data_8WP7
# 
_entry.id   8WP7 
# 
_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   8WP7         pdb_00008wp7 10.2210/pdb8wp7/pdb 
WWPDB D_1300039559 ?            ?                   
# 
_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                        8WP7 
_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 non-polymer syn SPERMIDINE                              145.246   1   ? ? ? ? 
3 water       nat water                                   18.015    143 ? ? ? ? 
# 
_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         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 SPERMIDINE SPD 
3 water      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 
SPD non-polymer         . SPERMIDINE      'N-(2-AMINO-PROPYL)-1,4-DIAMINOBUTANE; PA(34)' 'C7 H19 N3'      145.246 
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   7   ASP ASP 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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        SPD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   SPD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 SPD 1   201 201 SPD SPD A . 
C 3 HOH 1   301 8   HOH HOH A . 
C 3 HOH 2   302 110 HOH HOH A . 
C 3 HOH 3   303 75  HOH HOH A . 
C 3 HOH 4   304 66  HOH HOH A . 
C 3 HOH 5   305 60  HOH HOH A . 
C 3 HOH 6   306 140 HOH HOH A . 
C 3 HOH 7   307 117 HOH HOH A . 
C 3 HOH 8   308 43  HOH HOH A . 
C 3 HOH 9   309 109 HOH HOH A . 
C 3 HOH 10  310 131 HOH HOH A . 
C 3 HOH 11  311 71  HOH HOH A . 
C 3 HOH 12  312 119 HOH HOH A . 
C 3 HOH 13  313 10  HOH HOH A . 
C 3 HOH 14  314 40  HOH HOH A . 
C 3 HOH 15  315 13  HOH HOH A . 
C 3 HOH 16  316 79  HOH HOH A . 
C 3 HOH 17  317 38  HOH HOH A . 
C 3 HOH 18  318 62  HOH HOH A . 
C 3 HOH 19  319 47  HOH HOH A . 
C 3 HOH 20  320 107 HOH HOH A . 
C 3 HOH 21  321 84  HOH HOH A . 
C 3 HOH 22  322 18  HOH HOH A . 
C 3 HOH 23  323 48  HOH HOH A . 
C 3 HOH 24  324 82  HOH HOH A . 
C 3 HOH 25  325 55  HOH HOH A . 
C 3 HOH 26  326 114 HOH HOH A . 
C 3 HOH 27  327 25  HOH HOH A . 
C 3 HOH 28  328 99  HOH HOH A . 
C 3 HOH 29  329 50  HOH HOH A . 
C 3 HOH 30  330 113 HOH HOH A . 
C 3 HOH 31  331 34  HOH HOH A . 
C 3 HOH 32  332 95  HOH HOH A . 
C 3 HOH 33  333 6   HOH HOH A . 
C 3 HOH 34  334 11  HOH HOH A . 
C 3 HOH 35  335 2   HOH HOH A . 
C 3 HOH 36  336 1   HOH HOH A . 
C 3 HOH 37  337 132 HOH HOH A . 
C 3 HOH 38  338 29  HOH HOH A . 
C 3 HOH 39  339 57  HOH HOH A . 
C 3 HOH 40  340 111 HOH HOH A . 
C 3 HOH 41  341 4   HOH HOH A . 
C 3 HOH 42  342 12  HOH HOH A . 
C 3 HOH 43  343 56  HOH HOH A . 
C 3 HOH 44  344 141 HOH HOH A . 
C 3 HOH 45  345 123 HOH HOH A . 
C 3 HOH 46  346 52  HOH HOH A . 
C 3 HOH 47  347 144 HOH HOH A . 
C 3 HOH 48  348 46  HOH HOH A . 
C 3 HOH 49  349 83  HOH HOH A . 
C 3 HOH 50  350 22  HOH HOH A . 
C 3 HOH 51  351 7   HOH HOH A . 
C 3 HOH 52  352 42  HOH HOH A . 
C 3 HOH 53  353 59  HOH HOH A . 
C 3 HOH 54  354 30  HOH HOH A . 
C 3 HOH 55  355 129 HOH HOH A . 
C 3 HOH 56  356 125 HOH HOH A . 
C 3 HOH 57  357 68  HOH HOH A . 
C 3 HOH 58  358 16  HOH HOH A . 
C 3 HOH 59  359 81  HOH HOH A . 
C 3 HOH 60  360 64  HOH HOH A . 
C 3 HOH 61  361 139 HOH HOH A . 
C 3 HOH 62  362 142 HOH HOH A . 
C 3 HOH 63  363 44  HOH HOH A . 
C 3 HOH 64  364 32  HOH HOH A . 
C 3 HOH 65  365 51  HOH HOH A . 
C 3 HOH 66  366 45  HOH HOH A . 
C 3 HOH 67  367 26  HOH HOH A . 
C 3 HOH 68  368 76  HOH HOH A . 
C 3 HOH 69  369 127 HOH HOH A . 
C 3 HOH 70  370 112 HOH HOH A . 
C 3 HOH 71  371 70  HOH HOH A . 
C 3 HOH 72  372 65  HOH HOH A . 
C 3 HOH 73  373 54  HOH HOH A . 
C 3 HOH 74  374 135 HOH HOH A . 
C 3 HOH 75  375 23  HOH HOH A . 
C 3 HOH 76  376 5   HOH HOH A . 
C 3 HOH 77  377 97  HOH HOH A . 
C 3 HOH 78  378 122 HOH HOH A . 
C 3 HOH 79  379 3   HOH HOH A . 
C 3 HOH 80  380 118 HOH HOH A . 
C 3 HOH 81  381 31  HOH HOH A . 
C 3 HOH 82  382 19  HOH HOH A . 
C 3 HOH 83  383 108 HOH HOH A . 
C 3 HOH 84  384 33  HOH HOH A . 
C 3 HOH 85  385 69  HOH HOH A . 
C 3 HOH 86  386 74  HOH HOH A . 
C 3 HOH 87  387 28  HOH HOH A . 
C 3 HOH 88  388 61  HOH HOH A . 
C 3 HOH 89  389 35  HOH HOH A . 
C 3 HOH 90  390 27  HOH HOH A . 
C 3 HOH 91  391 21  HOH HOH A . 
C 3 HOH 92  392 17  HOH HOH A . 
C 3 HOH 93  393 101 HOH HOH A . 
C 3 HOH 94  394 41  HOH HOH A . 
C 3 HOH 95  395 102 HOH HOH A . 
C 3 HOH 96  396 133 HOH HOH A . 
C 3 HOH 97  397 24  HOH HOH A . 
C 3 HOH 98  398 20  HOH HOH A . 
C 3 HOH 99  399 39  HOH HOH A . 
C 3 HOH 100 400 80  HOH HOH A . 
C 3 HOH 101 401 53  HOH HOH A . 
C 3 HOH 102 402 105 HOH HOH A . 
C 3 HOH 103 403 36  HOH HOH A . 
C 3 HOH 104 404 116 HOH HOH A . 
C 3 HOH 105 405 72  HOH HOH A . 
C 3 HOH 106 406 15  HOH HOH A . 
C 3 HOH 107 407 58  HOH HOH A . 
C 3 HOH 108 408 126 HOH HOH A . 
C 3 HOH 109 409 78  HOH HOH A . 
C 3 HOH 110 410 87  HOH HOH A . 
C 3 HOH 111 411 85  HOH HOH A . 
C 3 HOH 112 412 14  HOH HOH A . 
C 3 HOH 113 413 93  HOH HOH A . 
C 3 HOH 114 414 88  HOH HOH A . 
C 3 HOH 115 415 73  HOH HOH A . 
C 3 HOH 116 416 138 HOH HOH A . 
C 3 HOH 117 417 63  HOH HOH A . 
C 3 HOH 118 418 115 HOH HOH A . 
C 3 HOH 119 419 9   HOH HOH A . 
C 3 HOH 120 420 94  HOH HOH A . 
C 3 HOH 121 421 100 HOH HOH A . 
C 3 HOH 122 422 37  HOH HOH A . 
C 3 HOH 123 423 86  HOH HOH A . 
C 3 HOH 124 424 90  HOH HOH A . 
C 3 HOH 125 425 128 HOH HOH A . 
C 3 HOH 126 426 136 HOH HOH A . 
C 3 HOH 127 427 67  HOH HOH A . 
C 3 HOH 128 428 134 HOH HOH A . 
C 3 HOH 129 429 120 HOH HOH A . 
C 3 HOH 130 430 130 HOH HOH A . 
C 3 HOH 131 431 77  HOH HOH A . 
C 3 HOH 132 432 91  HOH HOH A . 
C 3 HOH 133 433 121 HOH HOH A . 
C 3 HOH 134 434 106 HOH HOH A . 
C 3 HOH 135 435 89  HOH HOH A . 
C 3 HOH 136 436 124 HOH HOH A . 
C 3 HOH 137 437 104 HOH HOH A . 
C 3 HOH 138 438 92  HOH HOH A . 
C 3 HOH 139 439 137 HOH HOH A . 
C 3 HOH 140 440 98  HOH HOH A . 
C 3 HOH 141 441 49  HOH HOH A . 
C 3 HOH 142 442 103 HOH HOH A . 
C 3 HOH 143 443 143 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                     8WP7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.268 
_cell.length_a_esd                 ? 
_cell.length_b                     70.318 
_cell.length_b_esd                 ? 
_cell.length_c                     50.370 
_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                         8WP7 
_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                   8WP7 
_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             2.66 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.75 
_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 Sodium formate,
10% v/v Ethylene glycol, 
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   0.9791 
_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        0.9791 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          30.67 
_reflns.entry_id                                       8WP7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.91 
_reflns.d_resolution_low                               47.44 
_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                                     18423 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.300 
_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                                0.110 
_reflns.pdbx_Rpim_I_all                                0.036 
_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                              0.104 
_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                                    1.91 
_reflns_shell.d_res_low                                     2.01 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.800 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2641 
_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                               0.527 
_reflns_shell.pdbx_Rpim_I_all                               0.226 
_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                                  0.473 
_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                                 8WP7 
_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                            1.91 
_refine.ls_d_res_low                             35.16 
_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                     18389 
_refine.ls_number_reflns_R_free                  878 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 4.77 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1932 
_refine.ls_R_factor_R_free                       0.2238 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1917 
_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                          1.38 
_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                 23.09 
_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                            0.20 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.91 
_refine_hist.d_res_low                        35.16 
_refine_hist.number_atoms_solvent             143 
_refine_hist.number_atoms_total               1656 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1503 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003 ? 1535 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.564 ? 2064 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.410 ? 207  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.040 ? 231  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003 ? 267  ? 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' 1.91 2.03  . . 136 2850 99.00  . . . . 0.2487 . . . . . . . . . . . 0.2981 
'X-RAY DIFFRACTION' 2.03 2.18  . . 142 2871 100.00 . . . . 0.2101 . . . . . . . . . . . 0.2480 
'X-RAY DIFFRACTION' 2.18 2.40  . . 165 2892 100.00 . . . . 0.1909 . . . . . . . . . . . 0.2338 
'X-RAY DIFFRACTION' 2.40 2.75  . . 136 2880 100.00 . . . . 0.2080 . . . . . . . . . . . 0.2482 
'X-RAY DIFFRACTION' 2.75 3.46  . . 151 2935 100.00 . . . . 0.2033 . . . . . . . . . . . 0.2573 
'X-RAY DIFFRACTION' 3.46 35.16 . . 148 3083 100.00 . . . . 0.1705 . . . . . . . . . . . 0.1813 
# 
_struct.entry_id                     8WP7 
_struct.title                        
'Crystal structure of a TetR family regulator AmvR from Acinetobacter baumannii with spermidine bound' 
_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        8WP7 
_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 ? 
C N N 3 ? 
# 
_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              8WP7 
_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)' 3520  ? 
1 MORE         -4    ? 
1 'SSA (A^2)'  18640 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
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 1.0  0.0 0.0 0.0           0.0 1.0  0.0 0.0           0.0 0.0 1.0 0.0 
2 'point symmetry operation' ?     ?     -1.0 0.0 0.0 64.2680000000 0.0 -1.0 0.0 70.3180000000 0.0 0.0 1.0 0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 7   ? GLY A 25  ? ASP A 7   GLY A 25  1 ? 19 
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  ? LEU A 74  ? SER A 51  LEU A 74  1 ? 24 
HELX_P HELX_P5  AA5 SER A 78  ? LEU A 87  ? SER A 78  LEU A 87  1 ? 10 
HELX_P HELX_P6  AA6 LEU A 95  ? ILE A 109 ? LEU A 95  ILE A 109 1 ? 15 
HELX_P HELX_P7  AA7 ASP A 112 ? GLU A 140 ? ASP A 112 GLU A 140 1 ? 29 
HELX_P HELX_P8  AA8 ASN A 148 ? LYS A 168 ? ASN A 148 LYS A 168 1 ? 21 
HELX_P HELX_P9  AA9 ALA A 175 ? GLU A 177 ? ALA A 175 GLU A 177 5 ? 3  
HELX_P HELX_P10 AB1 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                   8WP7 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     91 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             54.15 
_pdbx_validate_torsion.psi             76.29 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x+1/2,y+1/2,-z 
4 -x,-y,z         
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         18.8677 
_pdbx_refine_tls.origin_y         27.2457 
_pdbx_refine_tls.origin_z         11.5422 
_pdbx_refine_tls.T[1][1]          0.1795 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0153 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0080 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2190 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0318 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2022 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.4021 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.5067 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.4993 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.7840 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.5654 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.6400 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0250 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0807 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0205 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0397 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.1197 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0999 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0142 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.2298 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0001 
_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 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 440 ? 5.85 . 
2 1 O ? A HOH 441 ? 6.15 . 
3 1 O ? A HOH 442 ? 6.31 . 
4 1 O ? A HOH 443 ? 6.37 . 
# 
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 
# 
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 
SPD N1   N N N 304 
SPD C2   C N N 305 
SPD C3   C N N 306 
SPD C4   C N N 307 
SPD C5   C N N 308 
SPD N6   N N N 309 
SPD C7   C N N 310 
SPD C8   C N N 311 
SPD C9   C N N 312 
SPD N10  N N N 313 
SPD HN11 H N N 314 
SPD HN12 H N N 315 
SPD H21  H N N 316 
SPD H22  H N N 317 
SPD H31  H N N 318 
SPD H32  H N N 319 
SPD H41  H N N 320 
SPD H42  H N N 321 
SPD H51  H N N 322 
SPD H52  H N N 323 
SPD HN6  H N N 324 
SPD H71  H N N 325 
SPD H72  H N N 326 
SPD H81  H N N 327 
SPD H82  H N N 328 
SPD H91  H N N 329 
SPD H92  H N N 330 
SPD H101 H N N 331 
SPD H102 H N N 332 
THR N    N N N 333 
THR CA   C N S 334 
THR C    C N N 335 
THR O    O N N 336 
THR CB   C N R 337 
THR OG1  O N N 338 
THR CG2  C N N 339 
THR OXT  O N N 340 
THR H    H N N 341 
THR H2   H N N 342 
THR HA   H N N 343 
THR HB   H N N 344 
THR HG1  H N N 345 
THR HG21 H N N 346 
THR HG22 H N N 347 
THR HG23 H N N 348 
THR HXT  H N N 349 
TRP N    N N N 350 
TRP CA   C N S 351 
TRP C    C N N 352 
TRP O    O N N 353 
TRP CB   C N N 354 
TRP CG   C Y N 355 
TRP CD1  C Y N 356 
TRP CD2  C Y N 357 
TRP NE1  N Y N 358 
TRP CE2  C Y N 359 
TRP CE3  C Y N 360 
TRP CZ2  C Y N 361 
TRP CZ3  C Y N 362 
TRP CH2  C Y N 363 
TRP OXT  O N N 364 
TRP H    H N N 365 
TRP H2   H N N 366 
TRP HA   H N N 367 
TRP HB2  H N N 368 
TRP HB3  H N N 369 
TRP HD1  H N N 370 
TRP HE1  H N N 371 
TRP HE3  H N N 372 
TRP HZ2  H N N 373 
TRP HZ3  H N N 374 
TRP HH2  H N N 375 
TRP HXT  H N N 376 
TYR N    N N N 377 
TYR CA   C N S 378 
TYR C    C N N 379 
TYR O    O N N 380 
TYR CB   C N N 381 
TYR CG   C Y N 382 
TYR CD1  C Y N 383 
TYR CD2  C Y N 384 
TYR CE1  C Y N 385 
TYR CE2  C Y N 386 
TYR CZ   C Y N 387 
TYR OH   O N N 388 
TYR OXT  O N N 389 
TYR H    H N N 390 
TYR H2   H N N 391 
TYR HA   H N N 392 
TYR HB2  H N N 393 
TYR HB3  H N N 394 
TYR HD1  H N N 395 
TYR HD2  H N N 396 
TYR HE1  H N N 397 
TYR HE2  H N N 398 
TYR HH   H N N 399 
TYR HXT  H N N 400 
VAL N    N N N 401 
VAL CA   C N S 402 
VAL C    C N N 403 
VAL O    O N N 404 
VAL CB   C N N 405 
VAL CG1  C N N 406 
VAL CG2  C N N 407 
VAL OXT  O N N 408 
VAL H    H N N 409 
VAL H2   H N N 410 
VAL HA   H N N 411 
VAL HB   H N N 412 
VAL HG11 H N N 413 
VAL HG12 H N N 414 
VAL HG13 H N N 415 
VAL HG21 H N N 416 
VAL HG22 H N N 417 
VAL HG23 H N N 418 
VAL HXT  H N N 419 
# 
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 
SPD N1  C2   sing N N 290 
SPD N1  HN11 sing N N 291 
SPD N1  HN12 sing N N 292 
SPD C2  C3   sing N N 293 
SPD C2  H21  sing N N 294 
SPD C2  H22  sing N N 295 
SPD C3  C4   sing N N 296 
SPD C3  H31  sing N N 297 
SPD C3  H32  sing N N 298 
SPD C4  C5   sing N N 299 
SPD C4  H41  sing N N 300 
SPD C4  H42  sing N N 301 
SPD C5  N6   sing N N 302 
SPD C5  H51  sing N N 303 
SPD C5  H52  sing N N 304 
SPD N6  C7   sing N N 305 
SPD N6  HN6  sing N N 306 
SPD C7  C8   sing N N 307 
SPD C7  H71  sing N N 308 
SPD C7  H72  sing N N 309 
SPD C8  C9   sing N N 310 
SPD C8  H81  sing N N 311 
SPD C8  H82  sing N N 312 
SPD C9  N10  sing N N 313 
SPD C9  H91  sing N N 314 
SPD C9  H92  sing N N 315 
SPD N10 H101 sing N N 316 
SPD N10 H102 sing N N 317 
THR N   CA   sing N N 318 
THR N   H    sing N N 319 
THR N   H2   sing N N 320 
THR CA  C    sing N N 321 
THR CA  CB   sing N N 322 
THR CA  HA   sing N N 323 
THR C   O    doub N N 324 
THR C   OXT  sing N N 325 
THR CB  OG1  sing N N 326 
THR CB  CG2  sing N N 327 
THR CB  HB   sing N N 328 
THR OG1 HG1  sing N N 329 
THR CG2 HG21 sing N N 330 
THR CG2 HG22 sing N N 331 
THR CG2 HG23 sing N N 332 
THR OXT HXT  sing N N 333 
TRP N   CA   sing N N 334 
TRP N   H    sing N N 335 
TRP N   H2   sing N N 336 
TRP CA  C    sing N N 337 
TRP CA  CB   sing N N 338 
TRP CA  HA   sing N N 339 
TRP C   O    doub N N 340 
TRP C   OXT  sing N N 341 
TRP CB  CG   sing N N 342 
TRP CB  HB2  sing N N 343 
TRP CB  HB3  sing N N 344 
TRP CG  CD1  doub Y N 345 
TRP CG  CD2  sing Y N 346 
TRP CD1 NE1  sing Y N 347 
TRP CD1 HD1  sing N N 348 
TRP CD2 CE2  doub Y N 349 
TRP CD2 CE3  sing Y N 350 
TRP NE1 CE2  sing Y N 351 
TRP NE1 HE1  sing N N 352 
TRP CE2 CZ2  sing Y N 353 
TRP CE3 CZ3  doub Y N 354 
TRP CE3 HE3  sing N N 355 
TRP CZ2 CH2  doub Y N 356 
TRP CZ2 HZ2  sing N N 357 
TRP CZ3 CH2  sing Y N 358 
TRP CZ3 HZ3  sing N N 359 
TRP CH2 HH2  sing N N 360 
TRP OXT HXT  sing N N 361 
TYR N   CA   sing N N 362 
TYR N   H    sing N N 363 
TYR N   H2   sing N N 364 
TYR CA  C    sing N N 365 
TYR CA  CB   sing N N 366 
TYR CA  HA   sing N N 367 
TYR C   O    doub N N 368 
TYR C   OXT  sing N N 369 
TYR CB  CG   sing N N 370 
TYR CB  HB2  sing N N 371 
TYR CB  HB3  sing N N 372 
TYR CG  CD1  doub Y N 373 
TYR CG  CD2  sing Y N 374 
TYR CD1 CE1  sing Y N 375 
TYR CD1 HD1  sing N N 376 
TYR CD2 CE2  doub Y N 377 
TYR CD2 HD2  sing N N 378 
TYR CE1 CZ   doub Y N 379 
TYR CE1 HE1  sing N N 380 
TYR CE2 CZ   sing Y N 381 
TYR CE2 HE2  sing N N 382 
TYR CZ  OH   sing N N 383 
TYR OH  HH   sing N N 384 
TYR OXT HXT  sing N N 385 
VAL N   CA   sing N N 386 
VAL N   H    sing N N 387 
VAL N   H2   sing N N 388 
VAL CA  C    sing N N 389 
VAL CA  CB   sing N N 390 
VAL CA  HA   sing N N 391 
VAL C   O    doub N N 392 
VAL C   OXT  sing N N 393 
VAL CB  CG1  sing N N 394 
VAL CB  CG2  sing N N 395 
VAL CB  HB   sing N N 396 
VAL CG1 HG11 sing N N 397 
VAL CG1 HG12 sing N N 398 
VAL CG1 HG13 sing N N 399 
VAL CG2 HG21 sing N N 400 
VAL CG2 HG22 sing N N 401 
VAL CG2 HG23 sing N N 402 
VAL OXT HXT  sing N N 403 
# 
_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          ? 
# 
_space_group.name_H-M_alt     'P 21 21 2' 
_space_group.name_Hall        'P 2 2ab' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8WP7 
_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]   0.015560 
_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]   0.014221 
_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]   0.019853 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP A 1 7   ? 6.226  8.172  25.537  1.00 54.51 ? 7   ASP A N   1 
ATOM   2    C CA  . ASP A 1 7   ? 6.199  8.127  24.075  1.00 65.55 ? 7   ASP A CA  1 
ATOM   3    C C   . ASP A 1 7   ? 5.645  9.431  23.507  1.00 61.08 ? 7   ASP A C   1 
ATOM   4    O O   . ASP A 1 7   ? 6.409  10.330 23.140  1.00 47.26 ? 7   ASP A O   1 
ATOM   5    C CB  . ASP A 1 7   ? 5.387  6.916  23.581  1.00 63.77 ? 7   ASP A CB  1 
ATOM   6    C CG  . ASP A 1 7   ? 4.017  6.811  24.236  1.00 63.42 ? 7   ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 7   ? 3.084  7.505  23.774  1.00 59.95 ? 7   ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 7   ? 3.872  6.034  25.204  1.00 63.21 ? 7   ASP A OD2 1 
ATOM   9    N N   . GLN A 1 8   ? 4.316  9.533  23.426  1.00 57.00 ? 8   GLN A N   1 
ATOM   10   C CA  . GLN A 1 8   ? 3.705  10.816 23.110  1.00 45.00 ? 8   GLN A CA  1 
ATOM   11   C C   . GLN A 1 8   ? 3.870  11.789 24.268  1.00 32.80 ? 8   GLN A C   1 
ATOM   12   O O   . GLN A 1 8   ? 3.997  12.996 24.048  1.00 36.69 ? 8   GLN A O   1 
ATOM   13   C CB  . GLN A 1 8   ? 2.226  10.629 22.755  1.00 44.62 ? 8   GLN A CB  1 
ATOM   14   C CG  . GLN A 1 8   ? 1.338  11.819 23.090  1.00 43.10 ? 8   GLN A CG  1 
ATOM   15   C CD  . GLN A 1 8   ? 0.074  11.875 22.248  1.00 62.08 ? 8   GLN A CD  1 
ATOM   16   O OE1 . GLN A 1 8   ? 0.132  11.960 21.019  1.00 55.87 ? 8   GLN A OE1 1 
ATOM   17   N NE2 . GLN A 1 8   ? -1.078 11.843 22.911  1.00 51.66 ? 8   GLN A NE2 1 
ATOM   18   N N   . ARG A 1 9   ? 3.906  11.283 25.502  1.00 35.45 ? 9   ARG A N   1 
ATOM   19   C CA  . ARG A 1 9   ? 4.097  12.167 26.646  1.00 33.96 ? 9   ARG A CA  1 
ATOM   20   C C   . ARG A 1 9   ? 5.503  12.760 26.656  1.00 33.58 ? 9   ARG A C   1 
ATOM   21   O O   . ARG A 1 9   ? 5.689  13.922 27.036  1.00 29.17 ? 9   ARG A O   1 
ATOM   22   C CB  . ARG A 1 9   ? 3.785  11.415 27.942  1.00 37.75 ? 9   ARG A CB  1 
ATOM   23   C CG  . ARG A 1 9   ? 2.277  11.241 28.154  1.00 37.08 ? 9   ARG A CG  1 
ATOM   24   C CD  . ARG A 1 9   ? 1.919  10.552 29.465  1.00 35.42 ? 9   ARG A CD  1 
ATOM   25   N NE  . ARG A 1 9   ? 2.336  9.154  29.470  1.00 39.98 ? 9   ARG A NE  1 
ATOM   26   C CZ  . ARG A 1 9   ? 1.967  8.263  30.380  1.00 45.38 ? 9   ARG A CZ  1 
ATOM   27   N NH1 . ARG A 1 9   ? 1.160  8.587  31.377  1.00 31.76 ? 9   ARG A NH1 1 
ATOM   28   N NH2 . ARG A 1 9   ? 2.408  7.012  30.279  1.00 42.81 ? 9   ARG A NH2 1 
ATOM   29   N N   . ARG A 1 10  ? 6.503  11.991 26.219  1.00 31.79 ? 10  ARG A N   1 
ATOM   30   C CA  . ARG A 1 10  ? 7.827  12.575 26.023  1.00 32.70 ? 10  ARG A CA  1 
ATOM   31   C C   . ARG A 1 10  ? 7.780  13.670 24.966  1.00 27.80 ? 10  ARG A C   1 
ATOM   32   O O   . ARG A 1 10  ? 8.372  14.741 25.139  1.00 29.74 ? 10  ARG A O   1 
ATOM   33   C CB  . ARG A 1 10  ? 8.833  11.492 25.632  1.00 37.60 ? 10  ARG A CB  1 
ATOM   34   C CG  . ARG A 1 10  ? 10.244 12.019 25.450  1.00 31.89 ? 10  ARG A CG  1 
ATOM   35   C CD  . ARG A 1 10  ? 11.222 10.923 25.042  1.00 35.59 ? 10  ARG A CD  1 
ATOM   36   N NE  . ARG A 1 10  ? 12.601 11.314 25.311  1.00 34.10 ? 10  ARG A NE  1 
ATOM   37   C CZ  . ARG A 1 10  ? 13.359 12.026 24.488  1.00 31.87 ? 10  ARG A CZ  1 
ATOM   38   N NH1 . ARG A 1 10  ? 12.904 12.452 23.322  1.00 31.40 ? 10  ARG A NH1 1 
ATOM   39   N NH2 . ARG A 1 10  ? 14.604 12.328 24.850  1.00 26.29 ? 10  ARG A NH2 1 
ATOM   40   N N   . GLU A 1 11  ? 7.048  13.432 23.875  1.00 30.65 ? 11  GLU A N   1 
ATOM   41   C CA  . GLU A 1 11  ? 6.942  14.433 22.820  1.00 32.71 ? 11  GLU A CA  1 
ATOM   42   C C   . GLU A 1 11  ? 6.247  15.698 23.313  1.00 30.67 ? 11  GLU A C   1 
ATOM   43   O O   . GLU A 1 11  ? 6.596  16.807 22.895  1.00 28.45 ? 11  GLU A O   1 
ATOM   44   C CB  . GLU A 1 11  ? 6.212  13.842 21.612  1.00 41.46 ? 11  GLU A CB  1 
ATOM   45   C CG  . GLU A 1 11  ? 5.851  14.867 20.547  1.00 47.04 ? 11  GLU A CG  1 
ATOM   46   C CD  . GLU A 1 11  ? 7.037  15.250 19.679  1.00 46.46 ? 11  GLU A CD  1 
ATOM   47   O OE1 . GLU A 1 11  ? 7.993  14.451 19.582  1.00 48.16 ? 11  GLU A OE1 1 
ATOM   48   O OE2 . GLU A 1 11  ? 7.011  16.356 19.096  1.00 59.04 ? 11  GLU A OE2 1 
ATOM   49   N N   . MET A 1 12  ? 5.265  15.560 24.208  1.00 31.95 ? 12  MET A N   1 
ATOM   50   C CA  . MET A 1 12  ? 4.599  16.757 24.718  1.00 29.31 ? 12  MET A CA  1 
ATOM   51   C C   . MET A 1 12  ? 5.504  17.558 25.643  1.00 25.28 ? 12  MET A C   1 
ATOM   52   O O   . MET A 1 12  ? 5.410  18.790 25.675  1.00 30.91 ? 12  MET A O   1 
ATOM   53   C CB  . MET A 1 12  ? 3.294  16.399 25.430  1.00 32.87 ? 12  MET A CB  1 
ATOM   54   C CG  . MET A 1 12  ? 2.386  15.472 24.638  1.00 48.94 ? 12  MET A CG  1 
ATOM   55   S SD  . MET A 1 12  ? 1.930  16.085 22.995  1.00 67.50 ? 12  MET A SD  1 
ATOM   56   C CE  . MET A 1 12  ? 1.501  17.793 23.336  1.00 48.24 ? 12  MET A CE  1 
ATOM   57   N N   . ILE A 1 13  ? 6.384  16.896 26.395  1.00 24.15 ? 13  ILE A N   1 
ATOM   58   C CA  . ILE A 1 13  ? 7.387  17.634 27.158  1.00 24.35 ? 13  ILE A CA  1 
ATOM   59   C C   . ILE A 1 13  ? 8.297  18.406 26.208  1.00 27.38 ? 13  ILE A C   1 
ATOM   60   O O   . ILE A 1 13  ? 8.579  19.596 26.408  1.00 25.47 ? 13  ILE A O   1 
ATOM   61   C CB  . ILE A 1 13  ? 8.191  16.676 28.055  1.00 23.87 ? 13  ILE A CB  1 
ATOM   62   C CG1 . ILE A 1 13  ? 7.312  16.137 29.182  1.00 29.93 ? 13  ILE A CG1 1 
ATOM   63   C CG2 . ILE A 1 13  ? 9.416  17.382 28.612  1.00 27.61 ? 13  ILE A CG2 1 
ATOM   64   C CD1 . ILE A 1 13  ? 7.871  14.889 29.857  1.00 30.19 ? 13  ILE A CD1 1 
ATOM   65   N N   . LEU A 1 14  ? 8.764  17.733 25.156  1.00 24.79 ? 14  LEU A N   1 
ATOM   66   C CA  . LEU A 1 14  ? 9.597  18.385 24.149  1.00 27.78 ? 14  LEU A CA  1 
ATOM   67   C C   . LEU A 1 14  ? 8.895  19.601 23.553  1.00 28.92 ? 14  LEU A C   1 
ATOM   68   O O   . LEU A 1 14  ? 9.511  20.658 23.383  1.00 26.77 ? 14  LEU A O   1 
ATOM   69   C CB  . LEU A 1 14  ? 9.956  17.380 23.056  1.00 30.85 ? 14  LEU A CB  1 
ATOM   70   C CG  . LEU A 1 14  ? 11.091 17.693 22.089  1.00 35.34 ? 14  LEU A CG  1 
ATOM   71   C CD1 . LEU A 1 14  ? 12.325 18.187 22.846  1.00 29.82 ? 14  LEU A CD1 1 
ATOM   72   C CD2 . LEU A 1 14  ? 11.416 16.461 21.248  1.00 42.44 ? 14  LEU A CD2 1 
ATOM   73   N N   . GLN A 1 15  ? 7.596  19.481 23.258  1.00 30.43 ? 15  GLN A N   1 
ATOM   74   C CA  . GLN A 1 15  ? 6.860  20.602 22.676  1.00 33.56 ? 15  GLN A CA  1 
ATOM   75   C C   . GLN A 1 15  ? 6.774  21.780 23.639  1.00 32.35 ? 15  GLN A C   1 
ATOM   76   O O   . GLN A 1 15  ? 6.850  22.939 23.215  1.00 31.38 ? 15  GLN A O   1 
ATOM   77   C CB  . GLN A 1 15  ? 5.458  20.152 22.259  1.00 33.55 ? 15  GLN A CB  1 
ATOM   78   C CG  . GLN A 1 15  ? 5.447  19.306 21.002  1.00 37.01 ? 15  GLN A CG  1 
ATOM   79   C CD  . GLN A 1 15  ? 5.895  20.084 19.780  1.00 41.83 ? 15  GLN A CD  1 
ATOM   80   O OE1 . GLN A 1 15  ? 5.684  21.295 19.689  1.00 41.93 ? 15  GLN A OE1 1 
ATOM   81   N NE2 . GLN A 1 15  ? 6.528  19.393 18.838  1.00 47.00 ? 15  GLN A NE2 1 
ATOM   82   N N   . ALA A 1 16  ? 6.592  21.508 24.936  1.00 31.36 ? 16  ALA A N   1 
ATOM   83   C CA  . ALA A 1 16  ? 6.604  22.587 25.917  1.00 26.73 ? 16  ALA A CA  1 
ATOM   84   C C   . ALA A 1 16  ? 7.962  23.279 25.951  1.00 30.10 ? 16  ALA A C   1 
ATOM   85   O O   . ALA A 1 16  ? 8.040  24.514 25.993  1.00 28.78 ? 16  ALA A O   1 
ATOM   86   C CB  . ALA A 1 16  ? 6.238  22.048 27.299  1.00 31.11 ? 16  ALA A CB  1 
ATOM   87   N N   . ALA A 1 17  ? 9.045  22.501 25.918  1.00 25.15 ? 17  ALA A N   1 
ATOM   88   C CA  . ALA A 1 17  ? 10.378 23.095 25.908  1.00 28.05 ? 17  ALA A CA  1 
ATOM   89   C C   . ALA A 1 17  ? 10.587 23.966 24.674  1.00 28.33 ? 17  ALA A C   1 
ATOM   90   O O   . ALA A 1 17  ? 11.202 25.036 24.754  1.00 29.75 ? 17  ALA A O   1 
ATOM   91   C CB  . ALA A 1 17  ? 11.438 21.995 25.975  1.00 25.24 ? 17  ALA A CB  1 
ATOM   92   N N   . MET A 1 18  ? 10.079 23.521 23.521  1.00 29.09 ? 18  MET A N   1 
ATOM   93   C CA  . MET A 1 18  ? 10.237 24.286 22.286  1.00 29.91 ? 18  MET A CA  1 
ATOM   94   C C   . MET A 1 18  ? 9.507  25.621 22.367  1.00 31.50 ? 18  MET A C   1 
ATOM   95   O O   . MET A 1 18  ? 10.016 26.644 21.892  1.00 31.87 ? 18  MET A O   1 
ATOM   96   C CB  . MET A 1 18  ? 9.731  23.460 21.103  1.00 28.24 ? 18  MET A CB  1 
ATOM   97   C CG  . MET A 1 18  ? 10.450 22.124 20.975  1.00 28.44 ? 18  MET A CG  1 
ATOM   98   S SD  . MET A 1 18  ? 9.748  20.978 19.767  1.00 32.53 ? 18  MET A SD  1 
ATOM   99   C CE  . MET A 1 18  ? 9.052  22.109 18.564  1.00 31.50 ? 18  MET A CE  1 
ATOM   100  N N   . GLN A 1 19  ? 8.310  25.628 22.962  1.00 30.51 ? 19  GLN A N   1 
ATOM   101  C CA  . GLN A 1 19  ? 7.561  26.870 23.136  1.00 28.80 ? 19  GLN A CA  1 
ATOM   102  C C   . GLN A 1 19  ? 8.352  27.883 23.953  1.00 33.11 ? 19  GLN A C   1 
ATOM   103  O O   . GLN A 1 19  ? 8.461  29.055 23.573  1.00 35.14 ? 19  GLN A O   1 
ATOM   104  C CB  . GLN A 1 19  ? 6.219  26.584 23.814  1.00 31.83 ? 19  GLN A CB  1 
ATOM   105  C CG  . GLN A 1 19  ? 5.077  27.452 23.324  1.00 47.40 ? 19  GLN A CG  1 
ATOM   106  C CD  . GLN A 1 19  ? 3.756  26.703 23.270  1.00 65.09 ? 19  GLN A CD  1 
ATOM   107  O OE1 . GLN A 1 19  ? 3.521  25.886 22.377  1.00 67.52 ? 19  GLN A OE1 1 
ATOM   108  N NE2 . GLN A 1 19  ? 2.888  26.977 24.236  1.00 59.44 ? 19  GLN A NE2 1 
ATOM   109  N N   . ILE A 1 20  ? 8.895  27.454 25.095  1.00 33.24 ? 20  ILE A N   1 
ATOM   110  C CA  . ILE A 1 20  ? 9.692  28.355 25.926  1.00 32.24 ? 20  ILE A CA  1 
ATOM   111  C C   . ILE A 1 20  ? 10.927 28.824 25.167  1.00 34.17 ? 20  ILE A C   1 
ATOM   112  O O   . ILE A 1 20  ? 11.296 30.005 25.216  1.00 32.79 ? 20  ILE A O   1 
ATOM   113  C CB  . ILE A 1 20  ? 10.071 27.666 27.250  1.00 28.67 ? 20  ILE A CB  1 
ATOM   114  C CG1 . ILE A 1 20  ? 8.824  27.395 28.096  1.00 36.11 ? 20  ILE A CG1 1 
ATOM   115  C CG2 . ILE A 1 20  ? 11.075 28.512 28.025  1.00 30.09 ? 20  ILE A CG2 1 
ATOM   116  C CD1 . ILE A 1 20  ? 8.965  26.187 29.011  1.00 37.62 ? 20  ILE A CD1 1 
ATOM   117  N N   . ALA A 1 21  ? 11.585 27.907 24.453  1.00 31.56 ? 21  ALA A N   1 
ATOM   118  C CA  . ALA A 1 21  ? 12.780 28.264 23.695  1.00 34.98 ? 21  ALA A CA  1 
ATOM   119  C C   . ALA A 1 21  ? 12.496 29.401 22.721  1.00 33.84 ? 21  ALA A C   1 
ATOM   120  O O   . ALA A 1 21  ? 13.187 30.425 22.726  1.00 33.72 ? 21  ALA A O   1 
ATOM   121  C CB  . ALA A 1 21  ? 13.308 27.037 22.952  1.00 32.16 ? 21  ALA A CB  1 
ATOM   122  N N   . LEU A 1 22  ? 11.466 29.237 21.885  1.00 33.25 ? 22  LEU A N   1 
ATOM   123  C CA  . LEU A 1 22  ? 11.119 30.254 20.895  1.00 40.41 ? 22  LEU A CA  1 
ATOM   124  C C   . LEU A 1 22  ? 10.816 31.594 21.553  1.00 44.05 ? 22  LEU A C   1 
ATOM   125  O O   . LEU A 1 22  ? 11.324 32.639 21.130  1.00 44.88 ? 22  LEU A O   1 
ATOM   126  C CB  . LEU A 1 22  ? 9.914  29.792 20.074  1.00 38.32 ? 22  LEU A CB  1 
ATOM   127  C CG  . LEU A 1 22  ? 10.140 29.052 18.758  1.00 39.78 ? 22  LEU A CG  1 
ATOM   128  C CD1 . LEU A 1 22  ? 8.843  29.012 17.961  1.00 42.01 ? 22  LEU A CD1 1 
ATOM   129  C CD2 . LEU A 1 22  ? 11.250 29.702 17.950  1.00 36.02 ? 22  LEU A CD2 1 
ATOM   130  N N   . ALA A 1 23  ? 9.986  31.580 22.596  1.00 38.44 ? 23  ALA A N   1 
ATOM   131  C CA  . ALA A 1 23  ? 9.499  32.824 23.176  1.00 38.63 ? 23  ALA A CA  1 
ATOM   132  C C   . ALA A 1 23  ? 10.517 33.487 24.095  1.00 44.68 ? 23  ALA A C   1 
ATOM   133  O O   . ALA A 1 23  ? 10.578 34.721 24.152  1.00 40.78 ? 23  ALA A O   1 
ATOM   134  C CB  . ALA A 1 23  ? 8.201  32.567 23.944  1.00 37.99 ? 23  ALA A CB  1 
ATOM   135  N N   . GLU A 1 24  ? 11.320 32.706 24.822  1.00 37.13 ? 24  GLU A N   1 
ATOM   136  C CA  . GLU A 1 24  ? 12.137 33.263 25.892  1.00 39.49 ? 24  GLU A CA  1 
ATOM   137  C C   . GLU A 1 24  ? 13.607 32.859 25.873  1.00 38.57 ? 24  GLU A C   1 
ATOM   138  O O   . GLU A 1 24  ? 14.386 33.439 26.637  1.00 43.81 ? 24  GLU A O   1 
ATOM   139  C CB  . GLU A 1 24  ? 11.539 32.892 27.259  1.00 43.41 ? 24  GLU A CB  1 
ATOM   140  C CG  . GLU A 1 24  ? 10.099 33.368 27.442  1.00 46.69 ? 24  GLU A CG  1 
ATOM   141  C CD  . GLU A 1 24  ? 9.451  32.834 28.705  1.00 48.29 ? 24  GLU A CD  1 
ATOM   142  O OE1 . GLU A 1 24  ? 10.042 33.002 29.795  1.00 48.54 ? 24  GLU A OE1 1 
ATOM   143  O OE2 . GLU A 1 24  ? 8.345  32.257 28.609  1.00 45.46 ? 24  GLU A OE2 1 
ATOM   144  N N   . GLY A 1 25  ? 14.016 31.900 25.043  1.00 35.49 ? 25  GLY A N   1 
ATOM   145  C CA  . GLY A 1 25  ? 15.414 31.518 24.969  1.00 32.28 ? 25  GLY A CA  1 
ATOM   146  C C   . GLY A 1 25  ? 15.792 30.397 25.923  1.00 35.33 ? 25  GLY A C   1 
ATOM   147  O O   . GLY A 1 25  ? 14.975 29.853 26.671  1.00 35.19 ? 25  GLY A O   1 
ATOM   148  N N   . PHE A 1 26  ? 17.087 30.066 25.898  1.00 34.67 ? 26  PHE A N   1 
ATOM   149  C CA  . PHE A 1 26  ? 17.587 28.891 26.611  1.00 32.32 ? 26  PHE A CA  1 
ATOM   150  C C   . PHE A 1 26  ? 17.582 29.077 28.126  1.00 34.52 ? 26  PHE A C   1 
ATOM   151  O O   . PHE A 1 26  ? 17.276 28.132 28.864  1.00 29.34 ? 26  PHE A O   1 
ATOM   152  C CB  . PHE A 1 26  ? 18.996 28.539 26.124  1.00 32.93 ? 26  PHE A CB  1 
ATOM   153  C CG  . PHE A 1 26  ? 19.039 27.978 24.727  1.00 32.97 ? 26  PHE A CG  1 
ATOM   154  C CD1 . PHE A 1 26  ? 18.576 26.694 24.473  1.00 28.61 ? 26  PHE A CD1 1 
ATOM   155  C CD2 . PHE A 1 26  ? 19.530 28.729 23.670  1.00 32.22 ? 26  PHE A CD2 1 
ATOM   156  C CE1 . PHE A 1 26  ? 18.613 26.164 23.194  1.00 28.73 ? 26  PHE A CE1 1 
ATOM   157  C CE2 . PHE A 1 26  ? 19.568 28.204 22.384  1.00 29.19 ? 26  PHE A CE2 1 
ATOM   158  C CZ  . PHE A 1 26  ? 19.109 26.924 22.148  1.00 27.07 ? 26  PHE A CZ  1 
ATOM   159  N N   . THR A 1 27  ? 17.936 30.268 28.621  1.00 33.56 ? 27  THR A N   1 
ATOM   160  C CA  . THR A 1 27  ? 18.056 30.428 30.071  1.00 37.03 ? 27  THR A CA  1 
ATOM   161  C C   . THR A 1 27  ? 16.732 30.167 30.778  1.00 30.77 ? 27  THR A C   1 
ATOM   162  O O   . THR A 1 27  ? 16.719 29.681 31.915  1.00 32.66 ? 27  THR A O   1 
ATOM   163  C CB  . THR A 1 27  ? 18.579 31.821 30.427  1.00 40.72 ? 27  THR A CB  1 
ATOM   164  O OG1 . THR A 1 27  ? 19.693 32.145 29.590  1.00 44.02 ? 27  THR A OG1 1 
ATOM   165  C CG2 . THR A 1 27  ? 19.024 31.864 31.885  1.00 37.66 ? 27  THR A CG2 1 
ATOM   166  N N   . ALA A 1 28  ? 15.612 30.450 30.114  1.00 29.49 ? 28  ALA A N   1 
ATOM   167  C CA  . ALA A 1 28  ? 14.303 30.195 30.704  1.00 32.78 ? 28  ALA A CA  1 
ATOM   168  C C   . ALA A 1 28  ? 13.939 28.714 30.748  1.00 32.20 ? 28  ALA A C   1 
ATOM   169  O O   . ALA A 1 28  ? 13.006 28.350 31.475  1.00 31.52 ? 28  ALA A O   1 
ATOM   170  C CB  . ALA A 1 28  ? 13.224 30.960 29.936  1.00 32.18 ? 28  ALA A CB  1 
ATOM   171  N N   . MET A 1 29  ? 14.637 27.856 30.006  1.00 26.74 ? 29  MET A N   1 
ATOM   172  C CA  . MET A 1 29  ? 14.236 26.453 29.883  1.00 30.16 ? 29  MET A CA  1 
ATOM   173  C C   . MET A 1 29  ? 14.779 25.613 31.038  1.00 30.24 ? 29  MET A C   1 
ATOM   174  O O   . MET A 1 29  ? 15.534 24.659 30.842  1.00 29.81 ? 29  MET A O   1 
ATOM   175  C CB  . MET A 1 29  ? 14.695 25.877 28.548  1.00 27.49 ? 29  MET A CB  1 
ATOM   176  C CG  . MET A 1 29  ? 14.189 26.607 27.319  1.00 34.62 ? 29  MET A CG  1 
ATOM   177  S SD  . MET A 1 29  ? 15.116 26.105 25.856  1.00 34.23 ? 29  MET A SD  1 
ATOM   178  C CE  . MET A 1 29  ? 14.550 24.415 25.680  1.00 27.22 ? 29  MET A CE  1 
ATOM   179  N N   . THR A 1 30  ? 14.391 25.976 32.257  1.00 30.80 ? 30  THR A N   1 
ATOM   180  C CA  . THR A 1 30  ? 14.693 25.092 33.370  1.00 29.49 ? 30  THR A CA  1 
ATOM   181  C C   . THR A 1 30  ? 13.713 23.925 33.365  1.00 31.99 ? 30  THR A C   1 
ATOM   182  O O   . THR A 1 30  ? 12.612 24.006 32.808  1.00 26.18 ? 30  THR A O   1 
ATOM   183  C CB  . THR A 1 30  ? 14.607 25.824 34.707  1.00 31.67 ? 30  THR A CB  1 
ATOM   184  O OG1 . THR A 1 30  ? 13.262 26.258 34.921  1.00 29.81 ? 30  THR A OG1 1 
ATOM   185  C CG2 . THR A 1 30  ? 15.524 27.039 34.703  1.00 29.68 ? 30  THR A CG2 1 
ATOM   186  N N   . VAL A 1 31  ? 14.132 22.824 33.991  1.00 29.07 ? 31  VAL A N   1 
ATOM   187  C CA  . VAL A 1 31  ? 13.267 21.654 34.095  1.00 26.63 ? 31  VAL A CA  1 
ATOM   188  C C   . VAL A 1 31  ? 11.989 22.005 34.844  1.00 30.67 ? 31  VAL A C   1 
ATOM   189  O O   . VAL A 1 31  ? 10.891 21.579 34.465  1.00 27.09 ? 31  VAL A O   1 
ATOM   190  C CB  . VAL A 1 31  ? 14.023 20.494 34.765  1.00 25.19 ? 31  VAL A CB  1 
ATOM   191  C CG1 . VAL A 1 31  ? 13.047 19.405 35.234  1.00 27.51 ? 31  VAL A CG1 1 
ATOM   192  C CG2 . VAL A 1 31  ? 15.052 19.920 33.799  1.00 26.06 ? 31  VAL A CG2 1 
ATOM   193  N N   . ARG A 1 32  ? 12.112 22.802 35.908  1.00 30.55 ? 32  ARG A N   1 
ATOM   194  C CA  . ARG A 1 32  ? 10.946 23.246 36.664  1.00 30.41 ? 32  ARG A CA  1 
ATOM   195  C C   . ARG A 1 32  ? 9.959  23.986 35.767  1.00 34.40 ? 32  ARG A C   1 
ATOM   196  O O   . ARG A 1 32  ? 8.753  23.709 35.782  1.00 28.92 ? 32  ARG A O   1 
ATOM   197  C CB  . ARG A 1 32  ? 11.406 24.136 37.824  1.00 39.65 ? 32  ARG A CB  1 
ATOM   198  C CG  . ARG A 1 32  ? 10.319 24.566 38.795  1.00 49.40 ? 32  ARG A CG  1 
ATOM   199  C CD  . ARG A 1 32  ? 9.607  23.374 39.400  1.00 46.36 ? 32  ARG A CD  1 
ATOM   200  N NE  . ARG A 1 32  ? 8.363  23.087 38.696  1.00 53.33 ? 32  ARG A NE  1 
ATOM   201  C CZ  . ARG A 1 32  ? 7.529  22.107 39.014  1.00 51.02 ? 32  ARG A CZ  1 
ATOM   202  N NH1 . ARG A 1 32  ? 7.775  21.291 40.027  1.00 44.44 ? 32  ARG A NH1 1 
ATOM   203  N NH2 . ARG A 1 32  ? 6.421  21.942 38.297  1.00 53.33 ? 32  ARG A NH2 1 
ATOM   204  N N   . ARG A 1 33  ? 10.461 24.930 34.969  1.00 30.73 ? 33  ARG A N   1 
ATOM   205  C CA  . ARG A 1 33  ? 9.605  25.677 34.054  1.00 30.48 ? 33  ARG A CA  1 
ATOM   206  C C   . ARG A 1 33  ? 8.937  24.760 33.034  1.00 31.42 ? 33  ARG A C   1 
ATOM   207  O O   . ARG A 1 33  ? 7.733  24.867 32.778  1.00 29.34 ? 33  ARG A O   1 
ATOM   208  C CB  . ARG A 1 33  ? 10.430 26.750 33.346  1.00 36.73 ? 33  ARG A CB  1 
ATOM   209  C CG  . ARG A 1 33  ? 9.645  27.573 32.354  1.00 36.23 ? 33  ARG A CG  1 
ATOM   210  C CD  . ARG A 1 33  ? 8.733  28.578 33.029  1.00 38.92 ? 33  ARG A CD  1 
ATOM   211  N NE  . ARG A 1 33  ? 7.819  29.157 32.052  1.00 46.01 ? 33  ARG A NE  1 
ATOM   212  C CZ  . ARG A 1 33  ? 8.110  30.208 31.298  1.00 43.68 ? 33  ARG A CZ  1 
ATOM   213  N NH1 . ARG A 1 33  ? 9.273  30.832 31.403  1.00 35.98 ? 33  ARG A NH1 1 
ATOM   214  N NH2 . ARG A 1 33  ? 7.219  30.634 30.407  1.00 42.69 ? 33  ARG A NH2 1 
ATOM   215  N N   . ILE A 1 34  ? 9.712  23.859 32.428  1.00 28.35 ? 34  ILE A N   1 
ATOM   216  C CA  . ILE A 1 34  ? 9.174  23.000 31.379  1.00 27.21 ? 34  ILE A CA  1 
