYR A 101 ? 0.31037 0.37029 0.36046 0.03635  0.05351  -0.01510 99  TYR A CE2 
695  C CZ  . TYR A 101 ? 0.34176 0.38844 0.38145 0.03346  0.05029  -0.01612 99  TYR A CZ  
696  O OH  . TYR A 101 ? 0.39101 0.42757 0.42352 0.03732  0.04984  -0.02258 99  TYR A OH  
697  N N   . GLN A 102 ? 0.27172 0.35104 0.35364 0.02495  0.04391  -0.00099 100 GLN A N   
698  C CA  . GLN A 102 ? 0.27647 0.35584 0.36275 0.03292  0.04312  -0.00352 100 GLN A CA  
699  C C   . GLN A 102 ? 0.23842 0.31288 0.32728 0.03147  0.03669  -0.00212 100 GLN A C   
700  O O   . GLN A 102 ? 0.29657 0.36324 0.38423 0.03654  0.03449  -0.00336 100 GLN A O   
701  C CB  . GLN A 102 ? 0.29461 0.39277 0.39224 0.03729  0.04728  -0.00254 100 GLN A CB  
702  C CG  . GLN A 102 ? 0.37751 0.47531 0.47996 0.04761  0.04807  -0.00529 100 GLN A CG  
703  C CD  . GLN A 102 ? 0.41157 0.50089 0.50595 0.05375  0.05278  -0.01147 100 GLN A CD  
704  O OE1 . GLN A 102 ? 0.45213 0.52469 0.53971 0.05624  0.05047  -0.01479 100 GLN A OE1 
705  N NE2 . GLN A 102 ? 0.54654 0.64841 0.64138 0.05558  0.05944  -0.01324 100 GLN A NE2 
706  N N   . TRP A 103 ? 0.24581 0.32469 0.33793 0.02422  0.03358  0.00043  101 TRP A N   
707  C CA  . TRP A 103 ? 0.27002 0.34591 0.36288 0.02223  0.02758  0.00077  101 TRP A CA  
708  C C   . TRP A 103 ? 0.28173 0.34079 0.36421 0.02300  0.02540  -0.00126 101 TRP A C   
709  O O   . TRP A 103 ? 0.26585 0.32193 0.34773 0.02592  0.02215  -0.00100 101 TRP A O   
710  C CB  . TRP A 103 ? 0.25837 0.33985 0.35513 0.01341  0.02502  0.00195  101 TRP A CB  
711  C CG  . TRP A 103 ? 0.25785 0.34157 0.35651 0.01076  0.01906  0.00131  101 TRP A CG  
712  C CD1 . TRP A 103 ? 0.28404 0.38262 0.39135 0.01156  0.01613  0.00297  101 TRP A CD1 
713  C CD2 . TRP A 103 ? 0.25892 0.33154 0.35050 0.00687  0.01529  -0.00142 101 TRP A CD2 
714  N NE1 . TRP A 103 ? 0.28108 0.37857 0.38566 0.00789  0.01052  0.00116  101 TRP A NE1 
715  C CE2 . TRP A 103 ? 0.25228 0.33368 0.34719 0.00526  0.01030  -0.00205 101 TRP A CE2 
716  C CE3 . TRP A 103 ? 0.29799 0.35515 0.38078 0.00523  0.01571  -0.00343 101 TRP A CE3 
717  C CZ2 . TRP A 103 ? 0.32372 0.39894 0.41261 0.00201  0.00626  -0.00568 101 TRP A CZ2 
718  C CZ3 . TRP A 103 ? 0.28578 0.33651 0.36417 0.00262  0.01187  -0.00659 101 TRP A CZ3 
719  C CH2 . TRP A 103 ? 0.32271 0.38235 0.40364 0.00107  0.00744  -0.00823 101 TRP A CH2 
720  N N   . HIS A 104 ? 0.23906 0.28857 0.31384 0.02025  0.02708  -0.00233 102 HIS A N   
721  C CA  . HIS A 104 ? 0.23835 0.27397 0.30427 0.02077  0.02525  -0.00389 102 HIS A CA  
722  C C   . HIS A 104 ? 0.26519 0.29528 0.32842 0.02710  0.02630  -0.00538 102 HIS A C   
723  O O   . HIS A 104 ? 0.27278 0.29598 0.33351 0.02851  0.02342  -0.00532 102 HIS A O   
724  C CB  . HIS A 104 ? 0.25277 0.28164 0.31246 0.01675  0.02664  -0.00370 102 HIS A CB  
725  C CG  . HIS A 104 ? 0.25058 0.27871 0.31233 0.01062  0.02444  -0.00260 102 HIS A CG  
726  N ND1 . HIS A 104 ? 0.25465 0.29064 0.32274 0.00599  0.02560  -0.00042 102 HIS A ND1 
727  C CD2 . HIS A 104 ? 0.28242 0.30265 0.34149 0.00839  0.02115  -0.00384 102 HIS A CD2 
728  C CE1 . HIS A 104 ? 0.26575 0.29670 0.33504 0.00078  0.02267  -0.00070 102 HIS A CE1 
729  N NE2 . HIS A 104 ? 0.28171 0.30306 0.34529 0.00273  0.02018  -0.00324 102 HIS A NE2 
730  N N   . VAL A 105 ? 0.26776 0.30065 0.33149 0.03074  0.03054  -0.00696 103 VAL A N   
731  C CA  . VAL A 105 ? 0.29832 0.32455 0.36079 0.03698  0.03138  -0.00961 103 VAL A CA  
732  C C   . VAL A 105 ? 0.33303 0.36151 0.40331 0.04117  0.02863  -0.00722 103 VAL A C   
733  O O   . VAL A 105 ? 0.33844 0.35731 0.40720 0.04353  0.02633  -0.00697 103 VAL A O   
734  C CB  . VAL A 105 ? 0.32758 0.35843 0.38981 0.04090  0.03693  -0.01309 103 VAL A CB  
735  C CG1 . VAL A 105 ? 0.36885 0.39211 0.43181 0.04810  0.03779  -0.01705 103 VAL A CG1 
736  C CG2 . VAL A 105 ? 0.34466 0.37284 0.39701 0.03680  0.03901  -0.01466 103 VAL A CG2 
737  N N   . ASP A 106 ? 0.31548 0.35756 0.39468 0.04162  0.02846  -0.00452 104 ASP A N   
738  C CA  . ASP A 106 ? 0.34858 0.39566 0.43581 0.04591  0.02550  -0.00100 104 ASP A CA  
739  C C   . ASP A 106 ? 0.36164 0.40408 0.44523 0.04267  0.02022  0.00181  104 ASP A C   
740  O O   . ASP A 106 ? 0.40317 0.44417 0.48992 0.04653  0.01766  0.00529  104 ASP A O   
741  C CB  . ASP A 106 ? 0.34568 0.41124 0.44339 0.04591  0.02575  0.00160  104 ASP A CB  
742  C CG  . ASP A 106 ? 0.36910 0.44302 0.47339 0.05164  0.03138  -0.00011 104 ASP A CG  
743  O OD1 . ASP A 106 ? 0.34730 0.41202 0.44858 0.05727  0.03477  -0.00390 104 ASP A OD1 
744  O OD2 . ASP A 106 ? 0.42360 0.51470 0.53686 0.05061  0.03238  0.00206  104 ASP A OD2 
745  N N   . LEU A 107 ? 0.35507 0.39560 0.43240 0.03595  0.01871  0.00071  105 LEU A N   
746  C CA  . LEU A 107 ? 0.34265 0.37924 0.41527 0.03343  0.01467  0.00221  105 LEU A CA  
747  C C   . LEU A 107 ? 0.40171 0.42513 0.46892 0.03537  0.01464  0.00233  105 LEU A C   
748  O O   . LEU A 107 ? 0.43774 0.45997 0.50506 0.03651  0.01183  0.00601  105 LEU A O   
749  C CB  . LEU A 107 ? 0.32349 0.35976 0.39129 0.02692  0.01371  -0.00027 105 LEU A CB  
750  C CG  . LEU A 107 ? 0.30677 0.35492 0.37940 0.02298  0.01167  -0.00050 105 LEU A CG  
751  C CD1 . LEU A 107 ? 0.29267 0.33556 0.36073 0.01707  0.01132  -0.00392 105 LEU A CD1 
752  C CD2 . LEU A 107 ? 0.36363 0.41936 0.43741 0.02406  0.00743  0.00210  105 LEU A CD2 
753  N N   . ALA A 108 ? 0.35493 0.36943 0.41732 0.03506  0.01746  -0.00117 106 ALA A N   
754  C CA  . ALA A 108 ? 0.40394 0.40659 0.46064 0.03477  0.01674  -0.00171 106 ALA A CA  
755  C C   . ALA A 108 ? 0.43137 0.42605 0.49039 0.03961  0.01780  -0.00255 106 ALA A C   
756  O O   . ALA A 108 ? 0.46601 0.45084 0.52213 0.03887  0.01628  -0.00219 106 ALA A O   
757  C CB  . ALA A 108 ? 0.38329 0.38111 0.43272 0.03097  0.01815  -0.00497 106 ALA A CB  
758  N N   . TYR A 109 ? 0.42671 0.42516 0.49144 0.04451  0.02041  -0.00401 107 TYR A N   
759  C CA  . TYR A 109 ? 0.46854 0.45732 0.53522 0.04981  0.02197  -0.00689 107 TYR A CA  
760  C C   . TYR A 109 ? 0.50064 0.48860 0.57638 0.05494  0.01967  -0.00156 107 TYR A C   
761  O O   . TYR A 109 ? 0.59814 0.58799 0.68160 0.06175  0.02164  -0.00223 107 TYR A O   
762  C CB  . TYR A 109 ? 0.48607 0.47922 0.55330 0.05330  0.02703  -0.01256 107 TYR A CB  
763  N N   . ARG A 110 ? 0.51122 0.49740 0.58637 0.05197  0.01556  0.00441  108 ARG A N   
764  C CA  . ARG A 110 ? 0.52866 0.51366 0.61156 0.05592  0.01268  0.01160  108 ARG A CA  
765  C C   . ARG A 110 ? 0.53322 0.50402 0.61349 0.05323  0.01025  0.01412  108 ARG A C   
766  O O   . ARG A 110 ? 0.51674 0.48409 0.58917 0.04726  0.00984  0.01198  108 ARG A O   
767  C CB  . ARG A 110 ? 0.55136 0.55193 0.63671 0.05440  0.00964  0.01846  108 ARG A CB  
768  C CG  . ARG A 110 ? 0.52523 0.53208 0.60209 0.04713  0.00870  0.01705  108 ARG A CG  
769  C CD  . ARG A 110 ? 0.51865 0.54148 0.59765 0.04594  0.00558  0.02204  108 ARG A CD  
770  N NE  . ARG A 110 ? 0.53439 0.56024 0.60563 0.04024  0.00362  0.02262  108 ARG A NE  
771  C CZ  . ARG A 110 ? 0.51970 0.55293 0.58648 0.03597  0.00354  0.01842  108 ARG A CZ  
772  N NH1 . ARG A 110 ? 0.46471 0.50290 0.53395 0.03537  0.00505  0.01409  108 ARG A NH1 
773  N NH2 . ARG A 110 ? 0.50447 0.54043 0.56478 0.03221  0.00201  0.01864  108 ARG A NH2 
774  N N   . GLU A 111 ? 0.57058 0.53335 0.65855 0.05763  0.00853  0.01925  109 GLU A N   
775  C CA  . GLU A 111 ? 0.53782 0.48707 0.62509 0.05419  0.00586  0.02307  109 GLU A CA  
776  C C   . GLU A 111 ? 0.52920 0.48785 0.61182 0.04771  0.00304  0.03028  109 GLU A C   
777  O O   . GLU A 111 ? 0.53155 0.50527 0.61496 0.04811  0.00180  0.03549  109 GLU A O   
778  C CB  . GLU A 111 ? 0.58554 0.52455 0.68364 0.06020  0.00413  0.02919  109 GLU A CB  
779  N N   . GLY A 112 ? 0.46988 0.42104 0.54747 0.04163  0.00210  0.02989  110 GLY A N   
780  C CA  . GLY A 112 ? 0.49525 0.45594 0.56874 0.03599  0.00017  0.03626  110 GLY A CA  
781  C C   . GLY A 112 ? 0.47911 0.45283 0.54497 0.03326  0.00160  0.03167  110 GLY A C   
782  O O   . GLY A 112 ? 0.45279 0.43683 0.51536 0.02994  0.00047  0.03605  110 GLY A O   
783  N N   . TYR A 113 ? 0.44110 0.41464 0.50426 0.03463  0.00420  0.02311  111 TYR A N   
784  C CA  . TYR A 113 ? 0.42636 0.40970 0.48352 0.03203  0.00539  0.01902  111 TYR A CA  
785  C C   . TYR A 113 ? 0.43518 0.41807 0.48670 0.02692  0.00493  0.01880  111 TYR A C   
786  O O   . TYR A 113 ? 0.46788 0.44129 0.51820 0.02474  0.00482  0.01715  111 TYR A O   
787  C CB  . TYR A 113 ? 0.42217 0.40359 0.47798 0.03365  0.00833  0.01129  111 TYR A CB  
788  C CG  . TYR A 113 ? 0.39399 0.38389 0.44549 0.03110  0.00935  0.00798  111 TYR A CG  
789  C CD1 . TYR A 113 ? 0.37288 0.37423 0.42653 0.03149  0.00866  0.00928  111 TYR A CD1 
790  C CD2 . TYR A 113 ? 0.40063 0.38679 0.44651 0.02819  0.01062  0.00366  111 TYR A CD2 
791  C CE1 . TYR A 113 ? 0.35094 0.35761 0.40156 0.02872  0.00927  0.00574  111 TYR A CE1 
792  C CE2 . TYR A 113 ? 0.35898 0.35072 0.40225 0.02621  0.01141  0.00130  111 TYR A CE2 
793  C CZ  . TYR A 113 ? 0.34987 0.35080 0.39568 0.02632  0.01077  0.00201  111 TYR A CZ  
794  O OH  . TYR A 113 ? 0.29243 0.29660 0.33640 0.02383  0.01125  -0.00089 111 TYR A OH  
795  N N   . ASN A 114 ? 0.40198 0.39607 0.45038 0.02512  0.00455  0.02004  112 ASN A N   
796  C CA  . ASN A 114 ? 0.37283 0.36926 0.41677 0.02151  0.00472  0.01936  112 ASN A CA  
797  C C   . ASN A 114 ? 0.37062 0.37580 0.41083 0.02136  0.00572  0.01508  112 ASN A C   
798  O O   . ASN A 114 ? 0.38101 0.39310 0.41845 0.01990  0.00577  0.01562  112 ASN A O   
799  C CB  . ASN A 114 ? 0.39292 0.39378 0.43794 0.01927  0.00312  0.02715  112 ASN A CB  
800  C CG  . ASN A 114 ? 0.41946 0.43283 0.46470 0.02050  0.00203  0.03231  112 ASN A CG  
801  O OD1 . ASN A 114 ? 0.38224 0.39862 0.42914 0.02335  0.00158  0.03147  112 ASN A OD1 
802  N ND2 . ASN A 114 ? 0.41903 0.44185 0.46254 0.01818  0.00158  0.03788  112 ASN A ND2 
803  N N   . GLY A 115 ? 0.34014 0.34515 0.38083 0.02283  0.00666  0.01067  113 GLY A N   
804  C CA  . GLY A 115 ? 0.31460 0.32482 0.35295 0.02209  0.00731  0.00603  113 GLY A CA  
805  C C   . GLY A 115 ? 0.33888 0.35821 0.37925 0.02280  0.00607  0.00613  113 GLY A C   
806  O O   . GLY A 115 ? 0.30874 0.33387 0.35126 0.02401  0.00435  0.01112  113 GLY A O   
807  N N   . THR A 116 ? 0.30349 0.32449 0.34365 0.02159  0.00654  0.00107  114 THR A N   
808  C CA  . THR A 116 ? 0.32284 0.35374 0.36507 0.02103  0.00473  0.00026  114 THR A CA  
809  C C   . THR A 116 ? 0.31549 0.35573 0.35328 0.01990  0.00294  -0.00076 114 THR A C   
810  O O   . THR A 116 ? 0.26057 0.29933 0.29407 0.01966  0.00391  -0.00236 114 THR A O   
811  C CB  . THR A 116 ? 0.33873 0.36824 0.38297 0.01884  0.00548  -0.00474 114 THR A CB  
812  O OG1 . THR A 116 ? 0.31339 0.33972 0.35379 0.01684  0.00573  -0.00964 114 THR A OG1 
813  C CG2 . THR A 116 ? 0.29773 0.31916 0.34437 0.01967  0.00816  -0.00433 114 THR A CG2 
814  N N   . LEU A 117 ? 0.28510 0.33680 0.32396 0.01932  0.00035  -0.00021 115 LEU A N   
815  C CA  . LEU A 117 ? 0.30021 0.36306 0.33349 0.01811  -0.00146 -0.00211 115 LEU A CA  
816  C C   . LEU A 117 ? 0.27670 0.33605 0.30602 0.01617  -0.00044 -0.01139 115 LEU A C   
817  O O   . LEU A 117 ? 0.27926 0.34368 0.30283 0.01648  -0.00005 -0.01413 115 LEU A O   
818  C CB  . LEU A 117 ? 0.28808 0.36540 0.32281 0.01724  -0.00516 -0.00049 115 LEU A CB  
819  C CG  . LEU A 117 ? 0.35341 0.43846 0.39052 0.01990  -0.00699 0.00998  115 LEU A CG  
820  C CD1 . LEU A 117 ? 0.39232 0.48930 0.43510 0.02011  -0.01054 0.01283  115 LEU A CD1 
821  C CD2 . LEU A 117 ? 0.33037 0.42429 0.36036 0.01975  -0.00747 0.01330  115 LEU A CD2 
822  N N   . LEU A 118 ? 0.25689 0.30780 0.28965 0.01440  0.00020  -0.01610 116 LEU A N   
823  C CA  . LEU A 118 ? 0.28447 0.32952 0.31481 0.01292  0.00095  -0.02446 116 LEU A CA  
824  C C   . LEU A 118 ? 0.31031 0.34709 0.33843 0.01562  0.00390  -0.02408 116 LEU A C   
825  O O   . LEU A 118 ? 0.27897 0.31548 0.30369 0.01659  0.00473  -0.02971 116 LEU A O   
826  C CB  . LEU A 118 ? 0.27862 0.31617 0.31434 0.00965  0.00074  -0.02777 116 LEU A CB  
827  C CG  . LEU A 118 ? 0.29156 0.33710 0.32936 0.00523  -0.00269 -0.03252 116 LEU A CG  
828  C CD1 . LEU A 118 ? 0.26223 0.32317 0.30016 0.00569  -0.00536 -0.02786 116 LEU A CD1 
829  C CD2 . LEU A 118 ? 0.32874 0.36810 0.37391 0.00148  -0.00246 -0.03253 116 LEU A CD2 
830  N N   . THR A 119 ? 0.31173 0.34246 0.34202 0.01703  0.00541  -0.01799 117 THR A N   
831  C CA  . THR A 119 ? 0.31235 0.33718 0.34122 0.01899  0.00753  -0.01713 117 THR A CA  
832  C C   . THR A 119 ? 0.32458 0.35895 0.34972 0.02049  0.00778  -0.01500 117 THR A C   
833  O O   . THR A 119 ? 0.33810 0.37352 0.36130 0.02216  0.00934  -0.01803 117 THR A O   
834  C CB  . THR A 119 ? 0.28204 0.29907 0.31337 0.01928  0.00851  -0.01201 117 THR A CB  
835  O OG1 . THR A 119 ? 0.33003 0.33991 0.36406 0.01789  0.00901  -0.01389 117 THR A OG1 
836  C CG2 . THR A 119 ? 0.28837 0.30193 0.31849 0.02065  0.00985  -0.01037 117 THR A CG2 
837  N N   . LYS A 120 ? 0.30304 0.34552 0.32780 0.02015  0.00636  -0.00929 118 LYS A N   
838  C CA  . LYS A 120 ? 0.26376 0.31733 0.28512 0.02079  0.00653  -0.00532 118 LYS A CA  
839  C C   . LYS A 120 ? 0.30552 0.36921 0.32151 0.02129  0.00690  -0.01227 118 LYS A C   
840  O O   . LYS A 120 ? 0.30387 0.37507 0.31680 0.02267  0.00883  -0.01206 118 LYS A O   
841  C CB  . LYS A 120 ? 0.28122 0.34127 0.30386 0.02029  0.00438  0.00299  118 LYS A CB  
842  C CG  . LYS A 120 ? 0.32849 0.37869 0.35619 0.02049  0.00433  0.00976  118 LYS A CG  
843  C CD  . LYS A 120 ? 0.34255 0.39887 0.37264 0.02093  0.00195  0.01803  118 LYS A CD  
844  C CE  . LYS A 120 ? 0.38389 0.42855 0.41980 0.02179  0.00177  0.02355  118 LYS A CE  
845  N NZ  . LYS A 120 ? 0.38323 0.43245 0.42324 0.02340  -0.00069 0.03150  118 LYS A NZ  
846  N N   . ALA A 121 ? 0.27498 0.33993 0.28990 0.02001  0.00512  -0.01899 119 ALA A N   
847  C CA  . ALA A 121 ? 0.32646 0.40091 0.33534 0.02028  0.00511  -0.02738 119 ALA A CA  
848  C C   . ALA A 121 ? 0.34214 0.40875 0.35087 0.02280  0.00805  -0.03526 119 ALA A C   
849  O O   . ALA A 121 ? 0.31052 0.38610 0.31441 0.02517  0.00998  -0.03988 119 ALA A O   
850  C CB  . ALA A 121 ? 0.30924 0.38680 0.31756 0.01724  0.00169  -0.03319 119 ALA A CB  
851  N N   . VAL A 122 ? 0.32079 0.37170 0.33502 0.02283  0.00861  -0.03635 120 VAL A N   
852  C CA  . VAL A 122 ? 0.36672 0.40906 0.38246 0.02591  0.01101  -0.04235 120 VAL A CA  
853  C C   . VAL A 122 ? 0.35917 0.40720 0.37477 0.02938  0.01386  -0.03758 120 VAL A C   
854  O O   . VAL A 122 ? 0.39207 0.44284 0.40692 0.03331  0.01634  -0.04298 120 VAL A O   
855  C CB  . VAL A 122 ? 0.35486 0.38054 0.37671 0.02466  0.01057  -0.04186 120 VAL A CB  
856  C CG1 . VAL A 122 ? 0.38691 0.40384 0.41168 0.02863  0.01282  -0.04460 120 VAL A CG1 
857  C CG2 . VAL A 122 ? 0.34744 0.36870 0.37055 0.02071  0.00805  -0.04742 120 VAL A CG2 
858  N N   . ILE A 123 ? 0.33977 0.39000 0.35684 0.02799  0.01354  -0.02770 121 ILE A N   
859  C CA  . ILE A 123 ? 0.40167 0.45799 0.41980 0.02976  0.01564  -0.02222 121 ILE A CA  
860  C C   . ILE A 123 ? 0.42192 0.49644 0.43518 0.03044  0.01701  -0.02112 121 ILE A C   
861  O O   . ILE A 123 ? 0.45536 0.53842 0.46862 0.03342  0.01995  -0.02209 121 ILE A O   
862  C CB  . ILE A 123 ? 0.38371 0.43383 0.40543 0.02711  0.01432  -0.01310 121 ILE A CB  
863  C CG1 . ILE A 123 ? 0.44989 0.48565 0.47547 0.02760  0.01420  -0.01474 121 ILE A CG1 
864  C CG2 . ILE A 123 ? 0.39068 0.44986 0.41343 0.02649  0.01527  -0.00544 121 ILE A CG2 
865  C CD1 . ILE A 123 ? 0.43966 0.46771 0.46742 0.02504  0.01281  -0.00881 121 ILE A CD1 
866  N N   . GLU A 124 ? 0.35061 0.43328 0.35979 0.02801  0.01505  -0.01887 122 GLU A N   
867  C CA  . GLU A 124 ? 0.37373 0.47575 0.37740 0.02825  0.01628  -0.01632 122 GLU A CA  
868  C C   . GLU A 124 ? 0.44307 0.55368 0.44081 0.03143  0.01838  -0.02823 122 GLU A C   
869  O O   . GLU A 124 ? 0.35071 0.47679 0.34496 0.03371  0.02159  -0.02846 122 GLU A O   
870  C CB  . GLU A 124 ? 0.39385 0.50287 0.39513 0.02498  0.01303  -0.00911 122 GLU A CB  
871  N N   . TYR A 125 ? 0.42526 0.52643 0.42207 0.03155  0.01680  -0.03862 123 TYR A N   
872  C CA  . TYR A 125 ? 0.43600 0.54440 0.42671 0.03436  0.01846  -0.05141 123 TYR A CA  
873  C C   . TYR A 125 ? 0.46703 0.56051 0.46241 0.03853  0.02053  -0.06113 123 TYR A C   
874  O O   . TYR A 125 ? 0.46804 0.55239 0.46257 0.03831  0.01910  -0.07217 123 TYR A O   
875  C CB  . TYR A 125 ? 0.43066 0.54314 0.41562 0.03073  0.01454  -0.05725 123 TYR A CB  
876  C CG  . TYR A 125 ? 0.45288 0.58316 0.43302 0.02785  0.01260  -0.04705 123 TYR A CG  
877  C CD1 . TYR A 125 ? 0.50810 0.66029 0.47972 0.02913  0.01466  -0.04676 123 TYR A CD1 
878  C CD2 . TYR A 125 ? 0.43932 0.56528 0.42389 0.02439  0.00904  -0.03684 123 TYR A CD2 
879  C CE1 . TYR A 125 ? 0.50823 0.67699 0.47592 0.02635  0.01262  -0.03527 123 TYR A CE1 
880  C CE2 . TYR A 125 ? 0.45265 0.59363 0.43427 0.02244  0.00701  -0.02624 123 TYR A CE2 
881  C CZ  . TYR A 125 ? 0.49398 0.65585 0.46731 0.02312  0.00854  -0.02474 123 TYR A CZ  
882  O OH  . TYR A 125 ? 0.49998 0.67646 0.47106 0.02096  0.00610  -0.01222 123 TYR A OH  
883  N N   . TRP A 126 ? 0.45645 0.54757 0.45750 0.04213  0.02355  -0.05664 124 TRP A N   
884  C CA  . TRP A 126 ? 0.51166 0.59128 0.51788 0.04754  0.02581  -0.06455 124 TRP A CA  
885  C C   . TRP A 126 ? 0.53327 0.61999 0.53433 0.05242  0.02855  -0.07864 124 TRP A C   
886  O O   . TRP A 126 ? 0.56150 0.63476 0.56653 0.05664  0.02944  -0.08824 124 TRP A O   
887  C CB  . TRP A 126 ? 0.52728 0.60962 0.54013 0.05082  0.02849  -0.05633 124 TRP A CB  
888  C CG  . TRP A 126 ? 0.50141 0.60609 0.51078 0.05098  0.03113  -0.05034 124 TRP A CG  
889  C CD1 . TRP A 126 ? 0.46883 0.58147 0.47764 0.04587  0.02971  -0.03804 124 TRP A CD1 
890  C CD2 . TRP A 126 ? 0.47573 0.59838 0.48188 0.05637  0.03587  -0.05619 124 TRP A CD2 
891  N NE1 . TRP A 126 ? 0.49803 0.63251 0.50374 0.04685  0.03298  -0.03454 124 TRP A NE1 
892  C CE2 . TRP A 126 ? 0.47119 0.61361 0.47484 0.05338  0.03708  -0.04557 124 TRP A CE2 
893  C CE3 . TRP A 126 ? 0.47140 0.59521 0.47692 0.06367  0.03941  -0.06951 124 TRP A CE3 
894  C CZ2 . TRP A 126 ? 0.51142 0.67713 0.51159 0.05701  0.04203  -0.04698 124 TRP A CZ2 
895  C CZ3 . TRP A 126 ? 0.52144 0.66823 0.52311 0.06827  0.04459  -0.07251 124 TRP A CZ3 
896  C CH2 . TRP A 126 ? 0.48047 0.64904 0.47933 0.06472  0.04599  -0.06087 124 TRP A CH2 
897  N N   . ASN A 127 ? 0.48507 0.59266 0.47730 0.05211  0.02994  -0.08010 125 ASN A N   
898  C CA  . ASN A 127 ? 0.49716 0.61452 0.48285 0.05713  0.03314  -0.09444 125 ASN A CA  
899  C C   . ASN A 127 ? 0.55532 0.66623 0.53467 0.05396  0.02955  -0.10739 125 ASN A C   
900  O O   . ASN A 127 ? 0.50866 0.62315 0.48271 0.05806  0.03169  -0.12238 125 ASN A O   
901  C CB  . ASN A 127 ? 0.50703 0.65280 0.48512 0.05802  0.03662  -0.08987 125 ASN A CB  
902  C CG  . ASN A 127 ? 0.50343 0.66123 0.47419 0.05070  0.03278  -0.08115 125 ASN A CG  
903  O OD1 . ASN A 127 ? 0.48174 0.63279 0.45719 0.04579  0.02944  -0.06839 125 ASN A OD1 
904  N ND2 . ASN A 127 ? 0.52003 0.69672 0.47924 0.05042  0.03328  -0.08787 125 ASN A ND2 
905  N N   . LEU A 128 ? 0.47425 0.57653 0.45438 0.04676  0.02417  -0.10256 126 LEU A N   
906  C CA  . LEU A 128 ? 0.52399 0.62105 0.49969 0.04222  0.01986  -0.11350 126 LEU A CA  
907  C C   . LEU A 128 ? 0.53824 0.60886 0.52388 0.04025  0.01734  -0.11530 126 LEU A C   
908  O O   . LEU A 128 ? 0.52001 0.58392 0.51043 0.03505  0.01409  -0.10533 126 LEU A O   
909  C CB  . LEU A 128 ? 0.48397 0.59516 0.45396 0.03544  0.01551  -0.10548 126 LEU A CB  
910  C CG  . LEU A 128 ? 0.49038 0.62888 0.45052 0.03568  0.01684  -0.09997 126 LEU A CG  
911  C CD1 . LEU A 128 ? 0.46688 0.61631 0.42219 0.02908  0.01120  -0.09469 126 LEU A CD1 
912  C CD2 . LEU A 128 ? 0.54179 0.69315 0.49260 0.04052  0.02064  -0.11468 126 LEU A CD2 
913  N N   . PRO A 129 ? 0.56317 0.61835 0.55278 0.04454  0.01894  -0.12718 127 PRO A N   
914  C CA  . PRO A 129 ? 0.54493 0.57481 0.54493 0.04247  0.01669  -0.12653 127 PRO A CA  
915  C C   . PRO A 129 ? 0.51494 0.53843 0.51518 0.03336  0.01101  -0.12818 127 PRO A C   
916  O O   . PRO A 129 ? 0.51299 0.51940 0.52190 0.02996  0.00903  -0.12328 127 PRO A O   
917  C CB  . PRO A 129 ? 0.59069 0.60695 0.59407 0.04929  0.01932  -0.14048 127 PRO A CB  
918  C CG  . PRO A 129 ? 0.59191 0.62741 0.58679 0.05588  0.02373  -0.14872 127 PRO A CG  
919  C CD  . PRO A 129 ? 0.57196 0.63270 0.55709 0.05194  0.02318  -0.14120 127 PRO A CD  
920  N N   . ASP A 130 ? 0.52107 0.55966 0.51227 0.02913  0.00828  -0.13426 128 ASP A N   
921  C CA  . ASP A 130 ? 0.44988 0.48651 0.44213 0.02012  0.00248  -0.13464 128 ASP A CA  
922  C C   . ASP A 130 ? 0.47728 0.51555 0.47508 0.01653  0.00103  -0.11755 128 ASP A C   
923  O O   . ASP A 130 ? 0.44120 0.46987 0.44569 0.01055  -0.00228 -0.11508 128 ASP A O   
924  C CB  . ASP A 130 ? 0.47392 0.53083 0.45465 0.01686  -0.00040 -0.14305 128 ASP A CB  
925  N N   . ILE A 131 ? 0.43227 0.48280 0.42787 0.01990  0.00356  -0.10581 129 ILE A N   
926  C CA  . ILE A 131 ? 0.38278 0.43368 0.38353 0.01705  0.00226  -0.09118 129 ILE A CA  
927  C C   . ILE A 131 ? 0.43324 0.46438 0.44362 0.01751  0.00355  -0.08621 129 ILE A C   
928  O O   . ILE A 131 ? 0.40331 0.42875 0.41930 0.01289  0.00130  -0.08086 129 ILE A O   
929  C CB  . ILE A 131 ? 0.40415 0.47109 0.40091 0.01972  0.00407  -0.07985 129 ILE A CB  
930  C CG1 . ILE A 131 ? 0.45246 0.54071 0.44046 0.01756  0.00155  -0.08073 129 ILE A CG1 
931  C CG2 . ILE A 131 ? 0.42646 0.48803 0.42996 0.01850  0.00377  -0.06630 129 ILE A CG2 
932  C CD1 . ILE A 131 ? 0.44331 0.54577 0.42281 0.02158  0.00455  -0.08466 129 ILE A CD1 
933  N N   . LYS A 132 ? 0.43664 0.45909 0.44927 0.02323  0.00722  -0.08712 130 LYS A N   
934  C CA  . LYS A 132 ? 0.45335 0.45865 0.47453 0.02356  0.00799  -0.08140 130 LYS A CA  
935  C C   . LYS A 132 ? 0.42654 0.41716 0.45316 0.01838  0.00518  -0.08678 130 LYS A C   
936  O O   . LYS A 132 ? 0.41758 0.39927 0.45045 0.01515  0.00444  -0.07938 130 LYS A O   
937  C CB  . LYS A 132 ? 0.48542 0.48444 0.50908 0.03082  0.01170  -0.08228 130 LYS A CB  
938  C CG  . LYS A 132 ? 0.51317 0.49668 0.54505 0.03097  0.01195  -0.07448 130 LYS A CG  
939  C CD  . LYS A 132 ? 0.56976 0.55306 0.60430 0.03794  0.01510  -0.07027 130 LYS A CD  
940  C CE  . LYS A 132 ? 0.59595 0.56091 0.63856 0.04031  0.01516  -0.07052 130 LYS A CE  
941  N NZ  . LYS A 132 ? 0.71684 0.67609 0.76118 0.04644  0.01680  -0.08210 130 LYS A NZ  
942  N N   . MET A 133 ? 0.41235 0.40100 0.43661 0.01700  0.00357  -0.09977 131 MET A N   
943  C CA  . MET A 133 ? 0.46890 0.44189 0.49965 0.01124  0.00064  -0.10498 131 MET A CA  
944  C C   . MET A 133 ? 0.43428 0.41479 0.46644 0.00266  -0.00333 -0.10097 131 MET A C   
945  O O   . MET A 133 ? 0.45111 0.42062 0.49124 -0.00272 -0.00492 -0.09768 131 MET A O   
946  C CB  . MET A 133 ? 0.48920 0.45525 0.51767 0.01235  -0.00006 -0.12163 131 MET A CB  
947  C CG  . MET A 133 ? 0.56359 0.52151 0.59540 0.00357  -0.00483 -0.12980 131 MET A CG  
948  S SD  . MET A 133 ? 0.88395 0.82814 0.91406 0.00654  -0.00493 -0.15048 131 MET A SD  
949  C CE  . MET A 133 ? 0.64173 0.56038 0.68325 0.01345  -0.00136 -0.14538 131 MET A CE  
950  N N   . LYS A 134 ? 0.40961 0.40986 0.43507 0.00149  -0.00484 -0.09973 132 LYS A N   
951  C CA  . LYS A 134 ? 0.40352 0.41296 0.43190 -0.00538 -0.00845 -0.09425 132 LYS A CA  
952  C C   . LYS A 134 ? 0.38244 0.39042 0.41658 -0.00480 -0.00656 -0.08010 132 LYS A C   
953  O O   . LYS A 134 ? 0.37094 0.37858 0.41174 -0.01031 -0.00838 -0.07576 132 LYS A O   
954  C CB  . LYS A 134 ? 0.39546 0.42709 0.41564 -0.00592 -0.01086 -0.09546 132 LYS A CB  
955  C CG  . LYS A 134 ? 0.48324 0.51922 0.49529 -0.00595 -0.01233 -0.11029 132 LYS A CG  
956  C CD  . LYS A 134 ? 0.49052 0.54980 0.49183 -0.00373 -0.01294 -0.10980 132 LYS A CD  
957  C CE  . LYS A 134 ? 0.54385 0.61892 0.54221 -0.01055 -0.01893 -0.11359 132 LYS A CE  
958  N NZ  . LYS A 134 ? 0.54902 0.61637 0.54751 -0.01663 -0.02270 -0.12951 132 LYS A NZ  
959  N N   . VAL A 135 ? 0.36556 0.37345 0.39745 0.00154  -0.00287 -0.07323 133 VAL A N   
960  C CA  . VAL A 135 ? 0.36674 0.37258 0.40307 0.00210  -0.00114 -0.06148 133 VAL A CA  
961  C C   . VAL A 135 ? 0.37526 0.36428 0.41844 0.00055  0.00002  -0.05981 133 VAL A C   
962  O O   . VAL A 135 ? 0.32089 0.30855 0.36928 -0.00267 0.00014  -0.05292 133 VAL A O   
963  C CB  . VAL A 135 ? 0.33441 0.34529 0.36641 0.00816  0.00172  -0.05518 133 VAL A CB  
964  C CG1 . VAL A 135 ? 0.29367 0.29996 0.32961 0.00874  0.00345  -0.04532 133 VAL A CG1 
965  C CG2 . VAL A 135 ? 0.34384 0.37228 0.37010 0.00871  0.00026  -0.05406 133 VAL A CG2 
966  N N   . GLU A 136 ? 0.37652 0.35328 0.42013 0.00310  0.00102  -0.06572 134 GLU A N   
967  C CA  . GLU A 136 ? 0.41390 0.37400 0.46465 0.00154  0.00159  -0.06330 134 GLU A CA  
968  C C   . GLU A 136 ? 0.41256 0.36904 0.46961 -0.00701 -0.00132 -0.06468 134 GLU A C   
969  O O   . GLU A 136 ? 0.40480 0.35600 0.46789 -0.01048 -0.00076 -0.05683 134 GLU A O   
970  C CB  . GLU A 136 ? 0.44332 0.39102 0.49451 0.00652  0.00270  -0.07043 134 GLU A CB  
971  C CG  . GLU A 136 ? 0.51736 0.44922 0.57543 0.00765  0.00388  -0.06434 134 GLU A CG  
972  C CD  . GLU A 136 ? 0.64580 0.56623 0.70557 0.01433  0.00516  -0.07051 134 GLU A CD  
973  O OE1 . GLU A 136 ? 0.64281 0.57086 0.69831 0.02148  0.00751  -0.07099 134 GLU A OE1 
974  O OE2 . GLU A 136 ? 0.66013 0.56395 0.72650 0.01246  0.00386  -0.07445 134 GLU A OE2 
975  N N   . ASP A 137 ? 0.38218 0.34327 0.43776 -0.01097 -0.00454 -0.07445 135 ASP A N   
976  C CA  . ASP A 137 ? 0.38993 0.34910 0.45227 -0.02024 -0.00804 -0.07661 135 ASP A CA  
977  C C   . ASP A 137 ? 0.40441 0.37766 0.47000 -0.02402 -0.00827 -0.06680 135 ASP A C   
978  O O   . ASP A 137 ? 0.39664 0.36730 0.47050 -0.03083 -0.00919 -0.06268 135 ASP A O   
979  C CB  . ASP A 137 ? 0.42835 0.39242 0.48694 -0.02366 -0.01201 -0.09014 135 ASP A CB  
980  C CG  . ASP A 137 ? 0.54112 0.48708 0.59991 -0.02221 -0.01232 -0.10212 135 ASP A CG  
981  O OD1 . ASP A 137 ? 0.54841 0.47584 0.61357 -0.02073 -0.01050 -0.09899 135 ASP A OD1 
982  O OD2 . ASP A 137 ? 0.58435 0.53504 0.63702 -0.02254 -0.01458 -0.11500 135 ASP A OD2 
983  N N   . PHE A 138 ? 0.35702 0.34571 0.41700 -0.01966 -0.00739 -0.06288 136 PHE A N   
