data_9CR5
# 
_entry.id   9CR5 
# 
_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   9CR5         pdb_00009cr5 10.2210/pdb9cr5/pdb 
WWPDB D_1000285084 ?            ?                   
# 
_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       2025-05-28 
_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                        9CR5 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-20 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              wladek@minorlab.org 
_pdbx_contact_author.name_first         Wladek 
_pdbx_contact_author.name_last          Minor 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7075-7090 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Majorek, K.A.'                                 1 0000-0002-0973-9085 
'Cooper, D.R.'                                  2 0000-0001-5240-9789 
'Joachimiak, A.'                                3 0000-0003-2535-6209 
'Minor, W.'                                     4 0000-0001-7075-7090 
'Midwest Center for Structural Genomics (MCSG)' 5 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biochem.Biophys.Res.Commun. 
_citation.journal_id_ASTM           BBRCA9 
_citation.journal_id_CSD            0146 
_citation.journal_id_ISSN           1090-2104 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            748 
_citation.language                  ? 
_citation.page_first                151299 
_citation.page_last                 151299 
_citation.title                     
'Structural, functional, and regulatory evaluation of a cysteine post-translationally modified Gcn5-related N-acetyltransferase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bbrc.2025.151299 
_citation.pdbx_database_id_PubMed   39826527 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Uychoco, P.'         1  ? 
primary 'Majorek, K.A.'       2  ? 
primary 'Ives, A.N.'          3  ? 
primary 'Le, V.T.B.'          4  ? 
primary 'Caro De Silva, P.L.' 5  ? 
primary 'Paurus, V.L.'        6  ? 
primary 'Attah, I.K.'         7  ? 
primary 'Lipton, M.S.'        8  ? 
primary 'Minor, W.'           9  ? 
primary 'Kuhn, M.L.'          10 ? 
# 
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 'Acetyltransferase PA2271' 19566.770 2   2.3.1.- ? ? ? 
2 non-polymer syn 'ACETYL COENZYME *A'       809.571   2   ?       ? ? ? 
3 non-polymer syn 'SODIUM ION'               22.990    5   ?       ? ? ? 
4 non-polymer syn 'CHLORIDE ION'             35.453    2   ?       ? ? ? 
5 water       nat water                      18.015    497 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'GCN5-related N-acetyltransferase,GNAT' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;H(MSE)DYRIRTSRDEDAALLPAIERSAGESFRLLPELAWIADAGVAGVDFHRRLIERGSHWLAEDADGQPVGFLAAERC
ADELHIAELSIAQAHQQQGLGRRLLERAVTYAHASHCRALTLTTFCDVPWNAPFYARLGFQRLTWQEAGERLRAILGHEQ
EIGFAADSRCA(MSE)RLVLGS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HMDYRIRTSRDEDAALLPAIERSAGESFRLLPELAWIADAGVAGVDFHRRLIERGSHWLAEDADGQPVGFLAAERCADEL
HIAELSIAQAHQQQGLGRRLLERAVTYAHASHCRALTLTTFCDVPWNAPFYARLGFQRLTWQEAGERLRAILGHEQEIGF
AADSRCAMRLVLGS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ACETYL COENZYME *A' ACO 
3 'SODIUM ION'         NA  
4 'CHLORIDE ION'       CL  
5 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   MSE n 
1 3   ASP n 
1 4   TYR n 
1 5   ARG n 
1 6   ILE n 
1 7   ARG n 
1 8   THR n 
1 9   SER n 
1 10  ARG n 
1 11  ASP n 
1 12  GLU n 
1 13  ASP n 
1 14  ALA n 
1 15  ALA n 
1 16  LEU n 
1 17  LEU n 
1 18  PRO n 
1 19  ALA n 
1 20  ILE n 
1 21  GLU n 
1 22  ARG n 
1 23  SER n 
1 24  ALA n 
1 25  GLY n 
1 26  GLU n 
1 27  SER n 
1 28  PHE n 
1 29  ARG n 
1 30  LEU n 
1 31  LEU n 
1 32  PRO n 
1 33  GLU n 
1 34  LEU n 
1 35  ALA n 
1 36  TRP n 
1 37  ILE n 
1 38  ALA n 
1 39  ASP n 
1 40  ALA n 
1 41  GLY n 
1 42  VAL n 
1 43  ALA n 
1 44  GLY n 
1 45  VAL n 
1 46  ASP n 
1 47  PHE n 
1 48  HIS n 
1 49  ARG n 
1 50  ARG n 
1 51  LEU n 
1 52  ILE n 
1 53  GLU n 
1 54  ARG n 
1 55  GLY n 
1 56  SER n 
1 57  HIS n 
1 58  TRP n 
1 59  LEU n 
1 60  ALA n 
1 61  GLU n 
1 62  ASP n 
1 63  ALA n 
1 64  ASP n 
1 65  GLY n 
1 66  GLN n 
1 67  PRO n 
1 68  VAL n 
1 69  GLY n 
1 70  PHE n 
1 71  LEU n 
1 72  ALA n 
1 73  ALA n 
1 74  GLU n 
1 75  ARG n 
1 76  CYS n 
1 77  ALA n 
1 78  ASP n 
1 79  GLU n 
1 80  LEU n 
1 81  HIS n 
1 82  ILE n 
1 83  ALA n 
1 84  GLU n 
1 85  LEU n 
1 86  SER n 
1 87  ILE n 
1 88  ALA n 
1 89  GLN n 
1 90  ALA n 
1 91  HIS n 
1 92  GLN n 
1 93  GLN n 
1 94  GLN n 
1 95  GLY n 
1 96  LEU n 
1 97  GLY n 
1 98  ARG n 
1 99  ARG n 
1 100 LEU n 
1 101 LEU n 
1 102 GLU n 
1 103 ARG n 
1 104 ALA n 
1 105 VAL n 
1 106 THR n 
1 107 TYR n 
1 108 ALA n 
1 109 HIS n 
1 110 ALA n 
1 111 SER n 
1 112 HIS n 
1 113 CYS n 
1 114 ARG n 
1 115 ALA n 
1 116 LEU n 
1 117 THR n 
1 118 LEU n 
1 119 THR n 
1 120 THR n 
1 121 PHE n 
1 122 CYS n 
1 123 ASP n 
1 124 VAL n 
1 125 PRO n 
1 126 TRP n 
1 127 ASN n 
1 128 ALA n 
1 129 PRO n 
1 130 PHE n 
1 131 TYR n 
1 132 ALA n 
1 133 ARG n 
1 134 LEU n 
1 135 GLY n 
1 136 PHE n 
1 137 GLN n 
1 138 ARG n 
1 139 LEU n 
1 140 THR n 
1 141 TRP n 
1 142 GLN n 
1 143 GLU n 
1 144 ALA n 
1 145 GLY n 
1 146 GLU n 
1 147 ARG n 
1 148 LEU n 
1 149 ARG n 
1 150 ALA n 
1 151 ILE n 
1 152 LEU n 
1 153 GLY n 
1 154 HIS n 
1 155 GLU n 
1 156 GLN n 
1 157 GLU n 
1 158 ILE n 
1 159 GLY n 
1 160 PHE n 
1 161 ALA n 
1 162 ALA n 
1 163 ASP n 
1 164 SER n 
1 165 ARG n 
1 166 CYS n 
1 167 ALA n 
1 168 MSE n 
1 169 ARG n 
1 170 LEU n 
1 171 VAL n 
1 172 LEU n 
1 173 GLY n 
1 174 SER 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                   174 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PA2271 
_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      'Pseudomonas aeruginosa' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     287 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACO non-polymer         . 'ACETYL COENZYME *A' ? 'C23 H38 N7 O17 P3 S' 809.571 
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 
CL  non-polymer         . 'CHLORIDE ION'       ? 'Cl -1'               35.453  
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 
MSE 'L-peptide linking' n SELENOMETHIONINE     ? 'C5 H11 N O2 Se'      196.106 
NA  non-polymer         . 'SODIUM ION'         ? 'Na 1'                22.990  
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE               ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE            ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE             ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE               ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   HIS 1   0   ?   ?   ?   A . n 
A 1 2   MSE 2   1   1   MSE MSE A . n 
A 1 3   ASP 3   2   2   ASP ASP A . n 
A 1 4   TYR 4   3   3   TYR TYR A . n 
A 1 5   ARG 5   4   4   ARG ARG A . n 
A 1 6   ILE 6   5   5   ILE ILE A . n 
A 1 7   ARG 7   6   6   ARG ARG A . n 
A 1 8   THR 8   7   7   THR THR A . n 
A 1 9   SER 9   8   8   SER SER A . n 
A 1 10  ARG 10  9   9   ARG ARG A . n 
A 1 11  ASP 11  10  10  ASP ASP A . n 
A 1 12  GLU 12  11  11  GLU GLU A . n 
A 1 13  ASP 13  12  12  ASP ASP A . n 
A 1 14  ALA 14  13  13  ALA ALA A . n 
A 1 15  ALA 15  14  14  ALA ALA A . n 
A 1 16  LEU 16  15  15  LEU LEU A . n 
A 1 17  LEU 17  16  16  LEU LEU A . n 
A 1 18  PRO 18  17  17  PRO PRO A . n 
A 1 19  ALA 19  18  18  ALA ALA A . n 
A 1 20  ILE 20  19  19  ILE ILE A . n 
A 1 21  GLU 21  20  20  GLU GLU A . n 
A 1 22  ARG 22  21  21  ARG ARG A . n 
A 1 23  SER 23  22  22  SER SER A . n 
A 1 24  ALA 24  23  23  ALA ALA A . n 
A 1 25  GLY 25  24  24  GLY GLY A . n 
A 1 26  GLU 26  25  25  GLU GLU A . n 
A 1 27  SER 27  26  26  SER SER A . n 
A 1 28  PHE 28  27  27  PHE PHE A . n 
A 1 29  ARG 29  28  28  ARG ARG A . n 
A 1 30  LEU 30  29  29  LEU LEU A . n 
A 1 31  LEU 31  30  30  LEU LEU A . n 
A 1 32  PRO 32  31  31  PRO PRO A . n 
A 1 33  GLU 33  32  32  GLU GLU A . n 
A 1 34  LEU 34  33  33  LEU LEU A . n 
A 1 35  ALA 35  34  34  ALA ALA A . n 
A 1 36  TRP 36  35  35  TRP TRP A . n 
A 1 37  ILE 37  36  36  ILE ILE A . n 
A 1 38  ALA 38  37  37  ALA ALA A . n 
A 1 39  ASP 39  38  38  ASP ASP A . n 
A 1 40  ALA 40  39  39  ALA ALA A . n 
A 1 41  GLY 41  40  40  GLY GLY A . n 
A 1 42  VAL 42  41  41  VAL VAL A . n 
A 1 43  ALA 43  42  42  ALA ALA A . n 
A 1 44  GLY 44  43  43  GLY GLY A . n 
A 1 45  VAL 45  44  44  VAL VAL A . n 
A 1 46  ASP 46  45  45  ASP ASP A . n 
A 1 47  PHE 47  46  46  PHE PHE A . n 
A 1 48  HIS 48  47  47  HIS HIS A . n 
A 1 49  ARG 49  48  48  ARG ARG A . n 
A 1 50  ARG 50  49  49  ARG ARG A . n 
A 1 51  LEU 51  50  50  LEU LEU A . n 
A 1 52  ILE 52  51  51  ILE ILE A . n 
A 1 53  GLU 53  52  52  GLU GLU A . n 
A 1 54  ARG 54  53  53  ARG ARG A . n 
A 1 55  GLY 55  54  54  GLY GLY A . n 
A 1 56  SER 56  55  55  SER SER A . n 
A 1 57  HIS 57  56  56  HIS HIS A . n 
A 1 58  TRP 58  57  57  TRP TRP A . n 
A 1 59  LEU 59  58  58  LEU LEU A . n 
A 1 60  ALA 60  59  59  ALA ALA A . n 
A 1 61  GLU 61  60  60  GLU GLU A . n 
A 1 62  ASP 62  61  61  ASP ASP A . n 
A 1 63  ALA 63  62  62  ALA ALA A . n 
A 1 64  ASP 64  63  63  ASP ASP A . n 
A 1 65  GLY 65  64  64  GLY GLY A . n 
A 1 66  GLN 66  65  65  GLN GLN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  VAL 68  67  67  VAL VAL A . n 
A 1 69  GLY 69  68  68  GLY GLY A . n 
A 1 70  PHE 70  69  69  PHE PHE A . n 
A 1 71  LEU 71  70  70  LEU LEU A . n 
A 1 72  ALA 72  71  71  ALA ALA A . n 
A 1 73  ALA 73  72  72  ALA ALA A . n 
A 1 74  GLU 74  73  73  GLU GLU A . n 
A 1 75  ARG 75  74  74  ARG ARG A . n 
A 1 76  CYS 76  75  75  CYS CYS A . n 
A 1 77  ALA 77  76  76  ALA ALA A . n 
A 1 78  ASP 78  77  77  ASP ASP A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  LEU 80  79  79  LEU LEU A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  ILE 82  81  81  ILE ILE A . n 
A 1 83  ALA 83  82  82  ALA ALA A . n 
A 1 84  GLU 84  83  83  GLU GLU A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  SER 86  85  85  SER SER A . n 
A 1 87  ILE 87  86  86  ILE ILE A . n 
A 1 88  ALA 88  87  87  ALA ALA A . n 
A 1 89  GLN 89  88  88  GLN GLN A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  HIS 91  90  90  HIS HIS A . n 
A 1 92  GLN 92  91  91  GLN GLN A . n 
A 1 93  GLN 93  92  92  GLN GLN A . n 
A 1 94  GLN 94  93  93  GLN GLN A . n 
A 1 95  GLY 95  94  94  GLY GLY A . n 
A 1 96  LEU 96  95  95  LEU LEU A . n 
A 1 97  GLY 97  96  96  GLY GLY A . n 
A 1 98  ARG 98  97  97  ARG ARG A . n 
A 1 99  ARG 99  98  98  ARG ARG A . n 
A 1 100 LEU 100 99  99  LEU LEU A . n 
A 1 101 LEU 101 100 100 LEU LEU A . n 
A 1 102 GLU 102 101 101 GLU GLU A . n 
A 1 103 ARG 103 102 102 ARG ARG A . n 
A 1 104 ALA 104 103 103 ALA ALA A . n 
A 1 105 VAL 105 104 104 VAL VAL A . n 
A 1 106 THR 106 105 105 THR THR A . n 
A 1 107 TYR 107 106 106 TYR TYR A . n 
A 1 108 ALA 108 107 107 ALA ALA A . n 
A 1 109 HIS 109 108 108 HIS HIS A . n 
A 1 110 ALA 110 109 109 ALA ALA A . n 
A 1 111 SER 111 110 110 SER SER A . n 
A 1 112 HIS 112 111 111 HIS HIS A . n 
A 1 113 CYS 113 112 112 CYS CYS A . n 
A 1 114 ARG 114 113 113 ARG ARG A . n 
A 1 115 ALA 115 114 114 ALA ALA A . n 
A 1 116 LEU 116 115 115 LEU LEU A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 THR 119 118 118 THR THR A . n 
A 1 120 THR 120 119 119 THR THR A . n 
A 1 121 PHE 121 120 120 PHE PHE A . n 
A 1 122 CYS 122 121 121 CYS CYS A . n 
A 1 123 ASP 123 122 122 ASP ASP A . n 
A 1 124 VAL 124 123 123 VAL VAL A . n 
A 1 125 PRO 125 124 124 PRO PRO A . n 
A 1 126 TRP 126 125 125 TRP TRP A . n 
A 1 127 ASN 127 126 126 ASN ASN A . n 
A 1 128 ALA 128 127 127 ALA ALA A . n 
A 1 129 PRO 129 128 128 PRO PRO A . n 
A 1 130 PHE 130 129 129 PHE PHE A . n 
A 1 131 TYR 131 130 130 TYR TYR A . n 
A 1 132 ALA 132 131 131 ALA ALA A . n 
A 1 133 ARG 133 132 132 ARG ARG A . n 
A 1 134 LEU 134 133 133 LEU LEU A . n 
A 1 135 GLY 135 134 134 GLY GLY A . n 
A 1 136 PHE 136 135 135 PHE PHE A . n 
A 1 137 GLN 137 136 136 GLN GLN A . n 
A 1 138 ARG 138 137 137 ARG ARG A . n 
A 1 139 LEU 139 138 138 LEU LEU A . n 
A 1 140 THR 140 139 139 THR THR A . n 
A 1 141 TRP 141 140 140 TRP TRP A . n 
A 1 142 GLN 142 141 141 GLN GLN A . n 
A 1 143 GLU 143 142 142 GLU GLU A . n 
A 1 144 ALA 144 143 143 ALA ALA A . n 
A 1 145 GLY 145 144 144 GLY GLY A . n 
A 1 146 GLU 146 145 145 GLU GLU A . n 
A 1 147 ARG 147 146 146 ARG ARG A . n 
A 1 148 LEU 148 147 147 LEU LEU A . n 
A 1 149 ARG 149 148 148 ARG ARG A . n 
A 1 150 ALA 150 149 149 ALA ALA A . n 
A 1 151 ILE 151 150 150 ILE ILE A . n 
A 1 152 LEU 152 151 151 LEU LEU A . n 
A 1 153 GLY 153 152 152 GLY GLY A . n 
A 1 154 HIS 154 153 153 HIS HIS A . n 
A 1 155 GLU 155 154 154 GLU GLU A . n 
A 1 156 GLN 156 155 155 GLN GLN A . n 
A 1 157 GLU 157 156 156 GLU GLU A . n 
A 1 158 ILE 158 157 157 ILE ILE A . n 
A 1 159 GLY 159 158 158 GLY GLY A . n 
A 1 160 PHE 160 159 159 PHE PHE A . n 
A 1 161 ALA 161 160 160 ALA ALA A . n 
A 1 162 ALA 162 161 161 ALA ALA A . n 
A 1 163 ASP 163 162 162 ASP ASP A . n 
A 1 164 SER 164 163 163 SER SER A . n 
A 1 165 ARG 165 164 164 ARG ARG A . n 
A 1 166 CYS 166 165 165 CYS CYS A . n 
A 1 167 ALA 167 166 166 ALA ALA A . n 
A 1 168 MSE 168 167 167 MSE MSE A . n 
A 1 169 ARG 169 168 168 ARG ARG A . n 
A 1 170 LEU 170 169 169 LEU LEU A . n 
A 1 171 VAL 171 170 170 VAL VAL A . n 
A 1 172 LEU 172 171 171 LEU LEU A . n 
A 1 173 GLY 173 172 172 GLY GLY A . n 
A 1 174 SER 174 173 ?   ?   ?   A . n 
B 1 1   HIS 1   0   ?   ?   ?   B . n 
B 1 2   MSE 2   1   1   MSE MSE B . n 
B 1 3   ASP 3   2   2   ASP ASP B . n 
B 1 4   TYR 4   3   3   TYR TYR B . n 
B 1 5   ARG 5   4   4   ARG ARG B . n 
B 1 6   ILE 6   5   5   ILE ILE B . n 
B 1 7   ARG 7   6   6   ARG ARG B . n 
B 1 8   THR 8   7   7   THR THR B . n 
B 1 9   SER 9   8   8   SER SER B . n 
B 1 10  ARG 10  9   9   ARG ARG B . n 
B 1 11  ASP 11  10  10  ASP ASP B . n 
B 1 12  GLU 12  11  11  GLU GLU B . n 
B 1 13  ASP 13  12  12  ASP ASP B . n 
B 1 14  ALA 14  13  13  ALA ALA B . n 
B 1 15  ALA 15  14  14  ALA ALA B . n 
B 1 16  LEU 16  15  15  LEU LEU B . n 
B 1 17  LEU 17  16  16  LEU LEU B . n 
B 1 18  PRO 18  17  17  PRO PRO B . n 
B 1 19  ALA 19  18  18  ALA ALA B . n 
B 1 20  ILE 20  19  19  ILE ILE B . n 
B 1 21  GLU 21  20  20  GLU GLU B . n 
B 1 22  ARG 22  21  21  ARG ARG B . n 
B 1 23  SER 23  22  22  SER SER B . n 
B 1 24  ALA 24  23  23  ALA ALA B . n 
B 1 25  GLY 25  24  24  GLY GLY B . n 
B 1 26  GLU 26  25  25  GLU GLU B . n 
B 1 27  SER 27  26  26  SER SER B . n 
B 1 28  PHE 28  27  27  PHE PHE B . n 
B 1 29  ARG 29  28  28  ARG ARG B . n 
B 1 30  LEU 30  29  29  LEU LEU B . n 
B 1 31  LEU 31  30  30  LEU LEU B . n 
B 1 32  PRO 32  31  31  PRO PRO B . n 
B 1 33  GLU 33  32  32  GLU GLU B . n 
B 1 34  LEU 34  33  33  LEU LEU B . n 
B 1 35  ALA 35  34  34  ALA ALA B . n 
B 1 36  TRP 36  35  35  TRP TRP B . n 
B 1 37  ILE 37  36  36  ILE ILE B . n 
B 1 38  ALA 38  37  37  ALA ALA B . n 
B 1 39  ASP 39  38  38  ASP ASP B . n 
B 1 40  ALA 40  39  39  ALA ALA B . n 
B 1 41  GLY 41  40  40  GLY GLY B . n 
B 1 42  VAL 42  41  41  VAL VAL B . n 
B 1 43  ALA 43  42  42  ALA ALA B . n 
B 1 44  GLY 44  43  43  GLY GLY B . n 
B 1 45  VAL 45  44  44  VAL VAL B . n 
B 1 46  ASP 46  45  45  ASP ASP B . n 
B 1 47  PHE 47  46  46  PHE PHE B . n 
B 1 48  HIS 48  47  47  HIS HIS B . n 
B 1 49  ARG 49  48  48  ARG ARG B . n 
B 1 50  ARG 50  49  49  ARG ARG B . n 
B 1 51  LEU 51  50  50  LEU LEU B . n 
B 1 52  ILE 52  51  51  ILE ILE B . n 
B 1 53  GLU 53  52  52  GLU GLU B . n 
B 1 54  ARG 54  53  53  ARG ARG B . n 
B 1 55  GLY 55  54  54  GLY GLY B . n 
B 1 56  SER 56  55  55  SER SER B . n 
B 1 57  HIS 57  56  56  HIS HIS B . n 
B 1 58  TRP 58  57  57  TRP TRP B . n 
B 1 59  LEU 59  58  58  LEU LEU B . n 
B 1 60  ALA 60  59  59  ALA ALA B . n 
B 1 61  GLU 61  60  60  GLU GLU B . n 
B 1 62  ASP 62  61  61  ASP ASP B . n 
B 1 63  ALA 63  62  62  ALA ALA B . n 
B 1 64  ASP 64  63  63  ASP ASP B . n 
B 1 65  GLY 65  64  64  GLY GLY B . n 
B 1 66  GLN 66  65  65  GLN GLN B . n 
B 1 67  PRO 67  66  66  PRO PRO B . n 
B 1 68  VAL 68  67  67  VAL VAL B . n 
B 1 69  GLY 69  68  68  GLY GLY B . n 
B 1 70  PHE 70  69  69  PHE PHE B . n 
B 1 71  LEU 71  70  70  LEU LEU B . n 
B 1 72  ALA 72  71  71  ALA ALA B . n 
B 1 73  ALA 73  72  72  ALA ALA B . n 
B 1 74  GLU 74  73  73  GLU GLU B . n 
B 1 75  ARG 75  74  74  ARG ARG B . n 
B 1 76  CYS 76  75  75  CYS CYS B . n 
B 1 77  ALA 77  76  76  ALA ALA B . n 
B 1 78  ASP 78  77  77  ASP ASP B . n 
B 1 79  GLU 79  78  78  GLU GLU B . n 
B 1 80  LEU 80  79  79  LEU LEU B . n 
B 1 81  HIS 81  80  80  HIS HIS B . n 
B 1 82  ILE 82  81  81  ILE ILE B . n 
B 1 83  ALA 83  82  82  ALA ALA B . n 
B 1 84  GLU 84  83  83  GLU GLU B . n 
B 1 85  LEU 85  84  84  LEU LEU B . n 
B 1 86  SER 86  85  85  SER SER B . n 
B 1 87  ILE 87  86  86  ILE ILE B . n 
B 1 88  ALA 88  87  87  ALA ALA B . n 
B 1 89  GLN 89  88  88  GLN GLN B . n 
B 1 90  ALA 90  89  89  ALA ALA B . n 
B 1 91  HIS 91  90  90  HIS HIS B . n 
B 1 92  GLN 92  91  91  GLN GLN B . n 
B 1 93  GLN 93  92  92  GLN GLN B . n 
B 1 94  GLN 94  93  93  GLN GLN B . n 
B 1 95  GLY 95  94  94  GLY GLY B . n 
B 1 96  LEU 96  95  95  LEU LEU B . n 
B 1 97  GLY 97  96  96  GLY GLY B . n 
B 1 98  ARG 98  97  97  ARG ARG B . n 
B 1 99  ARG 99  98  98  ARG ARG B . n 
B 1 100 LEU 100 99  99  LEU LEU B . n 
B 1 101 LEU 101 100 100 LEU LEU B . n 
B 1 102 GLU 102 101 101 GLU GLU B . n 
B 1 103 ARG 103 102 102 ARG ARG B . n 
B 1 104 ALA 104 103 103 ALA ALA B . n 
B 1 105 VAL 105 104 104 VAL VAL B . n 
B 1 106 THR 106 105 105 THR THR B . n 
B 1 107 TYR 107 106 106 TYR TYR B . n 
B 1 108 ALA 108 107 107 ALA ALA B . n 
B 1 109 HIS 109 108 108 HIS HIS B . n 
B 1 110 ALA 110 109 109 ALA ALA B . n 
B 1 111 SER 111 110 110 SER SER B . n 
B 1 112 HIS 112 111 111 HIS HIS B . n 
B 1 113 CYS 113 112 112 CYS CYS B . n 
B 1 114 ARG 114 113 113 ARG ARG B . n 
B 1 115 ALA 115 114 114 ALA ALA B . n 
B 1 116 LEU 116 115 115 LEU LEU B . n 
B 1 117 THR 117 116 116 THR THR B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 THR 119 118 118 THR THR B . n 
B 1 120 THR 120 119 119 THR THR B . n 
B 1 121 PHE 121 120 120 PHE PHE B . n 
B 1 122 CYS 122 121 121 CYS CYS B . n 
B 1 123 ASP 123 122 122 ASP ASP B . n 
B 1 124 VAL 124 123 123 VAL VAL B . n 
B 1 125 PRO 125 124 124 PRO PRO B . n 
B 1 126 TRP 126 125 125 TRP TRP B . n 
B 1 127 ASN 127 126 126 ASN ASN B . n 
B 1 128 ALA 128 127 127 ALA ALA B . n 
B 1 129 PRO 129 128 128 PRO PRO B . n 
B 1 130 PHE 130 129 129 PHE PHE B . n 
B 1 131 TYR 131 130 130 TYR TYR B . n 
B 1 132 ALA 132 131 131 ALA ALA B . n 
B 1 133 ARG 133 132 132 ARG ARG B . n 
B 1 134 LEU 134 133 133 LEU LEU B . n 
B 1 135 GLY 135 134 134 GLY GLY B . n 
B 1 136 PHE 136 135 135 PHE PHE B . n 
B 1 137 GLN 137 136 136 GLN GLN B . n 
B 1 138 ARG 138 137 137 ARG ARG B . n 
B 1 139 LEU 139 138 138 LEU LEU B . n 
B 1 140 THR 140 139 139 THR THR B . n 
B 1 141 TRP 141 140 140 TRP TRP B . n 
B 1 142 GLN 142 141 141 GLN GLN B . n 
B 1 143 GLU 143 142 142 GLU GLU B . n 
B 1 144 ALA 144 143 143 ALA ALA B . n 
B 1 145 GLY 145 144 144 GLY GLY B . n 
B 1 146 GLU 146 145 145 GLU GLU B . n 
B 1 147 ARG 147 146 146 ARG ARG B . n 
B 1 148 LEU 148 147 147 LEU LEU B . n 
B 1 149 ARG 149 148 148 ARG ARG B . n 
B 1 150 ALA 150 149 149 ALA ALA B . n 
B 1 151 ILE 151 150 150 ILE ILE B . n 
B 1 152 LEU 152 151 151 LEU LEU B . n 
B 1 153 GLY 153 152 152 GLY GLY B . n 
B 1 154 HIS 154 153 153 HIS HIS B . n 
B 1 155 GLU 155 154 154 GLU GLU B . n 
B 1 156 GLN 156 155 155 GLN GLN B . n 
B 1 157 GLU 157 156 156 GLU GLU B . n 
B 1 158 ILE 158 157 157 ILE ILE B . n 
B 1 159 GLY 159 158 158 GLY GLY B . n 
B 1 160 PHE 160 159 159 PHE PHE B . n 
B 1 161 ALA 161 160 160 ALA ALA B . n 
B 1 162 ALA 162 161 161 ALA ALA B . n 
B 1 163 ASP 163 162 162 ASP ASP B . n 
B 1 164 SER 164 163 163 SER SER B . n 
B 1 165 ARG 165 164 164 ARG ARG B . n 
B 1 166 CYS 166 165 165 CYS CYS B . n 
B 1 167 ALA 167 166 166 ALA ALA B . n 
B 1 168 MSE 168 167 167 MSE MSE B . n 
B 1 169 ARG 169 168 168 ARG ARG B . n 
B 1 170 LEU 170 169 169 LEU LEU B . n 
B 1 171 VAL 171 170 170 VAL VAL B . n 
B 1 172 LEU 172 171 171 LEU LEU B . n 
B 1 173 GLY 173 172 172 GLY GLY B . n 
B 1 174 SER 174 173 173 SER SER B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ACO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ACO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ACO 1   201 1423 ACO ACO A . 
D 3 NA  1   202 3    NA  NA  A . 
E 3 NA  1   203 4    NA  NA  A . 
F 3 NA  1   204 6    NA  NA  A . 
G 4 CL  1   205 3    CL  CL  A . 
H 2 ACO 1   201 1424 ACO ACO B . 
I 3 NA  1   202 5    NA  NA  B . 
J 3 NA  1   203 7    NA  NA  B . 
K 4 CL  1   204 2    CL  CL  B . 
L 5 HOH 1   301 216  HOH HOH A . 
L 5 HOH 2   302 76   HOH HOH A . 
L 5 HOH 3   303 298  HOH HOH A . 
L 5 HOH 4   304 223  HOH HOH A . 
L 5 HOH 5   305 648  HOH HOH A . 
L 5 HOH 6   306 628  HOH HOH A . 
L 5 HOH 7   307 293  HOH HOH A . 
L 5 HOH 8   308 187  HOH HOH A . 
L 5 HOH 9   309 380  HOH HOH A . 
L 5 HOH 10  310 87   HOH HOH A . 
L 5 HOH 11  311 589  HOH HOH A . 
L 5 HOH 12  312 278  HOH HOH A . 
L 5 HOH 13  313 313  HOH HOH A . 
L 5 HOH 14  314 425  HOH HOH A . 
L 5 HOH 15  315 599  HOH HOH A . 
L 5 HOH 16  316 512  HOH HOH A . 
L 5 HOH 17  317 573  HOH HOH A . 
L 5 HOH 18  318 339  HOH HOH A . 
L 5 HOH 19  319 311  HOH HOH A . 
L 5 HOH 20  320 323  HOH HOH A . 
L 5 HOH 21  321 374  HOH HOH A . 
L 5 HOH 22  322 93   HOH HOH A . 
L 5 HOH 23  323 281  HOH HOH A . 
L 5 HOH 24  324 235  HOH HOH A . 
L 5 HOH 25  325 463  HOH HOH A . 
L 5 HOH 26  326 31   HOH HOH A . 
L 5 HOH 27  327 577  HOH HOH A . 
L 5 HOH 28  328 156  HOH HOH A . 
L 5 HOH 29  329 265  HOH HOH A . 
L 5 HOH 30  330 327  HOH HOH A . 
L 5 HOH 31  331 639  HOH HOH A . 
L 5 HOH 32  332 259  HOH HOH A . 
L 5 HOH 33  333 54   HOH HOH A . 
L 5 HOH 34  334 152  HOH HOH A . 
L 5 HOH 35  335 179  HOH HOH A . 
L 5 HOH 36  336 436  HOH HOH A . 
L 5 HOH 37  337 447  HOH HOH A . 
L 5 HOH 38  338 198  HOH HOH A . 
L 5 HOH 39  339 63   HOH HOH A . 
L 5 HOH 40  340 23   HOH HOH A . 
L 5 HOH 41  341 414  HOH HOH A . 
L 5 HOH 42  342 295  HOH HOH A . 
L 5 HOH 43  343 319  HOH HOH A . 
L 5 HOH 44  344 343  HOH HOH A . 
L 5 HOH 45  345 564  HOH HOH A . 
L 5 HOH 46  346 190  HOH HOH A . 
L 5 HOH 47  347 201  HOH HOH A . 
L 5 HOH 48  348 102  HOH HOH A . 
L 5 HOH 49  349 444  HOH HOH A . 
L 5 HOH 50  350 338  HOH HOH A . 
L 5 HOH 51  351 390  HOH HOH A . 
L 5 HOH 52  352 25   HOH HOH A . 
L 5 HOH 53  353 361  HOH HOH A . 
L 5 HOH 54  354 271  HOH HOH A . 
L 5 HOH 55  355 483  HOH HOH A . 
L 5 HOH 56  356 534  HOH HOH A . 
L 5 HOH 57  357 142  HOH HOH A . 
L 5 HOH 58  358 188  HOH HOH A . 
L 5 HOH 59  359 683  HOH HOH A . 
L 5 HOH 60  360 316  HOH HOH A . 
L 5 HOH 61  361 536  HOH HOH A . 
L 5 HOH 62  362 636  HOH HOH A . 
L 5 HOH 63  363 110  HOH HOH A . 
L 5 HOH 64  364 6    HOH HOH A . 
L 5 HOH 65  365 74   HOH HOH A . 
L 5 HOH 66  366 148  HOH HOH A . 
L 5 HOH 67  367 104  HOH HOH A . 
L 5 HOH 68  368 132  HOH HOH A . 
L 5 HOH 69  369 358  HOH HOH A . 
L 5 HOH 70  370 164  HOH HOH A . 
L 5 HOH 71  371 516  HOH HOH A . 
L 5 HOH 72  372 38   HOH HOH A . 
L 5 HOH 73  373 46   HOH HOH A . 
L 5 HOH 74  374 241  HOH HOH A . 
L 5 HOH 75  375 177  HOH HOH A . 
L 5 HOH 76  376 99   HOH HOH A . 
L 5 HOH 77  377 60   HOH HOH A . 
L 5 HOH 78  378 246  HOH HOH A . 
L 5 HOH 79  379 403  HOH HOH A . 
L 5 HOH 80  380 117  HOH HOH A . 
L 5 HOH 81  381 97   HOH HOH A . 
L 5 HOH 82  382 65   HOH HOH A . 
L 5 HOH 83  383 539  HOH HOH A . 
L 5 HOH 84  384 195  HOH HOH A . 
L 5 HOH 85  385 19   HOH HOH A . 
L 5 HOH 86  386 30   HOH HOH A . 
L 5 HOH 87  387 279  HOH HOH A . 
L 5 HOH 88  388 304  HOH HOH A . 
L 5 HOH 89  389 82   HOH HOH A . 
L 5 HOH 90  390 29   HOH HOH A . 
L 5 HOH 91  391 453  HOH HOH A . 
L 5 HOH 92  392 169  HOH HOH A . 
L 5 HOH 93  393 664  HOH HOH A . 
L 5 HOH 94  394 505  HOH HOH A . 
L 5 HOH 95  395 517  HOH HOH A . 
L 5 HOH 96  396 270  HOH HOH A . 
L 5 HOH 97  397 454  HOH HOH A . 
L 5 HOH 98  398 106  HOH HOH A . 
L 5 HOH 99  399 172  HOH HOH A . 
L 5 HOH 100 400 675  HOH HOH A . 
L 5 HOH 101 401 78   HOH HOH A . 
L 5 HOH 102 402 283  HOH HOH A . 
L 5 HOH 103 403 685  HOH HOH A . 
L 5 HOH 104 404 129  HOH HOH A . 
L 5 HOH 105 405 43   HOH HOH A . 
L 5 HOH 106 406 184  HOH HOH A . 
L 5 HOH 107 407 22   HOH HOH A . 
L 5 HOH 108 408 61   HOH HOH A . 
L 5 HOH 109 409 83   HOH HOH A . 
L 5 HOH 110 410 44   HOH HOH A . 
L 5 HOH 111 411 91   HOH HOH A . 
L 5 HOH 112 412 371  HOH HOH A . 
L 5 HOH 113 413 377  HOH HOH A . 
L 5 HOH 114 414 68   HOH HOH A . 
L 5 HOH 115 415 108  HOH HOH A . 
L 5 HOH 116 416 296  HOH HOH A . 
L 5 HOH 117 417 437  HOH HOH A . 
L 5 HOH 118 418 112  HOH HOH A . 
L 5 HOH 119 419 481  HOH HOH A . 
L 5 HOH 120 420 79   HOH HOH A . 
L 5 HOH 121 421 282  HOH HOH A . 
L 5 HOH 122 422 42   HOH HOH A . 
L 5 HOH 123 423 49   HOH HOH A . 
L 5 HOH 124 424 445  HOH HOH A . 
L 5 HOH 125 425 588  HOH HOH A . 
L 5 HOH 126 426 191  HOH HOH A . 
L 5 HOH 127 427 71   HOH HOH A . 
L 5 HOH 128 428 105  HOH HOH A . 
L 5 HOH 129 429 84   HOH HOH A . 
L 5 HOH 130 430 462  HOH HOH A . 
L 5 HOH 131 431 210  HOH HOH A . 
L 5 HOH 132 432 248  HOH HOH A . 
L 5 HOH 133 433 136  HOH HOH A . 
L 5 HOH 134 434 204  HOH HOH A . 
L 5 HOH 135 435 510  HOH HOH A . 
L 5 HOH 136 436 206  HOH HOH A . 
L 5 HOH 137 437 487  HOH HOH A . 
L 5 HOH 138 438 228  HOH HOH A . 
L 5 HOH 139 439 202  HOH HOH A . 
L 5 HOH 140 440 514  HOH HOH A . 
L 5 HOH 141 441 682  HOH HOH A . 
L 5 HOH 142 442 189  HOH HOH A . 
L 5 HOH 143 443 134  HOH HOH A . 
L 5 HOH 144 444 538  HOH HOH A . 
L 5 HOH 145 445 352  HOH HOH A . 
L 5 HOH 146 446 272  HOH HOH A . 
L 5 HOH 147 447 397  HOH HOH A . 
L 5 HOH 148 448 660  HOH HOH A . 
L 5 HOH 149 449 429  HOH HOH A . 
L 5 HOH 150 450 107  HOH HOH A . 
L 5 HOH 151 451 508  HOH HOH A . 
L 5 HOH 152 452 261  HOH HOH A . 
L 5 HOH 153 453 67   HOH HOH A . 
L 5 HOH 154 454 562  HOH HOH A . 
L 5 HOH 155 455 115  HOH HOH A . 
L 5 HOH 156 456 288  HOH HOH A . 
L 5 HOH 157 457 62   HOH HOH A . 
L 5 HOH 158 458 59   HOH HOH A . 
L 5 HOH 159 459 155  HOH HOH A . 
L 5 HOH 160 460 122  HOH HOH A . 
L 5 HOH 161 461 372  HOH HOH A . 
L 5 HOH 162 462 64   HOH HOH A . 
L 5 HOH 163 463 111  HOH HOH A . 
L 5 HOH 164 464 154  HOH HOH A . 
L 5 HOH 165 465 408  HOH HOH A . 
L 5 HOH 166 466 94   HOH HOH A . 
L 5 HOH 167 467 369  HOH HOH A . 
L 5 HOH 168 468 197  HOH HOH A . 
L 5 HOH 169 469 50   HOH HOH A . 
L 5 HOH 170 470 363  HOH HOH A . 
L 5 HOH 171 471 103  HOH HOH A . 
L 5 HOH 172 472 574  HOH HOH A . 
L 5 HOH 173 473 638  HOH HOH A . 
L 5 HOH 174 474 37   HOH HOH A . 
L 5 HOH 175 475 355  HOH HOH A . 
L 5 HOH 176 476 231  HOH HOH A . 
L 5 HOH 177 477 482  HOH HOH A . 
L 5 HOH 178 478 634  HOH HOH A . 