ATOM   217  C C   . ILE A 1 34  ? 8.116  22.063 31.948  1.00 23.11 ? 34  ILE A C   1 
ATOM   218  O O   . ILE A 1 34  ? 7.072  21.833 31.327  1.00 27.17 ? 34  ILE A O   1 
ATOM   219  C CB  . ILE A 1 34  ? 10.319 22.228 30.699  1.00 26.75 ? 34  ILE A CB  1 
ATOM   220  C CG1 . ILE A 1 34  ? 11.176 23.183 29.864  1.00 26.29 ? 34  ILE A CG1 1 
ATOM   221  C CG2 . ILE A 1 34  ? 9.773  21.111 29.822  1.00 27.69 ? 34  ILE A CG2 1 
ATOM   222  C CD1 . ILE A 1 34  ? 12.518 22.610 29.480  1.00 28.30 ? 34  ILE A CD1 1 
ATOM   223  N N   . ALA A 1 35  ? 8.371  21.505 33.135  1.00 24.50 ? 35  ALA A N   1 
ATOM   224  C CA  . ALA A 1 35  ? 7.392  20.630 33.776  1.00 26.17 ? 35  ALA A CA  1 
ATOM   225  C C   . ALA A 1 35  ? 6.080  21.361 34.035  1.00 32.17 ? 35  ALA A C   1 
ATOM   226  O O   . ALA A 1 35  ? 4.996  20.822 33.778  1.00 29.17 ? 35  ALA A O   1 
ATOM   227  C CB  . ALA A 1 35  ? 7.963  20.071 35.079  1.00 28.92 ? 35  ALA A CB  1 
ATOM   228  N N   . THR A 1 36  ? 6.159  22.593 34.544  1.00 30.99 ? 36  THR A N   1 
ATOM   229  C CA  . THR A 1 36  ? 4.952  23.384 34.756  1.00 33.49 ? 36  THR A CA  1 
ATOM   230  C C   . THR A 1 36  ? 4.210  23.604 33.443  1.00 30.70 ? 36  THR A C   1 
ATOM   231  O O   . THR A 1 36  ? 2.996  23.397 33.362  1.00 33.25 ? 36  THR A O   1 
ATOM   232  C CB  . THR A 1 36  ? 5.312  24.721 35.407  1.00 35.03 ? 36  THR A CB  1 
ATOM   233  O OG1 . THR A 1 36  ? 5.935  24.481 36.677  1.00 35.57 ? 36  THR A OG1 1 
ATOM   234  C CG2 . THR A 1 36  ? 4.067  25.565 35.613  1.00 36.76 ? 36  THR A CG2 1 
ATOM   235  N N   . GLU A 1 37  ? 4.936  23.998 32.393  1.00 36.28 ? 37  GLU A N   1 
ATOM   236  C CA  . GLU A 1 37  ? 4.301  24.284 31.109  1.00 31.08 ? 37  GLU A CA  1 
ATOM   237  C C   . GLU A 1 37  ? 3.731  23.027 30.460  1.00 36.31 ? 37  GLU A C   1 
ATOM   238  O O   . GLU A 1 37  ? 2.687  23.093 29.803  1.00 32.70 ? 37  GLU A O   1 
ATOM   239  C CB  . GLU A 1 37  ? 5.306  24.952 30.174  1.00 35.00 ? 37  GLU A CB  1 
ATOM   240  C CG  . GLU A 1 37  ? 5.514  26.432 30.459  1.00 50.17 ? 37  GLU A CG  1 
ATOM   241  C CD  . GLU A 1 37  ? 4.299  27.265 30.111  1.00 55.93 ? 37  GLU A CD  1 
ATOM   242  O OE1 . GLU A 1 37  ? 3.915  27.285 28.922  1.00 68.26 ? 37  GLU A OE1 1 
ATOM   243  O OE2 . GLU A 1 37  ? 3.724  27.890 31.026  1.00 65.26 ? 37  GLU A OE2 1 
ATOM   244  N N   . ALA A 1 38  ? 4.398  21.882 30.620  1.00 30.27 ? 38  ALA A N   1 
ATOM   245  C CA  . ALA A 1 38  ? 3.888  20.624 30.090  1.00 30.75 ? 38  ALA A CA  1 
ATOM   246  C C   . ALA A 1 38  ? 2.831  19.989 30.981  1.00 33.52 ? 38  ALA A C   1 
ATOM   247  O O   . ALA A 1 38  ? 2.255  18.965 30.590  1.00 30.61 ? 38  ALA A O   1 
ATOM   248  C CB  . ALA A 1 38  ? 5.036  19.633 29.886  1.00 27.86 ? 38  ALA A CB  1 
ATOM   249  N N   . GLN A 1 39  ? 2.569  20.570 32.154  1.00 31.88 ? 39  GLN A N   1 
ATOM   250  C CA  . GLN A 1 39  ? 1.698  19.982 33.174  1.00 30.63 ? 39  GLN A CA  1 
ATOM   251  C C   . GLN A 1 39  ? 2.112  18.546 33.496  1.00 32.36 ? 39  GLN A C   1 
ATOM   252  O O   . GLN A 1 39  ? 1.308  17.610 33.465  1.00 31.13 ? 39  GLN A O   1 
ATOM   253  C CB  . GLN A 1 39  ? 0.229  20.050 32.759  1.00 32.86 ? 39  GLN A CB  1 
ATOM   254  C CG  . GLN A 1 39  ? -0.250 21.435 32.354  1.00 36.02 ? 39  GLN A CG  1 
ATOM   255  C CD  . GLN A 1 39  ? -1.673 21.411 31.823  1.00 51.20 ? 39  GLN A CD  1 
ATOM   256  O OE1 . GLN A 1 39  ? -2.626 21.241 32.584  1.00 54.17 ? 39  GLN A OE1 1 
ATOM   257  N NE2 . GLN A 1 39  ? -1.822 21.576 30.513  1.00 47.10 ? 39  GLN A NE2 1 
ATOM   258  N N   . THR A 1 40  ? 3.396  18.377 33.801  1.00 31.38 ? 40  THR A N   1 
ATOM   259  C CA  . THR A 1 40  ? 3.897  17.091 34.265  1.00 26.86 ? 40  THR A CA  1 
ATOM   260  C C   . THR A 1 40  ? 4.766  17.314 35.497  1.00 34.49 ? 40  THR A C   1 
ATOM   261  O O   . THR A 1 40  ? 4.808  18.426 36.034  1.00 28.82 ? 40  THR A O   1 
ATOM   262  C CB  . THR A 1 40  ? 4.668  16.373 33.149  1.00 28.85 ? 40  THR A CB  1 
ATOM   263  O OG1 . THR A 1 40  ? 4.927  15.014 33.529  1.00 28.64 ? 40  THR A OG1 1 
ATOM   264  C CG2 . THR A 1 40  ? 5.988  17.070 32.860  1.00 26.41 ? 40  THR A CG2 1 
ATOM   265  N N   . SER A 1 41  ? 5.443  16.270 35.961  1.00 27.19 ? 41  SER A N   1 
ATOM   266  C CA  . SER A 1 41  ? 6.346  16.366 37.098  1.00 27.56 ? 41  SER A CA  1 
ATOM   267  C C   . SER A 1 41  ? 7.775  16.554 36.612  1.00 25.71 ? 41  SER A C   1 
ATOM   268  O O   . SER A 1 41  ? 8.140  16.105 35.523  1.00 25.04 ? 41  SER A O   1 
ATOM   269  C CB  . SER A 1 41  ? 6.267  15.109 37.965  1.00 25.99 ? 41  SER A CB  1 
ATOM   270  O OG  . SER A 1 41  ? 6.733  13.985 37.235  1.00 24.26 ? 41  SER A OG  1 
ATOM   271  N N   . THR A 1 42  ? 8.592  17.224 37.431  1.00 25.12 ? 42  THR A N   1 
ATOM   272  C CA  . THR A 1 42  ? 10.016 17.277 37.119  1.00 23.45 ? 42  THR A CA  1 
ATOM   273  C C   . THR A 1 42  ? 10.608 15.877 37.078  1.00 26.07 ? 42  THR A C   1 
ATOM   274  O O   . THR A 1 42  ? 11.520 15.609 36.287  1.00 25.19 ? 42  THR A O   1 
ATOM   275  C CB  . THR A 1 42  ? 10.770 18.145 38.132  1.00 30.58 ? 42  THR A CB  1 
ATOM   276  O OG1 . THR A 1 42  ? 10.522 17.675 39.466  1.00 28.18 ? 42  THR A OG1 1 
ATOM   277  C CG2 . THR A 1 42  ? 10.325 19.595 38.018  1.00 28.93 ? 42  THR A CG2 1 
ATOM   278  N N   . GLY A 1 43  ? 10.082 14.965 37.899  1.00 27.18 ? 43  GLY A N   1 
ATOM   279  C CA  . GLY A 1 43  ? 10.547 13.590 37.850  1.00 28.13 ? 43  GLY A CA  1 
ATOM   280  C C   . GLY A 1 43  ? 10.383 12.971 36.475  1.00 24.55 ? 43  GLY A C   1 
ATOM   281  O O   . GLY A 1 43  ? 11.272 12.269 35.990  1.00 25.22 ? 43  GLY A O   1 
ATOM   282  N N   . GLN A 1 44  ? 9.251  13.233 35.820  1.00 22.77 ? 44  GLN A N   1 
ATOM   283  C CA  . GLN A 1 44  ? 9.074  12.653 34.496  1.00 25.71 ? 44  GLN A CA  1 
ATOM   284  C C   . GLN A 1 44  ? 9.908  13.369 33.442  1.00 23.51 ? 44  GLN A C   1 
ATOM   285  O O   . GLN A 1 44  ? 10.301 12.745 32.450  1.00 24.77 ? 44  GLN A O   1 
ATOM   286  C CB  . GLN A 1 44  ? 7.598  12.635 34.099  1.00 24.97 ? 44  GLN A CB  1 
ATOM   287  C CG  . GLN A 1 44  ? 6.818  11.543 34.826  1.00 27.35 ? 44  GLN A CG  1 
ATOM   288  C CD  . GLN A 1 44  ? 7.395  10.161 34.548  1.00 31.66 ? 44  GLN A CD  1 
ATOM   289  O OE1 . GLN A 1 44  ? 7.172  9.586  33.488  1.00 34.30 ? 44  GLN A OE1 1 
ATOM   290  N NE2 . GLN A 1 44  ? 8.129  9.617  35.517  1.00 35.83 ? 44  GLN A NE2 1 
ATOM   291  N N   . VAL A 1 45  ? 10.209 14.656 33.633  1.00 19.93 ? 45  VAL A N   1 
ATOM   292  C CA  . VAL A 1 45  ? 11.141 15.321 32.722  1.00 21.10 ? 45  VAL A CA  1 
ATOM   293  C C   . VAL A 1 45  ? 12.517 14.673 32.816  1.00 22.41 ? 45  VAL A C   1 
ATOM   294  O O   . VAL A 1 45  ? 13.143 14.353 31.799  1.00 22.41 ? 45  VAL A O   1 
ATOM   295  C CB  . VAL A 1 45  ? 11.213 16.831 33.013  1.00 24.55 ? 45  VAL A CB  1 
ATOM   296  C CG1 . VAL A 1 45  ? 12.207 17.486 32.067  1.00 25.69 ? 45  VAL A CG1 1 
ATOM   297  C CG2 . VAL A 1 45  ? 9.845  17.471 32.857  1.00 23.75 ? 45  VAL A CG2 1 
ATOM   298  N N   . HIS A 1 46  ? 12.996 14.444 34.044  1.00 24.47 ? 46  HIS A N   1 
ATOM   299  C CA  . HIS A 1 46  ? 14.299 13.810 34.223  1.00 27.25 ? 46  HIS A CA  1 
ATOM   300  C C   . HIS A 1 46  ? 14.295 12.366 33.743  1.00 28.65 ? 46  HIS A C   1 
ATOM   301  O O   . HIS A 1 46  ? 15.337 11.850 33.328  1.00 30.18 ? 46  HIS A O   1 
ATOM   302  C CB  . HIS A 1 46  ? 14.722 13.866 35.692  1.00 29.24 ? 46  HIS A CB  1 
ATOM   303  C CG  . HIS A 1 46  ? 15.082 15.240 36.168  1.00 29.26 ? 46  HIS A CG  1 
ATOM   304  N ND1 . HIS A 1 46  ? 16.036 16.017 35.545  1.00 28.57 ? 46  HIS A ND1 1 
ATOM   305  C CD2 . HIS A 1 46  ? 14.634 15.965 37.221  1.00 29.72 ? 46  HIS A CD2 1 
ATOM   306  C CE1 . HIS A 1 46  ? 16.148 17.168 36.186  1.00 29.30 ? 46  HIS A CE1 1 
ATOM   307  N NE2 . HIS A 1 46  ? 15.311 17.161 37.207  1.00 28.72 ? 46  HIS A NE2 1 
ATOM   308  N N   . HIS A 1 47  ? 13.143 11.696 33.801  1.00 28.93 ? 47  HIS A N   1 
ATOM   309  C CA  . HIS A 1 47  ? 13.067 10.319 33.325  1.00 27.96 ? 47  HIS A CA  1 
ATOM   310  C C   . HIS A 1 47  ? 13.252 10.248 31.815  1.00 32.93 ? 47  HIS A C   1 
ATOM   311  O O   . HIS A 1 47  ? 13.876 9.310  31.303  1.00 30.36 ? 47  HIS A O   1 
ATOM   312  C CB  . HIS A 1 47  ? 11.731 9.698  33.734  1.00 32.25 ? 47  HIS A CB  1 
ATOM   313  C CG  . HIS A 1 47  ? 11.422 8.411  33.034  1.00 35.71 ? 47  HIS A CG  1 
ATOM   314  N ND1 . HIS A 1 47  ? 11.995 7.212  33.398  1.00 38.00 ? 47  HIS A ND1 1 
ATOM   315  C CD2 . HIS A 1 47  ? 10.603 8.136  31.991  1.00 38.12 ? 47  HIS A CD2 1 
ATOM   316  C CE1 . HIS A 1 47  ? 11.540 6.252  32.612  1.00 44.55 ? 47  HIS A CE1 1 
ATOM   317  N NE2 . HIS A 1 47  ? 10.695 6.787  31.748  1.00 45.66 ? 47  HIS A NE2 1 
ATOM   318  N N   . HIS A 1 48  ? 12.728 11.234 31.086  1.00 25.05 ? 48  HIS A N   1 
ATOM   319  C CA  . HIS A 1 48  ? 12.735 11.200 29.629  1.00 29.34 ? 48  HIS A CA  1 
ATOM   320  C C   . HIS A 1 48  ? 13.971 11.828 29.003  1.00 26.86 ? 48  HIS A C   1 
ATOM   321  O O   . HIS A 1 48  ? 14.233 11.589 27.819  1.00 28.02 ? 48  HIS A O   1 
ATOM   322  C CB  . HIS A 1 48  ? 11.496 11.910 29.077  1.00 26.18 ? 48  HIS A CB  1 
ATOM   323  C CG  . HIS A 1 48  ? 10.235 11.125 29.234  1.00 32.10 ? 48  HIS A CG  1 
ATOM   324  N ND1 . HIS A 1 48  ? 10.041 9.903  28.626  1.00 38.18 ? 48  HIS A ND1 1 
ATOM   325  C CD2 . HIS A 1 48  ? 9.100  11.386 29.926  1.00 33.72 ? 48  HIS A CD2 1 
ATOM   326  C CE1 . HIS A 1 48  ? 8.842  9.444  28.938  1.00 36.24 ? 48  HIS A CE1 1 
ATOM   327  N NE2 . HIS A 1 48  ? 8.250  10.325 29.724  1.00 31.09 ? 48  HIS A NE2 1 
ATOM   328  N N   . PHE A 1 49  ? 14.728 12.627 29.748  1.00 24.52 ? 49  PHE A N   1 
ATOM   329  C CA  . PHE A 1 49  ? 15.850 13.368 29.188  1.00 28.28 ? 49  PHE A CA  1 
ATOM   330  C C   . PHE A 1 49  ? 17.057 13.243 30.104  1.00 28.43 ? 49  PHE A C   1 
ATOM   331  O O   . PHE A 1 49  ? 16.939 13.429 31.319  1.00 28.36 ? 49  PHE A O   1 
ATOM   332  C CB  . PHE A 1 49  ? 15.460 14.834 28.975  1.00 26.76 ? 49  PHE A CB  1 
ATOM   333  C CG  . PHE A 1 49  ? 14.325 15.014 28.007  1.00 25.59 ? 49  PHE A CG  1 
ATOM   334  C CD1 . PHE A 1 49  ? 14.568 15.112 26.646  1.00 26.50 ? 49  PHE A CD1 1 
ATOM   335  C CD2 . PHE A 1 49  ? 13.018 15.063 28.453  1.00 26.06 ? 49  PHE A CD2 1 
ATOM   336  C CE1 . PHE A 1 49  ? 13.527 15.271 25.750  1.00 27.32 ? 49  PHE A CE1 1 
ATOM   337  C CE2 . PHE A 1 49  ? 11.969 15.217 27.560  1.00 25.61 ? 49  PHE A CE2 1 
ATOM   338  C CZ  . PHE A 1 49  ? 12.226 15.321 26.207  1.00 25.96 ? 49  PHE A CZ  1 
ATOM   339  N N   . SER A 1 50  ? 18.219 12.937 29.516  1.00 29.39 ? 50  SER A N   1 
ATOM   340  C CA  . SER A 1 50  ? 19.405 12.622 30.312  1.00 34.08 ? 50  SER A CA  1 
ATOM   341  C C   . SER A 1 50  ? 19.887 13.812 31.132  1.00 33.38 ? 50  SER A C   1 
ATOM   342  O O   . SER A 1 50  ? 20.510 13.621 32.181  1.00 34.73 ? 50  SER A O   1 
ATOM   343  C CB  . SER A 1 50  ? 20.532 12.121 29.409  1.00 31.93 ? 50  SER A CB  1 
ATOM   344  O OG  . SER A 1 50  ? 20.034 11.204 28.452  1.00 42.85 ? 50  SER A OG  1 
ATOM   345  N N   . SER A 1 51  ? 19.620 15.034 30.678  1.00 26.59 ? 51  SER A N   1 
ATOM   346  C CA  . SER A 1 51  ? 20.029 16.224 31.411  1.00 26.84 ? 51  SER A CA  1 
ATOM   347  C C   . SER A 1 51  ? 19.245 17.410 30.873  1.00 26.75 ? 51  SER A C   1 
ATOM   348  O O   . SER A 1 51  ? 18.649 17.339 29.796  1.00 25.78 ? 51  SER A O   1 
ATOM   349  C CB  . SER A 1 51  ? 21.538 16.476 31.290  1.00 32.41 ? 51  SER A CB  1 
ATOM   350  O OG  . SER A 1 51  ? 21.873 17.016 30.019  1.00 30.34 ? 51  SER A OG  1 
ATOM   351  N N   . ALA A 1 52  ? 19.260 18.509 31.632  1.00 25.15 ? 52  ALA A N   1 
ATOM   352  C CA  . ALA A 1 52  ? 18.595 19.719 31.163  1.00 26.45 ? 52  ALA A CA  1 
ATOM   353  C C   . ALA A 1 52  ? 19.198 20.199 29.849  1.00 27.07 ? 52  ALA A C   1 
ATOM   354  O O   . ALA A 1 52  ? 18.476 20.675 28.966  1.00 24.04 ? 52  ALA A O   1 
ATOM   355  C CB  . ALA A 1 52  ? 18.678 20.816 32.222  1.00 24.92 ? 52  ALA A CB  1 
ATOM   356  N N   . SER A 1 53  ? 20.521 20.072 29.698  1.00 25.10 ? 53  SER A N   1 
ATOM   357  C CA  . SER A 1 53  ? 21.173 20.491 28.460  1.00 28.82 ? 53  SER A CA  1 
ATOM   358  C C   . SER A 1 53  ? 20.801 19.579 27.300  1.00 27.88 ? 53  SER A C   1 
ATOM   359  O O   . SER A 1 53  ? 20.684 20.038 26.157  1.00 22.68 ? 53  SER A O   1 
ATOM   360  C CB  . SER A 1 53  ? 22.691 20.523 28.647  1.00 30.91 ? 53  SER A CB  1 
ATOM   361  O OG  . SER A 1 53  ? 23.099 21.756 29.211  1.00 37.15 ? 53  SER A OG  1 
ATOM   362  N N   . HIS A 1 54  ? 20.627 18.281 27.571  1.00 21.20 ? 54  HIS A N   1 
ATOM   363  C CA  . HIS A 1 54  ? 20.126 17.374 26.544  1.00 22.91 ? 54  HIS A CA  1 
ATOM   364  C C   . HIS A 1 54  ? 18.760 17.828 26.044  1.00 25.61 ? 54  HIS A C   1 
ATOM   365  O O   . HIS A 1 54  ? 18.497 17.826 24.836  1.00 27.10 ? 54  HIS A O   1 
ATOM   366  C CB  . HIS A 1 54  ? 20.032 15.948 27.092  1.00 25.43 ? 54  HIS A CB  1 
ATOM   367  C CG  . HIS A 1 54  ? 21.329 15.200 27.095  1.00 28.51 ? 54  HIS A CG  1 
ATOM   368  N ND1 . HIS A 1 54  ? 22.302 15.400 28.052  1.00 32.02 ? 54  HIS A ND1 1 
ATOM   369  C CD2 . HIS A 1 54  ? 21.806 14.239 26.269  1.00 28.49 ? 54  HIS A CD2 1 
ATOM   370  C CE1 . HIS A 1 54  ? 23.323 14.596 27.813  1.00 29.58 ? 54  HIS A CE1 1 
ATOM   371  N NE2 . HIS A 1 54  ? 23.049 13.883 26.735  1.00 34.91 ? 54  HIS A NE2 1 
ATOM   372  N N   . LEU A 1 55  ? 17.880 18.221 26.968  1.00 21.86 ? 55  LEU A N   1 
ATOM   373  C CA  . LEU A 1 55  ? 16.550 18.701 26.605  1.00 22.27 ? 55  LEU A CA  1 
ATOM   374  C C   . LEU A 1 55  ? 16.637 19.977 25.777  1.00 24.14 ? 55  LEU A C   1 
ATOM   375  O O   . LEU A 1 55  ? 15.918 20.139 24.783  1.00 22.58 ? 55  LEU A O   1 
ATOM   376  C CB  . LEU A 1 55  ? 15.736 18.951 27.875  1.00 21.71 ? 55  LEU A CB  1 
ATOM   377  C CG  . LEU A 1 55  ? 14.271 19.386 27.797  1.00 26.18 ? 55  LEU A CG  1 
ATOM   378  C CD1 . LEU A 1 55  ? 13.554 18.816 26.578  1.00 28.00 ? 55  LEU A CD1 1 
ATOM   379  C CD2 . LEU A 1 55  ? 13.544 19.041 29.090  1.00 25.21 ? 55  LEU A CD2 1 
ATOM   380  N N   . LYS A 1 56  ? 17.497 20.908 26.191  1.00 23.75 ? 56  LYS A N   1 
ATOM   381  C CA  . LYS A 1 56  ? 17.658 22.152 25.444  1.00 21.72 ? 56  LYS A CA  1 
ATOM   382  C C   . LYS A 1 56  ? 18.145 21.879 24.027  1.00 21.39 ? 56  LYS A C   1 
ATOM   383  O O   . LYS A 1 56  ? 17.633 22.461 23.062  1.00 21.17 ? 56  LYS A O   1 
ATOM   384  C CB  . LYS A 1 56  ? 18.634 23.074 26.176  1.00 24.98 ? 56  LYS A CB  1 
ATOM   385  C CG  . LYS A 1 56  ? 18.038 23.786 27.385  1.00 27.22 ? 56  LYS A CG  1 
ATOM   386  C CD  . LYS A 1 56  ? 19.127 24.502 28.181  1.00 30.04 ? 56  LYS A CD  1 
ATOM   387  C CE  . LYS A 1 56  ? 18.598 25.016 29.510  1.00 31.71 ? 56  LYS A CE  1 
ATOM   388  N NZ  . LYS A 1 56  ? 19.640 25.747 30.290  1.00 33.31 ? 56  LYS A NZ  1 
ATOM   389  N N   . ALA A 1 57  ? 19.129 20.985 23.883  1.00 21.05 ? 57  ALA A N   1 
ATOM   390  C CA  . ALA A 1 57  ? 19.670 20.665 22.565  1.00 22.73 ? 57  ALA A CA  1 
ATOM   391  C C   . ALA A 1 57  ? 18.645 19.944 21.702  1.00 23.17 ? 57  ALA A C   1 
ATOM   392  O O   . ALA A 1 57  ? 18.535 20.215 20.500  1.00 23.32 ? 57  ALA A O   1 
ATOM   393  C CB  . ALA A 1 57  ? 20.932 19.811 22.708  1.00 21.04 ? 57  ALA A CB  1 
ATOM   394  N N   . GLU A 1 58  ? 17.901 19.006 22.291  1.00 22.68 ? 58  GLU A N   1 
ATOM   395  C CA  . GLU A 1 58  ? 16.865 18.302 21.542  1.00 25.47 ? 58  GLU A CA  1 
ATOM   396  C C   . GLU A 1 58  ? 15.785 19.260 21.049  1.00 25.39 ? 58  GLU A C   1 
ATOM   397  O O   . GLU A 1 58  ? 15.346 19.171 19.897  1.00 24.49 ? 58  GLU A O   1 
ATOM   398  C CB  . GLU A 1 58  ? 16.252 17.206 22.413  1.00 28.69 ? 58  GLU A CB  1 
ATOM   399  C CG  . GLU A 1 58  ? 15.393 16.219 21.660  1.00 43.30 ? 58  GLU A CG  1 
ATOM   400  C CD  . GLU A 1 58  ? 15.354 14.841 22.303  1.00 37.37 ? 58  GLU A CD  1 
ATOM   401  O OE1 . GLU A 1 58  ? 16.066 14.614 23.304  1.00 40.19 ? 58  GLU A OE1 1 
ATOM   402  O OE2 . GLU A 1 58  ? 14.587 13.989 21.811  1.00 43.81 ? 58  GLU A OE2 1 
ATOM   403  N N   . ALA A 1 59  ? 15.337 20.174 21.914  1.00 24.37 ? 59  ALA A N   1 
ATOM   404  C CA  . ALA A 1 59  ? 14.335 21.157 21.514  1.00 23.38 ? 59  ALA A CA  1 
ATOM   405  C C   . ALA A 1 59  ? 14.871 22.083 20.429  1.00 25.43 ? 59  ALA A C   1 
ATOM   406  O O   . ALA A 1 59  ? 14.155 22.426 19.479  1.00 24.34 ? 59  ALA A O   1 
ATOM   407  C CB  . ALA A 1 59  ? 13.887 21.963 22.734  1.00 22.40 ? 59  ALA A CB  1 
ATOM   408  N N   . PHE A 1 60  ? 16.130 22.502 20.558  1.00 22.44 ? 60  PHE A N   1 
ATOM   409  C CA  . PHE A 1 60  ? 16.741 23.354 19.546  1.00 23.43 ? 60  PHE A CA  1 
ATOM   410  C C   . PHE A 1 60  ? 16.753 22.665 18.188  1.00 23.20 ? 60  PHE A C   1 
ATOM   411  O O   . PHE A 1 60  ? 16.363 23.258 17.176  1.00 26.70 ? 60  PHE A O   1 
ATOM   412  C CB  . PHE A 1 60  ? 18.159 23.736 19.971  1.00 19.47 ? 60  PHE A CB  1 
ATOM   413  C CG  . PHE A 1 60  ? 18.960 24.395 18.879  1.00 27.14 ? 60  PHE A CG  1 
ATOM   414  C CD1 . PHE A 1 60  ? 18.653 25.677 18.453  1.00 26.42 ? 60  PHE A CD1 1 
ATOM   415  C CD2 . PHE A 1 60  ? 20.010 23.722 18.271  1.00 28.38 ? 60  PHE A CD2 1 
ATOM   416  C CE1 . PHE A 1 60  ? 19.391 26.285 17.448  1.00 30.29 ? 60  PHE A CE1 1 
ATOM   417  C CE2 . PHE A 1 60  ? 20.751 24.321 17.265  1.00 23.94 ? 60  PHE A CE2 1 
ATOM   418  C CZ  . PHE A 1 60  ? 20.438 25.604 16.854  1.00 25.10 ? 60  PHE A CZ  1 
ATOM   419  N N   . LEU A 1 61  ? 17.184 21.401 18.146  1.00 23.81 ? 61  LEU A N   1 
ATOM   420  C CA  . LEU A 1 61  ? 17.208 20.686 16.873  1.00 26.79 ? 61  LEU A CA  1 
ATOM   421  C C   . LEU A 1 61  ? 15.806 20.540 16.297  1.00 30.11 ? 61  LEU A C   1 
ATOM   422  O O   . LEU A 1 61  ? 15.603 20.727 15.093  1.00 28.79 ? 61  LEU A O   1 
ATOM   423  C CB  . LEU A 1 61  ? 17.873 19.320 17.043  1.00 27.65 ? 61  LEU A CB  1 
ATOM   424  C CG  . LEU A 1 61  ? 19.391 19.382 17.216  1.00 31.59 ? 61  LEU A CG  1 
ATOM   425  C CD1 . LEU A 1 61  ? 19.961 18.014 17.554  1.00 33.23 ? 61  LEU A CD1 1 
ATOM   426  C CD2 . LEU A 1 61  ? 20.045 19.954 15.968  1.00 30.17 ? 61  LEU A CD2 1 
ATOM   427  N N   . LYS A 1 62  ? 14.820 20.233 17.146  1.00 29.71 ? 62  LYS A N   1 
ATOM   428  C CA  . LYS A 1 62  ? 13.439 20.141 16.681  1.00 27.74 ? 62  LYS A CA  1 
ATOM   429  C C   . LYS A 1 62  ? 12.969 21.458 16.079  1.00 29.85 ? 62  LYS A C   1 
ATOM   430  O O   . LYS A 1 62  ? 12.300 21.472 15.039  1.00 27.94 ? 62  LYS A O   1 
ATOM   431  C CB  . LYS A 1 62  ? 12.524 19.733 17.837  1.00 28.70 ? 62  LYS A CB  1 
ATOM   432  C CG  . LYS A 1 62  ? 12.331 18.241 17.979  1.00 40.36 ? 62  LYS A CG  1 
ATOM   433  C CD  . LYS A 1 62  ? 11.388 17.707 16.919  1.00 46.01 ? 62  LYS A CD  1 
ATOM   434  C CE  . LYS A 1 62  ? 10.040 17.354 17.522  1.00 54.22 ? 62  LYS A CE  1 
ATOM   435  N NZ  . LYS A 1 62  ? 8.993  17.228 16.471  1.00 60.15 ? 62  LYS A NZ  1 
ATOM   436  N N   . LEU A 1 63  ? 13.312 22.581 16.715  1.00 25.62 ? 63  LEU A N   1 
ATOM   437  C CA  . LEU A 1 63  ? 12.887 23.874 16.191  1.00 28.14 ? 63  LEU A CA  1 
ATOM   438  C C   . LEU A 1 63  ? 13.571 24.204 14.871  1.00 32.41 ? 63  LEU A C   1 
ATOM   439  O O   . LEU A 1 63  ? 12.989 24.903 14.032  1.00 29.72 ? 63  LEU A O   1 
ATOM   440  C CB  . LEU A 1 63  ? 13.145 24.968 17.226  1.00 26.41 ? 63  LEU A CB  1 
ATOM   441  C CG  . LEU A 1 63  ? 12.142 24.978 18.387  1.00 27.62 ? 63  LEU A CG  1 
ATOM   442  C CD1 . LEU A 1 63  ? 12.632 25.850 19.522  1.00 27.94 ? 63  LEU A CD1 1 
ATOM   443  C CD2 . LEU A 1 63  ? 10.783 25.459 17.897  1.00 28.16 ? 63  LEU A CD2 1 
ATOM   444  N N   . MET A 1 64  ? 14.793 23.708 14.663  1.00 30.18 ? 64  MET A N   1 
ATOM   445  C CA  . MET A 1 64  ? 15.492 23.985 13.414  1.00 34.78 ? 64  MET A CA  1 
ATOM   446  C C   . MET A 1 64  ? 14.899 23.175 12.264  1.00 39.90 ? 64  MET A C   1 
ATOM   447  O O   . MET A 1 64  ? 14.781 23.679 11.140  1.00 35.54 ? 64  MET A O   1 
ATOM   448  C CB  . MET A 1 64  ? 16.988 23.704 13.580  1.00 36.59 ? 64  MET A CB  1 
ATOM   449  C CG  . MET A 1 64  ? 17.719 24.742 14.442  1.00 26.11 ? 64  MET A CG  1 
ATOM   450  S SD  . MET A 1 64  ? 17.379 26.476 14.033  1.00 34.24 ? 64  MET A SD  1 
ATOM   451  C CE  . MET A 1 64  ? 16.219 26.960 15.309  1.00 33.34 ? 64  MET A CE  1 
ATOM   452  N N   . GLU A 1 65  ? 14.512 21.921 12.525  1.00 35.25 ? 65  GLU A N   1 
ATOM   453  C CA  . GLU A 1 65  ? 13.769 21.159 11.523  1.00 41.28 ? 65  GLU A CA  1 
ATOM   454  C C   . GLU A 1 65  ? 12.430 21.819 11.228  1.00 38.89 ? 65  GLU A C   1 
ATOM   455  O O   . GLU A 1 65  ? 11.969 21.826 10.081  1.00 42.95 ? 65  GLU A O   1 
ATOM   456  C CB  . GLU A 1 65  ? 13.561 19.716 11.990  1.00 38.69 ? 65  GLU A CB  1 
ATOM   457  C CG  . GLU A 1 65  ? 14.741 19.134 12.732  1.00 43.26 ? 65  GLU A CG  1 
ATOM   458  C CD  . GLU A 1 65  ? 14.941 17.656 12.480  1.00 67.72 ? 65  GLU A CD  1 
ATOM   459  O OE1 . GLU A 1 65  ? 13.965 16.984 12.088  1.00 80.59 ? 65  GLU A OE1 1 
ATOM   460  O OE2 . GLU A 1 65  ? 16.074 17.168 12.688  1.00 63.18 ? 65  GLU A OE2 1 
ATOM   461  N N   . GLN A 1 66  ? 11.794 22.384 12.255  1.00 37.50 ? 66  GLN A N   1 
ATOM   462  C CA  . GLN A 1 66  ? 10.567 23.142 12.048  1.00 40.18 ? 66  GLN A CA  1 
ATOM   463  C C   . GLN A 1 66  ? 10.814 24.354 11.159  1.00 42.35 ? 66  GLN A C   1 
ATOM   464  O O   . GLN A 1 66  ? 9.986  24.682 10.300  1.00 40.79 ? 66  GLN A O   1 
ATOM   465  C CB  . GLN A 1 66  ? 9.992  23.564 13.397  1.00 37.97 ? 66  GLN A CB  1 
ATOM   466  C CG  . GLN A 1 66  ? 8.606  24.150 13.335  1.00 42.86 ? 66  GLN A CG  1 
ATOM   467  C CD  . GLN A 1 66  ? 7.989  24.265 14.709  1.00 38.24 ? 66  GLN A CD  1 
ATOM   468  O OE1 . GLN A 1 66  ? 8.073  25.309 15.353  1.00 39.65 ? 66  GLN A OE1 1 
ATOM   469  N NE2 . GLN A 1 66  ? 7.369  23.187 15.169  1.00 40.77 ? 66  GLN A NE2 1 
ATOM   470  N N   . LEU A 1 67  ? 11.950 25.031 11.346  1.00 37.94 ? 67  LEU A N   1 
ATOM   471  C CA  . LEU A 1 67  ? 12.292 26.151 10.474  1.00 39.16 ? 67  LEU A CA  1 
ATOM   472  C C   . LEU A 1 67  ? 12.500 25.674 9.041   1.00 39.70 ? 67  LEU A C   1 
ATOM   473  O O   . LEU A 1 67  ? 12.058 26.329 8.090   1.00 43.58 ? 67  LEU A O   1 
ATOM   474  C CB  . LEU A 1 67  ? 13.542 26.865 10.999  1.00 39.37 ? 67  LEU A CB  1 
ATOM   475  C CG  . LEU A 1 67  ? 14.403 27.687 10.029  1.00 42.56 ? 67  LEU A CG  1 
ATOM   476  C CD1 . LEU A 1 67  ? 13.596 28.792 9.362   1.00 46.26 ? 67  LEU A CD1 1 
ATOM   477  C CD2 . LEU A 1 67  ? 15.634 28.261 10.721  1.00 43.86 ? 67  LEU A CD2 1 
ATOM   478  N N   . ASP A 1 68  ? 13.165 24.527 8.871   1.00 40.85 ? 68  ASP A N   1 
ATOM   479  C CA  . ASP A 1 68  ? 13.301 23.919 7.549   1.00 40.25 ? 68  ASP A CA  1 
ATOM   480  C C   . ASP A 1 68  ? 11.937 23.691 6.908   1.00 49.71 ? 68  ASP A C   1 
ATOM   481  O O   . ASP A 1 68  ? 11.707 24.064 5.752   1.00 43.73 ? 68  ASP A O   1 
ATOM   482  C CB  . ASP A 1 68  ? 14.065 22.597 7.662   1.00 41.38 ? 68  ASP A CB  1 
ATOM   483  C CG  . ASP A 1 68  ? 15.548 22.797 7.904   1.00 58.21 ? 68  ASP A CG  1 
ATOM   484  O OD1 . ASP A 1 68  ? 15.971 23.962 8.066   1.00 60.56 ? 68  ASP A OD1 1 
ATOM   485  O OD2 . ASP A 1 68  ? 16.291 21.791 7.923   1.00 65.89 ? 68  ASP A OD2 1 
ATOM   486  N N   . GLU A 1 69  ? 11.017 23.077 7.656   1.00 41.25 ? 69  GLU A N   1 
ATOM   487  C CA  . GLU A 1 69  ? 9.678  22.818 7.137   1.00 44.97 ? 69  GLU A CA  1 
ATOM   488  C C   . GLU A 1 69  ? 8.997  24.110 6.713   1.00 43.55 ? 69  GLU A C   1 
ATOM   489  O O   . GLU A 1 69  ? 8.455  24.205 5.606   1.00 51.09 ? 69  GLU A O   1 
ATOM   490  C CB  . GLU A 1 69  ? 8.844  22.100 8.196   1.00 45.31 ? 69  GLU A CB  1 
ATOM   491  C CG  . GLU A 1 69  ? 9.053  20.601 8.240   1.00 58.75 ? 69  GLU A CG  1 
ATOM   492  C CD  . GLU A 1 69  ? 8.560  19.994 9.538   1.00 68.13 ? 69  GLU A CD  1 
ATOM   493  O OE1 . GLU A 1 69  ? 9.037  18.897 9.899   1.00 69.33 ? 69  GLU A OE1 1 
ATOM   494  O OE2 . GLU A 1 69  ? 7.696  20.617 10.194  1.00 60.35 ? 69  GLU A OE2 1 
ATOM   495  N N   . ILE A 1 70  ? 9.024  25.122 7.585   1.00 40.51 ? 70  ILE A N   1 
ATOM   496  C CA  . ILE A 1 70  ? 8.385  26.399 7.278   1.00 42.46 ? 70  ILE A CA  1 
ATOM   497  C C   . ILE A 1 70  ? 8.965  26.985 5.999   1.00 56.18 ? 70  ILE A C   1 
ATOM   498  O O   . ILE A 1 70  ? 8.232  27.446 5.115   1.00 47.55 ? 70  ILE A O   1 
ATOM   499  C CB  . ILE A 1 70  ? 8.540  27.374 8.458   1.00 47.85 ? 70  ILE A CB  1 
ATOM   500  C CG1 . ILE A 1 70  ? 7.660  26.947 9.632   1.00 42.76 ? 70  ILE A CG1 1 
ATOM   501  C CG2 . ILE A 1 70  ? 8.169  28.781 8.029   1.00 49.76 ? 70  ILE A CG2 1 
ATOM   502  C CD1 . ILE A 1 70  ? 7.733  27.895 10.808  1.00 42.60 ? 70  ILE A CD1 1 
ATOM   503  N N   . GLU A 1 71  ? 10.296 26.969 5.881   1.00 46.22 ? 71  GLU A N   1 
ATOM   504  C CA  . GLU A 1 71  ? 10.943 27.526 4.700   1.00 48.91 ? 71  GLU A CA  1 
ATOM   505  C C   . GLU A 1 71  ? 10.503 26.804 3.433   1.00 47.99 ? 71  GLU A C   1 
ATOM   506  O O   . GLU A 1 71  ? 10.435 27.416 2.360   1.00 48.95 ? 71  GLU A O   1 
ATOM   507  C CB  . GLU A 1 71  ? 12.462 27.452 4.845   1.00 39.01 ? 71  GLU A CB  1 
ATOM   508  C CG  . GLU A 1 71  ? 13.066 28.571 5.677   1.00 38.41 ? 71  GLU A CG  1 
ATOM   509  C CD  . GLU A 1 71  ? 14.571 28.432 5.814   1.00 53.45 ? 71  GLU A CD  1 
ATOM   510  O OE1 . GLU A 1 71  ? 15.235 29.432 6.166   1.00 47.46 ? 71  GLU A OE1 1 
ATOM   511  O OE2 . GLU A 1 71  ? 15.093 27.329 5.542   1.00 45.58 ? 71  GLU A OE2 1 
ATOM   512  N N   . GLN A 1 72  ? 10.196 25.511 3.537   1.00 52.04 ? 72  GLN A N   1 
ATOM   513  C CA  . GLN A 1 72  ? 9.811  24.725 2.375   1.00 58.97 ? 72  GLN A CA  1 
ATOM   514  C C   . GLN A 1 72  ? 8.377  24.981 1.934   1.00 57.98 ? 72  GLN A C   1 
ATOM   515  O O   . GLN A 1 72  ? 7.995  24.534 0.848   1.00 53.96 ? 72  GLN A O   1 
ATOM   516  C CB  . GLN A 1 72  ? 10.006 23.234 2.663   1.00 56.02 ? 72  GLN A CB  1 
ATOM   517  C CG  . GLN A 1 72  ? 11.459 22.791 2.572   1.00 64.04 ? 72  GLN A CG  1 
ATOM   518  C CD  . GLN A 1 72  ? 11.917 22.542 1.146   1.00 74.71 ? 72  GLN A CD  1 
ATOM   519  O OE1 . GLN A 1 72  ? 11.257 22.945 0.186   1.00 79.53 ? 72  GLN A OE1 1 
ATOM   520  N NE2 . GLN A 1 72  ? 13.065 21.889 1.001   1.00 70.04 ? 72  GLN A NE2 1 
ATOM   521  N N   . THR A 1 73  ? 7.581  25.691 2.737   1.00 58.14 ? 73  THR A N   1 
ATOM   522  C CA  . THR A 1 73  ? 6.229  26.042 2.323   1.00 62.05 ? 73  THR A CA  1 
ATOM   523  C C   . THR A 1 73  ? 6.173  27.325 1.504   1.00 59.92 ? 73  THR A C   1 
ATOM   524  O O   . THR A 1 73  ? 5.198  27.526 0.772   1.00 63.62 ? 73  THR A O   1 
ATOM   525  C CB  . THR A 1 73  ? 5.300  26.168 3.536   1.00 55.89 ? 73  THR A CB  1 
ATOM   526  O OG1 . THR A 1 73  ? 5.354  27.504 4.052   1.00 59.46 ? 73  THR A OG1 1 
ATOM   527  C CG2 . THR A 1 73  ? 5.676  25.179 4.618   1.00 50.02 ? 73  THR A CG2 1 
ATOM   528  N N   . LEU A 1 74  ? 7.172  28.202 1.606   1.00 55.56 ? 74  LEU A N   1 
ATOM   529  C CA  . LEU A 1 74  ? 7.216  29.338 0.692   1.00 57.37 ? 74  LEU A CA  1 
ATOM   530  C C   . LEU A 1 74  ? 7.430  28.851 -0.737  1.00 63.18 ? 74  LEU A C   1 
ATOM   531  O O   . LEU A 1 74  ? 8.306  28.025 -1.010  1.00 62.59 ? 74  LEU A O   1 
ATOM   532  C CB  . LEU A 1 74  ? 8.299  30.347 1.083   1.00 55.75 ? 74  LEU A CB  1 
ATOM   533  C CG  . LEU A 1 74  ? 8.302  30.976 2.481   1.00 62.02 ? 74  LEU A CG  1 
ATOM   534  C CD1 . LEU A 1 74  ? 6.878  31.302 2.944   1.00 69.57 ? 74  LEU A CD1 1 
ATOM   535  C CD2 . LEU A 1 74  ? 9.040  30.147 3.504   1.00 53.36 ? 74  LEU A CD2 1 
ATOM   536  N N   . GLN A 1 75  ? 6.609  29.370 -1.644  1.00 57.97 ? 75  GLN A N   1 
ATOM   537  C CA  . GLN A 1 75  ? 6.606  28.924 -3.027  1.00 56.63 ? 75  GLN A CA  1 
ATOM   538  C C   . GLN A 1 75  ? 7.800  29.500 -3.773  1.00 46.58 ? 75  GLN A C   1 
ATOM   539  O O   . GLN A 1 75  ? 8.131  30.679 -3.627  1.00 57.77 ? 75  GLN A O   1 
ATOM   540  C CB  . GLN A 1 75  ? 5.305  29.354 -3.703  1.00 56.26 ? 75  GLN A CB  1 
ATOM   541  C CG  . GLN A 1 75  ? 4.111  29.328 -2.760  1.00 65.52 ? 75  GLN A CG  1 
ATOM   542  C CD  . GLN A 1 75  ? 2.804  29.644 -3.454  1.00 80.20 ? 75  GLN A CD  1 
ATOM   543  O OE1 . GLN A 1 75  ? 2.102  30.585 -3.081  1.00 81.19 ? 75  GLN A OE1 1 
ATOM   544  N NE2 . GLN A 1 75  ? 2.466  28.857 -4.468  1.00 74.04 ? 75  GLN A NE2 1 
ATOM   545  N N   . THR A 1 76  ? 8.451  28.657 -4.570  1.00 57.01 ? 76  THR A N   1 
ATOM   546  C CA  . THR A 1 76  ? 9.545  29.092 -5.424  1.00 51.93 ? 76  THR A CA  1 
ATOM   547  C C   . THR A 1 76  ? 9.383  28.458 -6.796  1.00 50.01 ? 76  THR A C   1 
ATOM   548  O O   . THR A 1 76  ? 8.816  27.371 -6.933  1.00 58.36 ? 76  THR A O   1 
ATOM   549  C CB  . THR A 1 76  ? 10.923 28.715 -4.855  1.00 46.97 ? 76  THR A CB  1 
ATOM   550  O OG1 . THR A 1 76  ? 10.963 27.309 -4.577  1.00 53.77 ? 76  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 76  ? 11.209 29.492 -3.579  1.00 45.82 ? 76  THR A CG2 1 
ATOM   552  N N   . THR A 1 77  ? 9.888  29.153 -7.809  1.00 47.18 ? 77  THR A N   1 
ATOM   553  C CA  . THR A 1 77  ? 9.968  28.621 -9.160  1.00 52.72 ? 77  THR A CA  1 
ATOM   554  C C   . THR A 1 77  ? 11.404 28.445 -9.621  1.00 53.96 ? 77  THR A C   1 
ATOM   555  O O   . THR A 1 77  ? 11.633 28.013 -10.756 1.00 52.45 ? 77  THR A O   1 
ATOM   556  C CB  . THR A 1 77  ? 9.224  29.535 -10.138 1.00 48.68 ? 77  THR A CB  1 
ATOM   557  O OG1 . THR A 1 77  ? 9.810  30.843 -10.098 1.00 48.07 ? 77  THR A OG1 1 
ATOM   558  C CG2 . THR A 1 77  ? 7.748  29.620 -9.763  1.00 46.98 ? 77  THR A CG2 1 
ATOM   559  N N   . SER A 1 78  ? 12.375 28.771 -8.772  1.00 40.36 ? 78  SER A N   1 
ATOM   560  C CA  . SER A 1 78  ? 13.775 28.657 -9.135  1.00 41.52 ? 78  SER A CA  1 
ATOM   561  C C   . SER A 1 78  ? 14.571 28.311 -7.889  1.00 35.28 ? 78  SER A C   1 
ATOM   562  O O   . SER A 1 78  ? 14.167 28.627 -6.766  1.00 34.53 ? 78  SER A O   1 
ATOM   563  C CB  . SER A 1 78  ? 14.307 29.954 -9.755  1.00 45.14 ? 78  SER A CB  1 
ATOM   564  O OG  . SER A 1 78  ? 14.173 31.040 -8.854  1.00 39.29 ? 78  SER A OG  1 
ATOM   565  N N   . GLN A 1 79  ? 15.706 27.648 -8.100  1.00 31.82 ? 79  GLN A N   1 
ATOM   566  C CA  . GLN A 1 79  ? 16.617 27.416 -6.990  1.00 29.71 ? 79  GLN A CA  1 
ATOM   567  C C   . GLN A 1 79  ? 17.311 28.705 -6.576  1.00 30.69 ? 79  GLN A C   1 
ATOM   568  O O   . GLN A 1 79  ? 17.746 28.830 -5.427  1.00 33.34 ? 79  GLN A O   1 
ATOM   569  C CB  . GLN A 1 79  ? 17.640 26.344 -7.359  1.00 31.32 ? 79  GLN A CB  1 
ATOM   570  C CG  . GLN A 1 79  ? 17.046 24.956 -7.426  1.00 34.45 ? 79  GLN A CG  1 
ATOM   571  C CD  . GLN A 1 79  ? 16.172 24.655 -6.232  1.00 31.95 ? 79  GLN A CD  1 
ATOM   572  O OE1 . GLN A 1 79  ? 16.665 24.459 -5.125  1.00 32.04 ? 79  GLN A OE1 1 
ATOM   573  N NE2 . GLN A 1 79  ? 14.863 24.613 -6.452  1.00 38.43 ? 79  GLN A NE2 1 
ATOM   574  N N   . PHE A 1 80  ? 17.427 29.664 -7.498  1.00 30.46 ? 80  PHE A N   1 
ATOM   575  C CA  . PHE A 1 80  ? 17.935 30.985 -7.147  1.00 28.39 ? 80  PHE A CA  1 
ATOM   576  C C   . PHE A 1 80  ? 17.119 31.582 -6.008  1.00 31.66 ? 80  PHE A C   1 
ATOM   577  O O   . PHE A 1 80  ? 17.674 32.044 -5.004  1.00 30.28 ? 80  PHE A O   1 
ATOM   578  C CB  . PHE A 1 80  ? 17.907 31.876 -8.392  1.00 36.04 ? 80  PHE A CB  1 
ATOM   579  C CG  . PHE A 1 80  ? 18.589 33.205 -8.227  1.00 44.26 ? 80  PHE A CG  1 
ATOM   580  C CD1 . PHE A 1 80  ? 19.969 33.284 -8.141  1.00 41.72 ? 80  PHE A CD1 1 
ATOM   581  C CD2 . PHE A 1 80  ? 17.855 34.382 -8.243  1.00 46.92 ? 80  PHE A CD2 1 
ATOM   582  C CE1 . PHE A 1 80  ? 20.604 34.509 -8.015  1.00 46.65 ? 80  PHE A CE1 1 
ATOM   583  C CE2 . PHE A 1 80  ? 18.481 35.610 -8.126  1.00 50.76 ? 80  PHE A CE2 1 
ATOM   584  C CZ  . PHE A 1 80  ? 19.860 35.673 -8.011  1.00 54.53 ? 80  PHE A CZ  1 
ATOM   585  N N   . GLN A 1 81  ? 15.792 31.536 -6.128  1.00 31.20 ? 81  GLN A N   1 
ATOM   586  C CA  . GLN A 1 81  ? 14.921 31.992 -5.049  1.00 33.35 ? 81  GLN A CA  1 
ATOM   587  C C   . GLN A 1 81  ? 15.089 31.131 -3.805  1.00 32.66 ? 81  GLN A C   1 
ATOM   588  O O   . GLN A 1 81  ? 15.154 31.648 -2.682  1.00 30.98 ? 81  GLN A O   1 
ATOM   589  C CB  . GLN A 1 81  ? 13.465 31.952 -5.514  1.00 31.20 ? 81  GLN A CB  1 
ATOM   590  C CG  . GLN A 1 81  ? 13.003 33.168 -6.292  1.00 38.69 ? 81  GLN A CG  1 
ATOM   591  C CD  . GLN A 1 81  ? 11.788 32.861 -7.157  1.00 56.14 ? 81  GLN A CD  1 
ATOM   592  O OE1 . GLN A 1 81  ? 11.359 31.710 -7.259  1.00 54.17 ? 81  GLN A OE1 1 
ATOM   593  N NE2 . GLN A 1 81  ? 11.238 33.887 -7.795  1.00 58.24 ? 81  GLN A NE2 1 
ATOM   594  N N   . ARG A 1 82  ? 15.123 29.808 -3.986  1.00 31.30 ? 82  ARG A N   1 
ATOM   595  C CA  . ARG A 1 82  ? 15.317 28.897 -2.863  1.00 30.21 ? 82  ARG A CA  1 
ATOM   596  C C   . ARG A 1 82  ? 16.578 29.242 -2.080  1.00 27.58 ? 82  ARG A C   1 
ATOM   597  O O   . ARG A 1 82  ? 16.567 29.233 -0.845  1.00 29.17 ? 82  ARG A O   1 
ATOM   598  C CB  . ARG A 1 82  ? 15.381 27.455 -3.370  1.00 38.64 ? 82  ARG A CB  1 
ATOM   599  C CG  . ARG A 1 82  ? 15.486 26.383 -2.289  1.00 44.90 ? 82  ARG A CG  1 
ATOM   600  C CD  . ARG A 1 82  ? 14.376 26.465 -1.250  1.00 44.74 ? 82  ARG A CD  1 
ATOM   601  N NE  . ARG A 1 82  ? 13.052 26.356 -1.849  1.00 49.82 ? 82  ARG A NE  1 
ATOM   602  C CZ  . ARG A 1 82  ? 11.925 26.720 -1.250  1.00 64.56 ? 82  ARG A CZ  1 
ATOM   603  N NH1 . ARG A 1 82  ? 11.924 27.219 -0.023  1.00 58.14 ? 82  ARG A NH1 1 
ATOM   604  N NH2 . ARG A 1 82  ? 10.769 26.574 -1.894  1.00 59.77 ? 82  ARG A NH2 1 
ATOM   605  N N   . LEU A 1 83  ? 17.674 29.560 -2.778  1.00 24.61 ? 83  LEU A N   1 
ATOM   606  C CA  . LEU A 1 83  ? 18.931 29.834 -2.082  1.00 29.02 ? 83  LEU A CA  1 
ATOM   607  C C   . LEU A 1 83  ? 18.839 31.088 -1.223  1.00 30.30 ? 83  LEU A C   1 
ATOM   608  O O   . LEU A 1 83  ? 19.398 31.128 -0.120  1.00 27.48 ? 83  LEU A O   1 
ATOM   609  C CB  . LEU A 1 83  ? 20.085 29.963 -3.077  1.00 29.40 ? 83  LEU A CB  1 
ATOM   610  C CG  . LEU A 1 83  ? 20.747 28.679 -3.568  1.00 31.20 ? 83  LEU A CG  1 
ATOM   611  C CD1 . LEU A 1 83  ? 21.779 29.014 -4.637  1.00 22.01 ? 83  LEU A CD1 1 
ATOM   612  C CD2 . LEU A 1 83  ? 21.393 27.927 -2.405  1.00 28.52 ? 83  LEU A CD2 1 
ATOM   613  N N   . PHE A 1 84  ? 18.150 32.126 -1.711  1.00 28.61 ? 84  PHE A N   1 
ATOM   614  C CA  . PHE A 1 84  ? 17.989 33.338 -0.906  1.00 32.17 ? 84  PHE A CA  1 
ATOM   615  C C   . PHE A 1 84  ? 17.295 33.033 0.411   1.00 31.47 ? 84  PHE A C   1 
ATOM   616  O O   . PHE A 1 84  ? 17.669 33.576 1.458   1.00 35.44 ? 84  PHE A O   1 
ATOM   617  C CB  . PHE A 1 84  ? 17.192 34.400 -1.663  1.00 36.86 ? 84  PHE A CB  1 
ATOM   618  C CG  . PHE A 1 84  ? 18.002 35.193 -2.636  1.00 42.50 ? 84  PHE A CG  1 
ATOM   619  C CD1 . PHE A 1 84  ? 18.193 34.738 -3.925  1.00 45.31 ? 84  PHE A CD1 1 
ATOM   620  C CD2 . PHE A 1 84  ? 18.581 36.393 -2.260  1.00 48.28 ? 84  PHE A CD2 1 
ATOM   621  C CE1 . PHE A 1 84  ? 18.934 35.468 -4.829  1.00 51.90 ? 84  PHE A CE1 1 
ATOM   622  C CE2 . PHE A 1 84  ? 19.326 37.128 -3.160  1.00 48.61 ? 84  PHE A CE2 1 
ATOM   623  C CZ  . PHE A 1 84  ? 19.499 36.661 -4.448  1.00 47.80 ? 84  PHE A CZ  1 
ATOM   624  N N   . ILE A 1 85  ? 16.277 32.176 0.376   1.00 25.64 ? 85  ILE A N   1 
ATOM   625  C CA  . ILE A 1 85  ? 15.571 31.808 1.596   1.00 28.11 ? 85  ILE A CA  1 
ATOM   626  C C   . ILE A 1 85  ? 16.491 31.010 2.514   1.00 30.49 ? 85  ILE A C   1 
ATOM   627  O O   . ILE A 1 85  ? 16.629 31.316 3.705   1.00 27.73 ? 85  ILE A O   1 
ATOM   628  C CB  . ILE A 1 85  ? 14.294 31.025 1.250   1.00 30.41 ? 85  ILE A CB  1 
ATOM   629  C CG1 . ILE A 1 85  ? 13.252 31.965 0.636   1.00 37.82 ? 85  ILE A CG1 1 
ATOM   630  C CG2 . ILE A 1 85  ? 13.729 30.353 2.496   1.00 30.37 ? 85  ILE A CG2 1 
ATOM   631  C CD1 . ILE A 1 85  ? 12.078 31.248 -0.009  1.00 43.10 ? 85  ILE A CD1 1 
ATOM   632  N N   . LEU A 1 86  ? 17.150 29.985 1.965   1.00 26.64 ? 86  LEU A N   1 
ATOM   633  C CA  . LEU A 1 86  ? 18.045 29.153 2.764   1.00 26.57 ? 86  LEU A CA  1 
ATOM   634  C C   . LEU A 1 86  ? 19.173 29.966 3.388   1.00 27.50 ? 86  LEU A C   1 
ATOM   635  O O   . LEU A 1 86  ? 19.595 29.674 4.511   1.00 33.63 ? 86  LEU A O   1 
ATOM   636  C CB  . LEU A 1 86  ? 18.623 28.029 1.901   1.00 30.37 ? 86  LEU A CB  1 
ATOM   637  C CG  . LEU A 1 86  ? 17.765 26.786 1.669   1.00 35.86 ? 86  LEU A CG  1 
ATOM   638  C CD1 . LEU A 1 86  ? 18.377 25.917 0.581   1.00 33.00 ? 86  LEU A CD1 1 
ATOM   639  C CD2 . LEU A 1 86  ? 17.600 25.992 2.958   1.00 40.87 ? 86  LEU A CD2 1 
ATOM   640  N N   . LEU A 1 87  ? 19.674 30.979 2.689   1.00 24.26 ? 87  LEU A N   1 
ATOM   641  C CA  . LEU A 1 87  ? 20.771 31.794 3.197   1.00 27.87 ? 87  LEU A CA  1 
ATOM   642  C C   . LEU A 1 87  ? 20.314 32.967 4.059   1.00 42.19 ? 87  LEU A C   1 
ATOM   643  O O   . LEU A 1 87  ? 21.157 33.766 4.481   1.00 39.24 ? 87  LEU A O   1 
ATOM   644  C CB  . LEU A 1 87  ? 21.626 32.310 2.034   1.00 31.05 ? 87  LEU A CB  1 
ATOM   645  C CG  . LEU A 1 87  ? 22.353 31.231 1.228   1.00 27.13 ? 87  LEU A CG  1 
ATOM   646  C CD1 . LEU A 1 87  ? 22.949 31.825 -0.029  1.00 27.80 ? 87  LEU A CD1 1 
ATOM   647  C CD2 . LEU A 1 87  ? 23.447 30.599 2.088   1.00 29.19 ? 87  LEU A CD2 1 
ATOM   648  N N   . GLY A 1 88  ? 19.016 33.095 4.333   1.00 34.37 ? 88  GLY A N   1 
ATOM   649  C CA  . GLY A 1 88  ? 18.545 34.126 5.238   1.00 34.34 ? 88  GLY A CA  1 
ATOM   650  C C   . GLY A 1 88  ? 18.447 35.514 4.653   1.00 35.76 ? 88  GLY A C   1 
ATOM   651  O O   . GLY A 1 88  ? 18.312 36.482 5.406   1.00 44.29 ? 88  GLY A O   1 
ATOM   652  N N   . ALA A 1 89  ? 18.502 35.649 3.332   1.00 39.07 ? 89  ALA A N   1 
ATOM   653  C CA  . ALA A 1 89  ? 18.427 36.965 2.713   1.00 44.18 ? 89  ALA A CA  1 
ATOM   654  C C   . ALA A 1 89  ? 17.000 37.447 2.492   1.00 51.51 ? 89  ALA A C   1 
ATOM   655  O O   . ALA A 1 89  ? 16.814 38.542 1.951   1.00 56.96 ? 89  ALA A O   1 
