data_8WP6
# 
_entry.id   8WP6 
# 
_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   8WP6         pdb_00008wp6 10.2210/pdb8wp6/pdb 
WWPDB D_1300039558 ?            ?                   
# 
_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       2025-04-16 
_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                        8WP6 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-09 
_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 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 jmma@ahu.edu.cn   Jinming Ma   ? 'principal investigator/group leader' 0000-0002-3199-9860 
4 wangn6@ahu.edu.cn Na      Wang ? 'principal investigator/group leader' 0000-0002-9561-0666 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ma, J.M.' 1 0000-0002-3199-9860 
'Ge, H.H.' 2 0000-0001-7176-6853 
'Wang, N.' 3 0000-0002-9561-0666 
# 
_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                     
'Crystal Structure of Acinetobacter baumannii LysR family regulator AceR effector binding domain (apo)' 
_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 'Ma, J.M.' 1 ? 
primary 'Ge, H.H.' 2 ? 
# 
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' 22146.275 1  ? ? ? ? 
2 water   nat water                                   18.015    96 ? ? ? ? 
# 
_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       
;MAYLNRDQRREMILQAAMQIALAEGFTAMTVRRIATEAQTSTGQVHHHFSSASHLKAEAFLKLMEQLDEIEQTLQTTSQF
QRLFILLGAENIDRLQPYLRLWNEAELLIEQDIEIQKAYNLAMQSWHQAIVQSIECGQKEGEFKNRSNSTDIAWRLIAFV
CGLEGIYKLGLQGLAEEDFKRHTEAIIRLELL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAYLNRDQRREMILQAAMQIALAEGFTAMTVRRIATEAQTSTGQVHHHFSSASHLKAEAFLKLMEQLDEIEQTLQTTSQF
QRLFILLGAENIDRLQPYLRLWNEAELLIEQDIEIQKAYNLAMQSWHQAIVQSIECGQKEGEFKNRSNSTDIAWRLIAFV
CGLEGIYKLGLQGLAEEDFKRHTEAIIRLELL
;
_entity_poly.pdbx_strand_id                 A 
_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   ALA n 
1 3   TYR n 
1 4   LEU n 
1 5   ASN n 
1 6   ARG n 
1 7   ASP n 
1 8   GLN n 
1 9   ARG n 
1 10  ARG n 
1 11  GLU n 
1 12  MET n 
1 13  ILE n 
1 14  LEU n 
1 15  GLN n 
1 16  ALA n 
1 17  ALA n 
1 18  MET n 
1 19  GLN n 
1 20  ILE n 
1 21  ALA n 
1 22  LEU n 
1 23  ALA n 
1 24  GLU n 
1 25  GLY n 
1 26  PHE n 
1 27  THR n 
1 28  ALA n 
1 29  MET n 
1 30  THR n 
1 31  VAL n 
1 32  ARG n 
1 33  ARG n 
1 34  ILE n 
1 35  ALA n 
1 36  THR n 
1 37  GLU n 
1 38  ALA n 
1 39  GLN n 
1 40  THR n 
1 41  SER n 
1 42  THR n 
1 43  GLY n 
1 44  GLN n 
1 45  VAL n 
1 46  HIS n 
1 47  HIS n 
1 48  HIS n 
1 49  PHE n 
1 50  SER n 
1 51  SER n 
1 52  ALA n 
1 53  SER n 
1 54  HIS n 
1 55  LEU n 
1 56  LYS n 
1 57  ALA n 
1 58  GLU n 
1 59  ALA n 
1 60  PHE n 
1 61  LEU n 
1 62  LYS n 
1 63  LEU n 
1 64  MET n 
1 65  GLU n 
1 66  GLN n 
1 67  LEU n 
1 68  ASP n 
1 69  GLU n 
1 70  ILE n 
1 71  GLU n 
1 72  GLN n 
1 73  THR n 
1 74  LEU n 
1 75  GLN n 
1 76  THR n 
1 77  THR n 
1 78  SER n 
1 79  GLN n 
1 80  PHE n 
1 81  GLN n 
1 82  ARG n 
1 83  LEU n 
1 84  PHE n 
1 85  ILE n 
1 86  LEU n 
1 87  LEU n 
1 88  GLY n 
1 89  ALA n 
1 90  GLU n 
1 91  ASN n 
1 92  ILE n 
1 93  ASP n 
1 94  ARG n 
1 95  LEU n 
1 96  GLN n 
1 97  PRO n 
1 98  TYR n 
1 99  LEU n 
1 100 ARG n 
1 101 LEU n 
1 102 TRP n 
1 103 ASN n 
1 104 GLU n 
1 105 ALA n 
1 106 GLU n 
1 107 LEU n 
1 108 LEU n 
1 109 ILE n 
1 110 GLU n 
1 111 GLN n 
1 112 ASP n 
1 113 ILE n 
1 114 GLU n 
1 115 ILE n 
1 116 GLN n 
1 117 LYS n 
1 118 ALA n 
1 119 TYR n 
1 120 ASN n 
1 121 LEU n 
1 122 ALA n 
1 123 MET n 
1 124 GLN n 
1 125 SER n 
1 126 TRP n 
1 127 HIS n 
1 128 GLN n 
1 129 ALA n 
1 130 ILE n 
1 131 VAL n 
1 132 GLN n 
1 133 SER n 
1 134 ILE n 
1 135 GLU n 
1 136 CYS n 
1 137 GLY n 
1 138 GLN n 
1 139 LYS n 
1 140 GLU n 
1 141 GLY n 
1 142 GLU n 
1 143 PHE n 
1 144 LYS n 
1 145 ASN n 
1 146 ARG n 
1 147 SER n 
1 148 ASN n 
1 149 SER n 
1 150 THR n 
1 151 ASP n 
1 152 ILE n 
1 153 ALA n 
1 154 TRP n 
1 155 ARG n 
1 156 LEU n 
1 157 ILE n 
1 158 ALA n 
1 159 PHE n 
1 160 VAL n 
1 161 CYS n 
1 162 GLY n 
1 163 LEU n 
1 164 GLU n 
1 165 GLY n 
1 166 ILE n 
1 167 TYR n 
1 168 LYS n 
1 169 LEU n 
1 170 GLY n 
1 171 LEU n 
1 172 GLN n 
1 173 GLY n 
1 174 LEU n 
1 175 ALA n 
1 176 GLU n 
1 177 GLU n 
1 178 ASP n 
1 179 PHE n 
1 180 LYS n 
1 181 ARG n 
1 182 HIS n 
1 183 THR n 
1 184 GLU n 
1 185 ALA n 
1 186 ILE n 
1 187 ILE n 
1 188 ARG n 
1 189 LEU n 
1 190 GLU n 
1 191 LEU n 
1 192 LEU 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                   192 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ABCAM1_2317 
_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   ALA 2   2   ?   ?   ?   A . n 
A 1 3   TYR 3   3   ?   ?   ?   A . n 
A 1 4   LEU 4   4   ?   ?   ?   A . n 
A 1 5   ASN 5   5   ?   ?   ?   A . n 
A 1 6   ARG 6   6   ?   ?   ?   A . n 
A 1 7   ASP 7   7   ?   ?   ?   A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  MET 18  18  18  MET MET A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  ILE 20  20  20  ILE ILE A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  THR 27  27  27  THR THR A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  MET 29  29  29  MET MET A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ARG 32  32  32  ARG ARG A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  GLN 39  39  39  GLN GLN A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  GLN 44  44  44  GLN GLN A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  HIS 47  47  47  HIS HIS A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  SER 51  51  51  SER SER A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  HIS 54  54  54  HIS HIS A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  MET 64  64  64  MET MET A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  GLN 66  66  66  GLN GLN A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  GLN 72  72  72  GLN GLN A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  GLN 75  75  75  GLN GLN A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  SER 78  78  78  SER SER A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  PHE 84  84  84  PHE PHE A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  ASN 91  91  91  ASN ASN A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  ASP 93  93  93  ASP ASP A . n 
A 1 94  ARG 94  94  94  ARG ARG A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  TYR 98  98  98  TYR TYR A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 TRP 102 102 102 TRP TRP A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 GLN 111 111 111 GLN GLN A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 TYR 119 119 119 TYR TYR A . n 
A 1 120 ASN 120 120 120 ASN ASN A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 MET 123 123 123 MET MET A . n 
A 1 124 GLN 124 124 124 GLN GLN A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 TRP 126 126 126 TRP TRP A . n 
A 1 127 HIS 127 127 127 HIS HIS A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 GLN 132 132 132 GLN GLN A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 CYS 136 136 136 CYS CYS A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 GLU 142 142 142 GLU GLU A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 LYS 144 144 144 LYS LYS A . n 
A 1 145 ASN 145 145 145 ASN ASN A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 ASN 148 148 148 ASN ASN A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 CYS 161 161 161 CYS CYS A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 GLN 172 172 172 GLN GLN A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 GLU 176 176 176 GLU GLU A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 ASP 178 178 178 ASP ASP A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 LYS 180 180 180 LYS LYS A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 HIS 182 182 182 HIS HIS A . n 
A 1 183 THR 183 183 183 THR THR A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 GLU 190 190 190 GLU GLU A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 LEU 192 192 192 LEU LEU A . 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 
B 2 HOH 1  201 59  HOH HOH A . 
B 2 HOH 2  202 9   HOH HOH A . 
B 2 HOH 3  203 93  HOH HOH A . 
B 2 HOH 4  204 62  HOH HOH A . 
B 2 HOH 5  205 96  HOH HOH A . 
B 2 HOH 6  206 70  HOH HOH A . 
B 2 HOH 7  207 12  HOH HOH A . 
B 2 HOH 8  208 94  HOH HOH A . 
B 2 HOH 9  209 35  HOH HOH A . 
B 2 HOH 10 210 53  HOH HOH A . 
B 2 HOH 11 211 48  HOH HOH A . 
B 2 HOH 12 212 18  HOH HOH A . 
B 2 HOH 13 213 64  HOH HOH A . 
B 2 HOH 14 214 3   HOH HOH A . 
B 2 HOH 15 215 75  HOH HOH A . 
B 2 HOH 16 216 45  HOH HOH A . 
B 2 HOH 17 217 23  HOH HOH A . 
B 2 HOH 18 218 31  HOH HOH A . 
B 2 HOH 19 219 10  HOH HOH A . 
B 2 HOH 20 220 92  HOH HOH A . 
B 2 HOH 21 221 63  HOH HOH A . 
B 2 HOH 22 222 41  HOH HOH A . 
B 2 HOH 23 223 54  HOH HOH A . 
B 2 HOH 24 224 30  HOH HOH A . 
B 2 HOH 25 225 11  HOH HOH A . 
B 2 HOH 26 226 1   HOH HOH A . 
B 2 HOH 27 227 58  HOH HOH A . 
B 2 HOH 28 228 26  HOH HOH A . 
B 2 HOH 29 229 66  HOH HOH A . 
B 2 HOH 30 230 2   HOH HOH A . 
B 2 HOH 31 231 27  HOH HOH A . 
B 2 HOH 32 232 8   HOH HOH A . 
B 2 HOH 33 233 29  HOH HOH A . 
B 2 HOH 34 234 15  HOH HOH A . 
B 2 HOH 35 235 14  HOH HOH A . 
B 2 HOH 36 236 97  HOH HOH A . 
B 2 HOH 37 237 7   HOH HOH A . 
B 2 HOH 38 238 42  HOH HOH A . 
B 2 HOH 39 239 65  HOH HOH A . 
B 2 HOH 40 240 19  HOH HOH A . 
B 2 HOH 41 241 20  HOH HOH A . 
B 2 HOH 42 242 17  HOH HOH A . 
B 2 HOH 43 243 38  HOH HOH A . 
B 2 HOH 44 244 74  HOH HOH A . 
B 2 HOH 45 245 16  HOH HOH A . 
B 2 HOH 46 246 25  HOH HOH A . 
B 2 HOH 47 247 51  HOH HOH A . 
B 2 HOH 48 248 13  HOH HOH A . 
B 2 HOH 49 249 55  HOH HOH A . 
B 2 HOH 50 250 28  HOH HOH A . 
B 2 HOH 51 251 34  HOH HOH A . 
B 2 HOH 52 252 72  HOH HOH A . 
B 2 HOH 53 253 21  HOH HOH A . 
B 2 HOH 54 254 24  HOH HOH A . 
B 2 HOH 55 255 73  HOH HOH A . 
B 2 HOH 56 256 47  HOH HOH A . 
B 2 HOH 57 257 52  HOH HOH A . 
B 2 HOH 58 258 46  HOH HOH A . 
B 2 HOH 59 259 5   HOH HOH A . 
B 2 HOH 60 260 32  HOH HOH A . 
B 2 HOH 61 261 61  HOH HOH A . 
B 2 HOH 62 262 22  HOH HOH A . 
B 2 HOH 63 263 68  HOH HOH A . 
B 2 HOH 64 264 77  HOH HOH A . 
B 2 HOH 65 265 43  HOH HOH A . 
B 2 HOH 66 266 4   HOH HOH A . 
B 2 HOH 67 267 50  HOH HOH A . 
B 2 HOH 68 268 90  HOH HOH A . 
B 2 HOH 69 269 95  HOH HOH A . 
B 2 HOH 70 270 82  HOH HOH A . 
B 2 HOH 71 271 44  HOH HOH A . 
B 2 HOH 72 272 36  HOH HOH A . 
B 2 HOH 73 273 49  HOH HOH A . 
B 2 HOH 74 274 98  HOH HOH A . 
B 2 HOH 75 275 60  HOH HOH A . 
B 2 HOH 76 276 86  HOH HOH A . 
B 2 HOH 77 277 84  HOH HOH A . 
B 2 HOH 78 278 69  HOH HOH A . 
B 2 HOH 79 279 39  HOH HOH A . 
B 2 HOH 80 280 83  HOH HOH A . 
B 2 HOH 81 281 6   HOH HOH A . 
B 2 HOH 82 282 76  HOH HOH A . 
B 2 HOH 83 283 101 HOH HOH A . 
B 2 HOH 84 284 67  HOH HOH A . 
B 2 HOH 85 285 56  HOH HOH A . 
B 2 HOH 86 286 78  HOH HOH A . 
B 2 HOH 87 287 81  HOH HOH A . 
B 2 HOH 88 288 99  HOH HOH A . 
B 2 HOH 89 289 87  HOH HOH A . 
B 2 HOH 90 290 57  HOH HOH A . 
B 2 HOH 91 291 79  HOH HOH A . 
B 2 HOH 92 292 80  HOH HOH A . 
B 2 HOH 93 293 40  HOH HOH A . 
B 2 HOH 94 294 89  HOH HOH A . 
B 2 HOH 95 295 37  HOH HOH A . 
B 2 HOH 96 296 91  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.19.2_4158: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8WP6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.154 
_cell.length_a_esd                 ? 
_cell.length_b                     69.596 
_cell.length_b_esd                 ? 
_cell.length_c                     50.771 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         8WP6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_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                   8WP6 
_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             2.56 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.93 
_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          EVAPORATION 
_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    
;0.2 M Ammonium fluoride,
20% w/v PEG 3350
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     80 
_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 EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-11 
_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   0.987 
_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 BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8WP6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.87 
_reflns.d_resolution_low                               50.77 
_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                                     18445 
_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                           94.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.100 
_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                                0.080 
_reflns.pdbx_Rpim_I_all                                0.025 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.076 
_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                                    1.87 
_reflns_shell.d_res_low                                     1.97 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.700 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1921 
_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                               0.645 
_reflns_shell.pdbx_Rpim_I_all                               0.237 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.596 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8WP6 
_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                            1.87 
_refine.ls_d_res_low                             50.77 
_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                     18409 
_refine.ls_number_reflns_R_free                  876 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.14 
_refine.ls_percent_reflns_R_free                 4.76 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2012 
_refine.ls_R_factor_R_free                       0.2285 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1998 
_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                          1.39 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.30 
_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                            0.18 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1495 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             96 
_refine_hist.number_atoms_total               1591 
_refine_hist.d_res_high                       1.87 
_refine_hist.d_res_low                        50.77 
# 
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' ? 0.004 ? 1518 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.736 ? 2045 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.313 ? 199  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041 ? 230  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004 ? 265  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.87 1.98  . . 109 2146 71.00  . . . . 0.2542 . . . . . . . . . . . 0.2743 
'X-RAY DIFFRACTION' 1.98 2.13  . . 144 2924 95.00  . . . . 0.2237 . . . . . . . . . . . 0.2372 
'X-RAY DIFFRACTION' 2.14 2.35  . . 163 3020 99.00  . . . . 0.2031 . . . . . . . . . . . 0.2629 
'X-RAY DIFFRACTION' 2.35 2.69  . . 141 3093 99.00  . . . . 0.2174 . . . . . . . . . . . 0.2530 
'X-RAY DIFFRACTION' 2.69 3.39  . . 174 3084 100.00 . . . . 0.2232 . . . . . . . . . . . 0.2179 
'X-RAY DIFFRACTION' 3.39 50.77 . . 145 3266 100.00 . . . . 0.1779 . . . . . . . . . . . 0.2167 
# 
_struct.entry_id                     8WP6 
_struct.title                        'Crystal structure of a TetR family regulator AmvR from Acinetobacter baumannii (APO FORM)' 
_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        8WP6 
_struct_keywords.text            'TetR family regulator, effector-binding domain, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0D5YGI2_ACIBA 
_struct_ref.pdbx_db_accession          A0A0D5YGI2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAYLNRDQRREMILQAAMQIALAEGFTAMTVRRIATEAQTSTGQVHHHFSSASHLKAEAFLKLMEQLDEIEQTLQTTSQF
QRLFILLGAENIDRLQPYLRLWNEAELLIEQDIEIQKAYNLAMQSWHQAIVQSIECGQKEGEFKNRSNSTDIAWRLIAFV
CGLEGIYKLGLQGLAEEDFKRHTEAIIRLELL
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8WP6 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 192 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A0D5YGI2 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  192 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       192 
# 
_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)' 2470  ? 
1 MORE         -16   ? 
1 'SSA (A^2)'  18610 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_665 -x+1,-y+1,z -1.0000000000 0.0000000000 0.0000000000 64.1540000000 0.0000000000 -1.0000000000 
0.0000000000 69.5960000000 0.0000000000 0.0000000000 1.0000000000 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 GLN A 8   ? GLY A 25  ? GLN A 8   GLY A 25  1 ? 18 
HELX_P HELX_P2  AA2 THR A 30  ? GLN A 39  ? THR A 30  GLN A 39  1 ? 10 
HELX_P HELX_P3  AA3 SER A 41  ? PHE A 49  ? SER A 41  PHE A 49  1 ? 9  
HELX_P HELX_P4  AA4 SER A 51  ? GLN A 72  ? SER A 51  GLN A 72  1 ? 22 
HELX_P HELX_P5  AA5 SER A 78  ? LEU A 87  ? SER A 78  LEU A 87  1 ? 10 
HELX_P HELX_P6  AA6 ILE A 92  ? ARG A 94  ? ILE A 92  ARG A 94  5 ? 3  
HELX_P HELX_P7  AA7 LEU A 95  ? ILE A 109 ? LEU A 95  ILE A 109 1 ? 15 
HELX_P HELX_P8  AA8 ASP A 112 ? GLU A 140 ? ASP A 112 GLU A 140 1 ? 29 
HELX_P HELX_P9  AA9 ASN A 148 ? LYS A 168 ? ASN A 148 LYS A 168 1 ? 21 
HELX_P HELX_P10 AB1 ALA A 175 ? GLU A 177 ? ALA A 175 GLU A 177 5 ? 3  
HELX_P HELX_P11 AB2 ASP A 178 ? LEU A 192 ? ASP A 178 LEU A 192 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   8WP6 
_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 
# 
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 ASN A 91  ? ? 34.53   57.16 
2 1 GLN A 111 ? ? -155.07 -5.08 
# 
_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         18.7767 
_pdbx_refine_tls.origin_y         27.2906 
_pdbx_refine_tls.origin_z         11.4410 
_pdbx_refine_tls.T[1][1]          0.2336 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0205 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0123 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2965 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0416 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2646 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.8957 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          1.0469 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.9246 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.3530 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -1.1270 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.1487 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0098 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0866 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0881 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0006 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.1399 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.1995 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0217 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.2864 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0028 
_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   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_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                       296 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.27 
_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 ALA 2 ? A ALA 2 
3 1 Y 1 A TYR 3 ? A TYR 3 
4 1 Y 1 A LEU 4 ? A LEU 4 
5 1 Y 1 A ASN 5 ? A ASN 5 
6 1 Y 1 A ARG 6 ? A ARG 6 
7 1 Y 1 A ASP 7 ? A ASP 7 
# 
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           32071215 
_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          ? 
# 
_atom_sites.entry_id                    8WP6 
_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]   0.015587 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014369 
_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]   0.019696 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
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   . GLN A 1 8   ? 3.508  9.327  24.039  1.00 58.07  ? 8   GLN A N   1 
ATOM   2    C CA  . GLN A 1 8   ? 3.707  10.648 23.459  1.00 54.51  ? 8   GLN A CA  1 
ATOM   3    C C   . GLN A 1 8   ? 3.841  11.673 24.579  1.00 37.93  ? 8   GLN A C   1 
ATOM   4    O O   . GLN A 1 8   ? 3.961  12.876 24.340  1.00 49.26  ? 8   GLN A O   1 
ATOM   5    C CB  . GLN A 1 8   ? 2.547  11.010 22.538  1.00 71.21  ? 8   GLN A CB  1 
ATOM   6    C CG  . GLN A 1 8   ? 1.438  11.760 23.242  1.00 67.30  ? 8   GLN A CG  1 
ATOM   7    C CD  . GLN A 1 8   ? 0.236  10.907 23.487  1.00 88.26  ? 8   GLN A CD  1 
ATOM   8    O OE1 . GLN A 1 8   ? 0.331  9.874  24.142  1.00 83.74  ? 8   GLN A OE1 1 
ATOM   9    N NE2 . GLN A 1 8   ? -0.911 11.334 22.975  1.00 73.71  ? 8   GLN A NE2 1 
ATOM   10   N N   . ARG A 1 9   ? 3.815  11.182 25.818  1.00 42.06  ? 9   ARG A N   1 
ATOM   11   C CA  . ARG A 1 9   ? 3.996  12.076 26.954  1.00 39.53  ? 9   ARG A CA  1 
ATOM   12   C C   . ARG A 1 9   ? 5.391  12.683 26.959  1.00 37.34  ? 9   ARG A C   1 
ATOM   13   O O   . ARG A 1 9   ? 5.556  13.843 27.354  1.00 34.67  ? 9   ARG A O   1 
ATOM   14   C CB  . ARG A 1 9   ? 3.700  11.330 28.254  1.00 42.71  ? 9   ARG A CB  1 
ATOM   15   C CG  . ARG A 1 9   ? 2.204  11.131 28.467  1.00 46.83  ? 9   ARG A CG  1 
ATOM   16   C CD  . ARG A 1 9   ? 1.883  10.389 29.752  1.00 54.48  ? 9   ARG A CD  1 
ATOM   17   N NE  . ARG A 1 9   ? 2.222  8.974  29.666  1.00 59.29  ? 9   ARG A NE  1 
ATOM   18   C CZ  . ARG A 1 9   ? 1.875  8.068  30.568  1.00 58.30  ? 9   ARG A CZ  1 
ATOM   19   N NH1 . ARG A 1 9   ? 1.136  8.387  31.618  1.00 40.23  ? 9   ARG A NH1 1 
ATOM   20   N NH2 . ARG A 1 9   ? 2.269  6.808  30.407  1.00 53.58  ? 9   ARG A NH2 1 
ATOM   21   N N   . ARG A 1 10  ? 6.397  11.928 26.507  1.00 35.07  ? 10  ARG A N   1 
ATOM   22   C CA  . ARG A 1 10  ? 7.716  12.510 26.276  1.00 37.35  ? 10  ARG A CA  1 
ATOM   23   C C   . ARG A 1 10  ? 7.665  13.573 25.186  1.00 34.34  ? 10  ARG A C   1 
ATOM   24   O O   . ARG A 1 10  ? 8.312  14.619 25.297  1.00 35.39  ? 10  ARG A O   1 
ATOM   25   C CB  . ARG A 1 10  ? 8.720  11.418 25.906  1.00 38.07  ? 10  ARG A CB  1 
ATOM   26   C CG  . ARG A 1 10  ? 10.137 11.933 25.765  1.00 37.75  ? 10  ARG A CG  1 
ATOM   27   C CD  . ARG A 1 10  ? 11.106 10.836 25.359  1.00 45.71  ? 10  ARG A CD  1 
ATOM   28   N NE  . ARG A 1 10  ? 12.491 11.238 25.580  1.00 41.24  ? 10  ARG A NE  1 
ATOM   29   C CZ  . ARG A 1 10  ? 13.237 11.884 24.694  1.00 36.35  ? 10  ARG A CZ  1 
ATOM   30   N NH1 . ARG A 1 10  ? 12.751 12.254 23.519  1.00 38.78  ? 10  ARG A NH1 1 
ATOM   31   N NH2 . ARG A 1 10  ? 14.499 12.176 24.998  1.00 41.36  ? 10  ARG A NH2 1 
ATOM   32   N N   . GLU A 1 11  ? 6.906  13.320 24.116  1.00 33.69  ? 11  GLU A N   1 
ATOM   33   C CA  . GLU A 1 11  ? 6.776  14.310 23.052  1.00 37.16  ? 11  GLU A CA  1 
ATOM   34   C C   . GLU A 1 11  ? 6.096  15.578 23.553  1.00 30.46  ? 11  GLU A C   1 
ATOM   35   O O   . GLU A 1 11  ? 6.445  16.685 23.131  1.00 33.98  ? 11  GLU A O   1 
ATOM   36   C CB  . GLU A 1 11  ? 6.007  13.711 21.872  1.00 46.56  ? 11  GLU A CB  1 
ATOM   37   C CG  . GLU A 1 11  ? 5.777  14.676 20.718  1.00 51.15  ? 11  GLU A CG  1 
ATOM   38   C CD  . GLU A 1 11  ? 7.027  14.936 19.901  1.00 46.44  ? 11  GLU A CD  1 
ATOM   39   O OE1 . GLU A 1 11  ? 7.923  14.066 19.880  1.00 53.23  ? 11  GLU A OE1 1 
ATOM   40   O OE2 . GLU A 1 11  ? 7.111  16.016 19.280  1.00 66.19  ? 11  GLU A OE2 1 
ATOM   41   N N   . MET A 1 12  ? 5.120  15.438 24.455  1.00 36.46  ? 12  MET A N   1 
ATOM   42   C CA  . MET A 1 12  ? 4.445  16.622 24.982  1.00 34.32  ? 12  MET A CA  1 
ATOM   43   C C   . MET A 1 12  ? 5.363  17.441 25.878  1.00 33.76  ? 12  MET A C   1 
ATOM   44   O O   . MET A 1 12  ? 5.251  18.673 25.907  1.00 34.42  ? 12  MET A O   1 
ATOM   45   C CB  . MET A 1 12  ? 3.169  16.228 25.733  1.00 39.30  ? 12  MET A CB  1 
ATOM   46   C CG  . MET A 1 12  ? 2.089  15.571 24.857  1.00 58.89  ? 12  MET A CG  1 
ATOM   47   S SD  . MET A 1 12  ? 1.789  16.281 23.210  1.00 87.85  ? 12  MET A SD  1 
ATOM   48   C CE  . MET A 1 12  ? 1.723  18.053 23.517  1.00 57.40  ? 12  MET A CE  1 
ATOM   49   N N   . ILE A 1 13  ? 6.281  16.792 26.599  1.00 28.40  ? 13  ILE A N   1 
ATOM   50   C CA  . ILE A 1 13  ? 7.277  17.542 27.362  1.00 28.54  ? 13  ILE A CA  1 
ATOM   51   C C   . ILE A 1 13  ? 8.179  18.320 26.408  1.00 32.77  ? 13  ILE A C   1 
ATOM   52   O O   . ILE A 1 13  ? 8.446  19.512 26.602  1.00 33.85  ? 13  ILE A O   1 
ATOM   53   C CB  . ILE A 1 13  ? 8.097  16.598 28.257  1.00 25.11  ? 13  ILE A CB  1 
ATOM   54   C CG1 . ILE A 1 13  ? 7.273  16.129 29.453  1.00 32.40  ? 13  ILE A CG1 1 
ATOM   55   C CG2 . ILE A 1 13  ? 9.350  17.304 28.758  1.00 32.91  ? 13  ILE A CG2 1 
ATOM   56   C CD1 . ILE A 1 13  ? 7.820  14.865 30.086  1.00 33.78  ? 13  ILE A CD1 1 
ATOM   57   N N   . LEU A 1 14  ? 8.664  17.645 25.362  1.00 28.87  ? 14  LEU A N   1 
ATOM   58   C CA  . LEU A 1 14  ? 9.480  18.305 24.344  1.00 31.11  ? 14  LEU A CA  1 
ATOM   59   C C   . LEU A 1 14  ? 8.765  19.506 23.740  1.00 32.68  ? 14  LEU A C   1 
ATOM   60   O O   . LEU A 1 14  ? 9.366  20.570 23.566  1.00 31.55  ? 14  LEU A O   1 
ATOM   61   C CB  . LEU A 1 14  ? 9.853  17.306 23.249  1.00 37.98  ? 14  LEU A CB  1 
ATOM   62   C CG  . LEU A 1 14  ? 11.061 17.606 22.362  1.00 40.62  ? 14  LEU A CG  1 
ATOM   63   C CD1 . LEU A 1 14  ? 12.301 17.936 23.179  1.00 30.23  ? 14  LEU A CD1 1 
ATOM   64   C CD2 . LEU A 1 14  ? 11.328 16.434 21.421  1.00 51.69  ? 14  LEU A CD2 1 
ATOM   65   N N   . GLN A 1 15  ? 7.475  19.362 23.421  1.00 30.43  ? 15  GLN A N   1 
ATOM   66   C CA  . GLN A 1 15  ? 6.741  20.474 22.822  1.00 33.59  ? 15  GLN A CA  1 
ATOM   67   C C   . GLN A 1 15  ? 6.641  21.659 23.777  1.00 39.33  ? 15  GLN A C   1 
ATOM   68   O O   . GLN A 1 15  ? 6.670  22.817 23.342  1.00 40.29  ? 15  GLN A O   1 
ATOM   69   C CB  . GLN A 1 15  ? 5.348  20.015 22.389  1.00 44.88  ? 15  GLN A CB  1 
ATOM   70   C CG  . GLN A 1 15  ? 5.360  19.170 21.135  1.00 47.75  ? 15  GLN A CG  1 
ATOM   71   C CD  . GLN A 1 15  ? 5.773  19.960 19.907  1.00 46.57  ? 15  GLN A CD  1 
ATOM   72   O OE1 . GLN A 1 15  ? 5.595  21.178 19.844  1.00 47.25  ? 15  GLN A OE1 1 
ATOM   73   N NE2 . GLN A 1 15  ? 6.344  19.269 18.929  1.00 49.57  ? 15  GLN A NE2 1 
ATOM   74   N N   . ALA A 1 16  ? 6.520  21.393 25.082  1.00 40.18  ? 16  ALA A N   1 
ATOM   75   C CA  . ALA A 1 16  ? 6.499  22.477 26.060  1.00 32.48  ? 16  ALA A CA  1 
ATOM   76   C C   . ALA A 1 16  ? 7.843  23.195 26.122  1.00 35.26  ? 16  ALA A C   1 
ATOM   77   O O   . ALA A 1 16  ? 7.892  24.430 26.192  1.00 34.00  ? 16  ALA A O   1 
ATOM   78   C CB  . ALA A 1 16  ? 6.117  21.937 27.440  1.00 35.27  ? 16  ALA A CB  1 
ATOM   79   N N   . ALA A 1 17  ? 8.946  22.439 26.109  1.00 31.02  ? 17  ALA A N   1 
ATOM   80   C CA  . ALA A 1 17  ? 10.267 23.060 26.073  1.00 31.03  ? 17  ALA A CA  1 
ATOM   81   C C   . ALA A 1 17  ? 10.452 23.905 24.816  1.00 33.41  ? 17  ALA A C   1 
ATOM   82   O O   . ALA A 1 17  ? 11.072 24.974 24.865  1.00 37.97  ? 17  ALA A O   1 
ATOM   83   C CB  . ALA A 1 17  ? 11.351 21.986 26.165  1.00 33.43  ? 17  ALA A CB  1 
ATOM   84   N N   . MET A 1 18  ? 9.923  23.442 23.678  1.00 30.78  ? 18  MET A N   1 
ATOM   85   C CA  . MET A 1 18  ? 10.051 24.198 22.430  1.00 36.43  ? 18  MET A CA  1 
ATOM   86   C C   . MET A 1 18  ? 9.311  25.530 22.498  1.00 35.25  ? 18  MET A C   1 
ATOM   87   O O   . MET A 1 18  ? 9.763  26.527 21.921  1.00 37.30  ? 18  MET A O   1 
ATOM   88   C CB  . MET A 1 18  ? 9.544  23.358 21.255  1.00 30.22  ? 18  MET A CB  1 
ATOM   89   C CG  . MET A 1 18  ? 10.268 22.029 21.112  1.00 36.54  ? 18  MET A CG  1 
ATOM   90   S SD  . MET A 1 18  ? 9.536  20.861 19.949  1.00 39.58  ? 18  MET A SD  1 
ATOM   91   C CE  . MET A 1 18  ? 9.349  21.875 18.486  1.00 38.10  ? 18  MET A CE  1 
ATOM   92   N N   . GLN A 1 19  ? 8.163  25.564 23.182  1.00 39.20  ? 19  GLN A N   1 
ATOM   93   C CA  . GLN A 1 19  ? 7.418  26.814 23.310  1.00 36.11  ? 19  GLN A CA  1 
ATOM   94   C C   . GLN A 1 19  ? 8.187  27.831 24.145  1.00 48.47  ? 19  GLN A C   1 
ATOM   95   O O   . GLN A 1 19  ? 8.279  29.009 23.778  1.00 43.92  ? 19  GLN A O   1 
ATOM   96   C CB  . GLN A 1 19  ? 6.042  26.548 23.919  1.00 36.98  ? 19  GLN A CB  1 
ATOM   97   C CG  . GLN A 1 19  ? 5.058  27.690 23.720  1.00 58.55  ? 19  GLN A CG  1 
ATOM   98   C CD  . GLN A 1 19  ? 4.216  27.958 24.952  1.00 74.48  ? 19  GLN A CD  1 
ATOM   99   O OE1 . GLN A 1 19  ? 4.688  28.545 25.927  1.00 80.45  ? 19  GLN A OE1 1 
ATOM   100  N NE2 . GLN A 1 19  ? 2.961  27.524 24.915  1.00 68.84  ? 19  GLN A NE2 1 
ATOM   101  N N   . ILE A 1 20  ? 8.741  27.394 25.281  1.00 44.69  ? 20  ILE A N   1 
ATOM   102  C CA  . ILE A 1 20  ? 9.543  28.283 26.117  1.00 42.42  ? 20  ILE A CA  1 
ATOM   103  C C   . ILE A 1 20  ? 10.781 28.751 25.359  1.00 40.44  ? 20  ILE A C   1 
ATOM   104  O O   . ILE A 1 20  ? 11.163 29.926 25.427  1.00 41.67  ? 20  ILE A O   1 
ATOM   105  C CB  . ILE A 1 20  ? 9.922  27.578 27.432  1.00 36.93  ? 20  ILE A CB  1 
ATOM   106  C CG1 . ILE A 1 20  ? 8.676  27.320 28.281  1.00 40.80  ? 20  ILE A CG1 1 
ATOM   107  C CG2 . ILE A 1 20  ? 10.913 28.417 28.223  1.00 45.48  ? 20  ILE A CG2 1 
ATOM   108  C CD1 . ILE A 1 20  ? 8.822  26.134 29.205  1.00 42.64  ? 20  ILE A CD1 1 
ATOM   109  N N   . ALA A 1 21  ? 11.426 27.839 24.627  1.00 32.97  ? 21  ALA A N   1 
ATOM   110  C CA  . ALA A 1 21  ? 12.615 28.199 23.857  1.00 39.95  ? 21  ALA A CA  1 
ATOM   111  C C   . ALA A 1 21  ? 12.310 29.302 22.851  1.00 44.38  ? 21  ALA A C   1 
ATOM   112  O O   . ALA A 1 21  ? 13.013 30.318 22.793  1.00 43.64  ? 21  ALA A O   1 
ATOM   113  C CB  . ALA A 1 21  ? 13.168 26.966 23.141  1.00 34.31  ? 21  ALA A CB  1 
ATOM   114  N N   . LEU A 1 22  ? 11.259 29.114 22.051  1.00 43.46  ? 22  LEU A N   1 
ATOM   115  C CA  . LEU A 1 22  ? 10.912 30.088 21.020  1.00 50.88  ? 22  LEU A CA  1 
ATOM   116  C C   . LEU A 1 22  ? 10.574 31.446 21.623  1.00 57.24  ? 22  LEU A C   1 
ATOM   117  O O   . LEU A 1 22  ? 10.954 32.488 21.076  1.00 59.76  ? 22  LEU A O   1 
ATOM   118  C CB  . LEU A 1 22  ? 9.736  29.569 20.195  1.00 52.62  ? 22  LEU A CB  1 
ATOM   119  C CG  . LEU A 1 22  ? 9.796  29.606 18.668  1.00 53.60  ? 22  LEU A CG  1 
ATOM   120  C CD1 . LEU A 1 22  ? 11.172 29.221 18.150  1.00 49.18  ? 22  LEU A CD1 1 
ATOM   121  C CD2 . LEU A 1 22  ? 8.724  28.692 18.089  1.00 48.18  ? 22  LEU A CD2 1 
ATOM   122  N N   . ALA A 1 23  ? 9.870  31.456 22.754  1.00 48.28  ? 23  ALA A N   1 
ATOM   123  C CA  . ALA A 1 23  ? 9.350  32.696 23.316  1.00 49.56  ? 23  ALA A CA  1 
ATOM   124  C C   . ALA A 1 23  ? 10.320 33.395 24.261  1.00 59.67  ? 23  ALA A C   1 
ATOM   125  O O   . ALA A 1 23  ? 10.331 34.630 24.316  1.00 55.26  ? 23  ALA A O   1 
ATOM   126  C CB  . ALA A 1 23  ? 8.037  32.425 24.055  1.00 54.97  ? 23  ALA A CB  1 
ATOM   127  N N   . GLU A 1 24  ? 11.133 32.647 25.011  1.00 44.19  ? 24  GLU A N   1 
ATOM   128  C CA  . GLU A 1 24  ? 11.954 33.244 26.056  1.00 50.35  ? 24  GLU A CA  1 
ATOM   129  C C   . GLU A 1 24  ? 13.422 32.838 26.032  1.00 50.89  ? 24  GLU A C   1 
ATOM   130  O O   . GLU A 1 24  ? 14.215 33.452 26.754  1.00 58.48  ? 24  GLU A O   1 
ATOM   131  C CB  . GLU A 1 24  ? 11.373 32.914 27.442  1.00 57.31  ? 24  GLU A CB  1 
ATOM   132  C CG  . GLU A 1 24  ? 9.948  33.415 27.646  1.00 60.86  ? 24  GLU A CG  1 
ATOM   133  C CD  . GLU A 1 24  ? 9.294  32.833 28.883  1.00 61.62  ? 24  GLU A CD  1 
ATOM   134  O OE1 . GLU A 1 24  ? 9.870  32.976 29.981  1.00 66.99  ? 24  GLU A OE1 1 
ATOM   135  O OE2 . GLU A 1 24  ? 8.203  32.237 28.757  1.00 65.56  ? 24  GLU A OE2 1 
ATOM   136  N N   . GLY A 1 25  ? 13.811 31.841 25.243  1.00 43.18  ? 25  GLY A N   1 
ATOM   137  C CA  . GLY A 1 25  ? 15.206 31.460 25.146  1.00 40.05  ? 25  GLY A CA  1 
ATOM   138  C C   . GLY A 1 25  ? 15.594 30.335 26.085  1.00 52.01  ? 25  GLY A C   1 
ATOM   139  O O   . GLY A 1 25  ? 14.782 29.765 26.821  1.00 42.35  ? 25  GLY A O   1 
ATOM   140  N N   . PHE A 1 26  ? 16.893 30.027 26.062  1.00 47.52  ? 26  PHE A N   1 
ATOM   141  C CA  . PHE A 1 26  ? 17.401 28.847 26.755  1.00 41.65  ? 26  PHE A CA  1 
ATOM   142  C C   . PHE A 1 26  ? 17.394 29.011 28.272  1.00 46.49  ? 26  PHE A C   1 
ATOM   143  O O   . PHE A 1 26  ? 17.096 28.054 28.996  1.00 40.58  ? 26  PHE A O   1 
ATOM   144  C CB  . PHE A 1 26  ? 18.811 28.520 26.261  1.00 40.47  ? 26  PHE A CB  1 
ATOM   145  C CG  . PHE A 1 26  ? 18.856 27.912 24.880  1.00 32.92  ? 26  PHE A CG  1 
ATOM   146  C CD1 . PHE A 1 26  ? 18.354 26.639 24.661  1.00 36.38  ? 26  PHE A CD1 1 
ATOM   147  C CD2 . PHE A 1 26  ? 19.393 28.608 23.806  1.00 35.54  ? 26  PHE A CD2 1 
ATOM   148  C CE1 . PHE A 1 26  ? 18.395 26.063 23.399  1.00 30.53  ? 26  PHE A CE1 1 
ATOM   149  C CE2 . PHE A 1 26  ? 19.440 28.038 22.544  1.00 32.59  ? 26  PHE A CE2 1 
ATOM   150  C CZ  . PHE A 1 26  ? 18.934 26.770 22.338  1.00 33.16  ? 26  PHE A CZ  1 
ATOM   151  N N   . THR A 1 27  ? 17.744 30.198 28.781  1.00 46.62  ? 27  THR A N   1 
ATOM   152  C CA  . THR A 1 27  ? 17.878 30.343 30.230  1.00 54.57  ? 27  THR A CA  1 
ATOM   153  C C   . THR A 1 27  ? 16.565 30.086 30.957  1.00 46.32  ? 27  THR A C   1 
ATOM   154  O O   . THR A 1 27  ? 16.574 29.614 32.099  1.00 44.34  ? 27  THR A O   1 
ATOM   155  C CB  . THR A 1 27  ? 18.410 31.728 30.590  1.00 58.80  ? 27  THR A CB  1 
ATOM   156  O OG1 . THR A 1 27  ? 19.340 32.166 29.592  1.00 65.12  ? 27  THR A OG1 1 
ATOM   157  C CG2 . THR A 1 27  ? 19.097 31.695 31.946  1.00 53.58  ? 27  THR A CG2 1 
ATOM   158  N N   . ALA A 1 28  ? 15.435 30.386 30.318  1.00 38.67  ? 28  ALA A N   1 
ATOM   159  C CA  . ALA A 1 28  ? 14.133 30.141 30.925  1.00 47.73  ? 28  ALA A CA  1 
ATOM   160  C C   . ALA A 1 28  ? 13.755 28.667 30.938  1.00 43.40  ? 28  ALA A C   1 
ATOM   161  O O   . ALA A 1 28  ? 12.758 28.309 31.573  1.00 39.84  ? 28  ALA A O   1 
ATOM   162  C CB  . ALA A 1 28  ? 13.052 30.931 30.188  1.00 38.23  ? 28  ALA A CB  1 
ATOM   163  N N   . MET A 1 29  ? 14.523 27.811 30.270  1.00 35.51  ? 29  MET A N   1 
ATOM   164  C CA  . MET A 1 29  ? 14.148 26.410 30.082  1.00 36.76  ? 29  MET A CA  1 
ATOM   165  C C   . MET A 1 29  ? 14.633 25.545 31.244  1.00 36.99  ? 29  MET A C   1 
ATOM   166  O O   . MET A 1 29  ? 15.388 24.588 31.069  1.00 38.66  ? 29  MET A O   1 
ATOM   167  C CB  . MET A 1 29  ? 14.701 25.894 28.759  1.00 33.20  ? 29  MET A CB  1 
ATOM   168  C CG  . MET A 1 29  ? 13.997 26.421 27.527  1.00 43.12  ? 29  MET A CG  1 
ATOM   169  S SD  . MET A 1 29  ? 14.933 25.952 26.063  1.00 39.42  ? 29  MET A SD  1 
ATOM   170  C CE  . MET A 1 29  ? 14.280 24.302 25.805  1.00 35.80  ? 29  MET A CE  1 
ATOM   171  N N   . THR A 1 30  ? 14.184 25.893 32.449  1.00 38.80  ? 30  THR A N   1 
ATOM   172  C CA  . THR A 1 30  ? 14.468 25.050 33.597  1.00 36.17  ? 30  THR A CA  1 
ATOM   173  C C   . THR A 1 30  ? 13.508 23.868 33.616  1.00 41.84  ? 30  THR A C   1 
ATOM   174  O O   . THR A 1 30  ? 12.417 23.911 33.039  1.00 33.43  ? 30  THR A O   1 
ATOM   175  C CB  . THR A 1 30  ? 14.331 25.825 34.909  1.00 41.54  ? 30  THR A CB  1 
ATOM   176  O OG1 . THR A 1 30  ? 13.022 26.398 34.985  1.00 40.77  ? 30  THR A OG1 1 
ATOM   177  C CG2 . THR A 1 30  ? 15.367 26.935 34.983  1.00 42.48  ? 30  THR A CG2 1 
ATOM   178  N N   . VAL A 1 31  ? 13.924 22.802 34.297  1.00 35.08  ? 31  VAL A N   1 
ATOM   179  C CA  . VAL A 1 31  ? 13.061 21.630 34.412  1.00 33.83  ? 31  VAL A CA  1 