984  C CA  . PHE A 138 ? 0.38035 0.38091 0.44409 -0.02104 -0.00677 -0.05339 136 PHE A CA  
985  C C   . PHE A 138 ? 0.38487 0.37678 0.45238 -0.01972 -0.00293 -0.04434 136 PHE A C   
986  O O   . PHE A 138 ? 0.33512 0.33095 0.40924 -0.02400 -0.00238 -0.03847 136 PHE A O   
987  C CB  . PHE A 138 ? 0.31262 0.32812 0.37027 -0.01562 -0.00645 -0.05029 136 PHE A CB  
988  C CG  . PHE A 138 ? 0.36063 0.38542 0.42258 -0.01483 -0.00497 -0.04075 136 PHE A CG  
989  C CD1 . PHE A 138 ? 0.31599 0.35314 0.38470 -0.01972 -0.00738 -0.03914 136 PHE A CD1 
990  C CD2 . PHE A 138 ? 0.35221 0.37335 0.41227 -0.00935 -0.00114 -0.03398 136 PHE A CD2 
991  C CE1 . PHE A 138 ? 0.32495 0.37100 0.39870 -0.01798 -0.00541 -0.03106 136 PHE A CE1 
992  C CE2 . PHE A 138 ? 0.33231 0.36072 0.39630 -0.00807 0.00061  -0.02688 136 PHE A CE2 
993  C CZ  . PHE A 138 ? 0.33510 0.37608 0.40614 -0.01181 -0.00120 -0.02542 136 PHE A CZ  
994  N N   . ASN A 139 ? 0.33560 0.31761 0.39897 -0.01390 -0.00024 -0.04294 137 ASN A N   
995  C CA  . ASN A 139 ? 0.37798 0.35376 0.44341 -0.01261 0.00294  -0.03431 137 ASN A CA  
996  C C   . ASN A 139 ? 0.37517 0.33962 0.44803 -0.01849 0.00264  -0.03236 137 ASN A C   
997  O O   . ASN A 139 ? 0.36020 0.32623 0.43654 -0.02074 0.00466  -0.02419 137 ASN A O   
998  C CB  . ASN A 139 ? 0.38745 0.35743 0.44718 -0.00544 0.00508  -0.03310 137 ASN A CB  
999  C CG  . ASN A 139 ? 0.38699 0.36807 0.44102 -0.00080 0.00605  -0.03092 137 ASN A CG  
1000 O OD1 . ASN A 139 ? 0.45508 0.44593 0.51011 -0.00185 0.00615  -0.02750 137 ASN A OD1 
1001 N ND2 . ASN A 139 ? 0.38040 0.36018 0.42948 0.00443  0.00682  -0.03247 137 ASN A ND2 
1002 N N   . LYS A 140 ? 0.34511 0.29838 0.42070 -0.02132 0.00021  -0.03963 138 LYS A N   
1003 C CA  . LYS A 140 ? 0.38114 0.32354 0.46558 -0.02858 -0.00079 -0.03717 138 LYS A CA  
1004 C C   . LYS A 140 ? 0.41629 0.37102 0.50692 -0.03684 -0.00227 -0.03485 138 LYS A C   
1005 O O   . LYS A 140 ? 0.36005 0.31415 0.45755 -0.04220 -0.00108 -0.02672 138 LYS A O   
1006 C CB  . LYS A 140 ? 0.41315 0.33919 0.50012 -0.03008 -0.00354 -0.04702 138 LYS A CB  
1007 C CG  . LYS A 140 ? 0.41958 0.33047 0.50482 -0.02250 -0.00180 -0.04744 138 LYS A CG  
1008 N N   . TRP A 141 ? 0.38770 0.35556 0.47636 -0.03801 -0.00487 -0.04114 139 TRP A N   
1009 C CA  . TRP A 141 ? 0.37064 0.35350 0.46611 -0.04506 -0.00649 -0.03845 139 TRP A CA  
1010 C C   . TRP A 141 ? 0.32717 0.32087 0.42435 -0.04288 -0.00224 -0.02731 139 TRP A C   
1011 O O   . TRP A 141 ? 0.32737 0.32697 0.43290 -0.04919 -0.00147 -0.02129 139 TRP A O   
1012 C CB  . TRP A 141 ? 0.37190 0.36962 0.46381 -0.04488 -0.01011 -0.04573 139 TRP A CB  
1013 C CG  . TRP A 141 ? 0.33013 0.34601 0.43000 -0.05137 -0.01228 -0.04269 139 TRP A CG  
1014 C CD1 . TRP A 141 ? 0.37868 0.39738 0.48649 -0.06157 -0.01675 -0.04685 139 TRP A CD1 
1015 C CD2 . TRP A 141 ? 0.31911 0.35345 0.42073 -0.04792 -0.01027 -0.03514 139 TRP A CD2 
1016 N NE1 . TRP A 141 ? 0.34187 0.38172 0.45678 -0.06480 -0.01762 -0.04154 139 TRP A NE1 
1017 C CE2 . TRP A 141 ? 0.32894 0.37839 0.44034 -0.05586 -0.01345 -0.03440 139 TRP A CE2 
1018 C CE3 . TRP A 141 ? 0.30761 0.34673 0.40426 -0.03892 -0.00623 -0.02932 139 TRP A CE3 
1019 C CZ2 . TRP A 141 ? 0.35792 0.42787 0.47478 -0.05392 -0.01225 -0.02759 139 TRP A CZ2 
1020 C CZ3 . TRP A 141 ? 0.33224 0.38927 0.43375 -0.03707 -0.00512 -0.02345 139 TRP A CZ3 
1021 C CH2 . TRP A 141 ? 0.29950 0.37220 0.41127 -0.04395 -0.00789 -0.02243 139 TRP A CH2 
1022 N N   . LYS A 142 ? 0.35860 0.35562 0.44815 -0.03421 0.00065  -0.02483 140 LYS A N   
1023 C CA  . LYS A 142 ? 0.37273 0.37999 0.46298 -0.03145 0.00466  -0.01642 140 LYS A CA  
1024 C C   . LYS A 142 ? 0.37288 0.37292 0.46614 -0.03412 0.00788  -0.00881 140 LYS A C   
1025 O O   . LYS A 142 ? 0.32813 0.33879 0.42669 -0.03712 0.01038  -0.00248 140 LYS A O   
1026 C CB  . LYS A 142 ? 0.32392 0.33305 0.40543 -0.02232 0.00657  -0.01619 140 LYS A CB  
1027 C CG  . LYS A 142 ? 0.31819 0.33591 0.39992 -0.01907 0.01068  -0.00946 140 LYS A CG  
1028 C CD  . LYS A 142 ? 0.36197 0.38232 0.43696 -0.01128 0.01149  -0.01017 140 LYS A CD  
1029 C CE  . LYS A 142 ? 0.33962 0.34682 0.40714 -0.00779 0.01171  -0.01157 140 LYS A CE  
1030 N NZ  . LYS A 142 ? 0.34486 0.35381 0.40664 -0.00140 0.01293  -0.01073 140 LYS A NZ  
1031 N N   . TYR A 143 ? 0.37371 0.35722 0.46386 -0.03267 0.00802  -0.00867 141 TYR A N   
1032 C CA  . TYR A 143 ? 0.36423 0.34095 0.45767 -0.03589 0.01032  -0.00018 141 TYR A CA  
1033 C C   . TYR A 143 ? 0.37496 0.35323 0.47932 -0.04619 0.00897  0.00260  141 TYR A C   
1034 O O   . TYR A 143 ? 0.36267 0.34755 0.47132 -0.05016 0.01189  0.01165  141 TYR A O   
1035 C CB  . TYR A 143 ? 0.39229 0.35066 0.48263 -0.03259 0.00969  -0.00036 141 TYR A CB  
1036 C CG  . TYR A 143 ? 0.37894 0.32978 0.47336 -0.03626 0.01129  0.00989  141 TYR A CG  
1037 C CD1 . TYR A 143 ? 0.39082 0.33185 0.49485 -0.04444 0.00922  0.01188  141 TYR A CD1 
1038 C CD2 . TYR A 143 ? 0.36894 0.32290 0.45764 -0.03212 0.01453  0.01793  141 TYR A CD2 
1039 C CE1 . TYR A 143 ? 0.42105 0.35563 0.52950 -0.04829 0.01054  0.02308  141 TYR A CE1 
1040 C CE2 . TYR A 143 ? 0.38421 0.33338 0.47609 -0.03574 0.01578  0.02865  141 TYR A CE2 
1041 C CZ  . TYR A 143 ? 0.39681 0.33633 0.49887 -0.04375 0.01387  0.03184  141 TYR A CZ  
1042 O OH  . TYR A 143 ? 0.44627 0.38068 0.55237 -0.04784 0.01485  0.04398  141 TYR A OH  
1043 N N   . GLU A 144 ? 0.39155 0.36496 0.50049 -0.05117 0.00455  -0.00518 142 GLU A N   
1044 C CA  . GLU A 144 ? 0.37328 0.34387 0.49349 -0.06223 0.00247  -0.00279 142 GLU A CA  
1045 C C   . GLU A 144 ? 0.38886 0.38142 0.51625 -0.06789 0.00329  0.00132  142 GLU A C   
1046 O O   . GLU A 144 ? 0.40629 0.40172 0.54303 -0.07636 0.00415  0.00898  142 GLU A O   
1047 C CB  . GLU A 144 ? 0.39074 0.34788 0.51323 -0.06605 -0.00293 -0.01410 142 GLU A CB  
1048 C CG  . GLU A 144 ? 0.44392 0.37798 0.56349 -0.06170 -0.00311 -0.01608 142 GLU A CG  
1049 C CD  . GLU A 144 ? 0.53910 0.46150 0.65605 -0.06025 -0.00716 -0.03055 142 GLU A CD  
1050 O OE1 . GLU A 144 ? 0.52577 0.46014 0.63933 -0.06057 -0.00959 -0.03925 142 GLU A OE1 
1051 O OE2 . GLU A 144 ? 0.57037 0.47261 0.68772 -0.05732 -0.00756 -0.03313 142 GLU A OE2 
1052 N N   . ILE A 145 ? 0.33546 0.34446 0.45964 -0.06325 0.00315  -0.00266 143 ILE A N   
1053 C CA  . ILE A 145 ? 0.34741 0.37889 0.47968 -0.06714 0.00414  0.00157  143 ILE A CA  
1054 C C   . ILE A 145 ? 0.38405 0.42492 0.51605 -0.06399 0.01071  0.01180  143 ILE A C   
1055 O O   . ILE A 145 ? 0.34585 0.40063 0.48717 -0.07015 0.01288  0.01872  143 ILE A O   
1056 C CB  . ILE A 145 ? 0.33856 0.38465 0.46831 -0.06226 0.00172  -0.00476 143 ILE A CB  
1057 C CG1 . ILE A 145 ? 0.34206 0.41201 0.48313 -0.06719 0.00150  -0.00093 143 ILE A CG1 
1058 C CG2 . ILE A 145 ? 0.33789 0.38496 0.45702 -0.05014 0.00506  -0.00462 143 ILE A CG2 
1059 C CD1 . ILE A 145 ? 0.35061 0.43670 0.49061 -0.06193 -0.00113 -0.00506 143 ILE A CD1 
1060 N N   . PHE A 146 ? 0.34785 0.38240 0.46914 -0.05472 0.01396  0.01260  144 PHE A N   
1061 C CA  . PHE A 146 ? 0.39737 0.43864 0.51597 -0.05166 0.01998  0.02091  144 PHE A CA  
1062 C C   . PHE A 146 ? 0.38588 0.42110 0.50963 -0.05973 0.02131  0.02975  144 PHE A C   
1063 O O   . PHE A 146 ? 0.40029 0.44994 0.52908 -0.06338 0.02543  0.03782  144 PHE A O   
1064 C CB  . PHE A 146 ? 0.34207 0.37466 0.44786 -0.04159 0.02170  0.01879  144 PHE A CB  
1065 C CG  . PHE A 146 ? 0.35955 0.40047 0.46043 -0.03753 0.02748  0.02486  144 PHE A CG  
1066 C CD1 . PHE A 146 ? 0.34626 0.40620 0.44989 -0.03501 0.03129  0.02589  144 PHE A CD1 
1067 C CD2 . PHE A 146 ? 0.38238 0.41300 0.47591 -0.03590 0.02901  0.02921  144 PHE A CD2 
1068 C CE1 . PHE A 146 ? 0.38466 0.45249 0.48272 -0.03090 0.03692  0.02976  144 PHE A CE1 
1069 C CE2 . PHE A 146 ? 0.38763 0.42726 0.47512 -0.03255 0.03407  0.03395  144 PHE A CE2 
1070 C CZ  . PHE A 146 ? 0.38965 0.44746 0.47888 -0.03008 0.03819  0.03353  144 PHE A CZ  
1071 N N   . ALA A 147 ? 0.37633 0.39071 0.49970 -0.06257 0.01792  0.02870  145 ALA A N   
1072 C CA  . ALA A 147 ? 0.42160 0.42732 0.55084 -0.07027 0.01849  0.03825  145 ALA A CA  
1073 C C   . ALA A 147 ? 0.44505 0.46036 0.58822 -0.08218 0.01741  0.04221  145 ALA A C   
1074 O O   . ALA A 147 ? 0.50446 0.52742 0.65311 -0.08818 0.02076  0.05356  145 ALA A O   
1075 C CB  . ALA A 147 ? 0.42641 0.40647 0.55428 -0.06990 0.01455  0.03518  145 ALA A CB  
1076 N N   . GLU A 148 ? 0.44980 0.46627 0.59888 -0.08633 0.01259  0.03337  146 GLU A N   
1077 C CA  . GLU A 148 ? 0.45040 0.47753 0.61372 -0.09862 0.01074  0.03651  146 GLU A CA  
1078 C C   . GLU A 148 ? 0.44412 0.49925 0.61202 -0.09908 0.01628  0.04473  146 GLU A C   
1079 O O   . GLU A 148 ? 0.46432 0.52988 0.64416 -0.10953 0.01718  0.05298  146 GLU A O   
1080 C CB  . GLU A 148 ? 0.47001 0.49738 0.63701 -0.10196 0.00425  0.02436  146 GLU A CB  
1081 C CG  . GLU A 148 ? 0.53780 0.57092 0.72043 -0.11692 0.00040  0.02618  146 GLU A CG  
1082 C CD  . GLU A 148 ? 0.63617 0.68352 0.82256 -0.11949 -0.00483 0.01632  146 GLU A CD  
1083 O OE1 . GLU A 148 ? 0.65092 0.69329 0.82739 -0.11164 -0.00749 0.00569  146 GLU A OE1 
1084 O OE2 . GLU A 148 ? 0.69825 0.76302 0.89779 -0.12978 -0.00652 0.01975  146 GLU A OE2 
1085 N N   . TYR A 149 ? 0.43854 0.50624 0.59783 -0.08793 0.02025  0.04270  147 TYR A N   
1086 C CA  . TYR A 149 ? 0.43332 0.52682 0.59659 -0.08680 0.02645  0.04985  147 TYR A CA  
1087 C C   . TYR A 149 ? 0.45569 0.54931 0.61534 -0.08750 0.03232  0.06107  147 TYR A C   
1088 O O   . TYR A 149 ? 0.45932 0.57072 0.62734 -0.09387 0.03640  0.07045  147 TYR A O   
1089 C CB  . TYR A 149 ? 0.41686 0.52231 0.57303 -0.07436 0.02876  0.04356  147 TYR A CB  
1090 C CG  . TYR A 149 ? 0.37304 0.49320 0.53770 -0.07515 0.02498  0.03780  147 TYR A CG  
1091 C CD1 . TYR A 149 ? 0.37604 0.52154 0.55414 -0.08018 0.02695  0.04287  147 TYR A CD1 
1092 C CD2 . TYR A 149 ? 0.35504 0.46593 0.51462 -0.07095 0.01942  0.02805  147 TYR A CD2 
1093 C CE1 . TYR A 149 ? 0.31859 0.47960 0.50532 -0.08085 0.02283  0.03842  147 TYR A CE1 
1094 C CE2 . TYR A 149 ? 0.34778 0.47369 0.51458 -0.07181 0.01540  0.02378  147 TYR A CE2 
1095 C CZ  . TYR A 149 ? 0.35759 0.50852 0.53816 -0.07661 0.01687  0.02906  147 TYR A CZ  
1096 O OH  . TYR A 149 ? 0.29505 0.46284 0.48348 -0.07724 0.01230  0.02557  147 TYR A OH  
1097 N N   . LEU A 150 ? 0.44587 0.52156 0.59342 -0.08148 0.03270  0.06097  148 LEU A N   
1098 C CA  . LEU A 150 ? 0.48127 0.56099 0.62203 -0.07952 0.03845  0.07073  148 LEU A CA  
1099 C C   . LEU A 150 ? 0.56830 0.62918 0.70985 -0.08599 0.03652  0.07956  148 LEU A C   
1100 O O   . LEU A 150 ? 0.57537 0.63642 0.70888 -0.08332 0.04008  0.08750  148 LEU A O   
1101 C CB  . LEU A 150 ? 0.44153 0.52007 0.56719 -0.06655 0.04091  0.06477  148 LEU A CB  
1102 C CG  . LEU A 150 ? 0.37778 0.47514 0.50264 -0.05902 0.04401  0.05808  148 LEU A CG  
1103 C CD1 . LEU A 150 ? 0.40441 0.49784 0.51460 -0.04791 0.04643  0.05353  148 LEU A CD1 
1104 C CD2 . LEU A 150 ? 0.43296 0.55672 0.56634 -0.06279 0.04990  0.06508  148 LEU A CD2 
1105 N N   . ALA A 151 ? 0.58021 0.62492 0.73143 -0.09438 0.03078  0.07849  149 ALA A N   
1106 C CA  . ALA A 151 ? 0.61019 0.63257 0.76235 -0.09844 0.02836  0.08580  149 ALA A CA  
1107 C C   . ALA A 151 ? 0.64287 0.67498 0.80130 -0.10728 0.03223  0.10275  149 ALA A C   
1108 O O   . ALA A 151 ? 0.67285 0.69524 0.82670 -0.10651 0.03312  0.11261  149 ALA A O   
1109 C CB  . ALA A 151 ? 0.59993 0.60045 0.76090 -0.10454 0.02121  0.07847  149 ALA A CB  
1110 N N   . GLU A 152 ? 0.63148 0.68460 0.80067 -0.11572 0.03461  0.10737  150 GLU A N   
1111 C CA  . GLU A 152 ? 0.63063 0.69586 0.80513 -0.12407 0.03908  0.12461  150 GLU A CA  
1112 C C   . GLU A 152 ? 0.58259 0.66705 0.74374 -0.11578 0.04659  0.13034  150 GLU A C   
1113 O O   . GLU A 152 ? 0.58871 0.68314 0.75074 -0.12128 0.05067  0.14550  150 GLU A O   
1114 C CB  . GLU A 152 ? 0.62858 0.71338 0.81966 -0.13624 0.03983  0.12892  150 GLU A CB  
1115 N N   . GLU A 153 ? 0.56781 0.65717 0.71643 -0.10314 0.04831  0.11878  151 GLU A N   
1116 C CA  . GLU A 153 ? 0.51454 0.62477 0.65108 -0.09532 0.05557  0.12082  151 GLU A CA  
1117 C C   . GLU A 153 ? 0.56364 0.66150 0.68332 -0.08557 0.05522  0.11862  151 GLU A C   
1118 O O   . GLU A 153 ? 0.55133 0.66317 0.66094 -0.08259 0.06047  0.12490  151 GLU A O   
1119 C CB  . GLU A 153 ? 0.50206 0.63151 0.63880 -0.08851 0.05861  0.10944  151 GLU A CB  
1120 N N   . ILE A 154 ? 0.53298 0.60701 0.64930 -0.08069 0.04923  0.10965  152 ILE A N   
1121 C CA  . ILE A 154 ? 0.50797 0.57142 0.60965 -0.07112 0.04823  0.10594  152 ILE A CA  
1122 C C   . ILE A 154 ? 0.51063 0.54670 0.61560 -0.07281 0.04182  0.10780  152 ILE A C   
1123 O O   . ILE A 154 ? 0.53132 0.55377 0.64620 -0.07657 0.03735  0.10219  152 ILE A O   
1124 C CB  . ILE A 154 ? 0.49409 0.55981 0.58849 -0.06099 0.04823  0.09041  152 ILE A CB  
1125 C CG1 . ILE A 154 ? 0.52550 0.61487 0.61196 -0.05590 0.05509  0.08914  152 ILE A CG1 
1126 C CG2 . ILE A 154 ? 0.44771 0.49502 0.53210 -0.05330 0.04427  0.08443  152 ILE A CG2 
1127 C CD1 . ILE A 154 ? 0.52276 0.61392 0.60442 -0.04648 0.05517  0.07494  152 ILE A CD1 
1128 N N   . ASN A 155 ? 0.50150 0.53011 0.59860 -0.06994 0.04122  0.11548  153 ASN A N   
1129 C CA  . ASN A 155 ? 0.51334 0.51672 0.61638 -0.07167 0.03561  0.11931  153 ASN A CA  
1130 C C   . ASN A 155 ? 0.44947 0.43609 0.54903 -0.06328 0.03126  0.10494  153 ASN A C   
1131 O O   . ASN A 155 ? 0.40793 0.40204 0.49915 -0.05617 0.03236  0.09396  153 ASN A O   
1132 C CB  . ASN A 155 ? 0.52005 0.52175 0.61832 -0.07188 0.03591  0.13493  153 ASN A CB  
1133 C CG  . ASN A 155 ? 0.50771 0.51724 0.58957 -0.06223 0.03712  0.13248  153 ASN A CG  
1134 O OD1 . ASN A 155 ? 0.49643 0.50195 0.57199 -0.05437 0.03566  0.11909  153 ASN A OD1 
1135 N ND2 . ASN A 155 ? 0.55416 0.57557 0.62907 -0.06350 0.03952  0.14600  153 ASN A ND2 
1136 N N   . ASN A 156 ? 0.47462 0.43814 0.58134 -0.06415 0.02640  0.10534  154 ASN A N   
1137 C CA  . ASN A 156 ? 0.47807 0.42650 0.58304 -0.05688 0.02261  0.09169  154 ASN A CA  
1138 C C   . ASN A 156 ? 0.43195 0.38499 0.52357 -0.04660 0.02330  0.08829  154 ASN A C   
1139 O O   . ASN A 156 ? 0.43688 0.39020 0.52368 -0.04061 0.02256  0.07580  154 ASN A O   
1140 C CB  . ASN A 156 ? 0.50603 0.42916 0.62073 -0.05851 0.01799  0.09348  154 ASN A CB  
1141 C CG  . ASN A 156 ? 0.51795 0.43247 0.64569 -0.06789 0.01572  0.08957  154 ASN A CG  
1142 O OD1 . ASN A 156 ? 0.52776 0.45644 0.65733 -0.07261 0.01714  0.08464  154 ASN A OD1 
1143 N ND2 . ASN A 156 ? 0.50859 0.39984 0.64600 -0.07043 0.01187  0.09131  154 ASN A ND2 
1144 N N   . ALA A 157 ? 0.44209 0.39983 0.52771 -0.04505 0.02446  0.09980  155 ALA A N   
1145 C CA  . ALA A 157 ? 0.44189 0.40482 0.51519 -0.03645 0.02444  0.09691  155 ALA A CA  
1146 C C   . ALA A 157 ? 0.40080 0.38079 0.46494 -0.03360 0.02782  0.08740  155 ALA A C   
1147 O O   . ALA A 157 ? 0.38432 0.36307 0.44233 -0.02696 0.02665  0.07752  155 ALA A O   
1148 C CB  . ALA A 157 ? 0.44563 0.41385 0.51388 -0.03662 0.02480  0.11197  155 ALA A CB  
1149 N N   . ARG A 158 ? 0.38217 0.37835 0.44612 -0.03837 0.03215  0.09049  156 ARG A N   
1150 C CA  . ARG A 158 ? 0.42248 0.43371 0.47911 -0.03466 0.03556  0.08112  156 ARG A CA  
1151 C C   . ARG A 158 ? 0.35712 0.36346 0.41953 -0.03324 0.03401  0.06874  156 ARG A C   
1152 O O   . ARG A 158 ? 0.39819 0.40860 0.45453 -0.02740 0.03452  0.05924  156 ARG A O   
1153 C CB  . ARG A 158 ? 0.41220 0.44391 0.46799 -0.03914 0.04126  0.08740  156 ARG A CB  
1154 C CG  . ARG A 158 ? 0.49917 0.54345 0.54225 -0.03708 0.04407  0.09378  156 ARG A CG  
1155 C CD  . ARG A 158 ? 0.48928 0.55650 0.53065 -0.04045 0.05072  0.09804  156 ARG A CD  
1156 N NE  . ARG A 158 ? 0.54927 0.62550 0.58596 -0.04467 0.05251  0.11289  156 ARG A NE  
1157 C CZ  . ARG A 158 ? 0.62992 0.70830 0.67619 -0.05312 0.05344  0.12633  156 ARG A CZ  
1158 N NH1 . ARG A 158 ? 0.60985 0.68215 0.67095 -0.05872 0.05262  0.12573  156 ARG A NH1 
1159 N NH2 . ARG A 158 ? 0.58385 0.67170 0.62477 -0.05665 0.05504  0.14107  156 ARG A NH2 
1160 N N   . LEU A 159 ? 0.36953 0.36707 0.44352 -0.03880 0.03175  0.06883  157 LEU A N   
1161 C CA  . LEU A 159 ? 0.40294 0.39658 0.48164 -0.03778 0.02948  0.05725  157 LEU A CA  
1162 C C   . LEU A 159 ? 0.33959 0.32176 0.41247 -0.03019 0.02632  0.04866  157 LEU A C   
1163 O O   . LEU A 159 ? 0.32467 0.31207 0.39321 -0.02538 0.02656  0.04012  157 LEU A O   
1164 C CB  . LEU A 159 ? 0.41556 0.40022 0.50704 -0.04591 0.02673  0.05850  157 LEU A CB  
1165 C CG  . LEU A 159 ? 0.45979 0.45924 0.55946 -0.05431 0.02960  0.06479  157 LEU A CG  
1166 C CD1 . LEU A 159 ? 0.50853 0.49648 0.62140 -0.06367 0.02591  0.06634  157 LEU A CD1 
1167 C CD2 . LEU A 159 ? 0.44735 0.46432 0.54622 -0.05159 0.03192  0.05730  157 LEU A CD2 
1168 N N   . ARG A 160 ? 0.34686 0.31417 0.42023 -0.02878 0.02350  0.05168  158 ARG A N   
1169 C CA  . ARG A 160 ? 0.37088 0.32926 0.43993 -0.02161 0.02088  0.04412  158 ARG A CA  
1170 C C   . ARG A 160 ? 0.32408 0.29228 0.38221 -0.01566 0.02248  0.04199  158 ARG A C   
1171 O O   . ARG A 160 ? 0.31608 0.28362 0.37093 -0.01094 0.02137  0.03359  158 ARG A O   
1172 C CB  . ARG A 160 ? 0.35921 0.30199 0.43175 -0.02027 0.01816  0.04908  158 ARG A CB  
1173 C CG  . ARG A 160 ? 0.40257 0.33031 0.48606 -0.02449 0.01554  0.04654  158 ARG A CG  
1174 C CD  . ARG A 160 ? 0.45701 0.36744 0.54467 -0.02094 0.01293  0.05026  158 ARG A CD  
1175 N NE  . ARG A 160 ? 0.47431 0.38485 0.56240 -0.02239 0.01348  0.06504  158 ARG A NE  
1176 C CZ  . ARG A 160 ? 0.46732 0.36948 0.56418 -0.02886 0.01288  0.07486  158 ARG A CZ  
1177 N NH1 . ARG A 160 ? 0.47349 0.36565 0.58009 -0.03532 0.01154  0.07088  158 ARG A NH1 
1178 N NH2 . ARG A 160 ? 0.50381 0.40817 0.59971 -0.02943 0.01330  0.08949  158 ARG A NH2 
1179 N N   . ILE A 161 ? 0.31543 0.29310 0.36769 -0.01626 0.02497  0.04941  159 ILE A N   
1180 C CA  . ILE A 161 ? 0.30623 0.29228 0.34781 -0.01137 0.02609  0.04641  159 ILE A CA  
1181 C C   . ILE A 161 ? 0.28068 0.27571 0.32055 -0.00990 0.02839  0.03797  159 ILE A C   
1182 O O   . ILE A 161 ? 0.25976 0.25435 0.29493 -0.00525 0.02750  0.03095  159 ILE A O   
1183 C CB  . ILE A 161 ? 0.34856 0.34378 0.38329 -0.01280 0.02808  0.05581  159 ILE A CB  
1184 C CG1 . ILE A 161 ? 0.34107 0.32794 0.37564 -0.01157 0.02472  0.06364  159 ILE A CG1 
1185 C CG2 . ILE A 161 ? 0.30830 0.31527 0.33201 -0.00944 0.03032  0.05055  159 ILE A CG2 
1186 C CD1 . ILE A 161 ? 0.42743 0.42318 0.45745 -0.01460 0.02614  0.07594  159 ILE A CD1 
1187 N N   . ILE A 162 ? 0.28100 0.28467 0.32578 -0.01382 0.03130  0.03925  160 ILE A N   
1188 C CA  . ILE A 162 ? 0.27403 0.28732 0.31882 -0.01152 0.03359  0.03220  160 ILE A CA  
1189 C C   . ILE A 162 ? 0.26036 0.26666 0.30896 -0.00915 0.03036  0.02425  160 ILE A C   
1190 O O   . ILE A 162 ? 0.28364 0.29192 0.32860 -0.00438 0.03038  0.01810  160 ILE A O   
1191 C CB  . ILE A 162 ? 0.27611 0.30212 0.32757 -0.01632 0.03728  0.03618  160 ILE A CB  
1192 C CG1 . ILE A 162 ? 0.29584 0.33308 0.34119 -0.01744 0.04157  0.04304  160 ILE A CG1 
1193 C CG2 . ILE A 162 ? 0.27030 0.30581 0.32463 -0.01311 0.03902  0.02907  160 ILE A CG2 
1194 C CD1 . ILE A 162 ? 0.29436 0.34538 0.34760 -0.02358 0.04550  0.04976  160 ILE A CD1 
1195 N N   . VAL A 163 ? 0.26792 0.26574 0.32363 -0.01254 0.02742  0.02422  161 VAL A N   
1196 C CA  . VAL A 163 ? 0.28936 0.28282 0.34753 -0.01060 0.02443  0.01650  161 VAL A CA  
1197 C C   . VAL A 163 ? 0.28304 0.26959 0.33443 -0.00490 0.02261  0.01288  161 VAL A C   
1198 O O   . VAL A 163 ? 0.27906 0.26779 0.32855 -0.00141 0.02182  0.00744  161 VAL A O   
1199 C CB  . VAL A 163 ? 0.32446 0.31032 0.39096 -0.01588 0.02162  0.01584  161 VAL A CB  
1200 C CG1 . VAL A 163 ? 0.29129 0.27375 0.35834 -0.01374 0.01844  0.00729  161 VAL A CG1 
1201 C CG2 . VAL A 163 ? 0.26789 0.26358 0.34233 -0.02230 0.02309  0.01892  161 VAL A CG2 
1202 N N   . SER A 164 ? 0.25790 0.23771 0.30595 -0.00392 0.02196  0.01695  162 SER A N   
1203 C CA  . SER A 164 ? 0.28021 0.25618 0.32284 0.00105  0.02032  0.01425  162 SER A CA  
1204 C C   . SER A 164 ? 0.29040 0.27379 0.32622 0.00388  0.02182  0.01219  162 SER A C   
1205 O O   . SER A 164 ? 0.27199 0.25455 0.30556 0.00707  0.02052  0.00773  162 SER A O   
1206 C CB  . SER A 164 ? 0.30072 0.27005 0.34243 0.00173  0.01905  0.02001  162 SER A CB  
1207 O OG  . SER A 164 ? 0.33277 0.29848 0.37244 0.00623  0.01696  0.01685  162 SER A OG  
1208 N N   . ALA A 165 ? 0.28281 0.27353 0.31543 0.00263  0.02469  0.01525  163 ALA A N   
1209 C CA  . ALA A 165 ? 0.29142 0.28807 0.31793 0.00548  0.02641  0.01160  163 ALA A CA  
1210 C C   . ALA A 165 ? 0.28329 0.28207 0.31351 0.00762  0.02668  0.00594  163 ALA A C   
1211 O O   . ALA A 165 ? 0.26951 0.26737 0.29642 0.01090  0.02619  0.00190  163 ALA A O   
1212 C CB  . ALA A 165 ? 0.28669 0.29254 0.30931 0.00397  0.03019  0.01494  163 ALA A CB  
1213 N N   . MET A 166 ? 0.28230 0.28411 0.32000 0.00551  0.02700  0.00607  164 MET A N   
1214 C CA  . MET A 166 ? 0.27330 0.27921 0.31480 0.00790  0.02682  0.00193  164 MET A CA  
1215 C C   . MET A 166 ? 0.28924 0.28903 0.33067 0.00960  0.02324  -0.00104 164 MET A C   
1216 O O   . MET A 166 ? 0.29463 0.29567 0.33582 0.01284  0.02266  -0.00350 164 MET A O   
1217 C CB  . MET A 166 ? 0.29879 0.31272 0.34870 0.00481  0.02771  0.00307  164 MET A CB  
1218 C CG  . MET A 166 ? 0.30321 0.32567 0.35422 0.00252  0.03177  0.00704  164 MET A CG  
1219 S SD  . MET A 166 ? 0.32263 0.35460 0.37052 0.00825  0.03631  0.00424  164 MET A SD  
1220 C CE  . MET A 166 ? 0.30787 0.33312 0.34338 0.00968  0.03683  0.00397  164 MET A CE  
1221 N N   . ASN A 167 ? 0.28143 0.27486 0.32340 0.00771  0.02102  -0.00054 165 ASN A N   
1222 C CA  . ASN A 167 ? 0.31164 0.30093 0.35234 0.00975  0.01837  -0.00335 165 ASN A CA  
1223 C C   . ASN A 167 ? 0.31177 0.29892 0.34685 0.01275  0.01814  -0.00332 165 ASN A C   
1224 O O   . ASN A 167 ? 0.31591 0.30312 0.35037 0.01464  0.01666  -0.00503 165 ASN A O   
1225 C CB  . ASN A 167 ? 0.33999 0.32264 0.38257 0.00810  0.01675  -0.00358 165 ASN A CB  
1226 C CG  . ASN A 167 ? 0.36920 0.35282 0.41770 0.00452  0.01574  -0.00578 165 ASN A CG  
1227 O OD1 . ASN A 167 ? 0.37582 0.36645 0.42642 0.00417  0.01508  -0.00813 165 ASN A OD1 
1228 N ND2 . ASN A 167 ? 0.38010 0.35663 0.43188 0.00159  0.01521  -0.00473 165 ASN A ND2 
1229 N N   . GLY A 168 ? 0.30424 0.29057 0.33513 0.01263  0.01939  -0.00115 166 GLY A N   
1230 C CA  . GLY A 168 ? 0.29134 0.27621 0.31714 0.01441  0.01861  -0.00192 166 GLY A CA  
1231 C C   . GLY A 168 ? 0.28797 0.27438 0.31329 0.01635  0.01938  -0.00478 166 GLY A C   
1232 O O   . GLY A 168 ? 0.28461 0.26832 0.30818 0.01737  0.01781  -0.00594 166 GLY A O   
1233 N N   . ILE A 169 ? 0.25393 0.24477 0.28199 0.01695  0.02176  -0.00556 167 ILE A N   
1234 C CA  . ILE A 169 ? 0.24850 0.24036 0.27845 0.02007  0.02248  -0.00803 167 ILE A CA  
1235 C C   . ILE A 169 ? 0.27151 0.26253 0.30528 0.02105  0.01979  -0.00752 167 ILE A C   
1236 O O   . ILE A 169 ? 0.28724 0.27598 0.32200 0.02347  0.01909  -0.00811 167 ILE A O   
1237 C CB  . ILE A 169 ? 0.28690 0.28644 0.32093 0.02104  0.02579  -0.00826 167 ILE A CB  
1238 C CG1 . ILE A 169 ? 0.26463 0.26675 0.29336 0.02060  0.02907  -0.00885 167 ILE A CG1 
1239 C CG2 . ILE A 169 ? 0.29375 0.29528 0.33275 0.02538  0.02624  -0.00996 167 ILE A CG2 
1240 C CD1 . ILE A 169 ? 0.33379 0.34639 0.36695 0.02137  0.03321  -0.00847 167 ILE A CD1 
1241 N N   . LEU A 170 ? 0.22665 0.21940 0.26246 0.01916  0.01823  -0.00640 168 LEU A N   
1242 C CA  . LEU A 170 ? 0.26756 0.26235 0.30566 0.01977  0.01586  -0.00598 168 LEU A CA  
1243 C C   . LEU A 170 ? 0.30688 0.29809 0.34169 0.01970  0.01411  -0.00529 168 LEU A C   
1244 O O   . LEU A 170 ? 0.30921 0.30314 0.34505 0.02039  0.01254  -0.00405 168 LEU A O   
1245 C CB  . LEU A 170 ? 0.25784 0.25689 0.29883 0.01756  0.01497  -0.00677 168 LEU A CB  
1246 C CG  . LEU A 170 ? 0.27201 0.27701 0.31804 0.01620  0.01617  -0.00681 168 LEU A CG  
1247 C CD1 . LEU A 170 ? 0.24976 0.25761 0.29846 0.01296  0.01422  -0.00850 168 LEU A CD1 
1248 C CD2 . LEU A 170 ? 0.22796 0.23898 0.27788 0.01930  0.01656  -0.00579 168 LEU A CD2 
1249 N N   . LEU A 171 ? 0.31656 0.30371 0.34790 0.01877  0.01428  -0.00527 169 LEU A N   
1250 C CA  . LEU A 171 ? 0.31835 0.30429 0.34789 0.01857  0.01269  -0.00414 169 LEU A CA  
1251 C C   . LEU A 171 ? 0.35837 0.34211 0.38796 0.01893  0.01186  -0.00318 169 LEU A C   
1252 O O   . LEU A 171 ? 0.35236 0.33214 0.38067 0.01925  0.01262  -0.00467 169 LEU A O   
1253 C CB  . LEU A 171 ? 0.36308 0.34664 0.38980 0.01761  0.01263  -0.00369 169 LEU A CB  
1254 C CG  . LEU A 171 ? 0.37239 0.35763 0.39915 0.01762  0.01111  -0.00223 169 LEU A CG  
1255 C CD1 . LEU A 171 ? 0.39022 0.37740 0.41924 0.01899  0.01141  -0.00301 169 LEU A CD1 
1256 C CD2 . LEU A 171 ? 0.39697 0.38092 0.42095 0.01651  0.01024  -0.00101 169 LEU A CD2 
1257 N N   . PRO A 172 ? 0.36521 0.35131 0.39640 0.01885  0.01041  -0.00074 170 PRO A N   
1258 C CA  . PRO A 172 ? 0.39337 0.37548 0.42595 0.01865  0.00931  0.00120  170 PRO A CA  
1259 C C   . PRO A 172 ? 0.37062 0.34765 0.40071 0.01625  0.00835  0.00031  170 PRO A C   
1260 O O   . PRO A 172 ? 0.40343 0.38284 0.43131 0.01493  0.00809  0.00000  170 PRO A O   
1261 C CB  . PRO A 172 ? 0.40368 0.39185 0.43839 0.01831  0.00802  0.00561  170 PRO A CB  
1262 C CG  . PRO A 172 ? 0.35730 0.35190 0.39018 0.01801  0.00852  0.00450  170 PRO A CG  
1263 C CD  . PRO A 172 ? 0.37356 0.36631 0.40536 0.01890  0.00987  0.00039  170 PRO A CD  
1264 N N   . ALA A 173 ? 0.38236 0.35217 0.41324 0.01586  0.00759  -0.00042 171 ALA A N   
1265 C CA  . ALA A 173 ? 0.45125 0.41542 0.47962 0.01277  0.00600  -0.00255 171 ALA A CA  
1266 C C   . ALA A 173 ? 0.45130 0.41578 0.47402 0.01270  0.00709  -0.00697 171 ALA A C   
1267 O O   . ALA A 173 ? 0.47213 0.43565 0.49150 0.00964  0.00529  -0.00850 171 ALA A O   
1268 C CB  . ALA A 173 ? 0.45084 0.41908 0.48060 0.00890  0.00363  0.00147  171 ALA A CB  
1269 N N   . SER A 174 ? 0.46073 0.42782 0.48249 0.01552  0.00977  -0.00840 172 SER A N   
1270 C CA  . SER A 174 ? 0.44402 0.41275 0.46044 0.01527  0.01116  -0.01104 172 SER A CA  
1271 C C   . SER A 174 ? 0.45961 0.42340 0.47262 0.01617  0.01235  -0.01661 172 SER A C   
1272 O O   . SER A 174 ? 0.44580 0.40439 0.46225 0.01854  0.01299  -0.01856 172 SER A O   
1273 C CB  . SER A 174 ? 0.45436 0.42831 0.47206 0.01692  0.01356  -0.00951 172 SER A CB  
1274 O OG  . SER A 174 ? 0.51625 0.49056 0.53487 0.01935  0.01634  -0.01196 172 SER A OG  