ATOM   656  C CB  . ALA A 1 89  ? 19.174 36.962 1.377   1.00 41.06 ? 89  ALA A CB  1 
ATOM   657  N N   . GLU A 1 90  ? 15.989 36.678 2.893   1.00 53.17 ? 90  GLU A N   1 
ATOM   658  C CA  . GLU A 1 90  ? 14.614 37.058 2.604   1.00 58.07 ? 90  GLU A CA  1 
ATOM   659  C C   . GLU A 1 90  ? 13.929 37.806 3.738   1.00 64.17 ? 90  GLU A C   1 
ATOM   660  O O   . GLU A 1 90  ? 12.957 38.524 3.476   1.00 75.82 ? 90  GLU A O   1 
ATOM   661  C CB  . GLU A 1 90  ? 13.781 35.824 2.250   1.00 58.78 ? 90  GLU A CB  1 
ATOM   662  C CG  . GLU A 1 90  ? 13.851 35.461 0.782   1.00 59.08 ? 90  GLU A CG  1 
ATOM   663  C CD  . GLU A 1 90  ? 13.445 36.611 -0.116  1.00 62.81 ? 90  GLU A CD  1 
ATOM   664  O OE1 . GLU A 1 90  ? 12.303 37.100 0.009   1.00 67.13 ? 90  GLU A OE1 1 
ATOM   665  O OE2 . GLU A 1 90  ? 14.268 37.016 -0.960  1.00 64.58 ? 90  GLU A OE2 1 
ATOM   666  N N   . ASN A 1 91  ? 14.408 37.663 4.974   1.00 75.36 ? 91  ASN A N   1 
ATOM   667  C CA  . ASN A 1 91  ? 13.822 38.340 6.126   1.00 89.52 ? 91  ASN A CA  1 
ATOM   668  C C   . ASN A 1 91  ? 12.330 38.054 6.237   1.00 83.22 ? 91  ASN A C   1 
ATOM   669  O O   . ASN A 1 91  ? 11.495 38.901 5.900   1.00 80.38 ? 91  ASN A O   1 
ATOM   670  C CB  . ASN A 1 91  ? 14.070 39.849 6.056   1.00 93.00 ? 91  ASN A CB  1 
ATOM   671  C CG  . ASN A 1 91  ? 13.897 40.531 7.402   1.00 97.79 ? 91  ASN A CG  1 
ATOM   672  O OD1 . ASN A 1 91  ? 12.888 40.343 8.084   1.00 90.86 ? 91  ASN A OD1 1 
ATOM   673  N ND2 . ASN A 1 91  ? 14.887 41.326 7.791   1.00 98.54 ? 91  ASN A ND2 1 
ATOM   674  N N   . ILE A 1 92  ? 11.993 36.860 6.706   1.00 66.31 ? 92  ILE A N   1 
ATOM   675  C CA  . ILE A 1 92  ? 10.617 36.469 6.976   1.00 59.28 ? 92  ILE A CA  1 
ATOM   676  C C   . ILE A 1 92  ? 10.361 36.686 8.460   1.00 63.77 ? 92  ILE A C   1 
ATOM   677  O O   . ILE A 1 92  ? 11.029 36.078 9.306   1.00 50.16 ? 92  ILE A O   1 
ATOM   678  C CB  . ILE A 1 92  ? 10.365 35.009 6.573   1.00 57.72 ? 92  ILE A CB  1 
ATOM   679  C CG1 . ILE A 1 92  ? 10.515 34.847 5.059   1.00 63.77 ? 92  ILE A CG1 1 
ATOM   680  C CG2 . ILE A 1 92  ? 8.987  34.558 7.024   1.00 56.48 ? 92  ILE A CG2 1 
ATOM   681  C CD1 . ILE A 1 92  ? 11.167 33.549 4.647   1.00 57.87 ? 92  ILE A CD1 1 
ATOM   682  N N   . ASP A 1 93  ? 9.403  37.560 8.783   1.00 64.59 ? 93  ASP A N   1 
ATOM   683  C CA  . ASP A 1 93  ? 9.130  37.879 10.181  1.00 66.33 ? 93  ASP A CA  1 
ATOM   684  C C   . ASP A 1 93  ? 8.655  36.666 10.970  1.00 58.93 ? 93  ASP A C   1 
ATOM   685  O O   . ASP A 1 93  ? 8.771  36.655 12.200  1.00 55.86 ? 93  ASP A O   1 
ATOM   686  C CB  . ASP A 1 93  ? 8.100  39.007 10.273  1.00 66.78 ? 93  ASP A CB  1 
ATOM   687  C CG  . ASP A 1 93  ? 6.946  38.823 9.311   1.00 79.52 ? 93  ASP A CG  1 
ATOM   688  O OD1 . ASP A 1 93  ? 6.338  37.731 9.309   1.00 85.84 ? 93  ASP A OD1 1 
ATOM   689  O OD2 . ASP A 1 93  ? 6.639  39.775 8.562   1.00 86.79 ? 93  ASP A OD2 1 
ATOM   690  N N   . ARG A 1 94  ? 8.128  35.648 10.288  1.00 53.23 ? 94  ARG A N   1 
ATOM   691  C CA  . ARG A 1 94  ? 7.756  34.407 10.956  1.00 54.79 ? 94  ARG A CA  1 
ATOM   692  C C   . ARG A 1 94  ? 8.969  33.701 11.553  1.00 58.15 ? 94  ARG A C   1 
ATOM   693  O O   . ARG A 1 94  ? 8.850  33.019 12.577  1.00 50.27 ? 94  ARG A O   1 
ATOM   694  C CB  . ARG A 1 94  ? 7.042  33.490 9.962   1.00 53.18 ? 94  ARG A CB  1 
ATOM   695  C CG  . ARG A 1 94  ? 6.618  32.143 10.507  1.00 58.22 ? 94  ARG A CG  1 
ATOM   696  C CD  . ARG A 1 94  ? 5.310  31.694 9.881   1.00 63.34 ? 94  ARG A CD  1 
ATOM   697  N NE  . ARG A 1 94  ? 4.866  30.411 10.412  1.00 68.07 ? 94  ARG A NE  1 
ATOM   698  C CZ  . ARG A 1 94  ? 4.333  29.445 9.676   1.00 70.83 ? 94  ARG A CZ  1 
ATOM   699  N NH1 . ARG A 1 94  ? 4.166  29.583 8.370   1.00 68.05 ? 94  ARG A NH1 1 
ATOM   700  N NH2 . ARG A 1 94  ? 3.961  28.311 10.264  1.00 62.36 ? 94  ARG A NH2 1 
ATOM   701  N N   . LEU A 1 95  ? 10.141 33.860 10.941  1.00 50.45 ? 95  LEU A N   1 
ATOM   702  C CA  . LEU A 1 95  ? 11.326 33.112 11.340  1.00 43.62 ? 95  LEU A CA  1 
ATOM   703  C C   . LEU A 1 95  ? 12.201 33.842 12.348  1.00 48.70 ? 95  LEU A C   1 
ATOM   704  O O   . LEU A 1 95  ? 13.149 33.239 12.866  1.00 51.61 ? 95  LEU A O   1 
ATOM   705  C CB  . LEU A 1 95  ? 12.165 32.761 10.106  1.00 45.78 ? 95  LEU A CB  1 
ATOM   706  C CG  . LEU A 1 95  ? 11.389 32.205 8.913   1.00 53.30 ? 95  LEU A CG  1 
ATOM   707  C CD1 . LEU A 1 95  ? 12.325 31.849 7.774   1.00 59.28 ? 95  LEU A CD1 1 
ATOM   708  C CD2 . LEU A 1 95  ? 10.593 30.993 9.349   1.00 58.61 ? 95  LEU A CD2 1 
ATOM   709  N N   . GLN A 1 96  ? 11.914 35.108 12.646  1.00 47.37 ? 96  GLN A N   1 
ATOM   710  C CA  . GLN A 1 96  ? 12.794 35.870 13.522  1.00 50.58 ? 96  GLN A CA  1 
ATOM   711  C C   . GLN A 1 96  ? 12.998 35.265 14.914  1.00 50.15 ? 96  GLN A C   1 
ATOM   712  O O   . GLN A 1 96  ? 14.114 35.388 15.436  1.00 47.85 ? 96  GLN A O   1 
ATOM   713  C CB  . GLN A 1 96  ? 12.298 37.319 13.624  1.00 53.04 ? 96  GLN A CB  1 
ATOM   714  C CG  . GLN A 1 96  ? 12.154 38.007 12.271  1.00 54.90 ? 96  GLN A CG  1 
ATOM   715  C CD  . GLN A 1 96  ? 13.391 37.840 11.393  1.00 70.27 ? 96  GLN A CD  1 
ATOM   716  O OE1 . GLN A 1 96  ? 14.398 38.525 11.577  1.00 68.71 ? 96  GLN A OE1 1 
ATOM   717  N NE2 . GLN A 1 96  ? 13.313 36.927 10.428  1.00 63.29 ? 96  GLN A NE2 1 
ATOM   718  N N   . PRO A 1 97  ? 12.007 34.624 15.555  1.00 47.93 ? 97  PRO A N   1 
ATOM   719  C CA  . PRO A 1 97  ? 12.330 33.930 16.812  1.00 44.38 ? 97  PRO A CA  1 
ATOM   720  C C   . PRO A 1 97  ? 13.218 32.717 16.605  1.00 37.75 ? 97  PRO A C   1 
ATOM   721  O O   . PRO A 1 97  ? 14.044 32.420 17.477  1.00 37.07 ? 97  PRO A O   1 
ATOM   722  C CB  . PRO A 1 97  ? 10.948 33.546 17.369  1.00 43.19 ? 97  PRO A CB  1 
ATOM   723  C CG  . PRO A 1 97  ? 9.980  34.415 16.621  1.00 43.48 ? 97  PRO A CG  1 
ATOM   724  C CD  . PRO A 1 97  ? 10.569 34.529 15.264  1.00 45.23 ? 97  PRO A CD  1 
ATOM   725  N N   . TYR A 1 98  ? 13.079 32.008 15.481  1.00 35.74 ? 98  TYR A N   1 
ATOM   726  C CA  . TYR A 1 98  ? 13.979 30.892 15.205  1.00 41.06 ? 98  TYR A CA  1 
ATOM   727  C C   . TYR A 1 98  ? 15.398 31.387 14.966  1.00 40.07 ? 98  TYR A C   1 
ATOM   728  O O   . TYR A 1 98  ? 16.368 30.756 15.405  1.00 34.80 ? 98  TYR A O   1 
ATOM   729  C CB  . TYR A 1 98  ? 13.502 30.093 13.992  1.00 35.53 ? 98  TYR A CB  1 
ATOM   730  C CG  . TYR A 1 98  ? 12.152 29.425 14.138  1.00 38.85 ? 98  TYR A CG  1 
ATOM   731  C CD1 . TYR A 1 98  ? 10.977 30.167 14.078  1.00 40.66 ? 98  TYR A CD1 1 
ATOM   732  C CD2 . TYR A 1 98  ? 12.052 28.051 14.327  1.00 33.57 ? 98  TYR A CD2 1 
ATOM   733  C CE1 . TYR A 1 98  ? 9.740  29.562 14.202  1.00 39.92 ? 98  TYR A CE1 1 
ATOM   734  C CE2 . TYR A 1 98  ? 10.815 27.434 14.457  1.00 37.84 ? 98  TYR A CE2 1 
ATOM   735  C CZ  . TYR A 1 98  ? 9.663  28.194 14.391  1.00 39.43 ? 98  TYR A CZ  1 
ATOM   736  O OH  . TYR A 1 98  ? 8.430  27.591 14.515  1.00 38.15 ? 98  TYR A OH  1 
ATOM   737  N N   . LEU A 1 99  ? 15.536 32.508 14.257  1.00 41.43 ? 99  LEU A N   1 
ATOM   738  C CA  . LEU A 1 99  ? 16.853 33.075 13.994  1.00 35.38 ? 99  LEU A CA  1 
ATOM   739  C C   . LEU A 1 99  ? 17.465 33.666 15.255  1.00 39.88 ? 99  LEU A C   1 
ATOM   740  O O   . LEU A 1 99  ? 18.689 33.621 15.431  1.00 37.97 ? 99  LEU A O   1 
ATOM   741  C CB  . LEU A 1 99  ? 16.744 34.135 12.898  1.00 39.09 ? 99  LEU A CB  1 
ATOM   742  C CG  . LEU A 1 99  ? 16.290 33.598 11.536  1.00 46.26 ? 99  LEU A CG  1 
ATOM   743  C CD1 . LEU A 1 99  ? 16.118 34.728 10.523  1.00 38.57 ? 99  LEU A CD1 1 
ATOM   744  C CD2 . LEU A 1 99  ? 17.259 32.543 11.015  1.00 41.47 ? 99  LEU A CD2 1 
ATOM   745  N N   . ARG A 1 100 ? 16.634 34.222 16.141  1.00 35.69 ? 100 ARG A N   1 
ATOM   746  C CA  . ARG A 1 100 ? 17.130 34.679 17.434  1.00 43.84 ? 100 ARG A CA  1 
ATOM   747  C C   . ARG A 1 100 ? 17.644 33.508 18.263  1.00 37.55 ? 100 ARG A C   1 
ATOM   748  O O   . ARG A 1 100 ? 18.653 33.629 18.968  1.00 34.92 ? 100 ARG A O   1 
ATOM   749  C CB  . ARG A 1 100 ? 16.026 35.434 18.180  1.00 43.79 ? 100 ARG A CB  1 
ATOM   750  C CG  . ARG A 1 100 ? 16.531 36.338 19.302  1.00 47.78 ? 100 ARG A CG  1 
ATOM   751  C CD  . ARG A 1 100 ? 15.803 36.103 20.624  1.00 52.46 ? 100 ARG A CD  1 
ATOM   752  N NE  . ARG A 1 100 ? 15.693 34.691 20.974  1.00 57.31 ? 100 ARG A NE  1 
ATOM   753  C CZ  . ARG A 1 100 ? 14.545 34.037 21.101  1.00 58.06 ? 100 ARG A CZ  1 
ATOM   754  N NH1 . ARG A 1 100 ? 13.380 34.642 20.926  1.00 43.50 ? 100 ARG A NH1 1 
ATOM   755  N NH2 . ARG A 1 100 ? 14.567 32.744 21.415  1.00 54.50 ? 100 ARG A NH2 1 
ATOM   756  N N   . LEU A 1 101 ? 16.966 32.362 18.184  1.00 34.48 ? 101 LEU A N   1 
ATOM   757  C CA  . LEU A 1 101 ? 17.425 31.178 18.906  1.00 36.13 ? 101 LEU A CA  1 
ATOM   758  C C   . LEU A 1 101 ? 18.724 30.639 18.323  1.00 27.32 ? 101 LEU A C   1 
ATOM   759  O O   . LEU A 1 101 ? 19.628 30.237 19.067  1.00 28.41 ? 101 LEU A O   1 
ATOM   760  C CB  . LEU A 1 101 ? 16.351 30.095 18.875  1.00 29.62 ? 101 LEU A CB  1 
ATOM   761  C CG  . LEU A 1 101 ? 16.553 28.990 19.908  1.00 28.58 ? 101 LEU A CG  1 
ATOM   762  C CD1 . LEU A 1 101 ? 16.551 29.571 21.312  1.00 32.55 ? 101 LEU A CD1 1 
ATOM   763  C CD2 . LEU A 1 101 ? 15.481 27.936 19.744  1.00 32.62 ? 101 LEU A CD2 1 
ATOM   764  N N   . TRP A 1 102 ? 18.826 30.607 16.993  1.00 30.99 ? 102 TRP A N   1 
ATOM   765  C CA  . TRP A 1 102 ? 20.061 30.165 16.352  1.00 34.21 ? 102 TRP A CA  1 
ATOM   766  C C   . TRP A 1 102 ? 21.244 31.004 16.820  1.00 30.62 ? 102 TRP A C   1 
ATOM   767  O O   . TRP A 1 102 ? 22.291 30.467 17.202  1.00 28.79 ? 102 TRP A O   1 
ATOM   768  C CB  . TRP A 1 102 ? 19.908 30.228 14.830  1.00 33.82 ? 102 TRP A CB  1 
ATOM   769  C CG  . TRP A 1 102 ? 21.158 29.875 14.075  1.00 34.82 ? 102 TRP A CG  1 
ATOM   770  C CD1 . TRP A 1 102 ? 22.312 30.607 13.991  1.00 44.59 ? 102 TRP A CD1 1 
ATOM   771  C CD2 . TRP A 1 102 ? 21.383 28.686 13.313  1.00 41.68 ? 102 TRP A CD2 1 
ATOM   772  N NE1 . TRP A 1 102 ? 23.235 29.947 13.216  1.00 41.68 ? 102 TRP A NE1 1 
ATOM   773  C CE2 . TRP A 1 102 ? 22.690 28.765 12.788  1.00 38.77 ? 102 TRP A CE2 1 
ATOM   774  C CE3 . TRP A 1 102 ? 20.603 27.564 13.016  1.00 40.53 ? 102 TRP A CE3 1 
ATOM   775  C CZ2 . TRP A 1 102 ? 23.233 27.766 11.985  1.00 38.40 ? 102 TRP A CZ2 1 
ATOM   776  C CZ3 . TRP A 1 102 ? 21.144 26.573 12.219  1.00 49.08 ? 102 TRP A CZ3 1 
ATOM   777  C CH2 . TRP A 1 102 ? 22.447 26.681 11.711  1.00 40.00 ? 102 TRP A CH2 1 
ATOM   778  N N   . ASN A 1 103 ? 21.091 32.330 16.807  1.00 30.05 ? 103 ASN A N   1 
ATOM   779  C CA  . ASN A 1 103 ? 22.174 33.199 17.255  1.00 32.16 ? 103 ASN A CA  1 
ATOM   780  C C   . ASN A 1 103 ? 22.471 32.978 18.732  1.00 31.51 ? 103 ASN A C   1 
ATOM   781  O O   . ASN A 1 103 ? 23.632 33.025 19.157  1.00 32.85 ? 103 ASN A O   1 
ATOM   782  C CB  . ASN A 1 103 ? 21.813 34.660 16.996  1.00 34.77 ? 103 ASN A CB  1 
ATOM   783  C CG  . ASN A 1 103 ? 21.903 35.028 15.528  1.00 40.10 ? 103 ASN A CG  1 
ATOM   784  O OD1 . ASN A 1 103 ? 22.845 34.648 14.835  1.00 45.39 ? 103 ASN A OD1 1 
ATOM   785  N ND2 . ASN A 1 103 ? 20.924 35.787 15.051  1.00 54.14 ? 103 ASN A ND2 1 
ATOM   786  N N   . GLU A 1 104 ? 21.427 32.730 19.526  1.00 29.41 ? 104 GLU A N   1 
ATOM   787  C CA  . GLU A 1 104 ? 21.603 32.403 20.936  1.00 30.54 ? 104 GLU A CA  1 
ATOM   788  C C   . GLU A 1 104 ? 22.417 31.126 21.107  1.00 29.09 ? 104 GLU A C   1 
ATOM   789  O O   . GLU A 1 104 ? 23.338 31.064 21.933  1.00 29.91 ? 104 GLU A O   1 
ATOM   790  C CB  . GLU A 1 104 ? 20.233 32.251 21.595  1.00 33.03 ? 104 GLU A CB  1 
ATOM   791  C CG  . GLU A 1 104 ? 20.106 32.879 22.958  1.00 45.17 ? 104 GLU A CG  1 
ATOM   792  C CD  . GLU A 1 104 ? 18.718 32.693 23.533  1.00 46.96 ? 104 GLU A CD  1 
ATOM   793  O OE1 . GLU A 1 104 ? 17.730 33.041 22.845  1.00 47.08 ? 104 GLU A OE1 1 
ATOM   794  O OE2 . GLU A 1 104 ? 18.617 32.176 24.663  1.00 41.91 ? 104 GLU A OE2 1 
ATOM   795  N N   . ALA A 1 105 ? 22.074 30.086 20.344  1.00 25.04 ? 105 ALA A N   1 
ATOM   796  C CA  . ALA A 1 105 ? 22.798 28.824 20.440  1.00 26.86 ? 105 ALA A CA  1 
ATOM   797  C C   . ALA A 1 105 ? 24.261 29.000 20.057  1.00 28.28 ? 105 ALA A C   1 
ATOM   798  O O   . ALA A 1 105 ? 25.143 28.360 20.640  1.00 26.73 ? 105 ALA A O   1 
ATOM   799  C CB  . ALA A 1 105 ? 22.136 27.772 19.553  1.00 23.72 ? 105 ALA A CB  1 
ATOM   800  N N   . GLU A 1 106 ? 24.536 29.871 19.081  1.00 26.76 ? 106 GLU A N   1 
ATOM   801  C CA  . GLU A 1 106 ? 25.914 30.112 18.663  1.00 29.39 ? 106 GLU A CA  1 
ATOM   802  C C   . GLU A 1 106 ? 26.791 30.563 19.819  1.00 29.22 ? 106 GLU A C   1 
ATOM   803  O O   . GLU A 1 106 ? 27.971 30.205 19.875  1.00 31.42 ? 106 GLU A O   1 
ATOM   804  C CB  . GLU A 1 106 ? 25.952 31.149 17.541  1.00 28.05 ? 106 GLU A CB  1 
ATOM   805  C CG  . GLU A 1 106 ? 27.180 31.039 16.650  1.00 33.36 ? 106 GLU A CG  1 
ATOM   806  C CD  . GLU A 1 106 ? 27.249 32.145 15.615  1.00 50.24 ? 106 GLU A CD  1 
ATOM   807  O OE1 . GLU A 1 106 ? 26.214 32.807 15.377  1.00 43.93 ? 106 GLU A OE1 1 
ATOM   808  O OE2 . GLU A 1 106 ? 28.345 32.364 15.057  1.00 52.09 ? 106 GLU A OE2 1 
ATOM   809  N N   . LEU A 1 107 ? 26.241 31.336 20.753  1.00 32.94 ? 107 LEU A N   1 
ATOM   810  C CA  . LEU A 1 107 ? 27.036 31.793 21.886  1.00 30.02 ? 107 LEU A CA  1 
ATOM   811  C C   . LEU A 1 107 ? 27.226 30.704 22.938  1.00 42.17 ? 107 LEU A C   1 
ATOM   812  O O   . LEU A 1 107 ? 28.203 30.748 23.694  1.00 43.19 ? 107 LEU A O   1 
ATOM   813  C CB  . LEU A 1 107 ? 26.387 33.027 22.513  1.00 38.56 ? 107 LEU A CB  1 
ATOM   814  C CG  . LEU A 1 107 ? 26.254 34.234 21.579  1.00 50.52 ? 107 LEU A CG  1 
ATOM   815  C CD1 . LEU A 1 107 ? 25.692 35.439 22.316  1.00 50.51 ? 107 LEU A CD1 1 
ATOM   816  C CD2 . LEU A 1 107 ? 27.596 34.565 20.941  1.00 47.72 ? 107 LEU A CD2 1 
ATOM   817  N N   . LEU A 1 108 ? 26.328 29.718 22.994  1.00 28.79 ? 108 LEU A N   1 
ATOM   818  C CA  . LEU A 1 108 ? 26.375 28.707 24.043  1.00 27.21 ? 108 LEU A CA  1 
ATOM   819  C C   . LEU A 1 108 ? 27.284 27.530 23.715  1.00 26.40 ? 108 LEU A C   1 
ATOM   820  O O   . LEU A 1 108 ? 27.563 26.721 24.608  1.00 30.38 ? 108 LEU A O   1 
ATOM   821  C CB  . LEU A 1 108 ? 24.968 28.183 24.332  1.00 29.48 ? 108 LEU A CB  1 
ATOM   822  C CG  . LEU A 1 108 ? 23.997 29.112 25.051  1.00 42.62 ? 108 LEU A CG  1 
ATOM   823  C CD1 . LEU A 1 108 ? 22.648 28.419 25.209  1.00 34.91 ? 108 LEU A CD1 1 
ATOM   824  C CD2 . LEU A 1 108 ? 24.561 29.506 26.406  1.00 38.03 ? 108 LEU A CD2 1 
ATOM   825  N N   . ILE A 1 109 ? 27.752 27.407 22.472  1.00 24.05 ? 109 ILE A N   1 
ATOM   826  C CA  . ILE A 1 109 ? 28.583 26.267 22.094  1.00 30.25 ? 109 ILE A CA  1 
ATOM   827  C C   . ILE A 1 109 ? 29.902 26.224 22.849  1.00 29.97 ? 109 ILE A C   1 
ATOM   828  O O   . ILE A 1 109 ? 30.535 25.164 22.914  1.00 30.42 ? 109 ILE A O   1 
ATOM   829  C CB  . ILE A 1 109 ? 28.824 26.265 20.571  1.00 28.09 ? 109 ILE A CB  1 
ATOM   830  C CG1 . ILE A 1 109 ? 29.738 27.425 20.165  1.00 31.91 ? 109 ILE A CG1 1 
ATOM   831  C CG2 . ILE A 1 109 ? 27.493 26.273 19.821  1.00 25.05 ? 109 ILE A CG2 1 
ATOM   832  C CD1 . ILE A 1 109 ? 30.047 27.469 18.680  1.00 30.23 ? 109 ILE A CD1 1 
ATOM   833  N N   . GLU A 1 110 ? 30.339 27.343 23.425  1.00 26.91 ? 110 GLU A N   1 
ATOM   834  C CA  . GLU A 1 110 ? 31.584 27.367 24.180  1.00 33.89 ? 110 GLU A CA  1 
ATOM   835  C C   . GLU A 1 110 ? 31.413 26.975 25.643  1.00 42.94 ? 110 GLU A C   1 
ATOM   836  O O   . GLU A 1 110 ? 32.418 26.760 26.329  1.00 40.42 ? 110 GLU A O   1 
ATOM   837  C CB  . GLU A 1 110 ? 32.223 28.756 24.109  1.00 37.22 ? 110 GLU A CB  1 
ATOM   838  C CG  . GLU A 1 110 ? 32.676 29.162 22.722  1.00 47.72 ? 110 GLU A CG  1 
ATOM   839  C CD  . GLU A 1 110 ? 32.944 30.649 22.620  1.00 58.85 ? 110 GLU A CD  1 
ATOM   840  O OE1 . GLU A 1 110 ? 33.805 31.148 23.376  1.00 60.15 ? 110 GLU A OE1 1 
ATOM   841  O OE2 . GLU A 1 110 ? 32.291 31.317 21.789  1.00 54.78 ? 110 GLU A OE2 1 
ATOM   842  N N   . GLN A 1 111 ? 30.181 26.879 26.140  1.00 31.10 ? 111 GLN A N   1 
ATOM   843  C CA  . GLN A 1 111 ? 29.959 26.579 27.547  1.00 41.13 ? 111 GLN A CA  1 
ATOM   844  C C   . GLN A 1 111 ? 28.953 25.463 27.794  1.00 40.76 ? 111 GLN A C   1 
ATOM   845  O O   . GLN A 1 111 ? 28.775 25.064 28.951  1.00 35.30 ? 111 GLN A O   1 
ATOM   846  C CB  . GLN A 1 111 ? 29.514 27.845 28.297  1.00 40.80 ? 111 GLN A CB  1 
ATOM   847  C CG  . GLN A 1 111 ? 28.110 28.313 27.961  1.00 48.08 ? 111 GLN A CG  1 
ATOM   848  C CD  . GLN A 1 111 ? 27.832 29.715 28.468  1.00 58.34 ? 111 GLN A CD  1 
ATOM   849  O OE1 . GLN A 1 111 ? 27.207 29.899 29.515  1.00 62.60 ? 111 GLN A OE1 1 
ATOM   850  N NE2 . GLN A 1 111 ? 28.307 30.714 27.732  1.00 53.95 ? 111 GLN A NE2 1 
ATOM   851  N N   . ASP A 1 112 ? 28.309 24.934 26.753  1.00 33.05 ? 112 ASP A N   1 
ATOM   852  C CA  . ASP A 1 112 ? 27.367 23.827 26.889  1.00 32.96 ? 112 ASP A CA  1 
ATOM   853  C C   . ASP A 1 112 ? 27.734 22.742 25.887  1.00 29.63 ? 112 ASP A C   1 
ATOM   854  O O   . ASP A 1 112 ? 27.665 22.968 24.675  1.00 27.02 ? 112 ASP A O   1 
ATOM   855  C CB  . ASP A 1 112 ? 25.924 24.293 26.670  1.00 31.11 ? 112 ASP A CB  1 
ATOM   856  C CG  . ASP A 1 112 ? 24.905 23.217 27.015  1.00 39.60 ? 112 ASP A CG  1 
ATOM   857  O OD1 . ASP A 1 112 ? 24.918 22.146 26.363  1.00 34.58 ? 112 ASP A OD1 1 
ATOM   858  O OD2 . ASP A 1 112 ? 24.091 23.443 27.939  1.00 36.40 ? 112 ASP A OD2 1 
ATOM   859  N N   . ILE A 1 113 ? 28.077 21.557 26.396  1.00 28.12 ? 113 ILE A N   1 
ATOM   860  C CA  . ILE A 1 113 ? 28.587 20.483 25.545  1.00 31.63 ? 113 ILE A CA  1 
ATOM   861  C C   . ILE A 1 113 ? 27.491 19.952 24.624  1.00 30.49 ? 113 ILE A C   1 
ATOM   862  O O   . ILE A 1 113 ? 27.758 19.559 23.480  1.00 24.38 ? 113 ILE A O   1 
ATOM   863  C CB  . ILE A 1 113 ? 29.191 19.341 26.392  1.00 44.52 ? 113 ILE A CB  1 
ATOM   864  C CG1 . ILE A 1 113 ? 30.179 19.846 27.463  1.00 49.70 ? 113 ILE A CG1 1 
ATOM   865  C CG2 . ILE A 1 113 ? 29.871 18.322 25.492  1.00 49.08 ? 113 ILE A CG2 1 
ATOM   866  C CD1 . ILE A 1 113 ? 29.556 20.480 28.724  1.00 48.34 ? 113 ILE A CD1 1 
ATOM   867  N N   . GLU A 1 114 ? 26.249 19.906 25.107  1.00 24.20 ? 114 GLU A N   1 
ATOM   868  C CA  . GLU A 1 114 ? 25.175 19.366 24.277  1.00 27.13 ? 114 GLU A CA  1 
ATOM   869  C C   . GLU A 1 114 ? 24.760 20.348 23.188  1.00 26.62 ? 114 GLU A C   1 
ATOM   870  O O   . GLU A 1 114 ? 24.432 19.936 22.070  1.00 22.42 ? 114 GLU A O   1 
ATOM   871  C CB  . GLU A 1 114 ? 23.969 19.003 25.141  1.00 24.65 ? 114 GLU A CB  1 
ATOM   872  C CG  . GLU A 1 114 ? 24.262 18.013 26.256  1.00 29.94 ? 114 GLU A CG  1 
ATOM   873  C CD  . GLU A 1 114 ? 24.991 16.771 25.775  1.00 35.74 ? 114 GLU A CD  1 
ATOM   874  O OE1 . GLU A 1 114 ? 24.569 16.177 24.762  1.00 36.26 ? 114 GLU A OE1 1 
ATOM   875  O OE2 . GLU A 1 114 ? 25.989 16.384 26.422  1.00 42.90 ? 114 GLU A OE2 1 
ATOM   876  N N   . ILE A 1 115 ? 24.753 21.645 23.497  1.00 18.86 ? 115 ILE A N   1 
ATOM   877  C CA  . ILE A 1 115 ? 24.430 22.639 22.480  1.00 20.76 ? 115 ILE A CA  1 
ATOM   878  C C   . ILE A 1 115 ? 25.543 22.716 21.447  1.00 25.74 ? 115 ILE A C   1 
ATOM   879  O O   . ILE A 1 115 ? 25.291 22.933 20.256  1.00 23.94 ? 115 ILE A O   1 
ATOM   880  C CB  . ILE A 1 115 ? 24.164 24.007 23.137  1.00 23.13 ? 115 ILE A CB  1 
ATOM   881  C CG1 . ILE A 1 115 ? 23.026 23.899 24.156  1.00 29.63 ? 115 ILE A CG1 1 
ATOM   882  C CG2 . ILE A 1 115 ? 23.832 25.046 22.083  1.00 26.62 ? 115 ILE A CG2 1 
ATOM   883  C CD1 . ILE A 1 115 ? 21.666 23.708 23.535  1.00 33.62 ? 115 ILE A CD1 1 
ATOM   884  N N   . GLN A 1 116 ? 26.791 22.525 21.886  1.00 25.56 ? 116 GLN A N   1 
ATOM   885  C CA  . GLN A 1 116 ? 27.925 22.501 20.966  1.00 25.90 ? 116 GLN A CA  1 
ATOM   886  C C   . GLN A 1 116 ? 27.730 21.444 19.886  1.00 26.09 ? 116 GLN A C   1 
ATOM   887  O O   . GLN A 1 116 ? 27.900 21.718 18.690  1.00 26.78 ? 116 GLN A O   1 
ATOM   888  C CB  . GLN A 1 116 ? 29.219 22.246 21.747  1.00 25.58 ? 116 GLN A CB  1 
ATOM   889  C CG  . GLN A 1 116 ? 30.501 22.542 20.977  1.00 30.38 ? 116 GLN A CG  1 
ATOM   890  C CD  . GLN A 1 116 ? 31.006 21.342 20.206  1.00 41.30 ? 116 GLN A CD  1 
ATOM   891  O OE1 . GLN A 1 116 ? 30.741 20.196 20.575  1.00 36.22 ? 116 GLN A OE1 1 
ATOM   892  N NE2 . GLN A 1 116 ? 31.767 21.596 19.145  1.00 40.41 ? 116 GLN A NE2 1 
ATOM   893  N N   . LYS A 1 117 ? 27.359 20.226 20.289  1.00 24.99 ? 117 LYS A N   1 
ATOM   894  C CA  . LYS A 1 117 ? 27.136 19.162 19.316  1.00 26.86 ? 117 LYS A CA  1 
ATOM   895  C C   . LYS A 1 117 ? 25.913 19.444 18.452  1.00 25.83 ? 117 LYS A C   1 
ATOM   896  O O   . LYS A 1 117 ? 25.935 19.196 17.241  1.00 23.40 ? 117 LYS A O   1 
ATOM   897  C CB  . LYS A 1 117 ? 26.987 17.814 20.026  1.00 25.59 ? 117 LYS A CB  1 
ATOM   898  C CG  . LYS A 1 117 ? 28.211 17.404 20.841  1.00 33.32 ? 117 LYS A CG  1 
ATOM   899  C CD  . LYS A 1 117 ? 28.029 16.026 21.472  1.00 32.53 ? 117 LYS A CD  1 
ATOM   900  C CE  . LYS A 1 117 ? 27.141 16.091 22.699  1.00 37.55 ? 117 LYS A CE  1 
ATOM   901  N NZ  . LYS A 1 117 ? 27.081 14.789 23.431  1.00 39.22 ? 117 LYS A NZ  1 
ATOM   902  N N   . ALA A 1 118 ? 24.836 19.957 19.054  1.00 22.47 ? 118 ALA A N   1 
ATOM   903  C CA  . ALA A 1 118 ? 23.611 20.194 18.295  1.00 22.58 ? 118 ALA A CA  1 
ATOM   904  C C   . ALA A 1 118 ? 23.791 21.328 17.295  1.00 22.46 ? 118 ALA A C   1 
ATOM   905  O O   . ALA A 1 118 ? 23.248 21.274 16.186  1.00 21.45 ? 118 ALA A O   1 
ATOM   906  C CB  . ALA A 1 118 ? 22.448 20.493 19.243  1.00 25.06 ? 118 ALA A CB  1 
ATOM   907  N N   . TYR A 1 119 ? 24.546 22.364 17.669  1.00 19.98 ? 119 TYR A N   1 
ATOM   908  C CA  . TYR A 1 119 ? 24.802 23.462 16.738  1.00 22.24 ? 119 TYR A CA  1 
ATOM   909  C C   . TYR A 1 119 ? 25.538 22.973 15.498  1.00 24.14 ? 119 TYR A C   1 
ATOM   910  O O   . TYR A 1 119 ? 25.226 23.391 14.376  1.00 21.98 ? 119 TYR A O   1 
ATOM   911  C CB  . TYR A 1 119 ? 25.602 24.566 17.425  1.00 22.58 ? 119 TYR A CB  1 
ATOM   912  C CG  . TYR A 1 119 ? 25.746 25.824 16.587  1.00 22.60 ? 119 TYR A CG  1 
ATOM   913  C CD1 . TYR A 1 119 ? 24.737 26.779 16.552  1.00 26.97 ? 119 TYR A CD1 1 
ATOM   914  C CD2 . TYR A 1 119 ? 26.880 26.043 15.819  1.00 22.47 ? 119 TYR A CD2 1 
ATOM   915  C CE1 . TYR A 1 119 ? 24.858 27.925 15.783  1.00 25.59 ? 119 TYR A CE1 1 
ATOM   916  C CE2 . TYR A 1 119 ? 27.013 27.189 15.043  1.00 24.05 ? 119 TYR A CE2 1 
ATOM   917  C CZ  . TYR A 1 119 ? 25.998 28.125 15.031  1.00 31.44 ? 119 TYR A CZ  1 
ATOM   918  O OH  . TYR A 1 119 ? 26.121 29.268 14.265  1.00 26.49 ? 119 TYR A OH  1 
ATOM   919  N N   . ASN A 1 120 ? 26.523 22.090 15.678  1.00 22.23 ? 120 ASN A N   1 
ATOM   920  C CA  . ASN A 1 120 ? 27.246 21.566 14.524  1.00 25.55 ? 120 ASN A CA  1 
ATOM   921  C C   . ASN A 1 120 ? 26.354 20.677 13.670  1.00 25.33 ? 120 ASN A C   1 
ATOM   922  O O   . ASN A 1 120 ? 26.462 20.685 12.440  1.00 24.29 ? 120 ASN A O   1 
ATOM   923  C CB  . ASN A 1 120 ? 28.490 20.803 14.978  1.00 26.38 ? 120 ASN A CB  1 
ATOM   924  C CG  . ASN A 1 120 ? 29.641 21.723 15.301  1.00 29.34 ? 120 ASN A CG  1 
ATOM   925  O OD1 . ASN A 1 120 ? 29.533 22.943 15.155  1.00 24.63 ? 120 ASN A OD1 1 
ATOM   926  N ND2 . ASN A 1 120 ? 30.755 21.148 15.735  1.00 26.18 ? 120 ASN A ND2 1 
ATOM   927  N N   . LEU A 1 121 ? 25.472 19.901 14.303  1.00 21.09 ? 121 LEU A N   1 
ATOM   928  C CA  . LEU A 1 121 ? 24.525 19.092 13.543  1.00 24.71 ? 121 LEU A CA  1 
ATOM   929  C C   . LEU A 1 121 ? 23.640 19.968 12.668  1.00 23.53 ? 121 LEU A C   1 
ATOM   930  O O   . LEU A 1 121 ? 23.378 19.639 11.506  1.00 23.30 ? 121 LEU A O   1 
ATOM   931  C CB  . LEU A 1 121 ? 23.664 18.259 14.493  1.00 26.62 ? 121 LEU A CB  1 
ATOM   932  C CG  . LEU A 1 121 ? 24.292 17.003 15.098  1.00 39.74 ? 121 LEU A CG  1 
ATOM   933  C CD1 . LEU A 1 121 ? 23.396 16.449 16.199  1.00 34.50 ? 121 LEU A CD1 1 
ATOM   934  C CD2 . LEU A 1 121 ? 24.543 15.954 14.028  1.00 36.43 ? 121 LEU A CD2 1 
ATOM   935  N N   . ALA A 1 122 ? 23.170 21.091 13.214  1.00 23.12 ? 122 ALA A N   1 
ATOM   936  C CA  . ALA A 1 122 ? 22.339 22.002 12.437  1.00 24.68 ? 122 ALA A CA  1 
ATOM   937  C C   . ALA A 1 122 ? 23.137 22.680 11.334  1.00 25.49 ? 122 ALA A C   1 
ATOM   938  O O   . ALA A 1 122 ? 22.590 22.964 10.260  1.00 21.94 ? 122 ALA A O   1 
ATOM   939  C CB  . ALA A 1 122 ? 21.708 23.045 13.357  1.00 25.24 ? 122 ALA A CB  1 
ATOM   940  N N   . MET A 1 123 ? 24.424 22.955 11.579  1.00 23.04 ? 123 MET A N   1 
ATOM   941  C CA  . MET A 1 123 ? 25.263 23.534 10.534  1.00 24.98 ? 123 MET A CA  1 
ATOM   942  C C   . MET A 1 123 ? 25.464 22.543 9.397   1.00 22.90 ? 123 MET A C   1 
ATOM   943  O O   . MET A 1 123 ? 25.426 22.919 8.220   1.00 23.91 ? 123 MET A O   1 
ATOM   944  C CB  . MET A 1 123 ? 26.617 23.967 11.109  1.00 23.10 ? 123 MET A CB  1 
ATOM   945  C CG  . MET A 1 123 ? 26.545 25.232 11.953  1.00 24.28 ? 123 MET A CG  1 
ATOM   946  S SD  . MET A 1 123 ? 26.441 26.756 10.991  1.00 29.83 ? 123 MET A SD  1 
ATOM   947  C CE  . MET A 1 123 ? 27.586 26.391 9.667   1.00 27.69 ? 123 MET A CE  1 
ATOM   948  N N   . GLN A 1 124 ? 25.662 21.264 9.728   1.00 19.99 ? 124 GLN A N   1 
ATOM   949  C CA  . GLN A 1 124 ? 25.820 20.261 8.682   1.00 24.65 ? 124 GLN A CA  1 
ATOM   950  C C   . GLN A 1 124 ? 24.527 20.081 7.897   1.00 26.56 ? 124 GLN A C   1 
ATOM   951  O O   . GLN A 1 124 ? 24.557 19.872 6.679   1.00 28.08 ? 124 GLN A O   1 
ATOM   952  C CB  . GLN A 1 124 ? 26.263 18.928 9.285   1.00 28.49 ? 124 GLN A CB  1 
ATOM   953  C CG  . GLN A 1 124 ? 27.614 18.975 9.970   1.00 28.77 ? 124 GLN A CG  1 
ATOM   954  C CD  . GLN A 1 124 ? 28.784 18.787 9.016   1.00 37.15 ? 124 GLN A CD  1 
ATOM   955  O OE1 . GLN A 1 124 ? 28.604 18.504 7.829   1.00 34.75 ? 124 GLN A OE1 1 
ATOM   956  N NE2 . GLN A 1 124 ? 29.996 18.936 9.540   1.00 35.00 ? 124 GLN A NE2 1 
ATOM   957  N N   . SER A 1 125 ? 23.379 20.156 8.580   1.00 22.80 ? 125 SER A N   1 
ATOM   958  C CA  . SER A 1 125 ? 22.095 20.062 7.894   1.00 23.71 ? 125 SER A CA  1 
ATOM   959  C C   . SER A 1 125 ? 21.883 21.248 6.962   1.00 27.82 ? 125 SER A C   1 
ATOM   960  O O   . SER A 1 125 ? 21.376 21.086 5.846   1.00 24.45 ? 125 SER A O   1 
ATOM   961  C CB  . SER A 1 125 ? 20.958 19.985 8.913   1.00 27.97 ? 125 SER A CB  1 
ATOM   962  O OG  . SER A 1 125 ? 20.947 18.728 9.569   1.00 41.06 ? 125 SER A OG  1 
ATOM   963  N N   . TRP A 1 126 ? 22.239 22.449 7.424   1.00 22.49 ? 126 TRP A N   1 
ATOM   964  C CA  . TRP A 1 126 ? 22.161 23.644 6.590   1.00 23.39 ? 126 TRP A CA  1 
ATOM   965  C C   . TRP A 1 126 ? 23.010 23.485 5.336   1.00 25.57 ? 126 TRP A C   1 
ATOM   966  O O   . TRP A 1 126 ? 22.558 23.775 4.220   1.00 24.37 ? 126 TRP A O   1 
ATOM   967  C CB  . TRP A 1 126 ? 22.623 24.853 7.406   1.00 24.83 ? 126 TRP A CB  1 
ATOM   968  C CG  . TRP A 1 126 ? 22.423 26.204 6.769   1.00 25.60 ? 126 TRP A CG  1 
ATOM   969  C CD1 . TRP A 1 126 ? 21.562 26.530 5.757   1.00 27.02 ? 126 TRP A CD1 1 
ATOM   970  C CD2 . TRP A 1 126 ? 23.114 27.412 7.117   1.00 27.55 ? 126 TRP A CD2 1 
ATOM   971  N NE1 . TRP A 1 126 ? 21.676 27.873 5.459   1.00 26.28 ? 126 TRP A NE1 1 
ATOM   972  C CE2 . TRP A 1 126 ? 22.623 28.433 6.279   1.00 26.35 ? 126 TRP A CE2 1 
ATOM   973  C CE3 . TRP A 1 126 ? 24.106 27.726 8.055   1.00 25.46 ? 126 TRP A CE3 1 
ATOM   974  C CZ2 . TRP A 1 126 ? 23.085 29.748 6.352   1.00 30.61 ? 126 TRP A CZ2 1 
ATOM   975  C CZ3 . TRP A 1 126 ? 24.565 29.036 8.129   1.00 25.58 ? 126 TRP A CZ3 1 
ATOM   976  C CH2 . TRP A 1 126 ? 24.053 30.029 7.281   1.00 29.19 ? 126 TRP A CH2 1 
ATOM   977  N N   . HIS A 1 127 ? 24.252 23.023 5.504   1.00 22.05 ? 127 HIS A N   1 
ATOM   978  C CA  . HIS A 1 127 ? 25.128 22.791 4.362   1.00 24.01 ? 127 HIS A CA  1 
ATOM   979  C C   . HIS A 1 127 ? 24.510 21.806 3.377   1.00 28.50 ? 127 HIS A C   1 
ATOM   980  O O   . HIS A 1 127 ? 24.558 22.021 2.160   1.00 24.91 ? 127 HIS A O   1 
ATOM   981  C CB  . HIS A 1 127 ? 26.490 22.287 4.843   1.00 25.75 ? 127 HIS A CB  1 
ATOM   982  C CG  . HIS A 1 127 ? 27.434 21.955 3.733   1.00 27.25 ? 127 HIS A CG  1 
ATOM   983  N ND1 . HIS A 1 127 ? 27.653 20.663 3.301   1.00 30.85 ? 127 HIS A ND1 1 
ATOM   984  C CD2 . HIS A 1 127 ? 28.207 22.748 2.954   1.00 25.59 ? 127 HIS A CD2 1 
ATOM   985  C CE1 . HIS A 1 127 ? 28.526 20.675 2.310   1.00 28.14 ? 127 HIS A CE1 1 
ATOM   986  N NE2 . HIS A 1 127 ? 28.877 21.927 2.080   1.00 25.81 ? 127 HIS A NE2 1 
ATOM   987  N N   . GLN A 1 128 ? 23.917 20.722 3.884   1.00 26.92 ? 128 GLN A N   1 
ATOM   988  C CA  . GLN A 1 128 ? 23.312 19.734 2.997   1.00 30.92 ? 128 GLN A CA  1 
ATOM   989  C C   . GLN A 1 128 ? 22.090 20.290 2.273   1.00 29.97 ? 128 GLN A C   1 
ATOM   990  O O   . GLN A 1 128 ? 21.844 19.930 1.117   1.00 28.59 ? 128 GLN A O   1 
ATOM   991  C CB  . GLN A 1 128 ? 22.931 18.481 3.788   1.00 29.01 ? 128 GLN A CB  1 
ATOM   992  C CG  . GLN A 1 128 ? 24.099 17.536 4.037   1.00 38.71 ? 128 GLN A CG  1 
ATOM   993  C CD  . GLN A 1 128 ? 24.949 17.316 2.794   1.00 52.42 ? 128 GLN A CD  1 
ATOM   994  O OE1 . GLN A 1 128 ? 24.510 16.685 1.828   1.00 50.22 ? 128 GLN A OE1 1 
ATOM   995  N NE2 . GLN A 1 128 ? 26.171 17.842 2.811   1.00 47.89 ? 128 GLN A NE2 1 
ATOM   996  N N   . ALA A 1 129 ? 21.307 21.146 2.931   1.00 24.26 ? 129 ALA A N   1 
ATOM   997  C CA  . ALA A 1 129 ? 20.171 21.761 2.252   1.00 25.05 ? 129 ALA A CA  1 
ATOM   998  C C   . ALA A 1 129 ? 20.634 22.661 1.114   1.00 28.47 ? 129 ALA A C   1 
ATOM   999  O O   . ALA A 1 129 ? 19.995 22.718 0.055   1.00 25.60 ? 129 ALA A O   1 
ATOM   1000 C CB  . ALA A 1 129 ? 19.322 22.547 3.250   1.00 26.76 ? 129 ALA A CB  1 
ATOM   1001 N N   . ILE A 1 130 ? 21.744 23.374 1.315   1.00 24.00 ? 130 ILE A N   1 
ATOM   1002 C CA  . ILE A 1 130 ? 22.271 24.237 0.263   1.00 22.76 ? 130 ILE A CA  1 
ATOM   1003 C C   . ILE A 1 130 ? 22.865 23.400 -0.865  1.00 25.61 ? 130 ILE A C   1 
ATOM   1004 O O   . ILE A 1 130 ? 22.691 23.717 -2.048  1.00 23.20 ? 130 ILE A O   1 
ATOM   1005 C CB  . ILE A 1 130 ? 23.296 25.216 0.860   1.00 24.18 ? 130 ILE A CB  1 
ATOM   1006 C CG1 . ILE A 1 130 ? 22.575 26.217 1.769   1.00 21.01 ? 130 ILE A CG1 1 
ATOM   1007 C CG2 . ILE A 1 130 ? 24.047 25.958 -0.249  1.00 20.73 ? 130 ILE A CG2 1 
ATOM   1008 C CD1 . ILE A 1 130 ? 23.518 27.062 2.587   1.00 29.16 ? 130 ILE A CD1 1 
ATOM   1009 N N   . VAL A 1 131 ? 23.567 22.314 -0.523  1.00 22.78 ? 131 VAL A N   1 
ATOM   1010 C CA  . VAL A 1 131 ? 24.075 21.394 -1.544  1.00 24.96 ? 131 VAL A CA  1 
ATOM   1011 C C   . VAL A 1 131 ? 22.932 20.873 -2.411  1.00 26.07 ? 131 VAL A C   1 
ATOM   1012 O O   . VAL A 1 131 ? 23.020 20.866 -3.645  1.00 24.72 ? 131 VAL A O   1 
ATOM   1013 C CB  . VAL A 1 131 ? 24.848 20.234 -0.890  1.00 29.94 ? 131 VAL A CB  1 
ATOM   1014 C CG1 . VAL A 1 131 ? 25.128 19.139 -1.914  1.00 31.15 ? 131 VAL A CG1 1 
ATOM   1015 C CG2 . VAL A 1 131 ? 26.156 20.733 -0.287  1.00 28.70 ? 131 VAL A CG2 1 
ATOM   1016 N N   . GLN A 1 132 ? 21.850 20.413 -1.775  1.00 24.48 ? 132 GLN A N   1 
ATOM   1017 C CA  . GLN A 1 132 ? 20.719 19.870 -2.526  1.00 26.50 ? 132 GLN A CA  1 
ATOM   1018 C C   . GLN A 1 132 ? 20.111 20.916 -3.451  1.00 26.10 ? 132 GLN A C   1 
ATOM   1019 O O   . GLN A 1 132 ? 19.709 20.603 -4.577  1.00 27.22 ? 132 GLN A O   1 
ATOM   1020 C CB  . GLN A 1 132 ? 19.652 19.335 -1.571  1.00 35.40 ? 132 GLN A CB  1 
ATOM   1021 C CG  . GLN A 1 132 ? 19.995 18.014 -0.913  1.00 49.08 ? 132 GLN A CG  1 
ATOM   1022 C CD  . GLN A 1 132 ? 18.903 17.539 0.023   1.00 65.03 ? 132 GLN A CD  1 
ATOM   1023 O OE1 . GLN A 1 132 ? 19.177 16.946 1.066   1.00 72.75 ? 132 GLN A OE1 1 
ATOM   1024 N NE2 . GLN A 1 132 ? 17.652 17.795 -0.350  1.00 67.74 ? 132 GLN A NE2 1 
ATOM   1025 N N   . SER A 1 133 ? 20.028 22.164 -2.984  1.00 23.41 ? 133 SER A N   1 
ATOM   1026 C CA  . SER A 1 133 ? 19.506 23.246 -3.812  1.00 27.10 ? 133 SER A CA  1 
ATOM   1027 C C   . SER A 1 133 ? 20.409 23.511 -5.012  1.00 28.41 ? 133 SER A C   1 
ATOM   1028 O O   . SER A 1 133 ? 19.927 23.712 -6.135  1.00 26.05 ? 133 SER A O   1 
ATOM   1029 C CB  . SER A 1 133 ? 19.349 24.511 -2.966  1.00 31.85 ? 133 SER A CB  1 
ATOM   1030 O OG  . SER A 1 133 ? 18.801 25.568 -3.733  1.00 29.00 ? 133 SER A OG  1 
ATOM   1031 N N   . ILE A 1 134 ? 21.725 23.537 -4.790  1.00 24.16 ? 134 ILE A N   1 
ATOM   1032 C CA  . ILE A 1 134 ? 22.664 23.756 -5.886  1.00 21.20 ? 134 ILE A CA  1 
ATOM   1033 C C   . ILE A 1 134 ? 22.570 22.619 -6.895  1.00 25.86 ? 134 ILE A C   1 
ATOM   1034 O O   . ILE A 1 134 ? 22.511 22.841 -8.110  1.00 29.36 ? 134 ILE A O   1 
ATOM   1035 C CB  . ILE A 1 134 ? 24.098 23.908 -5.346  1.00 23.06 ? 134 ILE A CB  1 
ATOM   1036 C CG1 . ILE A 1 134 ? 24.233 25.197 -4.536  1.00 19.39 ? 134 ILE A CG1 1 
ATOM   1037 C CG2 . ILE A 1 134 ? 25.114 23.901 -6.494  1.00 22.51 ? 134 ILE A CG2 1 
ATOM   1038 C CD1 . ILE A 1 134 ? 25.559 25.315 -3.798  1.00 26.94 ? 134 ILE A CD1 1 
ATOM   1039 N N   . GLU A 1 135 ? 22.540 21.381 -6.403  1.00 25.04 ? 135 GLU A N   1 
ATOM   1040 C CA  . GLU A 1 135 ? 22.525 20.243 -7.313  1.00 28.56 ? 135 GLU A CA  1 
ATOM   1041 C C   . GLU A 1 135 ? 21.206 20.149 -8.067  1.00 31.06 ? 135 GLU A C   1 
ATOM   1042 O O   . GLU A 1 135 ? 21.190 19.733 -9.231  1.00 30.05 ? 135 GLU A O   1 
ATOM   1043 C CB  . GLU A 1 135 ? 22.819 18.957 -6.539  1.00 29.20 ? 135 GLU A CB  1 
ATOM   1044 C CG  . GLU A 1 135 ? 24.247 18.938 -5.995  1.00 38.03 ? 135 GLU A CG  1 
ATOM   1045 C CD  . GLU A 1 135 ? 24.729 17.555 -5.614  1.00 49.69 ? 135 GLU A CD  1 
ATOM   1046 O OE1 . GLU A 1 135 ? 23.882 16.690 -5.315  1.00 48.70 ? 135 GLU A OE1 1 
ATOM   1047 O OE2 . GLU A 1 135 ? 25.961 17.335 -5.614  1.00 56.53 ? 135 GLU A OE2 1 
ATOM   1048 N N   . CYS A 1 136 ? 20.100 20.545 -7.437  1.00 27.27 ? 136 CYS A N   1 
ATOM   1049 C CA  . CYS A 1 136 ? 18.832 20.598 -8.155  1.00 27.35 ? 136 CYS A CA  1 
ATOM   1050 C C   . CYS A 1 136 ? 18.870 21.674 -9.232  1.00 26.55 ? 136 CYS A C   1 
ATOM   1051 O O   . CYS A 1 136 ? 18.488 21.431 -10.380 1.00 28.92 ? 136 CYS A O   1 
ATOM   1052 C CB  . CYS A 1 136 ? 17.686 20.847 -7.175  1.00 34.48 ? 136 CYS A CB  1 
ATOM   1053 S SG  . CYS A 1 136 ? 16.059 20.995 -7.953  1.00 37.35 ? 136 CYS A SG  1 
ATOM   1054 N N   . GLY A 1 137 ? 19.354 22.870 -8.882  1.00 26.78 ? 137 GLY A N   1 
ATOM   1055 C CA  . GLY A 1 137 ? 19.463 23.928 -9.873  1.00 23.31 ? 137 GLY A CA  1 
ATOM   1056 C C   . GLY A 1 137 ? 20.375 23.558 -11.028 1.00 27.36 ? 137 GLY A C   1 
ATOM   1057 O O   . GLY A 1 137 ? 20.113 23.915 -12.180 1.00 29.65 ? 137 GLY A O   1 
ATOM   1058 N N   . GLN A 1 138 ? 21.457 22.834 -10.738 1.00 26.25 ? 138 GLN A N   1 
ATOM   1059 C CA  . GLN A 1 138 ? 22.354 22.389 -11.799 1.00 29.70 ? 138 GLN A CA  1 
ATOM   1060 C C   . GLN A 1 138 ? 21.680 21.331 -12.669 1.00 28.88 ? 138 GLN A C   1 
ATOM   1061 O O   . GLN A 1 138 ? 21.742 21.393 -13.902 1.00 33.48 ? 138 GLN A O   1 
ATOM   1062 C CB  . GLN A 1 138 ? 23.651 21.858 -11.185 1.00 33.33 ? 138 GLN A CB  1 
ATOM   1063 C CG  . GLN A 1 138 ? 24.527 22.944 -10.564 1.00 33.88 ? 138 GLN A CG  1 
ATOM   1064 C CD  . GLN A 1 138 ? 25.777 22.392 -9.902  1.00 38.35 ? 138 GLN A CD  1 
ATOM   1065 O OE1 . GLN A 1 138 ? 25.779 21.273 -9.387  1.00 35.69 ? 138 GLN A OE1 1 
ATOM   1066 N NE2 . GLN A 1 138 ? 26.840 23.187 -9.888  1.00 35.91 ? 138 GLN A NE2 1 
ATOM   1067 N N   . LYS A 1 139 ? 21.019 20.358 -12.042 1.00 26.76 ? 139 LYS A N   1 
ATOM   1068 C CA  . LYS A 1 139 ? 20.348 19.314 -12.814 1.00 30.13 ? 139 LYS A CA  1 
ATOM   1069 C C   . LYS A 1 139 ? 19.199 19.877 -13.643 1.00 33.28 ? 139 LYS A C   1 
ATOM   1070 O O   . LYS A 1 139 ? 18.852 19.314 -14.689 1.00 34.77 ? 139 LYS A O   1 
ATOM   1071 C CB  . LYS A 1 139 ? 19.841 18.215 -11.881 1.00 31.84 ? 139 LYS A CB  1 
ATOM   1072 C CG  . LYS A 1 139 ? 19.510 16.917 -12.597 1.00 34.84 ? 139 LYS A CG  1 
ATOM   1073 C CD  . LYS A 1 139 ? 19.520 15.730 -11.649 1.00 43.90 ? 139 LYS A CD  1 
ATOM   1074 C CE  . LYS A 1 139 ? 18.616 14.612 -12.157 1.00 39.82 ? 139 LYS A CE  1 
ATOM   1075 N NZ  . LYS A 1 139 ? 17.490 14.347 -11.215 1.00 56.49 ? 139 LYS A NZ  1 
ATOM   1076 N N   . GLU A 1 140 ? 18.603 20.983 -13.205 1.00 32.10 ? 140 GLU A N   1 
ATOM   1077 C CA  . GLU A 1 140 ? 17.486 21.584 -13.921 1.00 32.93 ? 140 GLU A CA  1 
ATOM   1078 C C   . GLU A 1 140 ? 17.925 22.603 -14.961 1.00 34.40 ? 140 GLU A C   1 
ATOM   1079 O O   . GLU A 1 140 ? 17.070 23.181 -15.639 1.00 33.78 ? 140 GLU A O   1 
ATOM   1080 C CB  . GLU A 1 140 ? 16.509 22.226 -12.928 1.00 36.46 ? 140 GLU A CB  1 
ATOM   1081 C CG  . GLU A 1 140 ? 15.838 21.208 -12.014 1.00 37.64 ? 140 GLU A CG  1 
ATOM   1082 C CD  . GLU A 1 140 ? 14.597 21.747 -11.323 1.00 51.20 ? 140 GLU A CD  1 
ATOM   1083 O OE1 . GLU A 1 140 ? 14.391 22.978 -11.336 1.00 55.12 ? 140 GLU A OE1 1 
ATOM   1084 O OE2 . GLU A 1 140 ? 13.829 20.932 -10.766 1.00 45.39 ? 140 GLU A OE2 1 
ATOM   1085 N N   . GLY A 1 141 ? 19.229 22.819 -15.119 1.00 29.18 ? 141 GLY A N   1 
ATOM   1086 C CA  . GLY A 1 141 ? 19.742 23.699 -16.145 1.00 30.28 ? 141 GLY A CA  1 
ATOM   1087 C C   . GLY A 1 141 ? 19.805 25.157 -15.763 1.00 35.27 ? 141 GLY A C   1 
ATOM   1088 O O   . GLY A 1 141 ? 20.181 25.985 -16.604 1.00 41.29 ? 141 GLY A O   1 
ATOM   1089 N N   . GLU A 1 142 ? 19.463 25.497 -14.523 1.00 35.21 ? 142 GLU A N   1 
ATOM   1090 C CA  . GLU A 1 142 ? 19.439 26.882 -14.073 1.00 34.50 ? 142 GLU A CA  1 
ATOM   1091 C C   . GLU A 1 142 ? 20.805 27.354 -13.571 1.00 38.32 ? 142 GLU A C   1 
ATOM   1092 O O   . GLU A 1 142 ? 21.194 28.501 -13.819 1.00 32.49 ? 142 GLU A O   1 
ATOM   1093 C CB  . GLU A 1 142 ? 18.377 27.040 -12.981 1.00 34.10 ? 142 GLU A CB  1 
ATOM   1094 C CG  . GLU A 1 142 ? 18.542 28.260 -12.109 1.00 36.02 ? 142 GLU A CG  1 
ATOM   1095 C CD  . GLU A 1 142 ? 17.594 28.257 -10.931 1.00 40.07 ? 142 GLU A CD  1 