ATOM   180  C C   . VAL A 1 31  ? 11.777 21.990 35.149  1.00 37.26  ? 31  VAL A C   1 
ATOM   181  O O   . VAL A 1 31  ? 10.685 21.546 34.774  1.00 38.10  ? 31  VAL A O   1 
ATOM   182  C CB  . VAL A 1 31  ? 13.817 20.476 35.094  1.00 36.01  ? 31  VAL A CB  1 
ATOM   183  C CG1 . VAL A 1 31  ? 12.847 19.379 35.525  1.00 37.32  ? 31  VAL A CG1 1 
ATOM   184  C CG2 . VAL A 1 31  ? 14.886 19.926 34.154  1.00 34.06  ? 31  VAL A CG2 1 
ATOM   185  N N   . ARG A 1 32  ? 11.889 22.809 36.200  1.00 38.37  ? 32  ARG A N   1 
ATOM   186  C CA  . ARG A 1 32  ? 10.715 23.302 36.920  1.00 39.72  ? 32  ARG A CA  1 
ATOM   187  C C   . ARG A 1 32  ? 9.732  23.984 35.978  1.00 40.61  ? 32  ARG A C   1 
ATOM   188  O O   . ARG A 1 32  ? 8.530  23.693 35.987  1.00 40.99  ? 32  ARG A O   1 
ATOM   189  C CB  . ARG A 1 32  ? 11.163 24.279 38.014  1.00 47.04  ? 32  ARG A CB  1 
ATOM   190  C CG  . ARG A 1 32  ? 10.125 24.663 39.057  1.00 58.88  ? 32  ARG A CG  1 
ATOM   191  C CD  . ARG A 1 32  ? 9.408  23.469 39.654  1.00 65.32  ? 32  ARG A CD  1 
ATOM   192  N NE  . ARG A 1 32  ? 8.122  23.232 39.010  1.00 82.56  ? 32  ARG A NE  1 
ATOM   193  C CZ  . ARG A 1 32  ? 7.285  22.261 39.345  1.00 76.12  ? 32  ARG A CZ  1 
ATOM   194  N NH1 . ARG A 1 32  ? 7.556  21.425 40.335  1.00 64.83  ? 32  ARG A NH1 1 
ATOM   195  N NH2 . ARG A 1 32  ? 6.144  22.129 38.675  1.00 73.21  ? 32  ARG A NH2 1 
ATOM   196  N N   . ARG A 1 33  ? 10.236 24.907 35.159  1.00 39.13  ? 33  ARG A N   1 
ATOM   197  C CA  . ARG A 1 33  ? 9.381  25.657 34.247  1.00 39.83  ? 33  ARG A CA  1 
ATOM   198  C C   . ARG A 1 33  ? 8.734  24.747 33.211  1.00 43.82  ? 33  ARG A C   1 
ATOM   199  O O   . ARG A 1 33  ? 7.534  24.862 32.933  1.00 42.01  ? 33  ARG A O   1 
ATOM   200  C CB  . ARG A 1 33  ? 10.207 26.743 33.559  1.00 40.60  ? 33  ARG A CB  1 
ATOM   201  C CG  . ARG A 1 33  ? 9.457  27.540 32.525  1.00 54.16  ? 33  ARG A CG  1 
ATOM   202  C CD  . ARG A 1 33  ? 8.382  28.412 33.141  1.00 52.13  ? 33  ARG A CD  1 
ATOM   203  N NE  . ARG A 1 33  ? 7.612  29.074 32.096  1.00 56.26  ? 33  ARG A NE  1 
ATOM   204  C CZ  . ARG A 1 33  ? 7.998  30.177 31.471  1.00 60.45  ? 33  ARG A CZ  1 
ATOM   205  N NH1 . ARG A 1 33  ? 9.152  30.763 31.751  1.00 44.40  ? 33  ARG A NH1 1 
ATOM   206  N NH2 . ARG A 1 33  ? 7.216  30.696 30.528  1.00 58.16  ? 33  ARG A NH2 1 
ATOM   207  N N   . ILE A 1 34  ? 9.519  23.841 32.625  1.00 36.72  ? 34  ILE A N   1 
ATOM   208  C CA  . ILE A 1 34  ? 9.018  22.981 31.557  1.00 34.44  ? 34  ILE A CA  1 
ATOM   209  C C   . ILE A 1 34  ? 7.964  22.018 32.089  1.00 28.95  ? 34  ILE A C   1 
ATOM   210  O O   . ILE A 1 34  ? 6.941  21.773 31.436  1.00 34.68  ? 34  ILE A O   1 
ATOM   211  C CB  . ILE A 1 34  ? 10.194 22.239 30.892  1.00 29.10  ? 34  ILE A CB  1 
ATOM   212  C CG1 . ILE A 1 34  ? 11.006 23.198 30.015  1.00 28.98  ? 34  ILE A CG1 1 
ATOM   213  C CG2 . ILE A 1 34  ? 9.701  21.052 30.071  1.00 29.11  ? 34  ILE A CG2 1 
ATOM   214  C CD1 . ILE A 1 34  ? 12.400 22.708 29.716  1.00 31.85  ? 34  ILE A CD1 1 
ATOM   215  N N   . ALA A 1 35  ? 8.195  21.459 33.279  1.00 30.74  ? 35  ALA A N   1 
ATOM   216  C CA  . ALA A 1 35  ? 7.209  20.579 33.901  1.00 33.44  ? 35  ALA A CA  1 
ATOM   217  C C   . ALA A 1 35  ? 5.892  21.309 34.140  1.00 39.77  ? 35  ALA A C   1 
ATOM   218  O O   . ALA A 1 35  ? 4.812  20.777 33.855  1.00 36.83  ? 35  ALA A O   1 
ATOM   219  C CB  . ALA A 1 35  ? 7.759  20.023 35.215  1.00 34.89  ? 35  ALA A CB  1 
ATOM   220  N N   . THR A 1 36  ? 5.964  22.531 34.671  1.00 38.11  ? 36  THR A N   1 
ATOM   221  C CA  . THR A 1 36  ? 4.762  23.337 34.860  1.00 38.92  ? 36  THR A CA  1 
ATOM   222  C C   . THR A 1 36  ? 4.033  23.555 33.537  1.00 42.87  ? 36  THR A C   1 
ATOM   223  O O   . THR A 1 36  ? 2.808  23.406 33.458  1.00 44.32  ? 36  THR A O   1 
ATOM   224  C CB  . THR A 1 36  ? 5.133  24.677 35.496  1.00 46.32  ? 36  THR A CB  1 
ATOM   225  O OG1 . THR A 1 36  ? 5.725  24.445 36.781  1.00 43.69  ? 36  THR A OG1 1 
ATOM   226  C CG2 . THR A 1 36  ? 3.897  25.547 35.665  1.00 48.82  ? 36  THR A CG2 1 
ATOM   227  N N   . GLU A 1 37  ? 4.777  23.895 32.481  1.00 49.76  ? 37  GLU A N   1 
ATOM   228  C CA  . GLU A 1 37  ? 4.154  24.184 31.192  1.00 38.40  ? 37  GLU A CA  1 
ATOM   229  C C   . GLU A 1 37  ? 3.541  22.937 30.565  1.00 46.02  ? 37  GLU A C   1 
ATOM   230  O O   . GLU A 1 37  ? 2.466  23.009 29.960  1.00 43.14  ? 37  GLU A O   1 
ATOM   231  C CB  . GLU A 1 37  ? 5.172  24.814 30.243  1.00 44.13  ? 37  GLU A CB  1 
ATOM   232  C CG  . GLU A 1 37  ? 5.599  26.215 30.640  1.00 53.74  ? 37  GLU A CG  1 
ATOM   233  C CD  . GLU A 1 37  ? 4.458  27.209 30.579  1.00 64.59  ? 37  GLU A CD  1 
ATOM   234  O OE1 . GLU A 1 37  ? 4.156  27.703 29.471  1.00 70.85  ? 37  GLU A OE1 1 
ATOM   235  O OE2 . GLU A 1 37  ? 3.864  27.497 31.639  1.00 72.61  ? 37  GLU A OE2 1 
ATOM   236  N N   . ALA A 1 38  ? 4.207  21.789 30.686  1.00 34.03  ? 38  ALA A N   1 
ATOM   237  C CA  . ALA A 1 38  ? 3.665  20.541 30.162  1.00 34.03  ? 38  ALA A CA  1 
ATOM   238  C C   . ALA A 1 38  ? 2.668  19.885 31.109  1.00 37.72  ? 38  ALA A C   1 
ATOM   239  O O   . ALA A 1 38  ? 2.131  18.822 30.772  1.00 39.47  ? 38  ALA A O   1 
ATOM   240  C CB  . ALA A 1 38  ? 4.797  19.555 29.853  1.00 33.22  ? 38  ALA A CB  1 
ATOM   241  N N   . GLN A 1 39  ? 2.411  20.495 32.267  1.00 37.35  ? 39  GLN A N   1 
ATOM   242  C CA  . GLN A 1 39  ? 1.539  19.949 33.309  1.00 35.63  ? 39  GLN A CA  1 
ATOM   243  C C   . GLN A 1 39  ? 1.942  18.521 33.683  1.00 38.74  ? 39  GLN A C   1 
ATOM   244  O O   . GLN A 1 39  ? 1.144  17.582 33.651  1.00 38.39  ? 39  GLN A O   1 
ATOM   245  C CB  . GLN A 1 39  ? 0.067  20.011 32.890  1.00 47.81  ? 39  GLN A CB  1 
ATOM   246  C CG  . GLN A 1 39  ? -0.426 21.400 32.521  1.00 49.76  ? 39  GLN A CG  1 
ATOM   247  C CD  . GLN A 1 39  ? -1.771 21.364 31.817  1.00 74.46  ? 39  GLN A CD  1 
ATOM   248  O OE1 . GLN A 1 39  ? -1.896 21.783 30.666  1.00 72.56  ? 39  GLN A OE1 1 
ATOM   249  N NE2 . GLN A 1 39  ? -2.785 20.856 32.508  1.00 52.36  ? 39  GLN A NE2 1 
ATOM   250  N N   . THR A 1 40  ? 3.210  18.374 34.053  1.00 38.61  ? 40  THR A N   1 
ATOM   251  C CA  . THR A 1 40  ? 3.732  17.093 34.507  1.00 32.89  ? 40  THR A CA  1 
ATOM   252  C C   . THR A 1 40  ? 4.614  17.347 35.724  1.00 42.99  ? 40  THR A C   1 
ATOM   253  O O   . THR A 1 40  ? 4.704  18.471 36.230  1.00 39.91  ? 40  THR A O   1 
ATOM   254  C CB  . THR A 1 40  ? 4.474  16.366 33.374  1.00 37.29  ? 40  THR A CB  1 
ATOM   255  O OG1 . THR A 1 40  ? 4.759  15.017 33.773  1.00 38.13  ? 40  THR A OG1 1 
ATOM   256  C CG2 . THR A 1 40  ? 5.776  17.082 33.011  1.00 30.83  ? 40  THR A CG2 1 
ATOM   257  N N   . SER A 1 41  ? 5.250  16.288 36.211  1.00 31.35  ? 41  SER A N   1 
ATOM   258  C CA  . SER A 1 41  ? 6.148  16.365 37.351  1.00 34.06  ? 41  SER A CA  1 
ATOM   259  C C   . SER A 1 41  ? 7.585  16.530 36.874  1.00 32.16  ? 41  SER A C   1 
ATOM   260  O O   . SER A 1 41  ? 7.957  16.067 35.793  1.00 29.69  ? 41  SER A O   1 
ATOM   261  C CB  . SER A 1 41  ? 6.030  15.105 38.211  1.00 32.56  ? 41  SER A CB  1 
ATOM   262  O OG  . SER A 1 41  ? 6.489  13.977 37.483  1.00 35.19  ? 41  SER A OG  1 
ATOM   263  N N   . THR A 1 42  ? 8.399  17.203 37.692  1.00 34.09  ? 42  THR A N   1 
ATOM   264  C CA  . THR A 1 42  ? 9.821  17.272 37.374  1.00 33.48  ? 42  THR A CA  1 
ATOM   265  C C   . THR A 1 42  ? 10.434 15.880 37.324  1.00 31.97  ? 42  THR A C   1 
ATOM   266  O O   . THR A 1 42  ? 11.360 15.637 36.543  1.00 31.28  ? 42  THR A O   1 
ATOM   267  C CB  . THR A 1 42  ? 10.559 18.153 38.388  1.00 38.06  ? 42  THR A CB  1 
ATOM   268  O OG1 . THR A 1 42  ? 10.338 17.653 39.713  1.00 38.23  ? 42  THR A OG1 1 
ATOM   269  C CG2 . THR A 1 42  ? 10.071 19.589 38.304  1.00 42.16  ? 42  THR A CG2 1 
ATOM   270  N N   . GLY A 1 43  ? 9.912  14.948 38.129  1.00 33.19  ? 43  GLY A N   1 
ATOM   271  C CA  . GLY A 1 43  ? 10.382 13.574 38.062  1.00 36.73  ? 43  GLY A CA  1 
ATOM   272  C C   . GLY A 1 43  ? 10.188 12.949 36.693  1.00 31.96  ? 43  GLY A C   1 
ATOM   273  O O   . GLY A 1 43  ? 11.046 12.207 36.214  1.00 33.45  ? 43  GLY A O   1 
ATOM   274  N N   . GLN A 1 44  ? 9.057  13.237 36.043  1.00 30.10  ? 44  GLN A N   1 
ATOM   275  C CA  . GLN A 1 44  ? 8.835  12.707 34.701  1.00 29.58  ? 44  GLN A CA  1 
ATOM   276  C C   . GLN A 1 44  ? 9.731  13.385 33.671  1.00 29.90  ? 44  GLN A C   1 
ATOM   277  O O   . GLN A 1 44  ? 10.163 12.742 32.704  1.00 29.80  ? 44  GLN A O   1 
ATOM   278  C CB  . GLN A 1 44  ? 7.363  12.854 34.318  1.00 32.11  ? 44  GLN A CB  1 
ATOM   279  C CG  . GLN A 1 44  ? 6.516  11.656 34.744  1.00 37.24  ? 44  GLN A CG  1 
ATOM   280  C CD  . GLN A 1 44  ? 6.831  10.407 33.940  1.00 49.11  ? 44  GLN A CD  1 
ATOM   281  O OE1 . GLN A 1 44  ? 7.374  9.436  34.465  1.00 44.32  ? 44  GLN A OE1 1 
ATOM   282  N NE2 . GLN A 1 44  ? 6.491  10.428 32.657  1.00 49.26  ? 44  GLN A NE2 1 
ATOM   283  N N   . VAL A 1 45  ? 10.028 14.674 33.851  1.00 27.77  ? 45  VAL A N   1 
ATOM   284  C CA  . VAL A 1 45  ? 10.974 15.324 32.949  1.00 25.15  ? 45  VAL A CA  1 
ATOM   285  C C   . VAL A 1 45  ? 12.343 14.670 33.072  1.00 29.51  ? 45  VAL A C   1 
ATOM   286  O O   . VAL A 1 45  ? 13.008 14.389 32.065  1.00 30.07  ? 45  VAL A O   1 
ATOM   287  C CB  . VAL A 1 45  ? 11.042 16.839 33.221  1.00 31.39  ? 45  VAL A CB  1 
ATOM   288  C CG1 . VAL A 1 45  ? 12.078 17.496 32.297  1.00 27.84  ? 45  VAL A CG1 1 
ATOM   289  C CG2 . VAL A 1 45  ? 9.674  17.478 33.029  1.00 28.59  ? 45  VAL A CG2 1 
ATOM   290  N N   . HIS A 1 46  ? 12.777 14.391 34.306  1.00 31.12  ? 46  HIS A N   1 
ATOM   291  C CA  . HIS A 1 46  ? 14.076 13.755 34.501  1.00 37.44  ? 46  HIS A CA  1 
ATOM   292  C C   . HIS A 1 46  ? 14.087 12.317 34.001  1.00 38.04  ? 46  HIS A C   1 
ATOM   293  O O   . HIS A 1 46  ? 15.136 11.824 33.569  1.00 41.10  ? 46  HIS A O   1 
ATOM   294  C CB  . HIS A 1 46  ? 14.469 13.806 35.975  1.00 34.06  ? 46  HIS A CB  1 
ATOM   295  C CG  . HIS A 1 46  ? 14.839 15.176 36.445  1.00 33.30  ? 46  HIS A CG  1 
ATOM   296  N ND1 . HIS A 1 46  ? 15.832 15.920 35.844  1.00 35.85  ? 46  HIS A ND1 1 
ATOM   297  C CD2 . HIS A 1 46  ? 14.345 15.943 37.444  1.00 36.20  ? 46  HIS A CD2 1 
ATOM   298  C CE1 . HIS A 1 46  ? 15.940 17.084 36.461  1.00 38.41  ? 46  HIS A CE1 1 
ATOM   299  N NE2 . HIS A 1 46  ? 15.049 17.123 37.435  1.00 40.77  ? 46  HIS A NE2 1 
ATOM   300  N N   . HIS A 1 47  ? 12.946 11.629 34.059  1.00 39.74  ? 47  HIS A N   1 
ATOM   301  C CA  . HIS A 1 47  ? 12.883 10.262 33.553  1.00 34.50  ? 47  HIS A CA  1 
ATOM   302  C C   . HIS A 1 47  ? 13.118 10.220 32.048  1.00 39.37  ? 47  HIS A C   1 
ATOM   303  O O   . HIS A 1 47  ? 13.868 9.372  31.551  1.00 40.08  ? 47  HIS A O   1 
ATOM   304  C CB  . HIS A 1 47  ? 11.532 9.640  33.903  1.00 38.90  ? 47  HIS A CB  1 
ATOM   305  C CG  . HIS A 1 47  ? 11.320 8.283  33.309  1.00 49.86  ? 47  HIS A CG  1 
ATOM   306  N ND1 . HIS A 1 47  ? 10.433 8.053  32.279  1.00 48.95  ? 47  HIS A ND1 1 
ATOM   307  C CD2 . HIS A 1 47  ? 11.873 7.082  33.603  1.00 53.15  ? 47  HIS A CD2 1 
ATOM   308  C CE1 . HIS A 1 47  ? 10.454 6.772  31.959  1.00 50.75  ? 47  HIS A CE1 1 
ATOM   309  N NE2 . HIS A 1 47  ? 11.318 6.160  32.750  1.00 45.58  ? 47  HIS A NE2 1 
ATOM   310  N N   . HIS A 1 48  ? 12.505 11.144 31.308  1.00 31.23  ? 48  HIS A N   1 
ATOM   311  C CA  . HIS A 1 48  ? 12.557 11.112 29.852  1.00 36.74  ? 48  HIS A CA  1 
ATOM   312  C C   . HIS A 1 48  ? 13.809 11.749 29.264  1.00 38.96  ? 48  HIS A C   1 
ATOM   313  O O   . HIS A 1 48  ? 14.142 11.459 28.110  1.00 35.60  ? 48  HIS A O   1 
ATOM   314  C CB  . HIS A 1 48  ? 11.320 11.800 29.273  1.00 32.52  ? 48  HIS A CB  1 
ATOM   315  C CG  . HIS A 1 48  ? 10.060 11.018 29.459  1.00 40.20  ? 48  HIS A CG  1 
ATOM   316  N ND1 . HIS A 1 48  ? 9.878  9.765  28.912  1.00 42.18  ? 48  HIS A ND1 1 
ATOM   317  C CD2 . HIS A 1 48  ? 8.922  11.304 30.134  1.00 35.78  ? 48  HIS A CD2 1 
ATOM   318  C CE1 . HIS A 1 48  ? 8.681  9.314  29.241  1.00 36.47  ? 48  HIS A CE1 1 
ATOM   319  N NE2 . HIS A 1 48  ? 8.081  10.229 29.982  1.00 42.88  ? 48  HIS A NE2 1 
ATOM   320  N N   . PHE A 1 49  ? 14.507 12.601 30.010  1.00 35.23  ? 49  PHE A N   1 
ATOM   321  C CA  . PHE A 1 49  ? 15.636 13.353 29.473  1.00 39.05  ? 49  PHE A CA  1 
ATOM   322  C C   . PHE A 1 49  ? 16.829 13.253 30.414  1.00 39.72  ? 49  PHE A C   1 
ATOM   323  O O   . PHE A 1 49  ? 16.692 13.475 31.620  1.00 36.47  ? 49  PHE A O   1 
ATOM   324  C CB  . PHE A 1 49  ? 15.235 14.813 29.244  1.00 31.34  ? 49  PHE A CB  1 
ATOM   325  C CG  . PHE A 1 49  ? 14.149 14.974 28.223  1.00 27.92  ? 49  PHE A CG  1 
ATOM   326  C CD1 . PHE A 1 49  ? 14.454 15.030 26.872  1.00 32.93  ? 49  PHE A CD1 1 
ATOM   327  C CD2 . PHE A 1 49  ? 12.819 15.004 28.607  1.00 32.16  ? 49  PHE A CD2 1 
ATOM   328  C CE1 . PHE A 1 49  ? 13.453 15.159 25.923  1.00 36.61  ? 49  PHE A CE1 1 
ATOM   329  C CE2 . PHE A 1 49  ? 11.811 15.127 27.662  1.00 38.62  ? 49  PHE A CE2 1 
ATOM   330  C CZ  . PHE A 1 49  ? 12.128 15.204 26.320  1.00 37.61  ? 49  PHE A CZ  1 
ATOM   331  N N   . SER A 1 50  ? 18.005 12.947 29.851  1.00 41.07  ? 50  SER A N   1 
ATOM   332  C CA  . SER A 1 50  ? 19.172 12.624 30.670  1.00 49.25  ? 50  SER A CA  1 
ATOM   333  C C   . SER A 1 50  ? 19.668 13.822 31.469  1.00 41.46  ? 50  SER A C   1 
ATOM   334  O O   . SER A 1 50  ? 20.247 13.648 32.547  1.00 47.11  ? 50  SER A O   1 
ATOM   335  C CB  . SER A 1 50  ? 20.297 12.080 29.788  1.00 45.36  ? 50  SER A CB  1 
ATOM   336  O OG  . SER A 1 50  ? 19.779 11.222 28.786  1.00 57.77  ? 50  SER A OG  1 
ATOM   337  N N   . SER A 1 51  ? 19.464 15.034 30.965  1.00 38.14  ? 51  SER A N   1 
ATOM   338  C CA  . SER A 1 51  ? 19.874 16.233 31.678  1.00 38.11  ? 51  SER A CA  1 
ATOM   339  C C   . SER A 1 51  ? 19.055 17.401 31.155  1.00 35.64  ? 51  SER A C   1 
ATOM   340  O O   . SER A 1 51  ? 18.441 17.320 30.089  1.00 33.00  ? 51  SER A O   1 
ATOM   341  C CB  . SER A 1 51  ? 21.377 16.506 31.516  1.00 36.65  ? 51  SER A CB  1 
ATOM   342  O OG  . SER A 1 51  ? 21.671 17.082 30.250  1.00 33.59  ? 51  SER A OG  1 
ATOM   343  N N   . ALA A 1 52  ? 19.057 18.493 31.922  1.00 32.20  ? 52  ALA A N   1 
ATOM   344  C CA  . ALA A 1 52  ? 18.386 19.705 31.467  1.00 38.91  ? 52  ALA A CA  1 
ATOM   345  C C   . ALA A 1 52  ? 18.982 20.200 30.155  1.00 38.27  ? 52  ALA A C   1 
ATOM   346  O O   . ALA A 1 52  ? 18.263 20.720 29.291  1.00 28.65  ? 52  ALA A O   1 
ATOM   347  C CB  . ALA A 1 52  ? 18.468 20.785 32.544  1.00 34.38  ? 52  ALA A CB  1 
ATOM   348  N N   . SER A 1 53  ? 20.295 20.028 29.978  1.00 30.32  ? 53  SER A N   1 
ATOM   349  C CA  . SER A 1 53  ? 20.938 20.440 28.733  1.00 32.28  ? 53  SER A CA  1 
ATOM   350  C C   . SER A 1 53  ? 20.588 19.512 27.573  1.00 32.17  ? 53  SER A C   1 
ATOM   351  O O   . SER A 1 53  ? 20.503 19.966 26.428  1.00 29.67  ? 53  SER A O   1 
ATOM   352  C CB  . SER A 1 53  ? 22.452 20.507 28.930  1.00 41.75  ? 53  SER A CB  1 
ATOM   353  O OG  . SER A 1 53  ? 22.835 21.801 29.364  1.00 43.18  ? 53  SER A OG  1 
ATOM   354  N N   . HIS A 1 54  ? 20.397 18.217 27.839  1.00 29.06  ? 54  HIS A N   1 
ATOM   355  C CA  . HIS A 1 54  ? 19.907 17.316 26.798  1.00 31.49  ? 54  HIS A CA  1 
ATOM   356  C C   . HIS A 1 54  ? 18.541 17.763 26.291  1.00 29.05  ? 54  HIS A C   1 
ATOM   357  O O   . HIS A 1 54  ? 18.278 17.741 25.083  1.00 29.69  ? 54  HIS A O   1 
ATOM   358  C CB  . HIS A 1 54  ? 19.820 15.886 27.333  1.00 34.20  ? 54  HIS A CB  1 
ATOM   359  C CG  . HIS A 1 54  ? 21.124 15.150 27.330  1.00 34.92  ? 54  HIS A CG  1 
ATOM   360  N ND1 . HIS A 1 54  ? 22.070 15.307 28.321  1.00 39.98  ? 54  HIS A ND1 1 
ATOM   361  C CD2 . HIS A 1 54  ? 21.628 14.232 26.471  1.00 39.00  ? 54  HIS A CD2 1 
ATOM   362  C CE1 . HIS A 1 54  ? 23.105 14.526 28.066  1.00 39.20  ? 54  HIS A CE1 1 
ATOM   363  N NE2 . HIS A 1 54  ? 22.863 13.864 26.949  1.00 52.00  ? 54  HIS A NE2 1 
ATOM   364  N N   . LEU A 1 55  ? 17.653 18.160 27.208  1.00 26.34  ? 55  LEU A N   1 
ATOM   365  C CA  . LEU A 1 55  ? 16.322 18.620 26.822  1.00 28.12  ? 55  LEU A CA  1 
ATOM   366  C C   . LEU A 1 55  ? 16.400 19.896 25.990  1.00 29.16  ? 55  LEU A C   1 
ATOM   367  O O   . LEU A 1 55  ? 15.699 20.034 24.981  1.00 26.76  ? 55  LEU A O   1 
ATOM   368  C CB  . LEU A 1 55  ? 15.475 18.839 28.081  1.00 29.10  ? 55  LEU A CB  1 
ATOM   369  C CG  . LEU A 1 55  ? 14.041 19.362 27.973  1.00 31.96  ? 55  LEU A CG  1 
ATOM   370  C CD1 . LEU A 1 55  ? 13.270 18.676 26.853  1.00 29.79  ? 55  LEU A CD1 1 
ATOM   371  C CD2 . LEU A 1 55  ? 13.329 19.192 29.307  1.00 31.90  ? 55  LEU A CD2 1 
ATOM   372  N N   . LYS A 1 56  ? 17.245 20.842 26.404  1.00 25.88  ? 56  LYS A N   1 
ATOM   373  C CA  . LYS A 1 56  ? 17.409 22.080 25.647  1.00 25.47  ? 56  LYS A CA  1 
ATOM   374  C C   . LYS A 1 56  ? 17.891 21.801 24.233  1.00 26.31  ? 56  LYS A C   1 
ATOM   375  O O   . LYS A 1 56  ? 17.403 22.405 23.272  1.00 28.03  ? 56  LYS A O   1 
ATOM   376  C CB  . LYS A 1 56  ? 18.402 23.002 26.356  1.00 28.49  ? 56  LYS A CB  1 
ATOM   377  C CG  . LYS A 1 56  ? 17.848 23.702 27.587  1.00 31.70  ? 56  LYS A CG  1 
ATOM   378  C CD  . LYS A 1 56  ? 18.955 24.498 28.271  1.00 30.83  ? 56  LYS A CD  1 
ATOM   379  C CE  . LYS A 1 56  ? 18.448 25.226 29.506  1.00 39.55  ? 56  LYS A CE  1 
ATOM   380  N NZ  . LYS A 1 56  ? 19.559 25.520 30.456  1.00 40.32  ? 56  LYS A NZ  1 
ATOM   381  N N   . ALA A 1 57  ? 18.864 20.895 24.087  1.00 29.82  ? 57  ALA A N   1 
ATOM   382  C CA  . ALA A 1 57  ? 19.436 20.626 22.773  1.00 27.25  ? 57  ALA A CA  1 
ATOM   383  C C   . ALA A 1 57  ? 18.458 19.867 21.891  1.00 27.52  ? 57  ALA A C   1 
ATOM   384  O O   . ALA A 1 57  ? 18.392 20.101 20.679  1.00 30.23  ? 57  ALA A O   1 
ATOM   385  C CB  . ALA A 1 57  ? 20.743 19.843 22.916  1.00 25.55  ? 57  ALA A CB  1 
ATOM   386  N N   . GLU A 1 58  ? 17.705 18.942 22.477  1.00 25.54  ? 58  GLU A N   1 
ATOM   387  C CA  . GLU A 1 58  ? 16.720 18.202 21.703  1.00 23.61  ? 58  GLU A CA  1 
ATOM   388  C C   . GLU A 1 58  ? 15.591 19.113 21.232  1.00 29.18  ? 58  GLU A C   1 
ATOM   389  O O   . GLU A 1 58  ? 15.107 18.975 20.103  1.00 28.06  ? 58  GLU A O   1 
ATOM   390  C CB  . GLU A 1 58  ? 16.184 17.040 22.534  1.00 30.96  ? 58  GLU A CB  1 
ATOM   391  C CG  . GLU A 1 58  ? 15.481 15.982 21.720  1.00 44.26  ? 58  GLU A CG  1 
ATOM   392  C CD  . GLU A 1 58  ? 15.209 14.722 22.515  1.00 46.73  ? 58  GLU A CD  1 
ATOM   393  O OE1 . GLU A 1 58  ? 15.878 14.505 23.548  1.00 53.52  ? 58  GLU A OE1 1 
ATOM   394  O OE2 . GLU A 1 58  ? 14.318 13.950 22.108  1.00 50.93  ? 58  GLU A OE2 1 
ATOM   395  N N   . ALA A 1 59  ? 15.173 20.062 22.072  1.00 27.06  ? 59  ALA A N   1 
ATOM   396  C CA  . ALA A 1 59  ? 14.145 21.013 21.657  1.00 28.04  ? 59  ALA A CA  1 
ATOM   397  C C   . ALA A 1 59  ? 14.678 21.963 20.595  1.00 36.63  ? 59  ALA A C   1 
ATOM   398  O O   . ALA A 1 59  ? 13.957 22.324 19.654  1.00 30.16  ? 59  ALA A O   1 
ATOM   399  C CB  . ALA A 1 59  ? 13.639 21.799 22.865  1.00 30.07  ? 59  ALA A CB  1 
ATOM   400  N N   . PHE A 1 60  ? 15.935 22.385 20.740  1.00 26.47  ? 60  PHE A N   1 
ATOM   401  C CA  . PHE A 1 60  ? 16.564 23.233 19.735  1.00 28.55  ? 60  PHE A CA  1 
ATOM   402  C C   . PHE A 1 60  ? 16.591 22.545 18.376  1.00 28.78  ? 60  PHE A C   1 
ATOM   403  O O   . PHE A 1 60  ? 16.229 23.145 17.359  1.00 31.81  ? 60  PHE A O   1 
ATOM   404  C CB  . PHE A 1 60  ? 17.977 23.614 20.184  1.00 27.02  ? 60  PHE A CB  1 
ATOM   405  C CG  . PHE A 1 60  ? 18.797 24.279 19.108  1.00 29.97  ? 60  PHE A CG  1 
ATOM   406  C CD1 . PHE A 1 60  ? 18.506 25.566 18.688  1.00 29.31  ? 60  PHE A CD1 1 
ATOM   407  C CD2 . PHE A 1 60  ? 19.864 23.616 18.526  1.00 37.44  ? 60  PHE A CD2 1 
ATOM   408  C CE1 . PHE A 1 60  ? 19.260 26.179 17.698  1.00 32.96  ? 60  PHE A CE1 1 
ATOM   409  C CE2 . PHE A 1 60  ? 20.624 24.222 17.534  1.00 33.78  ? 60  PHE A CE2 1 
ATOM   410  C CZ  . PHE A 1 60  ? 20.323 25.506 17.125  1.00 31.53  ? 60  PHE A CZ  1 
ATOM   411  N N   . LEU A 1 61  ? 17.006 21.275 18.344  1.00 29.02  ? 61  LEU A N   1 
ATOM   412  C CA  . LEU A 1 61  ? 17.074 20.548 17.081  1.00 31.78  ? 61  LEU A CA  1 
ATOM   413  C C   . LEU A 1 61  ? 15.691 20.358 16.474  1.00 30.56  ? 61  LEU A C   1 
ATOM   414  O O   . LEU A 1 61  ? 15.535 20.412 15.249  1.00 35.14  ? 61  LEU A O   1 
ATOM   415  C CB  . LEU A 1 61  ? 17.760 19.198 17.288  1.00 35.35  ? 61  LEU A CB  1 
ATOM   416  C CG  . LEU A 1 61  ? 19.281 19.236 17.414  1.00 35.39  ? 61  LEU A CG  1 
ATOM   417  C CD1 . LEU A 1 61  ? 19.824 17.847 17.720  1.00 38.89  ? 61  LEU A CD1 1 
ATOM   418  C CD2 . LEU A 1 61  ? 19.914 19.802 16.151  1.00 33.81  ? 61  LEU A CD2 1 
ATOM   419  N N   . LYS A 1 62  ? 14.676 20.135 17.313  1.00 29.66  ? 62  LYS A N   1 
ATOM   420  C CA  . LYS A 1 62  ? 13.308 20.033 16.816  1.00 31.83  ? 62  LYS A CA  1 
ATOM   421  C C   . LYS A 1 62  ? 12.846 21.352 16.214  1.00 39.87  ? 62  LYS A C   1 
ATOM   422  O O   . LYS A 1 62  ? 12.186 21.371 15.168  1.00 38.85  ? 62  LYS A O   1 
ATOM   423  C CB  . LYS A 1 62  ? 12.368 19.605 17.949  1.00 33.04  ? 62  LYS A CB  1 
ATOM   424  C CG  . LYS A 1 62  ? 12.374 18.118 18.239  1.00 45.55  ? 62  LYS A CG  1 
ATOM   425  C CD  . LYS A 1 62  ? 11.840 17.327 17.052  1.00 54.95  ? 62  LYS A CD  1 
ATOM   426  C CE  . LYS A 1 62  ? 10.401 16.884 17.291  1.00 64.65  ? 62  LYS A CE  1 
ATOM   427  N NZ  . LYS A 1 62  ? 10.308 15.476 17.774  1.00 70.76  ? 62  LYS A NZ  1 
ATOM   428  N N   . LEU A 1 63  ? 13.190 22.469 16.857  1.00 33.57  ? 63  LEU A N   1 
ATOM   429  C CA  . LEU A 1 63  ? 12.807 23.769 16.321  1.00 32.26  ? 63  LEU A CA  1 
ATOM   430  C C   . LEU A 1 63  ? 13.548 24.083 15.028  1.00 40.50  ? 63  LEU A C   1 
ATOM   431  O O   . LEU A 1 63  ? 13.007 24.773 14.155  1.00 38.16  ? 63  LEU A O   1 
ATOM   432  C CB  . LEU A 1 63  ? 13.058 24.850 17.371  1.00 35.16  ? 63  LEU A CB  1 
ATOM   433  C CG  . LEU A 1 63  ? 12.012 24.865 18.491  1.00 33.59  ? 63  LEU A CG  1 
ATOM   434  C CD1 . LEU A 1 63  ? 12.398 25.831 19.590  1.00 29.21  ? 63  LEU A CD1 1 
ATOM   435  C CD2 . LEU A 1 63  ? 10.645 25.222 17.924  1.00 37.30  ? 63  LEU A CD2 1 
ATOM   436  N N   . MET A 1 64  ? 14.777 23.581 14.882  1.00 39.65  ? 64  MET A N   1 
ATOM   437  C CA  . MET A 1 64  ? 15.539 23.833 13.664  1.00 44.33  ? 64  MET A CA  1 
ATOM   438  C C   . MET A 1 64  ? 15.008 22.991 12.510  1.00 50.11  ? 64  MET A C   1 
ATOM   439  O O   . MET A 1 64  ? 14.916 23.468 11.372  1.00 42.97  ? 64  MET A O   1 
ATOM   440  C CB  . MET A 1 64  ? 17.022 23.545 13.909  1.00 44.96  ? 64  MET A CB  1 
ATOM   441  C CG  . MET A 1 64  ? 17.732 24.620 14.727  1.00 31.74  ? 64  MET A CG  1 
ATOM   442  S SD  . MET A 1 64  ? 17.415 26.305 14.175  1.00 39.84  ? 64  MET A SD  1 
ATOM   443  C CE  . MET A 1 64  ? 16.498 26.988 15.552  1.00 46.19  ? 64  MET A CE  1 
ATOM   444  N N   . GLU A 1 65  ? 14.655 21.732 12.789  1.00 40.81  ? 65  GLU A N   1 
ATOM   445  C CA  . GLU A 1 65  ? 13.954 20.915 11.802  1.00 51.54  ? 65  GLU A CA  1 
ATOM   446  C C   . GLU A 1 65  ? 12.625 21.553 11.424  1.00 51.35  ? 65  GLU A C   1 
ATOM   447  O O   . GLU A 1 65  ? 12.184 21.470 10.272  1.00 49.78  ? 65  GLU A O   1 
ATOM   448  C CB  . GLU A 1 65  ? 13.723 19.510 12.359  1.00 57.26  ? 65  GLU A CB  1 
ATOM   449  C CG  . GLU A 1 65  ? 14.743 18.475 11.922  1.00 67.50  ? 65  GLU A CG  1 
ATOM   450  C CD  . GLU A 1 65  ? 15.131 17.542 13.053  1.00 84.50  ? 65  GLU A CD  1 
ATOM   451  O OE1 . GLU A 1 65  ? 16.339 17.259 13.209  1.00 77.35  ? 65  GLU A OE1 1 
ATOM   452  O OE2 . GLU A 1 65  ? 14.225 17.093 13.789  1.00 82.53  ? 65  GLU A OE2 1 
ATOM   453  N N   . GLN A 1 66  ? 11.977 22.196 12.393  1.00 48.19  ? 66  GLN A N   1 
ATOM   454  C CA  . GLN A 1 66  ? 10.720 22.888 12.147  1.00 41.85  ? 66  GLN A CA  1 
ATOM   455  C C   . GLN A 1 66  ? 10.937 24.120 11.274  1.00 53.66  ? 66  GLN A C   1 
ATOM   456  O O   . GLN A 1 66  ? 10.095 24.450 10.430  1.00 53.78  ? 66  GLN A O   1 
ATOM   457  C CB  . GLN A 1 66  ? 10.102 23.252 13.494  1.00 53.06  ? 66  GLN A CB  1 
ATOM   458  C CG  . GLN A 1 66  ? 8.972  24.236 13.492  1.00 58.13  ? 66  GLN A CG  1 
ATOM   459  C CD  . GLN A 1 66  ? 8.028  23.980 14.648  1.00 50.24  ? 66  GLN A CD  1 
ATOM   460  O OE1 . GLN A 1 66  ? 7.525  22.868 14.821  1.00 61.01  ? 66  GLN A OE1 1 
ATOM   461  N NE2 . GLN A 1 66  ? 7.799  25.004 15.462  1.00 43.86  ? 66  GLN A NE2 1 
ATOM   462  N N   . LEU A 1 67  ? 12.073 24.800 11.455  1.00 48.73  ? 67  LEU A N   1 
ATOM   463  C CA  . LEU A 1 67  ? 12.418 25.943 10.614  1.00 50.64  ? 67  LEU A CA  1 
ATOM   464  C C   . LEU A 1 67  ? 12.608 25.526 9.161   1.00 43.43  ? 67  LEU A C   1 
ATOM   465  O O   . LEU A 1 67  ? 12.157 26.222 8.242   1.00 48.24  ? 67  LEU A O   1 
ATOM   466  C CB  . LEU A 1 67  ? 13.683 26.611 11.156  1.00 46.07  ? 67  LEU A CB  1 
ATOM   467  C CG  . LEU A 1 67  ? 14.486 27.572 10.272  1.00 47.36  ? 67  LEU A CG  1 
ATOM   468  C CD1 . LEU A 1 67  ? 13.632 28.705 9.759   1.00 60.14  ? 67  LEU A CD1 1 
ATOM   469  C CD2 . LEU A 1 67  ? 15.683 28.116 11.029  1.00 50.41  ? 67  LEU A CD2 1 
ATOM   470  N N   . ASP A 1 68  ? 13.285 24.398 8.934   1.00 42.13  ? 68  ASP A N   1 
ATOM   471  C CA  . ASP A 1 68  ? 13.447 23.884 7.578   1.00 54.92  ? 68  ASP A CA  1 
ATOM   472  C C   . ASP A 1 68  ? 12.101 23.518 6.961   1.00 63.62  ? 68  ASP A C   1 
ATOM   473  O O   . ASP A 1 68  ? 11.849 23.807 5.784   1.00 60.50  ? 68  ASP A O   1 
ATOM   474  C CB  . ASP A 1 68  ? 14.397 22.683 7.597   1.00 57.13  ? 68  ASP A CB  1 
ATOM   475  C CG  . ASP A 1 68  ? 14.223 21.770 6.394   1.00 83.95  ? 68  ASP A CG  1 
ATOM   476  O OD1 . ASP A 1 68  ? 14.871 22.013 5.352   1.00 79.26  ? 68  ASP A OD1 1 
ATOM   477  O OD2 . ASP A 1 68  ? 13.465 20.783 6.508   1.00 85.48  ? 68  ASP A OD2 1 
ATOM   478  N N   . GLU A 1 69  ? 11.222 22.890 7.745   1.00 57.79  ? 69  GLU A N   1 
ATOM   479  C CA  . GLU A 1 69  ? 9.885  22.556 7.265   1.00 60.04  ? 69  GLU A CA  1 
ATOM   480  C C   . GLU A 1 69  ? 9.126  23.806 6.840   1.00 60.51  ? 69  GLU A C   1 
ATOM   481  O O   . GLU A 1 69  ? 8.542  23.853 5.751   1.00 62.74  ? 69  GLU A O   1 
ATOM   482  C CB  . GLU A 1 69  ? 9.122  21.813 8.361   1.00 69.04  ? 69  GLU A CB  1 
ATOM   483  C CG  . GLU A 1 69  ? 9.302  20.311 8.333   1.00 76.80  ? 69  GLU A CG  1 
ATOM   484  C CD  . GLU A 1 69  ? 8.859  19.652 9.627   1.00 82.65  ? 69  GLU A CD  1 
ATOM   485  O OE1 . GLU A 1 69  ? 7.840  20.088 10.207  1.00 79.95  ? 69  GLU A OE1 1 
ATOM   486  O OE2 . GLU A 1 69  ? 9.539  18.703 10.071  1.00 78.64  ? 69  GLU A OE2 1 
ATOM   487  N N   . ILE A 1 70  ? 9.127  24.832 7.693   1.00 47.02  ? 70  ILE A N   1 
ATOM   488  C CA  . ILE A 1 70  ? 8.440  26.079 7.372   1.00 51.30  ? 70  ILE A CA  1 
ATOM   489  C C   . ILE A 1 70  ? 9.016  26.680 6.097   1.00 67.94  ? 70  ILE A C   1 
ATOM   490  O O   . ILE A 1 70  ? 8.281  27.178 5.234   1.00 60.59  ? 70  ILE A O   1 
ATOM   491  C CB  . ILE A 1 70  ? 8.556  27.061 8.550   1.00 56.98  ? 70  ILE A CB  1 
ATOM   492  C CG1 . ILE A 1 70  ? 7.711  26.592 9.734   1.00 54.52  ? 70  ILE A CG1 1 
ATOM   493  C CG2 . ILE A 1 70  ? 8.080  28.435 8.122   1.00 59.36  ? 70  ILE A CG2 1 
ATOM   494  C CD1 . ILE A 1 70  ? 7.489  27.667 10.778  1.00 62.98  ? 70  ILE A CD1 1 
ATOM   495  N N   . GLU A 1 71  ? 10.343 26.629 5.956   1.00 52.49  ? 71  GLU A N   1 
ATOM   496  C CA  . GLU A 1 71  ? 10.994 27.205 4.787   1.00 53.82  ? 71  GLU A CA  1 
ATOM   497  C C   . GLU A 1 71  ? 10.600 26.479 3.507   1.00 54.05  ? 71  GLU A C   1 
ATOM   498  O O   . GLU A 1 71  ? 10.527 27.104 2.443   1.00 57.28  ? 71  GLU A O   1 
ATOM   499  C CB  . GLU A 1 71  ? 12.510 27.187 4.975   1.00 48.76  ? 71  GLU A CB  1 
ATOM   500  C CG  . GLU A 1 71  ? 13.058 28.417 5.695   1.00 55.80  ? 71  GLU A CG  1 
ATOM   501  C CD  . GLU A 1 71  ? 14.568 28.376 5.855   1.00 57.96  ? 71  GLU A CD  1 
ATOM   502  O OE1 . GLU A 1 71  ? 15.189 27.424 5.340   1.00 60.23  ? 71  GLU A OE1 1 
ATOM   503  O OE2 . GLU A 1 71  ? 15.134 29.288 6.496   1.00 51.48  ? 71  GLU A OE2 1 
ATOM   504  N N   . GLN A 1 72  ? 10.331 25.175 3.587   1.00 59.19  ? 72  GLN A N   1 
ATOM   505  C CA  . GLN A 1 72  ? 9.941  24.407 2.410   1.00 56.51  ? 72  GLN A CA  1 
ATOM   506  C C   . GLN A 1 72  ? 8.511  24.678 1.966   1.00 70.20  ? 72  GLN A C   1 
ATOM   507  O O   . GLN A 1 72  ? 8.083  24.107 0.958   1.00 64.98  ? 72  GLN A O   1 
ATOM   508  C CB  . GLN A 1 72  ? 10.106 22.910 2.670   1.00 59.30  ? 72  GLN A CB  1 
ATOM   509  C CG  . GLN A 1 72  ? 11.524 22.402 2.518   1.00 64.11  ? 72  GLN A CG  1 
ATOM   510  C CD  . GLN A 1 72  ? 11.742 21.107 3.269   1.00 88.41  ? 72  GLN A CD  1 
ATOM   511  O OE1 . GLN A 1 72  ? 11.667 21.069 4.497   1.00 88.33  ? 72  GLN A OE1 1 
ATOM   512  N NE2 . GLN A 1 72  ? 12.016 20.035 2.534   1.00 94.16  ? 72  GLN A NE2 1 
ATOM   513  N N   . THR A 1 73  ? 7.762  25.513 2.684   1.00 72.56  ? 73  THR A N   1 
ATOM   514  C CA  . THR A 1 73  ? 6.402  25.846 2.286   1.00 76.34  ? 73  THR A CA  1 
ATOM   515  C C   . THR A 1 73  ? 6.290  27.214 1.630   1.00 69.40  ? 73  THR A C   1 
ATOM   516  O O   . THR A 1 73  ? 5.250  27.509 1.031   1.00 79.84  ? 73  THR A O   1 
ATOM   517  C CB  . THR A 1 73  ? 5.453  25.779 3.490   1.00 69.62  ? 73  THR A CB  1 
ATOM   518  O OG1 . THR A 1 73  ? 5.585  26.968 4.279   1.00 71.08  ? 73  THR A OG1 1 
ATOM   519  C CG2 . THR A 1 73  ? 5.763  24.562 4.345   1.00 67.00  ? 73  THR A CG2 1 
ATOM   520  N N   . LEU A 1 74  ? 7.313  28.059 1.734   1.00 70.41  ? 74  LEU A N   1 
ATOM   521  C CA  . LEU A 1 74  ? 7.351  29.250 0.898   1.00 75.50  ? 74  LEU A CA  1 
ATOM   522  C C   . LEU A 1 74  ? 7.434  28.844 -0.563  1.00 76.08  ? 74  LEU A C   1 
ATOM   523  O O   . LEU A 1 74  ? 8.264  28.015 -0.948  1.00 67.54  ? 74  LEU A O   1 
ATOM   524  C CB  . LEU A 1 74  ? 8.528  30.150 1.261   1.00 72.16  ? 74  LEU A CB  1 
ATOM   525  C CG  . LEU A 1 74  ? 8.521  30.811 2.635   1.00 73.72  ? 74  LEU A CG  1 
ATOM   526  C CD1 . LEU A 1 74  ? 9.304  30.008 3.639   1.00 64.36  ? 74  LEU A CD1 1 
ATOM   527  C CD2 . LEU A 1 74  ? 9.092  32.207 2.493   1.00 73.06  ? 74  LEU A CD2 1 
ATOM   528  N N   . GLN A 1 75  ? 6.559  29.421 -1.375  1.00 75.45  ? 75  GLN A N   1 
ATOM   529  C CA  . GLN A 1 75  ? 6.498  29.059 -2.779  1.00 74.89  ? 75  GLN A CA  1 
ATOM   530  C C   . GLN A 1 75  ? 7.638  29.728 -3.533  1.00 64.03  ? 75  GLN A C   1 
ATOM   531  O O   . GLN A 1 75  ? 7.833  30.944 -3.437  1.00 65.46  ? 75  GLN A O   1 
ATOM   532  C CB  . GLN A 1 75  ? 5.147  29.455 -3.367  1.00 75.63  ? 75  GLN A CB  1 
ATOM   533  C CG  . GLN A 1 75  ? 3.979  28.890 -2.575  1.00 87.19  ? 75  GLN A CG  1 
ATOM   534  C CD  . GLN A 1 75  ? 3.267  27.772 -3.306  1.00 104.66 ? 75  GLN A CD  1 
ATOM   535  O OE1 . GLN A 1 75  ? 3.896  26.823 -3.774  1.00 100.50 ? 75  GLN A OE1 1 
ATOM   536  N NE2 . GLN A 1 75  ? 1.947  27.875 -3.403  1.00 94.37  ? 75  GLN A NE2 1 
ATOM   537  N N   . THR A 1 76  ? 8.408  28.921 -4.256  1.00 62.86  ? 76  THR A N   1 
ATOM   538  C CA  . THR A 1 76  ? 9.480  29.404 -5.110  1.00 69.50  ? 76  THR A CA  1 
ATOM   539  C C   . THR A 1 76  ? 9.282  28.858 -6.514  1.00 73.36  ? 76  THR A C   1 
ATOM   540  O O   . THR A 1 76  ? 8.698  27.787 -6.706  1.00 65.23  ? 76  THR A O   1 
ATOM   541  C CB  . THR A 1 76  ? 10.861 28.986 -4.587  1.00 66.97  ? 76  THR A CB  1 
ATOM   542  O OG1 . THR A 1 76  ? 10.966 27.556 -4.603  1.00 62.13  ? 76  THR A OG1 1 
ATOM   543  C CG2 . THR A 1 76  ? 11.071 29.493 -3.171  1.00 53.93  ? 76  THR A CG2 1 
ATOM   544  N N   . THR A 1 77  ? 9.765  29.611 -7.498  1.00 65.22  ? 77  THR A N   1 
ATOM   545  C CA  . THR A 1 77  ? 9.755  29.165 -8.881  1.00 73.99  ? 77  THR A CA  1 
ATOM   546  C C   . THR A 1 77  ? 11.128 28.726 -9.363  1.00 72.52  ? 77  THR A C   1 
ATOM   547  O O   . THR A 1 77  ? 11.225 28.084 -10.414 1.00 69.33  ? 77  THR A O   1 
ATOM   548  C CB  . THR A 1 77  ? 9.227  30.279 -9.794  1.00 74.49  ? 77  THR A CB  1 
ATOM   549  O OG1 . THR A 1 77  ? 9.775  31.537 -9.380  1.00 73.69  ? 77  THR A OG1 1 
ATOM   550  C CG2 . THR A 1 77  ? 7.711  30.346 -9.718  1.00 75.90  ? 77  THR A CG2 1 
ATOM   551  N N   . SER A 1 78  ? 12.183 29.042 -8.616  1.00 55.24  ? 78  SER A N   1 
ATOM   552  C CA  . SER A 1 78  ? 13.540 28.738 -9.029  1.00 51.95  ? 78  SER A CA  1 
ATOM   553  C C   . SER A 1 78  ? 14.347 28.317 -7.813  1.00 52.39  ? 78  SER A C   1 
ATOM   554  O O   . SER A 1 78  ? 13.983 28.604 -6.669  1.00 43.11  ? 78  SER A O   1 
ATOM   555  C CB  . SER A 1 78  ? 14.208 29.946 -9.693  1.00 63.15  ? 78  SER A CB  1 
ATOM   556  O OG  . SER A 1 78  ? 14.118 31.092 -8.862  1.00 48.98  ? 78  SER A OG  1 
ATOM   557  N N   . GLN A 1 79  ? 15.458 27.629 -8.073  1.00 39.84  ? 79  GLN A N   1 
ATOM   558  C CA  . GLN A 1 79  ? 16.384 27.324 -6.993  1.00 38.64  ? 79  GLN A CA  1 
ATOM   559  C C   . GLN A 1 79  ? 17.137 28.569 -6.549  1.00 45.64  ? 79  GLN A C   1 
ATOM   560  O O   . GLN A 1 79  ? 17.635 28.611 -5.420  1.00 40.80  ? 79  GLN A O   1 
ATOM   561  C CB  . GLN A 1 79  ? 17.366 26.237 -7.429  1.00 45.15  ? 79  GLN A CB  1 
ATOM   562  C CG  . GLN A 1 79  ? 16.800 24.826 -7.408  1.00 49.45  ? 79  GLN A CG  1 
ATOM   563  C CD  . GLN A 1 79  ? 15.873 24.575 -6.241  1.00 45.53  ? 79  GLN A CD  1 
ATOM   564  O OE1 . GLN A 1 79  ? 16.320 24.326 -5.120  1.00 40.52  ? 79  GLN A OE1 1 
ATOM   565  N NE2 . GLN A 1 79  ? 14.570 24.616 -6.503  1.00 48.22  ? 79  GLN A NE2 1 
ATOM   566  N N   . PHE A 1 80  ? 17.239 29.571 -7.425  1.00 38.59  ? 80  PHE A N   1 
ATOM   567  C CA  . PHE A 1 80  ? 17.806 30.861 -7.046  1.00 35.31  ? 80  PHE A CA  1 
ATOM   568  C C   . PHE A 1 80  ? 17.015 31.476 -5.898  1.00 46.48  ? 80  PHE A C   1 
ATOM   569  O O   . PHE A 1 80  ? 17.590 31.961 -4.914  1.00 39.43  ? 80  PHE A O   1 
ATOM   570  C CB  . PHE A 1 80  ? 17.814 31.768 -8.279  1.00 43.61  ? 80  PHE A CB  1 
ATOM   571  C CG  . PHE A 1 80  ? 18.605 33.033 -8.126  1.00 53.85  ? 80  PHE A CG  1 
ATOM   572  C CD1 . PHE A 1 80  ? 19.987 33.007 -8.100  1.00 51.75  ? 80  PHE A CD1 1 
ATOM   573  C CD2 . PHE A 1 80  ? 17.964 34.261 -8.104  1.00 66.03  ? 80  PHE A CD2 1 
ATOM   574  C CE1 . PHE A 1 80  ? 20.716 34.180 -7.994  1.00 61.91  ? 80  PHE A CE1 1 
ATOM   575  C CE2 . PHE A 1 80  ? 18.686 35.436 -8.008  1.00 65.75  ? 80  PHE A CE2 1 
ATOM   576  C CZ  . PHE A 1 80  ? 20.064 35.393 -7.945  1.00 63.17  ? 80  PHE A CZ  1 
ATOM   577  N N   . GLN A 1 81  ? 15.686 31.431 -5.999  1.00 42.46  ? 81  GLN A N   1 
ATOM   578  C CA  . GLN A 1 81  ? 14.819 31.927 -4.936  1.00 43.93  ? 81  GLN A CA  1 
ATOM   579  C C   . GLN A 1 81  ? 14.978 31.113 -3.660  1.00 42.42  ? 81  GLN A C   1 
ATOM   580  O O   . GLN A 1 81  ? 15.043 31.673 -2.558  1.00 37.34  ? 81  GLN A O   1 
ATOM   581  C CB  . GLN A 1 81  ? 13.367 31.883 -5.406  1.00 44.17  ? 81  GLN A CB  1 
ATOM   582  C CG  . GLN A 1 81  ? 12.662 33.219 -5.486  1.00 68.87  ? 81  GLN A CG  1 
ATOM   583  C CD  . GLN A 1 81  ? 11.177 33.052 -5.750  1.00 89.53  ? 81  GLN A CD  1 
ATOM   584  O OE1 . GLN A 1 81  ? 10.774 32.603 -6.825  1.00 77.18  ? 81  GLN A OE1 1 
ATOM   585  N NE2 . GLN A 1 81  ? 10.356 33.391 -4.760  1.00 78.42  ? 81  GLN A NE2 1 
ATOM   586  N N   . ARG A 1 82  ? 15.017 29.785 -3.782  1.00 34.65  ? 82  ARG A N   1 
ATOM   587  C CA  . ARG A 1 82  ? 15.131 28.966 -2.583  1.00 38.89  ? 82  ARG A CA  1 
ATOM   588  C C   . ARG A 1 82  ? 16.467 29.175 -1.885  1.00 35.88  ? 82  ARG A C   1 
ATOM   589  O O   . ARG A 1 82  ? 16.543 29.053 -0.661  1.00 38.93  ? 82  ARG A O   1 