1275 N N   . THR A 175 ? 0.43925 0.40493 0.44536 0.01450  0.01245  -0.01922 173 THR A N   
1276 C CA  . THR A 175 ? 0.47672 0.43864 0.47728 0.01471  0.01323  -0.02616 173 THR A CA  
1277 C C   . THR A 175 ? 0.39271 0.36235 0.38645 0.01519  0.01614  -0.02731 173 THR A C   
1278 O O   . THR A 175 ? 0.41926 0.39544 0.41308 0.01440  0.01662  -0.02180 173 THR A O   
1279 C CB  . THR A 175 ? 0.49411 0.45166 0.49139 0.01024  0.00895  -0.02861 173 THR A CB  
1280 O OG1 . THR A 175 ? 0.48665 0.45209 0.47848 0.00716  0.00718  -0.02613 173 THR A OG1 
1281 C CG2 . THR A 175 ? 0.49620 0.44948 0.50071 0.00827  0.00590  -0.02445 173 THR A CG2 
1282 N N   . TYR A 176 ? 0.44368 0.41254 0.43150 0.01644  0.01817  -0.03448 174 TYR A N   
1283 C CA  . TYR A 176 ? 0.43085 0.40921 0.41081 0.01662  0.02136  -0.03558 174 TYR A CA  
1284 C C   . TYR A 176 ? 0.40677 0.39269 0.39145 0.01848  0.02511  -0.02960 174 TYR A C   
1285 O O   . TYR A 176 ? 0.36963 0.36335 0.35102 0.01638  0.02577  -0.02437 174 TYR A O   
1286 C CB  . TYR A 176 ? 0.40700 0.39070 0.37916 0.01197  0.01795  -0.03299 174 TYR A CB  
1287 C CG  . TYR A 176 ? 0.45501 0.43562 0.41941 0.00914  0.01475  -0.04053 174 TYR A CG  
1288 C CD1 . TYR A 176 ? 0.44270 0.42568 0.39796 0.01023  0.01732  -0.04927 174 TYR A CD1 
1289 C CD2 . TYR A 176 ? 0.42570 0.40227 0.39187 0.00498  0.00912  -0.03930 174 TYR A CD2 
1290 C CE1 . TYR A 176 ? 0.45958 0.43943 0.40702 0.00705  0.01397  -0.05765 174 TYR A CE1 
1291 C CE2 . TYR A 176 ? 0.43864 0.41281 0.39804 0.00111  0.00548  -0.04657 174 TYR A CE2 
1292 C CZ  . TYR A 176 ? 0.47224 0.44732 0.42191 0.00204  0.00772  -0.05625 174 TYR A CZ  
1293 O OH  . TYR A 176 ? 0.45856 0.43064 0.40077 -0.00220 0.00384  -0.06525 174 TYR A OH  
1294 N N   . LEU A 177 ? 0.38127 0.36494 0.37452 0.02199  0.02706  -0.02960 175 LEU A N   
1295 C CA  . LEU A 177 ? 0.35609 0.34674 0.35548 0.02262  0.02956  -0.02400 175 LEU A CA  
1296 C C   . LEU A 177 ? 0.35335 0.35475 0.34905 0.02333  0.03457  -0.02445 175 LEU A C   
1297 O O   . LEU A 177 ? 0.35621 0.35959 0.34747 0.02621  0.03757  -0.03111 175 LEU A O   
1298 C CB  . LEU A 177 ? 0.37674 0.36477 0.38587 0.02613  0.02997  -0.02413 175 LEU A CB  
1299 C CG  . LEU A 177 ? 0.42710 0.40798 0.44102 0.02521  0.02566  -0.02141 175 LEU A CG  
1300 C CD1 . LEU A 177 ? 0.42061 0.40216 0.44362 0.02884  0.02623  -0.02040 175 LEU A CD1 
1301 C CD2 . LEU A 177 ? 0.42231 0.40535 0.43601 0.02138  0.02346  -0.01582 175 LEU A CD2 
1302 N N   . PRO A 178 ? 0.33639 0.34498 0.33415 0.02069  0.03572  -0.01754 176 PRO A N   
1303 C CA  . PRO A 178 ? 0.37493 0.39577 0.37087 0.02073  0.04091  -0.01623 176 PRO A CA  
1304 C C   . PRO A 178 ? 0.36363 0.38951 0.36653 0.02552  0.04513  -0.02023 176 PRO A C   
1305 O O   . PRO A 178 ? 0.34737 0.36961 0.35955 0.02732  0.04371  -0.01976 176 PRO A O   
1306 C CB  . PRO A 178 ? 0.36066 0.38476 0.36094 0.01616  0.04013  -0.00680 176 PRO A CB  
1307 C CG  . PRO A 178 ? 0.36547 0.37915 0.37203 0.01549  0.03534  -0.00532 176 PRO A CG  
1308 C CD  . PRO A 178 ? 0.33755 0.34295 0.33993 0.01748  0.03238  -0.01076 176 PRO A CD  
1309 N N   . THR A 179 ? 0.35992 0.39556 0.35810 0.02803  0.05034  -0.02422 177 THR A N   
1310 C CA  . THR A 179 ? 0.35057 0.39366 0.35539 0.03379  0.05532  -0.02843 177 THR A CA  
1311 C C   . THR A 179 ? 0.34843 0.40735 0.35970 0.03144  0.05934  -0.02125 177 THR A C   
1312 O O   . THR A 179 ? 0.32007 0.38336 0.32891 0.02533  0.05881  -0.01368 177 THR A O   
1313 C CB  . THR A 179 ? 0.42333 0.46857 0.41940 0.03872  0.05934  -0.03858 177 THR A CB  
1314 O OG1 . THR A 179 ? 0.33953 0.39920 0.32648 0.03627  0.06362  -0.03700 177 THR A OG1 
1315 C CG2 . THR A 179 ? 0.40477 0.43449 0.39285 0.03836  0.05456  -0.04511 177 THR A CG2 
1316 N N   . TRP A 180 ? 0.35733 0.42506 0.37827 0.03622  0.06315  -0.02297 178 TRP A N   
1317 C CA  . TRP A 180 ? 0.33292 0.41808 0.36113 0.03353  0.06726  -0.01633 178 TRP A CA  
1318 C C   . TRP A 180 ? 0.34776 0.44568 0.36621 0.03082  0.07222  -0.01434 178 TRP A C   
1319 O O   . TRP A 180 ? 0.35791 0.46350 0.37771 0.02393  0.07260  -0.00502 178 TRP A O   
1320 C CB  . TRP A 180 ? 0.33903 0.43486 0.37916 0.04023  0.07114  -0.01914 178 TRP A CB  
1321 C CG  . TRP A 180 ? 0.35492 0.47303 0.40061 0.03800  0.07718  -0.01375 178 TRP A CG  
1322 C CD1 . TRP A 180 ? 0.39477 0.52983 0.44087 0.04349  0.08486  -0.01750 178 TRP A CD1 
1323 C CD2 . TRP A 180 ? 0.36976 0.49559 0.42177 0.02917  0.07602  -0.00348 178 TRP A CD2 
1324 N NE1 . TRP A 180 ? 0.36506 0.52006 0.41763 0.03820  0.08881  -0.00909 178 TRP A NE1 
1325 C CE2 . TRP A 180 ? 0.34012 0.48865 0.39676 0.02892  0.08310  -0.00026 178 TRP A CE2 
1326 C CE3 . TRP A 180 ? 0.33181 0.44722 0.38662 0.02147  0.06971  0.00288  178 TRP A CE3 
1327 C CZ2 . TRP A 180 ? 0.33753 0.49801 0.40179 0.02013  0.08366  0.01009  178 TRP A CZ2 
1328 C CZ3 . TRP A 180 ? 0.33280 0.45810 0.39480 0.01343  0.07015  0.01178  178 TRP A CZ3 
1329 C CH2 . TRP A 180 ? 0.35248 0.49982 0.41941 0.01223  0.07686  0.01585  178 TRP A CH2 
1330 N N   . GLU A 181 ? 0.34702 0.44683 0.35513 0.03573  0.07572  -0.02287 179 GLU A N   
1331 C CA  . GLU A 181 ? 0.39091 0.50536 0.38799 0.03326  0.08058  -0.02111 179 GLU A CA  
1332 C C   . GLU A 181 ? 0.41544 0.52438 0.40379 0.02529  0.07589  -0.01311 179 GLU A C   
1333 O O   . GLU A 181 ? 0.43909 0.56155 0.42369 0.02040  0.07874  -0.00485 179 GLU A O   
1334 C CB  . GLU A 181 ? 0.42277 0.53939 0.40912 0.04031  0.08474  -0.03398 179 GLU A CB  
1335 N N   . ASP A 182 ? 0.38180 0.47220 0.36775 0.02400  0.06883  -0.01438 180 ASP A N   
1336 C CA  . ASP A 182 ? 0.39455 0.47983 0.37576 0.01726  0.06403  -0.00555 180 ASP A CA  
1337 C C   . ASP A 182 ? 0.43024 0.51944 0.42201 0.01163  0.06383  0.00631  180 ASP A C   
1338 O O   . ASP A 182 ? 0.40670 0.50315 0.39518 0.00635  0.06454  0.01580  180 ASP A O   
1339 C CB  . ASP A 182 ? 0.38678 0.45298 0.36754 0.01729  0.05678  -0.00838 180 ASP A CB  
1340 C CG  . ASP A 182 ? 0.39699 0.45689 0.36785 0.02094  0.05557  -0.01939 180 ASP A CG  
1341 O OD1 . ASP A 182 ? 0.42542 0.49483 0.38608 0.02264  0.05943  -0.02495 180 ASP A OD1 
1342 O OD2 . ASP A 182 ? 0.40787 0.45331 0.38148 0.02188  0.05070  -0.02288 180 ASP A OD2 
1343 N N   . ILE A 183 ? 0.35596 0.43959 0.36057 0.01226  0.06222  0.00614  181 ILE A N   
1344 C CA  . ILE A 183 ? 0.41772 0.50301 0.43318 0.00630  0.06113  0.01560  181 ILE A CA  
1345 C C   . ILE A 183 ? 0.42474 0.52980 0.44332 0.00332  0.06742  0.02188  181 ILE A C   
1346 O O   . ILE A 183 ? 0.45793 0.56609 0.47991 -0.00372 0.06709  0.03241  181 ILE A O   
1347 C CB  . ILE A 183 ? 0.37440 0.45268 0.40190 0.00782  0.05818  0.01251  181 ILE A CB  
1348 C CG1 . ILE A 183 ? 0.36582 0.42658 0.39018 0.01051  0.05247  0.00723  181 ILE A CG1 
1349 C CG2 . ILE A 183 ? 0.38970 0.46898 0.42781 0.00088  0.05646  0.02066  181 ILE A CG2 
1350 C CD1 . ILE A 183 ? 0.41455 0.46430 0.43474 0.00615  0.04782  0.01243  181 ILE A CD1 
1351 N N   . GLU A 184 ? 0.41694 0.53579 0.43555 0.00871  0.07338  0.01583  182 GLU A N   
1352 C CA  . GLU A 184 ? 0.43227 0.57337 0.45423 0.00638  0.08030  0.02163  182 GLU A CA  
1353 C C   . GLU A 184 ? 0.48507 0.63468 0.49462 0.00221  0.08267  0.02848  182 GLU A C   
1354 O O   . GLU A 184 ? 0.46422 0.62798 0.47770 -0.00401 0.08595  0.03931  182 GLU A O   
1355 C CB  . GLU A 184 ? 0.41555 0.56993 0.43992 0.01487  0.08659  0.01233  182 GLU A CB  
1356 C CG  . GLU A 184 ? 0.48951 0.67054 0.51480 0.01411  0.09525  0.01663  182 GLU A CG  
1357 C CD  . GLU A 184 ? 0.53097 0.72634 0.56453 0.02284  0.10138  0.00869  182 GLU A CD  
1358 O OE1 . GLU A 184 ? 0.56076 0.75238 0.58679 0.03190  0.10350  -0.00340 182 GLU A OE1 
1359 O OE2 . GLU A 184 ? 0.49607 0.70681 0.54435 0.02066  0.10400  0.01454  182 GLU A OE2 
1360 N N   . SER A 185 ? 0.49811 0.63994 0.49302 0.00486  0.08059  0.02322  183 SER A N   
1361 C CA  . SER A 185 ? 0.50182 0.65224 0.48379 0.00088  0.08169  0.03029  183 SER A CA  
1362 C C   . SER A 185 ? 0.52458 0.66655 0.51071 -0.00714 0.07657  0.04435  183 SER A C   
1363 O O   . SER A 185 ? 0.54672 0.70005 0.52843 -0.01238 0.07849  0.05572  183 SER A O   
1364 C CB  . SER A 185 ? 0.52815 0.67189 0.49427 0.00518  0.07938  0.02049  183 SER A CB  
1365 O OG  . SER A 185 ? 0.57254 0.72458 0.53361 0.01246  0.08483  0.00733  183 SER A OG  
1366 N N   . LEU A 186 ? 0.52392 0.64625 0.51867 -0.00790 0.07020  0.04391  184 LEU A N   
1367 C CA  . LEU A 186 ? 0.54461 0.65624 0.54450 -0.01431 0.06525  0.05556  184 LEU A CA  
1368 C C   . LEU A 186 ? 0.54452 0.66275 0.55789 -0.02118 0.06735  0.06577  184 LEU A C   
1369 O O   . LEU A 186 ? 0.54438 0.65883 0.56061 -0.02751 0.06520  0.07807  184 LEU A O   
1370 C CB  . LEU A 186 ? 0.53445 0.62408 0.53815 -0.01205 0.05830  0.04998  184 LEU A CB  
1371 C CG  . LEU A 186 ? 0.51532 0.59054 0.52680 -0.01690 0.05301  0.05884  184 LEU A CG  
1372 C CD1 . LEU A 186 ? 0.57747 0.64769 0.57952 -0.01672 0.04948  0.06408  184 LEU A CD1 
1373 C CD2 . LEU A 186 ? 0.46496 0.52479 0.48414 -0.01445 0.04877  0.05094  184 LEU A CD2 
1374 N N   . TYR A 187 ? 0.55168 0.68017 0.57408 -0.02028 0.07133  0.06157  185 TYR A N   
1375 C CA  . TYR A 187 ? 0.58245 0.71997 0.61861 -0.02779 0.07332  0.07107  185 TYR A CA  
1376 C C   . TYR A 187 ? 0.54229 0.70402 0.57556 -0.03168 0.08052  0.08072  185 TYR A C   
1377 O O   . TYR A 187 ? 0.51451 0.69079 0.53586 -0.02673 0.08574  0.07657  185 TYR A O   
1378 C CB  . TYR A 187 ? 0.59871 0.73911 0.64739 -0.02554 0.07381  0.06328  185 TYR A CB  
1379 C CG  . TYR A 187 ? 0.62565 0.78057 0.68911 -0.03327 0.07650  0.07173  185 TYR A CG  
1380 C CD1 . TYR A 187 ? 0.64692 0.79495 0.71825 -0.04343 0.07331  0.08340  185 TYR A CD1 
1381 C CD2 . TYR A 187 ? 0.63334 0.80850 0.70433 -0.03045 0.08190  0.06802  185 TYR A CD2 
1382 C CE1 . TYR A 187 ? 0.65192 0.81313 0.73777 -0.05189 0.07530  0.09133  185 TYR A CE1 
1383 C CE2 . TYR A 187 ? 0.60646 0.79708 0.69230 -0.03823 0.08408  0.07612  185 TYR A CE2 
1384 C CZ  . TYR A 187 ? 0.65289 0.83645 0.74601 -0.04958 0.08062  0.08775  185 TYR A CZ  
1385 O OH  . TYR A 187 ? 0.63100 0.82995 0.73975 -0.05863 0.08239  0.09602  185 TYR A OH  
1386 N N   . THR B 14  ? 0.54935 1.05023 0.81783 -0.13371 -0.00093 0.21247  12  THR B N   
1387 C CA  . THR B 14  ? 0.58788 1.05849 0.84737 -0.13146 -0.00358 0.20308  12  THR B CA  
1388 C C   . THR B 14  ? 0.52249 0.99672 0.77713 -0.11460 0.00064  0.19165  12  THR B C   
1389 O O   . THR B 14  ? 0.57142 1.07019 0.82968 -0.10381 0.00566  0.19036  12  THR B O   
1390 C CB  . THR B 14  ? 0.58514 1.03207 0.84865 -0.14563 -0.01458 0.20048  12  THR B CB  
1391 O OG1 . THR B 14  ? 0.49938 0.91585 0.75352 -0.14440 -0.01667 0.19257  12  THR B OG1 
1392 C CG2 . THR B 14  ? 0.63304 1.09305 0.90426 -0.14472 -0.01919 0.19567  12  THR B CG2 
1393 N N   . LEU B 15  ? 0.53527 0.98389 0.78243 -0.11260 -0.00180 0.18344  13  LEU B N   
1394 C CA  . LEU B 15  ? 0.45305 0.89992 0.69377 -0.09665 0.00272  0.17303  13  LEU B CA  
1395 C C   . LEU B 15  ? 0.38590 0.82916 0.63097 -0.09498 -0.00362 0.16578  13  LEU B C   
1396 O O   . LEU B 15  ? 0.40195 0.82611 0.64755 -0.10610 -0.01219 0.16402  13  LEU B O   
1397 C CB  . LEU B 15  ? 0.42715 0.84906 0.65691 -0.09547 0.00405  0.16922  13  LEU B CB  
1398 C CG  . LEU B 15  ? 0.35731 0.78067 0.57889 -0.07826 0.01146  0.16031  13  LEU B CG  
1399 C CD1 . LEU B 15  ? 0.40422 0.85455 0.62513 -0.06793 0.02051  0.16247  13  LEU B CD1 
1400 C CD2 . LEU B 15  ? 0.35664 0.75651 0.56827 -0.07910 0.01218  0.15804  13  LEU B CD2 
1401 N N   . SER B 16  ? 0.30925 0.76922 0.55659 -0.08056 0.00040  0.16102  14  SER B N   
1402 C CA  . SER B 16  ? 0.31739 0.77345 0.56781 -0.07760 -0.00578 0.15479  14  SER B CA  
1403 C C   . SER B 16  ? 0.29781 0.72738 0.53938 -0.07558 -0.00831 0.14670  14  SER B C   
1404 O O   . SER B 16  ? 0.27901 0.69758 0.51250 -0.07081 -0.00295 0.14427  14  SER B O   
1405 C CB  . SER B 16  ? 0.30532 0.78175 0.56003 -0.06083 -0.00076 0.15155  14  SER B CB  
1406 O OG  . SER B 16  ? 0.26896 0.74359 0.51630 -0.04584 0.00823  0.14578  14  SER B OG  
1407 N N   . ASP B 17  ? 0.29655 0.71710 0.53929 -0.07897 -0.01666 0.14244  15  ASP B N   
1408 C CA  . ASP B 17  ? 0.28519 0.68329 0.51983 -0.07561 -0.01890 0.13460  15  ASP B CA  
1409 C C   . ASP B 17  ? 0.23267 0.63347 0.46315 -0.05594 -0.01197 0.12842  15  ASP B C   
1410 O O   . ASP B 17  ? 0.25605 0.62832 0.47101 -0.04924 -0.01036 0.11990  15  ASP B O   
1411 C CB  . ASP B 17  ? 0.32149 0.70836 0.55573 -0.08408 -0.02995 0.13080  15  ASP B CB  
1412 C CG  . ASP B 17  ? 0.37133 0.74907 0.60762 -0.10363 -0.03735 0.13415  15  ASP B CG  
1413 O OD1 . ASP B 17  ? 0.46880 0.82861 0.70090 -0.11136 -0.03655 0.13517  15  ASP B OD1 
1414 O OD2 . ASP B 17  ? 0.38890 0.77543 0.63045 -0.11093 -0.04415 0.13537  15  ASP B OD2 
1415 N N   . GLU B 18  ? 0.22413 0.64793 0.46196 -0.04515 -0.00794 0.12989  16  GLU B N   
1416 C CA  . GLU B 18  ? 0.23735 0.66206 0.47231 -0.02623 -0.00103 0.12354  16  GLU B CA  
1417 C C   . GLU B 18  ? 0.20507 0.62524 0.43233 -0.02125 0.00793  0.12125  16  GLU B C   
1418 O O   . GLU B 18  ? 0.18429 0.58429 0.39975 -0.01053 0.01121  0.11240  16  GLU B O   
1419 C CB  . GLU B 18  ? 0.20078 0.64771 0.44423 -0.01524 0.00206  0.12489  16  GLU B CB  
1420 C CG  . GLU B 18  ? 0.16707 0.61311 0.40800 0.00499  0.00995  0.11748  16  GLU B CG  
1421 C CD  . GLU B 18  ? 0.17395 0.62827 0.41088 0.01088  0.02035  0.11586  16  GLU B CD  
1422 O OE1 . GLU B 18  ? 0.17785 0.64949 0.41869 0.00381  0.02230  0.12248  16  GLU B OE1 
1423 O OE2 . GLU B 18  ? 0.17082 0.61400 0.39975 0.02187  0.02627  0.10793  16  GLU B OE2 
1424 N N   . LYS B 19  ? 0.20352 0.63372 0.43121 -0.02893 0.01128  0.12762  17  LYS B N   
1425 C CA  . LYS B 19  ? 0.20735 0.63599 0.42649 -0.02415 0.01961  0.12610  17  LYS B CA  
1426 C C   . LYS B 19  ? 0.22623 0.62705 0.43450 -0.03161 0.01697  0.12420  17  LYS B C   
1427 O O   . LYS B 19  ? 0.20045 0.58582 0.39572 -0.02278 0.02167  0.11689  17  LYS B O   
1428 C CB  . LYS B 19  ? 0.22654 0.67544 0.44839 -0.02906 0.02374  0.13424  17  LYS B CB  
1429 C CG  . LYS B 19  ? 0.26032 0.71770 0.47402 -0.01787 0.03386  0.13075  17  LYS B CG  
1430 C CD  . LYS B 19  ? 0.28990 0.76891 0.50588 -0.02340 0.03745  0.13984  17  LYS B CD  
1431 C CE  . LYS B 19  ? 0.21427 0.71847 0.43846 -0.01413 0.04138  0.13941  17  LYS B CE  
1432 N NZ  . LYS B 19  ? 0.25768 0.78406 0.48536 -0.02147 0.04387  0.14970  17  LYS B NZ  
1433 N N   . ARG B 20  ? 0.23285 0.61907 0.44184 -0.04689 0.00868  0.12822  18  ARG B N   
1434 C CA  . ARG B 20  ? 0.24675 0.59707 0.44131 -0.05205 0.00526  0.12374  18  ARG B CA  
1435 C C   . ARG B 20  ? 0.20325 0.52829 0.38466 -0.04019 0.00491  0.11124  18  ARG B C   
1436 O O   . ARG B 20  ? 0.17724 0.48309 0.34600 -0.03523 0.00803  0.10586  18  ARG B O   
1437 C CB  . ARG B 20  ? 0.30788 0.64560 0.50636 -0.06885 -0.00417 0.12763  18  ARG B CB  
1438 C CG  . ARG B 20  ? 0.33432 0.64145 0.52255 -0.07664 -0.00666 0.12687  18  ARG B CG  
1439 C CD  . ARG B 20  ? 0.37647 0.67851 0.57309 -0.09476 -0.01477 0.13307  18  ARG B CD  
1440 N NE  . ARG B 20  ? 0.42172 0.69497 0.61118 -0.10240 -0.01709 0.13362  18  ARG B NE  
1441 C CZ  . ARG B 20  ? 0.36059 0.60220 0.53644 -0.09791 -0.01876 0.12396  18  ARG B CZ  
1442 N NH1 . ARG B 20  ? 0.33906 0.57192 0.50606 -0.08716 -0.01886 0.11299  18  ARG B NH1 
1443 N NH2 . ARG B 20  ? 0.36991 0.58864 0.54182 -0.10435 -0.02034 0.12613  18  ARG B NH2 
1444 N N   . ASN B 21  ? 0.21776 0.54325 0.40236 -0.03606 0.00076  0.10730  19  ASN B N   
1445 C CA  . ASN B 21  ? 0.22816 0.53058 0.40129 -0.02563 0.00023  0.09697  19  ASN B CA  
1446 C C   . ASN B 21  ? 0.20394 0.51085 0.37341 -0.01012 0.00872  0.09174  19  ASN B C   
1447 O O   . ASN B 21  ? 0.23243 0.51670 0.39023 -0.00294 0.00977  0.08342  19  ASN B O   
1448 C CB  . ASN B 21  ? 0.26311 0.56880 0.44144 -0.02489 -0.00619 0.09604  19  ASN B CB  
1449 C CG  . ASN B 21  ? 0.29856 0.59001 0.47442 -0.03922 -0.01525 0.09650  19  ASN B CG  
1450 O OD1 . ASN B 21  ? 0.34440 0.61130 0.50990 -0.04509 -0.01663 0.09311  19  ASN B OD1 
1451 N ND2 . ASN B 21  ? 0.31483 0.62309 0.50101 -0.04542 -0.02148 0.10078  19  ASN B ND2 
1452 N N   . HIS B 22  ? 0.19901 0.53539 0.37852 -0.00512 0.01487  0.09605  20  HIS B N   
1453 C CA  . HIS B 22  ? 0.20661 0.54864 0.38286 0.00978  0.02325  0.08968  20  HIS B CA  
1454 C C   . HIS B 22  ? 0.19495 0.52486 0.35830 0.00892  0.02755  0.08682  20  HIS B C   
1455 O O   . HIS B 22  ? 0.19696 0.51423 0.35080 0.01914  0.03136  0.07763  20  HIS B O   
1456 C CB  . HIS B 22  ? 0.16548 0.54478 0.35658 0.01530  0.02884  0.09483  20  HIS B CB  
1457 C CG  . HIS B 22  ? 0.16446 0.55544 0.35200 0.02696  0.03875  0.08966  20  HIS B CG  
1458 N ND1 . HIS B 22  ? 0.16539 0.54857 0.34929 0.04272  0.04283  0.07892  20  HIS B ND1 
1459 C CD2 . HIS B 22  ? 0.17229 0.58220 0.35882 0.02483  0.04526  0.09346  20  HIS B CD2 
1460 C CE1 . HIS B 22  ? 0.18349 0.58043 0.36402 0.04999  0.05142  0.07491  20  HIS B CE1 
1461 N NE2 . HIS B 22  ? 0.17623 0.58968 0.35719 0.03939  0.05303  0.08371  20  HIS B NE2 
1462 N N   . ILE B 23  ? 0.17917 0.51324 0.34270 -0.00344 0.02666  0.09510  21  ILE B N   
1463 C CA  . ILE B 23  ? 0.20206 0.52358 0.35333 -0.00525 0.02937  0.09406  21  ILE B CA  
1464 C C   . ILE B 23  ? 0.23785 0.52412 0.37652 -0.00421 0.02510  0.08575  21  ILE B C   
1465 O O   . ILE B 23  ? 0.21394 0.48880 0.34160 0.00220  0.02840  0.07907  21  ILE B O   
1466 C CB  . ILE B 23  ? 0.18519 0.51482 0.34061 -0.01982 0.02777  0.10649  21  ILE B CB  
1467 C CG1 . ILE B 23  ? 0.20259 0.57009 0.37221 -0.02208 0.03193  0.11606  21  ILE B CG1 
1468 C CG2 . ILE B 23  ? 0.23693 0.55764 0.38068 -0.02085 0.03078  0.10742  21  ILE B CG2 
1469 C CD1 . ILE B 23  ? 0.20458 0.57884 0.38234 -0.03912 0.02814  0.12987  21  ILE B CD1 
1470 N N   . LEU B 24  ? 0.22189 0.49187 0.36195 -0.01087 0.01766  0.08585  22  LEU B N   
1471 C CA  . LEU B 24  ? 0.21487 0.45309 0.34352 -0.01054 0.01375  0.07849  22  LEU B CA  
1472 C C   . LEU B 24  ? 0.23373 0.46359 0.35671 0.00271  0.01642  0.06853  22  LEU B C   
1473 O O   . LEU B 24  ? 0.25270 0.46409 0.36495 0.00650  0.01764  0.06212  22  LEU B O   
1474 C CB  . LEU B 24  ? 0.22296 0.44906 0.35418 -0.01997 0.00565  0.07988  22  LEU B CB  
1475 C CG  . LEU B 24  ? 0.26120 0.48403 0.39571 -0.03450 0.00157  0.08754  22  LEU B CG  
1476 C CD1 . LEU B 24  ? 0.23228 0.44756 0.37034 -0.04309 -0.00635 0.08717  22  LEU B CD1 
1477 C CD2 . LEU B 24  ? 0.24454 0.44456 0.36870 -0.03655 0.00193  0.08605  22  LEU B CD2 
1478 N N   . THR B 25  ? 0.24186 0.48530 0.37297 0.00978  0.01713  0.06764  23  THR B N   
1479 C CA  . THR B 25  ? 0.27524 0.50856 0.40271 0.02206  0.01897  0.05905  23  THR B CA  
1480 C C   . THR B 25  ? 0.25189 0.49116 0.37564 0.03197  0.02657  0.05318  23  THR B C   
1481 O O   . THR B 25  ? 0.25845 0.48107 0.37514 0.03956  0.02784  0.04469  23  THR B O   
1482 C CB  . THR B 25  ? 0.23450 0.48007 0.37293 0.02739  0.01700  0.06085  23  THR B CB  
1483 O OG1 . THR B 25  ? 0.23423 0.51027 0.38482 0.03023  0.02116  0.06586  23  THR B OG1 
1484 C CG2 . THR B 25  ? 0.26010 0.49949 0.40030 0.01775  0.00873  0.06516  23  THR B CG2 
1485 N N   . THR B 26  ? 0.25758 0.52099 0.38581 0.03155  0.03158  0.05740  24  THR B N   
1486 C CA  . THR B 26  ? 0.25224 0.52294 0.37476 0.03978  0.03884  0.05119  24  THR B CA  
1487 C C   . THR B 26  ? 0.27430 0.52516 0.38286 0.03598  0.03814  0.04766  24  THR B C   
1488 O O   . THR B 26  ? 0.26797 0.50814 0.36837 0.04349  0.04072  0.03800  24  THR B O   
1489 C CB  . THR B 26  ? 0.25148 0.55508 0.38114 0.03860  0.04432  0.05800  24  THR B CB  
1490 O OG1 . THR B 26  ? 0.23024 0.55475 0.37314 0.04622  0.04675  0.05871  24  THR B OG1 
1491 C CG2 . THR B 26  ? 0.25401 0.56555 0.37436 0.04418  0.05130  0.05232  24  THR B CG2 
1492 N N   . ALA B 27  ? 0.20873 0.45472 0.31531 0.02423  0.03440  0.05554  25  ALA B N   
1493 C CA  . ALA B 27  ? 0.28905 0.51744 0.38409 0.02069  0.03324  0.05376  25  ALA B CA  
1494 C C   . ALA B 27  ? 0.28701 0.48793 0.37527 0.02432  0.02999  0.04497  25  ALA B C   
1495 O O   . ALA B 27  ? 0.30313 0.49409 0.38237 0.02846  0.03167  0.03802  25  ALA B O   
1496 C CB  . ALA B 27  ? 0.25416 0.48003 0.35087 0.00788  0.02917  0.06445  25  ALA B CB  
1497 N N   . LEU B 28  ? 0.26945 0.45981 0.36204 0.02269  0.02535  0.04529  26  LEU B N   
1498 C CA  . LEU B 28  ? 0.32502 0.49127 0.41158 0.02559  0.02248  0.03829  26  LEU B CA  
1499 C C   . LEU B 28  ? 0.33442 0.49807 0.41823 0.03670  0.02650  0.02901  26  LEU B C   
1500 O O   . LEU B 28  ? 0.32188 0.46898 0.39760 0.03842  0.02636  0.02276  26  LEU B O   
1501 C CB  . LEU B 28  ? 0.30620 0.46674 0.39788 0.02275  0.01730  0.04069  26  LEU B CB  
1502 C CG  . LEU B 28  ? 0.30764 0.45809 0.39782 0.01155  0.01187  0.04538  26  LEU B CG  
1503 C CD1 . LEU B 28  ? 0.33743 0.48537 0.43155 0.00908  0.00677  0.04657  26  LEU B CD1 
1504 C CD2 . LEU B 28  ? 0.31202 0.44076 0.39217 0.00985  0.01085  0.04130  26  LEU B CD2 
1505 N N   . ASN B 29  ? 0.30375 0.48402 0.39498 0.04432  0.03016  0.02780  27  ASN B N   
1506 C CA  . ASN B 29  ? 0.34108 0.51863 0.43044 0.05527  0.03438  0.01796  27  ASN B CA  
1507 C C   . ASN B 29  ? 0.36167 0.54107 0.44150 0.05585  0.03812  0.01253  27  ASN B C   
1508 O O   . ASN B 29  ? 0.39647 0.56112 0.46974 0.05995  0.03862  0.00356  27  ASN B O   
1509 C CB  . ASN B 29  ? 0.35535 0.55238 0.45573 0.06404  0.03809  0.01788  27  ASN B CB  
1510 C CG  . ASN B 29  ? 0.48710 0.67255 0.59371 0.07090  0.03568  0.01586  27  ASN B CG  
1511 O OD1 . ASN B 29  ? 0.49341 0.66574 0.59976 0.06573  0.03003  0.02005  27  ASN B OD1 
1512 N ND2 . ASN B 29  ? 0.53146 0.72247 0.64392 0.08285  0.04000  0.00973  27  ASN B ND2 
1513 N N   . LEU B 30  ? 0.33093 0.52863 0.40982 0.05092  0.04028  0.01849  28  LEU B N   
1514 C CA  . LEU B 30  ? 0.30173 0.50305 0.37050 0.05045  0.04306  0.01497  28  LEU B CA  
1515 C C   . LEU B 30  ? 0.40193 0.58018 0.46200 0.04557  0.03869  0.01315  28  LEU B C   
1516 O O   . LEU B 30  ? 0.38343 0.55436 0.43565 0.04906  0.03974  0.00444  28  LEU B O   
1517 C CB  . LEU B 30  ? 0.29437 0.51872 0.36410 0.04424  0.04519  0.02503  28  LEU B CB  
1518 C CG  . LEU B 30  ? 0.28984 0.54368 0.36609 0.04939  0.05142  0.02626  28  LEU B CG  
1519 C CD1 . LEU B 30  ? 0.28139 0.55676 0.35925 0.04089  0.05273  0.03886  28  LEU B CD1 
1520 C CD2 . LEU B 30  ? 0.35194 0.61240 0.42184 0.06002  0.05726  0.01342  28  LEU B CD2 
1521 N N   . PHE B 31  ? 0.33939 0.50704 0.40109 0.03732  0.03376  0.02098  29  PHE B N   
1522 C CA  . PHE B 31  ? 0.40618 0.55420 0.46094 0.03290  0.02999  0.02023  29  PHE B CA  
1523 C C   . PHE B 31  ? 0.43971 0.56877 0.49179 0.03786  0.02882  0.01084  29  PHE B C   
1524 O O   . PHE B 31  ? 0.43099 0.54972 0.47622 0.03776  0.02806  0.00607  29  PHE B O   
1525 C CB  . PHE B 31  ? 0.39706 0.53667 0.45525 0.02430  0.02528  0.02890  29  PHE B CB  
1526 C CG  . PHE B 31  ? 0.37058 0.52536 0.43235 0.01752  0.02551  0.03946  29  PHE B CG  
1527 C CD1 . PHE B 31  ? 0.34024 0.51057 0.39827 0.01760  0.02889  0.04223  29  PHE B CD1 
1528 C CD2 . PHE B 31  ? 0.31542 0.46920 0.38431 0.01042  0.02204  0.04685  29  PHE B CD2 
1529 C CE1 . PHE B 31  ? 0.36439 0.54853 0.42618 0.01069  0.02905  0.05360  29  PHE B CE1 
1530 C CE2 . PHE B 31  ? 0.32072 0.48704 0.39409 0.00305  0.02189  0.05727  29  PHE B CE2 
1531 C CZ  . PHE B 31  ? 0.35313 0.53467 0.42336 0.00321  0.02555  0.06136  29  PHE B CZ  
1532 N N   . ASP B 32  ? 0.41205 0.53721 0.47021 0.04186  0.02838  0.00908  30  ASP B N   
1533 C CA  . ASP B 32  ? 0.48320 0.58967 0.53988 0.04564  0.02694  0.00229  30  ASP B CA  
1534 C C   . ASP B 32  ? 0.49842 0.60292 0.55035 0.05149  0.02997  -0.00782 30  ASP B C   
1535 O O   . ASP B 32  ? 0.50997 0.59827 0.55792 0.05137  0.02832  -0.01308 30  ASP B O   
1536 C CB  . ASP B 32  ? 0.46087 0.56665 0.52567 0.04969  0.02611  0.00368  30  ASP B CB  
1537 C CG  . ASP B 32  ? 0.55705 0.64282 0.62094 0.05195  0.02387  -0.00022 30  ASP B CG  
1538 O OD1 . ASP B 32  ? 0.52617 0.59942 0.58622 0.04621  0.02045  0.00213  30  ASP B OD1 
1539 O OD2 . ASP B 32  ? 0.58223 0.66502 0.64981 0.05959  0.02568  -0.00531 30  ASP B OD2 
1540 N N   . GLN B 33  ? 0.47547 0.59729 0.52743 0.05596  0.03437  -0.01089 31  GLN B N   
1541 C CA  . GLN B 33  ? 0.52220 0.64280 0.56974 0.06220  0.03734  -0.02250 31  GLN B CA  
1542 C C   . GLN B 33  ? 0.52182 0.65198 0.55974 0.05930  0.03856  -0.02495 31  GLN B C   
1543 O O   . GLN B 33  ? 0.53437 0.65813 0.56640 0.06161  0.03892  -0.03507 31  GLN B O   
1544 C CB  . GLN B 33  ? 0.54812 0.68042 0.60253 0.07161  0.04187  -0.02699 31  GLN B CB  
1545 C CG  . GLN B 33  ? 0.55480 0.70034 0.60481 0.07798  0.04713  -0.03711 31  GLN B CG  
1546 C CD  . GLN B 33  ? 0.60359 0.76730 0.66245 0.08625  0.05203  -0.03726 31  GLN B CD  
1547 O OE1 . GLN B 33  ? 0.62060 0.78893 0.68896 0.08587  0.05089  -0.02822 31  GLN B OE1 
1548 N NE2 . GLN B 33  ? 0.62376 0.79819 0.67996 0.09417  0.05742  -0.04823 31  GLN B NE2 
1549 N N   . PHE B 34  ? 0.47920 0.62349 0.51544 0.05353  0.03850  -0.01543 32  PHE B N   
1550 C CA  . PHE B 34  ? 0.50303 0.65652 0.53007 0.05021  0.03879  -0.01535 32  PHE B CA  
1551 C C   . PHE B 34  ? 0.50248 0.64913 0.52743 0.04188  0.03436  -0.00574 32  PHE B C   
1552 O O   . PHE B 34  ? 0.51227 0.66569 0.53007 0.03935  0.03384  -0.00469 32  PHE B O   
1553 C CB  . PHE B 34  ? 0.47457 0.65563 0.50000 0.05172  0.04371  -0.01254 32  PHE B CB  
1554 C CG  . PHE B 34  ? 0.48882 0.68052 0.51702 0.06092  0.04907  -0.02178 32  PHE B CG  
1555 C CD1 . PHE B 34  ? 0.50822 0.70594 0.54716 0.06433  0.05099  -0.01803 32  PHE B CD1 
1556 C CD2 . PHE B 34  ? 0.51366 0.70871 0.53409 0.06657  0.05192  -0.03518 32  PHE B CD2 
1557 C CE1 . PHE B 34  ? 0.51238 0.72053 0.55508 0.07413  0.05624  -0.02659 32  PHE B CE1 
1558 C CE2 . PHE B 34  ? 0.52007 0.72337 0.54337 0.07614  0.05717  -0.04518 32  PHE B CE2 
1559 C CZ  . PHE B 34  ? 0.56929 0.77916 0.60426 0.08048  0.05956  -0.04059 32  PHE B CZ  
1560 N N   . GLY B 35  ? 0.45755 0.59191 0.48840 0.03793  0.03112  0.00110  33  GLY B N   
1561 C CA  . GLY B 35  ? 0.46915 0.59633 0.49906 0.03098  0.02731  0.00950  33  GLY B CA  
1562 C C   . GLY B 35  ? 0.44311 0.58540 0.47547 0.02603  0.02783  0.02118  33  GLY B C   
1563 O O   . GLY B 35  ? 0.43698 0.59894 0.47032 0.02761  0.03158  0.02304  33  GLY B O   
1564 N N   . PHE B 36  ? 0.43802 0.57094 0.47201 0.01988  0.02412  0.02943  34  PHE B N   