ATOM   1096 O OE1 . GLU A 1 142 ? 16.965 27.208 -10.669 1.00 44.12 ? 142 GLU A OE1 1 
ATOM   1097 O OE2 . GLU A 1 142 ? 17.462 29.313 -10.278 1.00 39.98 ? 142 GLU A OE2 1 
ATOM   1098 N N   . PHE A 1 143 ? 21.547 26.489 -12.886 1.00 30.25 ? 143 PHE A N   1 
ATOM   1099 C CA  . PHE A 1 143 ? 22.863 26.822 -12.360 1.00 33.08 ? 143 PHE A CA  1 
ATOM   1100 C C   . PHE A 1 143 ? 23.957 26.215 -13.227 1.00 38.30 ? 143 PHE A C   1 
ATOM   1101 O O   . PHE A 1 143 ? 23.772 25.160 -13.840 1.00 33.95 ? 143 PHE A O   1 
ATOM   1102 C CB  . PHE A 1 143 ? 23.029 26.316 -10.927 1.00 28.60 ? 143 PHE A CB  1 
ATOM   1103 C CG  . PHE A 1 143 ? 22.161 27.016 -9.923  1.00 26.80 ? 143 PHE A CG  1 
ATOM   1104 C CD1 . PHE A 1 143 ? 21.695 28.299 -10.157 1.00 29.02 ? 143 PHE A CD1 1 
ATOM   1105 C CD2 . PHE A 1 143 ? 21.828 26.394 -8.733  1.00 24.10 ? 143 PHE A CD2 1 
ATOM   1106 C CE1 . PHE A 1 143 ? 20.904 28.944 -9.221  1.00 32.98 ? 143 PHE A CE1 1 
ATOM   1107 C CE2 . PHE A 1 143 ? 21.038 27.032 -7.790  1.00 24.92 ? 143 PHE A CE2 1 
ATOM   1108 C CZ  . PHE A 1 143 ? 20.572 28.307 -8.036  1.00 29.50 ? 143 PHE A CZ  1 
ATOM   1109 N N   . LYS A 1 144 ? 25.110 26.879 -13.247 1.00 36.38 ? 144 LYS A N   1 
ATOM   1110 C CA  . LYS A 1 144 ? 26.294 26.377 -13.927 1.00 38.44 ? 144 LYS A CA  1 
ATOM   1111 C C   . LYS A 1 144 ? 27.067 25.418 -13.025 1.00 41.76 ? 144 LYS A C   1 
ATOM   1112 O O   . LYS A 1 144 ? 26.794 25.285 -11.830 1.00 40.19 ? 144 LYS A O   1 
ATOM   1113 C CB  . LYS A 1 144 ? 27.197 27.530 -14.363 1.00 38.83 ? 144 LYS A CB  1 
ATOM   1114 C CG  . LYS A 1 144 ? 26.734 28.233 -15.623 1.00 52.80 ? 144 LYS A CG  1 
ATOM   1115 C CD  . LYS A 1 144 ? 25.732 29.329 -15.312 1.00 52.85 ? 144 LYS A CD  1 
ATOM   1116 C CE  . LYS A 1 144 ? 25.747 30.399 -16.391 1.00 62.17 ? 144 LYS A CE  1 
ATOM   1117 N NZ  . LYS A 1 144 ? 25.810 29.794 -17.750 1.00 63.84 ? 144 LYS A NZ  1 
ATOM   1118 N N   . ASN A 1 145 ? 28.059 24.757 -13.617 1.00 43.74 ? 145 ASN A N   1 
ATOM   1119 C CA  . ASN A 1 145 ? 28.863 23.744 -12.946 1.00 47.73 ? 145 ASN A CA  1 
ATOM   1120 C C   . ASN A 1 145 ? 30.323 24.174 -12.842 1.00 49.48 ? 145 ASN A C   1 
ATOM   1121 O O   . ASN A 1 145 ? 31.237 23.382 -13.078 1.00 58.88 ? 145 ASN A O   1 
ATOM   1122 C CB  . ASN A 1 145 ? 28.753 22.407 -13.674 1.00 49.00 ? 145 ASN A CB  1 
ATOM   1123 C CG  . ASN A 1 145 ? 27.366 21.807 -13.581 1.00 63.67 ? 145 ASN A CG  1 
ATOM   1124 O OD1 . ASN A 1 145 ? 26.511 22.054 -14.435 1.00 64.14 ? 145 ASN A OD1 1 
ATOM   1125 N ND2 . ASN A 1 145 ? 27.133 21.010 -12.543 1.00 67.15 ? 145 ASN A ND2 1 
ATOM   1126 N N   . ARG A 1 146 ? 30.555 25.442 -12.487 1.00 49.62 ? 146 ARG A N   1 
ATOM   1127 C CA  . ARG A 1 146 ? 31.915 25.963 -12.355 1.00 55.46 ? 146 ARG A CA  1 
ATOM   1128 C C   . ARG A 1 146 ? 32.723 25.154 -11.347 1.00 51.82 ? 146 ARG A C   1 
ATOM   1129 O O   . ARG A 1 146 ? 33.769 24.585 -11.676 1.00 59.46 ? 146 ARG A O   1 
ATOM   1130 C CB  . ARG A 1 146 ? 31.871 27.432 -11.931 1.00 49.03 ? 146 ARG A CB  1 
ATOM   1131 C CG  . ARG A 1 146 ? 32.163 28.418 -13.034 1.00 59.80 ? 146 ARG A CG  1 
ATOM   1132 C CD  . ARG A 1 146 ? 31.653 29.795 -12.649 1.00 53.02 ? 146 ARG A CD  1 
ATOM   1133 N NE  . ARG A 1 146 ? 30.905 30.413 -13.734 1.00 53.69 ? 146 ARG A NE  1 
ATOM   1134 C CZ  . ARG A 1 146 ? 29.708 30.963 -13.592 1.00 55.15 ? 146 ARG A CZ  1 
ATOM   1135 N NH1 . ARG A 1 146 ? 29.099 30.998 -12.417 1.00 46.12 ? 146 ARG A NH1 1 
ATOM   1136 N NH2 . ARG A 1 146 ? 29.104 31.486 -14.655 1.00 61.65 ? 146 ARG A NH2 1 
ATOM   1137 N N   . SER A 1 147 ? 32.255 25.112 -10.105 1.00 45.55 ? 147 SER A N   1 
ATOM   1138 C CA  . SER A 1 147 ? 32.883 24.354 -9.038  1.00 48.97 ? 147 SER A CA  1 
ATOM   1139 C C   . SER A 1 147 ? 31.891 23.329 -8.509  1.00 50.89 ? 147 SER A C   1 
ATOM   1140 O O   . SER A 1 147 ? 30.692 23.382 -8.801  1.00 45.48 ? 147 SER A O   1 
ATOM   1141 C CB  . SER A 1 147 ? 33.358 25.275 -7.908  1.00 47.52 ? 147 SER A CB  1 
ATOM   1142 O OG  . SER A 1 147 ? 33.203 26.639 -8.265  1.00 45.30 ? 147 SER A OG  1 
ATOM   1143 N N   . ASN A 1 148 ? 32.398 22.385 -7.723  1.00 44.57 ? 148 ASN A N   1 
ATOM   1144 C CA  . ASN A 1 148 ? 31.526 21.351 -7.190  1.00 45.81 ? 148 ASN A CA  1 
ATOM   1145 C C   . ASN A 1 148 ? 30.631 21.931 -6.098  1.00 39.90 ? 148 ASN A C   1 
ATOM   1146 O O   . ASN A 1 148 ? 30.953 22.941 -5.463  1.00 35.44 ? 148 ASN A O   1 
ATOM   1147 C CB  . ASN A 1 148 ? 32.350 20.157 -6.687  1.00 50.02 ? 148 ASN A CB  1 
ATOM   1148 C CG  . ASN A 1 148 ? 33.040 20.415 -5.358  1.00 50.60 ? 148 ASN A CG  1 
ATOM   1149 O OD1 . ASN A 1 148 ? 32.399 20.679 -4.340  1.00 49.84 ? 148 ASN A OD1 1 
ATOM   1150 N ND2 . ASN A 1 148 ? 34.367 20.341 -5.365  1.00 58.79 ? 148 ASN A ND2 1 
ATOM   1151 N N   . SER A 1 149 ? 29.489 21.276 -5.892  1.00 39.46 ? 149 SER A N   1 
ATOM   1152 C CA  . SER A 1 149 ? 28.433 21.841 -5.060  1.00 32.76 ? 149 SER A CA  1 
ATOM   1153 C C   . SER A 1 149 ? 28.808 21.883 -3.584  1.00 29.89 ? 149 SER A C   1 
ATOM   1154 O O   . SER A 1 149 ? 28.315 22.747 -2.850  1.00 27.93 ? 149 SER A O   1 
ATOM   1155 C CB  . SER A 1 149 ? 27.150 21.041 -5.258  1.00 34.02 ? 149 SER A CB  1 
ATOM   1156 O OG  . SER A 1 149 ? 27.341 19.704 -4.834  1.00 34.68 ? 149 SER A OG  1 
ATOM   1157 N N   . THR A 1 150 ? 29.647 20.956 -3.117  1.00 29.82 ? 150 THR A N   1 
ATOM   1158 C CA  . THR A 1 150 ? 30.052 20.992 -1.714  1.00 31.47 ? 150 THR A CA  1 
ATOM   1159 C C   . THR A 1 150 ? 30.916 22.213 -1.430  1.00 29.85 ? 150 THR A C   1 
ATOM   1160 O O   . THR A 1 150 ? 30.759 22.866 -0.389  1.00 27.85 ? 150 THR A O   1 
ATOM   1161 C CB  . THR A 1 150 ? 30.793 19.705 -1.344  1.00 35.02 ? 150 THR A CB  1 
ATOM   1162 O OG1 . THR A 1 150 ? 29.881 18.605 -1.390  1.00 39.49 ? 150 THR A OG1 1 
ATOM   1163 C CG2 . THR A 1 150 ? 31.382 19.798 0.061   1.00 33.62 ? 150 THR A CG2 1 
ATOM   1164 N N   . ASP A 1 151 ? 31.822 22.546 -2.356  1.00 27.09 ? 151 ASP A N   1 
ATOM   1165 C CA  . ASP A 1 151 ? 32.681 23.713 -2.183  1.00 28.31 ? 151 ASP A CA  1 
ATOM   1166 C C   . ASP A 1 151 ? 31.861 24.994 -2.179  1.00 25.85 ? 151 ASP A C   1 
ATOM   1167 O O   . ASP A 1 151 ? 32.068 25.878 -1.339  1.00 21.94 ? 151 ASP A O   1 
ATOM   1168 C CB  . ASP A 1 151 ? 33.726 23.772 -3.300  1.00 31.18 ? 151 ASP A CB  1 
ATOM   1169 C CG  . ASP A 1 151 ? 34.901 22.845 -3.061  1.00 39.20 ? 151 ASP A CG  1 
ATOM   1170 O OD1 . ASP A 1 151 ? 35.134 22.449 -1.898  1.00 34.18 ? 151 ASP A OD1 1 
ATOM   1171 O OD2 . ASP A 1 151 ? 35.607 22.530 -4.045  1.00 39.68 ? 151 ASP A OD2 1 
ATOM   1172 N N   . ILE A 1 152 ? 30.936 25.122 -3.133  1.00 24.11 ? 152 ILE A N   1 
ATOM   1173 C CA  . ILE A 1 152 ? 30.132 26.335 -3.238  1.00 26.92 ? 152 ILE A CA  1 
ATOM   1174 C C   . ILE A 1 152 ? 29.272 26.512 -1.997  1.00 21.38 ? 152 ILE A C   1 
ATOM   1175 O O   . ILE A 1 152 ? 29.118 27.626 -1.484  1.00 18.59 ? 152 ILE A O   1 
ATOM   1176 C CB  . ILE A 1 152 ? 29.270 26.299 -4.515  1.00 25.65 ? 152 ILE A CB  1 
ATOM   1177 C CG1 . ILE A 1 152 ? 30.161 26.207 -5.758  1.00 26.06 ? 152 ILE A CG1 1 
ATOM   1178 C CG2 . ILE A 1 152 ? 28.365 27.528 -4.579  1.00 21.99 ? 152 ILE A CG2 1 
ATOM   1179 C CD1 . ILE A 1 152 ? 29.393 25.894 -7.042  1.00 31.55 ? 152 ILE A CD1 1 
ATOM   1180 N N   . ALA A 1 153 ? 28.695 25.418 -1.497  1.00 20.77 ? 153 ALA A N   1 
ATOM   1181 C CA  . ALA A 1 153 ? 27.834 25.509 -0.325  1.00 24.19 ? 153 ALA A CA  1 
ATOM   1182 C C   . ALA A 1 153 ? 28.597 26.023 0.891   1.00 23.63 ? 153 ALA A C   1 
ATOM   1183 O O   . ALA A 1 153 ? 28.094 26.877 1.630   1.00 20.68 ? 153 ALA A O   1 
ATOM   1184 C CB  . ALA A 1 153 ? 27.210 24.149 -0.028  1.00 21.64 ? 153 ALA A CB  1 
ATOM   1185 N N   . TRP A 1 154 ? 29.807 25.509 1.129   1.00 22.32 ? 154 TRP A N   1 
ATOM   1186 C CA  . TRP A 1 154 ? 30.579 26.014 2.261   1.00 26.22 ? 154 TRP A CA  1 
ATOM   1187 C C   . TRP A 1 154 ? 30.955 27.477 2.056   1.00 20.61 ? 154 TRP A C   1 
ATOM   1188 O O   . TRP A 1 154 ? 30.911 28.275 3.001   1.00 22.46 ? 154 TRP A O   1 
ATOM   1189 C CB  . TRP A 1 154 ? 31.830 25.159 2.497   1.00 25.74 ? 154 TRP A CB  1 
ATOM   1190 C CG  . TRP A 1 154 ? 31.566 23.847 3.214   1.00 23.59 ? 154 TRP A CG  1 
ATOM   1191 C CD1 . TRP A 1 154 ? 31.919 22.599 2.792   1.00 32.06 ? 154 TRP A CD1 1 
ATOM   1192 C CD2 . TRP A 1 154 ? 30.888 23.669 4.468   1.00 25.82 ? 154 TRP A CD2 1 
ATOM   1193 N NE1 . TRP A 1 154 ? 31.507 21.655 3.706   1.00 29.16 ? 154 TRP A NE1 1 
ATOM   1194 C CE2 . TRP A 1 154 ? 30.872 22.285 4.743   1.00 26.33 ? 154 TRP A CE2 1 
ATOM   1195 C CE3 . TRP A 1 154 ? 30.293 24.544 5.384   1.00 26.75 ? 154 TRP A CE3 1 
ATOM   1196 C CZ2 . TRP A 1 154 ? 30.285 21.756 5.890   1.00 31.02 ? 154 TRP A CZ2 1 
ATOM   1197 C CZ3 . TRP A 1 154 ? 29.710 24.014 6.527   1.00 28.31 ? 154 TRP A CZ3 1 
ATOM   1198 C CH2 . TRP A 1 154 ? 29.709 22.633 6.767   1.00 29.49 ? 154 TRP A CH2 1 
ATOM   1199 N N   . ARG A 1 155 ? 31.302 27.855 0.825   1.00 19.40 ? 155 ARG A N   1 
ATOM   1200 C CA  . ARG A 1 155 ? 31.652 29.248 0.558   1.00 19.19 ? 155 ARG A CA  1 
ATOM   1201 C C   . ARG A 1 155 ? 30.461 30.177 0.774   1.00 22.90 ? 155 ARG A C   1 
ATOM   1202 O O   . ARG A 1 155 ? 30.618 31.289 1.291   1.00 21.80 ? 155 ARG A O   1 
ATOM   1203 C CB  . ARG A 1 155 ? 32.194 29.378 -0.864  1.00 25.75 ? 155 ARG A CB  1 
ATOM   1204 C CG  . ARG A 1 155 ? 33.564 28.730 -1.050  1.00 24.99 ? 155 ARG A CG  1 
ATOM   1205 C CD  . ARG A 1 155 ? 34.359 29.422 -2.140  1.00 24.02 ? 155 ARG A CD  1 
ATOM   1206 N NE  . ARG A 1 155 ? 33.864 29.099 -3.473  1.00 26.72 ? 155 ARG A NE  1 
ATOM   1207 C CZ  . ARG A 1 155 ? 34.345 28.132 -4.244  1.00 35.00 ? 155 ARG A CZ  1 
ATOM   1208 N NH1 . ARG A 1 155 ? 35.321 27.338 -3.833  1.00 28.65 ? 155 ARG A NH1 1 
ATOM   1209 N NH2 . ARG A 1 155 ? 33.839 27.963 -5.465  1.00 32.44 ? 155 ARG A NH2 1 
ATOM   1210 N N   . LEU A 1 156 ? 29.263 29.747 0.370   1.00 21.34 ? 156 LEU A N   1 
ATOM   1211 C CA  . LEU A 1 156 ? 28.066 30.554 0.593   1.00 18.78 ? 156 LEU A CA  1 
ATOM   1212 C C   . LEU A 1 156 ? 27.781 30.707 2.083   1.00 22.99 ? 156 LEU A C   1 
ATOM   1213 O O   . LEU A 1 156 ? 27.496 31.810 2.564   1.00 19.04 ? 156 LEU A O   1 
ATOM   1214 C CB  . LEU A 1 156 ? 26.871 29.920 -0.124  1.00 20.15 ? 156 LEU A CB  1 
ATOM   1215 C CG  . LEU A 1 156 ? 26.895 29.988 -1.653  1.00 21.40 ? 156 LEU A CG  1 
ATOM   1216 C CD1 . LEU A 1 156 ? 25.646 29.338 -2.264  1.00 21.82 ? 156 LEU A CD1 1 
ATOM   1217 C CD2 . LEU A 1 156 ? 27.034 31.434 -2.119  1.00 21.91 ? 156 LEU A CD2 1 
ATOM   1218 N N   . ILE A 1 157 ? 27.861 29.605 2.833   1.00 17.59 ? 157 ILE A N   1 
ATOM   1219 C CA  . ILE A 1 157 ? 27.650 29.679 4.276   1.00 19.66 ? 157 ILE A CA  1 
ATOM   1220 C C   . ILE A 1 157 ? 28.689 30.583 4.917   1.00 20.09 ? 157 ILE A C   1 
ATOM   1221 O O   . ILE A 1 157 ? 28.364 31.428 5.762   1.00 22.74 ? 157 ILE A O   1 
ATOM   1222 C CB  . ILE A 1 157 ? 27.670 28.270 4.895   1.00 20.12 ? 157 ILE A CB  1 
ATOM   1223 C CG1 . ILE A 1 157 ? 26.333 27.574 4.661   1.00 21.23 ? 157 ILE A CG1 1 
ATOM   1224 C CG2 . ILE A 1 157 ? 27.983 28.344 6.386   1.00 24.71 ? 157 ILE A CG2 1 
ATOM   1225 C CD1 . ILE A 1 157 ? 26.366 26.089 4.971   1.00 28.47 ? 157 ILE A CD1 1 
ATOM   1226 N N   . ALA A 1 158 ? 29.953 30.430 4.522   1.00 18.12 ? 158 ALA A N   1 
ATOM   1227 C CA  . ALA A 1 158 ? 31.002 31.274 5.080   1.00 20.13 ? 158 ALA A CA  1 
ATOM   1228 C C   . ALA A 1 158 ? 30.714 32.743 4.809   1.00 20.61 ? 158 ALA A C   1 
ATOM   1229 O O   . ALA A 1 158 ? 30.887 33.594 5.691   1.00 21.03 ? 158 ALA A O   1 
ATOM   1230 C CB  . ALA A 1 158 ? 32.361 30.874 4.499   1.00 21.80 ? 158 ALA A CB  1 
ATOM   1231 N N   . PHE A 1 159 ? 30.242 33.056 3.604   1.00 18.46 ? 159 PHE A N   1 
ATOM   1232 C CA  . PHE A 1 159 ? 29.975 34.449 3.265   1.00 20.83 ? 159 PHE A CA  1 
ATOM   1233 C C   . PHE A 1 159 ? 28.904 35.051 4.163   1.00 20.08 ? 159 PHE A C   1 
ATOM   1234 O O   . PHE A 1 159 ? 29.107 36.120 4.750   1.00 21.69 ? 159 PHE A O   1 
ATOM   1235 C CB  . PHE A 1 159 ? 29.560 34.590 1.805   1.00 21.27 ? 159 PHE A CB  1 
ATOM   1236 C CG  . PHE A 1 159 ? 29.281 36.007 1.425   1.00 23.93 ? 159 PHE A CG  1 
ATOM   1237 C CD1 . PHE A 1 159 ? 30.327 36.897 1.224   1.00 26.92 ? 159 PHE A CD1 1 
ATOM   1238 C CD2 . PHE A 1 159 ? 27.981 36.467 1.323   1.00 22.82 ? 159 PHE A CD2 1 
ATOM   1239 C CE1 . PHE A 1 159 ? 30.074 38.222 0.897   1.00 29.13 ? 159 PHE A CE1 1 
ATOM   1240 C CE2 . PHE A 1 159 ? 27.721 37.787 0.995   1.00 26.36 ? 159 PHE A CE2 1 
ATOM   1241 C CZ  . PHE A 1 159 ? 28.769 38.664 0.781   1.00 28.96 ? 159 PHE A CZ  1 
ATOM   1242 N N   . VAL A 1 160 ? 27.738 34.404 4.252   1.00 21.71 ? 160 VAL A N   1 
ATOM   1243 C CA  . VAL A 1 160 ? 26.639 35.017 4.992   1.00 19.27 ? 160 VAL A CA  1 
ATOM   1244 C C   . VAL A 1 160 ? 26.948 35.058 6.483   1.00 20.25 ? 160 VAL A C   1 
ATOM   1245 O O   . VAL A 1 160 ? 26.602 36.026 7.167   1.00 20.63 ? 160 VAL A O   1 
ATOM   1246 C CB  . VAL A 1 160 ? 25.295 34.318 4.691   1.00 22.62 ? 160 VAL A CB  1 
ATOM   1247 C CG1 . VAL A 1 160 ? 24.994 34.359 3.195   1.00 26.49 ? 160 VAL A CG1 1 
ATOM   1248 C CG2 . VAL A 1 160 ? 25.303 32.873 5.173   1.00 21.55 ? 160 VAL A CG2 1 
ATOM   1249 N N   . CYS A 1 161 ? 27.623 34.035 7.012   1.00 20.18 ? 161 CYS A N   1 
ATOM   1250 C CA  . CYS A 1 161 ? 28.030 34.093 8.414   1.00 21.72 ? 161 CYS A CA  1 
ATOM   1251 C C   . CYS A 1 161 ? 29.051 35.198 8.645   1.00 18.80 ? 161 CYS A C   1 
ATOM   1252 O O   . CYS A 1 161 ? 28.973 35.925 9.641   1.00 21.39 ? 161 CYS A O   1 
ATOM   1253 C CB  . CYS A 1 161 ? 28.594 32.748 8.867   1.00 21.17 ? 161 CYS A CB  1 
ATOM   1254 S SG  . CYS A 1 161 ? 27.387 31.406 8.922   1.00 27.64 ? 161 CYS A SG  1 
ATOM   1255 N N   . GLY A 1 162 ? 30.014 35.340 7.733   1.00 17.77 ? 162 GLY A N   1 
ATOM   1256 C CA  . GLY A 1 162 ? 30.998 36.400 7.870   1.00 20.15 ? 162 GLY A CA  1 
ATOM   1257 C C   . GLY A 1 162 ? 30.396 37.783 7.729   1.00 20.60 ? 162 GLY A C   1 
ATOM   1258 O O   . GLY A 1 162 ? 30.808 38.721 8.415   1.00 18.76 ? 162 GLY A O   1 
ATOM   1259 N N   . LEU A 1 163 ? 29.414 37.934 6.839   1.00 17.68 ? 163 LEU A N   1 
ATOM   1260 C CA  . LEU A 1 163 ? 28.797 39.246 6.662   1.00 19.67 ? 163 LEU A CA  1 
ATOM   1261 C C   . LEU A 1 163 ? 28.003 39.648 7.900   1.00 23.61 ? 163 LEU A C   1 
ATOM   1262 O O   . LEU A 1 163 ? 28.093 40.794 8.361   1.00 21.51 ? 163 LEU A O   1 
ATOM   1263 C CB  . LEU A 1 163 ? 27.913 39.241 5.412   1.00 22.51 ? 163 LEU A CB  1 
ATOM   1264 C CG  . LEU A 1 163 ? 27.449 40.598 4.884   1.00 33.55 ? 163 LEU A CG  1 
ATOM   1265 C CD1 . LEU A 1 163 ? 28.595 41.604 4.892   1.00 27.48 ? 163 LEU A CD1 1 
ATOM   1266 C CD2 . LEU A 1 163 ? 26.844 40.452 3.491   1.00 31.78 ? 163 LEU A CD2 1 
ATOM   1267 N N   . GLU A 1 164 ? 27.234 38.714 8.463   1.00 22.42 ? 164 GLU A N   1 
ATOM   1268 C CA  . GLU A 1 164 ? 26.538 38.980 9.720   1.00 26.41 ? 164 GLU A CA  1 
ATOM   1269 C C   . GLU A 1 164 ? 27.516 39.307 10.841  1.00 25.02 ? 164 GLU A C   1 
ATOM   1270 O O   . GLU A 1 164 ? 27.234 40.160 11.693  1.00 25.30 ? 164 GLU A O   1 
ATOM   1271 C CB  . GLU A 1 164 ? 25.687 37.775 10.113  1.00 29.42 ? 164 GLU A CB  1 
ATOM   1272 C CG  . GLU A 1 164 ? 24.691 37.338 9.065   1.00 44.77 ? 164 GLU A CG  1 
ATOM   1273 C CD  . GLU A 1 164 ? 24.192 35.929 9.322   1.00 59.36 ? 164 GLU A CD  1 
ATOM   1274 O OE1 . GLU A 1 164 ? 23.726 35.273 8.364   1.00 53.11 ? 164 GLU A OE1 1 
ATOM   1275 O OE2 . GLU A 1 164 ? 24.277 35.479 10.485  1.00 72.93 ? 164 GLU A OE2 1 
ATOM   1276 N N   . GLY A 1 165 ? 28.657 38.619 10.878  1.00 22.19 ? 165 GLY A N   1 
ATOM   1277 C CA  . GLY A 1 165 ? 29.652 38.918 11.898  1.00 20.94 ? 165 GLY A CA  1 
ATOM   1278 C C   . GLY A 1 165 ? 30.192 40.331 11.788  1.00 24.76 ? 165 GLY A C   1 
ATOM   1279 O O   . GLY A 1 165 ? 30.443 40.993 12.799  1.00 27.54 ? 165 GLY A O   1 
ATOM   1280 N N   . ILE A 1 166 ? 30.374 40.815 10.560  1.00 21.78 ? 166 ILE A N   1 
ATOM   1281 C CA  . ILE A 1 166 ? 30.885 42.165 10.355  1.00 23.05 ? 166 ILE A CA  1 
ATOM   1282 C C   . ILE A 1 166 ? 29.842 43.195 10.773  1.00 28.41 ? 166 ILE A C   1 
ATOM   1283 O O   . ILE A 1 166 ? 30.174 44.245 11.340  1.00 22.39 ? 166 ILE A O   1 
ATOM   1284 C CB  . ILE A 1 166 ? 31.311 42.347 8.887   1.00 27.66 ? 166 ILE A CB  1 
ATOM   1285 C CG1 . ILE A 1 166 ? 32.547 41.502 8.580   1.00 35.96 ? 166 ILE A CG1 1 
ATOM   1286 C CG2 . ILE A 1 166 ? 31.664 43.779 8.616   1.00 36.47 ? 166 ILE A CG2 1 
ATOM   1287 C CD1 . ILE A 1 166 ? 33.720 41.802 9.474   1.00 36.69 ? 166 ILE A CD1 1 
ATOM   1288 N N   . TYR A 1 167 ? 28.563 42.914 10.494  1.00 23.43 ? 167 TYR A N   1 
ATOM   1289 C CA  . TYR A 1 167 ? 27.490 43.806 10.929  1.00 27.33 ? 167 TYR A CA  1 
ATOM   1290 C C   . TYR A 1 167 ? 27.446 43.939 12.442  1.00 25.12 ? 167 TYR A C   1 
ATOM   1291 O O   . TYR A 1 167 ? 27.118 45.013 12.960  1.00 28.52 ? 167 TYR A O   1 
ATOM   1292 C CB  . TYR A 1 167 ? 26.137 43.295 10.436  1.00 24.60 ? 167 TYR A CB  1 
ATOM   1293 C CG  . TYR A 1 167 ? 25.956 43.361 8.945   1.00 29.99 ? 167 TYR A CG  1 
ATOM   1294 C CD1 . TYR A 1 167 ? 26.632 44.300 8.183   1.00 35.10 ? 167 TYR A CD1 1 
ATOM   1295 C CD2 . TYR A 1 167 ? 25.110 42.474 8.295   1.00 33.52 ? 167 TYR A CD2 1 
ATOM   1296 C CE1 . TYR A 1 167 ? 26.465 44.359 6.820   1.00 37.05 ? 167 TYR A CE1 1 
ATOM   1297 C CE2 . TYR A 1 167 ? 24.938 42.524 6.936   1.00 28.47 ? 167 TYR A CE2 1 
ATOM   1298 C CZ  . TYR A 1 167 ? 25.615 43.467 6.202   1.00 33.04 ? 167 TYR A CZ  1 
ATOM   1299 O OH  . TYR A 1 167 ? 25.446 43.515 4.838   1.00 44.38 ? 167 TYR A OH  1 
ATOM   1300 N N   . LYS A 1 168 ? 27.757 42.860 13.165  1.00 21.95 ? 168 LYS A N   1 
ATOM   1301 C CA  . LYS A 1 168 ? 27.730 42.897 14.620  1.00 24.57 ? 168 LYS A CA  1 
ATOM   1302 C C   . LYS A 1 168 ? 28.745 43.871 15.201  1.00 25.81 ? 168 LYS A C   1 
ATOM   1303 O O   . LYS A 1 168 ? 28.608 44.264 16.365  1.00 26.36 ? 168 LYS A O   1 
ATOM   1304 C CB  . LYS A 1 168 ? 27.986 41.504 15.192  1.00 29.19 ? 168 LYS A CB  1 
ATOM   1305 C CG  . LYS A 1 168 ? 27.171 41.198 16.435  1.00 47.83 ? 168 LYS A CG  1 
ATOM   1306 C CD  . LYS A 1 168 ? 27.450 39.797 16.964  1.00 44.66 ? 168 LYS A CD  1 
ATOM   1307 C CE  . LYS A 1 168 ? 27.632 39.816 18.477  1.00 46.14 ? 168 LYS A CE  1 
ATOM   1308 N NZ  . LYS A 1 168 ? 27.176 38.546 19.118  1.00 51.21 ? 168 LYS A NZ  1 
ATOM   1309 N N   . LEU A 1 169 ? 29.754 44.270 14.427  1.00 23.41 ? 169 LEU A N   1 
ATOM   1310 C CA  . LEU A 1 169 ? 30.805 45.129 14.960  1.00 23.46 ? 169 LEU A CA  1 
ATOM   1311 C C   . LEU A 1 169 ? 30.369 46.577 15.108  1.00 27.40 ? 169 LEU A C   1 
ATOM   1312 O O   . LEU A 1 169 ? 30.958 47.305 15.916  1.00 28.15 ? 169 LEU A O   1 
ATOM   1313 C CB  . LEU A 1 169 ? 32.050 45.072 14.069  1.00 24.21 ? 169 LEU A CB  1 
ATOM   1314 C CG  . LEU A 1 169 ? 32.735 43.713 13.905  1.00 20.74 ? 169 LEU A CG  1 
ATOM   1315 C CD1 . LEU A 1 169 ? 33.861 43.816 12.885  1.00 23.71 ? 169 LEU A CD1 1 
ATOM   1316 C CD2 . LEU A 1 169 ? 33.264 43.196 15.224  1.00 21.82 ? 169 LEU A CD2 1 
ATOM   1317 N N   . GLY A 1 170 ? 29.365 47.013 14.350  1.00 27.32 ? 170 GLY A N   1 
ATOM   1318 C CA  . GLY A 1 170 ? 28.941 48.399 14.398  1.00 24.17 ? 170 GLY A CA  1 
ATOM   1319 C C   . GLY A 1 170 ? 29.950 49.321 13.748  1.00 30.14 ? 170 GLY A C   1 
ATOM   1320 O O   . GLY A 1 170 ? 30.302 50.368 14.303  1.00 28.38 ? 170 GLY A O   1 
ATOM   1321 N N   . LEU A 1 171 ? 30.430 48.933 12.571  1.00 23.44 ? 171 LEU A N   1 
ATOM   1322 C CA  . LEU A 1 171 ? 31.372 49.741 11.817  1.00 30.64 ? 171 LEU A CA  1 
ATOM   1323 C C   . LEU A 1 171 ? 30.666 50.925 11.168  1.00 39.65 ? 171 LEU A C   1 
ATOM   1324 O O   . LEU A 1 171 ? 29.478 50.863 10.839  1.00 36.09 ? 171 LEU A O   1 
ATOM   1325 C CB  . LEU A 1 171 ? 32.055 48.897 10.741  1.00 31.17 ? 171 LEU A CB  1 
ATOM   1326 C CG  . LEU A 1 171 ? 32.908 47.742 11.264  1.00 32.09 ? 171 LEU A CG  1 
ATOM   1327 C CD1 . LEU A 1 171 ? 33.244 46.764 10.150  1.00 25.58 ? 171 LEU A CD1 1 
ATOM   1328 C CD2 . LEU A 1 171 ? 34.176 48.293 11.888  1.00 30.63 ? 171 LEU A CD2 1 
ATOM   1329 N N   . GLN A 1 172 ? 31.413 52.012 10.991  1.00 37.37 ? 172 GLN A N   1 
ATOM   1330 C CA  . GLN A 1 172 ? 30.890 53.196 10.326  1.00 39.74 ? 172 GLN A CA  1 
ATOM   1331 C C   . GLN A 1 172 ? 30.860 52.976 8.820   1.00 40.97 ? 172 GLN A C   1 
ATOM   1332 O O   . GLN A 1 172 ? 31.724 52.298 8.259   1.00 38.95 ? 172 GLN A O   1 
ATOM   1333 C CB  . GLN A 1 172 ? 31.750 54.419 10.654  1.00 43.38 ? 172 GLN A CB  1 
ATOM   1334 C CG  . GLN A 1 172 ? 31.885 54.722 12.139  1.00 46.70 ? 172 GLN A CG  1 
ATOM   1335 C CD  . GLN A 1 172 ? 30.555 55.011 12.809  1.00 49.70 ? 172 GLN A CD  1 
ATOM   1336 O OE1 . GLN A 1 172 ? 29.938 56.048 12.567  1.00 53.66 ? 172 GLN A OE1 1 
ATOM   1337 N NE2 . GLN A 1 172 ? 30.111 54.097 13.664  1.00 44.23 ? 172 GLN A NE2 1 
ATOM   1338 N N   . GLY A 1 173 ? 29.857 53.553 8.165   1.00 42.80 ? 173 GLY A N   1 
ATOM   1339 C CA  . GLY A 1 173 ? 29.781 53.475 6.719   1.00 32.59 ? 173 GLY A CA  1 
ATOM   1340 C C   . GLY A 1 173 ? 29.529 52.092 6.166   1.00 36.20 ? 173 GLY A C   1 
ATOM   1341 O O   . GLY A 1 173 ? 29.963 51.791 5.051   1.00 46.87 ? 173 GLY A O   1 
ATOM   1342 N N   . LEU A 1 174 ? 28.844 51.235 6.919   1.00 37.95 ? 174 LEU A N   1 
ATOM   1343 C CA  . LEU A 1 174 ? 28.458 49.908 6.452   1.00 36.28 ? 174 LEU A CA  1 
ATOM   1344 C C   . LEU A 1 174 ? 26.996 49.687 6.810   1.00 38.76 ? 174 LEU A C   1 
ATOM   1345 O O   . LEU A 1 174 ? 26.636 49.712 7.992   1.00 40.29 ? 174 LEU A O   1 
ATOM   1346 C CB  . LEU A 1 174 ? 29.333 48.822 7.078   1.00 33.10 ? 174 LEU A CB  1 
ATOM   1347 C CG  . LEU A 1 174 ? 28.994 47.391 6.663   1.00 42.17 ? 174 LEU A CG  1 
ATOM   1348 C CD1 . LEU A 1 174 ? 29.063 47.230 5.150   1.00 44.02 ? 174 LEU A CD1 1 
ATOM   1349 C CD2 . LEU A 1 174 ? 29.899 46.404 7.355   1.00 32.81 ? 174 LEU A CD2 1 
ATOM   1350 N N   . ALA A 1 175 ? 26.158 49.469 5.797   1.00 38.84 ? 175 ALA A N   1 
ATOM   1351 C CA  . ALA A 1 175 ? 24.711 49.407 5.973   1.00 35.85 ? 175 ALA A CA  1 
ATOM   1352 C C   . ALA A 1 175 ? 24.245 47.955 5.992   1.00 40.42 ? 175 ALA A C   1 
ATOM   1353 O O   . ALA A 1 175 ? 24.423 47.228 5.008   1.00 35.78 ? 175 ALA A O   1 
ATOM   1354 C CB  . ALA A 1 175 ? 23.998 50.181 4.865   1.00 41.12 ? 175 ALA A CB  1 
ATOM   1355 N N   . GLU A 1 176 ? 23.627 47.549 7.107   1.00 40.17 ? 176 GLU A N   1 
ATOM   1356 C CA  . GLU A 1 176 ? 23.049 46.211 7.209   1.00 36.42 ? 176 GLU A CA  1 
ATOM   1357 C C   . GLU A 1 176 ? 22.055 45.937 6.089   1.00 41.12 ? 176 GLU A C   1 
ATOM   1358 O O   . GLU A 1 176 ? 21.852 44.779 5.708   1.00 35.09 ? 176 GLU A O   1 
ATOM   1359 C CB  . GLU A 1 176 ? 22.345 46.047 8.555   1.00 41.85 ? 176 GLU A CB  1 
ATOM   1360 C CG  . GLU A 1 176 ? 23.243 46.161 9.762   1.00 38.77 ? 176 GLU A CG  1 
ATOM   1361 C CD  . GLU A 1 176 ? 22.656 45.473 10.974  1.00 40.32 ? 176 GLU A CD  1 
ATOM   1362 O OE1 . GLU A 1 176 ? 21.623 44.782 10.830  1.00 44.86 ? 176 GLU A OE1 1 
ATOM   1363 O OE2 . GLU A 1 176 ? 23.212 45.646 12.075  1.00 39.12 ? 176 GLU A OE2 1 
ATOM   1364 N N   . GLU A 1 177 ? 21.423 46.988 5.560   1.00 34.58 ? 177 GLU A N   1 
ATOM   1365 C CA  . GLU A 1 177 ? 20.399 46.836 4.532   1.00 40.22 ? 177 GLU A CA  1 
ATOM   1366 C C   . GLU A 1 177 ? 20.946 46.231 3.244   1.00 40.99 ? 177 GLU A C   1 
ATOM   1367 O O   . GLU A 1 177 ? 20.166 45.707 2.440   1.00 39.85 ? 177 GLU A O   1 
ATOM   1368 C CB  . GLU A 1 177 ? 19.764 48.197 4.233   1.00 45.65 ? 177 GLU A CB  1 
ATOM   1369 C CG  . GLU A 1 177 ? 18.712 48.653 5.240   1.00 56.53 ? 177 GLU A CG  1 
ATOM   1370 C CD  . GLU A 1 177 ? 19.232 48.688 6.668   1.00 65.24 ? 177 GLU A CD  1 
ATOM   1371 O OE1 . GLU A 1 177 ? 18.854 47.799 7.463   1.00 62.78 ? 177 GLU A OE1 1 
ATOM   1372 O OE2 . GLU A 1 177 ? 20.034 49.592 6.988   1.00 68.04 ? 177 GLU A OE2 1 
ATOM   1373 N N   . ASP A 1 178 ? 22.259 46.292 3.028   1.00 35.35 ? 178 ASP A N   1 
ATOM   1374 C CA  . ASP A 1 178 ? 22.886 45.772 1.817   1.00 32.64 ? 178 ASP A CA  1 
ATOM   1375 C C   . ASP A 1 178 ? 23.054 44.255 1.818   1.00 32.15 ? 178 ASP A C   1 
ATOM   1376 O O   . ASP A 1 178 ? 23.607 43.720 0.851   1.00 33.07 ? 178 ASP A O   1 
ATOM   1377 C CB  . ASP A 1 178 ? 24.262 46.417 1.620   1.00 34.52 ? 178 ASP A CB  1 
ATOM   1378 C CG  . ASP A 1 178 ? 24.176 47.848 1.133   1.00 42.67 ? 178 ASP A CG  1 
ATOM   1379 O OD1 . ASP A 1 178 ? 23.161 48.205 0.498   1.00 43.42 ? 178 ASP A OD1 1 
ATOM   1380 O OD2 . ASP A 1 178 ? 25.134 48.611 1.379   1.00 40.86 ? 178 ASP A OD2 1 
ATOM   1381 N N   . PHE A 1 179 ? 22.607 43.558 2.869   1.00 29.52 ? 179 PHE A N   1 
ATOM   1382 C CA  . PHE A 1 179 ? 22.861 42.122 2.982   1.00 29.65 ? 179 PHE A CA  1 
ATOM   1383 C C   . PHE A 1 179 ? 22.332 41.357 1.773   1.00 34.49 ? 179 PHE A C   1 
ATOM   1384 O O   . PHE A 1 179 ? 23.048 40.538 1.183   1.00 29.22 ? 179 PHE A O   1 
ATOM   1385 C CB  . PHE A 1 179 ? 22.251 41.580 4.278   1.00 27.21 ? 179 PHE A CB  1 
ATOM   1386 C CG  . PHE A 1 179 ? 22.495 40.108 4.492   1.00 29.39 ? 179 PHE A CG  1 
ATOM   1387 C CD1 . PHE A 1 179 ? 21.635 39.162 3.957   1.00 35.61 ? 179 PHE A CD1 1 
ATOM   1388 C CD2 . PHE A 1 179 ? 23.607 39.671 5.191   1.00 34.06 ? 179 PHE A CD2 1 
ATOM   1389 C CE1 . PHE A 1 179 ? 21.863 37.813 4.139   1.00 38.85 ? 179 PHE A CE1 1 
ATOM   1390 C CE2 . PHE A 1 179 ? 23.841 38.318 5.374   1.00 31.16 ? 179 PHE A CE2 1 
ATOM   1391 C CZ  . PHE A 1 179 ? 22.968 37.392 4.847   1.00 33.48 ? 179 PHE A CZ  1 
ATOM   1392 N N   . LYS A 1 180 ? 21.073 41.603 1.395   1.00 28.90 ? 180 LYS A N   1 
ATOM   1393 C CA  . LYS A 1 180 ? 20.493 40.917 0.244   1.00 32.06 ? 180 LYS A CA  1 
ATOM   1394 C C   . LYS A 1 180 ? 21.279 41.201 -1.030  1.00 33.68 ? 180 LYS A C   1 
ATOM   1395 O O   . LYS A 1 180 ? 21.576 40.289 -1.810  1.00 32.82 ? 180 LYS A O   1 
ATOM   1396 C CB  . LYS A 1 180 ? 19.034 41.330 0.063   1.00 39.55 ? 180 LYS A CB  1 
ATOM   1397 C CG  . LYS A 1 180 ? 18.310 40.494 -0.974  1.00 44.12 ? 180 LYS A CG  1 
ATOM   1398 C CD  . LYS A 1 180 ? 16.809 40.695 -0.917  1.00 49.53 ? 180 LYS A CD  1 
ATOM   1399 C CE  . LYS A 1 180 ? 16.098 39.453 -1.407  1.00 57.15 ? 180 LYS A CE  1 
ATOM   1400 N NZ  . LYS A 1 180 ? 16.522 39.083 -2.789  1.00 52.84 ? 180 LYS A NZ  1 
ATOM   1401 N N   . ARG A 1 181 ? 21.609 42.473 -1.263  1.00 33.52 ? 181 ARG A N   1 
ATOM   1402 C CA  . ARG A 1 181 ? 22.337 42.849 -2.469  1.00 29.45 ? 181 ARG A CA  1 
ATOM   1403 C C   . ARG A 1 181 ? 23.675 42.119 -2.562  1.00 27.74 ? 181 ARG A C   1 
ATOM   1404 O O   . ARG A 1 181 ? 24.042 41.614 -3.631  1.00 28.50 ? 181 ARG A O   1 
ATOM   1405 C CB  . ARG A 1 181 ? 22.522 44.367 -2.490  1.00 34.45 ? 181 ARG A CB  1 
ATOM   1406 C CG  . ARG A 1 181 ? 23.480 44.889 -3.537  1.00 43.08 ? 181 ARG A CG  1 
ATOM   1407 C CD  . ARG A 1 181 ? 23.391 46.407 -3.623  1.00 45.61 ? 181 ARG A CD  1 
ATOM   1408 N NE  . ARG A 1 181 ? 24.179 47.074 -2.592  1.00 41.53 ? 181 ARG A NE  1 
ATOM   1409 C CZ  . ARG A 1 181 ? 25.483 47.303 -2.676  1.00 39.14 ? 181 ARG A CZ  1 
ATOM   1410 N NH1 . ARG A 1 181 ? 26.185 46.920 -3.728  1.00 38.31 ? 181 ARG A NH1 1 
ATOM   1411 N NH2 . ARG A 1 181 ? 26.096 47.935 -1.678  1.00 39.03 ? 181 ARG A NH2 1 
ATOM   1412 N N   . HIS A 1 182 ? 24.408 42.033 -1.448  1.00 24.97 ? 182 HIS A N   1 
ATOM   1413 C CA  . HIS A 1 182 ? 25.687 41.333 -1.449  1.00 21.25 ? 182 HIS A CA  1 
ATOM   1414 C C   . HIS A 1 182 ? 25.505 39.836 -1.655  1.00 25.09 ? 182 HIS A C   1 
ATOM   1415 O O   . HIS A 1 182 ? 26.254 39.211 -2.414  1.00 23.81 ? 182 HIS A O   1 
ATOM   1416 C CB  . HIS A 1 182 ? 26.435 41.594 -0.141  1.00 25.05 ? 182 HIS A CB  1 
ATOM   1417 C CG  . HIS A 1 182 ? 27.016 42.969 -0.041  1.00 32.05 ? 182 HIS A CG  1 
ATOM   1418 N ND1 . HIS A 1 182 ? 27.811 43.513 -1.030  1.00 28.71 ? 182 HIS A ND1 1 
ATOM   1419 C CD2 . HIS A 1 182 ? 26.922 43.911 0.926   1.00 27.89 ? 182 HIS A CD2 1 
ATOM   1420 C CE1 . HIS A 1 182 ? 28.181 44.729 -0.673  1.00 29.25 ? 182 HIS A CE1 1 
ATOM   1421 N NE2 . HIS A 1 182 ? 27.654 44.996 0.510   1.00 28.21 ? 182 HIS A NE2 1 
ATOM   1422 N N   . THR A 1 183 ? 24.522 39.241 -0.977  1.00 28.00 ? 183 THR A N   1 
ATOM   1423 C CA  . THR A 1 183 ? 24.294 37.809 -1.127  1.00 29.15 ? 183 THR A CA  1 
ATOM   1424 C C   . THR A 1 183 ? 23.911 37.463 -2.563  1.00 29.73 ? 183 THR A C   1 
ATOM   1425 O O   . THR A 1 183 ? 24.381 36.459 -3.113  1.00 28.84 ? 183 THR A O   1 
ATOM   1426 C CB  . THR A 1 183 ? 23.215 37.350 -0.147  1.00 28.77 ? 183 THR A CB  1 
ATOM   1427 O OG1 . THR A 1 183 ? 23.624 37.667 1.188   1.00 33.41 ? 183 THR A OG1 1 
ATOM   1428 C CG2 . THR A 1 183 ? 22.996 35.848 -0.248  1.00 37.56 ? 183 THR A CG2 1 
ATOM   1429 N N   . GLU A 1 184 ? 23.067 38.286 -3.191  1.00 29.69 ? 184 GLU A N   1 
ATOM   1430 C CA  . GLU A 1 184 ? 22.731 38.054 -4.593  1.00 30.00 ? 184 GLU A CA  1 
ATOM   1431 C C   . GLU A 1 184 ? 23.972 38.083 -5.472  1.00 29.65 ? 184 GLU A C   1 
ATOM   1432 O O   . GLU A 1 184 ? 24.128 37.248 -6.372  1.00 27.73 ? 184 GLU A O   1 
ATOM   1433 C CB  . GLU A 1 184 ? 21.724 39.093 -5.085  1.00 33.93 ? 184 GLU A CB  1 
ATOM   1434 C CG  . GLU A 1 184 ? 21.573 39.080 -6.600  1.00 38.62 ? 184 GLU A CG  1 
ATOM   1435 C CD  . GLU A 1 184 ? 20.404 39.902 -7.096  1.00 50.37 ? 184 GLU A CD  1 
ATOM   1436 O OE1 . GLU A 1 184 ? 19.630 40.412 -6.258  1.00 55.98 ? 184 GLU A OE1 1 
ATOM   1437 O OE2 . GLU A 1 184 ? 20.263 40.037 -8.331  1.00 56.13 ? 184 GLU A OE2 1 
ATOM   1438 N N   . ALA A 1 185 ? 24.867 39.043 -5.232  1.00 28.39 ? 185 ALA A N   1 
ATOM   1439 C CA  . ALA A 1 185 ? 26.067 39.149 -6.050  1.00 27.30 ? 185 ALA A CA  1 
ATOM   1440 C C   . ALA A 1 185 ? 26.921 37.890 -5.949  1.00 31.24 ? 185 ALA A C   1 
ATOM   1441 O O   . ALA A 1 185 ? 27.434 37.401 -6.960  1.00 29.99 ? 185 ALA A O   1 
ATOM   1442 C CB  . ALA A 1 185 ? 26.872 40.383 -5.644  1.00 26.44 ? 185 ALA A CB  1 
ATOM   1443 N N   . ILE A 1 186 ? 27.077 37.342 -4.740  1.00 28.73 ? 186 ILE A N   1 
ATOM   1444 C CA  . ILE A 1 186 ? 27.900 36.146 -4.580  1.00 24.18 ? 186 ILE A CA  1 
ATOM   1445 C C   . ILE A 1 186 ? 27.223 34.932 -5.211  1.00 25.78 ? 186 ILE A C   1 
ATOM   1446 O O   . ILE A 1 186 ? 27.877 34.125 -5.880  1.00 25.38 ? 186 ILE A O   1 
ATOM   1447 C CB  . ILE A 1 186 ? 28.231 35.912 -3.094  1.00 22.96 ? 186 ILE A CB  1 
ATOM   1448 C CG1 . ILE A 1 186 ? 29.025 37.097 -2.539  1.00 28.93 ? 186 ILE A CG1 1 
ATOM   1449 C CG2 . ILE A 1 186 ? 29.018 34.623 -2.913  1.00 24.93 ? 186 ILE A CG2 1 
ATOM   1450 C CD1 . ILE A 1 186 ? 30.384 37.268 -3.188  1.00 29.43 ? 186 ILE A CD1 1 
ATOM   1451 N N   . ILE A 1 187 ? 25.911 34.775 -5.007  1.00 26.92 ? 187 ILE A N   1 
ATOM   1452 C CA  . ILE A 1 187 ? 25.189 33.674 -5.652  1.00 26.44 ? 187 ILE A CA  1 
ATOM   1453 C C   . ILE A 1 187 ? 25.374 33.736 -7.165  1.00 28.43 ? 187 ILE A C   1 
ATOM   1454 O O   . ILE A 1 187 ? 25.682 32.729 -7.814  1.00 29.65 ? 187 ILE A O   1 
ATOM   1455 C CB  . ILE A 1 187 ? 23.697 33.702 -5.271  1.00 25.28 ? 187 ILE A CB  1 
ATOM   1456 C CG1 . ILE A 1 187 ? 23.509 33.411 -3.782  1.00 30.84 ? 187 ILE A CG1 1 
ATOM   1457 C CG2 . ILE A 1 187 ? 22.919 32.689 -6.106  1.00 24.35 ? 187 ILE A CG2 1 
ATOM   1458 C CD1 . ILE A 1 187 ? 22.100 33.686 -3.291  1.00 30.12 ? 187 ILE A CD1 1 
ATOM   1459 N N   . ARG A 1 188 ? 25.208 34.928 -7.742  1.00 28.26 ? 188 ARG A N   1 
ATOM   1460 C CA  . ARG A 1 188 ? 25.337 35.090 -9.187  1.00 30.09 ? 188 ARG A CA  1 
ATOM   1461 C C   . ARG A 1 188 ? 26.732 34.716 -9.670  1.00 29.48 ? 188 ARG A C   1 
ATOM   1462 O O   . ARG A 1 188 ? 26.885 34.022 -10.682 1.00 33.88 ? 188 ARG A O   1 
ATOM   1463 C CB  . ARG A 1 188 ? 25.004 36.530 -9.577  1.00 34.39 ? 188 ARG A CB  1 
ATOM   1464 C CG  . ARG A 1 188 ? 23.522 36.831 -9.576  1.00 41.74 ? 188 ARG A CG  1 
ATOM   1465 C CD  . ARG A 1 188 ? 23.217 38.148 -10.271 1.00 45.81 ? 188 ARG A CD  1 
ATOM   1466 N NE  . ARG A 1 188 ? 21.791 38.444 -10.212 1.00 53.69 ? 188 ARG A NE  1 
ATOM   1467 C CZ  . ARG A 1 188 ? 20.915 38.060 -11.130 1.00 49.02 ? 188 ARG A CZ  1 
ATOM   1468 N NH1 . ARG A 1 188 ? 21.294 37.390 -12.206 1.00 52.13 ? 188 ARG A NH1 1 
ATOM   1469 N NH2 . ARG A 1 188 ? 19.629 38.353 -10.963 1.00 50.90 ? 188 ARG A NH2 1 
ATOM   1470 N N   . LEU A 1 189 ? 27.769 35.179 -8.967  1.00 28.11 ? 189 LEU A N   1 
ATOM   1471 C CA  . LEU A 1 189 ? 29.132 34.868 -9.384  1.00 31.87 ? 189 LEU A CA  1 
ATOM   1472 C C   . LEU A 1 189 ? 29.414 33.377 -9.293  1.00 32.49 ? 189 LEU A C   1 
ATOM   1473 O O   . LEU A 1 189 ? 30.109 32.815 -10.147 1.00 30.95 ? 189 LEU A O   1 
ATOM   1474 C CB  . LEU A 1 189 ? 30.142 35.643 -8.538  1.00 31.21 ? 189 LEU A CB  1 
ATOM   1475 C CG  . LEU A 1 189 ? 30.127 37.164 -8.663  1.00 37.95 ? 189 LEU A CG  1 
ATOM   1476 C CD1 . LEU A 1 189 ? 30.985 37.783 -7.570  1.00 40.76 ? 189 LEU A CD1 1 
ATOM   1477 C CD2 . LEU A 1 189 ? 30.619 37.578 -10.046 1.00 37.07 ? 189 LEU A CD2 1 
ATOM   1478 N N   . GLU A 1 190 ? 28.890 32.715 -8.262  1.00 27.02 ? 190 GLU A N   1 
ATOM   1479 C CA  . GLU A 1 190 ? 29.222 31.311 -8.071  1.00 27.78 ? 190 GLU A CA  1 
ATOM   1480 C C   . GLU A 1 190 ? 28.435 30.395 -8.998  1.00 29.48 ? 190 GLU A C   1 
ATOM   1481 O O   . GLU A 1 190 ? 28.974 29.377 -9.445  1.00 31.46 ? 190 GLU A O   1 
ATOM   1482 C CB  . GLU A 1 190 ? 28.990 30.909 -6.614  1.00 26.79 ? 190 GLU A CB  1 
ATOM   1483 C CG  . GLU A 1 190 ? 30.021 31.490 -5.661  1.00 31.15 ? 190 GLU A CG  1 
ATOM   1484 C CD  . GLU A 1 190 ? 31.096 30.489 -5.285  1.00 41.68 ? 190 GLU A CD  1 
ATOM   1485 O OE1 . GLU A 1 190 ? 31.547 29.725 -6.171  1.00 39.16 ? 190 GLU A OE1 1 
ATOM   1486 O OE2 . GLU A 1 190 ? 31.502 30.478 -4.104  1.00 38.64 ? 190 GLU A OE2 1 
ATOM   1487 N N   . LEU A 1 191 ? 27.180 30.734 -9.310  1.00 30.27 ? 191 LEU A N   1 
ATOM   1488 C CA  . LEU A 1 191 ? 26.277 29.780 -9.949  1.00 27.52 ? 191 LEU A CA  1 
ATOM   1489 C C   . LEU A 1 191 ? 25.616 30.257 -11.234 1.00 34.60 ? 191 LEU A C   1 
ATOM   1490 O O   . LEU A 1 191 ? 25.061 29.419 -11.955 1.00 33.39 ? 191 LEU A O   1 
ATOM   1491 C CB  . LEU A 1 191 ? 25.175 29.351 -8.967  1.00 28.00 ? 191 LEU A CB  1 
ATOM   1492 C CG  . LEU A 1 191 ? 25.661 28.568 -7.748  1.00 29.09 ? 191 LEU A CG  1 
ATOM   1493 C CD1 . LEU A 1 191 ? 24.730 28.785 -6.566  1.00 22.89 ? 191 LEU A CD1 1 
ATOM   1494 C CD2 . LEU A 1 191 ? 25.779 27.084 -8.087  1.00 26.26 ? 191 LEU A CD2 1 
ATOM   1495 N N   . LEU A 1 192 ? 25.646 31.548 -11.546 1.00 37.04 ? 192 LEU A N   1 
ATOM   1496 C CA  . LEU A 1 192 ? 25.029 32.055 -12.774 1.00 42.56 ? 192 LEU A CA  1 
ATOM   1497 C C   . LEU A 1 192 ? 26.052 32.699 -13.706 1.00 52.92 ? 192 LEU A C   1 
ATOM   1498 O O   . LEU A 1 192 ? 25.693 33.244 -14.751 1.00 65.15 ? 192 LEU A O   1 
ATOM   1499 C CB  . LEU A 1 192 ? 23.926 33.065 -12.451 1.00 39.58 ? 192 LEU A CB  1 
ATOM   1500 C CG  . LEU A 1 192 ? 22.761 32.582 -11.590 1.00 39.44 ? 192 LEU A CG  1 
ATOM   1501 C CD1 . LEU A 1 192 ? 21.780 33.717 -11.347 1.00 41.90 ? 192 LEU A CD1 1 
ATOM   1502 C CD2 . LEU A 1 192 ? 22.069 31.421 -12.277 1.00 41.32 ? 192 LEU A CD2 1 
ATOM   1503 O OXT . LEU A 1 192 ? 27.254 32.698 -13.439 1.00 50.51 ? 192 LEU A OXT 1 
HETATM 1504 N N1  . SPD B 2 .   ? 17.984 28.592 6.881   1.00 44.85 ? 201 SPD A N1  1 
HETATM 1505 C C2  . SPD B 2 .   ? 19.157 29.088 7.579   1.00 48.66 ? 201 SPD A C2  1 
HETATM 1506 C C3  . SPD B 2 .   ? 19.417 28.270 8.844   1.00 41.49 ? 201 SPD A C3  1 
HETATM 1507 C C4  . SPD B 2 .   ? 19.830 29.207 9.978   1.00 43.86 ? 201 SPD A C4  1 
HETATM 1508 C C5  . SPD B 2 .   ? 20.684 30.356 9.443   1.00 45.33 ? 201 SPD A C5  1 
HETATM 1509 N N6  . SPD B 2 .   ? 21.547 30.846 10.501  1.00 54.09 ? 201 SPD A N6  1 
HETATM 1510 C C7  . SPD B 2 .   ? 21.815 32.259 10.307  1.00 55.60 ? 201 SPD A C7  1 
HETATM 1511 C C8  . SPD B 2 .   ? 22.965 32.690 11.215  1.00 60.69 ? 201 SPD A C8  1 
HETATM 1512 C C9  . SPD B 2 .   ? 24.282 32.143 10.671  1.00 56.14 ? 201 SPD A C9  1 
HETATM 1513 N N10 . SPD B 2 .   ? 25.299 32.209 11.706  1.00 48.79 ? 201 SPD A N10 1 
HETATM 1514 O O   . HOH C 3 .   ? 26.291 45.322 3.890   1.00 36.68 ? 301 HOH A O   1 
HETATM 1515 O O   . HOH C 3 .   ? 28.459 17.656 -2.944  1.00 45.57 ? 302 HOH A O   1 
HETATM 1516 O O   . HOH C 3 .   ? 27.196 14.621 27.319  1.00 49.05 ? 303 HOH A O   1 
HETATM 1517 O O   . HOH C 3 .   ? 22.801 16.134 23.225  1.00 40.26 ? 304 HOH A O   1 
HETATM 1518 O O   . HOH C 3 .   ? 22.836 17.167 0.241   1.00 41.91 ? 305 HOH A O   1 
HETATM 1519 O O   . HOH C 3 .   ? 15.749 14.662 -9.647  1.00 53.86 ? 306 HOH A O   1 
HETATM 1520 O O   . HOH C 3 .   ? 28.055 29.694 12.928  1.00 39.73 ? 307 HOH A O   1 
HETATM 1521 O O   . HOH C 3 .   ? 4.794  20.186 38.126  1.00 50.91 ? 308 HOH A O   1 
HETATM 1522 O O   . HOH C 3 .   ? 6.774  32.624 -3.068  1.00 62.76 ? 309 HOH A O   1 
HETATM 1523 O O   . HOH C 3 .   ? 1.969  25.841 28.657  1.00 50.21 ? 310 HOH A O   1 
HETATM 1524 O O   . HOH C 3 .   ? 8.727  32.541 -8.691  1.00 60.66 ? 311 HOH A O   1 
HETATM 1525 O O   . HOH C 3 .   ? 19.164 41.791 -4.272  1.00 54.13 ? 312 HOH A O   1 
HETATM 1526 O O   . HOH C 3 .   ? 15.960 32.879 28.458  1.00 38.93 ? 313 HOH A O   1 
HETATM 1527 O O   . HOH C 3 .   ? 11.740 34.428 30.906  1.00 47.93 ? 314 HOH A O   1 
HETATM 1528 O O   . HOH C 3 .   ? 20.267 17.742 -16.006 1.00 40.92 ? 315 HOH A O   1 
HETATM 1529 O O   . HOH C 3 .   ? 18.284 14.116 24.326  1.00 41.09 ? 316 HOH A O   1 
HETATM 1530 O O   . HOH C 3 .   ? 13.800 14.627 19.522  1.00 43.95 ? 317 HOH A O   1 
HETATM 1531 O O   . HOH C 3 .   ? 31.539 17.990 19.640  1.00 41.86 ? 318 HOH A O   1 
HETATM 1532 O O   . HOH C 3 .   ? 23.434 22.579 -15.359 1.00 53.23 ? 319 HOH A O   1 
HETATM 1533 O O   . HOH C 3 .   ? 14.594 33.247 -10.019 1.00 47.84 ? 320 HOH A O   1 
HETATM 1534 O O   . HOH C 3 .   ? 5.726  23.788 21.081  1.00 44.13 ? 321 HOH A O   1 
HETATM 1535 O O   . HOH C 3 .   ? -0.878 12.051 25.472  1.00 36.96 ? 322 HOH A O   1 