L 5 HOH 179 479 540  HOH HOH A . 
L 5 HOH 180 480 566  HOH HOH A . 
L 5 HOH 181 481 384  HOH HOH A . 
L 5 HOH 182 482 553  HOH HOH A . 
L 5 HOH 183 483 480  HOH HOH A . 
L 5 HOH 184 484 559  HOH HOH A . 
L 5 HOH 185 485 687  HOH HOH A . 
L 5 HOH 186 486 592  HOH HOH A . 
L 5 HOH 187 487 421  HOH HOH A . 
L 5 HOH 188 488 561  HOH HOH A . 
L 5 HOH 189 489 590  HOH HOH A . 
L 5 HOH 190 490 506  HOH HOH A . 
L 5 HOH 191 491 535  HOH HOH A . 
L 5 HOH 192 492 303  HOH HOH A . 
L 5 HOH 193 493 593  HOH HOH A . 
L 5 HOH 194 494 666  HOH HOH A . 
L 5 HOH 195 495 379  HOH HOH A . 
L 5 HOH 196 496 398  HOH HOH A . 
L 5 HOH 197 497 684  HOH HOH A . 
L 5 HOH 198 498 681  HOH HOH A . 
L 5 HOH 199 499 252  HOH HOH A . 
L 5 HOH 200 500 542  HOH HOH A . 
L 5 HOH 201 501 276  HOH HOH A . 
L 5 HOH 202 502 196  HOH HOH A . 
L 5 HOH 203 503 285  HOH HOH A . 
L 5 HOH 204 504 300  HOH HOH A . 
L 5 HOH 205 505 306  HOH HOH A . 
L 5 HOH 206 506 423  HOH HOH A . 
L 5 HOH 207 507 477  HOH HOH A . 
L 5 HOH 208 508 200  HOH HOH A . 
L 5 HOH 209 509 153  HOH HOH A . 
L 5 HOH 210 510 242  HOH HOH A . 
L 5 HOH 211 511 182  HOH HOH A . 
L 5 HOH 212 512 537  HOH HOH A . 
L 5 HOH 213 513 144  HOH HOH A . 
L 5 HOH 214 514 631  HOH HOH A . 
L 5 HOH 215 515 336  HOH HOH A . 
L 5 HOH 216 516 334  HOH HOH A . 
L 5 HOH 217 517 268  HOH HOH A . 
L 5 HOH 218 518 392  HOH HOH A . 
L 5 HOH 219 519 357  HOH HOH A . 
L 5 HOH 220 520 266  HOH HOH A . 
L 5 HOH 221 521 262  HOH HOH A . 
L 5 HOH 222 522 165  HOH HOH A . 
L 5 HOH 223 523 488  HOH HOH A . 
L 5 HOH 224 524 325  HOH HOH A . 
L 5 HOH 225 525 665  HOH HOH A . 
L 5 HOH 226 526 309  HOH HOH A . 
L 5 HOH 227 527 575  HOH HOH A . 
L 5 HOH 228 528 229  HOH HOH A . 
L 5 HOH 229 529 225  HOH HOH A . 
L 5 HOH 230 530 181  HOH HOH A . 
L 5 HOH 231 531 267  HOH HOH A . 
L 5 HOH 232 532 366  HOH HOH A . 
L 5 HOH 233 533 139  HOH HOH A . 
L 5 HOH 234 534 603  HOH HOH A . 
L 5 HOH 235 535 507  HOH HOH A . 
L 5 HOH 236 536 356  HOH HOH A . 
L 5 HOH 237 537 391  HOH HOH A . 
L 5 HOH 238 538 667  HOH HOH A . 
L 5 HOH 239 539 479  HOH HOH A . 
L 5 HOH 240 540 686  HOH HOH A . 
L 5 HOH 241 541 632  HOH HOH A . 
L 5 HOH 242 542 320  HOH HOH A . 
L 5 HOH 243 543 552  HOH HOH A . 
L 5 HOH 244 544 411  HOH HOH A . 
L 5 HOH 245 545 368  HOH HOH A . 
L 5 HOH 246 546 565  HOH HOH A . 
L 5 HOH 247 547 615  HOH HOH A . 
L 5 HOH 248 548 591  HOH HOH A . 
L 5 HOH 249 549 509  HOH HOH A . 
L 5 HOH 250 550 376  HOH HOH A . 
L 5 HOH 251 551 273  HOH HOH A . 
L 5 HOH 252 552 679  HOH HOH A . 
M 5 HOH 1   301 629  HOH HOH B . 
M 5 HOH 2   302 522  HOH HOH B . 
M 5 HOH 3   303 415  HOH HOH B . 
M 5 HOH 4   304 652  HOH HOH B . 
M 5 HOH 5   305 610  HOH HOH B . 
M 5 HOH 6   306 301  HOH HOH B . 
M 5 HOH 7   307 162  HOH HOH B . 
M 5 HOH 8   308 649  HOH HOH B . 
M 5 HOH 9   309 622  HOH HOH B . 
M 5 HOH 10  310 386  HOH HOH B . 
M 5 HOH 11  311 32   HOH HOH B . 
M 5 HOH 12  312 26   HOH HOH B . 
M 5 HOH 13  313 547  HOH HOH B . 
M 5 HOH 14  314 69   HOH HOH B . 
M 5 HOH 15  315 158  HOH HOH B . 
M 5 HOH 16  316 247  HOH HOH B . 
M 5 HOH 17  317 645  HOH HOH B . 
M 5 HOH 18  318 460  HOH HOH B . 
M 5 HOH 19  319 305  HOH HOH B . 
M 5 HOH 20  320 619  HOH HOH B . 
M 5 HOH 21  321 100  HOH HOH B . 
M 5 HOH 22  322 611  HOH HOH B . 
M 5 HOH 23  323 307  HOH HOH B . 
M 5 HOH 24  324 623  HOH HOH B . 
M 5 HOH 25  325 222  HOH HOH B . 
M 5 HOH 26  326 322  HOH HOH B . 
M 5 HOH 27  327 294  HOH HOH B . 
M 5 HOH 28  328 81   HOH HOH B . 
M 5 HOH 29  329 194  HOH HOH B . 
M 5 HOH 30  330 245  HOH HOH B . 
M 5 HOH 31  331 123  HOH HOH B . 
M 5 HOH 32  332 473  HOH HOH B . 
M 5 HOH 33  333 662  HOH HOH B . 
M 5 HOH 34  334 351  HOH HOH B . 
M 5 HOH 35  335 80   HOH HOH B . 
M 5 HOH 36  336 354  HOH HOH B . 
M 5 HOH 37  337 625  HOH HOH B . 
M 5 HOH 38  338 395  HOH HOH B . 
M 5 HOH 39  339 21   HOH HOH B . 
M 5 HOH 40  340 340  HOH HOH B . 
M 5 HOH 41  341 406  HOH HOH B . 
M 5 HOH 42  342 455  HOH HOH B . 
M 5 HOH 43  343 41   HOH HOH B . 
M 5 HOH 44  344 13   HOH HOH B . 
M 5 HOH 45  345 217  HOH HOH B . 
M 5 HOH 46  346 527  HOH HOH B . 
M 5 HOH 47  347 226  HOH HOH B . 
M 5 HOH 48  348 257  HOH HOH B . 
M 5 HOH 49  349 208  HOH HOH B . 
M 5 HOH 50  350 362  HOH HOH B . 
M 5 HOH 51  351 677  HOH HOH B . 
M 5 HOH 52  352 131  HOH HOH B . 
M 5 HOH 53  353 370  HOH HOH B . 
M 5 HOH 54  354 207  HOH HOH B . 
M 5 HOH 55  355 569  HOH HOH B . 
M 5 HOH 56  356 410  HOH HOH B . 
M 5 HOH 57  357 277  HOH HOH B . 
M 5 HOH 58  358 70   HOH HOH B . 
M 5 HOH 59  359 240  HOH HOH B . 
M 5 HOH 60  360 367  HOH HOH B . 
M 5 HOH 61  361 378  HOH HOH B . 
M 5 HOH 62  362 52   HOH HOH B . 
M 5 HOH 63  363 92   HOH HOH B . 
M 5 HOH 64  364 47   HOH HOH B . 
M 5 HOH 65  365 53   HOH HOH B . 
M 5 HOH 66  366 613  HOH HOH B . 
M 5 HOH 67  367 297  HOH HOH B . 
M 5 HOH 68  368 609  HOH HOH B . 
M 5 HOH 69  369 178  HOH HOH B . 
M 5 HOH 70  370 548  HOH HOH B . 
M 5 HOH 71  371 33   HOH HOH B . 
M 5 HOH 72  372 98   HOH HOH B . 
M 5 HOH 73  373 113  HOH HOH B . 
M 5 HOH 74  374 289  HOH HOH B . 
M 5 HOH 75  375 39   HOH HOH B . 
M 5 HOH 76  376 118  HOH HOH B . 
M 5 HOH 77  377 457  HOH HOH B . 
M 5 HOH 78  378 308  HOH HOH B . 
M 5 HOH 79  379 120  HOH HOH B . 
M 5 HOH 80  380 95   HOH HOH B . 
M 5 HOH 81  381 251  HOH HOH B . 
M 5 HOH 82  382 260  HOH HOH B . 
M 5 HOH 83  383 674  HOH HOH B . 
M 5 HOH 84  384 515  HOH HOH B . 
M 5 HOH 85  385 269  HOH HOH B . 
M 5 HOH 86  386 27   HOH HOH B . 
M 5 HOH 87  387 287  HOH HOH B . 
M 5 HOH 88  388 57   HOH HOH B . 
M 5 HOH 89  389 34   HOH HOH B . 
M 5 HOH 90  390 101  HOH HOH B . 
M 5 HOH 91  391 171  HOH HOH B . 
M 5 HOH 92  392 383  HOH HOH B . 
M 5 HOH 93  393 77   HOH HOH B . 
M 5 HOH 94  394 427  HOH HOH B . 
M 5 HOH 95  395 286  HOH HOH B . 
M 5 HOH 96  396 73   HOH HOH B . 
M 5 HOH 97  397 550  HOH HOH B . 
M 5 HOH 98  398 321  HOH HOH B . 
M 5 HOH 99  399 496  HOH HOH B . 
M 5 HOH 100 400 501  HOH HOH B . 
M 5 HOH 101 401 192  HOH HOH B . 
M 5 HOH 102 402 450  HOH HOH B . 
M 5 HOH 103 403 524  HOH HOH B . 
M 5 HOH 104 404 56   HOH HOH B . 
M 5 HOH 105 405 555  HOH HOH B . 
M 5 HOH 106 406 227  HOH HOH B . 
M 5 HOH 107 407 442  HOH HOH B . 
M 5 HOH 108 408 275  HOH HOH B . 
M 5 HOH 109 409 124  HOH HOH B . 
M 5 HOH 110 410 250  HOH HOH B . 
M 5 HOH 111 411 45   HOH HOH B . 
M 5 HOH 112 412 72   HOH HOH B . 
M 5 HOH 113 413 292  HOH HOH B . 
M 5 HOH 114 414 90   HOH HOH B . 
M 5 HOH 115 415 237  HOH HOH B . 
M 5 HOH 116 416 109  HOH HOH B . 
M 5 HOH 117 417 402  HOH HOH B . 
M 5 HOH 118 418 167  HOH HOH B . 
M 5 HOH 119 419 174  HOH HOH B . 
M 5 HOH 120 420 612  HOH HOH B . 
M 5 HOH 121 421 642  HOH HOH B . 
M 5 HOH 122 422 433  HOH HOH B . 
M 5 HOH 123 423 493  HOH HOH B . 
M 5 HOH 124 424 404  HOH HOH B . 
M 5 HOH 125 425 125  HOH HOH B . 
M 5 HOH 126 426 66   HOH HOH B . 
M 5 HOH 127 427 443  HOH HOH B . 
M 5 HOH 128 428 519  HOH HOH B . 
M 5 HOH 129 429 526  HOH HOH B . 
M 5 HOH 130 430 314  HOH HOH B . 
M 5 HOH 131 431 183  HOH HOH B . 
M 5 HOH 132 432 446  HOH HOH B . 
M 5 HOH 133 433 676  HOH HOH B . 
M 5 HOH 134 434 651  HOH HOH B . 
M 5 HOH 135 435 504  HOH HOH B . 
M 5 HOH 136 436 219  HOH HOH B . 
M 5 HOH 137 437 264  HOH HOH B . 
M 5 HOH 138 438 643  HOH HOH B . 
M 5 HOH 139 439 128  HOH HOH B . 
M 5 HOH 140 440 315  HOH HOH B . 
M 5 HOH 141 441 688  HOH HOH B . 
M 5 HOH 142 442 256  HOH HOH B . 
M 5 HOH 143 443 135  HOH HOH B . 
M 5 HOH 144 444 149  HOH HOH B . 
M 5 HOH 145 445 96   HOH HOH B . 
M 5 HOH 146 446 606  HOH HOH B . 
M 5 HOH 147 447 530  HOH HOH B . 
M 5 HOH 148 448 503  HOH HOH B . 
M 5 HOH 149 449 420  HOH HOH B . 
M 5 HOH 150 450 258  HOH HOH B . 
M 5 HOH 151 451 346  HOH HOH B . 
M 5 HOH 152 452 494  HOH HOH B . 
M 5 HOH 153 453 166  HOH HOH B . 
M 5 HOH 154 454 347  HOH HOH B . 
M 5 HOH 155 455 173  HOH HOH B . 
M 5 HOH 156 456 238  HOH HOH B . 
M 5 HOH 157 457 653  HOH HOH B . 
M 5 HOH 158 458 523  HOH HOH B . 
M 5 HOH 159 459 529  HOH HOH B . 
M 5 HOH 160 460 598  HOH HOH B . 
M 5 HOH 161 461 497  HOH HOH B . 
M 5 HOH 162 462 396  HOH HOH B . 
M 5 HOH 163 463 130  HOH HOH B . 
M 5 HOH 164 464 360  HOH HOH B . 
M 5 HOH 165 465 500  HOH HOH B . 
M 5 HOH 166 466 86   HOH HOH B . 
M 5 HOH 167 467 461  HOH HOH B . 
M 5 HOH 168 468 89   HOH HOH B . 
M 5 HOH 169 469 85   HOH HOH B . 
M 5 HOH 170 470 388  HOH HOH B . 
M 5 HOH 171 471 624  HOH HOH B . 
M 5 HOH 172 472 572  HOH HOH B . 
M 5 HOH 173 473 531  HOH HOH B . 
M 5 HOH 174 474 502  HOH HOH B . 
M 5 HOH 175 475 359  HOH HOH B . 
M 5 HOH 176 476 570  HOH HOH B . 
M 5 HOH 177 477 126  HOH HOH B . 
M 5 HOH 178 478 560  HOH HOH B . 
M 5 HOH 179 479 567  HOH HOH B . 
M 5 HOH 180 480 170  HOH HOH B . 
M 5 HOH 181 481 399  HOH HOH B . 
M 5 HOH 182 482 456  HOH HOH B . 
M 5 HOH 183 483 551  HOH HOH B . 
M 5 HOH 184 484 620  HOH HOH B . 
M 5 HOH 185 485 413  HOH HOH B . 
M 5 HOH 186 486 400  HOH HOH B . 
M 5 HOH 187 487 671  HOH HOH B . 
M 5 HOH 188 488 263  HOH HOH B . 
M 5 HOH 189 489 499  HOH HOH B . 
M 5 HOH 190 490 669  HOH HOH B . 
M 5 HOH 191 491 385  HOH HOH B . 
M 5 HOH 192 492 646  HOH HOH B . 
M 5 HOH 193 493 159  HOH HOH B . 
M 5 HOH 194 494 549  HOH HOH B . 
M 5 HOH 195 495 647  HOH HOH B . 
M 5 HOH 196 496 381  HOH HOH B . 
M 5 HOH 197 497 513  HOH HOH B . 
M 5 HOH 198 498 579  HOH HOH B . 
M 5 HOH 199 499 114  HOH HOH B . 
M 5 HOH 200 500 348  HOH HOH B . 
M 5 HOH 201 501 249  HOH HOH B . 
M 5 HOH 202 502 236  HOH HOH B . 
M 5 HOH 203 503 419  HOH HOH B . 
M 5 HOH 204 504 495  HOH HOH B . 
M 5 HOH 205 505 424  HOH HOH B . 
M 5 HOH 206 506 147  HOH HOH B . 
M 5 HOH 207 507 616  HOH HOH B . 
M 5 HOH 208 508 633  HOH HOH B . 
M 5 HOH 209 509 205  HOH HOH B . 
M 5 HOH 210 510 290  HOH HOH B . 
M 5 HOH 211 511 364  HOH HOH B . 
M 5 HOH 212 512 498  HOH HOH B . 
M 5 HOH 213 513 627  HOH HOH B . 
M 5 HOH 214 514 626  HOH HOH B . 
M 5 HOH 215 515 350  HOH HOH B . 
M 5 HOH 216 516 243  HOH HOH B . 
M 5 HOH 217 517 255  HOH HOH B . 
M 5 HOH 218 518 387  HOH HOH B . 
M 5 HOH 219 519 329  HOH HOH B . 
M 5 HOH 220 520 670  HOH HOH B . 
M 5 HOH 221 521 138  HOH HOH B . 
M 5 HOH 222 522 232  HOH HOH B . 
M 5 HOH 223 523 680  HOH HOH B . 
M 5 HOH 224 524 280  HOH HOH B . 
M 5 HOH 225 525 528  HOH HOH B . 
M 5 HOH 226 526 532  HOH HOH B . 
M 5 HOH 227 527 284  HOH HOH B . 
M 5 HOH 228 528 431  HOH HOH B . 
M 5 HOH 229 529 604  HOH HOH B . 
M 5 HOH 230 530 432  HOH HOH B . 
M 5 HOH 231 531 525  HOH HOH B . 
M 5 HOH 232 532 475  HOH HOH B . 
M 5 HOH 233 533 168  HOH HOH B . 
M 5 HOH 234 534 558  HOH HOH B . 
M 5 HOH 235 535 492  HOH HOH B . 
M 5 HOH 236 536 220  HOH HOH B . 
M 5 HOH 237 537 556  HOH HOH B . 
M 5 HOH 238 538 230  HOH HOH B . 
M 5 HOH 239 539 299  HOH HOH B . 
M 5 HOH 240 540 621  HOH HOH B . 
M 5 HOH 241 541 545  HOH HOH B . 
M 5 HOH 242 542 644  HOH HOH B . 
M 5 HOH 243 543 233  HOH HOH B . 
M 5 HOH 244 544 678  HOH HOH B . 
M 5 HOH 245 545 546  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A MSE 1 ? CG ? A MSE 2 CG 
2 1 Y 1 A MSE 1 ? SE ? A MSE 2 SE 
3 1 Y 1 A MSE 1 ? CE ? A MSE 2 CE 
4 1 Y 1 B MSE 1 ? CG ? B MSE 2 CG 
5 1 Y 1 B MSE 1 ? SE ? B MSE 2 SE 
6 1 Y 1 B MSE 1 ? CE ? B MSE 2 CE 
# 
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   ? ? ? 1.17.1_3660 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CR5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     128.407 
_cell.length_a_esd                 ? 
_cell.length_b                     131.110 
_cell.length_b_esd                 ? 
_cell.length_c                     44.721 
_cell.length_c_esd                 ? 
_cell.volume                       752897.791 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9CR5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CR5 
_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             2.42 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.17 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_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 calcium chloride, 100 mM Tris pH 8.0, 20% PEG 6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      'Beryllium Lenses' 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 300 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-03-03 
_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                    'Diamond [111]' 
_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   0.978 
_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                        'APS BEAMLINE 21-ID-G' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-G 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          26.29 
_reflns.entry_id                                       9CR5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.56 
_reflns.d_resolution_low                               50 
_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                                     53569 
_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                                8.5 
_reflns.pdbx_netI_over_av_sigmaI                       12.55 
_reflns.pdbx_netI_over_sigmaI                          12.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.091 
_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                                0.122 
_reflns.pdbx_Rpim_I_all                                0.041 
_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                              0.114 
_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                                    1.57 
_reflns_shell.d_res_low                                     1.60 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.25 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2666 
_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                               7.2 
_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                               0.956 
_reflns_shell.pdbx_Rpim_I_all                               0.349 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.738 
_reflns_shell.pdbx_CC_star                                  0.922 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.20 
_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                                 9CR5 
_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                            1.56 
_refine.ls_d_res_low                             25.24 
_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                     53543 
_refine.ls_number_reflns_R_free                  2727 
_refine.ls_number_reflns_R_work                  50816 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.97 
_refine.ls_percent_reflns_R_free                 5.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1685 
_refine.ls_R_factor_R_free                       0.2015 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1668 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.0405 
_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                            0.1809 
_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                       1.56 
_refine_hist.d_res_low                        25.24 
_refine_hist.number_atoms_solvent             497 
_refine_hist.number_atoms_total               3315 
_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        2709 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         109 
_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' ? 0.0091  ? 3038 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0889  ? 4152 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0628  ? 435  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0069  ? 550  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 26.6569 ? 1140 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.56 1.59  . . 122 2191 81.79  . . . . 0.2452 . . . . . . . . . . . 0.2658 
'X-RAY DIFFRACTION' 1.59 1.62  . . 148 2655 99.86  . . . . 0.2314 . . . . . . . . . . . 0.2793 
'X-RAY DIFFRACTION' 1.62 1.65  . . 130 2676 99.89  . . . . 0.2187 . . . . . . . . . . . 0.2498 
'X-RAY DIFFRACTION' 1.65 1.69  . . 163 2630 99.96  . . . . 0.2083 . . . . . . . . . . . 0.2819 
'X-RAY DIFFRACTION' 1.69 1.73  . . 140 2712 100.00 . . . . 0.2042 . . . . . . . . . . . 0.2314 
'X-RAY DIFFRACTION' 1.73 1.77  . . 148 2613 99.89  . . . . 0.2049 . . . . . . . . . . . 0.2333 
'X-RAY DIFFRACTION' 1.77 1.82  . . 140 2697 100.00 . . . . 0.1923 . . . . . . . . . . . 0.2596 
'X-RAY DIFFRACTION' 1.82 1.87  . . 159 2672 99.96  . . . . 0.1883 . . . . . . . . . . . 0.2149 
'X-RAY DIFFRACTION' 1.87 1.93  . . 131 2699 99.96  . . . . 0.1865 . . . . . . . . . . . 0.2707 
'X-RAY DIFFRACTION' 1.93 2.00  . . 145 2681 99.96  . . . . 0.1876 . . . . . . . . . . . 0.2498 
'X-RAY DIFFRACTION' 2.00 2.08  . . 146 2680 100.00 . . . . 0.1843 . . . . . . . . . . . 0.2181 
'X-RAY DIFFRACTION' 2.08 2.18  . . 150 2680 100.00 . . . . 0.1770 . . . . . . . . . . . 0.2074 
'X-RAY DIFFRACTION' 2.18 2.29  . . 137 2711 100.00 . . . . 0.1668 . . . . . . . . . . . 0.2040 
'X-RAY DIFFRACTION' 2.29 2.44  . . 164 2678 100.00 . . . . 0.1701 . . . . . . . . . . . 0.2089 
'X-RAY DIFFRACTION' 2.44 2.62  . . 150 2735 99.90  . . . . 0.1706 . . . . . . . . . . . 0.1838 
'X-RAY DIFFRACTION' 2.62 2.89  . . 130 2694 99.96  . . . . 0.1708 . . . . . . . . . . . 0.1851 
'X-RAY DIFFRACTION' 2.89 3.30  . . 126 2777 99.90  . . . . 0.1666 . . . . . . . . . . . 0.1830 
'X-RAY DIFFRACTION' 3.30 4.16  . . 140 2765 99.76  . . . . 0.1439 . . . . . . . . . . . 0.2098 
'X-RAY DIFFRACTION' 4.16 25.24 . . 158 2870 99.51  . . . . 0.1514 . . . . . . . . . . . 0.1691 
# 
_struct.entry_id                     9CR5 
_struct.title                        'Crystal structure of GNAT superfamily acetyltransferase PA2271 from Pseudomonas aeruginosa' 
_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        9CR5 
_struct_keywords.text            
;GNAT, acetyltransferase, Structural Genomics, PSI-2, Protein Structure Initiative, Midwest Center for Structural Genomics, MCSG, TRANSFERASE
;
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
K N N 4 ? 
L N N 5 ? 
M N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ATSE1_PSEAE 
_struct_ref.pdbx_db_accession          Q9I1K2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MDYRIRTSRDEDAALLPAIERSAGESFRLLPELAWIADAGVAGVDFHRRLIERGSHWLAEDADGQPVGFLAAERCADELH
IAELSIAQAHQQQGLGRRLLERAVTYAHASHCRALTLTTFCDVPWNAPFYARLGFQRLTWQEAGERLRAILGHEQEIGFA
ADSRCAMRLVL
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CR5 A 2 ? 172 ? Q9I1K2 1 ? 171 ? 1 171 
2 1 9CR5 B 2 ? 172 ? Q9I1K2 1 ? 171 ? 1 171 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CR5 HIS A 1   ? UNP Q9I1K2 ? ? 'expression tag' 0   1 
1 9CR5 GLY A 173 ? UNP Q9I1K2 ? ? 'expression tag' 172 2 
1 9CR5 SER A 174 ? UNP Q9I1K2 ? ? 'expression tag' 173 3 
2 9CR5 HIS B 1   ? UNP Q9I1K2 ? ? 'expression tag' 0   4 
2 9CR5 GLY B 173 ? UNP Q9I1K2 ? ? 'expression tag' 172 5 
2 9CR5 SER B 174 ? UNP Q9I1K2 ? ? 'expression tag' 173 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,L 
2 1 B,H,I,J,K,M   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ARG A 10  ? ALA A 15  ? ARG A 9   ALA A 14  5 ? 6  
HELX_P HELX_P2  AA2 LEU A 16  ? GLY A 25  ? LEU A 15  GLY A 24  1 ? 10 
HELX_P HELX_P3  AA3 GLU A 26  ? ALA A 40  ? GLU A 25  ALA A 39  5 ? 15 
HELX_P HELX_P4  AA4 GLY A 44  ? GLY A 55  ? GLY A 43  GLY A 54  1 ? 12 
HELX_P HELX_P5  AA5 GLN A 89  ? GLN A 92  ? GLN A 88  GLN A 91  5 ? 4  
HELX_P HELX_P6  AA6 GLY A 95  ? SER A 111 ? GLY A 94  SER A 110 1 ? 17 
HELX_P HELX_P7  AA7 ASN A 127 ? LEU A 134 ? ASN A 126 LEU A 133 1 ? 8  
HELX_P HELX_P8  AA8 THR A 140 ? ILE A 158 ? THR A 139 ILE A 157 1 ? 19 
HELX_P HELX_P9  AA9 ALA A 161 ? ASP A 163 ? ALA A 160 ASP A 162 5 ? 3  
HELX_P HELX_P10 AB1 ARG B 10  ? ALA B 15  ? ARG B 9   ALA B 14  5 ? 6  
HELX_P HELX_P11 AB2 LEU B 16  ? GLU B 26  ? LEU B 15  GLU B 25  1 ? 11 
HELX_P HELX_P12 AB3 SER B 27  ? ARG B 29  ? SER B 26  ARG B 28  5 ? 3  
HELX_P HELX_P13 AB4 LEU B 31  ? ALA B 40  ? LEU B 30  ALA B 39  5 ? 10 
HELX_P HELX_P14 AB5 GLY B 44  ? GLY B 55  ? GLY B 43  GLY B 54  1 ? 12 
HELX_P HELX_P15 AB6 GLN B 89  ? GLN B 92  ? GLN B 88  GLN B 91  5 ? 4  
HELX_P HELX_P16 AB7 GLY B 95  ? SER B 111 ? GLY B 94  SER B 110 1 ? 17 
HELX_P HELX_P17 AB8 ASN B 127 ? LEU B 134 ? ASN B 126 LEU B 133 1 ? 8  
HELX_P HELX_P18 AB9 THR B 140 ? ILE B 158 ? THR B 139 ILE B 157 1 ? 19 
HELX_P HELX_P19 AC1 ALA B 161 ? ASP B 163 ? ALA B 160 ASP B 162 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? A MSE 2   C   ? ? ? 1_555 A ASP 3   N   ? ? A MSE 1   A ASP 2   1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale2  covale both ? A ALA 167 C   ? ? ? 1_555 A MSE 168 N   ? ? A ALA 166 A MSE 167 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale3  covale both ? A MSE 168 C   ? ? ? 1_555 A ARG 169 N   ? ? A MSE 167 A ARG 168 1_555 ? ? ? ? ? ? ? 1.343 ? ? 
covale4  covale both ? B MSE 2   C   ? ? ? 1_555 B ASP 3   N   ? ? B MSE 1   B ASP 2   1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale5  covale both ? B ALA 167 C   ? ? ? 1_555 B MSE 168 N   ? ? B ALA 166 B MSE 167 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale6  covale both ? B MSE 168 C   ? ? ? 1_555 B ARG 169 N   ? ? B MSE 167 B ARG 168 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
metalc1  metalc ?    ? A GLU 21  OE1 ? ? ? 1_555 E NA  .   NA  ? ? A GLU 20  A NA  203 1_555 ? ? ? ? ? ? ? 2.322 ? ? 
metalc2  metalc ?    ? A ASP 39  OD1 ? ? ? 1_555 F NA  .   NA  ? ? A ASP 38  A NA  204 1_555 ? ? ? ? ? ? ? 2.451 ? ? 
metalc3  metalc ?    ? A ASP 78  OD1 ? ? ? 1_555 D NA  .   NA  ? ? A ASP 77  A NA  202 1_555 ? ? ? ? ? ? ? 2.625 ? ? 
metalc4  metalc ?    ? A ASP 78  OD2 ? ? ? 1_555 D NA  .   NA  ? ? A ASP 77  A NA  202 1_555 ? ? ? ? ? ? ? 2.681 ? ? 
metalc5  metalc ?    ? A ASP 78  OD1 ? ? ? 1_555 D NA  .   NA  ? ? A ASP 77  A NA  202 3_454 ? ? ? ? ? ? ? 2.605 ? ? 
metalc6  metalc ?    ? A ASP 78  OD2 ? ? ? 1_555 D NA  .   NA  ? ? A ASP 77  A NA  202 3_454 ? ? ? ? ? ? ? 2.666 ? ? 
metalc7  metalc ?    ? A GLU 84  OE1 ? ? ? 1_555 E NA  .   NA  ? ? A GLU 83  A NA  203 1_555 ? ? ? ? ? ? ? 2.415 ? ? 
metalc8  metalc ?    ? A HIS 112 O   ? ? ? 1_555 D NA  .   NA  ? ? A HIS 111 A NA  202 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc9  metalc ?    ? A HIS 112 O   ? ? ? 1_555 D NA  .   NA  ? ? A HIS 111 A NA  202 3_454 ? ? ? ? ? ? ? 2.286 ? ? 
metalc10 metalc ?    ? E NA  .   NA  ? ? ? 1_555 L HOH .   O   ? ? A NA  203 A HOH 317 4_555 ? ? ? ? ? ? ? 2.502 ? ? 
metalc11 metalc ?    ? E NA  .   NA  ? ? ? 1_555 L HOH .   O   ? ? A NA  203 A HOH 422 1_555 ? ? ? ? ? ? ? 2.508 ? ? 
metalc12 metalc ?    ? E NA  .   NA  ? ? ? 1_555 L HOH .   O   ? ? A NA  203 A HOH 450 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc13 metalc ?    ? E NA  .   NA  ? ? ? 1_555 L HOH .   O   ? ? A NA  203 A HOH 476 1_555 ? ? ? ? ? ? ? 2.404 ? ? 
metalc14 metalc ?    ? F NA  .   NA  ? ? ? 1_555 L HOH .   O   ? ? A NA  204 A HOH 314 1_555 ? ? ? ? ? ? ? 2.465 ? ? 
metalc15 metalc ?    ? F NA  .   NA  ? ? ? 4_555 B SER 174 O   ? ? A NA  204 B SER 173 1_555 ? ? ? ? ? ? ? 2.460 ? ? 
metalc16 metalc ?    ? F NA  .   NA  ? ? ? 4_555 B SER 174 OXT ? ? A NA  204 B SER 173 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc17 metalc ?    ? F NA  .   NA  ? ? ? 1_555 M HOH .   O   ? ? A NA  204 B HOH 330 4_555 ? ? ? ? ? ? ? 2.350 ? ? 
metalc18 metalc ?    ? F NA  .   NA  ? ? ? 1_555 M HOH .   O   ? ? A NA  204 B HOH 449 4_555 ? ? ? ? ? ? ? 2.526 ? ? 
metalc19 metalc ?    ? F NA  .   NA  ? ? ? 1_555 M HOH .   O   ? ? A NA  204 B HOH 466 4_555 ? ? ? ? ? ? ? 2.503 ? ? 
metalc20 metalc ?    ? L HOH .   O   ? ? ? 6_455 J NA  .   NA  ? ? A HOH 472 B NA  203 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc21 metalc ?    ? B GLU 21  OE1 ? ? ? 1_555 I NA  .   NA  ? ? B GLU 20  B NA  202 1_555 ? ? ? ? ? ? ? 2.269 ? ? 
metalc22 metalc ?    ? B GLU 84  OE1 ? ? ? 1_555 I NA  .   NA  ? ? B GLU 83  B NA  202 1_555 ? ? ? ? ? ? ? 2.442 ? ? 
metalc23 metalc ?    ? B GLN 92  OE1 ? ? ? 1_555 J NA  .   NA  ? ? B GLN 91  B NA  203 1_555 ? ? ? ? ? ? ? 2.258 ? ? 
metalc24 metalc ?    ? I NA  .   NA  ? ? ? 1_555 M HOH .   O   ? ? B NA  202 B HOH 325 1_555 ? ? ? ? ? ? ? 2.358 ? ? 
metalc25 metalc ?    ? I NA  .   NA  ? ? ? 1_555 M HOH .   O   ? ? B NA  202 B HOH 333 3_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc26 metalc ?    ? I NA  .   NA  ? ? ? 1_555 M HOH .   O   ? ? B NA  202 B HOH 448 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc27 metalc ?    ? I NA  .   NA  ? ? ? 1_555 M HOH .   O   ? ? B NA  202 B HOH 480 1_555 ? ? ? ? ? ? ? 2.471 ? ? 
metalc28 metalc ?    ? J NA  .   NA  ? ? ? 1_555 M HOH .   O   ? ? B NA  203 B HOH 368 1_555 ? ? ? ? ? ? ? 2.395 ? ? 
metalc29 metalc ?    ? J NA  .   NA  ? ? ? 1_555 M HOH .   O   ? ? B NA  203 B HOH 407 1_555 ? ? ? ? ? ? ? 2.455 ? ? 
metalc30 metalc ?    ? J NA  .   NA  ? ? ? 1_555 M HOH .   O   ? ? B NA  203 B HOH 427 1_555 ? ? ? ? ? ? ? 2.385 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE1 ? A GLU 21  ? A GLU 20  ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 OE1 ? A GLU 84  ? A GLU 83  ? 1_555 96.5  ? 
2  OE1 ? A GLU 21  ? A GLU 20  ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 317 ? 4_555 92.8  ? 
3  OE1 ? A GLU 84  ? A GLU 83  ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 317 ? 4_555 87.5  ? 
4  OE1 ? A GLU 21  ? A GLU 20  ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 422 ? 1_555 88.0  ? 
5  OE1 ? A GLU 84  ? A GLU 83  ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 422 ? 1_555 167.4 ? 
6  O   ? L HOH .   ? A HOH 317 ? 4_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 422 ? 1_555 104.1 ? 
7  OE1 ? A GLU 21  ? A GLU 20  ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 450 ? 1_555 100.4 ? 
8  OE1 ? A GLU 84  ? A GLU 83  ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 450 ? 1_555 81.2  ? 
9  O   ? L HOH .   ? A HOH 317 ? 4_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 450 ? 1_555 163.5 ? 
10 O   ? L HOH .   ? A HOH 422 ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 450 ? 1_555 86.4  ? 
11 OE1 ? A GLU 21  ? A GLU 20  ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 476 ? 1_555 167.0 ? 
12 OE1 ? A GLU 84  ? A GLU 83  ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 476 ? 1_555 94.3  ? 
13 O   ? L HOH .   ? A HOH 317 ? 4_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 476 ? 1_555 80.5  ? 
14 O   ? L HOH .   ? A HOH 422 ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 476 ? 1_555 82.9  ? 
15 O   ? L HOH .   ? A HOH 450 ? 1_555 NA ? E NA . ? A NA 203 ? 1_555 O   ? L HOH .   ? A HOH 476 ? 1_555 88.3  ? 
16 OD1 ? A ASP 39  ? A ASP 38  ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? L HOH .   ? A HOH 314 ? 1_555 84.9  ? 
17 OD1 ? A ASP 39  ? A ASP 38  ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? B SER 174 ? B SER 173 ? 1_555 48.1  ? 
18 O   ? L HOH .   ? A HOH 314 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? B SER 174 ? B SER 173 ? 1_555 123.4 ? 
19 OD1 ? A ASP 39  ? A ASP 38  ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 OXT ? B SER 174 ? B SER 173 ? 1_555 58.1  ? 
20 O   ? L HOH .   ? A HOH 314 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 OXT ? B SER 174 ? B SER 173 ? 1_555 133.2 ? 
21 O   ? B SER 174 ? B SER 173 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 OXT ? B SER 174 ? B SER 173 ? 1_555 10.7  ? 
22 OD1 ? A ASP 39  ? A ASP 38  ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 330 ? 4_555 164.7 ? 
23 O   ? L HOH .   ? A HOH 314 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 330 ? 4_555 81.5  ? 
24 O   ? B SER 174 ? B SER 173 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 330 ? 4_555 137.6 ? 
25 OXT ? B SER 174 ? B SER 173 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 330 ? 4_555 129.2 ? 
26 OD1 ? A ASP 39  ? A ASP 38  ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 449 ? 4_555 91.8  ? 
27 O   ? L HOH .   ? A HOH 314 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 449 ? 4_555 77.4  ? 
28 O   ? B SER 174 ? B SER 173 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 449 ? 4_555 124.6 ? 
29 OXT ? B SER 174 ? B SER 173 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 449 ? 4_555 126.5 ? 
30 O   ? M HOH .   ? B HOH 330 ? 4_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 449 ? 4_555 91.9  ? 
31 OD1 ? A ASP 39  ? A ASP 38  ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 466 ? 4_555 90.6  ? 
32 O   ? L HOH .   ? A HOH 314 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 466 ? 4_555 120.1 ? 
33 O   ? B SER 174 ? B SER 173 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 466 ? 4_555 48.3  ? 
34 OXT ? B SER 174 ? B SER 173 ? 1_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 466 ? 4_555 43.0  ? 
35 O   ? M HOH .   ? B HOH 330 ? 4_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 466 ? 4_555 90.3  ? 
36 O   ? M HOH .   ? B HOH 449 ? 4_555 NA ? F NA . ? A NA 204 ? 1_555 O   ? M HOH .   ? B HOH 466 ? 4_555 162.5 ? 
37 OD1 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 OD2 ? A ASP 78  ? A ASP 77  ? 1_555 48.2  ? 
38 OD1 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 OD1 ? A ASP 78  ? A ASP 77  ? 1_555 0.0   ? 
39 OD2 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 OD1 ? A ASP 78  ? A ASP 77  ? 1_555 48.2  ? 
40 OD1 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 OD2 ? A ASP 78  ? A ASP 77  ? 1_555 48.2  ? 
41 OD2 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 OD2 ? A ASP 78  ? A ASP 77  ? 1_555 0.0   ? 
42 OD1 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 OD2 ? A ASP 78  ? A ASP 77  ? 1_555 48.2  ? 
43 OD1 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 O   ? A HIS 112 ? A HIS 111 ? 1_555 75.6  ? 
44 OD2 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 O   ? A HIS 112 ? A HIS 111 ? 1_555 107.7 ? 
45 OD1 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 O   ? A HIS 112 ? A HIS 111 ? 1_555 75.6  ? 
46 OD2 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 O   ? A HIS 112 ? A HIS 111 ? 1_555 107.7 ? 
47 OD1 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 O   ? A HIS 112 ? A HIS 111 ? 1_555 75.6  ? 
48 OD2 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 O   ? A HIS 112 ? A HIS 111 ? 1_555 107.7 ? 
49 OD1 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 O   ? A HIS 112 ? A HIS 111 ? 1_555 75.6  ? 
50 OD2 ? A ASP 78  ? A ASP 77  ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 O   ? A HIS 112 ? A HIS 111 ? 1_555 107.7 ? 