1565 C CA  . PHE B 36  ? 0.45097 0.59419 0.48953 0.01390  0.02381  0.04164  34  PHE B CA  
1566 C C   . PHE B 36  ? 0.52601 0.68706 0.55969 0.01266  0.02563  0.04771  34  PHE B C   
1567 O O   . PHE B 36  ? 0.53618 0.71560 0.57280 0.01001  0.02800  0.05579  34  PHE B O   
1568 C CB  . PHE B 36  ? 0.46852 0.59395 0.51117 0.00791  0.01914  0.04780  34  PHE B CB  
1569 C CG  . PHE B 36  ? 0.43872 0.55014 0.48582 0.00771  0.01713  0.04360  34  PHE B CG  
1570 C CD1 . PHE B 36  ? 0.40947 0.50382 0.45359 0.01075  0.01561  0.03556  34  PHE B CD1 
1571 C CD2 . PHE B 36  ? 0.38836 0.50607 0.44263 0.00419  0.01672  0.04817  34  PHE B CD2 
1572 C CE1 . PHE B 36  ? 0.38020 0.46370 0.42725 0.01040  0.01376  0.03262  34  PHE B CE1 
1573 C CE2 . PHE B 36  ? 0.38310 0.49009 0.44061 0.00374  0.01431  0.04469  34  PHE B CE2 
1574 C CZ  . PHE B 36  ? 0.40495 0.49485 0.45825 0.00707  0.01292  0.03695  34  PHE B CZ  
1575 N N   . GLN B 37  ? 0.55309 0.71098 0.57942 0.01433  0.02451  0.04439  35  GLN B N   
1576 C CA  . GLN B 37  ? 0.58494 0.75946 0.60577 0.01263  0.02513  0.05150  35  GLN B CA  
1577 C C   . GLN B 37  ? 0.51015 0.71033 0.52679 0.01567  0.03049  0.04925  35  GLN B C   
1578 O O   . GLN B 37  ? 0.48048 0.69974 0.49706 0.01227  0.03229  0.06002  35  GLN B O   
1579 C CB  . GLN B 37  ? 0.61864 0.78569 0.63261 0.01452  0.02243  0.04637  35  GLN B CB  
1580 C CG  . GLN B 37  ? 0.65952 0.80444 0.67815 0.01194  0.01770  0.05004  35  GLN B CG  
1581 C CD  . GLN B 37  ? 0.68065 0.80619 0.70050 0.01491  0.01667  0.03863  35  GLN B CD  
1582 O OE1 . GLN B 37  ? 0.56431 0.68427 0.58778 0.01604  0.01808  0.03407  35  GLN B OE1 
1583 N NE2 . GLN B 37  ? 0.59863 0.71519 0.61609 0.01596  0.01407  0.03509  35  GLN B NE2 
1584 N N   . HIS B 38  ? 0.50351 0.70444 0.51699 0.02224  0.03330  0.03534  36  HIS B N   
1585 C CA  . HIS B 38  ? 0.50031 0.72438 0.50890 0.02699  0.03889  0.02965  36  HIS B CA  
1586 C C   . HIS B 38  ? 0.46659 0.70958 0.48230 0.02577  0.04296  0.03793  36  HIS B C   
1587 O O   . HIS B 38  ? 0.45053 0.71837 0.46200 0.02846  0.04809  0.03713  36  HIS B O   
1588 C CB  . HIS B 38  ? 0.53772 0.75170 0.54447 0.03454  0.04037  0.01247  36  HIS B CB  
1589 C CG  . HIS B 38  ? 0.66577 0.89811 0.66400 0.04047  0.04513  0.00164  36  HIS B CG  
1590 N ND1 . HIS B 38  ? 0.65654 0.88115 0.65368 0.04777  0.04709  -0.01436 36  HIS B ND1 
1591 C CD2 . HIS B 38  ? 0.69313 0.95119 0.68324 0.04025  0.04837  0.00409  36  HIS B CD2 
1592 C CE1 . HIS B 38  ? 0.71095 0.95483 0.69955 0.05207  0.05139  -0.02276 36  HIS B CE1 
1593 N NE2 . HIS B 38  ? 0.73733 1.00301 0.72088 0.04761  0.05237  -0.01182 36  HIS B NE2 
1594 N N   . ILE B 39  ? 0.45506 0.68864 0.48134 0.02154  0.04082  0.04557  37  ILE B N   
1595 C CA  . ILE B 39  ? 0.36101 0.61029 0.39637 0.02129  0.04425  0.05031  37  ILE B CA  
1596 C C   . ILE B 39  ? 0.39431 0.65292 0.43564 0.01170  0.04285  0.06771  37  ILE B C   
1597 O O   . ILE B 39  ? 0.40216 0.64233 0.44895 0.00532  0.03765  0.07428  37  ILE B O   
1598 C CB  . ILE B 39  ? 0.35218 0.58530 0.39601 0.02371  0.04247  0.04479  37  ILE B CB  
1599 C CG1 . ILE B 39  ? 0.36997 0.59184 0.40928 0.03279  0.04360  0.02889  37  ILE B CG1 
1600 C CG2 . ILE B 39  ? 0.35535 0.60743 0.41006 0.02305  0.04541  0.05083  37  ILE B CG2 
1601 C CD1 . ILE B 39  ? 0.36895 0.61146 0.40560 0.04107  0.05014  0.02042  37  ILE B CD1 
1602 N N   . SER B 40  ? 0.31801 0.60540 0.35938 0.01062  0.04771  0.07493  38  SER B N   
1603 C CA  . SER B 40  ? 0.33037 0.62848 0.37837 0.00072  0.04667  0.09284  38  SER B CA  
1604 C C   . SER B 40  ? 0.34425 0.65021 0.40596 -0.00273 0.04745  0.09797  38  SER B C   
1605 O O   . SER B 40  ? 0.31931 0.62512 0.38519 0.00348  0.04914  0.08826  38  SER B O   
1606 C CB  . SER B 40  ? 0.31583 0.64340 0.35682 -0.00009 0.05136  0.10053  38  SER B CB  
1607 O OG  . SER B 40  ? 0.29650 0.65110 0.33725 0.00632  0.05874  0.09452  38  SER B OG  
1608 N N   . ILE B 41  ? 0.34826 0.66070 0.41785 -0.01323 0.04562  0.11419  39  ILE B N   
1609 C CA  . ILE B 41  ? 0.38783 0.71364 0.47111 -0.01835 0.04636  0.12119  39  ILE B CA  
1610 C C   . ILE B 41  ? 0.33436 0.69438 0.41859 -0.01162 0.05457  0.11843  39  ILE B C   
1611 O O   . ILE B 41  ? 0.33245 0.70013 0.42525 -0.00775 0.05631  0.11347  39  ILE B O   
1612 C CB  . ILE B 41  ? 0.37909 0.70684 0.47042 -0.03191 0.04305  0.13997  39  ILE B CB  
1613 C CG1 . ILE B 41  ? 0.42993 0.72200 0.52331 -0.03810 0.03483  0.14115  39  ILE B CG1 
1614 C CG2 . ILE B 41  ? 0.33489 0.68201 0.44043 -0.03779 0.04435  0.14750  39  ILE B CG2 
1615 C CD1 . ILE B 41  ? 0.35346 0.64342 0.45585 -0.05167 0.03104  0.15941  39  ILE B CD1 
1616 N N   . MET B 42  ? 0.29068 0.67280 0.36592 -0.00946 0.05982  0.12127  40  MET B N   
1617 C CA  . MET B 42  ? 0.34078 0.75441 0.41539 -0.00229 0.06751  0.11715  40  MET B CA  
1618 C C   . MET B 42  ? 0.29251 0.70444 0.36451 0.01132  0.07156  0.09801  40  MET B C   
1619 O O   . MET B 42  ? 0.26626 0.69186 0.34279 0.01770  0.07492  0.09255  40  MET B O   
1620 C CB  . MET B 42  ? 0.39443 0.82402 0.45616 -0.00214 0.06940  0.12095  40  MET B CB  
1621 C CG  . MET B 42  ? 0.42806 0.86339 0.49375 -0.01437 0.06563  0.14084  40  MET B CG  
1622 S SD  . MET B 42  ? 0.65280 1.10980 0.73219 -0.01843 0.06687  0.14926  40  MET B SD  
1623 C CE  . MET B 42  ? 0.52495 1.00195 0.59847 -0.00289 0.07472  0.13086  40  MET B CE  
1624 N N   . ARG B 43  ? 0.28552 0.67051 0.34785 0.01619  0.06810  0.08585  41  ARG B N   
1625 C CA  . ARG B 43  ? 0.30269 0.67769 0.36363 0.02809  0.06984  0.06790  41  ARG B CA  
1626 C C   . ARG B 43  ? 0.30491 0.66959 0.37999 0.02830  0.06696  0.06784  41  ARG B C   
1627 O O   . ARG B 43  ? 0.21940 0.59409 0.30039 0.03749  0.07104  0.05983  41  ARG B O   
1628 C CB  . ARG B 43  ? 0.29883 0.64587 0.34788 0.03078  0.06568  0.05719  41  ARG B CB  
1629 C CG  . ARG B 43  ? 0.32512 0.65452 0.37359 0.04108  0.06576  0.04000  41  ARG B CG  
1630 C CD  . ARG B 43  ? 0.29751 0.64805 0.34441 0.05243  0.07363  0.02841  41  ARG B CD  
1631 N NE  . ARG B 43  ? 0.41611 0.74606 0.45997 0.06198  0.07322  0.01121  41  ARG B NE  
1632 C CZ  . ARG B 43  ? 0.40130 0.71290 0.43383 0.06279  0.07047  0.00176  41  ARG B CZ  
1633 N NH1 . ARG B 43  ? 0.44229 0.75422 0.46505 0.05562  0.06781  0.00742  41  ARG B NH1 
1634 N NH2 . ARG B 43  ? 0.44517 0.73824 0.47707 0.07085  0.07017  -0.01310 41  ARG B NH2 
1635 N N   . ILE B 44  ? 0.27028 0.61553 0.35090 0.01849  0.05981  0.07664  42  ILE B N   
1636 C CA  . ILE B 44  ? 0.29338 0.62955 0.38628 0.01704  0.05599  0.07741  42  ILE B CA  
1637 C C   . ILE B 44  ? 0.27715 0.64493 0.38320 0.01625  0.06016  0.08507  42  ILE B C   
1638 O O   . ILE B 44  ? 0.25166 0.62407 0.36683 0.02235  0.06082  0.08048  42  ILE B O   
1639 C CB  . ILE B 44  ? 0.28180 0.59369 0.37675 0.00551  0.04781  0.08538  42  ILE B CB  
1640 C CG1 . ILE B 44  ? 0.33212 0.61252 0.41671 0.00818  0.04373  0.07609  42  ILE B CG1 
1641 C CG2 . ILE B 44  ? 0.29174 0.60243 0.39990 0.00110  0.04387  0.08919  42  ILE B CG2 
1642 C CD1 . ILE B 44  ? 0.36713 0.62625 0.45162 -0.00213 0.03710  0.08369  42  ILE B CD1 
1643 N N   . ILE B 45  ? 0.24935 0.64042 0.35724 0.00861  0.06294  0.09788  43  ILE B N   
1644 C CA  . ILE B 45  ? 0.26912 0.68914 0.38832 0.00612  0.06603  0.10647  43  ILE B CA  
1645 C C   . ILE B 45  ? 0.28039 0.71557 0.39651 0.02005  0.07235  0.09471  43  ILE B C   
1646 O O   . ILE B 45  ? 0.24357 0.69023 0.36984 0.02344  0.07315  0.09444  43  ILE B O   
1647 C CB  . ILE B 45  ? 0.30888 0.73909 0.42483 -0.00483 0.06524  0.12098  43  ILE B CB  
1648 C CG1 . ILE B 45  ? 0.30750 0.72537 0.43336 -0.01999 0.05810  0.13469  43  ILE B CG1 
1649 C CG2 . ILE B 45  ? 0.35444 0.81222 0.47082 -0.00196 0.06976  0.12364  43  ILE B CG2 
1650 C CD1 . ILE B 45  ? 0.37309 0.79199 0.49405 -0.02988 0.05640  0.14820  43  ILE B CD1 
1651 N N   . THR B 46  ? 0.26863 0.70398 0.37071 0.02807  0.07667  0.08469  44  THR B N   
1652 C CA  . THR B 46  ? 0.28663 0.73329 0.38525 0.04136  0.08255  0.07177  44  THR B CA  
1653 C C   . THR B 46  ? 0.28403 0.71636 0.38908 0.05208  0.08244  0.05926  44  THR B C   
1654 O O   . THR B 46  ? 0.25611 0.69809 0.36847 0.06015  0.08519  0.05462  44  THR B O   
1655 C CB  . THR B 46  ? 0.30037 0.74938 0.38180 0.04607  0.08615  0.06329  44  THR B CB  
1656 O OG1 . THR B 46  ? 0.37337 0.83264 0.44923 0.03524  0.08474  0.07705  44  THR B OG1 
1657 C CG2 . THR B 46  ? 0.33615 0.80164 0.41502 0.05736  0.09234  0.05250  44  THR B CG2 
1658 N N   . GLU B 47  ? 0.27052 0.68001 0.37371 0.05259  0.07913  0.05435  45  GLU B N   
1659 C CA  . GLU B 47  ? 0.27375 0.66906 0.38411 0.06238  0.07813  0.04439  45  GLU B CA  
1660 C C   . GLU B 47  ? 0.26403 0.66553 0.39110 0.05937  0.07469  0.05310  45  GLU B C   
1661 O O   . GLU B 47  ? 0.25259 0.65588 0.38711 0.06915  0.07595  0.04710  45  GLU B O   
1662 C CB  . GLU B 47  ? 0.24410 0.60103 0.34487 0.06056  0.07134  0.03782  45  GLU B CB  
1663 C CG  . GLU B 47  ? 0.40066 0.74934 0.48475 0.06219  0.07306  0.02931  45  GLU B CG  
1664 C CD  . GLU B 47  ? 0.44585 0.78941 0.52557 0.07622  0.07739  0.01165  45  GLU B CD  
1665 O OE1 . GLU B 47  ? 0.46732 0.80526 0.55700 0.08437  0.07753  0.00666  45  GLU B OE1 
1666 O OE2 . GLU B 47  ? 0.45721 0.80123 0.52392 0.07879  0.08003  0.00297  45  GLU B OE2 
1667 N N   . ALA B 48  ? 0.23506 0.63732 0.36764 0.04550  0.06949  0.06691  46  ALA B N   
1668 C CA  . ALA B 48  ? 0.23898 0.64815 0.38738 0.04130  0.06534  0.07483  46  ALA B CA  
1669 C C   . ALA B 48  ? 0.24440 0.67862 0.39948 0.04129  0.06821  0.08033  46  ALA B C   
1670 O O   . ALA B 48  ? 0.19359 0.63484 0.36135 0.03824  0.06457  0.08629  46  ALA B O   
1671 C CB  . ALA B 48  ? 0.23315 0.62522 0.38177 0.02527  0.05678  0.08505  46  ALA B CB  
1672 N N   . LYS B 49  ? 0.24806 0.69686 0.39482 0.04439  0.07430  0.07857  47  LYS B N   
1673 C CA  . LYS B 49  ? 0.25463 0.72940 0.40691 0.04502  0.07788  0.08359  47  LYS B CA  
1674 C C   . LYS B 49  ? 0.25397 0.73942 0.41669 0.03031  0.07293  0.09982  47  LYS B C   
1675 O O   . LYS B 49  ? 0.24099 0.74165 0.41554 0.03044  0.07238  0.10413  47  LYS B O   
1676 C CB  . LYS B 49  ? 0.25778 0.73837 0.41771 0.05919  0.08111  0.07421  47  LYS B CB  
1677 C CG  . LYS B 49  ? 0.27203 0.73459 0.42485 0.07282  0.08383  0.05797  47  LYS B CG  
1678 C CD  . LYS B 49  ? 0.27776 0.74784 0.43848 0.08686  0.08789  0.04961  47  LYS B CD  
1679 C CE  . LYS B 49  ? 0.36299 0.81144 0.51738 0.10010  0.09009  0.03303  47  LYS B CE  
1680 N NZ  . LYS B 49  ? 0.40554 0.82830 0.55311 0.09639  0.08534  0.03068  47  LYS B NZ  
1681 N N   . ILE B 50  ? 0.23459 0.71113 0.39329 0.01729  0.06899  0.10887  48  ILE B N   
1682 C CA  . ILE B 50  ? 0.25070 0.73392 0.41827 0.00198  0.06387  0.12404  48  ILE B CA  
1683 C C   . ILE B 50  ? 0.27768 0.77144 0.43761 -0.00525 0.06605  0.13326  48  ILE B C   
1684 O O   . ILE B 50  ? 0.28255 0.77420 0.42939 -0.00045 0.06994  0.12850  48  ILE B O   
1685 C CB  . ILE B 50  ? 0.25055 0.71123 0.42296 -0.00894 0.05562  0.12821  48  ILE B CB  
1686 C CG1 . ILE B 50  ? 0.30331 0.74316 0.46409 -0.00971 0.05542  0.12481  48  ILE B CG1 
1687 C CG2 . ILE B 50  ? 0.30814 0.76270 0.48967 -0.00307 0.05229  0.12152  48  ILE B CG2 
1688 C CD1 . ILE B 50  ? 0.27597 0.69713 0.44001 -0.02468 0.04796  0.13363  48  ILE B CD1 
1689 N N   . ALA B 51  ? 0.22648 0.73249 0.39493 -0.01694 0.06311  0.14678  49  ALA B N   
1690 C CA  . ALA B 51  ? 0.23740 0.75118 0.40075 -0.02600 0.06340  0.15847  49  ALA B CA  
1691 C C   . ALA B 51  ? 0.28887 0.77730 0.44662 -0.03503 0.05841  0.16284  49  ALA B C   
1692 O O   . ALA B 51  ? 0.24943 0.71703 0.41281 -0.04093 0.05247  0.16253  49  ALA B O   
1693 C CB  . ALA B 51  ? 0.24712 0.77818 0.42263 -0.03687 0.06073  0.17212  49  ALA B CB  
1694 N N   . LYS B 52  ? 0.27220 0.76297 0.41875 -0.03571 0.06069  0.16676  50  LYS B N   
1695 C CA  . LYS B 52  ? 0.29503 0.76299 0.43662 -0.04394 0.05609  0.17248  50  LYS B CA  
1696 C C   . LYS B 52  ? 0.29922 0.75451 0.45282 -0.05932 0.04834  0.18469  50  LYS B C   
1697 O O   . LYS B 52  ? 0.33144 0.76075 0.48628 -0.06509 0.04308  0.18461  50  LYS B O   
1698 C CB  . LYS B 52  ? 0.31291 0.79044 0.44279 -0.04392 0.05877  0.17852  50  LYS B CB  
1699 C CG  . LYS B 52  ? 0.36789 0.82175 0.49258 -0.05095 0.05406  0.18470  50  LYS B CG  
1700 C CD  . LYS B 52  ? 0.44185 0.90581 0.55358 -0.04874 0.05653  0.18893  50  LYS B CD  
1701 C CE  . LYS B 52  ? 0.41283 0.87152 0.52883 -0.06147 0.05113  0.20705  50  LYS B CE  
1702 N NZ  . LYS B 52  ? 0.46249 0.92984 0.56635 -0.05927 0.05249  0.21172  50  LYS B NZ  
1703 N N   . GLN B 53  ? 0.29058 0.76374 0.45335 -0.06610 0.04748  0.19454  51  GLN B N   
1704 C CA  . GLN B 53  ? 0.32996 0.79147 0.50413 -0.08146 0.03983  0.20585  51  GLN B CA  
1705 C C   . GLN B 53  ? 0.33688 0.78247 0.51981 -0.08405 0.03468  0.19891  51  GLN B C   
1706 O O   . GLN B 53  ? 0.37020 0.79381 0.55871 -0.09567 0.02736  0.20334  51  GLN B O   
1707 C CB  . GLN B 53  ? 0.46151 0.94920 0.64330 -0.08736 0.04073  0.21756  51  GLN B CB  
1708 C CG  . GLN B 53  ? 0.46774 0.95189 0.66439 -0.10078 0.03385  0.22539  51  GLN B CG  
1709 C CD  . GLN B 53  ? 0.61099 1.10654 0.81333 -0.11234 0.03195  0.24197  51  GLN B CD  
1710 O OE1 . GLN B 53  ? 0.60353 1.12003 0.80035 -0.10875 0.03708  0.24791  51  GLN B OE1 
1711 N NE2 . GLN B 53  ? 0.63206 1.11422 0.84568 -0.12646 0.02433  0.24917  51  GLN B NE2 
1712 N N   . SER B 54  ? 0.32508 0.77989 0.50888 -0.07291 0.03805  0.18737  52  SER B N   
1713 C CA  . SER B 54  ? 0.33149 0.77225 0.52278 -0.07448 0.03275  0.18066  52  SER B CA  
1714 C C   . SER B 54  ? 0.31378 0.72485 0.49932 -0.07527 0.02944  0.17487  52  SER B C   
1715 O O   . SER B 54  ? 0.28671 0.68016 0.47845 -0.08279 0.02244  0.17338  52  SER B O   
1716 C CB  . SER B 54  ? 0.31504 0.77162 0.50883 -0.06091 0.03693  0.17014  52  SER B CB  
1717 O OG  . SER B 54  ? 0.27613 0.76141 0.47490 -0.05806 0.04105  0.17434  52  SER B OG  
1718 N N   . PHE B 55  ? 0.31971 0.72567 0.49325 -0.06728 0.03425  0.17063  53  PHE B N   
1719 C CA  . PHE B 55  ? 0.26888 0.64761 0.43733 -0.06813 0.03139  0.16596  53  PHE B CA  
1720 C C   . PHE B 55  ? 0.29368 0.65084 0.46558 -0.08320 0.02421  0.17601  53  PHE B C   
1721 O O   . PHE B 55  ? 0.34822 0.68112 0.52278 -0.08864 0.01812  0.17249  53  PHE B O   
1722 C CB  . PHE B 55  ? 0.26518 0.64401 0.41977 -0.05751 0.03772  0.16045  53  PHE B CB  
1723 C CG  . PHE B 55  ? 0.33869 0.68111 0.48280 -0.05621 0.03299  0.15312  53  PHE B CG  
1724 C CD1 . PHE B 55  ? 0.36292 0.68800 0.50402 -0.06480 0.02935  0.16191  53  PHE B CD1 
1725 C CD2 . PHE B 55  ? 0.31128 0.63496 0.44854 -0.04592 0.03164  0.13742  53  PHE B CD2 
1726 C CE1 . PHE B 55  ? 0.33342 0.62531 0.46524 -0.06250 0.02492  0.15461  53  PHE B CE1 
1727 C CE2 . PHE B 55  ? 0.32213 0.61244 0.44944 -0.04452 0.02719  0.13035  53  PHE B CE2 
1728 C CZ  . PHE B 55  ? 0.34028 0.61531 0.46503 -0.05249 0.02396  0.13853  53  PHE B CZ  
1729 N N   . TYR B 56  ? 0.29601 0.65967 0.46726 -0.08942 0.02439  0.18779  54  TYR B N   
1730 C CA  . TYR B 56  ? 0.35682 0.69685 0.53097 -0.10215 0.01770  0.19704  54  TYR B CA  
1731 C C   . TYR B 56  ? 0.38417 0.71830 0.57101 -0.11459 0.01051  0.20079  54  TYR B C   
1732 O O   . TYR B 56  ? 0.40669 0.71457 0.59670 -0.12466 0.00382  0.20409  54  TYR B O   
1733 C CB  . TYR B 56  ? 0.33890 0.68632 0.50790 -0.10383 0.01982  0.20890  54  TYR B CB  
1734 C CG  . TYR B 56  ? 0.36221 0.70952 0.51740 -0.09343 0.02499  0.20497  54  TYR B CG  
1735 C CD1 . TYR B 56  ? 0.38600 0.70566 0.53611 -0.09403 0.02210  0.20372  54  TYR B CD1 
1736 C CD2 . TYR B 56  ? 0.38272 0.75697 0.52963 -0.08286 0.03248  0.20165  54  TYR B CD2 
1737 C CE1 . TYR B 56  ? 0.42433 0.74477 0.56168 -0.08485 0.02640  0.20015  54  TYR B CE1 
1738 C CE2 . TYR B 56  ? 0.35420 0.72835 0.48760 -0.07380 0.03661  0.19674  54  TYR B CE2 
1739 C CZ  . TYR B 56  ? 0.42769 0.77574 0.55644 -0.07507 0.03348  0.19644  54  TYR B CZ  
1740 O OH  . TYR B 56  ? 0.43781 0.78717 0.55294 -0.06637 0.03721  0.19165  54  TYR B OH  
1741 N N   . MET B 57  ? 0.32623 0.68288 0.52021 -0.11366 0.01147  0.19934  55  MET B N   
1742 C CA  . MET B 57  ? 0.39053 0.74103 0.59580 -0.12489 0.00401  0.20022  55  MET B CA  
1743 C C   . MET B 57  ? 0.37069 0.69704 0.57595 -0.12582 -0.00141 0.18924  55  MET B C   
1744 O O   . MET B 57  ? 0.38519 0.69145 0.59575 -0.13733 -0.00936 0.18921  55  MET B O   
1745 C CB  . MET B 57  ? 0.40506 0.78659 0.61777 -0.12223 0.00636  0.20074  55  MET B CB  
1746 C CG  . MET B 57  ? 0.43394 0.83391 0.65282 -0.12986 0.00681  0.21380  55  MET B CG  
1747 S SD  . MET B 57  ? 0.62568 1.06744 0.84928 -0.12063 0.01355  0.21381  55  MET B SD  
1748 C CE  . MET B 57  ? 0.53625 0.97510 0.76666 -0.11823 0.00900  0.20231  55  MET B CE  
1749 N N   . ALA B 58  ? 0.33932 0.66727 0.53841 -0.11369 0.00268  0.17923  56  ALA B N   
1750 C CA  . ALA B 58  ? 0.33319 0.64200 0.53171 -0.11293 -0.00204 0.16844  56  ALA B CA  
1751 C C   . ALA B 58  ? 0.35974 0.63051 0.54528 -0.11124 -0.00475 0.16244  56  ALA B C   
1752 O O   . ALA B 58  ? 0.33061 0.57507 0.51342 -0.11437 -0.01151 0.15406  56  ALA B O   
1753 C CB  . ALA B 58  ? 0.35542 0.67614 0.54835 -0.09652 0.00257  0.15706  56  ALA B CB  
1754 N N   . PHE B 59  ? 0.34257 0.61133 0.51983 -0.10585 0.00040  0.16616  57  PHE B N   
1755 C CA  . PHE B 59  ? 0.35296 0.58972 0.51726 -0.10042 -0.00099 0.15910  57  PHE B CA  
1756 C C   . PHE B 59  ? 0.36614 0.59761 0.53070 -0.10661 -0.00037 0.17215  57  PHE B C   
1757 O O   . PHE B 59  ? 0.39060 0.64754 0.55578 -0.10544 0.00561  0.18216  57  PHE B O   
1758 C CB  . PHE B 59  ? 0.32958 0.56854 0.48096 -0.08381 0.00459  0.14746  57  PHE B CB  
1759 C CG  . PHE B 59  ? 0.31925 0.56467 0.47113 -0.07666 0.00448  0.13647  57  PHE B CG  
1760 C CD1 . PHE B 59  ? 0.35522 0.57784 0.50514 -0.07785 -0.00181 0.12710  57  PHE B CD1 
1761 C CD2 . PHE B 59  ? 0.31617 0.59132 0.47083 -0.06850 0.01070  0.13592  57  PHE B CD2 
1762 C CE1 . PHE B 59  ? 0.32290 0.55234 0.47361 -0.07159 -0.00246 0.11881  57  PHE B CE1 
1763 C CE2 . PHE B 59  ? 0.30872 0.58942 0.46549 -0.06148 0.01019  0.12720  57  PHE B CE2 
1764 C CZ  . PHE B 59  ? 0.31436 0.57222 0.46908 -0.06326 0.00337  0.11937  57  PHE B CZ  
1765 N N   . PRO B 60  ? 0.34643 0.54636 0.51074 -0.11290 -0.00628 0.17279  58  PRO B N   
1766 C CA  . PRO B 60  ? 0.39422 0.58944 0.56218 -0.12039 -0.00665 0.18814  58  PRO B CA  
1767 C C   . PRO B 60  ? 0.36354 0.55672 0.51950 -0.11006 -0.00227 0.18910  58  PRO B C   
1768 O O   . PRO B 60  ? 0.39696 0.59607 0.55525 -0.11461 -0.00108 0.20403  58  PRO B O   
1769 C CB  . PRO B 60  ? 0.45129 0.61065 0.62415 -0.12960 -0.01498 0.18624  58  PRO B CB  
1770 C CG  . PRO B 60  ? 0.42159 0.57455 0.59493 -0.12991 -0.01892 0.17191  58  PRO B CG  
1771 C CD  . PRO B 60  ? 0.39279 0.56233 0.55619 -0.11554 -0.01333 0.16138  58  PRO B CD  
1772 N N   . SER B 61  ? 0.34103 0.52652 0.48470 -0.09704 -0.00028 0.17439  59  SER B N   
1773 C CA  . SER B 61  ? 0.36816 0.54929 0.50006 -0.08730 0.00272  0.17276  59  SER B CA  
1774 C C   . SER B 61  ? 0.34474 0.52874 0.46616 -0.07432 0.00601  0.15609  59  SER B C   
1775 O O   . SER B 61  ? 0.35307 0.53345 0.47619 -0.07304 0.00450  0.14594  59  SER B O   
1776 C CB  . SER B 61  ? 0.34372 0.49132 0.47443 -0.08866 -0.00247 0.17320  59  SER B CB  
1777 O OG  . SER B 61  ? 0.36886 0.49171 0.49677 -0.08546 -0.00617 0.15793  59  SER B OG  
1778 N N   . LYS B 62  ? 0.29268 0.48353 0.40350 -0.06513 0.01015  0.15372  60  LYS B N   
1779 C CA  . LYS B 62  ? 0.35243 0.54276 0.45360 -0.05321 0.01288  0.13779  60  LYS B CA  
1780 C C   . LYS B 62  ? 0.34250 0.50166 0.44041 -0.05044 0.00825  0.12617  60  LYS B C   
1781 O O   . LYS B 62  ? 0.32011 0.47591 0.41469 -0.04423 0.00878  0.11380  60  LYS B O   
1782 C CB  . LYS B 62  ? 0.35318 0.55597 0.44353 -0.04517 0.01745  0.13700  60  LYS B CB  
1783 C CG  . LYS B 62  ? 0.39634 0.60578 0.47907 -0.03403 0.02136  0.12173  60  LYS B CG  
1784 C CD  . LYS B 62  ? 0.44500 0.64295 0.51641 -0.02640 0.02141  0.11354  60  LYS B CD  
1785 C CE  . LYS B 62  ? 0.46121 0.66783 0.52560 -0.01615 0.02567  0.09947  60  LYS B CE  
1786 N NZ  . LYS B 62  ? 0.44369 0.64030 0.49747 -0.01021 0.02520  0.09211  60  LYS B NZ  
1787 N N   . ASP B 63  ? 0.30455 0.44122 0.40358 -0.05449 0.00395  0.13026  61  ASP B N   
1788 C CA  . ASP B 63  ? 0.39653 0.50532 0.49226 -0.05142 0.00025  0.11909  61  ASP B CA  
1789 C C   . ASP B 63  ? 0.34273 0.44111 0.44476 -0.05758 -0.00378 0.11435  61  ASP B C   
1790 O O   . ASP B 63  ? 0.35820 0.44182 0.45585 -0.05354 -0.00543 0.10243  61  ASP B O   
1791 C CB  . ASP B 63  ? 0.39934 0.48858 0.49486 -0.05225 -0.00256 0.12445  61  ASP B CB  
1792 C CG  . ASP B 63  ? 0.46580 0.56439 0.55319 -0.04474 0.00058  0.12643  61  ASP B CG  
1793 O OD1 . ASP B 63  ? 0.45884 0.57552 0.53947 -0.03855 0.00485  0.12067  61  ASP B OD1 
1794 O OD2 . ASP B 63  ? 0.45409 0.54240 0.54215 -0.04495 -0.00143 0.13369  61  ASP B OD2 
1795 N N   . SER B 64  ? 0.35489 0.46240 0.46701 -0.06776 -0.00553 0.12373  62  SER B N   
1796 C CA  . SER B 64  ? 0.36490 0.46804 0.48308 -0.07426 -0.00960 0.11914  62  SER B CA  
1797 C C   . SER B 64  ? 0.35607 0.47668 0.47180 -0.06789 -0.00689 0.11103  62  SER B C   
1798 O O   . SER B 64  ? 0.34918 0.46013 0.46303 -0.06671 -0.00975 0.10118  62  SER B O   
1799 C CB  . SER B 64  ? 0.38123 0.49275 0.51206 -0.08756 -0.01218 0.13222  62  SER B CB  
1800 O OG  . SER B 64  ? 0.45308 0.54961 0.58944 -0.09597 -0.01841 0.12743  62  SER B OG  
1801 N N   . PHE B 65  ? 0.33247 0.47942 0.44834 -0.06349 -0.00131 0.11535  63  PHE B N   
1802 C CA  . PHE B 65  ? 0.29319 0.45630 0.40705 -0.05510 0.00212  0.10764  63  PHE B CA  
1803 C C   . PHE B 65  ? 0.32812 0.47405 0.43150 -0.04506 0.00232  0.09435  63  PHE B C   
1804 O O   . PHE B 65  ? 0.28308 0.42687 0.38612 -0.04187 0.00092  0.08656  63  PHE B O   
1805 C CB  . PHE B 65  ? 0.32871 0.52005 0.44267 -0.05062 0.00889  0.11339  63  PHE B CB  
1806 C CG  . PHE B 65  ? 0.29257 0.50036 0.40525 -0.04062 0.01319  0.10541  63  PHE B CG  
1807 C CD1 . PHE B 65  ? 0.27987 0.50400 0.40219 -0.04239 0.01272  0.10650  63  PHE B CD1 
1808 C CD2 . PHE B 65  ? 0.25729 0.46352 0.35998 -0.02941 0.01728  0.09671  63  PHE B CD2 
1809 C CE1 . PHE B 65  ? 0.25723 0.49538 0.37968 -0.03203 0.01662  0.09954  63  PHE B CE1 
1810 C CE2 . PHE B 65  ? 0.29555 0.51419 0.39799 -0.01991 0.02110  0.08908  63  PHE B CE2 
1811 C CZ  . PHE B 65  ? 0.22800 0.46228 0.34073 -0.02069 0.02085  0.09068  63  PHE B CZ  
1812 N N   . ILE B 66  ? 0.29707 0.43196 0.39230 -0.04022 0.00389  0.09246  64  ILE B N   
1813 C CA  . ILE B 66  ? 0.29196 0.41290 0.37819 -0.03128 0.00444  0.08067  64  ILE B CA  
1814 C C   . ILE B 66  ? 0.32052 0.41897 0.40599 -0.03401 -0.00062 0.07432  64  ILE B C   
1815 O O   . ILE B 66  ? 0.34147 0.43461 0.42272 -0.02850 -0.00071 0.06540  64  ILE B O   
1816 C CB  . ILE B 66  ? 0.33263 0.44945 0.41137 -0.02648 0.00679  0.08083  64  ILE B CB  
1817 C CG1 . ILE B 66  ? 0.37555 0.51527 0.45131 -0.02001 0.01245  0.08015  64  ILE B CG1 
1818 C CG2 . ILE B 66  ? 0.38420 0.47994 0.45571 -0.02109 0.00541  0.07105  64  ILE B CG2 
1819 C CD1 . ILE B 66  ? 0.44577 0.58879 0.51497 -0.01714 0.01456  0.08229  64  ILE B CD1 
1820 N N   . ILE B 67  ? 0.29390 0.37966 0.38372 -0.04272 -0.00492 0.07871  65  ILE B N   
1821 C CA  . ILE B 67  ? 0.33310 0.39939 0.42153 -0.04543 -0.00956 0.07122  65  ILE B CA  
1822 C C   . ILE B 67  ? 0.32075 0.39802 0.41270 -0.04769 -0.01153 0.06850  65  ILE B C   
1823 O O   . ILE B 67  ? 0.31529 0.38402 0.40255 -0.04519 -0.01348 0.06007  65  ILE B O   
1824 C CB  . ILE B 67  ? 0.37991 0.42899 0.47287 -0.05418 -0.01381 0.07550  65  ILE B CB  
1825 C CG1 . ILE B 67  ? 0.42772 0.45864 0.51545 -0.04921 -0.01303 0.07362  65  ILE B CG1 
1826 C CG2 . ILE B 67  ? 0.41530 0.45107 0.50906 -0.06002 -0.01911 0.06849  65  ILE B CG2 
1827 C CD1 . ILE B 67  ? 0.50005 0.51294 0.59355 -0.05637 -0.01683 0.07857  65  ILE B CD1 
1828 N N   . GLU B 68  ? 0.33967 0.43811 0.44021 -0.05226 -0.01098 0.07634  66  GLU B N   
1829 C CA  . GLU B 68  ? 0.32736 0.44016 0.43266 -0.05338 -0.01275 0.07485  66  GLU B CA  
1830 C C   . GLU B 68  ? 0.27602 0.39618 0.37629 -0.04167 -0.00908 0.06851  66  GLU B C   
1831 O O   . GLU B 68  ? 0.32502 0.44563 0.42484 -0.04011 -0.01163 0.06380  66  GLU B O   
1832 C CB  . GLU B 68  ? 0.29030 0.42717 0.40734 -0.06027 -0.01224 0.08550  66  GLU B CB  
1833 C CG  . GLU B 68  ? 0.32082 0.45037 0.44517 -0.07399 -0.01802 0.09067  66  GLU B CG  
1834 C CD  . GLU B 68  ? 0.38240 0.53715 0.51961 -0.08200 -0.01949 0.09882  66  GLU B CD  
1835 O OE1 . GLU B 68  ? 0.38677 0.55125 0.52659 -0.08157 -0.02214 0.09496  66  GLU B OE1 
1836 O OE2 . GLU B 68  ? 0.40680 0.57208 0.55208 -0.08933 -0.01843 0.10982  66  GLU B OE2 
1837 N N   . CYS B 69  ? 0.22927 0.35529 0.32584 -0.03357 -0.00341 0.06845  67  CYS B N   
1838 C CA  . CYS B 69  ? 0.27153 0.40058 0.36359 -0.02257 -0.00014 0.06152  67  CYS B CA  
1839 C C   . CYS B 69  ? 0.29338 0.40038 0.37699 -0.01955 -0.00240 0.05313  67  CYS B C   
1840 O O   . CYS B 69  ? 0.26385 0.37087 0.34632 -0.01484 -0.00306 0.04869  67  CYS B O   
1841 C CB  . CYS B 69  ? 0.30139 0.43879 0.39001 -0.01540 0.00590  0.06144  67  CYS B CB  
1842 S SG  . CYS B 69  ? 0.32707 0.49476 0.42382 -0.01647 0.01043  0.07027  67  CYS B SG  
1843 N N   . LEU B 70  ? 0.33465 0.42368 0.41273 -0.02172 -0.00334 0.05154  68  LEU B N   
1844 C CA  . LEU B 70  ? 0.33675 0.40689 0.40709 -0.01876 -0.00476 0.04376  68  LEU B CA  
1845 C C   . LEU B 70  ? 0.35349 0.41952 0.42426 -0.02325 -0.00956 0.04114  68  LEU B C   
1846 O O   . LEU B 70  ? 0.35040 0.41065 0.41600 -0.01917 -0.01010 0.03565  68  LEU B O   
1847 C CB  . LEU B 70  ? 0.36203 0.41554 0.42843 -0.02047 -0.00508 0.04324  68  LEU B CB  
1848 C CG  . LEU B 70  ? 0.40509 0.44180 0.46380 -0.01623 -0.00526 0.03527  68  LEU B CG  
1849 C CD1 . LEU B 70  ? 0.39621 0.43715 0.45107 -0.00782 -0.00142 0.03182  68  LEU B CD1 
1850 C CD2 . LEU B 70  ? 0.42643 0.44737 0.48334 -0.01792 -0.00605 0.03498  68  LEU B CD2 
1851 N N   . ASP B 71  ? 0.35344 0.42405 0.43051 -0.03216 -0.01326 0.04549  69  ASP B N   
1852 C CA  . ASP B 71  ? 0.37336 0.44054 0.45006 -0.03769 -0.01865 0.04226  69  ASP B CA  
1853 C C   . ASP B 71  ? 0.36112 0.44533 0.44073 -0.03400 -0.01914 0.04303  69  ASP B C   
1854 O O   . ASP B 71  ? 0.30725 0.38860 0.38276 -0.03411 -0.02250 0.03893  69  ASP B O   