HETATM 1536 O O   . HOH C 3 .   ? 20.289 30.265 -15.469 1.00 43.91 ? 323 HOH A O   1 
HETATM 1537 O O   . HOH C 3 .   ? 25.322 34.425 17.755  1.00 43.27 ? 324 HOH A O   1 
HETATM 1538 O O   . HOH C 3 .   ? 22.240 33.344 7.424   1.00 39.79 ? 325 HOH A O   1 
HETATM 1539 O O   . HOH C 3 .   ? 13.928 40.102 1.636   1.00 68.99 ? 326 HOH A O   1 
HETATM 1540 O O   . HOH C 3 .   ? 23.632 42.480 -6.071  1.00 36.95 ? 327 HOH A O   1 
HETATM 1541 O O   . HOH C 3 .   ? 19.170 18.125 -5.251  1.00 39.55 ? 328 HOH A O   1 
HETATM 1542 O O   . HOH C 3 .   ? 27.410 18.861 5.218   1.00 44.63 ? 329 HOH A O   1 
HETATM 1543 O O   . HOH C 3 .   ? 8.449  7.000  35.697  1.00 42.98 ? 330 HOH A O   1 
HETATM 1544 O O   . HOH C 3 .   ? 14.822 18.351 39.520  1.00 40.68 ? 331 HOH A O   1 
HETATM 1545 O O   . HOH C 3 .   ? 15.022 25.536 -11.595 1.00 45.28 ? 332 HOH A O   1 
HETATM 1546 O O   . HOH C 3 .   ? 31.272 40.108 15.166  1.00 27.81 ? 333 HOH A O   1 
HETATM 1547 O O   . HOH C 3 .   ? 32.383 52.024 14.415  1.00 36.24 ? 334 HOH A O   1 
HETATM 1548 O O   . HOH C 3 .   ? 25.553 46.909 11.820  1.00 26.69 ? 335 HOH A O   1 
HETATM 1549 O O   . HOH C 3 .   ? 29.364 46.878 11.232  1.00 27.64 ? 336 HOH A O   1 
HETATM 1550 O O   . HOH C 3 .   ? 7.925  26.077 -4.079  1.00 53.93 ? 337 HOH A O   1 
HETATM 1551 O O   . HOH C 3 .   ? 27.511 17.267 16.256  1.00 30.57 ? 338 HOH A O   1 
HETATM 1552 O O   . HOH C 3 .   ? 19.528 19.193 5.419   1.00 35.94 ? 339 HOH A O   1 
HETATM 1553 O O   . HOH C 3 .   ? 17.758 12.401 34.339  1.00 45.62 ? 340 HOH A O   1 
HETATM 1554 O O   . HOH C 3 .   ? 32.046 24.103 18.237  1.00 29.69 ? 341 HOH A O   1 
HETATM 1555 O O   . HOH C 3 .   ? 31.599 28.926 -8.733  1.00 32.66 ? 342 HOH A O   1 
HETATM 1556 O O   . HOH C 3 .   ? 23.347 32.454 24.238  1.00 38.77 ? 343 HOH A O   1 
HETATM 1557 O O   . HOH C 3 .   ? 19.904 23.171 10.307  1.00 39.19 ? 344 HOH A O   1 
HETATM 1558 O O   . HOH C 3 .   ? 8.096  11.892 18.744  1.00 56.11 ? 345 HOH A O   1 
HETATM 1559 O O   . HOH C 3 .   ? 17.436 31.464 -11.911 1.00 46.60 ? 346 HOH A O   1 
HETATM 1560 O O   . HOH C 3 .   ? 12.292 22.067 -8.850  1.00 52.06 ? 347 HOH A O   1 
HETATM 1561 O O   . HOH C 3 .   ? 29.016 26.658 -10.623 1.00 38.82 ? 348 HOH A O   1 
HETATM 1562 O O   . HOH C 3 .   ? 27.864 47.303 1.912   1.00 43.37 ? 349 HOH A O   1 
HETATM 1563 O O   . HOH C 3 .   ? 10.340 27.472 -13.089 1.00 48.17 ? 350 HOH A O   1 
HETATM 1564 O O   . HOH C 3 .   ? 29.372 23.850 17.719  1.00 26.28 ? 351 HOH A O   1 
HETATM 1565 O O   . HOH C 3 .   ? 3.844  13.402 31.611  1.00 40.61 ? 352 HOH A O   1 
HETATM 1566 O O   . HOH C 3 .   ? 31.051 34.150 -12.342 1.00 40.87 ? 353 HOH A O   1 
HETATM 1567 O O   . HOH C 3 .   ? 26.993 51.861 9.649   1.00 38.23 ? 354 HOH A O   1 
HETATM 1568 O O   . HOH C 3 .   ? 24.470 17.710 30.587  1.00 45.39 ? 355 HOH A O   1 
HETATM 1569 O O   . HOH C 3 .   ? 10.194 19.845 14.349  1.00 40.35 ? 356 HOH A O   1 
HETATM 1570 O O   . HOH C 3 .   ? 13.006 24.849 -4.148  1.00 49.61 ? 357 HOH A O   1 
HETATM 1571 O O   . HOH C 3 .   ? 17.292 22.262 -0.253  1.00 34.50 ? 358 HOH A O   1 
HETATM 1572 O O   . HOH C 3 .   ? 12.124 36.507 19.323  1.00 52.34 ? 359 HOH A O   1 
HETATM 1573 O O   . HOH C 3 .   ? 12.980 10.516 37.311  1.00 42.42 ? 360 HOH A O   1 
HETATM 1574 O O   . HOH C 3 .   ? 18.152 45.371 8.625   1.00 54.29 ? 361 HOH A O   1 
HETATM 1575 O O   . HOH C 3 .   ? 29.788 18.392 -4.658  1.00 50.67 ? 362 HOH A O   1 
HETATM 1576 O O   . HOH C 3 .   ? 5.661  29.381 28.354  1.00 55.28 ? 363 HOH A O   1 
HETATM 1577 O O   . HOH C 3 .   ? 32.638 38.126 10.432  1.00 29.41 ? 364 HOH A O   1 
HETATM 1578 O O   . HOH C 3 .   ? 18.176 32.881 27.330  1.00 44.69 ? 365 HOH A O   1 
HETATM 1579 O O   . HOH C 3 .   ? 23.347 17.072 10.397  1.00 34.55 ? 366 HOH A O   1 
HETATM 1580 O O   . HOH C 3 .   ? 32.367 51.443 3.634   1.00 37.34 ? 367 HOH A O   1 
HETATM 1581 O O   . HOH C 3 .   ? 27.998 46.095 18.412  1.00 39.11 ? 368 HOH A O   1 
HETATM 1582 O O   . HOH C 3 .   ? 20.091 44.564 -0.138  1.00 42.09 ? 369 HOH A O   1 
HETATM 1583 O O   . HOH C 3 .   ? 28.305 35.290 -13.090 1.00 51.04 ? 370 HOH A O   1 
HETATM 1584 O O   . HOH C 3 .   ? 21.568 30.513 28.261  1.00 40.20 ? 371 HOH A O   1 
HETATM 1585 O O   . HOH C 3 .   ? 8.620  24.807 -8.088  1.00 52.60 ? 372 HOH A O   1 
HETATM 1586 O O   . HOH C 3 .   ? 12.767 16.180 40.315  1.00 41.16 ? 373 HOH A O   1 
HETATM 1587 O O   . HOH C 3 .   ? 7.677  19.756 16.270  1.00 48.84 ? 374 HOH A O   1 
HETATM 1588 O O   . HOH C 3 .   ? 17.901 14.817 33.602  1.00 38.21 ? 375 HOH A O   1 
HETATM 1589 O O   . HOH C 3 .   ? 23.295 17.472 21.216  1.00 33.18 ? 376 HOH A O   1 
HETATM 1590 O O   . HOH C 3 .   ? 6.019  35.455 7.630   1.00 55.94 ? 377 HOH A O   1 
HETATM 1591 O O   . HOH C 3 .   ? 23.404 18.167 -10.099 1.00 47.64 ? 378 HOH A O   1 
HETATM 1592 O O   . HOH C 3 .   ? 1.351  14.823 32.883  1.00 27.97 ? 379 HOH A O   1 
HETATM 1593 O O   . HOH C 3 .   ? 23.623 26.088 28.900  1.00 44.11 ? 380 HOH A O   1 
HETATM 1594 O O   . HOH C 3 .   ? 15.475 16.715 18.449  1.00 34.53 ? 381 HOH A O   1 
HETATM 1595 O O   . HOH C 3 .   ? 11.777 30.211 33.265  1.00 36.99 ? 382 HOH A O   1 
HETATM 1596 O O   . HOH C 3 .   ? 24.572 40.604 12.664  1.00 42.67 ? 383 HOH A O   1 
HETATM 1597 O O   . HOH C 3 .   ? 21.437 23.665 31.114  1.00 35.15 ? 384 HOH A O   1 
HETATM 1598 O O   . HOH C 3 .   ? 18.940 43.215 3.186   1.00 40.54 ? 385 HOH A O   1 
HETATM 1599 O O   . HOH C 3 .   ? 13.392 24.558 -8.937  1.00 44.22 ? 386 HOH A O   1 
HETATM 1600 O O   . HOH C 3 .   ? 22.273 20.003 31.996  1.00 32.31 ? 387 HOH A O   1 
HETATM 1601 O O   . HOH C 3 .   ? 36.157 25.733 -6.100  1.00 43.90 ? 388 HOH A O   1 
HETATM 1602 O O   . HOH C 3 .   ? 10.626 11.750 21.650  1.00 42.90 ? 389 HOH A O   1 
HETATM 1603 O O   . HOH C 3 .   ? 27.093 50.655 3.294   1.00 39.42 ? 390 HOH A O   1 
HETATM 1604 O O   . HOH C 3 .   ? 27.555 39.296 -9.184  1.00 37.39 ? 391 HOH A O   1 
HETATM 1605 O O   . HOH C 3 .   ? 13.585 27.322 -12.823 1.00 39.59 ? 392 HOH A O   1 
HETATM 1606 O O   . HOH C 3 .   ? 26.345 17.323 29.177  1.00 40.58 ? 393 HOH A O   1 
HETATM 1607 O O   . HOH C 3 .   ? 27.083 47.459 9.821   1.00 30.98 ? 394 HOH A O   1 
HETATM 1608 O O   . HOH C 3 .   ? 12.219 8.242  27.529  1.00 40.86 ? 395 HOH A O   1 
HETATM 1609 O O   . HOH C 3 .   ? 10.266 19.799 41.508  1.00 46.55 ? 396 HOH A O   1 
HETATM 1610 O O   . HOH C 3 .   ? 18.099 12.625 26.561  1.00 34.87 ? 397 HOH A O   1 
HETATM 1611 O O   . HOH C 3 .   ? 30.413 18.341 16.663  1.00 33.66 ? 398 HOH A O   1 
HETATM 1612 O O   . HOH C 3 .   ? 20.255 15.986 23.276  1.00 36.99 ? 399 HOH A O   1 
HETATM 1613 O O   . HOH C 3 .   ? 27.756 55.283 9.392   1.00 50.61 ? 400 HOH A O   1 
HETATM 1614 O O   . HOH C 3 .   ? 7.920  6.581  32.854  1.00 44.07 ? 401 HOH A O   1 
HETATM 1615 O O   . HOH C 3 .   ? 21.279 31.815 26.000  1.00 46.65 ? 402 HOH A O   1 
HETATM 1616 O O   . HOH C 3 .   ? 3.577  14.777 28.993  1.00 41.10 ? 403 HOH A O   1 
HETATM 1617 O O   . HOH C 3 .   ? 20.341 10.921 33.502  1.00 46.62 ? 404 HOH A O   1 
HETATM 1618 O O   . HOH C 3 .   ? 21.431 27.606 28.731  1.00 38.89 ? 405 HOH A O   1 
HETATM 1619 O O   . HOH C 3 .   ? 7.135  18.184 39.901  1.00 31.32 ? 406 HOH A O   1 
HETATM 1620 O O   . HOH C 3 .   ? 1.029  5.865  32.734  1.00 39.59 ? 407 HOH A O   1 
HETATM 1621 O O   . HOH C 3 .   ? 15.502 12.077 -11.647 1.00 55.60 ? 408 HOH A O   1 
HETATM 1622 O O   . HOH C 3 .   ? 16.329 30.560 34.813  1.00 41.61 ? 409 HOH A O   1 
HETATM 1623 O O   . HOH C 3 .   ? 21.491 34.267 30.894  1.00 53.88 ? 410 HOH A O   1 
HETATM 1624 O O   . HOH C 3 .   ? 16.737 39.326 -6.711  1.00 51.71 ? 411 HOH A O   1 
HETATM 1625 O O   . HOH C 3 .   ? 34.099 52.105 12.595  1.00 34.71 ? 412 HOH A O   1 
HETATM 1626 O O   . HOH C 3 .   ? 8.928  14.449 40.778  1.00 25.13 ? 413 HOH A O   1 
HETATM 1627 O O   . HOH C 3 .   ? 9.357  9.896  22.063  1.00 40.30 ? 414 HOH A O   1 
HETATM 1628 O O   . HOH C 3 .   ? 16.949 38.795 -9.182  1.00 59.21 ? 415 HOH A O   1 
HETATM 1629 O O   . HOH C 3 .   ? 18.000 21.290 10.751  1.00 43.07 ? 416 HOH A O   1 
HETATM 1630 O O   . HOH C 3 .   ? 12.575 37.913 17.032  1.00 51.64 ? 417 HOH A O   1 
HETATM 1631 O O   . HOH C 3 .   ? 5.798  8.016  29.264  1.00 43.78 ? 418 HOH A O   1 
HETATM 1632 O O   . HOH C 3 .   ? 1.978  16.210 28.511  1.00 31.26 ? 419 HOH A O   1 
HETATM 1633 O O   . HOH C 3 .   ? 19.357 16.864 -7.925  1.00 39.41 ? 420 HOH A O   1 
HETATM 1634 O O   . HOH C 3 .   ? 18.668 31.212 -14.322 1.00 46.57 ? 421 HOH A O   1 
HETATM 1635 O O   . HOH C 3 .   ? 25.772 53.369 6.892   1.00 45.67 ? 422 HOH A O   1 
HETATM 1636 O O   . HOH C 3 .   ? 26.592 53.197 4.146   1.00 47.52 ? 423 HOH A O   1 
HETATM 1637 O O   . HOH C 3 .   ? 20.236 16.523 20.607  1.00 44.70 ? 424 HOH A O   1 
HETATM 1638 O O   . HOH C 3 .   ? 29.872 48.151 0.995   1.00 47.94 ? 425 HOH A O   1 
HETATM 1639 O O   . HOH C 3 .   ? 11.206 29.654 35.693  1.00 42.65 ? 426 HOH A O   1 
HETATM 1640 O O   . HOH C 3 .   ? 0.193  13.958 26.275  1.00 52.10 ? 427 HOH A O   1 
HETATM 1641 O O   . HOH C 3 .   ? 27.025 15.159 17.561  1.00 43.53 ? 428 HOH A O   1 
HETATM 1642 O O   . HOH C 3 .   ? 12.567 32.663 33.304  1.00 47.03 ? 429 HOH A O   1 
HETATM 1643 O O   . HOH C 3 .   ? 17.884 11.272 36.670  1.00 46.56 ? 430 HOH A O   1 
HETATM 1644 O O   . HOH C 3 .   ? 20.043 15.079 -15.399 1.00 48.71 ? 431 HOH A O   1 
HETATM 1645 O O   . HOH C 3 .   ? 25.443 41.137 -9.166  1.00 40.73 ? 432 HOH A O   1 
HETATM 1646 O O   . HOH C 3 .   ? 19.966 12.444 22.548  1.00 54.64 ? 433 HOH A O   1 
HETATM 1647 O O   . HOH C 3 .   ? 38.806 25.452 -6.148  1.00 47.41 ? 434 HOH A O   1 
HETATM 1648 O O   . HOH C 3 .   ? 30.275 14.681 27.103  1.00 54.67 ? 435 HOH A O   1 
HETATM 1649 O O   . HOH C 3 .   ? 7.758  26.762 -13.075 1.00 46.05 ? 436 HOH A O   1 
HETATM 1650 O O   . HOH C 3 .   ? 25.740 15.540 10.473  1.00 45.06 ? 437 HOH A O   1 
HETATM 1651 O O   . HOH C 3 .   ? 18.528 14.992 19.035  1.00 54.89 ? 438 HOH A O   1 
HETATM 1652 O O   . HOH C 3 .   ? 40.066 23.423 -7.451  1.00 54.65 ? 439 HOH A O   1 
HETATM 1653 O O   . HOH C 3 .   ? 36.564 53.548 13.310  1.00 47.17 ? 440 HOH A O   1 
HETATM 1654 O O   . HOH C 3 .   ? 21.843 14.599 18.646  1.00 51.18 ? 441 HOH A O   1 
HETATM 1655 O O   . HOH C 3 .   ? 20.070 14.327 16.658  1.00 48.38 ? 442 HOH A O   1 
HETATM 1656 O O   . HOH C 3 .   ? 25.786 12.919 16.143  1.00 55.80 ? 443 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   . ASP A 7   ? 0.6462 0.7331 0.6917 -0.0657 -0.0007 0.0434  7   ASP A N   
2    C CA  . ASP A 7   ? 0.7860 0.8756 0.8291 -0.0711 -0.0033 0.0434  7   ASP A CA  
3    C C   . ASP A 7   ? 0.7237 0.8241 0.7728 -0.0681 -0.0054 0.0478  7   ASP A C   
4    O O   . ASP A 7   ? 0.5501 0.6470 0.5985 -0.0640 -0.0055 0.0468  7   ASP A O   
5    C CB  . ASP A 7   ? 0.7631 0.8563 0.8034 -0.0803 -0.0044 0.0438  7   ASP A CB  
6    C CG  . ASP A 7   ? 0.7526 0.8577 0.7994 -0.0809 -0.0048 0.0485  7   ASP A CG  
7    O OD1 . ASP A 7   ? 0.7020 0.8204 0.7553 -0.0813 -0.0071 0.0539  7   ASP A OD1 
8    O OD2 . ASP A 7   ? 0.7512 0.8528 0.7976 -0.0810 -0.0025 0.0473  7   ASP A OD2 
9    N N   . GLN A 8   ? 0.6654 0.7793 0.7209 -0.0701 -0.0067 0.0534  8   GLN A N   
10   C CA  . GLN A 8   ? 0.5070 0.6321 0.5706 -0.0658 -0.0076 0.0591  8   GLN A CA  
11   C C   . GLN A 8   ? 0.3522 0.4741 0.4200 -0.0562 -0.0033 0.0597  8   GLN A C   
12   O O   . GLN A 8   ? 0.3996 0.5235 0.4709 -0.0508 -0.0025 0.0618  8   GLN A O   
13   C CB  . GLN A 8   ? 0.4943 0.6359 0.5653 -0.0706 -0.0100 0.0663  8   GLN A CB  
14   C CG  . GLN A 8   ? 0.4669 0.6205 0.5502 -0.0637 -0.0083 0.0739  8   GLN A CG  
15   C CD  . GLN A 8   ? 0.6983 0.8705 0.7901 -0.0689 -0.0122 0.0826  8   GLN A CD  
16   O OE1 . GLN A 8   ? 0.6188 0.7957 0.7084 -0.0744 -0.0168 0.0842  8   GLN A OE1 
17   N NE2 . GLN A 8   ? 0.5594 0.7425 0.6611 -0.0674 -0.0104 0.0889  8   GLN A NE2 
18   N N   . ARG A 9   ? 0.3882 0.5043 0.4546 -0.0545 -0.0003 0.0576  9   ARG A N   
19   C CA  . ARG A 9   ? 0.3705 0.4816 0.4382 -0.0468 0.0041  0.0576  9   ARG A CA  
20   C C   . ARG A 9   ? 0.3719 0.4710 0.4331 -0.0434 0.0045  0.0529  9   ARG A C   
21   O O   . ARG A 9   ? 0.3165 0.4132 0.3786 -0.0375 0.0074  0.0537  9   ARG A O   
22   C CB  . ARG A 9   ? 0.4201 0.5276 0.4866 -0.0470 0.0069  0.0565  9   ARG A CB  
23   C CG  . ARG A 9   ? 0.4045 0.5247 0.4796 -0.0481 0.0080  0.0624  9   ARG A CG  
24   C CD  . ARG A 9   ? 0.3852 0.5016 0.4590 -0.0481 0.0113  0.0615  9   ARG A CD  
25   N NE  . ARG A 9   ? 0.4468 0.5579 0.5142 -0.0542 0.0088  0.0573  9   ARG A NE  
26   C CZ  . ARG A 9   ? 0.5163 0.6254 0.5825 -0.0561 0.0105  0.0566  9   ARG A CZ  
27   N NH1 . ARG A 9   ? 0.3415 0.4534 0.4120 -0.0527 0.0145  0.0595  9   ARG A NH1 
28   N NH2 . ARG A 9   ? 0.4875 0.5911 0.5480 -0.0615 0.0087  0.0530  9   ARG A NH2 
29   N N   . ARG A 10  ? 0.3539 0.4452 0.4087 -0.0471 0.0022  0.0483  10  ARG A N   
30   C CA  . ARG A 10  ? 0.3701 0.4521 0.4202 -0.0444 0.0020  0.0449  10  ARG A CA  
31   C C   . ARG A 10  ? 0.3054 0.3925 0.3582 -0.0424 0.0008  0.0470  10  ARG A C   
32   O O   . ARG A 10  ? 0.3318 0.4144 0.3837 -0.0374 0.0023  0.0464  10  ARG A O   
33   C CB  . ARG A 10  ? 0.4369 0.5105 0.4814 -0.0487 0.0005  0.0407  10  ARG A CB  
34   C CG  . ARG A 10  ? 0.3689 0.4333 0.4096 -0.0459 0.0004  0.0379  10  ARG A CG  
35   C CD  . ARG A 10  ? 0.4197 0.4758 0.4565 -0.0497 0.0001  0.0347  10  ARG A CD  
36   N NE  . ARG A 10  ? 0.4044 0.4520 0.4392 -0.0464 0.0005  0.0330  10  ARG A NE  
37   C CZ  . ARG A 10  ? 0.3773 0.4223 0.4112 -0.0449 -0.0003 0.0319  10  ARG A CZ  
38   N NH1 . ARG A 10  ? 0.3696 0.4195 0.4038 -0.0463 -0.0016 0.0322  10  ARG A NH1 
39   N NH2 . ARG A 10  ? 0.3095 0.3474 0.3421 -0.0423 -0.0001 0.0310  10  ARG A NH2 
40   N N   . GLU A 11  ? 0.3374 0.4339 0.3932 -0.0467 -0.0020 0.0497  11  GLU A N   
41   C CA  . GLU A 11  ? 0.3606 0.4629 0.4192 -0.0454 -0.0037 0.0525  11  GLU A CA  
42   C C   . GLU A 11  ? 0.3301 0.4388 0.3963 -0.0385 -0.0006 0.0575  11  GLU A C   
43   O O   . GLU A 11  ? 0.3019 0.4099 0.3691 -0.0343 0.0001  0.0584  11  GLU A O   
44   C CB  . GLU A 11  ? 0.4678 0.5798 0.5275 -0.0530 -0.0078 0.0553  11  GLU A CB  
45   C CG  . GLU A 11  ? 0.5339 0.6552 0.5981 -0.0522 -0.0100 0.0601  11  GLU A CG  
46   C CD  . GLU A 11  ? 0.5317 0.6443 0.5894 -0.0522 -0.0112 0.0559  11  GLU A CD  
47   O OE1 . GLU A 11  ? 0.5597 0.6610 0.6093 -0.0554 -0.0111 0.0499  11  GLU A OE1 
48   O OE2 . GLU A 11  ? 0.6884 0.8055 0.7495 -0.0488 -0.0118 0.0589  11  GLU A OE2 
49   N N   . MET A 12  ? 0.3428 0.4568 0.4142 -0.0371 0.0022  0.0609  12  MET A N   
50   C CA  . MET A 12  ? 0.3056 0.4239 0.3842 -0.0302 0.0069  0.0659  12  MET A CA  
51   C C   . MET A 12  ? 0.2610 0.3658 0.3336 -0.0245 0.0115  0.0618  12  MET A C   
52   O O   . MET A 12  ? 0.3315 0.4359 0.4069 -0.0189 0.0153  0.0643  12  MET A O   
53   C CB  . MET A 12  ? 0.3452 0.4723 0.4313 -0.0301 0.0095  0.0709  12  MET A CB  
54   C CG  . MET A 12  ? 0.5426 0.6831 0.6337 -0.0372 0.0045  0.0750  12  MET A CG  
55   S SD  . MET A 12  ? 0.7706 0.9254 0.8686 -0.0395 -0.0003 0.0817  12  MET A SD  
56   C CE  . MET A 12  ? 0.5220 0.6805 0.6302 -0.0289 0.0061  0.0882  12  MET A CE  
57   N N   . ILE A 13  ? 0.2533 0.3469 0.3174 -0.0263 0.0113  0.0560  13  ILE A N   
58   C CA  . ILE A 13  ? 0.2625 0.3434 0.3194 -0.0227 0.0143  0.0522  13  ILE A CA  
59   C C   . ILE A 13  ? 0.3026 0.3805 0.3572 -0.0213 0.0123  0.0506  13  ILE A C   
60   O O   . ILE A 13  ? 0.2806 0.3536 0.3336 -0.0168 0.0158  0.0508  13  ILE A O   
61   C CB  . ILE A 13  ? 0.2621 0.3335 0.3114 -0.0258 0.0133  0.0476  13  ILE A CB  
62   C CG1 . ILE A 13  ? 0.3380 0.4107 0.3885 -0.0263 0.0164  0.0491  13  ILE A CG1 
63   C CG2 . ILE A 13  ? 0.3161 0.3755 0.3574 -0.0238 0.0145  0.0441  13  ILE A CG2 
64   C CD1 . ILE A 13  ? 0.3450 0.4118 0.3902 -0.0304 0.0143  0.0457  13  ILE A CD1 
65   N N   . LEU A 14  ? 0.2695 0.3492 0.3232 -0.0255 0.0073  0.0489  14  LEU A N   
66   C CA  . LEU A 14  ? 0.3088 0.3861 0.3606 -0.0247 0.0053  0.0474  14  LEU A CA  
67   C C   . LEU A 14  ? 0.3187 0.4035 0.3767 -0.0206 0.0070  0.0523  14  LEU A C   
68   O O   . LEU A 14  ? 0.2938 0.3735 0.3497 -0.0168 0.0086  0.0514  14  LEU A O   
69   C CB  . LEU A 14  ? 0.3479 0.4265 0.3979 -0.0306 0.0006  0.0455  14  LEU A CB  
70   C CG  . LEU A 14  ? 0.4081 0.4809 0.4540 -0.0311 -0.0015 0.0424  14  LEU A CG  
71   C CD1 . LEU A 14  ? 0.3435 0.4050 0.3844 -0.0276 0.0003  0.0389  14  LEU A CD1 
72   C CD2 . LEU A 14  ? 0.4996 0.5708 0.5422 -0.0377 -0.0044 0.0400  14  LEU A CD2 
73   N N   . GLN A 15  ? 0.3308 0.4282 0.3971 -0.0213 0.0068  0.0581  15  GLN A N   
74   C CA  . GLN A 15  ? 0.3648 0.4712 0.4392 -0.0172 0.0085  0.0645  15  GLN A CA  
75   C C   . GLN A 15  ? 0.3512 0.4515 0.4264 -0.0098 0.0160  0.0657  15  GLN A C   
76   O O   . GLN A 15  ? 0.3381 0.4384 0.4156 -0.0053 0.0185  0.0680  15  GLN A O   
77   C CB  . GLN A 15  ? 0.3560 0.4785 0.4404 -0.0199 0.0067  0.0718  15  GLN A CB  
78   C CG  . GLN A 15  ? 0.3979 0.5272 0.4809 -0.0278 -0.0005 0.0718  15  GLN A CG  
79   C CD  . GLN A 15  ? 0.4586 0.5895 0.5411 -0.0276 -0.0031 0.0729  15  GLN A CD  
80   O OE1 . GLN A 15  ? 0.4570 0.5909 0.5453 -0.0215 -0.0001 0.0772  15  GLN A OE1 
81   N NE2 . GLN A 15  ? 0.5275 0.6554 0.6028 -0.0343 -0.0080 0.0689  15  GLN A NE2 
82   N N   . ALA A 16  ? 0.3415 0.4359 0.4141 -0.0089 0.0202  0.0641  16  ALA A N   
83   C CA  . ALA A 16  ? 0.2867 0.3722 0.3569 -0.0032 0.0282  0.0642  16  ALA A CA  
84   C C   . ALA A 16  ? 0.3372 0.4094 0.3971 -0.0022 0.0284  0.0585  16  ALA A C   
85   O O   . ALA A 16  ? 0.3223 0.3897 0.3816 0.0026  0.0337  0.0596  16  ALA A O   
86   C CB  . ALA A 16  ? 0.3450 0.4252 0.4120 -0.0038 0.0321  0.0629  16  ALA A CB  
87   N N   . ALA A 17  ? 0.2791 0.3453 0.3314 -0.0067 0.0231  0.0528  17  ALA A N   
88   C CA  . ALA A 17  ? 0.3224 0.3774 0.3659 -0.0064 0.0226  0.0481  17  ALA A CA  
89   C C   . ALA A 17  ? 0.3238 0.3822 0.3704 -0.0039 0.0215  0.0496  17  ALA A C   
90   O O   . ALA A 17  ? 0.3460 0.3964 0.3879 -0.0010 0.0246  0.0481  17  ALA A O   
91   C CB  . ALA A 17  ? 0.2903 0.3407 0.3281 -0.0115 0.0170  0.0433  17  ALA A CB  
92   N N   . MET A 18  ? 0.3272 0.3972 0.3811 -0.0057 0.0170  0.0527  18  MET A N   
93   C CA  . MET A 18  ? 0.3353 0.4092 0.3920 -0.0041 0.0154  0.0546  18  MET A CA  
94   C C   . MET A 18  ? 0.3527 0.4290 0.4151 0.0023  0.0217  0.0599  18  MET A C   
95   O O   . MET A 18  ? 0.3593 0.4316 0.4200 0.0054  0.0233  0.0597  18  MET A O   
96   C CB  . MET A 18  ? 0.3083 0.3942 0.3703 -0.0089 0.0093  0.0573  18  MET A CB  
97   C CG  . MET A 18  ? 0.3142 0.3960 0.3703 -0.0152 0.0045  0.0520  18  MET A CG  
98   S SD  . MET A 18  ? 0.3611 0.4544 0.4204 -0.0227 -0.0015 0.0545  18  MET A SD  
99   C CE  . MET A 18  ? 0.3418 0.4468 0.4084 -0.0207 -0.0026 0.0615  18  MET A CE  
100  N N   . GLN A 19  ? 0.3356 0.4183 0.4054 0.0046  0.0261  0.0652  19  GLN A N   
101  C CA  . GLN A 19  ? 0.3112 0.3955 0.3876 0.0114  0.0339  0.0711  19  GLN A CA  
102  C C   . GLN A 19  ? 0.3747 0.4422 0.4410 0.0148  0.0408  0.0665  19  GLN A C   
103  O O   . GLN A 19  ? 0.4011 0.4657 0.4683 0.0194  0.0450  0.0685  19  GLN A O   
104  C CB  . GLN A 19  ? 0.3440 0.4361 0.4294 0.0130  0.0383  0.0771  19  GLN A CB  
105  C CG  . GLN A 19  ? 0.5325 0.6364 0.6321 0.0186  0.0429  0.0873  19  GLN A CG  
106  C CD  . GLN A 19  ? 0.7468 0.8672 0.8591 0.0171  0.0413  0.0949  19  GLN A CD  
107  O OE1 . GLN A 19  ? 0.7721 0.9049 0.8884 0.0115  0.0328  0.0969  19  GLN A OE1 
108  N NE2 . GLN A 19  ? 0.6736 0.7934 0.7916 0.0215  0.0499  0.0991  19  GLN A NE2 
109  N N   . ILE A 20  ? 0.3836 0.4397 0.4397 0.0122  0.0421  0.0608  20  ILE A N   
110  C CA  . ILE A 20  ? 0.3804 0.4199 0.4247 0.0136  0.0480  0.0563  20  ILE A CA  
111  C C   . ILE A 20  ? 0.4086 0.4429 0.4468 0.0127  0.0439  0.0523  20  ILE A C   
112  O O   . ILE A 20  ? 0.3957 0.4211 0.4291 0.0158  0.0493  0.0516  20  ILE A O   
113  C CB  . ILE A 20  ? 0.3419 0.3716 0.3759 0.0094  0.0485  0.0514  20  ILE A CB  
114  C CG1 . ILE A 20  ? 0.4334 0.4661 0.4725 0.0109  0.0545  0.0553  20  ILE A CG1 
115  C CG2 . ILE A 20  ? 0.3704 0.3830 0.3900 0.0085  0.0527  0.0464  20  ILE A CG2 
116  C CD1 . ILE A 20  ? 0.4551 0.4856 0.4888 0.0056  0.0512  0.0519  20  ILE A CD1 
117  N N   . ALA A 21  ? 0.3740 0.4130 0.4122 0.0083  0.0350  0.0496  21  ALA A N   
118  C CA  . ALA A 21  ? 0.4205 0.4550 0.4537 0.0073  0.0310  0.0460  21  ALA A CA  
119  C C   . ALA A 21  ? 0.4031 0.4412 0.4416 0.0120  0.0335  0.0498  21  ALA A C   
120  O O   . ALA A 21  ? 0.4067 0.4354 0.4389 0.0141  0.0368  0.0476  21  ALA A O   
121  C CB  . ALA A 21  ? 0.3825 0.4225 0.4168 0.0023  0.0224  0.0438  21  ALA A CB  
122  N N   . LEU A 22  ? 0.3871 0.4392 0.4371 0.0134  0.0320  0.0559  22  LEU A N   
123  C CA  . LEU A 22  ? 0.4737 0.5315 0.5304 0.0177  0.0337  0.0609  22  LEU A CA  
124  C C   . LEU A 22  ? 0.5227 0.5723 0.5786 0.0241  0.0441  0.0632  22  LEU A C   
125  O O   . LEU A 22  ? 0.5361 0.5799 0.5892 0.0270  0.0468  0.0627  22  LEU A O   
126  C CB  . LEU A 22  ? 0.4369 0.5124 0.5066 0.0173  0.0303  0.0686  22  LEU A CB  
127  C CG  . LEU A 22  ? 0.4519 0.5364 0.5231 0.0119  0.0210  0.0686  22  LEU A CG  
128  C CD1 . LEU A 22  ? 0.4699 0.5721 0.5541 0.0120  0.0191  0.0782  22  LEU A CD1 
129  C CD2 . LEU A 22  ? 0.4086 0.4863 0.4737 0.0122  0.0191  0.0648  22  LEU A CD2 
130  N N   . ALA A 23  ? 0.4515 0.4997 0.5094 0.0261  0.0508  0.0656  23  ALA A N   
131  C CA  . ALA A 23  ? 0.4563 0.4968 0.5147 0.0324  0.0624  0.0688  23  ALA A CA  
132  C C   . ALA A 23  ? 0.5450 0.5654 0.5871 0.0314  0.0678  0.0615  23  ALA A C   
133  O O   . ALA A 23  ? 0.4996 0.5110 0.5388 0.0357  0.0761  0.0624  23  ALA A O   
134  C CB  . ALA A 23  ? 0.4437 0.4894 0.5104 0.0348  0.0686  0.0745  23  ALA A CB  
135  N N   . GLU A 24  ? 0.4556 0.4686 0.4867 0.0254  0.0634  0.0547  24  GLU A N   
136  C CA  . GLU A 24  ? 0.4969 0.4915 0.5120 0.0231  0.0686  0.0488  24  GLU A CA  
137  C C   . GLU A 24  ? 0.4908 0.4794 0.4952 0.0170  0.0605  0.0420  24  GLU A C   
138  O O   . GLU A 24  ? 0.5667 0.5407 0.5574 0.0143  0.0640  0.0377  24  GLU A O   
139  C CB  . GLU A 24  ? 0.5501 0.5385 0.5607 0.0215  0.0744  0.0484  24  GLU A CB  
140  C CG  . GLU A 24  ? 0.5869 0.5793 0.6079 0.0279  0.0844  0.0555  24  GLU A CG  
141  C CD  . GLU A 24  ? 0.6097 0.5976 0.6276 0.0262  0.0894  0.0553  24  GLU A CD  
142  O OE1 . GLU A 24  ? 0.6235 0.5953 0.6254 0.0220  0.0932  0.0498  24  GLU A OE1 
143  O OE2 . GLU A 24  ? 0.5652 0.5658 0.5962 0.0286  0.0896  0.0610  24  GLU A OE2 
144  N N   . GLY A 25  ? 0.4466 0.4455 0.4564 0.0143  0.0504  0.0413  25  GLY A N   
145  C CA  . GLY A 25  ? 0.4103 0.4043 0.4121 0.0092  0.0435  0.0360  25  GLY A CA  
146  C C   . GLY A 25  ? 0.4513 0.4431 0.4480 0.0036  0.0395  0.0333  25  GLY A C   
147  O O   . GLY A 25  ? 0.4482 0.4420 0.4466 0.0032  0.0418  0.0348  25  GLY A O   
148  N N   . PHE A 26  ? 0.4462 0.4342 0.4370 -0.0007 0.0337  0.0297  26  PHE A N   
149  C CA  . PHE A 26  ? 0.4173 0.4053 0.4055 -0.0060 0.0286  0.0281  26  PHE A CA  
150  C C   . PHE A 26  ? 0.4522 0.4299 0.4293 -0.0093 0.0330  0.0269  26  PHE A C   
151  O O   . PHE A 26  ? 0.3859 0.3655 0.3633 -0.0120 0.0315  0.0273  26  PHE A O   
152  C CB  . PHE A 26  ? 0.4258 0.4130 0.4124 -0.0092 0.0218  0.0258  26  PHE A CB  
153  C CG  . PHE A 26  ? 0.4199 0.4165 0.4163 -0.0077 0.0170  0.0266  26  PHE A CG  
154  C CD1 . PHE A 26  ? 0.3596 0.3644 0.3630 -0.0090 0.0135  0.0277  26  PHE A CD1 
155  C CD2 . PHE A 26  ? 0.4103 0.4066 0.4076 -0.0055 0.0165  0.0260  26  PHE A CD2 
156  C CE1 . PHE A 26  ? 0.3566 0.3683 0.3668 -0.0088 0.0098  0.0281  26  PHE A CE1 
157  C CE2 . PHE A 26  ? 0.3669 0.3707 0.3716 -0.0050 0.0124  0.0265  26  PHE A CE2 
158  C CZ  . PHE A 26  ? 0.3356 0.3466 0.3461 -0.0070 0.0092  0.0274  26  PHE A CZ  
159  N N   . THR A 27  ? 0.4477 0.4135 0.4139 -0.0098 0.0385  0.0252  27  THR A N   
160  C CA  . THR A 27  ? 0.4999 0.4542 0.4528 -0.0148 0.0423  0.0236  27  THR A CA  
161  C C   . THR A 27  ? 0.4197 0.3745 0.3747 -0.0128 0.0485  0.0255  27  THR A C   
162  O O   . THR A 27  ? 0.4479 0.3977 0.3954 -0.0176 0.0489  0.0247  27  THR A O   
163  C CB  . THR A 27  ? 0.5559 0.4959 0.4953 -0.0163 0.0484  0.0213  27  THR A CB  
164  O OG1 . THR A 27  ? 0.5972 0.5383 0.5369 -0.0169 0.0431  0.0201  27  THR A OG1 
165  C CG2 . THR A 27  ? 0.5268 0.4545 0.4498 -0.0242 0.0501  0.0193  27  THR A CG2 
166  N N   . ALA A 28  ? 0.3977 0.3594 0.3636 -0.0061 0.0530  0.0286  28  ALA A N   
167  C CA  . ALA A 28  ? 0.4372 0.4009 0.4073 -0.0037 0.0591  0.0314  28  ALA A CA  
168  C C   . ALA A 28  ? 0.4233 0.3984 0.4016 -0.0056 0.0524  0.0326  28  ALA A C   
169  O O   . ALA A 28  ? 0.4141 0.3897 0.3939 -0.0052 0.0567  0.0343  28  ALA A O   
170  C CB  . ALA A 28  ? 0.4241 0.3934 0.4052 0.0041  0.0658  0.0358  28  ALA A CB  
171  N N   . MET A 29  ? 0.3498 0.3331 0.3333 -0.0076 0.0429  0.0319  29  MET A N   
172  C CA  . MET A 29  ? 0.3867 0.3807 0.3786 -0.0091 0.0373  0.0332  29  MET A CA  
173  C C   . MET A 29  ? 0.3921 0.3808 0.3760 -0.0150 0.0346  0.0312  29  MET A C   
174  O O   . MET A 29  ? 0.3848 0.3772 0.3705 -0.0182 0.0274  0.0305  29  MET A O   
175  C CB  . MET A 29  ? 0.3468 0.3505 0.3472 -0.0088 0.0298  0.0334  29  MET A CB  
176  C CG  . MET A 29  ? 0.4322 0.4425 0.4406 -0.0039 0.0311  0.0359  29  MET A CG  
177  S SD  . MET A 29  ? 0.4237 0.4402 0.4366 -0.0053 0.0228  0.0346  29  MET A SD  
178  C CE  . MET A 29  ? 0.3292 0.3557 0.3493 -0.0086 0.0178  0.0357  29  MET A CE  
179  N N   . THR A 30  ? 0.4052 0.3848 0.3802 -0.0165 0.0409  0.0308  30  THR A N   
180  C CA  . THR A 30  ? 0.3919 0.3681 0.3603 -0.0222 0.0382  0.0299  30  THR A CA  
181  C C   . THR A 30  ? 0.4169 0.4032 0.3953 -0.0212 0.0369  0.0321  30  THR A C   
182  O O   . THR A 30  ? 0.3376 0.3314 0.3257 -0.0164 0.0401  0.0346  30  THR A O   
183  C CB  . THR A 30  ? 0.4294 0.3912 0.3829 -0.0255 0.0455  0.0284  30  THR A CB  
184  O OG1 . THR A 30  ? 0.4050 0.3659 0.3617 -0.0209 0.0546  0.0302  30  THR A OG1 
185  C CG2 . THR A 30  ? 0.4115 0.3624 0.3538 -0.0273 0.0475  0.0261  30  THR A CG2 
186  N N   . VAL A 31  ? 0.3805 0.3674 0.3568 -0.0259 0.0319  0.0316  31  VAL A N   
187  C CA  . VAL A 31  ? 0.3441 0.3393 0.3283 -0.0258 0.0307  0.0334  31  VAL A CA  
188  C C   . VAL A 31  ? 0.3964 0.3891 0.3796 -0.0238 0.0389  0.0347  31  VAL A C   
189  O O   . VAL A 31  ? 0.3446 0.3465 0.3382 -0.0207 0.0403  0.0372  31  VAL A O   
190  C CB  . VAL A 31  ? 0.3272 0.3216 0.3082 -0.0313 0.0249  0.0330  31  VAL A CB  
191  C CG1 . VAL A 31  ? 0.3532 0.3529 0.3390 -0.0318 0.0255  0.0344  31  VAL A CG1 
192  C CG2 . VAL A 31  ? 0.3345 0.3342 0.3213 -0.0318 0.0177  0.0329  31  VAL A CG2 
193  N N   . ARG A 32  ? 0.4036 0.3834 0.3740 -0.0259 0.0449  0.0332  32  ARG A N   
194  C CA  . ARG A 32  ? 0.4041 0.3790 0.3724 -0.0238 0.0545  0.0344  32  ARG A CA  
195  C C   . ARG A 32  ? 0.4487 0.4300 0.4283 -0.0164 0.0601  0.0375  32  ARG A C   
196  O O   . ARG A 32  ? 0.3739 0.3621 0.3629 -0.0131 0.0640  0.0408  32  ARG A O   
197  C CB  . ARG A 32  ? 0.5331 0.4903 0.4831 -0.0281 0.0606  0.0317  32  ARG A CB  
198  C CG  . ARG A 32  ? 0.6613 0.6097 0.6060 -0.0272 0.0719  0.0323  32  ARG A CG  
199  C CD  . ARG A 32  ? 0.6194 0.5735 0.5685 -0.0286 0.0705  0.0337  32  ARG A CD  
200  N NE  . ARG A 32  ? 0.6975 0.6648 0.6639 -0.0220 0.0728  0.0377  32  ARG A NE  
201  C CZ  . ARG A 32  ? 0.6636 0.6381 0.6369 -0.0220 0.0724  0.0396  32  ARG A CZ  
202  N NH1 . ARG A 32  ? 0.5847 0.5544 0.5494 -0.0278 0.0701  0.0378  32  ARG A NH1 
203  N NH2 . ARG A 32  ? 0.6833 0.6706 0.6725 -0.0164 0.0741  0.0439  32  ARG A NH2 
204  N N   . ARG A 33  ? 0.4027 0.3826 0.3825 -0.0138 0.0604  0.0370  33  ARG A N   
205  C CA  . ARG A 33  ? 0.3934 0.3801 0.3846 -0.0067 0.0652  0.0409  33  ARG A CA  
206  C C   . ARG A 33  ? 0.3937 0.3986 0.4014 -0.0046 0.0590  0.0446  33  ARG A C   
207  O O   . ARG A 33  ? 0.3609 0.3742 0.3797 -0.0003 0.0634  0.0495  33  ARG A O   
208  C CB  . ARG A 33  ? 0.4753 0.4573 0.4630 -0.0051 0.0652  0.0394  33  ARG A CB  
209  C CG  . ARG A 33  ? 0.4626 0.4519 0.4622 0.0021  0.0697  0.0439  33  ARG A CG  
210  C CD  . ARG A 33  ? 0.5002 0.4807 0.4981 0.0064  0.0831  0.0465  33  ARG A CD  
211  N NE  . ARG A 33  ? 0.5812 0.5725 0.5946 0.0137  0.0868  0.0529  33  ARG A NE  
212  C CZ  . ARG A 33  ? 0.5518 0.5414 0.5664 0.0175  0.0892  0.0539  33  ARG A CZ  
213  N NH1 . ARG A 33  ? 0.4631 0.4399 0.4641 0.0147  0.0888  0.0486  33  ARG A NH1 
214  N NH2 . ARG A 33  ? 0.5301 0.5316 0.5604 0.0240  0.0919  0.0610  33  ARG A NH2 
215  N N   . ILE A 34  ? 0.3524 0.3633 0.3617 -0.0080 0.0491  0.0427  34  ILE A N   
216  C CA  . ILE A 34  ? 0.3285 0.3547 0.3508 -0.0074 0.0433  0.0455  34  ILE A CA  
217  C C   . ILE A 34  ? 0.2727 0.3051 0.3003 -0.0084 0.0444  0.0479  34  ILE A C   
218  O O   . ILE A 34  ? 0.3160 0.3608 0.3555 -0.0063 0.0444  0.0526  34  ILE A O   
219  C CB  . ILE A 34  ? 0.3225 0.3505 0.3433 -0.0113 0.0341  0.0424  34  ILE A CB  
220  C CG1 . ILE A 34  ? 0.3185 0.3434 0.3372 -0.0095 0.0330  0.0411  34  ILE A CG1 
221  C CG2 . ILE A 34  ? 0.3267 0.3679 0.3577 -0.0127 0.0286  0.0445  34  ILE A CG2 
222  C CD1 . ILE A 34  ? 0.3459 0.3685 0.3608 -0.0133 0.0258  0.0376  34  ILE A CD1 
223  N N   . ALA A 35  ? 0.2958 0.3203 0.3148 -0.0122 0.0451  0.0452  35  ALA A N   
224  C CA  . ALA A 35  ? 0.3141 0.3432 0.3371 -0.0133 0.0466  0.0472  35  ALA A CA  
225  C C   . ALA A 35  ? 0.3872 0.4185 0.4166 -0.0083 0.0558  0.0518  35  ALA A C   
226  O O   . ALA A 35  ? 0.3416 0.3846 0.3822 -0.0071 0.0559  0.0561  35  ALA A O   
227  C CB  . ALA A 35  ? 0.3564 0.3748 0.3674 -0.0182 0.0464  0.0437  35  ALA A CB  
228  N N   . THR A 36  ? 0.3784 0.3982 0.4009 -0.0055 0.0641  0.0514  36  THR A N   
229  C CA  . THR A 36  ? 0.4074 0.4281 0.4369 0.0001  0.0745  0.0564  36  THR A CA  
230  C C   . THR A 36  ? 0.3610 0.3981 0.4075 0.0048  0.0728  0.0628  36  THR A C   
231  O O   . THR A 36  ? 0.3854 0.4334 0.4445 0.0075  0.0759  0.0689  36  THR A O   
232  C CB  . THR A 36  ? 0.4367 0.4401 0.4543 0.0018  0.0842  0.0543  36  THR A CB  
233  O OG1 . THR A 36  ? 0.4541 0.4427 0.4548 -0.0040 0.0854  0.0490  36  THR A OG1 
234  C CG2 . THR A 36  ? 0.4560 0.4592 0.4816 0.0084  0.0967  0.0601  36  THR A CG2 
235  N N   . GLU A 37  ? 0.4304 0.4703 0.4778 0.0053  0.0675  0.0619  37  GLU A N   
236  C CA  . GLU A 37  ? 0.3544 0.4096 0.4167 0.0091  0.0655  0.0682  37  GLU A CA  
237  C C   . GLU A 37  ? 0.4119 0.4835 0.4842 0.0056  0.0572  0.0710  37  GLU A C   
238  O O   . GLU A 37  ? 0.3566 0.4428 0.4430 0.0081  0.0575  0.0785  37  GLU A O   
239  C CB  . GLU A 37  ? 0.4061 0.4588 0.4649 0.0096  0.0615  0.0658  37  GLU A CB  
240  C CG  . GLU A 37  ? 0.6041 0.6446 0.6576 0.0144  0.0709  0.0658  37  GLU A CG  
241  C CD  . GLU A 37  ? 0.6696 0.7182 0.7372 0.0215  0.0790  0.0745  37  GLU A CD  
242  O OE1 . GLU A 37  ? 0.8165 0.8802 0.8967 0.0232  0.0743  0.0800  37  GLU A OE1 
243  O OE2 . GLU A 37  ? 0.7913 0.8311 0.8574 0.0250  0.0904  0.0763  37  GLU A OE2 
244  N N   . ALA A 38  ? 0.3384 0.4081 0.4038 -0.0004 0.0499  0.0657  38  ALA A N   
245  C CA  . ALA A 38  ? 0.3377 0.4204 0.4103 -0.0046 0.0429  0.0676  38  ALA A CA  
246  C C   . ALA A 38  ? 0.3702 0.4565 0.4470 -0.0051 0.0466  0.0704  38  ALA A C   
247  O O   . ALA A 38  ? 0.3275 0.4251 0.4106 -0.0088 0.0416  0.0725  38  ALA A O   
248  C CB  . ALA A 38  ? 0.3055 0.3837 0.3694 -0.0104 0.0349  0.0611  38  ALA A CB  
249  N N   . GLN A 39  ? 0.3542 0.4304 0.4267 -0.0020 0.0556  0.0702  39  GLN A N   
250  C CA  . GLN A 39  ? 0.3378 0.4142 0.4120 -0.0027 0.0600  0.0718  39  GLN A CA  
251  C C   . GLN A 39  ? 0.3618 0.4377 0.4300 -0.0093 0.0529  0.0672  39  GLN A C   
252  O O   . GLN A 39  ? 0.3406 0.4264 0.4158 -0.0116 0.0507  0.0699  39  GLN A O   
253  C CB  . GLN A 39  ? 0.3549 0.4474 0.4461 0.0006  0.0630  0.0809  39  GLN A CB  
254  C CG  . GLN A 39  ? 0.3912 0.4863 0.4912 0.0077  0.0703  0.0871  39  GLN A CG  
255  C CD  . GLN A 39  ? 0.5706 0.6847 0.6898 0.0104  0.0718  0.0978  39  GLN A CD  
256  O OE1 . GLN A 39  ? 0.6056 0.7218 0.7307 0.0121  0.0783  0.1018  39  GLN A OE1 
257  N NE2 . GLN A 39  ? 0.5107 0.6391 0.6398 0.0103  0.0657  0.1029  39  GLN A NE2 
258  N N   . THR A 40  ? 0.3576 0.4218 0.4131 -0.0123 0.0494  0.0606  40  THR A N   
259  C CA  . THR A 40  ? 0.3032 0.3647 0.3526 -0.0179 0.0440  0.0566  40  THR A CA  
260  C C   . THR A 40  ? 0.4100 0.4553 0.4451 -0.0196 0.0468  0.0519  40  THR A C   
261  O O   . THR A 40  ? 0.3432 0.3792 0.3726 -0.0168 0.0536  0.0517  40  THR A O   
262  C CB  . THR A 40  ? 0.3265 0.3930 0.3768 -0.0214 0.0350  0.0545  40  THR A CB  
263  O OG1 . THR A 40  ? 0.3252 0.3908 0.3722 -0.0264 0.0309  0.0520  40  THR A OG1 
264  C CG2 . THR A 40  ? 0.3010 0.3587 0.3437 -0.0208 0.0332  0.0508  40  THR A CG2 
265  N N   . SER A 41  ? 0.3210 0.3626 0.3497 -0.0245 0.0418  0.0487  41  SER A N   
266  C CA  . SER A 41  ? 0.3347 0.3626 0.3499 -0.0274 0.0427  0.0451  41  SER A CA  
267  C C   . SER A 41  ? 0.3145 0.3380 0.3243 -0.0290 0.0370  0.0423  41  SER A C   
268  O O   . SER A 41  ? 0.3015 0.3323 0.3176 -0.0291 0.0314  0.0423  41  SER A O   
269  C CB  . SER A 41  ? 0.3161 0.3430 0.3284 -0.0318 0.0407  0.0443  41  SER A CB  
270  O OG  . SER A 41  ? 0.2904 0.3239 0.3074 -0.0343 0.0332  0.0438  41  SER A OG  
271  N N   . THR A 42  ? 0.3151 0.3265 0.3129 -0.0308 0.0389  0.0401  42  THR A N   
272  C CA  . THR A 42  ? 0.2968 0.3045 0.2896 -0.0332 0.0330  0.0380  42  THR A CA  
273  C C   . THR A 42  ? 0.3279 0.3395 0.3232 -0.0369 0.0260  0.0380  42  THR A C   
274  O O   . THR A 42  ? 0.3150 0.3290 0.3132 -0.0373 0.0208  0.0375  42  THR A O   
275  C CB  . THR A 42  ? 0.3966 0.3906 0.3748 -0.0362 0.0357  0.0362  42  THR A CB  
276  O OG1 . THR A 42  ? 0.3710 0.3588 0.3411 -0.0403 0.0379  0.0361  42  THR A OG1 
277  C CG2 . THR A 42  ? 0.3785 0.3670 0.3537 -0.0323 0.0434  0.0360  42  THR A CG2 
278  N N   . GLY A 43  ? 0.3419 0.3539 0.3367 -0.0393 0.0267  0.0387  43  GLY A N   
279  C CA  . GLY A 43  ? 0.3518 0.3674 0.3498 -0.0423 0.0211  0.0391  43  GLY A CA  
280  C C   . GLY A 43  ? 0.2996 0.3246 0.3084 -0.0406 0.0180  0.0394  43  GLY A C   
281  O O   . GLY A 43  ? 0.3073 0.3328 0.3180 -0.0422 0.0135  0.0392  43  GLY A O   
282  N N   . GLN A 44  ? 0.2725 0.3047 0.2880 -0.0378 0.0206  0.0404  44  GLN A N   
283  C CA  . GLN A 44  ? 0.3040 0.3448 0.3279 -0.0377 0.0173  0.0407  44  GLN A CA  
284  C C   . GLN A 44  ? 0.2761 0.3165 0.3006 -0.0361 0.0150  0.0398  44  GLN A C   
285  O O   . GLN A 44  ? 0.2899 0.3334 0.3179 -0.0375 0.0115  0.0391  44  GLN A O   
286  C CB  . GLN A 44  ? 0.2889 0.3393 0.3204 -0.0364 0.0197  0.0432  44  GLN A CB  
287  C CG  . GLN A 44  ? 0.3178 0.3706 0.3506 -0.0390 0.0207  0.0441  44  GLN A CG  
288  C CD  . GLN A 44  ? 0.3727 0.4250 0.4053 -0.0432 0.0164  0.0427  44  GLN A CD  
289  O OE1 . GLN A 44  ? 0.4025 0.4609 0.4398 -0.0450 0.0141  0.0428  44  GLN A OE1 
290  N NE2 . GLN A 44  ? 0.4299 0.4747 0.4568 -0.0451 0.0159  0.0416  44  GLN A NE2 
291  N N   . VAL A 45  ? 0.2338 0.2693 0.2540 -0.0334 0.0173  0.0394  45  VAL A N   
292  C CA  . VAL A 45  ? 0.2492 0.2833 0.2691 -0.0321 0.0150  0.0382  45  VAL A CA  
293  C C   . VAL A 45  ? 0.2686 0.2977 0.2853 -0.0350 0.0107  0.0369  45  VAL A C   
294  O O   . VAL A 45  ? 0.2668 0.2977 0.2869 -0.0352 0.0077  0.0363  45  VAL A O   
295  C CB  . VAL A 45  ? 0.2963 0.3250 0.3113 -0.0291 0.0190  0.0380  45  VAL A CB  
296  C CG1 . VAL A 45  ? 0.3115 0.3386 0.3260 -0.0279 0.0164  0.0368  45  VAL A CG1 
297  C CG2 . VAL A 45  ? 0.2826 0.3167 0.3030 -0.0254 0.0242  0.0406  45  VAL A CG2 
298  N N   . HIS A 46  ? 0.2988 0.3217 0.3091 -0.0374 0.0107  0.0370  46  HIS A N   
299  C CA  . HIS A 46  ? 0.3357 0.3551 0.3445 -0.0402 0.0067  0.0374  46  HIS A CA  
300  C C   . HIS A 46  ? 0.3499 0.3734 0.3653 -0.0416 0.0047  0.0380  46  HIS A C   
301  O O   . HIS A 46  ? 0.3689 0.3910 0.3867 -0.0424 0.0021  0.0386  46  HIS A O   
302  C CB  . HIS A 46  ? 0.3659 0.3788 0.3663 -0.0434 0.0067  0.0384  46  HIS A CB  
303  C CG  . HIS A 46  ? 0.3713 0.3776 0.3628 -0.0436 0.0085  0.0376  46  HIS A CG  
304  N ND1 . HIS A 46  ? 0.3635 0.3679 0.3540 -0.0428 0.0066  0.0370  46  HIS A ND1 
305  C CD2 . HIS A 46  ? 0.3825 0.3822 0.3645 -0.0450 0.0125  0.0370  46  HIS A CD2 
306  C CE1 . HIS A 46  ? 0.3785 0.3757 0.3591 -0.0439 0.0093  0.0361  46  HIS A CE1 
307  N NE2 . HIS A 46  ? 0.3743 0.3679 0.3492 -0.0453 0.0132  0.0360  46  HIS A NE2 
308  N N   . HIS A 47  ? 0.3510 0.3789 0.3694 -0.0420 0.0064  0.0381  47  HIS A N   
309  C CA  . HIS A 47  ? 0.3362 0.3667 0.3594 -0.0441 0.0053  0.0383  47  HIS A CA  
310  C C   . HIS A 47  ? 0.3968 0.4300 0.4243 -0.0436 0.0043  0.0371  47  HIS A C   
311  O O   . HIS A 47  ? 0.3643 0.3954 0.3938 -0.0453 0.0036  0.0370  47  HIS A O   
312  C CB  . HIS A 47  ? 0.3886 0.4234 0.4134 -0.0453 0.0074  0.0388  47  HIS A CB  
313  C CG  . HIS A 47  ? 0.4301 0.4678 0.4591 -0.0479 0.0070  0.0385  47  HIS A CG  
314  N ND1 . HIS A 47  ? 0.4603 0.4941 0.4894 -0.0502 0.0066  0.0391  47  HIS A ND1 
315  C CD2 . HIS A 47  ? 0.4574 0.5011 0.4899 -0.0491 0.0071  0.0380  47  HIS A CD2 
316  C CE1 . HIS A 47  ? 0.5416 0.5776 0.5734 -0.0527 0.0073  0.0383  47  HIS A CE1 
317  N NE2 . HIS A 47  ? 0.5532 0.5953 0.5865 -0.0526 0.0072  0.0375  47  HIS A NE2 
318  N N   . HIS A 48  ? 0.2954 0.3324 0.3239 -0.0415 0.0048  0.0365  48  HIS A N   
319  C CA  . HIS A 48  ? 0.3477 0.3878 0.3792 -0.0419 0.0037  0.0356  48  HIS A CA  
320  C C   . HIS A 48  ? 0.3182 0.3538 0.3486 -0.0403 0.0024  0.0345  48  HIS A C   
321  O O   . HIS A 48  ? 0.3323 0.3683 0.3642 -0.0414 0.0016  0.0335  48  HIS A O   
322  C CB  . HIS A 48  ? 0.3041 0.3523 0.3384 -0.0406 0.0045  0.0366  48  HIS A CB  