51 O   ? A HIS 112 ? A HIS 111 ? 1_555 NA ? D NA . ? A NA 202 ? 1_555 O   ? A HIS 112 ? A HIS 111 ? 1_555 0.0   ? 
52 O   ? L HOH .   ? A HOH 472 ? 6_455 NA ? J NA . ? B NA 203 ? 1_555 OE1 ? B GLN 92  ? B GLN 91  ? 1_555 164.6 ? 
53 O   ? L HOH .   ? A HOH 472 ? 6_455 NA ? J NA . ? B NA 203 ? 1_555 O   ? M HOH .   ? B HOH 368 ? 1_555 87.3  ? 
54 OE1 ? B GLN 92  ? B GLN 91  ? 1_555 NA ? J NA . ? B NA 203 ? 1_555 O   ? M HOH .   ? B HOH 368 ? 1_555 77.4  ? 
55 O   ? L HOH .   ? A HOH 472 ? 6_455 NA ? J NA . ? B NA 203 ? 1_555 O   ? M HOH .   ? B HOH 407 ? 1_555 95.2  ? 
56 OE1 ? B GLN 92  ? B GLN 91  ? 1_555 NA ? J NA . ? B NA 203 ? 1_555 O   ? M HOH .   ? B HOH 407 ? 1_555 77.5  ? 
57 O   ? M HOH .   ? B HOH 368 ? 1_555 NA ? J NA . ? B NA 203 ? 1_555 O   ? M HOH .   ? B HOH 407 ? 1_555 66.2  ? 
58 O   ? L HOH .   ? A HOH 472 ? 6_455 NA ? J NA . ? B NA 203 ? 1_555 O   ? M HOH .   ? B HOH 427 ? 1_555 89.1  ? 
59 OE1 ? B GLN 92  ? B GLN 91  ? 1_555 NA ? J NA . ? B NA 203 ? 1_555 O   ? M HOH .   ? B HOH 427 ? 1_555 101.0 ? 
60 O   ? M HOH .   ? B HOH 368 ? 1_555 NA ? J NA . ? B NA 203 ? 1_555 O   ? M HOH .   ? B HOH 427 ? 1_555 126.4 ? 
61 O   ? M HOH .   ? B HOH 407 ? 1_555 NA ? J NA . ? B NA 203 ? 1_555 O   ? M HOH .   ? B HOH 427 ? 1_555 166.9 ? 
62 OE1 ? B GLU 21  ? B GLU 20  ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 OE1 ? B GLU 84  ? B GLU 83  ? 1_555 91.8  ? 
63 OE1 ? B GLU 21  ? B GLU 20  ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 325 ? 1_555 93.0  ? 
64 OE1 ? B GLU 84  ? B GLU 83  ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 325 ? 1_555 167.7 ? 
65 OE1 ? B GLU 21  ? B GLU 20  ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 333 ? 3_555 90.9  ? 
66 OE1 ? B GLU 84  ? B GLU 83  ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 333 ? 3_555 88.9  ? 
67 O   ? M HOH .   ? B HOH 325 ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 333 ? 3_555 102.3 ? 
68 OE1 ? B GLU 21  ? B GLU 20  ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 448 ? 1_555 99.1  ? 
69 OE1 ? B GLU 84  ? B GLU 83  ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 448 ? 1_555 81.6  ? 
70 O   ? M HOH .   ? B HOH 325 ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 448 ? 1_555 86.4  ? 
71 O   ? M HOH .   ? B HOH 333 ? 3_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 448 ? 1_555 166.4 ? 
72 OE1 ? B GLU 21  ? B GLU 20  ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 480 ? 1_555 170.2 ? 
73 OE1 ? B GLU 84  ? B GLU 83  ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 480 ? 1_555 93.2  ? 
74 O   ? M HOH .   ? B HOH 325 ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 480 ? 1_555 83.8  ? 
75 O   ? M HOH .   ? B HOH 333 ? 3_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 480 ? 1_555 80.8  ? 
76 O   ? M HOH .   ? B HOH 448 ? 1_555 NA ? I NA . ? B NA 202 ? 1_555 O   ? M HOH .   ? B HOH 480 ? 1_555 89.9  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 MSE A 2   ? . . . . MSE A 1   ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
2 MSE A 168 ? . . . . MSE A 167 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
3 MSE B 2   ? . . . . MSE B 1   ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
4 MSE B 168 ? . . . . MSE B 167 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 5   ? THR A 8   ? ARG A 4   THR A 7   
AA1 2 HIS A 57  ? GLU A 61  ? HIS A 56  GLU A 60  
AA1 3 PRO A 67  ? CYS A 76  ? PRO A 66  CYS A 75  
AA1 4 GLU A 79  ? ILE A 87  ? GLU A 78  ILE A 86  
AA1 5 ALA A 115 ? PHE A 121 ? ALA A 114 PHE A 120 
AA1 6 ARG A 165 ? VAL A 171 ? ARG A 164 VAL A 170 
AA1 7 GLN A 137 ? ARG A 138 ? GLN A 136 ARG A 137 
AA2 1 ARG B 5   ? THR B 8   ? ARG B 4   THR B 7   
AA2 2 HIS B 57  ? GLU B 61  ? HIS B 56  GLU B 60  
AA2 3 PRO B 67  ? CYS B 76  ? PRO B 66  CYS B 75  
AA2 4 GLU B 79  ? ILE B 87  ? GLU B 78  ILE B 86  
AA2 5 ALA B 115 ? PHE B 121 ? ALA B 114 PHE B 120 
AA2 6 ARG B 165 ? VAL B 171 ? ARG B 164 VAL B 170 
AA2 7 GLN B 137 ? ARG B 138 ? GLN B 136 ARG B 137 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 7   ? N ARG A 6   O LEU A 59  ? O LEU A 58  
AA1 2 3 N ALA A 60  ? N ALA A 59  O VAL A 68  ? O VAL A 67  
AA1 3 4 N GLU A 74  ? N GLU A 73  O HIS A 81  ? O HIS A 80  
AA1 4 5 N ILE A 82  ? N ILE A 81  O THR A 117 ? O THR A 116 
AA1 5 6 N LEU A 118 ? N LEU A 117 O MSE A 168 ? O MSE A 167 
AA1 6 7 O ARG A 169 ? O ARG A 168 N GLN A 137 ? N GLN A 136 
AA2 1 2 N ARG B 7   ? N ARG B 6   O LEU B 59  ? O LEU B 58  
AA2 2 3 N ALA B 60  ? N ALA B 59  O VAL B 68  ? O VAL B 67  
AA2 3 4 N CYS B 76  ? N CYS B 75  O GLU B 79  ? O GLU B 78  
AA2 4 5 N ILE B 82  ? N ILE B 81  O THR B 117 ? O THR B 116 
AA2 5 6 N LEU B 116 ? N LEU B 115 O LEU B 170 ? O LEU B 169 
AA2 6 7 O ARG B 169 ? O ARG B 168 N GLN B 137 ? N GLN B 136 
# 
_pdbx_entry_details.entry_id                   9CR5 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 55  ? ? -102.13 57.84   
2 1 ALA A 76  ? ? 54.92   -124.46 
3 1 ASN A 126 ? ? -111.54 -110.02 
4 1 SER B 55  ? ? -101.51 54.35   
5 1 ALA B 76  ? ? 52.69   -120.34 
6 1 ASN B 126 ? ? -112.87 -115.76 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'PSI, Protein Structure Initiative' 
_pdbx_SG_project.full_name_of_center   'Midwest Center for Structural Genomics' 
_pdbx_SG_project.initial_of_center     MCSG 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A MSE 2   A MSE 1   ? MET 'modified residue' 
2 A MSE 168 A MSE 167 ? MET 'modified residue' 
3 B MSE 2   B MSE 1   ? MET 'modified residue' 
4 B MSE 168 B MSE 167 ? MET 'modified residue' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A NA  202 ? D NA  . 
2 1 A HOH 459 ? L HOH . 
3 1 B HOH 485 ? M HOH . 
4 1 B HOH 505 ? M HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -38.4292950302 20.2205912906 -20.1937106294  0.484078661558 ? -0.052762605364   ? 0.0363531556601 
? 0.321757923618 ? 0.0478018162207  ? 0.206314989445 ? 5.98954072882 ? -5.34892091686   ? 2.31022880936   ? 5.39067296139 ? 
-1.01393335017   ? 6.57867957504 ? -0.377978381172  ? 0.570153548474   ? 0.684587203498    ? -1.67444154189  ? 0.210544947881    ? 
-0.343283472458 ? -0.956184300581  ? 0.561374001453   ? 0.11909120668    ? 
2  'X-RAY DIFFRACTION' ? refined -32.9301545201 8.86724088361 -9.5085058677   0.168150298691 ? 0.0189814665994   ? 0.0212529191197 
? 0.158011536388 ? 0.030248862657   ? 0.150162962324 ? 7.19739511014 ? 1.88501742185    ? 4.77892578035   ? 4.38460495696 ? 
2.24408000017    ? 3.41655817487 ? 0.159918224269   ? 0.246341958921   ? -0.142151416015   ? -0.285292991561 ? 0.0952186348287   ? 
-0.145878851728 ? 0.066380915844   ? 0.262275940998   ? -0.216791838309  ? 
3  'X-RAY DIFFRACTION' ? refined -33.2543639912 6.04440134694 2.44752376207   0.238289135082 ? -0.0839860834562  ? 
-0.0302540940913  ? 0.328253012921 ? 0.0552746316881  ? 0.152596672272 ? 2.89728266446 ? -0.636599707625  ? 2.58122911339   ? 
3.84854738513 ? -2.33484110102   ? 3.07277042483 ? 0.450367030032   ? -0.545238524405  ? -0.230919189315   ? 0.384596084901  ? 
-0.204022392411   ? -0.272353783879 ? 0.794568950476   ? -0.447591798976  ? -0.126412265598  ? 
4  'X-RAY DIFFRACTION' ? refined -46.5141096271 3.95016878921 -16.8956782212  0.410219508287 ? -0.00758859762152 ? 
-0.0715153753305  ? 0.267317230444 ? -0.0275943384968 ? 0.291978597981 ? 3.14860756434 ? -1.26586157261   ? -2.90985033172  ? 
4.6162731957  ? -0.0634530649533 ? 3.08791971606 ? -0.250819886192  ? 0.289164119418   ? -0.617050071235   ? -0.599552977451 ? 
-0.112165047344   ? 0.805125196894  ? 0.551811008711   ? -0.606679286178  ? 0.404889115507   ? 
5  'X-RAY DIFFRACTION' ? refined -38.0295995978 16.7196841238 -18.8512034736  0.437009665838 ? 0.0082509106562   ? 
-0.0102063974763  ? 0.291560292329 ? 0.0567565976033  ? 0.153516479123 ? 8.57935147491 ? 3.42256832799    ? 0.0254879816009 ? 
8.3887819149  ? -0.299567997889  ? 4.31621672359 ? -0.136523914901  ? 0.725017304919   ? 0.172948521078    ? -1.19771478992  ? 
0.0976827386387   ? -0.276202295522 ? -0.0969646545036 ? 0.383681379199   ? 0.0498452126875  ? 
6  'X-RAY DIFFRACTION' ? refined -44.6018198213 17.5702356635 -10.0255798904  0.189967705648 ? 0.00132486779863  ? 
-0.0422076428916  ? 0.164894042041 ? 0.0108418393818  ? 0.136169519637 ? 9.04158189853 ? 0.212103565662   ? 1.1029935512    ? 
3.60892108628 ? 0.0489986642408  ? 1.07760117865 ? -0.0717262599298 ? 0.00272869105813 ? 0.319395882798    ? -0.204912011709 ? 
-0.00817628594064 ? 0.319060246854  ? -0.0907081034006 ? -0.0390266033163 ? 0.082359103085   ? 
7  'X-RAY DIFFRACTION' ? refined -48.0738169556 15.8779925635 -0.655044897089 0.133478158184 ? 0.0118023134485   ? 
0.00788191007529  ? 0.16402434295  ? 0.00883592008303 ? 0.213545517873 ? 8.97269920066 ? -1.62452179253   ? 5.91232064345   ? 
3.21522184281 ? -1.31906562683   ? 6.38739723802 ? -0.0664522381225 ? -0.181231568045  ? 0.255182783033    ? 0.0583033040398 ? 
-0.0244126836323  ? 0.449594903107  ? -0.090720161909  ? -0.23194336204   ? 0.126805058379   ? 
8  'X-RAY DIFFRACTION' ? refined -48.595164752  20.5154066907 3.32409763605   0.276962733465 ? 0.0443329662283   ? 0.0481492808212 
? 0.211777096498 ? 0.00290926838759 ? 0.28181936461  ? 6.36999646436 ? 5.41950027716    ? -2.06474522118  ? 8.87431764372 ? 
-3.0639770268    ? 6.54821045955 ? -0.0889280507578 ? -0.0442269925774 ? 0.424628671596    ? 0.809825263793  ? 0.206022591315    ? 
0.722439096386  ? -0.0881036843533 ? 0.0314930869142  ? -0.133644605078  ? 
9  'X-RAY DIFFRACTION' ? refined -51.050653015  8.60939546755 4.38483653491   0.244952761531 ? 0.00501460727073  ? 0.0739326204988 
? 0.246130218228 ? 0.0262734813351  ? 0.274682873807 ? 3.35769549514 ? -1.57581862984   ? 0.704122984616  ? 6.60723514433 ? 
-0.906340048484  ? 2.20667847334 ? -0.12772539878   ? -0.149724881028  ? -0.136013247731   ? 0.598022124575  ? 0.174491240206    ? 
0.741761510243  ? -0.0106723707768 ? -0.201901686059  ? -0.0508922294499 ? 
10 'X-RAY DIFFRACTION' ? refined -14.3517151906 28.4447698165 -3.6609268995   0.225425416017 ? 8.75925892789e-05 ? 
0.000451708284809 ? 0.217613577799 ? 0.0521585632095  ? 0.180125823097 ? 4.30357406656 ? 0.493729559043   ? 0.894799370914  ? 
5.48832962991 ? 3.17910821114    ? 8.09666160929 ? 0.00848382892709 ? 0.468268277836   ? 0.156663420391    ? -0.493879907415 ? 
0.144721292669    ? 0.0872708466381 ? -0.0981357922433 ? 0.0990558241909  ? -0.186056150223  ? 
11 'X-RAY DIFFRACTION' ? refined -9.70168148403 34.1542101851 16.5574626797   0.261200507598 ? -0.00923811317861 ? 
-0.0187037744478  ? 0.237461003959 ? -0.0322164728601 ? 0.316105111147 ? 4.89076197528 ? -5.30042221029   ? -5.89367963353  ? 
5.77761956543 ? 6.47315451061    ? 7.28628419837 ? 0.0765753001013  ? -0.095638512622  ? 0.717932413625    ? 0.340850649795  ? 
0.148296074625    ? -0.703373289249 ? 0.192535361409   ? 0.186926166687   ? -0.249738859363  ? 
12 'X-RAY DIFFRACTION' ? refined -9.4660607933  22.8879854648 -5.36705859619  0.29719573429  ? -0.0285352312985  ? 0.0310475479482 
? 0.27388908172  ? 0.0175204728967  ? 0.140600916828 ? 5.71840742095 ? 1.06671729204    ? 1.51976431687   ? 3.63841505919 ? 
-0.320600021759  ? 5.97888259308 ? -0.286111279327  ? 0.781580959294   ? 0.0535614731123   ? -0.470581036679 ? 0.219286388672    ? 
-0.187432056209 ? 0.0169590045718  ? 0.374613344165   ? 0.0512142129539  ? 
13 'X-RAY DIFFRACTION' ? refined -17.7195552947 19.5346126027 1.38332033298   0.214181752186 ? 0.00159234185097  ? 0.0208031503012 
? 0.218415379556 ? -0.0125118577871 ? 0.167509432477 ? 3.29521854187 ? 0.00171586522071 ? 0.878390881158  ? 2.78863281742 ? 
-0.611944158777  ? 1.68656483946 ? 0.0394955469597  ? 0.0707356832248  ? -0.00730155365859 ? 0.16646540537   ? 0.0616494996857   ? 
0.104180896889  ? -0.0389741387129 ? -0.0501911710927 ? -0.0717150655675 ? 
14 'X-RAY DIFFRACTION' ? refined -15.5919290902 16.3504631724 10.7795189583   0.184518233986 ? -0.0168617029283  ? 
-0.0054933346596  ? 0.206809429475 ? 0.0287905894876  ? 0.192455833467 ? 3.93989197279 ? 1.54175358804    ? 2.39894866976   ? 
8.83091298831 ? 5.6349150536     ? 5.96137124582 ? 0.067131943252   ? -0.260881909597  ? 0.108173373893    ? 0.300967986603  ? 
-0.0063159661641  ? 0.09664172424   ? 0.162376727239   ? -0.0934286911197 ? -0.0200209410937 ? 
15 'X-RAY DIFFRACTION' ? refined -20.1494177616 15.4257929831 14.8158078357   0.26373653171  ? -0.0534012346251  ? 0.0197320539677 
? 0.35884812703  ? -0.0094245027187 ? 0.174169283668 ? 7.72996643183 ? -4.43999618837   ? 5.17817039302   ? 6.47444588745 ? 
-3.14776441848   ? 3.50764179946 ? 0.140852773306   ? -0.982637493856  ? 0.0195082602888   ? 0.427215289778  ? 0.0196949482635   ? 
0.110075366867  ? 0.188022881419   ? -0.415917402445  ? -0.136579167513  ? 
16 'X-RAY DIFFRACTION' ? refined -8.05950152947 13.763136127  15.7458766304   0.306202341358 ? 0.0164415395561   ? 
-0.0563072384076  ? 0.268914668784 ? 0.0184496339209  ? 0.190334368178 ? 8.21455790391 ? 3.44858940782    ? 2.16397505022   ? 
3.48094277611 ? 1.29979704468    ? 2.31185609028 ? 0.39618087811    ? -0.428017388403  ? -0.170491634796   ? 0.398571681496  ? 
-0.205081103359   ? -0.026441102336 ? 0.49960884332    ? -0.0700278860891 ? -0.213749763225  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid    1  through    9 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid   10  through   29 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid   30  through   43 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid   44  through   53 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid   54  through   65 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid   66  through  109 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid  110  through  126 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid  127  through  139 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid  140  through  172 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid    1  through   27 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid   28  through   38 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid   39  through   65 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid   66  through  109 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid  110  through  126 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid  127  through  139 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid  140  through  173 )
;
# 
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 552 ? 5.82 . 
2 1 O ? B HOH 544 ? 6.07 . 
3 1 O ? B HOH 545 ? 6.87 . 
# 
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 HIS 0   ? A HIS 1   
2 1 Y 1 A SER 173 ? A SER 174 
3 1 Y 1 B HIS 0   ? B HIS 1   
# 
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 
ACO N1A  N  Y N 1   
ACO C2A  C  Y N 2   
ACO N3A  N  Y N 3   
ACO C4A  C  Y N 4   
ACO C5A  C  Y N 5   
ACO C6A  C  Y N 6   
ACO N6A  N  N N 7   
ACO N7A  N  Y N 8   
ACO C8A  C  Y N 9   
ACO N9A  N  Y N 10  
ACO C1B  C  N R 11  
ACO C2B  C  N R 12  
ACO O2B  O  N N 13  
ACO C3B  C  N S 14  
ACO O3B  O  N N 15  
ACO P3B  P  N N 16  
ACO O7A  O  N N 17  
ACO O8A  O  N N 18  
ACO O9A  O  N N 19  
ACO C4B  C  N R 20  
ACO O4B  O  N N 21  
ACO C5B  C  N N 22  
ACO O5B  O  N N 23  
ACO P1A  P  N S 24  
ACO O1A  O  N N 25  
ACO O2A  O  N N 26  
ACO O3A  O  N N 27  
ACO P2A  P  N S 28  
ACO O4A  O  N N 29  
ACO O5A  O  N N 30  
ACO O6A  O  N N 31  
ACO CBP  C  N N 32  
ACO CCP  C  N N 33  
ACO CDP  C  N N 34  
ACO CEP  C  N N 35  
ACO CAP  C  N R 36  
ACO OAP  O  N N 37  
ACO C9P  C  N N 38  
ACO O9P  O  N N 39  
ACO N8P  N  N N 40  
ACO C7P  C  N N 41  
ACO C6P  C  N N 42  
ACO C5P  C  N N 43  
ACO O5P  O  N N 44  
ACO N4P  N  N N 45  
ACO C3P  C  N N 46  
ACO C2P  C  N N 47  
ACO S1P  S  N N 48  
ACO C    C  N N 49  
ACO O    O  N N 50  
ACO CH3  C  N N 51  
ACO H2A  H  N N 52  
ACO H61A H  N N 53  
ACO H62A H  N N 54  
ACO H8A  H  N N 55  
ACO H1B  H  N N 56  
ACO H2B  H  N N 57  
ACO HO2A H  N N 58  
ACO H3B  H  N N 59  
ACO HOA8 H  N N 60  
ACO HOA9 H  N N 61  
ACO H4B  H  N N 62  
ACO H51A H  N N 63  
ACO H52A H  N N 64  
ACO HOA2 H  N N 65  
ACO HOA5 H  N N 66  
ACO H121 H  N N 67  
ACO H122 H  N N 68  
ACO H131 H  N N 69  
ACO H132 H  N N 70  
ACO H133 H  N N 71  
ACO H141 H  N N 72  
ACO H142 H  N N 73  
ACO H143 H  N N 74  
ACO H10  H  N N 75  
ACO HO1  H  N N 76  
ACO HN8  H  N N 77  
ACO H71  H  N N 78  
ACO H72  H  N N 79  
ACO H61  H  N N 80  
ACO H62  H  N N 81  
ACO HN4  H  N N 82  
ACO H31  H  N N 83  
ACO H32  H  N N 84  
ACO H21  H  N N 85  
ACO H22  H  N N 86  
ACO HH31 H  N N 87  
ACO HH32 H  N N 88  
ACO HH33 H  N N 89  
ALA N    N  N N 90  
ALA CA   C  N S 91  
ALA C    C  N N 92  
ALA O    O  N N 93  
ALA CB   C  N N 94  
ALA OXT  O  N N 95  
ALA H    H  N N 96  
ALA H2   H  N N 97  
ALA HA   H  N N 98  
ALA HB1  H  N N 99  
ALA HB2  H  N N 100 
ALA HB3  H  N N 101 
ALA HXT  H  N N 102 
ARG N    N  N N 103 
ARG CA   C  N S 104 
ARG C    C  N N 105 
ARG O    O  N N 106 
ARG CB   C  N N 107 
ARG CG   C  N N 108 
ARG CD   C  N N 109 
ARG NE   N  N N 110 
ARG CZ   C  N N 111 
ARG NH1  N  N N 112 
ARG NH2  N  N N 113 
ARG OXT  O  N N 114 
ARG H    H  N N 115 
ARG H2   H  N N 116 
ARG HA   H  N N 117 
ARG HB2  H  N N 118 
ARG HB3  H  N N 119 
ARG HG2  H  N N 120 
ARG HG3  H  N N 121 
ARG HD2  H  N N 122 
ARG HD3  H  N N 123 
ARG HE   H  N N 124 
ARG HH11 H  N N 125 
ARG HH12 H  N N 126 
ARG HH21 H  N N 127 
ARG HH22 H  N N 128 
ARG HXT  H  N N 129 
ASN N    N  N N 130 
ASN CA   C  N S 131 
ASN C    C  N N 132 
ASN O    O  N N 133 
ASN CB   C  N N 134 
ASN CG   C  N N 135 
ASN OD1  O  N N 136 
ASN ND2  N  N N 137 
ASN OXT  O  N N 138 
ASN H    H  N N 139 
ASN H2   H  N N 140 
ASN HA   H  N N 141 
ASN HB2  H  N N 142 
ASN HB3  H  N N 143 
ASN HD21 H  N N 144 
ASN HD22 H  N N 145 
ASN HXT  H  N N 146 
ASP N    N  N N 147 
ASP CA   C  N S 148 
ASP C    C  N N 149 
ASP O    O  N N 150 
ASP CB   C  N N 151 
ASP CG   C  N N 152 
ASP OD1  O  N N 153 
ASP OD2  O  N N 154 
ASP OXT  O  N N 155 
ASP H    H  N N 156 
ASP H2   H  N N 157 
ASP HA   H  N N 158 
ASP HB2  H  N N 159 
ASP HB3  H  N N 160 
ASP HD2  H  N N 161 
ASP HXT  H  N N 162 
CL  CL   CL N N 163 
CYS N    N  N N 164 
CYS CA   C  N R 165 
CYS C    C  N N 166 
CYS O    O  N N 167 
CYS CB   C  N N 168 
CYS SG   S  N N 169 
CYS OXT  O  N N 170 
CYS H    H  N N 171 
CYS H2   H  N N 172 
CYS HA   H  N N 173 
CYS HB2  H  N N 174 
CYS HB3  H  N N 175 
CYS HG   H  N N 176 
CYS HXT  H  N N 177 
GLN N    N  N N 178 
GLN CA   C  N S 179 
GLN C    C  N N 180 
GLN O    O  N N 181 
GLN CB   C  N N 182 
GLN CG   C  N N 183 
GLN CD   C  N N 184 
GLN OE1  O  N N 185 
GLN NE2  N  N N 186 
GLN OXT  O  N N 187 
GLN H    H  N N 188 
GLN H2   H  N N 189 
GLN HA   H  N N 190 
GLN HB2  H  N N 191 
GLN HB3  H  N N 192 
GLN HG2  H  N N 193 
GLN HG3  H  N N 194 
GLN HE21 H  N N 195 
GLN HE22 H  N N 196 
GLN HXT  H  N N 197 
GLU N    N  N N 198 
GLU CA   C  N S 199 
GLU C    C  N N 200 
GLU O    O  N N 201 
GLU CB   C  N N 202 
GLU CG   C  N N 203 
GLU CD   C  N N 204 
GLU OE1  O  N N 205 
GLU OE2  O  N N 206 
GLU OXT  O  N N 207 
GLU H    H  N N 208 
GLU H2   H  N N 209 
GLU HA   H  N N 210 
GLU HB2  H  N N 211 
GLU HB3  H  N N 212 
GLU HG2  H  N N 213 
GLU HG3  H  N N 214 
GLU HE2  H  N N 215 
GLU HXT  H  N N 216 
GLY N    N  N N 217 
GLY CA   C  N N 218 
GLY C    C  N N 219 
GLY O    O  N N 220 
GLY OXT  O  N N 221 
GLY H    H  N N 222 
GLY H2   H  N N 223 
GLY HA2  H  N N 224 
GLY HA3  H  N N 225 
GLY HXT  H  N N 226 
HIS N    N  N N 227 
HIS CA   C  N S 228 
HIS C    C  N N 229 
HIS O    O  N N 230 
HIS CB   C  N N 231 
HIS CG   C  Y N 232 
HIS ND1  N  Y N 233 
HIS CD2  C  Y N 234 
HIS CE1  C  Y N 235 
HIS NE2  N  Y N 236 
HIS OXT  O  N N 237 
HIS H    H  N N 238 
HIS H2   H  N N 239 
HIS HA   H  N N 240 
HIS HB2  H  N N 241 
HIS HB3  H  N N 242 
HIS HD1  H  N N 243 
HIS HD2  H  N N 244 
HIS HE1  H  N N 245 
HIS HE2  H  N N 246 
HIS HXT  H  N N 247 
HOH O    O  N N 248 
HOH H1   H  N N 249 
HOH H2   H  N N 250 
ILE N    N  N N 251 
ILE CA   C  N S 252 
ILE C    C  N N 253 
ILE O    O  N N 254 
ILE CB   C  N S 255 
ILE CG1  C  N N 256 
ILE CG2  C  N N 257 
ILE CD1  C  N N 258 
ILE OXT  O  N N 259 
ILE H    H  N N 260 
ILE H2   H  N N 261 
ILE HA   H  N N 262 
ILE HB   H  N N 263 
ILE HG12 H  N N 264 
ILE HG13 H  N N 265 
ILE HG21 H  N N 266 
ILE HG22 H  N N 267 
ILE HG23 H  N N 268 
ILE HD11 H  N N 269 
ILE HD12 H  N N 270 
ILE HD13 H  N N 271 
ILE HXT  H  N N 272 
LEU N    N  N N 273 
LEU CA   C  N S 274 
LEU C    C  N N 275 
LEU O    O  N N 276 
LEU CB   C  N N 277 
LEU CG   C  N N 278 
LEU CD1  C  N N 279 
LEU CD2  C  N N 280 
LEU OXT  O  N N 281 
LEU H    H  N N 282 
LEU H2   H  N N 283 
LEU HA   H  N N 284 
LEU HB2  H  N N 285 
LEU HB3  H  N N 286 
LEU HG   H  N N 287 
LEU HD11 H  N N 288 
LEU HD12 H  N N 289 
LEU HD13 H  N N 290 
LEU HD21 H  N N 291 
LEU HD22 H  N N 292 
LEU HD23 H  N N 293 
LEU HXT  H  N N 294 
MSE N    N  N N 295 
MSE CA   C  N S 296 
MSE C    C  N N 297 
MSE O    O  N N 298 
MSE OXT  O  N N 299 
MSE CB   C  N N 300 
MSE CG   C  N N 301 
MSE SE   SE N N 302 
MSE CE   C  N N 303 
MSE H    H  N N 304 
MSE H2   H  N N 305 
MSE HA   H  N N 306 
MSE HXT  H  N N 307 
MSE HB2  H  N N 308 
MSE HB3  H  N N 309 
MSE HG2  H  N N 310 
MSE HG3  H  N N 311 
MSE HE1  H  N N 312 
MSE HE2  H  N N 313 
MSE HE3  H  N N 314 
NA  NA   NA N N 315 
PHE N    N  N N 316 
PHE CA   C  N S 317 
PHE C    C  N N 318 
PHE O    O  N N 319 
PHE CB   C  N N 320 
PHE CG   C  Y N 321 
PHE CD1  C  Y N 322 
PHE CD2  C  Y N 323 
PHE CE1  C  Y N 324 
PHE CE2  C  Y N 325 
PHE CZ   C  Y N 326 
PHE OXT  O  N N 327 
PHE H    H  N N 328 
PHE H2   H  N N 329 
PHE HA   H  N N 330 
PHE HB2  H  N N 331 
PHE HB3  H  N N 332 
PHE HD1  H  N N 333 
PHE HD2  H  N N 334 
PHE HE1  H  N N 335 
PHE HE2  H  N N 336 
PHE HZ   H  N N 337 
PHE HXT  H  N N 338 
PRO N    N  N N 339 
PRO CA   C  N S 340 
PRO C    C  N N 341 
PRO O    O  N N 342 
PRO CB   C  N N 343 
PRO CG   C  N N 344 
PRO CD   C  N N 345 
PRO OXT  O  N N 346 
PRO H    H  N N 347 
PRO HA   H  N N 348 
PRO HB2  H  N N 349 
PRO HB3  H  N N 350 
PRO HG2  H  N N 351 
PRO HG3  H  N N 352 
PRO HD2  H  N N 353 
PRO HD3  H  N N 354 
PRO HXT  H  N N 355 
SER N    N  N N 356 
SER CA   C  N S 357 
SER C    C  N N 358 
SER O    O  N N 359 
SER CB   C  N N 360 
SER OG   O  N N 361 
SER OXT  O  N N 362 
SER H    H  N N 363 
SER H2   H  N N 364 
SER HA   H  N N 365 
SER HB2  H  N N 366 
SER HB3  H  N N 367 
SER HG   H  N N 368 
SER HXT  H  N N 369 
THR N    N  N N 370 
THR CA   C  N S 371 
THR C    C  N N 372 
THR O    O  N N 373 
THR CB   C  N R 374 
THR OG1  O  N N 375 
THR CG2  C  N N 376 
THR OXT  O  N N 377 
THR H    H  N N 378 
THR H2   H  N N 379 
THR HA   H  N N 380 
THR HB   H  N N 381 
THR HG1  H  N N 382 
THR HG21 H  N N 383 
THR HG22 H  N N 384 
THR HG23 H  N N 385 
THR HXT  H  N N 386 
TRP N    N  N N 387 
TRP CA   C  N S 388 
TRP C    C  N N 389 
TRP O    O  N N 390 
TRP CB   C  N N 391 
TRP CG   C  Y N 392 
TRP CD1  C  Y N 393 
TRP CD2  C  Y N 394 
TRP NE1  N  Y N 395 
TRP CE2  C  Y N 396 
TRP CE3  C  Y N 397 
TRP CZ2  C  Y N 398 
TRP CZ3  C  Y N 399 
TRP CH2  C  Y N 400 
TRP OXT  O  N N 401 
TRP H    H  N N 402 
TRP H2   H  N N 403 
TRP HA   H  N N 404 
TRP HB2  H  N N 405 
TRP HB3  H  N N 406 
TRP HD1  H  N N 407 
TRP HE1  H  N N 408 
TRP HE3  H  N N 409 
TRP HZ2  H  N N 410 
TRP HZ3  H  N N 411 
TRP HH2  H  N N 412 
TRP HXT  H  N N 413 
TYR N    N  N N 414 
TYR CA   C  N S 415 
TYR C    C  N N 416 
TYR O    O  N N 417 
TYR CB   C  N N 418 
TYR CG   C  Y N 419 
TYR CD1  C  Y N 420 
TYR CD2  C  Y N 421 
TYR CE1  C  Y N 422 
TYR CE2  C  Y N 423 
TYR CZ   C  Y N 424 
TYR OH   O  N N 425 
TYR OXT  O  N N 426 
TYR H    H  N N 427 
TYR H2   H  N N 428 
TYR HA   H  N N 429 
TYR HB2  H  N N 430 
TYR HB3  H  N N 431 
TYR HD1  H  N N 432 
TYR HD2  H  N N 433 
TYR HE1  H  N N 434 
TYR HE2  H  N N 435 
TYR HH   H  N N 436 
TYR HXT  H  N N 437 
VAL N    N  N N 438 
VAL CA   C  N S 439 
VAL C    C  N N 440 
VAL O    O  N N 441 
VAL CB   C  N N 442 
VAL CG1  C  N N 443 
VAL CG2  C  N N 444 
VAL OXT  O  N N 445 
VAL H    H  N N 446 
VAL H2   H  N N 447 
VAL HA   H  N N 448 
VAL HB   H  N N 449 
VAL HG11 H  N N 450 
VAL HG12 H  N N 451 
VAL HG13 H  N N 452 
VAL HG21 H  N N 453 
VAL HG22 H  N N 454 
VAL HG23 H  N N 455 
VAL HXT  H  N N 456 
# 
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 
ACO N1A C2A  sing Y N 1   
ACO N1A C6A  doub Y N 2   
ACO C2A N3A  doub Y N 3   
ACO C2A H2A  sing N N 4   
ACO N3A C4A  sing Y N 5   
ACO C4A C5A  doub Y N 6   
ACO C4A N9A  sing Y N 7   
ACO C5A C6A  sing Y N 8   
ACO C5A N7A  sing Y N 9   
ACO C6A N6A  sing N N 10  
ACO N6A H61A sing N N 11  
ACO N6A H62A sing N N 12  
ACO N7A C8A  doub Y N 13  
ACO C8A N9A  sing Y N 14  
ACO C8A H8A  sing N N 15  
ACO N9A C1B  sing N N 16  
ACO C1B C2B  sing N N 17  
ACO C1B O4B  sing N N 18  
ACO C1B H1B  sing N N 19  
ACO C2B O2B  sing N N 20  
ACO C2B C3B  sing N N 21  
ACO C2B H2B  sing N N 22  
ACO O2B HO2A sing N N 23  
ACO C3B O3B  sing N N 24  
ACO C3B C4B  sing N N 25  
ACO C3B H3B  sing N N 26  
ACO O3B P3B  sing N N 27  
ACO P3B O7A  doub N N 28  
ACO P3B O8A  sing N N 29  
ACO P3B O9A  sing N N 30  
ACO O8A HOA8 sing N N 31  
ACO O9A HOA9 sing N N 32  
ACO C4B O4B  sing N N 33  
ACO C4B C5B  sing N N 34  
ACO C4B H4B  sing N N 35  
ACO C5B O5B  sing N N 36  
ACO C5B H51A sing N N 37  
ACO C5B H52A sing N N 38  
ACO O5B P1A  sing N N 39  
ACO P1A O1A  doub N N 40  
ACO P1A O2A  sing N N 41  
ACO P1A O3A  sing N N 42  
ACO O2A HOA2 sing N N 43  
ACO O3A P2A  sing N N 44  
ACO P2A O4A  doub N N 45  
ACO P2A O5A  sing N N 46  
ACO P2A O6A  sing N N 47  
ACO O5A HOA5 sing N N 48  
ACO O6A CCP  sing N N 49  
ACO CBP CCP  sing N N 50  
ACO CBP CDP  sing N N 51  
ACO CBP CEP  sing N N 52  
ACO CBP CAP  sing N N 53  
ACO CCP H121 sing N N 54  
ACO CCP H122 sing N N 55  
ACO CDP H131 sing N N 56  
ACO CDP H132 sing N N 57  
ACO CDP H133 sing N N 58  
ACO CEP H141 sing N N 59  
ACO CEP H142 sing N N 60  
ACO CEP H143 sing N N 61  
ACO CAP OAP  sing N N 62  
ACO CAP C9P  sing N N 63  
ACO CAP H10  sing N N 64  
ACO OAP HO1  sing N N 65  