1855 C CB  . ASP B 71  ? 0.40609 0.47321 0.48982 -0.04923 -0.02287 0.04668  69  ASP B CB  
1856 C CG  . ASP B 71  ? 0.46843 0.51182 0.54756 -0.05394 -0.02569 0.04162  69  ASP B CG  
1857 O OD1 . ASP B 71  ? 0.50459 0.53433 0.57473 -0.04951 -0.02558 0.03345  69  ASP B OD1 
1858 O OD2 . ASP B 71  ? 0.49010 0.52870 0.57537 -0.06194 -0.02776 0.04624  69  ASP B OD2 
1859 N N   . MET B 72  ? 0.32067 0.42326 0.40709 -0.02974 -0.01553 0.04826  70  MET B N   
1860 C CA  . MET B 72  ? 0.34233 0.46101 0.43321 -0.02475 -0.01578 0.04941  70  MET B CA  
1861 C C   . MET B 72  ? 0.30850 0.41990 0.39293 -0.01402 -0.01268 0.04446  70  MET B C   
1862 O O   . MET B 72  ? 0.25431 0.36949 0.33895 -0.01055 -0.01469 0.04389  70  MET B O   
1863 C CB  . MET B 72  ? 0.34659 0.48936 0.44859 -0.02377 -0.01288 0.05643  70  MET B CB  
1864 C CG  . MET B 72  ? 0.37568 0.53187 0.48122 -0.01219 -0.00892 0.05612  70  MET B CG  
1865 S SD  . MET B 72  ? 0.29879 0.48383 0.41630 -0.00902 -0.00353 0.06268  70  MET B SD  
1866 C CE  . MET B 72  ? 0.34079 0.54745 0.47134 -0.01827 -0.00927 0.07036  70  MET B CE  
1867 N N   . GLU B 73  ? 0.31976 0.42075 0.39876 -0.00928 -0.00828 0.04142  71  GLU B N   
1868 C CA  . GLU B 73  ? 0.32652 0.41726 0.39920 -0.00112 -0.00606 0.03628  71  GLU B CA  
1869 C C   . GLU B 73  ? 0.33678 0.41303 0.40197 -0.00373 -0.00972 0.03246  71  GLU B C   
1870 O O   . GLU B 73  ? 0.34438 0.41915 0.40736 0.00093  -0.01019 0.03123  71  GLU B O   
1871 C CB  . GLU B 73  ? 0.32996 0.41332 0.39840 0.00276  -0.00144 0.03355  71  GLU B CB  
1872 C CG  . GLU B 73  ? 0.35873 0.42966 0.42094 0.00919  0.00033  0.02806  71  GLU B CG  
1873 C CD  . GLU B 73  ? 0.42406 0.50215 0.49008 0.01764  0.00277  0.02723  71  GLU B CD  
1874 O OE1 . GLU B 73  ? 0.42719 0.52093 0.50094 0.01931  0.00284  0.03086  71  GLU B OE1 
1875 O OE2 . GLU B 73  ? 0.44479 0.51239 0.50687 0.02261  0.00445  0.02301  71  GLU B OE2 
1876 N N   . ILE B 74  ? 0.30799 0.37366 0.36933 -0.01094 -0.01223 0.03069  72  ILE B N   
1877 C CA  . ILE B 74  ? 0.35515 0.40854 0.40849 -0.01300 -0.01511 0.02584  72  ILE B CA  
1878 C C   . ILE B 74  ? 0.33792 0.40130 0.39239 -0.01553 -0.01979 0.02737  72  ILE B C   
1879 O O   . ILE B 74  ? 0.32633 0.38722 0.37519 -0.01253 -0.02068 0.02564  72  ILE B O   
1880 C CB  . ILE B 74  ? 0.36832 0.40795 0.41824 -0.01944 -0.01667 0.02260  72  ILE B CB  
1881 C CG1 . ILE B 74  ? 0.34126 0.37025 0.38850 -0.01518 -0.01233 0.02094  72  ILE B CG1 
1882 C CG2 . ILE B 74  ? 0.32176 0.35206 0.36367 -0.02240 -0.01997 0.01666  72  ILE B CG2 
1883 C CD1 . ILE B 74  ? 0.34691 0.36389 0.39419 -0.02026 -0.01337 0.02005  72  ILE B CD1 
1884 N N   . ASN B 75  ? 0.31815 0.39492 0.38042 -0.02118 -0.02299 0.03161  73  ASN B N   
1885 C CA  . ASN B 75  ? 0.31243 0.40146 0.37665 -0.02409 -0.02823 0.03364  73  ASN B CA  
1886 C C   . ASN B 75  ? 0.28829 0.38707 0.35507 -0.01486 -0.02666 0.03711  73  ASN B C   
1887 O O   . ASN B 75  ? 0.28759 0.38951 0.35087 -0.01425 -0.03014 0.03766  73  ASN B O   
1888 C CB  . ASN B 75  ? 0.34312 0.44728 0.41754 -0.03189 -0.03166 0.03848  73  ASN B CB  
1889 C CG  . ASN B 75  ? 0.39955 0.49259 0.47212 -0.04257 -0.03495 0.03524  73  ASN B CG  
1890 O OD1 . ASN B 75  ? 0.47943 0.55816 0.54277 -0.04573 -0.03751 0.02846  73  ASN B OD1 
1891 N ND2 . ASN B 75  ? 0.42268 0.52300 0.50463 -0.04841 -0.03501 0.04027  73  ASN B ND2 
1892 N N   . ARG B 76  ? 0.28284 0.38587 0.35536 -0.00740 -0.02147 0.03935  74  ARG B N   
1893 C CA  . ARG B 76  ? 0.29600 0.40645 0.37275 0.00215  -0.01974 0.04226  74  ARG B CA  
1894 C C   . ARG B 76  ? 0.31373 0.40910 0.38164 0.00689  -0.01870 0.03926  74  ARG B C   
1895 O O   . ARG B 76  ? 0.29582 0.39526 0.36472 0.01120  -0.02052 0.04263  74  ARG B O   
1896 C CB  . ARG B 76  ? 0.33454 0.45227 0.41894 0.00896  -0.01405 0.04339  74  ARG B CB  
1897 C CG  . ARG B 76  ? 0.41835 0.53553 0.50555 0.02038  -0.01080 0.04344  74  ARG B CG  
1898 C CD  . ARG B 76  ? 0.42050 0.53942 0.51129 0.02724  -0.00441 0.04084  74  ARG B CD  
1899 N NE  . ARG B 76  ? 0.46240 0.56373 0.54450 0.02809  -0.00121 0.03488  74  ARG B NE  
1900 C CZ  . ARG B 76  ? 0.48700 0.57500 0.56536 0.03362  0.00017  0.03168  74  ARG B CZ  
1901 N NH1 . ARG B 76  ? 0.53470 0.62300 0.61684 0.03910  -0.00126 0.03438  74  ARG B NH1 
1902 N NH2 . ARG B 76  ? 0.54428 0.61890 0.61579 0.03343  0.00279  0.02644  74  ARG B NH2 
1903 N N   . LEU B 77  ? 0.31273 0.39171 0.37283 0.00612  -0.01585 0.03395  75  LEU B N   
1904 C CA  . LEU B 77  ? 0.31119 0.37718 0.36332 0.00919  -0.01482 0.03150  75  LEU B CA  
1905 C C   . LEU B 77  ? 0.32065 0.38616 0.36536 0.00402  -0.01953 0.03133  75  LEU B C   
1906 O O   . LEU B 77  ? 0.32644 0.39034 0.36745 0.00712  -0.02009 0.03339  75  LEU B O   
1907 C CB  . LEU B 77  ? 0.33405 0.38548 0.38074 0.00909  -0.01092 0.02609  75  LEU B CB  
1908 C CG  . LEU B 77  ? 0.33553 0.38625 0.38666 0.01462  -0.00613 0.02508  75  LEU B CG  
1909 C CD1 . LEU B 77  ? 0.36459 0.40403 0.41044 0.01232  -0.00391 0.02068  75  LEU B CD1 
1910 C CD2 . LEU B 77  ? 0.33357 0.38173 0.38695 0.02251  -0.00379 0.02547  75  LEU B CD2 
1911 N N   . LYS B 78  ? 0.29182 0.35831 0.33386 -0.00417 -0.02295 0.02872  76  LYS B N   
1912 C CA  . LYS B 78  ? 0.30788 0.37560 0.34196 -0.00944 -0.02777 0.02708  76  LYS B CA  
1913 C C   . LYS B 78  ? 0.33399 0.41810 0.37206 -0.00812 -0.03207 0.03384  76  LYS B C   
1914 O O   . LYS B 78  ? 0.32161 0.40768 0.35247 -0.00826 -0.03466 0.03500  76  LYS B O   
1915 C CB  . LYS B 78  ? 0.33614 0.40164 0.36832 -0.01880 -0.03121 0.02224  76  LYS B CB  
1916 C CG  . LYS B 78  ? 0.32103 0.36911 0.34791 -0.02035 -0.02808 0.01540  76  LYS B CG  
1917 C CD  . LYS B 78  ? 0.34344 0.38765 0.36780 -0.02966 -0.03257 0.01010  76  LYS B CD  
1918 C CE  . LYS B 78  ? 0.37457 0.40101 0.39552 -0.03030 -0.02962 0.00389  76  LYS B CE  
1919 N NZ  . LYS B 78  ? 0.41855 0.43843 0.43835 -0.03909 -0.03403 -0.00172 76  LYS B NZ  
1920 N N   . GLN B 79  ? 0.34238 0.44026 0.39221 -0.00674 -0.03293 0.03898  77  GLN B N   
1921 C CA  . GLN B 79  ? 0.34731 0.46281 0.40257 -0.00538 -0.03759 0.04600  77  GLN B CA  
1922 C C   . GLN B 79  ? 0.34149 0.45579 0.39873 0.00477  -0.03510 0.05123  77  GLN B C   
1923 O O   . GLN B 79  ? 0.34690 0.46892 0.40251 0.00609  -0.03899 0.05664  77  GLN B O   
1924 C CB  . GLN B 79  ? 0.33873 0.47178 0.40742 -0.00703 -0.03917 0.05020  77  GLN B CB  
1925 C CG  . GLN B 79  ? 0.37473 0.52723 0.45344 -0.00119 -0.04197 0.05895  77  GLN B CG  
1926 C CD  . GLN B 79  ? 0.49140 0.65961 0.58574 0.00296  -0.03950 0.06328  77  GLN B CD  
1927 O OE1 . GLN B 79  ? 0.48950 0.65524 0.58954 0.01294  -0.03375 0.06417  77  GLN B OE1 
1928 N NE2 . GLN B 79  ? 0.45729 0.64344 0.55907 -0.00459 -0.04404 0.06605  77  GLN B NE2 
1929 N N   . SER B 80  ? 0.28691 0.39107 0.34741 0.01160  -0.02894 0.04975  78  SER B N   
1930 C CA  . SER B 80  ? 0.32002 0.41925 0.38291 0.02073  -0.02651 0.05378  78  SER B CA  
1931 C C   . SER B 80  ? 0.35003 0.43960 0.40149 0.01914  -0.02757 0.05415  78  SER B C   
1932 O O   . SER B 80  ? 0.33342 0.42688 0.38604 0.02313  -0.02966 0.06139  78  SER B O   
1933 C CB  . SER B 80  ? 0.37416 0.46257 0.44080 0.02657  -0.01998 0.04965  78  SER B CB  
1934 O OG  . SER B 80  ? 0.43900 0.52141 0.50961 0.03512  -0.01792 0.05289  78  SER B OG  
1935 N N   . LEU B 81  ? 0.33065 0.40876 0.37152 0.01355  -0.02605 0.04710  79  LEU B N   
1936 C CA  . LEU B 81  ? 0.34525 0.41546 0.37520 0.01230  -0.02576 0.04689  79  LEU B CA  
1937 C C   . LEU B 81  ? 0.33212 0.41382 0.35449 0.00701  -0.03165 0.04944  79  LEU B C   
1938 O O   . LEU B 81  ? 0.34670 0.43114 0.36476 0.00875  -0.03296 0.05553  79  LEU B O   
1939 C CB  . LEU B 81  ? 0.33251 0.38851 0.35475 0.00912  -0.02178 0.03824  79  LEU B CB  
1940 C CG  . LEU B 81  ? 0.32207 0.37101 0.33340 0.00788  -0.02019 0.03712  79  LEU B CG  
1941 C CD1 . LEU B 81  ? 0.31289 0.35858 0.32717 0.01350  -0.01825 0.04439  79  LEU B CD1 
1942 C CD2 . LEU B 81  ? 0.32597 0.36259 0.33242 0.00587  -0.01601 0.02854  79  LEU B CD2 
1943 N N   . SER B 82  ? 0.31010 0.39876 0.33058 -0.00003 -0.03545 0.04496  80  SER B N   
1944 C CA  . SER B 82  ? 0.38701 0.48923 0.40103 -0.00590 -0.04216 0.04639  80  SER B CA  
1945 C C   . SER B 82  ? 0.38005 0.49749 0.39998 -0.00129 -0.04604 0.05798  80  SER B C   
1946 O O   . SER B 82  ? 0.35834 0.48379 0.36993 -0.00290 -0.04979 0.06217  80  SER B O   
1947 C CB  . SER B 82  ? 0.38038 0.48949 0.39763 -0.01350 -0.04626 0.04165  80  SER B CB  
1948 O OG  . SER B 82  ? 0.45253 0.54732 0.46370 -0.01838 -0.04382 0.03148  80  SER B OG  
1949 N N   . ASN B 83  ? 0.38645 0.51008 0.42104 0.00446  -0.04551 0.06345  81  ASN B N   
1950 C CA  . ASN B 83  ? 0.40236 0.54059 0.44525 0.01029  -0.04915 0.07500  81  ASN B CA  
1951 C C   . ASN B 83  ? 0.39781 0.52691 0.43898 0.01738  -0.04645 0.08169  81  ASN B C   
1952 O O   . ASN B 83  ? 0.37488 0.51424 0.41518 0.01918  -0.05071 0.09138  81  ASN B O   
1953 C CB  . ASN B 83  ? 0.40005 0.54700 0.46006 0.01599  -0.04815 0.07822  81  ASN B CB  
1954 C CG  . ASN B 83  ? 0.45624 0.61187 0.52735 0.02608  -0.04938 0.08986  81  ASN B CG  
1955 O OD1 . ASN B 83  ? 0.47388 0.61706 0.55029 0.03475  -0.04437 0.09156  81  ASN B OD1 
1956 N ND2 . ASN B 83  ? 0.47919 0.65550 0.55380 0.02492  -0.05643 0.09792  81  ASN B ND2 
1957 N N   . LEU B 84  ? 0.38487 0.49550 0.42652 0.02124  -0.03977 0.07758  82  LEU B N   
1958 C CA  . LEU B 84  ? 0.41727 0.51764 0.45856 0.02684  -0.03719 0.08387  82  LEU B CA  
1959 C C   . LEU B 84  ? 0.40445 0.50619 0.43105 0.02145  -0.03913 0.08622  82  LEU B C   
1960 O O   . LEU B 84  ? 0.44750 0.55411 0.47397 0.02423  -0.04147 0.09717  82  LEU B O   
1961 C CB  . LEU B 84  ? 0.39845 0.47949 0.44222 0.03006  -0.03017 0.07725  82  LEU B CB  
1962 C CG  . LEU B 84  ? 0.38572 0.45524 0.43387 0.03648  -0.02767 0.08406  82  LEU B CG  
1963 C CD1 . LEU B 84  ? 0.40985 0.48450 0.47301 0.04560  -0.02918 0.09206  82  LEU B CD1 
1964 C CD2 . LEU B 84  ? 0.36930 0.42072 0.41709 0.03708  -0.02154 0.07602  82  LEU B CD2 
1965 N N   . LEU B 85  ? 0.37430 0.47257 0.38854 0.01403  -0.03810 0.07638  83  LEU B N   
1966 C CA  . LEU B 85  ? 0.43498 0.53665 0.43422 0.00918  -0.03926 0.07721  83  LEU B CA  
1967 C C   . LEU B 85  ? 0.43756 0.55985 0.43217 0.00593  -0.04690 0.08357  83  LEU B C   
1968 O O   . LEU B 85  ? 0.43274 0.56234 0.41807 0.00473  -0.04872 0.09039  83  LEU B O   
1969 C CB  . LEU B 85  ? 0.36323 0.45667 0.35141 0.00308  -0.03620 0.06382  83  LEU B CB  
1970 C CG  . LEU B 85  ? 0.36269 0.43793 0.35516 0.00570  -0.02928 0.05733  83  LEU B CG  
1971 C CD1 . LEU B 85  ? 0.36406 0.43208 0.34646 0.00060  -0.02654 0.04519  83  LEU B CD1 
1972 C CD2 . LEU B 85  ? 0.38112 0.44778 0.37688 0.01069  -0.02530 0.06459  83  LEU B CD2 
1973 N N   . GLY B 86  ? 0.39483 0.52840 0.39597 0.00408  -0.05162 0.08211  84  GLY B N   
1974 C CA  . GLY B 86  ? 0.44605 0.60112 0.44374 0.00021  -0.05975 0.08759  84  GLY B CA  
1975 C C   . GLY B 86  ? 0.40760 0.57461 0.41478 0.00726  -0.06331 0.10372  84  GLY B C   
1976 O O   . GLY B 86  ? 0.44648 0.63267 0.44915 0.00454  -0.07028 0.11066  84  GLY B O   
1977 N N   . GLN B 87  ? 0.41814 0.57437 0.43862 0.01641  -0.05900 0.10966  85  GLN B N   
1978 C CA  . GLN B 87  ? 0.43471 0.59907 0.46558 0.02438  -0.06197 0.12533  85  GLN B CA  
1979 C C   . GLN B 87  ? 0.44646 0.60827 0.46767 0.02453  -0.06180 0.13478  85  GLN B C   
1980 O O   . GLN B 87  ? 0.41723 0.59074 0.44257 0.02852  -0.06645 0.14946  85  GLN B O   
1981 C CB  . GLN B 87  ? 0.49731 0.64907 0.54600 0.03447  -0.05710 0.12674  85  GLN B CB  
1982 C CG  . GLN B 87  ? 0.51485 0.68158 0.57908 0.03873  -0.06015 0.12861  85  GLN B CG  
1983 C CD  . GLN B 87  ? 0.62733 0.78514 0.70947 0.05104  -0.05602 0.13285  85  GLN B CD  
1984 O OE1 . GLN B 87  ? 0.68719 0.85610 0.78197 0.05901  -0.05944 0.14441  85  GLN B OE1 
1985 N NE2 . GLN B 87  ? 0.61579 0.75377 0.69923 0.05298  -0.04872 0.12302  85  GLN B NE2 
1986 N N   . CYS B 88  ? 0.47109 0.61944 0.47995 0.02016  -0.05660 0.12749  86  CYS B N   
1987 C CA  . CYS B 88  ? 0.46655 0.61418 0.46579 0.01926  -0.05571 0.13653  86  CYS B CA  
1988 C C   . CYS B 88  ? 0.49228 0.66309 0.47778 0.01342  -0.06256 0.14187  86  CYS B C   
1989 O O   . CYS B 88  ? 0.46386 0.64743 0.44295 0.00757  -0.06696 0.13351  86  CYS B O   
1990 C CB  . CYS B 88  ? 0.46260 0.59382 0.45214 0.01546  -0.04837 0.12631  86  CYS B CB  
1991 S SG  . CYS B 88  ? 0.48100 0.58607 0.48513 0.02150  -0.04076 0.12019  86  CYS B SG  
1992 N N   . GLY B 89  ? 0.50838 0.68488 0.48930 0.01456  -0.06370 0.15624  87  GLY B N   
1993 C CA  . GLY B 89  ? 0.52381 0.72365 0.48964 0.00895  -0.06990 0.16211  87  GLY B CA  
1994 C C   . GLY B 89  ? 0.57249 0.77452 0.51743 0.00006  -0.06732 0.14761  87  GLY B C   
1995 O O   . GLY B 89  ? 0.54776 0.73267 0.48944 -0.00107 -0.05986 0.13700  87  GLY B O   
1996 N N   . LYS B 90  ? 0.60033 0.82475 0.53116 -0.00610 -0.07386 0.14676  88  LYS B N   
1997 C CA  . LYS B 90  ? 0.63891 0.86765 0.54852 -0.01407 -0.07192 0.13275  88  LYS B CA  
1998 C C   . LYS B 90  ? 0.64040 0.86357 0.54068 -0.01371 -0.06472 0.13760  88  LYS B C   
1999 O O   . LYS B 90  ? 0.55273 0.78538 0.45213 -0.01166 -0.06601 0.15550  88  LYS B O   
2000 C CB  . LYS B 90  ? 0.64563 0.90161 0.54115 -0.02049 -0.08095 0.13306  88  LYS B CB  
2001 N N   . ASP B 91  ? 0.63090 0.83907 0.52563 -0.01561 -0.05713 0.12269  89  ASP B N   
2002 C CA  . ASP B 91  ? 0.61723 0.82209 0.50284 -0.01618 -0.04964 0.12492  89  ASP B CA  
2003 C C   . ASP B 91  ? 0.57171 0.76480 0.47186 -0.01056 -0.04609 0.14167  89  ASP B C   
2004 O O   . ASP B 91  ? 0.52705 0.72348 0.42099 -0.01156 -0.04198 0.15078  89  ASP B O   
2005 C CB  . ASP B 91  ? 0.66753 0.89698 0.53178 -0.02131 -0.05199 0.12871  89  ASP B CB  
2006 C CG  . ASP B 91  ? 0.72546 0.96513 0.57374 -0.02745 -0.05521 0.10986  89  ASP B CG  
2007 O OD1 . ASP B 91  ? 0.76904 0.99352 0.62208 -0.02804 -0.05364 0.09312  89  ASP B OD1 
2008 O OD2 . ASP B 91  ? 0.77835 1.04118 0.60948 -0.03189 -0.05966 0.11199  89  ASP B OD2 
2009 N N   . ASP B 92  ? 0.59135 0.77093 0.51113 -0.00481 -0.04752 0.14597  90  ASP B N   
2010 C CA  . ASP B 92  ? 0.53911 0.70187 0.47365 0.00040  -0.04331 0.15737  90  ASP B CA  
2011 C C   . ASP B 92  ? 0.48426 0.62595 0.42327 0.00057  -0.03573 0.14267  90  ASP B C   
2012 O O   . ASP B 92  ? 0.43980 0.56658 0.39257 0.00456  -0.03500 0.13679  90  ASP B O   
2013 C CB  . ASP B 92  ? 0.50124 0.66048 0.45439 0.00744  -0.04831 0.16897  90  ASP B CB  
2014 C CG  . ASP B 92  ? 0.51676 0.65825 0.48455 0.01265  -0.04471 0.18140  90  ASP B CG  
2015 O OD1 . ASP B 92  ? 0.47981 0.60908 0.44548 0.01027  -0.03798 0.17867  90  ASP B OD1 
2016 O OD2 . ASP B 92  ? 0.57330 0.71295 0.55565 0.01917  -0.04874 0.19377  90  ASP B OD2 
2017 N N   . HIS B 93  ? 0.41705 0.55948 0.34405 -0.00366 -0.02990 0.13715  91  HIS B N   
2018 C CA  . HIS B 93  ? 0.49819 0.62480 0.42712 -0.00408 -0.02331 0.12179  91  HIS B CA  
2019 C C   . HIS B 93  ? 0.44235 0.54879 0.38822 -0.00007 -0.01953 0.12647  91  HIS B C   
2020 O O   . HIS B 93  ? 0.38808 0.48021 0.34109 0.00149  -0.01674 0.11475  91  HIS B O   
2021 C CB  . HIS B 93  ? 0.51701 0.65200 0.42975 -0.00873 -0.01789 0.11534  91  HIS B CB  
2022 C CG  . HIS B 93  ? 0.54445 0.69808 0.43944 -0.01271 -0.02145 0.10786  91  HIS B CG  
2023 N ND1 . HIS B 93  ? 0.55778 0.73176 0.43735 -0.01607 -0.02191 0.11548  91  HIS B ND1 
2024 C CD2 . HIS B 93  ? 0.53783 0.69315 0.42807 -0.01436 -0.02517 0.09352  91  HIS B CD2 
2025 C CE1 . HIS B 93  ? 0.58998 0.77739 0.45523 -0.01943 -0.02586 0.10482  91  HIS B CE1 
2026 N NE2 . HIS B 93  ? 0.56326 0.73874 0.43522 -0.01874 -0.02800 0.09133  91  HIS B NE2 
2027 N N   . THR B 94  ? 0.40382 0.50865 0.35647 0.00141  -0.01980 0.14351  92  THR B N   
2028 C CA  . THR B 94  ? 0.41714 0.50131 0.38673 0.00501  -0.01712 0.14719  92  THR B CA  
2029 C C   . THR B 94  ? 0.42928 0.50316 0.41230 0.01100  -0.02033 0.14231  92  THR B C   
2030 O O   . THR B 94  ? 0.38490 0.44238 0.37732 0.01317  -0.01711 0.13349  92  THR B O   
2031 C CB  . THR B 94  ? 0.44247 0.52600 0.41789 0.00538  -0.01791 0.16745  92  THR B CB  
2032 O OG1 . THR B 94  ? 0.55697 0.65035 0.52094 -0.00063 -0.01370 0.17205  92  THR B OG1 
2033 C CG2 . THR B 94  ? 0.45372 0.51381 0.44750 0.00904  -0.01594 0.17002  92  THR B CG2 
2034 N N   . SER B 95  ? 0.37721 0.46250 0.36151 0.01378  -0.02670 0.14844  93  SER B N   
2035 C CA  . SER B 95  ? 0.41148 0.49041 0.40927 0.01988  -0.02941 0.14474  93  SER B CA  
2036 C C   . SER B 95  ? 0.39168 0.46819 0.38662 0.01816  -0.02770 0.12641  93  SER B C   
2037 O O   . SER B 95  ? 0.37209 0.43737 0.37846 0.02240  -0.02644 0.12008  93  SER B O   
2038 C CB  . SER B 95  ? 0.42815 0.52343 0.42834 0.02293  -0.03682 0.15590  93  SER B CB  
2039 N N   . ILE B 96  ? 0.38357 0.47028 0.36343 0.01212  -0.02751 0.11772  94  ILE B N   
2040 C CA  . ILE B 96  ? 0.38503 0.46751 0.36277 0.01017  -0.02590 0.10116  94  ILE B CA  
2041 C C   . ILE B 96  ? 0.42201 0.48692 0.40414 0.01079  -0.01926 0.09344  94  ILE B C   
2042 O O   . ILE B 96  ? 0.32306 0.37879 0.31242 0.01272  -0.01791 0.08453  94  ILE B O   
2043 C CB  . ILE B 96  ? 0.38436 0.47998 0.34518 0.00380  -0.02737 0.09318  94  ILE B CB  
2044 C CG1 . ILE B 96  ? 0.44311 0.55720 0.40044 0.00256  -0.03507 0.09924  94  ILE B CG1 
2045 C CG2 . ILE B 96  ? 0.41174 0.49951 0.37152 0.00179  -0.02525 0.07679  94  ILE B CG2 
2046 C CD1 . ILE B 96  ? 0.49502 0.62322 0.43407 -0.00414 -0.03713 0.09198  94  ILE B CD1 
2047 N N   . LEU B 97  ? 0.39225 0.45411 0.37010 0.00876  -0.01514 0.09726  95  LEU B N   
2048 C CA  . LEU B 97  ? 0.38066 0.42814 0.36292 0.00866  -0.00927 0.09054  95  LEU B CA  
2049 C C   . LEU B 97  ? 0.34917 0.38183 0.34724 0.01360  -0.00890 0.09354  95  LEU B C   
2050 O O   . LEU B 97  ? 0.31621 0.33772 0.31969 0.01455  -0.00589 0.08436  95  LEU B O   
2051 C CB  . LEU B 97  ? 0.36508 0.41563 0.34053 0.00493  -0.00520 0.09579  95  LEU B CB  
2052 C CG  . LEU B 97  ? 0.38462 0.42275 0.36587 0.00418  0.00042  0.09107  95  LEU B CG  
2053 C CD1 . LEU B 97  ? 0.39107 0.43103 0.36477 0.00239  0.00356  0.07657  95  LEU B CD1 
2054 C CD2 . LEU B 97  ? 0.41221 0.45311 0.39256 0.00102  0.00327  0.10250  95  LEU B CD2 
2055 N N   . LYS B 98  ? 0.33188 0.36438 0.33742 0.01705  -0.01200 0.10628  96  LYS B N   
2056 C CA  . LYS B 98  ? 0.34805 0.36565 0.36888 0.02262  -0.01171 0.10824  96  LYS B CA  
2057 C C   . LYS B 98  ? 0.33156 0.34901 0.35868 0.02719  -0.01335 0.09982  96  LYS B C   
2058 O O   . LYS B 98  ? 0.33968 0.34482 0.37566 0.03051  -0.01101 0.09330  96  LYS B O   
2059 C CB  . LYS B 98  ? 0.37179 0.38877 0.39949 0.02564  -0.01464 0.12482  96  LYS B CB  
2060 C CG  . LYS B 98  ? 0.37579 0.37462 0.41948 0.03131  -0.01400 0.12779  96  LYS B CG  
2061 C CD  . LYS B 98  ? 0.42891 0.43043 0.47992 0.03602  -0.01845 0.14452  96  LYS B CD  
2062 C CE  . LYS B 98  ? 0.49771 0.47933 0.56551 0.04247  -0.01801 0.14766  96  LYS B CE  
2063 N NZ  . LYS B 98  ? 0.54317 0.50783 0.61341 0.03942  -0.01323 0.13679  96  LYS B NZ  
2064 N N   . SER B 99  ? 0.31579 0.34804 0.33777 0.02660  -0.01722 0.09927  97  SER B N   
2065 C CA  . SER B 99  ? 0.35793 0.39322 0.38534 0.02943  -0.01862 0.09167  97  SER B CA  
2066 C C   . SER B 99  ? 0.35843 0.38697 0.38275 0.02662  -0.01476 0.07772  97  SER B C   
2067 O O   . SER B 99  ? 0.32592 0.34978 0.35803 0.02998  -0.01352 0.07174  97  SER B O   
2068 C CB  . SER B 99  ? 0.37382 0.42766 0.39541 0.02712  -0.02403 0.09410  97  SER B CB  
2069 O OG  . SER B 99  ? 0.45318 0.51455 0.48315 0.03234  -0.02831 0.10623  97  SER B OG  
2070 N N   . PHE B 100 ? 0.33484 0.36433 0.34769 0.02079  -0.01283 0.07268  98  PHE B N   
2071 C CA  . PHE B 100 ? 0.31585 0.33942 0.32590 0.01839  -0.00950 0.06055  98  PHE B CA  
2072 C C   . PHE B 100 ? 0.33209 0.34166 0.34966 0.02082  -0.00536 0.05772  98  PHE B C   
2073 O O   . PHE B 100 ? 0.31310 0.31788 0.33420 0.02183  -0.00370 0.04967  98  PHE B O   
2074 C CB  . PHE B 100 ? 0.33273 0.36074 0.32970 0.01289  -0.00816 0.05661  98  PHE B CB  
2075 C CG  . PHE B 100 ? 0.34114 0.36468 0.33488 0.01070  -0.00564 0.04470  98  PHE B CG  
2076 C CD1 . PHE B 100 ? 0.30197 0.32949 0.29401 0.00894  -0.00829 0.03841  98  PHE B CD1 
2077 C CD2 . PHE B 100 ? 0.31727 0.33291 0.31071 0.01020  -0.00089 0.04054  98  PHE B CD2 
2078 C CE1 . PHE B 100 ? 0.31084 0.33281 0.30083 0.00714  -0.00617 0.02874  98  PHE B CE1 
2079 C CE2 . PHE B 100 ? 0.31699 0.32894 0.30827 0.00895  0.00117  0.03068  98  PHE B CE2 
2080 C CZ  . PHE B 100 ? 0.30235 0.31650 0.29203 0.00768  -0.00144 0.02507  98  PHE B CZ  
2081 N N   . TYR B 101 ? 0.30782 0.31139 0.32791 0.02121  -0.00399 0.06468  99  TYR B N   
2082 C CA  . TYR B 101 ? 0.32313 0.31313 0.35116 0.02279  -0.00094 0.06238  99  TYR B CA  
2083 C C   . TYR B 101 ? 0.35969 0.34417 0.39849 0.02895  -0.00187 0.06069  99  TYR B C   
2084 O O   . TYR B 101 ? 0.32973 0.30803 0.37203 0.03020  0.00026  0.05211  99  TYR B O   
2085 C CB  . TYR B 101 ? 0.30920 0.29426 0.33899 0.02117  -0.00014 0.07208  99  TYR B CB  
2086 C CG  . TYR B 101 ? 0.37685 0.34672 0.41677 0.02255  0.00172  0.07098  99  TYR B CG  
2087 C CD1 . TYR B 101 ? 0.36822 0.33258 0.40773 0.01898  0.00501  0.06349  99  TYR B CD1 
2088 C CD2 . TYR B 101 ? 0.37768 0.33868 0.42808 0.02743  -0.00006 0.07715  99  TYR B CD2 
2089 C CE1 . TYR B 101 ? 0.40497 0.35601 0.45338 0.01928  0.00605  0.06145  99  TYR B CE1 
2090 C CE2 . TYR B 101 ? 0.39901 0.34452 0.45848 0.02827  0.00137  0.07446  99  TYR B CE2 
2091 C CZ  . TYR B 101 ? 0.40731 0.34819 0.46532 0.02368  0.00421  0.06641  99  TYR B CZ  
2092 O OH  . TYR B 101 ? 0.50161 0.42757 0.56839 0.02362  0.00498  0.06286  99  TYR B OH  
2093 N N   . GLN B 102 ? 0.35744 0.34518 0.40172 0.03328  -0.00493 0.06911  100 GLN B N   
2094 C CA  . GLN B 102 ? 0.38249 0.36568 0.43814 0.04048  -0.00528 0.06783  100 GLN B CA  
2095 C C   . GLN B 102 ? 0.38666 0.37742 0.44219 0.04167  -0.00493 0.05893  100 GLN B C   
2096 O O   . GLN B 102 ? 0.40364 0.38967 0.46631 0.04635  -0.00308 0.05314  100 GLN B O   
2097 C CB  . GLN B 102 ? 0.36608 0.35368 0.42827 0.04552  -0.00891 0.07969  100 GLN B CB  
2098 C CG  . GLN B 102 ? 0.47778 0.45729 0.55372 0.05435  -0.00851 0.07935  100 GLN B CG  
2099 C CD  . GLN B 102 ? 0.49802 0.45785 0.57943 0.05501  -0.00576 0.07673  100 GLN B CD  
2100 O OE1 . GLN B 102 ? 0.53677 0.48958 0.61569 0.05030  -0.00565 0.08270  100 GLN B OE1 
2101 N NE2 . GLN B 102 ? 0.53553 0.48727 0.62444 0.06044  -0.00354 0.06766  100 GLN B NE2 
2102 N N   . TRP B 103 ? 0.33045 0.33312 0.37800 0.03727  -0.00667 0.05772  101 TRP B N   
2103 C CA  . TRP B 103 ? 0.35365 0.36332 0.40168 0.03711  -0.00653 0.05057  101 TRP B CA  
2104 C C   . TRP B 103 ? 0.35835 0.35948 0.40540 0.03594  -0.00261 0.04104  101 TRP B C   
2105 O O   . TRP B 103 ? 0.33045 0.33361 0.38209 0.03867  -0.00130 0.03608  101 TRP B O   
2106 C CB  . TRP B 103 ? 0.32609 0.34737 0.36560 0.03127  -0.00954 0.05063  101 TRP B CB  
2107 C CG  . TRP B 103 ? 0.33948 0.36848 0.38024 0.02962  -0.01016 0.04498  101 TRP B CG  
2108 C CD1 . TRP B 103 ? 0.31776 0.35968 0.36454 0.03108  -0.01316 0.04795  101 TRP B CD1 
2109 C CD2 . TRP B 103 ? 0.31300 0.33831 0.34955 0.02564  -0.00802 0.03684  101 TRP B CD2 
2110 N NE1 . TRP B 103 ? 0.32326 0.36922 0.36988 0.02757  -0.01277 0.04223  101 TRP B NE1 
2111 C CE2 . TRP B 103 ? 0.32708 0.36225 0.36733 0.02440  -0.00975 0.03566  101 TRP B CE2 
2112 C CE3 . TRP B 103 ? 0.32934 0.34480 0.36035 0.02310  -0.00495 0.03128  101 TRP B CE3 
2113 C CZ2 . TRP B 103 ? 0.31410 0.34791 0.35238 0.02050  -0.00857 0.02975  101 TRP B CZ2 
2114 C CZ3 . TRP B 103 ? 0.33275 0.34729 0.36205 0.02020  -0.00386 0.02512  101 TRP B CZ3 
2115 C CH2 . TRP B 103 ? 0.37449 0.39741 0.40725 0.01882  -0.00572 0.02472  101 TRP B CH2 
2116 N N   . HIS B 104 ? 0.30875 0.30218 0.35005 0.03195  -0.00069 0.03896  102 HIS B N   
2117 C CA  . HIS B 104 ? 0.32414 0.31076 0.36495 0.03080  0.00245  0.03088  102 HIS B CA  
2118 C C   . HIS B 104 ? 0.33159 0.30873 0.38019 0.03519  0.00419  0.02877  102 HIS B C   
2119 O O   . HIS B 104 ? 0.35790 0.33423 0.40858 0.03688  0.00588  0.02185  102 HIS B O   
2120 C CB  . HIS B 104 ? 0.31522 0.29872 0.34885 0.02557  0.00390  0.02973  102 HIS B CB  
2121 C CG  . HIS B 104 ? 0.29493 0.28554 0.32060 0.02167  0.00306  0.02754  102 HIS B CG  
2122 N ND1 . HIS B 104 ? 0.31093 0.30842 0.33085 0.01953  0.00075  0.03198  102 HIS B ND1 
2123 C CD2 . HIS B 104 ? 0.31229 0.30355 0.33490 0.01954  0.00398  0.02119  102 HIS B CD2 
2124 C CE1 . HIS B 104 ? 0.29848 0.29959 0.31203 0.01616  0.00033  0.02705  102 HIS B CE1 
2125 N NE2 . HIS B 104 ? 0.30116 0.29779 0.31686 0.01630  0.00231  0.02096  102 HIS B NE2 
2126 N N   . VAL B 105 ? 0.35001 0.31967 0.40284 0.03684  0.00369  0.03455  103 VAL B N   
2127 C CA  . VAL B 105 ? 0.37895 0.33728 0.44002 0.04110  0.00494  0.03162  103 VAL B CA  
2128 C C   . VAL B 105 ? 0.43041 0.39321 0.49769 0.04816  0.00516  0.02809  103 VAL B C   
2129 O O   . VAL B 105 ? 0.40853 0.36679 0.47891 0.05099  0.00722  0.01994  103 VAL B O   
2130 C CB  . VAL B 105 ? 0.40804 0.35683 0.47412 0.04179  0.00379  0.04034  103 VAL B CB  
2131 C CG1 . VAL B 105 ? 0.41312 0.34852 0.48913 0.04714  0.00454  0.03677  103 VAL B CG1 
2132 C CG2 . VAL B 105 ? 0.39188 0.33719 0.45273 0.03447  0.00458  0.04315  103 VAL B CG2 
2133 N N   . ASP B 106 ? 0.38064 0.35426 0.44969 0.05095  0.00307  0.03394  104 ASP B N   
2134 C CA  . ASP B 106 ? 0.38409 0.36452 0.46072 0.05823  0.00356  0.03189  104 ASP B CA  
2135 C C   . ASP B 106 ? 0.39190 0.38095 0.46511 0.05674  0.00562  0.02383  104 ASP B C   
2136 O O   . ASP B 106 ? 0.41902 0.41012 0.49710 0.06212  0.00798  0.01805  104 ASP B O   
2137 C CB  . ASP B 106 ? 0.40006 0.39261 0.48021 0.06076  0.00025  0.04128  104 ASP B CB  
2138 C CG  . ASP B 106 ? 0.50092 0.48594 0.58879 0.06602  -0.00156 0.05006  104 ASP B CG  
2139 O OD1 . ASP B 106 ? 0.55975 0.52906 0.65265 0.06913  0.00016  0.04769  104 ASP B OD1 
2140 O OD2 . ASP B 106 ? 0.52354 0.51809 0.61248 0.06655  -0.00513 0.05982  104 ASP B OD2 
2141 N N   . LEU B 107 ? 0.36201 0.35627 0.42693 0.04968  0.00488  0.02348  105 LEU B N   
2142 C CA  . LEU B 107 ? 0.36723 0.36872 0.42916 0.04755  0.00648  0.01760  105 LEU B CA  
2143 C C   . LEU B 107 ? 0.43846 0.43180 0.49912 0.04792  0.00937  0.00959  105 LEU B C   
2144 O O   . LEU B 107 ? 0.44075 0.44005 0.50254 0.05029  0.01145  0.00438  105 LEU B O   