323  C CG  . HIS A 48  ? 0.3759 0.4305 0.4131 -0.0431 0.0053  0.0381  48  HIS A CG  
324  N ND1 . HIS A 48  ? 0.4523 0.5082 0.4903 -0.0477 0.0043  0.0374  48  HIS A ND1 
325  C CD2 . HIS A 48  ? 0.3940 0.4537 0.4335 -0.0419 0.0075  0.0403  48  HIS A CD2 
326  C CE1 . HIS A 48  ? 0.4246 0.4870 0.4652 -0.0496 0.0051  0.0392  48  HIS A CE1 
327  N NE2 . HIS A 48  ? 0.3580 0.4232 0.4002 -0.0458 0.0070  0.0411  48  HIS A NE2 
328  N N   . PHE A 49  ? 0.2911 0.3224 0.3182 -0.0384 0.0021  0.0349  49  PHE A N   
329  C CA  . PHE A 49  ? 0.3402 0.3679 0.3663 -0.0369 0.0008  0.0342  49  PHE A CA  
330  C C   . PHE A 49  ? 0.3448 0.3669 0.3685 -0.0378 -0.0005 0.0355  49  PHE A C   
331  O O   . PHE A 49  ? 0.3459 0.3662 0.3655 -0.0386 -0.0002 0.0366  49  PHE A O   
332  C CB  . PHE A 49  ? 0.3212 0.3502 0.3454 -0.0339 0.0019  0.0337  49  PHE A CB  
333  C CG  . PHE A 49  ? 0.3027 0.3388 0.3307 -0.0330 0.0027  0.0339  49  PHE A CG  
334  C CD1 . PHE A 49  ? 0.3129 0.3509 0.3431 -0.0332 0.0013  0.0330  49  PHE A CD1 
335  C CD2 . PHE A 49  ? 0.3063 0.3478 0.3362 -0.0325 0.0048  0.0355  49  PHE A CD2 
336  C CE1 . PHE A 49  ? 0.3196 0.3652 0.3531 -0.0334 0.0012  0.0341  49  PHE A CE1 
337  C CE2 . PHE A 49  ? 0.2961 0.3460 0.3308 -0.0322 0.0049  0.0370  49  PHE A CE2 
338  C CZ  . PHE A 49  ? 0.2992 0.3515 0.3356 -0.0329 0.0028  0.0365  49  PHE A CZ  
339  N N   . SER A 50  ? 0.3570 0.3765 0.3834 -0.0379 -0.0018 0.0360  50  SER A N   
340  C CA  . SER A 50  ? 0.4174 0.4335 0.4440 -0.0392 -0.0035 0.0388  50  SER A CA  
341  C C   . SER A 50  ? 0.4114 0.4251 0.4318 -0.0394 -0.0050 0.0396  50  SER A C   
342  O O   . SER A 50  ? 0.4297 0.4417 0.4480 -0.0418 -0.0068 0.0426  50  SER A O   
343  C CB  . SER A 50  ? 0.3891 0.4030 0.4211 -0.0388 -0.0037 0.0398  50  SER A CB  
344  O OG  . SER A 50  ? 0.5262 0.5404 0.5614 -0.0392 -0.0014 0.0381  50  SER A OG  
345  N N   . SER A 51  ? 0.3266 0.3399 0.3437 -0.0374 -0.0042 0.0372  51  SER A N   
346  C CA  . SER A 51  ? 0.3336 0.3429 0.3431 -0.0381 -0.0046 0.0373  51  SER A CA  
347  C C   . SER A 51  ? 0.3335 0.3428 0.3402 -0.0351 -0.0017 0.0346  51  SER A C   
348  O O   . SER A 51  ? 0.3182 0.3315 0.3299 -0.0326 -0.0007 0.0333  51  SER A O   
349  C CB  . SER A 51  ? 0.4048 0.4119 0.4148 -0.0392 -0.0076 0.0393  51  SER A CB  
350  O OG  . SER A 51  ? 0.3774 0.3849 0.3905 -0.0364 -0.0073 0.0374  51  SER A OG  
351  N N   . ALA A 52  ? 0.3177 0.3220 0.3159 -0.0357 -0.0001 0.0341  52  ALA A N   
352  C CA  . ALA A 52  ? 0.3352 0.3385 0.3312 -0.0324 0.0036  0.0321  52  ALA A CA  
353  C C   . ALA A 52  ? 0.3413 0.3461 0.3413 -0.0299 0.0022  0.0312  52  ALA A C   
354  O O   . ALA A 52  ? 0.3007 0.3087 0.3039 -0.0265 0.0042  0.0303  52  ALA A O   
355  C CB  . ALA A 52  ? 0.3224 0.3174 0.3069 -0.0342 0.0066  0.0315  52  ALA A CB  
356  N N   . SER A 53  ? 0.3170 0.3198 0.3171 -0.0317 -0.0013 0.0318  53  SER A N   
357  C CA  . SER A 53  ? 0.3626 0.3661 0.3663 -0.0295 -0.0024 0.0309  53  SER A CA  
358  C C   . SER A 53  ? 0.3461 0.3550 0.3581 -0.0280 -0.0029 0.0305  53  SER A C   
359  O O   . SER A 53  ? 0.2791 0.2895 0.2933 -0.0258 -0.0024 0.0291  53  SER A O   
360  C CB  . SER A 53  ? 0.3904 0.3909 0.3932 -0.0320 -0.0057 0.0325  53  SER A CB  
361  O OG  . SER A 53  ? 0.4742 0.4692 0.4681 -0.0334 -0.0051 0.0319  53  SER A OG  
362  N N   . HIS A 54  ? 0.2596 0.2706 0.2754 -0.0299 -0.0037 0.0317  54  HIS A N   
363  C CA  . HIS A 54  ? 0.2780 0.2929 0.2996 -0.0297 -0.0033 0.0310  54  HIS A CA  
364  C C   . HIS A 54  ? 0.3105 0.3302 0.3323 -0.0280 -0.0016 0.0300  54  HIS A C   
365  O O   . HIS A 54  ? 0.3276 0.3501 0.3520 -0.0276 -0.0018 0.0292  54  HIS A O   
366  C CB  . HIS A 54  ? 0.3087 0.3243 0.3331 -0.0322 -0.0035 0.0325  54  HIS A CB  
367  C CG  . HIS A 54  ? 0.3476 0.3600 0.3755 -0.0333 -0.0047 0.0344  54  HIS A CG  
368  N ND1 . HIS A 54  ? 0.3932 0.4034 0.4199 -0.0344 -0.0066 0.0372  54  HIS A ND1 
369  C CD2 . HIS A 54  ? 0.3462 0.3572 0.3791 -0.0338 -0.0037 0.0346  54  HIS A CD2 
370  C CE1 . HIS A 54  ? 0.3608 0.3698 0.3934 -0.0348 -0.0069 0.0398  54  HIS A CE1 
371  N NE2 . HIS A 54  ? 0.4272 0.4357 0.4635 -0.0342 -0.0046 0.0380  54  HIS A NE2 
372  N N   . LEU A 55  ? 0.2635 0.2843 0.2828 -0.0274 0.0003  0.0307  55  LEU A N   
373  C CA  . LEU A 55  ? 0.2661 0.2925 0.2874 -0.0253 0.0025  0.0313  55  LEU A CA  
374  C C   . LEU A 55  ? 0.2899 0.3163 0.3109 -0.0222 0.0033  0.0309  55  LEU A C   
375  O O   . LEU A 55  ? 0.2667 0.2993 0.2919 -0.0212 0.0033  0.0319  55  LEU A O   
376  C CB  . LEU A 55  ? 0.2603 0.2859 0.2788 -0.0249 0.0055  0.0324  55  LEU A CB  
377  C CG  . LEU A 55  ? 0.3137 0.3454 0.3357 -0.0224 0.0089  0.0343  55  LEU A CG  
378  C CD1 . LEU A 55  ? 0.3312 0.3722 0.3604 -0.0230 0.0069  0.0356  55  LEU A CD1 
379  C CD2 . LEU A 55  ? 0.3023 0.3330 0.3224 -0.0232 0.0118  0.0353  55  LEU A CD2 
380  N N   . LYS A 56  ? 0.2890 0.3088 0.3047 -0.0213 0.0040  0.0300  56  LYS A N   
381  C CA  . LYS A 56  ? 0.2639 0.2826 0.2787 -0.0182 0.0052  0.0295  56  LYS A CA  
382  C C   . LYS A 56  ? 0.2575 0.2789 0.2762 -0.0185 0.0023  0.0288  56  LYS A C   
383  O O   . LYS A 56  ? 0.2525 0.2781 0.2739 -0.0165 0.0028  0.0294  56  LYS A O   
384  C CB  . LYS A 56  ? 0.3106 0.3206 0.3177 -0.0185 0.0062  0.0283  56  LYS A CB  
385  C CG  . LYS A 56  ? 0.3428 0.3479 0.3435 -0.0180 0.0109  0.0287  56  LYS A CG  
386  C CD  . LYS A 56  ? 0.3850 0.3806 0.3759 -0.0206 0.0111  0.0274  56  LYS A CD  
387  C CE  . LYS A 56  ? 0.4114 0.4000 0.3934 -0.0219 0.0161  0.0273  56  LYS A CE  
388  N NZ  . LYS A 56  ? 0.4389 0.4175 0.4092 -0.0260 0.0162  0.0260  56  LYS A NZ  
389  N N   . ALA A 57  ? 0.2539 0.2728 0.2732 -0.0211 -0.0003 0.0278  57  ALA A N   
390  C CA  . ALA A 57  ? 0.2742 0.2934 0.2960 -0.0218 -0.0020 0.0267  57  ALA A CA  
391  C C   . ALA A 57  ? 0.2765 0.3021 0.3018 -0.0235 -0.0024 0.0272  57  ALA A C   
392  O O   . ALA A 57  ? 0.2775 0.3052 0.3035 -0.0237 -0.0030 0.0268  57  ALA A O   
393  C CB  . ALA A 57  ? 0.2541 0.2685 0.2767 -0.0240 -0.0034 0.0264  57  ALA A CB  
394  N N   . GLU A 58  ? 0.2688 0.2974 0.2955 -0.0255 -0.0021 0.0281  58  GLU A N   
395  C CA  . GLU A 58  ? 0.3011 0.3362 0.3304 -0.0282 -0.0027 0.0289  58  GLU A CA  
396  C C   . GLU A 58  ? 0.2968 0.3396 0.3284 -0.0262 -0.0025 0.0313  58  GLU A C   
397  O O   . GLU A 58  ? 0.2834 0.3310 0.3162 -0.0284 -0.0040 0.0321  58  GLU A O   
398  C CB  . GLU A 58  ? 0.3410 0.3778 0.3713 -0.0306 -0.0023 0.0297  58  GLU A CB  
399  C CG  . GLU A 58  ? 0.5239 0.5658 0.5556 -0.0350 -0.0031 0.0301  58  GLU A CG  
400  C CD  . GLU A 58  ? 0.4496 0.4891 0.4811 -0.0383 -0.0024 0.0296  58  GLU A CD  
401  O OE1 . GLU A 58  ? 0.4873 0.5216 0.5182 -0.0369 -0.0016 0.0293  58  GLU A OE1 
402  O OE2 . GLU A 58  ? 0.5300 0.5730 0.5616 -0.0426 -0.0027 0.0298  58  GLU A OE2 
403  N N   . ALA A 59  ? 0.2834 0.3271 0.3154 -0.0223 -0.0002 0.0330  59  ALA A N   
404  C CA  . ALA A 59  ? 0.2672 0.3181 0.3030 -0.0193 0.0012  0.0364  59  ALA A CA  
405  C C   . ALA A 59  ? 0.2937 0.3437 0.3289 -0.0176 0.0004  0.0360  59  ALA A C   
406  O O   . ALA A 59  ? 0.2760 0.3337 0.3150 -0.0176 -0.0006 0.0391  59  ALA A O   
407  C CB  . ALA A 59  ? 0.2555 0.3045 0.2909 -0.0153 0.0056  0.0379  59  ALA A CB  
408  N N   . PHE A 60  ? 0.2604 0.3014 0.2908 -0.0165 0.0006  0.0328  60  PHE A N   
409  C CA  . PHE A 60  ? 0.2739 0.3131 0.3032 -0.0150 -0.0001 0.0321  60  PHE A CA  
410  C C   . PHE A 60  ? 0.2696 0.3121 0.2998 -0.0190 -0.0032 0.0317  60  PHE A C   
411  O O   . PHE A 60  ? 0.3117 0.3591 0.3435 -0.0187 -0.0041 0.0336  60  PHE A O   
412  C CB  . PHE A 60  ? 0.2288 0.2580 0.2531 -0.0141 0.0003  0.0289  60  PHE A CB  
413  C CG  . PHE A 60  ? 0.3273 0.3537 0.3502 -0.0133 -0.0007 0.0275  60  PHE A CG  
414  C CD1 . PHE A 60  ? 0.3176 0.3454 0.3408 -0.0097 0.0010  0.0289  60  PHE A CD1 
415  C CD2 . PHE A 60  ? 0.3449 0.3669 0.3666 -0.0160 -0.0026 0.0250  60  PHE A CD2 
416  C CE1 . PHE A 60  ? 0.3680 0.3931 0.3897 -0.0090 0.0001  0.0276  60  PHE A CE1 
417  C CE2 . PHE A 60  ? 0.2901 0.3091 0.3105 -0.0154 -0.0031 0.0237  60  PHE A CE2 
418  C CZ  . PHE A 60  ? 0.3043 0.3250 0.3244 -0.0120 -0.0021 0.0248  60  PHE A CZ  
419  N N   . LEU A 61  ? 0.2788 0.3182 0.3075 -0.0233 -0.0045 0.0295  61  LEU A N   
420  C CA  . LEU A 61  ? 0.3169 0.3569 0.3442 -0.0282 -0.0064 0.0286  61  LEU A CA  
421  C C   . LEU A 61  ? 0.3544 0.4053 0.3845 -0.0310 -0.0081 0.0322  61  LEU A C   
422  O O   . LEU A 61  ? 0.3369 0.3910 0.3659 -0.0338 -0.0100 0.0332  61  LEU A O   
423  C CB  . LEU A 61  ? 0.3306 0.3641 0.3559 -0.0320 -0.0059 0.0258  61  LEU A CB  
424  C CG  . LEU A 61  ? 0.3842 0.4080 0.4080 -0.0302 -0.0048 0.0233  61  LEU A CG  
425  C CD1 . LEU A 61  ? 0.4070 0.4250 0.4307 -0.0331 -0.0034 0.0221  61  LEU A CD1 
426  C CD2 . LEU A 61  ? 0.3682 0.3885 0.3896 -0.0304 -0.0050 0.0218  61  LEU A CD2 
427  N N   . LYS A 62  ? 0.3460 0.4030 0.3797 -0.0307 -0.0076 0.0349  62  LYS A N   
428  C CA  . LYS A 62  ? 0.3157 0.3847 0.3535 -0.0334 -0.0093 0.0396  62  LYS A CA  
429  C C   . LYS A 62  ? 0.3386 0.4148 0.3806 -0.0297 -0.0096 0.0440  62  LYS A C   
430  O O   . LYS A 62  ? 0.3111 0.3958 0.3547 -0.0335 -0.0125 0.0476  62  LYS A O   
431  C CB  . LYS A 62  ? 0.3249 0.3988 0.3669 -0.0324 -0.0079 0.0420  62  LYS A CB  
432  C CG  . LYS A 62  ? 0.4736 0.5466 0.5133 -0.0386 -0.0089 0.0403  62  LYS A CG  
433  C CD  . LYS A 62  ? 0.5419 0.6242 0.5821 -0.0454 -0.0121 0.0433  62  LYS A CD  
434  C CE  . LYS A 62  ? 0.6403 0.7333 0.6864 -0.0465 -0.0124 0.0480  62  LYS A CE  
435  N NZ  . LYS A 62  ? 0.7105 0.8160 0.7590 -0.0526 -0.0162 0.0531  62  LYS A NZ  
436  N N   . LEU A 63  ? 0.2859 0.3584 0.3292 -0.0229 -0.0065 0.0440  63  LEU A N   
437  C CA  . LEU A 63  ? 0.3144 0.3927 0.3621 -0.0186 -0.0056 0.0485  63  LEU A CA  
438  C C   . LEU A 63  ? 0.3705 0.4466 0.4145 -0.0206 -0.0082 0.0470  63  LEU A C   
439  O O   . LEU A 63  ? 0.3323 0.4167 0.3803 -0.0201 -0.0095 0.0519  63  LEU A O   
440  C CB  . LEU A 63  ? 0.2944 0.3666 0.3423 -0.0114 -0.0005 0.0482  63  LEU A CB  
441  C CG  . LEU A 63  ? 0.3068 0.3830 0.3595 -0.0087 0.0033  0.0516  63  LEU A CG  
442  C CD1 . LEU A 63  ? 0.3156 0.3815 0.3645 -0.0035 0.0089  0.0493  63  LEU A CD1 
443  C CD2 . LEU A 63  ? 0.3057 0.3958 0.3684 -0.0069 0.0039  0.0598  63  LEU A CD2 
444  N N   . MET A 64  ? 0.3480 0.4135 0.3851 -0.0230 -0.0089 0.0410  64  MET A N   
445  C CA  . MET A 64  ? 0.4088 0.4709 0.4417 -0.0251 -0.0107 0.0392  64  MET A CA  
446  C C   . MET A 64  ? 0.4723 0.5404 0.5033 -0.0330 -0.0144 0.0408  64  MET A C   
447  O O   . MET A 64  ? 0.4161 0.4879 0.4462 -0.0350 -0.0166 0.0429  64  MET A O   
448  C CB  . MET A 64  ? 0.4380 0.4870 0.4652 -0.0250 -0.0095 0.0330  64  MET A CB  
449  C CG  . MET A 64  ? 0.3074 0.3502 0.3345 -0.0185 -0.0066 0.0317  64  MET A CG  
450  S SD  . MET A 64  ? 0.4082 0.4548 0.4379 -0.0127 -0.0051 0.0352  64  MET A SD  
451  C CE  . MET A 64  ? 0.3932 0.4454 0.4284 -0.0080 -0.0015 0.0396  64  MET A CE  
452  N N   . GLU A 65  ? 0.4136 0.4825 0.4433 -0.0384 -0.0152 0.0399  65  GLU A N   
453  C CA  . GLU A 65  ? 0.4888 0.5640 0.5157 -0.0471 -0.0186 0.0420  65  GLU A CA  
454  C C   . GLU A 65  ? 0.4506 0.5418 0.4851 -0.0469 -0.0213 0.0503  65  GLU A C   
455  O O   . GLU A 65  ? 0.5005 0.5983 0.5331 -0.0530 -0.0250 0.0536  65  GLU A O   
456  C CB  . GLU A 65  ? 0.4578 0.5303 0.4819 -0.0526 -0.0182 0.0397  65  GLU A CB  
457  C CG  . GLU A 65  ? 0.5213 0.5802 0.5421 -0.0503 -0.0147 0.0336  65  GLU A CG  
458  C CD  . GLU A 65  ? 0.8357 0.8875 0.8500 -0.0578 -0.0137 0.0301  65  GLU A CD  
459  O OE1 . GLU A 65  ? 0.9972 1.0553 1.0097 -0.0648 -0.0158 0.0322  65  GLU A OE1 
460  O OE2 . GLU A 65  ? 0.7832 0.8230 0.7944 -0.0569 -0.0106 0.0256  65  GLU A OE2 
461  N N   . GLN A 66  ? 0.4281 0.5256 0.4712 -0.0401 -0.0192 0.0542  66  GLN A N   
462  C CA  . GLN A 66  ? 0.4537 0.5666 0.5065 -0.0382 -0.0204 0.0632  66  GLN A CA  
463  C C   . GLN A 66  ? 0.4801 0.5948 0.5341 -0.0351 -0.0210 0.0660  66  GLN A C   
464  O O   . GLN A 66  ? 0.4546 0.5820 0.5133 -0.0380 -0.0245 0.0733  66  GLN A O   
465  C CB  . GLN A 66  ? 0.4219 0.5378 0.4830 -0.0306 -0.0160 0.0660  66  GLN A CB  
466  C CG  . GLN A 66  ? 0.4744 0.6067 0.5474 -0.0284 -0.0162 0.0763  66  GLN A CG  
467  C CD  . GLN A 66  ? 0.4132 0.5469 0.4931 -0.0224 -0.0111 0.0784  66  GLN A CD  
468  O OE1 . GLN A 66  ? 0.4310 0.5610 0.5144 -0.0142 -0.0055 0.0795  66  GLN A OE1 
469  N NE2 . GLN A 66  ? 0.4434 0.5813 0.5242 -0.0269 -0.0124 0.0788  66  GLN A NE2 
470  N N   . LEU A 67  ? 0.4296 0.5324 0.4796 -0.0297 -0.0179 0.0607  67  LEU A N   
471  C CA  . LEU A 67  ? 0.4449 0.5479 0.4951 -0.0270 -0.0183 0.0625  67  LEU A CA  
472  C C   . LEU A 67  ? 0.4539 0.5574 0.4970 -0.0357 -0.0232 0.0617  67  LEU A C   
473  O O   . LEU A 67  ? 0.4994 0.6115 0.5451 -0.0370 -0.0259 0.0675  67  LEU A O   
474  C CB  . LEU A 67  ? 0.4535 0.5426 0.4996 -0.0205 -0.0141 0.0564  67  LEU A CB  
475  C CG  . LEU A 67  ? 0.4973 0.5808 0.5390 -0.0195 -0.0145 0.0545  67  LEU A CG  
476  C CD1 . LEU A 67  ? 0.5380 0.6327 0.5869 -0.0165 -0.0150 0.0627  67  LEU A CD1 
477  C CD2 . LEU A 67  ? 0.5197 0.5896 0.5573 -0.0139 -0.0104 0.0484  67  LEU A CD2 
478  N N   . ASP A 68  ? 0.4749 0.5687 0.5087 -0.0422 -0.0239 0.0550  68  ASP A N   
479  C CA  . ASP A 68  ? 0.4707 0.5631 0.4957 -0.0520 -0.0276 0.0537  68  ASP A CA  
480  C C   . ASP A 68  ? 0.5841 0.6925 0.6123 -0.0591 -0.0326 0.0618  68  ASP A C   
481  O O   . ASP A 68  ? 0.5072 0.6212 0.5331 -0.0640 -0.0363 0.0657  68  ASP A O   
482  C CB  . ASP A 68  ? 0.4924 0.5717 0.5081 -0.0575 -0.0259 0.0458  68  ASP A CB  
483  C CG  . ASP A 68  ? 0.7120 0.7759 0.7237 -0.0526 -0.0219 0.0388  68  ASP A CG  
484  O OD1 . ASP A 68  ? 0.7408 0.8041 0.7562 -0.0451 -0.0207 0.0394  68  ASP A OD1 
485  O OD2 . ASP A 68  ? 0.8152 0.8678 0.8204 -0.0563 -0.0198 0.0331  68  ASP A OD2 
486  N N   . GLU A 69  ? 0.4723 0.5888 0.5061 -0.0602 -0.0330 0.0650  69  GLU A N   
487  C CA  . GLU A 69  ? 0.5125 0.6457 0.5506 -0.0673 -0.0381 0.0737  69  GLU A CA  
488  C C   . GLU A 69  ? 0.4861 0.6337 0.5349 -0.0626 -0.0399 0.0836  69  GLU A C   
489  O O   . GLU A 69  ? 0.5785 0.7363 0.6264 -0.0701 -0.0452 0.0898  69  GLU A O   
490  C CB  . GLU A 69  ? 0.5126 0.6521 0.5569 -0.0670 -0.0372 0.0758  69  GLU A CB  
491  C CG  . GLU A 69  ? 0.6892 0.8201 0.7230 -0.0760 -0.0375 0.0693  69  GLU A CG  
492  C CD  . GLU A 69  ? 0.8055 0.9382 0.8451 -0.0729 -0.0350 0.0692  69  GLU A CD  
493  O OE1 . GLU A 69  ? 0.8270 0.9486 0.8588 -0.0766 -0.0331 0.0624  69  GLU A OE1 
494  O OE2 . GLU A 69  ? 0.6987 0.8435 0.7507 -0.0667 -0.0344 0.0762  69  GLU A OE2 
495  N N   . ILE A 70  ? 0.4441 0.5923 0.5028 -0.0507 -0.0352 0.0855  70  ILE A N   
496  C CA  . ILE A 70  ? 0.4608 0.6215 0.5309 -0.0448 -0.0352 0.0954  70  ILE A CA  
497  C C   . ILE A 70  ? 0.6374 0.7958 0.7014 -0.0477 -0.0381 0.0953  70  ILE A C   
498  O O   . ILE A 70  ? 0.5216 0.6941 0.5909 -0.0509 -0.0424 0.1047  70  ILE A O   
499  C CB  . ILE A 70  ? 0.5278 0.6841 0.6062 -0.0318 -0.0278 0.0952  70  ILE A CB  
500  C CG1 . ILE A 70  ? 0.4586 0.6209 0.5453 -0.0291 -0.0250 0.0983  70  ILE A CG1 
501  C CG2 . ILE A 70  ? 0.5459 0.7106 0.6340 -0.0250 -0.0263 0.1039  70  ILE A CG2 
502  C CD1 . ILE A 70  ? 0.4562 0.6130 0.5493 -0.0173 -0.0169 0.0984  70  ILE A CD1 
503  N N   . GLU A 71  ? 0.5208 0.6618 0.5738 -0.0468 -0.0359 0.0851  71  GLU A N   
504  C CA  . GLU A 71  ? 0.5583 0.6952 0.6047 -0.0492 -0.0379 0.0840  71  GLU A CA  
505  C C   . GLU A 71  ? 0.5471 0.6904 0.5858 -0.0627 -0.0447 0.0869  71  GLU A C   
506  O O   . GLU A 71  ? 0.5579 0.7064 0.5953 -0.0657 -0.0481 0.0915  71  GLU A O   
507  C CB  . GLU A 71  ? 0.4431 0.5599 0.4791 -0.0468 -0.0340 0.0725  71  GLU A CB  
508  C CG  . GLU A 71  ? 0.4359 0.5462 0.4771 -0.0347 -0.0283 0.0706  71  GLU A CG  
509  C CD  . GLU A 71  ? 0.6357 0.7278 0.6673 -0.0333 -0.0253 0.0602  71  GLU A CD  
510  O OE1 . GLU A 71  ? 0.5615 0.6472 0.5945 -0.0255 -0.0216 0.0583  71  GLU A OE1 
511  O OE2 . GLU A 71  ? 0.5418 0.6258 0.5645 -0.0404 -0.0264 0.0542  71  GLU A OE2 
512  N N   . GLN A 72  ? 0.6007 0.7432 0.6334 -0.0715 -0.0466 0.0843  72  GLN A N   
513  C CA  . GLN A 72  ? 0.6905 0.8368 0.7131 -0.0860 -0.0525 0.0860  72  GLN A CA  
514  C C   . GLN A 72  ? 0.6671 0.8363 0.6994 -0.0908 -0.0588 0.0995  72  GLN A C   
515  O O   . GLN A 72  ? 0.6174 0.7917 0.6412 -0.1037 -0.0647 0.1028  72  GLN A O   
516  C CB  . GLN A 72  ? 0.6602 0.7961 0.6721 -0.0941 -0.0514 0.0784  72  GLN A CB  
517  C CG  . GLN A 72  ? 0.7736 0.8870 0.7727 -0.0940 -0.0465 0.0662  72  GLN A CG  
518  C CD  . GLN A 72  ? 0.9164 1.0219 0.9004 -0.1051 -0.0486 0.0634  72  GLN A CD  
519  O OE1 . GLN A 72  ? 0.9740 1.0907 0.9570 -0.1117 -0.0542 0.0706  72  GLN A OE1 
520  N NE2 . GLN A 72  ? 0.8678 0.9534 0.8400 -0.1072 -0.0438 0.0533  72  GLN A NE2 
521  N N   . THR A 73  ? 0.6590 0.8417 0.7085 -0.0811 -0.0573 0.1079  73  THR A N   
522  C CA  . THR A 73  ? 0.6966 0.9026 0.7583 -0.0844 -0.0628 0.1225  73  THR A CA  
523  C C   . THR A 73  ? 0.6647 0.8792 0.7329 -0.0807 -0.0645 0.1307  73  THR A C   
524  O O   . THR A 73  ? 0.7029 0.9363 0.7778 -0.0868 -0.0708 0.1431  73  THR A O   
525  C CB  . THR A 73  ? 0.6092 0.8267 0.6879 -0.0760 -0.0596 0.1291  73  THR A CB  
526  O OG1 . THR A 73  ? 0.6494 0.8686 0.7411 -0.0616 -0.0539 0.1332  73  THR A OG1 
527  C CG2 . THR A 73  ? 0.5410 0.7456 0.6141 -0.0750 -0.0553 0.1189  73  THR A CG2 
528  N N   . LEU A 74  ? 0.6143 0.8158 0.6808 -0.0711 -0.0594 0.1248  74  LEU A N   
529  C CA  . LEU A 74  ? 0.6340 0.8417 0.7041 -0.0689 -0.0612 0.1316  74  LEU A CA  
530  C C   . LEU A 74  ? 0.7130 0.9196 0.7680 -0.0836 -0.0684 0.1307  74  LEU A C   
531  O O   . LEU A 74  ? 0.7169 0.9064 0.7548 -0.0905 -0.0679 0.1190  74  LEU A O   
532  C CB  . LEU A 74  ? 0.6186 0.8113 0.6885 -0.0565 -0.0540 0.1247  74  LEU A CB  
533  C CG  . LEU A 74  ? 0.6953 0.8845 0.7766 -0.0422 -0.0457 0.1240  74  LEU A CG  
534  C CD1 . LEU A 74  ? 0.7780 0.9875 0.8780 -0.0381 -0.0455 0.1378  74  LEU A CD1 
535  C CD2 . LEU A 74  ? 0.5938 0.7668 0.6670 -0.0409 -0.0415 0.1116  74  LEU A CD2 
536  N N   . GLN A 75  ? 0.6388 0.8635 0.7002 -0.0885 -0.0746 0.1436  75  GLN A N   
537  C CA  . GLN A 75  ? 0.6261 0.8525 0.6732 -0.1042 -0.0823 0.1448  75  GLN A CA  
538  C C   . GLN A 75  ? 0.5081 0.7184 0.5434 -0.1030 -0.0803 0.1372  75  GLN A C   
539  O O   . GLN A 75  ? 0.6469 0.8568 0.6912 -0.0910 -0.0765 0.1392  75  GLN A O   
540  C CB  . GLN A 75  ? 0.6083 0.8614 0.6677 -0.1097 -0.0901 0.1629  75  GLN A CB  
541  C CG  . GLN A 75  ? 0.7128 0.9844 0.7922 -0.1041 -0.0896 0.1735  75  GLN A CG  
542  C CD  . GLN A 75  ? 0.8849 1.1846 0.9775 -0.1108 -0.0979 0.1925  75  GLN A CD  
543  O OE1 . GLN A 75  ? 0.8851 1.2004 0.9992 -0.0998 -0.0956 0.2051  75  GLN A OE1 
544  N NE2 . GLN A 75  ? 0.8108 1.1133 0.8892 -0.1284 -0.1054 0.1941  75  GLN A NE2 
545  N N   . THR A 76  ? 0.6518 0.8480 0.6663 -0.1156 -0.0823 0.1281  76  THR A N   
546  C CA  . THR A 76  ? 0.5967 0.7778 0.5984 -0.1166 -0.0809 0.1212  76  THR A CA  
547  C C   . THR A 76  ? 0.5783 0.7594 0.5624 -0.1353 -0.0878 0.1224  76  THR A C   
548  O O   . THR A 76  ? 0.6859 0.8697 0.6619 -0.1480 -0.0915 0.1227  76  THR A O   
549  C CB  . THR A 76  ? 0.5455 0.7014 0.5376 -0.1108 -0.0728 0.1052  76  THR A CB  
550  O OG1 . THR A 76  ? 0.6382 0.7852 0.6195 -0.1195 -0.0720 0.0979  76  THR A OG1 
551  C CG2 . THR A 76  ? 0.5264 0.6808 0.5336 -0.0931 -0.0661 0.1038  76  THR A CG2 
552  N N   . THR A 77  ? 0.5462 0.7233 0.5232 -0.1375 -0.0893 0.1228  77  THR A N   
553  C CA  . THR A 77  ? 0.6247 0.7969 0.5814 -0.1555 -0.0945 0.1219  77  THR A CA  
554  C C   . THR A 77  ? 0.6553 0.8008 0.5939 -0.1565 -0.0884 0.1074  77  THR A C   
555  O O   . THR A 77  ? 0.6456 0.7826 0.5648 -0.1712 -0.0910 0.1048  77  THR A O   
556  C CB  . THR A 77  ? 0.5650 0.7571 0.5275 -0.1600 -0.1026 0.1366  77  THR A CB  
557  O OG1 . THR A 77  ? 0.5547 0.7450 0.5270 -0.1456 -0.0988 0.1374  77  THR A OG1 
558  C CG2 . THR A 77  ? 0.5280 0.7480 0.5091 -0.1604 -0.1089 0.1524  77  THR A CG2 
559  N N   . SER A 78  ? 0.4859 0.6178 0.4300 -0.1419 -0.0802 0.0984  78  SER A N   
560  C CA  . SER A 78  ? 0.5135 0.6211 0.4432 -0.1414 -0.0739 0.0856  78  SER A CA  
561  C C   . SER A 78  ? 0.4372 0.5314 0.3719 -0.1298 -0.0657 0.0756  78  SER A C   
562  O O   . SER A 78  ? 0.4189 0.5228 0.3701 -0.1186 -0.0645 0.0791  78  SER A O   
563  C CB  . SER A 78  ? 0.5586 0.6657 0.4907 -0.1349 -0.0738 0.0878  78  SER A CB  
564  O OG  . SER A 78  ? 0.4744 0.5915 0.4268 -0.1182 -0.0717 0.0928  78  SER A OG  
565  N N   . GLN A 79  ? 0.4057 0.4774 0.3260 -0.1329 -0.0597 0.0637  79  GLN A N   
566  C CA  . GLN A 79  ? 0.3815 0.4404 0.3069 -0.1216 -0.0520 0.0548  79  GLN A CA  
567  C C   . GLN A 79  ? 0.3905 0.4486 0.3271 -0.1067 -0.0489 0.0545  79  GLN A C   
568  O O   . GLN A 79  ? 0.4219 0.4768 0.3681 -0.0954 -0.0444 0.0510  79  GLN A O   
569  C CB  . GLN A 79  ? 0.4153 0.4510 0.3238 -0.1289 -0.0458 0.0435  79  GLN A CB  
570  C CG  . GLN A 79  ? 0.4591 0.4925 0.3573 -0.1417 -0.0465 0.0421  79  GLN A CG  
571  C CD  . GLN A 79  ? 0.4182 0.4655 0.3303 -0.1366 -0.0485 0.0465  79  GLN A CD  
572  O OE1 . GLN A 79  ? 0.4185 0.4603 0.3387 -0.1266 -0.0434 0.0419  79  GLN A OE1 
573  N NE2 . GLN A 79  ? 0.4932 0.5589 0.4081 -0.1439 -0.0560 0.0560  79  GLN A NE2 
574  N N   . PHE A 80  ? 0.3874 0.4481 0.3220 -0.1070 -0.0514 0.0582  80  PHE A N   
575  C CA  . PHE A 80  ? 0.3571 0.4189 0.3026 -0.0933 -0.0489 0.0592  80  PHE A CA  
576  C C   . PHE A 80  ? 0.3871 0.4645 0.3512 -0.0824 -0.0494 0.0665  80  PHE A C   
577  O O   . PHE A 80  ? 0.3686 0.4410 0.3408 -0.0706 -0.0443 0.0628  80  PHE A O   
578  C CB  . PHE A 80  ? 0.4543 0.5197 0.3952 -0.0970 -0.0525 0.0641  80  PHE A CB  
579  C CG  . PHE A 80  ? 0.5567 0.6195 0.5054 -0.0844 -0.0492 0.0638  80  PHE A CG  
580  C CD1 . PHE A 80  ? 0.5327 0.5769 0.4756 -0.0798 -0.0429 0.0536  80  PHE A CD1 
581  C CD2 . PHE A 80  ? 0.5809 0.6598 0.5422 -0.0779 -0.0521 0.0744  80  PHE A CD2 
582  C CE1 . PHE A 80  ? 0.5940 0.6355 0.5429 -0.0692 -0.0400 0.0533  80  PHE A CE1 
583  C CE2 . PHE A 80  ? 0.6287 0.7040 0.5959 -0.0669 -0.0484 0.0739  80  PHE A CE2 
584  C CZ  . PHE A 80  ? 0.6850 0.7414 0.6453 -0.0629 -0.0425 0.0630  80  PHE A CZ  
585  N N   . GLN A 81  ? 0.3729 0.4690 0.3436 -0.0869 -0.0553 0.0770  81  GLN A N   
586  C CA  . GLN A 81  ? 0.3893 0.5002 0.3777 -0.0773 -0.0550 0.0845  81  GLN A CA  
587  C C   . GLN A 81  ? 0.3820 0.4863 0.3724 -0.0738 -0.0508 0.0778  81  GLN A C   
588  O O   . GLN A 81  ? 0.3570 0.4618 0.3584 -0.0621 -0.0465 0.0777  81  GLN A O   
589  C CB  . GLN A 81  ? 0.3526 0.4853 0.3475 -0.0844 -0.0624 0.0977  81  GLN A CB  
590  C CG  . GLN A 81  ? 0.4406 0.5866 0.4430 -0.0823 -0.0659 0.1087  81  GLN A CG  
591  C CD  . GLN A 81  ? 0.6551 0.8202 0.6579 -0.0948 -0.0748 0.1209  81  GLN A CD  
592  O OE1 . GLN A 81  ? 0.6322 0.7989 0.6273 -0.1063 -0.0784 0.1198  81  GLN A OE1 
593  N NE2 . GLN A 81  ? 0.6737 0.8536 0.6855 -0.0931 -0.0785 0.1329  81  GLN A NE2 
594  N N   . ARG A 82  ? 0.3707 0.4685 0.3500 -0.0845 -0.0519 0.0727  82  ARG A N   
595  C CA  . ARG A 82  ? 0.3588 0.4497 0.3392 -0.0820 -0.0480 0.0664  82  ARG A CA  
596  C C   . ARG A 82  ? 0.3302 0.4060 0.3118 -0.0712 -0.0411 0.0578  82  ARG A C   
597  O O   . ARG A 82  ? 0.3474 0.4236 0.3375 -0.0631 -0.0379 0.0566  82  ARG A O   
598  C CB  . ARG A 82  ? 0.4734 0.5556 0.4389 -0.0956 -0.0489 0.0611  82  ARG A CB  
599  C CG  . ARG A 82  ? 0.5546 0.6305 0.5209 -0.0945 -0.0452 0.0555  82  ARG A CG  
600  C CD  . ARG A 82  ? 0.5423 0.6345 0.5231 -0.0892 -0.0470 0.0627  82  ARG A CD  
601  N NE  . ARG A 82  ? 0.6000 0.7100 0.5828 -0.0980 -0.0539 0.0727  82  ARG A NE  
602  C CZ  . ARG A 82  ? 0.7758 0.9040 0.7733 -0.0937 -0.0565 0.0822  82  ARG A CZ  
603  N NH1 . ARG A 82  ? 0.6897 0.8195 0.6999 -0.0809 -0.0521 0.0825  82  ARG A NH1 
604  N NH2 . ARG A 82  ? 0.7089 0.8539 0.7081 -0.1030 -0.0633 0.0921  82  ARG A NH2 
605  N N   . LEU A 83  ? 0.2998 0.3625 0.2729 -0.0715 -0.0388 0.0520  83  LEU A N   
606  C CA  . LEU A 83  ? 0.3600 0.4087 0.3340 -0.0625 -0.0328 0.0442  83  LEU A CA  
607  C C   . LEU A 83  ? 0.3699 0.4249 0.3566 -0.0499 -0.0310 0.0480  83  LEU A C   
608  O O   . LEU A 83  ? 0.3348 0.3836 0.3256 -0.0425 -0.0268 0.0438  83  LEU A O   
609  C CB  . LEU A 83  ? 0.3733 0.4075 0.3362 -0.0655 -0.0306 0.0382  83  LEU A CB  
610  C CG  . LEU A 83  ? 0.4054 0.4247 0.3552 -0.0748 -0.0280 0.0306  83  LEU A CG  
611  C CD1 . LEU A 83  ? 0.2967 0.3030 0.2365 -0.0773 -0.0256 0.0261  83  LEU A CD1 
612  C CD2 . LEU A 83  ? 0.3733 0.3839 0.3265 -0.0700 -0.0230 0.0248  83  LEU A CD2 
613  N N   . PHE A 84  ? 0.3425 0.4093 0.3351 -0.0476 -0.0337 0.0561  84  PHE A N   
614  C CA  . PHE A 84  ? 0.3822 0.4539 0.3864 -0.0357 -0.0306 0.0600  84  PHE A CA  
615  C C   . PHE A 84  ? 0.3682 0.4461 0.3815 -0.0311 -0.0289 0.0622  84  PHE A C   
616  O O   . PHE A 84  ? 0.4185 0.4915 0.4366 -0.0223 -0.0240 0.0599  84  PHE A O   
617  C CB  . PHE A 84  ? 0.4351 0.5200 0.4455 -0.0344 -0.0335 0.0702  84  PHE A CB  
618  C CG  . PHE A 84  ? 0.5110 0.5887 0.5152 -0.0341 -0.0331 0.0682  84  PHE A CG  
619  C CD1 . PHE A 84  ? 0.5511 0.6262 0.5441 -0.0446 -0.0372 0.0670  84  PHE A CD1 
620  C CD2 . PHE A 84  ? 0.5845 0.6568 0.5929 -0.0239 -0.0283 0.0672  84  PHE A CD2 
621  C CE1 . PHE A 84  ? 0.6389 0.7070 0.6259 -0.0445 -0.0368 0.0652  84  PHE A CE1 
622  C CE2 . PHE A 84  ? 0.5929 0.6584 0.5956 -0.0237 -0.0280 0.0654  84  PHE A CE2 
623  C CZ  . PHE A 84  ? 0.5867 0.6505 0.5791 -0.0337 -0.0323 0.0645  84  PHE A CZ  
624  N N   . ILE A 85  ? 0.2901 0.3786 0.3053 -0.0377 -0.0327 0.0667  85  ILE A N   
625  C CA  . ILE A 85  ? 0.3166 0.4111 0.3402 -0.0340 -0.0311 0.0689  85  ILE A CA  
626  C C   . ILE A 85  ? 0.3532 0.4336 0.3716 -0.0329 -0.0274 0.0590  85  ILE A C   
627  O O   . ILE A 85  ? 0.3174 0.3950 0.3411 -0.0252 -0.0232 0.0576  85  ILE A O   
628  C CB  . ILE A 85  ? 0.3399 0.4494 0.3663 -0.0424 -0.0366 0.0762  85  ILE A CB  
629  C CG1 . ILE A 85  ? 0.4247 0.5515 0.4610 -0.0412 -0.0397 0.0886  85  ILE A CG1 
630  C CG2 . ILE A 85  ? 0.3362 0.4490 0.3688 -0.0402 -0.0347 0.0762  85  ILE A CG2 
631  C CD1 . ILE A 85  ? 0.4858 0.6283 0.5233 -0.0519 -0.0467 0.0968  85  ILE A CD1 
632  N N   . LEU A 86  ? 0.3113 0.3821 0.3188 -0.0410 -0.0285 0.0525  86  LEU A N   
633  C CA  . LEU A 86  ? 0.3161 0.3740 0.3195 -0.0403 -0.0250 0.0442  86  LEU A CA  
634  C C   . LEU A 86  ? 0.3309 0.3786 0.3355 -0.0315 -0.0205 0.0396  86  LEU A C   
635  O O   . LEU A 86  ? 0.4095 0.4520 0.4161 -0.0276 -0.0176 0.0361  86  LEU A O   
636  C CB  . LEU A 86  ? 0.3714 0.4194 0.3630 -0.0501 -0.0256 0.0386  86  LEU A CB  
637  C CG  . LEU A 86  ? 0.4407 0.4935 0.4283 -0.0601 -0.0285 0.0400  86  LEU A CG  
638  C CD1 . LEU A 86  ? 0.4132 0.4540 0.3868 -0.0702 -0.0279 0.0347  86  LEU A CD1 
639  C CD2 . LEU A 86  ? 0.5028 0.5552 0.4950 -0.0575 -0.0263 0.0382  86  LEU A CD2 
640  N N   . LEU A 87  ? 0.2913 0.3363 0.2943 -0.0289 -0.0201 0.0398  87  LEU A N   
641  C CA  . LEU A 87  ? 0.3402 0.3754 0.3434 -0.0216 -0.0161 0.0356  87  LEU A CA  
642  C C   . LEU A 87  ? 0.5172 0.5576 0.5283 -0.0128 -0.0135 0.0398  87  LEU A C   
643  O O   . LEU A 87  ? 0.4828 0.5151 0.4931 -0.0072 -0.0101 0.0367  87  LEU A O   
644  C CB  . LEU A 87  ? 0.3850 0.4130 0.3817 -0.0231 -0.0161 0.0330  87  LEU A CB  
645  C CG  . LEU A 87  ? 0.3417 0.3601 0.3290 -0.0312 -0.0164 0.0275  87  LEU A CG  
646  C CD1 . LEU A 87  ? 0.3541 0.3671 0.3350 -0.0333 -0.0167 0.0263  87  LEU A CD1 
647  C CD2 . LEU A 87  ? 0.3718 0.3790 0.3585 -0.0291 -0.0127 0.0212  87  LEU A CD2 
648  N N   . GLY A 88  ? 0.4114 0.4644 0.4301 -0.0116 -0.0145 0.0469  88  GLY A N   
649  C CA  . GLY A 88  ? 0.4075 0.4637 0.4337 -0.0031 -0.0104 0.0509  88  GLY A CA  
650  C C   . GLY A 88  ? 0.4238 0.4823 0.4529 0.0019  -0.0087 0.0555  88  GLY A C   
651  O O   . GLY A 88  ? 0.5309 0.5878 0.5642 0.0094  -0.0035 0.0574  88  GLY A O   
652  N N   . ALA A 89  ? 0.4656 0.5270 0.4919 -0.0022 -0.0124 0.0573  89  ALA A N   
653  C CA  . ALA A 89  ? 0.5285 0.5922 0.5577 0.0025  -0.0109 0.0621  89  ALA A CA  
654  C C   . ALA A 89  ? 0.6122 0.6925 0.6527 0.0045  -0.0118 0.0738  89  ALA A C   
655  O O   . ALA A 89  ? 0.6787 0.7625 0.7232 0.0087  -0.0104 0.0794  89  ALA A O   
656  C CB  . ALA A 89  ? 0.4934 0.5525 0.5144 -0.0029 -0.0143 0.0591  89  ALA A CB  
657  N N   . GLU A 90  ? 0.6277 0.7186 0.6740 0.0019  -0.0139 0.0783  90  GLU A N   
658  C CA  . GLU A 90  ? 0.6799 0.7884 0.7383 0.0030  -0.0153 0.0908  90  GLU A CA  
659  C C   . GLU A 90  ? 0.7523 0.8638 0.8219 0.0128  -0.0081 0.0961  90  GLU A C   
660  O O   . GLU A 90  ? 0.8917 1.0160 0.9730 0.0167  -0.0070 0.1073  90  GLU A O   
661  C CB  . GLU A 90  ? 0.6847 0.8050 0.7438 -0.0065 -0.0221 0.0944  90  GLU A CB  
662  C CG  . GLU A 90  ? 0.6895 0.8138 0.7414 -0.0164 -0.0294 0.0957  90  GLU A CG  
663  C CD  . GLU A 90  ? 0.7314 0.8654 0.7897 -0.0139 -0.0305 0.1054  90  GLU A CD  
664  O OE1 . GLU A 90  ? 0.7763 0.9260 0.8485 -0.0102 -0.0303 0.1172  90  GLU A OE1 
665  O OE2 . GLU A 90  ? 0.7593 0.8853 0.8093 -0.0155 -0.0314 0.1016  90  GLU A OE2 
666  N N   . ASN A 91  ? 0.8990 0.9990 0.9653 0.0166  -0.0029 0.0889  91  ASN A N   
667  C CA  . ASN A 91  ? 1.0757 1.1755 1.1501 0.0251  0.0052  0.0927  91  ASN A CA  
668  C C   . ASN A 91  ? 0.9856 1.1031 1.0734 0.0252  0.0042  0.1039  91  ASN A C   
669  O O   . ASN A 91  ? 0.9422 1.0704 1.0416 0.0301  0.0066  0.1147  91  ASN A O   
670  C CB  . ASN A 91  ? 1.1210 1.2149 1.1974 0.0333  0.0121  0.0952  91  ASN A CB  
671  C CG  . ASN A 91  ? 1.1838 1.2693 1.2625 0.0414  0.0223  0.0948  91  ASN A CG  
672  O OD1 . ASN A 91  ? 1.0906 1.1835 1.1783 0.0438  0.0254  0.1007  91  ASN A OD1 
673  N ND2 . ASN A 91  ? 1.2016 1.2708 1.2716 0.0449  0.0280  0.0879  91  ASN A ND2 
674  N N   . ILE A 92  ? 0.7705 0.8914 0.8576 0.0200  0.0009  0.1018  92  ILE A N   
675  C CA  . ILE A 92  ? 0.6720 0.8089 0.7714 0.0197  0.0001  0.1116  92  ILE A CA  
676  C C   . ILE A 92  ? 0.7299 0.8603 0.8327 0.0268  0.0089  0.1103  92  ILE A C   
677  O O   . ILE A 92  ? 0.5647 0.6829 0.6583 0.0253  0.0100  0.1006  92  ILE A O   
678  C CB  . ILE A 92  ? 0.6512 0.7954 0.7467 0.0088  -0.0086 0.1101  92  ILE A CB  
679  C CG1 . ILE A 92  ? 0.7272 0.8776 0.8182 0.0008  -0.0166 0.1121  92  ILE A CG1 
680  C CG2 . ILE A 92  ? 0.6260 0.7860 0.7340 0.0085  -0.0090 0.1194  92  ILE A CG2 
681  C CD1 . ILE A 92  ? 0.6592 0.8028 0.7367 -0.0097 -0.0226 0.1031  92  ILE A CD1 
682  N N   . ASP A 93  ? 0.7333 0.8713 0.8495 0.0345  0.0156  0.1205  93  ASP A N   
683  C CA  . ASP A 93  ? 0.7571 0.8872 0.8758 0.0413  0.0255  0.1196  93  ASP A CA  
684  C C   . ASP A 93  ? 0.6623 0.7958 0.7812 0.0370  0.0233  0.1176  93  ASP A C   
685  O O   . ASP A 93  ? 0.6282 0.7508 0.7435 0.0403  0.0300  0.1128  93  ASP A O   
686  C CB  . ASP A 93  ? 0.7550 0.8932 0.8892 0.0504  0.0340  0.1323  93  ASP A CB  
687  C CG  . ASP A 93  ? 0.9032 1.0652 1.0530 0.0480  0.0278  0.1463  93  ASP A CG  
688  O OD1 . ASP A 93  ? 0.9783 1.1519 1.1313 0.0416  0.0213  0.1484  93  ASP A OD1 
689  O OD2 . ASP A 93  ? 0.9898 1.1593 1.1486 0.0523  0.0294  0.1555  93  ASP A OD2 
690  N N   . ARG A 94  ? 0.5842 0.7320 0.7063 0.0292  0.0141  0.1212  94  ARG A N   
691  C CA  . ARG A 94  ? 0.6034 0.7538 0.7244 0.0242  0.0113  0.1186  94  ARG A CA  
692  C C   . ARG A 94  ? 0.6571 0.7901 0.7623 0.0207  0.0104  0.1045  94  ARG A C   
693  O O   . ARG A 94  ? 0.5593 0.6882 0.6624 0.0200  0.0123  0.1008  94  ARG A O   
694  C CB  . ARG A 94  ? 0.5756 0.7438 0.7011 0.0151  0.0013  0.1248  94  ARG A CB  
695  C CG  . ARG A 94  ? 0.6388 0.8104 0.7628 0.0088  -0.0021 0.1224  94  ARG A CG  
696  C CD  . ARG A 94  ? 0.6922 0.8861 0.8282 0.0036  -0.0080 0.1346  94  ARG A CD  
697  N NE  . ARG A 94  ? 0.7516 0.9487 0.8861 -0.0026 -0.0110 0.1324  94  ARG A NE  
698  C CZ  . ARG A 94  ? 0.7826 0.9919 0.9166 -0.0131 -0.0195 0.1359  94  ARG A CZ  
699  N NH1 . ARG A 94  ? 0.7438 0.9635 0.8782 -0.0193 -0.0264 0.1418  94  ARG A NH1 
700  N NH2 . ARG A 94  ? 0.6756 0.8862 0.8078 -0.0182 -0.0211 0.1333  94  ARG A NH2 
701  N N   . LEU A 95  ? 0.5666 0.6894 0.6610 0.0185  0.0077  0.0972  95  LEU A N   
702  C CA  . LEU A 95  ? 0.4893 0.5977 0.5703 0.0144  0.0059  0.0852  95  LEU A CA  
703  C C   . LEU A 95  ? 0.5615 0.6532 0.6356 0.0202  0.0131  0.0786  95  LEU A C   
704  O O   . LEU A 95  ? 0.6054 0.6859 0.6698 0.0172  0.0121  0.0699  95  LEU A O   
705  C CB  . LEU A 95  ? 0.5201 0.6263 0.5930 0.0080  -0.0009 0.0810  95  LEU A CB  
706  C CG  . LEU A 95  ? 0.6089 0.7303 0.6859 0.0009  -0.0083 0.0876  95  LEU A CG  
707  C CD1 . LEU A 95  ? 0.6901 0.8058 0.7566 -0.0059 -0.0136 0.0820  95  LEU A CD1 
708  C CD2 . LEU A 95  ? 0.6727 0.8019 0.7524 -0.0044 -0.0111 0.0891  95  LEU A CD2 
709  N N   . GLN A 96  ? 0.5439 0.6333 0.6225 0.0278  0.0207  0.0829  96  GLN A N   
710  C CA  . GLN A 96  ? 0.5933 0.6656 0.6631 0.0319  0.0276  0.0763  96  GLN A CA  
711  C C   . GLN A 96  ? 0.5928 0.6561 0.6565 0.0307  0.0304  0.0706  96  GLN A C   
712  O O   . GLN A 96  ? 0.5722 0.6214 0.6247 0.0296  0.0315  0.0627  96  GLN A O   
713  C CB  . GLN A 96  ? 0.6229 0.6938 0.6987 0.0402  0.0367  0.0826  96  GLN A CB  
714  C CG  . GLN A 96  ? 0.6414 0.7210 0.7234 0.0417  0.0342  0.0888  96  GLN A CG  
715  C CD  . GLN A 96  ? 0.8415 0.9151 0.9134 0.0369  0.0275  0.0816  96  GLN A CD  
716  O OE1 . GLN A 96  ? 0.8293 0.8890 0.8923 0.0387  0.0309  0.0754  96  GLN A OE1 
717  N NE2 . GLN A 96  ? 0.7494 0.8330 0.8223 0.0302  0.0184  0.0824  96  GLN A NE2 
718  N N   . PRO A 97  ? 0.5602 0.6307 0.6302 0.0304  0.0314  0.0743  97  PRO A N   
719  C CA  . PRO A 97  ? 0.5208 0.5822 0.5834 0.0280  0.0328  0.0681  97  PRO A CA  
720  C C   . PRO A 97  ? 0.4398 0.4992 0.4952 0.0208  0.0246  0.0612  97  PRO A C   
721  O O   . PRO A 97  ? 0.4380 0.4861 0.4843 0.0190  0.0253  0.0546  97  PRO A O   
722  C CB  . PRO A 97  ? 0.4989 0.5705 0.5716 0.0296  0.0357  0.0750  97  PRO A CB  
723  C CG  . PRO A 97  ? 0.4945 0.5776 0.5800 0.0348  0.0386  0.0852  97  PRO A CG  
724  C CD  . PRO A 97  ? 0.5157 0.6028 0.6000 0.0321  0.0317  0.0847  97  PRO A CD  
725  N N   . TYR A 98  ? 0.4098 0.4794 0.4686 0.0164  0.0172  0.0629  98  TYR A N   
726  C CA  . TYR A 98  ? 0.4809 0.5466 0.5326 0.0099  0.0109  0.0563  98  TYR A CA  
727  C C   . TYR A 98  ? 0.4753 0.5289 0.5183 0.0100  0.0107  0.0501  98  TYR A C   
728  O O   . TYR A 98  ? 0.4137 0.4589 0.4498 0.0070  0.0091  0.0440  98  TYR A O   
729  C CB  . TYR A 98  ? 0.4057 0.4830 0.4611 0.0043  0.0041  0.0594  98  TYR A CB  
730  C CG  . TYR A 98  ? 0.4407 0.5312 0.5044 0.0023  0.0028  0.0657  98  TYR A CG  
731  C CD1 . TYR A 98  ? 0.4562 0.5579 0.5308 0.0067  0.0057  0.0747  98  TYR A CD1 
732  C CD2 . TYR A 98  ? 0.3740 0.4661 0.4354 -0.0039 -0.0009 0.0631  98  TYR A CD2 
733  C CE1 . TYR A 98  ? 0.4396 0.5545 0.5229 0.0047  0.0044  0.0813  98  TYR A CE1 
734  C CE2 . TYR A 98  ? 0.4215 0.5258 0.4903 -0.0062 -0.0023 0.0688  98  TYR A CE2 
735  C CZ  . TYR A 98  ? 0.4340 0.5502 0.5139 -0.0020 0.0001  0.0781  98  TYR A CZ  
736  O OH  . TYR A 98  ? 0.4106 0.5401 0.4989 -0.0044 -0.0014 0.0847  98  TYR A OH  
737  N N   . LEU A 99  ? 0.4924 0.5455 0.5362 0.0135  0.0125  0.0521  99  LEU A N   
738  C CA  . LEU A 99  ? 0.4220 0.4641 0.4580 0.0138  0.0126  0.0466  99  LEU A CA  
739  C C   . LEU A 99  ? 0.4855 0.5150 0.5148 0.0164  0.0181  0.0427  99  LEU A C   
740  O O   . LEU A 99  ? 0.4670 0.4871 0.4887 0.0143  0.0168  0.0371  99  LEU A O   
741  C CB  . LEU A 99  ? 0.4671 0.5123 0.5059 0.0169  0.0132  0.0504  99  LEU A CB  
742  C CG  . LEU A 99  ? 0.5526 0.6093 0.5957 0.0127  0.0069  0.0540  99  LEU A CG  
743  C CD1 . LEU A 99  ? 0.4529 0.5135 0.4993 0.0160  0.0077  0.0588  99  LEU A CD1 
744  C CD2 . LEU A 99  ? 0.4959 0.5478 0.5320 0.0061  0.0016  0.0477  99  LEU A CD2 
745  N N   . ARG A 100 ? 0.4318 0.4609 0.4635 0.0204  0.0245  0.0460  100 ARG A N   
746  C CA  . ARG A 100 ? 0.5421 0.5584 0.5654 0.0213  0.0300  0.0422  100 ARG A CA  
747  C C   . ARG A 100 ? 0.4651 0.4782 0.4836 0.0161  0.0263  0.0378  100 ARG A C   
748  O O   . ARG A 100 ? 0.4382 0.4408 0.4477 0.0139  0.0267  0.0331  100 ARG A O   
749  C CB  . ARG A 100 ? 0.5405 0.5562 0.5672 0.0264  0.0387  0.0469  100 ARG A CB  
750  C CG  . ARG A 100 ? 0.6000 0.5997 0.6158 0.0275  0.0465  0.0433  100 ARG A CG  
751  C CD  . ARG A 100 ? 0.6610 0.6572 0.6752 0.0276  0.0522  0.0441  100 ARG A CD  
752  N NE  . ARG A 100 ? 0.7196 0.7223 0.7358 0.0230  0.0458  0.0429  100 ARG A NE  
753  C CZ  . ARG A 100 ? 0.7227 0.7356 0.7479 0.0239  0.0459  0.0474  100 ARG A CZ  
754  N NH1 . ARG A 100 ? 0.5330 0.5521 0.5677 0.0294  0.0519  0.0543  100 ARG A NH1 
755  N NH2 . ARG A 100 ? 0.6760 0.6933 0.7016 0.0193  0.0401  0.0457  100 ARG A NH2 
756  N N   . LEU A 101 ? 0.4209 0.4436 0.4454 0.0136  0.0224  0.0397  101 LEU A N   
757  C CA  . LEU A 101 ? 0.4438 0.4641 0.4647 0.0089  0.0190  0.0361  101 LEU A CA  
758  C C   . LEU A 101 ? 0.3347 0.3515 0.3518 0.0051  0.0135  0.0318  101 LEU A C   
759  O O   . LEU A 101 ? 0.3526 0.3625 0.3642 0.0023  0.0124  0.0283  101 LEU A O   
760  C CB  . LEU A 101 ? 0.3554 0.3866 0.3836 0.0072  0.0166  0.0394  101 LEU A CB  
761  C CG  . LEU A 101 ? 0.3442 0.3725 0.3692 0.0034  0.0152  0.0367  101 LEU A CG  
762  C CD1 . LEU A 101 ? 0.3995 0.4189 0.4186 0.0049  0.0210  0.0357  101 LEU A CD1 
763  C CD2 . LEU A 101 ? 0.3894 0.4286 0.4215 0.0014  0.0128  0.0398  101 LEU A CD2 
764  N N   . TRP A 102 ? 0.3785 0.4001 0.3988 0.0047  0.0102  0.0325  102 TRP A N   
765  C CA  . TRP A 102 ? 0.4218 0.4391 0.4388 0.0015  0.0063  0.0286  102 TRP A CA  
766  C C   . TRP A 102 ? 0.3821 0.3889 0.3925 0.0025  0.0081  0.0254  102 TRP A C   