ACO C9P O9P  doub N N 66  
ACO C9P N8P  sing N N 67  
ACO N8P C7P  sing N N 68  
ACO N8P HN8  sing N N 69  
ACO C7P C6P  sing N N 70  
ACO C7P H71  sing N N 71  
ACO C7P H72  sing N N 72  
ACO C6P C5P  sing N N 73  
ACO C6P H61  sing N N 74  
ACO C6P H62  sing N N 75  
ACO C5P O5P  doub N N 76  
ACO C5P N4P  sing N N 77  
ACO N4P C3P  sing N N 78  
ACO N4P HN4  sing N N 79  
ACO C3P C2P  sing N N 80  
ACO C3P H31  sing N N 81  
ACO C3P H32  sing N N 82  
ACO C2P S1P  sing N N 83  
ACO C2P H21  sing N N 84  
ACO C2P H22  sing N N 85  
ACO S1P C    sing N N 86  
ACO C   O    doub N N 87  
ACO C   CH3  sing N N 88  
ACO CH3 HH31 sing N N 89  
ACO CH3 HH32 sing N N 90  
ACO CH3 HH33 sing N N 91  
ALA N   CA   sing N N 92  
ALA N   H    sing N N 93  
ALA N   H2   sing N N 94  
ALA CA  C    sing N N 95  
ALA CA  CB   sing N N 96  
ALA CA  HA   sing N N 97  
ALA C   O    doub N N 98  
ALA C   OXT  sing N N 99  
ALA CB  HB1  sing N N 100 
ALA CB  HB2  sing N N 101 
ALA CB  HB3  sing N N 102 
ALA OXT HXT  sing N N 103 
ARG N   CA   sing N N 104 
ARG N   H    sing N N 105 
ARG N   H2   sing N N 106 
ARG CA  C    sing N N 107 
ARG CA  CB   sing N N 108 
ARG CA  HA   sing N N 109 
ARG C   O    doub N N 110 
ARG C   OXT  sing N N 111 
ARG CB  CG   sing N N 112 
ARG CB  HB2  sing N N 113 
ARG CB  HB3  sing N N 114 
ARG CG  CD   sing N N 115 
ARG CG  HG2  sing N N 116 
ARG CG  HG3  sing N N 117 
ARG CD  NE   sing N N 118 
ARG CD  HD2  sing N N 119 
ARG CD  HD3  sing N N 120 
ARG NE  CZ   sing N N 121 
ARG NE  HE   sing N N 122 
ARG CZ  NH1  sing N N 123 
ARG CZ  NH2  doub N N 124 
ARG NH1 HH11 sing N N 125 
ARG NH1 HH12 sing N N 126 
ARG NH2 HH21 sing N N 127 
ARG NH2 HH22 sing N N 128 
ARG OXT HXT  sing N N 129 
ASN N   CA   sing N N 130 
ASN N   H    sing N N 131 
ASN N   H2   sing N N 132 
ASN CA  C    sing N N 133 
ASN CA  CB   sing N N 134 
ASN CA  HA   sing N N 135 
ASN C   O    doub N N 136 
ASN C   OXT  sing N N 137 
ASN CB  CG   sing N N 138 
ASN CB  HB2  sing N N 139 
ASN CB  HB3  sing N N 140 
ASN CG  OD1  doub N N 141 
ASN CG  ND2  sing N N 142 
ASN ND2 HD21 sing N N 143 
ASN ND2 HD22 sing N N 144 
ASN OXT HXT  sing N N 145 
ASP N   CA   sing N N 146 
ASP N   H    sing N N 147 
ASP N   H2   sing N N 148 
ASP CA  C    sing N N 149 
ASP CA  CB   sing N N 150 
ASP CA  HA   sing N N 151 
ASP C   O    doub N N 152 
ASP C   OXT  sing N N 153 
ASP CB  CG   sing N N 154 
ASP CB  HB2  sing N N 155 
ASP CB  HB3  sing N N 156 
ASP CG  OD1  doub N N 157 
ASP CG  OD2  sing N N 158 
ASP OD2 HD2  sing N N 159 
ASP OXT HXT  sing N N 160 
CYS N   CA   sing N N 161 
CYS N   H    sing N N 162 
CYS N   H2   sing N N 163 
CYS CA  C    sing N N 164 
CYS CA  CB   sing N N 165 
CYS CA  HA   sing N N 166 
CYS C   O    doub N N 167 
CYS C   OXT  sing N N 168 
CYS CB  SG   sing N N 169 
CYS CB  HB2  sing N N 170 
CYS CB  HB3  sing N N 171 
CYS SG  HG   sing N N 172 
CYS OXT HXT  sing N N 173 
GLN N   CA   sing N N 174 
GLN N   H    sing N N 175 
GLN N   H2   sing N N 176 
GLN CA  C    sing N N 177 
GLN CA  CB   sing N N 178 
GLN CA  HA   sing N N 179 
GLN C   O    doub N N 180 
GLN C   OXT  sing N N 181 
GLN CB  CG   sing N N 182 
GLN CB  HB2  sing N N 183 
GLN CB  HB3  sing N N 184 
GLN CG  CD   sing N N 185 
GLN CG  HG2  sing N N 186 
GLN CG  HG3  sing N N 187 
GLN CD  OE1  doub N N 188 
GLN CD  NE2  sing N N 189 
GLN NE2 HE21 sing N N 190 
GLN NE2 HE22 sing N N 191 
GLN OXT HXT  sing N N 192 
GLU N   CA   sing N N 193 
GLU N   H    sing N N 194 
GLU N   H2   sing N N 195 
GLU CA  C    sing N N 196 
GLU CA  CB   sing N N 197 
GLU CA  HA   sing N N 198 
GLU C   O    doub N N 199 
GLU C   OXT  sing N N 200 
GLU CB  CG   sing N N 201 
GLU CB  HB2  sing N N 202 
GLU CB  HB3  sing N N 203 
GLU CG  CD   sing N N 204 
GLU CG  HG2  sing N N 205 
GLU CG  HG3  sing N N 206 
GLU CD  OE1  doub N N 207 
GLU CD  OE2  sing N N 208 
GLU OE2 HE2  sing N N 209 
GLU OXT HXT  sing N N 210 
GLY N   CA   sing N N 211 
GLY N   H    sing N N 212 
GLY N   H2   sing N N 213 
GLY CA  C    sing N N 214 
GLY CA  HA2  sing N N 215 
GLY CA  HA3  sing N N 216 
GLY C   O    doub N N 217 
GLY C   OXT  sing N N 218 
GLY OXT HXT  sing N N 219 
HIS N   CA   sing N N 220 
HIS N   H    sing N N 221 
HIS N   H2   sing N N 222 
HIS CA  C    sing N N 223 
HIS CA  CB   sing N N 224 
HIS CA  HA   sing N N 225 
HIS C   O    doub N N 226 
HIS C   OXT  sing N N 227 
HIS CB  CG   sing N N 228 
HIS CB  HB2  sing N N 229 
HIS CB  HB3  sing N N 230 
HIS CG  ND1  sing Y N 231 
HIS CG  CD2  doub Y N 232 
HIS ND1 CE1  doub Y N 233 
HIS ND1 HD1  sing N N 234 
HIS CD2 NE2  sing Y N 235 
HIS CD2 HD2  sing N N 236 
HIS CE1 NE2  sing Y N 237 
HIS CE1 HE1  sing N N 238 
HIS NE2 HE2  sing N N 239 
HIS OXT HXT  sing N N 240 
HOH O   H1   sing N N 241 
HOH O   H2   sing N N 242 
ILE N   CA   sing N N 243 
ILE N   H    sing N N 244 
ILE N   H2   sing N N 245 
ILE CA  C    sing N N 246 
ILE CA  CB   sing N N 247 
ILE CA  HA   sing N N 248 
ILE C   O    doub N N 249 
ILE C   OXT  sing N N 250 
ILE CB  CG1  sing N N 251 
ILE CB  CG2  sing N N 252 
ILE CB  HB   sing N N 253 
ILE CG1 CD1  sing N N 254 
ILE CG1 HG12 sing N N 255 
ILE CG1 HG13 sing N N 256 
ILE CG2 HG21 sing N N 257 
ILE CG2 HG22 sing N N 258 
ILE CG2 HG23 sing N N 259 
ILE CD1 HD11 sing N N 260 
ILE CD1 HD12 sing N N 261 
ILE CD1 HD13 sing N N 262 
ILE OXT HXT  sing N N 263 
LEU N   CA   sing N N 264 
LEU N   H    sing N N 265 
LEU N   H2   sing N N 266 
LEU CA  C    sing N N 267 
LEU CA  CB   sing N N 268 
LEU CA  HA   sing N N 269 
LEU C   O    doub N N 270 
LEU C   OXT  sing N N 271 
LEU CB  CG   sing N N 272 
LEU CB  HB2  sing N N 273 
LEU CB  HB3  sing N N 274 
LEU CG  CD1  sing N N 275 
LEU CG  CD2  sing N N 276 
LEU CG  HG   sing N N 277 
LEU CD1 HD11 sing N N 278 
LEU CD1 HD12 sing N N 279 
LEU CD1 HD13 sing N N 280 
LEU CD2 HD21 sing N N 281 
LEU CD2 HD22 sing N N 282 
LEU CD2 HD23 sing N N 283 
LEU OXT HXT  sing N N 284 
MSE N   CA   sing N N 285 
MSE N   H    sing N N 286 
MSE N   H2   sing N N 287 
MSE CA  C    sing N N 288 
MSE CA  CB   sing N N 289 
MSE CA  HA   sing N N 290 
MSE C   O    doub N N 291 
MSE C   OXT  sing N N 292 
MSE OXT HXT  sing N N 293 
MSE CB  CG   sing N N 294 
MSE CB  HB2  sing N N 295 
MSE CB  HB3  sing N N 296 
MSE CG  SE   sing N N 297 
MSE CG  HG2  sing N N 298 
MSE CG  HG3  sing N N 299 
MSE SE  CE   sing N N 300 
MSE CE  HE1  sing N N 301 
MSE CE  HE2  sing N N 302 
MSE CE  HE3  sing N N 303 
PHE N   CA   sing N N 304 
PHE N   H    sing N N 305 
PHE N   H2   sing N N 306 
PHE CA  C    sing N N 307 
PHE CA  CB   sing N N 308 
PHE CA  HA   sing N N 309 
PHE C   O    doub N N 310 
PHE C   OXT  sing N N 311 
PHE CB  CG   sing N N 312 
PHE CB  HB2  sing N N 313 
PHE CB  HB3  sing N N 314 
PHE CG  CD1  doub Y N 315 
PHE CG  CD2  sing Y N 316 
PHE CD1 CE1  sing Y N 317 
PHE CD1 HD1  sing N N 318 
PHE CD2 CE2  doub Y N 319 
PHE CD2 HD2  sing N N 320 
PHE CE1 CZ   doub Y N 321 
PHE CE1 HE1  sing N N 322 
PHE CE2 CZ   sing Y N 323 
PHE CE2 HE2  sing N N 324 
PHE CZ  HZ   sing N N 325 
PHE OXT HXT  sing N N 326 
PRO N   CA   sing N N 327 
PRO N   CD   sing N N 328 
PRO N   H    sing N N 329 
PRO CA  C    sing N N 330 
PRO CA  CB   sing N N 331 
PRO CA  HA   sing N N 332 
PRO C   O    doub N N 333 
PRO C   OXT  sing N N 334 
PRO CB  CG   sing N N 335 
PRO CB  HB2  sing N N 336 
PRO CB  HB3  sing N N 337 
PRO CG  CD   sing N N 338 
PRO CG  HG2  sing N N 339 
PRO CG  HG3  sing N N 340 
PRO CD  HD2  sing N N 341 
PRO CD  HD3  sing N N 342 
PRO OXT HXT  sing N N 343 
SER N   CA   sing N N 344 
SER N   H    sing N N 345 
SER N   H2   sing N N 346 
SER CA  C    sing N N 347 
SER CA  CB   sing N N 348 
SER CA  HA   sing N N 349 
SER C   O    doub N N 350 
SER C   OXT  sing N N 351 
SER CB  OG   sing N N 352 
SER CB  HB2  sing N N 353 
SER CB  HB3  sing N N 354 
SER OG  HG   sing N N 355 
SER OXT HXT  sing N N 356 
THR N   CA   sing N N 357 
THR N   H    sing N N 358 
THR N   H2   sing N N 359 
THR CA  C    sing N N 360 
THR CA  CB   sing N N 361 
THR CA  HA   sing N N 362 
THR C   O    doub N N 363 
THR C   OXT  sing N N 364 
THR CB  OG1  sing N N 365 
THR CB  CG2  sing N N 366 
THR CB  HB   sing N N 367 
THR OG1 HG1  sing N N 368 
THR CG2 HG21 sing N N 369 
THR CG2 HG22 sing N N 370 
THR CG2 HG23 sing N N 371 
THR OXT HXT  sing N N 372 
TRP N   CA   sing N N 373 
TRP N   H    sing N N 374 
TRP N   H2   sing N N 375 
TRP CA  C    sing N N 376 
TRP CA  CB   sing N N 377 
TRP CA  HA   sing N N 378 
TRP C   O    doub N N 379 
TRP C   OXT  sing N N 380 
TRP CB  CG   sing N N 381 
TRP CB  HB2  sing N N 382 
TRP CB  HB3  sing N N 383 
TRP CG  CD1  doub Y N 384 
TRP CG  CD2  sing Y N 385 
TRP CD1 NE1  sing Y N 386 
TRP CD1 HD1  sing N N 387 
TRP CD2 CE2  doub Y N 388 
TRP CD2 CE3  sing Y N 389 
TRP NE1 CE2  sing Y N 390 
TRP NE1 HE1  sing N N 391 
TRP CE2 CZ2  sing Y N 392 
TRP CE3 CZ3  doub Y N 393 
TRP CE3 HE3  sing N N 394 
TRP CZ2 CH2  doub Y N 395 
TRP CZ2 HZ2  sing N N 396 
TRP CZ3 CH2  sing Y N 397 
TRP CZ3 HZ3  sing N N 398 
TRP CH2 HH2  sing N N 399 
TRP OXT HXT  sing N N 400 
TYR N   CA   sing N N 401 
TYR N   H    sing N N 402 
TYR N   H2   sing N N 403 
TYR CA  C    sing N N 404 
TYR CA  CB   sing N N 405 
TYR CA  HA   sing N N 406 
TYR C   O    doub N N 407 
TYR C   OXT  sing N N 408 
TYR CB  CG   sing N N 409 
TYR CB  HB2  sing N N 410 
TYR CB  HB3  sing N N 411 
TYR CG  CD1  doub Y N 412 
TYR CG  CD2  sing Y N 413 
TYR CD1 CE1  sing Y N 414 
TYR CD1 HD1  sing N N 415 
TYR CD2 CE2  doub Y N 416 
TYR CD2 HD2  sing N N 417 
TYR CE1 CZ   doub Y N 418 
TYR CE1 HE1  sing N N 419 
TYR CE2 CZ   sing Y N 420 
TYR CE2 HE2  sing N N 421 
TYR CZ  OH   sing N N 422 
TYR OH  HH   sing N N 423 
TYR OXT HXT  sing N N 424 
VAL N   CA   sing N N 425 
VAL N   H    sing N N 426 
VAL N   H2   sing N N 427 
VAL CA  C    sing N N 428 
VAL CA  CB   sing N N 429 
VAL CA  HA   sing N N 430 
VAL C   O    doub N N 431 
VAL C   OXT  sing N N 432 
VAL CB  CG1  sing N N 433 
VAL CB  CG2  sing N N 434 
VAL CB  HB   sing N N 435 
VAL CG1 HG11 sing N N 436 
VAL CG1 HG12 sing N N 437 
VAL CG1 HG13 sing N N 438 
VAL CG2 HG21 sing N N 439 
VAL CG2 HG22 sing N N 440 
VAL CG2 HG23 sing N N 441 
VAL OXT HXT  sing N N 442 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           'U54 GM094585' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2CNM 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CR5 
_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]   0.007788 
_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]   0.007627 
_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]   0.022361 
_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.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 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.
;
? 
NA ? ? 9.38062  1.54875 ? ? 3.38349  72.32734 ? ? 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.
;
? 
P  ? ? 9.51135  5.44231 ? ? 1.42069  35.72801 ? ? 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.
;
? 
SE ? ? 26.02326 7.89457 ? ? 1.54240  29.12501 ? ? 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 
HETATM 1    N  N   . MSE A 1 2   ? -28.24900 28.18700 -18.22300 1.000 85.19752 ? 1   MSE A N   1 
HETATM 2    C  CA  . MSE A 1 2   ? -28.60800 27.91300 -16.83800 1.000 80.73212 ? 1   MSE A CA  1 
HETATM 3    C  C   . MSE A 1 2   ? -30.11600 27.78400 -16.71900 1.000 80.83577 ? 1   MSE A C   1 
HETATM 4    O  O   . MSE A 1 2   ? -30.69100 27.94700 -15.63800 1.000 82.70091 ? 1   MSE A O   1 
HETATM 5    C  CB  . MSE A 1 2   ? -28.08700 29.01500 -15.91400 1.000 89.63025 ? 1   MSE A CB  1 
ATOM   6    N  N   . ASP A 1 3   ? -30.75600 27.47600 -17.84200 1.000 71.34864 ? 2   ASP A N   1 
ATOM   7    C  CA  . ASP A 1 3   ? -32.20100 27.43500 -17.92200 1.000 56.27341 ? 2   ASP A CA  1 
ATOM   8    C  C   . ASP A 1 3   ? -32.68400 26.00500 -18.12400 1.000 50.19296 ? 2   ASP A C   1 
ATOM   9    O  O   . ASP A 1 3   ? -31.97700 25.14400 -18.65300 1.000 54.13408 ? 2   ASP A O   1 
ATOM   10   C  CB  . ASP A 1 3   ? -32.72900 28.33200 -19.04300 1.000 54.97348 ? 2   ASP A CB  1 
ATOM   11   C  CG  . ASP A 1 3   ? -32.93700 29.77100 -18.58400 1.000 75.98836 ? 2   ASP A CG  1 
ATOM   12   O  OD1 . ASP A 1 3   ? -33.52600 29.96600 -17.49700 1.000 76.68429 ? 2   ASP A OD1 1 
ATOM   13   O  OD2 . ASP A 1 3   ? -32.50700 30.70300 -19.30100 1.000 83.13570 ? 2   ASP A OD2 1 
ATOM   14   N  N   . TYR A 1 4   ? -33.89800 25.77400 -17.67600 1.000 42.50203 ? 3   TYR A N   1 
ATOM   15   C  CA  . TYR A 1 4   ? -34.52000 24.47100 -17.69600 1.000 37.89003 ? 3   TYR A CA  1 
ATOM   16   C  C   . TYR A 1 4   ? -35.89400 24.61600 -18.33000 1.000 35.32264 ? 3   TYR A C   1 
ATOM   17   O  O   . TYR A 1 4   ? -36.46800 25.71400 -18.37200 1.000 40.34198 ? 3   TYR A O   1 
ATOM   18   C  CB  . TYR A 1 4   ? -34.65200 23.90600 -16.27500 1.000 35.11684 ? 3   TYR A CB  1 
ATOM   19   C  CG  . TYR A 1 4   ? -33.34400 23.68500 -15.52900 1.000 35.27990 ? 3   TYR A CG  1 
ATOM   20   C  CD1 . TYR A 1 4   ? -32.68700 22.46700 -15.60300 1.000 31.22394 ? 3   TYR A CD1 1 
ATOM   21   C  CD2 . TYR A 1 4   ? -32.79000 24.68200 -14.73300 1.000 35.98127 ? 3   TYR A CD2 1 
ATOM   22   C  CE1 . TYR A 1 4   ? -31.50100 22.24900 -14.91600 1.000 36.41904 ? 3   TYR A CE1 1 
ATOM   23   C  CE2 . TYR A 1 4   ? -31.60800 24.46800 -14.03700 1.000 42.26111 ? 3   TYR A CE2 1 
ATOM   24   C  CZ  . TYR A 1 4   ? -30.97100 23.23800 -14.13100 1.000 39.07125 ? 3   TYR A CZ  1 
ATOM   25   O  OH  . TYR A 1 4   ? -29.78800 23.02100 -13.45500 1.000 39.83164 ? 3   TYR A OH  1 
ATOM   26   N  N   A ARG A 1 5   ? -36.42200 23.49600 -18.82100 0.390 32.58823 ? 4   ARG A N   1 
ATOM   27   N  N   B ARG A 1 5   ? -36.40800 23.50400 -18.84500 0.610 32.67146 ? 4   ARG A N   1 
ATOM   28   C  CA  A ARG A 1 5   ? -37.75000 23.44400 -19.41500 0.390 34.95677 ? 4   ARG A CA  1 
ATOM   29   C  CA  B ARG A 1 5   ? -37.75200 23.45000 -19.39000 0.610 33.66802 ? 4   ARG A CA  1 
ATOM   30   C  C   A ARG A 1 5   ? -38.54200 22.28500 -18.82500 0.390 33.91176 ? 4   ARG A C   1 
ATOM   31   C  C   B ARG A 1 5   ? -38.52800 22.31300 -18.73900 0.610 34.19149 ? 4   ARG A C   1 
ATOM   32   O  O   A ARG A 1 5   ? -37.99300 21.20600 -18.58700 0.390 34.02644 ? 4   ARG A O   1 
ATOM   33   O  O   B ARG A 1 5   ? -37.95800 21.28800 -18.36200 0.610 34.84485 ? 4   ARG A O   1 
ATOM   34   C  CB  A ARG A 1 5   ? -37.66100 23.30600 -20.94500 0.390 40.98629 ? 4   ARG A CB  1 
ATOM   35   C  CB  B ARG A 1 5   ? -37.72100 23.28500 -20.92300 0.610 41.57023 ? 4   ARG A CB  1 
ATOM   36   C  CG  A ARG A 1 5   ? -39.00000 23.14100 -21.64000 0.390 41.80753 ? 4   ARG A CG  1 
ATOM   37   C  CG  B ARG A 1 5   ? -37.12500 24.48800 -21.65100 0.610 44.92881 ? 4   ARG A CG  1 
ATOM   38   C  CD  A ARG A 1 5   ? -38.86800 23.33700 -23.13700 0.390 49.66230 ? 4   ARG A CD  1 
ATOM   39   C  CD  B ARG A 1 5   ? -36.84000 24.16900 -23.11000 0.610 49.89537 ? 4   ARG A CD  1 
ATOM   40   N  NE  A ARG A 1 5   ? -39.89900 22.61700 -23.88200 0.390 49.50350 ? 4   ARG A NE  1 
ATOM   41   N  NE  B ARG A 1 5   ? -35.95200 23.01400 -23.20900 0.610 54.50958 ? 4   ARG A NE  1 
ATOM   42   C  CZ  A ARG A 1 5   ? -39.77000 21.36400 -24.30500 0.390 43.43783 ? 4   ARG A CZ  1 
ATOM   43   C  CZ  B ARG A 1 5   ? -34.66000 23.08200 -23.51000 0.610 56.53743 ? 4   ARG A CZ  1 
ATOM   44   N  NH1 A ARG A 1 5   ? -38.65800 20.69100 -24.04800 0.390 43.48509 ? 4   ARG A NH1 1 
ATOM   45   N  NH1 B ARG A 1 5   ? -34.09500 24.25500 -23.77000 0.610 56.99201 ? 4   ARG A NH1 1 
ATOM   46   N  NH2 A ARG A 1 5   ? -40.74900 20.78300 -24.98600 0.390 42.46930 ? 4   ARG A NH2 1 
ATOM   47   N  NH2 B ARG A 1 5   ? -33.93800 21.97200 -23.56300 0.610 48.50609 ? 4   ARG A NH2 1 
ATOM   48   N  N   . ILE A 1 6   ? -39.83500 22.51500 -18.59500 1.000 29.37548 ? 5   ILE A N   1 
ATOM   49   C  CA  . ILE A 1 6   ? -40.75700 21.49600 -18.09800 1.000 29.95094 ? 5   ILE A CA  1 
ATOM   50   C  C   . ILE A 1 6   ? -41.55700 20.98900 -19.28700 1.000 31.56816 ? 5   ILE A C   1 
ATOM   51   O  O   . ILE A 1 6   ? -42.12800 21.78800 -20.03100 1.000 32.87660 ? 5   ILE A O   1 
ATOM   52   C  CB  . ILE A 1 6   ? -41.70000 22.08000 -17.02700 1.000 30.68648 ? 5   ILE A CB  1 
ATOM   53   C  CG1 . ILE A 1 6   ? -40.91800 22.73700 -15.89400 1.000 34.28544 ? 5   ILE A CG1 1 
ATOM   54   C  CG2 . ILE A 1 6   ? -42.66200 21.02000 -16.47400 1.000 32.07524 ? 5   ILE A CG2 1 
ATOM   55   C  CD1 . ILE A 1 6   ? -39.93800 21.82300 -15.23200 1.000 29.51105 ? 5   ILE A CD1 1 
ATOM   56   N  N   . ARG A 1 7   ? -41.62900 19.66900 -19.45900 1.000 26.81604 ? 6   ARG A N   1 
ATOM   57   C  CA  . ARG A 1 7   ? -42.45300 19.09500 -20.51600 1.000 26.78732 ? 6   ARG A CA  1 
ATOM   58   C  C   . ARG A 1 7   ? -43.07100 17.78000 -20.05600 1.000 26.01889 ? 6   ARG A C   1 
ATOM   59   O  O   . ARG A 1 7   ? -42.67400 17.20000 -19.04800 1.000 25.80763 ? 6   ARG A O   1 
ATOM   60   C  CB  . ARG A 1 7   ? -41.64200 18.84500 -21.79800 1.000 32.47026 ? 6   ARG A CB  1 
ATOM   61   C  CG  . ARG A 1 7   ? -40.43100 17.95100 -21.58900 1.000 29.47935 ? 6   ARG A CG  1 
ATOM   62   C  CD  . ARG A 1 7   ? -39.96900 17.43700 -22.91200 1.000 33.68671 ? 6   ARG A CD  1 
ATOM   63   N  NE  . ARG A 1 7   ? -38.73600 16.66100 -22.85500 1.000 32.99718 ? 6   ARG A NE  1 
ATOM   64   C  CZ  . ARG A 1 7   ? -38.69500 15.33500 -22.73200 1.000 35.76619 ? 6   ARG A CZ  1 
ATOM   65   N  NH1 . ARG A 1 7   ? -39.82300 14.65000 -22.64500 1.000 33.15395 ? 6   ARG A NH1 1 
ATOM   66   N  NH2 . ARG A 1 7   ? -37.52800 14.69900 -22.73500 1.000 35.64557 ? 6   ARG A NH2 1 
ATOM   67   N  N   . THR A 1 8   ? -44.04600 17.30400 -20.83100 1.000 29.45458 ? 7   THR A N   1 
ATOM   68   C  CA  A THR A 1 8   ? -44.57000 15.96500 -20.59800 0.570 30.64163 ? 7   THR A CA  1 
ATOM   69   C  CA  B THR A 1 8   ? -44.58500 15.96800 -20.63800 0.430 30.81674 ? 7   THR A CA  1 
ATOM   70   C  C   . THR A 1 8   ? -43.49400 14.93300 -20.88100 1.000 27.67938 ? 7   THR A C   1 
ATOM   71   O  O   . THR A 1 8   ? -42.69400 15.07400 -21.81000 1.000 30.47237 ? 7   THR A O   1 
ATOM   72   C  CB  A THR A 1 8   ? -45.78800 15.68000 -21.48400 0.570 31.77023 ? 7   THR A CB  1 
ATOM   73   C  CB  B THR A 1 8   ? -45.75200 15.77600 -21.61300 0.430 32.19655 ? 7   THR A CB  1 
ATOM   74   O  OG1 A THR A 1 8   ? -45.43100 15.84900 -22.86100 0.570 34.65706 ? 7   THR A OG1 1 
ATOM   75   O  OG1 B THR A 1 8   ? -46.64000 16.89200 -21.49400 0.430 33.78062 ? 7   THR A OG1 1 
ATOM   76   C  CG2 A THR A 1 8   ? -46.91700 16.61000 -21.13300 0.570 32.27000 ? 7   THR A CG2 1 
ATOM   77   C  CG2 B THR A 1 8   ? -46.51500 14.53100 -21.33100 0.430 34.03321 ? 7   THR A CG2 1 
ATOM   78   N  N   . SER A 1 9   ? -43.46700 13.87800 -20.05600 1.000 25.28810 ? 8   SER A N   1 
ATOM   79   C  CA  . SER A 1 9   ? -42.56600 12.76400 -20.28300 1.000 25.09161 ? 8   SER A CA  1 
ATOM   80   C  C   . SER A 1 9   ? -43.05500 11.88900 -21.43800 1.000 28.37088 ? 8   SER A C   1 
ATOM   81   O  O   . SER A 1 9   ? -44.25100 11.80900 -21.71500 1.000 32.77594 ? 8   SER A O   1 
ATOM   82   C  CB  . SER A 1 9   ? -42.46000 11.91900 -19.01100 1.000 25.82374 ? 8   SER A CB  1 
ATOM   83   O  OG  . SER A 1 9   ? -42.10600 12.77000 -17.93200 1.000 23.31404 ? 8   SER A OG  1 
ATOM   84   N  N   . ARG A 1 10  ? -42.11300 11.24300 -22.12300 1.000 27.53725 ? 9   ARG A N   1 
ATOM   85   C  CA  . ARG A 1 10  ? -42.41300 10.36700 -23.24500 1.000 35.51739 ? 9   ARG A CA  1 
ATOM   86   C  C   . ARG A 1 10  ? -41.83000 8.99600  -22.95600 1.000 35.41718 ? 9   ARG A C   1 
ATOM   87   O  O   . ARG A 1 10  ? -40.99700 8.84000  -22.05500 1.000 29.01310 ? 9   ARG A O   1 
ATOM   88   C  CB  . ARG A 1 10  ? -41.85100 10.91800 -24.56700 1.000 38.55418 ? 9   ARG A CB  1 
ATOM   89   C  CG  . ARG A 1 10  ? -42.29000 12.34600 -24.88900 1.000 38.28204 ? 9   ARG A CG  1 
ATOM   90   C  CD  . ARG A 1 10  ? -41.73800 12.83900 -26.23400 1.000 48.52786 ? 9   ARG A CD  1 
ATOM   91   N  NE  . ARG A 1 10  ? -40.33900 13.28400 -26.17100 1.000 60.44775 ? 9   ARG A NE  1 
ATOM   92   C  CZ  . ARG A 1 10  ? -39.93900 14.56000 -26.09700 1.000 58.06310 ? 9   ARG A CZ  1 
ATOM   93   N  NH1 . ARG A 1 10  ? -40.83000 15.54900 -26.07300 1.000 56.05731 ? 9   ARG A NH1 1 
ATOM   94   N  NH2 . ARG A 1 10  ? -38.63800 14.85400 -26.05300 1.000 51.46445 ? 9   ARG A NH2 1 
ATOM   95   N  N   . ASP A 1 11  ? -42.26500 8.00400  -23.74600 1.000 34.38377 ? 10  ASP A N   1 
ATOM   96   C  CA  . ASP A 1 11  ? -41.89000 6.62400  -23.44000 1.000 33.01856 ? 10  ASP A CA  1 
ATOM   97   C  C   . ASP A 1 11  ? -40.38200 6.45100  -23.45200 1.000 29.31975 ? 10  ASP A C   1 
ATOM   98   O  O   . ASP A 1 11  ? -39.82700 5.72800  -22.62000 1.000 27.93679 ? 10  ASP A O   1 
ATOM   99   C  CB  . ASP A 1 11  ? -42.53800 5.66500  -24.43700 1.000 40.91308 ? 10  ASP A CB  1 
ATOM   100  C  CG  . ASP A 1 11  ? -44.01800 5.50200  -24.20100 1.000 57.01106 ? 10  ASP A CG  1 
ATOM   101  O  OD1 . ASP A 1 11  ? -44.79500 5.82000  -25.13200 1.000 70.53157 ? 10  ASP A OD1 1 
ATOM   102  O  OD2 . ASP A 1 11  ? -44.40100 5.07400  -23.08100 1.000 60.68430 ? 10  ASP A OD2 1 
ATOM   103  N  N   . GLU A 1 12  ? -39.70800 7.11000  -24.40000 1.000 32.29632 ? 11  GLU A N   1 
ATOM   104  C  CA  . GLU A 1 12  ? -38.26000 7.02100  -24.51700 1.000 35.03515 ? 11  GLU A CA  1 
ATOM   105  C  C   . GLU A 1 12  ? -37.53300 7.61800  -23.32000 1.000 34.99931 ? 11  GLU A C   1 
ATOM   106  O  O   . GLU A 1 12  ? -36.35900 7.30400  -23.11100 1.000 38.88412 ? 11  GLU A O   1 
ATOM   107  C  CB  . GLU A 1 12  ? -37.82600 7.72100  -25.81000 1.000 39.00464 ? 11  GLU A CB  1 
ATOM   108  C  CG  . GLU A 1 12  ? -38.24800 9.17200  -25.80000 1.000 47.33745 ? 11  GLU A CG  1 
ATOM   109  C  CD  . GLU A 1 12  ? -37.99900 9.88800  -27.09900 1.000 59.74536 ? 11  GLU A CD  1 
ATOM   110  O  OE1 . GLU A 1 12  ? -37.44100 9.26800  -28.03100 1.000 69.32669 ? 11  GLU A OE1 1 
ATOM   111  O  OE2 . GLU A 1 12  ? -38.36800 11.07900 -27.18800 1.000 60.02421 ? 11  GLU A OE2 1 
ATOM   112  N  N   . ASP A 1 13  ? -38.19600 8.45100  -22.51200 1.000 30.40847 ? 12  ASP A N   1 
ATOM   113  C  CA  . ASP A 1 13  ? -37.55800 9.00700  -21.31900 1.000 28.44510 ? 12  ASP A CA  1 
ATOM   114  C  C   . ASP A 1 13  ? -37.53100 8.05100  -20.13200 1.000 27.95317 ? 12  ASP A C   1 
ATOM   115  O  O   . ASP A 1 13  ? -36.72700 8.24700  -19.20800 1.000 25.69340 ? 12  ASP A O   1 
ATOM   116  C  CB  . ASP A 1 13  ? -38.27900 10.27500 -20.86200 1.000 27.83975 ? 12  ASP A CB  1 
ATOM   117  C  CG  . ASP A 1 13  ? -38.32100 11.35500 -21.93200 1.000 32.73482 ? 12  ASP A CG  1 
ATOM   118  O  OD1 . ASP A 1 13  ? -37.25900 11.67400 -22.51100 1.000 38.94912 ? 12  ASP A OD1 1 
ATOM   119  O  OD2 . ASP A 1 13  ? -39.42400 11.87300 -22.22400 1.000 31.92539 ? 12  ASP A OD2 1 
ATOM   120  N  N   . ALA A 1 14  ? -38.37300 7.00500  -20.13800 1.000 25.47710 ? 13  ALA A N   1 
ATOM   121  C  CA  . ALA A 1 14  ? -38.57800 6.22700  -18.92000 1.000 24.06998 ? 13  ALA A CA  1 
ATOM   122  C  C   . ALA A 1 14  ? -37.28000 5.60300  -18.43000 1.000 23.18164 ? 13  ALA A C   1 
ATOM   123  O  O   . ALA A 1 14  ? -37.02500 5.56200  -17.22300 1.000 25.31689 ? 13  ALA A O   1 
ATOM   124  C  CB  . ALA A 1 14  ? -39.63000 5.13900  -19.15200 1.000 26.84746 ? 13  ALA A CB  1 
ATOM   125  N  N   . ALA A 1 15  ? -36.45800 5.09400  -19.35600 1.000 27.10726 ? 14  ALA A N   1 
ATOM   126  C  CA  . ALA A 1 15  ? -35.23800 4.38500  -18.97400 1.000 26.93608 ? 14  ALA A CA  1 
ATOM   127  C  C   . ALA A 1 15  ? -34.25700 5.25500  -18.19100 1.000 27.73452 ? 14  ALA A C   1 
ATOM   128  O  O   . ALA A 1 15  ? -33.41900 4.71700  -17.45100 1.000 27.43271 ? 14  ALA A O   1 
ATOM   129  C  CB  . ALA A 1 15  ? -34.55400 3.81600  -20.21900 1.000 27.58707 ? 14  ALA A CB  1 
ATOM   130  N  N   . LEU A 1 16  ? -34.33600 6.58800  -18.33400 1.000 24.56113 ? 15  LEU A N   1 
ATOM   131  C  CA  . LEU A 1 16  ? -33.44700 7.52300  -17.65300 1.000 26.58354 ? 15  LEU A CA  1 
ATOM   132  C  C   . LEU A 1 16  ? -33.92900 7.90100  -16.26000 1.000 25.35106 ? 15  LEU A C   1 
ATOM   133  O  O   . LEU A 1 16  ? -33.16600 8.51000  -15.48600 1.000 24.40008 ? 15  LEU A O   1 
ATOM   134  C  CB  . LEU A 1 16  ? -33.30500 8.80700  -18.50500 1.000 24.11340 ? 15  LEU A CB  1 
ATOM   135  C  CG  . LEU A 1 16  ? -32.65900 8.63400  -19.88900 1.000 29.72119 ? 15  LEU A CG  1 
ATOM   136  C  CD1 . LEU A 1 16  ? -32.66500 9.95100  -20.70700 1.000 32.52128 ? 15  LEU A CD1 1 
ATOM   137  C  CD2 . LEU A 1 16  ? -31.25000 8.14900  -19.71200 1.000 34.68545 ? 15  LEU A CD2 1 
ATOM   138  N  N   . LEU A 1 17  ? -35.18100 7.59700  -15.93300 1.000 23.21300 ? 16  LEU A N   1 
ATOM   139  C  CA  . LEU A 1 17  ? -35.75300 8.12900  -14.69500 1.000 21.45835 ? 16  LEU A CA  1 
ATOM   140  C  C   . LEU A 1 17  ? -35.29100 7.41400  -13.41200 1.000 22.87218 ? 16  LEU A C   1 
ATOM   141  O  O   . LEU A 1 17  ? -35.14100 8.09200  -12.38200 1.000 20.87601 ? 16  LEU A O   1 
ATOM   142  C  CB  . LEU A 1 17  ? -37.28100 8.12000  -14.80900 1.000 20.79540 ? 16  LEU A CB  1 
ATOM   143  C  CG  . LEU A 1 17  ? -37.79900 8.86800  -16.03600 1.000 24.65626 ? 16  LEU A CG  1 
ATOM   144  C  CD1 . LEU A 1 17  ? -39.31300 8.82000  -16.05000 1.000 29.84751 ? 16  LEU A CD1 1 
ATOM   145  C  CD2 . LEU A 1 17  ? -37.29600 10.34300 -16.08900 1.000 25.41103 ? 16  LEU A CD2 1 
ATOM   146  N  N   . PRO A 1 18  ? -35.06900 6.08600  -13.38000 1.000 23.33263 ? 17  PRO A N   1 
ATOM   147  C  CA  . PRO A 1 18  ? -34.56100 5.50300  -12.12400 1.000 22.34780 ? 17  PRO A CA  1 
ATOM   148  C  C   . PRO A 1 18  ? -33.26100 6.15200  -11.64500 1.000 25.48981 ? 17  PRO A C   1 
ATOM   149  O  O   . PRO A 1 18  ? -33.12200 6.38000  -10.43700 1.000 23.80325 ? 17  PRO A O   1 
ATOM   150  C  CB  . PRO A 1 18  ? -34.39200 4.01100  -12.46600 1.000 24.90510 ? 17  PRO A CB  1 
ATOM   151  C  CG  . PRO A 1 18  ? -35.54700 3.78600  -13.43400 1.000 24.22430 ? 17  PRO A CG  1 
ATOM   152  C  CD  . PRO A 1 18  ? -35.50900 5.02100  -14.31900 1.000 20.48102 ? 17  PRO A CD  1 
ATOM   153  N  N   . ALA A 1 19  ? -32.32600 6.50800  -12.54800 1.000 22.89737 ? 18  ALA A N   1 