ATOM   590  C CB  . ARG A 1 82  ? 14.938 27.488 -2.911  1.00 40.35  ? 82  ARG A CB  1 
ATOM   591  C CG  . ARG A 1 82  ? 14.400 26.699 -1.718  1.00 59.67  ? 82  ARG A CG  1 
ATOM   592  C CD  . ARG A 1 82  ? 13.615 25.476 -2.148  1.00 61.35  ? 82  ARG A CD  1 
ATOM   593  N NE  . ARG A 1 82  ? 14.475 24.516 -2.829  1.00 83.73  ? 82  ARG A NE  1 
ATOM   594  C CZ  . ARG A 1 82  ? 14.532 23.223 -2.538  1.00 82.60  ? 82  ARG A CZ  1 
ATOM   595  N NH1 . ARG A 1 82  ? 13.777 22.695 -1.588  1.00 76.41  ? 82  ARG A NH1 1 
ATOM   596  N NH2 . ARG A 1 82  ? 15.374 22.443 -3.211  1.00 60.38  ? 82  ARG A NH2 1 
ATOM   597  N N   . LEU A 1 83  ? 17.526 29.495 -2.635  1.00 36.14  ? 83  LEU A N   1 
ATOM   598  C CA  . LEU A 1 83  ? 18.812 29.759 -1.994  1.00 29.54  ? 83  LEU A CA  1 
ATOM   599  C C   . LEU A 1 83  ? 18.759 31.024 -1.145  1.00 33.25  ? 83  LEU A C   1 
ATOM   600  O O   . LEU A 1 83  ? 19.313 31.054 -0.038  1.00 30.41  ? 83  LEU A O   1 
ATOM   601  C CB  . LEU A 1 83  ? 19.919 29.859 -3.043  1.00 35.17  ? 83  LEU A CB  1 
ATOM   602  C CG  . LEU A 1 83  ? 20.576 28.547 -3.476  1.00 34.75  ? 83  LEU A CG  1 
ATOM   603  C CD1 . LEU A 1 83  ? 21.694 28.827 -4.473  1.00 31.24  ? 83  LEU A CD1 1 
ATOM   604  C CD2 . LEU A 1 83  ? 21.129 27.798 -2.270  1.00 32.58  ? 83  LEU A CD2 1 
ATOM   605  N N   . PHE A 1 84  ? 18.103 32.077 -1.646  1.00 30.55  ? 84  PHE A N   1 
ATOM   606  C CA  . PHE A 1 84  ? 17.923 33.293 -0.853  1.00 41.24  ? 84  PHE A CA  1 
ATOM   607  C C   . PHE A 1 84  ? 17.242 32.991 0.472   1.00 36.25  ? 84  PHE A C   1 
ATOM   608  O O   . PHE A 1 84  ? 17.620 33.539 1.514   1.00 39.18  ? 84  PHE A O   1 
ATOM   609  C CB  . PHE A 1 84  ? 17.097 34.325 -1.622  1.00 36.99  ? 84  PHE A CB  1 
ATOM   610  C CG  . PHE A 1 84  ? 17.891 35.156 -2.578  1.00 47.37  ? 84  PHE A CG  1 
ATOM   611  C CD1 . PHE A 1 84  ? 18.698 36.185 -2.122  1.00 58.22  ? 84  PHE A CD1 1 
ATOM   612  C CD2 . PHE A 1 84  ? 17.825 34.916 -3.937  1.00 59.40  ? 84  PHE A CD2 1 
ATOM   613  C CE1 . PHE A 1 84  ? 19.428 36.955 -3.005  1.00 53.81  ? 84  PHE A CE1 1 
ATOM   614  C CE2 . PHE A 1 84  ? 18.548 35.682 -4.820  1.00 66.42  ? 84  PHE A CE2 1 
ATOM   615  C CZ  . PHE A 1 84  ? 19.350 36.700 -4.357  1.00 65.30  ? 84  PHE A CZ  1 
ATOM   616  N N   . ILE A 1 85  ? 16.225 32.129 0.446   1.00 32.20  ? 85  ILE A N   1 
ATOM   617  C CA  . ILE A 1 85  ? 15.507 31.777 1.665   1.00 32.68  ? 85  ILE A CA  1 
ATOM   618  C C   . ILE A 1 85  ? 16.410 30.980 2.604   1.00 32.04  ? 85  ILE A C   1 
ATOM   619  O O   . ILE A 1 85  ? 16.516 31.286 3.797   1.00 35.41  ? 85  ILE A O   1 
ATOM   620  C CB  . ILE A 1 85  ? 14.226 31.000 1.315   1.00 33.61  ? 85  ILE A CB  1 
ATOM   621  C CG1 . ILE A 1 85  ? 13.206 31.925 0.641   1.00 35.48  ? 85  ILE A CG1 1 
ATOM   622  C CG2 . ILE A 1 85  ? 13.630 30.357 2.562   1.00 39.89  ? 85  ILE A CG2 1 
ATOM   623  C CD1 . ILE A 1 85  ? 12.015 31.192 0.051   1.00 42.56  ? 85  ILE A CD1 1 
ATOM   624  N N   . LEU A 1 86  ? 17.071 29.946 2.078   1.00 32.19  ? 86  LEU A N   1 
ATOM   625  C CA  . LEU A 1 86  ? 17.932 29.114 2.915   1.00 29.97  ? 86  LEU A CA  1 
ATOM   626  C C   . LEU A 1 86  ? 19.091 29.902 3.510   1.00 36.02  ? 86  LEU A C   1 
ATOM   627  O O   . LEU A 1 86  ? 19.543 29.590 4.616   1.00 36.76  ? 86  LEU A O   1 
ATOM   628  C CB  . LEU A 1 86  ? 18.469 27.930 2.113   1.00 37.27  ? 86  LEU A CB  1 
ATOM   629  C CG  . LEU A 1 86  ? 17.482 26.838 1.712   1.00 42.12  ? 86  LEU A CG  1 
ATOM   630  C CD1 . LEU A 1 86  ? 18.124 25.899 0.699   1.00 43.86  ? 86  LEU A CD1 1 
ATOM   631  C CD2 . LEU A 1 86  ? 17.008 26.075 2.943   1.00 46.45  ? 86  LEU A CD2 1 
ATOM   632  N N   . LEU A 1 87  ? 19.588 30.916 2.805   1.00 33.72  ? 87  LEU A N   1 
ATOM   633  C CA  . LEU A 1 87  ? 20.700 31.716 3.308   1.00 33.15  ? 87  LEU A CA  1 
ATOM   634  C C   . LEU A 1 87  ? 20.262 32.906 4.156   1.00 46.72  ? 87  LEU A C   1 
ATOM   635  O O   . LEU A 1 87  ? 21.121 33.686 4.585   1.00 41.19  ? 87  LEU A O   1 
ATOM   636  C CB  . LEU A 1 87  ? 21.572 32.202 2.145   1.00 29.56  ? 87  LEU A CB  1 
ATOM   637  C CG  . LEU A 1 87  ? 22.315 31.084 1.410   1.00 30.81  ? 87  LEU A CG  1 
ATOM   638  C CD1 . LEU A 1 87  ? 22.937 31.602 0.135   1.00 30.03  ? 87  LEU A CD1 1 
ATOM   639  C CD2 . LEU A 1 87  ? 23.387 30.485 2.326   1.00 33.70  ? 87  LEU A CD2 1 
ATOM   640  N N   . GLY A 1 88  ? 18.963 33.064 4.412   1.00 41.35  ? 88  GLY A N   1 
ATOM   641  C CA  . GLY A 1 88  ? 18.479 34.098 5.308   1.00 41.36  ? 88  GLY A CA  1 
ATOM   642  C C   . GLY A 1 88  ? 18.322 35.474 4.701   1.00 44.87  ? 88  GLY A C   1 
ATOM   643  O O   . GLY A 1 88  ? 18.133 36.443 5.445   1.00 48.30  ? 88  GLY A O   1 
ATOM   644  N N   . ALA A 1 89  ? 18.377 35.595 3.379   1.00 43.60  ? 89  ALA A N   1 
ATOM   645  C CA  . ALA A 1 89  ? 18.321 36.901 2.736   1.00 48.03  ? 89  ALA A CA  1 
ATOM   646  C C   . ALA A 1 89  ? 16.908 37.458 2.608   1.00 54.97  ? 89  ALA A C   1 
ATOM   647  O O   . ALA A 1 89  ? 16.752 38.586 2.130   1.00 56.07  ? 89  ALA A O   1 
ATOM   648  C CB  . ALA A 1 89  ? 18.965 36.829 1.349   1.00 45.29  ? 89  ALA A CB  1 
ATOM   649  N N   . GLU A 1 90  ? 15.879 36.719 3.022   1.00 60.76  ? 90  GLU A N   1 
ATOM   650  C CA  . GLU A 1 90  ? 14.505 37.137 2.779   1.00 57.94  ? 90  GLU A CA  1 
ATOM   651  C C   . GLU A 1 90  ? 13.726 37.448 4.051   1.00 70.94  ? 90  GLU A C   1 
ATOM   652  O O   . GLU A 1 90  ? 12.550 37.818 3.954   1.00 83.98  ? 90  GLU A O   1 
ATOM   653  C CB  . GLU A 1 90  ? 13.768 36.068 1.965   1.00 55.41  ? 90  GLU A CB  1 
ATOM   654  C CG  . GLU A 1 90  ? 14.151 36.065 0.493   1.00 58.05  ? 90  GLU A CG  1 
ATOM   655  C CD  . GLU A 1 90  ? 13.159 36.808 -0.380  1.00 80.95  ? 90  GLU A CD  1 
ATOM   656  O OE1 . GLU A 1 90  ? 12.442 37.689 0.142   1.00 83.02  ? 90  GLU A OE1 1 
ATOM   657  O OE2 . GLU A 1 90  ? 13.101 36.515 -1.593  1.00 87.87  ? 90  GLU A OE2 1 
ATOM   658  N N   . ASN A 1 91  ? 14.346 37.306 5.229   1.00 62.59  ? 91  ASN A N   1 
ATOM   659  C CA  . ASN A 1 91  ? 13.792 37.685 6.532   1.00 82.05  ? 91  ASN A CA  1 
ATOM   660  C C   . ASN A 1 91  ? 12.278 37.505 6.707   1.00 82.32  ? 91  ASN A C   1 
ATOM   661  O O   . ASN A 1 91  ? 11.556 38.437 7.079   1.00 85.38  ? 91  ASN A O   1 
ATOM   662  C CB  . ASN A 1 91  ? 14.276 39.114 6.879   1.00 84.37  ? 91  ASN A CB  1 
ATOM   663  C CG  . ASN A 1 91  ? 13.530 40.244 6.142   1.00 89.18  ? 91  ASN A CG  1 
ATOM   664  O OD1 . ASN A 1 91  ? 12.506 40.050 5.487   1.00 86.58  ? 91  ASN A OD1 1 
ATOM   665  N ND2 . ASN A 1 91  ? 14.059 41.455 6.283   1.00 88.19  ? 91  ASN A ND2 1 
ATOM   666  N N   . ILE A 1 92  ? 11.802 36.274 6.503   1.00 80.31  ? 92  ILE A N   1 
ATOM   667  C CA  . ILE A 1 92  ? 10.408 35.948 6.786   1.00 64.97  ? 92  ILE A CA  1 
ATOM   668  C C   . ILE A 1 92  ? 10.109 36.221 8.253   1.00 72.33  ? 92  ILE A C   1 
ATOM   669  O O   . ILE A 1 92  ? 10.849 35.790 9.148   1.00 56.09  ? 92  ILE A O   1 
ATOM   670  C CB  . ILE A 1 92  ? 10.116 34.482 6.426   1.00 70.24  ? 92  ILE A CB  1 
ATOM   671  C CG1 . ILE A 1 92  ? 10.585 34.136 5.007   1.00 66.65  ? 92  ILE A CG1 1 
ATOM   672  C CG2 . ILE A 1 92  ? 8.636  34.164 6.587   1.00 73.47  ? 92  ILE A CG2 1 
ATOM   673  C CD1 . ILE A 1 92  ? 10.439 35.254 3.984   1.00 68.21  ? 92  ILE A CD1 1 
ATOM   674  N N   . ASP A 1 93  ? 9.008  36.933 8.509   1.00 73.08  ? 93  ASP A N   1 
ATOM   675  C CA  . ASP A 1 93  ? 8.689  37.336 9.876   1.00 76.04  ? 93  ASP A CA  1 
ATOM   676  C C   . ASP A 1 93  ? 8.365  36.139 10.761  1.00 62.82  ? 93  ASP A C   1 
ATOM   677  O O   . ASP A 1 93  ? 8.595  36.189 11.974  1.00 65.60  ? 93  ASP A O   1 
ATOM   678  C CB  . ASP A 1 93  ? 7.525  38.324 9.866   1.00 80.74  ? 93  ASP A CB  1 
ATOM   679  C CG  . ASP A 1 93  ? 7.856  39.598 9.117   1.00 93.78  ? 93  ASP A CG  1 
ATOM   680  O OD1 . ASP A 1 93  ? 8.402  40.531 9.743   1.00 95.67  ? 93  ASP A OD1 1 
ATOM   681  O OD2 . ASP A 1 93  ? 7.579  39.664 7.900   1.00 94.59  ? 93  ASP A OD2 1 
ATOM   682  N N   . ARG A 1 94  ? 7.833  35.064 10.176  1.00 63.21  ? 94  ARG A N   1 
ATOM   683  C CA  . ARG A 1 94  ? 7.565  33.846 10.934  1.00 64.37  ? 94  ARG A CA  1 
ATOM   684  C C   . ARG A 1 94  ? 8.820  33.320 11.621  1.00 64.47  ? 94  ARG A C   1 
ATOM   685  O O   . ARG A 1 94  ? 8.753  32.812 12.747  1.00 71.52  ? 94  ARG A O   1 
ATOM   686  C CB  . ARG A 1 94  ? 6.988  32.771 10.008  1.00 54.82  ? 94  ARG A CB  1 
ATOM   687  C CG  . ARG A 1 94  ? 5.474  32.696 9.965   1.00 72.07  ? 94  ARG A CG  1 
ATOM   688  C CD  . ARG A 1 94  ? 5.031  31.434 9.234   1.00 76.65  ? 94  ARG A CD  1 
ATOM   689  N NE  . ARG A 1 94  ? 4.704  30.341 10.143  1.00 82.95  ? 94  ARG A NE  1 
ATOM   690  C CZ  . ARG A 1 94  ? 4.527  29.082 9.765   1.00 74.72  ? 94  ARG A CZ  1 
ATOM   691  N NH1 . ARG A 1 94  ? 4.641  28.719 8.498   1.00 67.97  ? 94  ARG A NH1 1 
ATOM   692  N NH2 . ARG A 1 94  ? 4.233  28.163 10.682  1.00 70.20  ? 94  ARG A NH2 1 
ATOM   693  N N   . LEU A 1 95  ? 9.975  33.443 10.965  1.00 60.17  ? 95  LEU A N   1 
ATOM   694  C CA  . LEU A 1 95  ? 11.178 32.756 11.416  1.00 50.87  ? 95  LEU A CA  1 
ATOM   695  C C   . LEU A 1 95  ? 12.048 33.592 12.344  1.00 56.08  ? 95  LEU A C   1 
ATOM   696  O O   . LEU A 1 95  ? 13.084 33.098 12.800  1.00 62.24  ? 95  LEU A O   1 
ATOM   697  C CB  . LEU A 1 95  ? 12.013 32.305 10.215  1.00 56.19  ? 95  LEU A CB  1 
ATOM   698  C CG  . LEU A 1 95  ? 11.246 31.832 8.982   1.00 59.23  ? 95  LEU A CG  1 
ATOM   699  C CD1 . LEU A 1 95  ? 12.113 31.951 7.737   1.00 68.68  ? 95  LEU A CD1 1 
ATOM   700  C CD2 . LEU A 1 95  ? 10.708 30.437 9.160   1.00 65.99  ? 95  LEU A CD2 1 
ATOM   701  N N   . GLN A 1 96  ? 11.664 34.834 12.635  1.00 60.93  ? 96  GLN A N   1 
ATOM   702  C CA  . GLN A 1 96  ? 12.489 35.669 13.510  1.00 58.86  ? 96  GLN A CA  1 
ATOM   703  C C   . GLN A 1 96  ? 12.727 35.071 14.895  1.00 58.36  ? 96  GLN A C   1 
ATOM   704  O O   . GLN A 1 96  ? 13.880 35.146 15.368  1.00 51.37  ? 96  GLN A O   1 
ATOM   705  C CB  . GLN A 1 96  ? 11.874 37.070 13.617  1.00 67.66  ? 96  GLN A CB  1 
ATOM   706  C CG  . GLN A 1 96  ? 11.948 37.881 12.322  1.00 71.47  ? 96  GLN A CG  1 
ATOM   707  C CD  . GLN A 1 96  ? 13.190 37.574 11.493  1.00 83.81  ? 96  GLN A CD  1 
ATOM   708  O OE1 . GLN A 1 96  ? 14.286 38.057 11.790  1.00 77.44  ? 96  GLN A OE1 1 
ATOM   709  N NE2 . GLN A 1 96  ? 13.019 36.786 10.437  1.00 77.45  ? 96  GLN A NE2 1 
ATOM   710  N N   . PRO A 1 97  ? 11.754 34.479 15.597  1.00 63.51  ? 97  PRO A N   1 
ATOM   711  C CA  . PRO A 1 97  ? 12.106 33.838 16.871  1.00 57.56  ? 97  PRO A CA  1 
ATOM   712  C C   . PRO A 1 97  ? 12.950 32.589 16.686  1.00 47.66  ? 97  PRO A C   1 
ATOM   713  O O   . PRO A 1 97  ? 13.709 32.230 17.595  1.00 54.14  ? 97  PRO A O   1 
ATOM   714  C CB  . PRO A 1 97  ? 10.748 33.532 17.514  1.00 53.14  ? 97  PRO A CB  1 
ATOM   715  C CG  . PRO A 1 97  ? 9.772  33.504 16.406  1.00 56.79  ? 97  PRO A CG  1 
ATOM   716  C CD  . PRO A 1 97  ? 10.364 34.170 15.199  1.00 61.82  ? 97  PRO A CD  1 
ATOM   717  N N   . TYR A 1 98  ? 12.856 31.929 15.529  1.00 48.27  ? 98  TYR A N   1 
ATOM   718  C CA  . TYR A 1 98  ? 13.722 30.786 15.262  1.00 51.69  ? 98  TYR A CA  1 
ATOM   719  C C   . TYR A 1 98  ? 15.168 31.231 15.086  1.00 51.13  ? 98  TYR A C   1 
ATOM   720  O O   . TYR A 1 98  ? 16.092 30.578 15.584  1.00 41.42  ? 98  TYR A O   1 
ATOM   721  C CB  . TYR A 1 98  ? 13.252 30.045 14.011  1.00 36.68  ? 98  TYR A CB  1 
ATOM   722  C CG  . TYR A 1 98  ? 11.962 29.272 14.162  1.00 49.87  ? 98  TYR A CG  1 
ATOM   723  C CD1 . TYR A 1 98  ? 10.738 29.928 14.134  1.00 51.39  ? 98  TYR A CD1 1 
ATOM   724  C CD2 . TYR A 1 98  ? 11.962 27.891 14.320  1.00 39.87  ? 98  TYR A CD2 1 
ATOM   725  C CE1 . TYR A 1 98  ? 9.550  29.236 14.260  1.00 55.33  ? 98  TYR A CE1 1 
ATOM   726  C CE2 . TYR A 1 98  ? 10.774 27.187 14.449  1.00 42.66  ? 98  TYR A CE2 1 
ATOM   727  C CZ  . TYR A 1 98  ? 9.572  27.866 14.418  1.00 43.93  ? 98  TYR A CZ  1 
ATOM   728  O OH  . TYR A 1 98  ? 8.382  27.183 14.540  1.00 50.36  ? 98  TYR A OH  1 
ATOM   729  N N   . LEU A 1 99  ? 15.382 32.338 14.369  1.00 49.21  ? 99  LEU A N   1 
ATOM   730  C CA  . LEU A 1 99  ? 16.734 32.848 14.164  1.00 48.48  ? 99  LEU A CA  1 
ATOM   731  C C   . LEU A 1 99  ? 17.301 33.462 15.434  1.00 51.19  ? 99  LEU A C   1 
ATOM   732  O O   . LEU A 1 99  ? 18.518 33.424 15.651  1.00 43.23  ? 99  LEU A O   1 
ATOM   733  C CB  . LEU A 1 99  ? 16.740 33.873 13.028  1.00 47.63  ? 99  LEU A CB  1 
ATOM   734  C CG  . LEU A 1 99  ? 16.152 33.377 11.706  1.00 56.00  ? 99  LEU A CG  1 
ATOM   735  C CD1 . LEU A 1 99  ? 16.089 34.501 10.677  1.00 54.03  ? 99  LEU A CD1 1 
ATOM   736  C CD2 . LEU A 1 99  ? 16.957 32.196 11.177  1.00 46.98  ? 99  LEU A CD2 1 
ATOM   737  N N   . ARG A 1 100 ? 16.440 34.035 16.279  1.00 41.88  ? 100 ARG A N   1 
ATOM   738  C CA  . ARG A 1 100 ? 16.887 34.521 17.579  1.00 50.45  ? 100 ARG A CA  1 
ATOM   739  C C   . ARG A 1 100 ? 17.432 33.379 18.430  1.00 45.36  ? 100 ARG A C   1 
ATOM   740  O O   . ARG A 1 100 ? 18.441 33.540 19.127  1.00 43.67  ? 100 ARG A O   1 
ATOM   741  C CB  . ARG A 1 100 ? 15.731 35.241 18.280  1.00 56.45  ? 100 ARG A CB  1 
ATOM   742  C CG  . ARG A 1 100 ? 16.142 36.194 19.399  1.00 63.96  ? 100 ARG A CG  1 
ATOM   743  C CD  . ARG A 1 100 ? 15.256 36.015 20.623  1.00 67.24  ? 100 ARG A CD  1 
ATOM   744  N NE  . ARG A 1 100 ? 14.915 34.613 20.822  1.00 78.93  ? 100 ARG A NE  1 
ATOM   745  C CZ  . ARG A 1 100 ? 13.680 34.160 21.002  1.00 75.15  ? 100 ARG A CZ  1 
ATOM   746  N NH1 . ARG A 1 100 ? 12.640 34.981 21.064  1.00 66.09  ? 100 ARG A NH1 1 
ATOM   747  N NH2 . ARG A 1 100 ? 13.483 32.851 21.126  1.00 66.82  ? 100 ARG A NH2 1 
ATOM   748  N N   . LEU A 1 101 ? 16.793 32.208 18.366  1.00 44.79  ? 101 LEU A N   1 
ATOM   749  C CA  . LEU A 1 101 ? 17.276 31.055 19.120  1.00 40.00  ? 101 LEU A CA  1 
ATOM   750  C C   . LEU A 1 101 ? 18.570 30.516 18.526  1.00 36.57  ? 101 LEU A C   1 
ATOM   751  O O   . LEU A 1 101 ? 19.475 30.103 19.261  1.00 38.10  ? 101 LEU A O   1 
ATOM   752  C CB  . LEU A 1 101 ? 16.212 29.961 19.140  1.00 36.79  ? 101 LEU A CB  1 
ATOM   753  C CG  . LEU A 1 101 ? 16.438 28.821 20.131  1.00 39.02  ? 101 LEU A CG  1 
ATOM   754  C CD1 . LEU A 1 101 ? 16.471 29.360 21.557  1.00 42.30  ? 101 LEU A CD1 1 
ATOM   755  C CD2 . LEU A 1 101 ? 15.383 27.738 19.973  1.00 39.42  ? 101 LEU A CD2 1 
ATOM   756  N N   . TRP A 1 102 ? 18.668 30.510 17.194  1.00 34.46  ? 102 TRP A N   1 
ATOM   757  C CA  . TRP A 1 102 ? 19.884 30.055 16.529  1.00 32.64  ? 102 TRP A CA  1 
ATOM   758  C C   . TRP A 1 102 ? 21.087 30.887 16.958  1.00 36.35  ? 102 TRP A C   1 
ATOM   759  O O   . TRP A 1 102 ? 22.138 30.341 17.312  1.00 35.45  ? 102 TRP A O   1 
ATOM   760  C CB  . TRP A 1 102 ? 19.691 30.109 15.012  1.00 32.24  ? 102 TRP A CB  1 
ATOM   761  C CG  . TRP A 1 102 ? 20.950 29.938 14.209  1.00 33.57  ? 102 TRP A CG  1 
ATOM   762  C CD1 . TRP A 1 102 ? 21.780 30.928 13.769  1.00 43.71  ? 102 TRP A CD1 1 
ATOM   763  C CD2 . TRP A 1 102 ? 21.509 28.706 13.735  1.00 45.43  ? 102 TRP A CD2 1 
ATOM   764  N NE1 . TRP A 1 102 ? 22.826 30.389 13.055  1.00 54.78  ? 102 TRP A NE1 1 
ATOM   765  C CE2 . TRP A 1 102 ? 22.684 29.027 13.020  1.00 40.57  ? 102 TRP A CE2 1 
ATOM   766  C CE3 . TRP A 1 102 ? 21.134 27.363 13.847  1.00 47.24  ? 102 TRP A CE3 1 
ATOM   767  C CZ2 . TRP A 1 102 ? 23.484 28.057 12.420  1.00 35.32  ? 102 TRP A CZ2 1 
ATOM   768  C CZ3 . TRP A 1 102 ? 21.932 26.399 13.253  1.00 53.40  ? 102 TRP A CZ3 1 
ATOM   769  C CH2 . TRP A 1 102 ? 23.093 26.752 12.547  1.00 46.59  ? 102 TRP A CH2 1 
ATOM   770  N N   . ASN A 1 103 ? 20.951 32.216 16.939  1.00 37.47  ? 103 ASN A N   1 
ATOM   771  C CA  . ASN A 1 103 ? 22.046 33.068 17.397  1.00 46.32  ? 103 ASN A CA  1 
ATOM   772  C C   . ASN A 1 103 ? 22.324 32.854 18.876  1.00 38.84  ? 103 ASN A C   1 
ATOM   773  O O   . ASN A 1 103 ? 23.479 32.914 19.313  1.00 41.89  ? 103 ASN A O   1 
ATOM   774  C CB  . ASN A 1 103 ? 21.732 34.536 17.120  1.00 45.45  ? 103 ASN A CB  1 
ATOM   775  C CG  . ASN A 1 103 ? 21.559 34.821 15.644  1.00 59.67  ? 103 ASN A CG  1 
ATOM   776  O OD1 . ASN A 1 103 ? 22.321 34.324 14.813  1.00 60.04  ? 103 ASN A OD1 1 
ATOM   777  N ND2 . ASN A 1 103 ? 20.553 35.622 15.309  1.00 63.73  ? 103 ASN A ND2 1 
ATOM   778  N N   . GLU A 1 104 ? 21.277 32.604 19.665  1.00 38.13  ? 104 GLU A N   1 
ATOM   779  C CA  . GLU A 1 104 ? 21.474 32.322 21.080  1.00 37.51  ? 104 GLU A CA  1 
ATOM   780  C C   . GLU A 1 104 ? 22.258 31.031 21.278  1.00 36.85  ? 104 GLU A C   1 
ATOM   781  O O   . GLU A 1 104 ? 23.150 30.961 22.133  1.00 36.90  ? 104 GLU A O   1 
ATOM   782  C CB  . GLU A 1 104 ? 20.125 32.245 21.790  1.00 42.63  ? 104 GLU A CB  1 
ATOM   783  C CG  . GLU A 1 104 ? 20.226 32.422 23.289  1.00 40.94  ? 104 GLU A CG  1 
ATOM   784  C CD  . GLU A 1 104 ? 18.871 32.446 23.964  1.00 54.27  ? 104 GLU A CD  1 
ATOM   785  O OE1 . GLU A 1 104 ? 18.758 31.905 25.080  1.00 48.22  ? 104 GLU A OE1 1 
ATOM   786  O OE2 . GLU A 1 104 ? 17.920 32.999 23.376  1.00 60.87  ? 104 GLU A OE2 1 
ATOM   787  N N   . ALA A 1 105 ? 21.932 29.994 20.499  1.00 33.69  ? 105 ALA A N   1 
ATOM   788  C CA  . ALA A 1 105 ? 22.663 28.734 20.588  1.00 33.23  ? 105 ALA A CA  1 
ATOM   789  C C   . ALA A 1 105 ? 24.127 28.926 20.226  1.00 44.39  ? 105 ALA A C   1 
ATOM   790  O O   . ALA A 1 105 ? 25.017 28.346 20.861  1.00 35.27  ? 105 ALA A O   1 
ATOM   791  C CB  . ALA A 1 105 ? 22.023 27.692 19.670  1.00 31.07  ? 105 ALA A CB  1 
ATOM   792  N N   . GLU A 1 106 ? 24.390 29.745 19.205  1.00 32.54  ? 106 GLU A N   1 
ATOM   793  C CA  . GLU A 1 106 ? 25.755 30.007 18.770  1.00 32.60  ? 106 GLU A CA  1 
ATOM   794  C C   . GLU A 1 106 ? 26.635 30.494 19.913  1.00 44.10  ? 106 GLU A C   1 
ATOM   795  O O   . GLU A 1 106 ? 27.826 30.166 19.962  1.00 43.11  ? 106 GLU A O   1 
ATOM   796  C CB  . GLU A 1 106 ? 25.730 31.031 17.633  1.00 36.15  ? 106 GLU A CB  1 
ATOM   797  C CG  . GLU A 1 106 ? 26.958 31.018 16.749  1.00 48.04  ? 106 GLU A CG  1 
ATOM   798  C CD  . GLU A 1 106 ? 27.210 32.365 16.108  1.00 57.28  ? 106 GLU A CD  1 
ATOM   799  O OE1 . GLU A 1 106 ? 26.327 32.841 15.363  1.00 66.98  ? 106 GLU A OE1 1 
ATOM   800  O OE2 . GLU A 1 106 ? 28.286 32.947 16.356  1.00 66.73  ? 106 GLU A OE2 1 
ATOM   801  N N   . LEU A 1 107 ? 26.069 31.255 20.850  1.00 44.12  ? 107 LEU A N   1 
ATOM   802  C CA  . LEU A 1 107 ? 26.829 31.730 21.999  1.00 47.16  ? 107 LEU A CA  1 
ATOM   803  C C   . LEU A 1 107 ? 27.011 30.666 23.075  1.00 51.09  ? 107 LEU A C   1 
ATOM   804  O O   . LEU A 1 107 ? 27.950 30.767 23.872  1.00 55.10  ? 107 LEU A O   1 
ATOM   805  C CB  . LEU A 1 107 ? 26.147 32.957 22.609  1.00 54.92  ? 107 LEU A CB  1 
ATOM   806  C CG  . LEU A 1 107 ? 26.172 34.257 21.801  1.00 49.15  ? 107 LEU A CG  1 
ATOM   807  C CD1 . LEU A 1 107 ? 25.817 35.442 22.691  1.00 54.39  ? 107 LEU A CD1 1 
ATOM   808  C CD2 . LEU A 1 107 ? 27.537 34.460 21.155  1.00 55.27  ? 107 LEU A CD2 1 
ATOM   809  N N   . LEU A 1 108 ? 26.148 29.652 23.114  1.00 33.95  ? 108 LEU A N   1 
ATOM   810  C CA  . LEU A 1 108 ? 26.180 28.650 24.169  1.00 37.91  ? 108 LEU A CA  1 
ATOM   811  C C   . LEU A 1 108 ? 27.058 27.452 23.847  1.00 32.55  ? 108 LEU A C   1 
ATOM   812  O O   . LEU A 1 108 ? 27.319 26.640 24.741  1.00 37.16  ? 108 LEU A O   1 
ATOM   813  C CB  . LEU A 1 108 ? 24.765 28.157 24.475  1.00 37.55  ? 108 LEU A CB  1 
ATOM   814  C CG  . LEU A 1 108 ? 23.835 29.170 25.131  1.00 48.81  ? 108 LEU A CG  1 
ATOM   815  C CD1 . LEU A 1 108 ? 22.440 28.590 25.217  1.00 44.83  ? 108 LEU A CD1 1 
ATOM   816  C CD2 . LEU A 1 108 ? 24.354 29.525 26.514  1.00 46.59  ? 108 LEU A CD2 1 
ATOM   817  N N   . ILE A 1 109 ? 27.521 27.316 22.604  1.00 33.38  ? 109 ILE A N   1 
ATOM   818  C CA  . ILE A 1 109 ? 28.357 26.175 22.262  1.00 46.09  ? 109 ILE A CA  1 
ATOM   819  C C   . ILE A 1 109 ? 29.683 26.200 23.009  1.00 36.40  ? 109 ILE A C   1 
ATOM   820  O O   . ILE A 1 109 ? 30.368 25.174 23.072  1.00 41.62  ? 109 ILE A O   1 
ATOM   821  C CB  . ILE A 1 109 ? 28.575 26.112 20.737  1.00 35.51  ? 109 ILE A CB  1 
ATOM   822  C CG1 . ILE A 1 109 ? 29.427 27.290 20.267  1.00 39.13  ? 109 ILE A CG1 1 
ATOM   823  C CG2 . ILE A 1 109 ? 27.234 26.082 20.014  1.00 34.19  ? 109 ILE A CG2 1 
ATOM   824  C CD1 . ILE A 1 109 ? 29.690 27.286 18.781  1.00 36.88  ? 109 ILE A CD1 1 
ATOM   825  N N   . GLU A 1 110 ? 30.061 27.344 23.589  1.00 31.77  ? 110 GLU A N   1 
ATOM   826  C CA  . GLU A 1 110 ? 31.278 27.454 24.382  1.00 38.00  ? 110 GLU A CA  1 
ATOM   827  C C   . GLU A 1 110 ? 31.045 27.246 25.875  1.00 57.38  ? 110 GLU A C   1 
ATOM   828  O O   . GLU A 1 110 ? 31.913 27.612 26.675  1.00 67.11  ? 110 GLU A O   1 
ATOM   829  C CB  . GLU A 1 110 ? 31.945 28.815 24.181  1.00 49.08  ? 110 GLU A CB  1 
ATOM   830  C CG  . GLU A 1 110 ? 32.390 29.133 22.777  1.00 52.66  ? 110 GLU A CG  1 
ATOM   831  C CD  . GLU A 1 110 ? 32.535 30.626 22.566  1.00 73.27  ? 110 GLU A CD  1 
ATOM   832  O OE1 . GLU A 1 110 ? 32.251 31.107 21.451  1.00 71.53  ? 110 GLU A OE1 1 
ATOM   833  O OE2 . GLU A 1 110 ? 32.935 31.319 23.527  1.00 78.95  ? 110 GLU A OE2 1 
ATOM   834  N N   . GLN A 1 111 ? 29.909 26.676 26.277  1.00 44.79  ? 111 GLN A N   1 
ATOM   835  C CA  . GLN A 1 111 ? 29.738 26.366 27.694  1.00 53.16  ? 111 GLN A CA  1 
ATOM   836  C C   . GLN A 1 111 ? 28.748 25.233 27.923  1.00 48.79  ? 111 GLN A C   1 
ATOM   837  O O   . GLN A 1 111 ? 28.582 24.776 29.058  1.00 39.45  ? 111 GLN A O   1 
ATOM   838  C CB  . GLN A 1 111 ? 29.304 27.608 28.478  1.00 55.97  ? 111 GLN A CB  1 
ATOM   839  C CG  . GLN A 1 111 ? 27.919 28.123 28.153  1.00 57.63  ? 111 GLN A CG  1 
ATOM   840  C CD  . GLN A 1 111 ? 27.835 29.632 28.254  1.00 67.27  ? 111 GLN A CD  1 
ATOM   841  O OE1 . GLN A 1 111 ? 27.017 30.172 29.001  1.00 74.45  ? 111 GLN A OE1 1 
ATOM   842  N NE2 . GLN A 1 111 ? 28.683 30.323 27.501  1.00 61.41  ? 111 GLN A NE2 1 
ATOM   843  N N   . ASP A 1 112 ? 28.103 24.753 26.861  1.00 39.54  ? 112 ASP A N   1 
ATOM   844  C CA  . ASP A 1 112 ? 27.153 23.649 26.964  1.00 42.81  ? 112 ASP A CA  1 
ATOM   845  C C   . ASP A 1 112 ? 27.531 22.576 25.952  1.00 38.42  ? 112 ASP A C   1 
ATOM   846  O O   . ASP A 1 112 ? 27.449 22.805 24.742  1.00 35.74  ? 112 ASP A O   1 
ATOM   847  C CB  . ASP A 1 112 ? 25.719 24.137 26.752  1.00 36.52  ? 112 ASP A CB  1 
ATOM   848  C CG  . ASP A 1 112 ? 24.692 23.121 27.201  1.00 44.88  ? 112 ASP A CG  1 
ATOM   849  O OD1 . ASP A 1 112 ? 24.738 21.976 26.701  1.00 38.01  ? 112 ASP A OD1 1 
ATOM   850  O OD2 . ASP A 1 112 ? 23.870 23.450 28.084  1.00 44.37  ? 112 ASP A OD2 1 
ATOM   851  N N   . ILE A 1 113 ? 27.914 21.398 26.454  1.00 36.57  ? 113 ILE A N   1 
ATOM   852  C CA  . ILE A 1 113 ? 28.411 20.329 25.589  1.00 39.28  ? 113 ILE A CA  1 
ATOM   853  C C   . ILE A 1 113 ? 27.305 19.796 24.681  1.00 40.09  ? 113 ILE A C   1 
ATOM   854  O O   . ILE A 1 113 ? 27.555 19.441 23.523  1.00 34.53  ? 113 ILE A O   1 
ATOM   855  C CB  . ILE A 1 113 ? 29.056 19.192 26.415  1.00 47.82  ? 113 ILE A CB  1 
ATOM   856  C CG1 . ILE A 1 113 ? 30.021 19.707 27.503  1.00 61.14  ? 113 ILE A CG1 1 
ATOM   857  C CG2 . ILE A 1 113 ? 29.768 18.204 25.499  1.00 59.57  ? 113 ILE A CG2 1 
ATOM   858  C CD1 . ILE A 1 113 ? 29.381 20.249 28.793  1.00 58.23  ? 113 ILE A CD1 1 
ATOM   859  N N   . GLU A 1 114 ? 26.068 19.718 25.181  1.00 32.35  ? 114 GLU A N   1 
ATOM   860  C CA  . GLU A 1 114 ? 24.997 19.196 24.336  1.00 27.37  ? 114 GLU A CA  1 
ATOM   861  C C   . GLU A 1 114 ? 24.573 20.207 23.279  1.00 32.21  ? 114 GLU A C   1 
ATOM   862  O O   . GLU A 1 114 ? 24.214 19.827 22.159  1.00 27.43  ? 114 GLU A O   1 
ATOM   863  C CB  . GLU A 1 114 ? 23.798 18.775 25.182  1.00 37.07  ? 114 GLU A CB  1 
ATOM   864  C CG  . GLU A 1 114 ? 24.159 17.885 26.349  1.00 39.78  ? 114 GLU A CG  1 
ATOM   865  C CD  . GLU A 1 114 ? 24.812 16.588 25.903  1.00 45.96  ? 114 GLU A CD  1 
ATOM   866  O OE1 . GLU A 1 114 ? 24.337 15.987 24.917  1.00 45.50  ? 114 GLU A OE1 1 
ATOM   867  O OE2 . GLU A 1 114 ? 25.792 16.158 26.551  1.00 60.23  ? 114 GLU A OE2 1 
ATOM   868  N N   . ILE A 1 115 ? 24.582 21.493 23.621  1.00 25.94  ? 115 ILE A N   1 
ATOM   869  C CA  . ILE A 1 115 ? 24.236 22.504 22.633  1.00 27.32  ? 115 ILE A CA  1 
ATOM   870  C C   . ILE A 1 115 ? 25.350 22.614 21.600  1.00 33.41  ? 115 ILE A C   1 
ATOM   871  O O   . ILE A 1 115 ? 25.091 22.866 20.420  1.00 29.49  ? 115 ILE A O   1 
ATOM   872  C CB  . ILE A 1 115 ? 23.954 23.848 23.329  1.00 29.16  ? 115 ILE A CB  1 
ATOM   873  C CG1 . ILE A 1 115 ? 22.649 23.768 24.126  1.00 33.71  ? 115 ILE A CG1 1 
ATOM   874  C CG2 . ILE A 1 115 ? 23.823 24.962 22.303  1.00 35.25  ? 115 ILE A CG2 1 
ATOM   875  C CD1 . ILE A 1 115 ? 21.421 23.636 23.264  1.00 47.99  ? 115 ILE A CD1 1 
ATOM   876  N N   . GLN A 1 116 ? 26.599 22.404 22.020  1.00 34.99  ? 116 GLN A N   1 
ATOM   877  C CA  . GLN A 1 116 ? 27.714 22.381 21.076  1.00 29.06  ? 116 GLN A CA  1 
ATOM   878  C C   . GLN A 1 116 ? 27.512 21.313 20.008  1.00 30.96  ? 116 GLN A C   1 
ATOM   879  O O   . GLN A 1 116 ? 27.701 21.569 18.812  1.00 34.60  ? 116 GLN A O   1 
ATOM   880  C CB  . GLN A 1 116 ? 29.026 22.144 21.826  1.00 30.39  ? 116 GLN A CB  1 
ATOM   881  C CG  . GLN A 1 116 ? 30.254 22.509 21.024  1.00 38.82  ? 116 GLN A CG  1 
ATOM   882  C CD  . GLN A 1 116 ? 30.889 21.292 20.391  1.00 56.96  ? 116 GLN A CD  1 
ATOM   883  O OE1 . GLN A 1 116 ? 30.681 20.165 20.845  1.00 48.98  ? 116 GLN A OE1 1 
ATOM   884  N NE2 . GLN A 1 116 ? 31.664 21.509 19.333  1.00 45.98  ? 116 GLN A NE2 1 
ATOM   885  N N   . LYS A 1 117 ? 27.127 20.105 20.422  1.00 27.94  ? 117 LYS A N   1 
ATOM   886  C CA  . LYS A 1 117 ? 26.910 19.026 19.464  1.00 30.54  ? 117 LYS A CA  1 
ATOM   887  C C   . LYS A 1 117 ? 25.687 19.285 18.592  1.00 31.82  ? 117 LYS A C   1 
ATOM   888  O O   . LYS A 1 117 ? 25.707 19.007 17.386  1.00 29.47  ? 117 LYS A O   1 
ATOM   889  C CB  . LYS A 1 117 ? 26.771 17.695 20.202  1.00 29.99  ? 117 LYS A CB  1 
ATOM   890  C CG  . LYS A 1 117 ? 28.085 17.182 20.794  1.00 36.15  ? 117 LYS A CG  1 
ATOM   891  C CD  . LYS A 1 117 ? 27.902 15.826 21.465  1.00 44.52  ? 117 LYS A CD  1 
ATOM   892  C CE  . LYS A 1 117 ? 26.771 15.855 22.480  1.00 46.47  ? 117 LYS A CE  1 
ATOM   893  N NZ  . LYS A 1 117 ? 26.772 14.648 23.359  1.00 54.94  ? 117 LYS A NZ  1 
ATOM   894  N N   . ALA A 1 118 ? 24.608 19.806 19.181  1.00 29.73  ? 118 ALA A N   1 
ATOM   895  C CA  . ALA A 1 118 ? 23.383 20.016 18.412  1.00 26.93  ? 118 ALA A CA  1 
ATOM   896  C C   . ALA A 1 118 ? 23.562 21.125 17.386  1.00 26.23  ? 118 ALA A C   1 
ATOM   897  O O   . ALA A 1 118 ? 23.015 21.048 16.281  1.00 27.22  ? 118 ALA A O   1 
ATOM   898  C CB  . ALA A 1 118 ? 22.220 20.341 19.351  1.00 29.56  ? 118 ALA A CB  1 
ATOM   899  N N   . TYR A 1 119 ? 24.314 22.170 17.742  1.00 25.06  ? 119 TYR A N   1 
ATOM   900  C CA  . TYR A 1 119 ? 24.562 23.260 16.802  1.00 28.45  ? 119 TYR A CA  1 
ATOM   901  C C   . TYR A 1 119 ? 25.305 22.760 15.571  1.00 29.88  ? 119 TYR A C   1 
ATOM   902  O O   . TYR A 1 119 ? 24.993 23.158 14.442  1.00 27.76  ? 119 TYR A O   1 
ATOM   903  C CB  . TYR A 1 119 ? 25.352 24.372 17.492  1.00 27.78  ? 119 TYR A CB  1 
ATOM   904  C CG  . TYR A 1 119 ? 25.515 25.625 16.652  1.00 32.72  ? 119 TYR A CG  1 
ATOM   905  C CD1 . TYR A 1 119 ? 24.548 26.625 16.666  1.00 32.78  ? 119 TYR A CD1 1 
ATOM   906  C CD2 . TYR A 1 119 ? 26.622 25.798 15.836  1.00 28.00  ? 119 TYR A CD2 1 
ATOM   907  C CE1 . TYR A 1 119 ? 24.689 27.769 15.902  1.00 29.80  ? 119 TYR A CE1 1 
ATOM   908  C CE2 . TYR A 1 119 ? 26.772 26.941 15.066  1.00 31.97  ? 119 TYR A CE2 1 
ATOM   909  C CZ  . TYR A 1 119 ? 25.800 27.921 15.104  1.00 34.76  ? 119 TYR A CZ  1 
ATOM   910  O OH  . TYR A 1 119 ? 25.940 29.059 14.344  1.00 32.40  ? 119 TYR A OH  1 
ATOM   911  N N   . ASN A 1 120 ? 26.287 21.878 15.768  1.00 27.19  ? 120 ASN A N   1 
ATOM   912  C CA  . ASN A 1 120 ? 27.026 21.330 14.633  1.00 24.67  ? 120 ASN A CA  1 
ATOM   913  C C   . ASN A 1 120 ? 26.143 20.442 13.769  1.00 26.83  ? 120 ASN A C   1 
ATOM   914  O O   . ASN A 1 120 ? 26.267 20.446 12.538  1.00 30.80  ? 120 ASN A O   1 
ATOM   915  C CB  . ASN A 1 120 ? 28.245 20.554 15.129  1.00 26.24  ? 120 ASN A CB  1 
ATOM   916  C CG  . ASN A 1 120 ? 29.419 21.456 15.437  1.00 31.33  ? 120 ASN A CG  1 
ATOM   917  O OD1 . ASN A 1 120 ? 29.329 22.676 15.309  1.00 31.37  ? 120 ASN A OD1 1 
ATOM   918  N ND2 . ASN A 1 120 ? 30.525 20.861 15.863  1.00 30.81  ? 120 ASN A ND2 1 
ATOM   919  N N   . LEU A 1 121 ? 25.262 19.656 14.391  1.00 24.94  ? 121 LEU A N   1 
ATOM   920  C CA  . LEU A 1 121 ? 24.316 18.860 13.613  1.00 26.90  ? 121 LEU A CA  1 
ATOM   921  C C   . LEU A 1 121 ? 23.415 19.750 12.765  1.00 28.15  ? 121 LEU A C   1 
ATOM   922  O O   . LEU A 1 121 ? 23.139 19.438 11.602  1.00 30.10  ? 121 LEU A O   1 
ATOM   923  C CB  . LEU A 1 121 ? 23.469 17.988 14.540  1.00 33.43  ? 121 LEU A CB  1 
ATOM   924  C CG  . LEU A 1 121 ? 24.095 16.680 15.022  1.00 42.73  ? 121 LEU A CG  1 
ATOM   925  C CD1 . LEU A 1 121 ? 23.386 16.205 16.286  1.00 34.70  ? 121 LEU A CD1 1 
ATOM   926  C CD2 . LEU A 1 121 ? 24.057 15.619 13.929  1.00 46.02  ? 121 LEU A CD2 1 
ATOM   927  N N   . ALA A 1 122 ? 22.945 20.864 13.333  1.00 23.62  ? 122 ALA A N   1 
ATOM   928  C CA  . ALA A 1 122 ? 22.116 21.793 12.570  1.00 26.06  ? 122 ALA A CA  1 
ATOM   929  C C   . ALA A 1 122 ? 22.909 22.446 11.445  1.00 26.42  ? 122 ALA A C   1 
ATOM   930  O O   . ALA A 1 122 ? 22.365 22.708 10.365  1.00 27.58  ? 122 ALA A O   1 
ATOM   931  C CB  . ALA A 1 122 ? 21.528 22.856 13.502  1.00 27.52  ? 122 ALA A CB  1 
ATOM   932  N N   . MET A 1 123 ? 24.197 22.718 11.680  1.00 28.63  ? 123 MET A N   1 
ATOM   933  C CA  . MET A 1 123 ? 25.047 23.277 10.630  1.00 28.03  ? 123 MET A CA  1 
ATOM   934  C C   . MET A 1 123 ? 25.186 22.311 9.460   1.00 32.62  ? 123 MET A C   1 
ATOM   935  O O   . MET A 1 123 ? 25.096 22.713 8.293   1.00 27.19  ? 123 MET A O   1 
ATOM   936  C CB  . MET A 1 123 ? 26.424 23.633 11.196  1.00 29.46  ? 123 MET A CB  1 
ATOM   937  C CG  . MET A 1 123 ? 26.477 24.908 12.037  1.00 34.49  ? 123 MET A CG  1 
ATOM   938  S SD  . MET A 1 123 ? 26.319 26.431 11.062  1.00 36.80  ? 123 MET A SD  1 
ATOM   939  C CE  . MET A 1 123 ? 27.218 25.978 9.587   1.00 29.80  ? 123 MET A CE  1 
ATOM   940  N N   . GLN A 1 124 ? 25.426 21.031 9.751   1.00 28.26  ? 124 GLN A N   1 
ATOM   941  C CA  . GLN A 1 124 ? 25.522 20.043 8.680   1.00 27.22  ? 124 GLN A CA  1 
ATOM   942  C C   . GLN A 1 124 ? 24.197 19.897 7.944   1.00 31.78  ? 124 GLN A C   1 
ATOM   943  O O   . GLN A 1 124 ? 24.177 19.730 6.718   1.00 34.57  ? 124 GLN A O   1 
ATOM   944  C CB  . GLN A 1 124 ? 25.968 18.690 9.237   1.00 36.29  ? 124 GLN A CB  1 
ATOM   945  C CG  . GLN A 1 124 ? 27.307 18.715 9.957   1.00 36.32  ? 124 GLN A CG  1 
ATOM   946  C CD  . GLN A 1 124 ? 28.487 18.520 9.021   1.00 49.90  ? 124 GLN A CD  1 
ATOM   947  O OE1 . GLN A 1 124 ? 28.319 18.393 7.807   1.00 41.37  ? 124 GLN A OE1 1 
ATOM   948  N NE2 . GLN A 1 124 ? 29.693 18.492 9.586   1.00 42.43  ? 124 GLN A NE2 1 
ATOM   949  N N   . SER A 1 125 ? 23.081 19.948 8.677   1.00 26.68  ? 125 SER A N   1 
ATOM   950  C CA  . SER A 1 125 ? 21.770 19.882 8.041   1.00 26.72  ? 125 SER A CA  1 
ATOM   951  C C   . SER A 1 125 ? 21.552 21.071 7.115   1.00 28.78  ? 125 SER A C   1 
ATOM   952  O O   . SER A 1 125 ? 20.993 20.925 6.020   1.00 28.93  ? 125 SER A O   1 
ATOM   953  C CB  . SER A 1 125 ? 20.674 19.829 9.104   1.00 35.81  ? 125 SER A CB  1 
ATOM   954  O OG  . SER A 1 125 ? 20.672 18.576 9.767   1.00 43.10  ? 125 SER A OG  1 
ATOM   955  N N   . TRP A 1 126 ? 21.989 22.256 7.547   1.00 26.25  ? 126 TRP A N   1 
ATOM   956  C CA  . TRP A 1 126 ? 21.897 23.457 6.724   1.00 29.24  ? 126 TRP A CA  1 
ATOM   957  C C   . TRP A 1 126 ? 22.736 23.313 5.462   1.00 30.40  ? 126 TRP A C   1 
ATOM   958  O O   . TRP A 1 126 ? 22.279 23.627 4.357   1.00 29.94  ? 126 TRP A O   1 
ATOM   959  C CB  . TRP A 1 126 ? 22.361 24.658 7.545   1.00 28.79  ? 126 TRP A CB  1 
ATOM   960  C CG  . TRP A 1 126 ? 22.151 26.013 6.932   1.00 27.77  ? 126 TRP A CG  1 
ATOM   961  C CD1 . TRP A 1 126 ? 21.274 26.356 5.941   1.00 34.53  ? 126 TRP A CD1 1 
ATOM   962  C CD2 . TRP A 1 126 ? 22.866 27.208 7.269   1.00 28.04  ? 126 TRP A CD2 1 
ATOM   963  N NE1 . TRP A 1 126 ? 21.392 27.700 5.651   1.00 29.24  ? 126 TRP A NE1 1 
ATOM   964  C CE2 . TRP A 1 126 ? 22.362 28.242 6.456   1.00 26.01  ? 126 TRP A CE2 1 
ATOM   965  C CE3 . TRP A 1 126 ? 23.881 27.502 8.187   1.00 31.09  ? 126 TRP A CE3 1 
ATOM   966  C CZ2 . TRP A 1 126 ? 22.838 29.550 6.532   1.00 31.91  ? 126 TRP A CZ2 1 
ATOM   967  C CZ3 . TRP A 1 126 ? 24.356 28.802 8.260   1.00 32.45  ? 126 TRP A CZ3 1 
ATOM   968  C CH2 . TRP A 1 126 ? 23.830 29.811 7.437   1.00 29.70  ? 126 TRP A CH2 1 
ATOM   969  N N   . HIS A 1 127 ? 23.977 22.835 5.613   1.00 29.06  ? 127 HIS A N   1 
ATOM   970  C CA  . HIS A 1 127 ? 24.842 22.618 4.459   1.00 29.85  ? 127 HIS A CA  1 
ATOM   971  C C   . HIS A 1 127 ? 24.221 21.626 3.484   1.00 33.81  ? 127 HIS A C   1 
ATOM   972  O O   . HIS A 1 127 ? 24.279 21.821 2.264   1.00 27.58  ? 127 HIS A O   1 
ATOM   973  C CB  . HIS A 1 127 ? 26.217 22.128 4.925   1.00 32.58  ? 127 HIS A CB  1 
ATOM   974  C CG  . HIS A 1 127 ? 27.068 21.561 3.829   1.00 34.25  ? 127 HIS A CG  1 
ATOM   975  N ND1 . HIS A 1 127 ? 27.871 22.348 3.031   1.00 33.24  ? 127 HIS A ND1 1 
ATOM   976  C CD2 . HIS A 1 127 ? 27.244 20.289 3.401   1.00 30.43  ? 127 HIS A CD2 1 
ATOM   977  C CE1 . HIS A 1 127 ? 28.503 21.584 2.156   1.00 29.31  ? 127 HIS A CE1 1 
ATOM   978  N NE2 . HIS A 1 127 ? 28.139 20.330 2.359   1.00 38.61  ? 127 HIS A NE2 1 
ATOM   979  N N   . GLN A 1 128 ? 23.611 20.559 4.000   1.00 29.63  ? 128 GLN A N   1 
ATOM   980  C CA  . GLN A 1 128 ? 23.031 19.564 3.105   1.00 32.90  ? 128 GLN A CA  1 
ATOM   981  C C   . GLN A 1 128 ? 21.800 20.106 2.385   1.00 34.65  ? 128 GLN A C   1 
ATOM   982  O O   . GLN A 1 128 ? 21.536 19.722 1.242   1.00 33.89  ? 128 GLN A O   1 
ATOM   983  C CB  . GLN A 1 128 ? 22.692 18.290 3.883   1.00 34.04  ? 128 GLN A CB  1 
ATOM   984  C CG  . GLN A 1 128 ? 22.151 17.159 3.011   1.00 46.93  ? 128 GLN A CG  1 
ATOM   985  C CD  . GLN A 1 128 ? 22.950 16.973 1.725   1.00 65.02  ? 128 GLN A CD  1 
ATOM   986  O OE1 . GLN A 1 128 ? 24.154 16.707 1.758   1.00 58.21  ? 128 GLN A OE1 1 
ATOM   987  N NE2 . GLN A 1 128 ? 22.277 17.104 0.584   1.00 53.59  ? 128 GLN A NE2 1 
ATOM   988  N N   . ALA A 1 129 ? 21.041 21.000 3.025   1.00 30.24  ? 129 ALA A N   1 
ATOM   989  C CA  . ALA A 1 129 ? 19.908 21.615 2.340   1.00 30.65  ? 129 ALA A CA  1 
ATOM   990  C C   . ALA A 1 129 ? 20.362 22.558 1.232   1.00 33.39  ? 129 ALA A C   1 
ATOM   991  O O   . ALA A 1 129 ? 19.664 22.711 0.222   1.00 32.80  ? 129 ALA A O   1 
ATOM   992  C CB  . ALA A 1 129 ? 19.024 22.358 3.341   1.00 30.67  ? 129 ALA A CB  1 
ATOM   993  N N   . ILE A 1 130 ? 21.518 23.203 1.400   1.00 27.94  ? 130 ILE A N   1 
ATOM   994  C CA  . ILE A 1 130 ? 22.049 24.055 0.342   1.00 25.10  ? 130 ILE A CA  1 
ATOM   995  C C   . ILE A 1 130 ? 22.599 23.206 -0.795  1.00 28.48  ? 130 ILE A C   1 
ATOM   996  O O   . ILE A 1 130 ? 22.377 23.505 -1.976  1.00 31.64  ? 130 ILE A O   1 
ATOM   997  C CB  . ILE A 1 130 ? 23.112 25.008 0.919   1.00 23.31  ? 130 ILE A CB  1 
ATOM   998  C CG1 . ILE A 1 130 ? 22.504 25.832 2.055   1.00 28.96  ? 130 ILE A CG1 1 
ATOM   999  C CG2 . ILE A 1 130 ? 23.707 25.897 -0.177  1.00 25.49  ? 130 ILE A CG2 1 
ATOM   1000 C CD1 . ILE A 1 130 ? 21.995 27.182 1.636   1.00 48.49  ? 130 ILE A CD1 1 