2145 C CB  . LEU B 107 ? 0.36211 0.36773 0.41632 0.04016  0.00469  0.01923  105 LEU B CB  
2146 C CG  . LEU B 107 ? 0.41510 0.42934 0.46694 0.03668  0.00492  0.01670  105 LEU B CG  
2147 C CD1 . LEU B 107 ? 0.37240 0.40052 0.43083 0.03946  0.00404  0.01979  105 LEU B CD1 
2148 C CD2 . LEU B 107 ? 0.35128 0.36451 0.39589 0.02989  0.00286  0.01775  105 LEU B CD2 
2149 N N   . ALA B 108 ? 0.39410 0.37530 0.45263 0.04539  0.00942  0.00880  106 ALA B N   
2150 C CA  . ALA B 108 ? 0.43546 0.40965 0.49292 0.04464  0.01132  0.00114  106 ALA B CA  
2151 C C   . ALA B 108 ? 0.48276 0.45091 0.54684 0.05111  0.01269  -0.00386 106 ALA B C   
2152 O O   . ALA B 108 ? 0.51469 0.48373 0.57781 0.05235  0.01449  -0.01210 106 ALA B O   
2153 C CB  . ALA B 108 ? 0.41337 0.37829 0.46774 0.03915  0.01081  0.00234  106 ALA B CB  
2154 N N   . TYR B 109 ? 0.49345 0.45544 0.56424 0.05559  0.01179  0.00079  107 TYR B N   
2155 C CA  . TYR B 109 ? 0.50503 0.45950 0.58317 0.06279  0.01324  -0.00486 107 TYR B CA  
2156 C C   . TYR B 109 ? 0.51717 0.48478 0.59856 0.06981  0.01531  -0.00829 107 TYR B C   
2157 O O   . TYR B 109 ? 0.55317 0.51703 0.63871 0.07601  0.01756  -0.01641 107 TYR B O   
2158 C CB  . TYR B 109 ? 0.51039 0.45266 0.59635 0.06615  0.01156  0.00207  107 TYR B CB  
2159 C CG  . TYR B 109 ? 0.52136 0.44653 0.61372 0.06987  0.01250  -0.00510 107 TYR B CG  
2160 N N   . ARG B 110 ? 0.50733 0.49065 0.58723 0.06881  0.01469  -0.00276 108 ARG B N   
2161 C CA  . ARG B 110 ? 0.51186 0.51066 0.59602 0.07481  0.01684  -0.00458 108 ARG B CA  
2162 C C   . ARG B 110 ? 0.58642 0.59406 0.66428 0.07235  0.01949  -0.01206 108 ARG B C   
2163 O O   . ARG B 110 ? 0.64013 0.64057 0.71526 0.07301  0.02127  -0.02101 108 ARG B O   
2164 C CB  . ARG B 110 ? 0.48949 0.50270 0.57599 0.07378  0.01454  0.00505  108 ARG B CB  
2165 N N   . GLY B 112 ? 0.51215 0.53201 0.58381 0.08235  0.02931  -0.04131 110 GLY B N   
2166 C CA  . GLY B 112 ? 0.60991 0.63185 0.67260 0.07872  0.03036  -0.04980 110 GLY B CA  
2167 C C   . GLY B 112 ? 0.63023 0.64972 0.68587 0.06868  0.02718  -0.04465 110 GLY B C   
2168 O O   . GLY B 112 ? 0.62056 0.65040 0.66914 0.06467  0.02763  -0.04585 110 GLY B O   
2169 N N   . TYR B 113 ? 0.60039 0.60648 0.65824 0.06506  0.02406  -0.03862 111 TYR B N   
2170 C CA  . TYR B 113 ? 0.56581 0.57205 0.61910 0.05703  0.02148  -0.03136 111 TYR B CA  
2171 C C   . TYR B 113 ? 0.59488 0.59885 0.64143 0.05153  0.02063  -0.03592 111 TYR B C   
2172 O O   . TYR B 113 ? 0.60545 0.59698 0.65215 0.04982  0.01947  -0.04046 111 TYR B O   
2173 C CB  . TYR B 113 ? 0.54687 0.54112 0.60375 0.05535  0.01896  -0.02460 111 TYR B CB  
2174 C CG  . TYR B 113 ? 0.54378 0.53838 0.59620 0.04823  0.01680  -0.01805 111 TYR B CG  
2175 C CD1 . TYR B 113 ? 0.50852 0.51240 0.56063 0.04649  0.01588  -0.01110 111 TYR B CD1 
2176 C CD2 . TYR B 113 ? 0.52768 0.51321 0.57686 0.04321  0.01563  -0.01929 111 TYR B CD2 
2177 C CE1 . TYR B 113 ? 0.49862 0.50087 0.54644 0.04035  0.01398  -0.00672 111 TYR B CE1 
2178 C CE2 . TYR B 113 ? 0.49112 0.47695 0.53672 0.03785  0.01424  -0.01430 111 TYR B CE2 
2179 C CZ  . TYR B 113 ? 0.49787 0.49109 0.54240 0.03669  0.01350  -0.00859 111 TYR B CZ  
2180 O OH  . TYR B 113 ? 0.48728 0.47905 0.52801 0.03179  0.01229  -0.00531 111 TYR B OH  
2181 N N   . ASN B 114 ? 0.58626 0.60267 0.62785 0.04829  0.02081  -0.03347 112 ASN B N   
2182 C CA  . ASN B 114 ? 0.54919 0.56625 0.58514 0.04280  0.01932  -0.03435 112 ASN B CA  
2183 C C   . ASN B 114 ? 0.52287 0.54116 0.55789 0.03800  0.01759  -0.02536 112 ASN B C   
2184 O O   . ASN B 114 ? 0.54450 0.56976 0.57589 0.03490  0.01699  -0.02312 112 ASN B O   
2185 C CB  . ASN B 114 ? 0.55904 0.58992 0.58982 0.04376  0.02090  -0.03938 112 ASN B CB  
2186 C CG  . ASN B 114 ? 0.54550 0.59229 0.57541 0.04373  0.02231  -0.03247 112 ASN B CG  
2187 O OD1 . ASN B 114 ? 0.53790 0.58691 0.57253 0.04539  0.02301  -0.02717 112 ASN B OD1 
2188 N ND2 . ASN B 114 ? 0.49898 0.55806 0.52330 0.04155  0.02250  -0.03203 112 ASN B ND2 
2189 N N   . GLY B 115 ? 0.51758 0.52912 0.55582 0.03752  0.01663  -0.02020 113 GLY B N   
2190 C CA  . GLY B 115 ? 0.47732 0.48971 0.51409 0.03323  0.01510  -0.01354 113 GLY B CA  
2191 C C   . GLY B 115 ? 0.46259 0.48253 0.50168 0.03368  0.01506  -0.00810 113 GLY B C   
2192 O O   . GLY B 115 ? 0.45140 0.48149 0.49256 0.03677  0.01671  -0.00856 113 GLY B O   
2193 N N   . THR B 116 ? 0.43246 0.44867 0.47132 0.03033  0.01316  -0.00327 114 THR B N   
2194 C CA  . THR B 116 ? 0.44263 0.46560 0.48417 0.02957  0.01220  0.00163  114 THR B CA  
2195 C C   . THR B 116 ? 0.39537 0.42831 0.43684 0.02684  0.01238  0.00461  114 THR B C   
2196 O O   . THR B 116 ? 0.36998 0.40293 0.40855 0.02506  0.01268  0.00418  114 THR B O   
2197 C CB  . THR B 116 ? 0.43036 0.44668 0.47056 0.02627  0.00975  0.00468  114 THR B CB  
2198 O OG1 . THR B 116 ? 0.37183 0.38472 0.40862 0.02192  0.00886  0.00524  114 THR B OG1 
2199 C CG2 . THR B 116 ? 0.44826 0.45529 0.48787 0.02795  0.00970  0.00335  114 THR B CG2 
2200 N N   . LEU B 117 ? 0.36892 0.41149 0.41447 0.02639  0.01200  0.00861  115 LEU B N   
2201 C CA  . LEU B 117 ? 0.35211 0.40499 0.39900 0.02278  0.01205  0.01313  115 LEU B CA  
2202 C C   . LEU B 117 ? 0.35360 0.39824 0.39821 0.01680  0.00947  0.01593  115 LEU B C   
2203 O O   . LEU B 117 ? 0.33751 0.38533 0.38176 0.01411  0.00962  0.01905  115 LEU B O   
2204 C CB  . LEU B 117 ? 0.39654 0.46206 0.44977 0.02273  0.01179  0.01727  115 LEU B CB  
2205 C CG  . LEU B 117 ? 0.42352 0.50689 0.48056 0.02238  0.01408  0.02107  115 LEU B CG  
2206 C CD1 . LEU B 117 ? 0.41605 0.50471 0.46912 0.02586  0.01769  0.01760  115 LEU B CD1 
2207 C CD2 . LEU B 117 ? 0.46105 0.55722 0.52533 0.02637  0.01506  0.02228  115 LEU B CD2 
2208 N N   . LEU B 118 ? 0.31677 0.35095 0.35985 0.01496  0.00718  0.01495  116 LEU B N   
2209 C CA  . LEU B 118 ? 0.34890 0.37405 0.38990 0.01030  0.00512  0.01589  116 LEU B CA  
2210 C C   . LEU B 118 ? 0.34866 0.36744 0.38658 0.01176  0.00636  0.01380  116 LEU B C   
2211 O O   . LEU B 118 ? 0.36411 0.38034 0.40245 0.00925  0.00556  0.01645  116 LEU B O   
2212 C CB  . LEU B 118 ? 0.32987 0.34695 0.36857 0.00857  0.00287  0.01395  116 LEU B CB  
2213 C CG  . LEU B 118 ? 0.35860 0.38241 0.39983 0.00706  0.00068  0.01597  116 LEU B CG  
2214 C CD1 . LEU B 118 ? 0.38092 0.39691 0.41791 0.00370  -0.00212 0.01388  116 LEU B CD1 
2215 C CD2 . LEU B 118 ? 0.37285 0.40728 0.41969 0.00333  -0.00039 0.02070  116 LEU B CD2 
2216 N N   . THR B 119 ? 0.32864 0.34496 0.36440 0.01563  0.00798  0.00958  117 THR B N   
2217 C CA  . THR B 119 ? 0.37893 0.39207 0.41268 0.01671  0.00878  0.00770  117 THR B CA  
2218 C C   . THR B 119 ? 0.33758 0.36045 0.37176 0.01687  0.00951  0.01029  117 THR B C   
2219 O O   . THR B 119 ? 0.36546 0.38740 0.39928 0.01590  0.00883  0.01257  117 THR B O   
2220 C CB  . THR B 119 ? 0.36939 0.37914 0.40177 0.01968  0.01002  0.00276  117 THR B CB  
2221 O OG1 . THR B 119 ? 0.38386 0.38578 0.41537 0.01908  0.00947  0.00191  117 THR B OG1 
2222 C CG2 . THR B 119 ? 0.33823 0.34738 0.36940 0.02013  0.01035  0.00079  117 THR B CG2 
2223 N N   . LYS B 120 ? 0.36444 0.39788 0.39949 0.01854  0.01102  0.01030  118 LYS B N   
2224 C CA  . LYS B 120 ? 0.32720 0.37290 0.36163 0.01845  0.01211  0.01326  118 LYS B CA  
2225 C C   . LYS B 120 ? 0.34923 0.39623 0.38598 0.01391  0.01050  0.02128  118 LYS B C   
2226 O O   . LYS B 120 ? 0.34605 0.39786 0.38180 0.01300  0.01027  0.02539  118 LYS B O   
2227 C CB  . LYS B 120 ? 0.38457 0.44274 0.42012 0.02133  0.01460  0.01178  118 LYS B CB  
2228 C CG  . LYS B 120 ? 0.40667 0.46307 0.44027 0.02631  0.01630  0.00336  118 LYS B CG  
2229 C CD  . LYS B 120 ? 0.40831 0.47725 0.44366 0.03047  0.01928  0.00110  118 LYS B CD  
2230 C CE  . LYS B 120 ? 0.47561 0.53854 0.51039 0.03567  0.02058  -0.00792 118 LYS B CE  
2231 N NZ  . LYS B 120 ? 0.50201 0.57549 0.53956 0.04132  0.02383  -0.01137 118 LYS B NZ  
2232 N N   . ALA B 121 ? 0.31509 0.35801 0.35526 0.01069  0.00899  0.02397  119 ALA B N   
2233 C CA  . ALA B 121 ? 0.36983 0.41225 0.41337 0.00549  0.00710  0.03143  119 ALA B CA  
2234 C C   . ALA B 121 ? 0.37868 0.40830 0.42159 0.00482  0.00533  0.03218  119 ALA B C   
2235 O O   . ALA B 121 ? 0.37200 0.40263 0.41711 0.00256  0.00436  0.03899  119 ALA B O   
2236 C CB  . ALA B 121 ? 0.35894 0.39943 0.40641 0.00137  0.00519  0.03282  119 ALA B CB  
2237 N N   . VAL B 122 ? 0.34217 0.36035 0.38284 0.00698  0.00500  0.02596  120 VAL B N   
2238 C CA  . VAL B 122 ? 0.37005 0.37726 0.41105 0.00757  0.00390  0.02588  120 VAL B CA  
2239 C C   . VAL B 122 ? 0.35232 0.36594 0.39253 0.01030  0.00452  0.02817  120 VAL B C   
2240 O O   . VAL B 122 ? 0.37658 0.38702 0.41945 0.01013  0.00320  0.03321  120 VAL B O   
2241 C CB  . VAL B 122 ? 0.38320 0.38031 0.42175 0.00944  0.00418  0.01869  120 VAL B CB  
2242 C CG1 . VAL B 122 ? 0.35065 0.33895 0.39022 0.01147  0.00393  0.01787  120 VAL B CG1 
2243 C CG2 . VAL B 122 ? 0.36760 0.35949 0.40610 0.00621  0.00279  0.01701  120 VAL B CG2 
2244 N N   . ILE B 123 ? 0.31518 0.33786 0.35205 0.01286  0.00620  0.02449  121 ILE B N   
2245 C CA  . ILE B 123 ? 0.34547 0.37690 0.38056 0.01473  0.00627  0.02584  121 ILE B CA  
2246 C C   . ILE B 123 ? 0.38328 0.42549 0.41920 0.01267  0.00582  0.03464  121 ILE B C   
2247 O O   . ILE B 123 ? 0.34056 0.38525 0.37750 0.01284  0.00434  0.04051  121 ILE B O   
2248 C CB  . ILE B 123 ? 0.36267 0.40081 0.39376 0.01714  0.00795  0.01855  121 ILE B CB  
2249 C CG1 . ILE B 123 ? 0.34274 0.37094 0.37379 0.01858  0.00802  0.01200  121 ILE B CG1 
2250 C CG2 . ILE B 123 ? 0.39893 0.45058 0.42682 0.01798  0.00785  0.01975  121 ILE B CG2 
2251 C CD1 . ILE B 123 ? 0.35477 0.38514 0.38352 0.02017  0.00941  0.00509  121 ILE B CD1 
2252 N N   . GLU B 124 ? 0.33074 0.38103 0.36683 0.01077  0.00713  0.03661  122 GLU B N   
2253 C CA  . GLU B 124 ? 0.39369 0.45818 0.43003 0.00858  0.00748  0.04537  122 GLU B CA  
2254 C C   . GLU B 124 ? 0.41917 0.47679 0.46129 0.00432  0.00509  0.05554  122 GLU B C   
2255 O O   . GLU B 124 ? 0.38574 0.45204 0.42855 0.00277  0.00445  0.06494  122 GLU B O   
2256 C CB  . GLU B 124 ? 0.36256 0.44010 0.39839 0.00822  0.01022  0.04434  122 GLU B CB  
2257 N N   . TYR B 125 ? 0.42180 0.46372 0.46802 0.00221  0.00354  0.05401  123 TYR B N   
2258 C CA  . TYR B 125 ? 0.41863 0.45327 0.47111 -0.00268 0.00116  0.06301  123 TYR B CA  
2259 C C   . TYR B 125 ? 0.47261 0.48851 0.52803 -0.00116 -0.00110 0.06187  123 TYR B C   
2260 O O   . TYR B 125 ? 0.49166 0.49326 0.55095 -0.00415 -0.00285 0.06068  123 TYR B O   
2261 C CB  . TYR B 125 ? 0.44208 0.47585 0.49808 -0.00791 0.00074  0.06315  123 TYR B CB  
2262 C CG  . TYR B 125 ? 0.44687 0.50159 0.50257 -0.00950 0.00315  0.06756  123 TYR B CG  
2263 C CD1 . TYR B 125 ? 0.50299 0.56879 0.56216 -0.01387 0.00311  0.07959  123 TYR B CD1 
2264 C CD2 . TYR B 125 ? 0.40833 0.47248 0.46066 -0.00615 0.00576  0.06003  123 TYR B CD2 
2265 C CE1 . TYR B 125 ? 0.46946 0.55742 0.52807 -0.01480 0.00618  0.08329  123 TYR B CE1 
2266 C CE2 . TYR B 125 ? 0.45028 0.53435 0.50272 -0.00621 0.00862  0.06285  123 TYR B CE2 
2267 C CZ  . TYR B 125 ? 0.45532 0.55235 0.51059 -0.01052 0.00909  0.07417  123 TYR B CZ  
2268 O OH  . TYR B 125 ? 0.45180 0.57122 0.50698 -0.01011 0.01271  0.07657  123 TYR B OH  
2269 N N   . TRP B 126 ? 0.48179 0.49861 0.53581 0.00352  -0.00119 0.06207  124 TRP B N   
2270 C CA  . TRP B 126 ? 0.52295 0.52433 0.58136 0.00613  -0.00297 0.06229  124 TRP B CA  
2271 C C   . TRP B 126 ? 0.55050 0.54238 0.61638 0.00238  -0.00551 0.07227  124 TRP B C   
2272 O O   . TRP B 126 ? 0.54659 0.52098 0.61733 0.00377  -0.00696 0.07062  124 TRP B O   
2273 C CB  . TRP B 126 ? 0.49169 0.50024 0.54896 0.01146  -0.00307 0.06340  124 TRP B CB  
2274 C CG  . TRP B 126 ? 0.49208 0.51812 0.54775 0.01038  -0.00359 0.07314  124 TRP B CG  
2275 C CD1 . TRP B 126 ? 0.46279 0.50681 0.51155 0.01005  -0.00184 0.07111  124 TRP B CD1 
2276 C CD2 . TRP B 126 ? 0.50932 0.53711 0.57005 0.00942  -0.00593 0.08665  124 TRP B CD2 
2277 N NE1 . TRP B 126 ? 0.46731 0.52600 0.51533 0.00877  -0.00273 0.08206  124 TRP B NE1 
2278 C CE2 . TRP B 126 ? 0.50690 0.55631 0.56237 0.00817  -0.00539 0.09273  124 TRP B CE2 
2279 C CE3 . TRP B 126 ? 0.53400 0.54684 0.60340 0.00972  -0.00844 0.09432  124 TRP B CE3 
2280 C CZ2 . TRP B 126 ? 0.52161 0.57990 0.57963 0.00681  -0.00739 0.10744  124 TRP B CZ2 
2281 C CZ3 . TRP B 126 ? 0.51430 0.53375 0.58766 0.00861  -0.01065 0.10935  124 TRP B CZ3 
2282 C CH2 . TRP B 126 ? 0.52252 0.56541 0.58992 0.00692  -0.01015 0.11643  124 TRP B CH2 
2283 N N   . ASN B 127 ? 0.52875 0.53181 0.59597 -0.00239 -0.00587 0.08243  125 ASN B N   
2284 C CA  . ASN B 127 ? 0.56655 0.56266 0.64169 -0.00702 -0.00845 0.09467  125 ASN B CA  
2285 C C   . ASN B 127 ? 0.57913 0.56402 0.65876 -0.01411 -0.00978 0.09348  125 ASN B C   
2286 O O   . ASN B 127 ? 0.60363 0.58044 0.69097 -0.01933 -0.01229 0.10335  125 ASN B O   
2287 C CB  . ASN B 127 ? 0.55612 0.57291 0.63040 -0.00958 -0.00800 0.10769  125 ASN B CB  
2288 C CG  . ASN B 127 ? 0.56935 0.60597 0.63737 -0.01179 -0.00485 0.10432  125 ASN B CG  
2289 O OD1 . ASN B 127 ? 0.56057 0.60776 0.62112 -0.00719 -0.00254 0.09594  125 ASN B OD1 
2290 N ND2 . ASN B 127 ? 0.56891 0.61083 0.64095 -0.01885 -0.00476 0.11098  125 ASN B ND2 
2291 N N   . LEU B 128 ? 0.57179 0.55711 0.64723 -0.01505 -0.00854 0.08264  126 LEU B N   
2292 C CA  . LEU B 128 ? 0.54549 0.52218 0.62463 -0.02210 -0.01042 0.08036  126 LEU B CA  
2293 C C   . LEU B 128 ? 0.54552 0.50694 0.62134 -0.01910 -0.01074 0.06653  126 LEU B C   
2294 O O   . LEU B 128 ? 0.53348 0.50182 0.60328 -0.01732 -0.00902 0.05813  126 LEU B O   
2295 C CB  . LEU B 128 ? 0.53649 0.53238 0.61418 -0.02649 -0.00891 0.08192  126 LEU B CB  
2296 C CG  . LEU B 128 ? 0.55595 0.57274 0.63529 -0.02922 -0.00732 0.09443  126 LEU B CG  
2297 C CD1 . LEU B 128 ? 0.51996 0.55599 0.59800 -0.03157 -0.00502 0.09275  126 LEU B CD1 
2298 C CD2 . LEU B 128 ? 0.52996 0.54099 0.61823 -0.03627 -0.01012 0.10823  126 LEU B CD2 
2299 N N   . PRO B 129 ? 0.56935 0.51024 0.64899 -0.01809 -0.01274 0.06393  127 PRO B N   
2300 C CA  . PRO B 129 ? 0.57089 0.49972 0.64608 -0.01364 -0.01209 0.05048  127 PRO B CA  
2301 C C   . PRO B 129 ? 0.56264 0.48939 0.63433 -0.01865 -0.01322 0.04182  127 PRO B C   
2302 O O   . PRO B 129 ? 0.50051 0.42191 0.56654 -0.01508 -0.01218 0.03096  127 PRO B O   
2303 C CB  . PRO B 129 ? 0.59774 0.50568 0.67942 -0.01145 -0.01389 0.05082  127 PRO B CB  
2304 C CG  . PRO B 129 ? 0.60173 0.51434 0.69003 -0.01152 -0.01476 0.06564  127 PRO B CG  
2305 C CD  . PRO B 129 ? 0.57720 0.50618 0.66535 -0.01919 -0.01509 0.07369  127 PRO B CD  
2306 N N   . ASP B 130 ? 0.53875 0.47130 0.61380 -0.02694 -0.01539 0.04680  128 ASP B N   
2307 C CA  . ASP B 130 ? 0.52961 0.46405 0.60150 -0.03171 -0.01698 0.03939  128 ASP B CA  
2308 C C   . ASP B 130 ? 0.52267 0.47459 0.58782 -0.02775 -0.01410 0.03611  128 ASP B C   
2309 O O   . ASP B 130 ? 0.48914 0.44199 0.54990 -0.02880 -0.01495 0.02863  128 ASP B O   
2310 C CB  . ASP B 130 ? 0.58652 0.52379 0.66574 -0.04224 -0.02049 0.04647  128 ASP B CB  
2311 N N   . ILE B 131 ? 0.52206 0.48753 0.58622 -0.02314 -0.01094 0.04135  129 ILE B N   
2312 C CA  . ILE B 131 ? 0.46104 0.44104 0.51996 -0.01924 -0.00830 0.03794  129 ILE B CA  
2313 C C   . ILE B 131 ? 0.46213 0.43494 0.51445 -0.01311 -0.00675 0.02850  129 ILE B C   
2314 O O   . ILE B 131 ? 0.38159 0.35737 0.42976 -0.01248 -0.00659 0.02287  129 ILE B O   
2315 C CB  . ILE B 131 ? 0.44287 0.43885 0.50228 -0.01645 -0.00548 0.04489  129 ILE B CB  
2316 C CG1 . ILE B 131 ? 0.45889 0.46631 0.52453 -0.02308 -0.00639 0.05439  129 ILE B CG1 
2317 C CG2 . ILE B 131 ? 0.36593 0.37250 0.41989 -0.01068 -0.00247 0.03953  129 ILE B CG2 
2318 C CD1 . ILE B 131 ? 0.45294 0.48137 0.51758 -0.02052 -0.00302 0.05842  129 ILE B CD1 
2319 N N   . LYS B 132 ? 0.44784 0.41230 0.49982 -0.00858 -0.00564 0.02762  130 LYS B N   
2320 C CA  . LYS B 132 ? 0.44513 0.40355 0.49207 -0.00332 -0.00392 0.01937  130 LYS B CA  
2321 C C   . LYS B 132 ? 0.47327 0.42133 0.51735 -0.00584 -0.00559 0.01172  130 LYS B C   
2322 O O   . LYS B 132 ? 0.45359 0.40307 0.49185 -0.00355 -0.00429 0.00541  130 LYS B O   
2323 C CB  . LYS B 132 ? 0.45176 0.40409 0.50104 0.00158  -0.00285 0.02071  130 LYS B CB  
2324 C CG  . LYS B 132 ? 0.50111 0.44900 0.54679 0.00701  -0.00065 0.01305  130 LYS B CG  
2325 C CD  . LYS B 132 ? 0.55066 0.49032 0.60118 0.01141  -0.00039 0.01443  130 LYS B CD  
2326 C CE  . LYS B 132 ? 0.58047 0.52863 0.63033 0.01704  0.00206  0.01410  130 LYS B CE  
2327 N NZ  . LYS B 132 ? 0.54790 0.50161 0.59158 0.01752  0.00419  0.00767  130 LYS B NZ  
2328 N N   . MET B 133 ? 0.48656 0.42465 0.53443 -0.01111 -0.00869 0.01227  131 MET B N   
2329 C CA  . MET B 133 ? 0.50307 0.43146 0.54717 -0.01387 -0.01065 0.00344  131 MET B CA  
2330 C C   . MET B 133 ? 0.44301 0.38234 0.48340 -0.01822 -0.01234 0.00206  131 MET B C   
2331 O O   . MET B 133 ? 0.44797 0.38658 0.48157 -0.01777 -0.01254 -0.00539 131 MET B O   
2332 C CB  . MET B 133 ? 0.56188 0.47462 0.61165 -0.01877 -0.01398 0.00340  131 MET B CB  
2333 C CG  . MET B 133 ? 0.61375 0.51016 0.66380 -0.01322 -0.01266 -0.00283 131 MET B CG  
2334 S SD  . MET B 133 ? 0.81500 0.69142 0.87524 -0.01745 -0.01629 0.00067  131 MET B SD  
2335 C CE  . MET B 133 ? 0.64819 0.52703 0.70919 -0.03010 -0.02149 0.00090  131 MET B CE  
2336 N N   . LYS B 134 ? 0.43528 0.38655 0.48022 -0.02204 -0.01343 0.00970  132 LYS B N   
2337 C CA  . LYS B 134 ? 0.44205 0.40628 0.48510 -0.02465 -0.01478 0.00960  132 LYS B CA  
2338 C C   . LYS B 134 ? 0.42262 0.39404 0.45967 -0.01794 -0.01164 0.00693  132 LYS B C   
2339 O O   . LYS B 134 ? 0.34671 0.32274 0.37941 -0.01858 -0.01290 0.00366  132 LYS B O   
2340 C CB  . LYS B 134 ? 0.38595 0.36399 0.43631 -0.02853 -0.01548 0.01873  132 LYS B CB  
2341 C CG  . LYS B 134 ? 0.47177 0.44617 0.52869 -0.03789 -0.01977 0.02193  132 LYS B CG  
2342 C CD  . LYS B 134 ? 0.47090 0.46143 0.53583 -0.04135 -0.01938 0.03247  132 LYS B CD  
2343 C CE  . LYS B 134 ? 0.49837 0.48385 0.57136 -0.05163 -0.02356 0.03731  132 LYS B CE  
2344 N NZ  . LYS B 134 ? 0.51974 0.50896 0.59390 -0.05921 -0.02838 0.03370  132 LYS B NZ  
2345 N N   . VAL B 135 ? 0.34981 0.32281 0.38692 -0.01195 -0.00794 0.00887  133 VAL B N   
2346 C CA  . VAL B 135 ? 0.37159 0.35035 0.40431 -0.00654 -0.00526 0.00678  133 VAL B CA  
2347 C C   . VAL B 135 ? 0.39708 0.36737 0.42340 -0.00437 -0.00440 -0.00014 133 VAL B C   
2348 O O   . VAL B 135 ? 0.35011 0.32456 0.37187 -0.00296 -0.00392 -0.00213 133 VAL B O   
2349 C CB  . VAL B 135 ? 0.35763 0.34165 0.39241 -0.00187 -0.00210 0.01016  133 VAL B CB  
2350 C CG1 . VAL B 135 ? 0.35212 0.33909 0.38320 0.00299  0.00033  0.00735  133 VAL B CG1 
2351 C CG2 . VAL B 135 ? 0.35744 0.35336 0.39716 -0.00357 -0.00228 0.01629  133 VAL B CG2 
2352 N N   . GLU B 136 ? 0.37236 0.33140 0.39869 -0.00380 -0.00404 -0.00340 134 GLU B N   
2353 C CA  . GLU B 136 ? 0.42464 0.37675 0.44504 -0.00180 -0.00287 -0.01084 134 GLU B CA  
2354 C C   . GLU B 136 ? 0.41786 0.37054 0.43279 -0.00637 -0.00584 -0.01530 134 GLU B C   
2355 O O   . GLU B 136 ? 0.40666 0.36198 0.41453 -0.00490 -0.00471 -0.01942 134 GLU B O   
2356 C CB  . GLU B 136 ? 0.45640 0.39594 0.47957 -0.00004 -0.00228 -0.01379 134 GLU B CB  
2357 C CG  . GLU B 136 ? 0.51671 0.45672 0.54375 0.00580  0.00087  -0.01086 134 GLU B CG  
2358 C CD  . GLU B 136 ? 0.60317 0.53114 0.63533 0.00798  0.00077  -0.01173 134 GLU B CD  
2359 O OE1 . GLU B 136 ? 0.60432 0.52326 0.63979 0.00387  -0.00227 -0.01115 134 GLU B OE1 
2360 O OE2 . GLU B 136 ? 0.65404 0.58161 0.68792 0.01381  0.00358  -0.01262 134 GLU B OE2 
2361 N N   . ASP B 137 ? 0.43484 0.38618 0.45298 -0.01252 -0.00988 -0.01412 135 ASP B N   
2362 C CA  . ASP B 137 ? 0.43836 0.39160 0.45148 -0.01785 -0.01367 -0.01860 135 ASP B CA  
2363 C C   . ASP B 137 ? 0.40552 0.37326 0.41546 -0.01716 -0.01400 -0.01522 135 ASP B C   
2364 O O   . ASP B 137 ? 0.42310 0.39425 0.42547 -0.01846 -0.01548 -0.01936 135 ASP B O   
2365 C CB  . ASP B 137 ? 0.44626 0.39645 0.46536 -0.02562 -0.01837 -0.01698 135 ASP B CB  
2366 C CG  . ASP B 137 ? 0.53726 0.46973 0.55719 -0.02763 -0.01951 -0.02344 135 ASP B CG  
2367 O OD1 . ASP B 137 ? 0.60670 0.53364 0.63292 -0.03447 -0.02335 -0.02163 135 ASP B OD1 
2368 O OD2 . ASP B 137 ? 0.56024 0.48429 0.57524 -0.02231 -0.01649 -0.03034 135 ASP B OD2 
2369 N N   . PHE B 138 ? 0.36386 0.34047 0.37939 -0.01476 -0.01264 -0.00773 136 PHE B N   
2370 C CA  . PHE B 138 ? 0.37975 0.36851 0.39399 -0.01291 -0.01284 -0.00405 136 PHE B CA  
2371 C C   . PHE B 138 ? 0.37308 0.36085 0.38100 -0.00780 -0.00952 -0.00595 136 PHE B C   
2372 O O   . PHE B 138 ? 0.36191 0.35647 0.36540 -0.00766 -0.01065 -0.00493 136 PHE B O   
2373 C CB  . PHE B 138 ? 0.35493 0.35231 0.37709 -0.01061 -0.01159 0.00297  136 PHE B CB  
2374 C CG  . PHE B 138 ? 0.37589 0.38193 0.39780 -0.00601 -0.01043 0.00623  136 PHE B CG  
2375 C CD1 . PHE B 138 ? 0.34845 0.36425 0.37027 -0.00767 -0.01378 0.00871  136 PHE B CD1 
2376 C CD2 . PHE B 138 ? 0.38487 0.38870 0.40705 -0.00019 -0.00640 0.00683  136 PHE B CD2 
2377 C CE1 . PHE B 138 ? 0.34221 0.36453 0.36501 -0.00285 -0.01293 0.01263  136 PHE B CE1 
2378 C CE2 . PHE B 138 ? 0.31798 0.32696 0.34086 0.00385  -0.00558 0.00974  136 PHE B CE2 
2379 C CZ  . PHE B 138 ? 0.29883 0.31656 0.32243 0.00297  -0.00870 0.01306  136 PHE B CZ  
2380 N N   . ASN B 139 ? 0.34485 0.32584 0.35319 -0.00376 -0.00557 -0.00737 137 ASN B N   
2381 C CA  . ASN B 139 ? 0.37290 0.35382 0.37636 0.00012  -0.00229 -0.00868 137 ASN B CA  
2382 C C   . ASN B 139 ? 0.38055 0.35966 0.37526 -0.00149 -0.00264 -0.01466 137 ASN B C   
2383 O O   . ASN B 139 ? 0.34483 0.32898 0.33401 -0.00024 -0.00133 -0.01397 137 ASN B O   
2384 C CB  . ASN B 139 ? 0.37117 0.34691 0.37788 0.00405  0.00151  -0.00917 137 ASN B CB  
2385 C CG  . ASN B 139 ? 0.40668 0.38654 0.41935 0.00640  0.00252  -0.00415 137 ASN B CG  
2386 O OD1 . ASN B 139 ? 0.36500 0.35056 0.37830 0.00731  0.00221  -0.00087 137 ASN B OD1 
2387 N ND2 . ASN B 139 ? 0.42412 0.40135 0.44125 0.00764  0.00358  -0.00358 137 ASN B ND2 
2388 N N   . LYS B 140 ? 0.34899 0.32074 0.34233 -0.00424 -0.00423 -0.02066 138 LYS B N   
2389 C CA  . LYS B 140 ? 0.41777 0.38812 0.40183 -0.00601 -0.00484 -0.02830 138 LYS B CA  
2390 C C   . LYS B 140 ? 0.40310 0.38373 0.38167 -0.01025 -0.00906 -0.02674 138 LYS B C   
2391 O O   . LYS B 140 ? 0.38294 0.36979 0.35251 -0.01000 -0.00845 -0.02861 138 LYS B O   
2392 C CB  . LYS B 140 ? 0.42050 0.37849 0.40587 -0.00812 -0.00620 -0.03558 138 LYS B CB  
2393 C CG  . LYS B 140 ? 0.47760 0.43353 0.45377 -0.01187 -0.00866 -0.04508 138 LYS B CG  
2394 C CD  . LYS B 140 ? 0.52161 0.46360 0.50203 -0.01557 -0.01161 -0.05081 138 LYS B CD  
2395 C CE  . LYS B 140 ? 0.58620 0.51804 0.55988 -0.01358 -0.00976 -0.06341 138 LYS B CE  
2396 N NZ  . LYS B 140 ? 0.54858 0.48432 0.51138 -0.01917 -0.01364 -0.07185 138 LYS B NZ  
2397 N N   . TRP B 141 ? 0.39898 0.38364 0.38336 -0.01408 -0.01331 -0.02230 139 TRP B N   
2398 C CA  . TRP B 141 ? 0.36420 0.36111 0.34572 -0.01765 -0.01783 -0.01906 139 TRP B CA  
2399 C C   . TRP B 141 ? 0.34535 0.35157 0.32516 -0.01326 -0.01590 -0.01202 139 TRP B C   
2400 O O   . TRP B 141 ? 0.32463 0.34003 0.29730 -0.01467 -0.01818 -0.01082 139 TRP B O   
2401 C CB  . TRP B 141 ? 0.36641 0.36770 0.35751 -0.02156 -0.02181 -0.01416 139 TRP B CB  
2402 C CG  . TRP B 141 ? 0.32620 0.34233 0.31708 -0.02457 -0.02669 -0.00948 139 TRP B CG  
2403 C CD1 . TRP B 141 ? 0.35918 0.38086 0.34654 -0.03170 -0.03264 -0.01290 139 TRP B CD1 
2404 C CD2 . TRP B 141 ? 0.33029 0.35809 0.32557 -0.02039 -0.02649 -0.00035 139 TRP B CD2 
2405 N NE1 . TRP B 141 ? 0.26328 0.30124 0.25247 -0.03207 -0.03625 -0.00569 139 TRP B NE1 
2406 C CE2 . TRP B 141 ? 0.30246 0.34376 0.29685 -0.02467 -0.03239 0.00224  139 TRP B CE2 
2407 C CE3 . TRP B 141 ? 0.32202 0.34965 0.32221 -0.01340 -0.02214 0.00541  139 TRP B CE3 
2408 C CZ2 . TRP B 141 ? 0.33988 0.39464 0.33903 -0.02121 -0.03385 0.01135  139 TRP B CZ2 
2409 C CZ3 . TRP B 141 ? 0.32199 0.36081 0.32647 -0.01018 -0.02343 0.01331  139 TRP B CZ3 
2410 C CH2 . TRP B 141 ? 0.30383 0.35614 0.30812 -0.01359 -0.02912 0.01669  139 TRP B CH2 
2411 N N   . LYS B 142 ? 0.33825 0.34204 0.32444 -0.00820 -0.01197 -0.00720 140 LYS B N   
2412 C CA  . LYS B 142 ? 0.33322 0.34358 0.31995 -0.00446 -0.01064 -0.00000 140 LYS B CA  
2413 C C   . LYS B 142 ? 0.36528 0.37594 0.34310 -0.00322 -0.00773 -0.00148 140 LYS B C   
2414 O O   . LYS B 142 ? 0.32071 0.33948 0.29484 -0.00288 -0.00870 0.00410  140 LYS B O   
2415 C CB  . LYS B 142 ? 0.30370 0.31042 0.29966 -0.00001 -0.00755 0.00396  140 LYS B CB  
2416 C CG  . LYS B 142 ? 0.31843 0.32824 0.31614 0.00388  -0.00604 0.01046  140 LYS B CG  
2417 C CD  . LYS B 142 ? 0.34592 0.35246 0.35273 0.00781  -0.00384 0.01269  140 LYS B CD  
2418 C CE  . LYS B 142 ? 0.31482 0.31305 0.32219 0.00864  -0.00018 0.00798  140 LYS B CE  
2419 N NZ  . LYS B 142 ? 0.33036 0.32649 0.34387 0.01246  0.00203  0.01040  140 LYS B NZ  
2420 N N   . TYR B 143 ? 0.34351 0.34657 0.31840 -0.00231 -0.00400 -0.00812 141 TYR B N   
2421 C CA  . TYR B 143 ? 0.35421 0.36020 0.31990 -0.00167 -0.00096 -0.01066 141 TYR B CA  
2422 C C   . TYR B 143 ? 0.35797 0.37230 0.31286 -0.00565 -0.00462 -0.01349 141 TYR B C   
2423 O O   . TYR B 143 ? 0.31400 0.33792 0.26187 -0.00579 -0.00429 -0.00923 141 TYR B O   
2424 C CB  . TYR B 143 ? 0.32733 0.32496 0.29271 0.00043  0.00336  -0.01855 141 TYR B CB  
2425 C CG  . TYR B 143 ? 0.33976 0.34260 0.29587 0.00152  0.00733  -0.02205 141 TYR B CG  
2426 C CD1 . TYR B 143 ? 0.38579 0.39181 0.33088 -0.00072 0.00629  -0.03007 141 TYR B CD1 
2427 C CD2 . TYR B 143 ? 0.35412 0.35994 0.31237 0.00435  0.01215  -0.01761 141 TYR B CD2 
2428 C CE1 . TYR B 143 ? 0.37987 0.39327 0.31552 0.00061  0.01056  -0.03352 141 TYR B CE1 
2429 C CE2 . TYR B 143 ? 0.37379 0.38722 0.32392 0.00511  0.01637  -0.01990 141 TYR B CE2 
2430 C CZ  . TYR B 143 ? 0.39331 0.41104 0.33194 0.00365  0.01588  -0.02779 141 TYR B CZ  
2431 O OH  . TYR B 143 ? 0.41435 0.44189 0.34434 0.00480  0.02075  -0.03018 141 TYR B OH  
2432 N N   . GLU B 144 ? 0.36159 0.37305 0.31513 -0.00950 -0.00855 -0.02014 142 GLU B N   
2433 C CA  . GLU B 144 ? 0.36576 0.38407 0.30758 -0.01386 -0.01199 -0.02608 142 GLU B CA  
2434 C C   . GLU B 144 ? 0.39959 0.43243 0.33897 -0.01641 -0.01706 -0.01773 142 GLU B C   
2435 O O   . GLU B 144 ? 0.42025 0.46365 0.34801 -0.01824 -0.01828 -0.01846 142 GLU B O   