ATOM   154  C  CA  . ALA A 1 19  ? -31.08300 7.12400  -12.09200 1.000 23.35387 ? 18  ALA A CA  1 
ATOM   155  C  C   . ALA A 1 19  ? -31.34200 8.48900  -11.46700 1.000 22.69070 ? 18  ALA A C   1 
ATOM   156  O  O   . ALA A 1 19  ? -30.63200 8.88000  -10.53500 1.000 22.79191 ? 18  ALA A O   1 
ATOM   157  C  CB  . ALA A 1 19  ? -30.07900 7.28100  -13.25100 1.000 24.39223 ? 18  ALA A CB  1 
ATOM   158  N  N   . ILE A 1 20  ? -32.33900 9.22700  -11.97100 1.000 22.52358 ? 19  ILE A N   1 
ATOM   159  C  CA  . ILE A 1 20  ? -32.69600 10.50700 -11.35400 1.000 21.81461 ? 19  ILE A CA  1 
ATOM   160  C  C   . ILE A 1 20  ? -33.26400 10.30200 -9.95600  1.000 21.25705 ? 19  ILE A C   1 
ATOM   161  O  O   . ILE A 1 20  ? -32.93900 11.04400 -9.01800  1.000 21.46896 ? 19  ILE A O   1 
ATOM   162  C  CB  . ILE A 1 20  ? -33.68500 11.27000 -12.25600 1.000 22.47381 ? 19  ILE A CB  1 
ATOM   163  C  CG1 . ILE A 1 20  ? -32.97800 11.65000 -13.54300 1.000 23.61987 ? 19  ILE A CG1 1 
ATOM   164  C  CG2 . ILE A 1 20  ? -34.25400 12.47600 -11.50800 1.000 26.32215 ? 19  ILE A CG2 1 
ATOM   165  C  CD1 . ILE A 1 20  ? -33.91800 12.16100 -14.66700 1.000 27.04314 ? 19  ILE A CD1 1 
ATOM   166  N  N   . GLU A 1 21  ? -34.11200 9.28700  -9.77200  1.000 22.25728 ? 20  GLU A N   1 
ATOM   167  C  CA  . GLU A 1 21  ? -34.65200 9.07800  -8.43200  1.000 22.74470 ? 20  GLU A CA  1 
ATOM   168  C  C   . GLU A 1 21  ? -33.55200 8.64000  -7.46800  1.000 22.69973 ? 20  GLU A C   1 
ATOM   169  O  O   . GLU A 1 21  ? -33.52900 9.07600  -6.31000  1.000 24.00678 ? 20  GLU A O   1 
ATOM   170  C  CB  . GLU A 1 21  ? -35.80000 8.05300  -8.47200  1.000 21.04380 ? 20  GLU A CB  1 
ATOM   171  C  CG  . GLU A 1 21  ? -36.60700 8.02000  -7.16100  1.000 23.95063 ? 20  GLU A CG  1 
ATOM   172  C  CD  . GLU A 1 21  ? -37.74800 7.00900  -7.14900  1.000 30.94029 ? 20  GLU A CD  1 
ATOM   173  O  OE1 . GLU A 1 21  ? -38.14000 6.59500  -6.04100  1.000 32.74988 ? 20  GLU A OE1 1 
ATOM   174  O  OE2 . GLU A 1 21  ? -38.24000 6.62100  -8.22600  1.000 26.72245 ? 20  GLU A OE2 1 
ATOM   175  N  N   A ARG A 1 22  ? -32.61000 7.81800  -7.93500  0.680 21.08576 ? 21  ARG A N   1 
ATOM   176  N  N   B ARG A 1 22  ? -32.61000 7.82500  -7.94700  0.320 21.60089 ? 21  ARG A N   1 
ATOM   177  C  CA  A ARG A 1 22  ? -31.48300 7.41000  -7.09300  0.680 22.49593 ? 21  ARG A CA  1 
ATOM   178  C  CA  B ARG A 1 22  ? -31.48600 7.39400  -7.12000  0.320 22.61592 ? 21  ARG A CA  1 
ATOM   179  C  C   A ARG A 1 22  ? -30.62200 8.60000  -6.70700  0.680 24.28043 ? 21  ARG A C   1 
ATOM   180  C  C   B ARG A 1 22  ? -30.60700 8.57300  -6.72300  0.320 23.46717 ? 21  ARG A C   1 
ATOM   181  O  O   A ARG A 1 22  ? -30.24400 8.75900  -5.53700  0.680 23.31687 ? 21  ARG A O   1 
ATOM   182  O  O   B ARG A 1 22  ? -30.18900 8.68700  -5.56400  0.320 24.50896 ? 21  ARG A O   1 
ATOM   183  C  CB  A ARG A 1 22  ? -30.63000 6.36700  -7.80700  0.680 23.80287 ? 21  ARG A CB  1 
ATOM   184  C  CB  B ARG A 1 22  ? -30.66400 6.35000  -7.87200  0.320 24.64587 ? 21  ARG A CB  1 
ATOM   185  C  CG  A ARG A 1 22  ? -31.32600 5.04100  -7.97800  0.680 27.02516 ? 21  ARG A CG  1 
ATOM   186  C  CG  B ARG A 1 22  ? -29.95200 5.35500  -6.98000  0.320 27.79167 ? 21  ARG A CG  1 
ATOM   187  C  CD  A ARG A 1 22  ? -30.34900 3.88400  -8.19100  0.680 34.01139 ? 21  ARG A CD  1 
ATOM   188  C  CD  B ARG A 1 22  ? -29.30400 4.24900  -7.80200  0.320 32.45809 ? 21  ARG A CD  1 
ATOM   189  N  NE  A ARG A 1 22  ? -31.08200 2.74200  -8.72100  0.680 41.07207 ? 21  ARG A NE  1 
ATOM   190  N  NE  B ARG A 1 22  ? -30.17300 3.76600  -8.87300  0.320 35.35064 ? 21  ARG A NE  1 
ATOM   191  C  CZ  A ARG A 1 22  ? -31.26500 2.51300  -10.01600 0.680 40.05615 ? 21  ARG A CZ  1 
ATOM   192  C  CZ  B ARG A 1 22  ? -31.00800 2.73500  -8.76400  0.320 39.94296 ? 21  ARG A CZ  1 
ATOM   193  N  NH1 A ARG A 1 22  ? -31.97300 1.45400  -10.40600 0.680 41.49584 ? 21  ARG A NH1 1 
ATOM   194  N  NH1 B ARG A 1 22  ? -31.75100 2.37200  -9.80100  0.320 39.54351 ? 21  ARG A NH1 1 
ATOM   195  N  NH2 A ARG A 1 22  ? -30.72800 3.33800  -10.91700 0.680 33.02892 ? 21  ARG A NH2 1 
ATOM   196  N  NH2 B ARG A 1 22  ? -31.10800 2.06700  -7.62100  0.320 45.62155 ? 21  ARG A NH2 1 
ATOM   197  N  N   . SER A 1 23  ? -30.32400 9.46500  -7.67400  1.000 22.05196 ? 22  SER A N   1 
ATOM   198  C  CA  . SER A 1 23  ? -29.54500 10.66800 -7.37600  1.000 21.68852 ? 22  SER A CA  1 
ATOM   199  C  C   . SER A 1 23  ? -30.26000 11.58600 -6.38300  1.000 23.80638 ? 22  SER A C   1 
ATOM   200  O  O   . SER A 1 23  ? -29.63300 12.10600 -5.46000  1.000 23.03470 ? 22  SER A O   1 
ATOM   201  C  CB  . SER A 1 23  ? -29.26300 11.41400 -8.67700  1.000 22.25180 ? 22  SER A CB  1 
ATOM   202  O  OG  . SER A 1 23  ? -28.53400 12.61000 -8.42500  1.000 22.85542 ? 22  SER A OG  1 
ATOM   203  N  N   . ALA A 1 24  ? -31.56700 11.83200 -6.58100  1.000 19.63986 ? 23  ALA A N   1 
ATOM   204  C  CA  . ALA A 1 24  ? -32.32300 12.68200 -5.66900  1.000 19.77823 ? 23  ALA A CA  1 
ATOM   205  C  C   . ALA A 1 24  ? -32.22000 12.18800 -4.22500  1.000 21.20281 ? 23  ALA A C   1 
ATOM   206  O  O   . ALA A 1 24  ? -32.11200 12.99000 -3.29400  1.000 22.83040 ? 23  ALA A O   1 
ATOM   207  C  CB  . ALA A 1 24  ? -33.78700 12.74500 -6.12500  1.000 19.98415 ? 23  ALA A CB  1 
ATOM   208  N  N   . GLY A 1 25  ? -32.29900 10.87600 -4.01300  1.000 19.69498 ? 24  GLY A N   1 
ATOM   209  C  CA  . GLY A 1 25  ? -32.28700 10.33600 -2.65200  1.000 22.73988 ? 24  GLY A CA  1 
ATOM   210  C  C   . GLY A 1 25  ? -30.96800 10.49700 -1.92300  1.000 20.03846 ? 24  GLY A C   1 
ATOM   211  O  O   . GLY A 1 25  ? -30.93400 10.27200 -0.70500  1.000 22.36958 ? 24  GLY A O   1 
ATOM   212  N  N   . GLU A 1 26  ? -29.89000 10.89800 -2.62600  1.000 20.40521 ? 25  GLU A N   1 
ATOM   213  C  CA  . GLU A 1 26  ? -28.62200 11.14200 -1.93500  1.000 20.84844 ? 25  GLU A CA  1 
ATOM   214  C  C   . GLU A 1 26  ? -28.75100 12.21200 -0.85700  1.000 21.00014 ? 25  GLU A C   1 
ATOM   215  O  O   . GLU A 1 26  ? -27.93200 12.24400 0.07200   1.000 20.91701 ? 25  GLU A O   1 
ATOM   216  C  CB  . GLU A 1 26  ? -27.51900 11.56000 -2.92000  1.000 21.76551 ? 25  GLU A CB  1 
ATOM   217  C  CG  . GLU A 1 26  ? -27.05300 10.44400 -3.83500  1.000 21.93358 ? 25  GLU A CG  1 
ATOM   218  C  CD  . GLU A 1 26  ? -26.20300 9.43400  -3.10500  1.000 27.92519 ? 25  GLU A CD  1 
ATOM   219  O  OE1 . GLU A 1 26  ? -25.42900 9.84500  -2.21500  1.000 28.70657 ? 25  GLU A OE1 1 
ATOM   220  O  OE2 . GLU A 1 26  ? -26.28200 8.25100  -3.44000  1.000 30.78760 ? 25  GLU A OE2 1 
ATOM   221  N  N   . SER A 1 27  ? -29.77900 13.06800 -0.93900  1.000 23.65262 ? 26  SER A N   1 
ATOM   222  C  CA  . SER A 1 27  ? -29.97500 14.10800 0.07500   1.000 24.64348 ? 26  SER A CA  1 
ATOM   223  C  C   . SER A 1 27  ? -30.24700 13.54300 1.46600   1.000 25.18106 ? 26  SER A C   1 
ATOM   224  O  O   . SER A 1 27  ? -30.09200 14.25400 2.45900   1.000 30.17592 ? 26  SER A O   1 
ATOM   225  C  CB  . SER A 1 27  ? -31.15500 15.01700 -0.32400  1.000 27.57265 ? 26  SER A CB  1 
ATOM   226  O  OG  . SER A 1 27  ? -30.89000 15.64300 -1.57900  1.000 29.88859 ? 26  SER A OG  1 
ATOM   227  N  N   . PHE A 1 28  ? -30.64200 12.28500 1.57000   1.000 18.30821 ? 27  PHE A N   1 
ATOM   228  C  CA  . PHE A 1 28  ? -30.95000 11.71300 2.86900   1.000 20.11087 ? 27  PHE A CA  1 
ATOM   229  C  C   . PHE A 1 28  ? -29.72800 11.16200 3.61100   1.000 19.43701 ? 27  PHE A C   1 
ATOM   230  O  O   . PHE A 1 28  ? -29.84200 10.83100 4.79800   1.000 21.68091 ? 27  PHE A O   1 
ATOM   231  C  CB  . PHE A 1 28  ? -32.01700 10.59400 2.69500   1.000 21.94888 ? 27  PHE A CB  1 
ATOM   232  C  CG  . PHE A 1 28  ? -33.42700 11.11300 2.41900   1.000 20.43197 ? 27  PHE A CG  1 
ATOM   233  C  CD1 . PHE A 1 28  ? -34.29800 11.40400 3.45100   1.000 24.01942 ? 27  PHE A CD1 1 
ATOM   234  C  CD2 . PHE A 1 28  ? -33.84200 11.34900 1.11200   1.000 26.14728 ? 27  PHE A CD2 1 
ATOM   235  C  CE1 . PHE A 1 28  ? -35.58500 11.89200 3.20400   1.000 26.74092 ? 27  PHE A CE1 1 
ATOM   236  C  CE2 . PHE A 1 28  ? -35.14500 11.83800 0.84900   1.000 23.69046 ? 27  PHE A CE2 1 
ATOM   237  C  CZ  . PHE A 1 28  ? -35.99400 12.11900 1.88300   1.000 25.20251 ? 27  PHE A CZ  1 
ATOM   238  N  N   . ARG A 1 29  ? -28.55500 11.09400 2.98300   1.000 22.68892 ? 28  ARG A N   1 
ATOM   239  C  CA  . ARG A 1 29  ? -27.42300 10.49400 3.69000   1.000 20.81802 ? 28  ARG A CA  1 
ATOM   240  C  C   . ARG A 1 29  ? -26.97900 11.31000 4.90900   1.000 21.00108 ? 28  ARG A C   1 
ATOM   241  O  O   . ARG A 1 29  ? -26.37200 10.73900 5.81300   1.000 23.59577 ? 28  ARG A O   1 
ATOM   242  C  CB  . ARG A 1 29  ? -26.21600 10.31600 2.76600   1.000 24.85807 ? 28  ARG A CB  1 
ATOM   243  C  CG  . ARG A 1 29  ? -26.44600 9.36800  1.62400   1.000 21.73750 ? 28  ARG A CG  1 
ATOM   244  C  CD  . ARG A 1 29  ? -25.11400 8.89000  1.02200   1.000 21.89941 ? 28  ARG A CD  1 
ATOM   245  N  NE  . ARG A 1 29  ? -25.42900 8.11200  -0.16500  1.000 23.50589 ? 28  ARG A NE  1 
ATOM   246  C  CZ  . ARG A 1 29  ? -25.80400 6.82000  -0.16400  1.000 22.44506 ? 28  ARG A CZ  1 
ATOM   247  N  NH1 . ARG A 1 29  ? -25.85100 6.07500  0.95900   1.000 26.09835 ? 28  ARG A NH1 1 
ATOM   248  N  NH2 . ARG A 1 29  ? -26.13300 6.24600  -1.31600  1.000 24.03895 ? 28  ARG A NH2 1 
ATOM   249  N  N   . LEU A 1 30  ? -27.26200 12.61700 4.95100   1.000 22.21461 ? 29  LEU A N   1 
ATOM   250  C  CA  . LEU A 1 30  ? -26.87100 13.43300 6.09200   1.000 22.74482 ? 29  LEU A CA  1 
ATOM   251  C  C   . LEU A 1 30  ? -28.00200 13.63500 7.10500   1.000 24.60474 ? 29  LEU A C   1 
ATOM   252  O  O   . LEU A 1 30  ? -27.88200 14.48300 7.99900   1.000 26.37441 ? 29  LEU A O   1 
ATOM   253  C  CB  . LEU A 1 30  ? -26.29700 14.77400 5.60000   1.000 32.68572 ? 29  LEU A CB  1 
ATOM   254  C  CG  . LEU A 1 30  ? -24.91800 14.55700 4.94300   1.000 34.32022 ? 29  LEU A CG  1 
ATOM   255  C  CD1 . LEU A 1 30  ? -24.17400 15.86800 4.70800   1.000 38.16211 ? 29  LEU A CD1 1 
ATOM   256  C  CD2 . LEU A 1 30  ? -24.06500 13.64400 5.78500   1.000 41.43485 ? 29  LEU A CD2 1 
ATOM   257  N  N   . LEU A 1 31  ? -29.07900 12.83200 7.01500   1.000 22.74576 ? 30  LEU A N   1 
ATOM   258  C  CA  . LEU A 1 31  ? -30.07600 12.69200 8.07300   1.000 24.43287 ? 30  LEU A CA  1 
ATOM   259  C  C   . LEU A 1 31  ? -29.89200 11.33200 8.73700   1.000 23.43309 ? 30  LEU A C   1 
ATOM   260  O  O   . LEU A 1 31  ? -30.33300 10.32200 8.18000   1.000 25.91509 ? 30  LEU A O   1 
ATOM   261  C  CB  . LEU A 1 31  ? -31.49300 12.79900 7.50400   1.000 27.51112 ? 30  LEU A CB  1 
ATOM   262  C  CG  . LEU A 1 31  ? -31.87800 14.03500 6.68800   1.000 30.11585 ? 30  LEU A CG  1 
ATOM   263  C  CD1 . LEU A 1 31  ? -33.33900 13.96700 6.28100   1.000 28.37057 ? 30  LEU A CD1 1 
ATOM   264  C  CD2 . LEU A 1 31  ? -31.66800 15.25800 7.48700   1.000 35.68692 ? 30  LEU A CD2 1 
ATOM   265  N  N   . PRO A 1 32  ? -29.30100 11.26000 9.92400   1.000 25.46954 ? 31  PRO A N   1 
ATOM   266  C  CA  . PRO A 1 32  ? -28.93200 9.94700  10.48400  1.000 29.02189 ? 31  PRO A CA  1 
ATOM   267  C  C   . PRO A 1 32  ? -30.08900 8.96000  10.59100  1.000 34.13273 ? 31  PRO A C   1 
ATOM   268  O  O   . PRO A 1 32  ? -29.90400 7.79400  10.24300  1.000 34.15175 ? 31  PRO A O   1 
ATOM   269  C  CB  . PRO A 1 32  ? -28.35500 10.32100 11.85200  1.000 30.54505 ? 31  PRO A CB  1 
ATOM   270  C  CG  . PRO A 1 32  ? -27.73800 11.68300 11.60500  1.000 28.73412 ? 31  PRO A CG  1 
ATOM   271  C  CD  . PRO A 1 32  ? -28.70600 12.37200 10.68200  1.000 26.69348 ? 31  PRO A CD  1 
ATOM   272  N  N   . GLU A 1 33  ? -31.27800 9.39500  11.01400  1.000 31.06372 ? 32  GLU A N   1 
ATOM   273  C  CA  . GLU A 1 33  ? -32.41000 8.47800  11.16100  1.000 35.27525 ? 32  GLU A CA  1 
ATOM   274  C  C   . GLU A 1 33  ? -32.94000 7.97600  9.82300   1.000 31.68331 ? 32  GLU A C   1 
ATOM   275  O  O   . GLU A 1 33  ? -33.54100 6.89300  9.76400   1.000 33.24909 ? 32  GLU A O   1 
ATOM   276  C  CB  . GLU A 1 33  ? -33.54000 9.16800  11.92800  1.000 36.37419 ? 32  GLU A CB  1 
ATOM   277  C  CG  . GLU A 1 33  ? -33.18600 9.50400  13.37200  1.000 53.98441 ? 32  GLU A CG  1 
ATOM   278  C  CD  . GLU A 1 33  ? -34.31900 10.20400 14.12000  1.000 69.57644 ? 32  GLU A CD  1 
ATOM   279  O  OE1 . GLU A 1 33  ? -34.03200 10.94400 15.09000  1.000 73.88955 ? 32  GLU A OE1 1 
ATOM   280  O  OE2 . GLU A 1 33  ? -35.49700 10.01100 13.74200  1.000 70.65080 ? 32  GLU A OE2 1 
ATOM   281  N  N   . LEU A 1 34  ? -32.74000 8.73400  8.74900   1.000 26.76233 ? 33  LEU A N   1 
ATOM   282  C  CA  . LEU A 1 34  ? -33.29900 8.38400  7.45700   1.000 23.98473 ? 33  LEU A CA  1 
ATOM   283  C  C   . LEU A 1 34  ? -32.24600 8.04900  6.40600   1.000 26.18341 ? 33  LEU A C   1 
ATOM   284  O  O   . LEU A 1 34  ? -32.58800 7.96400  5.21000   1.000 25.52983 ? 33  LEU A O   1 
ATOM   285  C  CB  . LEU A 1 34  ? -34.20400 9.51700  6.95000   1.000 27.11212 ? 33  LEU A CB  1 
ATOM   286  C  CG  . LEU A 1 34  ? -35.33100 9.88900  7.91800   1.000 29.37051 ? 33  LEU A CG  1 
ATOM   287  C  CD1 . LEU A 1 34  ? -36.19100 11.02600 7.35500   1.000 31.65575 ? 33  LEU A CD1 1 
ATOM   288  C  CD2 . LEU A 1 34  ? -36.21200 8.68200  8.23500   1.000 30.68421 ? 33  LEU A CD2 1 
ATOM   289  N  N   . ALA A 1 35  ? -30.97700 7.85200  6.80300   1.000 27.24455 ? 34  ALA A N   1 
ATOM   290  C  CA  . ALA A 1 35  ? -29.94100 7.68800  5.79000   1.000 25.65497 ? 34  ALA A CA  1 
ATOM   291  C  C   . ALA A 1 35  ? -30.18100 6.44600  4.95400   1.000 28.13205 ? 34  ALA A C   1 
ATOM   292  O  O   . ALA A 1 35  ? -29.78800 6.40500  3.78100   1.000 24.96872 ? 34  ALA A O   1 
ATOM   293  C  CB  . ALA A 1 35  ? -28.56100 7.63900  6.42600   1.000 26.18392 ? 34  ALA A CB  1 
ATOM   294  N  N   . TRP A 1 36  ? -30.83700 5.43500  5.53100   1.000 28.72203 ? 35  TRP A N   1 
ATOM   295  C  CA  . TRP A 1 36  ? -31.17100 4.24900  4.75200   1.000 28.78959 ? 35  TRP A CA  1 
ATOM   296  C  C   . TRP A 1 36  ? -31.97600 4.55500  3.49600   1.000 28.59477 ? 35  TRP A C   1 
ATOM   297  O  O   . TRP A 1 36  ? -31.95600 3.74300  2.55500   1.000 29.01175 ? 35  TRP A O   1 
ATOM   298  C  CB  . TRP A 1 36  ? -31.92500 3.24300  5.64400   1.000 28.81605 ? 35  TRP A CB  1 
ATOM   299  C  CG  . TRP A 1 36  ? -33.32400 3.64900  6.05800   1.000 26.03884 ? 35  TRP A CG  1 
ATOM   300  C  CD1 . TRP A 1 36  ? -33.68400 4.33500  7.19200   1.000 30.31887 ? 35  TRP A CD1 1 
ATOM   301  C  CD2 . TRP A 1 36  ? -34.54200 3.35800  5.36100   1.000 28.45633 ? 35  TRP A CD2 1 
ATOM   302  N  NE1 . TRP A 1 36  ? -35.05000 4.49800  7.22600   1.000 35.37928 ? 35  TRP A NE1 1 
ATOM   303  C  CE2 . TRP A 1 36  ? -35.59900 3.90700  6.11600   1.000 31.09502 ? 35  TRP A CE2 1 
ATOM   304  C  CE3 . TRP A 1 36  ? -34.83900 2.69700  4.16400   1.000 28.34115 ? 35  TRP A CE3 1 
ATOM   305  C  CZ2 . TRP A 1 36  ? -36.93300 3.81200  5.71300   1.000 36.87541 ? 35  TRP A CZ2 1 
ATOM   306  C  CZ3 . TRP A 1 36  ? -36.16200 2.60800  3.76100   1.000 32.36260 ? 35  TRP A CZ3 1 
ATOM   307  C  CH2 . TRP A 1 36  ? -37.19700 3.15200  4.54600   1.000 34.17168 ? 35  TRP A CH2 1 
ATOM   308  N  N   . ILE A 1 37  ? -32.70300 5.67900  3.46200   1.000 25.50665 ? 36  ILE A N   1 
ATOM   309  C  CA  . ILE A 1 37  ? -33.55100 5.99300  2.30700   1.000 28.84148 ? 36  ILE A CA  1 
ATOM   310  C  C   . ILE A 1 37  ? -32.70600 6.09000  1.04500   1.000 26.74655 ? 36  ILE A C   1 
ATOM   311  O  O   . ILE A 1 37  ? -33.16100 5.73100  -0.04800  1.000 27.81139 ? 36  ILE A O   1 
ATOM   312  C  CB  . ILE A 1 37  ? -34.33000 7.30900  2.54700   1.000 27.33486 ? 36  ILE A CB  1 
ATOM   313  C  CG1 . ILE A 1 37  ? -35.35600 7.19500  3.68600   1.000 29.97750 ? 36  ILE A CG1 1 
ATOM   314  C  CG2 . ILE A 1 37  ? -35.03400 7.78400  1.26300   1.000 31.14309 ? 36  ILE A CG2 1 
ATOM   315  C  CD1 . ILE A 1 37  ? -36.60700 6.45900  3.33000   1.000 34.32932 ? 36  ILE A CD1 1 
ATOM   316  N  N   . ALA A 1 38  ? -31.45300 6.55400  1.17700   1.000 23.38748 ? 37  ALA A N   1 
ATOM   317  C  CA  . ALA A 1 38  ? -30.61700 6.78200  0.00700   1.000 25.83431 ? 37  ALA A CA  1 
ATOM   318  C  C   . ALA A 1 38  ? -30.32700 5.51900  -0.77700  1.000 24.66013 ? 37  ALA A C   1 
ATOM   319  O  O   . ALA A 1 38  ? -30.01200 5.60300  -1.97000  1.000 27.09154 ? 37  ALA A O   1 
ATOM   320  C  CB  . ALA A 1 38  ? -29.29900 7.43100  0.42600   1.000 24.13691 ? 37  ALA A CB  1 
ATOM   321  N  N   . ASP A 1 39  ? -30.43500 4.34800  -0.14300  1.000 26.02472 ? 38  ASP A N   1 
ATOM   322  C  CA  . ASP A 1 39  ? -30.21200 3.07400  -0.80300  1.000 28.42292 ? 38  ASP A CA  1 
ATOM   323  C  C   . ASP A 1 39  ? -31.48700 2.23500  -0.84800  1.000 30.21280 ? 38  ASP A C   1 
ATOM   324  O  O   . ASP A 1 39  ? -31.42100 1.04300  -1.13800  1.000 37.13603 ? 38  ASP A O   1 
ATOM   325  C  CB  . ASP A 1 39  ? -29.05100 2.34900  -0.12000  1.000 31.20203 ? 38  ASP A CB  1 
ATOM   326  C  CG  . ASP A 1 39  ? -27.73800 3.14900  -0.21900  1.000 33.15153 ? 38  ASP A CG  1 
ATOM   327  O  OD1 . ASP A 1 39  ? -27.36100 3.53200  -1.35000  1.000 31.40355 ? 38  ASP A OD1 1 
ATOM   328  O  OD2 . ASP A 1 39  ? -27.10200 3.39200  0.82200   1.000 31.50472 ? 38  ASP A OD2 1 
ATOM   329  N  N   . ALA A 1 40  ? -32.64200 2.85500  -0.60200  1.000 35.37338 ? 39  ALA A N   1 
ATOM   330  C  CA  . ALA A 1 40  ? -33.93900 2.22300  -0.78900  1.000 41.53364 ? 39  ALA A CA  1 
ATOM   331  C  C   . ALA A 1 40  ? -34.23500 2.05900  -2.28100  1.000 29.70852 ? 39  ALA A C   1 
ATOM   332  O  O   . ALA A 1 40  ? -33.57800 2.63600  -3.15400  1.000 34.85878 ? 39  ALA A O   1 
ATOM   333  C  CB  . ALA A 1 40  ? -35.03400 3.05300  -0.11800  1.000 41.14634 ? 39  ALA A CB  1 
ATOM   334  N  N   . GLY A 1 41  ? -35.26700 1.29200  -2.58000  1.000 35.86109 ? 40  GLY A N   1 
ATOM   335  C  CA  . GLY A 1 41  ? -35.60100 1.06200  -3.96800  1.000 29.49311 ? 40  GLY A CA  1 
ATOM   336  C  C   . GLY A 1 41  ? -36.06800 2.33300  -4.64000  1.000 27.57205 ? 40  GLY A C   1 
ATOM   337  O  O   . GLY A 1 41  ? -36.36800 3.32300  -3.97500  1.000 29.05835 ? 40  GLY A O   1 
ATOM   338  N  N   . VAL A 1 42  ? -36.04800 2.30400  -5.96900  1.000 24.25969 ? 41  VAL A N   1 
ATOM   339  C  CA  . VAL A 1 42  ? -36.66900 3.34200  -6.78000  1.000 22.84565 ? 41  VAL A CA  1 
ATOM   340  C  C   . VAL A 1 42  ? -37.58800 2.66200  -7.78200  1.000 25.45913 ? 41  VAL A C   1 
ATOM   341  O  O   . VAL A 1 42  ? -37.43500 1.47800  -8.10200  1.000 30.08319 ? 41  VAL A O   1 
ATOM   342  C  CB  . VAL A 1 42  ? -35.64600 4.25100  -7.50700  1.000 24.82616 ? 41  VAL A CB  1 
ATOM   343  C  CG1 . VAL A 1 42  ? -34.68900 4.89200  -6.49600  1.000 26.16868 ? 41  VAL A CG1 1 
ATOM   344  C  CG2 . VAL A 1 42  ? -34.91300 3.49300  -8.58900  1.000 28.91429 ? 41  VAL A CG2 1 
ATOM   345  N  N   . ALA A 1 43  ? -38.57700 3.41400  -8.26700  1.000 24.43122 ? 42  ALA A N   1 
ATOM   346  C  CA  . ALA A 1 43  ? -39.54200 2.81700  -9.18000  1.000 31.72584 ? 42  ALA A CA  1 
ATOM   347  C  C   . ALA A 1 43  ? -38.86200 2.33800  -10.46500 1.000 28.88132 ? 42  ALA A C   1 
ATOM   348  O  O   . ALA A 1 43  ? -37.93600 2.97400  -10.98600 1.000 29.34178 ? 42  ALA A O   1 
ATOM   349  C  CB  . ALA A 1 43  ? -40.65200 3.81500  -9.51800  1.000 29.24159 ? 42  ALA A CB  1 
ATOM   350  N  N   . GLY A 1 44  ? -39.34600 1.24300  -10.98700 1.000 29.07853 ? 43  GLY A N   1 
ATOM   351  C  CA  . GLY A 1 44  ? -38.82300 0.73300  -12.23600 1.000 33.96395 ? 43  GLY A CA  1 
ATOM   352  C  C   . GLY A 1 44  ? -39.46100 1.37100  -13.45900 1.000 35.60189 ? 43  GLY A C   1 
ATOM   353  O  O   . GLY A 1 44  ? -40.37800 2.18300  -13.37100 1.000 30.09970 ? 43  GLY A O   1 
ATOM   354  N  N   . VAL A 1 45  ? -38.96000 0.97700  -14.63200 1.000 29.55283 ? 44  VAL A N   1 
ATOM   355  C  CA  . VAL A 1 45  ? -39.42100 1.61400  -15.86400 1.000 26.37633 ? 44  VAL A CA  1 
ATOM   356  C  C   . VAL A 1 45  ? -40.88100 1.30400  -16.17500 1.000 28.35625 ? 44  VAL A C   1 
ATOM   357  O  O   . VAL A 1 45  ? -41.56200 2.13700  -16.80000 1.000 31.82263 ? 44  VAL A O   1 
ATOM   358  C  CB  . VAL A 1 45  ? -38.52000 1.25600  -17.06800 1.000 34.05518 ? 44  VAL A CB  1 
ATOM   359  C  CG1 . VAL A 1 45  ? -37.08000 1.70300  -16.82900 1.000 35.50719 ? 44  VAL A CG1 1 
ATOM   360  C  CG2 . VAL A 1 45  ? -38.59400 -0.22600 -17.40900 1.000 35.70143 ? 44  VAL A CG2 1 
ATOM   361  N  N   A ASP A 1 46  ? -41.37700 0.12300  -15.75400 0.700 32.65134 ? 45  ASP A N   1 
ATOM   362  N  N   B ASP A 1 46  ? -41.40500 0.15000  -15.76900 0.300 31.76608 ? 45  ASP A N   1 
ATOM   363  C  CA  A ASP A 1 46  ? -42.77500 -0.25700 -15.97900 0.700 30.26392 ? 45  ASP A CA  1 
ATOM   364  C  CA  B ASP A 1 46  ? -42.79200 -0.12800 -16.12800 0.300 31.83973 ? 45  ASP A CA  1 
ATOM   365  C  C   A ASP A 1 46  ? -43.72600 0.74500  -15.33400 0.700 30.82008 ? 45  ASP A C   1 
ATOM   366  C  C   B ASP A 1 46  ? -43.78300 0.70500  -15.31500 0.300 30.28879 ? 45  ASP A C   1 
ATOM   367  O  O   A ASP A 1 46  ? -44.73600 1.14200  -15.92800 0.700 29.26432 ? 45  ASP A O   1 
ATOM   368  O  O   B ASP A 1 46  ? -44.90600 0.93000  -15.78000 0.300 30.00106 ? 45  ASP A O   1 
ATOM   369  C  CB  A ASP A 1 46  ? -43.03400 -1.70000 -15.47200 0.700 33.38068 ? 45  ASP A CB  1 
ATOM   370  C  CB  B ASP A 1 46  ? -43.07600 -1.62500 -16.00700 0.300 32.75961 ? 45  ASP A CB  1 
ATOM   371  C  CG  A ASP A 1 46  ? -42.97400 -1.86300 -13.90500 0.700 38.39462 ? 45  ASP A CG  1 
ATOM   372  C  CG  B ASP A 1 46  ? -42.28300 -2.44500 -17.02100 0.300 34.04545 ? 45  ASP A CG  1 
ATOM   373  O  OD1 A ASP A 1 46  ? -42.25700 -1.11600 -13.18500 0.700 35.57215 ? 45  ASP A OD1 1 
ATOM   374  O  OD1 B ASP A 1 46  ? -41.39500 -3.21300 -16.60800 0.300 29.84586 ? 45  ASP A OD1 1 
ATOM   375  O  OD2 A ASP A 1 46  ? -43.67100 -2.76700 -13.37700 0.700 37.65429 ? 45  ASP A OD2 1 
ATOM   376  O  OD2 B ASP A 1 46  ? -42.52700 -2.28800 -18.23900 0.300 32.63054 ? 45  ASP A OD2 1 
ATOM   377  N  N   . PHE A 1 47  ? -43.39300 1.19000  -14.13100 1.000 27.07416 ? 46  PHE A N   1 
ATOM   378  C  CA  . PHE A 1 47  ? -44.22900 2.14200  -13.41400 1.000 27.92322 ? 46  PHE A CA  1 
ATOM   379  C  C   . PHE A 1 47  ? -44.31700 3.45800  -14.16800 1.000 25.74783 ? 46  PHE A C   1 
ATOM   380  O  O   . PHE A 1 47  ? -45.40500 4.01600  -14.36900 1.000 26.30639 ? 46  PHE A O   1 
ATOM   381  C  CB  . PHE A 1 47  ? -43.63600 2.35200  -12.03000 1.000 28.68339 ? 46  PHE A CB  1 
ATOM   382  C  CG  . PHE A 1 47  ? -44.25500 3.45700  -11.26700 1.000 27.07349 ? 46  PHE A CG  1 
ATOM   383  C  CD1 . PHE A 1 47  ? -45.47900 3.28100  -10.65200 1.000 31.96486 ? 46  PHE A CD1 1 
ATOM   384  C  CD2 . PHE A 1 47  ? -43.59900 4.65300  -11.13500 1.000 30.82681 ? 46  PHE A CD2 1 
ATOM   385  C  CE1 . PHE A 1 47  ? -46.05700 4.31900  -9.92400  1.000 37.28728 ? 46  PHE A CE1 1 
ATOM   386  C  CE2 . PHE A 1 47  ? -44.18600 5.69300  -10.40500 1.000 34.81295 ? 46  PHE A CE2 1 
ATOM   387  C  CZ  . PHE A 1 47  ? -45.40900 5.49300  -9.80800  1.000 31.34351 ? 46  PHE A CZ  1 
ATOM   388  N  N   . HIS A 1 48  ? -43.17200 3.95700  -14.60500 1.000 26.11020 ? 47  HIS A N   1 
ATOM   389  C  CA  . HIS A 1 48  ? -43.12600 5.21200  -15.33900 1.000 23.96013 ? 47  HIS A CA  1 
ATOM   390  C  C   . HIS A 1 48  ? -43.87900 5.13100  -16.65900 1.000 23.55823 ? 47  HIS A C   1 
ATOM   391  O  O   . HIS A 1 48  ? -44.63700 6.02500  -16.99900 1.000 24.10020 ? 47  HIS A O   1 
ATOM   392  C  CB  . HIS A 1 48  ? -41.68300 5.63800  -15.58400 1.000 29.89498 ? 47  HIS A CB  1 
ATOM   393  C  CG  . HIS A 1 48  ? -40.94600 6.01800  -14.34000 1.000 24.21378 ? 47  HIS A CG  1 
ATOM   394  N  ND1 . HIS A 1 48  ? -41.28700 7.11400  -13.58200 1.000 24.59976 ? 47  HIS A ND1 1 
ATOM   395  C  CD2 . HIS A 1 48  ? -39.87800 5.45600  -13.73000 1.000 25.04940 ? 47  HIS A CD2 1 
ATOM   396  C  CE1 . HIS A 1 48  ? -40.46600 7.20700  -12.55300 1.000 25.33285 ? 47  HIS A CE1 1 
ATOM   397  N  NE2 . HIS A 1 48  ? -39.60000 6.21400  -12.62000 1.000 26.17675 ? 47  HIS A NE2 1 
ATOM   398  N  N   . ARG A 1 49  ? -43.66700 4.04700  -17.39400 1.000 24.84099 ? 48  ARG A N   1 
ATOM   399  C  CA  . ARG A 1 49  ? -44.35000 3.85800  -18.66100 1.000 26.39835 ? 48  ARG A CA  1 
ATOM   400  C  C   . ARG A 1 49  ? -45.85100 3.77600  -18.43400 1.000 27.67660 ? 48  ARG A C   1 
ATOM   401  O  O   . ARG A 1 49  ? -46.62300 4.34700  -19.19500 1.000 30.40219 ? 48  ARG A O   1 
ATOM   402  C  CB  . ARG A 1 49  ? -43.86000 2.59300  -19.36500 1.000 28.59449 ? 48  ARG A CB  1 
ATOM   403  C  CG  . ARG A 1 49  ? -42.50200 2.72200  -20.02100 1.000 30.43230 ? 48  ARG A CG  1 
ATOM   404  C  CD  . ARG A 1 49  ? -42.12800 1.44100  -20.75200 1.000 35.23053 ? 48  ARG A CD  1 
ATOM   405  N  NE  . ARG A 1 49  ? -40.89900 1.58100  -21.52100 1.000 35.80256 ? 48  ARG A NE  1 
ATOM   406  C  CZ  . ARG A 1 49  ? -40.86200 1.88000  -22.81300 1.000 41.48729 ? 48  ARG A CZ  1 
ATOM   407  N  NH1 . ARG A 1 49  ? -41.98600 2.06600  -23.48000 1.000 38.27645 ? 48  ARG A NH1 1 
ATOM   408  N  NH2 . ARG A 1 49  ? -39.70300 1.98600  -23.43900 1.000 47.54529 ? 48  ARG A NH2 1 
ATOM   409  N  N   A ARG A 1 50  ? -46.29200 3.19000  -17.33700 0.760 28.04312 ? 49  ARG A N   1 
ATOM   410  N  N   B ARG A 1 50  ? -46.29100 3.20000  -17.32500 0.240 28.01543 ? 49  ARG A N   1 
ATOM   411  C  CA  A ARG A 1 50  ? -47.72900 3.11300  -17.10400 0.760 28.32306 ? 49  ARG A CA  1 
ATOM   412  C  CA  B ARG A 1 50  ? -47.73200 3.12000  -17.10500 0.240 30.06514 ? 49  ARG A CA  1 
ATOM   413  C  C   A ARG A 1 50  ? -48.37600 4.49400  -16.94400 0.760 27.93426 ? 49  ARG A C   1 
ATOM   414  C  C   B ARG A 1 50  ? -48.38100 4.49500  -16.94100 0.240 28.48284 ? 49  ARG A C   1 
ATOM   415  O  O   A ARG A 1 50  ? -49.41000 4.76600  -17.53900 0.760 29.66142 ? 49  ARG A O   1 
ATOM   416  O  O   B ARG A 1 50  ? -49.42700 4.76200  -17.52500 0.240 30.22601 ? 49  ARG A O   1 
ATOM   417  C  CB  A ARG A 1 50  ? -48.03900 2.24400  -15.88500 0.760 31.82635 ? 49  ARG A CB  1 
ATOM   418  C  CB  B ARG A 1 50  ? -48.08300 2.23500  -15.90900 0.240 33.27237 ? 49  ARG A CB  1 
ATOM   419  C  CG  A ARG A 1 50  ? -49.51700 2.14300  -15.55500 0.760 39.19525 ? 49  ARG A CG  1 