ATOM   1001 N N   . VAL A 1 131 ? 23.307 22.125 -0.456  1.00 25.99  ? 131 VAL A N   1 
ATOM   1002 C CA  . VAL A 1 131 ? 23.787 21.180 -1.465  1.00 27.36  ? 131 VAL A CA  1 
ATOM   1003 C C   . VAL A 1 131 ? 22.625 20.672 -2.307  1.00 30.15  ? 131 VAL A C   1 
ATOM   1004 O O   . VAL A 1 131 ? 22.701 20.616 -3.539  1.00 31.36  ? 131 VAL A O   1 
ATOM   1005 C CB  . VAL A 1 131 ? 24.533 20.013 -0.791  1.00 32.30  ? 131 VAL A CB  1 
ATOM   1006 C CG1 . VAL A 1 131 ? 24.823 18.910 -1.801  1.00 34.00  ? 131 VAL A CG1 1 
ATOM   1007 C CG2 . VAL A 1 131 ? 25.821 20.502 -0.124  1.00 29.22  ? 131 VAL A CG2 1 
ATOM   1008 N N   . GLN A 1 132 ? 21.533 20.281 -1.646  1.00 31.07  ? 132 GLN A N   1 
ATOM   1009 C CA  . GLN A 1 132 ? 20.380 19.744 -2.361  1.00 36.82  ? 132 GLN A CA  1 
ATOM   1010 C C   . GLN A 1 132 ? 19.785 20.777 -3.310  1.00 33.34  ? 132 GLN A C   1 
ATOM   1011 O O   . GLN A 1 132 ? 19.411 20.449 -4.443  1.00 35.59  ? 132 GLN A O   1 
ATOM   1012 C CB  . GLN A 1 132 ? 19.333 19.263 -1.358  1.00 36.78  ? 132 GLN A CB  1 
ATOM   1013 C CG  . GLN A 1 132 ? 18.149 18.555 -1.972  1.00 52.85  ? 132 GLN A CG  1 
ATOM   1014 C CD  . GLN A 1 132 ? 16.846 19.259 -1.661  1.00 75.38  ? 132 GLN A CD  1 
ATOM   1015 O OE1 . GLN A 1 132 ? 16.613 20.383 -2.109  1.00 68.69  ? 132 GLN A OE1 1 
ATOM   1016 N NE2 . GLN A 1 132 ? 15.996 18.610 -0.870  1.00 64.09  ? 132 GLN A NE2 1 
ATOM   1017 N N   . SER A 1 133 ? 19.693 22.034 -2.865  1.00 33.17  ? 133 SER A N   1 
ATOM   1018 C CA  . SER A 1 133 ? 19.165 23.093 -3.721  1.00 35.98  ? 133 SER A CA  1 
ATOM   1019 C C   . SER A 1 133 ? 20.093 23.375 -4.895  1.00 33.67  ? 133 SER A C   1 
ATOM   1020 O O   . SER A 1 133 ? 19.629 23.605 -6.020  1.00 31.39  ? 133 SER A O   1 
ATOM   1021 C CB  . SER A 1 133 ? 18.942 24.369 -2.909  1.00 40.09  ? 133 SER A CB  1 
ATOM   1022 O OG  . SER A 1 133 ? 18.609 25.447 -3.770  1.00 35.73  ? 133 SER A OG  1 
ATOM   1023 N N   . ILE A 1 134 ? 21.405 23.383 -4.650  1.00 30.68  ? 134 ILE A N   1 
ATOM   1024 C CA  . ILE A 1 134 ? 22.364 23.617 -5.727  1.00 27.71  ? 134 ILE A CA  1 
ATOM   1025 C C   . ILE A 1 134 ? 22.271 22.504 -6.759  1.00 35.37  ? 134 ILE A C   1 
ATOM   1026 O O   . ILE A 1 134 ? 22.192 22.754 -7.968  1.00 33.69  ? 134 ILE A O   1 
ATOM   1027 C CB  . ILE A 1 134 ? 23.791 23.732 -5.162  1.00 26.31  ? 134 ILE A CB  1 
ATOM   1028 C CG1 . ILE A 1 134 ? 23.971 25.046 -4.407  1.00 31.70  ? 134 ILE A CG1 1 
ATOM   1029 C CG2 . ILE A 1 134 ? 24.828 23.640 -6.288  1.00 27.66  ? 134 ILE A CG2 1 
ATOM   1030 C CD1 . ILE A 1 134 ? 25.222 25.064 -3.543  1.00 30.63  ? 134 ILE A CD1 1 
ATOM   1031 N N   . GLU A 1 135 ? 22.278 21.254 -6.295  1.00 33.47  ? 135 GLU A N   1 
ATOM   1032 C CA  . GLU A 1 135 ? 22.260 20.131 -7.224  1.00 36.94  ? 135 GLU A CA  1 
ATOM   1033 C C   . GLU A 1 135 ? 20.937 20.048 -7.975  1.00 42.55  ? 135 GLU A C   1 
ATOM   1034 O O   . GLU A 1 135 ? 20.908 19.624 -9.136  1.00 36.23  ? 135 GLU A O   1 
ATOM   1035 C CB  . GLU A 1 135 ? 22.555 18.834 -6.466  1.00 46.46  ? 135 GLU A CB  1 
ATOM   1036 C CG  . GLU A 1 135 ? 24.055 18.567 -6.321  1.00 52.49  ? 135 GLU A CG  1 
ATOM   1037 C CD  . GLU A 1 135 ? 24.369 17.388 -5.423  1.00 58.29  ? 135 GLU A CD  1 
ATOM   1038 O OE1 . GLU A 1 135 ? 23.434 16.643 -5.065  1.00 67.17  ? 135 GLU A OE1 1 
ATOM   1039 O OE2 . GLU A 1 135 ? 25.557 17.204 -5.079  1.00 71.23  ? 135 GLU A OE2 1 
ATOM   1040 N N   . CYS A 1 136 ? 19.838 20.465 -7.346  1.00 32.64  ? 136 CYS A N   1 
ATOM   1041 C CA  . CYS A 1 136 ? 18.572 20.520 -8.067  1.00 42.51  ? 136 CYS A CA  1 
ATOM   1042 C C   . CYS A 1 136 ? 18.607 21.598 -9.143  1.00 37.64  ? 136 CYS A C   1 
ATOM   1043 O O   . CYS A 1 136 ? 18.168 21.367 -10.273 1.00 39.56  ? 136 CYS A O   1 
ATOM   1044 C CB  . CYS A 1 136 ? 17.423 20.764 -7.092  1.00 42.73  ? 136 CYS A CB  1 
ATOM   1045 S SG  . CYS A 1 136 ? 15.836 21.055 -7.890  1.00 51.72  ? 136 CYS A SG  1 
ATOM   1046 N N   . GLY A 1 137 ? 19.146 22.777 -8.818  1.00 35.66  ? 137 GLY A N   1 
ATOM   1047 C CA  . GLY A 1 137 ? 19.260 23.829 -9.816  1.00 31.75  ? 137 GLY A CA  1 
ATOM   1048 C C   . GLY A 1 137 ? 20.183 23.466 -10.962 1.00 36.69  ? 137 GLY A C   1 
ATOM   1049 O O   . GLY A 1 137 ? 19.941 23.854 -12.109 1.00 39.15  ? 137 GLY A O   1 
ATOM   1050 N N   . GLN A 1 138 ? 21.245 22.710 -10.677 1.00 38.49  ? 138 GLN A N   1 
ATOM   1051 C CA  . GLN A 1 138 ? 22.122 22.241 -11.746 1.00 37.15  ? 138 GLN A CA  1 
ATOM   1052 C C   . GLN A 1 138 ? 21.429 21.190 -12.607 1.00 34.44  ? 138 GLN A C   1 
ATOM   1053 O O   . GLN A 1 138 ? 21.528 21.224 -13.840 1.00 43.26  ? 138 GLN A O   1 
ATOM   1054 C CB  . GLN A 1 138 ? 23.413 21.690 -11.145 1.00 42.31  ? 138 GLN A CB  1 
ATOM   1055 C CG  . GLN A 1 138 ? 24.213 22.736 -10.393 1.00 36.20  ? 138 GLN A CG  1 
ATOM   1056 C CD  . GLN A 1 138 ? 25.472 22.176 -9.771  1.00 44.79  ? 138 GLN A CD  1 
ATOM   1057 O OE1 . GLN A 1 138 ? 25.466 21.075 -9.219  1.00 42.32  ? 138 GLN A OE1 1 
ATOM   1058 N NE2 . GLN A 1 138 ? 26.553 22.944 -9.825  1.00 42.59  ? 138 GLN A NE2 1 
ATOM   1059 N N   . LYS A 1 139 ? 20.723 20.248 -11.977 1.00 39.49  ? 139 LYS A N   1 
ATOM   1060 C CA  . LYS A 1 139 ? 19.999 19.225 -12.730 1.00 47.43  ? 139 LYS A CA  1 
ATOM   1061 C C   . LYS A 1 139 ? 18.901 19.828 -13.599 1.00 51.77  ? 139 LYS A C   1 
ATOM   1062 O O   . LYS A 1 139 ? 18.592 19.295 -14.673 1.00 50.19  ? 139 LYS A O   1 
ATOM   1063 C CB  . LYS A 1 139 ? 19.403 18.197 -11.765 1.00 39.27  ? 139 LYS A CB  1 
ATOM   1064 C CG  . LYS A 1 139 ? 19.284 16.779 -12.324 1.00 53.67  ? 139 LYS A CG  1 
ATOM   1065 C CD  . LYS A 1 139 ? 18.040 16.093 -11.768 1.00 63.05  ? 139 LYS A CD  1 
ATOM   1066 C CE  . LYS A 1 139 ? 18.186 14.577 -11.700 1.00 62.04  ? 139 LYS A CE  1 
ATOM   1067 N NZ  . LYS A 1 139 ? 18.726 13.998 -12.960 1.00 58.11  ? 139 LYS A NZ  1 
ATOM   1068 N N   . GLU A 1 140 ? 18.298 20.929 -13.155 1.00 43.81  ? 140 GLU A N   1 
ATOM   1069 C CA  . GLU A 1 140 ? 17.204 21.554 -13.885 1.00 44.27  ? 140 GLU A CA  1 
ATOM   1070 C C   . GLU A 1 140 ? 17.682 22.507 -14.967 1.00 45.57  ? 140 GLU A C   1 
ATOM   1071 O O   . GLU A 1 140 ? 16.849 23.058 -15.697 1.00 43.15  ? 140 GLU A O   1 
ATOM   1072 C CB  . GLU A 1 140 ? 16.287 22.296 -12.910 1.00 51.99  ? 140 GLU A CB  1 
ATOM   1073 C CG  . GLU A 1 140 ? 15.617 21.394 -11.889 1.00 54.15  ? 140 GLU A CG  1 
ATOM   1074 C CD  . GLU A 1 140 ? 14.205 21.825 -11.574 1.00 69.76  ? 140 GLU A CD  1 
ATOM   1075 O OE1 . GLU A 1 140 ? 13.792 22.886 -12.084 1.00 77.88  ? 140 GLU A OE1 1 
ATOM   1076 O OE2 . GLU A 1 140 ? 13.516 21.112 -10.813 1.00 67.20  ? 140 GLU A OE2 1 
ATOM   1077 N N   . GLY A 1 141 ? 18.992 22.702 -15.101 1.00 40.89  ? 141 GLY A N   1 
ATOM   1078 C CA  . GLY A 1 141 ? 19.529 23.601 -16.096 1.00 42.85  ? 141 GLY A CA  1 
ATOM   1079 C C   . GLY A 1 141 ? 19.601 25.042 -15.659 1.00 46.27  ? 141 GLY A C   1 
ATOM   1080 O O   . GLY A 1 141 ? 20.032 25.893 -16.447 1.00 49.71  ? 141 GLY A O   1 
ATOM   1081 N N   . GLU A 1 142 ? 19.193 25.346 -14.427 1.00 42.78  ? 142 GLU A N   1 
ATOM   1082 C CA  . GLU A 1 142 ? 19.200 26.725 -13.963 1.00 41.78  ? 142 GLU A CA  1 
ATOM   1083 C C   . GLU A 1 142 ? 20.578 27.169 -13.482 1.00 41.98  ? 142 GLU A C   1 
ATOM   1084 O O   . GLU A 1 142 ? 20.944 28.326 -13.689 1.00 38.28  ? 142 GLU A O   1 
ATOM   1085 C CB  . GLU A 1 142 ? 18.150 26.902 -12.862 1.00 43.64  ? 142 GLU A CB  1 
ATOM   1086 C CG  . GLU A 1 142 ? 18.370 28.095 -11.966 1.00 46.60  ? 142 GLU A CG  1 
ATOM   1087 C CD  . GLU A 1 142 ? 17.335 28.194 -10.863 1.00 60.04  ? 142 GLU A CD  1 
ATOM   1088 O OE1 . GLU A 1 142 ? 16.718 27.161 -10.520 1.00 54.77  ? 142 GLU A OE1 1 
ATOM   1089 O OE2 . GLU A 1 142 ? 17.156 29.307 -10.326 1.00 52.19  ? 142 GLU A OE2 1 
ATOM   1090 N N   . PHE A 1 143 ? 21.361 26.280 -12.869 1.00 42.14  ? 143 PHE A N   1 
ATOM   1091 C CA  . PHE A 1 143 ? 22.677 26.612 -12.335 1.00 37.87  ? 143 PHE A CA  1 
ATOM   1092 C C   . PHE A 1 143 ? 23.783 25.994 -13.185 1.00 44.19  ? 143 PHE A C   1 
ATOM   1093 O O   . PHE A 1 143 ? 23.634 24.888 -13.712 1.00 39.94  ? 143 PHE A O   1 
ATOM   1094 C CB  . PHE A 1 143 ? 22.835 26.106 -10.895 1.00 33.85  ? 143 PHE A CB  1 
ATOM   1095 C CG  . PHE A 1 143 ? 21.986 26.828 -9.885  1.00 31.93  ? 143 PHE A CG  1 
ATOM   1096 C CD1 . PHE A 1 143 ? 21.481 28.091 -10.144 1.00 39.32  ? 143 PHE A CD1 1 
ATOM   1097 C CD2 . PHE A 1 143 ? 21.699 26.234 -8.669  1.00 31.91  ? 143 PHE A CD2 1 
ATOM   1098 C CE1 . PHE A 1 143 ? 20.705 28.748 -9.206  1.00 39.60  ? 143 PHE A CE1 1 
ATOM   1099 C CE2 . PHE A 1 143 ? 20.918 26.885 -7.725  1.00 39.31  ? 143 PHE A CE2 1 
ATOM   1100 C CZ  . PHE A 1 143 ? 20.421 28.143 -7.996  1.00 35.67  ? 143 PHE A CZ  1 
ATOM   1101 N N   . LYS A 1 144 ? 24.910 26.704 -13.295 1.00 41.48  ? 144 LYS A N   1 
ATOM   1102 C CA  . LYS A 1 144 ? 26.115 26.109 -13.861 1.00 44.98  ? 144 LYS A CA  1 
ATOM   1103 C C   . LYS A 1 144 ? 26.787 25.199 -12.836 1.00 52.69  ? 144 LYS A C   1 
ATOM   1104 O O   . LYS A 1 144 ? 26.377 25.117 -11.675 1.00 44.75  ? 144 LYS A O   1 
ATOM   1105 C CB  . LYS A 1 144 ? 27.109 27.178 -14.318 1.00 50.06  ? 144 LYS A CB  1 
ATOM   1106 C CG  . LYS A 1 144 ? 26.500 28.469 -14.826 1.00 57.65  ? 144 LYS A CG  1 
ATOM   1107 C CD  . LYS A 1 144 ? 26.891 28.740 -16.273 1.00 68.86  ? 144 LYS A CD  1 
ATOM   1108 C CE  . LYS A 1 144 ? 26.300 30.053 -16.772 1.00 78.80  ? 144 LYS A CE  1 
ATOM   1109 N NZ  . LYS A 1 144 ? 27.057 30.627 -17.919 1.00 79.27  ? 144 LYS A NZ  1 
ATOM   1110 N N   . ASN A 1 145 ? 27.851 24.517 -13.268 1.00 49.32  ? 145 ASN A N   1 
ATOM   1111 C CA  . ASN A 1 145 ? 28.625 23.660 -12.368 1.00 64.82  ? 145 ASN A CA  1 
ATOM   1112 C C   . ASN A 1 145 ? 30.129 23.849 -12.591 1.00 52.87  ? 145 ASN A C   1 
ATOM   1113 O O   . ASN A 1 145 ? 30.850 22.941 -12.993 1.00 60.30  ? 145 ASN A O   1 
ATOM   1114 C CB  . ASN A 1 145 ? 28.224 22.194 -12.529 1.00 66.30  ? 145 ASN A CB  1 
ATOM   1115 C CG  . ASN A 1 145 ? 27.871 21.841 -13.953 1.00 65.50  ? 145 ASN A CG  1 
ATOM   1116 O OD1 . ASN A 1 145 ? 28.750 21.685 -14.801 1.00 83.62  ? 145 ASN A OD1 1 
ATOM   1117 N ND2 . ASN A 1 145 ? 26.576 21.702 -14.226 1.00 62.59  ? 145 ASN A ND2 1 
ATOM   1118 N N   . ARG A 1 146 ? 30.624 25.055 -12.303 1.00 56.31  ? 146 ARG A N   1 
ATOM   1119 C CA  . ARG A 1 146 ? 32.063 25.294 -12.375 1.00 58.82  ? 146 ARG A CA  1 
ATOM   1120 C C   . ARG A 1 146 ? 32.797 24.677 -11.191 1.00 62.10  ? 146 ARG A C   1 
ATOM   1121 O O   . ARG A 1 146 ? 33.952 24.260 -11.330 1.00 80.90  ? 146 ARG A O   1 
ATOM   1122 C CB  . ARG A 1 146 ? 32.354 26.794 -12.455 1.00 56.18  ? 146 ARG A CB  1 
ATOM   1123 C CG  . ARG A 1 146 ? 31.435 27.661 -11.618 1.00 48.93  ? 146 ARG A CG  1 
ATOM   1124 C CD  . ARG A 1 146 ? 31.629 29.137 -11.932 1.00 56.88  ? 146 ARG A CD  1 
ATOM   1125 N NE  . ARG A 1 146 ? 31.105 29.494 -13.246 1.00 58.32  ? 146 ARG A NE  1 
ATOM   1126 C CZ  . ARG A 1 146 ? 30.019 30.228 -13.444 1.00 62.99  ? 146 ARG A CZ  1 
ATOM   1127 N NH1 . ARG A 1 146 ? 29.297 30.682 -12.432 1.00 54.94  ? 146 ARG A NH1 1 
ATOM   1128 N NH2 . ARG A 1 146 ? 29.646 30.512 -14.688 1.00 60.20  ? 146 ARG A NH2 1 
ATOM   1129 N N   . SER A 1 147 ? 32.154 24.614 -10.028 1.00 50.39  ? 147 SER A N   1 
ATOM   1130 C CA  . SER A 1 147 ? 32.700 23.946 -8.857  1.00 56.81  ? 147 SER A CA  1 
ATOM   1131 C C   . SER A 1 147 ? 31.695 22.912 -8.374  1.00 59.66  ? 147 SER A C   1 
ATOM   1132 O O   . SER A 1 147 ? 30.524 22.921 -8.768  1.00 56.78  ? 147 SER A O   1 
ATOM   1133 C CB  . SER A 1 147 ? 33.027 24.941 -7.734  1.00 50.91  ? 147 SER A CB  1 
ATOM   1134 O OG  . SER A 1 147 ? 33.100 26.267 -8.227  1.00 48.11  ? 147 SER A OG  1 
ATOM   1135 N N   . ASN A 1 148 ? 32.158 22.005 -7.521  1.00 44.06  ? 148 ASN A N   1 
ATOM   1136 C CA  . ASN A 1 148 ? 31.272 20.974 -7.007  1.00 47.24  ? 148 ASN A CA  1 
ATOM   1137 C C   . ASN A 1 148 ? 30.352 21.555 -5.940  1.00 49.34  ? 148 ASN A C   1 
ATOM   1138 O O   . ASN A 1 148 ? 30.672 22.550 -5.283  1.00 39.92  ? 148 ASN A O   1 
ATOM   1139 C CB  . ASN A 1 148 ? 32.078 19.777 -6.481  1.00 56.58  ? 148 ASN A CB  1 
ATOM   1140 C CG  . ASN A 1 148 ? 32.600 19.971 -5.068  1.00 59.01  ? 148 ASN A CG  1 
ATOM   1141 O OD1 . ASN A 1 148 ? 31.839 20.026 -4.101  1.00 55.36  ? 148 ASN A OD1 1 
ATOM   1142 N ND2 . ASN A 1 148 ? 33.919 20.058 -4.943  1.00 67.19  ? 148 ASN A ND2 1 
ATOM   1143 N N   . SER A 1 149 ? 29.190 20.921 -5.782  1.00 40.98  ? 149 SER A N   1 
ATOM   1144 C CA  . SER A 1 149 ? 28.125 21.496 -4.969  1.00 39.22  ? 149 SER A CA  1 
ATOM   1145 C C   . SER A 1 149 ? 28.487 21.546 -3.488  1.00 36.82  ? 149 SER A C   1 
ATOM   1146 O O   . SER A 1 149 ? 28.026 22.442 -2.770  1.00 34.01  ? 149 SER A O   1 
ATOM   1147 C CB  . SER A 1 149 ? 26.834 20.706 -5.189  1.00 40.94  ? 149 SER A CB  1 
ATOM   1148 O OG  . SER A 1 149 ? 26.917 19.417 -4.609  1.00 42.69  ? 149 SER A OG  1 
ATOM   1149 N N   . THR A 1 150 ? 29.302 20.605 -3.006  1.00 35.40  ? 150 THR A N   1 
ATOM   1150 C CA  . THR A 1 150 ? 29.688 20.635 -1.598  1.00 40.25  ? 150 THR A CA  1 
ATOM   1151 C C   . THR A 1 150 ? 30.579 21.837 -1.303  1.00 31.81  ? 150 THR A C   1 
ATOM   1152 O O   . THR A 1 150 ? 30.421 22.496 -0.267  1.00 32.24  ? 150 THR A O   1 
ATOM   1153 C CB  . THR A 1 150 ? 30.387 19.329 -1.216  1.00 42.32  ? 150 THR A CB  1 
ATOM   1154 O OG1 . THR A 1 150 ? 29.473 18.237 -1.376  1.00 44.82  ? 150 THR A OG1 1 
ATOM   1155 C CG2 . THR A 1 150 ? 30.859 19.371 0.232   1.00 37.64  ? 150 THR A CG2 1 
ATOM   1156 N N   . ASP A 1 151 ? 31.502 22.148 -2.217  1.00 32.92  ? 151 ASP A N   1 
ATOM   1157 C CA  . ASP A 1 151 ? 32.389 23.295 -2.043  1.00 33.13  ? 151 ASP A CA  1 
ATOM   1158 C C   . ASP A 1 151 ? 31.613 24.604 -2.069  1.00 32.80  ? 151 ASP A C   1 
ATOM   1159 O O   . ASP A 1 151 ? 31.855 25.496 -1.246  1.00 32.99  ? 151 ASP A O   1 
ATOM   1160 C CB  . ASP A 1 151 ? 33.455 23.302 -3.137  1.00 38.23  ? 151 ASP A CB  1 
ATOM   1161 C CG  . ASP A 1 151 ? 34.598 22.355 -2.849  1.00 50.80  ? 151 ASP A CG  1 
ATOM   1162 O OD1 . ASP A 1 151 ? 34.744 21.928 -1.689  1.00 40.53  ? 151 ASP A OD1 1 
ATOM   1163 O OD2 . ASP A 1 151 ? 35.349 22.033 -3.794  1.00 57.01  ? 151 ASP A OD2 1 
ATOM   1164 N N   . ILE A 1 152 ? 30.684 24.741 -3.017  1.00 26.57  ? 152 ILE A N   1 
ATOM   1165 C CA  . ILE A 1 152 ? 29.912 25.975 -3.139  1.00 24.71  ? 152 ILE A CA  1 
ATOM   1166 C C   . ILE A 1 152 ? 29.052 26.191 -1.903  1.00 26.52  ? 152 ILE A C   1 
ATOM   1167 O O   . ILE A 1 152 ? 28.918 27.318 -1.410  1.00 27.44  ? 152 ILE A O   1 
ATOM   1168 C CB  . ILE A 1 152 ? 29.050 25.945 -4.416  1.00 25.97  ? 152 ILE A CB  1 
ATOM   1169 C CG1 . ILE A 1 152 ? 29.930 25.916 -5.665  1.00 28.55  ? 152 ILE A CG1 1 
ATOM   1170 C CG2 . ILE A 1 152 ? 28.134 27.163 -4.458  1.00 25.76  ? 152 ILE A CG2 1 
ATOM   1171 C CD1 . ILE A 1 152 ? 29.160 25.640 -6.945  1.00 31.00  ? 152 ILE A CD1 1 
ATOM   1172 N N   . ALA A 1 153 ? 28.440 25.118 -1.391  1.00 26.92  ? 153 ALA A N   1 
ATOM   1173 C CA  . ALA A 1 153 ? 27.576 25.247 -0.221  1.00 29.97  ? 153 ALA A CA  1 
ATOM   1174 C C   . ALA A 1 153 ? 28.343 25.750 0.995   1.00 29.62  ? 153 ALA A C   1 
ATOM   1175 O O   . ALA A 1 153 ? 27.851 26.615 1.730   1.00 25.47  ? 153 ALA A O   1 
ATOM   1176 C CB  . ALA A 1 153 ? 26.906 23.910 0.093   1.00 28.78  ? 153 ALA A CB  1 
ATOM   1177 N N   . TRP A 1 154 ? 29.539 25.206 1.247   1.00 28.42  ? 154 TRP A N   1 
ATOM   1178 C CA  . TRP A 1 154 ? 30.316 25.696 2.384   1.00 29.01  ? 154 TRP A CA  1 
ATOM   1179 C C   . TRP A 1 154 ? 30.725 27.149 2.181   1.00 25.44  ? 154 TRP A C   1 
ATOM   1180 O O   . TRP A 1 154 ? 30.730 27.937 3.135   1.00 28.71  ? 154 TRP A O   1 
ATOM   1181 C CB  . TRP A 1 154 ? 31.554 24.824 2.627   1.00 26.48  ? 154 TRP A CB  1 
ATOM   1182 C CG  . TRP A 1 154 ? 31.275 23.522 3.353   1.00 27.66  ? 154 TRP A CG  1 
ATOM   1183 C CD1 . TRP A 1 154 ? 31.626 22.267 2.943   1.00 33.99  ? 154 TRP A CD1 1 
ATOM   1184 C CD2 . TRP A 1 154 ? 30.577 23.354 4.599   1.00 29.90  ? 154 TRP A CD2 1 
ATOM   1185 N NE1 . TRP A 1 154 ? 31.202 21.332 3.859   1.00 31.57  ? 154 TRP A NE1 1 
ATOM   1186 C CE2 . TRP A 1 154 ? 30.556 21.972 4.882   1.00 28.36  ? 154 TRP A CE2 1 
ATOM   1187 C CE3 . TRP A 1 154 ? 29.973 24.235 5.502   1.00 34.20  ? 154 TRP A CE3 1 
ATOM   1188 C CZ2 . TRP A 1 154 ? 29.953 21.453 6.026   1.00 34.53  ? 154 TRP A CZ2 1 
ATOM   1189 C CZ3 . TRP A 1 154 ? 29.376 23.716 6.640   1.00 34.17  ? 154 TRP A CZ3 1 
ATOM   1190 C CH2 . TRP A 1 154 ? 29.369 22.337 6.889   1.00 34.58  ? 154 TRP A CH2 1 
ATOM   1191 N N   . ARG A 1 155 ? 31.048 27.532 0.945   1.00 24.23  ? 155 ARG A N   1 
ATOM   1192 C CA  . ARG A 1 155 ? 31.450 28.913 0.699   1.00 24.54  ? 155 ARG A CA  1 
ATOM   1193 C C   . ARG A 1 155 ? 30.281 29.870 0.897   1.00 27.60  ? 155 ARG A C   1 
ATOM   1194 O O   . ARG A 1 155 ? 30.463 30.969 1.434   1.00 23.82  ? 155 ARG A O   1 
ATOM   1195 C CB  . ARG A 1 155 ? 32.043 29.043 -0.706  1.00 24.86  ? 155 ARG A CB  1 
ATOM   1196 C CG  . ARG A 1 155 ? 33.435 28.417 -0.824  1.00 31.04  ? 155 ARG A CG  1 
ATOM   1197 C CD  . ARG A 1 155 ? 34.225 28.976 -2.007  1.00 25.20  ? 155 ARG A CD  1 
ATOM   1198 N NE  . ARG A 1 155 ? 33.668 28.560 -3.290  1.00 28.56  ? 155 ARG A NE  1 
ATOM   1199 C CZ  . ARG A 1 155 ? 34.137 27.554 -4.018  1.00 39.20  ? 155 ARG A CZ  1 
ATOM   1200 N NH1 . ARG A 1 155 ? 35.143 26.805 -3.595  1.00 35.43  ? 155 ARG A NH1 1 
ATOM   1201 N NH2 . ARG A 1 155 ? 33.589 27.296 -5.203  1.00 35.19  ? 155 ARG A NH2 1 
ATOM   1202 N N   . LEU A 1 156 ? 29.077 29.466 0.475   1.00 23.65  ? 156 LEU A N   1 
ATOM   1203 C CA  . LEU A 1 156 ? 27.891 30.293 0.686   1.00 20.90  ? 156 LEU A CA  1 
ATOM   1204 C C   . LEU A 1 156 ? 27.577 30.441 2.171   1.00 27.20  ? 156 LEU A C   1 
ATOM   1205 O O   . LEU A 1 156 ? 27.267 31.541 2.642   1.00 24.27  ? 156 LEU A O   1 
ATOM   1206 C CB  . LEU A 1 156 ? 26.699 29.684 -0.060  1.00 24.16  ? 156 LEU A CB  1 
ATOM   1207 C CG  . LEU A 1 156 ? 26.691 29.772 -1.592  1.00 30.18  ? 156 LEU A CG  1 
ATOM   1208 C CD1 . LEU A 1 156 ? 25.462 29.084 -2.183  1.00 30.25  ? 156 LEU A CD1 1 
ATOM   1209 C CD2 . LEU A 1 156 ? 26.753 31.217 -2.082  1.00 25.11  ? 156 LEU A CD2 1 
ATOM   1210 N N   . ILE A 1 157 ? 27.651 29.341 2.928   1.00 23.08  ? 157 ILE A N   1 
ATOM   1211 C CA  . ILE A 1 157 ? 27.432 29.428 4.369   1.00 24.22  ? 157 ILE A CA  1 
ATOM   1212 C C   . ILE A 1 157 ? 28.501 30.300 5.011   1.00 24.95  ? 157 ILE A C   1 
ATOM   1213 O O   . ILE A 1 157 ? 28.204 31.162 5.848   1.00 26.77  ? 157 ILE A O   1 
ATOM   1214 C CB  . ILE A 1 157 ? 27.393 28.018 4.986   1.00 24.23  ? 157 ILE A CB  1 
ATOM   1215 C CG1 . ILE A 1 157 ? 26.063 27.340 4.654   1.00 28.12  ? 157 ILE A CG1 1 
ATOM   1216 C CG2 . ILE A 1 157 ? 27.627 28.079 6.509   1.00 25.77  ? 157 ILE A CG2 1 
ATOM   1217 C CD1 . ILE A 1 157 ? 25.968 25.919 5.151   1.00 35.83  ? 157 ILE A CD1 1 
ATOM   1218 N N   . ALA A 1 158 ? 29.757 30.111 4.611   1.00 23.01  ? 158 ALA A N   1 
ATOM   1219 C CA  . ALA A 1 158 ? 30.839 30.912 5.168   1.00 27.06  ? 158 ALA A CA  1 
ATOM   1220 C C   . ALA A 1 158 ? 30.603 32.392 4.918   1.00 24.69  ? 158 ALA A C   1 
ATOM   1221 O O   . ALA A 1 158 ? 30.831 33.222 5.805   1.00 25.79  ? 158 ALA A O   1 
ATOM   1222 C CB  . ALA A 1 158 ? 32.178 30.478 4.573   1.00 26.71  ? 158 ALA A CB  1 
ATOM   1223 N N   . PHE A 1 159 ? 30.119 32.734 3.723   1.00 25.18  ? 159 PHE A N   1 
ATOM   1224 C CA  . PHE A 1 159 ? 29.904 34.134 3.380   1.00 27.76  ? 159 PHE A CA  1 
ATOM   1225 C C   . PHE A 1 159 ? 28.839 34.767 4.262   1.00 22.82  ? 159 PHE A C   1 
ATOM   1226 O O   . PHE A 1 159 ? 29.046 35.849 4.823   1.00 25.38  ? 159 PHE A O   1 
ATOM   1227 C CB  . PHE A 1 159 ? 29.513 34.279 1.911   1.00 27.62  ? 159 PHE A CB  1 
ATOM   1228 C CG  . PHE A 1 159 ? 29.282 35.698 1.515   1.00 28.40  ? 159 PHE A CG  1 
ATOM   1229 C CD1 . PHE A 1 159 ? 30.356 36.561 1.356   1.00 26.95  ? 159 PHE A CD1 1 
ATOM   1230 C CD2 . PHE A 1 159 ? 28.002 36.191 1.362   1.00 26.45  ? 159 PHE A CD2 1 
ATOM   1231 C CE1 . PHE A 1 159 ? 30.153 37.888 1.024   1.00 32.67  ? 159 PHE A CE1 1 
ATOM   1232 C CE2 . PHE A 1 159 ? 27.792 37.519 1.025   1.00 32.74  ? 159 PHE A CE2 1 
ATOM   1233 C CZ  . PHE A 1 159 ? 28.869 38.367 0.858   1.00 29.88  ? 159 PHE A CZ  1 
ATOM   1234 N N   . VAL A 1 160 ? 27.674 34.125 4.374   1.00 25.84  ? 160 VAL A N   1 
ATOM   1235 C CA  . VAL A 1 160 ? 26.588 34.755 5.112   1.00 23.59  ? 160 VAL A CA  1 
ATOM   1236 C C   . VAL A 1 160 ? 26.905 34.793 6.605   1.00 22.06  ? 160 VAL A C   1 
ATOM   1237 O O   . VAL A 1 160 ? 26.578 35.767 7.288   1.00 25.09  ? 160 VAL A O   1 
ATOM   1238 C CB  . VAL A 1 160 ? 25.236 34.070 4.816   1.00 25.48  ? 160 VAL A CB  1 
ATOM   1239 C CG1 . VAL A 1 160 ? 24.900 34.155 3.321   1.00 30.63  ? 160 VAL A CG1 1 
ATOM   1240 C CG2 . VAL A 1 160 ? 25.247 32.624 5.262   1.00 30.50  ? 160 VAL A CG2 1 
ATOM   1241 N N   . CYS A 1 161 ? 27.563 33.759 7.135   1.00 23.04  ? 161 CYS A N   1 
ATOM   1242 C CA  . CYS A 1 161 ? 27.959 33.809 8.542   1.00 26.74  ? 161 CYS A CA  1 
ATOM   1243 C C   . CYS A 1 161 ? 29.007 34.888 8.770   1.00 25.70  ? 161 CYS A C   1 
ATOM   1244 O O   . CYS A 1 161 ? 28.962 35.599 9.781   1.00 26.77  ? 161 CYS A O   1 
ATOM   1245 C CB  . CYS A 1 161 ? 28.487 32.451 9.000   1.00 25.50  ? 161 CYS A CB  1 
ATOM   1246 S SG  . CYS A 1 161 ? 27.260 31.136 8.983   1.00 34.19  ? 161 CYS A SG  1 
ATOM   1247 N N   . GLY A 1 162 ? 29.947 35.029 7.835   1.00 25.01  ? 162 GLY A N   1 
ATOM   1248 C CA  . GLY A 1 162 ? 30.963 36.061 7.965   1.00 24.99  ? 162 GLY A CA  1 
ATOM   1249 C C   . GLY A 1 162 ? 30.391 37.458 7.849   1.00 26.46  ? 162 GLY A C   1 
ATOM   1250 O O   . GLY A 1 162 ? 30.766 38.357 8.607   1.00 27.47  ? 162 GLY A O   1 
ATOM   1251 N N   . LEU A 1 163 ? 29.468 37.656 6.907   1.00 25.67  ? 163 LEU A N   1 
ATOM   1252 C CA  . LEU A 1 163 ? 28.840 38.962 6.751   1.00 26.88  ? 163 LEU A CA  1 
ATOM   1253 C C   . LEU A 1 163 ? 28.059 39.343 8.001   1.00 27.40  ? 163 LEU A C   1 
ATOM   1254 O O   . LEU A 1 163 ? 28.159 40.475 8.491   1.00 26.86  ? 163 LEU A O   1 
ATOM   1255 C CB  . LEU A 1 163 ? 27.937 38.955 5.516   1.00 27.61  ? 163 LEU A CB  1 
ATOM   1256 C CG  . LEU A 1 163 ? 27.527 40.327 4.987   1.00 34.65  ? 163 LEU A CG  1 
ATOM   1257 C CD1 . LEU A 1 163 ? 28.719 41.273 4.937   1.00 34.42  ? 163 LEU A CD1 1 
ATOM   1258 C CD2 . LEU A 1 163 ? 26.873 40.182 3.623   1.00 29.08  ? 163 LEU A CD2 1 
ATOM   1259 N N   . GLU A 1 164 ? 27.283 38.403 8.545   1.00 27.76  ? 164 GLU A N   1 
ATOM   1260 C CA  . GLU A 1 164 ? 26.546 38.690 9.774   1.00 31.41  ? 164 GLU A CA  1 
ATOM   1261 C C   . GLU A 1 164 ? 27.486 38.880 10.961  1.00 33.67  ? 164 GLU A C   1 
ATOM   1262 O O   . GLU A 1 164 ? 27.190 39.671 11.862  1.00 29.77  ? 164 GLU A O   1 
ATOM   1263 C CB  . GLU A 1 164 ? 25.530 37.577 10.033  1.00 38.09  ? 164 GLU A CB  1 
ATOM   1264 C CG  . GLU A 1 164 ? 24.490 37.474 8.912   1.00 45.42  ? 164 GLU A CG  1 
ATOM   1265 C CD  . GLU A 1 164 ? 23.575 36.270 9.040   1.00 71.22  ? 164 GLU A CD  1 
ATOM   1266 O OE1 . GLU A 1 164 ? 24.084 35.155 9.292   1.00 65.11  ? 164 GLU A OE1 1 
ATOM   1267 O OE2 . GLU A 1 164 ? 22.346 36.438 8.874   1.00 69.37  ? 164 GLU A OE2 1 
ATOM   1268 N N   . GLY A 1 165 ? 28.629 38.193 10.971  1.00 29.62  ? 165 GLY A N   1 
ATOM   1269 C CA  . GLY A 1 165 ? 29.614 38.440 12.012  1.00 26.63  ? 165 GLY A CA  1 
ATOM   1270 C C   . GLY A 1 165 ? 30.175 39.847 11.959  1.00 30.02  ? 165 GLY A C   1 
ATOM   1271 O O   . GLY A 1 165 ? 30.403 40.475 12.996  1.00 32.23  ? 165 GLY A O   1 
ATOM   1272 N N   . ILE A 1 166 ? 30.387 40.373 10.751  1.00 23.26  ? 166 ILE A N   1 
ATOM   1273 C CA  . ILE A 1 166 ? 30.948 41.713 10.615  1.00 26.69  ? 166 ILE A CA  1 
ATOM   1274 C C   . ILE A 1 166 ? 29.905 42.765 10.980  1.00 33.91  ? 166 ILE A C   1 
ATOM   1275 O O   . ILE A 1 166 ? 30.234 43.825 11.530  1.00 29.43  ? 166 ILE A O   1 
ATOM   1276 C CB  . ILE A 1 166 ? 31.496 41.917 9.189   1.00 34.61  ? 166 ILE A CB  1 
ATOM   1277 C CG1 . ILE A 1 166 ? 32.704 41.015 8.933   1.00 38.62  ? 166 ILE A CG1 1 
ATOM   1278 C CG2 . ILE A 1 166 ? 31.978 43.328 9.015   1.00 46.02  ? 166 ILE A CG2 1 
ATOM   1279 C CD1 . ILE A 1 166 ? 33.566 40.781 10.144  1.00 46.09  ? 166 ILE A CD1 1 
ATOM   1280 N N   . TYR A 1 167 ? 28.628 42.490 10.685  1.00 28.85  ? 167 TYR A N   1 
ATOM   1281 C CA  . TYR A 1 167 ? 27.552 43.379 11.126  1.00 31.64  ? 167 TYR A CA  1 
ATOM   1282 C C   . TYR A 1 167 ? 27.531 43.535 12.642  1.00 30.59  ? 167 TYR A C   1 
ATOM   1283 O O   . TYR A 1 167 ? 27.199 44.610 13.157  1.00 32.52  ? 167 TYR A O   1 
ATOM   1284 C CB  . TYR A 1 167 ? 26.199 42.853 10.650  1.00 32.50  ? 167 TYR A CB  1 
ATOM   1285 C CG  . TYR A 1 167 ? 25.984 42.967 9.167   1.00 30.23  ? 167 TYR A CG  1 
ATOM   1286 C CD1 . TYR A 1 167 ? 26.676 43.906 8.415   1.00 29.96  ? 167 TYR A CD1 1 
ATOM   1287 C CD2 . TYR A 1 167 ? 25.094 42.127 8.513   1.00 35.89  ? 167 TYR A CD2 1 
ATOM   1288 C CE1 . TYR A 1 167 ? 26.482 44.012 7.051   1.00 33.85  ? 167 TYR A CE1 1 
ATOM   1289 C CE2 . TYR A 1 167 ? 24.898 42.223 7.146   1.00 30.18  ? 167 TYR A CE2 1 
ATOM   1290 C CZ  . TYR A 1 167 ? 25.590 43.165 6.425   1.00 36.98  ? 167 TYR A CZ  1 
ATOM   1291 O OH  . TYR A 1 167 ? 25.390 43.259 5.065   1.00 46.90  ? 167 TYR A OH  1 
ATOM   1292 N N   . LYS A 1 168 ? 27.847 42.464 13.375  1.00 28.80  ? 168 LYS A N   1 
ATOM   1293 C CA  . LYS A 1 168 ? 27.819 42.530 14.832  1.00 31.10  ? 168 LYS A CA  1 
ATOM   1294 C C   . LYS A 1 168 ? 28.862 43.484 15.391  1.00 36.99  ? 168 LYS A C   1 
ATOM   1295 O O   . LYS A 1 168 ? 28.763 43.871 16.559  1.00 32.49  ? 168 LYS A O   1 
ATOM   1296 C CB  . LYS A 1 168 ? 28.029 41.145 15.445  1.00 34.54  ? 168 LYS A CB  1 
ATOM   1297 C CG  . LYS A 1 168 ? 26.854 40.191 15.296  1.00 56.31  ? 168 LYS A CG  1 
ATOM   1298 C CD  . LYS A 1 168 ? 27.060 38.945 16.156  1.00 53.07  ? 168 LYS A CD  1 
ATOM   1299 C CE  . LYS A 1 168 ? 27.178 37.693 15.306  1.00 61.61  ? 168 LYS A CE  1 
ATOM   1300 N NZ  . LYS A 1 168 ? 25.842 37.098 15.012  1.00 67.53  ? 168 LYS A NZ  1 
ATOM   1301 N N   . LEU A 1 169 ? 29.854 43.873 14.591  1.00 30.19  ? 169 LEU A N   1 
ATOM   1302 C CA  . LEU A 1 169 ? 30.920 44.730 15.094  1.00 35.68  ? 169 LEU A CA  1 
ATOM   1303 C C   . LEU A 1 169 ? 30.476 46.174 15.260  1.00 36.75  ? 169 LEU A C   1 
ATOM   1304 O O   . LEU A 1 169 ? 31.058 46.900 16.074  1.00 33.15  ? 169 LEU A O   1 
ATOM   1305 C CB  . LEU A 1 169 ? 32.125 44.660 14.157  1.00 30.97  ? 169 LEU A CB  1 
ATOM   1306 C CG  . LEU A 1 169 ? 32.828 43.300 14.097  1.00 26.80  ? 169 LEU A CG  1 
ATOM   1307 C CD1 . LEU A 1 169 ? 34.015 43.360 13.142  1.00 30.11  ? 169 LEU A CD1 1 
ATOM   1308 C CD2 . LEU A 1 169 ? 33.281 42.848 15.472  1.00 27.87  ? 169 LEU A CD2 1 
ATOM   1309 N N   . GLY A 1 170 ? 29.458 46.605 14.520  1.00 33.85  ? 170 GLY A N   1 
ATOM   1310 C CA  . GLY A 1 170 ? 29.053 47.995 14.547  1.00 30.79  ? 170 GLY A CA  1 
ATOM   1311 C C   . GLY A 1 170 ? 30.064 48.898 13.868  1.00 35.84  ? 170 GLY A C   1 
ATOM   1312 O O   . GLY A 1 170 ? 30.395 49.969 14.386  1.00 36.08  ? 170 GLY A O   1 
ATOM   1313 N N   . LEU A 1 171 ? 30.567 48.473 12.710  1.00 32.82  ? 171 LEU A N   1 
ATOM   1314 C CA  . LEU A 1 171 ? 31.456 49.297 11.907  1.00 36.01  ? 171 LEU A CA  1 
ATOM   1315 C C   . LEU A 1 171 ? 30.682 50.457 11.282  1.00 53.14  ? 171 LEU A C   1 
ATOM   1316 O O   . LEU A 1 171 ? 29.460 50.408 11.122  1.00 50.32  ? 171 LEU A O   1 
ATOM   1317 C CB  . LEU A 1 171 ? 32.126 48.455 10.822  1.00 36.67  ? 171 LEU A CB  1 
ATOM   1318 C CG  . LEU A 1 171 ? 33.040 47.354 11.359  1.00 35.72  ? 171 LEU A CG  1 
ATOM   1319 C CD1 . LEU A 1 171 ? 33.449 46.399 10.258  1.00 33.46  ? 171 LEU A CD1 1 
ATOM   1320 C CD2 . LEU A 1 171 ? 34.269 47.978 12.000  1.00 40.82  ? 171 LEU A CD2 1 
ATOM   1321 N N   . GLN A 1 172 ? 31.416 51.509 10.914  1.00 45.07  ? 172 GLN A N   1 
ATOM   1322 C CA  . GLN A 1 172 ? 30.787 52.771 10.537  1.00 51.28  ? 172 GLN A CA  1 
ATOM   1323 C C   . GLN A 1 172 ? 30.468 52.901 9.053   1.00 58.35  ? 172 GLN A C   1 
ATOM   1324 O O   . GLN A 1 172 ? 29.607 53.712 8.695   1.00 73.05  ? 172 GLN A O   1 
ATOM   1325 C CB  . GLN A 1 172 ? 31.669 53.949 10.959  1.00 56.51  ? 172 GLN A CB  1 
ATOM   1326 C CG  . GLN A 1 172 ? 31.846 54.044 12.460  1.00 62.75  ? 172 GLN A CG  1 
ATOM   1327 C CD  . GLN A 1 172 ? 30.889 55.037 13.084  1.00 69.95  ? 172 GLN A CD  1 
ATOM   1328 O OE1 . GLN A 1 172 ? 29.682 54.981 12.850  1.00 72.55  ? 172 GLN A OE1 1 
ATOM   1329 N NE2 . GLN A 1 172 ? 31.421 55.953 13.885  1.00 73.76  ? 172 GLN A NE2 1 
ATOM   1330 N N   . GLY A 1 173 ? 31.126 52.147 8.179   1.00 46.16  ? 173 GLY A N   1 
ATOM   1331 C CA  . GLY A 1 173 ? 30.844 52.311 6.764   1.00 62.40  ? 173 GLY A CA  1 
ATOM   1332 C C   . GLY A 1 173 ? 30.112 51.141 6.143   1.00 51.62  ? 173 GLY A C   1 
ATOM   1333 O O   . GLY A 1 173 ? 30.243 50.884 4.942   1.00 50.58  ? 173 GLY A O   1 
ATOM   1334 N N   . LEU A 1 174 ? 29.329 50.426 6.945   1.00 45.36  ? 174 LEU A N   1 
ATOM   1335 C CA  . LEU A 1 174 ? 28.754 49.152 6.533   1.00 42.10  ? 174 LEU A CA  1 
ATOM   1336 C C   . LEU A 1 174 ? 27.274 49.132 6.880   1.00 46.22  ? 174 LEU A C   1 
ATOM   1337 O O   . LEU A 1 174 ? 26.909 49.184 8.060   1.00 42.73  ? 174 LEU A O   1 
ATOM   1338 C CB  . LEU A 1 174 ? 29.479 47.989 7.208   1.00 42.40  ? 174 LEU A CB  1 
ATOM   1339 C CG  . LEU A 1 174 ? 29.143 46.596 6.691   1.00 48.44  ? 174 LEU A CG  1 
ATOM   1340 C CD1 . LEU A 1 174 ? 29.414 46.494 5.203   1.00 43.83  ? 174 LEU A CD1 1 
ATOM   1341 C CD2 . LEU A 1 174 ? 29.943 45.576 7.455   1.00 42.82  ? 174 LEU A CD2 1 
ATOM   1342 N N   . ALA A 1 175 ? 26.427 49.045 5.859   1.00 40.96  ? 175 ALA A N   1 
ATOM   1343 C CA  . ALA A 1 175 ? 24.982 49.081 6.035   1.00 39.15  ? 175 ALA A CA  1 
ATOM   1344 C C   . ALA A 1 175 ? 24.436 47.658 6.058   1.00 40.68  ? 175 ALA A C   1 
ATOM   1345 O O   . ALA A 1 175 ? 24.610 46.908 5.091   1.00 39.73  ? 175 ALA A O   1 
ATOM   1346 C CB  . ALA A 1 175 ? 24.323 49.896 4.923   1.00 42.91  ? 175 ALA A CB  1 
ATOM   1347 N N   . GLU A 1 176 ? 23.773 47.297 7.163   1.00 38.11  ? 176 GLU A N   1 
ATOM   1348 C CA  . GLU A 1 176 ? 23.154 45.979 7.279   1.00 31.27  ? 176 GLU A CA  1 
ATOM   1349 C C   . GLU A 1 176 ? 22.147 45.727 6.166   1.00 42.68  ? 176 GLU A C   1 
ATOM   1350 O O   . GLU A 1 176 ? 21.942 44.577 5.762   1.00 35.78  ? 176 GLU A O   1 
ATOM   1351 C CB  . GLU A 1 176 ? 22.463 45.844 8.637   1.00 44.51  ? 176 GLU A CB  1 
ATOM   1352 C CG  . GLU A 1 176 ? 23.396 45.835 9.836   1.00 43.88  ? 176 GLU A CG  1 
ATOM   1353 C CD  . GLU A 1 176 ? 22.759 45.202 11.063  1.00 41.12  ? 176 GLU A CD  1 
ATOM   1354 O OE1 . GLU A 1 176 ? 21.678 44.586 10.930  1.00 50.54  ? 176 GLU A OE1 1 
ATOM   1355 O OE2 . GLU A 1 176 ? 23.329 45.333 12.163  1.00 42.81  ? 176 GLU A OE2 1 
ATOM   1356 N N   . GLU A 1 177 ? 21.505 46.783 5.665   1.00 37.19  ? 177 GLU A N   1 
ATOM   1357 C CA  . GLU A 1 177 ? 20.477 46.646 4.641   1.00 43.99  ? 177 GLU A CA  1 
ATOM   1358 C C   . GLU A 1 177 ? 21.025 46.149 3.307   1.00 44.37  ? 177 GLU A C   1 
ATOM   1359 O O   . GLU A 1 177 ? 20.232 45.826 2.416   1.00 49.12  ? 177 GLU A O   1 
ATOM   1360 C CB  . GLU A 1 177 ? 19.749 47.982 4.441   1.00 48.64  ? 177 GLU A CB  1 
ATOM   1361 C CG  . GLU A 1 177 ? 19.445 48.758 5.735   1.00 68.89  ? 177 GLU A CG  1 
ATOM   1362 C CD  . GLU A 1 177 ? 20.658 49.476 6.319   1.00 84.11  ? 177 GLU A CD  1 
ATOM   1363 O OE1 . GLU A 1 177 ? 21.278 50.281 5.592   1.00 88.93  ? 177 GLU A OE1 1 
ATOM   1364 O OE2 . GLU A 1 177 ? 20.996 49.228 7.499   1.00 69.54  ? 177 GLU A OE2 1 
ATOM   1365 N N   . ASP A 1 178 ? 22.346 46.076 3.150   1.00 41.13  ? 178 ASP A N   1 
ATOM   1366 C CA  . ASP A 1 178 ? 22.971 45.587 1.926   1.00 34.89  ? 178 ASP A CA  1 
ATOM   1367 C C   . ASP A 1 178 ? 23.127 44.070 1.895   1.00 36.61  ? 178 ASP A C   1 
ATOM   1368 O O   . ASP A 1 178 ? 23.666 43.549 0.912   1.00 33.91  ? 178 ASP A O   1 
ATOM   1369 C CB  . ASP A 1 178 ? 24.349 46.229 1.744   1.00 39.75  ? 178 ASP A CB  1 
ATOM   1370 C CG  . ASP A 1 178 ? 24.268 47.677 1.310   1.00 52.34  ? 178 ASP A CG  1 
ATOM   1371 O OD1 . ASP A 1 178 ? 23.198 48.092 0.820   1.00 55.35  ? 178 ASP A OD1 1 
ATOM   1372 O OD2 . ASP A 1 178 ? 25.280 48.395 1.450   1.00 50.65  ? 178 ASP A OD2 1 
ATOM   1373 N N   . PHE A 1 179 ? 22.674 43.359 2.932   1.00 34.32  ? 179 PHE A N   1 
ATOM   1374 C CA  . PHE A 1 179 ? 22.923 41.921 3.029   1.00 33.26  ? 179 PHE A CA  1 
ATOM   1375 C C   . PHE A 1 179 ? 22.380 41.161 1.823   1.00 40.28  ? 179 PHE A C   1 
ATOM   1376 O O   . PHE A 1 179 ? 23.069 40.304 1.260   1.00 32.48  ? 179 PHE A O   1 
ATOM   1377 C CB  . PHE A 1 179 ? 22.326 41.366 4.322   1.00 34.70  ? 179 PHE A CB  1 
ATOM   1378 C CG  . PHE A 1 179 ? 22.489 39.877 4.470   1.00 34.88  ? 179 PHE A CG  1 
ATOM   1379 C CD1 . PHE A 1 179 ? 23.636 39.340 5.027   1.00 38.11  ? 179 PHE A CD1 1 
ATOM   1380 C CD2 . PHE A 1 179 ? 21.471 39.016 4.083   1.00 42.85  ? 179 PHE A CD2 1 
ATOM   1381 C CE1 . PHE A 1 179 ? 23.781 37.969 5.165   1.00 34.61  ? 179 PHE A CE1 1 
ATOM   1382 C CE2 . PHE A 1 179 ? 21.608 37.647 4.222   1.00 41.14  ? 179 PHE A CE2 1 
ATOM   1383 C CZ  . PHE A 1 179 ? 22.764 37.123 4.766   1.00 38.65  ? 179 PHE A CZ  1 
ATOM   1384 N N   . LYS A 1 180 ? 21.131 41.432 1.436   1.00 34.42  ? 180 LYS A N   1 
ATOM   1385 C CA  . LYS A 1 180 ? 20.552 40.743 0.285   1.00 36.35  ? 180 LYS A CA  1 
ATOM   1386 C C   . LYS A 1 180 ? 21.362 41.007 -0.977  1.00 33.28  ? 180 LYS A C   1 
ATOM   1387 O O   . LYS A 1 180 ? 21.679 40.080 -1.733  1.00 36.16  ? 180 LYS A O   1 
ATOM   1388 C CB  . LYS A 1 180 ? 19.100 41.174 0.083   1.00 41.19  ? 180 LYS A CB  1 
ATOM   1389 C CG  . LYS A 1 180 ? 18.363 40.324 -0.940  1.00 45.30  ? 180 LYS A CG  1 
ATOM   1390 C CD  . LYS A 1 180 ? 17.019 40.918 -1.310  1.00 51.52  ? 180 LYS A CD  1 
ATOM   1391 C CE  . LYS A 1 180 ? 16.400 40.155 -2.470  1.00 67.35  ? 180 LYS A CE  1 
ATOM   1392 N NZ  . LYS A 1 180 ? 16.124 38.737 -2.109  1.00 70.15  ? 180 LYS A NZ  1 
ATOM   1393 N N   . ARG A 1 181 ? 21.709 42.274 -1.215  1.00 36.02  ? 181 ARG A N   1 
ATOM   1394 C CA  . ARG A 1 181 ? 22.464 42.643 -2.408  1.00 39.40  ? 181 ARG A CA  1 
ATOM   1395 C C   . ARG A 1 181 ? 23.803 41.912 -2.473  1.00 36.35  ? 181 ARG A C   1 
ATOM   1396 O O   . ARG A 1 181 ? 24.194 41.413 -3.535  1.00 33.21  ? 181 ARG A O   1 
ATOM   1397 C CB  . ARG A 1 181 ? 22.670 44.157 -2.427  1.00 41.09  ? 181 ARG A CB  1 
ATOM   1398 C CG  . ARG A 1 181 ? 23.654 44.656 -3.454  1.00 45.19  ? 181 ARG A CG  1 
ATOM   1399 C CD  . ARG A 1 181 ? 23.536 46.163 -3.613  1.00 51.45  ? 181 ARG A CD  1 
ATOM   1400 N NE  . ARG A 1 181 ? 24.318 46.870 -2.603  1.00 43.41  ? 181 ARG A NE  1 
ATOM   1401 C CZ  . ARG A 1 181 ? 25.625 47.078 -2.676  1.00 50.67  ? 181 ARG A CZ  1 
ATOM   1402 N NH1 . ARG A 1 181 ? 26.341 46.628 -3.694  1.00 44.98  ? 181 ARG A NH1 1 
ATOM   1403 N NH2 . ARG A 1 181 ? 26.230 47.755 -1.703  1.00 58.44  ? 181 ARG A NH2 1 
ATOM   1404 N N   . HIS A 1 182 ? 24.520 41.841 -1.351  1.00 29.45  ? 182 HIS A N   1 
ATOM   1405 C CA  . HIS A 1 182 ? 25.788 41.117 -1.330  1.00 25.53  ? 182 HIS A CA  1 
ATOM   1406 C C   . HIS A 1 182 ? 25.574 39.622 -1.529  1.00 30.96  ? 182 HIS A C   1 
ATOM   1407 O O   . HIS A 1 182 ? 26.313 38.977 -2.284  1.00 30.63  ? 182 HIS A O   1 
ATOM   1408 C CB  . HIS A 1 182 ? 26.518 41.373 -0.013  1.00 29.10  ? 182 HIS A CB  1 
ATOM   1409 C CG  . HIS A 1 182 ? 27.123 42.739 0.088   1.00 37.20  ? 182 HIS A CG  1 
ATOM   1410 N ND1 . HIS A 1 182 ? 27.879 43.296 -0.917  1.00 36.35  ? 182 HIS A ND1 1 