2436 C CB  . GLU B 144 ? 0.38857 0.39776 0.33081 -0.01807 -0.01522 -0.03616 142 GLU B CB  
2437 C CG  . GLU B 144 ? 0.45068 0.44691 0.39222 -0.01490 -0.01028 -0.04560 142 GLU B CG  
2438 C CD  . GLU B 144 ? 0.54836 0.53206 0.49228 -0.01870 -0.01342 -0.05484 142 GLU B CD  
2439 O OE1 . GLU B 144 ? 0.55719 0.54247 0.50489 -0.02454 -0.01938 -0.05286 142 GLU B OE1 
2440 O OE2 . GLU B 144 ? 0.53575 0.50792 0.47929 -0.01567 -0.00987 -0.06332 142 GLU B OE2 
2441 N N   . ILE B 145 ? 0.37554 0.41070 0.32562 -0.01614 -0.01997 -0.00946 143 ILE B N   
2442 C CA  . ILE B 145 ? 0.34967 0.39939 0.29938 -0.01712 -0.02465 -0.00022 143 ILE B CA  
2443 C C   . ILE B 145 ? 0.37995 0.43516 0.32595 -0.01316 -0.02146 0.00811  143 ILE B C   
2444 O O   . ILE B 145 ? 0.34551 0.41380 0.28466 -0.01454 -0.02465 0.01378  143 ILE B O   
2445 C CB  . ILE B 145 ? 0.35055 0.40230 0.31406 -0.01627 -0.02751 0.00672  143 ILE B CB  
2446 C CG1 . ILE B 145 ? 0.38001 0.44842 0.34385 -0.01741 -0.03336 0.01543  143 ILE B CG1 
2447 C CG2 . ILE B 145 ? 0.37959 0.42356 0.35306 -0.00991 -0.02242 0.01213  143 ILE B CG2 
2448 C CD1 . ILE B 145 ? 0.41035 0.48460 0.38747 -0.01737 -0.03691 0.02068  143 ILE B CD1 
2449 N N   . PHE B 146 ? 0.35286 0.39878 0.30368 -0.00873 -0.01548 0.00964  144 PHE B N   
2450 C CA  . PHE B 146 ? 0.37547 0.42479 0.32377 -0.00600 -0.01196 0.01732  144 PHE B CA  
2451 C C   . PHE B 146 ? 0.39889 0.45562 0.33245 -0.00831 -0.01017 0.01286  144 PHE B C   
2452 O O   . PHE B 146 ? 0.36375 0.43242 0.29045 -0.00911 -0.01129 0.02054  144 PHE B O   
2453 C CB  . PHE B 146 ? 0.36912 0.40656 0.32627 -0.00209 -0.00638 0.01771  144 PHE B CB  
2454 C CG  . PHE B 146 ? 0.34688 0.38582 0.30519 0.00001  -0.00313 0.02682  144 PHE B CG  
2455 C CD1 . PHE B 146 ? 0.38793 0.43088 0.35127 0.00154  -0.00575 0.03845  144 PHE B CD1 
2456 C CD2 . PHE B 146 ? 0.37083 0.40696 0.32671 0.00046  0.00253  0.02420  144 PHE B CD2 
2457 C CE1 . PHE B 146 ? 0.37449 0.41679 0.34008 0.00279  -0.00305 0.04750  144 PHE B CE1 
2458 C CE2 . PHE B 146 ? 0.40325 0.44102 0.36122 0.00111  0.00540  0.03326  144 PHE B CE2 
2459 C CZ  . PHE B 146 ? 0.40931 0.44898 0.37217 0.00196  0.00252  0.04495  144 PHE B CZ  
2460 N N   . ALA B 147 ? 0.38196 0.43240 0.31053 -0.00907 -0.00732 0.00053  145 ALA B N   
2461 C CA  . ALA B 147 ? 0.42501 0.48296 0.33895 -0.01069 -0.00518 -0.00647 145 ALA B CA  
2462 C C   . ALA B 147 ? 0.45386 0.52522 0.35658 -0.01541 -0.01144 -0.00728 145 ALA B C   
2463 O O   . ALA B 147 ? 0.42912 0.51356 0.31893 -0.01667 -0.01058 -0.00644 145 ALA B O   
2464 C CB  . ALA B 147 ? 0.43395 0.48062 0.34690 -0.00977 -0.00176 -0.02073 145 ALA B CB  
2465 N N   . GLU B 148 ? 0.41100 0.48136 0.31828 -0.01851 -0.01793 -0.00854 146 GLU B N   
2466 C CA  . GLU B 148 ? 0.41700 0.50175 0.31433 -0.02371 -0.02477 -0.00926 146 GLU B CA  
2467 C C   . GLU B 148 ? 0.42650 0.52742 0.32121 -0.02291 -0.02688 0.00576  146 GLU B C   
2468 O O   . GLU B 148 ? 0.41486 0.53118 0.29564 -0.02598 -0.02944 0.00595  146 GLU B O   
2469 C CB  . GLU B 148 ? 0.45109 0.53332 0.35605 -0.02784 -0.03157 -0.01212 146 GLU B CB  
2470 C CG  . GLU B 148 ? 0.53088 0.62384 0.42318 -0.03497 -0.03816 -0.02068 146 GLU B CG  
2471 C CD  . GLU B 148 ? 0.62009 0.70206 0.50351 -0.03754 -0.03622 -0.03890 146 GLU B CD  
2472 O OE1 . GLU B 148 ? 0.60098 0.67439 0.48135 -0.03293 -0.02872 -0.04409 146 GLU B OE1 
2473 O OE2 . GLU B 148 ? 0.67438 0.75774 0.55327 -0.04431 -0.04246 -0.04820 146 GLU B OE2 
2474 N N   . TYR B 149 ? 0.41488 0.51260 0.32264 -0.01871 -0.02599 0.01846  147 TYR B N   
2475 C CA  . TYR B 149 ? 0.45090 0.56159 0.35798 -0.01730 -0.02798 0.03386  147 TYR B CA  
2476 C C   . TYR B 149 ? 0.45772 0.57191 0.35645 -0.01601 -0.02191 0.03794  147 TYR B C   
2477 O O   . TYR B 149 ? 0.47852 0.60745 0.37028 -0.01684 -0.02382 0.04872  147 TYR B O   
2478 C CB  . TYR B 149 ? 0.45154 0.55636 0.37615 -0.01265 -0.02901 0.04543  147 TYR B CB  
2479 C CG  . TYR B 149 ? 0.41695 0.52763 0.34940 -0.01378 -0.03611 0.04703  147 TYR B CG  
2480 C CD1 . TYR B 149 ? 0.48143 0.61062 0.40986 -0.01592 -0.04317 0.05498  147 TYR B CD1 
2481 C CD2 . TYR B 149 ? 0.41866 0.51869 0.36278 -0.01293 -0.03586 0.04144  147 TYR B CD2 
2482 C CE1 . TYR B 149 ? 0.41996 0.55696 0.35679 -0.01717 -0.04973 0.05676  147 TYR B CE1 
2483 C CE2 . TYR B 149 ? 0.39298 0.50073 0.34514 -0.01433 -0.04188 0.04347  147 TYR B CE2 
2484 C CZ  . TYR B 149 ? 0.43635 0.56269 0.38538 -0.01642 -0.04879 0.05097  147 TYR B CZ  
2485 O OH  . TYR B 149 ? 0.41691 0.55304 0.37538 -0.01795 -0.05482 0.05333  147 TYR B OH  
2486 N N   . LEU B 150 ? 0.45157 0.55448 0.35079 -0.01427 -0.01474 0.03019  148 LEU B N   
2487 C CA  . LEU B 150 ? 0.48769 0.59386 0.38369 -0.01277 -0.00844 0.03677  148 LEU B CA  
2488 C C   . LEU B 150 ? 0.53174 0.64050 0.41615 -0.01336 -0.00212 0.02527  148 LEU B C   
2489 O O   . LEU B 150 ? 0.50131 0.61572 0.38334 -0.01260 0.00342  0.03149  148 LEU B O   
2490 C CB  . LEU B 150 ? 0.43846 0.53037 0.35070 -0.00892 -0.00489 0.04368  148 LEU B CB  
2491 C CG  . LEU B 150 ? 0.48217 0.57482 0.40401 -0.00706 -0.00742 0.06067  148 LEU B CG  
2492 C CD1 . LEU B 150 ? 0.53921 0.63650 0.46490 -0.00673 -0.01495 0.06520  148 LEU B CD1 
2493 C CD2 . LEU B 150 ? 0.43646 0.51241 0.37342 -0.00372 -0.00395 0.06191  148 LEU B CD2 
2494 N N   . ALA B 151 ? 0.54253 0.64780 0.42030 -0.01462 -0.00260 0.00901  149 ALA B N   
2495 C CA  . ALA B 151 ? 0.54957 0.65439 0.41971 -0.01317 0.00446  -0.00272 149 ALA B CA  
2496 C C   . ALA B 151 ? 0.58206 0.70698 0.43472 -0.01492 0.00696  -0.00209 149 ALA B C   
2497 O O   . ALA B 151 ? 0.57430 0.70221 0.42103 -0.01288 0.01405  -0.00989 149 ALA B O   
2498 C CB  . ALA B 151 ? 0.50558 0.59839 0.37477 -0.01334 0.00342  -0.02053 149 ALA B CB  
2499 N N   . GLU B 152 ? 0.54784 0.68827 0.39239 -0.01824 0.00168  0.00769  150 GLU B N   
2500 C CA  . GLU B 152 ? 0.58333 0.74502 0.41144 -0.01987 0.00466  0.01120  150 GLU B CA  
2501 C C   . GLU B 152 ? 0.55636 0.72501 0.38994 -0.01907 0.00839  0.03052  150 GLU B C   
2502 O O   . GLU B 152 ? 0.61118 0.79694 0.43319 -0.02006 0.01317  0.03433  150 GLU B O   
2503 C CB  . GLU B 152 ? 0.60697 0.78550 0.42032 -0.02452 -0.00311 0.01106  150 GLU B CB  
2504 C CG  . GLU B 152 ? 0.63160 0.80416 0.43872 -0.02697 -0.00766 -0.00831 150 GLU B CG  
2505 C CD  . GLU B 152 ? 0.64496 0.82510 0.43444 -0.02704 -0.00245 -0.02547 150 GLU B CD  
2506 O OE1 . GLU B 152 ? 0.63346 0.80176 0.42718 -0.02279 0.00509  -0.03549 150 GLU B OE1 
2507 O OE2 . GLU B 152 ? 0.67357 0.87281 0.44484 -0.03089 -0.00562 -0.02883 150 GLU B OE2 
2508 N N   . GLU B 153 ? 0.53654 0.69234 0.38757 -0.01747 0.00654  0.04233  151 GLU B N   
2509 C CA  . GLU B 153 ? 0.54014 0.69764 0.39940 -0.01703 0.00971  0.06012  151 GLU B CA  
2510 C C   . GLU B 153 ? 0.54524 0.68881 0.41722 -0.01452 0.01676  0.05759  151 GLU B C   
2511 O O   . GLU B 153 ? 0.53415 0.68108 0.41106 -0.01528 0.02084  0.06991  151 GLU B O   
2512 C CB  . GLU B 153 ? 0.53453 0.68649 0.40563 -0.01653 0.00280  0.07518  151 GLU B CB  
2513 C CG  . GLU B 153 ? 0.60825 0.77803 0.46934 -0.01893 -0.00414 0.08503  151 GLU B CG  
2514 C CD  . GLU B 153 ? 0.63308 0.82274 0.48279 -0.02150 -0.00116 0.09817  151 GLU B CD  
2515 O OE1 . GLU B 153 ? 0.64740 0.85221 0.47993 -0.02368 0.00231  0.08927  151 GLU B OE1 
2516 O OE2 . GLU B 153 ? 0.67535 0.86550 0.53344 -0.02128 -0.00216 0.11749  151 GLU B OE2 
2517 N N   . ILE B 154 ? 0.50170 0.63034 0.37970 -0.01203 0.01784  0.04290  152 ILE B N   
2518 C CA  . ILE B 154 ? 0.47826 0.59410 0.36943 -0.00955 0.02331  0.04074  152 ILE B CA  
2519 C C   . ILE B 154 ? 0.47053 0.58405 0.35691 -0.00724 0.02773  0.02279  152 ILE B C   
2520 O O   . ILE B 154 ? 0.48631 0.59231 0.37021 -0.00657 0.02410  0.01096  152 ILE B O   
2521 C CB  . ILE B 154 ? 0.50187 0.59896 0.40948 -0.00780 0.01938  0.04330  152 ILE B CB  
2522 C CG1 . ILE B 154 ? 0.51659 0.61290 0.43246 -0.00871 0.01681  0.06085  152 ILE B CG1 
2523 C CG2 . ILE B 154 ? 0.44377 0.52891 0.36292 -0.00550 0.02438  0.03802  152 ILE B CG2 
2524 C CD1 . ILE B 154 ? 0.52969 0.61201 0.45751 -0.00657 0.01146  0.06233  152 ILE B CD1 
2525 N N   . ASN B 155 ? 0.44907 0.56881 0.33544 -0.00593 0.03545  0.02110  153 ASN B N   
2526 C CA  . ASN B 155 ? 0.43317 0.55051 0.31676 -0.00232 0.04011  0.00438  153 ASN B CA  
2527 C C   . ASN B 155 ? 0.45013 0.54692 0.34787 0.00067  0.03855  -0.00244 153 ASN B C   
2528 O O   . ASN B 155 ? 0.42107 0.50735 0.33121 0.00008  0.03554  0.00580  153 ASN B O   
2529 C CB  . ASN B 155 ? 0.43925 0.57084 0.32111 -0.00097 0.04917  0.00513  153 ASN B CB  
2530 C CG  . ASN B 155 ? 0.44755 0.57607 0.34527 -0.00163 0.05219  0.01692  153 ASN B CG  
2531 O OD1 . ASN B 155 ? 0.48181 0.59513 0.39221 -0.00209 0.04812  0.02186  153 ASN B OD1 
2532 N ND2 . ASN B 155 ? 0.51701 0.66148 0.41380 -0.00209 0.05948  0.02130  153 ASN B ND2 
2533 N N   . ASN B 156 ? 0.40551 0.49680 0.30099 0.00416  0.04068  -0.01787 154 ASN B N   
2534 C CA  . ASN B 156 ? 0.42923 0.50183 0.33639 0.00681  0.03854  -0.02451 154 ASN B CA  
2535 C C   . ASN B 156 ? 0.41446 0.48160 0.33720 0.00836  0.04114  -0.01701 154 ASN B C   
2536 O O   . ASN B 156 ? 0.36191 0.41581 0.29497 0.00849  0.03732  -0.01513 154 ASN B O   
2537 C CB  . ASN B 156 ? 0.43620 0.50400 0.33942 0.01093  0.04134  -0.04120 154 ASN B CB  
2538 C CG  . ASN B 156 ? 0.47528 0.54338 0.36476 0.00866  0.03712  -0.05133 154 ASN B CG  
2539 O OD1 . ASN B 156 ? 0.53796 0.60560 0.42446 0.00411  0.03043  -0.04656 154 ASN B OD1 
2540 N ND2 . ASN B 156 ? 0.47349 0.54272 0.35499 0.01197  0.04093  -0.06601 154 ASN B ND2 
2541 N N   . ALA B 157 ? 0.39563 0.47416 0.32020 0.00911  0.04753  -0.01273 155 ALA B N   
2542 C CA  . ALA B 157 ? 0.35382 0.42798 0.29349 0.00998  0.04968  -0.00719 155 ALA B CA  
2543 C C   . ALA B 157 ? 0.36659 0.43366 0.31399 0.00619  0.04487  0.00487  155 ALA B C   
2544 O O   . ALA B 157 ? 0.33607 0.39147 0.29494 0.00697  0.04275  0.00535  155 ALA B O   
2545 C CB  . ALA B 157 ? 0.39526 0.48575 0.33585 0.01039  0.05730  -0.00393 155 ALA B CB  
2546 N N   . ARG B 158 ? 0.32845 0.40287 0.26968 0.00244  0.04313  0.01461  156 ARG B N   
2547 C CA  . ARG B 158 ? 0.37883 0.44611 0.32766 -0.00033 0.03871  0.02625  156 ARG B CA  
2548 C C   . ARG B 158 ? 0.34472 0.39928 0.29536 0.00080  0.03225  0.02285  156 ARG B C   
2549 O O   . ARG B 158 ? 0.32765 0.37150 0.28888 0.00095  0.02956  0.02678  156 ARG B O   
2550 C CB  . ARG B 158 ? 0.36842 0.44799 0.31039 -0.00407 0.03870  0.03873  156 ARG B CB  
2551 C CG  . ARG B 158 ? 0.45007 0.53641 0.39912 -0.00666 0.04385  0.04756  156 ARG B CG  
2552 C CD  . ARG B 158 ? 0.51119 0.61114 0.45538 -0.01106 0.04526  0.06208  156 ARG B CD  
2553 N NE  . ARG B 158 ? 0.60401 0.72367 0.53552 -0.01101 0.05102  0.05857  156 ARG B NE  
2554 C CZ  . ARG B 158 ? 0.58047 0.71653 0.50974 -0.01467 0.05582  0.06914  156 ARG B CZ  
2555 N NH1 . ARG B 158 ? 0.65596 0.78942 0.59594 -0.01927 0.05537  0.08418  156 ARG B NH1 
2556 N NH2 . ARG B 158 ? 0.60869 0.76425 0.52499 -0.01382 0.06141  0.06429  156 ARG B NH2 
2557 N N   . LEU B 159 ? 0.33562 0.39158 0.27648 0.00145  0.02984  0.01474  157 LEU B N   
2558 C CA  . LEU B 159 ? 0.35490 0.39997 0.29882 0.00205  0.02408  0.01079  157 LEU B CA  
2559 C C   . LEU B 159 ? 0.34486 0.37737 0.30005 0.00464  0.02477  0.00553  157 LEU B C   
2560 O O   . LEU B 159 ? 0.29637 0.32032 0.25974 0.00494  0.02131  0.00838  157 LEU B O   
2561 C CB  . LEU B 159 ? 0.37833 0.42664 0.31063 0.00141  0.02178  0.00109  157 LEU B CB  
2562 C CG  . LEU B 159 ? 0.39117 0.45160 0.31167 -0.00172 0.01820  0.00527  157 LEU B CG  
2563 C CD1 . LEU B 159 ? 0.44633 0.50769 0.35636 -0.00287 0.01566  -0.00750 157 LEU B CD1 
2564 C CD2 . LEU B 159 ? 0.39458 0.45361 0.32110 -0.00290 0.01249  0.01637  157 LEU B CD2 
2565 N N   . ARG B 160 ? 0.33500 0.36752 0.29070 0.00699  0.02927  -0.00217 158 ARG B N   
2566 C CA  . ARG B 160 ? 0.34017 0.36251 0.30620 0.00961  0.02961  -0.00636 158 ARG B CA  
2567 C C   . ARG B 160 ? 0.31849 0.33836 0.29528 0.00894  0.02994  0.00157  158 ARG B C   
2568 O O   . ARG B 160 ? 0.30605 0.31715 0.29049 0.00972  0.02733  0.00139  158 ARG B O   
2569 C CB  . ARG B 160 ? 0.33247 0.35669 0.29781 0.01309  0.03438  -0.01515 158 ARG B CB  
2570 C CG  . ARG B 160 ? 0.35892 0.37831 0.31716 0.01444  0.03287  -0.02586 158 ARG B CG  
2571 C CD  . ARG B 160 ? 0.38325 0.40190 0.34270 0.01938  0.03758  -0.03529 158 ARG B CD  
2572 N NE  . ARG B 160 ? 0.43262 0.46540 0.38703 0.02086  0.04383  -0.03592 158 ARG B NE  
2573 C CZ  . ARG B 160 ? 0.44477 0.48423 0.38769 0.02209  0.04651  -0.04412 158 ARG B CZ  
2574 N NH1 . ARG B 160 ? 0.46120 0.49314 0.39643 0.02150  0.04295  -0.05312 158 ARG B NH1 
2575 N NH2 . ARG B 160 ? 0.40286 0.45774 0.34198 0.02364  0.05300  -0.04367 158 ARG B NH2 
2576 N N   . ILE B 161 ? 0.32691 0.35472 0.30425 0.00700  0.03297  0.00859  159 ILE B N   
2577 C CA  . ILE B 161 ? 0.30232 0.32662 0.29020 0.00535  0.03289  0.01554  159 ILE B CA  
2578 C C   . ILE B 161 ? 0.31333 0.32945 0.30410 0.00444  0.02791  0.02092  159 ILE B C   
2579 O O   . ILE B 161 ? 0.34080 0.34856 0.34006 0.00501  0.02614  0.02075  159 ILE B O   
2580 C CB  . ILE B 161 ? 0.28595 0.32071 0.27432 0.00237  0.03705  0.02286  159 ILE B CB  
2581 C CG1 . ILE B 161 ? 0.36722 0.41009 0.35770 0.00413  0.04235  0.01745  159 ILE B CG1 
2582 C CG2 . ILE B 161 ? 0.29966 0.32895 0.29829 -0.00095 0.03570  0.03149  159 ILE B CG2 
2583 C CD1 . ILE B 161 ? 0.38977 0.44794 0.37678 0.00162  0.04746  0.02320  159 ILE B CD1 
2584 N N   . ILE B 162 ? 0.30342 0.32303 0.28724 0.00342  0.02558  0.02556  160 ILE B N   
2585 C CA  . ILE B 162 ? 0.29273 0.30618 0.28070 0.00350  0.02115  0.03182  160 ILE B CA  
2586 C C   . ILE B 162 ? 0.30607 0.31195 0.29730 0.00601  0.01796  0.02548  160 ILE B C   
2587 O O   . ILE B 162 ? 0.27684 0.27540 0.27608 0.00730  0.01608  0.02730  160 ILE B O   
2588 C CB  . ILE B 162 ? 0.32964 0.35117 0.30954 0.00217  0.01896  0.03906  160 ILE B CB  
2589 C CG1 . ILE B 162 ? 0.31852 0.34695 0.29748 -0.00072 0.02170  0.04903  160 ILE B CG1 
2590 C CG2 . ILE B 162 ? 0.32988 0.34638 0.31427 0.00381  0.01377  0.04397  160 ILE B CG2 
2591 C CD1 . ILE B 162 ? 0.39006 0.43082 0.35798 -0.00231 0.02025  0.05573  160 ILE B CD1 
2592 N N   . VAL B 163 ? 0.29947 0.30711 0.28469 0.00659  0.01735  0.01789  161 VAL B N   
2593 C CA  . VAL B 163 ? 0.29701 0.29875 0.28560 0.00800  0.01430  0.01329  161 VAL B CA  
2594 C C   . VAL B 163 ? 0.32105 0.31614 0.31786 0.00964  0.01586  0.00999  161 VAL B C   
2595 O O   . VAL B 163 ? 0.31617 0.30679 0.31868 0.01089  0.01383  0.00995  161 VAL B O   
2596 C CB  . VAL B 163 ? 0.29644 0.30012 0.27748 0.00721  0.01299  0.00610  161 VAL B CB  
2597 C CG1 . VAL B 163 ? 0.33076 0.32824 0.31684 0.00786  0.01046  0.00217  161 VAL B CG1 
2598 C CG2 . VAL B 163 ? 0.31547 0.32699 0.28837 0.00504  0.00983  0.00918  161 VAL B CG2 
2599 N N   . SER B 164 ? 0.28865 0.28490 0.28624 0.00980  0.01954  0.00737  162 SER B N   
2600 C CA  . SER B 164 ? 0.27392 0.26599 0.27926 0.01106  0.02043  0.00495  162 SER B CA  
2601 C C   . SER B 164 ? 0.28982 0.27899 0.30195 0.01018  0.01998  0.00974  162 SER B C   
2602 O O   . SER B 164 ? 0.27650 0.26147 0.29416 0.01118  0.01882  0.00779  162 SER B O   
2603 C CB  . SER B 164 ? 0.30100 0.29691 0.30658 0.01189  0.02420  0.00123  162 SER B CB  
2604 O OG  . SER B 164 ? 0.31717 0.31096 0.33016 0.01319  0.02443  -0.00085 162 SER B OG  
2605 N N   . ALA B 165 ? 0.28494 0.27602 0.29663 0.00817  0.02071  0.01602  163 ALA B N   
2606 C CA  . ALA B 165 ? 0.26522 0.25058 0.28416 0.00723  0.01973  0.02035  163 ALA B CA  
2607 C C   . ALA B 165 ? 0.30450 0.28430 0.32551 0.00979  0.01639  0.02081  163 ALA B C   
2608 O O   . ALA B 165 ? 0.28605 0.25960 0.31352 0.01077  0.01552  0.01945  163 ALA B O   
2609 C CB  . ALA B 165 ? 0.23979 0.22766 0.25856 0.00421  0.02100  0.02863  163 ALA B CB  
2610 N N   . MET B 166 ? 0.30427 0.28737 0.32012 0.01092  0.01446  0.02239  164 MET B N   
2611 C CA  . MET B 166 ? 0.28800 0.26857 0.30708 0.01380  0.01160  0.02244  164 MET B CA  
2612 C C   . MET B 166 ? 0.30041 0.27988 0.32146 0.01529  0.01145  0.01559  164 MET B C   
2613 O O   . MET B 166 ? 0.29702 0.27389 0.32314 0.01780  0.01049  0.01461  164 MET B O   
2614 C CB  . MET B 166 ? 0.26895 0.25544 0.28331 0.01413  0.00893  0.02622  164 MET B CB  
2615 C CG  . MET B 166 ? 0.32495 0.31578 0.33523 0.01255  0.00851  0.03390  164 MET B CG  
2616 S SD  . MET B 166 ? 0.35828 0.34139 0.37814 0.01460  0.00778  0.04255  164 MET B SD  
2617 C CE  . MET B 166 ? 0.34450 0.32137 0.36795 0.01121  0.01150  0.04221  164 MET B CE  
2618 N N   . ASN B 167 ? 0.30357 0.28534 0.32095 0.01418  0.01248  0.01105  165 ASN B N   
2619 C CA  . ASN B 167 ? 0.31901 0.29982 0.33906 0.01539  0.01221  0.00640  165 ASN B CA  
2620 C C   . ASN B 167 ? 0.30971 0.28764 0.33501 0.01588  0.01339  0.00445  165 ASN B C   
2621 O O   . ASN B 167 ? 0.31498 0.29301 0.34287 0.01736  0.01277  0.00185  165 ASN B O   
2622 C CB  . ASN B 167 ? 0.29577 0.27797 0.31202 0.01453  0.01269  0.00271  165 ASN B CB  
2623 C CG  . ASN B 167 ? 0.35241 0.33646 0.36488 0.01361  0.01030  0.00258  165 ASN B CG  
2624 O OD1 . ASN B 167 ? 0.38308 0.36902 0.39771 0.01406  0.00813  0.00475  165 ASN B OD1 
2625 N ND2 . ASN B 167 ? 0.35889 0.34301 0.36614 0.01229  0.01064  -0.00042 165 ASN B ND2 
2626 N N   . GLY B 168 ? 0.33150 0.30805 0.35839 0.01414  0.01495  0.00575  166 GLY B N   
2627 C CA  . GLY B 168 ? 0.30785 0.28191 0.34006 0.01356  0.01526  0.00333  166 GLY B CA  
2628 C C   . GLY B 168 ? 0.35221 0.32077 0.38839 0.01520  0.01394  0.00314  166 GLY B C   
2629 O O   . GLY B 168 ? 0.35447 0.32173 0.39351 0.01584  0.01353  -0.00142 166 GLY B O   
2630 N N   . ILE B 169 ? 0.31785 0.28373 0.35424 0.01634  0.01320  0.00784  167 ILE B N   
2631 C CA  . ILE B 169 ? 0.32570 0.28627 0.36676 0.01962  0.01209  0.00758  167 ILE B CA  
2632 C C   . ILE B 169 ? 0.35309 0.31777 0.39397 0.02297  0.01173  0.00265  167 ILE B C   
2633 O O   . ILE B 169 ? 0.32616 0.28778 0.37085 0.02584  0.01174  -0.00119 167 ILE B O   
2634 C CB  . ILE B 169 ? 0.34902 0.30855 0.39044 0.02101  0.01098  0.01507  167 ILE B CB  
2635 C CG1 . ILE B 169 ? 0.30229 0.25752 0.34496 0.01739  0.01158  0.02094  167 ILE B CG1 
2636 C CG2 . ILE B 169 ? 0.36884 0.32453 0.41594 0.02619  0.00986  0.01524  167 ILE B CG2 
2637 C CD1 . ILE B 169 ? 0.34616 0.30108 0.38922 0.01865  0.01017  0.02988  167 ILE B CD1 
2638 N N   . LEU B 170 ? 0.30971 0.28144 0.34637 0.02255  0.01155  0.00254  168 LEU B N   
2639 C CA  . LEU B 170 ? 0.35550 0.33276 0.39237 0.02485  0.01132  -0.00031 168 LEU B CA  
2640 C C   . LEU B 170 ? 0.36462 0.34406 0.40091 0.02405  0.01205  -0.00525 168 LEU B C   
2641 O O   . LEU B 170 ? 0.34824 0.33343 0.38450 0.02577  0.01218  -0.00719 168 LEU B O   
2642 C CB  . LEU B 170 ? 0.32004 0.30327 0.35376 0.02383  0.01025  0.00246  168 LEU B CB  
2643 C CG  . LEU B 170 ? 0.33783 0.32249 0.37095 0.02398  0.00864  0.00749  168 LEU B CG  
2644 C CD1 . LEU B 170 ? 0.29646 0.28623 0.32572 0.02127  0.00717  0.00822  168 LEU B CD1 
2645 C CD2 . LEU B 170 ? 0.37576 0.36258 0.41427 0.02830  0.00807  0.00920  168 LEU B CD2 
2646 N N   . LEU B 171 ? 0.38072 0.35783 0.41670 0.02136  0.01245  -0.00659 169 LEU B N   
2647 C CA  . LEU B 171 ? 0.37538 0.35613 0.41133 0.02070  0.01245  -0.01075 169 LEU B CA  
2648 C C   . LEU B 171 ? 0.39457 0.37403 0.43254 0.02269  0.01240  -0.01580 169 LEU B C   
2649 O O   . LEU B 171 ? 0.40581 0.37765 0.44692 0.02335  0.01243  -0.01654 169 LEU B O   
2650 C CB  . LEU B 171 ? 0.39523 0.37528 0.43207 0.01748  0.01268  -0.01082 169 LEU B CB  
2651 C CG  . LEU B 171 ? 0.42988 0.41662 0.46651 0.01665  0.01217  -0.01270 169 LEU B CG  
2652 C CD1 . LEU B 171 ? 0.39994 0.39056 0.43426 0.01784  0.01219  -0.00983 169 LEU B CD1 
2653 C CD2 . LEU B 171 ? 0.37701 0.36427 0.41673 0.01361  0.01238  -0.01285 169 LEU B CD2 
2654 N N   . PRO B 172 ? 0.40297 0.38964 0.43919 0.02412  0.01244  -0.01911 170 PRO B N   
2655 C CA  . PRO B 172 ? 0.42550 0.41172 0.46256 0.02639  0.01275  -0.02578 170 PRO B CA  
2656 C C   . PRO B 172 ? 0.36165 0.34245 0.40029 0.02314  0.01165  -0.03055 170 PRO B C   
2657 O O   . PRO B 172 ? 0.43440 0.41717 0.47296 0.01933  0.01073  -0.02884 170 PRO B O   
2658 C CB  . PRO B 172 ? 0.42261 0.42114 0.45596 0.02774  0.01318  -0.02724 170 PRO B CB  
2659 C CG  . PRO B 172 ? 0.43618 0.43931 0.46781 0.02501  0.01236  -0.02139 170 PRO B CG  
2660 C CD  . PRO B 172 ? 0.38180 0.37739 0.41521 0.02395  0.01231  -0.01655 170 PRO B CD  
2661 N N   . ALA B 173 ? 0.32452 0.29802 0.36569 0.02473  0.01170  -0.03651 171 ALA B N   
2662 C CA  . ALA B 173 ? 0.45839 0.42411 0.50246 0.02093  0.01021  -0.04177 171 ALA B CA  
2663 C C   . ALA B 173 ? 0.41114 0.36982 0.45930 0.01638  0.00967  -0.03539 171 ALA B C   
2664 O O   . ALA B 173 ? 0.37593 0.33192 0.42690 0.01133  0.00823  -0.03765 171 ALA B O   
2665 C CB  . ALA B 173 ? 0.36231 0.33756 0.40278 0.01802  0.00867  -0.04769 171 ALA B CB  
2666 N N   . SER B 174 ? 0.43619 0.39333 0.48467 0.01771  0.01075  -0.02739 172 SER B N   
2667 C CA  . SER B 174 ? 0.43080 0.38276 0.48232 0.01379  0.01080  -0.02103 172 SER B CA  
2668 C C   . SER B 174 ? 0.45940 0.39809 0.51711 0.01235  0.01001  -0.02212 172 SER B C   
2669 O O   . SER B 174 ? 0.47440 0.40587 0.53420 0.01670  0.00992  -0.02551 172 SER B O   
2670 C CB  . SER B 174 ? 0.44646 0.40037 0.49564 0.01584  0.01186  -0.01315 172 SER B CB  
2671 O OG  . SER B 174 ? 0.48246 0.43258 0.53275 0.02083  0.01187  -0.01213 172 SER B OG  
2672 N N   . THR B 175 ? 0.44536 0.38080 0.50696 0.00635  0.00955  -0.01892 173 THR B N   
2673 C CA  . THR B 175 ? 0.45948 0.38091 0.52824 0.00353  0.00842  -0.01892 173 THR B CA  
2674 C C   . THR B 175 ? 0.42270 0.34321 0.49455 -0.00140 0.00917  -0.00838 173 THR B C   
2675 O O   . THR B 175 ? 0.37231 0.30369 0.44009 -0.00215 0.01078  -0.00315 173 THR B O   
2676 C CB  . THR B 175 ? 0.45801 0.37683 0.52951 -0.00080 0.00634  -0.02868 173 THR B CB  
2677 O OG1 . THR B 175 ? 0.56200 0.46447 0.64139 -0.00397 0.00489  -0.02934 173 THR B OG1 
2678 C CG2 . THR B 175 ? 0.43233 0.36323 0.50365 -0.00716 0.00591  -0.02738 173 THR B CG2 
2679 N N   . TYR B 176 ? 0.41068 0.31812 0.48986 -0.00466 0.00817  -0.00521 174 TYR B N   
2680 C CA  . TYR B 176 ? 0.41666 0.32350 0.49926 -0.00976 0.00903  0.00626  174 TYR B CA  
2681 C C   . TYR B 176 ? 0.41892 0.33362 0.49529 -0.00566 0.01091  0.01499  174 TYR B C   
2682 O O   . TYR B 176 ? 0.39137 0.31655 0.46472 -0.00876 0.01280  0.02136  174 TYR B O   
2683 C CB  . TYR B 176 ? 0.43166 0.34813 0.51631 -0.01766 0.00950  0.00683  174 TYR B CB  
2684 C CG  . TYR B 176 ? 0.44668 0.35435 0.53978 -0.02462 0.00698  0.00191  174 TYR B CG  
2685 C CD1 . TYR B 176 ? 0.46692 0.36090 0.56874 -0.02986 0.00594  0.00828  174 TYR B CD1 
2686 C CD2 . TYR B 176 ? 0.42384 0.33716 0.51651 -0.02666 0.00521  -0.00865 174 TYR B CD2 
2687 C CE1 . TYR B 176 ? 0.45556 0.34022 0.56593 -0.03747 0.00311  0.00317  174 TYR B CE1 
2688 C CE2 . TYR B 176 ? 0.42059 0.32669 0.52076 -0.03405 0.00223  -0.01410 174 TYR B CE2 
2689 C CZ  . TYR B 176 ? 0.45342 0.34457 0.56263 -0.03971 0.00116  -0.00873 174 TYR B CZ  
2690 O OH  . TYR B 176 ? 0.52824 0.41094 0.64553 -0.04806 -0.00233 -0.01502 174 TYR B OH  
2691 N N   . LEU B 177 ? 0.38419 0.29473 0.45881 0.00140  0.01036  0.01477  175 LEU B N   
2692 C CA  . LEU B 177 ? 0.41308 0.33257 0.48112 0.00523  0.01130  0.02107  175 LEU B CA  
2693 C C   . LEU B 177 ? 0.34523 0.26513 0.41389 0.00219  0.01175  0.03372  175 LEU B C   
2694 O O   . LEU B 177 ? 0.36079 0.26929 0.43672 0.00053  0.01065  0.03961  175 LEU B O   
2695 C CB  . LEU B 177 ? 0.39511 0.31139 0.46313 0.01303  0.01025  0.01883  175 LEU B CB  
2696 C CG  . LEU B 177 ? 0.44100 0.36233 0.50587 0.01621  0.01051  0.00783  175 LEU B CG  
2697 C CD1 . LEU B 177 ? 0.47467 0.39748 0.53935 0.02387  0.01015  0.00699  175 LEU B CD1 
2698 C CD2 . LEU B 177 ? 0.39561 0.32970 0.45361 0.01349  0.01166  0.00622  175 LEU B CD2 
2699 N N   . PRO B 178 ? 0.33297 0.26571 0.39394 0.00156  0.01329  0.03821  176 PRO B N   
2700 C CA  . PRO B 178 ? 0.40433 0.34019 0.46384 -0.00058 0.01370  0.05053  176 PRO B CA  
2701 C C   . PRO B 178 ? 0.39754 0.32650 0.45960 0.00455  0.01119  0.05676  176 PRO B C   
2702 O O   . PRO B 178 ? 0.42442 0.35332 0.48538 0.01057  0.00990  0.05174  176 PRO B O   
2703 C CB  . PRO B 178 ? 0.40122 0.35287 0.45016 -0.00064 0.01570  0.05014  176 PRO B CB  
2704 C CG  . PRO B 178 ? 0.38817 0.34185 0.43391 0.00345  0.01525  0.03954  176 PRO B CG  
2705 C CD  . PRO B 178 ? 0.35363 0.29794 0.40656 0.00362  0.01439  0.03215  176 PRO B CD  
2706 N N   . THR B 179 ? 0.42072 0.34420 0.48754 0.00217  0.01048  0.06844  177 THR B N   
2707 C CA  . THR B 179 ? 0.45309 0.37006 0.52407 0.00726  0.00782  0.07674  177 THR B CA  
2708 C C   . THR B 179 ? 0.43080 0.36260 0.49284 0.00778  0.00740  0.08622  177 THR B C   
2709 O O   . THR B 179 ? 0.40534 0.35035 0.45843 0.00351  0.00958  0.08696  177 THR B O   
2710 C CB  . THR B 179 ? 0.47547 0.37726 0.55740 0.00443  0.00669  0.08601  177 THR B CB  
2711 O OG1 . THR B 179 ? 0.46140 0.37055 0.54099 -0.00359 0.00850  0.09571  177 THR B OG1 
2712 C CG2 . THR B 179 ? 0.50039 0.38641 0.59112 0.00335  0.00649  0.07538  177 THR B CG2 
2713 N N   . TRP B 180 ? 0.44024 0.37040 0.50504 0.01332  0.00447  0.09349  178 TRP B N   
2714 C CA  . TRP B 180 ? 0.41931 0.36418 0.47586 0.01324  0.00314  0.10380  178 TRP B CA  
2715 C C   . TRP B 180 ? 0.41794 0.36718 0.47210 0.00631  0.00461  0.11607  178 TRP B C   
2716 O O   . TRP B 180 ? 0.38100 0.34660 0.42369 0.00299  0.00599  0.11867  178 TRP B O   
2717 C CB  . TRP B 180 ? 0.40894 0.35180 0.47119 0.02038  -0.00080 0.11148  178 TRP B CB  
2718 C CG  . TRP B 180 ? 0.37882 0.33500 0.43469 0.01900  -0.00288 0.12586  178 TRP B CG  
2719 C CD1 . TRP B 180 ? 0.42779 0.38020 0.48980 0.01975  -0.00524 0.14214  178 TRP B CD1 
2720 C CD2 . TRP B 180 ? 0.39676 0.37286 0.43823 0.01638  -0.00302 0.12540  178 TRP B CD2 
2721 N NE1 . TRP B 180 ? 0.39144 0.36232 0.44298 0.01774  -0.00695 0.15249  178 TRP B NE1 
2722 C CE2 . TRP B 180 ? 0.41583 0.40132 0.45427 0.01554  -0.00560 0.14148  178 TRP B CE2 
2723 C CE3 . TRP B 180 ? 0.39206 0.37831 0.42308 0.01468  -0.00144 0.11284  178 TRP B CE3 
2724 C CZ2 . TRP B 180 ? 0.39261 0.39854 0.41661 0.01275  -0.00658 0.14411  178 TRP B CZ2 
2725 C CZ3 . TRP B 180 ? 0.40058 0.40470 0.41833 0.01207  -0.00236 0.11503  178 TRP B CZ3 