ATOM   420  C  CG  B ARG A 1 50  ? -49.56700 1.91100  -15.84300 0.240 40.57308 ? 49  ARG A CG  1 
ATOM   421  C  CD  A ARG A 1 50  ? -49.78800 1.08400  -14.49700 0.760 43.83505 ? 49  ARG A CD  1 
ATOM   422  C  CD  B ARG A 1 50  ? -49.92900 1.01300  -14.67200 0.240 44.08464 ? 49  ARG A CD  1 
ATOM   423  N  NE  A ARG A 1 50  ? -49.36900 1.49200  -13.16100 0.760 44.60353 ? 49  ARG A NE  1 
ATOM   424  N  NE  B ARG A 1 50  ? -50.33100 1.77600  -13.49700 0.240 45.65473 ? 49  ARG A NE  1 
ATOM   425  C  CZ  A ARG A 1 50  ? -50.12800 2.19100  -12.32600 0.760 43.45163 ? 49  ARG A CZ  1 
ATOM   426  C  CZ  B ARG A 1 50  ? -49.61500 1.86000  -12.38400 0.240 43.95533 ? 49  ARG A CZ  1 
ATOM   427  N  NH1 A ARG A 1 50  ? -49.67700 2.52000  -11.13000 0.760 41.51693 ? 49  ARG A NH1 1 
ATOM   428  N  NH1 B ARG A 1 50  ? -50.05500 2.57700  -11.36200 0.240 41.46441 ? 49  ARG A NH1 1 
ATOM   429  N  NH2 A ARG A 1 50  ? -51.34200 2.56200  -12.69300 0.760 44.71428 ? 49  ARG A NH2 1 
ATOM   430  N  NH2 B ARG A 1 50  ? -48.46100 1.21800  -12.29300 0.240 43.86447 ? 49  ARG A NH2 1 
ATOM   431  N  N   . LEU A 1 51  ? -47.68100 5.40900  -16.27900 1.000 27.45688 ? 50  LEU A N   1 
ATOM   432  C  CA  . LEU A 1 51  ? -48.21900 6.74300  -16.04300 1.000 26.77299 ? 50  LEU A CA  1 
ATOM   433  C  C   . LEU A 1 51  ? -47.98200 7.65900  -17.24000 1.000 27.75830 ? 50  LEU A C   1 
ATOM   434  O  O   . LEU A 1 51  ? -48.82100 8.52000  -17.52600 1.000 26.97891 ? 50  LEU A O   1 
ATOM   435  C  CB  . LEU A 1 51  ? -47.64400 7.35300  -14.75000 1.000 23.42789 ? 50  LEU A CB  1 
ATOM   436  C  CG  . LEU A 1 51  ? -47.93600 6.50300  -13.50800 1.000 24.67910 ? 50  LEU A CG  1 
ATOM   437  C  CD1 . LEU A 1 51  ? -47.32900 7.16800  -12.26500 1.000 27.52244 ? 50  LEU A CD1 1 
ATOM   438  C  CD2 . LEU A 1 51  ? -49.41600 6.23000  -13.31900 1.000 29.63507 ? 50  LEU A CD2 1 
ATOM   439  N  N   . ILE A 1 52  ? -46.88200 7.46100  -17.97200 1.000 27.20272 ? 51  ILE A N   1 
ATOM   440  C  CA  . ILE A 1 52  ? -46.66700 8.21300  -19.20800 1.000 30.29193 ? 51  ILE A CA  1 
ATOM   441  C  C   . ILE A 1 52  ? -47.79100 7.94000  -20.21000 1.000 33.18090 ? 51  ILE A C   1 
ATOM   442  O  O   . ILE A 1 52  ? -48.24600 8.85200  -20.91900 1.000 34.43300 ? 51  ILE A O   1 
ATOM   443  C  CB  . ILE A 1 52  ? -45.28000 7.88200  -19.79300 1.000 32.11320 ? 51  ILE A CB  1 
ATOM   444  C  CG1 . ILE A 1 52  ? -44.17900 8.51500  -18.93800 1.000 25.94993 ? 51  ILE A CG1 1 
ATOM   445  C  CG2 . ILE A 1 52  ? -45.17700 8.37300  -21.26700 1.000 32.12476 ? 51  ILE A CG2 1 
ATOM   446  C  CD1 . ILE A 1 52  ? -42.78000 7.91400  -19.15300 1.000 26.74102 ? 51  ILE A CD1 1 
ATOM   447  N  N   A GLU A 1 53  ? -48.25900 6.68700  -20.28700 0.550 32.75476 ? 52  GLU A N   1 
ATOM   448  N  N   B GLU A 1 53  ? -48.26000 6.68600  -20.28000 0.450 32.81437 ? 52  GLU A N   1 
ATOM   449  C  CA  A GLU A 1 53  ? -49.36800 6.37000  -21.18500 0.550 35.47301 ? 52  GLU A CA  1 
ATOM   450  C  CA  B GLU A 1 53  ? -49.36900 6.35400  -21.17400 0.450 35.73654 ? 52  GLU A CA  1 
ATOM   451  C  C   A GLU A 1 53  ? -50.64100 7.10400  -20.77600 0.550 37.91940 ? 52  GLU A C   1 
ATOM   452  C  C   B GLU A 1 53  ? -50.64800 7.07500  -20.77000 0.450 37.87936 ? 52  GLU A C   1 
ATOM   453  O  O   A GLU A 1 53  ? -51.43000 7.52000  -21.63300 0.550 43.88418 ? 52  GLU A O   1 
ATOM   454  O  O   B GLU A 1 53  ? -51.45400 7.44100  -21.63300 0.450 43.43920 ? 52  GLU A O   1 
ATOM   455  C  CB  A GLU A 1 53  ? -49.60700 4.85900  -21.22100 0.550 38.16231 ? 52  GLU A CB  1 
ATOM   456  C  CB  B GLU A 1 53  ? -49.60100 4.84100  -21.19400 0.450 38.35025 ? 52  GLU A CB  1 
ATOM   457  C  CG  A GLU A 1 53  ? -50.91400 4.44500  -21.91000 0.550 46.02133 ? 52  GLU A CG  1 
ATOM   458  C  CG  B GLU A 1 53  ? -50.42800 4.33800  -22.38500 0.450 46.71138 ? 52  GLU A CG  1 
ATOM   459  C  CD  A GLU A 1 53  ? -50.81400 4.36200  -23.43300 0.550 50.41472 ? 52  GLU A CD  1 
ATOM   460  C  CD  B GLU A 1 53  ? -51.93700 4.42800  -22.17700 0.450 51.13797 ? 52  GLU A CD  1 
ATOM   461  O  OE1 A GLU A 1 53  ? -49.89900 4.97500  -24.01900 0.550 49.71547 ? 52  GLU A OE1 1 
ATOM   462  O  OE1 B GLU A 1 53  ? -52.65100 4.80500  -23.13500 0.450 53.76727 ? 52  GLU A OE1 1 
ATOM   463  O  OE2 A GLU A 1 53  ? -51.65900 3.67100  -24.04600 0.550 54.56197 ? 52  GLU A OE2 1 
ATOM   464  O  OE2 B GLU A 1 53  ? -52.41600 4.10600  -21.06800 0.450 48.16878 ? 52  GLU A OE2 1 
ATOM   465  N  N   . ARG A 1 54  ? -50.84900 7.29100  -19.46800 1.000 34.30579 ? 53  ARG A N   1 
ATOM   466  C  CA  . ARG A 1 54  ? -51.98700 8.06500  -18.99100 1.000 33.55362 ? 53  ARG A CA  1 
ATOM   467  C  C   . ARG A 1 54  ? -51.81300 9.56300  -19.21500 1.000 37.31944 ? 53  ARG A C   1 
ATOM   468  O  O   . ARG A 1 54  ? -52.80600 10.29400 -19.20400 1.000 35.86011 ? 53  ARG A O   1 
ATOM   469  C  CB  . ARG A 1 54  ? -52.21400 7.79900  -17.50500 1.000 38.40018 ? 53  ARG A CB  1 
ATOM   470  C  CG  . ARG A 1 54  ? -52.43500 6.31500  -17.15700 1.000 45.51039 ? 53  ARG A CG  1 
ATOM   471  C  CD  . ARG A 1 54  ? -53.11900 6.17500  -15.79900 1.000 49.61215 ? 53  ARG A CD  1 
ATOM   472  N  NE  . ARG A 1 54  ? -54.55200 6.44900  -15.91500 1.000 59.12306 ? 53  ARG A NE  1 
ATOM   473  C  CZ  . ARG A 1 54  ? -55.37800 6.59900  -14.88400 1.000 54.95906 ? 53  ARG A CZ  1 
ATOM   474  N  NH1 . ARG A 1 54  ? -56.66500 6.84000  -15.09000 1.000 61.56206 ? 53  ARG A NH1 1 
ATOM   475  N  NH2 . ARG A 1 54  ? -54.91100 6.51300  -13.64900 1.000 48.11135 ? 53  ARG A NH2 1 
ATOM   476  N  N   . GLY A 1 55  ? -50.58700 10.03100 -19.42100 1.000 34.55147 ? 54  GLY A N   1 
ATOM   477  C  CA  . GLY A 1 55  ? -50.32400 11.44100 -19.65500 1.000 32.95114 ? 54  GLY A CA  1 
ATOM   478  C  C   . GLY A 1 55  ? -50.02800 12.25700 -18.40900 1.000 32.62587 ? 54  GLY A C   1 
ATOM   479  O  O   . GLY A 1 55  ? -49.79700 13.47000 -18.51700 1.000 34.84222 ? 54  GLY A O   1 
ATOM   480  N  N   . SER A 1 56  ? -50.02700 11.64000 -17.23500 1.000 29.93936 ? 55  SER A N   1 
ATOM   481  C  CA  . SER A 1 56  ? -49.88200 12.36800 -15.97000 1.000 27.07383 ? 55  SER A CA  1 
ATOM   482  C  C   . SER A 1 56  ? -48.46700 12.24600 -15.41400 1.000 24.43913 ? 55  SER A C   1 
ATOM   483  O  O   . SER A 1 56  ? -48.25400 11.78200 -14.28500 1.000 24.36435 ? 55  SER A O   1 
ATOM   484  C  CB  . SER A 1 56  ? -50.89400 11.84800 -14.95800 1.000 29.51239 ? 55  SER A CB  1 
ATOM   485  O  OG  . SER A 1 56  ? -50.79300 10.42500 -14.81500 1.000 29.65499 ? 55  SER A OG  1 
ATOM   486  N  N   . HIS A 1 57  ? -47.49300 12.67300 -16.21500 1.000 23.75217 ? 56  HIS A N   1 
ATOM   487  C  CA  . HIS A 1 57  ? -46.08100 12.46100 -15.90500 1.000 23.15175 ? 56  HIS A CA  1 
ATOM   488  C  C   . HIS A 1 57  ? -45.26800 13.52600 -16.61600 1.000 20.80586 ? 56  HIS A C   1 
ATOM   489  O  O   . HIS A 1 57  ? -45.41100 13.68100 -17.83400 1.000 23.87506 ? 56  HIS A O   1 
ATOM   490  C  CB  . HIS A 1 57  ? -45.68100 11.04500 -16.37100 1.000 27.05772 ? 56  HIS A CB  1 
ATOM   491  C  CG  . HIS A 1 57  ? -44.40300 10.52500 -15.77500 1.000 23.92124 ? 56  HIS A CG  1 
ATOM   492  N  ND1 . HIS A 1 57  ? -43.20100 11.19500 -15.88400 1.000 24.70950 ? 56  HIS A ND1 1 
ATOM   493  C  CD2 . HIS A 1 57  ? -44.14600 9.40600  -15.05700 1.000 25.02921 ? 56  HIS A CD2 1 
ATOM   494  C  CE1 . HIS A 1 57  ? -42.26000 10.50400 -15.25900 1.000 22.44916 ? 56  HIS A CE1 1 
ATOM   495  N  NE2 . HIS A 1 57  ? -42.80700 9.41800  -14.74300 1.000 24.48973 ? 56  HIS A NE2 1 
ATOM   496  N  N   . TRP A 1 58  ? -44.42900 14.25900 -15.86500 1.000 26.00686 ? 57  TRP A N   1 
ATOM   497  C  CA  . TRP A 1 58  ? -43.70900 15.41600 -16.41200 1.000 22.33177 ? 57  TRP A CA  1 
ATOM   498  C  C   . TRP A 1 58  ? -42.25100 15.33200 -15.98900 1.000 22.34700 ? 57  TRP A C   1 
ATOM   499  O  O   . TRP A 1 58  ? -41.90800 14.67000 -15.00500 1.000 24.53933 ? 57  TRP A O   1 
ATOM   500  C  CB  . TRP A 1 58  ? -44.30100 16.78000 -15.95100 1.000 25.73783 ? 57  TRP A CB  1 
ATOM   501  C  CG  . TRP A 1 58  ? -45.75600 16.86500 -16.27400 1.000 23.53134 ? 57  TRP A CG  1 
ATOM   502  C  CD1 . TRP A 1 58  ? -46.30500 17.35900 -17.41500 1.000 25.15488 ? 57  TRP A CD1 1 
ATOM   503  C  CD2 . TRP A 1 58  ? -46.84400 16.35400 -15.48700 1.000 22.55674 ? 57  TRP A CD2 1 
ATOM   504  N  NE1 . TRP A 1 58  ? -47.67800 17.22800 -17.38600 1.000 29.04339 ? 57  TRP A NE1 1 
ATOM   505  C  CE2 . TRP A 1 58  ? -48.02100 16.57800 -16.22400 1.000 24.14588 ? 57  TRP A CE2 1 
ATOM   506  C  CE3 . TRP A 1 58  ? -46.92800 15.71500 -14.23100 1.000 23.48023 ? 57  TRP A CE3 1 
ATOM   507  C  CZ2 . TRP A 1 58  ? -49.28500 16.24000 -15.74100 1.000 28.17337 ? 57  TRP A CZ2 1 
ATOM   508  C  CZ3 . TRP A 1 58  ? -48.20000 15.34200 -13.76000 1.000 24.14536 ? 57  TRP A CZ3 1 
ATOM   509  C  CH2 . TRP A 1 58  ? -49.35100 15.60200 -14.52100 1.000 23.93902 ? 57  TRP A CH2 1 
ATOM   510  N  N   . LEU A 1 59  ? -41.38600 16.00400 -16.74800 1.000 22.59840 ? 58  LEU A N   1 
ATOM   511  C  CA  . LEU A 1 59  ? -39.98100 16.05400 -16.36200 1.000 24.04075 ? 58  LEU A CA  1 
ATOM   512  C  C   . LEU A 1 59  ? -39.42800 17.46700 -16.61500 1.000 24.14854 ? 58  LEU A C   1 
ATOM   513  O  O   . LEU A 1 59  ? -39.97300 18.26100 -17.38800 1.000 26.95645 ? 58  LEU A O   1 
ATOM   514  C  CB  . LEU A 1 59  ? -39.16000 14.94100 -17.07900 1.000 23.41060 ? 58  LEU A CB  1 
ATOM   515  C  CG  . LEU A 1 59  ? -39.08900 14.91100 -18.61300 1.000 22.28932 ? 58  LEU A CG  1 
ATOM   516  C  CD1 . LEU A 1 59  ? -38.13300 15.94000 -19.18500 1.000 31.11977 ? 58  LEU A CD1 1 
ATOM   517  C  CD2 . LEU A 1 59  ? -38.68600 13.47800 -19.06900 1.000 24.60205 ? 58  LEU A CD2 1 
ATOM   518  N  N   . ALA A 1 60  ? -38.33200 17.76700 -15.92300 1.000 24.53205 ? 59  ALA A N   1 
ATOM   519  C  CA  . ALA A 1 60  ? -37.50700 18.93400 -16.16300 1.000 27.19832 ? 59  ALA A CA  1 
ATOM   520  C  C   . ALA A 1 60  ? -36.27800 18.52300 -16.95500 1.000 25.78546 ? 59  ALA A C   1 
ATOM   521  O  O   . ALA A 1 60  ? -35.63900 17.52400 -16.62600 1.000 25.73537 ? 59  ALA A O   1 
ATOM   522  C  CB  . ALA A 1 60  ? -37.08400 19.54900 -14.83200 1.000 27.23609 ? 59  ALA A CB  1 
ATOM   523  N  N   . GLU A 1 61  ? -35.94400 19.28300 -17.99800 1.000 27.03805 ? 60  GLU A N   1 
ATOM   524  C  CA  . GLU A 1 61  ? -34.75200 19.00800 -18.78800 1.000 28.57652 ? 60  GLU A CA  1 
ATOM   525  C  C   . GLU A 1 61  ? -33.82800 20.21600 -18.75400 1.000 29.21868 ? 60  GLU A C   1 
ATOM   526  O  O   . GLU A 1 61  ? -34.28100 21.35900 -18.62900 1.000 32.50759 ? 60  GLU A O   1 
ATOM   527  C  CB  . GLU A 1 61  ? -35.09300 18.63800 -20.25200 1.000 33.17922 ? 60  GLU A CB  1 
ATOM   528  C  CG  . GLU A 1 61  ? -35.95300 19.66300 -20.95300 1.000 35.15155 ? 60  GLU A CG  1 
ATOM   529  C  CD  . GLU A 1 61  ? -36.20600 19.36800 -22.42900 1.000 45.07542 ? 60  GLU A CD  1 
ATOM   530  O  OE1 . GLU A 1 61  ? -36.34800 18.19700 -22.81900 1.000 49.98120 ? 60  GLU A OE1 1 
ATOM   531  O  OE2 . GLU A 1 61  ? -36.27300 20.32800 -23.21100 1.000 49.54159 ? 60  GLU A OE2 1 
ATOM   532  N  N   . ASP A 1 62  ? -32.52500 19.95400 -18.85200 1.000 30.54701 ? 61  ASP A N   1 
ATOM   533  C  CA  . ASP A 1 62  ? -31.56000 21.04300 -18.88600 1.000 32.93163 ? 61  ASP A CA  1 
ATOM   534  C  C   . ASP A 1 62  ? -31.46300 21.60900 -20.30100 1.000 38.11750 ? 61  ASP A C   1 
ATOM   535  O  O   . ASP A 1 62  ? -32.20300 21.23400 -21.22000 1.000 38.15323 ? 61  ASP A O   1 
ATOM   536  C  CB  . ASP A 1 62  ? -30.20600 20.59400 -18.32300 1.000 43.71688 ? 61  ASP A CB  1 
ATOM   537  C  CG  . ASP A 1 62  ? -29.43200 19.63800 -19.24500 1.000 46.93215 ? 61  ASP A CG  1 
ATOM   538  O  OD1 . ASP A 1 62  ? -29.80900 19.43800 -20.41100 1.000 40.83978 ? 61  ASP A OD1 1 
ATOM   539  O  OD2 . ASP A 1 62  ? -28.41900 19.07200 -18.77100 1.000 47.04504 ? 61  ASP A OD2 1 
ATOM   540  N  N   . ALA A 1 63  ? -30.52000 22.53200 -20.48400 1.000 40.08327 ? 62  ALA A N   1 
ATOM   541  C  CA  . ALA A 1 63  ? -30.45400 23.29600 -21.72100 1.000 44.96141 ? 62  ALA A CA  1 
ATOM   542  C  C   . ALA A 1 63  ? -30.11100 22.41600 -22.90800 1.000 49.77960 ? 62  ALA A C   1 
ATOM   543  O  O   . ALA A 1 63  ? -30.43400 22.76700 -24.05200 1.000 56.54181 ? 62  ALA A O   1 
ATOM   544  C  CB  . ALA A 1 63  ? -29.43100 24.41900 -21.57800 1.000 46.10111 ? 62  ALA A CB  1 
ATOM   545  N  N   . ASP A 1 64  ? -29.43800 21.29200 -22.66100 1.000 45.71627 ? 63  ASP A N   1 
ATOM   546  C  CA  . ASP A 1 64  ? -29.10600 20.31800 -23.68900 1.000 48.86878 ? 63  ASP A CA  1 
ATOM   547  C  C   . ASP A 1 64  ? -30.19100 19.26900 -23.86000 1.000 49.68774 ? 63  ASP A C   1 
ATOM   548  O  O   . ASP A 1 64  ? -29.96800 18.26800 -24.55000 1.000 53.93964 ? 63  ASP A O   1 
ATOM   549  C  CB  . ASP A 1 64  ? -27.78400 19.63300 -23.35400 1.000 54.38910 ? 63  ASP A CB  1 
ATOM   550  C  CG  . ASP A 1 64  ? -26.65100 20.61800 -23.17000 1.000 61.98952 ? 63  ASP A CG  1 
ATOM   551  O  OD1 . ASP A 1 64  ? -26.55500 21.57300 -23.96500 1.000 67.16955 ? 63  ASP A OD1 1 
ATOM   552  O  OD2 . ASP A 1 64  ? -25.85900 20.44100 -22.22300 1.000 66.87502 ? 63  ASP A OD2 1 
ATOM   553  N  N   . GLY A 1 65  ? -31.34800 19.46700 -23.23600 1.000 42.58288 ? 64  GLY A N   1 
ATOM   554  C  CA  . GLY A 1 65  ? -32.44000 18.52300 -23.33400 1.000 40.64058 ? 64  GLY A CA  1 
ATOM   555  C  C   . GLY A 1 65  ? -32.29700 17.25500 -22.51500 1.000 46.11125 ? 64  GLY A C   1 
ATOM   556  O  O   . GLY A 1 65  ? -33.06200 16.30800 -22.74200 1.000 44.54121 ? 64  GLY A O   1 
ATOM   557  N  N   . GLN A 1 66  ? -31.35200 17.20500 -21.54300 1.000 39.00898 ? 65  GLN A N   1 
ATOM   558  C  CA  . GLN A 1 66  ? -31.23700 15.97100 -20.75400 1.000 36.05049 ? 65  GLN A CA  1 
ATOM   559  C  C   . GLN A 1 66  ? -32.14300 16.04000 -19.53400 1.000 34.72272 ? 65  GLN A C   1 
ATOM   560  O  O   . GLN A 1 66  ? -32.12200 17.04200 -18.81400 1.000 30.85807 ? 65  GLN A O   1 
ATOM   561  C  CB  . GLN A 1 66  ? -29.80400 15.73500 -20.29700 1.000 41.24625 ? 65  GLN A CB  1 
ATOM   562  C  CG  . GLN A 1 66  ? -28.78900 15.57600 -21.42100 1.000 53.02491 ? 65  GLN A CG  1 
ATOM   563  C  CD  . GLN A 1 66  ? -29.09800 14.41000 -22.35700 1.000 59.07898 ? 65  GLN A CD  1 
ATOM   564  O  OE1 . GLN A 1 66  ? -29.68400 13.39800 -21.95100 1.000 60.40124 ? 65  GLN A OE1 1 
ATOM   565  N  NE2 . GLN A 1 66  ? -28.71200 14.55600 -23.62100 1.000 61.45403 ? 65  GLN A NE2 1 
ATOM   566  N  N   . PRO A 1 67  ? -32.94400 15.00300 -19.26300 1.000 30.07457 ? 66  PRO A N   1 
ATOM   567  C  CA  . PRO A 1 67  ? -33.80900 15.02800 -18.07900 1.000 26.05543 ? 66  PRO A CA  1 
ATOM   568  C  C   . PRO A 1 67  ? -32.98300 15.09600 -16.80400 1.000 26.60566 ? 66  PRO A C   1 
ATOM   569  O  O   . PRO A 1 67  ? -31.94000 14.44500 -16.69000 1.000 27.68042 ? 66  PRO A O   1 
ATOM   570  C  CB  . PRO A 1 67  ? -34.58700 13.70900 -18.18200 1.000 28.90444 ? 66  PRO A CB  1 
ATOM   571  C  CG  . PRO A 1 67  ? -34.61600 13.43700 -19.64300 1.000 29.75027 ? 66  PRO A CG  1 
ATOM   572  C  CD  . PRO A 1 67  ? -33.24600 13.85300 -20.13500 1.000 33.18371 ? 66  PRO A CD  1 
ATOM   573  N  N   . VAL A 1 68  ? -33.43600 15.94300 -15.87000 1.000 22.46613 ? 67  VAL A N   1 
ATOM   574  C  CA  . VAL A 1 68  ? -32.78100 16.11700 -14.57900 1.000 24.28634 ? 67  VAL A CA  1 
ATOM   575  C  C   . VAL A 1 68  ? -33.74300 16.00200 -13.40100 1.000 23.28910 ? 67  VAL A C   1 
ATOM   576  O  O   . VAL A 1 68  ? -33.30500 16.11800 -12.25200 1.000 22.43956 ? 67  VAL A O   1 
ATOM   577  C  CB  . VAL A 1 68  ? -32.02600 17.46500 -14.50000 1.000 23.77436 ? 67  VAL A CB  1 
ATOM   578  C  CG1 . VAL A 1 68  ? -30.91800 17.58000 -15.56600 1.000 29.06769 ? 67  VAL A CG1 1 
ATOM   579  C  CG2 . VAL A 1 68  ? -33.00000 18.64300 -14.54100 1.000 24.75278 ? 67  VAL A CG2 1 
ATOM   580  N  N   . GLY A 1 69  ? -35.04700 15.79400 -13.63800 1.000 21.53873 ? 68  GLY A N   1 
ATOM   581  C  CA  . GLY A 1 69  ? -36.01800 15.65100 -12.56200 1.000 20.87375 ? 68  GLY A CA  1 
ATOM   582  C  C   . GLY A 1 69  ? -37.35600 15.24500 -13.15400 1.000 19.88688 ? 68  GLY A C   1 
ATOM   583  O  O   . GLY A 1 69  ? -37.57100 15.36800 -14.36000 1.000 22.27489 ? 68  GLY A O   1 
ATOM   584  N  N   . PHE A 1 70  ? -38.23800 14.71600 -12.29700 1.000 20.52582 ? 69  PHE A N   1 
ATOM   585  C  CA  . PHE A 1 70  ? -39.53700 14.28700 -12.81800 1.000 21.52528 ? 69  PHE A CA  1 
ATOM   586  C  C   . PHE A 1 70  ? -40.59100 14.32400 -11.72000 1.000 19.95420 ? 69  PHE A C   1 
ATOM   587  O  O   . PHE A 1 70  ? -40.28700 14.30500 -10.53100 1.000 19.12868 ? 69  PHE A O   1 
ATOM   588  C  CB  . PHE A 1 70  ? -39.46600 12.87000 -13.44600 1.000 22.62586 ? 69  PHE A CB  1 
ATOM   589  C  CG  . PHE A 1 70  ? -39.22100 11.77800 -12.43600 1.000 20.29846 ? 69  PHE A CG  1 
ATOM   590  C  CD1 . PHE A 1 70  ? -40.28900 11.22200 -11.71100 1.000 22.32907 ? 69  PHE A CD1 1 
ATOM   591  C  CD2 . PHE A 1 70  ? -37.93800 11.29400 -12.22800 1.000 19.45900 ? 69  PHE A CD2 1 
ATOM   592  C  CE1 . PHE A 1 70  ? -40.04500 10.23700 -10.75700 1.000 20.65236 ? 69  PHE A CE1 1 
ATOM   593  C  CE2 . PHE A 1 70  ? -37.71000 10.33700 -11.27700 1.000 23.13295 ? 69  PHE A CE2 1 
ATOM   594  C  CZ  . PHE A 1 70  ? -38.76700 9.81500  -10.55300 1.000 20.37035 ? 69  PHE A CZ  1 
ATOM   595  N  N   . LEU A 1 71  ? -41.85600 14.33200 -12.15600 1.000 19.71710 ? 70  LEU A N   1 
ATOM   596  C  CA  . LEU A 1 71  ? -43.00100 14.21100 -11.26600 1.000 18.31976 ? 70  LEU A CA  1 
ATOM   597  C  C   . LEU A 1 71  ? -43.91300 13.17400 -11.90400 1.000 19.12203 ? 70  LEU A C   1 
ATOM   598  O  O   . LEU A 1 71  ? -44.36100 13.35000 -13.04000 1.000 20.52594 ? 70  LEU A O   1 
ATOM   599  C  CB  . LEU A 1 71  ? -43.72800 15.55500 -11.05300 1.000 19.73903 ? 70  LEU A CB  1 
ATOM   600  C  CG  . LEU A 1 71  ? -44.79000 15.58300 -9.93700  1.000 20.66151 ? 70  LEU A CG  1 
ATOM   601  C  CD1 . LEU A 1 71  ? -45.13600 17.04900 -9.56000  1.000 19.69903 ? 70  LEU A CD1 1 
ATOM   602  C  CD2 . LEU A 1 71  ? -46.10000 14.87300 -10.34800 1.000 23.97758 ? 70  LEU A CD2 1 
ATOM   603  N  N   . ALA A 1 72  ? -44.13500 12.06800 -11.19000 1.000 19.65641 ? 71  ALA A N   1 
ATOM   604  C  CA  . ALA A 1 72  ? -44.98900 10.96500 -11.63900 1.000 20.11325 ? 71  ALA A CA  1 
ATOM   605  C  C   . ALA A 1 72  ? -46.28400 10.99500 -10.83400 1.000 22.52557 ? 71  ALA A C   1 
ATOM   606  O  O   . ALA A 1 72  ? -46.24300 10.94100 -9.60300  1.000 22.28054 ? 71  ALA A O   1 
ATOM   607  C  CB  . ALA A 1 72  ? -44.27000 9.63400  -11.42700 1.000 21.98820 ? 71  ALA A CB  1 
ATOM   608  N  N   . ALA A 1 73  ? -47.42600 11.08900 -11.51600 1.000 22.70279 ? 72  ALA A N   1 
ATOM   609  C  CA  . ALA A 1 73  ? -48.72400 11.21700 -10.86500 1.000 21.47246 ? 72  ALA A CA  1 
ATOM   610  C  C   . ALA A 1 73  ? -49.71800 10.20400 -11.41800 1.000 23.33760 ? 72  ALA A C   1 
ATOM   611  O  O   . ALA A 1 73  ? -49.53000 9.64200  -12.50300 1.000 23.93070 ? 72  ALA A O   1 
ATOM   612  C  CB  . ALA A 1 73  ? -49.33500 12.60900 -11.06100 1.000 20.94918 ? 72  ALA A CB  1 
ATOM   613  N  N   . GLU A 1 74  ? -50.82000 10.01100 -10.69000 1.000 20.99829 ? 73  GLU A N   1 
ATOM   614  C  CA  . GLU A 1 74  ? -51.79300 9.00100  -11.09900 1.000 25.36192 ? 73  GLU A CA  1 
ATOM   615  C  C   . GLU A 1 74  ? -53.18100 9.47100  -10.70300 1.000 27.09279 ? 73  GLU A C   1 
ATOM   616  O  O   . GLU A 1 74  ? -53.39500 9.82300  -9.54100  1.000 25.57606 ? 73  GLU A O   1 
ATOM   617  C  CB  . GLU A 1 74  ? -51.49100 7.62800  -10.46600 1.000 27.71689 ? 73  GLU A CB  1 
ATOM   618  C  CG  . GLU A 1 74  ? -52.44900 6.58700  -10.97700 1.000 27.63004 ? 73  GLU A CG  1 
ATOM   619  C  CD  . GLU A 1 74  ? -52.10000 5.17500  -10.53800 1.000 35.62129 ? 73  GLU A CD  1 
ATOM   620  O  OE1 . GLU A 1 74  ? -51.16000 5.00600  -9.73600  1.000 38.03635 ? 73  GLU A OE1 1 
ATOM   621  O  OE2 . GLU A 1 74  ? -52.75800 4.24900  -11.03300 1.000 41.88469 ? 73  GLU A OE2 1 
ATOM   622  N  N   . ARG A 1 75  ? -54.11000 9.49100  -11.66600 1.000 25.50678 ? 74  ARG A N   1 
ATOM   623  C  CA  . ARG A 1 75  ? -55.50900 9.79100  -11.38000 1.000 27.42361 ? 74  ARG A CA  1 
ATOM   624  C  C   . ARG A 1 75  ? -56.13200 8.61300  -10.63400 1.000 29.53306 ? 74  ARG A C   1 
ATOM   625  O  O   . ARG A 1 75  ? -56.12400 7.47200  -11.12900 1.000 30.82464 ? 74  ARG A O   1 
ATOM   626  C  CB  . ARG A 1 75  ? -56.26100 10.07800 -12.68100 1.000 30.52581 ? 74  ARG A CB  1 
ATOM   627  C  CG  . ARG A 1 75  ? -57.79800 10.41600 -12.55900 1.000 32.99465 ? 74  ARG A CG  1 
ATOM   628  C  CD  . ARG A 1 75  ? -58.06000 11.68000 -11.77000 1.000 35.94801 ? 74  ARG A CD  1 
ATOM   629  N  NE  . ARG A 1 75  ? -59.44900 12.18600 -11.79900 1.000 34.54733 ? 74  ARG A NE  1 
ATOM   630  C  CZ  . ARG A 1 75  ? -59.94900 13.02600 -12.71300 1.000 38.35587 ? 74  ARG A CZ  1 
ATOM   631  N  NH1 . ARG A 1 75  ? -59.20400 13.42500 -13.73400 1.000 39.32836 ? 74  ARG A NH1 1 
ATOM   632  N  NH2 . ARG A 1 75  ? -61.20400 13.45800 -12.61300 1.000 34.97559 ? 74  ARG A NH2 1 
ATOM   633  N  N   . CYS A 1 76  ? -56.70700 8.90300  -9.46700  1.000 31.02317 ? 75  CYS A N   1 
ATOM   634  C  CA  . CYS A 1 76  ? -57.35200 7.93200  -8.58300  1.000 30.84988 ? 75  CYS A CA  1 
ATOM   635  C  C   . CYS A 1 76  ? -58.71700 8.48900  -8.19100  1.000 32.89405 ? 75  CYS A C   1 
ATOM   636  O  O   . CYS A 1 76  ? -58.80600 9.41000  -7.37200  1.000 32.06931 ? 75  CYS A O   1 
ATOM   637  C  CB  . CYS A 1 76  ? -56.49500 7.67900  -7.33800  1.000 33.59492 ? 75  CYS A CB  1 
ATOM   638  S  SG  . CYS A 1 76  ? -54.80200 7.04900  -7.61100  1.000 34.33547 ? 75  CYS A SG  1 
ATOM   639  N  N   . ALA A 1 77  ? -59.78000 7.94500  -8.77100  1.000 30.77272 ? 76  ALA A N   1 
ATOM   640  C  CA  . ALA A 1 77  ? -61.12700 8.52500  -8.62600  1.000 33.06753 ? 76  ALA A CA  1 
ATOM   641  C  C   . ALA A 1 77  ? -61.05600 9.98800  -9.06600  1.000 34.22323 ? 76  ALA A C   1 
ATOM   642  O  O   . ALA A 1 77  ? -60.60300 10.24900 -10.19400 1.000 33.65328 ? 76  ALA A O   1 
ATOM   643  C  CB  . ALA A 1 77  ? -61.63600 8.27700  -7.20000  1.000 37.94908 ? 76  ALA A CB  1 
ATOM   644  N  N   . ASP A 1 78  ? -61.45400 10.96300 -8.24100  1.000 34.26394 ? 77  ASP A N   1 
ATOM   645  C  CA  . ASP A 1 78  ? -61.42000 12.37000 -8.63100  1.000 32.50249 ? 77  ASP A CA  1 
ATOM   646  C  C   . ASP A 1 78  ? -60.19400 13.09900 -8.07100  1.000 28.66889 ? 77  ASP A C   1 
ATOM   647  O  O   . ASP A 1 78  ? -60.20900 14.33200 -7.97700  1.000 33.00985 ? 77  ASP A O   1 
ATOM   648  C  CB  . ASP A 1 78  ? -62.71200 13.07500 -8.18800  1.000 33.91511 ? 77  ASP A CB  1 
ATOM   649  C  CG  . ASP A 1 78  ? -63.24300 14.10700 -9.22400  1.000 36.57465 ? 77  ASP A CG  1 
ATOM   650  O  OD1 . ASP A 1 78  ? -62.78100 14.15000 -10.38100 1.000 36.58907 ? 77  ASP A OD1 1 
ATOM   651  O  OD2 . ASP A 1 78  ? -64.16500 14.85100 -8.86900  1.000 36.08540 ? 77  ASP A OD2 1 
ATOM   652  N  N   . GLU A 1 79  ? -59.12200 12.37600 -7.72400  1.000 28.06075 ? 78  GLU A N   1 
ATOM   653  C  CA  . GLU A 1 79  ? -57.90900 13.00700 -7.20500  1.000 26.92795 ? 78  GLU A CA  1 
ATOM   654  C  C   . GLU A 1 79  ? -56.71100 12.70600 -8.08800  1.000 28.54328 ? 78  GLU A C   1 
ATOM   655  O  O   . GLU A 1 79  ? -56.64500 11.65300 -8.72600  1.000 27.32973 ? 78  GLU A O   1 
ATOM   656  C  CB  . GLU A 1 79  ? -57.60600 12.53100 -5.78500  1.000 25.50110 ? 78  GLU A CB  1 
ATOM   657  C  CG  . GLU A 1 79  ? -58.64000 12.97300 -4.79100  1.000 29.34143 ? 78  GLU A CG  1 
ATOM   658  C  CD  . GLU A 1 79  ? -58.34200 12.51000 -3.38500  1.000 36.19651 ? 78  GLU A CD  1 
ATOM   659  O  OE1 . GLU A 1 79  ? -57.92100 11.33600 -3.21100  1.000 33.14883 ? 78  GLU A OE1 1 
ATOM   660  O  OE2 . GLU A 1 79  ? -58.57200 13.29900 -2.44300  1.000 33.40282 ? 78  GLU A OE2 1 
ATOM   661  N  N   . LEU A 1 80  ? -55.73700 13.63100 -8.11200  1.000 23.96445 ? 79  LEU A N   1 
ATOM   662  C  CA  . LEU A 1 80  ? -54.45400 13.37900 -8.75400  1.000 23.33305 ? 79  LEU A CA  1 
ATOM   663  C  C   . LEU A 1 80  ? -53.46700 13.09000 -7.64000  1.000 22.84499 ? 79  LEU A C   1 
ATOM   664  O  O   . LEU A 1 80  ? -53.14800 13.97400 -6.84100  1.000 22.21120 ? 79  LEU A O   1 
ATOM   665  C  CB  . LEU A 1 80  ? -53.99000 14.57500 -9.60000  1.000 22.65288 ? 79  LEU A CB  1 
ATOM   666  C  CG  . LEU A 1 80  ? -52.72800 14.21900 -10.41300 1.000 21.20615 ? 79  LEU A CG  1 
ATOM   667  C  CD1 . LEU A 1 80  ? -53.07900 13.21900 -11.51900 1.000 24.86857 ? 79  LEU A CD1 1 
ATOM   668  C  CD2 . LEU A 1 80  ? -52.10200 15.49600 -11.02200 1.000 25.11855 ? 79  LEU A CD2 1 
ATOM   669  N  N   . HIS A 1 81  ? -53.02100 11.83800 -7.55000  1.000 23.96120 ? 80  HIS A N   1 
ATOM   670  C  CA  . HIS A 1 81  ? -52.06600 11.44900 -6.52300  1.000 20.39200 ? 80  HIS A CA  1 
ATOM   671  C  C   . HIS A 1 81  ? -50.64000 11.68300 -7.01300  1.000 21.51910 ? 80  HIS A C   1 
ATOM   672  O  O   . HIS A 1 81  ? -50.28700 11.26700 -8.11900  1.000 23.03382 ? 80  HIS A O   1 
ATOM   673  C  CB  . HIS A 1 81  ? -52.26200 9.96900  -6.15200  1.000 23.44963 ? 80  HIS A CB  1 
ATOM   674  C  CG  . HIS A 1 81  ? -51.33700 9.49200  -5.06800  1.000 25.77326 ? 80  HIS A CG  1 
ATOM   675  N  ND1 . HIS A 1 81  ? -51.46000 9.88900  -3.75200  1.000 24.63684 ? 80  HIS A ND1 1 
ATOM   676  C  CD2 . HIS A 1 81  ? -50.29400 8.62600  -5.09900  1.000 24.23356 ? 80  HIS A CD2 1 
ATOM   677  C  CE1 . HIS A 1 81  ? -50.52000 9.31100  -3.02400  1.000 24.99836 ? 80  HIS A CE1 1 
ATOM   678  N  NE2 . HIS A 1 81  ? -49.79400 8.54000  -3.81800  1.000 27.65640 ? 80  HIS A NE2 1 
ATOM   679  N  N   . ILE A 1 82  ? -49.83000 12.39600 -6.22500  1.000 20.74991 ? 81  ILE A N   1 
ATOM   680  C  CA  . ILE A 1 82  ? -48.43100 12.62400 -6.58200  1.000 20.90916 ? 81  ILE A CA  1 
ATOM   681  C  C   . ILE A 1 82  ? -47.61300 11.46700 -6.00800  1.000 21.05970 ? 81  ILE A C   1 
ATOM   682  O  O   . ILE A 1 82  ? -47.34900 11.41700 -4.81200  1.000 24.27988 ? 81  ILE A O   1 
ATOM   683  C  CB  . ILE A 1 82  ? -47.93900 13.97300 -6.07200  1.000 20.85280 ? 81  ILE A CB  1 
ATOM   684  C  CG1 . ILE A 1 82  ? -48.80600 15.07000 -6.67500  1.000 22.90937 ? 81  ILE A CG1 1 
ATOM   685  C  CG2 . ILE A 1 82  ? -46.45200 14.15600 -6.41800  1.000 24.53273 ? 81  ILE A CG2 1 