ATOM   1411 C CD2 . HIS A 1 182 ? 27.076 43.659 1.081   1.00 30.84  ? 182 HIS A CD2 1 
ATOM   1412 C CE1 . HIS A 1 182 ? 28.274 44.504 -0.550  1.00 36.37  ? 182 HIS A CE1 1 
ATOM   1413 N NE2 . HIS A 1 182 ? 27.797 44.748 0.655   1.00 34.24  ? 182 HIS A NE2 1 
ATOM   1414 N N   . THR A 1 183 ? 24.579 39.049 -0.849  1.00 31.05  ? 183 THR A N   1 
ATOM   1415 C CA  . THR A 1 183 ? 24.316 37.622 -1.001  1.00 34.10  ? 183 THR A CA  1 
ATOM   1416 C C   . THR A 1 183 ? 23.903 37.282 -2.431  1.00 34.20  ? 183 THR A C   1 
ATOM   1417 O O   . THR A 1 183 ? 24.335 36.262 -2.982  1.00 34.46  ? 183 THR A O   1 
ATOM   1418 C CB  . THR A 1 183 ? 23.247 37.181 -0.001  1.00 36.49  ? 183 THR A CB  1 
ATOM   1419 O OG1 . THR A 1 183 ? 23.669 37.528 1.323   1.00 37.14  ? 183 THR A OG1 1 
ATOM   1420 C CG2 . THR A 1 183 ? 23.034 35.678 -0.068  1.00 45.26  ? 183 THR A CG2 1 
ATOM   1421 N N   . GLU A 1 184 ? 23.076 38.127 -3.054  1.00 34.51  ? 184 GLU A N   1 
ATOM   1422 C CA  . GLU A 1 184 ? 22.728 37.905 -4.456  1.00 34.86  ? 184 GLU A CA  1 
ATOM   1423 C C   . GLU A 1 184 ? 23.970 37.897 -5.338  1.00 38.02  ? 184 GLU A C   1 
ATOM   1424 O O   . GLU A 1 184 ? 24.110 37.042 -6.221  1.00 37.52  ? 184 GLU A O   1 
ATOM   1425 C CB  . GLU A 1 184 ? 21.751 38.973 -4.946  1.00 41.68  ? 184 GLU A CB  1 
ATOM   1426 C CG  . GLU A 1 184 ? 21.653 39.030 -6.468  1.00 52.41  ? 184 GLU A CG  1 
ATOM   1427 C CD  . GLU A 1 184 ? 20.400 39.721 -6.965  1.00 67.04  ? 184 GLU A CD  1 
ATOM   1428 O OE1 . GLU A 1 184 ? 19.610 40.209 -6.129  1.00 80.74  ? 184 GLU A OE1 1 
ATOM   1429 O OE2 . GLU A 1 184 ? 20.209 39.774 -8.199  1.00 70.84  ? 184 GLU A OE2 1 
ATOM   1430 N N   . ALA A 1 185 ? 24.884 38.843 -5.109  1.00 36.75  ? 185 ALA A N   1 
ATOM   1431 C CA  . ALA A 1 185 ? 26.088 38.929 -5.926  1.00 42.56  ? 185 ALA A CA  1 
ATOM   1432 C C   . ALA A 1 185 ? 26.921 37.659 -5.824  1.00 42.25  ? 185 ALA A C   1 
ATOM   1433 O O   . ALA A 1 185 ? 27.435 37.164 -6.834  1.00 36.99  ? 185 ALA A O   1 
ATOM   1434 C CB  . ALA A 1 185 ? 26.916 40.147 -5.513  1.00 34.85  ? 185 ALA A CB  1 
ATOM   1435 N N   . ILE A 1 186 ? 27.061 37.114 -4.615  1.00 33.33  ? 186 ILE A N   1 
ATOM   1436 C CA  . ILE A 1 186 ? 27.874 35.915 -4.437  1.00 29.05  ? 186 ILE A CA  1 
ATOM   1437 C C   . ILE A 1 186 ? 27.200 34.710 -5.078  1.00 32.80  ? 186 ILE A C   1 
ATOM   1438 O O   . ILE A 1 186 ? 27.852 33.913 -5.763  1.00 33.54  ? 186 ILE A O   1 
ATOM   1439 C CB  . ILE A 1 186 ? 28.163 35.682 -2.942  1.00 33.62  ? 186 ILE A CB  1 
ATOM   1440 C CG1 . ILE A 1 186 ? 29.106 36.763 -2.414  1.00 37.18  ? 186 ILE A CG1 1 
ATOM   1441 C CG2 . ILE A 1 186 ? 28.780 34.310 -2.720  1.00 30.62  ? 186 ILE A CG2 1 
ATOM   1442 C CD1 . ILE A 1 186 ? 30.492 36.718 -3.037  1.00 38.96  ? 186 ILE A CD1 1 
ATOM   1443 N N   . ILE A 1 187 ? 25.888 34.554 -4.869  1.00 31.36  ? 187 ILE A N   1 
ATOM   1444 C CA  . ILE A 1 187 ? 25.153 33.461 -5.507  1.00 31.71  ? 187 ILE A CA  1 
ATOM   1445 C C   . ILE A 1 187 ? 25.335 33.513 -7.019  1.00 35.52  ? 187 ILE A C   1 
ATOM   1446 O O   . ILE A 1 187 ? 25.620 32.498 -7.665  1.00 36.52  ? 187 ILE A O   1 
ATOM   1447 C CB  . ILE A 1 187 ? 23.664 33.509 -5.118  1.00 30.53  ? 187 ILE A CB  1 
ATOM   1448 C CG1 . ILE A 1 187 ? 23.480 33.179 -3.638  1.00 29.18  ? 187 ILE A CG1 1 
ATOM   1449 C CG2 . ILE A 1 187 ? 22.863 32.512 -5.944  1.00 35.94  ? 187 ILE A CG2 1 
ATOM   1450 C CD1 . ILE A 1 187 ? 22.067 33.430 -3.138  1.00 39.85  ? 187 ILE A CD1 1 
ATOM   1451 N N   . ARG A 1 188 ? 25.190 34.707 -7.600  1.00 35.26  ? 188 ARG A N   1 
ATOM   1452 C CA  . ARG A 1 188 ? 25.350 34.864 -9.044  1.00 43.15  ? 188 ARG A CA  1 
ATOM   1453 C C   . ARG A 1 188 ? 26.747 34.469 -9.504  1.00 38.65  ? 188 ARG A C   1 
ATOM   1454 O O   . ARG A 1 188 ? 26.900 33.801 -10.532 1.00 42.96  ? 188 ARG A O   1 
ATOM   1455 C CB  . ARG A 1 188 ? 25.048 36.305 -9.451  1.00 39.96  ? 188 ARG A CB  1 
ATOM   1456 C CG  . ARG A 1 188 ? 23.577 36.654 -9.428  1.00 47.57  ? 188 ARG A CG  1 
ATOM   1457 C CD  . ARG A 1 188 ? 23.321 38.008 -10.071 1.00 59.99  ? 188 ARG A CD  1 
ATOM   1458 N NE  . ARG A 1 188 ? 21.899 38.322 -10.084 1.00 61.33  ? 188 ARG A NE  1 
ATOM   1459 C CZ  . ARG A 1 188 ? 21.066 37.946 -11.045 1.00 62.91  ? 188 ARG A CZ  1 
ATOM   1460 N NH1 . ARG A 1 188 ? 21.490 37.267 -12.098 1.00 53.38  ? 188 ARG A NH1 1 
ATOM   1461 N NH2 . ARG A 1 188 ? 19.777 38.258 -10.947 1.00 60.72  ? 188 ARG A NH2 1 
ATOM   1462 N N   . LEU A 1 189 ? 27.782 34.876 -8.766  1.00 34.66  ? 189 LEU A N   1 
ATOM   1463 C CA  . LEU A 1 189 ? 29.143 34.566 -9.194  1.00 35.92  ? 189 LEU A CA  1 
ATOM   1464 C C   . LEU A 1 189 ? 29.414 33.070 -9.127  1.00 39.06  ? 189 LEU A C   1 
ATOM   1465 O O   . LEU A 1 189 ? 30.121 32.521 -9.980  1.00 35.71  ? 189 LEU A O   1 
ATOM   1466 C CB  . LEU A 1 189 ? 30.159 35.327 -8.340  1.00 40.94  ? 189 LEU A CB  1 
ATOM   1467 C CG  . LEU A 1 189 ? 30.132 36.852 -8.448  1.00 42.74  ? 189 LEU A CG  1 
ATOM   1468 C CD1 . LEU A 1 189 ? 31.068 37.467 -7.417  1.00 46.47  ? 189 LEU A CD1 1 
ATOM   1469 C CD2 . LEU A 1 189 ? 30.484 37.309 -9.859  1.00 50.68  ? 189 LEU A CD2 1 
ATOM   1470 N N   . GLU A 1 190 ? 28.860 32.393 -8.122  1.00 30.47  ? 190 GLU A N   1 
ATOM   1471 C CA  . GLU A 1 190 ? 29.157 30.979 -7.937  1.00 32.79  ? 190 GLU A CA  1 
ATOM   1472 C C   . GLU A 1 190 ? 28.359 30.096 -8.889  1.00 36.66  ? 190 GLU A C   1 
ATOM   1473 O O   . GLU A 1 190 ? 28.864 29.058 -9.330  1.00 41.08  ? 190 GLU A O   1 
ATOM   1474 C CB  . GLU A 1 190 ? 28.869 30.567 -6.490  1.00 33.59  ? 190 GLU A CB  1 
ATOM   1475 C CG  . GLU A 1 190 ? 29.883 31.089 -5.478  1.00 28.59  ? 190 GLU A CG  1 
ATOM   1476 C CD  . GLU A 1 190 ? 30.998 30.100 -5.182  1.00 46.28  ? 190 GLU A CD  1 
ATOM   1477 O OE1 . GLU A 1 190 ? 31.300 29.251 -6.049  1.00 45.05  ? 190 GLU A OE1 1 
ATOM   1478 O OE2 . GLU A 1 190 ? 31.575 30.174 -4.077  1.00 43.94  ? 190 GLU A OE2 1 
ATOM   1479 N N   . LEU A 1 191 ? 27.135 30.484 -9.172  1.00 32.74  ? 191 LEU A N   1 
ATOM   1480 C CA  . LEU A 1 191 ? 26.240 29.612 -9.915  1.00 36.66  ? 191 LEU A CA  1 
ATOM   1481 C C   . LEU A 1 191 ? 25.522 30.127 -11.140 1.00 44.12  ? 191 LEU A C   1 
ATOM   1482 O O   . LEU A 1 191 ? 25.017 29.343 -11.895 1.00 42.16  ? 191 LEU A O   1 
ATOM   1483 C CB  . LEU A 1 191 ? 25.154 29.174 -8.944  1.00 37.52  ? 191 LEU A CB  1 
ATOM   1484 C CG  . LEU A 1 191 ? 25.542 28.360 -7.730  1.00 31.74  ? 191 LEU A CG  1 
ATOM   1485 C CD1 . LEU A 1 191 ? 24.537 28.603 -6.641  1.00 34.03  ? 191 LEU A CD1 1 
ATOM   1486 C CD2 . LEU A 1 191 ? 25.583 26.903 -8.094  1.00 29.84  ? 191 LEU A CD2 1 
ATOM   1487 N N   . LEU A 1 192 ? 25.446 31.442 -11.244 1.00 43.17  ? 192 LEU A N   1 
ATOM   1488 C CA  . LEU A 1 192 ? 24.739 32.218 -12.266 1.00 54.63  ? 192 LEU A CA  1 
ATOM   1489 C C   . LEU A 1 192 ? 23.233 32.186 -12.206 1.00 64.50  ? 192 LEU A C   1 
ATOM   1490 O O   . LEU A 1 192 ? 22.559 31.294 -12.681 1.00 88.53  ? 192 LEU A O   1 
ATOM   1491 C CB  . LEU A 1 192 ? 25.297 32.013 -13.641 1.00 76.54  ? 192 LEU A CB  1 
ATOM   1492 C CG  . LEU A 1 192 ? 26.609 32.762 -13.682 1.00 90.63  ? 192 LEU A CG  1 
ATOM   1493 C CD1 . LEU A 1 192 ? 27.796 31.836 -13.717 1.00 64.84  ? 192 LEU A CD1 1 
ATOM   1494 C CD2 . LEU A 1 192 ? 26.603 33.737 -14.842 1.00 66.77  ? 192 LEU A CD2 1 
ATOM   1495 O OXT . LEU A 1 192 ? 22.624 33.066 -11.647 1.00 75.89  ? 192 LEU A OXT 1 
HETATM 1496 O O   . HOH B 2 .   ? 8.266  37.765 13.485  1.00 72.22  ? 201 HOH A O   1 
HETATM 1497 O O   . HOH B 2 .   ? 26.373 44.961 4.035   1.00 36.12  ? 202 HOH A O   1 
HETATM 1498 O O   . HOH B 2 .   ? 18.220 32.811 27.756  1.00 60.20  ? 203 HOH A O   1 
HETATM 1499 O O   . HOH B 2 .   ? 5.353  7.991  23.872  1.00 50.30  ? 204 HOH A O   1 
HETATM 1500 O O   . HOH B 2 .   ? 15.155 16.294 15.735  1.00 56.55  ? 205 HOH A O   1 
HETATM 1501 O O   . HOH B 2 .   ? 4.837  20.237 38.127  1.00 55.38  ? 206 HOH A O   1 
HETATM 1502 O O   . HOH B 2 .   ? 21.077 23.873 31.300  1.00 37.99  ? 207 HOH A O   1 
HETATM 1503 O O   . HOH B 2 .   ? 4.216  11.180 32.224  1.00 59.59  ? 208 HOH A O   1 
HETATM 1504 O O   . HOH B 2 .   ? 13.596 14.454 19.814  1.00 56.12  ? 209 HOH A O   1 
HETATM 1505 O O   . HOH B 2 .   ? 22.396 16.001 23.390  1.00 47.19  ? 210 HOH A O   1 
HETATM 1506 O O   . HOH B 2 .   ? 30.910 33.643 -12.072 1.00 44.84  ? 211 HOH A O   1 
HETATM 1507 O O   . HOH B 2 .   ? 31.484 28.428 -8.421  1.00 42.09  ? 212 HOH A O   1 
HETATM 1508 O O   . HOH B 2 .   ? 26.755 18.450 5.816   1.00 56.24  ? 213 HOH A O   1 
HETATM 1509 O O   . HOH B 2 .   ? 32.011 23.913 18.568  1.00 39.33  ? 214 HOH A O   1 
HETATM 1510 O O   . HOH B 2 .   ? 11.269 13.561 19.165  1.00 61.44  ? 215 HOH A O   1 
HETATM 1511 O O   . HOH B 2 .   ? 14.891 18.282 39.707  1.00 55.49  ? 216 HOH A O   1 
HETATM 1512 O O   . HOH B 2 .   ? 32.460 51.089 3.653   1.00 52.31  ? 217 HOH A O   1 
HETATM 1513 O O   . HOH B 2 .   ? 32.392 51.584 14.559  1.00 43.71  ? 218 HOH A O   1 
HETATM 1514 O O   . HOH B 2 .   ? 25.766 46.468 12.059  1.00 40.46  ? 219 HOH A O   1 
HETATM 1515 O O   . HOH B 2 .   ? 15.722 32.475 28.658  1.00 54.71  ? 220 HOH A O   1 
HETATM 1516 O O   . HOH B 2 .   ? 18.269 13.934 24.456  1.00 50.91  ? 221 HOH A O   1 
HETATM 1517 O O   . HOH B 2 .   ? 20.998 38.605 8.263   1.00 55.95  ? 222 HOH A O   1 
HETATM 1518 O O   . HOH B 2 .   ? 6.437  35.826 8.081   1.00 63.15  ? 223 HOH A O   1 
HETATM 1519 O O   . HOH B 2 .   ? 20.016 17.700 -16.220 1.00 41.00  ? 224 HOH A O   1 
HETATM 1520 O O   . HOH B 2 .   ? 17.083 22.262 -0.113  1.00 37.87  ? 225 HOH A O   1 
HETATM 1521 O O   . HOH B 2 .   ? 31.316 39.572 15.306  1.00 34.86  ? 226 HOH A O   1 
HETATM 1522 O O   . HOH B 2 .   ? 12.581 10.668 37.747  1.00 44.55  ? 227 HOH A O   1 
HETATM 1523 O O   . HOH B 2 .   ? 27.930 46.964 2.130   1.00 40.99  ? 228 HOH A O   1 
HETATM 1524 O O   . HOH B 2 .   ? 30.157 17.573 6.059   1.00 53.65  ? 229 HOH A O   1 
HETATM 1525 O O   . HOH B 2 .   ? 29.413 46.466 11.386  1.00 34.05  ? 230 HOH A O   1 
HETATM 1526 O O   . HOH B 2 .   ? 18.611 18.029 -5.234  1.00 43.64  ? 231 HOH A O   1 
HETATM 1527 O O   . HOH B 2 .   ? 29.235 23.725 17.764  1.00 32.97  ? 232 HOH A O   1 
HETATM 1528 O O   . HOH B 2 .   ? 17.787 29.275 6.912   1.00 42.16  ? 233 HOH A O   1 
HETATM 1529 O O   . HOH B 2 .   ? 10.700 11.500 21.957  1.00 45.05  ? 234 HOH A O   1 
HETATM 1530 O O   . HOH B 2 .   ? 27.448 17.166 16.486  1.00 41.38  ? 235 HOH A O   1 
HETATM 1531 O O   . HOH B 2 .   ? 17.191 31.456 -11.952 1.00 59.37  ? 236 HOH A O   1 
HETATM 1532 O O   . HOH B 2 .   ? 33.235 20.102 17.647  1.00 32.85  ? 237 HOH A O   1 
HETATM 1533 O O   . HOH B 2 .   ? 23.690 42.270 -6.062  1.00 47.16  ? 238 HOH A O   1 
HETATM 1534 O O   . HOH B 2 .   ? 17.803 13.996 34.058  1.00 48.54  ? 239 HOH A O   1 
HETATM 1535 O O   . HOH B 2 .   ? 23.234 17.363 21.509  1.00 37.99  ? 240 HOH A O   1 
HETATM 1536 O O   . HOH B 2 .   ? -1.094 11.878 25.669  1.00 42.99  ? 241 HOH A O   1 
HETATM 1537 O O   . HOH B 2 .   ? 28.771 26.571 -10.519 1.00 44.22  ? 242 HOH A O   1 
HETATM 1538 O O   . HOH B 2 .   ? 27.192 51.344 9.849   1.00 47.39  ? 243 HOH A O   1 
HETATM 1539 O O   . HOH B 2 .   ? 30.735 30.790 19.133  1.00 51.71  ? 244 HOH A O   1 
HETATM 1540 O O   . HOH B 2 .   ? 11.616 30.056 33.435  1.00 51.18  ? 245 HOH A O   1 
HETATM 1541 O O   . HOH B 2 .   ? 19.100 18.924 5.522   1.00 44.31  ? 246 HOH A O   1 
HETATM 1542 O O   . HOH B 2 .   ? 3.555  13.446 31.791  1.00 53.96  ? 247 HOH A O   1 
HETATM 1543 O O   . HOH B 2 .   ? 20.366 44.546 -0.237  1.00 37.52  ? 248 HOH A O   1 
HETATM 1544 O O   . HOH B 2 .   ? 13.222 24.840 -8.964  1.00 49.08  ? 249 HOH A O   1 
HETATM 1545 O O   . HOH B 2 .   ? 17.983 12.391 26.922  1.00 45.79  ? 250 HOH A O   1 
HETATM 1546 O O   . HOH B 2 .   ? 27.330 47.128 9.992   1.00 36.40  ? 251 HOH A O   1 
HETATM 1547 O O   . HOH B 2 .   ? 3.588  14.629 29.268  1.00 50.77  ? 252 HOH A O   1 
HETATM 1548 O O   . HOH B 2 .   ? 30.270 18.114 16.617  1.00 44.32  ? 253 HOH A O   1 
HETATM 1549 O O   . HOH B 2 .   ? 15.340 16.630 18.463  1.00 39.49  ? 254 HOH A O   1 
HETATM 1550 O O   . HOH B 2 .   ? 32.627 28.005 29.430  1.00 62.31  ? 255 HOH A O   1 
HETATM 1551 O O   . HOH B 2 .   ? 19.981 15.768 23.838  1.00 39.07  ? 256 HOH A O   1 
HETATM 1552 O O   . HOH B 2 .   ? 12.090 8.303  27.739  1.00 46.16  ? 257 HOH A O   1 
HETATM 1553 O O   . HOH B 2 .   ? 19.256 43.098 2.901   1.00 44.89  ? 258 HOH A O   1 
HETATM 1554 O O   . HOH B 2 .   ? 32.640 37.399 10.611  1.00 31.80  ? 259 HOH A O   1 
HETATM 1555 O O   . HOH B 2 .   ? 27.240 50.302 3.367   1.00 46.17  ? 260 HOH A O   1 
HETATM 1556 O O   . HOH B 2 .   ? 15.331 33.819 4.686   1.00 44.24  ? 261 HOH A O   1 
HETATM 1557 O O   . HOH B 2 .   ? 22.984 16.707 10.528  1.00 38.61  ? 262 HOH A O   1 
HETATM 1558 O O   . HOH B 2 .   ? 21.061 27.472 28.810  1.00 43.47  ? 263 HOH A O   1 
HETATM 1559 O O   . HOH B 2 .   ? 21.464 30.478 28.386  1.00 46.06  ? 264 HOH A O   1 
HETATM 1560 O O   . HOH B 2 .   ? 22.258 20.049 32.230  1.00 37.06  ? 265 HOH A O   1 
HETATM 1561 O O   . HOH B 2 .   ? 29.878 17.818 12.492  1.00 34.55  ? 266 HOH A O   1 
HETATM 1562 O O   . HOH B 2 .   ? 0.957  5.658  32.879  1.00 45.48  ? 267 HOH A O   1 
HETATM 1563 O O   . HOH B 2 .   ? 33.412 31.431 -13.458 1.00 62.66  ? 268 HOH A O   1 
HETATM 1564 O O   . HOH B 2 .   ? 24.011 36.529 -13.593 1.00 56.40  ? 269 HOH A O   1 
HETATM 1565 O O   . HOH B 2 .   ? 5.652  8.414  29.898  1.00 53.73  ? 270 HOH A O   1 
HETATM 1566 O O   . HOH B 2 .   ? 13.557 27.120 37.946  1.00 52.43  ? 271 HOH A O   1 
HETATM 1567 O O   . HOH B 2 .   ? 27.629 39.256 -9.117  1.00 45.73  ? 272 HOH A O   1 
HETATM 1568 O O   . HOH B 2 .   ? 27.369 11.625 23.847  1.00 60.47  ? 273 HOH A O   1 
HETATM 1569 O O   . HOH B 2 .   ? 34.690 18.661 -2.212  1.00 60.19  ? 274 HOH A O   1 
HETATM 1570 O O   . HOH B 2 .   ? 1.851  16.318 28.845  1.00 41.10  ? 275 HOH A O   1 
HETATM 1571 O O   . HOH B 2 .   ? 16.433 30.281 35.209  1.00 52.07  ? 276 HOH A O   1 
HETATM 1572 O O   . HOH B 2 .   ? 6.912  18.281 40.295  1.00 36.32  ? 277 HOH A O   1 
HETATM 1573 O O   . HOH B 2 .   ? 23.423 49.240 9.673   1.00 24.90  ? 278 HOH A O   1 
HETATM 1574 O O   . HOH B 2 .   ? 3.468  7.838  26.944  1.00 49.86  ? 279 HOH A O   1 
HETATM 1575 O O   . HOH B 2 .   ? 16.747 9.985  26.931  1.00 58.40  ? 280 HOH A O   1 
HETATM 1576 O O   . HOH B 2 .   ? 6.225  8.687  26.302  1.00 47.16  ? 281 HOH A O   1 
HETATM 1577 O O   . HOH B 2 .   ? 20.969 43.280 -6.321  1.00 54.28  ? 282 HOH A O   1 
HETATM 1578 O O   . HOH B 2 .   ? -6.043 19.812 32.872  1.00 54.38  ? 283 HOH A O   1 
HETATM 1579 O O   . HOH B 2 .   ? 19.764 16.631 6.870   1.00 58.30  ? 284 HOH A O   1 
HETATM 1580 O O   . HOH B 2 .   ? 19.131 16.837 -7.671  1.00 53.24  ? 285 HOH A O   1 
HETATM 1581 O O   . HOH B 2 .   ? 24.916 16.095 6.403   1.00 54.43  ? 286 HOH A O   1 
HETATM 1582 O O   . HOH B 2 .   ? 35.098 29.230 28.286  1.00 65.49  ? 287 HOH A O   1 
HETATM 1583 O O   . HOH B 2 .   ? 27.646 16.551 13.885  1.00 54.67  ? 288 HOH A O   1 
HETATM 1584 O O   . HOH B 2 .   ? 5.817  8.223  20.987  1.00 66.68  ? 289 HOH A O   1 
HETATM 1585 O O   . HOH B 2 .   ? 18.163 18.151 3.075   1.00 51.73  ? 290 HOH A O   1 
HETATM 1586 O O   . HOH B 2 .   ? 32.211 21.031 24.495  1.00 59.64  ? 291 HOH A O   1 
HETATM 1587 O O   . HOH B 2 .   ? 5.332  34.155 6.893   1.00 67.09  ? 292 HOH A O   1 
HETATM 1588 O O   . HOH B 2 .   ? 25.458 40.832 -8.970  1.00 48.30  ? 293 HOH A O   1 
HETATM 1589 O O   . HOH B 2 .   ? 7.700  9.585  19.566  1.00 56.28  ? 294 HOH A O   1 
HETATM 1590 O O   . HOH B 2 .   ? 25.299 15.013 10.606  1.00 57.88  ? 295 HOH A O   1 
HETATM 1591 O O   . HOH B 2 .   ? 7.273  6.378  19.978  1.00 59.88  ? 296 HOH A 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   . GLN A 8   ? 0.6645 0.8223 0.7196 -0.1043 -0.0147 0.0754  8   GLN A N   
2    C CA  . GLN A 8   ? 0.6153 0.7780 0.6779 -0.0974 -0.0142 0.0782  8   GLN A CA  
3    C C   . GLN A 8   ? 0.4039 0.5639 0.4735 -0.0859 -0.0061 0.0776  8   GLN A C   
4    O O   . GLN A 8   ? 0.5442 0.7066 0.6208 -0.0787 -0.0030 0.0798  8   GLN A O   
5    C CB  . GLN A 8   ? 0.8154 0.9998 0.8903 -0.1018 -0.0186 0.0898  8   GLN A CB  
6    C CG  . GLN A 8   ? 0.7538 0.9549 0.8484 -0.0947 -0.0132 0.0997  8   GLN A CG  
7    C CD  . GLN A 8   ? 1.0125 1.2280 1.1131 -0.1024 -0.0157 0.1071  8   GLN A CD  
8    O OE1 . GLN A 8   ? 0.9616 1.1680 1.0520 -0.1068 -0.0156 0.1009  8   GLN A OE1 
9    N NE2 . GLN A 8   ? 0.8142 1.0537 0.9328 -0.1041 -0.0180 0.1216  8   GLN A NE2 
10   N N   . ARG A 9   ? 0.4594 0.6131 0.5255 -0.0852 -0.0021 0.0743  9   ARG A N   
11   C CA  . ARG A 9   ? 0.4290 0.5764 0.4966 -0.0772 0.0065  0.0724  9   ARG A CA  
12   C C   . ARG A 9   ? 0.4096 0.5418 0.4673 -0.0734 0.0072  0.0653  9   ARG A C   
13   O O   . ARG A 9   ? 0.3767 0.5048 0.4358 -0.0671 0.0139  0.0648  9   ARG A O   
14   C CB  . ARG A 9   ? 0.4719 0.6154 0.5354 -0.0796 0.0097  0.0704  9   ARG A CB  
15   C CG  . ARG A 9   ? 0.5144 0.6739 0.5910 -0.0807 0.0120  0.0787  9   ARG A CG  
16   C CD  . ARG A 9   ? 0.6141 0.7696 0.6862 -0.0833 0.0155  0.0766  9   ARG A CD  
17   N NE  . ARG A 9   ? 0.6796 0.8309 0.7422 -0.0914 0.0083  0.0731  9   ARG A NE  
18   C CZ  . ARG A 9   ? 0.6687 0.8186 0.7279 -0.0954 0.0091  0.0723  9   ARG A CZ  
19   N NH1 . ARG A 9   ? 0.4372 0.5901 0.5012 -0.0927 0.0164  0.0746  9   ARG A NH1 
20   N NH2 . ARG A 9   ? 0.6136 0.7579 0.6643 -0.1022 0.0038  0.0694  9   ARG A NH2 
21   N N   . ARG A 10  ? 0.3873 0.5104 0.4350 -0.0775 0.0015  0.0605  10  ARG A N   
22   C CA  . ARG A 10  ? 0.4222 0.5338 0.4631 -0.0742 0.0012  0.0558  10  ARG A CA  
23   C C   . ARG A 10  ? 0.3803 0.4971 0.4272 -0.0701 0.0008  0.0581  10  ARG A C   
24   O O   . ARG A 10  ? 0.3963 0.5069 0.4415 -0.0647 0.0040  0.0559  10  ARG A O   
25   C CB  . ARG A 10  ? 0.4374 0.5392 0.4699 -0.0788 -0.0033 0.0522  10  ARG A CB  
26   C CG  . ARG A 10  ? 0.4387 0.5297 0.4658 -0.0754 -0.0035 0.0488  10  ARG A CG  
27   C CD  . ARG A 10  ? 0.5445 0.6258 0.5665 -0.0788 -0.0058 0.0472  10  ARG A CD  
28   N NE  . ARG A 10  ? 0.4917 0.5644 0.5108 -0.0756 -0.0056 0.0461  10  ARG A NE  
29   C CZ  . ARG A 10  ? 0.4312 0.5001 0.4498 -0.0727 -0.0064 0.0447  10  ARG A CZ  
30   N NH1 . ARG A 10  ? 0.4603 0.5328 0.4803 -0.0726 -0.0075 0.0440  10  ARG A NH1 
31   N NH2 . ARG A 10  ? 0.4974 0.5598 0.5142 -0.0705 -0.0065 0.0450  10  ARG A NH2 
32   N N   . GLU A 11  ? 0.3661 0.4946 0.4192 -0.0738 -0.0036 0.0630  11  GLU A N   
33   C CA  . GLU A 11  ? 0.4054 0.5412 0.4654 -0.0708 -0.0048 0.0670  11  GLU A CA  
34   C C   . GLU A 11  ? 0.3138 0.4570 0.3865 -0.0624 0.0029  0.0725  11  GLU A C   
35   O O   . GLU A 11  ? 0.3577 0.4995 0.4336 -0.0566 0.0054  0.0731  11  GLU A O   
36   C CB  . GLU A 11  ? 0.5192 0.6678 0.5822 -0.0793 -0.0118 0.0729  11  GLU A CB  
37   C CG  . GLU A 11  ? 0.5710 0.7304 0.6421 -0.0779 -0.0143 0.0793  11  GLU A CG  
38   C CD  . GLU A 11  ? 0.5192 0.6655 0.5797 -0.0775 -0.0165 0.0726  11  GLU A CD  
39   O OE1 . GLU A 11  ? 0.6148 0.7460 0.6617 -0.0816 -0.0177 0.0647  11  GLU A OE1 
40   O OE2 . GLU A 11  ? 0.7656 0.9168 0.8326 -0.0728 -0.0163 0.0761  11  GLU A OE2 
41   N N   . MET A 12  ? 0.3852 0.5349 0.4651 -0.0616 0.0079  0.0765  12  MET A N   
42   C CA  . MET A 12  ? 0.3526 0.5064 0.4448 -0.0532 0.0185  0.0820  12  MET A CA  
43   C C   . MET A 12  ? 0.3556 0.4903 0.4368 -0.0482 0.0269  0.0739  12  MET A C   
44   O O   . MET A 12  ? 0.3627 0.4951 0.4499 -0.0411 0.0357  0.0763  12  MET A O   
45   C CB  . MET A 12  ? 0.4086 0.5732 0.5115 -0.0537 0.0232  0.0888  12  MET A CB  
46   C CG  . MET A 12  ? 0.6450 0.8318 0.7609 -0.0596 0.0153  0.0996  12  MET A CG  
47   S SD  . MET A 12  ? 1.0013 1.2060 1.1309 -0.0597 0.0089  0.1107  12  MET A SD  
48   C CE  . MET A 12  ? 0.6115 0.8139 0.7555 -0.0452 0.0231  0.1155  12  MET A CE  
49   N N   . ILE A 13  ? 0.2977 0.4187 0.3626 -0.0526 0.0245  0.0652  13  ILE A N   
50   C CA  . ILE A 13  ? 0.3096 0.4134 0.3615 -0.0509 0.0301  0.0583  13  ILE A CA  
51   C C   . ILE A 13  ? 0.3650 0.4649 0.4151 -0.0478 0.0273  0.0564  13  ILE A C   
52   O O   . ILE A 13  ? 0.3822 0.4739 0.4300 -0.0433 0.0351  0.0550  13  ILE A O   
53   C CB  . ILE A 13  ? 0.2744 0.3683 0.3115 -0.0576 0.0261  0.0523  13  ILE A CB  
54   C CG1 . ILE A 13  ? 0.3668 0.4611 0.4030 -0.0604 0.0315  0.0532  13  ILE A CG1 
55   C CG2 . ILE A 13  ? 0.3829 0.4617 0.4057 -0.0585 0.0280  0.0466  13  ILE A CG2 
56   C CD1 . ILE A 13  ? 0.3888 0.4794 0.4154 -0.0675 0.0250  0.0504  13  ILE A CD1 
57   N N   . LEU A 14  ? 0.3143 0.4184 0.3642 -0.0507 0.0171  0.0561  14  LEU A N   
58   C CA  . LEU A 14  ? 0.3440 0.4452 0.3927 -0.0481 0.0141  0.0547  14  LEU A CA  
59   C C   . LEU A 14  ? 0.3570 0.4663 0.4185 -0.0415 0.0193  0.0608  14  LEU A C   
60   O O   . LEU A 14  ? 0.3459 0.4478 0.4050 -0.0370 0.0232  0.0588  14  LEU A O   
61   C CB  . LEU A 14  ? 0.4306 0.5349 0.4776 -0.0532 0.0043  0.0543  14  LEU A CB  
62   C CG  . LEU A 14  ? 0.4686 0.5651 0.5096 -0.0525 0.0005  0.0505  14  LEU A CG  
63   C CD1 . LEU A 14  ? 0.3449 0.4277 0.3760 -0.0512 0.0026  0.0452  14  LEU A CD1 
64   C CD2 . LEU A 14  ? 0.6103 0.7063 0.6473 -0.0589 -0.0063 0.0496  14  LEU A CD2 
65   N N   . GLN A 15  ? 0.3181 0.4437 0.3944 -0.0411 0.0197  0.0697  15  GLN A N   
66   C CA  . GLN A 15  ? 0.3491 0.4855 0.4417 -0.0344 0.0249  0.0787  15  GLN A CA  
67   C C   . GLN A 15  ? 0.4250 0.5506 0.5189 -0.0267 0.0399  0.0780  15  GLN A C   
68   O O   . GLN A 15  ? 0.4351 0.5598 0.5360 -0.0201 0.0460  0.0814  15  GLN A O   
69   C CB  . GLN A 15  ? 0.4788 0.6373 0.5889 -0.0366 0.0220  0.0909  15  GLN A CB  
70   C CG  . GLN A 15  ? 0.5121 0.6815 0.6206 -0.0454 0.0084  0.0933  15  GLN A CG  
71   C CD  . GLN A 15  ? 0.4950 0.6679 0.6065 -0.0438 0.0046  0.0962  15  GLN A CD  
72   O OE1 . GLN A 15  ? 0.4988 0.6744 0.6219 -0.0352 0.0120  0.1017  15  GLN A OE1 
73   N NE2 . GLN A 15  ? 0.5374 0.7086 0.6377 -0.0522 -0.0056 0.0925  15  GLN A NE2 
74   N N   . ALA A 16  ? 0.4418 0.5573 0.5275 -0.0282 0.0469  0.0735  16  ALA A N   
75   C CA  . ALA A 16  ? 0.3508 0.4510 0.4321 -0.0234 0.0629  0.0710  16  ALA A CA  
76   C C   . ALA A 16  ? 0.3981 0.4799 0.4618 -0.0241 0.0637  0.0617  16  ALA A C   
77   O O   . ALA A 16  ? 0.3853 0.4574 0.4491 -0.0187 0.0753  0.0618  16  ALA A O   
78   C CB  . ALA A 16  ? 0.3915 0.4840 0.4645 -0.0274 0.0694  0.0676  16  ALA A CB  
79   N N   . ALA A 17  ? 0.3509 0.4277 0.4000 -0.0309 0.0522  0.0546  17  ALA A N   
80   C CA  . ALA A 17  ? 0.3608 0.4233 0.3950 -0.0323 0.0510  0.0476  17  ALA A CA  
81   C C   . ALA A 17  ? 0.3863 0.4534 0.4297 -0.0261 0.0498  0.0507  17  ALA A C   
82   O O   . ALA A 17  ? 0.4507 0.5055 0.4866 -0.0240 0.0560  0.0473  17  ALA A O   
83   C CB  . ALA A 17  ? 0.3958 0.4560 0.4183 -0.0398 0.0387  0.0427  17  ALA A CB  
84   N N   . MET A 18  ? 0.3423 0.4268 0.4006 -0.0245 0.0416  0.0573  18  MET A N   
85   C CA  . MET A 18  ? 0.4088 0.4994 0.4760 -0.0198 0.0394  0.0614  18  MET A CA  
86   C C   . MET A 18  ? 0.3897 0.4804 0.4692 -0.0112 0.0533  0.0678  18  MET A C   
87   O O   . MET A 18  ? 0.4169 0.5031 0.4973 -0.0067 0.0562  0.0679  18  MET A O   
88   C CB  . MET A 18  ? 0.3203 0.4296 0.3984 -0.0228 0.0278  0.0679  18  MET A CB  
89   C CG  . MET A 18  ? 0.4055 0.5116 0.4713 -0.0310 0.0168  0.0617  18  MET A CG  
90   S SD  . MET A 18  ? 0.4359 0.5594 0.5087 -0.0383 0.0055  0.0679  18  MET A SD  
91   C CE  . MET A 18  ? 0.4098 0.5444 0.4935 -0.0353 0.0030  0.0756  18  MET A CE  
92   N N   . GLN A 19  ? 0.4346 0.5300 0.5248 -0.0084 0.0631  0.0739  19  GLN A N   
93   C CA  . GLN A 19  ? 0.3914 0.4852 0.4955 0.0008  0.0796  0.0814  19  GLN A CA  
94   C C   . GLN A 19  ? 0.5629 0.6301 0.6487 0.0018  0.0930  0.0717  19  GLN A C   
95   O O   . GLN A 19  ? 0.5058 0.5668 0.5963 0.0084  0.1025  0.0741  19  GLN A O   
96   C CB  . GLN A 19  ? 0.3937 0.4977 0.5138 0.0035  0.0884  0.0905  19  GLN A CB  
97   C CG  . GLN A 19  ? 0.6569 0.7670 0.8009 0.0145  0.1044  0.1037  19  GLN A CG  
98   C CD  . GLN A 19  ? 0.8608 0.9608 1.0082 0.0182  0.1239  0.1057  19  GLN A CD  
99   O OE1 . GLN A 19  ? 0.9517 1.0252 1.0800 0.0175  0.1379  0.0955  19  GLN A OE1 
100  N NE2 . GLN A 19  ? 0.7746 0.8954 0.9455 0.0209  0.1252  0.1193  19  GLN A NE2 
101  N N   . ILE A 20  ? 0.5276 0.5788 0.5915 -0.0058 0.0941  0.0614  20  ILE A N   
102  C CA  . ILE A 20  ? 0.5150 0.5401 0.5566 -0.0088 0.1054  0.0519  20  ILE A CA  
103  C C   . ILE A 20  ? 0.4947 0.5148 0.5271 -0.0098 0.0971  0.0470  20  ILE A C   
104  O O   . ILE A 20  ? 0.5180 0.5224 0.5427 -0.0076 0.1082  0.0441  20  ILE A O   
105  C CB  . ILE A 20  ? 0.4571 0.4696 0.4766 -0.0194 0.1048  0.0434  20  ILE A CB  
106  C CG1 . ILE A 20  ? 0.5033 0.5167 0.5302 -0.0180 0.1167  0.0475  20  ILE A CG1 
107  C CG2 . ILE A 20  ? 0.5830 0.5696 0.5755 -0.0265 0.1130  0.0337  20  ILE A CG2 
108  C CD1 . ILE A 20  ? 0.5311 0.5440 0.5448 -0.0279 0.1090  0.0428  20  ILE A CD1 
109  N N   . ALA A 21  ? 0.3959 0.4282 0.4288 -0.0134 0.0788  0.0461  21  ALA A N   
110  C CA  . ALA A 21  ? 0.4878 0.5165 0.5134 -0.0142 0.0707  0.0422  21  ALA A CA  
111  C C   . ALA A 21  ? 0.5379 0.5705 0.5778 -0.0051 0.0763  0.0480  21  ALA A C   
112  O O   . ALA A 21  ? 0.5363 0.5551 0.5667 -0.0040 0.0821  0.0439  21  ALA A O   
113  C CB  . ALA A 21  ? 0.4118 0.4530 0.4389 -0.0184 0.0527  0.0419  21  ALA A CB  
114  N N   . LEU A 22  ? 0.5120 0.5644 0.5748 0.0007  0.0743  0.0586  22  LEU A N   
115  C CA  . LEU A 22  ? 0.5979 0.6581 0.6773 0.0090  0.0781  0.0669  22  LEU A CA  
116  C C   . LEU A 22  ? 0.6832 0.7277 0.7639 0.0159  0.0991  0.0682  22  LEU A C   
117  O O   . LEU A 22  ? 0.7167 0.7551 0.7988 0.0208  0.1042  0.0689  22  LEU A O   
118  C CB  . LEU A 22  ? 0.6029 0.6895 0.7070 0.0117  0.0719  0.0805  22  LEU A CB  
119  C CG  . LEU A 22  ? 0.6057 0.7095 0.7214 0.0123  0.0600  0.0877  22  LEU A CG  
120  C CD1 . LEU A 22  ? 0.5588 0.6541 0.6558 0.0062  0.0476  0.0768  22  LEU A CD1 
121  C CD2 . LEU A 22  ? 0.5230 0.6520 0.6555 0.0090  0.0506  0.0991  22  LEU A CD2 
122  N N   . ALA A 23  ? 0.5732 0.6091 0.6524 0.0161  0.1128  0.0682  23  ALA A N   
123  C CA  . ALA A 23  ? 0.5937 0.6134 0.6761 0.0231  0.1363  0.0708  23  ALA A CA  
124  C C   . ALA A 23  ? 0.7425 0.7304 0.7942 0.0167  0.1471  0.0570  23  ALA A C   
125  O O   . ALA A 23  ? 0.6928 0.6640 0.7427 0.0218  0.1643  0.0571  23  ALA A O   
126  C CB  . ALA A 23  ? 0.6559 0.6804 0.7523 0.0266  0.1487  0.0785  23  ALA A CB  
127  N N   . GLU A 24  ? 0.5576 0.5367 0.5849 0.0049  0.1379  0.0462  24  GLU A N   
128  C CA  . GLU A 24  ? 0.6556 0.6056 0.6519 -0.0043 0.1479  0.0345  24  GLU A CA  
129  C C   . GLU A 24  ? 0.6706 0.6174 0.6456 -0.0151 0.1308  0.0258  24  GLU A C   
130  O O   . GLU A 24  ? 0.7828 0.7073 0.7317 -0.0242 0.1373  0.0175  24  GLU A O   
131  C CB  . GLU A 24  ? 0.7521 0.6892 0.7360 -0.0106 0.1597  0.0311  24  GLU A CB  
132  C CG  . GLU A 24  ? 0.7909 0.7270 0.7947 -0.0001 0.1808  0.0398  24  GLU A CG  
133  C CD  . GLU A 24  ? 0.8059 0.7342 0.8010 -0.0059 0.1894  0.0376  24  GLU A CD  
134  O OE1 . GLU A 24  ? 0.8925 0.7963 0.8563 -0.0183 0.1962  0.0268  24  GLU A OE1 
135  O OE2 . GLU A 24  ? 0.8416 0.7888 0.8607 0.0009  0.1893  0.0472  24  GLU A OE2 
136  N N   . GLY A 25  ? 0.5627 0.5304 0.5474 -0.0153 0.1102  0.0282  25  GLY A N   
137  C CA  . GLY A 25  ? 0.5289 0.4949 0.4978 -0.0239 0.0954  0.0223  25  GLY A CA  
138  C C   . GLY A 25  ? 0.6845 0.6512 0.6404 -0.0348 0.0865  0.0190  25  GLY A C   
139  O O   . GLY A 25  ? 0.5611 0.5294 0.5186 -0.0363 0.0907  0.0202  25  GLY A O   
140  N N   . PHE A 26  ? 0.6321 0.5979 0.5757 -0.0425 0.0742  0.0158  26  PHE A N   
141  C CA  . PHE A 26  ? 0.5587 0.5295 0.4945 -0.0520 0.0630  0.0154  26  PHE A CA  
142  C C   . PHE A 26  ? 0.6328 0.5875 0.5459 -0.0639 0.0716  0.0113  26  PHE A C   
143  O O   . PHE A 26  ? 0.5569 0.5165 0.4686 -0.0689 0.0680  0.0125  26  PHE A O   
144  C CB  . PHE A 26  ? 0.5431 0.5187 0.4757 -0.0561 0.0487  0.0157  26  PHE A CB  
145  C CG  . PHE A 26  ? 0.4354 0.4272 0.3883 -0.0472 0.0386  0.0195  26  PHE A CG  
146  C CD1 . PHE A 26  ? 0.4705 0.4758 0.4361 -0.0454 0.0315  0.0230  26  PHE A CD1 
147  C CD2 . PHE A 26  ? 0.4670 0.4590 0.4244 -0.0419 0.0367  0.0194  26  PHE A CD2 
148  C CE1 . PHE A 26  ? 0.3877 0.4047 0.3677 -0.0397 0.0234  0.0258  26  PHE A CE1 
149  C CE2 . PHE A 26  ? 0.4203 0.4250 0.3931 -0.0357 0.0281  0.0224  26  PHE A CE2 
150  C CZ  . PHE A 26  ? 0.4200 0.4365 0.4032 -0.0351 0.0218  0.0254  26  PHE A CZ  
151  N N   . THR A 27  ? 0.6480 0.5823 0.5410 -0.0699 0.0830  0.0063  27  THR A N   
152  C CA  . THR A 27  ? 0.7636 0.6803 0.6295 -0.0849 0.0904  0.0019  27  THR A CA  
153  C C   . THR A 27  ? 0.6596 0.5723 0.5281 -0.0829 0.1029  0.0018  27  THR A C   
154  O O   . THR A 27  ? 0.6422 0.5486 0.4939 -0.0950 0.1034  0.0000  27  THR A O   
155  C CB  . THR A 27  ? 0.8336 0.7258 0.6747 -0.0929 0.1028  -0.0042 27  THR A CB  
156  O OG1 . THR A 27  ? 0.9102 0.8076 0.7565 -0.0892 0.0942  -0.0033 27  THR A OG1 
157  C CG2 . THR A 27  ? 0.7831 0.6610 0.5916 -0.1141 0.1025  -0.0078 27  THR A CG2 
158  N N   . ALA A 28  ? 0.5540 0.4713 0.4441 -0.0683 0.1129  0.0048  28  ALA A N   
159  C CA  . ALA A 28  ? 0.6670 0.5828 0.5639 -0.0648 0.1253  0.0066  28  ALA A CA  
160  C C   . ALA A 28  ? 0.6002 0.5375 0.5115 -0.0640 0.1112  0.0111  28  ALA A C   
161  O O   . ALA A 28  ? 0.5539 0.4908 0.4688 -0.0633 0.1195  0.0125  28  ALA A O   
162  C CB  . ALA A 28  ? 0.5387 0.4559 0.4581 -0.0491 0.1399  0.0115  28  ALA A CB  
163  N N   . MET A 29  ? 0.4920 0.4463 0.4111 -0.0643 0.0916  0.0136  29  MET A N   
164  C CA  . MET A 29  ? 0.4960 0.4700 0.4305 -0.0623 0.0793  0.0182  29  MET A CA  
165  C C   . MET A 29  ? 0.5054 0.4768 0.4234 -0.0755 0.0729  0.0166  29  MET A C   
166  O O   . MET A 29  ? 0.5218 0.5044 0.4425 -0.0790 0.0579  0.0191  29  MET A O   
167  C CB  . MET A 29  ? 0.4400 0.4309 0.3906 -0.0563 0.0641  0.0217  29  MET A CB  
168  C CG  . MET A 29  ? 0.5559 0.5556 0.5269 -0.0438 0.0673  0.0257  29  MET A CG  
169  S SD  . MET A 29  ? 0.5012 0.5142 0.4822 -0.0406 0.0505  0.0276  29  MET A SD  
170  C CE  . MET A 29  ? 0.4449 0.4757 0.4396 -0.0408 0.0402  0.0320  29  MET A CE  
171  N N   . THR A 30  ? 0.5392 0.4950 0.4401 -0.0831 0.0857  0.0131  30  THR A N   
172  C CA  . THR A 30  ? 0.5113 0.4658 0.3972 -0.0962 0.0802  0.0127  30  THR A CA  
173  C C   . THR A 30  ? 0.5721 0.5420 0.4757 -0.0909 0.0764  0.0169  30  THR A C   
174  O O   . THR A 30  ? 0.4567 0.4338 0.3795 -0.0793 0.0826  0.0194  30  THR A O   
175  C CB  . THR A 30  ? 0.5970 0.5271 0.4543 -0.1086 0.0957  0.0068  30  THR A CB  
176  O OG1 . THR A 30  ? 0.5877 0.5090 0.4522 -0.0998 0.1147  0.0056  30  THR A OG1 
177  C CG2 . THR A 30  ? 0.6218 0.5352 0.4571 -0.1174 0.0987  0.0024  30  THR A CG2 
178  N N   . VAL A 31  ? 0.4866 0.4623 0.3841 -0.1001 0.0659  0.0188  31  VAL A N   
179  C CA  . VAL A 31  ? 0.4616 0.4504 0.3734 -0.0967 0.0624  0.0223  31  VAL A CA  
180  C C   . VAL A 31  ? 0.5090 0.4886 0.4180 -0.0957 0.0789  0.0202  31  VAL A C   
181  O O   . VAL A 31  ? 0.5096 0.5002 0.4379 -0.0866 0.0813  0.0237  31  VAL A O   
182  C CB  . VAL A 31  ? 0.4892 0.4846 0.3943 -0.1073 0.0495  0.0255  31  VAL A CB  
183  C CG1 . VAL A 31  ? 0.5001 0.5040 0.4141 -0.1063 0.0491  0.0279  31  VAL A CG1 
184  C CG2 . VAL A 31  ? 0.4567 0.4642 0.3731 -0.1043 0.0348  0.0298  31  VAL A CG2 
185  N N   . ARG A 32  ? 0.5384 0.4967 0.4226 -0.1058 0.0913  0.0150  32  ARG A N   
186  C CA  . ARG A 32  ? 0.5615 0.5063 0.4412 -0.1048 0.1109  0.0126  32  ARG A CA  
187  C C   . ARG A 32  ? 0.5636 0.5124 0.4669 -0.0882 0.1222  0.0156  32  ARG A C   
188  O O   . ARG A 32  ? 0.5603 0.5165 0.4805 -0.0805 0.1295  0.0198  32  ARG A O   
189  C CB  . ARG A 32  ? 0.6750 0.5917 0.5206 -0.1193 0.1243  0.0054  32  ARG A CB  
190  C CG  . ARG A 32  ? 0.8356 0.7329 0.6687 -0.1229 0.1459  0.0018  32  ARG A CG  
191  C CD  . ARG A 32  ? 0.9109 0.8197 0.7514 -0.1243 0.1416  0.0050  32  ARG A CD  
192  N NE  . ARG A 32  ? 1.1140 1.0370 0.9858 -0.1074 0.1475  0.0106  32  ARG A NE  
193  C CZ  . ARG A 32  ? 1.0246 0.9594 0.9081 -0.1056 0.1454  0.0143  32  ARG A CZ  
194  N NH1 . ARG A 32  ? 0.8876 0.8210 0.7545 -0.1187 0.1385  0.0125  32  ARG A NH1 
195  N NH2 . ARG A 32  ? 0.9731 0.9226 0.8859 -0.0909 0.1501  0.0208  32  ARG A NH2 
196  N N   . ARG A 33  ? 0.5454 0.4906 0.4509 -0.0829 0.1236  0.0148  33  ARG A N   
197  C CA  . ARG A 33  ? 0.5451 0.4946 0.4734 -0.0676 0.1344  0.0194  33  ARG A CA  
198  C C   . ARG A 33  ? 0.5760 0.5539 0.5352 -0.0570 0.1218  0.0279  33  ARG A C   
199  O O   . ARG A 33  ? 0.5432 0.5297 0.5234 -0.0473 0.1309  0.0346  33  ARG A O   
200  C CB  . ARG A 33  ? 0.5595 0.5003 0.4826 -0.0654 0.1358  0.0168  33  ARG A CB  
201  C CG  . ARG A 33  ? 0.7210 0.6681 0.6688 -0.0499 0.1452  0.0230  33  ARG A CG  
202  C CD  . ARG A 33  ? 0.7004 0.6309 0.6496 -0.0451 0.1714  0.0243  33  ARG A CD  
203  N NE  . ARG A 33  ? 0.7390 0.6807 0.7178 -0.0292 0.1790  0.0338  33  ARG A NE  
204  C CZ  . ARG A 33  ? 0.7946 0.7279 0.7743 -0.0239 0.1858  0.0337  33  ARG A CZ  
205  N NH1 . ARG A 33  ? 0.6073 0.5203 0.5593 -0.0333 0.1859  0.0239  33  ARG A NH1 
206  N NH2 . ARG A 33  ? 0.7511 0.6980 0.7607 -0.0095 0.1920  0.0447  33  ARG A NH2 
207  N N   . ILE A 34  ? 0.4803 0.4725 0.4423 -0.0595 0.1017  0.0284  34  ILE A N   
208  C CA  . ILE A 34  ? 0.4352 0.4514 0.4219 -0.0520 0.0897  0.0354  34  ILE A CA  
209  C C   . ILE A 34  ? 0.3597 0.3855 0.3550 -0.0527 0.0904  0.0391  34  ILE A C   
210  O O   . ILE A 34  ? 0.4193 0.4615 0.4368 -0.0452 0.0904  0.0467  34  ILE A O   
211  C CB  . ILE A 34  ? 0.3658 0.3899 0.3500 -0.0557 0.0711  0.0341  34  ILE A CB  
212  C CG1 . ILE A 34  ? 0.3661 0.3859 0.3493 -0.0519 0.0700  0.0326  34  ILE A CG1 
213  C CG2 . ILE A 34  ? 0.3531 0.3975 0.3554 -0.0525 0.0593  0.0395  34  ILE A CG2 
214  C CD1 . ILE A 34  ? 0.4050 0.4256 0.3797 -0.0575 0.0557  0.0302  34  ILE A CD1 
215  N N   . ALA A 35  ? 0.3911 0.4080 0.3690 -0.0625 0.0904  0.0348  35  ALA A N   
216  C CA  . ALA A 35  ? 0.4208 0.4448 0.4049 -0.0638 0.0922  0.0377  35  ALA A CA  
217  C C   . ALA A 35  ? 0.4980 0.5193 0.4937 -0.0564 0.1108  0.0418  35  ALA A C   
218  O O   . ALA A 35  ? 0.4485 0.4861 0.4646 -0.0509 0.1106  0.0492  35  ALA A O   
219  C CB  . ALA A 35  ? 0.4507 0.4632 0.4117 -0.0767 0.0904  0.0325  35  ALA A CB  
220  N N   . THR A 36  ? 0.4883 0.4885 0.4713 -0.0565 0.1281  0.0379  36  THR A N   
221  C CA  . THR A 36  ? 0.4958 0.4911 0.4917 -0.0479 0.1492  0.0429  36  THR A CA  
222  C C   . THR A 36  ? 0.5276 0.5451 0.5563 -0.0345 0.1471  0.0542  36  THR A C   
223  O O   . THR A 36  ? 0.5340 0.5646 0.5852 -0.0275 0.1540  0.0639  36  THR A O   
224  C CB  . THR A 36  ? 0.6066 0.5721 0.5813 -0.0507 0.1689  0.0360  36  THR A CB  
225  O OG1 . THR A 36  ? 0.5906 0.5363 0.5330 -0.0661 0.1707  0.0265  36  THR A OG1 
226  C CG2 . THR A 36  ? 0.6355 0.5937 0.6256 -0.0404 0.1941  0.0422  36  THR A CG2 
227  N N   . GLU A 37  ? 0.6119 0.6350 0.6440 -0.0316 0.1369  0.0543  37  GLU A N   
228  C CA  . GLU A 37  ? 0.4513 0.4953 0.5124 -0.0206 0.1343  0.0657  37  GLU A CA  
229  C C   . GLU A 37  ? 0.5327 0.6039 0.6119 -0.0210 0.1181  0.0734  37  GLU A C   
230  O O   . GLU A 37  ? 0.4811 0.5714 0.5865 -0.0138 0.1205  0.0861  37  GLU A O   
231  C CB  . GLU A 37  ? 0.5258 0.5677 0.5831 -0.0189 0.1269  0.0629  37  GLU A CB  
232  C CG  . GLU A 37  ? 0.6604 0.6773 0.7042 -0.0171 0.1446  0.0576  37  GLU A CG  
233  C CD  . GLU A 37  ? 0.7911 0.8071 0.8559 -0.0056 0.1660  0.0675  37  GLU A CD  
234  O OE1 . GLU A 37  ? 0.8577 0.8888 0.9454 0.0038  0.1646  0.0774  37  GLU A OE1 
235  O OE2 . GLU A 37  ? 0.9001 0.9001 0.9588 -0.0060 0.1850  0.0662  37  GLU A OE2 