767  O O   . TRP A 102 ? 0.3617 0.3633 0.3689 -0.0004 0.0061  0.0226  102 TRP A O   
768  C CB  . TRP A 102 ? 0.4141 0.4368 0.4340 0.0009  0.0036  0.0299  102 TRP A CB  
769  C CG  . TRP A 102 ? 0.4297 0.4469 0.4462 -0.0019 0.0009  0.0261  102 TRP A CG  
770  C CD1 . TRP A 102 ? 0.5576 0.5667 0.5699 -0.0006 0.0018  0.0233  102 TRP A CD1 
771  C CD2 . TRP A 102 ? 0.5162 0.5346 0.5330 -0.0067 -0.0024 0.0247  102 TRP A CD2 
772  N NE1 . TRP A 102 ? 0.5221 0.5281 0.5333 -0.0038 -0.0007 0.0207  102 TRP A NE1 
773  C CE2 . TRP A 102 ? 0.4829 0.4937 0.4964 -0.0076 -0.0028 0.0213  102 TRP A CE2 
774  C CE3 . TRP A 102 ? 0.4989 0.5234 0.5178 -0.0108 -0.0044 0.0260  102 TRP A CE3 
775  C CZ2 . TRP A 102 ? 0.4795 0.4877 0.4919 -0.0118 -0.0043 0.0192  102 TRP A CZ2 
776  C CZ3 . TRP A 102 ? 0.6089 0.6303 0.6255 -0.0157 -0.0061 0.0235  102 TRP A CZ3 
777  C CH2 . TRP A 102 ? 0.4979 0.5107 0.5113 -0.0159 -0.0056 0.0201  102 TRP A CH2 
778  N N   . ASN A 103 ? 0.3766 0.3803 0.3850 0.0064  0.0123  0.0264  103 ASN A N   
779  C CA  . ASN A 103 ? 0.4093 0.4025 0.4101 0.0066  0.0143  0.0234  103 ASN A CA  
780  C C   . ASN A 103 ? 0.4052 0.3921 0.4000 0.0040  0.0157  0.0218  103 ASN A C   
781  O O   . ASN A 103 ? 0.4262 0.4065 0.4154 0.0011  0.0141  0.0193  103 ASN A O   
782  C CB  . ASN A 103 ? 0.4439 0.4340 0.4432 0.0112  0.0196  0.0249  103 ASN A CB  
783  C CG  . ASN A 103 ? 0.5087 0.5031 0.5118 0.0129  0.0176  0.0260  103 ASN A CG  
784  O OD1 . ASN A 103 ? 0.5764 0.5696 0.5785 0.0103  0.0134  0.0234  103 ASN A OD1 
785  N ND2 . ASN A 103 ? 0.6834 0.6826 0.6911 0.0172  0.0209  0.0304  103 ASN A ND2 
786  N N   . GLU A 104 ? 0.3773 0.3667 0.3736 0.0048  0.0184  0.0238  104 GLU A N   
787  C CA  . GLU A 104 ? 0.3955 0.3793 0.3857 0.0017  0.0195  0.0226  104 GLU A CA  
788  C C   . GLU A 104 ? 0.3762 0.3618 0.3675 -0.0030 0.0134  0.0213  104 GLU A C   
789  O O   . GLU A 104 ? 0.3906 0.3701 0.3757 -0.0066 0.0122  0.0199  104 GLU A O   
790  C CB  . GLU A 104 ? 0.4249 0.4121 0.4179 0.0036  0.0237  0.0253  104 GLU A CB  
791  C CG  . GLU A 104 ? 0.5851 0.5622 0.5688 0.0028  0.0298  0.0245  104 GLU A CG  
792  C CD  . GLU A 104 ? 0.6053 0.5859 0.5930 0.0052  0.0346  0.0276  104 GLU A CD  
793  O OE1 . GLU A 104 ? 0.6017 0.5894 0.5979 0.0101  0.0374  0.0314  104 GLU A OE1 
794  O OE2 . GLU A 104 ? 0.5441 0.5212 0.5271 0.0020  0.0354  0.0267  104 GLU A OE2 
795  N N   . ALA A 105 ? 0.3195 0.3134 0.3186 -0.0032 0.0098  0.0223  105 ALA A N   
796  C CA  . ALA A 105 ? 0.3414 0.3365 0.3425 -0.0071 0.0053  0.0215  105 ALA A CA  
797  C C   . ALA A 105 ? 0.3617 0.3520 0.3608 -0.0086 0.0029  0.0198  105 ALA A C   
798  O O   . ALA A 105 ? 0.3429 0.3312 0.3416 -0.0118 0.0005  0.0199  105 ALA A O   
799  C CB  . ALA A 105 ? 0.2966 0.2997 0.3048 -0.0075 0.0031  0.0225  105 ALA A CB  
800  N N   . GLU A 106 ? 0.3430 0.3320 0.3417 -0.0063 0.0036  0.0190  106 GLU A N   
801  C CA  . GLU A 106 ? 0.3782 0.3628 0.3756 -0.0075 0.0018  0.0176  106 GLU A CA  
802  C C   . GLU A 106 ? 0.3804 0.3587 0.3712 -0.0103 0.0017  0.0174  106 GLU A C   
803  O O   . GLU A 106 ? 0.4083 0.3853 0.4002 -0.0129 -0.0011 0.0177  106 GLU A O   
804  C CB  . GLU A 106 ? 0.3618 0.3453 0.3585 -0.0045 0.0032  0.0167  106 GLU A CB  
805  C CG  . GLU A 106 ? 0.4294 0.4106 0.4276 -0.0055 0.0009  0.0155  106 GLU A CG  
806  C CD  . GLU A 106 ? 0.6444 0.6238 0.6409 -0.0027 0.0024  0.0145  106 GLU A CD  
807  O OE1 . GLU A 106 ? 0.5637 0.5455 0.5600 0.0002  0.0048  0.0156  106 GLU A OE1 
808  O OE2 . GLU A 106 ? 0.6691 0.6449 0.6653 -0.0034 0.0014  0.0133  106 GLU A OE2 
809  N N   . LEU A 107 ? 0.4312 0.4055 0.4151 -0.0102 0.0051  0.0173  107 LEU A N   
810  C CA  . LEU A 107 ? 0.3993 0.3668 0.3746 -0.0143 0.0051  0.0170  107 LEU A CA  
811  C C   . LEU A 107 ? 0.5523 0.5217 0.5282 -0.0186 0.0021  0.0188  107 LEU A C   
812  O O   . LEU A 107 ? 0.5679 0.5341 0.5390 -0.0234 -0.0003 0.0197  107 LEU A O   
813  C CB  . LEU A 107 ? 0.5131 0.4731 0.4788 -0.0134 0.0111  0.0159  107 LEU A CB  
814  C CG  . LEU A 107 ? 0.6659 0.6230 0.6306 -0.0091 0.0148  0.0148  107 LEU A CG  
815  C CD1 . LEU A 107 ? 0.6723 0.6201 0.6269 -0.0084 0.0222  0.0140  107 LEU A CD1 
816  C CD2 . LEU A 107 ? 0.6313 0.5863 0.5953 -0.0107 0.0116  0.0137  107 LEU A CD2 
817  N N   . LEU A 108 ? 0.3791 0.3542 0.3608 -0.0174 0.0019  0.0197  108 LEU A N   
818  C CA  . LEU A 108 ? 0.3583 0.3351 0.3403 -0.0212 -0.0003 0.0215  108 LEU A CA  
819  C C   . LEU A 108 ? 0.3439 0.3250 0.3340 -0.0228 -0.0049 0.0235  108 LEU A C   
820  O O   . LEU A 108 ? 0.3936 0.3761 0.3845 -0.0262 -0.0072 0.0259  108 LEU A O   
821  C CB  . LEU A 108 ? 0.3852 0.3656 0.3694 -0.0193 0.0021  0.0218  108 LEU A CB  
822  C CG  . LEU A 108 ? 0.5557 0.5312 0.5323 -0.0182 0.0076  0.0210  108 LEU A CG  
823  C CD1 . LEU A 108 ? 0.4546 0.4357 0.4363 -0.0161 0.0095  0.0222  108 LEU A CD1 
824  C CD2 . LEU A 108 ? 0.5041 0.4716 0.4694 -0.0235 0.0082  0.0209  108 LEU A CD2 
825  N N   . ILE A 109 ? 0.3114 0.2945 0.3078 -0.0205 -0.0057 0.0230  109 ILE A N   
826  C CA  . ILE A 109 ? 0.3863 0.3722 0.3909 -0.0215 -0.0083 0.0250  109 ILE A CA  
827  C C   . ILE A 109 ? 0.3831 0.3680 0.3877 -0.0253 -0.0113 0.0283  109 ILE A C   
828  O O   . ILE A 109 ? 0.3853 0.3730 0.3975 -0.0265 -0.0131 0.0316  109 ILE A O   
829  C CB  . ILE A 109 ? 0.3572 0.3435 0.3667 -0.0187 -0.0075 0.0234  109 ILE A CB  
830  C CG1 . ILE A 109 ? 0.4080 0.3903 0.4143 -0.0183 -0.0076 0.0226  109 ILE A CG1 
831  C CG2 . ILE A 109 ? 0.3178 0.3066 0.3274 -0.0161 -0.0054 0.0212  109 ILE A CG2 
832  C CD1 . ILE A 109 ? 0.3856 0.3674 0.3958 -0.0159 -0.0067 0.0209  109 ILE A CD1 
833  N N   . GLU A 110 ? 0.3485 0.3292 0.3447 -0.0277 -0.0117 0.0281  110 GLU A N   
834  C CA  . GLU A 110 ? 0.4371 0.4178 0.4326 -0.0326 -0.0154 0.0320  110 GLU A CA  
835  C C   . GLU A 110 ? 0.5532 0.5344 0.5439 -0.0375 -0.0172 0.0348  110 GLU A C   
836  O O   . GLU A 110 ? 0.5204 0.5035 0.5119 -0.0424 -0.0212 0.0395  110 GLU A O   
837  C CB  . GLU A 110 ? 0.4837 0.4593 0.4711 -0.0343 -0.0152 0.0306  110 GLU A CB  
838  C CG  . GLU A 110 ? 0.6152 0.5904 0.6075 -0.0302 -0.0141 0.0288  110 GLU A CG  
839  C CD  . GLU A 110 ? 0.7616 0.7305 0.7441 -0.0310 -0.0127 0.0262  110 GLU A CD  
840  O OE1 . GLU A 110 ? 0.7807 0.7475 0.7573 -0.0365 -0.0150 0.0283  110 GLU A OE1 
841  O OE2 . GLU A 110 ? 0.7116 0.6778 0.6921 -0.0266 -0.0091 0.0224  110 GLU A OE2 
842  N N   . GLN A 111 ? 0.4053 0.3852 0.3912 -0.0368 -0.0146 0.0325  111 GLN A N   
843  C CA  . GLN A 111 ? 0.5347 0.5137 0.5142 -0.0418 -0.0159 0.0346  111 GLN A CA  
844  C C   . GLN A 111 ? 0.5272 0.5099 0.5116 -0.0399 -0.0148 0.0348  111 GLN A C   
845  O O   . GLN A 111 ? 0.4596 0.4421 0.4397 -0.0441 -0.0160 0.0368  111 GLN A O   
846  C CB  . GLN A 111 ? 0.5385 0.5091 0.5026 -0.0447 -0.0127 0.0316  111 GLN A CB  
847  C CG  . GLN A 111 ? 0.6326 0.6002 0.5940 -0.0395 -0.0067 0.0273  111 GLN A CG  
848  C CD  . GLN A 111 ? 0.7708 0.7282 0.7178 -0.0414 -0.0019 0.0244  111 GLN A CD  
849  O OE1 . GLN A 111 ? 0.8297 0.7817 0.7672 -0.0444 0.0012  0.0238  111 GLN A OE1 
850  N NE2 . GLN A 111 ? 0.7171 0.6711 0.6619 -0.0398 -0.0006 0.0226  111 GLN A NE2 
851  N N   . ASP A 112 ? 0.4257 0.4117 0.4182 -0.0346 -0.0129 0.0329  112 ASP A N   
852  C CA  . ASP A 112 ? 0.4218 0.4115 0.4192 -0.0333 -0.0119 0.0331  112 ASP A CA  
853  C C   . ASP A 112 ? 0.3742 0.3682 0.3832 -0.0309 -0.0127 0.0343  112 ASP A C   
854  O O   . ASP A 112 ? 0.3403 0.3342 0.3522 -0.0277 -0.0112 0.0319  112 ASP A O   
855  C CB  . ASP A 112 ? 0.3997 0.3887 0.3937 -0.0300 -0.0078 0.0295  112 ASP A CB  
856  C CG  . ASP A 112 ? 0.5047 0.4975 0.5022 -0.0297 -0.0070 0.0300  112 ASP A CG  
857  O OD1 . ASP A 112 ? 0.4370 0.4340 0.4429 -0.0286 -0.0079 0.0307  112 ASP A OD1 
858  O OD2 . ASP A 112 ? 0.4669 0.4578 0.4583 -0.0307 -0.0048 0.0296  112 ASP A OD2 
859  N N   . ILE A 113 ? 0.3523 0.3491 0.3671 -0.0328 -0.0144 0.0380  113 ILE A N   
860  C CA  . ILE A 113 ? 0.3926 0.3914 0.4179 -0.0311 -0.0139 0.0397  113 ILE A CA  
861  C C   . ILE A 113 ? 0.3773 0.3767 0.4046 -0.0284 -0.0108 0.0360  113 ILE A C   
862  O O   . ILE A 113 ? 0.2986 0.2970 0.3308 -0.0267 -0.0091 0.0350  113 ILE A O   
863  C CB  . ILE A 113 ? 0.5528 0.5543 0.5844 -0.0336 -0.0157 0.0455  113 ILE A CB  
864  C CG1 . ILE A 113 ? 0.6190 0.6214 0.6478 -0.0378 -0.0198 0.0503  113 ILE A CG1 
865  C CG2 . ILE A 113 ? 0.6068 0.6086 0.6495 -0.0315 -0.0137 0.0477  113 ILE A CG2 
866  C CD1 . ILE A 113 ? 0.6064 0.6071 0.6233 -0.0418 -0.0212 0.0493  113 ILE A CD1 
867  N N   . GLU A 114 ? 0.2986 0.2993 0.3217 -0.0285 -0.0099 0.0342  114 GLU A N   
868  C CA  . GLU A 114 ? 0.3344 0.3369 0.3594 -0.0270 -0.0076 0.0316  114 GLU A CA  
869  C C   . GLU A 114 ? 0.3288 0.3312 0.3514 -0.0247 -0.0065 0.0284  114 GLU A C   
870  O O   . GLU A 114 ? 0.2746 0.2777 0.2997 -0.0242 -0.0054 0.0269  114 GLU A O   
871  C CB  . GLU A 114 ? 0.3030 0.3080 0.3255 -0.0279 -0.0070 0.0315  114 GLU A CB  
872  C CG  . GLU A 114 ? 0.3693 0.3747 0.3936 -0.0305 -0.0082 0.0348  114 GLU A CG  
873  C CD  . GLU A 114 ? 0.4403 0.4453 0.4725 -0.0309 -0.0077 0.0369  114 GLU A CD  
874  O OE1 . GLU A 114 ? 0.4461 0.4509 0.4809 -0.0302 -0.0055 0.0348  114 GLU A OE1 
875  O OE2 . GLU A 114 ? 0.5299 0.5346 0.5655 -0.0322 -0.0093 0.0411  114 GLU A OE2 
876  N N   . ILE A 115 ? 0.2329 0.2337 0.2500 -0.0236 -0.0065 0.0276  115 ILE A N   
877  C CA  . ILE A 115 ? 0.2576 0.2583 0.2730 -0.0210 -0.0053 0.0253  115 ILE A CA  
878  C C   . ILE A 115 ? 0.3205 0.3189 0.3387 -0.0206 -0.0060 0.0248  115 ILE A C   
879  O O   . ILE A 115 ? 0.2972 0.2961 0.3163 -0.0192 -0.0051 0.0231  115 ILE A O   
880  C CB  . ILE A 115 ? 0.2907 0.2889 0.2992 -0.0199 -0.0039 0.0247  115 ILE A CB  
881  C CG1 . ILE A 115 ? 0.3735 0.3731 0.3793 -0.0202 -0.0021 0.0253  115 ILE A CG1 
882  C CG2 . ILE A 115 ? 0.3351 0.3334 0.3428 -0.0167 -0.0023 0.0231  115 ILE A CG2 
883  C CD1 . ILE A 115 ? 0.4209 0.4262 0.4305 -0.0181 -0.0004 0.0252  115 ILE A CD1 
884  N N   . GLN A 116 ? 0.3184 0.3143 0.3383 -0.0220 -0.0075 0.0269  116 GLN A N   
885  C CA  . GLN A 116 ? 0.3223 0.3159 0.3461 -0.0215 -0.0075 0.0271  116 GLN A CA  
886  C C   . GLN A 116 ? 0.3232 0.3165 0.3517 -0.0214 -0.0055 0.0261  116 GLN A C   
887  O O   . GLN A 116 ? 0.3325 0.3238 0.3610 -0.0204 -0.0042 0.0241  116 GLN A O   
888  C CB  . GLN A 116 ? 0.3173 0.3103 0.3445 -0.0234 -0.0095 0.0312  116 GLN A CB  
889  C CG  . GLN A 116 ? 0.3775 0.3682 0.4086 -0.0226 -0.0094 0.0322  116 GLN A CG  
890  C CD  . GLN A 116 ? 0.5134 0.5029 0.5531 -0.0220 -0.0070 0.0337  116 GLN A CD  
891  O OE1 . GLN A 116 ? 0.4473 0.4379 0.4909 -0.0228 -0.0060 0.0355  116 GLN A OE1 
892  N NE2 . GLN A 116 ? 0.5022 0.4887 0.5446 -0.0206 -0.0053 0.0329  116 GLN A NE2 
893  N N   . LYS A 117 ? 0.3078 0.3024 0.3394 -0.0229 -0.0048 0.0274  117 LYS A N   
894  C CA  . LYS A 117 ? 0.3312 0.3240 0.3655 -0.0238 -0.0021 0.0262  117 LYS A CA  
895  C C   . LYS A 117 ? 0.3189 0.3137 0.3487 -0.0242 -0.0017 0.0230  117 LYS A C   
896  O O   . LYS A 117 ? 0.2894 0.2814 0.3184 -0.0253 0.0000  0.0210  117 LYS A O   
897  C CB  . LYS A 117 ? 0.3137 0.3069 0.3518 -0.0255 -0.0011 0.0285  117 LYS A CB  
898  C CG  . LYS A 117 ? 0.4099 0.4022 0.4540 -0.0254 -0.0015 0.0332  117 LYS A CG  
899  C CD  . LYS A 117 ? 0.3984 0.3909 0.4468 -0.0268 0.0000  0.0359  117 LYS A CD  
900  C CE  . LYS A 117 ? 0.4616 0.4587 0.5063 -0.0280 -0.0028 0.0364  117 LYS A CE  
901  N NZ  . LYS A 117 ? 0.4811 0.4787 0.5303 -0.0293 -0.0016 0.0396  117 LYS A NZ  
902  N N   . ALA A 118 ? 0.2757 0.2755 0.3027 -0.0237 -0.0032 0.0228  118 ALA A N   
903  C CA  . ALA A 118 ? 0.2765 0.2803 0.3011 -0.0241 -0.0032 0.0214  118 ALA A CA  
904  C C   . ALA A 118 ? 0.2760 0.2791 0.2983 -0.0224 -0.0034 0.0201  118 ALA A C   
905  O O   . ALA A 118 ? 0.2631 0.2678 0.2842 -0.0239 -0.0033 0.0191  118 ALA A O   
906  C CB  . ALA A 118 ? 0.3064 0.3158 0.3301 -0.0233 -0.0038 0.0226  118 ALA A CB  
907  N N   . TYR A 119 ? 0.2457 0.2466 0.2670 -0.0198 -0.0038 0.0202  119 TYR A N   
908  C CA  . TYR A 119 ? 0.2754 0.2750 0.2946 -0.0180 -0.0037 0.0190  119 TYR A CA  
909  C C   . TYR A 119 ? 0.3007 0.2960 0.3206 -0.0196 -0.0029 0.0175  119 TYR A C   
910  O O   . TYR A 119 ? 0.2738 0.2696 0.2916 -0.0199 -0.0028 0.0163  119 TYR A O   
911  C CB  . TYR A 119 ? 0.2813 0.2779 0.2985 -0.0157 -0.0040 0.0193  119 TYR A CB  
912  C CG  . TYR A 119 ? 0.2830 0.2782 0.2975 -0.0134 -0.0035 0.0181  119 TYR A CG  
913  C CD1 . TYR A 119 ? 0.3379 0.3364 0.3504 -0.0111 -0.0026 0.0185  119 TYR A CD1 
914  C CD2 . TYR A 119 ? 0.2827 0.2735 0.2976 -0.0134 -0.0035 0.0170  119 TYR A CD2 
915  C CE1 . TYR A 119 ? 0.3215 0.3187 0.3320 -0.0087 -0.0018 0.0179  119 TYR A CE1 
916  C CE2 . TYR A 119 ? 0.3041 0.2934 0.3163 -0.0113 -0.0030 0.0159  119 TYR A CE2 
917  C CZ  . TYR A 119 ? 0.3974 0.3899 0.4073 -0.0090 -0.0023 0.0163  119 TYR A CZ  
918  O OH  . TYR A 119 ? 0.3359 0.3270 0.3436 -0.0067 -0.0015 0.0157  119 TYR A OH  
919  N N   . ASN A 120 ? 0.2770 0.2678 0.3000 -0.0208 -0.0017 0.0180  120 ASN A N   
920  C CA  . ASN A 120 ? 0.3208 0.3057 0.3443 -0.0223 0.0007  0.0166  120 ASN A CA  
921  C C   . ASN A 120 ? 0.3190 0.3037 0.3397 -0.0261 0.0020  0.0150  120 ASN A C   
922  O O   . ASN A 120 ? 0.3082 0.2891 0.3256 -0.0281 0.0035  0.0131  120 ASN A O   
923  C CB  . ASN A 120 ? 0.3309 0.3113 0.3600 -0.0221 0.0025  0.0186  120 ASN A CB  
924  C CG  . ASN A 120 ? 0.3680 0.3474 0.3993 -0.0197 0.0014  0.0201  120 ASN A CG  
925  O OD1 . ASN A 120 ? 0.3091 0.2899 0.3367 -0.0181 -0.0004 0.0189  120 ASN A OD1 
926  N ND2 . ASN A 120 ? 0.3266 0.3039 0.3643 -0.0195 0.0025  0.0234  120 ASN A ND2 
927  N N   . LEU A 121 ? 0.2638 0.2523 0.2850 -0.0279 0.0016  0.0159  121 LEU A N   
928  C CA  . LEU A 121 ? 0.3108 0.2998 0.3284 -0.0326 0.0024  0.0147  121 LEU A CA  
929  C C   . LEU A 121 ? 0.2954 0.2898 0.3090 -0.0335 0.0000  0.0143  121 LEU A C   
930  O O   . LEU A 121 ? 0.2948 0.2869 0.3036 -0.0381 0.0006  0.0128  121 LEU A O   
931  C CB  . LEU A 121 ? 0.3330 0.3264 0.3521 -0.0340 0.0018  0.0160  121 LEU A CB  
932  C CG  . LEU A 121 ? 0.4999 0.4879 0.5223 -0.0349 0.0048  0.0167  121 LEU A CG  
933  C CD1 . LEU A 121 ? 0.4311 0.4247 0.4551 -0.0355 0.0035  0.0183  121 LEU A CD1 
934  C CD2 . LEU A 121 ? 0.4619 0.4413 0.4810 -0.0395 0.0093  0.0146  121 LEU A CD2 
935  N N   . ALA A 122 ? 0.2873 0.2885 0.3026 -0.0296 -0.0025 0.0160  122 ALA A N   
936  C CA  . ALA A 122 ? 0.3058 0.3129 0.3192 -0.0296 -0.0045 0.0170  122 ALA A CA  
937  C C   . ALA A 122 ? 0.3186 0.3208 0.3292 -0.0292 -0.0040 0.0153  122 ALA A C   
938  O O   . ALA A 122 ? 0.2737 0.2786 0.2811 -0.0319 -0.0053 0.0157  122 ALA A O   
939  C CB  . ALA A 122 ? 0.3096 0.3235 0.3259 -0.0247 -0.0056 0.0195  122 ALA A CB  
940  N N   . MET A 123 ? 0.2896 0.2848 0.3012 -0.0264 -0.0024 0.0139  123 MET A N   
941  C CA  . MET A 123 ? 0.3168 0.3065 0.3259 -0.0261 -0.0015 0.0122  123 MET A CA  
942  C C   . MET A 123 ? 0.2941 0.2772 0.2989 -0.0317 0.0008  0.0100  123 MET A C   
943  O O   . MET A 123 ? 0.3090 0.2904 0.3091 -0.0340 0.0007  0.0089  123 MET A O   
944  C CB  . MET A 123 ? 0.2937 0.2781 0.3057 -0.0223 -0.0003 0.0118  123 MET A CB  
945  C CG  . MET A 123 ? 0.3072 0.2954 0.3200 -0.0178 -0.0020 0.0131  123 MET A CG  
946  S SD  . MET A 123 ? 0.3783 0.3672 0.3878 -0.0154 -0.0026 0.0127  123 MET A SD  
947  C CE  . MET A 123 ? 0.3546 0.3351 0.3623 -0.0178 -0.0007 0.0101  123 MET A CE  
948  N N   . GLN A 124 ? 0.2584 0.2372 0.2641 -0.0343 0.0034  0.0095  124 GLN A N   
949  C CA  . GLN A 124 ? 0.3220 0.2923 0.3221 -0.0402 0.0070  0.0071  124 GLN A CA  
950  C C   . GLN A 124 ? 0.3469 0.3220 0.3404 -0.0464 0.0046  0.0071  124 GLN A C   
951  O O   . GLN A 124 ? 0.3705 0.3399 0.3565 -0.0519 0.0062  0.0051  124 GLN A O   
952  C CB  . GLN A 124 ? 0.3717 0.3360 0.3747 -0.0413 0.0111  0.0071  124 GLN A CB  
953  C CG  . GLN A 124 ? 0.3741 0.3342 0.3847 -0.0361 0.0135  0.0084  124 GLN A CG  
954  C CD  . GLN A 124 ? 0.4843 0.4332 0.4940 -0.0367 0.0188  0.0069  124 GLN A CD  
955  O OE1 . GLN A 124 ? 0.4588 0.4009 0.4607 -0.0415 0.0216  0.0041  124 GLN A OE1 
956  N NE2 . GLN A 124 ? 0.4552 0.4019 0.4727 -0.0322 0.0205  0.0090  124 GLN A NE2 
957  N N   . SER A 125 ? 0.2948 0.2806 0.2908 -0.0461 0.0010  0.0097  125 SER A N   
958  C CA  . SER A 125 ? 0.3055 0.2985 0.2969 -0.0520 -0.0021 0.0112  125 SER A CA  
959  C C   . SER A 125 ? 0.3568 0.3543 0.3460 -0.0517 -0.0050 0.0125  125 SER A C   
960  O O   . SER A 125 ? 0.3162 0.3143 0.2985 -0.0586 -0.0064 0.0127  125 SER A O   
961  C CB  . SER A 125 ? 0.3539 0.3583 0.3505 -0.0506 -0.0050 0.0145  125 SER A CB  
962  O OG  . SER A 125 ? 0.5209 0.5215 0.5178 -0.0529 -0.0027 0.0134  125 SER A OG  
963  N N   . TRP A 126 ? 0.2864 0.2870 0.2810 -0.0442 -0.0060 0.0137  126 TRP A N   
964  C CA  . TRP A 126 ? 0.2972 0.3012 0.2905 -0.0428 -0.0080 0.0151  126 TRP A CA  
965  C C   . TRP A 126 ? 0.3308 0.3243 0.3165 -0.0470 -0.0059 0.0117  126 TRP A C   
966  O O   . TRP A 126 ? 0.3166 0.3123 0.2969 -0.0518 -0.0080 0.0127  126 TRP A O   
967  C CB  . TRP A 126 ? 0.3129 0.3185 0.3121 -0.0341 -0.0078 0.0160  126 TRP A CB  
968  C CG  . TRP A 126 ? 0.3211 0.3311 0.3204 -0.0313 -0.0095 0.0182  126 TRP A CG  
969  C CD1 . TRP A 126 ? 0.3375 0.3545 0.3348 -0.0348 -0.0123 0.0214  126 TRP A CD1 
970  C CD2 . TRP A 126 ? 0.3458 0.3534 0.3474 -0.0245 -0.0083 0.0179  126 TRP A CD2 
971  N NE1 . TRP A 126 ? 0.3268 0.3460 0.3258 -0.0300 -0.0126 0.0232  126 TRP A NE1 
972  C CE2 . TRP A 126 ? 0.3291 0.3420 0.3303 -0.0237 -0.0099 0.0207  126 TRP A CE2 
973  C CE3 . TRP A 126 ? 0.3208 0.3224 0.3244 -0.0198 -0.0061 0.0158  126 TRP A CE3 
974  C CZ2 . TRP A 126 ? 0.3831 0.3943 0.3855 -0.0178 -0.0087 0.0210  126 TRP A CZ2 
975  C CZ3 . TRP A 126 ? 0.3227 0.3228 0.3267 -0.0148 -0.0053 0.0160  126 TRP A CZ3 
976  C CH2 . TRP A 126 ? 0.3672 0.3715 0.3704 -0.0136 -0.0063 0.0183  126 TRP A CH2 
977  N N   . HIS A 127 ? 0.2900 0.2721 0.2756 -0.0456 -0.0016 0.0081  127 HIS A N   
978  C CA  . HIS A 127 ? 0.3211 0.2914 0.2998 -0.0494 0.0019  0.0048  127 HIS A CA  
979  C C   . HIS A 127 ? 0.3825 0.3490 0.3513 -0.0595 0.0027  0.0035  127 HIS A C   
980  O O   . HIS A 127 ? 0.3412 0.3034 0.3017 -0.0646 0.0029  0.0023  127 HIS A O   
981  C CB  . HIS A 127 ? 0.3455 0.3052 0.3279 -0.0460 0.0072  0.0025  127 HIS A CB  
982  C CG  . HIS A 127 ? 0.3709 0.3174 0.3472 -0.0494 0.0124  -0.0008 127 HIS A CG  
983  N ND1 . HIS A 127 ? 0.4219 0.3574 0.3928 -0.0553 0.0180  -0.0032 127 HIS A ND1 
984  C CD2 . HIS A 127 ? 0.3522 0.2936 0.3264 -0.0480 0.0135  -0.0021 127 HIS A CD2 
985  C CE1 . HIS A 127 ? 0.3932 0.3170 0.3590 -0.0572 0.0228  -0.0058 127 HIS A CE1 
986  N NE2 . HIS A 127 ? 0.3618 0.2893 0.3296 -0.0528 0.0199  -0.0052 127 HIS A NE2 
987  N N   . GLN A 128 ? 0.3623 0.3298 0.3308 -0.0631 0.0034  0.0037  128 GLN A N   
988  C CA  . GLN A 128 ? 0.4180 0.3810 0.3757 -0.0739 0.0044  0.0024  128 GLN A CA  
989  C C   . GLN A 128 ? 0.4035 0.3783 0.3569 -0.0793 -0.0020 0.0059  128 GLN A C   
990  O O   . GLN A 128 ? 0.3916 0.3614 0.3333 -0.0890 -0.0019 0.0048  128 GLN A O   
991  C CB  . GLN A 128 ? 0.3939 0.3558 0.3526 -0.0763 0.0065  0.0021  128 GLN A CB  
992  C CG  . GLN A 128 ? 0.5216 0.4684 0.4807 -0.0750 0.0145  -0.0013 128 GLN A CG  
993  C CD  . GLN A 128 ? 0.7037 0.6349 0.6531 -0.0798 0.0204  -0.0051 128 GLN A CD  
994  O OE1 . GLN A 128 ? 0.6823 0.6067 0.6191 -0.0899 0.0223  -0.0072 128 GLN A OE1 
995  N NE2 . GLN A 128 ? 0.6465 0.5718 0.6012 -0.0731 0.0236  -0.0060 128 GLN A NE2 
996  N N   . ALA A 129 ? 0.3231 0.3131 0.2854 -0.0738 -0.0074 0.0107  129 ALA A N   
997  C CA  . ALA A 129 ? 0.3294 0.3322 0.2903 -0.0780 -0.0134 0.0158  129 ALA A CA  
998  C C   . ALA A 129 ? 0.3755 0.3752 0.3313 -0.0789 -0.0141 0.0155  129 ALA A C   
999  O O   . ALA A 129 ? 0.3402 0.3439 0.2885 -0.0872 -0.0176 0.0179  129 ALA A O   
1000 C CB  . ALA A 129 ? 0.3417 0.3602 0.3148 -0.0704 -0.0172 0.0214  129 ALA A CB  
1001 N N   . ILE A 130 ? 0.3198 0.3128 0.2793 -0.0709 -0.0112 0.0129  130 ILE A N   
1002 C CA  . ILE A 130 ? 0.3069 0.2960 0.2616 -0.0712 -0.0114 0.0123  130 ILE A CA  
1003 C C   . ILE A 130 ? 0.3526 0.3266 0.2938 -0.0805 -0.0074 0.0074  130 ILE A C   
1004 O O   . ILE A 130 ? 0.3253 0.2984 0.2577 -0.0870 -0.0093 0.0080  130 ILE A O   
1005 C CB  . ILE A 130 ? 0.3234 0.3095 0.2858 -0.0603 -0.0092 0.0110  130 ILE A CB  
1006 C CG1 . ILE A 130 ? 0.2750 0.2751 0.2481 -0.0525 -0.0127 0.0161  130 ILE A CG1 
1007 C CG2 . ILE A 130 ? 0.2840 0.2630 0.2406 -0.0609 -0.0082 0.0091  130 ILE A CG2 
1008 C CD1 . ILE A 130 ? 0.3773 0.3739 0.3569 -0.0428 -0.0102 0.0145  130 ILE A CD1 
1009 N N   . VAL A 131 ? 0.3217 0.2832 0.2607 -0.0816 -0.0013 0.0028  131 VAL A N   
1010 C CA  . VAL A 131 ? 0.3592 0.3043 0.2847 -0.0909 0.0043  -0.0019 131 VAL A CA  
1011 C C   . VAL A 131 ? 0.3762 0.3247 0.2895 -0.1038 0.0007  -0.0003 131 VAL A C   
1012 O O   . VAL A 131 ? 0.3660 0.3068 0.2663 -0.1125 0.0015  -0.0019 131 VAL A O   
1013 C CB  . VAL A 131 ? 0.4260 0.3585 0.3530 -0.0895 0.0119  -0.0057 131 VAL A CB  
1014 C CG1 . VAL A 131 ? 0.4523 0.3673 0.3641 -0.1004 0.0188  -0.0102 131 VAL A CG1 
1015 C CG2 . VAL A 131 ? 0.4085 0.3363 0.3458 -0.0787 0.0157  -0.0068 131 VAL A CG2 
1016 N N   . GLN A 132 ? 0.3512 0.3110 0.2681 -0.1060 -0.0033 0.0031  132 GLN A N   
1017 C CA  . GLN A 132 ? 0.3788 0.3433 0.2847 -0.1191 -0.0073 0.0054  132 GLN A CA  
1018 C C   . GLN A 132 ? 0.3708 0.3466 0.2742 -0.1226 -0.0144 0.0105  132 GLN A C   
1019 O O   . GLN A 132 ? 0.3907 0.3635 0.2798 -0.1354 -0.0161 0.0108  132 GLN A O   
1020 C CB  . GLN A 132 ? 0.4851 0.4621 0.3980 -0.1193 -0.0108 0.0091  132 GLN A CB  
1021 C CG  . GLN A 132 ? 0.6628 0.6282 0.5738 -0.1205 -0.0043 0.0046  132 GLN A CG  
1022 C CD  . GLN A 132 ? 0.8581 0.8365 0.7760 -0.1207 -0.0081 0.0084  132 GLN A CD  
1023 O OE1 . GLN A 132 ? 0.9547 0.9300 0.8793 -0.1151 -0.0044 0.0066  132 GLN A OE1 
1024 N NE2 . GLN A 132 ? 0.8878 0.8815 0.8047 -0.1272 -0.0155 0.0142  132 GLN A NE2 
1025 N N   . SER A 133 ? 0.3280 0.3166 0.2448 -0.1118 -0.0183 0.0150  133 SER A N   
1026 C CA  . SER A 133 ? 0.3711 0.3708 0.2877 -0.1135 -0.0245 0.0207  133 SER A CA  
1027 C C   . SER A 133 ? 0.3964 0.3822 0.3008 -0.1179 -0.0215 0.0164  133 SER A C   
1028 O O   . SER A 133 ? 0.3689 0.3576 0.2634 -0.1276 -0.0257 0.0194  133 SER A O   
1029 C CB  . SER A 133 ? 0.4211 0.4344 0.3547 -0.0998 -0.0271 0.0256  133 SER A CB  
1030 O OG  . SER A 133 ? 0.3807 0.4055 0.3156 -0.1007 -0.0326 0.0321  133 SER A OG  
1031 N N   . ILE A 134 ? 0.3472 0.3181 0.2525 -0.1110 -0.0145 0.0101  134 ILE A N   
1032 C CA  . ILE A 134 ? 0.3184 0.2746 0.2126 -0.1145 -0.0106 0.0057  134 ILE A CA  
1033 C C   . ILE A 134 ? 0.3883 0.3310 0.2634 -0.1298 -0.0075 0.0020  134 ILE A C   
1034 O O   . ILE A 134 ? 0.4384 0.3768 0.3004 -0.1390 -0.0089 0.0020  134 ILE A O   
1035 C CB  . ILE A 134 ? 0.3440 0.2877 0.2446 -0.1040 -0.0033 0.0004  134 ILE A CB  
1036 C CG1 . ILE A 134 ? 0.2883 0.2439 0.2044 -0.0907 -0.0065 0.0038  134 ILE A CG1 
1037 C CG2 . ILE A 134 ? 0.3470 0.2731 0.2354 -0.1086 0.0024  -0.0047 134 ILE A CG2 
1038 C CD1 . ILE A 134 ? 0.3846 0.3305 0.3083 -0.0808 -0.0005 -0.0003 134 ILE A CD1 
1039 N N   . GLU A 135 ? 0.3815 0.3164 0.2536 -0.1334 -0.0029 -0.0013 135 GLU A N   
1040 C CA  . GLU A 135 ? 0.4380 0.3568 0.2904 -0.1482 0.0019  -0.0056 135 GLU A CA  
1041 C C   . GLU A 135 ? 0.4695 0.3994 0.3112 -0.1621 -0.0062 -0.0006 135 GLU A C   
1042 O O   . GLU A 135 ? 0.4670 0.3853 0.2895 -0.1760 -0.0045 -0.0030 135 GLU A O   
1043 C CB  . GLU A 135 ? 0.4496 0.3573 0.3025 -0.1478 0.0095  -0.0099 135 GLU A CB  
1044 C CG  . GLU A 135 ? 0.5629 0.4577 0.4245 -0.1362 0.0183  -0.0144 135 GLU A CG  
1045 C CD  . GLU A 135 ? 0.7172 0.5956 0.5753 -0.1384 0.0282  -0.0190 135 GLU A CD  
1046 O OE1 . GLU A 135 ? 0.7050 0.5862 0.5591 -0.1450 0.0270  -0.0183 135 GLU A OE1 
1047 O OE2 . GLU A 135 ? 0.8083 0.6713 0.6682 -0.1332 0.0374  -0.0228 135 GLU A OE2 
1048 N N   . CYS A 136 ? 0.4101 0.3623 0.2639 -0.1591 -0.0149 0.0068  136 CYS A N   
1049 C CA  . CYS A 136 ? 0.4089 0.3749 0.2553 -0.1717 -0.0237 0.0136  136 CYS A CA  
1050 C C   . CYS A 136 ? 0.3989 0.3692 0.2409 -0.1743 -0.0283 0.0172  136 CYS A C   
1051 O O   . CYS A 136 ? 0.4357 0.4028 0.2605 -0.1895 -0.0311 0.0182  136 CYS A O   
1052 C CB  . CYS A 136 ? 0.4857 0.4753 0.3489 -0.1661 -0.0311 0.0217  136 CYS A CB  
1053 S SG  . CYS A 136 ? 0.5164 0.5276 0.3752 -0.1803 -0.0428 0.0327  136 CYS A SG  
1054 N N   . GLY A 137 ? 0.3948 0.3714 0.2511 -0.1602 -0.0291 0.0190  137 GLY A N   
1055 C CA  . GLY A 137 ? 0.3511 0.3310 0.2038 -0.1616 -0.0329 0.0222  137 GLY A CA  
1056 C C   . GLY A 137 ? 0.4165 0.3739 0.2491 -0.1711 -0.0267 0.0148  137 GLY A C   
1057 O O   . GLY A 137 ? 0.4493 0.4075 0.2699 -0.1813 -0.0308 0.0176  137 GLY A O   
1058 N N   . GLN A 138 ? 0.4106 0.3474 0.2393 -0.1680 -0.0165 0.0058  138 GLN A N   
1059 C CA  . GLN A 138 ? 0.4686 0.3817 0.2781 -0.1769 -0.0087 -0.0015 138 GLN A CA  
1060 C C   . GLN A 138 ? 0.4683 0.3734 0.2556 -0.1968 -0.0089 -0.0026 138 GLN A C   
1061 O O   . GLN A 138 ? 0.5357 0.4317 0.3048 -0.2090 -0.0089 -0.0037 138 GLN A O   
1062 C CB  . GLN A 138 ? 0.5195 0.4139 0.3332 -0.1677 0.0029  -0.0095 138 GLN A CB  
1063 C CG  . GLN A 138 ? 0.5191 0.4176 0.3505 -0.1506 0.0038  -0.0093 138 GLN A CG  
1064 C CD  . GLN A 138 ? 0.5790 0.4617 0.4164 -0.1420 0.0144  -0.0155 138 GLN A CD  
1065 O OE1 . GLN A 138 ? 0.5482 0.4236 0.3844 -0.1441 0.0195  -0.0181 138 GLN A OE1 
1066 N NE2 . GLN A 138 ? 0.5473 0.4253 0.3919 -0.1321 0.0176  -0.0173 138 GLN A NE2 
1067 N N   . LYS A 139 ? 0.4404 0.3485 0.2280 -0.2009 -0.0090 -0.0022 139 LYS A N   
1068 C CA  . LYS A 139 ? 0.4931 0.3932 0.2586 -0.2207 -0.0090 -0.0033 139 LYS A CA  
1069 C C   . LYS A 139 ? 0.5290 0.4474 0.2882 -0.2326 -0.0213 0.0055  139 LYS A C   
1070 O O   . LYS A 139 ? 0.5577 0.4684 0.2950 -0.2474 -0.0210 0.0053  139 LYS A O   
1071 C CB  . LYS A 139 ? 0.5131 0.4144 0.2821 -0.2217 -0.0071 -0.0041 139 LYS A CB  
1072 C CG  . LYS A 139 ? 0.5638 0.4510 0.3091 -0.2361 -0.0021 -0.0077 139 LYS A CG  
1073 C CD  . LYS A 139 ? 0.6798 0.5599 0.4283 -0.2329 0.0047  -0.0116 139 LYS A CD  
1074 C CE  . LYS A 139 ? 0.6350 0.5135 0.3646 -0.2455 0.0046  -0.0111 139 LYS A CE  
1075 N NZ  . LYS A 139 ? 0.8359 0.7335 0.5770 -0.2467 -0.0032 -0.0053 139 LYS A NZ  
1076 N N   . GLU A 140 ? 0.4991 0.4427 0.2778 -0.2225 -0.0309 0.0146  140 GLU A N   
1077 C CA  . GLU A 140 ? 0.5036 0.4675 0.2801 -0.2323 -0.0428 0.0250  140 GLU A CA  
1078 C C   . GLU A 140 ? 0.5247 0.4868 0.2954 -0.2334 -0.0449 0.0265  140 GLU A C   
1079 O O   . GLU A 140 ? 0.5117 0.4907 0.2809 -0.2414 -0.0549 0.0360  140 GLU A O   
1080 C CB  . GLU A 140 ? 0.5304 0.5231 0.3318 -0.2212 -0.0514 0.0353  140 GLU A CB  
1081 C CG  . GLU A 140 ? 0.5424 0.5398 0.3481 -0.2229 -0.0512 0.0354  140 GLU A CG  
1082 C CD  . GLU A 140 ? 0.6975 0.7245 0.5235 -0.2174 -0.0608 0.0474  140 GLU A CD  
1083 O OE1 . GLU A 140 ? 0.7370 0.7799 0.5773 -0.2083 -0.0660 0.0551  140 GLU A OE1 
1084 O OE2 . GLU A 140 ? 0.6211 0.6547 0.4488 -0.2220 -0.0625 0.0494  140 GLU A OE2 
1085 N N   . GLY A 141 ? 0.4662 0.4086 0.2340 -0.2260 -0.0358 0.0181  141 GLY A N   
1086 C CA  . GLY A 141 ? 0.4842 0.4218 0.2445 -0.2277 -0.0365 0.0183  141 GLY A CA  
1087 C C   . GLY A 141 ? 0.5344 0.4896 0.3163 -0.2114 -0.0415 0.0246  141 GLY A C   
1088 O O   . GLY A 141 ? 0.6130 0.5660 0.3899 -0.2121 -0.0428 0.0257  141 GLY A O   
1089 N N   . GLU A 142 ? 0.5207 0.4918 0.3253 -0.1969 -0.0437 0.0287  142 GLU A N   
1090 C CA  . GLU A 142 ? 0.4995 0.4869 0.3245 -0.1814 -0.0477 0.0350  142 GLU A CA  
1091 C C   . GLU A 142 ? 0.5500 0.5234 0.3824 -0.1664 -0.0391 0.0271  142 GLU A C   
1092 O O   . GLU A 142 ? 0.4731 0.4497 0.3116 -0.1586 -0.0401 0.0292  142 GLU A O   
1093 C CB  . GLU A 142 ? 0.4801 0.4905 0.3249 -0.1739 -0.0534 0.0434  142 GLU A CB  
1094 C CG  . GLU A 142 ? 0.4932 0.5150 0.3602 -0.1550 -0.0535 0.0471  142 GLU A CG  
1095 C CD  . GLU A 142 ? 0.5324 0.5726 0.4175 -0.1475 -0.0568 0.0537  142 GLU A CD  
1096 O OE1 . GLU A 142 ? 0.5843 0.6267 0.4655 -0.1556 -0.0580 0.0538  142 GLU A OE1 
1097 O OE2 . GLU A 142 ? 0.5215 0.5735 0.4242 -0.1338 -0.0576 0.0588  142 GLU A OE2 
1098 N N   . PHE A 143 ? 0.4531 0.4112 0.2851 -0.1626 -0.0307 0.0186  143 PHE A N   
1099 C CA  . PHE A 143 ? 0.4907 0.4362 0.3302 -0.1493 -0.0227 0.0118  143 PHE A CA  
1100 C C   . PHE A 143 ? 0.5712 0.4911 0.3930 -0.1566 -0.0138 0.0028  143 PHE A C   
1101 O O   . PHE A 143 ? 0.5258 0.4340 0.3302 -0.1706 -0.0110 -0.0004 143 PHE A O   
1102 C CB  . PHE A 143 ? 0.4289 0.3755 0.2823 -0.1390 -0.0190 0.0095  143 PHE A CB  
1103 C CG  . PHE A 143 ? 0.3924 0.3613 0.2646 -0.1292 -0.0256 0.0173  143 PHE A CG  
1104 C CD1 . PHE A 143 ? 0.4127 0.3969 0.2931 -0.1244 -0.0318 0.0247  143 PHE A CD1 
1105 C CD2 . PHE A 143 ? 0.3533 0.3271 0.2352 -0.1244 -0.0247 0.0173  143 PHE A CD2 
1106 C CE1 . PHE A 143 ? 0.4508 0.4539 0.3486 -0.1150 -0.0362 0.0320  143 PHE A CE1 
1107 C CE2 . PHE A 143 ? 0.3517 0.3446 0.2504 -0.1154 -0.0297 0.0242  143 PHE A CE2 
1108 C CZ  . PHE A 143 ? 0.4024 0.4095 0.3089 -0.1107 -0.0350 0.0315  143 PHE A CZ  
1109 N N   . LYS A 144 ? 0.5485 0.4591 0.3747 -0.1470 -0.0085 -0.0012 144 LYS A N   
1110 C CA  . LYS A 144 ? 0.5872 0.4731 0.4002 -0.1509 0.0015  -0.0095 144 LYS A CA  
1111 C C   . LYS A 144 ? 0.6315 0.5049 0.4502 -0.1450 0.0108  -0.0154 144 LYS A C   
1112 O O   . LYS A 144 ? 0.6031 0.4872 0.4366 -0.1366 0.0090  -0.0133 144 LYS A O   
1113 C CB  . LYS A 144 ? 0.5923 0.4745 0.4085 -0.1433 0.0030  -0.0105 144 LYS A CB  
1114 C CG  . LYS A 144 ? 0.7721 0.6580 0.5762 -0.1525 -0.0030 -0.0068 144 LYS A CG  
1115 C CD  . LYS A 144 ? 0.7596 0.6711 0.5772 -0.1469 -0.0139 0.0030  144 LYS A CD  
1116 C CE  . LYS A 144 ? 0.8787 0.7929 0.6904 -0.1497 -0.0180 0.0065  144 LYS A CE  
1117 N NZ  . LYS A 144 ? 0.9130 0.8121 0.7003 -0.1669 -0.0161 0.0032  144 LYS A NZ  
1118 N N   . ASN A 145 ? 0.6683 0.5186 0.4751 -0.1495 0.0213  -0.0225 145 ASN A N   
1119 C CA  . ASN A 145 ? 0.7223 0.5582 0.5330 -0.1453 0.0316  -0.0276 145 ASN A CA  
1120 C C   . ASN A 145 ? 0.7455 0.5702 0.5644 -0.1346 0.0395  -0.0310 145 ASN A C   
1121 O O   . ASN A 145 ? 0.8731 0.6777 0.6865 -0.1362 0.0509  -0.0362 145 ASN A O   
1122 C CB  . ASN A 145 ? 0.7517 0.5682 0.5416 -0.1604 0.0392  -0.0323 145 ASN A CB  
1123 C CG  . ASN A 145 ? 0.9361 0.7636 0.7193 -0.1709 0.0321  -0.0289 145 ASN A CG  
1124 O OD1 . ASN A 145 ? 0.9444 0.7779 0.7148 -0.1826 0.0249  -0.0259 145 ASN A OD1 
1125 N ND2 . ASN A 145 ? 0.9763 0.8068 0.7683 -0.1671 0.0337  -0.0288 145 ASN A ND2 
1126 N N   . ARG A 146 ? 0.7385 0.5761 0.5710 -0.1236 0.0340  -0.0278 146 ARG A N   
1127 C CA  . ARG A 146 ? 0.8122 0.6416 0.6534 -0.1134 0.0402  -0.0303 146 ARG A CA  
1128 C C   . ARG A 146 ? 0.7644 0.5871 0.6174 -0.1059 0.0480  -0.0322 146 ARG A C   
1129 O O   . ARG A 146 ? 0.8682 0.6727 0.7182 -0.1062 0.0587  -0.0361 146 ARG A O   
1130 C CB  . ARG A 146 ? 0.7206 0.5670 0.5752 -0.1029 0.0322  -0.0261 146 ARG A CB  
1131 C CG  . ARG A 146 ? 0.8609 0.7039 0.7075 -0.1050 0.0310  -0.0264 146 ARG A CG  
1132 C CD  . ARG A 146 ? 0.7648 0.6273 0.6224 -0.0970 0.0216  -0.0208 146 ARG A CD  
1133 N NE  . ARG A 146 ? 0.7752 0.6428 0.6218 -0.1049 0.0154  -0.0178 146 ARG A NE  
1134 C CZ  . ARG A 146 ? 0.7862 0.6725 0.6366 -0.1054 0.0061  -0.0111 146 ARG A CZ  
1135 N NH1 . ARG A 146 ? 0.6624 0.5632 0.5267 -0.0984 0.0021  -0.0073 146 ARG A NH1 
1136 N NH2 . ARG A 146 ? 0.8704 0.7611 0.7109 -0.1132 0.0008  -0.0075 146 ARG A NH2 
1137 N N   . SER A 147 ? 0.6754 0.5129 0.5423 -0.0991 0.0429  -0.0288 147 SER A N   
1138 C CA  . SER A 147 ? 0.7158 0.5500 0.5947 -0.0922 0.0487  -0.0292 147 SER A CA  
1139 C C   . SER A 147 ? 0.7394 0.5780 0.6162 -0.0975 0.0470  -0.0283 147 SER A C   
1140 O O   . SER A 147 ? 0.6704 0.5181 0.5395 -0.1047 0.0398  -0.0264 147 SER A O   
1141 C CB  . SER A 147 ? 0.6867 0.5340 0.5847 -0.0788 0.0445  -0.0260 147 SER A CB  
1142 O OG  . SER A 147 ? 0.6555 0.5119 0.5539 -0.0760 0.0379  -0.0242 147 SER A OG  
1143 N N   . ASN A 148 ? 0.6589 0.4914 0.5433 -0.0939 0.0536  -0.0290 148 ASN A N   
1144 C CA  . ASN A 148 ? 0.6742 0.5095 0.5566 -0.0987 0.0528  -0.0284 148 ASN A CA  
1145 C C   . ASN A 148 ? 0.5880 0.4455 0.4824 -0.0926 0.0421  -0.0236 148 ASN A C   
1146 O O   . ASN A 148 ? 0.5238 0.3920 0.4309 -0.0827 0.0377  -0.0211 148 ASN A O   
1147 C CB  . ASN A 148 ? 0.7305 0.5521 0.6178 -0.0964 0.0637  -0.0301 148 ASN A CB  
1148 C CG  . ASN A 148 ? 0.7279 0.5587 0.6360 -0.0834 0.0629  -0.0266 148 ASN A CG  
1149 O OD1 . ASN A 148 ? 0.7097 0.5568 0.6271 -0.0789 0.0550  -0.0233 148 ASN A OD1 
1150 N ND2 . ASN A 148 ? 0.8328 0.6530 0.7481 -0.0777 0.0712  -0.0270 148 ASN A ND2 
1151 N N   . SER A 149 ? 0.5820 0.4457 0.4717 -0.0991 0.0384  -0.0224 149 SER A N   
1152 C CA  . SER A 149 ? 0.4872 0.3718 0.3859 -0.0953 0.0283  -0.0176 149 SER A CA  
1153 C C   . SER A 149 ? 0.4425 0.3346 0.3585 -0.0839 0.0280  -0.0156 149 SER A C   
1154 O O   . SER A 149 ? 0.4093 0.3170 0.3348 -0.0775 0.0209  -0.0119 149 SER A O   
1155 C CB  . SER A 149 ? 0.5049 0.3937 0.3941 -0.1060 0.0250  -0.0166 149 SER A CB  
1156 O OG  . SER A 149 ? 0.5173 0.3955 0.4048 -0.1086 0.0321  -0.0192 149 SER A OG  
1157 N N   . THR A 150 ? 0.4440 0.3250 0.3639 -0.0816 0.0360  -0.0175 150 THR A N   
1158 C CA  . THR A 150 ? 0.4572 0.3455 0.3930 -0.0716 0.0353  -0.0150 150 THR A CA  
1159 C C   . THR A 150 ? 0.4320 0.3246 0.3775 -0.0624 0.0334  -0.0137 150 THR A C   
1160 O O   . THR A 150 ? 0.3991 0.3042 0.3549 -0.0554 0.0280  -0.0107 150 THR A O   
1161 C CB  . THR A 150 ? 0.5055 0.3811 0.4441 -0.0715 0.0445  -0.0163 150 THR A CB  
1162 O OG1 . THR A 150 ? 0.5657 0.4388 0.4960 -0.0796 0.0456  -0.0173 150 THR A OG1 
1163 C CG2 . THR A 150 ? 0.4797 0.3628 0.4351 -0.0615 0.0436  -0.0130 150 THR A CG2 
1164 N N   . ASP A 151 ? 0.4021 0.2839 0.3433 -0.0629 0.0380  -0.0160 151 ASP A N   
1165 C CA  . ASP A 151 ? 0.4137 0.2988 0.3630 -0.0550 0.0365  -0.0149 151 ASP A CA  
1166 C C   . ASP A 151 ? 0.3781 0.2770 0.3271 -0.0531 0.0275  -0.0129 151 ASP A C   
1167 O O   . ASP A 151 ? 0.3224 0.2302 0.2809 -0.0455 0.0238  -0.0106 151 ASP A O   
1168 C CB  . ASP A 151 ? 0.4571 0.3271 0.4006 -0.0568 0.0436  -0.0179 151 ASP A CB  
1169 C CG  . ASP A 151 ? 0.5605 0.4183 0.5105 -0.0545 0.0533  -0.0182 151 ASP A CG  
1170 O OD1 . ASP A 151 ? 0.4913 0.3545 0.4530 -0.0493 0.0532  -0.0153 151 ASP A OD1 
1171 O OD2 . ASP A 151 ? 0.5740 0.4164 0.5173 -0.0578 0.0614  -0.0210 151 ASP A OD2 
1172 N N   . ILE A 152 ? 0.3593 0.2597 0.2972 -0.0604 0.0245  -0.0133 152 ILE A N   
1173 C CA  . ILE A 152 ? 0.3903 0.3039 0.3287 -0.0586 0.0167  -0.0103 152 ILE A CA  
1174 C C   . ILE A 152 ? 0.3121 0.2405 0.2598 -0.0539 0.0113  -0.0065 152 ILE A C   
1175 O O   . ILE A 152 ? 0.2713 0.2092 0.2258 -0.0473 0.0074  -0.0039 152 ILE A O   
1176 C CB  . ILE A 152 ? 0.3787 0.2921 0.3037 -0.0685 0.0142  -0.0103 152 ILE A CB  
1177 C CG1 . ILE A 152 ? 0.3929 0.2902 0.3073 -0.0733 0.0201  -0.0144 152 ILE A CG1 
1178 C CG2 . ILE A 152 ? 0.3263 0.2551 0.2540 -0.0661 0.0063  -0.0056 152 ILE A CG2 
1179 C CD1 . ILE A 152 ? 0.4689 0.3628 0.3671 -0.0857 0.0186  -0.0149 152 ILE A CD1 
1180 N N   . ALA A 153 ? 0.3039 0.2335 0.2516 -0.0574 0.0118  -0.0062 153 ALA A N   
1181 C CA  . ALA A 153 ? 0.3400 0.2829 0.2960 -0.0535 0.0072  -0.0027 153 ALA A CA  
1182 C C   . ALA A 153 ? 0.3285 0.2735 0.2956 -0.0440 0.0078  -0.0020 153 ALA A C   
1183 O O   . ALA A 153 ? 0.2858 0.2413 0.2587 -0.0388 0.0037  0.0009  153 ALA A O   
1184 C CB  . ALA A 153 ? 0.3089 0.2509 0.2623 -0.0593 0.0084  -0.0030 153 ALA A CB  
1185 N N   . TRP A 154 ? 0.3143 0.2493 0.2844 -0.0420 0.0131  -0.0042 154 TRP A N   
1186 C CA  . TRP A 154 ? 0.3596 0.2972 0.3396 -0.0343 0.0129  -0.0028 154 TRP A CA  
1187 C C   . TRP A 154 ? 0.2873 0.2274 0.2683 -0.0297 0.0107  -0.0024 154 TRP A C   
1188 O O   . TRP A 154 ? 0.3066 0.2535 0.2931 -0.0244 0.0080  -0.0005 154 TRP A O   
1189 C CB  . TRP A 154 ? 0.3553 0.2829 0.3399 -0.0333 0.0190  -0.0038 154 TRP A CB  
1190 C CG  . TRP A 154 ? 0.3272 0.2543 0.3147 -0.0352 0.0210  -0.0030 154 TRP A CG  
1191 C CD1 . TRP A 154 ? 0.4390 0.3553 0.4239 -0.0393 0.0275  -0.0045 154 TRP A CD1 
1192 C CD2 . TRP A 154 ? 0.3506 0.2872 0.3434 -0.0331 0.0173  -0.0005 154 TRP A CD2 
1193 N NE1 . TRP A 154 ? 0.3999 0.3191 0.3889 -0.0397 0.0277  -0.0030 154 TRP A NE1 
1194 C CE2 . TRP A 154 ? 0.3583 0.2902 0.3520 -0.0360 0.0212  -0.0006 154 TRP A CE2 
1195 C CE3 . TRP A 154 ? 0.3573 0.3051 0.3538 -0.0291 0.0117  0.0017  154 TRP A CE3 
1196 C CZ2 . TRP A 154 ? 0.4138 0.3526 0.4122 -0.0351 0.0190  0.0015  154 TRP A CZ2 
1197 C CZ3 . TRP A 154 ? 0.3737 0.3276 0.3743 -0.0284 0.0100  0.0036  154 TRP A CZ3 
1198 C CH2 . TRP A 154 ? 0.3897 0.3395 0.3913 -0.0314 0.0132  0.0036  154 TRP A CH2 
1199 N N   . ARG A 155 ? 0.2763 0.2100 0.2508 -0.0321 0.0123  -0.0044 155 ARG A N   
1200 C CA  . ARG A 155 ? 0.2729 0.2084 0.2478 -0.0279 0.0105  -0.0041 155 ARG A CA  
1201 C C   . ARG A 155 ? 0.3159 0.2631 0.2909 -0.0261 0.0053  -0.0011 155 ARG A C   
1202 O O   . ARG A 155 ? 0.2995 0.2506 0.2782 -0.0205 0.0039  0.0002  155 ARG A O   
1203 C CB  . ARG A 155 ? 0.3617 0.2877 0.3290 -0.0316 0.0134  -0.0067 155 ARG A CB  
1204 C CG  . ARG A 155 ? 0.3556 0.2693 0.3246 -0.0315 0.0200  -0.0090 155 ARG A CG  
1205 C CD  . ARG A 155 ? 0.3475 0.2532 0.3119 -0.0317 0.0225  -0.0111 155 ARG A CD  
1206 N NE  . ARG A 155 ? 0.3878 0.2874 0.3402 -0.0393 0.0237  -0.0132 155 ARG A NE  
1207 C CZ  . ARG A 155 ? 0.4991 0.3855 0.4453 -0.0447 0.0303  -0.0161 155 ARG A CZ  
1208 N NH1 . ARG A 155 ? 0.4193 0.2976 0.3716 -0.0427 0.0367  -0.0167 155 ARG A NH1 
1209 N NH2 . ARG A 155 ? 0.4729 0.3536 0.4059 -0.0527 0.0308  -0.0180 155 ARG A NH2 
1210 N N   . LEU A 156 ? 0.2956 0.2486 0.2668 -0.0310 0.0027  0.0005  156 LEU A N   
1211 C CA  . LEU A 156 ? 0.2583 0.2235 0.2316 -0.0290 -0.0018 0.0048  156 LEU A CA  