ATOM   686  C  CD1 . ILE A 1 82  ? -48.52800 16.41400 -6.07500  1.000 27.73510 ? 81  ILE A CD1 1 
ATOM   687  N  N   . ALA A 1 83  ? -47.22200 10.52400 -6.87700  1.000 21.75016 ? 82  ALA A N   1 
ATOM   688  C  CA  . ALA A 1 83  ? -46.53800 9.31400  -6.41100  1.000 20.77784 ? 82  ALA A CA  1 
ATOM   689  C  C   . ALA A 1 83  ? -45.04900 9.54300  -6.13100  1.000 22.43367 ? 82  ALA A C   1 
ATOM   690  O  O   . ALA A 1 83  ? -44.49400 8.96200  -5.18400  1.000 24.04718 ? 82  ALA A O   1 
ATOM   691  C  CB  . ALA A 1 83  ? -46.71200 8.19900  -7.44400  1.000 26.80731 ? 82  ALA A CB  1 
ATOM   692  N  N   . GLU A 1 84  ? -44.39500 10.35500 -6.94600  1.000 22.80097 ? 83  GLU A N   1 
ATOM   693  C  CA  . GLU A 1 84  ? -42.97700 10.60200 -6.76200  1.000 22.12064 ? 83  GLU A CA  1 
ATOM   694  C  C   . GLU A 1 84  ? -42.62100 11.93400 -7.40500  1.000 22.91403 ? 83  GLU A C   1 
ATOM   695  O  O   . GLU A 1 84  ? -43.07800 12.23800 -8.51400  1.000 24.23755 ? 83  GLU A O   1 
ATOM   696  C  CB  . GLU A 1 84  ? -42.14300 9.46800  -7.36800  1.000 23.91807 ? 83  GLU A CB  1 
ATOM   697  C  CG  . GLU A 1 84  ? -40.62600 9.62400  -7.17200  1.000 23.01222 ? 83  GLU A CG  1 
ATOM   698  C  CD  . GLU A 1 84  ? -40.24000 9.73000  -5.72400  1.000 25.72371 ? 83  GLU A CD  1 
ATOM   699  O  OE1 . GLU A 1 84  ? -40.61700 8.85700  -4.92400  1.000 29.78395 ? 83  GLU A OE1 1 
ATOM   700  O  OE2 . GLU A 1 84  ? -39.56100 10.70800 -5.35800  1.000 30.40590 ? 83  GLU A OE2 1 
ATOM   701  N  N   . LEU A 1 85  ? -41.79600 12.71400 -6.69900  1.000 18.44813 ? 84  LEU A N   1 
ATOM   702  C  CA  . LEU A 1 85  ? -41.25400 13.97800 -7.20000  1.000 18.62830 ? 84  LEU A CA  1 
ATOM   703  C  C   . LEU A 1 85  ? -39.76400 13.97000 -6.83700  1.000 18.67479 ? 84  LEU A C   1 
ATOM   704  O  O   . LEU A 1 85  ? -39.44000 13.94100 -5.65300  1.000 20.89291 ? 84  LEU A O   1 
ATOM   705  C  CB  . LEU A 1 85  ? -41.97700 15.15100 -6.55900  1.000 19.95069 ? 84  LEU A CB  1 
ATOM   706  C  CG  . LEU A 1 85  ? -41.29700 16.49700 -6.77500  1.000 19.76793 ? 84  LEU A CG  1 
ATOM   707  C  CD1 . LEU A 1 85  ? -41.26500 16.91000 -8.26500  1.000 19.73289 ? 84  LEU A CD1 1 
ATOM   708  C  CD2 . LEU A 1 85  ? -42.02300 17.53700 -5.89900  1.000 23.22220 ? 84  LEU A CD2 1 
ATOM   709  N  N   . SER A 1 86  ? -38.87000 13.92100 -7.83900  1.000 18.76019 ? 85  SER A N   1 
ATOM   710  C  CA  . SER A 1 86  ? -37.42700 13.75100 -7.59500  1.000 18.53969 ? 85  SER A CA  1 
ATOM   711  C  C   . SER A 1 86  ? -36.62700 14.66000 -8.51600  1.000 18.70121 ? 85  SER A C   1 
ATOM   712  O  O   . SER A 1 86  ? -36.84700 14.67000 -9.72800  1.000 21.36322 ? 85  SER A O   1 
ATOM   713  C  CB  . SER A 1 86  ? -36.96800 12.28200 -7.78900  1.000 21.78561 ? 85  SER A CB  1 
ATOM   714  O  OG  . SER A 1 86  ? -37.18800 11.52500 -6.60600  1.000 23.94410 ? 85  SER A OG  1 
ATOM   715  N  N   . ILE A 1 87  ? -35.69600 15.43200 -7.95100  1.000 19.46972 ? 86  ILE A N   1 
ATOM   716  C  CA  . ILE A 1 87  ? -34.76400 16.24200 -8.73600  1.000 19.35557 ? 86  ILE A CA  1 
ATOM   717  C  C   . ILE A 1 87  ? -33.36100 15.72200 -8.47700  1.000 19.03942 ? 86  ILE A C   1 
ATOM   718  O  O   . ILE A 1 87  ? -32.96800 15.57100 -7.31800  1.000 21.14004 ? 86  ILE A O   1 
ATOM   719  C  CB  . ILE A 1 87  ? -34.85800 17.73400 -8.36600  1.000 21.11012 ? 86  ILE A CB  1 
ATOM   720  C  CG1 . ILE A 1 87  ? -36.28700 18.23700 -8.56500  1.000 24.93074 ? 86  ILE A CG1 1 
ATOM   721  C  CG2 . ILE A 1 87  ? -33.83300 18.52900 -9.19500  1.000 21.26479 ? 86  ILE A CG2 1 
ATOM   722  C  CD1 . ILE A 1 87  ? -36.74600 18.22800 -9.99700  1.000 24.40212 ? 86  ILE A CD1 1 
ATOM   723  N  N   . ALA A 1 88  ? -32.60400 15.46300 -9.54300  1.000 19.53351 ? 87  ALA A N   1 
ATOM   724  C  CA  . ALA A 1 88  ? -31.24200 14.95900 -9.36800  1.000 23.72980 ? 87  ALA A CA  1 
ATOM   725  C  C   . ALA A 1 88  ? -30.39900 15.92900 -8.52200  1.000 22.94424 ? 87  ALA A C   1 
ATOM   726  O  O   . ALA A 1 88  ? -30.55300 17.14600 -8.58400  1.000 23.64623 ? 87  ALA A O   1 
ATOM   727  C  CB  . ALA A 1 88  ? -30.58000 14.73900 -10.73000 1.000 26.74336 ? 87  ALA A CB  1 
ATOM   728  N  N   . GLN A 1 89  ? -29.49900 15.34100 -7.72300  1.000 23.29166 ? 88  GLN A N   1 
ATOM   729  C  CA  . GLN A 1 89  ? -28.72600 16.07600 -6.72100  1.000 22.56301 ? 88  GLN A CA  1 
ATOM   730  C  C   . GLN A 1 89  ? -28.11800 17.36800 -7.28000  1.000 25.25715 ? 88  GLN A C   1 
ATOM   731  O  O   . GLN A 1 89  ? -28.17900 18.43700 -6.64400  1.000 24.83170 ? 88  GLN A O   1 
ATOM   732  C  CB  . GLN A 1 89  ? -27.62600 15.12700 -6.20500  1.000 24.57655 ? 88  GLN A CB  1 
ATOM   733  C  CG  . GLN A 1 89  ? -26.68900 15.72900 -5.16600  1.000 26.85126 ? 88  GLN A CG  1 
ATOM   734  C  CD  . GLN A 1 89  ? -25.66000 14.70800 -4.67700  1.000 28.17061 ? 88  GLN A CD  1 
ATOM   735  O  OE1 . GLN A 1 89  ? -24.98100 14.06600 -5.48400  1.000 39.50629 ? 88  GLN A OE1 1 
ATOM   736  N  NE2 . GLN A 1 89  ? -25.52700 14.56600 -3.36600  1.000 27.43409 ? 88  GLN A NE2 1 
ATOM   737  N  N   . ALA A 1 90  ? -27.48300 17.27000 -8.45000  1.000 26.23155 ? 89  ALA A N   1 
ATOM   738  C  CA  . ALA A 1 90  ? -26.74900 18.38600 -9.02600  1.000 28.11579 ? 89  ALA A CA  1 
ATOM   739  C  C   . ALA A 1 90  ? -27.65300 19.51600 -9.47900  1.000 23.77969 ? 89  ALA A C   1 
ATOM   740  O  O   . ALA A 1 90  ? -27.15300 20.61300 -9.74300  1.000 29.56279 ? 89  ALA A O   1 
ATOM   741  C  CB  . ALA A 1 90  ? -25.89300 17.89800 -10.20300 1.000 32.50848 ? 89  ALA A CB  1 
ATOM   742  N  N   . HIS A 1 91  ? -28.97100 19.28700 -9.53400  1.000 24.79765 ? 90  HIS A N   1 
ATOM   743  C  CA  . HIS A 1 91  ? -29.90000 20.28400 -10.05000 1.000 24.65718 ? 90  HIS A CA  1 
ATOM   744  C  C   . HIS A 1 91  ? -30.93100 20.69100 -9.01000  1.000 26.80105 ? 90  HIS A C   1 
ATOM   745  O  O   . HIS A 1 91  ? -31.85800 21.44400 -9.33000  1.000 24.89103 ? 90  HIS A O   1 
ATOM   746  C  CB  . HIS A 1 91  ? -30.55600 19.74200 -11.32600 1.000 25.52440 ? 90  HIS A CB  1 
ATOM   747  C  CG  . HIS A 1 91  ? -29.56300 19.46000 -12.40700 1.000 29.16338 ? 90  HIS A CG  1 
ATOM   748  N  ND1 . HIS A 1 91  ? -29.06100 20.45500 -13.22200 1.000 32.58813 ? 90  HIS A ND1 1 
ATOM   749  C  CD2 . HIS A 1 91  ? -28.94500 18.31200 -12.78400 1.000 29.80000 ? 90  HIS A CD2 1 
ATOM   750  C  CE1 . HIS A 1 91  ? -28.18100 19.93100 -14.05900 1.000 33.42367 ? 90  HIS A CE1 1 
ATOM   751  N  NE2 . HIS A 1 91  ? -28.09000 18.63300 -13.81200 1.000 34.91176 ? 90  HIS A NE2 1 
ATOM   752  N  N   . GLN A 1 92  ? -30.77500 20.24500 -7.76300  1.000 24.37931 ? 91  GLN A N   1 
ATOM   753  C  CA  . GLN A 1 92  ? -31.66300 20.67600 -6.69000  1.000 24.95872 ? 91  GLN A CA  1 
ATOM   754  C  C   . GLN A 1 92  ? -31.47900 22.14900 -6.32800  1.000 24.90509 ? 91  GLN A C   1 
ATOM   755  O  O   . GLN A 1 92  ? -30.46400 22.79200 -6.63900  1.000 24.56881 ? 91  GLN A O   1 
ATOM   756  C  CB  . GLN A 1 92  ? -31.45000 19.80200 -5.44600  1.000 22.27884 ? 91  GLN A CB  1 
ATOM   757  C  CG  . GLN A 1 92  ? -31.96900 18.38600 -5.66500  1.000 21.92565 ? 91  GLN A CG  1 
ATOM   758  C  CD  . GLN A 1 92  ? -31.73500 17.45900 -4.46900  1.000 22.92678 ? 91  GLN A CD  1 
ATOM   759  O  OE1 . GLN A 1 92  ? -31.04800 17.82300 -3.50200  1.000 27.31598 ? 91  GLN A OE1 1 
ATOM   760  N  NE2 . GLN A 1 92  ? -32.25800 16.23500 -4.56500  1.000 23.31428 ? 91  GLN A NE2 1 
ATOM   761  N  N   . GLN A 1 93  ? -32.50500 22.69300 -5.67000  1.000 25.56395 ? 92  GLN A N   1 
ATOM   762  C  CA  . GLN A 1 93  ? -32.49700 24.05800 -5.13200  1.000 25.30428 ? 92  GLN A CA  1 
ATOM   763  C  C   . GLN A 1 93  ? -32.32500 25.11600 -6.23500  1.000 23.11793 ? 92  GLN A C   1 
ATOM   764  O  O   . GLN A 1 93  ? -31.72200 26.16600 -6.01300  1.000 29.61322 ? 92  GLN A O   1 
ATOM   765  C  CB  . GLN A 1 93  ? -31.43900 24.22300 -4.01800  1.000 27.19307 ? 92  GLN A CB  1 
ATOM   766  C  CG  . GLN A 1 93  ? -31.56800 23.10100 -2.96700  1.000 29.72160 ? 92  GLN A CG  1 
ATOM   767  C  CD  . GLN A 1 93  ? -30.97300 23.43500 -1.61400  1.000 33.88648 ? 92  GLN A CD  1 
ATOM   768  O  OE1 . GLN A 1 93  ? -31.11500 24.54000 -1.11600  1.000 41.15214 ? 92  GLN A OE1 1 
ATOM   769  N  NE2 . GLN A 1 93  ? -30.32300 22.47100 -1.00700  1.000 35.07958 ? 92  GLN A NE2 1 
ATOM   770  N  N   . GLN A 1 94  ? -32.87400 24.82400 -7.42600  1.000 25.91140 ? 93  GLN A N   1 
ATOM   771  C  CA  . GLN A 1 94  ? -32.93000 25.75200 -8.55600  1.000 26.26120 ? 93  GLN A CA  1 
ATOM   772  C  C   . GLN A 1 94  ? -34.35900 26.07300 -8.95600  1.000 28.65724 ? 93  GLN A C   1 
ATOM   773  O  O   . GLN A 1 94  ? -34.56400 26.69200 -10.00700 1.000 32.47604 ? 93  GLN A O   1 
ATOM   774  C  CB  . GLN A 1 94  ? -32.23500 25.18500 -9.80200  1.000 30.72219 ? 93  GLN A CB  1 
ATOM   775  C  CG  . GLN A 1 94  ? -30.80100 24.72400 -9.64600  1.000 30.48026 ? 93  GLN A CG  1 
ATOM   776  C  CD  . GLN A 1 94  ? -29.86700 25.86400 -9.43500  1.000 44.45833 ? 93  GLN A CD  1 
ATOM   777  O  OE1 . GLN A 1 94  ? -30.06000 26.92800 -10.00500 1.000 47.74854 ? 93  GLN A OE1 1 
ATOM   778  N  NE2 . GLN A 1 94  ? -28.85400 25.66300 -8.59900  1.000 47.37641 ? 93  GLN A NE2 1 
ATOM   779  N  N   . GLY A 1 95  ? -35.35800 25.61300 -8.19100  1.000 27.39778 ? 94  GLY A N   1 
ATOM   780  C  CA  . GLY A 1 95  ? -36.74300 25.94900 -8.46800  1.000 26.44797 ? 94  GLY A CA  1 
ATOM   781  C  C   . GLY A 1 95  ? -37.50900 24.88200 -9.22600  1.000 24.27209 ? 94  GLY A C   1 
ATOM   782  O  O   . GLY A 1 95  ? -38.70800 25.06600 -9.48000  1.000 28.14253 ? 94  GLY A O   1 
ATOM   783  N  N   . LEU A 1 96  ? -36.86200 23.79100 -9.60400  1.000 24.83709 ? 95  LEU A N   1 
ATOM   784  C  CA  . LEU A 1 96  ? -37.52200 22.82700 -10.49000 1.000 19.94511 ? 95  LEU A CA  1 
ATOM   785  C  C   . LEU A 1 96  ? -38.63100 22.03000 -9.79000  1.000 24.35056 ? 95  LEU A C   1 
ATOM   786  O  O   . LEU A 1 96  ? -39.65100 21.70900 -10.41500 1.000 23.98089 ? 95  LEU A O   1 
ATOM   787  C  CB  . LEU A 1 96  ? -36.48700 21.88700 -11.10800 1.000 23.14261 ? 95  LEU A CB  1 
ATOM   788  C  CG  . LEU A 1 96  ? -35.38300 22.60900 -11.89700 1.000 23.32116 ? 95  LEU A CG  1 
ATOM   789  C  CD1 . LEU A 1 96  ? -34.34300 21.61200 -12.40600 1.000 26.18097 ? 95  LEU A CD1 1 
ATOM   790  C  CD2 . LEU A 1 96  ? -35.97000 23.46500 -13.04900 1.000 26.96168 ? 95  LEU A CD2 1 
ATOM   791  N  N   . GLY A 1 97  ? -38.43000 21.63400 -8.52600  1.000 22.50805 ? 96  GLY A N   1 
ATOM   792  C  CA  . GLY A 1 97  ? -39.50300 20.95600 -7.81700  1.000 20.14664 ? 96  GLY A CA  1 
ATOM   793  C  C   . GLY A 1 97  ? -40.78400 21.76000 -7.81500  1.000 21.65677 ? 96  GLY A C   1 
ATOM   794  O  O   . GLY A 1 97  ? -41.86400 21.22900 -8.11200  1.000 21.52648 ? 96  GLY A O   1 
ATOM   795  N  N   A ARG A 1 98  ? -40.67300 23.05600 -7.50100  0.720 21.98947 ? 97  ARG A N   1 
ATOM   796  N  N   B ARG A 1 98  ? -40.68300 23.05600 -7.52000  0.280 21.59225 ? 97  ARG A N   1 
ATOM   797  C  CA  A ARG A 1 98  ? -41.83000 23.94800 -7.51200  0.720 21.21153 ? 97  ARG A CA  1 
ATOM   798  C  CA  B ARG A 1 98  ? -41.87400 23.89700 -7.51900  0.280 23.05843 ? 97  ARG A CA  1 
ATOM   799  C  C   A ARG A 1 98  ? -42.46500 23.99600 -8.90200  0.720 25.54727 ? 97  ARG A C   1 
ATOM   800  C  C   B ARG A 1 98  ? -42.48300 23.99200 -8.91400  0.280 24.42422 ? 97  ARG A C   1 
ATOM   801  O  O   A ARG A 1 98  ? -43.69200 23.92200 -9.03500  0.720 23.73125 ? 97  ARG A O   1 
ATOM   802  O  O   B ARG A 1 98  ? -43.71100 23.96300 -9.06300  0.280 24.43290 ? 97  ARG A O   1 
ATOM   803  C  CB  A ARG A 1 98  ? -41.41400 25.34900 -7.04100  0.720 25.64112 ? 97  ARG A CB  1 
ATOM   804  C  CB  B ARG A 1 98  ? -41.55500 25.29100 -6.97800  0.280 26.20717 ? 97  ARG A CB  1 
ATOM   805  C  CG  A ARG A 1 98  ? -42.43500 26.45300 -7.33800  0.720 29.82599 ? 97  ARG A CG  1 
ATOM   806  C  CG  B ARG A 1 98  ? -42.79200 26.17400 -6.90900  0.280 29.96606 ? 97  ARG A CG  1 
ATOM   807  C  CD  A ARG A 1 98  ? -43.69400 26.31400 -6.47600  0.720 28.76240 ? 97  ARG A CD  1 
ATOM   808  C  CD  B ARG A 1 98  ? -42.45700 27.61700 -6.57200  0.280 26.28768 ? 97  ARG A CD  1 
ATOM   809  N  NE  A ARG A 1 98  ? -44.56400 27.48900 -6.58300  0.720 30.07351 ? 97  ARG A NE  1 
ATOM   810  N  NE  B ARG A 1 98  ? -43.64100 28.46700 -6.64600  0.280 35.71831 ? 97  ARG A NE  1 
ATOM   811  C  CZ  A ARG A 1 98  ? -44.59800 28.49100 -5.71300  0.720 34.08342 ? 97  ARG A CZ  1 
ATOM   812  C  CZ  B ARG A 1 98  ? -44.26500 28.98100 -5.58900  0.280 38.55713 ? 97  ARG A CZ  1 
ATOM   813  N  NH1 A ARG A 1 98  ? -43.79700 28.49400 -4.64900  0.720 38.88738 ? 97  ARG A NH1 1 
ATOM   814  N  NH1 B ARG A 1 98  ? -43.81800 28.73500 -4.36400  0.280 36.41493 ? 97  ARG A NH1 1 
ATOM   815  N  NH2 A ARG A 1 98  ? -45.42500 29.51300 -5.91700  0.720 39.02360 ? 97  ARG A NH2 1 
ATOM   816  N  NH2 B ARG A 1 98  ? -45.33300 29.75000 -5.75700  0.280 38.80209 ? 97  ARG A NH2 1 
ATOM   817  N  N   . ARG A 1 99  ? -41.64600 24.10900 -9.95100  1.000 23.32465 ? 98  ARG A N   1 
ATOM   818  C  CA  . ARG A 1 99  ? -42.19800 24.20300 -11.30400 1.000 24.06336 ? 98  ARG A CA  1 
ATOM   819  C  C   . ARG A 1 99  ? -42.88200 22.90700 -11.72900 1.000 23.07006 ? 98  ARG A C   1 
ATOM   820  O  O   . ARG A 1 99  ? -43.88200 22.97200 -12.44700 1.000 25.72784 ? 98  ARG A O   1 
ATOM   821  C  CB  . ARG A 1 99  ? -41.11200 24.59900 -12.30300 1.000 23.52437 ? 98  ARG A CB  1 
ATOM   822  C  CG  . ARG A 1 99  ? -40.72400 26.06300 -12.19300 1.000 27.94190 ? 98  ARG A CG  1 
ATOM   823  C  CD  . ARG A 1 99  ? -39.39800 26.34700 -12.92100 1.000 31.33622 ? 98  ARG A CD  1 
ATOM   824  N  NE  . ARG A 1 99  ? -39.52000 26.27200 -14.37500 1.000 34.69120 ? 98  ARG A NE  1 
ATOM   825  C  CZ  . ARG A 1 99  ? -38.49700 26.38000 -15.21800 1.000 36.88457 ? 98  ARG A CZ  1 
ATOM   826  N  NH1 . ARG A 1 99  ? -37.26500 26.57600 -14.74700 1.000 38.65659 ? 98  ARG A NH1 1 
ATOM   827  N  NH2 . ARG A 1 99  ? -38.70300 26.30800 -16.53700 1.000 34.91938 ? 98  ARG A NH2 1 
ATOM   828  N  N   . LEU A 1 100 ? -42.36900 21.74500 -11.31800 1.000 19.85659 ? 99  LEU A N   1 
ATOM   829  C  CA  . LEU A 1 100 ? -43.06900 20.51300 -11.66700 1.000 19.86766 ? 99  LEU A CA  1 
ATOM   830  C  C   . LEU A 1 100 ? -44.39300 20.41300 -10.91900 1.000 23.19450 ? 99  LEU A C   1 
ATOM   831  O  O   . LEU A 1 100 ? -45.40500 20.01200 -11.50600 1.000 22.32767 ? 99  LEU A O   1 
ATOM   832  C  CB  . LEU A 1 100 ? -42.18100 19.29000 -11.37600 1.000 20.24535 ? 99  LEU A CB  1 
ATOM   833  C  CG  . LEU A 1 100 ? -41.02700 19.02900 -12.35700 1.000 22.63842 ? 99  LEU A CG  1 
ATOM   834  C  CD1 . LEU A 1 100 ? -40.00200 18.09500 -11.66800 1.000 25.72245 ? 99  LEU A CD1 1 
ATOM   835  C  CD2 . LEU A 1 100 ? -41.53500 18.37100 -13.64300 1.000 27.02651 ? 99  LEU A CD2 1 
ATOM   836  N  N   . LEU A 1 101 ? -44.41800 20.81100 -9.63600  1.000 20.46754 ? 100 LEU A N   1 
ATOM   837  C  CA  . LEU A 1 101 ? -45.68800 20.79000 -8.90300  1.000 21.06731 ? 100 LEU A CA  1 
ATOM   838  C  C   . LEU A 1 101 ? -46.70200 21.72600 -9.54200  1.000 22.96356 ? 100 LEU A C   1 
ATOM   839  O  O   . LEU A 1 101 ? -47.90300 21.41800 -9.61400  1.000 24.83116 ? 100 LEU A O   1 
ATOM   840  C  CB  . LEU A 1 101 ? -45.46400 21.18600 -7.43600  1.000 22.28999 ? 100 LEU A CB  1 
ATOM   841  C  CG  . LEU A 1 101 ? -44.77000 20.08400 -6.61600  1.000 22.45430 ? 100 LEU A CG  1 
ATOM   842  C  CD1 . LEU A 1 101 ? -44.17000 20.67800 -5.33800  1.000 26.72407 ? 100 LEU A CD1 1 
ATOM   843  C  CD2 . LEU A 1 101 ? -45.75500 18.97200 -6.23900  1.000 26.87234 ? 100 LEU A CD2 1 
ATOM   844  N  N   . GLU A 1 102 ? -46.23900 22.89300 -9.98900  1.000 22.76691 ? 101 GLU A N   1 
ATOM   845  C  CA  . GLU A 1 102 ? -47.14400 23.82200 -10.66300 1.000 24.25500 ? 101 GLU A CA  1 
ATOM   846  C  C   . GLU A 1 102 ? -47.77200 23.18900 -11.89900 1.000 24.96912 ? 101 GLU A C   1 
ATOM   847  O  O   . GLU A 1 102 ? -48.98400 23.31800 -12.12400 1.000 26.77972 ? 101 GLU A O   1 
ATOM   848  C  CB  . GLU A 1 102 ? -46.38400 25.10800 -11.00900 1.000 25.94772 ? 101 GLU A CB  1 
ATOM   849  C  CG  . GLU A 1 102 ? -46.24700 26.02200 -9.76700  1.000 33.35001 ? 101 GLU A CG  1 
ATOM   850  C  CD  . GLU A 1 102 ? -45.42100 27.28800 -9.96100  1.000 41.31525 ? 101 GLU A CD  1 
ATOM   851  O  OE1 . GLU A 1 102 ? -44.61600 27.34400 -10.91100 1.000 44.79707 ? 101 GLU A OE1 1 
ATOM   852  O  OE2 . GLU A 1 102 ? -45.56800 28.22100 -9.13200  1.000 40.42925 ? 101 GLU A OE2 1 
ATOM   853  N  N   . ARG A 1 103 ? -46.97400 22.45000 -12.68100 1.000 23.61148 ? 102 ARG A N   1 
ATOM   854  C  CA  . ARG A 1 103 ? -47.50500 21.76300 -13.85400 1.000 25.30204 ? 102 ARG A CA  1 
ATOM   855  C  C   . ARG A 1 103 ? -48.54300 20.71300 -13.46900 1.000 23.02048 ? 102 ARG A C   1 
ATOM   856  O  O   . ARG A 1 103 ? -49.58500 20.57900 -14.13600 1.000 27.52471 ? 102 ARG A O   1 
ATOM   857  C  CB  . ARG A 1 103 ? -46.35600 21.11900 -14.61700 1.000 27.61076 ? 102 ARG A CB  1 
ATOM   858  C  CG  . ARG A 1 103 ? -46.78800 20.48400 -15.89500 1.000 30.10366 ? 102 ARG A CG  1 
ATOM   859  C  CD  . ARG A 1 103 ? -47.49300 21.48100 -16.82300 1.000 33.57334 ? 102 ARG A CD  1 
ATOM   860  N  NE  . ARG A 1 103 ? -47.65000 20.78800 -18.08300 1.000 40.69882 ? 102 ARG A NE  1 
ATOM   861  C  CZ  . ARG A 1 103 ? -46.78500 20.85000 -19.08800 1.000 40.57991 ? 102 ARG A CZ  1 
ATOM   862  N  NH1 . ARG A 1 103 ? -47.00600 20.11200 -20.16700 1.000 36.12175 ? 102 ARG A NH1 1 
ATOM   863  N  NH2 . ARG A 1 103 ? -45.74000 21.67400 -19.03100 1.000 36.60154 ? 102 ARG A NH2 1 
ATOM   864  N  N   . ALA A 1 104 ? -48.27100 19.95200 -12.40700 1.000 22.86212 ? 103 ALA A N   1 
ATOM   865  C  CA  . ALA A 1 104 ? -49.19100 18.89400 -11.99400 1.000 21.81663 ? 103 ALA A CA  1 
ATOM   866  C  C   . ALA A 1 104 ? -50.52000 19.48700 -11.54700 1.000 20.82205 ? 103 ALA A C   1 
ATOM   867  O  O   . ALA A 1 104 ? -51.58000 18.92800 -11.83900 1.000 24.46660 ? 103 ALA A O   1 
ATOM   868  C  CB  . ALA A 1 104 ? -48.56800 18.05300 -10.86900 1.000 25.05159 ? 103 ALA A CB  1 
ATOM   869  N  N   A VAL A 1 105 ? -50.49000 20.61700 -10.83500 0.570 23.01031 ? 104 VAL A N   1 
ATOM   870  N  N   B VAL A 1 105 ? -50.48200 20.61500 -10.83800 0.430 22.90172 ? 104 VAL A N   1 
ATOM   871  C  CA  A VAL A 1 105 ? -51.76200 21.18800 -10.40600 0.570 25.10004 ? 104 VAL A CA  1 
ATOM   872  C  CA  B VAL A 1 105 ? -51.72600 21.23300 -10.39600 0.430 24.43249 ? 104 VAL A CA  1 
ATOM   873  C  C   A VAL A 1 105 ? -52.51000 21.79300 -11.58800 0.570 26.26873 ? 104 VAL A C   1 
ATOM   874  C  C   B VAL A 1 105 ? -52.50000 21.78800 -11.58600 0.430 26.12065 ? 104 VAL A C   1 
ATOM   875  O  O   A VAL A 1 105 ? -53.74400 21.73500 -11.63400 0.570 25.61942 ? 104 VAL A O   1 
ATOM   876  O  O   B VAL A 1 105 ? -53.73100 21.68900 -11.63800 0.430 25.24762 ? 104 VAL A O   1 
ATOM   877  C  CB  A VAL A 1 105 ? -51.56900 22.19900 -9.25600  0.570 25.51991 ? 104 VAL A CB  1 
ATOM   878  C  CB  B VAL A 1 105 ? -51.43900 22.30500 -9.33100  0.430 24.77165 ? 104 VAL A CB  1 
ATOM   879  C  CG1 A VAL A 1 105 ? -50.78100 23.39900 -9.69400  0.570 27.71476 ? 104 VAL A CG1 1 
ATOM   880  C  CG1 B VAL A 1 105 ? -52.72400 23.02000 -8.95000  0.430 28.28077 ? 104 VAL A CG1 1 
ATOM   881  C  CG2 A VAL A 1 105 ? -52.92800 22.60900 -8.68600  0.570 26.67753 ? 104 VAL A CG2 1 
ATOM   882  C  CG2 B VAL A 1 105 ? -50.81300 21.64700 -8.09900  0.430 20.59313 ? 104 VAL A CG2 1 
ATOM   883  N  N   . THR A 1 106 ? -51.79800 22.38100 -12.55700 1.000 26.97540 ? 105 THR A N   1 
ATOM   884  C  CA  . THR A 1 106 ? -52.46700 22.87900 -13.75400 1.000 25.05410 ? 105 THR A CA  1 
ATOM   885  C  C   . THR A 1 106 ? -53.15300 21.73000 -14.49800 1.000 27.04319 ? 105 THR A C   1 
ATOM   886  O  O   . THR A 1 106 ? -54.28800 21.87300 -14.98000 1.000 32.07608 ? 105 THR A O   1 
ATOM   887  C  CB  . THR A 1 106 ? -51.42600 23.58900 -14.63000 1.000 29.40239 ? 105 THR A CB  1 
ATOM   888  O  OG1 . THR A 1 106 ? -51.01900 24.81000 -13.98900 1.000 32.51146 ? 105 THR A OG1 1 
ATOM   889  C  CG2 . THR A 1 106 ? -51.96000 23.90900 -16.01300 1.000 33.09429 ? 105 THR A CG2 1 
ATOM   890  N  N   . TYR A 1 107 ? -52.49400 20.57900 -14.55900 1.000 28.10424 ? 106 TYR A N   1 
ATOM   891  C  CA  . TYR A 1 107 ? -53.09800 19.41700 -15.21000 1.000 25.88495 ? 106 TYR A CA  1 
ATOM   892  C  C   . TYR A 1 107 ? -54.27400 18.88300 -14.40300 1.000 28.78500 ? 106 TYR A C   1 
ATOM   893  O  O   . TYR A 1 107 ? -55.29800 18.47300 -14.97300 1.000 29.06064 ? 106 TYR A O   1 
ATOM   894  C  CB  . TYR A 1 107 ? -52.03400 18.32700 -15.39700 1.000 25.27086 ? 106 TYR A CB  1 
ATOM   895  C  CG  . TYR A 1 107 ? -52.55000 17.01000 -15.95000 1.000 24.36903 ? 106 TYR A CG  1 
ATOM   896  C  CD1 . TYR A 1 107 ? -52.60800 16.79400 -17.30800 1.000 25.23426 ? 106 TYR A CD1 1 
ATOM   897  C  CD2 . TYR A 1 107 ? -52.90600 15.97900 -15.09100 1.000 22.57245 ? 106 TYR A CD2 1 
ATOM   898  C  CE1 . TYR A 1 107 ? -53.05800 15.54000 -17.81200 1.000 30.42972 ? 106 TYR A CE1 1 
ATOM   899  C  CE2 . TYR A 1 107 ? -53.35300 14.75800 -15.57400 1.000 27.35408 ? 106 TYR A CE2 1 
ATOM   900  C  CZ  . TYR A 1 107 ? -53.43000 14.55900 -16.92400 1.000 32.05647 ? 106 TYR A CZ  1 
ATOM   901  O  OH  . TYR A 1 107 ? -53.87400 13.33400 -17.39000 1.000 36.17765 ? 106 TYR A OH  1 
ATOM   902  N  N   . ALA A 1 108 ? -54.13300 18.84600 -13.07500 1.000 24.86414 ? 107 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 108 ? -55.25000 18.41400 -12.23900 1.000 28.45017 ? 107 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 108 ? -56.47300 19.29300 -12.47400 1.000 28.68360 ? 107 ALA A C   1 
ATOM   905  O  O   . ALA A 1 108 ? -57.59700 18.78500 -12.58000 1.000 30.50671 ? 107 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 108 ? -54.85000 18.43200 -10.76300 1.000 25.29554 ? 107 ALA A CB  1 
ATOM   907  N  N   . HIS A 1 109 ? -56.28300 20.62000 -12.56900 1.000 27.59513 ? 108 HIS A N   1 
ATOM   908  C  CA  . HIS A 1 109 ? -57.42400 21.48000 -12.86400 1.000 29.19769 ? 108 HIS A CA  1 
ATOM   909  C  C   . HIS A 1 109 ? -57.98300 21.22800 -14.26300 1.000 32.21421 ? 108 HIS A C   1 
ATOM   910  O  O   . HIS A 1 109 ? -59.20500 21.15000 -14.44100 1.000 33.98942 ? 108 HIS A O   1 
ATOM   911  C  CB  . HIS A 1 109 ? -57.04500 22.95700 -12.70800 1.000 33.89913 ? 108 HIS A CB  1 
ATOM   912  C  CG  . HIS A 1 109 ? -58.22200 23.85600 -12.87900 1.000 38.09995 ? 108 HIS A CG  1 
ATOM   913  N  ND1 . HIS A 1 109 ? -58.56500 24.41300 -14.09300 1.000 43.19791 ? 108 HIS A ND1 1 
ATOM   914  C  CD2 . HIS A 1 109 ? -59.18900 24.22100 -12.00700 1.000 42.46989 ? 108 HIS A CD2 1 
ATOM   915  C  CE1 . HIS A 1 109 ? -59.66000 25.13700 -13.94200 1.000 46.56140 ? 108 HIS A CE1 1 
ATOM   916  N  NE2 . HIS A 1 109 ? -60.06900 25.01800 -12.69100 1.000 46.15074 ? 108 HIS A NE2 1 
ATOM   917  N  N   . ALA A 1 110 ? -57.11300 21.09200 -15.27400 1.000 30.54139 ? 109 ALA A N   1 
ATOM   918  C  CA  . ALA A 1 110 ? -57.61000 20.90800 -16.63600 1.000 34.53966 ? 109 ALA A CA  1 
ATOM   919  C  C   . ALA A 1 110 ? -58.39200 19.60400 -16.79700 1.000 32.83553 ? 109 ALA A C   1 
ATOM   920  O  O   . ALA A 1 110 ? -59.29600 19.53800 -17.64100 1.000 38.57482 ? 109 ALA A O   1 
ATOM   921  C  CB  . ALA A 1 110 ? -56.45500 20.93700 -17.63300 1.000 38.67241 ? 109 ALA A CB  1 
ATOM   922  N  N   . SER A 1 111 ? -58.05400 18.57400 -16.00700 1.000 34.77433 ? 110 SER A N   1 
ATOM   923  C  CA  . SER A 1 111 ? -58.67700 17.25400 -16.08200 1.000 33.16821 ? 110 SER A CA  1 
ATOM   924  C  C   . SER A 1 111 ? -59.77200 17.07700 -15.04500 1.000 35.51168 ? 110 SER A C   1 
ATOM   925  O  O   . SER A 1 111 ? -60.27000 15.95600 -14.85000 1.000 35.46468 ? 110 SER A O   1 
ATOM   926  C  CB  . SER A 1 111 ? -57.62800 16.15000 -15.93400 1.000 32.00962 ? 110 SER A CB  1 
ATOM   927  O  OG  . SER A 1 111 ? -57.00600 16.22400 -14.67600 1.000 31.02534 ? 110 SER A OG  1 
ATOM   928  N  N   . HIS A 1 112 ? -60.17400 18.17200 -14.40100 1.000 33.72137 ? 111 HIS A N   1 
ATOM   929  C  CA  . HIS A 1 112 ? -61.30800 18.21900 -13.48300 1.000 32.35927 ? 111 HIS A CA  1 
ATOM   930  C  C   . HIS A 1 112 ? -61.10200 17.35900 -12.23800 1.000 30.80498 ? 111 HIS A C   1 
ATOM   931  O  O   . HIS A 1 112 ? -62.04600 16.77700 -11.71100 1.000 32.32437 ? 111 HIS A O   1 
ATOM   932  C  CB  . HIS A 1 112 ? -62.63300 17.85200 -14.18200 1.000 34.91129 ? 111 HIS A CB  1 
ATOM   933  C  CG  . HIS A 1 112 ? -63.77300 18.68800 -13.71200 1.000 36.54729 ? 111 HIS A CG  1 
ATOM   934  N  ND1 . HIS A 1 112 ? -64.62800 18.29500 -12.70500 1.000 37.75475 ? 111 HIS A ND1 1 
ATOM   935  C  CD2 . HIS A 1 112 ? -64.16300 19.93400 -14.07200 1.000 38.08987 ? 111 HIS A CD2 1 
ATOM   936  C  CE1 . HIS A 1 112 ? -65.48500 19.26600 -12.45800 1.000 39.33134 ? 111 HIS A CE1 1 
ATOM   937  N  NE2 . HIS A 1 112 ? -65.22500 20.27200 -13.27500 1.000 39.73939 ? 111 HIS A NE2 1 
ATOM   938  N  N   . CYS A 1 113 ? -59.87500 17.31000 -11.72600 1.000 30.56555 ? 112 CYS A N   1 
ATOM   939  C  CA  . CYS A 1 113 ? -59.62500 16.70200 -10.42100 1.000 33.94761 ? 112 CYS A CA  1 
ATOM   940  C  C   . CYS A 1 113 ? -60.05700 17.64200 -9.30500  1.000 32.65230 ? 112 CYS A C   1 
ATOM   941  O  O   . CYS A 1 113 ? -59.82700 18.86000 -9.36500  1.000 33.84281 ? 112 CYS A O   1 
ATOM   942  C  CB  . CYS A 1 113 ? -58.13700 16.36400 -10.22600 1.000 30.41000 ? 112 CYS A CB  1 
ATOM   943  S  SG  . CYS A 1 113 ? -57.45500 15.18900 -11.39900 1.000 32.38802 ? 112 CYS A SG  1 
ATOM   944  N  N   . ARG A 1 114 ? -60.62400 17.05800 -8.25200  1.000 28.33436 ? 113 ARG A N   1 
ATOM   945  C  CA  . ARG A 1 114 ? -61.03300 17.81200 -7.07600  1.000 29.59269 ? 113 ARG A CA  1 
ATOM   946  C  C   . ARG A 1 114 ? -59.84700 18.21200 -6.20400  1.000 31.43888 ? 113 ARG A C   1 
ATOM   947  O  O   . ARG A 1 114 ? -59.87500 19.28000 -5.58100  1.000 33.62223 ? 113 ARG A O   1 
ATOM   948  C  CB  . ARG A 1 114 ? -62.02100 16.99800 -6.23700  1.000 35.37899 ? 113 ARG A CB  1 
ATOM   949  C  CG  . ARG A 1 114 ? -62.53100 17.78000 -5.02400  1.000 44.38632 ? 113 ARG A CG  1 
ATOM   950  C  CD  . ARG A 1 114 ? -63.53000 17.00800 -4.18400  1.000 60.65588 ? 113 ARG A CD  1 
ATOM   951  N  NE  . ARG A 1 114 ? -63.88600 17.77300 -2.99200  1.000 63.54110 ? 113 ARG A NE  1 