236  N N   . ALA A 38  ? 0.3845 0.4580 0.4504 -0.0299 0.1021  0.0671  38  ALA A N   
237  C CA  . ALA A 38  ? 0.3730 0.4682 0.4517 -0.0322 0.0881  0.0729  38  ALA A CA  
238  C C   . ALA A 38  ? 0.4173 0.5159 0.4998 -0.0343 0.0940  0.0758  38  ALA A C   
239  O O   . ALA A 38  ? 0.4306 0.5464 0.5227 -0.0372 0.0835  0.0807  38  ALA A O   
240  C CB  . ALA A 38  ? 0.3678 0.4624 0.4320 -0.0401 0.0705  0.0657  38  ALA A CB  
241  N N   . GLN A 39  ? 0.4214 0.5025 0.4951 -0.0337 0.1113  0.0726  39  GLN A N   
242  C CA  . GLN A 39  ? 0.3997 0.4801 0.4738 -0.0362 0.1191  0.0739  39  GLN A CA  
243  C C   . GLN A 39  ? 0.4420 0.5261 0.5039 -0.0461 0.1037  0.0687  39  GLN A C   
244  O O   . GLN A 39  ? 0.4284 0.5281 0.5020 -0.0473 0.0983  0.0743  39  GLN A O   
245  C CB  . GLN A 39  ? 0.5369 0.6379 0.6417 -0.0279 0.1257  0.0886  39  GLN A CB  
246  C CG  . GLN A 39  ? 0.5565 0.6558 0.6784 -0.0167 0.1427  0.0969  39  GLN A CG  
247  C CD  . GLN A 39  ? 0.8482 0.9756 1.0055 -0.0089 0.1441  0.1152  39  GLN A CD  
248  O OE1 . GLN A 39  ? 0.8123 0.9563 0.9882 -0.0037 0.1386  0.1250  39  GLN A OE1 
249  N NE2 . GLN A 39  ? 0.5628 0.6967 0.7298 -0.0090 0.1509  0.1211  39  GLN A NE2 
250  N N   . THR A 40  ? 0.4528 0.5226 0.4915 -0.0536 0.0970  0.0589  40  THR A N   
251  C CA  . THR A 40  ? 0.3839 0.4550 0.4108 -0.0628 0.0841  0.0547  40  THR A CA  
252  C C   . THR A 40  ? 0.5279 0.5774 0.5280 -0.0717 0.0887  0.0462  40  THR A C   
253  O O   . THR A 40  ? 0.4982 0.5308 0.4873 -0.0717 0.1027  0.0427  40  THR A O   
254  C CB  . THR A 40  ? 0.4345 0.5169 0.4655 -0.0636 0.0664  0.0552  40  THR A CB  
255  O OG1 . THR A 40  ? 0.4464 0.5315 0.4708 -0.0710 0.0561  0.0535  40  THR A OG1 
256  C CG2 . THR A 40  ? 0.3603 0.4317 0.3796 -0.0640 0.0634  0.0500  40  THR A CG2 
257  N N   . SER A 41  ? 0.3840 0.4341 0.3731 -0.0803 0.0774  0.0436  41  SER A N   
258  C CA  . SER A 41  ? 0.4322 0.4659 0.3961 -0.0914 0.0782  0.0378  41  SER A CA  
259  C C   . SER A 41  ? 0.4118 0.4428 0.3673 -0.0944 0.0675  0.0358  41  SER A C   
260  O O   . SER A 41  ? 0.3723 0.4153 0.3405 -0.0896 0.0564  0.0384  41  SER A O   
261  C CB  . SER A 41  ? 0.4136 0.4511 0.3723 -0.0993 0.0720  0.0386  41  SER A CB  
262  O OG  . SER A 41  ? 0.4388 0.4905 0.4078 -0.0986 0.0563  0.0418  41  SER A OG  
263  N N   . THR A 42  ? 0.4493 0.4639 0.3821 -0.1035 0.0715  0.0313  42  THR A N   
264  C CA  . THR A 42  ? 0.4445 0.4583 0.3693 -0.1080 0.0604  0.0309  42  THR A CA  
265  C C   . THR A 42  ? 0.4192 0.4458 0.3498 -0.1116 0.0448  0.0355  42  THR A C   
266  O O   . THR A 42  ? 0.4063 0.4391 0.3431 -0.1094 0.0346  0.0378  42  THR A O   
267  C CB  . THR A 42  ? 0.5180 0.5129 0.4152 -0.1206 0.0665  0.0265  42  THR A CB  
268  O OG1 . THR A 42  ? 0.5274 0.5163 0.4089 -0.1324 0.0689  0.0260  42  THR A OG1 
269  C CG2 . THR A 42  ? 0.5772 0.5563 0.4685 -0.1163 0.0838  0.0216  42  THR A CG2 
270  N N   . GLY A 43  ? 0.4339 0.4638 0.3634 -0.1164 0.0440  0.0373  43  GLY A N   
271  C CA  . GLY A 43  ? 0.4723 0.5138 0.4096 -0.1185 0.0313  0.0425  43  GLY A CA  
272  C C   . GLY A 43  ? 0.4008 0.4544 0.3591 -0.1081 0.0252  0.0448  43  GLY A C   
273  O O   . GLY A 43  ? 0.4161 0.4750 0.3800 -0.1081 0.0157  0.0483  43  GLY A O   
274  N N   . GLN A 44  ? 0.3720 0.4299 0.3419 -0.0999 0.0312  0.0437  44  GLN A N   
275  C CA  . GLN A 44  ? 0.3562 0.4250 0.3428 -0.0927 0.0253  0.0459  44  GLN A CA  
276  C C   . GLN A 44  ? 0.3601 0.4273 0.3485 -0.0885 0.0219  0.0450  44  GLN A C   
277  O O   . GLN A 44  ? 0.3546 0.4269 0.3507 -0.0862 0.0146  0.0466  44  GLN A O   
278  C CB  . GLN A 44  ? 0.3813 0.4581 0.3806 -0.0869 0.0315  0.0474  44  GLN A CB  
279  C CG  . GLN A 44  ? 0.4421 0.5264 0.4463 -0.0899 0.0298  0.0500  44  GLN A CG  
280  C CD  . GLN A 44  ? 0.5882 0.6793 0.5986 -0.0911 0.0196  0.0520  44  GLN A CD  
281  O OE1 . GLN A 44  ? 0.5300 0.6187 0.5354 -0.0962 0.0151  0.0526  44  GLN A OE1 
282  N NE2 . GLN A 44  ? 0.5841 0.6828 0.6048 -0.0871 0.0168  0.0535  44  GLN A NE2 
283  N N   . VAL A 45  ? 0.3389 0.3973 0.3191 -0.0878 0.0281  0.0421  45  VAL A N   
284  C CA  . VAL A 45  ? 0.3062 0.3625 0.2868 -0.0845 0.0246  0.0412  45  VAL A CA  
285  C C   . VAL A 45  ? 0.3635 0.4188 0.3390 -0.0899 0.0151  0.0432  45  VAL A C   
286  O O   . VAL A 45  ? 0.3669 0.4256 0.3499 -0.0862 0.0091  0.0447  45  VAL A O   
287  C CB  . VAL A 45  ? 0.3923 0.4372 0.3630 -0.0838 0.0342  0.0376  45  VAL A CB  
288  C CG1 . VAL A 45  ? 0.3480 0.3910 0.3189 -0.0808 0.0299  0.0367  45  VAL A CG1 
289  C CG2 . VAL A 45  ? 0.3531 0.3999 0.3335 -0.0767 0.0454  0.0380  45  VAL A CG2 
290  N N   . HIS A 46  ? 0.3892 0.4405 0.3528 -0.0990 0.0141  0.0445  46  HIS A N   
291  C CA  . HIS A 46  ? 0.4691 0.5224 0.4311 -0.1043 0.0052  0.0497  46  HIS A CA  
292  C C   . HIS A 46  ? 0.4693 0.5307 0.4453 -0.1013 -0.0005 0.0542  46  HIS A C   
293  O O   . HIS A 46  ? 0.5054 0.5689 0.4873 -0.1007 -0.0062 0.0590  46  HIS A O   
294  C CB  . HIS A 46  ? 0.4333 0.4820 0.3788 -0.1166 0.0049  0.0518  46  HIS A CB  
295  C CG  . HIS A 46  ? 0.4334 0.4709 0.3610 -0.1227 0.0099  0.0479  46  HIS A CG  
296  N ND1 . HIS A 46  ? 0.4670 0.5024 0.3928 -0.1218 0.0071  0.0481  46  HIS A ND1 
297  C CD2 . HIS A 46  ? 0.4802 0.5060 0.3892 -0.1304 0.0190  0.0432  46  HIS A CD2 
298  C CE1 . HIS A 46  ? 0.5101 0.5330 0.4165 -0.1292 0.0136  0.0437  46  HIS A CE1 
299  N NE2 . HIS A 46  ? 0.5460 0.5619 0.4412 -0.1347 0.0216  0.0404  46  HIS A NE2 
300  N N   . HIS A 47  ? 0.4877 0.5529 0.4691 -0.0997 0.0019  0.0531  47  HIS A N   
301  C CA  . HIS A 47  ? 0.4161 0.4863 0.4084 -0.0979 -0.0019 0.0565  47  HIS A CA  
302  C C   . HIS A 47  ? 0.4747 0.5453 0.4758 -0.0913 -0.0033 0.0553  47  HIS A C   
303  O O   . HIS A 47  ? 0.4821 0.5517 0.4889 -0.0906 -0.0062 0.0587  47  HIS A O   
304  C CB  . HIS A 47  ? 0.4697 0.5439 0.4644 -0.0986 0.0012  0.0553  47  HIS A CB  
305  C CG  . HIS A 47  ? 0.6045 0.6818 0.6080 -0.0977 -0.0014 0.0575  47  HIS A CG  
306  N ND1 . HIS A 47  ? 0.5897 0.6706 0.5996 -0.0945 -0.0004 0.0553  47  HIS A ND1 
307  C CD2 . HIS A 47  ? 0.6454 0.7222 0.6518 -0.1006 -0.0041 0.0623  47  HIS A CD2 
308  C CE1 . HIS A 47  ? 0.6116 0.6917 0.6251 -0.0964 -0.0020 0.0572  47  HIS A CE1 
309  N NE2 . HIS A 47  ? 0.5474 0.6245 0.5599 -0.0991 -0.0034 0.0614  47  HIS A NE2 
310  N N   . HIS A 48  ? 0.3709 0.4423 0.3733 -0.0866 -0.0004 0.0511  48  HIS A N   
311  C CA  . HIS A 48  ? 0.4382 0.5105 0.4473 -0.0820 -0.0019 0.0499  48  HIS A CA  
312  C C   . HIS A 48  ? 0.4682 0.5357 0.4763 -0.0795 -0.0039 0.0499  48  HIS A C   
313  O O   . HIS A 48  ? 0.4247 0.4907 0.4372 -0.0770 -0.0053 0.0495  48  HIS A O   
314  C CB  . HIS A 48  ? 0.3813 0.4595 0.3947 -0.0786 0.0013  0.0480  48  HIS A CB  
315  C CG  . HIS A 48  ? 0.4749 0.5601 0.4926 -0.0809 0.0022  0.0494  48  HIS A CG  
316  N ND1 . HIS A 48  ? 0.4987 0.5852 0.5188 -0.0841 -0.0009 0.0504  48  HIS A ND1 
317  C CD2 . HIS A 48  ? 0.4164 0.5069 0.4362 -0.0808 0.0067  0.0502  48  HIS A CD2 
318  C CE1 . HIS A 48  ? 0.4229 0.5166 0.4462 -0.0865 0.0003  0.0519  48  HIS A CE1 
319  N NE2 . HIS A 48  ? 0.5027 0.5997 0.5271 -0.0840 0.0049  0.0523  48  HIS A NE2 
320  N N   . PHE A 49  ? 0.4245 0.4887 0.4255 -0.0812 -0.0036 0.0501  49  PHE A N   
321  C CA  . PHE A 49  ? 0.4745 0.5350 0.4742 -0.0792 -0.0055 0.0502  49  PHE A CA  
322  C C   . PHE A 49  ? 0.4851 0.5442 0.4798 -0.0850 -0.0089 0.0555  49  PHE A C   
323  O O   . PHE A 49  ? 0.4473 0.5057 0.4326 -0.0915 -0.0082 0.0562  49  PHE A O   
324  C CB  . PHE A 49  ? 0.3791 0.4373 0.3743 -0.0761 -0.0012 0.0456  49  PHE A CB  
325  C CG  . PHE A 49  ? 0.3316 0.3945 0.3347 -0.0706 0.0011  0.0435  49  PHE A CG  
326  C CD1 . PHE A 49  ? 0.3930 0.4567 0.4016 -0.0667 -0.0014 0.0430  49  PHE A CD1 
327  C CD2 . PHE A 49  ? 0.3831 0.4504 0.3885 -0.0703 0.0055  0.0432  49  PHE A CD2 
328  C CE1 . PHE A 49  ? 0.4353 0.5052 0.4506 -0.0638 -0.0007 0.0428  49  PHE A CE1 
329  C CE2 . PHE A 49  ? 0.4591 0.5342 0.4740 -0.0663 0.0065  0.0441  49  PHE A CE2 
330  C CZ  . PHE A 49  ? 0.4443 0.5211 0.4635 -0.0637 0.0028  0.0441  49  PHE A CZ  
331  N N   . SER A 50  ? 0.5003 0.5591 0.5011 -0.0834 -0.0123 0.0601  50  SER A N   
332  C CA  . SER A 50  ? 0.6029 0.6643 0.6039 -0.0891 -0.0166 0.0689  50  SER A CA  
333  C C   . SER A 50  ? 0.5093 0.5692 0.4969 -0.0959 -0.0182 0.0689  50  SER A C   
334  O O   . SER A 50  ? 0.5815 0.6448 0.5639 -0.1048 -0.0221 0.0759  50  SER A O   
335  C CB  . SER A 50  ? 0.5495 0.6110 0.5629 -0.0845 -0.0181 0.0751  50  SER A CB  
336  O OG  . SER A 50  ? 0.7054 0.7633 0.7264 -0.0788 -0.0144 0.0720  50  SER A OG  
337  N N   . SER A 51  ? 0.4712 0.5258 0.4522 -0.0930 -0.0151 0.0617  51  SER A N   
338  C CA  . SER A 51  ? 0.4778 0.5274 0.4429 -0.1004 -0.0145 0.0602  51  SER A CA  
339  C C   . SER A 51  ? 0.4508 0.4929 0.4104 -0.0950 -0.0071 0.0507  51  SER A C   
340  O O   . SER A 51  ? 0.4133 0.4570 0.3834 -0.0857 -0.0050 0.0474  51  SER A O   
341  C CB  . SER A 51  ? 0.4581 0.5101 0.4244 -0.1035 -0.0205 0.0672  51  SER A CB  
342  O OG  . SER A 51  ? 0.4181 0.4676 0.3905 -0.0948 -0.0194 0.0636  51  SER A OG  
343  N N   . ALA A 52  ? 0.4159 0.4493 0.3582 -0.1020 -0.0026 0.0471  52  ALA A N   
344  C CA  . ALA A 52  ? 0.5053 0.5302 0.4432 -0.0965 0.0063  0.0395  52  ALA A CA  
345  C C   . ALA A 52  ? 0.4937 0.5199 0.4404 -0.0885 0.0039  0.0389  52  ALA A C   
346  O O   . ALA A 52  ? 0.3699 0.3953 0.3235 -0.0796 0.0089  0.0350  52  ALA A O   
347  C CB  . ALA A 52  ? 0.4600 0.4715 0.3749 -0.1070 0.0132  0.0357  52  ALA A CB  
348  N N   . SER A 53  ? 0.3917 0.4210 0.3394 -0.0916 -0.0038 0.0440  53  SER A N   
349  C CA  . SER A 53  ? 0.4134 0.4436 0.3694 -0.0843 -0.0060 0.0437  53  SER A CA  
350  C C   . SER A 53  ? 0.4040 0.4409 0.3776 -0.0748 -0.0079 0.0445  53  SER A C   
351  O O   . SER A 53  ? 0.3707 0.4068 0.3499 -0.0676 -0.0067 0.0415  53  SER A O   
352  C CB  . SER A 53  ? 0.5336 0.5658 0.4868 -0.0908 -0.0130 0.0504  53  SER A CB  
353  O OG  . SER A 53  ? 0.5604 0.5838 0.4964 -0.0976 -0.0103 0.0472  53  SER A OG  
354  N N   . HIS A 54  ? 0.3603 0.4027 0.3411 -0.0758 -0.0106 0.0486  54  HIS A N   
355  C CA  . HIS A 54  ? 0.3858 0.4315 0.3791 -0.0691 -0.0107 0.0481  54  HIS A CA  
356  C C   . HIS A 54  ? 0.3544 0.4006 0.3488 -0.0645 -0.0060 0.0424  54  HIS A C   
357  O O   . HIS A 54  ? 0.3598 0.4074 0.3608 -0.0594 -0.0061 0.0408  54  HIS A O   
358  C CB  . HIS A 54  ? 0.4170 0.4666 0.4158 -0.0720 -0.0126 0.0531  54  HIS A CB  
359  C CG  . HIS A 54  ? 0.4232 0.4744 0.4292 -0.0732 -0.0163 0.0614  54  HIS A CG  
360  N ND1 . HIS A 54  ? 0.4874 0.5417 0.4900 -0.0800 -0.0203 0.0686  54  HIS A ND1 
361  C CD2 . HIS A 54  ? 0.4715 0.5216 0.4886 -0.0690 -0.0157 0.0648  54  HIS A CD2 
362  C CE1 . HIS A 54  ? 0.4725 0.5298 0.4870 -0.0787 -0.0224 0.0777  54  HIS A CE1 
363  N NE2 . HIS A 54  ? 0.6331 0.6864 0.6564 -0.0715 -0.0185 0.0750  54  HIS A NE2 
364  N N   . LEU A 55  ? 0.3224 0.3678 0.3106 -0.0670 -0.0015 0.0404  55  LEU A N   
365  C CA  . LEU A 55  ? 0.3427 0.3906 0.3352 -0.0622 0.0040  0.0377  55  LEU A CA  
366  C C   . LEU A 55  ? 0.3565 0.4017 0.3496 -0.0568 0.0071  0.0354  55  LEU A C   
367  O O   . LEU A 55  ? 0.3211 0.3720 0.3236 -0.0515 0.0076  0.0358  55  LEU A O   
368  C CB  . LEU A 55  ? 0.3582 0.4036 0.3438 -0.0658 0.0104  0.0367  55  LEU A CB  
369  C CG  . LEU A 55  ? 0.3914 0.4397 0.3832 -0.0609 0.0184  0.0360  55  LEU A CG  
370  C CD1 . LEU A 55  ? 0.3551 0.4152 0.3616 -0.0565 0.0146  0.0389  55  LEU A CD1 
371  C CD2 . LEU A 55  ? 0.3940 0.4391 0.3791 -0.0655 0.0246  0.0356  55  LEU A CD2 
372  N N   . LYS A 56  ? 0.3213 0.3581 0.3040 -0.0591 0.0088  0.0336  56  LYS A N   
373  C CA  . LYS A 56  ? 0.3174 0.3504 0.3001 -0.0541 0.0123  0.0314  56  LYS A CA  
374  C C   . LYS A 56  ? 0.3231 0.3611 0.3153 -0.0494 0.0061  0.0326  56  LYS A C   
375  O O   . LYS A 56  ? 0.3417 0.3825 0.3406 -0.0437 0.0080  0.0323  56  LYS A O   
376  C CB  . LYS A 56  ? 0.3643 0.3864 0.3317 -0.0598 0.0142  0.0293  56  LYS A CB  
377  C CG  . LYS A 56  ? 0.4130 0.4248 0.3667 -0.0650 0.0241  0.0264  56  LYS A CG  
378  C CD  . LYS A 56  ? 0.4121 0.4124 0.3468 -0.0741 0.0247  0.0245  56  LYS A CD  
379  C CE  . LYS A 56  ? 0.5336 0.5193 0.4498 -0.0817 0.0364  0.0205  56  LYS A CE  
380  N NZ  . LYS A 56  ? 0.5536 0.5306 0.4479 -0.0963 0.0335  0.0203  56  LYS A NZ  
381  N N   . ALA A 57  ? 0.3671 0.4059 0.3601 -0.0521 -0.0006 0.0346  57  ALA A N   
382  C CA  . ALA A 57  ? 0.3319 0.3719 0.3315 -0.0485 -0.0045 0.0351  57  ALA A CA  
383  C C   . ALA A 57  ? 0.3307 0.3767 0.3383 -0.0467 -0.0052 0.0354  57  ALA A C   
384  O O   . ALA A 57  ? 0.3634 0.4106 0.3745 -0.0439 -0.0062 0.0347  57  ALA A O   
385  C CB  . ALA A 57  ? 0.3108 0.3490 0.3109 -0.0515 -0.0089 0.0387  57  ALA A CB  
386  N N   . GLU A 58  ? 0.3038 0.3536 0.3130 -0.0495 -0.0051 0.0367  58  GLU A N   
387  C CA  . GLU A 58  ? 0.2754 0.3313 0.2903 -0.0500 -0.0061 0.0374  58  GLU A CA  
388  C C   . GLU A 58  ? 0.3418 0.4052 0.3618 -0.0468 -0.0038 0.0383  58  GLU A C   
389  O O   . GLU A 58  ? 0.3244 0.3933 0.3486 -0.0472 -0.0062 0.0398  58  GLU A O   
390  C CB  . GLU A 58  ? 0.3677 0.4258 0.3828 -0.0542 -0.0062 0.0388  58  GLU A CB  
391  C CG  . GLU A 58  ? 0.5341 0.5956 0.5521 -0.0573 -0.0079 0.0395  58  GLU A CG  
392  C CD  . GLU A 58  ? 0.5656 0.6269 0.5831 -0.0616 -0.0078 0.0407  58  GLU A CD  
393  O OE1 . GLU A 58  ? 0.6534 0.7111 0.6690 -0.0621 -0.0073 0.0418  58  GLU A OE1 
394  O OE2 . GLU A 58  ? 0.6171 0.6822 0.6357 -0.0653 -0.0084 0.0413  58  GLU A OE2 
395  N N   . ALA A 59  ? 0.3151 0.3783 0.3346 -0.0442 0.0016  0.0384  59  ALA A N   
396  C CA  . ALA A 59  ? 0.3224 0.3928 0.3501 -0.0396 0.0059  0.0414  59  ALA A CA  
397  C C   . ALA A 59  ? 0.4312 0.5003 0.4604 -0.0356 0.0051  0.0411  59  ALA A C   
398  O O   . ALA A 59  ? 0.3431 0.4216 0.3814 -0.0333 0.0045  0.0456  59  ALA A O   
399  C CB  . ALA A 59  ? 0.3501 0.4165 0.3760 -0.0376 0.0151  0.0412  59  ALA A CB  
400  N N   . PHE A 60  ? 0.3089 0.3674 0.3294 -0.0355 0.0047  0.0371  60  PHE A N   
401  C CA  . PHE A 60  ? 0.3359 0.3921 0.3568 -0.0321 0.0037  0.0364  60  PHE A CA  
402  C C   . PHE A 60  ? 0.3358 0.3973 0.3605 -0.0338 -0.0028 0.0377  60  PHE A C   
403  O O   . PHE A 60  ? 0.3705 0.4377 0.4006 -0.0315 -0.0036 0.0402  60  PHE A O   
404  C CB  . PHE A 60  ? 0.3237 0.3686 0.3344 -0.0333 0.0033  0.0326  60  PHE A CB  
405  C CG  . PHE A 60  ? 0.3621 0.4041 0.3726 -0.0304 0.0012  0.0315  60  PHE A CG  
406  C CD1 . PHE A 60  ? 0.3529 0.3947 0.3659 -0.0255 0.0056  0.0319  60  PHE A CD1 
407  C CD2 . PHE A 60  ? 0.4582 0.4972 0.4670 -0.0323 -0.0041 0.0308  60  PHE A CD2 
408  C CE1 . PHE A 60  ? 0.4002 0.4394 0.4128 -0.0230 0.0035  0.0310  60  PHE A CE1 
409  C CE2 . PHE A 60  ? 0.4131 0.4489 0.4215 -0.0297 -0.0056 0.0297  60  PHE A CE2 
410  C CZ  . PHE A 60  ? 0.3840 0.4203 0.3938 -0.0254 -0.0025 0.0295  60  PHE A CZ  
411  N N   . LEU A 61  ? 0.3409 0.3997 0.3620 -0.0386 -0.0067 0.0364  61  LEU A N   
412  C CA  . LEU A 61  ? 0.3758 0.4351 0.3964 -0.0422 -0.0107 0.0364  61  LEU A CA  
413  C C   . LEU A 61  ? 0.3544 0.4260 0.3806 -0.0453 -0.0126 0.0408  61  LEU A C   
414  O O   . LEU A 61  ? 0.4114 0.4863 0.4373 -0.0483 -0.0158 0.0423  61  LEU A O   
415  C CB  . LEU A 61  ? 0.4254 0.4766 0.4412 -0.0465 -0.0115 0.0346  61  LEU A CB  
416  C CG  . LEU A 61  ? 0.4302 0.4713 0.4431 -0.0444 -0.0108 0.0330  61  LEU A CG  
417  C CD1 . LEU A 61  ? 0.4770 0.5115 0.4890 -0.0477 -0.0098 0.0338  61  LEU A CD1 
418  C CD2 . LEU A 61  ? 0.4122 0.4489 0.4234 -0.0428 -0.0115 0.0315  61  LEU A CD2 
419  N N   . LYS A 62  ? 0.3388 0.4181 0.3700 -0.0456 -0.0109 0.0438  62  LYS A N   
420  C CA  . LYS A 62  ? 0.3587 0.4529 0.3980 -0.0487 -0.0129 0.0504  62  LYS A CA  
421  C C   . LYS A 62  ? 0.4540 0.5577 0.5031 -0.0435 -0.0118 0.0561  62  LYS A C   
422  O O   . LYS A 62  ? 0.4355 0.5510 0.4896 -0.0475 -0.0163 0.0623  62  LYS A O   
423  C CB  . LYS A 62  ? 0.3703 0.4706 0.4145 -0.0489 -0.0101 0.0529  62  LYS A CB  
424  C CG  . LYS A 62  ? 0.5323 0.6287 0.5697 -0.0561 -0.0126 0.0503  62  LYS A CG  
425  C CD  . LYS A 62  ? 0.6504 0.7524 0.6852 -0.0653 -0.0181 0.0529  62  LYS A CD  
426  C CE  . LYS A 62  ? 0.7656 0.8829 0.8079 -0.0698 -0.0196 0.0597  62  LYS A CE  
427  N NZ  . LYS A 62  ? 0.8475 0.9589 0.8822 -0.0767 -0.0200 0.0566  62  LYS A NZ  
428  N N   . LEU A 63  ? 0.3752 0.4737 0.4265 -0.0354 -0.0055 0.0548  63  LEU A N   
429  C CA  . LEU A 63  ? 0.3529 0.4584 0.4145 -0.0294 -0.0024 0.0607  63  LEU A CA  
430  C C   . LEU A 63  ? 0.4593 0.5628 0.5169 -0.0307 -0.0076 0.0595  63  LEU A C   
431  O O   . LEU A 63  ? 0.4226 0.5374 0.4899 -0.0292 -0.0088 0.0670  63  LEU A O   
432  C CB  . LEU A 63  ? 0.3930 0.4887 0.4542 -0.0218 0.0078  0.0581  63  LEU A CB  
433  C CG  . LEU A 63  ? 0.3695 0.4690 0.4377 -0.0196 0.0157  0.0618  63  LEU A CG  
434  C CD1 . LEU A 63  ? 0.3213 0.4056 0.3829 -0.0149 0.0270  0.0571  63  LEU A CD1 
435  C CD2 . LEU A 63  ? 0.4035 0.5220 0.4915 -0.0166 0.0173  0.0744  63  LEU A CD2 
436  N N   . MET A 64  ? 0.4573 0.5472 0.5020 -0.0334 -0.0103 0.0513  64  MET A N   
437  C CA  . MET A 64  ? 0.5195 0.6055 0.5594 -0.0348 -0.0142 0.0496  64  MET A CA  
438  C C   . MET A 64  ? 0.5910 0.6843 0.6286 -0.0443 -0.0207 0.0528  64  MET A C   
439  O O   . MET A 64  ? 0.4983 0.5972 0.5370 -0.0465 -0.0242 0.0564  64  MET A O   
440  C CB  . MET A 64  ? 0.5366 0.6061 0.5654 -0.0344 -0.0136 0.0414  64  MET A CB  
441  C CG  . MET A 64  ? 0.3720 0.4340 0.3999 -0.0275 -0.0086 0.0387  64  MET A CG  
442  S SD  . MET A 64  ? 0.4706 0.5372 0.5060 -0.0205 -0.0050 0.0426  64  MET A SD  
443  C CE  . MET A 64  ? 0.5484 0.6166 0.5899 -0.0156 0.0044  0.0453  64  MET A CE  
444  N N   . GLU A 65  ? 0.4750 0.5678 0.5079 -0.0514 -0.0224 0.0516  65  GLU A N   
445  C CA  . GLU A 65  ? 0.6099 0.7097 0.6385 -0.0629 -0.0279 0.0552  65  GLU A CA  
446  C C   . GLU A 65  ? 0.5955 0.7174 0.6379 -0.0640 -0.0312 0.0671  65  GLU A C   
447  O O   . GLU A 65  ? 0.5735 0.7043 0.6137 -0.0732 -0.0373 0.0726  65  GLU A O   
448  C CB  . GLU A 65  ? 0.6864 0.7811 0.7082 -0.0696 -0.0276 0.0521  65  GLU A CB  
449  C CG  . GLU A 65  ? 0.8277 0.9031 0.8339 -0.0756 -0.0261 0.0440  65  GLU A CG  
450  C CD  . GLU A 65  ? 1.0469 1.1126 1.0512 -0.0738 -0.0219 0.0398  65  GLU A CD  
451  O OE1 . GLU A 65  ? 0.9629 1.0135 0.9625 -0.0706 -0.0180 0.0347  65  GLU A OE1 
452  O OE2 . GLU A 65  ? 1.0176 1.0917 1.0264 -0.0754 -0.0224 0.0427  65  GLU A OE2 
453  N N   . GLN A 66  ? 0.5478 0.6786 0.6046 -0.0552 -0.0267 0.0722  66  GLN A N   
454  C CA  . GLN A 66  ? 0.4542 0.6070 0.5291 -0.0537 -0.0275 0.0859  66  GLN A CA  
455  C C   . GLN A 66  ? 0.5998 0.7576 0.6816 -0.0490 -0.0278 0.0911  66  GLN A C   
456  O O   . GLN A 66  ? 0.5912 0.7682 0.6841 -0.0531 -0.0327 0.1037  66  GLN A O   
457  C CB  . GLN A 66  ? 0.5908 0.7469 0.6782 -0.0445 -0.0192 0.0887  66  GLN A CB  
458  C CG  . GLN A 66  ? 0.6411 0.8164 0.7512 -0.0380 -0.0151 0.1032  66  GLN A CG  
459  C CD  . GLN A 66  ? 0.5357 0.7170 0.6562 -0.0347 -0.0088 0.1075  66  GLN A CD  
460  O OE1 . GLN A 66  ? 0.6715 0.8582 0.7885 -0.0430 -0.0136 0.1080  66  GLN A OE1 
461  N NE2 . GLN A 66  ? 0.4521 0.6305 0.5838 -0.0232 0.0033  0.1102  66  GLN A NE2 
462  N N   . LEU A 67  ? 0.5448 0.6864 0.6204 -0.0412 -0.0232 0.0824  67  LEU A N   
463  C CA  . LEU A 67  ? 0.5668 0.7104 0.6470 -0.0368 -0.0232 0.0858  67  LEU A CA  
464  C C   . LEU A 67  ? 0.4775 0.6243 0.5483 -0.0483 -0.0326 0.0870  67  LEU A C   
465  O O   . LEU A 67  ? 0.5307 0.6917 0.6106 -0.0496 -0.0362 0.0972  67  LEU A O   
466  C CB  . LEU A 67  ? 0.5182 0.6420 0.5904 -0.0283 -0.0168 0.0751  67  LEU A CB  
467  C CG  . LEU A 67  ? 0.5369 0.6558 0.6069 -0.0250 -0.0174 0.0739  67  LEU A CG  
468  C CD1 . LEU A 67  ? 0.6872 0.8224 0.7754 -0.0198 -0.0155 0.0869  67  LEU A CD1 
469  C CD2 . LEU A 67  ? 0.5848 0.6845 0.6462 -0.0180 -0.0110 0.0636  67  LEU A CD2 
470  N N   . ASP A 68  ? 0.4720 0.6047 0.5242 -0.0570 -0.0356 0.0771  68  ASP A N   
471  C CA  . ASP A 68  ? 0.6387 0.7703 0.6778 -0.0702 -0.0425 0.0769  68  ASP A CA  
472  C C   . ASP A 68  ? 0.7399 0.8932 0.7842 -0.0823 -0.0500 0.0897  68  ASP A C   
473  O O   . ASP A 68  ? 0.6976 0.8608 0.7402 -0.0910 -0.0565 0.0968  68  ASP A O   
474  C CB  . ASP A 68  ? 0.6808 0.7901 0.6998 -0.0764 -0.0408 0.0641  68  ASP A CB  
475  C CG  . ASP A 68  ? 1.0271 1.1334 1.0292 -0.0939 -0.0459 0.0638  68  ASP A CG  
476  O OD1 . ASP A 68  ? 0.9740 1.0721 0.9656 -0.0984 -0.0470 0.0610  68  ASP A OD1 
477  O OD2 . ASP A 68  ? 1.0468 1.1571 1.0440 -0.1041 -0.0481 0.0657  68  ASP A OD2 
478  N N   . GLU A 69  ? 0.6609 0.8230 0.7117 -0.0839 -0.0498 0.0935  69  GLU A N   
479  C CA  . GLU A 69  ? 0.6793 0.8648 0.7373 -0.0956 -0.0572 0.1075  69  GLU A CA  
480  C C   . GLU A 69  ? 0.6693 0.8793 0.7504 -0.0903 -0.0594 0.1245  69  GLU A C   
481  O O   . GLU A 69  ? 0.6916 0.9187 0.7737 -0.1026 -0.0683 0.1362  69  GLU A O   
482  C CB  . GLU A 69  ? 0.7895 0.9800 0.8536 -0.0950 -0.0549 0.1088  69  GLU A CB  
483  C CG  . GLU A 69  ? 0.8997 1.0761 0.9421 -0.1085 -0.0568 0.0994  69  GLU A CG  
484  C CD  . GLU A 69  ? 0.9722 1.1481 1.0199 -0.1042 -0.0525 0.0974  69  GLU A CD  
485  O OE1 . GLU A 69  ? 0.9248 1.1203 0.9927 -0.0986 -0.0519 0.1086  69  GLU A OE1 
486  O OE2 . GLU A 69  ? 0.9332 1.0889 0.9657 -0.1060 -0.0490 0.0852  69  GLU A OE2 
487  N N   . ILE A 70  ? 0.4919 0.7033 0.5914 -0.0727 -0.0507 0.1267  70  ILE A N   
488  C CA  . ILE A 70  ? 0.5309 0.7633 0.6549 -0.0652 -0.0496 0.1435  70  ILE A CA  
489  C C   . ILE A 70  ? 0.7436 0.9761 0.8616 -0.0694 -0.0551 0.1450  70  ILE A C   
490  O O   . ILE A 70  ? 0.6382 0.8940 0.7701 -0.0744 -0.0613 0.1621  70  ILE A O   
491  C CB  . ILE A 70  ? 0.6003 0.8255 0.7392 -0.0459 -0.0359 0.1418  70  ILE A CB  
492  C CG1 . ILE A 70  ? 0.5641 0.7943 0.7130 -0.0425 -0.0302 0.1446  70  ILE A CG1 
493  C CG2 . ILE A 70  ? 0.6171 0.8585 0.7799 -0.0367 -0.0320 0.1576  70  ILE A CG2 
494  C CD1 . ILE A 70  ? 0.6666 0.8935 0.8329 -0.0255 -0.0153 0.1476  70  ILE A CD1 
495  N N   . GLU A 71  ? 0.5630 0.7703 0.6609 -0.0679 -0.0530 0.1283  71  GLU A N   
496  C CA  . GLU A 71  ? 0.5832 0.7877 0.6739 -0.0713 -0.0572 0.1280  71  GLU A CA  
497  C C   . GLU A 71  ? 0.5872 0.8016 0.6648 -0.0921 -0.0690 0.1339  71  GLU A C   
498  O O   . GLU A 71  ? 0.6236 0.8491 0.7038 -0.0973 -0.0748 0.1430  71  GLU A O   
499  C CB  . GLU A 71  ? 0.5350 0.7102 0.6073 -0.0657 -0.0519 0.1091  71  GLU A CB  
500  C CG  . GLU A 71  ? 0.6230 0.7906 0.7064 -0.0478 -0.0423 0.1063  71  GLU A CG  
501  C CD  . GLU A 71  ? 0.6650 0.8064 0.7308 -0.0441 -0.0385 0.0896  71  GLU A CD  
502  O OE1 . GLU A 71  ? 0.7039 0.8333 0.7512 -0.0540 -0.0423 0.0811  71  GLU A OE1 
503  O OE2 . GLU A 71  ? 0.5843 0.7168 0.6548 -0.0318 -0.0309 0.0857  71  GLU A OE2 
504  N N   . GLN A 72  ? 0.6587 0.8689 0.7212 -0.1055 -0.0725 0.1292  72  GLN A N   
505  C CA  . GLN A 72  ? 0.6286 0.8449 0.6737 -0.1284 -0.0828 0.1337  72  GLN A CA  
506  C C   . GLN A 72  ? 0.7837 1.0355 0.8479 -0.1373 -0.0921 0.1570  72  GLN A C   
507  O O   . GLN A 72  ? 0.7197 0.9801 0.7693 -0.1591 -0.1022 0.1633  72  GLN A O   
508  C CB  . GLN A 72  ? 0.6778 0.8758 0.6994 -0.1403 -0.0818 0.1212  72  GLN A CB  
509  C CG  . GLN A 72  ? 0.7583 0.9223 0.7554 -0.1402 -0.0752 0.1014  72  GLN A CG  
510  C CD  . GLN A 72  ? 1.0767 1.2222 1.0604 -0.1431 -0.0698 0.0897  72  GLN A CD  
511  O OE1 . GLN A 72  ? 1.0712 1.2169 1.0679 -0.1300 -0.0647 0.0877  72  GLN A OE1 
512  N NE2 . GLN A 72  ? 1.1645 1.2923 1.1210 -0.1609 -0.0698 0.0819  72  GLN A NE2 
513  N N   . THR A 73  ? 0.7963 1.0686 0.8921 -0.1222 -0.0885 0.1707  73  THR A N   
514  C CA  . THR A 73  ? 0.8241 1.1330 0.9435 -0.1288 -0.0963 0.1961  73  THR A CA  
515  C C   . THR A 73  ? 0.7230 1.0498 0.8640 -0.1212 -0.0974 0.2118  73  THR A C   
516  O O   . THR A 73  ? 0.8380 1.1974 0.9981 -0.1294 -0.1058 0.2355  73  THR A O   
517  C CB  . THR A 73  ? 0.7262 1.0490 0.8699 -0.1181 -0.0904 0.2047  73  THR A CB  
518  O OG1 . THR A 73  ? 0.7371 1.0586 0.9050 -0.0943 -0.0779 0.2068  73  THR A OG1 
519  C CG2 . THR A 73  ? 0.7072 1.0078 0.8308 -0.1208 -0.0867 0.1865  73  THR A CG2 
520  N N   . LEU A 74  ? 0.7426 1.0503 0.8823 -0.1061 -0.0891 0.2007  74  LEU A N   
521  C CA  . LEU A 74  ? 0.7978 1.1190 0.9518 -0.1021 -0.0911 0.2137  74  LEU A CA  
522  C C   . LEU A 74  ? 0.8101 1.1372 0.9433 -0.1256 -0.1052 0.2174  74  LEU A C   
523  O O   . LEU A 74  ? 0.7213 1.0237 0.8213 -0.1374 -0.1073 0.1989  74  LEU A O   
524  C CB  . LEU A 74  ? 0.7645 1.0609 0.9163 -0.0836 -0.0798 0.1989  74  LEU A CB  
525  C CG  . LEU A 74  ? 0.7806 1.0690 0.9512 -0.0611 -0.0645 0.1958  74  LEU A CG  
526  C CD1 . LEU A 74  ? 0.6788 0.9384 0.8283 -0.0580 -0.0583 0.1730  74  LEU A CD1 
527  C CD2 . LEU A 74  ? 0.7706 1.0532 0.9521 -0.0461 -0.0565 0.1970  74  LEU A CD2 
528  N N   . GLN A 75  ? 0.7846 1.1445 0.9375 -0.1329 -0.1141 0.2422  75  GLN A N   
529  C CA  . GLN A 75  ? 0.7827 1.1488 0.9140 -0.1577 -0.1274 0.2478  75  GLN A CA  
530  C C   . GLN A 75  ? 0.6548 1.0050 0.7731 -0.1555 -0.1271 0.2380  75  GLN A C   
531  O O   . GLN A 75  ? 0.6637 1.0189 0.8046 -0.1373 -0.1210 0.2444  75  GLN A O   
532  C CB  . GLN A 75  ? 0.7778 1.1696 0.9261 -0.1637 -0.1301 0.2749  75  GLN A CB  
533  C CG  . GLN A 75  ? 0.9150 1.3207 1.0771 -0.1632 -0.1285 0.2857  75  GLN A CG  
534  C CD  . GLN A 75  ? 1.1441 1.5523 1.2801 -0.1902 -0.1380 0.2910  75  GLN A CD  
535  O OE1 . GLN A 75  ? 1.1103 1.4980 1.2101 -0.2078 -0.1427 0.2738  75  GLN A OE1 
536  N NE2 . GLN A 75  ? 1.0002 1.4320 1.1534 -0.1938 -0.1398 0.3153  75  GLN A NE2 
537  N N   . THR A 76  ? 0.6606 0.9872 0.7407 -0.1732 -0.1312 0.2212  76  THR A N   
538  C CA  . THR A 76  ? 0.7566 1.0650 0.8191 -0.1745 -0.1307 0.2111  76  THR A CA  
539  C C   . THR A 76  ? 0.8141 1.1245 0.8487 -0.2039 -0.1417 0.2157  76  THR A C   
540  O O   . THR A 76  ? 0.7186 1.0259 0.7341 -0.2225 -0.1444 0.2156  76  THR A O   
541  C CB  . THR A 76  ? 0.7462 1.0130 0.7855 -0.1645 -0.1190 0.1820  76  THR A CB  
542  O OG1 . THR A 76  ? 0.7009 0.9493 0.7103 -0.1817 -0.1198 0.1688  76  THR A OG1 
543  C CG2 . THR A 76  ? 0.5756 0.8360 0.6375 -0.1373 -0.1066 0.1762  76  THR A CG2 
544  N N   . THR A 77  ? 0.7134 1.0218 0.7430 -0.2064 -0.1436 0.2181  77  THR A N   
545  C CA  . THR A 77  ? 0.8378 1.1374 0.8361 -0.2323 -0.1484 0.2185  77  THR A CA  
546  C C   . THR A 77  ? 0.8428 1.1078 0.8050 -0.2400 -0.1459 0.1945  77  THR A C   
547  O O   . THR A 77  ? 0.8185 1.0680 0.7477 -0.2633 -0.1470 0.1901  77  THR A O   
548  C CB  . THR A 77  ? 0.8303 1.1526 0.8472 -0.2334 -0.1520 0.2401  77  THR A CB  
549  O OG1 . THR A 77  ? 0.8094 1.1372 0.8535 -0.2084 -0.1479 0.2414  77  THR A OG1 
550  C CG2 . THR A 77  ? 0.8302 1.1830 0.8709 -0.2372 -0.1548 0.2657  77  THR A CG2 
551  N N   . SER A 78  ? 0.6284 0.8755 0.5950 -0.2195 -0.1382 0.1783  78  SER A N   
552  C CA  . SER A 78  ? 0.6095 0.8186 0.5457 -0.2211 -0.1300 0.1555  78  SER A CA  
553  C C   . SER A 78  ? 0.6238 0.8061 0.5609 -0.2011 -0.1161 0.1358  78  SER A C   
554  O O   . SER A 78  ? 0.4937 0.6869 0.4573 -0.1823 -0.1124 0.1395  78  SER A O   
555  C CB  . SER A 78  ? 0.7490 0.9586 0.6918 -0.2125 -0.1301 0.1579  78  SER A CB  
556  O OG  . SER A 78  ? 0.5521 0.7769 0.5320 -0.1853 -0.1259 0.1658  78  SER A OG  
557  N N   . GLN A 79  ? 0.4864 0.6331 0.3943 -0.2058 -0.1077 0.1154  79  GLN A N   
558  C CA  . GLN A 79  ? 0.4786 0.6008 0.3888 -0.1864 -0.0947 0.0983  79  GLN A CA  
559  C C   . GLN A 79  ? 0.5601 0.6821 0.4918 -0.1617 -0.0897 0.0967  79  GLN A C   
560  O O   . GLN A 79  ? 0.4982 0.6106 0.4414 -0.1431 -0.0813 0.0884  79  GLN A O   
561  C CB  . GLN A 79  ? 0.5849 0.6699 0.4608 -0.1979 -0.0858 0.0795  79  GLN A CB  
562  C CG  . GLN A 79  ? 0.6493 0.7256 0.5040 -0.2172 -0.0853 0.0760  79  GLN A CG  
563  C CD  . GLN A 79  ? 0.5859 0.6817 0.4625 -0.2089 -0.0879 0.0833  79  GLN A CD  
564  O OE1 . GLN A 79  ? 0.5226 0.6076 0.4095 -0.1916 -0.0794 0.0746  79  GLN A OE1 
565  N NE2 . GLN A 79  ? 0.6078 0.7330 0.4914 -0.2222 -0.0999 0.1003  79  GLN A NE2 
566  N N   . PHE A 80  ? 0.4662 0.5982 0.4020 -0.1626 -0.0947 0.1046  80  PHE A N   
567  C CA  . PHE A 80  ? 0.4166 0.5512 0.3738 -0.1403 -0.0904 0.1054  80  PHE A CA  
568  C C   . PHE A 80  ? 0.5402 0.6961 0.5297 -0.1229 -0.0893 0.1162  80  PHE A C   
569  O O   . PHE A 80  ? 0.4501 0.5965 0.4516 -0.1032 -0.0805 0.1089  80  PHE A O   
570  C CB  . PHE A 80  ? 0.5183 0.6640 0.4748 -0.1474 -0.0973 0.1152  80  PHE A CB  
571  C CG  . PHE A 80  ? 0.6442 0.7862 0.6155 -0.1275 -0.0920 0.1133  80  PHE A CG  
572  C CD1 . PHE A 80  ? 0.6320 0.7451 0.5891 -0.1204 -0.0834 0.0957  80  PHE A CD1 
573  C CD2 . PHE A 80  ? 0.7807 0.9483 0.7800 -0.1173 -0.0953 0.1304  80  PHE A CD2 
574  C CE1 . PHE A 80  ? 0.7577 0.8676 0.7269 -0.1039 -0.0791 0.0941  80  PHE A CE1 
575  C CE2 . PHE A 80  ? 0.7750 0.9373 0.7858 -0.1003 -0.0896 0.1283  80  PHE A CE2 
576  C CZ  . PHE A 80  ? 0.7573 0.8908 0.7520 -0.0942 -0.0821 0.1097  80  PHE A CZ  
577  N N   . GLN A 81  ? 0.4753 0.6595 0.4784 -0.1312 -0.0975 0.1341  81  GLN A N   
578  C CA  . GLN A 81  ? 0.4769 0.6813 0.5110 -0.1160 -0.0950 0.1457  81  GLN A CA  
579  C C   . GLN A 81  ? 0.4637 0.6530 0.4953 -0.1082 -0.0872 0.1329  81  GLN A C   
580  O O   . GLN A 81  ? 0.3936 0.5817 0.4433 -0.0892 -0.0789 0.1314  81  GLN A O   
581  C CB  . GLN A 81  ? 0.4637 0.7026 0.5121 -0.1291 -0.1060 0.1690  81  GLN A CB  
582  C CG  . GLN A 81  ? 0.7556 1.0230 0.8382 -0.1175 -0.1071 0.1909  81  GLN A CG  
583  C CD  . GLN A 81  ? 0.9989 1.3028 1.1000 -0.1295 -0.1172 0.2160  81  GLN A CD  
584  O OE1 . GLN A 81  ? 0.8428 1.1597 0.9301 -0.1528 -0.1298 0.2252  81  GLN A OE1 
585  N NE2 . GLN A 81  ? 0.8426 1.1629 0.9741 -0.1147 -0.1114 0.2276  81  GLN A NE2 
586  N N   . ARG A 82  ? 0.3771 0.5540 0.3854 -0.1236 -0.0891 0.1239  82  ARG A N   
587  C CA  . ARG A 82  ? 0.4357 0.5997 0.4425 -0.1169 -0.0822 0.1131  82  ARG A CA  
588  C C   . ARG A 82  ? 0.4074 0.5454 0.4103 -0.1008 -0.0717 0.0964  82  ARG A C   
589  O O   . ARG A 82  ? 0.4448 0.5779 0.4566 -0.0886 -0.0653 0.0914  82  ARG A O   
590  C CB  . ARG A 82  ? 0.4658 0.6198 0.4477 -0.1371 -0.0851 0.1070  82  ARG A CB  
591  C CG  . ARG A 82  ? 0.7078 0.8632 0.6963 -0.1331 -0.0818 0.1052  82  ARG A CG  
592  C CD  . ARG A 82  ? 0.7336 0.8926 0.7050 -0.1556 -0.0880 0.1080  82  ARG A CD  
593  N NE  . ARG A 82  ? 1.0378 1.1673 0.9762 -0.1697 -0.0843 0.0929  82  ARG A NE  
594  C CZ  . ARG A 82  ? 1.0354 1.1473 0.9557 -0.1789 -0.0799 0.0831  82  ARG A CZ  
595  N NH1 . ARG A 82  ? 0.9501 1.0720 0.8810 -0.1763 -0.0802 0.0865  82  ARG A NH1 
596  N NH2 . ARG A 82  ? 0.7736 0.8561 0.6646 -0.1906 -0.0738 0.0699  82  ARG A NH2 
597  N N   . LEU A 83  ? 0.4206 0.5425 0.4102 -0.1014 -0.0700 0.0883  83  LEU A N   
598  C CA  . LEU A 83  ? 0.3449 0.4449 0.3327 -0.0867 -0.0609 0.0747  83  LEU A CA  
599  C C   . LEU A 83  ? 0.3810 0.4902 0.3922 -0.0677 -0.0568 0.0796  83  LEU A C   
600  O O   . LEU A 83  ? 0.3477 0.4456 0.3623 -0.0560 -0.0497 0.0716  83  LEU A O   
601  C CB  . LEU A 83  ? 0.4281 0.5102 0.3980 -0.0919 -0.0597 0.0665  83  LEU A CB  
602  C CG  . LEU A 83  ? 0.4395 0.4975 0.3834 -0.1046 -0.0559 0.0544  83  LEU A CG  
603  C CD1 . LEU A 83  ? 0.4058 0.4460 0.3350 -0.1073 -0.0529 0.0472  83  LEU A CD1 
604  C CD2 . LEU A 83  ? 0.4165 0.4598 0.3617 -0.0955 -0.0478 0.0447  83  LEU A CD2 
605  N N   . PHE A 84  ? 0.3350 0.4639 0.3617 -0.0654 -0.0606 0.0933  84  PHE A N   
606  C CA  . PHE A 84  ? 0.4607 0.5968 0.5096 -0.0479 -0.0543 0.0991  84  PHE A CA  
607  C C   . PHE A 84  ? 0.3919 0.5326 0.4527 -0.0410 -0.0493 0.1005  84  PHE A C   
608  O O   . PHE A 84  ? 0.4302 0.5614 0.4972 -0.0276 -0.0405 0.0952  84  PHE A O   
609  C CB  . PHE A 84  ? 0.3929 0.5526 0.4600 -0.0476 -0.0586 0.1172  84  PHE A CB  
610  C CG  . PHE A 84  ? 0.5280 0.6818 0.5898 -0.0468 -0.0597 0.1158  84  PHE A CG  
611  C CD1 . PHE A 84  ? 0.6680 0.8093 0.7348 -0.0317 -0.0511 0.1098  84  PHE A CD1 
612  C CD2 . PHE A 84  ? 0.6822 0.8424 0.7323 -0.0625 -0.0692 0.1206  84  PHE A CD2 
613  C CE1 . PHE A 84  ? 0.6154 0.7515 0.6775 -0.0309 -0.0522 0.1086  84  PHE A CE1 
614  C CE2 . PHE A 84  ? 0.7746 0.9293 0.8196 -0.0620 -0.0701 0.1194  84  PHE A CE2 
615  C CZ  . PHE A 84  ? 0.7620 0.9051 0.8139 -0.0456 -0.0617 0.1135  84  PHE A CZ  
616  N N   . ILE A 85  ? 0.3353 0.4900 0.3979 -0.0511 -0.0548 0.1079  85  ILE A N   
617  C CA  . ILE A 85  ? 0.3360 0.4959 0.4098 -0.0455 -0.0503 0.1099  85  ILE A CA  
618  C C   . ILE A 85  ? 0.3408 0.4772 0.3993 -0.0429 -0.0450 0.0927  85  ILE A C   
619  O O   . ILE A 85  ? 0.3832 0.5135 0.4486 -0.0315 -0.0371 0.0890  85  ILE A O   
620  C CB  . ILE A 85  ? 0.3390 0.5206 0.4175 -0.0587 -0.0586 0.1226  85  ILE A CB  
621  C CG1 . ILE A 85  ? 0.3456 0.5555 0.4468 -0.0587 -0.0629 0.1441  85  ILE A CG1 
622  C CG2 . ILE A 85  ? 0.4159 0.5987 0.5008 -0.0549 -0.0542 0.1214  85  ILE A CG2 
623  C CD1 . ILE A 85  ? 0.4262 0.6604 0.5306 -0.0755 -0.0737 0.1590  85  ILE A CD1 
624  N N   . LEU A 86  ? 0.3543 0.4769 0.3917 -0.0540 -0.0485 0.0828  86  LEU A N   
625  C CA  . LEU A 86  ? 0.3370 0.4391 0.3625 -0.0518 -0.0434 0.0690  86  LEU A CA  
626  C C   . LEU A 86  ? 0.4185 0.5058 0.4445 -0.0390 -0.0366 0.0608  86  LEU A C   
627  O O   . LEU A 86  ? 0.4316 0.5088 0.4563 -0.0335 -0.0316 0.0540  86  LEU A O   
628  C CB  . LEU A 86  ? 0.4415 0.5295 0.4453 -0.0656 -0.0459 0.0611  86  LEU A CB  
629  C CG  . LEU A 86  ? 0.5026 0.5988 0.4990 -0.0813 -0.0514 0.0656  86  LEU A CG  
630  C CD1 . LEU A 86  ? 0.5390 0.6167 0.5106 -0.0958 -0.0515 0.0574  86  LEU A CD1 
631  C CD2 . LEU A 86  ? 0.5554 0.6525 0.5569 -0.0784 -0.0485 0.0642  86  LEU A CD2 
632  N N   . LEU A 87  ? 0.3892 0.4755 0.4164 -0.0353 -0.0367 0.0620  87  LEU A N   
633  C CA  . LEU A 87  ? 0.3868 0.4594 0.4133 -0.0247 -0.0307 0.0548  87  LEU A CA  
634  C C   . LEU A 87  ? 0.5517 0.6303 0.5932 -0.0130 -0.0246 0.0599  87  LEU A C   
635  O O   . LEU A 87  ? 0.4861 0.5532 0.5255 -0.0056 -0.0193 0.0545  87  LEU A O   
636  C CB  . LEU A 87  ? 0.3463 0.4120 0.3649 -0.0266 -0.0327 0.0522  87  LEU A CB  
637  C CG  . LEU A 87  ? 0.3726 0.4246 0.3735 -0.0368 -0.0347 0.0445  87  LEU A CG  
638  C CD1 . LEU A 87  ? 0.3667 0.4141 0.3602 -0.0402 -0.0367 0.0437  87  LEU A CD1 
639  C CD2 . LEU A 87  ? 0.4166 0.4519 0.4120 -0.0325 -0.0292 0.0348  87  LEU A CD2 
640  N N   . GLY A 88  ? 0.4733 0.5684 0.5293 -0.0118 -0.0241 0.0706  88  GLY A N   
641  C CA  . GLY A 88  ? 0.4679 0.5657 0.5380 -0.0007 -0.0150 0.0754  88  GLY A CA  
642  C C   . GLY A 88  ? 0.5064 0.6103 0.5883 0.0062  -0.0117 0.0838  88  GLY A C   
643  O O   . GLY A 88  ? 0.5481 0.6481 0.6390 0.0161  -0.0012 0.0859  88  GLY A O   
644  N N   . ALA A 89  ? 0.4876 0.5997 0.5692 0.0008  -0.0194 0.0889  89  ALA A N   
645  C CA  . ALA A 89  ? 0.5380 0.6558 0.6309 0.0072  -0.0166 0.0972  89  ALA A CA  
646  C C   . ALA A 89  ? 0.6099 0.7509 0.7279 0.0110  -0.0146 0.1163  89  ALA A C   
647  O O   . ALA A 89  ? 0.6173 0.7645 0.7485 0.0176  -0.0108 0.1258  89  ALA A O   
648  C CB  . ALA A 89  ? 0.5071 0.6247 0.5892 -0.0010 -0.0258 0.0958  89  ALA A CB  
649  N N   . GLU A 90  ? 0.6758 0.8303 0.8023 0.0074  -0.0163 0.1235  90  GLU A N   
650  C CA  . GLU A 90  ? 0.6227 0.8032 0.7756 0.0096  -0.0158 0.1446  90  GLU A CA  
651  C C   . GLU A 90  ? 0.7817 0.9628 0.9510 0.0205  -0.0024 0.1495  90  GLU A C   
652  O O   . GLU A 90  ? 0.9310 1.1340 1.1259 0.0240  0.0003  0.1686  90  GLU A O   
653  C CB  . GLU A 90  ? 0.5840 0.7853 0.7359 -0.0062 -0.0302 0.1536  90  GLU A CB  
654  C CG  . GLU A 90  ? 0.6189 0.8260 0.7609 -0.0176 -0.0419 0.1562  90  GLU A CG  
655  C CD  . GLU A 90  ? 0.8911 1.1274 1.0573 -0.0188 -0.0464 0.1803  90  GLU A CD  