1212 C C   . LEU A 156 ? 0.3069 0.2785 0.2881 -0.0234 -0.0025 0.0067  156 LEU A C   
1213 O O   . LEU A 156 ? 0.2540 0.2309 0.2386 -0.0181 -0.0035 0.0090  156 LEU A O   
1214 C CB  . LEU A 156 ? 0.2755 0.2464 0.2438 -0.0364 -0.0046 0.0069  156 LEU A CB  
1215 C CG  . LEU A 156 ? 0.2960 0.2624 0.2547 -0.0430 -0.0050 0.0062  156 LEU A CG  
1216 C CD1 . LEU A 156 ? 0.3009 0.2742 0.2540 -0.0518 -0.0087 0.0091  156 LEU A CD1 
1217 C CD2 . LEU A 156 ? 0.3012 0.2704 0.2608 -0.0385 -0.0064 0.0081  156 LEU A CD2 
1218 N N   . ILE A 157 ? 0.2383 0.2083 0.2217 -0.0248 -0.0013 0.0057  157 ILE A N   
1219 C CA  . ILE A 157 ? 0.2608 0.2358 0.2506 -0.0203 -0.0018 0.0073  157 ILE A CA  
1220 C C   . ILE A 157 ? 0.2665 0.2377 0.2591 -0.0148 -0.0005 0.0064  157 ILE A C   
1221 O O   . ILE A 157 ? 0.2978 0.2734 0.2928 -0.0105 -0.0012 0.0082  157 ILE A O   
1222 C CB  . ILE A 157 ? 0.2666 0.2398 0.2581 -0.0232 -0.0007 0.0064  157 ILE A CB  
1223 C CG1 . ILE A 157 ? 0.2790 0.2591 0.2686 -0.0281 -0.0029 0.0083  157 ILE A CG1 
1224 C CG2 . ILE A 157 ? 0.3222 0.2970 0.3196 -0.0187 -0.0005 0.0073  157 ILE A CG2 
1225 C CD1 . ILE A 157 ? 0.3722 0.3484 0.3613 -0.0323 -0.0010 0.0069  157 ILE A CD1 
1226 N N   . ALA A 158 ? 0.2448 0.2072 0.2366 -0.0152 0.0020  0.0038  158 ALA A N   
1227 C CA  . ALA A 158 ? 0.2705 0.2297 0.2647 -0.0109 0.0028  0.0034  158 ALA A CA  
1228 C C   . ALA A 158 ? 0.2766 0.2381 0.2685 -0.0076 0.0019  0.0041  158 ALA A C   
1229 O O   . ALA A 158 ? 0.2812 0.2435 0.2742 -0.0040 0.0019  0.0048  158 ALA A O   
1230 C CB  . ALA A 158 ? 0.2945 0.2446 0.2891 -0.0121 0.0059  0.0013  158 ALA A CB  
1231 N N   . PHE A 159 ? 0.2504 0.2126 0.2384 -0.0093 0.0014  0.0042  159 PHE A N   
1232 C CA  . PHE A 159 ? 0.2803 0.2446 0.2667 -0.0058 0.0009  0.0055  159 PHE A CA  
1233 C C   . PHE A 159 ? 0.2671 0.2393 0.2564 -0.0023 0.0002  0.0089  159 PHE A C   
1234 O O   . PHE A 159 ? 0.2879 0.2587 0.2773 0.0020  0.0017  0.0093  159 PHE A O   
1235 C CB  . PHE A 159 ? 0.2871 0.2521 0.2691 -0.0089 -0.0001 0.0060  159 PHE A CB  
1236 C CG  . PHE A 159 ? 0.3202 0.2877 0.3014 -0.0051 -0.0003 0.0082  159 PHE A CG  
1237 C CD1 . PHE A 159 ? 0.3609 0.3214 0.3404 -0.0023 0.0017  0.0059  159 PHE A CD1 
1238 C CD2 . PHE A 159 ? 0.3022 0.2793 0.2854 -0.0040 -0.0021 0.0130  159 PHE A CD2 
1239 C CE1 . PHE A 159 ? 0.3888 0.3508 0.3674 0.0015  0.0022  0.0079  159 PHE A CE1 
1240 C CE2 . PHE A 159 ? 0.3462 0.3255 0.3298 0.0002  -0.0014 0.0158  159 PHE A CE2 
1241 C CZ  . PHE A 159 ? 0.3827 0.3540 0.3635 0.0029  0.0009  0.0129  159 PHE A CZ  
1242 N N   . VAL A 160 ? 0.2846 0.2644 0.2757 -0.0043 -0.0016 0.0116  160 VAL A N   
1243 C CA  . VAL A 160 ? 0.2501 0.2375 0.2447 -0.0006 -0.0015 0.0156  160 VAL A CA  
1244 C C   . VAL A 160 ? 0.2628 0.2476 0.2590 0.0021  0.0004  0.0145  160 VAL A C   
1245 O O   . VAL A 160 ? 0.2673 0.2527 0.2640 0.0063  0.0026  0.0162  160 VAL A O   
1246 C CB  . VAL A 160 ? 0.2883 0.2857 0.2854 -0.0038 -0.0040 0.0195  160 VAL A CB  
1247 C CG1 . VAL A 160 ? 0.3375 0.3376 0.3316 -0.0077 -0.0064 0.0211  160 VAL A CG1 
1248 C CG2 . VAL A 160 ? 0.2749 0.2717 0.2722 -0.0080 -0.0049 0.0176  160 VAL A CG2 
1249 N N   . CYS A 161 ? 0.2630 0.2442 0.2594 -0.0006 0.0000  0.0120  161 CYS A N   
1250 C CA  . CYS A 161 ? 0.2833 0.2618 0.2803 0.0010  0.0011  0.0114  161 CYS A CA  
1251 C C   . CYS A 161 ? 0.2495 0.2213 0.2435 0.0033  0.0029  0.0097  161 CYS A C   
1252 O O   . CYS A 161 ? 0.2836 0.2536 0.2756 0.0054  0.0047  0.0102  161 CYS A O   
1253 C CB  . CYS A 161 ? 0.2762 0.2530 0.2751 -0.0024 0.0001  0.0100  161 CYS A CB  
1254 S SG  . CYS A 161 ? 0.3549 0.3388 0.3566 -0.0056 -0.0014 0.0117  161 CYS A SG  
1255 N N   . GLY A 162 ? 0.2386 0.2056 0.2312 0.0025  0.0028  0.0077  162 GLY A N   
1256 C CA  . GLY A 162 ? 0.2718 0.2326 0.2614 0.0042  0.0043  0.0063  162 GLY A CA  
1257 C C   . GLY A 162 ? 0.2785 0.2392 0.2650 0.0080  0.0065  0.0074  162 GLY A C   
1258 O O   . GLY A 162 ? 0.2580 0.2139 0.2409 0.0095  0.0086  0.0067  162 GLY A O   
1259 N N   . LEU A 163 ? 0.2393 0.2053 0.2272 0.0091  0.0062  0.0096  163 LEU A N   
1260 C CA  . LEU A 163 ? 0.2647 0.2313 0.2514 0.0133  0.0089  0.0118  163 LEU A CA  
1261 C C   . LEU A 163 ? 0.3141 0.2818 0.3011 0.0160  0.0120  0.0139  163 LEU A C   
1262 O O   . LEU A 163 ? 0.2905 0.2528 0.2739 0.0190  0.0161  0.0139  163 LEU A O   
1263 C CB  . LEU A 163 ? 0.2975 0.2711 0.2866 0.0134  0.0073  0.0150  163 LEU A CB  
1264 C CG  . LEU A 163 ? 0.4371 0.4115 0.4261 0.0178  0.0099  0.0182  163 LEU A CG  
1265 C CD1 . LEU A 163 ? 0.3653 0.3297 0.3492 0.0195  0.0127  0.0147  163 LEU A CD1 
1266 C CD2 . LEU A 163 ? 0.4117 0.3932 0.4027 0.0160  0.0069  0.0215  163 LEU A CD2 
1267 N N   . GLU A 164 ? 0.2959 0.2695 0.2865 0.0147  0.0106  0.0155  164 GLU A N   
1268 C CA  . GLU A 164 ? 0.3464 0.3201 0.3369 0.0167  0.0139  0.0172  164 GLU A CA  
1269 C C   . GLU A 164 ? 0.3341 0.2984 0.3182 0.0154  0.0158  0.0138  164 GLU A C   
1270 O O   . GLU A 164 ? 0.3407 0.3001 0.3207 0.0174  0.0206  0.0142  164 GLU A O   
1271 C CB  . GLU A 164 ? 0.3804 0.3619 0.3757 0.0147  0.0116  0.0190  164 GLU A CB  
1272 C CG  . GLU A 164 ? 0.5695 0.5611 0.5704 0.0143  0.0090  0.0228  164 GLU A CG  
1273 C CD  . GLU A 164 ? 0.7513 0.7488 0.7554 0.0105  0.0058  0.0233  164 GLU A CD  
1274 O OE1 . GLU A 164 ? 0.6691 0.6731 0.6755 0.0075  0.0025  0.0249  164 GLU A OE1 
1275 O OE2 . GLU A 164 ? 0.9241 0.9194 0.9275 0.0099  0.0066  0.0220  164 GLU A OE2 
1276 N N   . GLY A 165 ? 0.2995 0.2611 0.2826 0.0116  0.0124  0.0109  165 GLY A N   
1277 C CA  . GLY A 165 ? 0.2881 0.2421 0.2654 0.0093  0.0131  0.0087  165 GLY A CA  
1278 C C   . GLY A 165 ? 0.3413 0.2874 0.3121 0.0108  0.0166  0.0073  165 GLY A C   
1279 O O   . GLY A 165 ? 0.3812 0.3204 0.3448 0.0095  0.0195  0.0064  165 GLY A O   
1280 N N   . ILE A 166 ? 0.3030 0.2493 0.2751 0.0129  0.0166  0.0071  166 ILE A N   
1281 C CA  . ILE A 166 ? 0.3237 0.2622 0.2897 0.0145  0.0201  0.0058  166 ILE A CA  
1282 C C   . ILE A 166 ? 0.3935 0.3294 0.3566 0.0186  0.0264  0.0078  166 ILE A C   
1283 O O   . ILE A 166 ? 0.3231 0.2496 0.2781 0.0186  0.0311  0.0063  166 ILE A O   
1284 C CB  . ILE A 166 ? 0.3809 0.3205 0.3495 0.0157  0.0184  0.0053  166 ILE A CB  
1285 C CG1 . ILE A 166 ? 0.4857 0.4248 0.4560 0.0118  0.0142  0.0032  166 ILE A CG1 
1286 C CG2 . ILE A 166 ? 0.4970 0.4291 0.4596 0.0181  0.0225  0.0044  166 ILE A CG2 
1287 C CD1 . ILE A 166 ? 0.4986 0.4313 0.4642 0.0086  0.0141  0.0015  166 ILE A CD1 
1288 N N   . TYR A 167 ? 0.3256 0.2695 0.2952 0.0218  0.0271  0.0115  167 TYR A N   
1289 C CA  . TYR A 167 ? 0.3757 0.3180 0.3448 0.0263  0.0339  0.0146  167 TYR A CA  
1290 C C   . TYR A 167 ? 0.3526 0.2873 0.3146 0.0244  0.0381  0.0131  167 TYR A C   
1291 O O   . TYR A 167 ? 0.4003 0.3267 0.3567 0.0269  0.0457  0.0136  167 TYR A O   
1292 C CB  . TYR A 167 ? 0.3337 0.2880 0.3128 0.0293  0.0329  0.0199  167 TYR A CB  
1293 C CG  . TYR A 167 ? 0.3978 0.3593 0.3824 0.0308  0.0298  0.0224  167 TYR A CG  
1294 C CD1 . TYR A 167 ? 0.4655 0.4215 0.4466 0.0322  0.0311  0.0212  167 TYR A CD1 
1295 C CD2 . TYR A 167 ? 0.4359 0.4095 0.4284 0.0300  0.0253  0.0262  167 TYR A CD2 
1296 C CE1 . TYR A 167 ? 0.4867 0.4490 0.4721 0.0330  0.0281  0.0237  167 TYR A CE1 
1297 C CE2 . TYR A 167 ? 0.3685 0.3484 0.3646 0.0300  0.0221  0.0288  167 TYR A CE2 
1298 C CZ  . TYR A 167 ? 0.4295 0.4037 0.4220 0.0316  0.0235  0.0275  167 TYR A CZ  
1299 O OH  . TYR A 167 ? 0.5703 0.5504 0.5655 0.0310  0.0202  0.0302  167 TYR A OH  
1300 N N   . LYS A 168 ? 0.3117 0.2485 0.2736 0.0198  0.0337  0.0115  168 LYS A N   
1301 C CA  . LYS A 168 ? 0.3497 0.2796 0.3041 0.0169  0.0369  0.0103  168 LYS A CA  
1302 C C   . LYS A 168 ? 0.3740 0.2909 0.3159 0.0135  0.0400  0.0069  168 LYS A C   
1303 O O   . LYS A 168 ? 0.3869 0.2951 0.3196 0.0111  0.0449  0.0059  168 LYS A O   
1304 C CB  . LYS A 168 ? 0.4055 0.3409 0.3627 0.0123  0.0307  0.0097  168 LYS A CB  
1305 C CG  . LYS A 168 ? 0.6427 0.5770 0.5975 0.0114  0.0338  0.0108  168 LYS A CG  
1306 C CD  . LYS A 168 ? 0.5997 0.5397 0.5576 0.0070  0.0275  0.0105  168 LYS A CD  
1307 C CE  . LYS A 168 ? 0.6241 0.5566 0.5724 0.0022  0.0295  0.0094  168 LYS A CE  
1308 N NZ  . LYS A 168 ? 0.6845 0.6236 0.6375 0.0002  0.0262  0.0107  168 LYS A NZ  
1309 N N   . LEU A 169 ? 0.3448 0.2595 0.2853 0.0127  0.0376  0.0050  169 LEU A N   
1310 C CA  . LEU A 169 ? 0.3533 0.2564 0.2819 0.0083  0.0396  0.0019  169 LEU A CA  
1311 C C   . LEU A 169 ? 0.4097 0.3016 0.3298 0.0113  0.0491  0.0015  169 LEU A C   
1312 O O   . LEU A 169 ? 0.4275 0.3074 0.3345 0.0065  0.0528  -0.0011 169 LEU A O   
1313 C CB  . LEU A 169 ? 0.3615 0.2662 0.2922 0.0065  0.0341  0.0005  169 LEU A CB  
1314 C CG  . LEU A 169 ? 0.3119 0.2255 0.2505 0.0032  0.0259  0.0009  169 LEU A CG  
1315 C CD1 . LEU A 169 ? 0.3485 0.2626 0.2899 0.0027  0.0225  -0.0002 169 LEU A CD1 
1316 C CD2 . LEU A 169 ? 0.3279 0.2396 0.2615 -0.0034 0.0234  0.0008  169 LEU A CD2 
1317 N N   . GLY A 170 ? 0.4053 0.3006 0.3322 0.0185  0.0535  0.0045  170 GLY A N   
1318 C CA  . GLY A 170 ? 0.3711 0.2557 0.2916 0.0223  0.0635  0.0050  170 GLY A CA  
1319 C C   . GLY A 170 ? 0.4511 0.3285 0.3656 0.0215  0.0641  0.0024  170 GLY A C   
1320 O O   . GLY A 170 ? 0.4378 0.3011 0.3396 0.0194  0.0710  -0.0001 170 GLY A O   
1321 N N   . LEU A 171 ? 0.3607 0.2468 0.2833 0.0227  0.0572  0.0027  171 LEU A N   
1322 C CA  . LEU A 171 ? 0.4550 0.3357 0.3735 0.0224  0.0572  0.0005  171 LEU A CA  
1323 C C   . LEU A 171 ? 0.5702 0.4468 0.4893 0.0293  0.0652  0.0030  171 LEU A C   
1324 O O   . LEU A 171 ? 0.5199 0.4035 0.4479 0.0352  0.0678  0.0077  171 LEU A O   
1325 C CB  . LEU A 171 ? 0.4555 0.3462 0.3826 0.0215  0.0481  0.0002  171 LEU A CB  
1326 C CG  . LEU A 171 ? 0.4655 0.3602 0.3934 0.0151  0.0406  -0.0015 171 LEU A CG  
1327 C CD1 . LEU A 171 ? 0.3762 0.2811 0.3146 0.0156  0.0335  -0.0009 171 LEU A CD1 
1328 C CD2 . LEU A 171 ? 0.4539 0.3389 0.3710 0.0090  0.0406  -0.0047 171 LEU A CD2 
1329 N N   . GLN A 172 ? 0.5480 0.4136 0.4581 0.0284  0.0692  0.0004  172 GLN A N   
1330 C CA  . GLN A 172 ? 0.5795 0.4403 0.4900 0.0350  0.0771  0.0028  172 GLN A CA  
1331 C C   . GLN A 172 ? 0.5875 0.4597 0.5093 0.0390  0.0714  0.0055  172 GLN A C   
1332 O O   . GLN A 172 ? 0.5594 0.4370 0.4834 0.0354  0.0631  0.0032  172 GLN A O   
1333 C CB  . GLN A 172 ? 0.6362 0.4802 0.5319 0.0319  0.0835  -0.0013 172 GLN A CB  
1334 C CG  . GLN A 172 ? 0.6876 0.5180 0.5687 0.0260  0.0894  -0.0045 172 GLN A CG  
1335 C CD  . GLN A 172 ? 0.7269 0.5531 0.6084 0.0308  0.0994  -0.0012 172 GLN A CD  
1336 O OE1 . GLN A 172 ? 0.7797 0.5985 0.6605 0.0368  0.1097  0.0013  172 GLN A OE1 
1337 N NE2 . GLN A 172 ? 0.6556 0.4863 0.5386 0.0282  0.0970  -0.0007 172 GLN A NE2 
1338 N N   . GLY A 173 ? 0.6071 0.4829 0.5360 0.0462  0.0764  0.0109  173 GLY A N   
1339 C CA  . GLY A 173 ? 0.4715 0.3573 0.4095 0.0494  0.0715  0.0140  173 GLY A CA  
1340 C C   . GLY A 173 ? 0.5088 0.4098 0.4567 0.0475  0.0616  0.0156  173 GLY A C   
1341 O O   . GLY A 173 ? 0.6410 0.5475 0.5922 0.0466  0.0556  0.0153  173 GLY A O   
1342 N N   . LEU A 174 ? 0.5278 0.4346 0.4796 0.0466  0.0603  0.0171  174 LEU A N   
1343 C CA  . LEU A 174 ? 0.4989 0.4197 0.4598 0.0447  0.0519  0.0190  174 LEU A CA  
1344 C C   . LEU A 174 ? 0.5248 0.4539 0.4940 0.0485  0.0547  0.0254  174 LEU A C   
1345 O O   . LEU A 174 ? 0.5467 0.4711 0.5131 0.0487  0.0596  0.0250  174 LEU A O   
1346 C CB  . LEU A 174 ? 0.4602 0.3800 0.4175 0.0382  0.0460  0.0137  174 LEU A CB  
1347 C CG  . LEU A 174 ? 0.5683 0.5005 0.5336 0.0357  0.0383  0.0150  174 LEU A CG  
1348 C CD1 . LEU A 174 ? 0.5881 0.5267 0.5579 0.0359  0.0338  0.0166  174 LEU A CD1 
1349 C CD2 . LEU A 174 ? 0.4514 0.3815 0.4137 0.0300  0.0338  0.0105  174 LEU A CD2 
1350 N N   . ALA A 175 ? 0.5183 0.4600 0.4975 0.0511  0.0516  0.0315  175 ALA A N   
1351 C CA  . ALA A 175 ? 0.4738 0.4253 0.4630 0.0553  0.0545  0.0394  175 ALA A CA  
1352 C C   . ALA A 175 ? 0.5258 0.4893 0.5208 0.0513  0.0467  0.0403  175 ALA A C   
1353 O O   . ALA A 175 ? 0.4636 0.4349 0.4610 0.0476  0.0389  0.0403  175 ALA A O   
1354 C CB  . ALA A 175 ? 0.5354 0.4943 0.5327 0.0605  0.0561  0.0474  175 ALA A CB  
1355 N N   . GLU A 176 ? 0.5219 0.4860 0.5185 0.0516  0.0495  0.0411  176 GLU A N   
1356 C CA  . GLU A 176 ? 0.4687 0.4441 0.4712 0.0481  0.0431  0.0426  176 GLU A CA  
1357 C C   . GLU A 176 ? 0.5193 0.5105 0.5327 0.0490  0.0388  0.0506  176 GLU A C   
1358 O O   . GLU A 176 ? 0.4388 0.4392 0.4551 0.0441  0.0314  0.0508  176 GLU A O   
1359 C CB  . GLU A 176 ? 0.5376 0.5113 0.5411 0.0497  0.0484  0.0437  176 GLU A CB  
1360 C CG  . GLU A 176 ? 0.5074 0.4665 0.4992 0.0470  0.0518  0.0363  176 GLU A CG  
1361 C CD  . GLU A 176 ? 0.5267 0.4865 0.5190 0.0458  0.0534  0.0364  176 GLU A CD  
1362 O OE1 . GLU A 176 ? 0.5766 0.5489 0.5788 0.0467  0.0510  0.0416  176 GLU A OE1 
1363 O OE2 . GLU A 176 ? 0.5187 0.4666 0.5011 0.0434  0.0571  0.0315  176 GLU A OE2 
1364 N N   . GLU A 177 ? 0.4333 0.4278 0.4526 0.0547  0.0434  0.0577  177 GLU A N   
1365 C CA  . GLU A 177 ? 0.4957 0.5065 0.5261 0.0553  0.0393  0.0672  177 GLU A CA  
1366 C C   . GLU A 177 ? 0.5047 0.5204 0.5322 0.0490  0.0299  0.0651  177 GLU A C   
1367 O O   . GLU A 177 ? 0.4834 0.5132 0.5177 0.0462  0.0241  0.0716  177 GLU A O   
1368 C CB  . GLU A 177 ? 0.5616 0.5738 0.5990 0.0630  0.0469  0.0756  177 GLU A CB  
1369 C CG  . GLU A 177 ? 0.6965 0.7096 0.7417 0.0695  0.0562  0.0820  177 GLU A CG  
1370 C CD  . GLU A 177 ? 0.8154 0.8127 0.8507 0.0695  0.0628  0.0737  177 GLU A CD  
1371 O OE1 . GLU A 177 ? 0.7829 0.7831 0.8193 0.0671  0.0613  0.0726  177 GLU A OE1 
1372 O OE2 . GLU A 177 ? 0.8594 0.8410 0.8850 0.0712  0.0691  0.0684  177 GLU A OE2 
1373 N N   . ASP A 178 ? 0.4406 0.4446 0.4578 0.0463  0.0286  0.0565  178 ASP A N   
1374 C CA  . ASP A 178 ? 0.4071 0.4129 0.4203 0.0405  0.0213  0.0538  178 ASP A CA  
1375 C C   . ASP A 178 ? 0.4006 0.4095 0.4115 0.0331  0.0146  0.0497  178 ASP A C   
1376 O O   . ASP A 178 ? 0.4139 0.4222 0.4202 0.0276  0.0095  0.0468  178 ASP A O   
1377 C CB  . ASP A 178 ? 0.4387 0.4304 0.4425 0.0407  0.0233  0.0465  178 ASP A CB  
1378 C CG  . ASP A 178 ? 0.5424 0.5316 0.5474 0.0465  0.0285  0.0506  178 ASP A CG  
1379 O OD1 . ASP A 178 ? 0.5454 0.5457 0.5586 0.0489  0.0282  0.0597  178 ASP A OD1 
1380 O OD2 . ASP A 178 ? 0.5261 0.5025 0.5239 0.0482  0.0327  0.0452  178 ASP A OD2 
1381 N N   . PHE A 179 ? 0.3658 0.3767 0.3792 0.0328  0.0152  0.0493  179 PHE A N   
1382 C CA  . PHE A 179 ? 0.3679 0.3799 0.3786 0.0261  0.0099  0.0449  179 PHE A CA  
1383 C C   . PHE A 179 ? 0.4253 0.4476 0.4376 0.0200  0.0032  0.0485  179 PHE A C   
1384 O O   . PHE A 179 ? 0.3621 0.3802 0.3680 0.0139  -0.0006 0.0433  179 PHE A O   
1385 C CB  . PHE A 179 ? 0.3351 0.3493 0.3494 0.0272  0.0119  0.0455  179 PHE A CB  
1386 C CG  . PHE A 179 ? 0.3633 0.3781 0.3753 0.0208  0.0072  0.0412  179 PHE A CG  
1387 C CD1 . PHE A 179 ? 0.4371 0.4630 0.4528 0.0161  0.0022  0.0451  179 PHE A CD1 
1388 C CD2 . PHE A 179 ? 0.4279 0.4322 0.4339 0.0192  0.0077  0.0337  179 PHE A CD2 
1389 C CE1 . PHE A 179 ? 0.4794 0.5045 0.4923 0.0102  -0.0012 0.0410  179 PHE A CE1 
1390 C CE2 . PHE A 179 ? 0.3916 0.3961 0.3962 0.0138  0.0042  0.0305  179 PHE A CE2 
1391 C CZ  . PHE A 179 ? 0.4167 0.4309 0.4245 0.0095  0.0001  0.0338  179 PHE A CZ  
1392 N N   . LYS A 180 ? 0.3473 0.3829 0.3677 0.0212  0.0021  0.0578  180 LYS A N   
1393 C CA  . LYS A 180 ? 0.3837 0.4299 0.4046 0.0140  -0.0048 0.0622  180 LYS A CA  
1394 C C   . LYS A 180 ? 0.4085 0.4495 0.4218 0.0105  -0.0072 0.0596  180 LYS A C   
1395 O O   . LYS A 180 ? 0.4003 0.4401 0.4068 0.0023  -0.0119 0.0564  180 LYS A O   
1396 C CB  . LYS A 180 ? 0.4692 0.5319 0.5016 0.0164  -0.0055 0.0743  180 LYS A CB  
1397 C CG  . LYS A 180 ? 0.5228 0.5980 0.5554 0.0074  -0.0133 0.0796  180 LYS A CG  
1398 C CD  . LYS A 180 ? 0.5808 0.6743 0.6268 0.0092  -0.0145 0.0923  180 LYS A CD  
1399 C CE  . LYS A 180 ? 0.6740 0.7785 0.7191 -0.0011 -0.0221 0.0953  180 LYS A CE  
1400 N NZ  . LYS A 180 ? 0.6234 0.7266 0.6579 -0.0109 -0.0283 0.0935  180 LYS A NZ  
1401 N N   . ARG A 181 ? 0.4076 0.4446 0.4216 0.0164  -0.0035 0.0610  181 ARG A N   
1402 C CA  . ARG A 181 ? 0.3600 0.3919 0.3670 0.0135  -0.0054 0.0589  181 ARG A CA  
1403 C C   . ARG A 181 ? 0.3464 0.3647 0.3430 0.0089  -0.0060 0.0481  181 ARG A C   
1404 O O   . ARG A 181 ? 0.3590 0.3752 0.3486 0.0019  -0.0096 0.0460  181 ARG A O   
1405 C CB  . ARG A 181 ? 0.4236 0.4520 0.4332 0.0216  -0.0001 0.0615  181 ARG A CB  
1406 C CG  . ARG A 181 ? 0.5383 0.5586 0.5401 0.0200  -0.0007 0.0579  181 ARG A CG  
1407 C CD  . ARG A 181 ? 0.5693 0.5886 0.5751 0.0280  0.0045  0.0626  181 ARG A CD  
1408 N NE  . ARG A 181 ? 0.5229 0.5291 0.5261 0.0340  0.0115  0.0565  181 ARG A NE  
1409 C CZ  . ARG A 181 ? 0.4998 0.4927 0.4944 0.0334  0.0130  0.0481  181 ARG A CZ  
1410 N NH1 . ARG A 181 ? 0.4927 0.4824 0.4806 0.0277  0.0088  0.0445  181 ARG A NH1 
1411 N NH2 . ARG A 181 ? 0.5029 0.4852 0.4950 0.0380  0.0191  0.0436  181 ARG A NH2 
1412 N N   . HIS A 182 ? 0.3148 0.3238 0.3102 0.0122  -0.0021 0.0418  182 HIS A N   
1413 C CA  . HIS A 182 ? 0.2741 0.2713 0.2619 0.0084  -0.0022 0.0329  182 HIS A CA  
1414 C C   . HIS A 182 ? 0.3228 0.3222 0.3082 0.0007  -0.0061 0.0311  182 HIS A C   
1415 O O   . HIS A 182 ? 0.3113 0.3036 0.2897 -0.0049 -0.0072 0.0265  182 HIS A O   
1416 C CB  . HIS A 182 ? 0.3251 0.3137 0.3130 0.0131  0.0022  0.0281  182 HIS A CB  
1417 C CG  . HIS A 182 ? 0.4165 0.3982 0.4029 0.0188  0.0066  0.0273  182 HIS A CG  
1418 N ND1 . HIS A 182 ? 0.3779 0.3536 0.3594 0.0181  0.0066  0.0251  182 HIS A ND1 
1419 C CD2 . HIS A 182 ? 0.3643 0.3429 0.3524 0.0248  0.0116  0.0281  182 HIS A CD2 
1420 C CE1 . HIS A 182 ? 0.3870 0.3568 0.3677 0.0236  0.0111  0.0247  182 HIS A CE1 
1421 N NE2 . HIS A 182 ? 0.3723 0.3433 0.3564 0.0275  0.0145  0.0264  182 HIS A NE2 
1422 N N   . THR A 183 ? 0.3550 0.3632 0.3458 0.0002  -0.0073 0.0347  183 THR A N   
1423 C CA  . THR A 183 ? 0.3699 0.3797 0.3579 -0.0073 -0.0106 0.0330  183 THR A CA  
1424 C C   . THR A 183 ? 0.3777 0.3914 0.3604 -0.0153 -0.0149 0.0356  183 THR A C   
1425 O O   . THR A 183 ? 0.3712 0.3783 0.3462 -0.0226 -0.0159 0.0309  183 THR A O   
1426 C CB  . THR A 183 ? 0.3594 0.3789 0.3546 -0.0061 -0.0112 0.0371  183 THR A CB  
1427 O OG1 . THR A 183 ? 0.4190 0.4333 0.4172 0.0002  -0.0069 0.0343  183 THR A OG1 
1428 C CG2 . THR A 183 ? 0.4717 0.4920 0.4635 -0.0141 -0.0141 0.0351  183 THR A CG2 
1429 N N   . GLU A 184 ? 0.3726 0.3966 0.3589 -0.0143 -0.0171 0.0432  184 GLU A N   
1430 C CA  . GLU A 184 ? 0.3773 0.4052 0.3574 -0.0228 -0.0217 0.0463  184 GLU A CA  
1431 C C   . GLU A 184 ? 0.3811 0.3949 0.3505 -0.0260 -0.0203 0.0393  184 GLU A C   
1432 O O   . GLU A 184 ? 0.3614 0.3709 0.3213 -0.0354 -0.0224 0.0368  184 GLU A O   
1433 C CB  . GLU A 184 ? 0.4201 0.4618 0.4073 -0.0202 -0.0241 0.0568  184 GLU A CB  
1434 C CG  . GLU A 184 ? 0.4811 0.5256 0.4606 -0.0289 -0.0289 0.0599  184 GLU A CG  
1435 C CD  . GLU A 184 ? 0.6214 0.6829 0.6095 -0.0278 -0.0325 0.0725  184 GLU A CD  
1436 O OE1 . GLU A 184 ? 0.6850 0.7564 0.6858 -0.0201 -0.0307 0.0790  184 GLU A OE1 
1437 O OE2 . GLU A 184 ? 0.6953 0.7600 0.6774 -0.0348 -0.0369 0.0762  184 GLU A OE2 
1438 N N   . ALA A 185 ? 0.3674 0.3733 0.3379 -0.0187 -0.0162 0.0361  185 ALA A N   
1439 C CA  . ALA A 185 ? 0.3609 0.3538 0.3224 -0.0210 -0.0144 0.0299  185 ALA A CA  
1440 C C   . ALA A 185 ? 0.4168 0.3982 0.3720 -0.0261 -0.0125 0.0221  185 ALA A C   
1441 O O   . ALA A 185 ? 0.4069 0.3801 0.3526 -0.0331 -0.0124 0.0186  185 ALA A O   
1442 C CB  . ALA A 185 ? 0.3511 0.3379 0.3155 -0.0121 -0.0102 0.0279  185 ALA A CB  
1443 N N   . ILE A 186 ? 0.3837 0.3640 0.3439 -0.0229 -0.0106 0.0196  186 ILE A N   
1444 C CA  . ILE A 186 ? 0.3309 0.3008 0.2868 -0.0270 -0.0081 0.0132  186 ILE A CA  
1445 C C   . ILE A 186 ? 0.3529 0.3243 0.3024 -0.0369 -0.0105 0.0138  186 ILE A C   
1446 O O   . ILE A 186 ? 0.3543 0.3147 0.2954 -0.0431 -0.0082 0.0090  186 ILE A O   
1447 C CB  . ILE A 186 ? 0.3133 0.2825 0.2766 -0.0212 -0.0058 0.0113  186 ILE A CB  
1448 C CG1 . ILE A 186 ? 0.3890 0.3544 0.3558 -0.0132 -0.0032 0.0101  186 ILE A CG1 
1449 C CG2 . ILE A 186 ? 0.3423 0.3019 0.3029 -0.0251 -0.0032 0.0061  186 ILE A CG2 
1450 C CD1 . ILE A 186 ? 0.4010 0.3544 0.3630 -0.0138 -0.0003 0.0052  186 ILE A CD1 
1451 N N   . ILE A 187 ? 0.3617 0.3463 0.3149 -0.0387 -0.0147 0.0197  187 ILE A N   
1452 C CA  . ILE A 187 ? 0.3572 0.3441 0.3032 -0.0494 -0.0175 0.0208  187 ILE A CA  
1453 C C   . ILE A 187 ? 0.3882 0.3695 0.3224 -0.0577 -0.0187 0.0202  187 ILE A C   
1454 O O   . ILE A 187 ? 0.4107 0.3820 0.3339 -0.0668 -0.0171 0.0159  187 ILE A O   
1455 C CB  . ILE A 187 ? 0.3344 0.3386 0.2876 -0.0499 -0.0225 0.0289  187 ILE A CB  
1456 C CG1 . ILE A 187 ? 0.4004 0.4080 0.3632 -0.0433 -0.0207 0.0285  187 ILE A CG1 
1457 C CG2 . ILE A 187 ? 0.3245 0.3319 0.2688 -0.0625 -0.0263 0.0308  187 ILE A CG2 
1458 C CD1 . ILE A 187 ? 0.3826 0.4072 0.3547 -0.0414 -0.0243 0.0370  187 ILE A CD1 
1459 N N   . ARG A 188 ? 0.3837 0.3706 0.3194 -0.0549 -0.0209 0.0246  188 ARG A N   
1460 C CA  . ARG A 188 ? 0.4122 0.3947 0.3364 -0.0630 -0.0225 0.0247  188 ARG A CA  
1461 C C   . ARG A 188 ? 0.4141 0.3772 0.3288 -0.0650 -0.0166 0.0158  188 ARG A C   
1462 O O   . ARG A 188 ? 0.4773 0.4314 0.3786 -0.0755 -0.0160 0.0130  188 ARG A O   
1463 C CB  . ARG A 188 ? 0.4618 0.4536 0.3913 -0.0577 -0.0252 0.0313  188 ARG A CB  
1464 C CG  . ARG A 188 ? 0.5459 0.5573 0.4827 -0.0589 -0.0314 0.0420  188 ARG A CG  
1465 C CD  . ARG A 188 ? 0.5937 0.6131 0.5337 -0.0558 -0.0338 0.0492  188 ARG A CD  
1466 N NE  . ARG A 188 ? 0.6836 0.7231 0.6333 -0.0560 -0.0392 0.0609  188 ARG A NE  
1467 C CZ  . ARG A 188 ? 0.6229 0.6723 0.5675 -0.0671 -0.0457 0.0677  188 ARG A CZ  
1468 N NH1 . ARG A 188 ? 0.6709 0.7108 0.5991 -0.0793 -0.0473 0.0634  188 ARG A NH1 
1469 N NH2 . ARG A 188 ? 0.6363 0.7054 0.5923 -0.0663 -0.0503 0.0794  188 ARG A NH2 
1470 N N   . LEU A 189 ? 0.3970 0.3531 0.3180 -0.0556 -0.0120 0.0116  189 LEU A N   
1471 C CA  . LEU A 189 ? 0.4526 0.3913 0.3669 -0.0566 -0.0060 0.0042  189 LEU A CA  
1472 C C   . LEU A 189 ? 0.4656 0.3944 0.3743 -0.0631 -0.0022 -0.0005 189 LEU A C   
1473 O O   . LEU A 189 ? 0.4545 0.3689 0.3525 -0.0694 0.0023  -0.0053 189 LEU A O   
1474 C CB  . LEU A 189 ? 0.4424 0.3776 0.3659 -0.0456 -0.0025 0.0018  189 LEU A CB  
1475 C CG  . LEU A 189 ? 0.5245 0.4654 0.4522 -0.0389 -0.0042 0.0051  189 LEU A CG  
1476 C CD1 . LEU A 189 ? 0.5580 0.4963 0.4945 -0.0291 -0.0009 0.0029  189 LEU A CD1 
1477 C CD2 . LEU A 189 ? 0.5194 0.4522 0.4370 -0.0435 -0.0034 0.0036  189 LEU A CD2 
1478 N N   . GLU A 190 ? 0.3920 0.3272 0.3075 -0.0615 -0.0031 0.0007  190 GLU A N   
1479 C CA  . GLU A 190 ? 0.4063 0.3315 0.3177 -0.0664 0.0014  -0.0037 190 GLU A CA  
1480 C C   . GLU A 190 ? 0.4330 0.3560 0.3310 -0.0795 0.0000  -0.0035 190 GLU A C   
1481 O O   . GLU A 190 ? 0.4662 0.3744 0.3548 -0.0861 0.0058  -0.0085 190 GLU A O   
1482 C CB  . GLU A 190 ? 0.3877 0.3198 0.3106 -0.0603 0.0011  -0.0027 190 GLU A CB  
1483 C CG  . GLU A 190 ? 0.4402 0.3700 0.3735 -0.0497 0.0041  -0.0043 190 GLU A CG  
1484 C CD  . GLU A 190 ? 0.5772 0.4947 0.5118 -0.0495 0.0106  -0.0088 190 GLU A CD  
1485 O OE1 . GLU A 190 ? 0.5526 0.4574 0.4780 -0.0561 0.0154  -0.0122 190 GLU A OE1 
1486 O OE2 . GLU A 190 ? 0.5345 0.4545 0.4791 -0.0427 0.0114  -0.0084 190 GLU A OE2 
1487 N N   . LEU A 191 ? 0.4386 0.3758 0.3355 -0.0838 -0.0073 0.0027  191 LEU A N   
1488 C CA  . LEU A 191 ? 0.4074 0.3455 0.2928 -0.0968 -0.0098 0.0040  191 LEU A CA  
1489 C C   . LEU A 191 ? 0.4989 0.4419 0.3738 -0.1062 -0.0153 0.0083  191 LEU A C   
1490 O O   . LEU A 191 ? 0.4890 0.4292 0.3506 -0.1194 -0.0167 0.0084  191 LEU A O   
1491 C CB  . LEU A 191 ? 0.4056 0.3584 0.2999 -0.0958 -0.0142 0.0086  191 LEU A CB  
1492 C CG  . LEU A 191 ? 0.4187 0.3662 0.3206 -0.0898 -0.0092 0.0046  191 LEU A CG  
1493 C CD1 . LEU A 191 ? 0.3298 0.2943 0.2454 -0.0833 -0.0137 0.0101  191 LEU A CD1 
1494 C CD2 . LEU A 191 ? 0.3912 0.3254 0.2811 -0.1002 -0.0045 -0.0002 191 LEU A CD2 
1495 N N   . LEU A 192 ? 0.5258 0.4760 0.4056 -0.1006 -0.0184 0.0122  192 LEU A N   
1496 C CA  . LEU A 192 ? 0.5969 0.5529 0.4675 -0.1094 -0.0241 0.0174  192 LEU A CA  
1497 C C   . LEU A 192 ? 0.7350 0.6780 0.5975 -0.1093 -0.0205 0.0134  192 LEU A C   
1498 O O   . LEU A 192 ? 0.8913 0.8380 0.7461 -0.1158 -0.0248 0.0175  192 LEU A O   
1499 C CB  . LEU A 192 ? 0.5471 0.5258 0.4311 -0.1038 -0.0317 0.0279  192 LEU A CB  
1500 C CG  . LEU A 192 ? 0.5370 0.5313 0.4304 -0.1037 -0.0359 0.0337  192 LEU A CG  
1501 C CD1 . LEU A 192 ? 0.5564 0.5717 0.4641 -0.0970 -0.0418 0.0446  192 LEU A CD1 
1502 C CD2 . LEU A 192 ? 0.5656 0.5592 0.4450 -0.1198 -0.0390 0.0344  192 LEU A CD2 
1503 O OXT . LEU A 192 ? 0.7088 0.6379 0.5726 -0.1029 -0.0134 0.0065  192 LEU A OXT 
1504 N N1  . SPD B .   ? 0.5437 0.5983 0.5621 -0.0248 -0.0165 0.0404  201 SPD A N1  
1505 C C2  . SPD B .   ? 0.5962 0.6396 0.6130 -0.0190 -0.0129 0.0354  201 SPD A C2  
1506 C C3  . SPD B .   ? 0.5067 0.5456 0.5240 -0.0184 -0.0110 0.0322  201 SPD A C3  
1507 C C4  . SPD B .   ? 0.5375 0.5722 0.5569 -0.0111 -0.0075 0.0315  201 SPD A C4  
1508 C C5  . SPD B .   ? 0.5589 0.5877 0.5757 -0.0078 -0.0062 0.0300  201 SPD A C5  
1509 N N6  . SPD B .   ? 0.6732 0.6936 0.6883 -0.0038 -0.0031 0.0270  201 SPD A N6  
1510 C C7  . SPD B .   ? 0.6935 0.7112 0.7077 0.0009  -0.0008 0.0277  201 SPD A C7  
1511 C C8  . SPD B .   ? 0.7628 0.7702 0.7729 0.0029  0.0016  0.0237  201 SPD A C8  
1512 C C9  . SPD B .   ? 0.7085 0.7091 0.7154 -0.0003 -0.0002 0.0195  201 SPD A C9  
1513 N N10 . SPD B .   ? 0.6186 0.6120 0.6231 0.0001  0.0009  0.0170  201 SPD A N10 
1514 O O   . HOH C .   ? 0.4778 0.4482 0.4676 0.0354  0.0246  0.0295  301 HOH A O   
1515 O O   . HOH C .   ? 0.6548 0.5187 0.5580 -0.0996 0.0462  -0.0211 302 HOH A O   
1516 O O   . HOH C .   ? 0.6036 0.6095 0.6505 -0.0342 -0.0098 0.0498  303 HOH A O   
1517 O O   . HOH C .   ? 0.4967 0.5042 0.5288 -0.0301 -0.0031 0.0295  304 HOH A O   
1518 O O   . HOH C .   ? 0.5794 0.5137 0.4993 -0.1048 0.0135  -0.0053 305 HOH A O   
1519 O O   . HOH C .   ? 0.7802 0.7168 0.5494 -0.2446 -0.0191 0.0069  306 HOH A O   
1520 O O   . HOH C .   ? 0.5067 0.4895 0.5134 -0.0071 -0.0017 0.0130  307 HOH A O   
1521 O O   . HOH C .   ? 0.6391 0.6474 0.6480 -0.0154 0.0709  0.0492  308 HOH A O   
1522 O O   . HOH C .   ? 0.6886 0.9275 0.7687 -0.0724 -0.0740 0.1618  309 HOH A O   
1523 O O   . HOH C .   ? 0.5713 0.6626 0.6740 0.0218  0.0700  0.0908  310 HOH A O   
1524 O O   . HOH C .   ? 0.6905 0.9091 0.7051 -0.1194 -0.0958 0.1551  311 HOH A O   
1525 O O   . HOH C .   ? 0.6540 0.7284 0.6742 -0.0005 -0.0206 0.0836  312 HOH A O   
1526 O O   . HOH C .   ? 0.5188 0.4746 0.4856 0.0023  0.0605  0.0292  313 HOH A O   
1527 O O   . HOH C .   ? 0.6375 0.5763 0.6074 0.0154  0.1007  0.0398  314 HOH A O   
1528 O O   . HOH C .   ? 0.6632 0.5280 0.3637 -0.2532 0.0012  -0.0095 315 HOH A O   
1529 O O   . HOH C .   ? 0.5029 0.5252 0.5334 -0.0357 -0.0013 0.0292  316 HOH A O   
1530 O O   . HOH C .   ? 0.5294 0.5808 0.5599 -0.0470 -0.0056 0.0309  317 HOH A O   
1531 O O   . HOH C .   ? 0.5159 0.5015 0.5729 -0.0223 0.0008  0.0389  318 HOH A O   
1532 O O   . HOH C .   ? 0.7969 0.6710 0.5546 -0.2063 -0.0017 -0.0098 319 HOH A O   
1533 O O   . HOH C .   ? 0.5789 0.7015 0.5371 -0.1097 -0.0733 0.1011  320 HOH A O   
1534 O O   . HOH C .   ? 0.4866 0.6101 0.5802 -0.0046 0.0142  0.0802  321 HOH A O   
1535 O O   . HOH C .   ? 0.3778 0.5458 0.4806 -0.0548 0.0006  0.0843  322 HOH A O   
1536 O O   . HOH C .   ? 0.6112 0.6096 0.4475 -0.1655 -0.0532 0.0441  323 HOH A O   
1537 O O   . HOH C .   ? 0.5622 0.5350 0.5470 0.0021  0.0132  0.0164  324 HOH A O   
1538 O O   . HOH C .   ? 0.4941 0.5128 0.5050 -0.0008 -0.0038 0.0290  325 HOH A O   
1539 O O   . HOH C .   ? 0.8087 0.9282 0.8843 0.0182  -0.0083 0.1089  326 HOH A O   
1540 O O   . HOH C .   ? 0.4651 0.4891 0.4497 -0.0043 -0.0154 0.0545  327 HOH A O   
1541 O O   . HOH C .   ? 0.5625 0.5157 0.4245 -0.1596 -0.0101 0.0047  328 HOH A O   
1542 O O   . HOH C .   ? 0.5928 0.5298 0.5734 -0.0537 0.0209  -0.0011 329 HOH A O   
1543 O O   . HOH C .   ? 0.5204 0.5641 0.5486 -0.0515 0.0129  0.0412  330 HOH A O   
1544 O O   . HOH C .   ? 0.5399 0.5153 0.4905 -0.0517 0.0216  0.0347  331 HOH A O   
1545 O O   . HOH C .   ? 0.6009 0.6570 0.4627 -0.1868 -0.0689 0.0625  332 HOH A O   
1546 O O   . HOH C .   ? 0.3884 0.3234 0.3448 0.0006  0.0167  0.0056  333 HOH A O   
1547 O O   . HOH C .   ? 0.5523 0.3937 0.4311 0.0106  0.0740  -0.0071 334 HOH A O   
1548 O O   . HOH C .   ? 0.3744 0.3016 0.3381 0.0392  0.0576  0.0217  335 HOH A O   
1549 O O   . HOH C .   ? 0.3969 0.3098 0.3433 0.0266  0.0456  0.0081  336 HOH A O   
1550 O O   . HOH C .   ? 0.6206 0.8101 0.6184 -0.1345 -0.0842 0.1195  337 HOH A O   
1551 O O   . HOH C .   ? 0.3822 0.3618 0.4174 -0.0277 0.0071  0.0217  338 HOH A O   
1552 O O   . HOH C .   ? 0.4628 0.4666 0.4360 -0.0744 -0.0086 0.0144  339 HOH A O   
1553 O O   . HOH C .   ? 0.5691 0.5832 0.5810 -0.0451 -0.0026 0.0421  340 HOH A O   
1554 O O   . HOH C .   ? 0.3708 0.3542 0.4031 -0.0185 -0.0067 0.0280  341 HOH A O   
1555 O O   . HOH C .   ? 0.4866 0.3702 0.3843 -0.0746 0.0207  -0.0173 342 HOH A O   
1556 O O   . HOH C .   ? 0.5151 0.4774 0.4805 -0.0105 0.0203  0.0184  343 HOH A O   
1557 O O   . HOH C .   ? 0.4843 0.5098 0.4949 -0.0344 -0.0100 0.0226  344 HOH A O   
1558 O O   . HOH C .   ? 0.6673 0.7603 0.7042 -0.0714 -0.0127 0.0443  345 HOH A O   
1559 O O   . HOH C .   ? 0.6009 0.6647 0.5049 -0.1324 -0.0642 0.0700  346 HOH A O   
1560 O O   . HOH C .   ? 0.6756 0.7537 0.5489 -0.1992 -0.0719 0.0664  347 HOH A O   
1561 O O   . HOH C .   ? 0.5784 0.4578 0.4389 -0.1090 0.0165  -0.0168 348 HOH A O   
1562 O O   . HOH C .   ? 0.5697 0.5274 0.5508 0.0379  0.0269  0.0266  349 HOH A O   
1563 O O   . HOH C .   ? 0.5947 0.7474 0.4883 -0.2073 -0.1072 0.1188  350 HOH A O   
1564 O O   . HOH C .   ? 0.3289 0.3154 0.3541 -0.0176 -0.0049 0.0225  351 HOH A O   
1565 O O   . HOH C .   ? 0.4645 0.5526 0.5260 -0.0323 0.0222  0.0560  352 HOH A O   
1566 O O   . HOH C .   ? 0.5900 0.4909 0.4721 -0.0742 0.0041  -0.0075 353 HOH A O   
1567 O O   . HOH C .   ? 0.5369 0.4318 0.4838 0.0509  0.0785  0.0210  354 HOH A O   
1568 O O   . HOH C .   ? 0.5699 0.5736 0.5812 -0.0403 -0.0130 0.0428  355 HOH A O   
1569 O O   . HOH C .   ? 0.4606 0.5647 0.5079 -0.0464 -0.0182 0.0548  356 HOH A O   
1570 O O   . HOH C .   ? 0.6117 0.7114 0.5619 -0.1283 -0.0600 0.0693  357 HOH A O   
1571 O O   . HOH C .   ? 0.4436 0.4750 0.3923 -0.1006 -0.0286 0.0298  358 HOH A O   
1572 O O   . HOH C .   ? 0.6349 0.6662 0.6878 0.0408  0.0597  0.0677  359 HOH A O   
1573 O O   . HOH C .   ? 0.5289 0.5477 0.5351 -0.0487 0.0078  0.0414  360 HOH A O   
1574 O O   . HOH C .   ? 0.6703 0.6826 0.7100 0.0588  0.0520  0.0699  361 HOH A O   
1575 O O   . HOH C .   ? 0.7295 0.5744 0.6215 -0.1020 0.0536  -0.0254 362 HOH A O   
1576 O O   . HOH C .   ? 0.6643 0.7070 0.7291 0.0271  0.0789  0.0738  363 HOH A O   
1577 O O   . HOH C .   ? 0.3959 0.3451 0.3766 0.0040  0.0069  0.0049  364 HOH A O   
1578 O O   . HOH C .   ? 0.5931 0.5492 0.5557 -0.0023 0.0478  0.0247  365 HOH A O   
1579 O O   . HOH C .   ? 0.4448 0.4229 0.4449 -0.0501 0.0074  0.0092  366 HOH A O   
1580 O O   . HOH C .   ? 0.5238 0.4258 0.4690 0.0393  0.0458  0.0068  367 HOH A O   
1581 O O   . HOH C .   ? 0.5653 0.4470 0.4737 0.0086  0.0627  0.0037  368 HOH A O   
1582 O O   . HOH C .   ? 0.5068 0.5530 0.5392 0.0330  0.0078  0.0754  369 HOH A O   
1583 O O   . HOH C .   ? 0.7076 0.6423 0.5894 -0.0812 -0.0129 0.0088  370 HOH A O   
1584 O O   . HOH C .   ? 0.5391 0.4963 0.4922 -0.0202 0.0248  0.0205  371 HOH A O   
1585 O O   . HOH C .   ? 0.6314 0.7991 0.5680 -0.1835 -0.0963 0.1132  372 HOH A O   
1586 O O   . HOH C .   ? 0.5390 0.5241 0.5006 -0.0507 0.0243  0.0367  373 HOH A O   
1587 O O   . HOH C .   ? 0.5547 0.6804 0.6207 -0.0414 -0.0153 0.0664  374 HOH A O   
1588 O O   . HOH C .   ? 0.4786 0.4895 0.4838 -0.0417 -0.0011 0.0386  375 HOH A O   
1589 O O   . HOH C .   ? 0.4084 0.4136 0.4386 -0.0279 -0.0028 0.0261  376 HOH A O   
1590 O O   . HOH C .   ? 0.5944 0.7902 0.7409 0.0190  -0.0023 0.1490  377 HOH A O   
1591 O O   . HOH C .   ? 0.7155 0.5810 0.5135 -0.1825 0.0198  -0.0197 378 HOH A O   
1592 O O   . HOH C .   ? 0.2965 0.3941 0.3722 -0.0235 0.0363  0.0667  379 HOH A O   
1593 O O   . HOH C .   ? 0.5761 0.5531 0.5469 -0.0315 0.0025  0.0261  380 HOH A O   
1594 O O   . HOH C .   ? 0.4129 0.4574 0.4415 -0.0401 -0.0060 0.0290  381 HOH A O   
1595 O O   . HOH C .   ? 0.4969 0.4477 0.4610 -0.0023 0.0803  0.0349  382 HOH A O   
1596 O O   . HOH C .   ? 0.5560 0.5229 0.5424 0.0241  0.0290  0.0220  383 HOH A O   
1597 O O   . HOH C .   ? 0.4600 0.4427 0.4327 -0.0349 0.0043  0.0290  384 HOH A O   
1598 O O   . HOH C .   ? 0.4843 0.5310 0.5249 0.0371  0.0151  0.0731  385 HOH A O   
1599 O O   . HOH C .   ? 0.5684 0.6505 0.4614 -0.1745 -0.0704 0.0693  386 HOH A O   
1600 O O   . HOH C .   ? 0.4149 0.4098 0.4030 -0.0410 -0.0060 0.0361  387 HOH A O   
1601 O O   . HOH C .   ? 0.6304 0.4753 0.5623 -0.0561 0.0533  -0.0236 388 HOH A O   
1602 O O   . HOH C .   ? 0.5093 0.5759 0.5449 -0.0564 -0.0047 0.0358  389 HOH A O   
1603 O O   . HOH C .   ? 0.5261 0.4673 0.5044 0.0528  0.0484  0.0325  390 HOH A O   
1604 O O   . HOH C .   ? 0.5035 0.4766 0.4404 -0.0349 -0.0149 0.0235  391 HOH A O   
1605 O O   . HOH C .   ? 0.5128 0.6057 0.3859 -0.1913 -0.0850 0.0853  392 HOH A O   
1606 O O   . HOH C .   ? 0.5041 0.5093 0.5283 -0.0383 -0.0148 0.0462  393 HOH A O   
1607 O O   . HOH C .   ? 0.4292 0.3561 0.3919 0.0384  0.0509  0.0186  394 HOH A O   
1608 O O   . HOH C .   ? 0.4924 0.5337 0.5264 -0.0523 0.0038  0.0333  395 HOH A O   
1609 O O   . HOH C .   ? 0.6225 0.5820 0.5640 -0.0443 0.0538  0.0333  396 HOH A O   
1610 O O   . HOH C .   ? 0.4241 0.4453 0.4555 -0.0378 -0.0007 0.0322  397 HOH A O   
1611 O O   . HOH C .   ? 0.4189 0.3951 0.4649 -0.0224 0.0068  0.0275  398 HOH A O   
1612 O O   . HOH C .   ? 0.4534 0.4695 0.4826 -0.0314 -0.0025 0.0279  399 HOH A O   
1613 O O   . HOH C .   ? 0.7113 0.5730 0.6387 0.0571  0.1005  0.0189  400 HOH A O   
1614 O O   . HOH C .   ? 0.5279 0.5824 0.5643 -0.0541 0.0102  0.0402  401 HOH A O   
1615 O O   . HOH C .   ? 0.6155 0.5778 0.5792 -0.0103 0.0276  0.0206  402 HOH A O   
1616 O O   . HOH C .   ? 0.4613 0.5659 0.5343 -0.0301 0.0176  0.0619  403 HOH A O   
1617 O O   . HOH C .   ? 0.5774 0.5912 0.6026 -0.0457 -0.0069 0.0483  404 HOH A O   
1618 O O   . HOH C .   ? 0.5128 0.4854 0.4794 -0.0241 0.0145  0.0236  405 HOH A O   
1619 O O   . HOH C .   ? 0.4049 0.3979 0.3873 -0.0313 0.0563  0.0404  406 HOH A O   
1620 O O   . HOH C .   ? 0.4462 0.5495 0.5085 -0.0615 0.0148  0.0548  407 HOH A O   
1621 O O   . HOH C .   ? 0.8344 0.7335 0.5446 -0.2696 -0.0048 -0.0027 408 HOH A O   
1622 O O   . HOH C .   ? 0.5819 0.5017 0.4972 -0.0273 0.0640  0.0214  409 HOH A O   
1623 O O   . HOH C .   ? 0.7437 0.6547 0.6487 -0.0284 0.0493  0.0145  410 HOH A O   
1624 O O   . HOH C .   ? 0.6134 0.7236 0.6277 -0.0330 -0.0433 0.1010  411 HOH A O   
1625 O O   . HOH C .   ? 0.5282 0.3768 0.4139 0.0101  0.0637  -0.0090 412 HOH A O   
1626 O O   . HOH C .   ? 0.3253 0.3246 0.3049 -0.0450 0.0352  0.0391  413 HOH A O   
1627 O O   . HOH C .   ? 0.4753 0.5459 0.5100 -0.0649 -0.0042 0.0365  414 HOH A O   
1628 O O   . HOH C .   ? 0.7159 0.8254 0.7085 -0.0542 -0.0537 0.1021  415 HOH A O   
1629 O O   . HOH C .   ? 0.5295 0.5658 0.5411 -0.0433 -0.0121 0.0258  416 HOH A O   
1630 O O   . HOH C .   ? 0.6212 0.6599 0.6810 0.0453  0.0564  0.0729  417 HOH A O   
1631 O O   . HOH C .   ? 0.5114 0.5924 0.5597 -0.0566 0.0062  0.0444  418 HOH A O   
1632 O O   . HOH C .   ? 0.3258 0.4467 0.4151 -0.0238 0.0225  0.0728  419 HOH A O   
1633 O O   . HOH C .   ? 0.5873 0.5079 0.4024 -0.1926 -0.0034 -0.0031 420 HOH A O   
1634 O O   . HOH C .   ? 0.6221 0.6582 0.4892 -0.1532 -0.0629 0.0609  421 HOH A O   
1635 O O   . HOH C .   ? 0.6196 0.5291 0.5864 0.0650  0.0822  0.0351  422 HOH A O   
1636 O O   . HOH C .   ? 0.6361 0.5598 0.6097 0.0635  0.0680  0.0366  423 HOH A O   
1637 O O   . HOH C .   ? 0.5516 0.5674 0.5796 -0.0322 -0.0022 0.0247  424 HOH A O   
1638 O O   . HOH C .   ? 0.6360 0.5788 0.6067 0.0362  0.0272  0.0188  425 HOH A O   
1639 O O   . HOH C .   ? 0.5803 0.5140 0.5261 -0.0099 0.0890  0.0324  426 HOH A O   
1640 O O   . HOH C .   ? 0.5747 0.7283 0.6763 -0.0407 0.0082  0.0815  427 HOH A O   
1641 O O   . HOH C .   ? 0.5447 0.5244 0.5848 -0.0303 0.0097  0.0250  428 HOH A O   
1642 O O   . HOH C .   ? 0.6384 0.5645 0.5840 -0.0009 0.0935  0.0316  429 HOH A O   
1643 O O   . HOH C .   ? 0.5839 0.5951 0.5899 -0.0513 -0.0042 0.0471  430 HOH A O   
1644 O O   . HOH C .   ? 0.7744 0.6183 0.4581 -0.2583 0.0159  -0.0182 431 HOH A O   
1645 O O   . HOH C .   ? 0.5310 0.5328 0.4837 -0.0271 -0.0209 0.0419  432 HOH A O   
1646 O O   . HOH C .   ? 0.6775 0.6883 0.7103 -0.0394 0.0021  0.0274  433 HOH A O   
1647 O O   . HOH C .   ? 0.6762 0.5024 0.6228 -0.0476 0.0686  -0.0235 434 HOH A O   
1648 O O   . HOH C .   ? 0.6692 0.6764 0.7318 -0.0338 -0.0121 0.0613  435 HOH A O   
1649 O O   . HOH C .   ? 0.5506 0.7400 0.4593 -0.2213 -0.1173 0.1409  436 HOH A O   
1650 O O   . HOH C .   ? 0.5839 0.5397 0.5885 -0.0483 0.0191  0.0076  437 HOH A O   
1651 O O   . HOH C .   ? 0.6798 0.7003 0.7053 -0.0406 -0.0015 0.0233  438 HOH A O   
1652 O O   . HOH C .   ? 0.7818 0.5744 0.7202 -0.0543 0.0918  -0.0272 439 HOH A O   
1653 O O   . HOH C .   ? 0.7018 0.5291 0.5613 -0.0046 0.0642  -0.0158 440 HOH A O   
1654 O O   . HOH C .   ? 0.6385 0.6397 0.6664 -0.0377 0.0030  0.0218  441 HOH A O   
1655 O O   . HOH C .   ? 0.6044 0.6098 0.6239 -0.0459 0.0025  0.0189  442 HOH A O   
1656 O O   . HOH C .   ? 0.7061 0.6756 0.7385 -0.0388 0.0180  0.0203  443 HOH A O   
# 