2726 C CH2 . TRP B 180 ? 0.37923 0.39352 0.39305 0.01106  -0.00492 0.12986  178 TRP B CH2 
2727 N N   . GLU B 181 ? 0.43130 0.36633 0.49623 0.00371  0.00454  0.12327  179 GLU B N   
2728 C CA  . GLU B 181 ? 0.48690 0.42713 0.55068 -0.00378 0.00621  0.13640  179 GLU B CA  
2729 C C   . GLU B 181 ? 0.48003 0.43295 0.53570 -0.01011 0.01073  0.12959  179 GLU B C   
2730 O O   . GLU B 181 ? 0.46120 0.42951 0.50891 -0.01461 0.01293  0.13810  179 GLU B O   
2731 C CB  . GLU B 181 ? 0.50204 0.42249 0.58066 -0.00646 0.00514  0.14449  179 GLU B CB  
2732 C CG  . GLU B 181 ? 0.50104 0.40781 0.58921 0.00108  0.00091  0.15145  179 GLU B CG  
2733 C CD  . GLU B 181 ? 0.51981 0.42310 0.61384 -0.00197 -0.00079 0.17236  179 GLU B CD  
2734 O OE1 . GLU B 181 ? 0.50446 0.41023 0.59874 -0.01110 0.00157  0.17980  179 GLU B OE1 
2735 O OE2 . GLU B 181 ? 0.50564 0.40514 0.60453 0.00465  -0.00447 0.18251  179 GLU B OE2 
2736 N N   . ASP B 182 ? 0.43294 0.38131 0.49022 -0.00990 0.01225  0.11436  180 ASP B N   
2737 C CA  . ASP B 182 ? 0.46926 0.43024 0.51999 -0.01427 0.01635  0.10720  180 ASP B CA  
2738 C C   . ASP B 182 ? 0.45248 0.43173 0.48871 -0.01222 0.01760  0.10521  180 ASP B C   
2739 O O   . ASP B 182 ? 0.40749 0.40132 0.43663 -0.01619 0.02122  0.10765  180 ASP B O   
2740 C CB  . ASP B 182 ? 0.43041 0.38403 0.48523 -0.01306 0.01674  0.09171  180 ASP B CB  
2741 C CG  . ASP B 182 ? 0.47113 0.40807 0.53910 -0.01641 0.01560  0.09123  180 ASP B CG  
2742 O OD1 . ASP B 182 ? 0.51883 0.45127 0.59315 -0.02160 0.01552  0.10305  180 ASP B OD1 
2743 O OD2 . ASP B 182 ? 0.46043 0.38897 0.53222 -0.01429 0.01464  0.07918  180 ASP B OD2 
2744 N N   . ILE B 183 ? 0.36502 0.34413 0.39705 -0.00615 0.01473  0.10004  181 ILE B N   
2745 C CA  . ILE B 183 ? 0.38958 0.38370 0.40842 -0.00456 0.01512  0.09536  181 ILE B CA  
2746 C C   . ILE B 183 ? 0.45201 0.45931 0.46248 -0.00629 0.01443  0.10798  181 ILE B C   
2747 O O   . ILE B 183 ? 0.46548 0.48810 0.46377 -0.00789 0.01654  0.10556  181 ILE B O   
2748 C CB  . ILE B 183 ? 0.41724 0.40716 0.43604 0.00132  0.01182  0.08666  181 ILE B CB  
2749 C CG1 . ILE B 183 ? 0.38702 0.36942 0.41012 0.00234  0.01333  0.07335  181 ILE B CG1 
2750 C CG2 . ILE B 183 ? 0.39162 0.39571 0.39783 0.00224  0.01067  0.08405  181 ILE B CG2 
2751 C CD1 . ILE B 183 ? 0.35895 0.35096 0.37409 0.00036  0.01669  0.06502  181 ILE B CD1 
2752 N N   . GLU B 184 ? 0.43715 0.43904 0.45384 -0.00571 0.01137  0.12154  182 GLU B N   
2753 C CA  . GLU B 184 ? 0.43810 0.45386 0.44694 -0.00755 0.01023  0.13567  182 GLU B CA  
2754 C C   . GLU B 184 ? 0.45730 0.48445 0.46119 -0.01430 0.01517  0.14198  182 GLU B C   
2755 O O   . GLU B 184 ? 0.46794 0.51329 0.45952 -0.01632 0.01600  0.14823  182 GLU B O   
2756 C CB  . GLU B 184 ? 0.39639 0.40256 0.41529 -0.00505 0.00584  0.15043  182 GLU B CB  
2757 C CG  . GLU B 184 ? 0.45297 0.47553 0.46311 -0.00585 0.00329  0.16581  182 GLU B CG  
2758 C CD  . GLU B 184 ? 0.46948 0.48248 0.49112 -0.00355 -0.00082 0.18344  182 GLU B CD  
2759 O OE1 . GLU B 184 ? 0.51596 0.50810 0.55273 -0.00225 -0.00101 0.18416  182 GLU B OE1 
2760 O OE2 . GLU B 184 ? 0.58435 0.61070 0.60003 -0.00285 -0.00417 0.19662  182 GLU B OE2 
2761 N N   . SER B 185 ? 0.50200 0.52038 0.51524 -0.01804 0.01846  0.14019  183 SER B N   
2762 C CA  . SER B 185 ? 0.50999 0.54081 0.52053 -0.02468 0.02382  0.14526  183 SER B CA  
2763 C C   . SER B 185 ? 0.51399 0.56110 0.51204 -0.02415 0.02819  0.13244  183 SER B C   
2764 O O   . SER B 185 ? 0.54010 0.60619 0.52773 -0.02693 0.03179  0.13720  183 SER B O   
2765 C CB  . SER B 185 ? 0.49607 0.51322 0.52163 -0.02916 0.02538  0.14568  183 SER B CB  
2766 O OG  . SER B 185 ? 0.53462 0.53535 0.57202 -0.02994 0.02153  0.15774  183 SER B OG  
2767 N N   . LEU B 186 ? 0.48530 0.52532 0.48468 -0.02050 0.02823  0.11629  184 LEU B N   
2768 C CA  . LEU B 186 ? 0.50217 0.55444 0.49023 -0.01844 0.03135  0.10347  184 LEU B CA  
2769 C C   . LEU B 186 ? 0.51137 0.57836 0.48394 -0.01726 0.03025  0.10537  184 LEU B C   
2770 O O   . LEU B 186 ? 0.52303 0.60667 0.48464 -0.01846 0.03456  0.10262  184 LEU B O   
2771 C CB  . LEU B 186 ? 0.49209 0.53247 0.48347 -0.01379 0.02940  0.08843  184 LEU B CB  
2772 C CG  . LEU B 186 ? 0.54363 0.59183 0.52927 -0.01224 0.03350  0.07512  184 LEU B CG  
2773 C CD1 . LEU B 186 ? 0.52860 0.59070 0.51375 -0.01611 0.03965  0.07914  184 LEU B CD1 
2774 C CD2 . LEU B 186 ? 0.43798 0.47348 0.43206 -0.00952 0.03249  0.06421  184 LEU B CD2 
2775 N N   . TYR B 187 ? 0.48153 0.54352 0.45314 -0.01464 0.02440  0.10921  185 TYR B N   
2776 C CA  . TYR B 187 ? 0.52289 0.59957 0.48018 -0.01410 0.02199  0.11148  185 TYR B CA  
2777 C C   . TYR B 187 ? 0.50748 0.60123 0.45717 -0.01846 0.02434  0.12586  185 TYR B C   
2778 O O   . TYR B 187 ? 0.55547 0.66725 0.49065 -0.01972 0.02739  0.12208  185 TYR B O   
2779 C CB  . TYR B 187 ? 0.51697 0.58609 0.47794 -0.01063 0.01490  0.11533  185 TYR B CB  
2780 C CG  . TYR B 187 ? 0.55110 0.63622 0.49804 -0.01052 0.01122  0.11715  185 TYR B CG  
2781 C CD1 . TYR B 187 ? 0.57384 0.66654 0.50902 -0.01007 0.01128  0.10260  185 TYR B CD1 
2782 C CD2 . TYR B 187 ? 0.56815 0.66064 0.51406 -0.01107 0.00719  0.13367  185 TYR B CD2 
2783 C CE1 . TYR B 187 ? 0.60281 0.71058 0.52478 -0.01089 0.00720  0.10330  185 TYR B CE1 
2784 C CE2 . TYR B 187 ? 0.58959 0.69885 0.52235 -0.01143 0.00309  0.13573  185 TYR B CE2 
2785 C CZ  . TYR B 187 ? 0.60573 0.72287 0.52621 -0.01169 0.00298  0.11998  185 TYR B CZ  
2786 O OH  . TYR B 187 ? 0.64883 0.78328 0.55582 -0.01294 -0.00178 0.12133  185 TYR B OH  
2787 N N   . GLY B 188 ? 0.50920 0.59773 0.46831 -0.02075 0.02288  0.14268  186 GLY B N   
2788 C CA  . GLY B 188 ? 0.47349 0.57886 0.42525 -0.02484 0.02372  0.15957  186 GLY B CA  
2789 C C   . GLY B 188 ? 0.52056 0.64128 0.46759 -0.02990 0.03142  0.16143  186 GLY B C   
2790 O O   . GLY B 188 ? 0.46357 0.60399 0.40004 -0.03321 0.03315  0.17284  186 GLY B O   
2791 N N   . GLU B 189 ? 0.47098 0.58500 0.42593 -0.03054 0.03609  0.15127  187 GLU B N   
2792 C CA  . GLU B 189 ? 0.51701 0.64693 0.47016 -0.03507 0.04379  0.15337  187 GLU B CA  
2793 C C   . GLU B 189 ? 0.53810 0.69011 0.47306 -0.03327 0.04839  0.14277  187 GLU B C   
2794 O O   . GLU B 189 ? 0.52571 0.69609 0.45672 -0.03635 0.05536  0.14547  187 GLU B O   
2795 C CB  . GLU B 189 ? 0.48821 0.60597 0.45592 -0.03580 0.04676  0.14490  187 GLU B CB  
2796 N N   . GLN B 190 ? 0.56028 0.71131 0.48454 -0.02857 0.04461  0.13101  188 GLN B N   
2797 C CA  . GLN B 190 ? 0.56956 0.73521 0.47808 -0.02587 0.04822  0.11559  188 GLN B CA  
2798 C C   . GLN B 190 ? 0.60334 0.79579 0.49577 -0.02911 0.05147  0.12490  188 GLN B C   
2799 O O   . GLN B 190 ? 0.61538 0.81359 0.50245 -0.03125 0.04667  0.13868  188 GLN B O   
2800 C CB  . GLN B 190 ? 0.59402 0.74913 0.49744 -0.02163 0.04162  0.10354  188 GLN B CB  
2801 C CG  . GLN B 190 ? 0.55781 0.69814 0.46745 -0.01742 0.04249  0.08527  188 GLN B CG  
2802 C CD  . GLN B 190 ? 0.56179 0.69787 0.46268 -0.01434 0.03764  0.07191  188 GLN B CD  
2803 O OE1 . GLN B 190 ? 0.56159 0.70470 0.45165 -0.01251 0.04032  0.05788  188 GLN B OE1 
2804 N NE2 . GLN B 190 ? 0.56879 0.69371 0.47484 -0.01385 0.03032  0.07644  188 GLN B NE2 
2805 N N   . PHE B 191 ? 0.58375 0.79410 0.46881 -0.02916 0.05978  0.11812  189 PHE B N   
2806 C CA  . PHE B 191 ? 0.62882 0.86709 0.50076 -0.03309 0.06453  0.12965  189 PHE B CA  
2807 C C   . PHE B 191 ? 0.64602 0.89709 0.49859 -0.03304 0.05951  0.13088  189 PHE B C   
2808 O O   . PHE B 191 ? 0.65119 0.91911 0.49653 -0.03735 0.05890  0.14864  189 PHE B O   
2809 C CB  . PHE B 191 ? 0.61440 0.87116 0.48075 -0.03152 0.07476  0.11863  189 PHE B CB  
2810 N N   . HIS B 192 ? 0.67090 0.91481 0.51521 -0.02876 0.05540  0.11298  190 HIS B N   
2811 C CA  . HIS B 192 ? 0.66801 0.92540 0.49379 -0.02944 0.04995  0.11274  190 HIS B CA  
2812 C C   . HIS B 192 ? 0.64662 0.89921 0.47767 -0.03197 0.04128  0.13258  190 HIS B C   
2813 O O   . HIS B 192 ? 0.60003 0.86938 0.41650 -0.03380 0.03682  0.13917  190 HIS B O   
2814 C CB  . HIS B 192 ? 0.70059 0.94829 0.51951 -0.02525 0.04683  0.08909  190 HIS B CB  
2815 C CG  . HIS B 192 ? 0.70881 0.93467 0.53787 -0.02403 0.03745  0.08861  190 HIS B CG  
2816 N ND1 . HIS B 192 ? 0.72322 0.95414 0.54601 -0.02581 0.02888  0.09683  190 HIS B ND1 
2817 C CD2 . HIS B 192 ? 0.65770 0.85863 0.50308 -0.02110 0.03549  0.08150  190 HIS B CD2 
2818 C CE1 . HIS B 192 ? 0.65593 0.86613 0.49136 -0.02376 0.02248  0.09432  190 HIS B CE1 
2819 N NE2 . HIS B 192 ? 0.65997 0.85173 0.50862 -0.02101 0.02646  0.08505  190 HIS B NE2 
2820 N N   . HIS B 193 ? 0.65679 0.88726 0.50856 -0.03174 0.03868  0.14184  191 HIS B N   
2821 C CA  . HIS B 193 ? 0.62694 0.85136 0.48674 -0.03315 0.03143  0.16186  191 HIS B CA  
2822 C C   . HIS B 193 ? 0.60595 0.84763 0.46362 -0.03828 0.03402  0.18490  191 HIS B C   
2823 O O   . HIS B 193 ? 0.64583 0.88426 0.50977 -0.03879 0.02735  0.20026  191 HIS B O   
2824 C CB  . HIS B 193 ? 0.60917 0.80420 0.49179 -0.03098 0.02889  0.16294  191 HIS B CB  
2825 C CG  . HIS B 193 ? 0.60712 0.78570 0.49324 -0.02623 0.02329  0.14775  191 HIS B CG  
2826 N ND1 . HIS B 193 ? 0.64270 0.82952 0.51687 -0.02492 0.01718  0.14256  191 HIS B ND1 
2827 C CD2 . HIS B 193 ? 0.60273 0.75881 0.50279 -0.02307 0.02290  0.13683  191 HIS B CD2 
2828 C CE1 . HIS B 193 ? 0.64960 0.81928 0.53124 -0.02137 0.01349  0.12976  191 HIS B CE1 
2829 N NE2 . HIS B 193 ? 0.59664 0.74774 0.49352 -0.01993 0.01702  0.12627  191 HIS B NE2 
2830 N N   . HIS B 194 ? 0.58160 0.83588 0.43693 -0.04066 0.04227  0.18235  192 HIS B N   
2831 C CA  . HIS B 194 ? 0.62345 0.88660 0.48500 -0.04505 0.04407  0.19896  192 HIS B CA  
2832 C C   . HIS B 194 ? 0.58954 0.87995 0.43419 -0.04617 0.04733  0.19513  192 HIS B C   
2833 O O   . HIS B 194 ? 0.59374 0.89544 0.44188 -0.05000 0.05000  0.20778  192 HIS B O   
2834 C CB  . HIS B 194 ? 0.55236 0.80633 0.43031 -0.04793 0.05057  0.20289  192 HIS B CB  
2835 C CG  . HIS B 194 ? 0.52694 0.75370 0.42224 -0.04726 0.04728  0.20663  192 HIS B CG  
2836 N ND1 . HIS B 194 ? 0.51299 0.72329 0.42209 -0.04830 0.04058  0.22286  192 HIS B ND1 
2837 C CD2 . HIS B 194 ? 0.54732 0.75655 0.45048 -0.04394 0.04814  0.19137  192 HIS B CD2 
2838 C CE1 . HIS B 194 ? 0.48370 0.67007 0.40660 -0.04657 0.03873  0.22024  192 HIS B CE1 
2839 N NE2 . HIS B 194 ? 0.51937 0.70291 0.44036 -0.04347 0.04239  0.19844  192 HIS B NE2 
2840 N N   . HIS B 195 ? 0.60667 0.90769 0.43339 -0.04317 0.04682  0.17802  193 HIS B N   
2841 C CA  . HIS B 195 ? 0.62447 0.95071 0.43416 -0.04384 0.04931  0.17252  193 HIS B CA  
2842 C C   . HIS B 195 ? 0.66182 0.99401 0.45901 -0.04309 0.04048  0.17066  193 HIS B C   
2843 O O   . HIS B 195 ? 0.70307 1.02913 0.49240 -0.04029 0.03736  0.15470  193 HIS B O   
2844 C CB  . HIS B 195 ? 0.62404 0.95784 0.42443 -0.04087 0.05787  0.15066  193 HIS B CB  
2845 C CG  . HIS B 195 ? 0.64411 0.97634 0.45752 -0.04169 0.06663  0.15299  193 HIS B CG  
2846 N ND1 . HIS B 195 ? 0.57905 0.92028 0.40148 -0.04625 0.06952  0.17050  193 HIS B ND1 
2847 C CD2 . HIS B 195 ? 0.61402 0.93660 0.43458 -0.03884 0.07253  0.14074  193 HIS B CD2 
2848 C CE1 . HIS B 195 ? 0.52941 0.86733 0.36366 -0.04654 0.07671  0.16834  193 HIS B CE1 
2849 N NE2 . HIS B 195 ? 0.58833 0.91540 0.42191 -0.04184 0.07874  0.15056  193 HIS B NE2 
2850 N N   . HIS B 196 ? 0.70767 1.05217 0.50400 -0.04590 0.03621  0.18722  194 HIS B N   
2851 C CA  . HIS B 196 ? 0.68933 1.04082 0.47678 -0.04568 0.02714  0.18877  194 HIS B CA  
2852 C C   . HIS B 196 ? 0.67953 1.05662 0.45732 -0.04876 0.02691  0.19841  194 HIS B C   
2853 O O   . HIS B 196 ? 0.73474 1.13066 0.49707 -0.04917 0.03183  0.18637  194 HIS B O   
2854 C CB  . HIS B 196 ? 0.69538 1.02808 0.49878 -0.04472 0.01893  0.20375  194 HIS B CB  
2855 O O   . HOH C .   ? 0.50655 0.71592 0.46780 0.02141  0.01009  -0.00119 201 HOH A O   
2856 O O   . HOH C .   ? 0.51815 0.41506 0.62758 -0.04040 0.01071  0.05038  202 HOH A O   
2857 O O   . HOH C .   ? 0.48164 0.47552 0.46676 0.03215  0.03918  -0.04739 203 HOH A O   
2858 O O   . HOH C .   ? 0.54767 0.68226 0.55759 0.01466  0.00561  0.05099  204 HOH A O   
2859 O O   . HOH C .   ? 0.49593 0.42454 0.62116 -0.06557 0.01339  0.05481  205 HOH A O   
2860 O O   . HOH C .   ? 0.50408 0.45561 0.58957 -0.04456 -0.01480 -0.07348 206 HOH A O   
2861 O O   . HOH C .   ? 0.60780 0.70467 0.68674 -0.07338 0.05934  0.13892  207 HOH A O   
2862 O O   . HOH C .   ? 0.32982 0.56282 0.53939 -0.06538 0.03163  0.04370  208 HOH A O   
2863 O O   . HOH C .   ? 0.54668 0.53582 0.61119 0.02460  -0.00310 0.05238  209 HOH A O   
2864 O O   . HOH C .   ? 0.50351 0.57298 0.46919 0.04136  0.07031  -0.05348 210 HOH A O   
2865 O O   . HOH C .   ? 0.51572 0.55321 0.53238 0.03910  0.01828  -0.06190 211 HOH A O   
2866 O O   . HOH C .   ? 0.54939 0.62842 0.72489 -0.11223 0.03307  0.08814  212 HOH A O   
2867 O O   . HOH C .   ? 0.50913 0.71191 0.57446 0.04194  -0.04367 0.14504  213 HOH A O   
2868 O O   . HOH C .   ? 0.36117 0.41221 0.40424 0.02464  -0.00082 0.01884  214 HOH A O   
2869 O O   . HOH C .   ? 0.29986 0.61160 0.50871 -0.01350 0.07694  0.04988  215 HOH A O   
2870 O O   . HOH C .   ? 0.58475 0.69301 0.56579 0.07479  0.04087  -0.14075 216 HOH A O   
2871 O O   . HOH C .   ? 0.40339 0.54017 0.46675 0.02043  -0.02090 0.02068  217 HOH A O   
2872 O O   . HOH C .   ? 0.34583 0.34270 0.33060 0.01183  0.02135  -0.00997 218 HOH A O   
2873 O O   . HOH C .   ? 0.40173 0.40492 0.43754 0.01535  0.00858  -0.02383 219 HOH A O   
2874 O O   . HOH C .   ? 0.49804 0.52561 0.59268 0.05880  0.01728  0.00920  220 HOH A O   
2875 O O   . HOH C .   ? 0.51360 0.47942 0.55146 0.02196  0.00896  0.00025  221 HOH A O   
2876 O O   . HOH C .   ? 0.34779 0.36805 0.40489 0.02938  -0.00175 0.04199  222 HOH A O   
2877 O O   . HOH C .   ? 0.51552 0.49621 0.64955 -0.08732 0.02736  0.10344  223 HOH A O   
2878 O O   . HOH C .   ? 0.41157 0.55261 0.51144 -0.05013 -0.03646 -0.04458 224 HOH A O   
2879 O O   . HOH C .   ? 0.55253 0.84300 0.61511 -0.02140 -0.06899 -0.00427 225 HOH A O   
2880 O O   . HOH C .   ? 0.47661 0.55127 0.53901 -0.04592 -0.03236 -0.07994 226 HOH A O   
2881 O O   . HOH C .   ? 0.47828 0.48184 0.54738 -0.04068 -0.01973 -0.07997 227 HOH A O   
2882 O O   . HOH C .   ? 0.35390 0.51035 0.52985 -0.07021 0.00085  0.00983  228 HOH A O   
2883 O O   . HOH C .   ? 0.35286 0.47178 0.47870 0.03865  0.02618  0.00807  229 HOH A O   
2884 O O   . HOH C .   ? 0.42860 0.63105 0.43127 -0.02645 -0.04858 -0.06737 230 HOH A O   
2885 O O   . HOH C .   ? 0.50606 0.64835 0.50756 0.03342  0.02620  -0.01003 231 HOH A O   
2886 O O   . HOH C .   ? 0.50579 0.54988 0.51307 0.03728  0.01642  -0.08073 232 HOH A O   
2887 O O   . HOH C .   ? 0.49615 0.47291 0.50116 0.01199  0.01088  -0.01013 233 HOH A O   
2888 O O   . HOH C .   ? 0.39255 0.41035 0.44397 0.02852  0.00251  0.02338  234 HOH A O   
2889 O O   . HOH C .   ? 0.47534 0.52590 0.51624 0.01896  -0.00106 0.05006  235 HOH A O   
2890 O O   . HOH C .   ? 0.53950 0.54669 0.61069 0.04070  0.00140  0.03254  236 HOH A O   
2891 O O   . HOH C .   ? 0.37736 0.64647 0.59366 -0.03632 0.00160  0.02501  237 HOH A O   
2892 O O   . HOH C .   ? 0.29873 0.30477 0.33525 0.01940  0.00990  -0.00566 238 HOH A O   
2893 O O   . HOH C .   ? 0.44793 0.55041 0.46683 0.03231  0.02315  -0.00562 239 HOH A O   
2894 O O   . HOH C .   ? 0.46619 0.68173 0.39091 -0.01198 -0.03170 -0.13297 240 HOH A O   
2895 O O   . HOH C .   ? 0.58169 0.61092 0.59782 0.05181  0.02328  -0.09315 241 HOH A O   
2896 O O   . HOH C .   ? 0.48315 0.54311 0.49992 0.07314  0.03619  -0.10344 242 HOH A O   
2897 O O   . HOH C .   ? 0.56470 0.50971 0.69319 -0.08176 0.02402  0.13299  243 HOH A O   
2898 O O   . HOH C .   ? 0.48489 0.83709 0.36425 0.01827  0.00614  -0.03896 244 HOH A O   
2899 O O   . HOH C .   ? 0.34378 0.52641 0.40664 0.03921  -0.03692 0.11087  245 HOH A O   
2900 O O   . HOH C .   ? 0.46406 0.41955 0.61438 -0.09099 -0.00003 0.01465  246 HOH A O   
2901 O O   . HOH C .   ? 0.39304 0.47755 0.40380 0.05332  0.07775  -0.04511 247 HOH A O   
2902 O O   . HOH C .   ? 0.41094 0.38259 0.47688 -0.00989 0.01085  -0.01207 248 HOH A O   
2903 O O   . HOH C .   ? 0.43253 0.55182 0.49621 0.02919  -0.01734 0.03533  249 HOH A O   
2904 O O   . HOH C .   ? 0.58024 1.09327 0.52708 -0.02589 -0.10854 0.04787  250 HOH A O   
2905 O O   . HOH C .   ? 0.46729 0.45233 0.46611 0.01295  0.01655  -0.00848 251 HOH A O   
2906 O O   . HOH C .   ? 0.40074 0.40252 0.52604 -0.07165 -0.01006 -0.02752 252 HOH A O   
2907 O O   . HOH C .   ? 0.45636 0.41726 0.50445 0.00720  0.01433  -0.00060 253 HOH A O   
2908 O O   . HOH C .   ? 0.45095 0.46602 0.49998 -0.02765 -0.01814 -0.08807 254 HOH A O   
2909 O O   . HOH C .   ? 0.39534 0.45935 0.44770 0.01643  -0.00248 -0.00291 255 HOH A O   
2910 O O   . HOH C .   ? 0.39875 0.45411 0.43050 0.05321  0.06425  -0.03820 256 HOH A O   
2911 O O   . HOH C .   ? 0.54471 0.91351 0.63162 0.00968  -0.08445 0.06870  257 HOH A O   
2912 O O   . HOH C .   ? 0.40631 0.67870 0.59065 -0.04418 -0.03801 0.00508  258 HOH A O   
2913 O O   . HOH C .   ? 0.47084 0.85021 0.38432 0.00675  -0.00724 0.09049  259 HOH A O   
2914 O O   . HOH C .   ? 0.37513 0.39569 0.42238 0.01004  0.00636  -0.01667 260 HOH A O   
2915 O O   . HOH C .   ? 0.54929 0.96568 0.37773 -0.02489 -0.05061 -0.13989 261 HOH A O   
2916 O O   . HOH C .   ? 0.51903 0.51597 0.43225 -0.00121 0.00943  -0.07595 262 HOH A O   
2917 O O   . HOH C .   ? 0.66449 1.18761 0.59272 -0.00798 -0.08818 0.11380  263 HOH A O   
2918 O O   . HOH C .   ? 0.46648 0.75894 0.36459 0.02509  0.01207  -0.06905 264 HOH A O   
2919 O O   . HOH C .   ? 0.35227 0.54416 0.43636 0.04731  -0.04140 0.11013  265 HOH A O   
2920 O O   . HOH C .   ? 0.53558 0.70740 0.51798 0.02601  0.09759  -0.00707 266 HOH A O   
2921 O O   . HOH C .   ? 0.53922 0.51375 0.57409 0.02741  0.01691  -0.00983 267 HOH A O   
2922 O O   . HOH C .   ? 0.32232 0.37817 0.37697 0.02379  -0.00049 0.00777  268 HOH A O   
2923 O O   . HOH C .   ? 0.49855 0.83861 0.41874 0.01094  -0.00087 0.05640  269 HOH A O   
2924 O O   . HOH C .   ? 0.58613 0.46937 0.69458 -0.05062 -0.01354 -0.06678 270 HOH A O   
2925 O O   . HOH C .   ? 0.42210 0.55543 0.50228 0.04597  -0.03085 0.11942  271 HOH A O   
2926 O O   . HOH C .   ? 0.55626 0.52140 0.72139 -0.10496 0.00656  0.04465  272 HOH A O   
2927 O O   . HOH C .   ? 0.44987 0.47687 0.50787 0.00559  0.00728  -0.01445 273 HOH A O   
2928 O O   . HOH C .   ? 0.62840 1.07818 0.44371 -0.01667 -0.04049 -0.12218 274 HOH A O   
2929 O O   . HOH C .   ? 0.57038 0.87082 0.51172 0.01243  0.00577  0.05989  275 HOH A O   
2930 O O   . HOH C .   ? 0.33447 0.62902 0.55903 -0.01241 -0.00076 0.03043  276 HOH A O   
2931 O O   . HOH C .   ? 0.66336 0.65478 0.70772 0.06809  0.02695  -0.08524 277 HOH A O   
2932 O O   . HOH C .   ? 0.53272 0.56221 0.55703 0.04878  0.02262  -0.06602 278 HOH A O   
2933 O O   . HOH C .   ? 0.49782 0.71755 0.65750 -0.06032 -0.03878 -0.01546 279 HOH A O   
2934 O O   . HOH C .   ? 0.41616 0.58578 0.48779 0.02109  -0.02934 0.02977  280 HOH A O   
2935 O O   . HOH C .   ? 0.60745 0.53493 0.75140 -0.08258 0.00803  0.04516  281 HOH A O   
2936 O O   . HOH C .   ? 0.33230 0.64694 0.52781 -0.03990 -0.04801 0.01304  282 HOH A O   
2937 O O   . HOH C .   ? 0.53259 0.58386 0.54372 0.08238  0.03932  -0.13693 283 HOH A O   
2938 O O   . HOH C .   ? 0.48322 0.68565 0.56587 -0.08252 0.08757  0.15398  284 HOH A O   
2939 O O   . HOH C .   ? 0.74895 0.99872 0.71145 -0.03700 0.10122  0.11472  285 HOH A O   
2940 O O   . HOH D .   ? 0.47810 0.49089 0.53285 -0.04438 -0.02685 0.01913  201 HOH B O   
2941 O O   . HOH D .   ? 0.48795 0.59055 0.47886 0.01742  -0.03552 0.20085  202 HOH B O   
2942 O O   . HOH D .   ? 0.39107 0.52489 0.48208 0.02180  -0.02315 0.05524  203 HOH B O   
2943 O O   . HOH D .   ? 0.48291 0.43204 0.55215 -0.01063 0.01194  -0.00231 204 HOH B O   
2944 O O   . HOH D .   ? 0.40077 0.52252 0.38185 -0.01604 -0.05191 0.04716  205 HOH B O   
2945 O O   . HOH D .   ? 0.57487 0.50072 0.65957 -0.03030 0.01468  0.13188  206 HOH B O   
2946 O O   . HOH D .   ? 0.43963 0.43098 0.46003 0.01275  0.00427  0.00439  207 HOH B O   
2947 O O   . HOH D .   ? 0.52492 0.56330 0.43025 0.00132  0.01873  -0.04611 208 HOH B O   
2948 O O   . HOH D .   ? 0.41582 0.72013 0.61608 -0.09366 -0.03258 0.11688  209 HOH B O   
2949 O O   . HOH D .   ? 0.39516 0.77255 0.62762 -0.10595 -0.01878 0.14964  210 HOH B O   
2950 O O   . HOH D .   ? 0.43599 0.61696 0.48148 0.01442  -0.06486 0.10280  211 HOH B O   
2951 O O   . HOH D .   ? 0.45648 0.44740 0.47485 -0.03404 -0.02676 -0.00809 212 HOH B O   
2952 O O   . HOH D .   ? 0.49420 0.45056 0.55135 0.00167  0.01096  -0.01428 213 HOH B O   
2953 O O   . HOH D .   ? 0.44064 0.42553 0.49074 0.00731  -0.00002 0.03563  214 HOH B O   
2954 O O   . HOH D .   ? 0.39533 0.45441 0.44138 0.05677  0.02733  -0.02766 215 HOH B O   
2955 O O   . HOH D .   ? 0.36911 0.32110 0.43341 -0.01017 0.01651  0.01840  216 HOH B O   
2956 O O   . HOH D .   ? 0.40206 0.54260 0.54813 -0.09903 -0.01841 0.12363  217 HOH B O   
2957 O O   . HOH D .   ? 0.22348 0.58638 0.42673 0.00679  0.00574  0.09817  218 HOH B O   
2958 O O   . HOH D .   ? 0.44295 0.40736 0.43451 -0.02933 -0.02310 -0.03390 219 HOH B O   
2959 O O   . HOH D .   ? 0.30260 0.83930 0.43436 -0.02425 0.07235  0.16667  220 HOH B O   
2960 O O   . HOH D .   ? 0.42251 0.60477 0.60015 -0.12691 -0.02570 0.14181  221 HOH B O   
2961 O O   . HOH D .   ? 0.45685 0.41734 0.50517 0.03050  0.01264  -0.01478 222 HOH B O   
2962 O O   . HOH D .   ? 0.49416 0.38810 0.57404 0.00971  0.00807  -0.00511 223 HOH B O   
2963 O O   . HOH D .   ? 0.42144 0.42235 0.45495 0.02444  0.01157  -0.00384 224 HOH B O   
2964 O O   . HOH D .   ? 0.42547 0.41352 0.46171 -0.03184 -0.02163 0.00476  225 HOH B O   
2965 O O   . HOH D .   ? 0.23084 0.74234 0.48711 -0.01634 0.02008  0.14085  226 HOH B O   
2966 O O   . HOH D .   ? 0.44523 0.55609 0.52568 0.04239  -0.03074 0.07803  227 HOH B O   
2967 O O   . HOH D .   ? 0.24025 0.55132 0.39948 0.05270  0.03645  0.05917  228 HOH B O   
2968 O O   . HOH D .   ? 0.53792 0.68472 0.46883 -0.03172 0.02064  0.20106  229 HOH B O   
2969 O O   . HOH D .   ? 0.47314 0.44212 0.53416 0.00892  -0.00994 0.20738  230 HOH B O   
2970 O O   . HOH D .   ? 0.50923 0.46416 0.54711 -0.04444 -0.02806 -0.00542 231 HOH B O   
2971 O O   . HOH D .   ? 0.48281 0.64572 0.44284 -0.00378 -0.05858 0.10009  232 HOH B O   
2972 O O   . HOH D .   ? 0.44171 0.71936 0.65233 -0.13435 -0.02416 0.15523  233 HOH B O   
2973 O O   . HOH D .   ? 0.43508 0.50643 0.46524 0.01537  0.00319  0.04495  234 HOH B O   
2974 O O   . HOH D .   ? 0.47338 0.44180 0.53195 -0.00354 -0.00460 0.04238  235 HOH B O   
2975 O O   . HOH D .   ? 0.49931 0.59346 0.54052 0.03779  -0.03984 0.11941  236 HOH B O   
2976 O O   . HOH D .   ? 0.43827 0.42702 0.43305 0.00632  0.00416  -0.00432 237 HOH B O   
2977 O O   . HOH D .   ? 0.51015 0.60597 0.57957 0.07497  0.03457  -0.02158 238 HOH B O   
2978 O O   . HOH D .   ? 0.33908 0.47099 0.44959 -0.05490 -0.02307 0.06498  239 HOH B O   
2979 O O   . HOH D .   ? 0.51417 0.46955 0.57904 0.00399  -0.00531 0.04751  240 HOH B O   
2980 O O   . HOH D .   ? 0.26726 0.58614 0.44602 0.02875  0.01524  0.07917  241 HOH B O   
2981 O O   . HOH D .   ? 0.53424 0.68299 0.59669 -0.02279 0.01334  0.10791  242 HOH B O   
2982 O O   . HOH D .   ? 0.51770 0.47830 0.57595 0.05545  0.01879  -0.04813 243 HOH B O   
2983 O O   . HOH D .   ? 0.55982 0.49082 0.61784 0.02442  0.01002  -0.04561 244 HOH B O   
2984 O O   . HOH D .   ? 0.21943 0.72938 0.41857 -0.02667 0.05190  0.15284  245 HOH B O   
2985 O O   . HOH D .   ? 0.50862 0.60133 0.53334 0.04046  0.02607  -0.01737 246 HOH B O   
2986 O O   . HOH D .   ? 0.44905 0.56145 0.35131 0.01195  0.06002  -0.02252 247 HOH B O   
2987 O O   . HOH D .   ? 0.47342 0.51085 0.37874 -0.02268 -0.01691 -0.04615 248 HOH B O   
2988 O O   . HOH D .   ? 0.40044 0.72418 0.41875 0.03300  0.06109  0.04262  249 HOH B O   
2989 O O   . HOH D .   ? 0.50017 0.54369 0.55400 0.03400  0.01098  0.00977  250 HOH B O   
2990 O O   . HOH D .   ? 0.50965 0.61161 0.37638 -0.00358 0.02714  -0.02534 251 HOH B O   
2991 O O   . HOH D .   ? 0.39983 0.77501 0.46000 -0.02114 0.05475  0.14249  252 HOH B O   
2992 O O   . HOH D .   ? 0.60437 0.80961 0.59820 0.02511  0.03037  0.02326  253 HOH B O   
2993 O O   . HOH D .   ? 0.63155 0.51861 0.71054 0.01206  0.00566  -0.04283 254 HOH B O   
2994 O O   . HOH D .   ? 0.41294 0.56479 0.49212 -0.04287 0.00815  0.14910  255 HOH B O   
2995 O O   . HOH D .   ? 0.32156 0.85916 0.48053 -0.05371 0.06054  0.19753  256 HOH B O   
2996 O O   . HOH D .   ? 0.41333 0.70199 0.47457 -0.02481 0.03731  0.13413  257 HOH B O   
2997 O O   . HOH D .   ? 0.48209 0.38169 0.57047 0.02772  0.00048  0.09006  258 HOH B O   
2998 O O   . HOH D .   ? 0.54063 0.41025 0.63948 -0.01477 0.00216  -0.02001 259 HOH B O   
2999 O O   . HOH D .   ? 0.53804 0.48735 0.56888 0.02060  0.00964  -0.01117 260 HOH B O   
3000 O O   . HOH D .   ? 0.43076 0.46766 0.47807 0.02024  0.00539  0.01491  261 HOH B O   
3001 O O   . HOH D .   ? 0.35274 0.38234 0.41853 0.04595  -0.00358 0.03837  262 HOH B O   
3002 O O   . HOH D .   ? 0.56074 0.46464 0.66282 0.02764  -0.01089 0.17397  263 HOH B O   
3003 O O   . HOH D .   ? 0.52238 0.71375 0.43281 -0.03879 0.01883  0.23570  264 HOH B O   
3004 O O   . HOH D .   ? 0.63586 0.78670 0.55031 -0.01151 -0.01400 0.16738  265 HOH B O   
3005 O O   . HOH D .   ? 0.49985 0.38779 0.59620 0.01879  -0.00063 0.11488  266 HOH B O   
3006 O O   . HOH D .   ? 0.67216 0.57936 0.77617 0.04579  -0.01033 0.13530  267 HOH B O   
3007 O O   . HOH D .   ? 0.55081 0.69134 0.46721 0.01139  0.07374  -0.00577 268 HOH B O   
3008 O O   . HOH D .   ? 0.48414 0.47750 0.51069 0.01280  0.00503  0.00417  269 HOH B O   
3009 O O   . HOH D .   ? 0.59437 0.46885 0.69260 0.02649  0.00310  0.06315  270 HOH B O   
3010 O O   . HOH D .   ? 0.59870 0.67472 0.58247 -0.02542 0.01221  0.20860  271 HOH B O   
3011 O O   . HOH D .   ? 0.55174 0.44025 0.65660 0.03077  -0.00646 0.13691  272 HOH B O   
3012 O O   . HOH D .   ? 0.38237 0.55120 0.50253 -0.04574 -0.02457 0.06665  273 HOH B O   
3013 O O   . HOH D .   ? 0.55009 0.60405 0.59273 0.04078  -0.03405 0.16955  274 HOH B O   
3014 O O   . HOH D .   ? 0.50783 0.70261 0.42630 -0.03735 0.00731  0.26241  275 HOH B O   
3015 O O   . HOH D .   ? 0.56660 0.67761 0.53179 -0.03042 0.01121  0.23560  276 HOH B O   
# 