656  O OE1 . GLU A 90  ? 0.9046 1.1520 1.0976 -0.0057 -0.0367 0.1939  90  GLU A OE1 
657  O OE2 . GLU A 90  ? 0.9774 1.2253 1.1357 -0.0335 -0.0589 0.1865  90  GLU A OE2 
658  N N   . ASN A 91  ? 0.6881 0.8462 0.8438 0.0251  0.0062  0.1337  91  ASN A N   
659  C CA  . ASN A 91  ? 0.9335 1.0852 1.0990 0.0348  0.0214  0.1349  91  ASN A CA  
660  C C   . ASN A 91  ? 0.9204 1.0959 1.1114 0.0365  0.0237  0.1534  91  ASN A C   
661  O O   . ASN A 91  ? 0.9505 1.1304 1.1632 0.0476  0.0376  0.1655  91  ASN A O   
662  C CB  . ASN A 91  ? 0.9678 1.1023 1.1354 0.0467  0.0367  0.1325  91  ASN A CB  
663  C CG  . ASN A 91  ? 1.0144 1.1653 1.2088 0.0549  0.0425  0.1520  91  ASN A CG  
664  O OD1 . ASN A 91  ? 0.9652 1.1434 1.1809 0.0527  0.0361  0.1704  91  ASN A OD1 
665  N ND2 . ASN A 91  ? 1.0077 1.1418 1.2014 0.0639  0.0553  0.1490  91  ASN A ND2 
666  N N   . ILE A 92  ? 0.8912 1.0808 1.0794 0.0254  0.0114  0.1555  92  ILE A N   
667  C CA  . ILE A 92  ? 0.6821 0.8941 0.8925 0.0255  0.0126  0.1720  92  ILE A CA  
668  C C   . ILE A 92  ? 0.7784 0.9764 0.9935 0.0360  0.0300  0.1680  92  ILE A C   
669  O O   . ILE A 92  ? 0.5875 0.7627 0.7809 0.0349  0.0331  0.1497  92  ILE A O   
670  C CB  . ILE A 92  ? 0.7483 0.9722 0.9482 0.0098  -0.0033 0.1709  92  ILE A CB  
671  C CG1 . ILE A 92  ? 0.7049 0.9355 0.8921 -0.0033 -0.0190 0.1709  92  ILE A CG1 
672  C CG2 . ILE A 92  ? 0.7722 1.0231 0.9965 0.0084  -0.0038 0.1904  92  ILE A CG2 
673  C CD1 . ILE A 92  ? 0.7144 0.9593 0.9178 0.0001  -0.0201 0.1859  92  ILE A CD1 
674  N N   . ASP A 93  ? 0.7736 0.9855 1.0177 0.0457  0.0420  0.1862  93  ASP A N   
675  C CA  . ASP A 93  ? 0.8150 1.0108 1.0634 0.0560  0.0618  0.1830  93  ASP A CA  
676  C C   . ASP A 93  ? 0.6513 0.8456 0.8901 0.0496  0.0587  0.1757  93  ASP A C   
677  O O   . ASP A 93  ? 0.6978 0.8699 0.9249 0.0535  0.0714  0.1638  93  ASP A O   
678  C CB  . ASP A 93  ? 0.8572 1.0690 1.1417 0.0683  0.0769  0.2064  93  ASP A CB  
679  C CG  . ASP A 93  ? 1.0193 1.2296 1.3142 0.0763  0.0830  0.2137  93  ASP A CG  
680  O OD1 . ASP A 93  ? 1.0551 1.2382 1.3418 0.0853  0.1007  0.2041  93  ASP A OD1 
681  O OD2 . ASP A 93  ? 1.0162 1.2521 1.3258 0.0723  0.0701  0.2290  93  ASP A OD2 
682  N N   . ARG A 94  ? 0.6475 0.8646 0.8896 0.0386  0.0422  0.1828  94  ARG A N   
683  C CA  . ARG A 94  ? 0.6660 0.8819 0.8978 0.0315  0.0380  0.1755  94  ARG A CA  
684  C C   . ARG A 94  ? 0.6879 0.8746 0.8870 0.0276  0.0370  0.1508  94  ARG A C   
685  O O   . ARG A 94  ? 0.7837 0.9591 0.9745 0.0276  0.0428  0.1425  94  ARG A O   
686  C CB  . ARG A 94  ? 0.5354 0.7774 0.7702 0.0176  0.0190  0.1851  94  ARG A CB  
687  C CG  . ARG A 94  ? 0.7335 1.0059 0.9991 0.0181  0.0198  0.2087  94  ARG A CG  
688  C CD  . ARG A 94  ? 0.7865 1.0795 1.0463 0.0005  0.0004  0.2138  94  ARG A CD  
689  N NE  . ARG A 94  ? 0.8706 1.1593 1.1217 -0.0042 0.0001  0.2063  94  ARG A NE  
690  C CZ  . ARG A 94  ? 0.7681 1.0649 1.0059 -0.0201 -0.0144 0.2042  94  ARG A CZ  
691  N NH1 . ARG A 94  ? 0.6816 0.9901 0.9109 -0.0342 -0.0297 0.2084  94  ARG A NH1 
692  N NH2 . ARG A 94  ? 0.7149 1.0065 0.9460 -0.0227 -0.0128 0.1975  94  ARG A NH2 
693  N N   . LEU A 95  ? 0.6431 0.8184 0.8245 0.0241  0.0297  0.1401  95  LEU A N   
694  C CA  . LEU A 95  ? 0.5422 0.6953 0.6953 0.0184  0.0253  0.1199  95  LEU A CA  
695  C C   . LEU A 95  ? 0.6212 0.7480 0.7617 0.0256  0.0384  0.1077  95  LEU A C   
696  O O   . LEU A 95  ? 0.7122 0.8219 0.8309 0.0209  0.0351  0.0929  95  LEU A O   
697  C CB  . LEU A 95  ? 0.6139 0.7678 0.7534 0.0095  0.0107  0.1148  95  LEU A CB  
698  C CG  . LEU A 95  ? 0.6406 0.8196 0.7903 0.0006  -0.0019 0.1284  95  LEU A CG  
699  C CD1 . LEU A 95  ? 0.7652 0.9412 0.9031 -0.0053 -0.0112 0.1246  95  LEU A CD1 
700  C CD2 . LEU A 95  ? 0.7254 0.9121 0.8697 -0.0101 -0.0099 0.1280  95  LEU A CD2 
701  N N   . GLN A 96  ? 0.6796 0.8024 0.8330 0.0359  0.0536  0.1144  96  GLN A N   
702  C CA  . GLN A 96  ? 0.6678 0.7632 0.8056 0.0404  0.0669  0.1024  96  GLN A CA  
703  C C   . GLN A 96  ? 0.6728 0.7515 0.7930 0.0362  0.0717  0.0905  96  GLN A C   
704  O O   . GLN A 96  ? 0.5986 0.6573 0.6961 0.0323  0.0715  0.0767  96  GLN A O   
705  C CB  . GLN A 96  ? 0.7744 0.8667 0.9298 0.0520  0.0855  0.1127  96  GLN A CB  
706  C CG  . GLN A 96  ? 0.8142 0.9180 0.9834 0.0563  0.0821  0.1227  96  GLN A CG  
707  C CD  . GLN A 96  ? 0.9780 1.0778 1.1284 0.0490  0.0663  0.1120  96  GLN A CD  
708  O OE1 . GLN A 96  ? 0.9111 0.9891 1.0423 0.0488  0.0699  0.0991  96  GLN A OE1 
709  N NE2 . GLN A 96  ? 0.8890 1.0095 1.0443 0.0420  0.0493  0.1178  96  GLN A NE2 
710  N N   . PRO A 97  ? 0.7328 0.8188 0.8614 0.0360  0.0756  0.0953  97  PRO A N   
711  C CA  . PRO A 97  ? 0.6694 0.7393 0.7784 0.0303  0.0781  0.0832  97  PRO A CA  
712  C C   . PRO A 97  ? 0.5488 0.6202 0.6419 0.0204  0.0606  0.0740  97  PRO A C   
713  O O   . PRO A 97  ? 0.6426 0.6982 0.7162 0.0151  0.0608  0.0629  97  PRO A O   
714  C CB  . PRO A 97  ? 0.6046 0.6846 0.7299 0.0333  0.0865  0.0926  97  PRO A CB  
715  C CG  . PRO A 97  ? 0.6325 0.7403 0.7850 0.0368  0.0805  0.1098  97  PRO A CG  
716  C CD  . PRO A 97  ? 0.6941 0.8057 0.8490 0.0386  0.0743  0.1122  97  PRO A CD  
717  N N   . TYR A 98  ? 0.5481 0.6372 0.6486 0.0170  0.0463  0.0791  98  TYR A N   
718  C CA  . TYR A 98  ? 0.5971 0.6843 0.6825 0.0081  0.0324  0.0705  98  TYR A CA  
719  C C   . TYR A 98  ? 0.6008 0.6719 0.6701 0.0073  0.0306  0.0606  98  TYR A C   
720  O O   . TYR A 98  ? 0.4864 0.5470 0.5402 0.0019  0.0263  0.0515  98  TYR A O   
721  C CB  . TYR A 98  ? 0.3976 0.5044 0.4918 0.0031  0.0197  0.0780  98  TYR A CB  
722  C CG  . TYR A 98  ? 0.5546 0.6787 0.6615 0.0002  0.0177  0.0872  98  TYR A CG  
723  C CD1 . TYR A 98  ? 0.5615 0.7008 0.6904 0.0063  0.0248  0.1014  98  TYR A CD1 
724  C CD2 . TYR A 98  ? 0.4304 0.5560 0.5284 -0.0085 0.0095  0.0829  98  TYR A CD2 
725  C CE1 . TYR A 98  ? 0.6010 0.7581 0.7430 0.0033  0.0225  0.1113  98  TYR A CE1 
726  C CE2 . TYR A 98  ? 0.4569 0.5985 0.5657 -0.0120 0.0074  0.0914  98  TYR A CE2 
727  C CZ  . TYR A 98  ? 0.4601 0.6182 0.5910 -0.0064 0.0133  0.1058  98  TYR A CZ  
728  O OH  . TYR A 98  ? 0.5314 0.7075 0.6746 -0.0102 0.0109  0.1158  98  TYR A OH  
729  N N   . LEU A 99  ? 0.5751 0.6452 0.6493 0.0126  0.0338  0.0635  99  LEU A N   
730  C CA  . LEU A 99  ? 0.5756 0.6311 0.6354 0.0119  0.0324  0.0549  99  LEU A CA  
731  C C   . LEU A 99  ? 0.6215 0.6568 0.6668 0.0120  0.0429  0.0470  99  LEU A C   
732  O O   . LEU A 99  ? 0.5298 0.5534 0.5594 0.0076  0.0393  0.0388  99  LEU A O   
733  C CB  . LEU A 99  ? 0.5601 0.6205 0.6293 0.0173  0.0330  0.0607  99  LEU A CB  
734  C CG  . LEU A 99  ? 0.6551 0.7360 0.7368 0.0149  0.0223  0.0699  99  LEU A CG  
735  C CD1 . LEU A 99  ? 0.6246 0.7114 0.7169 0.0202  0.0238  0.0774  99  LEU A CD1 
736  C CD2 . LEU A 99  ? 0.5457 0.6252 0.6143 0.0060  0.0097  0.0628  99  LEU A CD2 
737  N N   . ARG A 100 ? 0.5034 0.5343 0.5535 0.0161  0.0566  0.0500  100 ARG A N   
738  C CA  . ARG A 100 ? 0.6250 0.6346 0.6573 0.0131  0.0675  0.0419  100 ARG A CA  
739  C C   . ARG A 100 ? 0.5665 0.5728 0.5841 0.0038  0.0597  0.0352  100 ARG A C   
740  O O   . ARG A 100 ? 0.5563 0.5480 0.5549 -0.0027 0.0600  0.0276  100 ARG A O   
741  C CB  . ARG A 100 ? 0.6999 0.7044 0.7406 0.0190  0.0857  0.0470  100 ARG A CB  
742  C CG  . ARG A 100 ? 0.8107 0.7882 0.8313 0.0163  0.1018  0.0391  100 ARG A CG  
743  C CD  . ARG A 100 ? 0.8555 0.8254 0.8738 0.0150  0.1148  0.0392  100 ARG A CD  
744  N NE  . ARG A 100 ? 0.9969 0.9824 1.0197 0.0109  0.1024  0.0406  100 ARG A NE  
745  C CZ  . ARG A 100 ? 0.9393 0.9370 0.9790 0.0149  0.1064  0.0484  100 ARG A CZ  
746  N NH1 . ARG A 100 ? 0.8196 0.8163 0.8751 0.0239  0.1234  0.0567  100 ARG A NH1 
747  N NH2 . ARG A 100 ? 0.8287 0.8397 0.8704 0.0101  0.0940  0.0487  100 ARG A NH2 
748  N N   . LEU A 101 ? 0.5515 0.5723 0.5782 0.0023  0.0522  0.0388  101 LEU A N   
749  C CA  . LEU A 101 ? 0.4951 0.5141 0.5105 -0.0058 0.0448  0.0339  101 LEU A CA  
750  C C   . LEU A 101 ? 0.4541 0.4731 0.4624 -0.0101 0.0324  0.0301  101 LEU A C   
751  O O   . LEU A 101 ? 0.4803 0.4917 0.4754 -0.0167 0.0291  0.0257  101 LEU A O   
752  C CB  . LEU A 101 ? 0.4456 0.4794 0.4729 -0.0062 0.0410  0.0390  101 LEU A CB  
753  C CG  . LEU A 101 ? 0.4779 0.5093 0.4954 -0.0136 0.0367  0.0352  101 LEU A CG  
754  C CD1 . LEU A 101 ? 0.5293 0.5451 0.5329 -0.0169 0.0478  0.0309  101 LEU A CD1 
755  C CD2 . LEU A 101 ? 0.4739 0.5204 0.5036 -0.0140 0.0324  0.0404  101 LEU A CD2 
756  N N   . TRP A 102 ? 0.4213 0.4492 0.4387 -0.0068 0.0259  0.0330  102 TRP A N   
757  C CA  . TRP A 102 ? 0.4007 0.4270 0.4124 -0.0099 0.0164  0.0299  102 TRP A CA  
758  C C   . TRP A 102 ? 0.4566 0.4693 0.4553 -0.0117 0.0188  0.0250  102 TRP A C   
759  O O   . TRP A 102 ? 0.4493 0.4581 0.4397 -0.0170 0.0134  0.0226  102 TRP A O   
760  C CB  . TRP A 102 ? 0.3892 0.4251 0.4107 -0.0069 0.0112  0.0336  102 TRP A CB  
761  C CG  . TRP A 102 ? 0.4095 0.4409 0.4252 -0.0087 0.0046  0.0303  102 TRP A CG  
762  C CD1 . TRP A 102 ? 0.5414 0.5660 0.5532 -0.0062 0.0058  0.0283  102 TRP A CD1 
763  C CD2 . TRP A 102 ? 0.5601 0.5924 0.5737 -0.0133 -0.0026 0.0290  102 TRP A CD2 
764  N NE1 . TRP A 102 ? 0.6836 0.7059 0.6919 -0.0087 -0.0007 0.0262  102 TRP A NE1 
765  C CE2 . TRP A 102 ? 0.5020 0.5280 0.5114 -0.0128 -0.0051 0.0266  102 TRP A CE2 
766  C CE3 . TRP A 102 ? 0.5813 0.6177 0.5959 -0.0177 -0.0060 0.0297  102 TRP A CE3 
767  C CZ2 . TRP A 102 ? 0.4373 0.4603 0.4444 -0.0160 -0.0094 0.0253  102 TRP A CZ2 
768  C CZ3 . TRP A 102 ? 0.6617 0.6941 0.6730 -0.0212 -0.0101 0.0280  102 TRP A CZ3 
769  C CH2 . TRP A 102 ? 0.5789 0.6043 0.5869 -0.0201 -0.0112 0.0260  102 TRP A CH2 
770  N N   . ASN A 103 ? 0.4737 0.4793 0.4709 -0.0077 0.0275  0.0246  103 ASN A N   
771  C CA  . ASN A 103 ? 0.5955 0.5867 0.5776 -0.0112 0.0304  0.0198  103 ASN A CA  
772  C C   . ASN A 103 ? 0.5091 0.4908 0.4760 -0.0197 0.0334  0.0165  103 ASN A C   
773  O O   . ASN A 103 ? 0.5542 0.5293 0.5082 -0.0269 0.0295  0.0141  103 ASN A O   
774  C CB  . ASN A 103 ? 0.5869 0.5702 0.5697 -0.0054 0.0413  0.0200  103 ASN A CB  
775  C CG  . ASN A 103 ? 0.7589 0.7524 0.7560 0.0018  0.0374  0.0243  103 ASN A CG  
776  O OD1 . ASN A 103 ? 0.7616 0.7602 0.7595 0.0005  0.0271  0.0238  103 ASN A OD1 
777  N ND2 . ASN A 103 ? 0.8053 0.8017 0.8143 0.0092  0.0463  0.0296  103 ASN A ND2 
778  N N   . GLU A 104 ? 0.4996 0.4813 0.4678 -0.0199 0.0400  0.0174  104 GLU A N   
779  C CA  . GLU A 104 ? 0.5000 0.4729 0.4525 -0.0294 0.0425  0.0145  104 GLU A CA  
780  C C   . GLU A 104 ? 0.4890 0.4703 0.4409 -0.0357 0.0295  0.0159  104 GLU A C   
781  O O   . GLU A 104 ? 0.4964 0.4717 0.4339 -0.0454 0.0267  0.0149  104 GLU A O   
782  C CB  . GLU A 104 ? 0.5639 0.5358 0.5200 -0.0274 0.0528  0.0156  104 GLU A CB  
783  C CG  . GLU A 104 ? 0.5545 0.5112 0.4899 -0.0378 0.0604  0.0113  104 GLU A CG  
784  C CD  . GLU A 104 ? 0.7231 0.6766 0.6622 -0.0350 0.0731  0.0123  104 GLU A CD  
785  O OE1 . GLU A 104 ? 0.6519 0.6008 0.5796 -0.0434 0.0743  0.0105  104 GLU A OE1 
786  O OE2 . GLU A 104 ? 0.8005 0.7570 0.7551 -0.0246 0.0819  0.0160  104 GLU A OE2 
787  N N   . ALA A 105 ? 0.4393 0.4343 0.4064 -0.0311 0.0220  0.0193  105 ALA A N   
788  C CA  . ALA A 105 ? 0.4308 0.4324 0.3995 -0.0356 0.0118  0.0214  105 ALA A CA  
789  C C   . ALA A 105 ? 0.5742 0.5735 0.5388 -0.0382 0.0059  0.0220  105 ALA A C   
790  O O   . ALA A 105 ? 0.4599 0.4602 0.4202 -0.0451 0.0005  0.0247  105 ALA A O   
791  C CB  . ALA A 105 ? 0.3947 0.4078 0.3782 -0.0307 0.0072  0.0240  105 ALA A CB  
792  N N   . GLU A 106 ? 0.4238 0.4212 0.3912 -0.0328 0.0067  0.0206  106 GLU A N   
793  C CA  . GLU A 106 ? 0.4263 0.4216 0.3909 -0.0346 0.0017  0.0214  106 GLU A CA  
794  C C   . GLU A 106 ? 0.5794 0.5677 0.5286 -0.0445 0.0017  0.0216  106 GLU A C   
795  O O   . GLU A 106 ? 0.5658 0.5572 0.5149 -0.0490 -0.0051 0.0258  106 GLU A O   
796  C CB  . GLU A 106 ? 0.4711 0.4638 0.4388 -0.0277 0.0044  0.0193  106 GLU A CB  
797  C CG  . GLU A 106 ? 0.6205 0.6141 0.5909 -0.0268 -0.0015 0.0206  106 GLU A CG  
798  C CD  . GLU A 106 ? 0.7408 0.7281 0.7075 -0.0234 0.0021  0.0179  106 GLU A CD  
799  O OE1 . GLU A 106 ? 0.8610 0.8497 0.8340 -0.0168 0.0059  0.0171  106 GLU A OE1 
800  O OE2 . GLU A 106 ? 0.8653 0.8470 0.8234 -0.0279 0.0008  0.0178  106 GLU A OE2 
801  N N   . LEU A 107 ? 0.5873 0.5659 0.5232 -0.0490 0.0097  0.0181  107 LEU A N   
802  C CA  . LEU A 107 ? 0.6351 0.6052 0.5516 -0.0617 0.0101  0.0179  107 LEU A CA  
803  C C   . LEU A 107 ? 0.6838 0.6599 0.5973 -0.0709 0.0044  0.0225  107 LEU A C   
804  O O   . LEU A 107 ? 0.7393 0.7141 0.6401 -0.0832 0.0000  0.0259  107 LEU A O   
805  C CB  . LEU A 107 ? 0.7444 0.6977 0.6445 -0.0645 0.0234  0.0116  107 LEU A CB  
806  C CG  . LEU A 107 ? 0.6750 0.6190 0.5736 -0.0582 0.0307  0.0078  107 LEU A CG  
807  C CD1 . LEU A 107 ? 0.7555 0.6786 0.6326 -0.0650 0.0453  0.0021  107 LEU A CD1 
808  C CD2 . LEU A 107 ? 0.7513 0.6987 0.6499 -0.0602 0.0216  0.0100  107 LEU A CD2 
809  N N   . LEU A 108 ? 0.4605 0.4441 0.3853 -0.0662 0.0039  0.0236  108 LEU A N   
810  C CA  . LEU A 108 ? 0.5097 0.4986 0.4320 -0.0744 -0.0004 0.0280  108 LEU A CA  
811  C C   . LEU A 108 ? 0.4326 0.4347 0.3695 -0.0738 -0.0107 0.0363  108 LEU A C   
812  O O   . LEU A 108 ? 0.4894 0.4972 0.4254 -0.0813 -0.0153 0.0422  108 LEU A O   
813  C CB  . LEU A 108 ? 0.5036 0.4931 0.4302 -0.0703 0.0054  0.0253  108 LEU A CB  
814  C CG  . LEU A 108 ? 0.6555 0.6311 0.5681 -0.0722 0.0181  0.0190  108 LEU A CG  
815  C CD1 . LEU A 108 ? 0.6003 0.5801 0.5230 -0.0659 0.0231  0.0184  108 LEU A CD1 
816  C CD2 . LEU A 108 ? 0.6386 0.6040 0.5275 -0.0882 0.0197  0.0184  108 LEU A CD2 
817  N N   . ILE A 109 ? 0.4372 0.4434 0.3875 -0.0651 -0.0135 0.0375  109 ILE A N   
818  C CA  . ILE A 109 ? 0.5901 0.6060 0.5550 -0.0637 -0.0202 0.0457  109 ILE A CA  
819  C C   . ILE A 109 ? 0.4671 0.4877 0.4283 -0.0738 -0.0265 0.0549  109 ILE A C   
820  O O   . ILE A 109 ? 0.5257 0.5557 0.5000 -0.0742 -0.0313 0.0647  109 ILE A O   
821  C CB  . ILE A 109 ? 0.4520 0.4680 0.4292 -0.0533 -0.0198 0.0443  109 ILE A CB  
822  C CG1 . ILE A 109 ? 0.5011 0.5129 0.4729 -0.0535 -0.0202 0.0431  109 ILE A CG1 
823  C CG2 . ILE A 109 ? 0.4349 0.4488 0.4153 -0.0457 -0.0150 0.0372  109 ILE A CG2 
824  C CD1 . ILE A 109 ? 0.4693 0.4804 0.4514 -0.0444 -0.0196 0.0416  109 ILE A CD1 
825  N N   . GLU A 110 ? 0.4162 0.4307 0.3600 -0.0829 -0.0262 0.0531  110 GLU A N   
826  C CA  . GLU A 110 ? 0.4953 0.5156 0.4329 -0.0958 -0.0333 0.0629  110 GLU A CA  
827  C C   . GLU A 110 ? 0.7456 0.7664 0.6683 -0.1102 -0.0350 0.0658  110 GLU A C   
828  O O   . GLU A 110 ? 0.8719 0.8954 0.7825 -0.1249 -0.0405 0.0728  110 GLU A O   
829  C CB  . GLU A 110 ? 0.6428 0.6555 0.5666 -0.1008 -0.0327 0.0599  110 GLU A CB  
830  C CG  . GLU A 110 ? 0.6839 0.6965 0.6203 -0.0890 -0.0321 0.0582  110 GLU A CG  
831  C CD  . GLU A 110 ? 0.9547 0.9551 0.8744 -0.0919 -0.0280 0.0508  110 GLU A CD  
832  O OE1 . GLU A 110 ? 0.9323 0.9276 0.8578 -0.0806 -0.0236 0.0443  110 GLU A OE1 
833  O OE2 . GLU A 110 ? 1.0349 1.0302 0.9345 -0.1066 -0.0288 0.0516  110 GLU A OE2 
834  N N   . GLN A 111 ? 0.5869 0.6055 0.5094 -0.1076 -0.0307 0.0612  111 GLN A N   
835  C CA  . GLN A 111 ? 0.6972 0.7167 0.6061 -0.1217 -0.0327 0.0648  111 GLN A CA  
836  C C   . GLN A 111 ? 0.6370 0.6605 0.5562 -0.1159 -0.0308 0.0643  111 GLN A C   
837  O O   . GLN A 111 ? 0.5207 0.5468 0.4316 -0.1265 -0.0329 0.0683  111 GLN A O   
838  C CB  . GLN A 111 ? 0.7482 0.7506 0.6277 -0.1331 -0.0253 0.0555  111 GLN A CB  
839  C CG  . GLN A 111 ? 0.7751 0.7637 0.6509 -0.1230 -0.0126 0.0424  111 GLN A CG  
840  C CD  . GLN A 111 ? 0.9109 0.8807 0.7645 -0.1281 -0.0031 0.0335  111 GLN A CD  
841  O OE1 . GLN A 111 ? 1.0128 0.9675 0.8483 -0.1337 0.0076  0.0263  111 GLN A OE1 
842  N NE2 . GLN A 111 ? 0.8363 0.8057 0.6912 -0.1262 -0.0056 0.0341  111 GLN A NE2 
843  N N   . ASP A 112 ? 0.5139 0.5384 0.4500 -0.1005 -0.0274 0.0600  112 ASP A N   
844  C CA  . ASP A 112 ? 0.5508 0.5790 0.4967 -0.0952 -0.0257 0.0595  112 ASP A CA  
845  C C   . ASP A 112 ? 0.4849 0.5214 0.4536 -0.0848 -0.0285 0.0650  112 ASP A C   
846  O O   . ASP A 112 ? 0.4495 0.4830 0.4255 -0.0750 -0.0259 0.0604  112 ASP A O   
847  C CB  . ASP A 112 ? 0.4760 0.4949 0.4166 -0.0889 -0.0166 0.0480  112 ASP A CB  
848  C CG  . ASP A 112 ? 0.5790 0.6015 0.5248 -0.0874 -0.0150 0.0478  112 ASP A CG  
849  O OD1 . ASP A 112 ? 0.4839 0.5144 0.4458 -0.0817 -0.0184 0.0522  112 ASP A OD1 
850  O OD2 . ASP A 112 ? 0.5789 0.5950 0.5119 -0.0926 -0.0094 0.0434  112 ASP A OD2 
851  N N   . ILE A 113 ? 0.4549 0.5006 0.4340 -0.0876 -0.0328 0.0752  113 ILE A N   
852  C CA  . ILE A 113 ? 0.4805 0.5314 0.4806 -0.0789 -0.0332 0.0817  113 ILE A CA  
853  C C   . ILE A 113 ? 0.4908 0.5362 0.4964 -0.0690 -0.0274 0.0729  113 ILE A C   
854  O O   . ILE A 113 ? 0.4176 0.4605 0.4337 -0.0611 -0.0249 0.0724  113 ILE A O   
855  C CB  . ILE A 113 ? 0.5813 0.6432 0.5925 -0.0841 -0.0376 0.0963  113 ILE A CB  
856  C CG1 . ILE A 113 ? 0.7498 0.8199 0.7532 -0.0978 -0.0452 0.1069  113 ILE A CG1 
857  C CG2 . ILE A 113 ? 0.7218 0.7864 0.7552 -0.0750 -0.0354 0.1044  113 ILE A CG2 
858  C CD1 . ILE A 113 ? 0.7216 0.7887 0.7021 -0.1109 -0.0466 0.1023  113 ILE A CD1 
859  N N   . GLU A 114 ? 0.3960 0.4391 0.3939 -0.0704 -0.0248 0.0663  114 GLU A N   
860  C CA  . GLU A 114 ? 0.3322 0.3724 0.3354 -0.0629 -0.0205 0.0596  114 GLU A CA  
861  C C   . GLU A 114 ? 0.3964 0.4314 0.3962 -0.0571 -0.0175 0.0513  114 GLU A C   
862  O O   . GLU A 114 ? 0.3342 0.3676 0.3404 -0.0513 -0.0156 0.0484  114 GLU A O   
863  C CB  . GLU A 114 ? 0.4563 0.4977 0.4546 -0.0659 -0.0187 0.0569  114 GLU A CB  
864  C CG  . GLU A 114 ? 0.4882 0.5351 0.4881 -0.0728 -0.0220 0.0653  114 GLU A CG  
865  C CD  . GLU A 114 ? 0.5602 0.6102 0.5760 -0.0693 -0.0226 0.0734  114 GLU A CD  
866  O OE1 . GLU A 114 ? 0.5536 0.5995 0.5756 -0.0630 -0.0187 0.0695  114 GLU A OE1 
867  O OE2 . GLU A 114 ? 0.7368 0.7931 0.7586 -0.0737 -0.0262 0.0847  114 GLU A OE2 
868  N N   . ILE A 115 ? 0.3218 0.3534 0.3106 -0.0595 -0.0166 0.0476  115 ILE A N   
869  C CA  . ILE A 115 ? 0.3412 0.3685 0.3284 -0.0536 -0.0134 0.0413  115 ILE A CA  
870  C C   . ILE A 115 ? 0.4166 0.4431 0.4099 -0.0500 -0.0158 0.0434  115 ILE A C   
871  O O   . ILE A 115 ? 0.3662 0.3908 0.3633 -0.0440 -0.0142 0.0397  115 ILE A O   
872  C CB  . ILE A 115 ? 0.3711 0.3923 0.3445 -0.0572 -0.0094 0.0370  115 ILE A CB  
873  C CG1 . ILE A 115 ? 0.4305 0.4508 0.3997 -0.0587 -0.0042 0.0341  115 ILE A CG1 
874  C CG2 . ILE A 115 ? 0.4496 0.4666 0.4232 -0.0508 -0.0060 0.0323  115 ILE A CG2 
875  C CD1 . ILE A 115 ? 0.6068 0.6307 0.5858 -0.0507 -0.0009 0.0314  115 ILE A CD1 
876  N N   . GLN A 116 ? 0.4351 0.4639 0.4303 -0.0541 -0.0197 0.0507  116 GLN A N   
877  C CA  . GLN A 116 ? 0.3574 0.3860 0.3609 -0.0503 -0.0210 0.0544  116 GLN A CA  
878  C C   . GLN A 116 ? 0.3784 0.4051 0.3928 -0.0440 -0.0182 0.0540  116 GLN A C   
879  O O   . GLN A 116 ? 0.4253 0.4475 0.4419 -0.0391 -0.0163 0.0507  116 GLN A O   
880  C CB  . GLN A 116 ? 0.3710 0.4055 0.3783 -0.0562 -0.0257 0.0655  116 GLN A CB  
881  C CG  . GLN A 116 ? 0.4754 0.5099 0.4896 -0.0532 -0.0268 0.0699  116 GLN A CG  
882  C CD  . GLN A 116 ? 0.6988 0.7347 0.7306 -0.0478 -0.0244 0.0776  116 GLN A CD  
883  O OE1 . GLN A 116 ? 0.5943 0.6332 0.6336 -0.0483 -0.0233 0.0827  116 GLN A OE1 
884  N NE2 . GLN A 116 ? 0.5587 0.5911 0.5971 -0.0424 -0.0222 0.0785  116 GLN A NE2 
885  N N   . LYS A 117 ? 0.3378 0.3665 0.3575 -0.0452 -0.0173 0.0571  117 LYS A N   
886  C CA  . LYS A 117 ? 0.3699 0.3938 0.3967 -0.0412 -0.0130 0.0562  117 LYS A CA  
887  C C   . LYS A 117 ? 0.3892 0.4098 0.4099 -0.0394 -0.0112 0.0469  117 LYS A C   
888  O O   . LYS A 117 ? 0.3613 0.3757 0.3828 -0.0372 -0.0082 0.0441  117 LYS A O   
889  C CB  . LYS A 117 ? 0.3601 0.3861 0.3931 -0.0435 -0.0118 0.0620  117 LYS A CB  
890  C CG  . LYS A 117 ? 0.4329 0.4633 0.4773 -0.0445 -0.0127 0.0747  117 LYS A CG  
891  C CD  . LYS A 117 ? 0.5357 0.5682 0.5879 -0.0460 -0.0106 0.0813  117 LYS A CD  
892  C CE  . LYS A 117 ? 0.5618 0.5991 0.6046 -0.0512 -0.0140 0.0772  117 LYS A CE  
893  N NZ  . LYS A 117 ? 0.6651 0.7066 0.7157 -0.0538 -0.0135 0.0857  117 LYS A NZ  
894  N N   . ALA A 118 ? 0.3634 0.3883 0.3780 -0.0411 -0.0124 0.0431  118 ALA A N   
895  C CA  . ALA A 118 ? 0.3285 0.3540 0.3406 -0.0398 -0.0112 0.0374  118 ALA A CA  
896  C C   . ALA A 118 ? 0.3209 0.3445 0.3311 -0.0364 -0.0113 0.0342  118 ALA A C   
897  O O   . ALA A 118 ? 0.3338 0.3568 0.3438 -0.0358 -0.0108 0.0317  118 ALA A O   
898  C CB  . ALA A 118 ? 0.3610 0.3921 0.3700 -0.0414 -0.0110 0.0360  118 ALA A CB  
899  N N   . TYR A 119 ? 0.3074 0.3300 0.3149 -0.0353 -0.0121 0.0346  119 TYR A N   
900  C CA  . TYR A 119 ? 0.3517 0.3720 0.3575 -0.0318 -0.0119 0.0319  119 TYR A CA  
901  C C   . TYR A 119 ? 0.3704 0.3856 0.3794 -0.0304 -0.0116 0.0321  119 TYR A C   
902  O O   . TYR A 119 ? 0.3444 0.3584 0.3522 -0.0288 -0.0113 0.0292  119 TYR A O   
903  C CB  . TYR A 119 ? 0.3454 0.3639 0.3461 -0.0325 -0.0123 0.0324  119 TYR A CB  
904  C CG  . TYR A 119 ? 0.4098 0.4254 0.4081 -0.0288 -0.0113 0.0293  119 TYR A CG  
905  C CD1 . TYR A 119 ? 0.4112 0.4273 0.4069 -0.0265 -0.0080 0.0265  119 TYR A CD1 
906  C CD2 . TYR A 119 ? 0.3506 0.3628 0.3506 -0.0271 -0.0127 0.0302  119 TYR A CD2 
907  C CE1 . TYR A 119 ? 0.3747 0.3883 0.3694 -0.0227 -0.0065 0.0246  119 TYR A CE1 
908  C CE2 . TYR A 119 ? 0.4025 0.4121 0.4002 -0.0238 -0.0119 0.0274  119 TYR A CE2 
909  C CZ  . TYR A 119 ? 0.4384 0.4488 0.4334 -0.0217 -0.0090 0.0247  119 TYR A CZ  
910  O OH  . TYR A 119 ? 0.4098 0.4177 0.4037 -0.0181 -0.0076 0.0229  119 TYR A OH  
911  N N   . ASN A 120 ? 0.3359 0.3479 0.3493 -0.0312 -0.0109 0.0364  120 ASN A N   
912  C CA  . ASN A 120 ? 0.3056 0.3099 0.3220 -0.0296 -0.0077 0.0368  120 ASN A CA  
913  C C   . ASN A 120 ? 0.3356 0.3351 0.3488 -0.0321 -0.0048 0.0331  120 ASN A C   
914  O O   . ASN A 120 ? 0.3894 0.3818 0.3989 -0.0325 -0.0024 0.0301  120 ASN A O   
915  C CB  . ASN A 120 ? 0.3231 0.3256 0.3481 -0.0292 -0.0057 0.0446  120 ASN A CB  
916  C CG  . ASN A 120 ? 0.3857 0.3913 0.4134 -0.0279 -0.0086 0.0492  120 ASN A CG  
917  O OD1 . ASN A 120 ? 0.3878 0.3949 0.4092 -0.0275 -0.0113 0.0452  120 ASN A OD1 
918  N ND2 . ASN A 120 ? 0.3752 0.3824 0.4132 -0.0278 -0.0076 0.0587  120 ASN A ND2 
919  N N   . LEU A 121 ? 0.3106 0.3135 0.3236 -0.0352 -0.0048 0.0334  121 LEU A N   
920  C CA  . LEU A 121 ? 0.3383 0.3376 0.3461 -0.0397 -0.0029 0.0300  121 LEU A CA  
921  C C   . LEU A 121 ? 0.3540 0.3586 0.3569 -0.0410 -0.0063 0.0266  121 LEU A C   
922  O O   . LEU A 121 ? 0.3827 0.3819 0.3790 -0.0456 -0.0051 0.0242  121 LEU A O   
923  C CB  . LEU A 121 ? 0.4192 0.4229 0.4280 -0.0428 -0.0032 0.0314  121 LEU A CB  
924  C CG  . LEU A 121 ? 0.5379 0.5344 0.5511 -0.0436 0.0018  0.0352  121 LEU A CG  
925  C CD1 . LEU A 121 ? 0.4327 0.4373 0.4484 -0.0453 -0.0004 0.0376  121 LEU A CD1 
926  C CD2 . LEU A 121 ? 0.5863 0.5687 0.5936 -0.0479 0.0088  0.0325  121 LEU A CD2 
927  N N   . ALA A 122 ? 0.2924 0.3071 0.2978 -0.0378 -0.0098 0.0273  122 ALA A N   
928  C CA  . ALA A 122 ? 0.3214 0.3430 0.3259 -0.0377 -0.0123 0.0266  122 ALA A CA  
929  C C   . ALA A 122 ? 0.3287 0.3445 0.3305 -0.0361 -0.0122 0.0249  122 ALA A C   
930  O O   . ALA A 122 ? 0.3436 0.3619 0.3425 -0.0392 -0.0140 0.0247  122 ALA A O   
931  C CB  . ALA A 122 ? 0.3355 0.3660 0.3443 -0.0334 -0.0129 0.0282  122 ALA A CB  
932  N N   . MET A 123 ? 0.3586 0.3677 0.3615 -0.0322 -0.0106 0.0247  123 MET A N   
933  C CA  . MET A 123 ? 0.3539 0.3565 0.3544 -0.0306 -0.0099 0.0232  123 MET A CA  
934  C C   . MET A 123 ? 0.4176 0.4098 0.4119 -0.0360 -0.0067 0.0211  123 MET A C   
935  O O   . MET A 123 ? 0.3514 0.3413 0.3402 -0.0384 -0.0073 0.0192  123 MET A O   
936  C CB  . MET A 123 ? 0.3723 0.3708 0.3763 -0.0263 -0.0088 0.0249  123 MET A CB  
937  C CG  . MET A 123 ? 0.4336 0.4383 0.4385 -0.0230 -0.0112 0.0255  123 MET A CG  
938  S SD  . MET A 123 ? 0.4633 0.4691 0.4658 -0.0197 -0.0122 0.0231  123 MET A SD  
939  C CE  . MET A 123 ? 0.3785 0.3750 0.3789 -0.0206 -0.0108 0.0217  123 MET A CE  
940  N N   . GLN A 124 ? 0.3650 0.3496 0.3590 -0.0386 -0.0022 0.0216  124 GLN A N   
941  C CA  . GLN A 124 ? 0.3595 0.3301 0.3448 -0.0450 0.0036  0.0188  124 GLN A CA  
942  C C   . GLN A 124 ? 0.4191 0.3938 0.3946 -0.0540 0.0002  0.0167  124 GLN A C   
943  O O   . GLN A 124 ? 0.4612 0.4268 0.4255 -0.0611 0.0023  0.0138  124 GLN A O   
944  C CB  . GLN A 124 ? 0.4767 0.4375 0.4647 -0.0456 0.0108  0.0206  124 GLN A CB  
945  C CG  . GLN A 124 ? 0.4736 0.4328 0.4737 -0.0378 0.0139  0.0259  124 GLN A CG  
946  C CD  . GLN A 124 ? 0.6507 0.5947 0.6507 -0.0361 0.0223  0.0261  124 GLN A CD  
947  O OE1 . GLN A 124 ? 0.5504 0.4827 0.5388 -0.0413 0.0265  0.0208  124 GLN A OE1 
948  N NE2 . GLN A 124 ? 0.5517 0.4959 0.5647 -0.0297 0.0252  0.0330  124 GLN A NE2 
949  N N   . SER A 125 ? 0.3486 0.3371 0.3280 -0.0548 -0.0049 0.0189  125 SER A N   
950  C CA  . SER A 125 ? 0.3484 0.3453 0.3217 -0.0636 -0.0094 0.0197  125 SER A CA  
951  C C   . SER A 125 ? 0.3720 0.3768 0.3448 -0.0637 -0.0143 0.0212  125 SER A C   
952  O O   . SER A 125 ? 0.3769 0.3821 0.3401 -0.0738 -0.0166 0.0215  125 SER A O   
953  C CB  . SER A 125 ? 0.4559 0.4678 0.4371 -0.0625 -0.0132 0.0234  125 SER A CB  
954  O OG  . SER A 125 ? 0.5511 0.5560 0.5305 -0.0653 -0.0093 0.0223  125 SER A OG  
955  N N   . TRP A 126 ? 0.3348 0.3456 0.3170 -0.0537 -0.0157 0.0225  126 TRP A N   
956  C CA  . TRP A 126 ? 0.3700 0.3875 0.3534 -0.0521 -0.0193 0.0244  126 TRP A CA  
957  C C   . TRP A 126 ? 0.3930 0.3966 0.3653 -0.0569 -0.0169 0.0206  126 TRP A C   
958  O O   . TRP A 126 ? 0.3880 0.3953 0.3542 -0.0639 -0.0204 0.0221  126 TRP A O   
959  C CB  . TRP A 126 ? 0.3595 0.3814 0.3529 -0.0408 -0.0189 0.0253  126 TRP A CB  
960  C CG  . TRP A 126 ? 0.3426 0.3724 0.3401 -0.0372 -0.0215 0.0283  126 TRP A CG  
961  C CD1 . TRP A 126 ? 0.4246 0.4648 0.4226 -0.0423 -0.0257 0.0330  126 TRP A CD1 
962  C CD2 . TRP A 126 ? 0.3451 0.3733 0.3470 -0.0285 -0.0197 0.0275  126 TRP A CD2 
963  N NE1 . TRP A 126 ? 0.3539 0.3991 0.3581 -0.0358 -0.0261 0.0358  126 TRP A NE1 
964  C CE2 . TRP A 126 ? 0.3153 0.3520 0.3210 -0.0273 -0.0220 0.0316  126 TRP A CE2 
965  C CE3 . TRP A 126 ? 0.3860 0.4066 0.3885 -0.0227 -0.0167 0.0247  126 TRP A CE3 
966  C CZ2 . TRP A 126 ? 0.3890 0.4249 0.3986 -0.0197 -0.0201 0.0318  126 TRP A CZ2 
967  C CZ3 . TRP A 126 ? 0.4029 0.4228 0.4073 -0.0168 -0.0156 0.0246  126 TRP A CZ3 
968  C CH2 . TRP A 126 ? 0.3648 0.3912 0.3725 -0.0148 -0.0166 0.0275  126 TRP A CH2 
969  N N   . HIS A 127 ? 0.3820 0.3700 0.3522 -0.0536 -0.0106 0.0166  127 HIS A N   
970  C CA  . HIS A 127 ? 0.4008 0.3727 0.3606 -0.0577 -0.0058 0.0128  127 HIS A CA  
971  C C   . HIS A 127 ? 0.4593 0.4225 0.4030 -0.0720 -0.0038 0.0105  127 HIS A C   
972  O O   . HIS A 127 ? 0.3864 0.3433 0.3182 -0.0797 -0.0038 0.0087  127 HIS A O   
973  C CB  . HIS A 127 ? 0.4386 0.3966 0.4026 -0.0512 0.0021  0.0114  127 HIS A CB  
974  C CG  . HIS A 127 ? 0.4701 0.4077 0.4236 -0.0557 0.0108  0.0077  127 HIS A CG  
975  N ND1 . HIS A 127 ? 0.4595 0.3920 0.4113 -0.0531 0.0119  0.0064  127 HIS A ND1 
976  C CD2 . HIS A 127 ? 0.4313 0.3504 0.3747 -0.0629 0.0205  0.0048  127 HIS A CD2 
977  C CE1 . HIS A 127 ? 0.4202 0.3319 0.3615 -0.0584 0.0220  0.0030  127 HIS A CE1 
978  N NE2 . HIS A 127 ? 0.5431 0.4453 0.4786 -0.0645 0.0280  0.0018  127 HIS A NE2 
979  N N   . GLN A 128 ? 0.4077 0.3695 0.3488 -0.0772 -0.0021 0.0105  128 GLN A N   
980  C CA  . GLN A 128 ? 0.4587 0.4099 0.3814 -0.0930 0.0005  0.0078  128 GLN A CA  
981  C C   . GLN A 128 ? 0.4769 0.4450 0.3944 -0.1033 -0.0097 0.0122  128 GLN A C   
982  O O   . GLN A 128 ? 0.4764 0.4359 0.3752 -0.1184 -0.0093 0.0104  128 GLN A O   
983  C CB  . GLN A 128 ? 0.4755 0.4209 0.3969 -0.0960 0.0052  0.0070  128 GLN A CB  
984  C CG  . GLN A 128 ? 0.6511 0.5815 0.5503 -0.1140 0.0098  0.0034  128 GLN A CG  
985  C CD  . GLN A 128 ? 0.8943 0.8009 0.7752 -0.1219 0.0187  -0.0023 128 GLN A CD  
986  O OE1 . GLN A 128 ? 0.8132 0.7017 0.6967 -0.1143 0.0298  -0.0053 128 GLN A OE1 
987  N NE2 . GLN A 128 ? 0.7555 0.6626 0.6182 -0.1379 0.0140  -0.0028 128 GLN A NE2 
988  N N   . ALA A 129 ? 0.4078 0.3996 0.3414 -0.0961 -0.0183 0.0188  129 ALA A N   
989  C CA  . ALA A 129 ? 0.4066 0.4176 0.3404 -0.1043 -0.0278 0.0262  129 ALA A CA  
990  C C   . ALA A 129 ? 0.4429 0.4533 0.3726 -0.1054 -0.0300 0.0268  129 ALA A C   
991  O O   . ALA A 129 ? 0.4354 0.4543 0.3567 -0.1183 -0.0363 0.0317  129 ALA A O   
992  C CB  . ALA A 129 ? 0.3920 0.4268 0.3467 -0.0945 -0.0334 0.0342  129 ALA A CB  
993  N N   . ILE A 130 ? 0.3749 0.3765 0.3102 -0.0930 -0.0256 0.0228  130 ILE A N   
994  C CA  . ILE A 130 ? 0.3414 0.3403 0.2720 -0.0938 -0.0269 0.0225  130 ILE A CA  
995  C C   . ILE A 130 ? 0.3996 0.3758 0.3068 -0.1075 -0.0209 0.0158  130 ILE A C   
996  O O   . ILE A 130 ? 0.4435 0.4202 0.3385 -0.1189 -0.0247 0.0173  130 ILE A O   
997  C CB  . ILE A 130 ? 0.3152 0.3118 0.2587 -0.0771 -0.0239 0.0206  130 ILE A CB  
998  C CG1 . ILE A 130 ? 0.3740 0.3895 0.3367 -0.0657 -0.0277 0.0264  130 ILE A CG1 
999  C CG2 . ILE A 130 ? 0.3456 0.3387 0.2842 -0.0775 -0.0249 0.0200  130 ILE A CG2 
1000 C CD1 . ILE A 130 ? 0.6128 0.6447 0.5850 -0.0621 -0.0332 0.0336  130 ILE A CD1 
1001 N N   . VAL A 131 ? 0.3775 0.3325 0.2777 -0.1074 -0.0107 0.0089  131 VAL A N   
1002 C CA  . VAL A 131 ? 0.4114 0.3403 0.2881 -0.1208 -0.0013 0.0020  131 VAL A CA  
1003 C C   . VAL A 131 ? 0.4521 0.3841 0.3093 -0.1421 -0.0066 0.0039  131 VAL A C   
1004 O O   . VAL A 131 ? 0.4782 0.3987 0.3145 -0.1567 -0.0053 0.0014  131 VAL A O   
1005 C CB  . VAL A 131 ? 0.4810 0.3891 0.3573 -0.1164 0.0116  -0.0032 131 VAL A CB  
1006 C CG1 . VAL A 131 ? 0.5211 0.3995 0.3711 -0.1321 0.0239  -0.0102 131 VAL A CG1 
1007 C CG2 . VAL A 131 ? 0.4371 0.3421 0.3312 -0.0981 0.0166  -0.0034 131 VAL A CG2 
1008 N N   . GLN A 132 ? 0.4566 0.4043 0.3195 -0.1455 -0.0127 0.0087  132 GLN A N   
1009 C CA  . GLN A 132 ? 0.5336 0.4867 0.3786 -0.1672 -0.0188 0.0121  132 GLN A CA  
1010 C C   . GLN A 132 ? 0.4831 0.4562 0.3276 -0.1752 -0.0308 0.0206  132 GLN A C   
1011 O O   . GLN A 132 ? 0.5214 0.4888 0.3422 -0.1966 -0.0331 0.0210  132 GLN A O   
1012 C CB  . GLN A 132 ? 0.5238 0.4938 0.3799 -0.1666 -0.0238 0.0174  132 GLN A CB  
1013 C CG  . GLN A 132 ? 0.7315 0.7071 0.5694 -0.1900 -0.0298 0.0215  132 GLN A CG  
1014 C CD  . GLN A 132 ? 0.9982 1.0105 0.8553 -0.1896 -0.0443 0.0356  132 GLN A CD  
1015 O OE1 . GLN A 132 ? 0.9034 0.9351 0.7716 -0.1868 -0.0526 0.0441  132 GLN A OE1 
1016 N NE2 . GLN A 132 ? 0.8500 0.8722 0.7130 -0.1915 -0.0464 0.0391  132 GLN A NE2 
1017 N N   . SER A 133 ? 0.4650 0.4609 0.3345 -0.1592 -0.0379 0.0280  133 SER A N   
1018 C CA  . SER A 133 ? 0.4925 0.5088 0.3658 -0.1644 -0.0485 0.0379  133 SER A CA  
1019 C C   . SER A 133 ? 0.4754 0.4733 0.3308 -0.1706 -0.0447 0.0319  133 SER A C   
1020 O O   . SER A 133 ? 0.4487 0.4532 0.2908 -0.1874 -0.0518 0.0374  133 SER A O   
1021 C CB  . SER A 133 ? 0.5261 0.5665 0.4306 -0.1441 -0.0535 0.0464  133 SER A CB  
1022 O OG  . SER A 133 ? 0.4634 0.5211 0.3732 -0.1470 -0.0616 0.0561  133 SER A OG  
1023 N N   . ILE A 134 ? 0.4447 0.4207 0.3004 -0.1577 -0.0338 0.0218  134 ILE A N   
1024 C CA  . ILE A 134 ? 0.4189 0.3754 0.2584 -0.1625 -0.0284 0.0156  134 ILE A CA  
1025 C C   . ILE A 134 ? 0.5350 0.4685 0.3406 -0.1869 -0.0227 0.0095  134 ILE A C   
1026 O O   . ILE A 134 ? 0.5210 0.4513 0.3078 -0.2027 -0.0259 0.0105  134 ILE A O   
1027 C CB  . ILE A 134 ? 0.4041 0.3426 0.2529 -0.1438 -0.0171 0.0074  134 ILE A CB  
1028 C CG1 . ILE A 134 ? 0.4565 0.4153 0.3327 -0.1235 -0.0230 0.0129  134 ILE A CG1 
1029 C CG2 . ILE A 134 ? 0.4365 0.3490 0.2653 -0.1506 -0.0079 -0.0003 134 ILE A CG2 
1030 C CD1 . ILE A 134 ? 0.4433 0.3893 0.3311 -0.1060 -0.0138 0.0071  134 ILE A CD1 
1031 N N   . GLU A 135 ? 0.5200 0.4358 0.3157 -0.1913 -0.0135 0.0032  135 GLU A N   
1032 C CA  . GLU A 135 ? 0.5849 0.4731 0.3455 -0.2150 -0.0047 -0.0041 135 GLU A CA  
1033 C C   . GLU A 135 ? 0.6560 0.5608 0.3998 -0.2399 -0.0177 0.0039  135 GLU A C   
1034 O O   . GLU A 135 ? 0.5929 0.4796 0.3043 -0.2634 -0.0147 0.0000  135 GLU A O   
1035 C CB  . GLU A 135 ? 0.7144 0.5801 0.4709 -0.2125 0.0092  -0.0117 135 GLU A CB  
1036 C CG  . GLU A 135 ? 0.7994 0.6363 0.5585 -0.1984 0.0269  -0.0206 135 GLU A CG  
1037 C CD  . GLU A 135 ? 0.8776 0.6970 0.6402 -0.1921 0.0403  -0.0250 135 GLU A CD  
1038 O OE1 . GLU A 135 ? 0.9906 0.8145 0.7470 -0.2021 0.0373  -0.0237 135 GLU A OE1 
1039 O OE2 . GLU A 135 ? 1.0439 0.8460 0.8165 -0.1774 0.0536  -0.0286 135 GLU A OE2 
1040 N N   . CYS A 136 ? 0.5120 0.4512 0.2771 -0.2361 -0.0320 0.0159  136 CYS A N   
1041 C CA  . CYS A 136 ? 0.6334 0.5943 0.3875 -0.2591 -0.0461 0.0273  136 CYS A CA  
1042 C C   . CYS A 136 ? 0.5684 0.5417 0.3202 -0.2654 -0.0551 0.0344  136 CYS A C   
1043 O O   . CYS A 136 ? 0.6024 0.5735 0.3270 -0.2920 -0.0602 0.0373  136 CYS A O   
1044 C CB  . CYS A 136 ? 0.6151 0.6112 0.3974 -0.2510 -0.0578 0.0402  136 CYS A CB  
1045 S SG  . CYS A 136 ? 0.7178 0.7501 0.4972 -0.2757 -0.0773 0.0598  136 CYS A SG  
1046 N N   . GLY A 137 ? 0.5304 0.5158 0.3088 -0.2424 -0.0568 0.0372  137 GLY A N   
1047 C CA  . GLY A 137 ? 0.4776 0.4736 0.2551 -0.2466 -0.0643 0.0438  137 GLY A CA  
1048 C C   . GLY A 137 ? 0.5627 0.5250 0.3063 -0.2614 -0.0546 0.0319  137 GLY A C   
1049 O O   . GLY A 137 ? 0.5975 0.5650 0.3249 -0.2795 -0.0620 0.0375  137 GLY A O   
1050 N N   . GLN A 138 ? 0.6007 0.5283 0.3335 -0.2545 -0.0374 0.0164  138 GLN A N   
1051 C CA  . GLN A 138 ? 0.6070 0.4983 0.3063 -0.2690 -0.0247 0.0046  138 GLN A CA  
1052 C C   . GLN A 138 ? 0.5908 0.4670 0.2508 -0.3027 -0.0238 0.0026  138 GLN A C   
1053 O O   . GLN A 138 ? 0.7155 0.5804 0.3478 -0.3197 -0.0222 0.0020  138 GLN A O   
1054 C CB  . GLN A 138 ? 0.6817 0.5415 0.3844 -0.2513 -0.0052 -0.0088 138 GLN A CB  
1055 C CG  . GLN A 138 ? 0.5888 0.4610 0.3257 -0.2214 -0.0059 -0.0070 138 GLN A CG  
1056 C CD  . GLN A 138 ? 0.7046 0.5498 0.4473 -0.2050 0.0120  -0.0172 138 GLN A CD  
1057 O OE1 . GLN A 138 ? 0.6799 0.5100 0.4181 -0.2062 0.0216  -0.0219 138 GLN A OE1 
1058 N NE2 . GLN A 138 ? 0.6742 0.5149 0.4292 -0.1892 0.0162  -0.0192 138 GLN A NE2 
1059 N N   . LYS A 139 ? 0.6553 0.5325 0.3126 -0.3090 -0.0234 0.0028  139 LYS A N   
1060 C CA  . LYS A 139 ? 0.7708 0.6381 0.3931 -0.3318 -0.0203 0.0036  139 LYS A CA  
1061 C C   . LYS A 139 ? 0.8170 0.7158 0.4343 -0.3478 -0.0377 0.0209  139 LYS A C   
1062 O O   . LYS A 139 ? 0.8124 0.6996 0.3950 -0.3679 -0.0339 0.0226  139 LYS A O   
1063 C CB  . LYS A 139 ? 0.6666 0.5334 0.2920 -0.3316 -0.0177 0.0021  139 LYS A CB  
1064 C CG  . LYS A 139 ? 0.8723 0.7092 0.4577 -0.3475 -0.0030 -0.0060 139 LYS A CG  
1065 C CD  . LYS A 139 ? 0.9850 0.8398 0.5707 -0.3562 -0.0113 0.0015  139 LYS A CD  
1066 C CE  . LYS A 139 ? 0.9931 0.8140 0.5502 -0.3627 0.0069  -0.0108 139 LYS A CE  
1067 N NZ  . LYS A 139 ? 0.9687 0.7562 0.4832 -0.3766 0.0225  -0.0199 139 LYS A NZ  
1068 N N   . GLU A 140 ? 0.6913 0.6300 0.3432 -0.3391 -0.0557 0.0353  140 GLU A N   
1069 C CA  . GLU A 140 ? 0.6847 0.6569 0.3403 -0.3516 -0.0715 0.0555  140 GLU A CA  
1070 C C   . GLU A 140 ? 0.7025 0.6755 0.3534 -0.3547 -0.0739 0.0593  140 GLU A C   
1071 O O   . GLU A 140 ? 0.6621 0.6610 0.3165 -0.3662 -0.0855 0.0771  140 GLU A O   
1072 C CB  . GLU A 140 ? 0.7536 0.7696 0.4520 -0.3383 -0.0875 0.0713  140 GLU A CB  
1073 C CG  . GLU A 140 ? 0.7776 0.7978 0.4819 -0.3372 -0.0870 0.0708  140 GLU A CG  
1074 C CD  . GLU A 140 ? 0.9518 1.0158 0.6831 -0.3373 -0.1023 0.0932  140 GLU A CD  
1075 O OE1 . GLU A 140 ? 1.0395 1.1308 0.7886 -0.3360 -0.1125 0.1095  140 GLU A OE1 
1076 O OE2 . GLU A 140 ? 0.9156 0.9861 0.6516 -0.3379 -0.1030 0.0951  140 GLU A OE2 
1077 N N   . GLY A 141 ? 0.6547 0.6001 0.2989 -0.3452 -0.0627 0.0438  141 GLY A N   
1078 C CA  . GLY A 141 ? 0.6814 0.6257 0.3209 -0.3472 -0.0642 0.0460  141 GLY A CA  
1079 C C   . GLY A 141 ? 0.7016 0.6770 0.3793 -0.3286 -0.0777 0.0547  141 GLY A C   
1080 O O   . GLY A 141 ? 0.7448 0.7221 0.4217 -0.3286 -0.0800 0.0575  141 GLY A O   
1081 N N   . GLU A 142 ? 0.6385 0.6384 0.3487 -0.3122 -0.0858 0.0595  142 GLU A N   
1082 C CA  . GLU A 142 ? 0.6030 0.6317 0.3528 -0.2869 -0.0931 0.0705  142 GLU A CA  
1083 C C   . GLU A 142 ? 0.6091 0.6160 0.3700 -0.2604 -0.0798 0.0567  142 GLU A C   
1084 O O   . GLU A 142 ? 0.5530 0.5710 0.3304 -0.2477 -0.0832 0.0616  142 GLU A O   
1085 C CB  . GLU A 142 ? 0.6043 0.6661 0.3878 -0.2742 -0.1013 0.0839  142 GLU A CB  
1086 C CG  . GLU A 142 ? 0.6224 0.7021 0.4462 -0.2423 -0.1012 0.0892  142 GLU A CG  
1087 C CD  . GLU A 142 ? 0.7729 0.8810 0.6274 -0.2307 -0.1064 0.1014  142 GLU A CD  
1088 O OE1 . GLU A 142 ? 0.7095 0.8167 0.5548 -0.2420 -0.1069 0.1006  142 GLU A OE1 
1089 O OE2 . GLU A 142 ? 0.6553 0.7849 0.5427 -0.2101 -0.1087 0.1114  142 GLU A OE2 
1090 N N   . PHE A 143 ? 0.6239 0.6006 0.3765 -0.2527 -0.0648 0.0407  143 PHE A N   
1091 C CA  . PHE A 143 ? 0.5722 0.5301 0.3368 -0.2284 -0.0525 0.0294  143 PHE A CA  
1092 C C   . PHE A 143 ? 0.6759 0.5941 0.4091 -0.2388 -0.0379 0.0146  143 PHE A C   
1093 O O   . PHE A 143 ? 0.6398 0.5357 0.3418 -0.2605 -0.0312 0.0080  143 PHE A O   
1094 C CB  . PHE A 143 ? 0.5158 0.4709 0.2996 -0.2093 -0.0455 0.0245  143 PHE A CB  
1095 C CG  . PHE A 143 ? 0.4688 0.4582 0.2862 -0.1938 -0.0559 0.0369  143 PHE A CG  
1096 C CD1 . PHE A 143 ? 0.5466 0.5644 0.3829 -0.1889 -0.0672 0.0503  143 PHE A CD1 
1097 C CD2 . PHE A 143 ? 0.4634 0.4553 0.2938 -0.1840 -0.0528 0.0354  143 PHE A CD2 
1098 C CE1 . PHE A 143 ? 0.5303 0.5765 0.3976 -0.1741 -0.0736 0.0618  143 PHE A CE1 
1099 C CE2 . PHE A 143 ? 0.5377 0.5584 0.3976 -0.1701 -0.0604 0.0462  143 PHE A CE2 
1100 C CZ  . PHE A 143 ? 0.4767 0.5236 0.3549 -0.1651 -0.0699 0.0593  143 PHE A CZ  
1101 N N   . LYS A 144 ? 0.6423 0.5501 0.3835 -0.2231 -0.0315 0.0093  144 LYS A N   
1102 C CA  . LYS A 144 ? 0.7075 0.5762 0.4256 -0.2269 -0.0142 -0.0048 144 LYS A CA  
1103 C C   . LYS A 144 ? 0.8092 0.6578 0.5350 -0.2126 0.0008  -0.0138 144 LYS A C   
1104 O O   . LYS A 144 ? 0.6955 0.5609 0.4440 -0.1994 -0.0033 -0.0098 144 LYS A O   
1105 C CB  . LYS A 144 ? 0.7702 0.6361 0.4960 -0.2148 -0.0125 -0.0062 144 LYS A CB  
1106 C CG  . LYS A 144 ? 0.8523 0.7491 0.5892 -0.2161 -0.0294 0.0064  144 LYS A CG  
1107 C CD  . LYS A 144 ? 1.0080 0.8903 0.7180 -0.2336 -0.0282 0.0039  144 LYS A CD  
1108 C CE  . LYS A 144 ? 1.1186 1.0333 0.8422 -0.2342 -0.0451 0.0183  144 LYS A CE  
1109 N NZ  . LYS A 144 ? 1.1344 1.0356 0.8418 -0.2408 -0.0425 0.0149  144 LYS A NZ  
1110 N N   . ASN A 145 ? 0.7848 0.5968 0.4922 -0.2152 0.0191  -0.0253 145 ASN A N   
1111 C CA  . ASN A 145 ? 0.9847 0.7768 0.7015 -0.2011 0.0350  -0.0320 145 ASN A CA  
1112 C C   . ASN A 145 ? 0.8398 0.6088 0.5604 -0.1881 0.0502  -0.0383 145 ASN A C   
1113 O O   . ASN A 145 ? 0.9513 0.6857 0.6542 -0.1938 0.0695  -0.0466 145 ASN A O   
1114 C CB  . ASN A 145 ? 1.0205 0.7878 0.7106 -0.2198 0.0463  -0.0383 145 ASN A CB  
1115 C CG  . ASN A 145 ? 1.0307 0.7784 0.6796 -0.2499 0.0489  -0.0426 145 ASN A CG  
1116 O OD1 . ASN A 145 ? 1.2765 0.9947 0.9060 -0.2551 0.0636  -0.0504 145 ASN A OD1 
1117 N ND2 . ASN A 145 ? 0.9925 0.7577 0.6278 -0.2703 0.0349  -0.0366 145 ASN A ND2 
1118 N N   . ARG A 146 ? 0.8688 0.6569 0.6139 -0.1700 0.0423  -0.0337 146 ARG A N   
1119 C CA  . ARG A 146 ? 0.9037 0.6743 0.6570 -0.1559 0.0552  -0.0377 146 ARG A CA  
1120 C C   . ARG A 146 ? 0.9400 0.7044 0.7150 -0.1379 0.0659  -0.0379 146 ARG A C   
1121 O O   . ARG A 146 ? 1.1859 0.9263 0.9616 -0.1316 0.0830  -0.0417 146 ARG A O   
1122 C CB  . ARG A 146 ? 0.8571 0.6497 0.6280 -0.1438 0.0432  -0.0325 146 ARG A CB  
1123 C CG  . ARG A 146 ? 0.7454 0.5748 0.5390 -0.1348 0.0246  -0.0234 146 ARG A CG  
1124 C CD  . ARG A 146 ? 0.8363 0.6833 0.6416 -0.1267 0.0145  -0.0186 146 ARG A CD  
1125 N NE  . ARG A 146 ? 0.8612 0.7092 0.6454 -0.1449 0.0082  -0.0171 146 ARG A NE  
1126 C CZ  . ARG A 146 ? 0.9099 0.7849 0.6987 -0.1504 -0.0075 -0.0077 146 ARG A CZ  
1127 N NH1 . ARG A 146 ? 0.7910 0.6925 0.6040 -0.1389 -0.0172 0.0002  146 ARG A NH1 
1128 N NH2 . ARG A 146 ? 0.8808 0.7565 0.6500 -0.1684 -0.0131 -0.0052 146 ARG A NH2 
1129 N N   . SER A 147 ? 0.7781 0.5644 0.5719 -0.1296 0.0567  -0.0328 147 SER A N   
1130 C CA  . SER A 147 ? 0.8541 0.6370 0.6673 -0.1152 0.0652  -0.0316 147 SER A CA  
1131 C C   . SER A 147 ? 0.8926 0.6758 0.6985 -0.1244 0.0647  -0.0319 147 SER A C   
1132 O O   . SER A 147 ? 0.8576 0.6508 0.6489 -0.1394 0.0543  -0.0313 147 SER A O   
1133 C CB  . SER A 147 ? 0.7602 0.5696 0.6048 -0.0948 0.0546  -0.0248 147 SER A CB  
1134 O OG  . SER A 147 ? 0.7191 0.5422 0.5666 -0.0920 0.0444  -0.0228 147 SER A OG  
1135 N N   . ASN A 148 ? 0.6947 0.4678 0.5116 -0.1159 0.0758  -0.0317 148 ASN A N   
1136 C CA  . ASN A 148 ? 0.7374 0.5094 0.5482 -0.1238 0.0765  -0.0322 148 ASN A CA  
1137 C C   . ASN A 148 ? 0.7459 0.5525 0.5761 -0.1163 0.0581  -0.0255 148 ASN A C   
1138 O O   . ASN A 148 ? 0.6125 0.4393 0.4650 -0.1011 0.0494  -0.0206 148 ASN A O   
1139 C CB  . ASN A 148 ? 0.8614 0.6102 0.6781 -0.1172 0.0960  -0.0333 148 ASN A CB  
1140 C CG  . ASN A 148 ? 0.8748 0.6423 0.7251 -0.0965 0.0924  -0.0256 148 ASN A CG  
1141 O OD1 . ASN A 148 ? 0.8175 0.6067 0.6791 -0.0931 0.0806  -0.0217 148 ASN A OD1 
1142 N ND2 . ASN A 148 ? 0.9761 0.7348 0.8420 -0.0836 0.1031  -0.0225 148 ASN A ND2 
1143 N N   . SER A 149 ? 0.6418 0.4536 0.4618 -0.1282 0.0532  -0.0254 149 SER A N   
1144 C CA  . SER A 149 ? 0.6037 0.4477 0.4388 -0.1242 0.0362  -0.0188 149 SER A CA  
1145 C C   . SER A 149 ? 0.5601 0.4163 0.4224 -0.1054 0.0354  -0.0147 149 SER A C   
1146 O O   . SER A 149 ? 0.5104 0.3921 0.3897 -0.0965 0.0230  -0.0093 149 SER A O   
1147 C CB  . SER A 149 ? 0.6308 0.4765 0.4483 -0.1426 0.0321  -0.0189 149 SER A CB  
1148 O OG  . SER A 149 ? 0.6595 0.4885 0.4738 -0.1437 0.0436  -0.0221 149 SER A OG  
1149 N N   . THR A 150 ? 0.5468 0.3849 0.4133 -0.0997 0.0491  -0.0165 150 THR A N   
1150 C CA  . THR A 150 ? 0.5956 0.4463 0.4872 -0.0836 0.0476  -0.0113 150 THR A CA  
1151 C C   . THR A 150 ? 0.4790 0.3413 0.3882 -0.0694 0.0429  -0.0077 150 THR A C   
1152 O O   . THR A 150 ? 0.4720 0.3550 0.3980 -0.0598 0.0335  -0.0030 150 THR A O   
1153 C CB  . THR A 150 ? 0.6281 0.4577 0.5220 -0.0813 0.0639  -0.0117 150 THR A CB  
1154 O OG1 . THR A 150 ? 0.6690 0.4882 0.5458 -0.0949 0.0679  -0.0153 150 THR A OG1 
1155 C CG2 . THR A 150 ? 0.5553 0.3995 0.4752 -0.0660 0.0614  -0.0045 150 THR A CG2 
1156 N N   . ASP A 151 ? 0.4997 0.3478 0.4034 -0.0691 0.0499  -0.0100 151 ASP A N   
1157 C CA  . ASP A 151 ? 0.4942 0.3520 0.4127 -0.0570 0.0458  -0.0068 151 ASP A CA  
1158 C C   . ASP A 151 ? 0.4820 0.3622 0.4023 -0.0566 0.0303  -0.0055 151 ASP A C   
1159 O O   . ASP A 151 ? 0.4737 0.3699 0.4098 -0.0459 0.0233  -0.0015 151 ASP A O   
1160 C CB  . ASP A 151 ? 0.5684 0.4051 0.4791 -0.0582 0.0573  -0.0098 151 ASP A CB  
1161 C CG  . ASP A 151 ? 0.7304 0.5492 0.6505 -0.0517 0.0737  -0.0073 151 ASP A CG  
1162 O OD1 . ASP A 151 ? 0.5918 0.4192 0.5290 -0.0439 0.0736  -0.0014 151 ASP A OD1 
1163 O OD2 . ASP A 151 ? 0.8197 0.6156 0.7308 -0.0545 0.0875  -0.0102 151 ASP A OD2 
1164 N N   . ILE A 152 ? 0.4081 0.2894 0.3120 -0.0689 0.0254  -0.0079 152 ILE A N   
1165 C CA  . ILE A 152 ? 0.3761 0.2791 0.2838 -0.0683 0.0120  -0.0045 152 ILE A CA  
1166 C C   . ILE A 152 ? 0.3872 0.3111 0.3094 -0.0623 0.0037  0.0002  152 ILE A C   
1167 O O   . ILE A 152 ? 0.3894 0.3294 0.3240 -0.0536 -0.0033 0.0039  152 ILE A O   
1168 C CB  . ILE A 152 ? 0.3991 0.3008 0.2870 -0.0848 0.0081  -0.0056 152 ILE A CB  
1169 C CG1 . ILE A 152 ? 0.4442 0.3244 0.3161 -0.0910 0.0164  -0.0108 152 ILE A CG1 
1170 C CG2 . ILE A 152 ? 0.3851 0.3124 0.2815 -0.0834 -0.0055 0.0010  152 ILE A CG2 
1171 C CD1 . ILE A 152 ? 0.4855 0.3599 0.3325 -0.1114 0.0142  -0.0124 152 ILE A CD1 
1172 N N   . ALA A 153 ? 0.3936 0.3159 0.3133 -0.0673 0.0056  0.0000  153 ALA A N   
1173 C CA  . ALA A 153 ? 0.4218 0.3627 0.3541 -0.0624 -0.0012 0.0044  153 ALA A CA  
1174 C C   . ALA A 153 ? 0.4100 0.3561 0.3592 -0.0481 -0.0008 0.0063  153 ALA A C   
1175 O O   . ALA A 153 ? 0.3487 0.3110 0.3082 -0.0420 -0.0072 0.0098  153 ALA A O   
1176 C CB  . ALA A 153 ? 0.4106 0.3467 0.3363 -0.0706 0.0018  0.0034  153 ALA A CB  
1177 N N   . TRP A 154 ? 0.3983 0.3309 0.3506 -0.0436 0.0075  0.0050  154 TRP A N   
1178 C CA  . TRP A 154 ? 0.3987 0.3377 0.3658 -0.0326 0.0066  0.0084  154 TRP A CA  
1179 C C   . TRP A 154 ? 0.3499 0.2959 0.3207 -0.0268 0.0018  0.0091  154 TRP A C   
1180 O O   . TRP A 154 ? 0.3849 0.3417 0.3642 -0.0207 -0.0026 0.0116  154 TRP A O   
1181 C CB  . TRP A 154 ? 0.3693 0.2949 0.3417 -0.0292 0.0162  0.0099  154 TRP A CB  
1182 C CG  . TRP A 154 ? 0.3846 0.3067 0.3595 -0.0312 0.0208  0.0115  154 TRP A CG  
1183 C CD1 . TRP A 154 ? 0.4722 0.3765 0.4426 -0.0350 0.0322  0.0105  154 TRP A CD1 
1184 C CD2 . TRP A 154 ? 0.4064 0.3417 0.3881 -0.0298 0.0152  0.0143  154 TRP A CD2 
1185 N NE1 . TRP A 154 ? 0.4394 0.3459 0.4143 -0.0356 0.0335  0.0129  154 TRP A NE1 
1186 C CE2 . TRP A 154 ? 0.3899 0.3159 0.3717 -0.0326 0.0226  0.0152  154 TRP A CE2 
1187 C CE3 . TRP A 154 ? 0.4533 0.4056 0.4403 -0.0266 0.0062  0.0161  154 TRP A CE3 
1188 C CZ2 . TRP A 154 ? 0.4632 0.3981 0.4506 -0.0324 0.0198  0.0180  154 TRP A CZ2 
1189 C CZ3 . TRP A 154 ? 0.4489 0.4088 0.4406 -0.0267 0.0042  0.0184  154 TRP A CZ3 
1190 C CH2 . TRP A 154 ? 0.4566 0.4088 0.4486 -0.0296 0.0102  0.0194  154 TRP A CH2 
1191 N N   . ARG A 155 ? 0.3397 0.2782 0.3025 -0.0297 0.0033  0.0066  155 ARG A N   
1192 C CA  . ARG A 155 ? 0.3407 0.2850 0.3068 -0.0243 -0.0008 0.0072  155 ARG A CA  
1193 C C   . ARG A 155 ? 0.3732 0.3336 0.3418 -0.0237 -0.0087 0.0094  155 ARG A C   
1194 O O   . ARG A 155 ? 0.3207 0.2882 0.2961 -0.0169 -0.0112 0.0110  155 ARG A O   
1195 C CB  . ARG A 155 ? 0.3520 0.2840 0.3084 -0.0281 0.0030  0.0042  155 ARG A CB  
1196 C CG  . ARG A 155 ? 0.4349 0.3510 0.3934 -0.0253 0.0127  0.0036  155 ARG A CG  
1197 C CD  . ARG A 155 ? 0.3664 0.2724 0.3186 -0.0258 0.0160  0.0013  155 ARG A CD  
1198 N NE  . ARG A 155 ? 0.4184 0.3137 0.3529 -0.0372 0.0185  -0.0031 155 ARG A NE  
1199 C CZ  . ARG A 155 ? 0.5638 0.4381 0.4875 -0.0434 0.0300  -0.0066 155 ARG A CZ  
1200 N NH1 . ARG A 155 ? 0.5171 0.3797 0.4493 -0.0377 0.0407  -0.0050 155 ARG A NH1 
1201 N NH2 . ARG A 155 ? 0.5229 0.3872 0.4268 -0.0563 0.0315  -0.0109 155 ARG A NH2 
1202 N N   . LEU A 156 ? 0.3231 0.2891 0.2864 -0.0313 -0.0117 0.0103  156 LEU A N   
1203 C CA  . LEU A 156 ? 0.2805 0.2637 0.2500 -0.0302 -0.0180 0.0150  156 LEU A CA  
1204 C C   . LEU A 156 ? 0.3542 0.3451 0.3340 -0.0233 -0.0181 0.0169  156 LEU A C   
1205 O O   . LEU A 156 ? 0.3119 0.3114 0.2990 -0.0171 -0.0194 0.0196  156 LEU A O   
1206 C CB  . LEU A 156 ? 0.3220 0.3112 0.2846 -0.0414 -0.0217 0.0175  156 LEU A CB  
1207 C CG  . LEU A 156 ? 0.4038 0.3889 0.3540 -0.0512 -0.0235 0.0173  156 LEU A CG  
1208 C CD1 . LEU A 156 ? 0.4049 0.3975 0.3468 -0.0652 -0.0281 0.0211  156 LEU A CD1 
1209 C CD2 . LEU A 156 ? 0.3346 0.3285 0.2910 -0.0458 -0.0272 0.0211  156 LEU A CD2 
1210 N N   . ILE A 157 ? 0.3035 0.2903 0.2831 -0.0248 -0.0156 0.0155  157 ILE A N   
1211 C CA  . ILE A 157 ? 0.3134 0.3062 0.3007 -0.0197 -0.0155 0.0171  157 ILE A CA  
1212 C C   . ILE A 157 ? 0.3226 0.3122 0.3133 -0.0129 -0.0141 0.0165  157 ILE A C   
1213 O O   . ILE A 157 ? 0.3426 0.3377 0.3369 -0.0088 -0.0144 0.0177  157 ILE A O   
1214 C CB  . ILE A 157 ? 0.3152 0.3038 0.3015 -0.0233 -0.0132 0.0164  157 ILE A CB  
1215 C CG1 . ILE A 157 ? 0.3634 0.3585 0.3467 -0.0306 -0.0155 0.0177  157 ILE A CG1 
1216 C CG2 . ILE A 157 ? 0.3316 0.3234 0.3244 -0.0185 -0.0126 0.0177  157 ILE A CG2 
1217 C CD1 . ILE A 157 ? 0.4637 0.4531 0.4445 -0.0350 -0.0126 0.0166  157 ILE A CD1 
1218 N N   . ALA A 158 ? 0.3020 0.2817 0.2906 -0.0123 -0.0117 0.0149  158 ALA A N   
1219 C CA  . ALA A 158 ? 0.3530 0.3308 0.3443 -0.0075 -0.0113 0.0155  158 ALA A CA  
1220 C C   . ALA A 158 ? 0.3220 0.3035 0.3126 -0.0041 -0.0129 0.0151  158 ALA A C   
1221 O O   . ALA A 158 ? 0.3353 0.3180 0.3265 -0.0015 -0.0126 0.0155  158 ALA A O   
1222 C CB  . ALA A 158 ? 0.3518 0.3197 0.3432 -0.0073 -0.0080 0.0155  158 ALA A CB  
1223 N N   . PHE A 159 ? 0.3286 0.3113 0.3170 -0.0052 -0.0141 0.0147  159 PHE A N   
1224 C CA  . PHE A 159 ? 0.3596 0.3459 0.3492 -0.0014 -0.0148 0.0156  159 PHE A CA  
1225 C C   . PHE A 159 ? 0.2926 0.2871 0.2872 0.0016  -0.0138 0.0183  159 PHE A C   
1226 O O   . PHE A 159 ? 0.3256 0.3181 0.3205 0.0057  -0.0110 0.0181  159 PHE A O   
1227 C CB  . PHE A 159 ? 0.3581 0.3463 0.3451 -0.0045 -0.0170 0.0166  159 PHE A CB  
1228 C CG  . PHE A 159 ? 0.3653 0.3581 0.3556 0.0000  -0.0174 0.0190  159 PHE A CG  
1229 C CD1 . PHE A 159 ? 0.3501 0.3357 0.3383 0.0038  -0.0158 0.0167  159 PHE A CD1 
1230 C CD2 . PHE A 159 ? 0.3344 0.3393 0.3315 0.0007  -0.0187 0.0249  159 PHE A CD2 
1231 C CE1 . PHE A 159 ? 0.4206 0.4090 0.4117 0.0081  -0.0151 0.0190  159 PHE A CE1 
1232 C CE2 . PHE A 159 ? 0.4110 0.4198 0.4133 0.0058  -0.0174 0.0286  159 PHE A CE2 
1233 C CZ  . PHE A 159 ? 0.3790 0.3786 0.3775 0.0095  -0.0154 0.0250  159 PHE A CZ  
1234 N N   . VAL A 160 ? 0.3271 0.3296 0.3251 -0.0010 -0.0150 0.0210  160 VAL A N   
1235 C CA  . VAL A 160 ? 0.2937 0.3041 0.2985 0.0025  -0.0125 0.0248  160 VAL A CA  
1236 C C   . VAL A 160 ? 0.2770 0.2819 0.2794 0.0040  -0.0086 0.0222  160 VAL A C   
1237 O O   . VAL A 160 ? 0.3154 0.3189 0.3190 0.0078  -0.0034 0.0229  160 VAL A O   
1238 C CB  . VAL A 160 ? 0.3117 0.3342 0.3221 -0.0012 -0.0152 0.0300  160 VAL A CB  
1239 C CG1 . VAL A 160 ? 0.3747 0.4037 0.3854 -0.0053 -0.0198 0.0339  160 VAL A CG1 
1240 C CG2 . VAL A 160 ? 0.3774 0.3978 0.3837 -0.0066 -0.0167 0.0274  160 VAL A CG2 
1241 N N   . CYS A 161 ? 0.2921 0.2927 0.2905 0.0004  -0.0102 0.0196  161 CYS A N   
1242 C CA  . CYS A 161 ? 0.3416 0.3378 0.3364 -0.0002 -0.0078 0.0183  161 CYS A CA  
1243 C C   . CYS A 161 ? 0.3330 0.3214 0.3220 0.0009  -0.0060 0.0164  161 CYS A C   
1244 O O   . CYS A 161 ? 0.3498 0.3339 0.3335 0.0003  -0.0019 0.0154  161 CYS A O   
1245 C CB  . CYS A 161 ? 0.3265 0.3217 0.3207 -0.0043 -0.0103 0.0182  161 CYS A CB  
1246 S SG  . CYS A 161 ? 0.4327 0.4351 0.4311 -0.0072 -0.0115 0.0198  161 CYS A SG  
1247 N N   . GLY A 162 ? 0.3256 0.3109 0.3139 0.0015  -0.0083 0.0157  162 GLY A N   
1248 C CA  . GLY A 162 ? 0.3294 0.3080 0.3122 0.0020  -0.0071 0.0143  162 GLY A CA  
1249 C C   . GLY A 162 ? 0.3494 0.3255 0.3305 0.0058  -0.0022 0.0135  162 GLY A C   
1250 O O   . GLY A 162 ? 0.3672 0.3359 0.3405 0.0044  0.0017  0.0118  162 GLY A O   
1251 N N   . LEU A 163 ? 0.3351 0.3171 0.3233 0.0096  -0.0019 0.0156  163 LEU A N   
1252 C CA  . LEU A 163 ? 0.3500 0.3310 0.3405 0.0145  0.0040  0.0172  163 LEU A CA  
1253 C C   . LEU A 163 ? 0.3581 0.3359 0.3472 0.0152  0.0118  0.0174  163 LEU A C   
1254 O O   . LEU A 163 ? 0.3564 0.3243 0.3398 0.0167  0.0197  0.0158  163 LEU A O   
1255 C CB  . LEU A 163 ? 0.3522 0.3440 0.3530 0.0173  0.0016  0.0223  163 LEU A CB  
1256 C CG  . LEU A 163 ? 0.4394 0.4316 0.4457 0.0232  0.0068  0.0261  163 LEU A CG  
1257 C CD1 . LEU A 163 ? 0.4434 0.4234 0.4407 0.0241  0.0091  0.0215  163 LEU A CD1 
1258 C CD2 . LEU A 163 ? 0.3614 0.3665 0.3770 0.0234  0.0014  0.0326  163 LEU A CD2 
1259 N N   . GLU A 164 ? 0.3592 0.3434 0.3522 0.0135  0.0109  0.0190  164 GLU A N   
1260 C CA  . GLU A 164 ? 0.4076 0.3875 0.3985 0.0136  0.0192  0.0190  164 GLU A CA  
1261 C C   . GLU A 164 ? 0.4457 0.4128 0.4208 0.0073  0.0215  0.0137  164 GLU A C   
1262 O O   . GLU A 164 ? 0.4025 0.3590 0.3697 0.0063  0.0313  0.0118  164 GLU A O   
1263 C CB  . GLU A 164 ? 0.4858 0.4766 0.4848 0.0127  0.0168  0.0222  164 GLU A CB  
1264 C CG  . GLU A 164 ? 0.5690 0.5740 0.5827 0.0166  0.0143  0.0293  164 GLU A CG  
1265 C CD  . GLU A 164 ? 0.8898 0.9061 0.9100 0.0139  0.0102  0.0326  164 GLU A CD  
1266 O OE1 . GLU A 164 ? 0.8149 0.8299 0.8290 0.0085  0.0046  0.0289  164 GLU A OE1 
1267 O OE2 . GLU A 164 ? 0.8587 0.8858 0.8913 0.0170  0.0129  0.0400  164 GLU A OE2 
1268 N N   . GLY A 165 ? 0.3960 0.3634 0.3660 0.0020  0.0134  0.0120  165 GLY A N   
1269 C CA  . GLY A 165 ? 0.3661 0.3241 0.3217 -0.0057 0.0139  0.0093  165 GLY A CA  
1270 C C   . GLY A 165 ? 0.4164 0.3625 0.3618 -0.0063 0.0195  0.0066  165 GLY A C   
1271 O O   . GLY A 165 ? 0.4534 0.3877 0.3836 -0.0130 0.0254  0.0038  165 GLY A O   
1272 N N   . ILE A 166 ? 0.3280 0.2758 0.2799 -0.0003 0.0183  0.0072  166 ILE A N   
1273 C CA  . ILE A 166 ? 0.3784 0.3146 0.3210 -0.0005 0.0238  0.0046  166 ILE A CA  
1274 C C   . ILE A 166 ? 0.4738 0.4002 0.4143 0.0035  0.0375  0.0038  166 ILE A C   
1275 O O   . ILE A 166 ? 0.4273 0.3378 0.3532 -0.0004 0.0462  0.0002  166 ILE A O   
1276 C CB  . ILE A 166 ? 0.4745 0.4157 0.4251 0.0047  0.0184  0.0059  166 ILE A CB  
1277 C CG1 . ILE A 166 ? 0.5232 0.4699 0.4744 0.0005  0.0082  0.0068  166 ILE A CG1 
1278 C CG2 . ILE A 166 ? 0.6258 0.5551 0.5677 0.0052  0.0246  0.0035  166 ILE A CG2 
1279 C CD1 . ILE A 166 ? 0.6227 0.5658 0.5627 -0.0092 0.0060  0.0068  166 ILE A CD1 
1280 N N   . TYR A 167 ? 0.4020 0.3370 0.3571 0.0107  0.0406  0.0079  167 TYR A N   
1281 C CA  . TYR A 167 ? 0.4395 0.3662 0.3963 0.0155  0.0555  0.0093  167 TYR A CA  
1282 C C   . TYR A 167 ? 0.4375 0.3485 0.3765 0.0074  0.0646  0.0044  167 TYR A C   
1283 O O   . TYR A 167 ? 0.4704 0.3643 0.4007 0.0078  0.0799  0.0024  167 TYR A O   
1284 C CB  . TYR A 167 ? 0.4382 0.3808 0.4158 0.0232  0.0554  0.0167  167 TYR A CB  
1285 C CG  . TYR A 167 ? 0.3996 0.3559 0.3932 0.0299  0.0493  0.0229  167 TYR A CG  
1286 C CD1 . TYR A 167 ? 0.3988 0.3495 0.3900 0.0322  0.0500  0.0220  167 TYR A CD1 
1287 C CD2 . TYR A 167 ? 0.4595 0.4345 0.4694 0.0325  0.0425  0.0299  167 TYR A CD2 
1288 C CE1 . TYR A 167 ? 0.4394 0.4027 0.4440 0.0371  0.0441  0.0280  167 TYR A CE1 
1289 C CE2 . TYR A 167 ? 0.3790 0.3667 0.4010 0.0359  0.0362  0.0361  167 TYR A CE2 
1290 C CZ  . TYR A 167 ? 0.4679 0.4498 0.4873 0.0383  0.0370  0.0352  167 TYR A CZ  
1291 O OH  . TYR A 167 ? 0.5857 0.5804 0.6160 0.0406  0.0305  0.0417  167 TYR A OH  
1292 N N   . LYS A 168 ? 0.4154 0.3308 0.3482 -0.0005 0.0565  0.0028  168 LYS A N   
1293 C CA  . LYS A 168 ? 0.4553 0.3567 0.3696 -0.0102 0.0640  -0.0013 168 LYS A CA  
1294 C C   . LYS A 168 ? 0.5442 0.4269 0.4344 -0.0206 0.0684  -0.0068 168 LYS A C   
1295 O O   . LYS A 168 ? 0.4993 0.3652 0.3698 -0.0299 0.0784  -0.0109 168 LYS A O   
1296 C CB  . LYS A 168 ? 0.4954 0.4077 0.4093 -0.0170 0.0528  -0.0004 168 LYS A CB  
1297 C CG  . LYS A 168 ? 0.7605 0.6869 0.6922 -0.0101 0.0513  0.0038  168 LYS A CG  
1298 C CD  . LYS A 168 ? 0.7188 0.6513 0.6463 -0.0182 0.0432  0.0039  168 LYS A CD  
1299 C CE  . LYS A 168 ? 0.8155 0.7662 0.7593 -0.0144 0.0301  0.0079  168 LYS A CE  
1300 N NZ  . LYS A 168 ? 0.8818 0.8431 0.8410 -0.0075 0.0316  0.0114  168 LYS A NZ  
1301 N N   . LEU A 169 ? 0.4577 0.3421 0.3475 -0.0204 0.0616  -0.0069 169 LEU A N   
1302 C CA  . LEU A 169 ? 0.5402 0.4086 0.4067 -0.0320 0.0641  -0.0113 169 LEU A CA  
1303 C C   . LEU A 169 ? 0.5654 0.4110 0.4200 -0.0306 0.0829  -0.0155 169 LEU A C   
1304 O O   . LEU A 169 ? 0.5350 0.3610 0.3635 -0.0435 0.0897  -0.0206 169 LEU A O   
1305 C CB  . LEU A 169 ? 0.4756 0.3539 0.3473 -0.0317 0.0511  -0.0092 169 LEU A CB  
1306 C CG  . LEU A 169 ? 0.4136 0.3105 0.2943 -0.0349 0.0348  -0.0046 169 LEU A CG  
1307 C CD1 . LEU A 169 ? 0.4512 0.3552 0.3375 -0.0337 0.0252  -0.0022 169 LEU A CD1 
1308 C CD2 . LEU A 169 ? 0.4336 0.3278 0.2978 -0.0500 0.0318  -0.0042 169 LEU A CD2 
1309 N N   . GLY A 170 ? 0.5220 0.3693 0.3947 -0.0162 0.0920  -0.0126 170 GLY A N   
1310 C CA  . GLY A 170 ? 0.4927 0.3187 0.3583 -0.0127 0.1113  -0.0148 170 GLY A CA  
1311 C C   . GLY A 170 ? 0.5616 0.3806 0.4194 -0.0141 0.1096  -0.0170 170 GLY A C   
1312 O O   . GLY A 170 ? 0.5801 0.3748 0.4158 -0.0216 0.1228  -0.0225 170 GLY A O   
1313 N N   . LEU A 171 ? 0.5112 0.3500 0.3857 -0.0079 0.0943  -0.0131 171 LEU A N   
1314 C CA  . LEU A 171 ? 0.5542 0.3888 0.4252 -0.0073 0.0922  -0.0142 171 LEU A CA  
1315 C C   . LEU A 171 ? 0.7711 0.5963 0.6517 0.0046  0.1079  -0.0119 171 LEU A C   
1316 O O   . LEU A 171 ? 0.7275 0.5582 0.6262 0.0152  0.1158  -0.0064 171 LEU A O   
1317 C CB  . LEU A 171 ? 0.5498 0.4071 0.4365 -0.0035 0.0730  -0.0104 171 LEU A CB  
1318 C CG  . LEU A 171 ? 0.5369 0.4035 0.4170 -0.0143 0.0585  -0.0107 171 LEU A CG  
1319 C CD1 . LEU A 171 ? 0.4951 0.3825 0.3939 -0.0083 0.0435  -0.0062 171 LEU A CD1 
1320 C CD2 . LEU A 171 ? 0.6140 0.4672 0.4699 -0.0284 0.0580  -0.0145 171 LEU A CD2 
1321 N N   . GLN A 172 ? 0.6768 0.4890 0.5467 0.0028  0.1122  -0.0148 172 GLN A N   
1322 C CA  . GLN A 172 ? 0.7586 0.5564 0.6334 0.0122  0.1305  -0.0130 172 GLN A CA  
1323 C C   . GLN A 172 ? 0.8328 0.6492 0.7350 0.0267  0.1247  -0.0047 172 GLN A C   
1324 O O   . GLN A 172 ? 1.0161 0.8279 0.9317 0.0376  0.1393  0.0010  172 GLN A O   
1325 C CB  . GLN A 172 ? 0.8433 0.6138 0.6901 0.0020  0.1410  -0.0207 172 GLN A CB  
1326 C CG  . GLN A 172 ? 0.9403 0.6878 0.7560 -0.0144 0.1506  -0.0286 172 GLN A CG  
1327 C CD  . GLN A 172 ? 1.0436 0.7630 0.8511 -0.0116 0.1786  -0.0306 172 GLN A CD  
1328 O OE1 . GLN A 172 ? 1.0666 0.7922 0.8976 0.0027  0.1882  -0.0238 172 GLN A OE1 
1329 N NE2 . GLN A 172 ? 1.1136 0.8015 0.8874 -0.0259 0.1927  -0.0392 172 GLN A NE2 
1330 N N   . GLY A 173 ? 0.6687 0.5055 0.5797 0.0269  0.1051  -0.0030 173 GLY A N   
1331 C CA  . GLY A 173 ? 0.8616 0.7144 0.7950 0.0382  0.0998  0.0045  173 GLY A CA  
1332 C C   . GLY A 173 ? 0.7091 0.5877 0.6644 0.0436  0.0876  0.0118  173 GLY A C   
1333 O O   . GLY A 173 ? 0.6864 0.5807 0.6545 0.0477  0.0766  0.0163  173 GLY A O   
1334 N N   . LEU A 174 ? 0.6278 0.5098 0.5860 0.0427  0.0899  0.0129  174 LEU A N   
1335 C CA  . LEU A 174 ? 0.5735 0.4784 0.5476 0.0444  0.0773  0.0182  174 LEU A CA  
1336 C C   . LEU A 174 ? 0.6186 0.5289 0.6086 0.0513  0.0876  0.0260  174 LEU A C   
1337 O O   . LEU A 174 ? 0.5816 0.4792 0.5628 0.0487  0.0986  0.0228  174 LEU A O   
1338 C CB  . LEU A 174 ? 0.5809 0.4876 0.5424 0.0344  0.0661  0.0117  174 LEU A CB  
1339 C CG  . LEU A 174 ? 0.6463 0.5738 0.6206 0.0347  0.0523  0.0156  174 LEU A CG  
1340 C CD1 . LEU A 174 ? 0.5803 0.5202 0.5649 0.0380  0.0424  0.0193  174 LEU A CD1 
1341 C CD2 . LEU A 174 ? 0.5794 0.5059 0.5416 0.0254  0.0440  0.0099  174 LEU A CD2 
1342 N N   . ALA A 175 ? 0.5379 0.4675 0.5510 0.0592  0.0839  0.0372  175 ALA A N   
1343 C CA  . ALA A 175 ? 0.5051 0.4440 0.5383 0.0666  0.0932  0.0481  175 ALA A CA  
1344 C C   . ALA A 175 ? 0.5156 0.4737 0.5563 0.0630  0.0806  0.0508  175 ALA A C   
1345 O O   . ALA A 175 ? 0.4962 0.4711 0.5420 0.0603  0.0649  0.0532  175 ALA A O   
1346 C CB  . ALA A 175 ? 0.5411 0.4922 0.5971 0.0763  0.0968  0.0617  175 ALA A CB  
1347 N N   . GLU A 176 ? 0.4848 0.4387 0.5246 0.0623  0.0885  0.0501  176 GLU A N   
1348 C CA  . GLU A 176 ? 0.3899 0.3610 0.4371 0.0591  0.0783  0.0531  176 GLU A CA  
1349 C C   . GLU A 176 ? 0.5174 0.5144 0.5897 0.0638  0.0714  0.0678  176 GLU A C   
1350 O O   . GLU A 176 ? 0.4236 0.4368 0.4990 0.0586  0.0576  0.0696  176 GLU A O   
1351 C CB  . GLU A 176 ? 0.5617 0.5234 0.6061 0.0590  0.0908  0.0516  176 GLU A CB  
1352 C CG  . GLU A 176 ? 0.5706 0.5092 0.5875 0.0504  0.0948  0.0377  176 GLU A CG  
1353 C CD  . GLU A 176 ? 0.5382 0.4731 0.5511 0.0471  0.1006  0.0359  176 GLU A CD  
1354 O OE1 . GLU A 176 ? 0.6456 0.5976 0.6771 0.0513  0.0989  0.0446  176 GLU A OE1 
1355 O OE2 . GLU A 176 ? 0.5736 0.4887 0.5641 0.0393  0.1068  0.0262  176 GLU A OE2 
1356 N N   . GLU A 177 ? 0.4405 0.4418 0.5306 0.0727  0.0812  0.0794  177 GLU A N   
1357 C CA  . GLU A 177 ? 0.5090 0.5374 0.6249 0.0762  0.0749  0.0967  177 GLU A CA  
1358 C C   . GLU A 177 ? 0.5101 0.5525 0.6234 0.0697  0.0561  0.0971  177 GLU A C   
1359 O O   . GLU A 177 ? 0.5567 0.6228 0.6869 0.0684  0.0475  0.1107  177 GLU A O   
1360 C CB  . GLU A 177 ? 0.5605 0.5898 0.6978 0.0879  0.0912  0.1108  177 GLU A CB  
1361 C CG  . GLU A 177 ? 0.8255 0.8315 0.9603 0.0945  0.1150  0.1078  177 GLU A CG  
1362 C CD  . GLU A 177 ? 1.0382 1.0125 1.1452 0.0918  0.1237  0.0909  177 GLU A CD  
1363 O OE1 . GLU A 177 ? 1.1015 1.0710 1.2065 0.0940  0.1237  0.0907  177 GLU A OE1 
1364 O OE2 . GLU A 177 ? 0.8669 0.8218 0.9534 0.0864  0.1299  0.0784  177 GLU A OE2 
1365 N N   . ASP A 178 ? 0.4809 0.5090 0.5728 0.0646  0.0501  0.0833  178 ASP A N   
1366 C CA  . ASP A 178 ? 0.4008 0.4377 0.4873 0.0580  0.0344  0.0819  178 ASP A CA  
1367 C C   . ASP A 178 ? 0.4238 0.4666 0.5006 0.0481  0.0215  0.0761  178 ASP A C   
1368 O O   . ASP A 178 ? 0.3905 0.4375 0.4603 0.0414  0.0102  0.0738  178 ASP A O   
1369 C CB  . ASP A 178 ? 0.4740 0.4926 0.5438 0.0576  0.0352  0.0708  178 ASP A CB  
1370 C CG  . ASP A 178 ? 0.6314 0.6467 0.7107 0.0659  0.0449  0.0777  178 ASP A CG  
1371 O OD1 . ASP A 178 ? 0.6569 0.6883 0.7580 0.0712  0.0479  0.0932  178 ASP A OD1 
1372 O OD2 . ASP A 178 ? 0.6205 0.6177 0.6862 0.0666  0.0496  0.0687  178 ASP A OD2 
1373 N N   . PHE A 179 ? 0.3955 0.4373 0.4713 0.0469  0.0241  0.0736  179 PHE A N   
1374 C CA  . PHE A 179 ? 0.3849 0.4288 0.4502 0.0380  0.0138  0.0670  179 PHE A CA  
1375 C C   . PHE A 179 ? 0.4656 0.5283 0.5366 0.0309  0.0016  0.0749  179 PHE A C   
1376 O O   . PHE A 179 ? 0.3721 0.4317 0.4301 0.0228  -0.0072 0.0680  179 PHE A O   
1377 C CB  . PHE A 179 ? 0.4034 0.4455 0.4696 0.0383  0.0193  0.0654  179 PHE A CB  
1378 C CG  . PHE A 179 ? 0.4079 0.4525 0.4651 0.0298  0.0098  0.0599  179 PHE A CG  
1379 C CD1 . PHE A 179 ? 0.4591 0.4891 0.4997 0.0259  0.0080  0.0479  179 PHE A CD1 
1380 C CD2 . PHE A 179 ? 0.5000 0.5619 0.5662 0.0252  0.0033  0.0678  179 PHE A CD2 
1381 C CE1 . PHE A 179 ? 0.4165 0.4480 0.4507 0.0189  0.0010  0.0439  179 PHE A CE1 
1382 C CE2 . PHE A 179 ? 0.4814 0.5434 0.5384 0.0172  -0.0038 0.0624  179 PHE A CE2 
1383 C CZ  . PHE A 179 ? 0.4602 0.5064 0.5019 0.0147  -0.0043 0.0504  179 PHE A CZ  
1384 N N   . LYS A 180 ? 0.3785 0.4605 0.4687 0.0327  0.0018  0.0901  180 LYS A N   
1385 C CA  . LYS A 180 ? 0.3953 0.4965 0.4892 0.0231  -0.0106 0.0991  180 LYS A CA  
1386 C C   . LYS A 180 ? 0.3605 0.4592 0.4449 0.0183  -0.0176 0.0969  180 LYS A C   
1387 O O   . LYS A 180 ? 0.4014 0.5002 0.4723 0.0069  -0.0272 0.0927  180 LYS A O   
1388 C CB  . LYS A 180 ? 0.4402 0.5654 0.5594 0.0262  -0.0092 0.1191  180 LYS A CB  
1389 C CG  . LYS A 180 ? 0.4841 0.6312 0.6058 0.0131  -0.0230 0.1297  180 LYS A CG  
1390 C CD  . LYS A 180 ? 0.5443 0.7189 0.6941 0.0158  -0.0229 0.1531  180 LYS A CD  
1391 C CE  . LYS A 180 ? 0.7378 0.9346 0.8866 -0.0006 -0.0385 0.1644  180 LYS A CE  
1392 N NZ  . LYS A 180 ? 0.7776 0.9742 0.9137 -0.0116 -0.0446 0.1579  180 LYS A NZ  
1393 N N   . ARG A 181 ? 0.3947 0.4891 0.4849 0.0265  -0.0116 0.0994  181 ARG A N   
1394 C CA  . ARG A 181 ? 0.4409 0.5330 0.5231 0.0226  -0.0175 0.0979  181 ARG A CA  
1395 C C   . ARG A 181 ? 0.4165 0.4894 0.4753 0.0168  -0.0210 0.0809  181 ARG A C   
1396 O O   . ARG A 181 ? 0.3803 0.4535 0.4282 0.0073  -0.0292 0.0790  181 ARG A O   
1397 C CB  . ARG A 181 ? 0.4605 0.5481 0.5525 0.0339  -0.0083 0.1021  181 ARG A CB  
1398 C CG  . ARG A 181 ? 0.5181 0.5988 0.6002 0.0318  -0.0124 0.0978  181 ARG A CG  
1399 C CD  . ARG A 181 ? 0.5924 0.6737 0.6886 0.0424  -0.0037 0.1064  181 ARG A CD  
1400 N NE  . ARG A 181 ? 0.5007 0.5594 0.5894 0.0509  0.0085  0.0950  181 ARG A NE  
1401 C CZ  . ARG A 181 ? 0.6043 0.6452 0.6756 0.0499  0.0082  0.0819  181 ARG A CZ  
1402 N NH1 . ARG A 181 ? 0.5359 0.5770 0.5961 0.0422  -0.0021 0.0777  181 ARG A NH1 
1403 N NH2 . ARG A 181 ? 0.7115 0.7332 0.7756 0.0557  0.0192  0.0734  181 ARG A NH2 
1404 N N   . HIS A 182 ? 0.3373 0.3933 0.3882 0.0216  -0.0144 0.0694  182 HIS A N   
1405 C CA  . HIS A 182 ? 0.2990 0.3391 0.3317 0.0168  -0.0170 0.0559  182 HIS A CA  
1406 C C   . HIS A 182 ? 0.3695 0.4124 0.3945 0.0066  -0.0237 0.0536  182 HIS A C   
1407 O O   . HIS A 182 ? 0.3721 0.4075 0.3843 -0.0006 -0.0278 0.0478  182 HIS A O   
1408 C CB  . HIS A 182 ? 0.3512 0.3759 0.3786 0.0227  -0.0093 0.0470  182 HIS A CB  
1409 C CG  . HIS A 182 ? 0.4570 0.4723 0.4843 0.0298  -0.0026 0.0455  182 HIS A CG  
1410 N ND1 . HIS A 182 ? 0.4488 0.4605 0.4719 0.0295  -0.0052 0.0443  182 HIS A ND1 
1411 C CD2 . HIS A 182 ? 0.3786 0.3855 0.4077 0.0365  0.0075  0.0446  182 HIS A CD2 
1412 C CE1 . HIS A 182 ? 0.4521 0.4546 0.4753 0.0361  0.0024  0.0430  182 HIS A CE1 
1413 N NE2 . HIS A 182 ? 0.4255 0.4241 0.4514 0.0399  0.0107  0.0429  182 HIS A NE2 
1414 N N   . THR A 183 ? 0.3652 0.4174 0.3973 0.0057  -0.0235 0.0580  183 THR A N   
1415 C CA  . THR A 183 ? 0.4058 0.4598 0.4300 -0.0045 -0.0290 0.0559  183 THR A CA  
1416 C C   . THR A 183 ? 0.4054 0.4689 0.4251 -0.0159 -0.0371 0.0619  183 THR A C   
1417 O O   . THR A 183 ? 0.4167 0.4715 0.4209 -0.0261 -0.0401 0.0556  183 THR A O   
1418 C CB  . THR A 183 ? 0.4297 0.4933 0.4636 -0.0031 -0.0272 0.0605  183 THR A CB  
1419 O OG1 . THR A 183 ? 0.4411 0.4940 0.4759 0.0056  -0.0193 0.0545  183 THR A OG1 
1420 C CG2 . THR A 183 ? 0.5440 0.6073 0.5683 -0.0138 -0.0320 0.0573  183 THR A CG2 
1421 N N   . GLU A 184 ? 0.3994 0.4800 0.4319 -0.0153 -0.0399 0.0748  184 GLU A N   
1422 C CA  . GLU A 184 ? 0.4025 0.4930 0.4291 -0.0282 -0.0486 0.0817  184 GLU A CA  
1423 C C   . GLU A 184 ? 0.4541 0.5276 0.4628 -0.0326 -0.0492 0.0717  184 GLU A C   
1424 O O   . GLU A 184 ? 0.4551 0.5236 0.4470 -0.0467 -0.0537 0.0686  184 GLU A O   
1425 C CB  . GLU A 184 ? 0.4746 0.5878 0.5212 -0.0253 -0.0512 0.0994  184 GLU A CB  
1426 C CG  . GLU A 184 ? 0.6100 0.7322 0.6491 -0.0386 -0.0605 0.1066  184 GLU A CG  
1427 C CD  . GLU A 184 ? 0.7783 0.9297 0.8391 -0.0399 -0.0658 0.1286  184 GLU A CD  
1428 O OE1 . GLU A 184 ? 0.9402 1.1038 1.0238 -0.0288 -0.0605 0.1384  184 GLU A OE1 
1429 O OE2 . GLU A 184 ? 0.8248 0.9868 0.8801 -0.0527 -0.0747 0.1370  184 GLU A OE2 
1430 N N   . ALA A 185 ? 0.4409 0.5037 0.4518 -0.0215 -0.0436 0.0665  185 ALA A N   
1431 C CA  . ALA A 185 ? 0.5245 0.5719 0.5207 -0.0244 -0.0435 0.0580  185 ALA A CA  
1432 C C   . ALA A 185 ? 0.5324 0.5615 0.5114 -0.0307 -0.0413 0.0457  185 ALA A C   
1433 O O   . ALA A 185 ? 0.4743 0.4934 0.4376 -0.0406 -0.0426 0.0413  185 ALA A O   
1434 C CB  . ALA A 185 ? 0.4274 0.4669 0.4297 -0.0111 -0.0374 0.0547  185 ALA A CB  
1435 N N   . ILE A 186 ? 0.4205 0.4440 0.4021 -0.0253 -0.0370 0.0405  186 ILE A N   
1436 C CA  . ILE A 186 ? 0.3761 0.3828 0.3450 -0.0297 -0.0336 0.0307  186 ILE A CA  
1437 C C   . ILE A 186 ? 0.4272 0.4345 0.3846 -0.0443 -0.0367 0.0315  186 ILE A C   
1438 O O   . ILE A 186 ? 0.4472 0.4386 0.3886 -0.0527 -0.0339 0.0249  186 ILE A O   
1439 C CB  . ILE A 186 ? 0.4329 0.4357 0.4087 -0.0208 -0.0290 0.0269  186 ILE A CB  
1440 C CG1 . ILE A 186 ? 0.4782 0.4754 0.4590 -0.0100 -0.0252 0.0243  186 ILE A CG1 
1441 C CG2 . ILE A 186 ? 0.4026 0.3917 0.3689 -0.0256 -0.0255 0.0200  186 ILE A CG2 
1442 C CD1 . ILE A 186 ? 0.5086 0.4910 0.4806 -0.0106 -0.0228 0.0181  186 ILE A CD1 
1443 N N   . ILE A 187 ? 0.4008 0.4253 0.3654 -0.0482 -0.0416 0.0399  187 ILE A N   
1444 C CA  . ILE A 187 ? 0.4088 0.4354 0.3609 -0.0645 -0.0456 0.0417  187 ILE A CA  
1445 C C   . ILE A 187 ? 0.4638 0.4860 0.3998 -0.0778 -0.0490 0.0423  187 ILE A C   
1446 O O   . ILE A 187 ? 0.4885 0.4951 0.4039 -0.0912 -0.0467 0.0358  187 ILE A O   
1447 C CB  . ILE A 187 ? 0.3814 0.4317 0.3471 -0.0664 -0.0516 0.0537  187 ILE A CB  
1448 C CG1 . ILE A 187 ? 0.3605 0.4111 0.3371 -0.0564 -0.0472 0.0513  187 ILE A CG1 
1449 C CG2 . ILE A 187 ? 0.4532 0.5080 0.4044 -0.0862 -0.0576 0.0574  187 ILE A CG2 
1450 C CD1 . ILE A 187 ? 0.4821 0.5560 0.4760 -0.0548 -0.0510 0.0638  187 ILE A CD1 
1451 N N   . ARG A 188 ? 0.4536 0.4881 0.3980 -0.0748 -0.0534 0.0500  188 ARG A N   
1452 C CA  . ARG A 188 ? 0.5596 0.5913 0.4887 -0.0880 -0.0574 0.0515  188 ARG A CA  
1453 C C   . ARG A 188 ? 0.5179 0.5218 0.4287 -0.0894 -0.0494 0.0379  188 ARG A C   
1454 O O   . ARG A 188 ? 0.5842 0.5755 0.4726 -0.1057 -0.0488 0.0341  188 ARG A O   
1455 C CB  . ARG A 188 ? 0.5079 0.5578 0.4527 -0.0814 -0.0624 0.0629  188 ARG A CB  
1456 C CG  . ARG A 188 ? 0.5887 0.6679 0.5506 -0.0844 -0.0706 0.0802  188 ARG A CG  
1457 C CD  . ARG A 188 ? 0.7357 0.8317 0.7119 -0.0802 -0.0749 0.0930  188 ARG A CD  
1458 N NE  . ARG A 188 ? 0.7360 0.8622 0.7319 -0.0829 -0.0821 0.1126  188 ARG A NE  
1459 C CZ  . ARG A 188 ? 0.7527 0.8955 0.7422 -0.1020 -0.0925 0.1246  188 ARG A CZ  
1460 N NH1 . ARG A 188 ? 0.6458 0.7757 0.6067 -0.1211 -0.0963 0.1178  188 ARG A NH1 
1461 N NH2 . ARG A 188 ? 0.7075 0.8804 0.7193 -0.1029 -0.0986 0.1447  188 ARG A NH2 
1462 N N   . LEU A 189 ? 0.4680 0.4615 0.3874 -0.0735 -0.0426 0.0310  189 LEU A N   
1463 C CA  . LEU A 189 ? 0.4965 0.4657 0.4025 -0.0735 -0.0345 0.0203  189 LEU A CA  
1464 C C   . LEU A 189 ? 0.5478 0.4979 0.4386 -0.0821 -0.0271 0.0124  189 LEU A C   
1465 O O   . LEU A 189 ? 0.5183 0.4477 0.3909 -0.0908 -0.0204 0.0057  189 LEU A O   
1466 C CB  . LEU A 189 ? 0.5568 0.5220 0.4769 -0.0556 -0.0298 0.0169  189 LEU A CB  
1467 C CG  . LEU A 189 ? 0.5711 0.5489 0.5037 -0.0466 -0.0339 0.0228  189 LEU A CG  
1468 C CD1 . LEU A 189 ? 0.6164 0.5891 0.5602 -0.0313 -0.0289 0.0190  189 LEU A CD1 
1469 C CD2 . LEU A 189 ? 0.6772 0.6503 0.5981 -0.0543 -0.0357 0.0231  189 LEU A CD2 
1470 N N   . GLU A 190 ? 0.4348 0.3902 0.3327 -0.0798 -0.0269 0.0132  190 GLU A N   
1471 C CA  . GLU A 190 ? 0.4745 0.4111 0.3603 -0.0861 -0.0186 0.0061  190 GLU A CA  
1472 C C   . GLU A 190 ? 0.5326 0.4641 0.3961 -0.1073 -0.0201 0.0061  190 GLU A C   
1473 O O   . GLU A 190 ? 0.6029 0.5103 0.4478 -0.1165 -0.0102 -0.0016 190 GLU A O   
1474 C CB  . GLU A 190 ? 0.4771 0.4210 0.3780 -0.0764 -0.0180 0.0071  190 GLU A CB  
1475 C CG  . GLU A 190 ? 0.4091 0.3513 0.3260 -0.0591 -0.0140 0.0053  190 GLU A CG  
1476 C CD  . GLU A 190 ? 0.6411 0.5626 0.5547 -0.0568 -0.0029 -0.0008 190 GLU A CD  
1477 O OE1 . GLU A 190 ? 0.6372 0.5401 0.5344 -0.0669 0.0044  -0.0054 190 GLU A OE1 
1478 O OE2 . GLU A 190 ? 0.6062 0.5297 0.5337 -0.0454 -0.0009 -0.0001 190 GLU A OE2 
1479 N N   . LEU A 191 ? 0.4751 0.4286 0.3402 -0.1159 -0.0315 0.0154  191 LEU A N   
1480 C CA  . LEU A 191 ? 0.5315 0.4847 0.3768 -0.1376 -0.0349 0.0174  191 LEU A CA  
1481 C C   . LEU A 191 ? 0.6259 0.5908 0.4597 -0.1539 -0.0446 0.0253  191 LEU A C   
1482 O O   . LEU A 191 ? 0.6108 0.5700 0.4212 -0.1761 -0.0463 0.0255  191 LEU A O   
1483 C CB  . LEU A 191 ? 0.5316 0.5038 0.3901 -0.1362 -0.0405 0.0240  191 LEU A CB  
1484 C CG  . LEU A 191 ? 0.4604 0.4204 0.3252 -0.1257 -0.0316 0.0168  191 LEU A CG  
1485 C CD1 . LEU A 191 ? 0.4743 0.4580 0.3606 -0.1169 -0.0381 0.0247  191 LEU A CD1 
1486 C CD2 . LEU A 191 ? 0.4526 0.3886 0.2927 -0.1414 -0.0230 0.0088  191 LEU A CD2 
1487 N N   . LEU A 192 ? 0.6031 0.5846 0.4524 -0.1447 -0.0510 0.0327  192 LEU A N   
1488 C CA  . LEU A 192 ? 0.7454 0.7408 0.5896 -0.1561 -0.0605 0.0422  192 LEU A CA  
1489 C C   . LEU A 192 ? 0.8491 0.8797 0.7219 -0.1473 -0.0715 0.0589  192 LEU A C   
1490 O O   . LEU A 192 ? 1.1457 1.1912 1.0270 -0.1462 -0.0778 0.0684  192 LEU A O   
1491 C CB  . LEU A 192 ? 1.0355 1.0242 0.8484 -0.1853 -0.0641 0.0431  192 LEU A CB  
1492 C CG  . LEU A 192 ? 1.2093 1.2189 1.0154 -0.2064 -0.0758 0.0554  192 LEU A CG  
1493 C CD1 . LEU A 192 ? 0.8674 0.8983 0.6979 -0.1961 -0.0796 0.0630  192 LEU A CD1 
1494 C CD2 . LEU A 192 ? 0.9288 0.9123 0.6957 -0.2328 -0.0704 0.0461  192 LEU A CD2 
1495 O OXT . LEU A 192 ? 0.9833 1.0279 0.8721 -0.1409 -0.0733 0.0640  192 LEU A OXT 
# 