ATOM   952  C  CZ  . ARG A 1 114 ? -63.12900 17.86800 -1.90000  1.000 56.68786 ? 113 ARG A CZ  1 
ATOM   953  N  NH1 . ARG A 1 114 ? -61.95300 17.23400 -1.82400  1.000 45.43954 ? 113 ARG A NH1 1 
ATOM   954  N  NH2 . ARG A 1 114 ? -63.55300 18.60100 -0.87900  1.000 60.08026 ? 113 ARG A NH2 1 
ATOM   955  N  N   . ALA A 1 115 ? -58.82400 17.37900 -6.12600  1.000 28.51091 ? 114 ALA A N   1 
ATOM   956  C  CA  . ALA A 1 115 ? -57.73700 17.58700 -5.17600  1.000 27.66097 ? 114 ALA A CA  1 
ATOM   957  C  C   . ALA A 1 115 ? -56.51100 16.82900 -5.64700  1.000 24.07364 ? 114 ALA A C   1 
ATOM   958  O  O   . ALA A 1 115 ? -56.59300 15.97300 -6.53300  1.000 27.34536 ? 114 ALA A O   1 
ATOM   959  C  CB  . ALA A 1 115 ? -58.10800 17.11400 -3.76500  1.000 30.31939 ? 114 ALA A CB  1 
ATOM   960  N  N   . LEU A 1 116 ? -55.36500 17.16400 -5.03200  1.000 23.01805 ? 115 LEU A N   1 
ATOM   961  C  CA  . LEU A 1 116 ? -54.10000 16.45000 -5.18400  1.000 22.27101 ? 115 LEU A CA  1 
ATOM   962  C  C   . LEU A 1 116 ? -53.70800 15.84100 -3.83900  1.000 22.94915 ? 115 LEU A C   1 
ATOM   963  O  O   . LEU A 1 116 ? -54.00100 16.39600 -2.77400  1.000 24.95487 ? 115 LEU A O   1 
ATOM   964  C  CB  . LEU A 1 116 ? -52.94800 17.33500 -5.68800  1.000 25.12867 ? 115 LEU A CB  1 
ATOM   965  C  CG  . LEU A 1 116 ? -53.08600 17.92400 -7.10100  1.000 26.46275 ? 115 LEU A CG  1 
ATOM   966  C  CD1 . LEU A 1 116 ? -53.90300 19.18800 -7.06300  1.000 30.65255 ? 115 LEU A CD1 1 
ATOM   967  C  CD2 . LEU A 1 116 ? -51.70100 18.17000 -7.68300  1.000 28.83027 ? 115 LEU A CD2 1 
ATOM   968  N  N   . THR A 1 117 ? -53.07700 14.67800 -3.88600  1.000 22.40834 ? 116 THR A N   1 
ATOM   969  C  CA  . THR A 1 117 ? -52.66900 13.98600 -2.66100  1.000 19.64602 ? 116 THR A CA  1 
ATOM   970  C  C   . THR A 1 117 ? -51.21300 13.52000 -2.74800  1.000 24.85362 ? 116 THR A C   1 
ATOM   971  O  O   . THR A 1 117 ? -50.63200 13.39000 -3.83300  1.000 21.78528 ? 116 THR A O   1 
ATOM   972  C  CB  . THR A 1 117 ? -53.57700 12.75400 -2.35900  1.000 23.16587 ? 116 THR A CB  1 
ATOM   973  O  OG1 . THR A 1 117 ? -53.48100 11.81300 -3.42100  1.000 23.68082 ? 116 THR A OG1 1 
ATOM   974  C  CG2 . THR A 1 117 ? -55.06100 13.14700 -2.24900  1.000 25.14381 ? 116 THR A CG2 1 
ATOM   975  N  N   . LEU A 1 118 ? -50.64700 13.22200 -1.57600  1.000 21.49024 ? 117 LEU A N   1 
ATOM   976  C  CA  . LEU A 1 118 ? -49.31600 12.63800 -1.47200  1.000 20.24555 ? 117 LEU A CA  1 
ATOM   977  C  C   . LEU A 1 118 ? -49.13200 12.08400 -0.05900  1.000 20.29144 ? 117 LEU A C   1 
ATOM   978  O  O   . LEU A 1 118 ? -49.95200 12.30600 0.83800   1.000 21.88847 ? 117 LEU A O   1 
ATOM   979  C  CB  . LEU A 1 118 ? -48.22000 13.66700 -1.81200  1.000 19.18115 ? 117 LEU A CB  1 
ATOM   980  C  CG  . LEU A 1 118 ? -48.16100 14.94900 -0.97700  1.000 25.50958 ? 117 LEU A CG  1 
ATOM   981  C  CD1 . LEU A 1 118 ? -47.41900 14.71800 0.35400   1.000 21.75781 ? 117 LEU A CD1 1 
ATOM   982  C  CD2 . LEU A 1 118 ? -47.46600 16.06000 -1.77200  1.000 22.23505 ? 117 LEU A CD2 1 
ATOM   983  N  N   . THR A 1 119 ? -48.06300 11.31300 0.11200   1.000 19.55265 ? 118 THR A N   1 
ATOM   984  C  CA  . THR A 1 119 ? -47.56800 10.94300 1.44600   1.000 21.46583 ? 118 THR A CA  1 
ATOM   985  C  C   . THR A 1 119 ? -46.09300 11.31400 1.50900   1.000 20.52559 ? 118 THR A C   1 
ATOM   986  O  O   . THR A 1 119 ? -45.39100 11.26100 0.49700   1.000 21.92926 ? 118 THR A O   1 
ATOM   987  C  CB  . THR A 1 119 ? -47.72700 9.41100  1.82200   1.000 23.85075 ? 118 THR A CB  1 
ATOM   988  O  OG1 . THR A 1 119 ? -46.91600 8.54700  0.98700   1.000 24.82894 ? 118 THR A OG1 1 
ATOM   989  C  CG2 . THR A 1 119 ? -49.17900 8.95100  1.80300   1.000 25.54089 ? 118 THR A CG2 1 
ATOM   990  N  N   . THR A 1 120 ? -45.62200 11.69400 2.68700   1.000 19.35722 ? 119 THR A N   1 
ATOM   991  C  CA  . THR A 1 120 ? -44.26000 12.22700 2.77400   1.000 20.05424 ? 119 THR A CA  1 
ATOM   992  C  C   . THR A 1 120 ? -43.82900 12.29100 4.24100   1.000 22.83681 ? 119 THR A C   1 
ATOM   993  O  O   . THR A 1 120 ? -44.58900 11.93200 5.14300   1.000 23.92833 ? 119 THR A O   1 
ATOM   994  C  CB  . THR A 1 120 ? -44.17400 13.60400 2.12000   1.000 22.10250 ? 119 THR A CB  1 
ATOM   995  O  OG1 . THR A 1 120 ? -42.78300 13.92700 1.90500   1.000 23.98528 ? 119 THR A OG1 1 
ATOM   996  C  CG2 . THR A 1 120 ? -44.81900 14.66400 3.02700   1.000 22.16400 ? 119 THR A CG2 1 
ATOM   997  N  N   . PHE A 1 121 ? -42.56900 12.69600 4.46000   1.000 20.11447 ? 120 PHE A N   1 
ATOM   998  C  CA  . PHE A 1 121 ? -42.04100 12.86000 5.81900   1.000 20.88327 ? 120 PHE A CA  1 
ATOM   999  C  C   . PHE A 1 121 ? -42.51500 14.17400 6.43400   1.000 24.56407 ? 120 PHE A C   1 
ATOM   1000 O  O   . PHE A 1 121 ? -42.45700 15.23900 5.79400   1.000 24.26060 ? 120 PHE A O   1 
ATOM   1001 C  CB  . PHE A 1 121 ? -40.50200 12.86000 5.83800   1.000 22.70636 ? 120 PHE A CB  1 
ATOM   1002 C  CG  . PHE A 1 121 ? -39.87800 11.52100 5.59200   1.000 20.02626 ? 120 PHE A CG  1 
ATOM   1003 C  CD1 . PHE A 1 121 ? -40.01000 10.46000 6.51900   1.000 20.70331 ? 120 PHE A CD1 1 
ATOM   1004 C  CD2 . PHE A 1 121 ? -39.14800 11.29500 4.42700   1.000 20.39556 ? 120 PHE A CD2 1 
ATOM   1005 C  CE1 . PHE A 1 121 ? -39.42700 9.21600  6.27200   1.000 23.00143 ? 120 PHE A CE1 1 
ATOM   1006 C  CE2 . PHE A 1 121 ? -38.56000 10.04400 4.20800   1.000 21.99717 ? 120 PHE A CE2 1 
ATOM   1007 C  CZ  . PHE A 1 121 ? -38.71700 9.01800  5.12100   1.000 23.93049 ? 120 PHE A CZ  1 
ATOM   1008 N  N   . CYS A 1 122 ? -42.91700 14.10900 7.70500   1.000 21.95201 ? 121 CYS A N   1 
ATOM   1009 C  CA  . CYS A 1 122 ? -43.42400 15.28500 8.42200   1.000 24.23986 ? 121 CYS A CA  1 
ATOM   1010 C  C   . CYS A 1 122 ? -42.34700 16.34300 8.67900   1.000 30.19633 ? 121 CYS A C   1 
ATOM   1011 O  O   . CYS A 1 122 ? -42.63200 17.55100 8.59900   1.000 31.04148 ? 121 CYS A O   1 
ATOM   1012 C  CB  . CYS A 1 122 ? -44.00800 14.85900 9.76600   1.000 30.54805 ? 121 CYS A CB  1 
ATOM   1013 S  SG  . CYS A 1 122 ? -45.40300 13.74500 9.66500   1.000 31.70981 ? 121 CYS A SG  1 
ATOM   1014 N  N   . ASP A 1 123 ? -41.13000 15.91900 9.05100   1.000 27.25610 ? 122 ASP A N   1 
ATOM   1015 C  CA  . ASP A 1 123 ? -40.11400 16.81200 9.60900   1.000 32.51768 ? 122 ASP A CA  1 
ATOM   1016 C  C   . ASP A 1 123 ? -38.84300 16.89300 8.76200   1.000 35.34058 ? 122 ASP A C   1 
ATOM   1017 O  O   . ASP A 1 123 ? -37.78400 17.26100 9.28800   1.000 48.19099 ? 122 ASP A O   1 
ATOM   1018 C  CB  . ASP A 1 123 ? -39.71500 16.38000 11.02500  1.000 40.55543 ? 122 ASP A CB  1 
ATOM   1019 C  CG  . ASP A 1 123 ? -40.88900 16.27400 11.97500  1.000 49.50577 ? 122 ASP A CG  1 
ATOM   1020 O  OD1 . ASP A 1 123 ? -41.78000 17.14000 11.94500  1.000 54.45267 ? 122 ASP A OD1 1 
ATOM   1021 O  OD2 . ASP A 1 123 ? -40.90500 15.31400 12.77200  1.000 56.69023 ? 122 ASP A OD2 1 
ATOM   1022 N  N   . VAL A 1 124 ? -38.89800 16.51500 7.48900   1.000 26.68906 ? 123 VAL A N   1 
ATOM   1023 C  CA  . VAL A 1 124 ? -37.79900 16.73200 6.54600   1.000 25.49604 ? 123 VAL A CA  1 
ATOM   1024 C  C   . VAL A 1 124 ? -38.07400 18.05900 5.84900   1.000 28.38186 ? 123 VAL A C   1 
ATOM   1025 O  O   . VAL A 1 124 ? -39.18300 18.26200 5.33400   1.000 27.34781 ? 123 VAL A O   1 
ATOM   1026 C  CB  . VAL A 1 124 ? -37.67900 15.55300 5.56300   1.000 22.77182 ? 123 VAL A CB  1 
ATOM   1027 C  CG1 . VAL A 1 124 ? -36.70700 15.86600 4.44000   1.000 24.26147 ? 123 VAL A CG1 1 
ATOM   1028 C  CG2 . VAL A 1 124 ? -37.19700 14.30300 6.31000   1.000 24.31186 ? 123 VAL A CG2 1 
ATOM   1029 N  N   . PRO A 1 125 ? -37.12700 19.00600 5.83600   1.000 29.39448 ? 124 PRO A N   1 
ATOM   1030 C  CA  . PRO A 1 125 ? -37.48700 20.37700 5.41100   1.000 30.37587 ? 124 PRO A CA  1 
ATOM   1031 C  C   . PRO A 1 125 ? -37.94900 20.48500 3.97000   1.000 29.17843 ? 124 PRO A C   1 
ATOM   1032 O  O   . PRO A 1 125 ? -38.73700 21.38700 3.64600   1.000 29.72293 ? 124 PRO A O   1 
ATOM   1033 C  CB  . PRO A 1 125 ? -36.19900 21.19000 5.63200   1.000 31.28938 ? 124 PRO A CB  1 
ATOM   1034 C  CG  . PRO A 1 125 ? -35.32000 20.35700 6.49400   1.000 32.34596 ? 124 PRO A CG  1 
ATOM   1035 C  CD  . PRO A 1 125 ? -35.74700 18.90600 6.34800   1.000 30.08466 ? 124 PRO A CD  1 
ATOM   1036 N  N   . TRP A 1 126 ? -37.48400 19.60600 3.08100   1.000 28.93599 ? 125 TRP A N   1 
ATOM   1037 C  CA  . TRP A 1 126 ? -37.90400 19.64600 1.69200   1.000 26.51054 ? 125 TRP A CA  1 
ATOM   1038 C  C   . TRP A 1 126 ? -39.08800 18.72600 1.43000   1.000 23.06374 ? 125 TRP A C   1 
ATOM   1039 O  O   . TRP A 1 126 ? -39.40800 18.46800 0.26600   1.000 26.49313 ? 125 TRP A O   1 
ATOM   1040 C  CB  . TRP A 1 126 ? -36.71700 19.30000 0.75900   1.000 25.76086 ? 125 TRP A CB  1 
ATOM   1041 C  CG  . TRP A 1 126 ? -36.15300 17.89500 0.96800   1.000 25.13675 ? 125 TRP A CG  1 
ATOM   1042 C  CD1 . TRP A 1 126 ? -36.61700 16.74000 0.39500   1.000 23.64060 ? 125 TRP A CD1 1 
ATOM   1043 C  CD2 . TRP A 1 126 ? -35.03700 17.52400 1.77800   1.000 26.67599 ? 125 TRP A CD2 1 
ATOM   1044 N  NE1 . TRP A 1 126 ? -35.86400 15.67100 0.82500   1.000 23.12816 ? 125 TRP A NE1 1 
ATOM   1045 C  CE2 . TRP A 1 126 ? -34.88300 16.12100 1.66300   1.000 23.26102 ? 125 TRP A CE2 1 
ATOM   1046 C  CE3 . TRP A 1 126 ? -34.14100 18.23700 2.59500   1.000 30.62735 ? 125 TRP A CE3 1 
ATOM   1047 C  CZ2 . TRP A 1 126 ? -33.88500 15.42200 2.33100   1.000 25.60053 ? 125 TRP A CZ2 1 
ATOM   1048 C  CZ3 . TRP A 1 126 ? -33.13200 17.53000 3.26200   1.000 31.48844 ? 125 TRP A CZ3 1 
ATOM   1049 C  CH2 . TRP A 1 126 ? -33.00900 16.14200 3.11400   1.000 34.24358 ? 125 TRP A CH2 1 
ATOM   1050 N  N   . ASN A 1 127 ? -39.74000 18.21000 2.48800   1.000 21.20102 ? 126 ASN A N   1 
ATOM   1051 C  CA  . ASN A 1 127 ? -40.96700 17.42800 2.33800   1.000 21.45329 ? 126 ASN A CA  1 
ATOM   1052 C  C   . ASN A 1 127 ? -42.17800 18.19300 2.90500   1.000 22.79904 ? 126 ASN A C   1 
ATOM   1053 O  O   . ASN A 1 127 ? -42.53200 19.24300 2.35600   1.000 21.84625 ? 126 ASN A O   1 
ATOM   1054 C  CB  . ASN A 1 127 ? -40.80500 16.03500 2.97200   1.000 21.50748 ? 126 ASN A CB  1 
ATOM   1055 C  CG  . ASN A 1 127 ? -39.88800 15.10500 2.16900   1.000 24.15939 ? 126 ASN A CG  1 
ATOM   1056 O  OD1 . ASN A 1 127 ? -39.48600 14.06600 2.68700   1.000 24.19867 ? 126 ASN A OD1 1 
ATOM   1057 N  ND2 . ASN A 1 127 ? -39.58600 15.45000 0.90600   1.000 22.66781 ? 126 ASN A ND2 1 
ATOM   1058 N  N   . ALA A 1 128 ? -42.77000 17.77100 4.02400   1.000 25.24265 ? 127 ALA A N   1 
ATOM   1059 C  CA  . ALA A 1 128 ? -44.06300 18.34100 4.41200   1.000 22.81253 ? 127 ALA A CA  1 
ATOM   1060 C  C   . ALA A 1 128 ? -44.03800 19.85200 4.60400   1.000 24.84853 ? 127 ALA A C   1 
ATOM   1061 O  O   . ALA A 1 128 ? -44.99500 20.51200 4.15400   1.000 23.09533 ? 127 ALA A O   1 
ATOM   1062 C  CB  . ALA A 1 128 ? -44.61000 17.64100 5.67200   1.000 22.70568 ? 127 ALA A CB  1 
ATOM   1063 N  N   . PRO A 1 129 ? -43.02700 20.45700 5.24300   1.000 24.18253 ? 128 PRO A N   1 
ATOM   1064 C  CA  . PRO A 1 129 ? -43.05400 21.93000 5.38400   1.000 25.13418 ? 128 PRO A CA  1 
ATOM   1065 C  C   . PRO A 1 129 ? -43.08800 22.67600 4.06000   1.000 26.12645 ? 128 PRO A C   1 
ATOM   1066 O  O   . PRO A 1 129 ? -43.75300 23.72900 3.95100   1.000 24.42330 ? 128 PRO A O   1 
ATOM   1067 C  CB  . PRO A 1 129 ? -41.76500 22.21700 6.16500   1.000 25.89974 ? 128 PRO A CB  1 
ATOM   1068 C  CG  . PRO A 1 129 ? -41.50800 20.92900 6.94600   1.000 29.47730 ? 128 PRO A CG  1 
ATOM   1069 C  CD  . PRO A 1 129 ? -41.85900 19.87600 5.93300   1.000 25.89328 ? 128 PRO A CD  1 
ATOM   1070 N  N   . PHE A 1 130 ? -42.32300 22.20100 3.07700   1.000 25.59868 ? 129 PHE A N   1 
ATOM   1071 C  CA  . PHE A 1 130 ? -42.36300 22.74800 1.72100   1.000 22.33027 ? 129 PHE A CA  1 
ATOM   1072 C  C   . PHE A 1 130 ? -43.76200 22.62000 1.11900   1.000 25.06305 ? 129 PHE A C   1 
ATOM   1073 O  O   . PHE A 1 130 ? -44.34700 23.61200 0.64900   1.000 24.27364 ? 129 PHE A O   1 
ATOM   1074 C  CB  . PHE A 1 130 ? -41.30300 22.02700 0.87300   1.000 22.51111 ? 129 PHE A CB  1 
ATOM   1075 C  CG  . PHE A 1 130 ? -41.41300 22.24100 -0.62000  1.000 22.30446 ? 129 PHE A CG  1 
ATOM   1076 C  CD1 . PHE A 1 130 ? -41.63400 23.49500 -1.16200  1.000 30.69975 ? 129 PHE A CD1 1 
ATOM   1077 C  CD2 . PHE A 1 130 ? -41.22800 21.17900 -1.48500  1.000 29.50578 ? 129 PHE A CD2 1 
ATOM   1078 C  CE1 . PHE A 1 130 ? -41.71700 23.65800 -2.55500  1.000 27.10510 ? 129 PHE A CE1 1 
ATOM   1079 C  CE2 . PHE A 1 130 ? -41.30100 21.34200 -2.87000  1.000 28.05739 ? 129 PHE A CE2 1 
ATOM   1080 C  CZ  . PHE A 1 130 ? -41.53600 22.58800 -3.40300  1.000 27.88802 ? 129 PHE A CZ  1 
ATOM   1081 N  N   . TYR A 1 131 ? -44.33900 21.41200 1.15600   1.000 21.31445 ? 130 TYR A N   1 
ATOM   1082 C  CA  . TYR A 1 131 ? -45.64700 21.23700 0.54200   1.000 18.88386 ? 130 TYR A CA  1 
ATOM   1083 C  C   . TYR A 1 131 ? -46.71600 22.05400 1.25700   1.000 21.75349 ? 130 TYR A C   1 
ATOM   1084 O  O   . TYR A 1 131 ? -47.68600 22.48600 0.62700   1.000 23.73816 ? 130 TYR A O   1 
ATOM   1085 C  CB  . TYR A 1 131 ? -46.05100 19.74300 0.52800   1.000 21.08565 ? 130 TYR A CB  1 
ATOM   1086 C  CG  . TYR A 1 131 ? -45.10200 18.85800 -0.23900  1.000 20.17385 ? 130 TYR A CG  1 
ATOM   1087 C  CD1 . TYR A 1 131 ? -44.72400 19.14700 -1.54700  1.000 25.22287 ? 130 TYR A CD1 1 
ATOM   1088 C  CD2 . TYR A 1 131 ? -44.58100 17.70800 0.34500   1.000 20.51660 ? 130 TYR A CD2 1 
ATOM   1089 C  CE1 . TYR A 1 131 ? -43.84200 18.29600 -2.25900  1.000 34.17172 ? 130 TYR A CE1 1 
ATOM   1090 C  CE2 . TYR A 1 131 ? -43.70000 16.88600 -0.34600  1.000 20.50554 ? 130 TYR A CE2 1 
ATOM   1091 C  CZ  . TYR A 1 131 ? -43.33700 17.16700 -1.63500  1.000 26.10930 ? 130 TYR A CZ  1 
ATOM   1092 O  OH  . TYR A 1 131 ? -42.45700 16.33500 -2.32100  1.000 26.45655 ? 130 TYR A OH  1 
ATOM   1093 N  N   . ALA A 1 132 ? -46.57900 22.24500 2.57300   1.000 22.60783 ? 131 ALA A N   1 
ATOM   1094 C  CA  . ALA A 1 132 ? -47.57200 23.02800 3.31600   1.000 24.46621 ? 131 ALA A CA  1 
ATOM   1095 C  C   . ALA A 1 132 ? -47.55800 24.47500 2.87100   1.000 26.30053 ? 131 ALA A C   1 
ATOM   1096 O  O   . ALA A 1 132 ? -48.60400 25.12700 2.81600   1.000 29.48761 ? 131 ALA A O   1 
ATOM   1097 C  CB  . ALA A 1 132 ? -47.32100 22.96000 4.82100   1.000 26.84096 ? 131 ALA A CB  1 
ATOM   1098 N  N   . ARG A 1 133 ? -46.37400 25.00900 2.56800   1.000 27.84054 ? 132 ARG A N   1 
ATOM   1099 C  CA  . ARG A 1 133 ? -46.33000 26.39500 2.11200   1.000 25.71145 ? 132 ARG A CA  1 
ATOM   1100 C  C   . ARG A 1 133 ? -47.06600 26.58700 0.79400   1.000 24.92279 ? 132 ARG A C   1 
ATOM   1101 O  O   . ARG A 1 133 ? -47.49900 27.72200 0.49800   1.000 30.17959 ? 132 ARG A O   1 
ATOM   1102 C  CB  . ARG A 1 133 ? -44.88800 26.88500 1.97200   1.000 27.22443 ? 132 ARG A CB  1 
ATOM   1103 C  CG  . ARG A 1 133 ? -44.16300 27.05300 3.29800   1.000 29.50451 ? 132 ARG A CG  1 
ATOM   1104 C  CD  . ARG A 1 133 ? -42.82400 27.76300 3.14900   1.000 29.53501 ? 132 ARG A CD  1 
ATOM   1105 N  NE  . ARG A 1 133 ? -41.85200 27.04300 2.31900   1.000 29.16672 ? 132 ARG A NE  1 
ATOM   1106 C  CZ  . ARG A 1 133 ? -40.96600 26.15800 2.78400   1.000 31.06771 ? 132 ARG A CZ  1 
ATOM   1107 N  NH1 . ARG A 1 133 ? -40.92800 25.84900 4.07300   1.000 32.55304 ? 132 ARG A NH1 1 
ATOM   1108 N  NH2 . ARG A 1 133 ? -40.11300 25.56600 1.94900   1.000 33.91739 ? 132 ARG A NH2 1 
ATOM   1109 N  N   . LEU A 1 134 ? -47.18200 25.52100 -0.00900  1.000 24.52985 ? 133 LEU A N   1 
ATOM   1110 C  CA  . LEU A 1 134 ? -47.89100 25.57300 -1.28100  1.000 26.26094 ? 133 LEU A CA  1 
ATOM   1111 C  C   . LEU A 1 134 ? -49.38700 25.34600 -1.15100  1.000 27.51872 ? 133 LEU A C   1 
ATOM   1112 O  O   . LEU A 1 134 ? -50.10800 25.47800 -2.14700  1.000 29.44479 ? 133 LEU A O   1 
ATOM   1113 C  CB  . LEU A 1 134 ? -47.30900 24.52800 -2.23600  1.000 25.02361 ? 133 LEU A CB  1 
ATOM   1114 C  CG  . LEU A 1 134 ? -45.78900 24.46700 -2.38200  1.000 27.62563 ? 133 LEU A CG  1 
ATOM   1115 C  CD1 . LEU A 1 134 ? -45.45500 23.35000 -3.36900  1.000 28.40837 ? 133 LEU A CD1 1 
ATOM   1116 C  CD2 . LEU A 1 134 ? -45.22900 25.80000 -2.86400  1.000 28.40972 ? 133 LEU A CD2 1 
ATOM   1117 N  N   . GLY A 1 135 ? -49.86700 24.95300 0.03000   1.000 24.70970 ? 134 GLY A N   1 
ATOM   1118 C  CA  . GLY A 1 135 ? -51.27800 24.76500 0.27900   1.000 27.34289 ? 134 GLY A CA  1 
ATOM   1119 C  C   . GLY A 1 135 ? -51.69000 23.34900 0.63500   1.000 28.20867 ? 134 GLY A C   1 
ATOM   1120 O  O   . GLY A 1 135 ? -52.88100 23.12600 0.91500   1.000 33.25639 ? 134 GLY A O   1 
ATOM   1121 N  N   . PHE A 1 136 ? -50.77900 22.37100 0.62500   1.000 24.45211 ? 135 PHE A N   1 
ATOM   1122 C  CA  . PHE A 1 136 ? -51.12300 21.00800 1.04700   1.000 23.57806 ? 135 PHE A CA  1 
ATOM   1123 C  C   . PHE A 1 136 ? -51.36800 21.01500 2.54300   1.000 26.64498 ? 135 PHE A C   1 
ATOM   1124 O  O   . PHE A 1 136 ? -50.66600 21.69900 3.29600   1.000 31.10350 ? 135 PHE A O   1 
ATOM   1125 C  CB  . PHE A 1 136 ? -49.98300 20.04400 0.70900   1.000 23.04923 ? 135 PHE A CB  1 
ATOM   1126 C  CG  . PHE A 1 136 ? -49.93300 19.62800 -0.75100  1.000 25.33585 ? 135 PHE A CG  1 
ATOM   1127 C  CD1 . PHE A 1 136 ? -49.23900 20.41400 -1.70200  1.000 23.15943 ? 135 PHE A CD1 1 
ATOM   1128 C  CD2 . PHE A 1 136 ? -50.56600 18.45000 -1.15900  1.000 27.32875 ? 135 PHE A CD2 1 
ATOM   1129 C  CE1 . PHE A 1 136 ? -49.20600 20.01900 -3.05400  1.000 25.30280 ? 135 PHE A CE1 1 
ATOM   1130 C  CE2 . PHE A 1 136 ? -50.54000 18.05300 -2.49000  1.000 25.33701 ? 135 PHE A CE2 1 
ATOM   1131 C  CZ  . PHE A 1 136 ? -49.86700 18.82000 -3.42900  1.000 23.52700 ? 135 PHE A CZ  1 
ATOM   1132 N  N   A GLN A 1 137 ? -52.37900 20.27500 2.97700   0.300 26.67861 ? 136 GLN A N   1 
ATOM   1133 N  N   B GLN A 1 137 ? -52.38300 20.28100 2.97300   0.700 25.92774 ? 136 GLN A N   1 
ATOM   1134 C  CA  A GLN A 1 137 ? -52.77500 20.22400 4.37600   0.300 29.80666 ? 136 GLN A CA  1 
ATOM   1135 C  CA  B GLN A 1 137 ? -52.78100 20.20900 4.37100   0.700 29.85120 ? 136 GLN A CA  1 
ATOM   1136 C  C   A GLN A 1 137 ? -52.48400 18.83800 4.92800   0.300 29.78381 ? 136 GLN A C   1 
ATOM   1137 C  C   B GLN A 1 137 ? -52.44200 18.83100 4.91000   0.700 30.57077 ? 136 GLN A C   1 
ATOM   1138 O  O   A GLN A 1 137 ? -52.86300 17.83500 4.31800   0.300 28.40663 ? 136 GLN A O   1 
ATOM   1139 O  O   B GLN A 1 137 ? -52.76100 17.82700 4.27400   0.700 28.10566 ? 136 GLN A O   1 
ATOM   1140 C  CB  A GLN A 1 137 ? -54.26200 20.54400 4.53800   0.300 34.52382 ? 136 GLN A CB  1 
ATOM   1141 C  CB  B GLN A 1 137 ? -54.28400 20.45200 4.52900   0.700 33.93820 ? 136 GLN A CB  1 
ATOM   1142 C  CG  A GLN A 1 137 ? -54.66100 20.93600 5.94800   0.300 37.90483 ? 136 GLN A CG  1 
ATOM   1143 C  CG  B GLN A 1 137 ? -54.77000 21.78200 3.99300   0.700 39.98077 ? 136 GLN A CG  1 
ATOM   1144 C  CD  A GLN A 1 137 ? -54.74600 22.44200 6.12400   0.300 49.62938 ? 136 GLN A CD  1 
ATOM   1145 C  CD  B GLN A 1 137 ? -54.52300 22.90500 4.96200   0.700 50.67115 ? 136 GLN A CD  1 
ATOM   1146 O  OE1 A GLN A 1 137 ? -55.46700 23.12900 5.39300   0.300 52.86326 ? 136 GLN A OE1 1 
ATOM   1147 O  OE1 B GLN A 1 137 ? -53.51900 23.61000 4.86200   0.700 54.20704 ? 136 GLN A OE1 1 
ATOM   1148 N  NE2 A GLN A 1 137 ? -54.00500 22.96600 7.09600   0.300 51.49421 ? 136 GLN A NE2 1 
ATOM   1149 N  NE2 B GLN A 1 137 ? -55.45200 23.09800 5.90100   0.700 54.28385 ? 136 GLN A NE2 1 
ATOM   1150 N  N   . ARG A 1 138 ? -51.82300 18.78700 6.07800   1.000 28.56593 ? 137 ARG A N   1 
ATOM   1151 C  CA  . ARG A 1 138 ? -51.59000 17.51000 6.74400   1.000 30.71925 ? 137 ARG A CA  1 
ATOM   1152 C  C   . ARG A 1 138 ? -52.92200 16.91700 7.18200   1.000 28.64965 ? 137 ARG A C   1 
ATOM   1153 O  O   . ARG A 1 138 ? -53.75200 17.61100 7.76800   1.000 34.56573 ? 137 ARG A O   1 
ATOM   1154 C  CB  . ARG A 1 138 ? -50.67500 17.70300 7.94800   1.000 34.60179 ? 137 ARG A CB  1 
ATOM   1155 C  CG  . ARG A 1 138 ? -50.41800 16.41100 8.73300   1.000 44.71818 ? 137 ARG A CG  1 
ATOM   1156 C  CD  . ARG A 1 138 ? -49.35300 16.63300 9.79600   1.000 47.53141 ? 137 ARG A CD  1 
ATOM   1157 N  NE  . ARG A 1 138 ? -49.16800 15.45900 10.64500  1.000 53.75045 ? 137 ARG A NE  1 
ATOM   1158 C  CZ  . ARG A 1 138 ? -48.11600 15.28800 11.43600  1.000 57.85922 ? 137 ARG A CZ  1 
ATOM   1159 N  NH1 . ARG A 1 138 ? -47.16500 16.21200 11.46500  1.000 58.42823 ? 137 ARG A NH1 1 
ATOM   1160 N  NH2 . ARG A 1 138 ? -48.00500 14.19700 12.18300  1.000 55.03648 ? 137 ARG A NH2 1 
ATOM   1161 N  N   . LEU A 1 139 ? -53.12000 15.61900 6.94300   1.000 30.26247 ? 138 LEU A N   1 
ATOM   1162 C  CA  . LEU A 1 139 ? -54.38200 14.95800 7.23800   1.000 29.00519 ? 138 LEU A CA  1 
ATOM   1163 C  C   . LEU A 1 139 ? -54.24300 14.08600 8.47600   1.000 33.58650 ? 138 LEU A C   1 
ATOM   1164 O  O   . LEU A 1 139 ? -53.23400 13.38600 8.63300   1.000 37.23947 ? 138 LEU A O   1 
ATOM   1165 C  CB  . LEU A 1 139 ? -54.82200 14.08300 6.06600   1.000 29.56647 ? 138 LEU A CB  1 
ATOM   1166 C  CG  . LEU A 1 139 ? -54.85400 14.78100 4.72400   1.000 27.33598 ? 138 LEU A CG  1 
ATOM   1167 C  CD1 . LEU A 1 139 ? -55.21900 13.79600 3.62100   1.000 30.60779 ? 138 LEU A CD1 1 
ATOM   1168 C  CD2 . LEU A 1 139 ? -55.86400 15.94800 4.81100   1.000 32.06984 ? 138 LEU A CD2 1 
ATOM   1169 N  N   . THR A 1 140 ? -55.26600 14.08400 9.33300   1.000 36.58303 ? 139 THR A N   1 
ATOM   1170 C  CA  . THR A 1 140 ? -55.32200 13.04200 10.35600  1.000 41.91733 ? 139 THR A CA  1 
ATOM   1171 C  C   . THR A 1 140 ? -55.54300 11.67800 9.70400   1.000 43.68297 ? 139 THR A C   1 
ATOM   1172 O  O   . THR A 1 140 ? -55.90200 11.57600 8.52700   1.000 42.19907 ? 139 THR A O   1 
ATOM   1173 C  CB  . THR A 1 140 ? -56.45000 13.28100 11.36300  1.000 45.52731 ? 139 THR A CB  1 
ATOM   1174 O  OG1 . THR A 1 140 ? -57.71700 13.10100 10.71600  1.000 45.37886 ? 139 THR A OG1 1 
ATOM   1175 C  CG2 . THR A 1 140 ? -56.37200 14.66300 11.95700  1.000 48.35037 ? 139 THR A CG2 1 
ATOM   1176 N  N   . TRP A 1 141 ? -55.33600 10.61500 10.49900  1.000 39.21018 ? 140 TRP A N   1 
ATOM   1177 C  CA  . TRP A 1 141 ? -55.61500 9.25500  10.03700  1.000 43.30829 ? 140 TRP A CA  1 
ATOM   1178 C  C   . TRP A 1 141 ? -57.02100 9.13200  9.45700   1.000 45.91311 ? 140 TRP A C   1 
ATOM   1179 O  O   . TRP A 1 141 ? -57.21300 8.50700  8.40600   1.000 41.46490 ? 140 TRP A O   1 
ATOM   1180 C  CB  . TRP A 1 141 ? -55.42800 8.27200  11.20000  1.000 42.46224 ? 140 TRP A CB  1 
ATOM   1181 C  CG  . TRP A 1 141 ? -55.41200 6.78500  10.84400  1.000 41.84804 ? 140 TRP A CG  1 
ATOM   1182 C  CD1 . TRP A 1 141 ? -56.36100 5.85800  11.16500  1.000 43.80219 ? 140 TRP A CD1 1 
ATOM   1183 C  CD2 . TRP A 1 141 ? -54.38300 6.07200  10.13800  1.000 41.40163 ? 140 TRP A CD2 1 
ATOM   1184 N  NE1 . TRP A 1 141 ? -55.99400 4.61900  10.69600  1.000 46.57957 ? 140 TRP A NE1 1 
ATOM   1185 C  CE2 . TRP A 1 141 ? -54.78500 4.72000  10.06200  1.000 45.24851 ? 140 TRP A CE2 1 
ATOM   1186 C  CE3 . TRP A 1 141 ? -53.16900 6.44600  9.55500   1.000 39.19614 ? 140 TRP A CE3 1 
ATOM   1187 C  CZ2 . TRP A 1 141 ? -54.01100 3.73900  9.41900   1.000 41.35378 ? 140 TRP A CZ2 1 
ATOM   1188 C  CZ3 . TRP A 1 141 ? -52.40300 5.47500  8.92000   1.000 38.84012 ? 140 TRP A CZ3 1 
ATOM   1189 C  CH2 . TRP A 1 141 ? -52.82900 4.13900  8.85500   1.000 42.71939 ? 140 TRP A CH2 1 
ATOM   1190 N  N   . GLN A 1 142 ? -58.01600 9.72300  10.12900  1.000 45.77208 ? 141 GLN A N   1 
ATOM   1191 C  CA  . GLN A 1 142 ? -59.39200 9.63900  9.65100   1.000 47.81347 ? 141 GLN A CA  1 
ATOM   1192 C  C   . GLN A 1 142 ? -59.59200 10.44600 8.37200   1.000 45.68096 ? 141 GLN A C   1 
ATOM   1193 O  O   . GLN A 1 142 ? -60.22600 9.96900  7.42500   1.000 47.73738 ? 141 GLN A O   1 
ATOM   1194 C  CB  . GLN A 1 142 ? -60.35200 10.11200 10.74200  1.000 55.47065 ? 141 GLN A CB  1 
ATOM   1195 C  CG  . GLN A 1 142 ? -61.56500 9.22600  10.93200  1.000 65.86269 ? 141 GLN A CG  1 
ATOM   1196 C  CD  . GLN A 1 142 ? -62.66200 9.51100  9.92600   1.000 71.47888 ? 141 GLN A CD  1 
ATOM   1197 O  OE1 . GLN A 1 142 ? -63.05600 10.66300 9.72700   1.000 71.80056 ? 141 GLN A OE1 1 
ATOM   1198 N  NE2 . GLN A 1 142 ? -63.16600 8.45800  9.28600   1.000 73.26708 ? 141 GLN A NE2 1 
ATOM   1199 N  N   . GLU A 1 143 ? -59.05500 11.67000 8.32200   1.000 44.48609 ? 142 GLU A N   1 
ATOM   1200 C  CA  . GLU A 1 143 ? -59.16000 12.50800 7.13200   1.000 41.63113 ? 142 GLU A CA  1 
ATOM   1201 C  C   . GLU A 1 143 ? -58.45800 11.90600 5.91900   1.000 38.78268 ? 142 GLU A C   1 
ATOM   1202 O  O   . GLU A 1 143 ? -58.76900 12.27900 4.77800   1.000 36.44755 ? 142 GLU A O   1 
ATOM   1203 C  CB  . GLU A 1 143 ? -58.56900 13.89300 7.42800   1.000 42.66555 ? 142 GLU A CB  1 
ATOM   1204 C  CG  . GLU A 1 143 ? -59.35700 14.71100 8.44600   1.000 43.45781 ? 142 GLU A CG  1 
ATOM   1205 C  CD  . GLU A 1 143 ? -58.59800 15.93200 8.93900   1.000 46.90468 ? 142 GLU A CD  1 
ATOM   1206 O  OE1 . GLU A 1 143 ? -57.35700 15.94000 8.84600   1.000 43.38626 ? 142 GLU A OE1 1 
ATOM   1207 O  OE2 . GLU A 1 143 ? -59.25000 16.89700 9.41300   1.000 52.42486 ? 142 GLU A OE2 1 
ATOM   1208 N  N   . ALA A 1 144 ? -57.50900 10.99900 6.13800   1.000 33.52887 ? 143 ALA A N   1 
ATOM   1209 C  CA  . ALA A 1 144 ? -56.73400 10.44900 5.02900   1.000 30.14946 ? 143 ALA A CA  1 
ATOM   1210 C  C   . ALA A 1 144 ? -57.59900 9.63200  4.06900   1.000 32.27795 ? 143 ALA A C   1 
ATOM   1211 O  O   . ALA A 1 144 ? -57.34600 9.64100  2.85400   1.000 31.92766 ? 143 ALA A O   1 
ATOM   1212 C  CB  . ALA A 1 144 ? -55.58800 9.58900  5.57200   1.000 35.04289 ? 143 ALA A CB  1 
ATOM   1213 N  N   . GLY A 1 145 ? -58.60200 8.92000  4.58200   1.000 32.18467 ? 144 GLY A N   1 
ATOM   1214 C  CA  . GLY A 1 145 ? -59.42700 8.05300  3.76200   1.000 35.04736 ? 144 GLY A CA  1 
ATOM   1215 C  C   . GLY A 1 145 ? -58.71600 6.74900  3.43100   1.000 33.35022 ? 144 GLY A C   1 
ATOM   1216 O  O   . GLY A 1 145 ? -57.52500 6.57900  3.67100   1.000 34.39447 ? 144 GLY A O   1 
ATOM   1217 N  N   . GLU A 1 146 ? -59.48100 5.81200  2.84800   1.000 37.37725 ? 145 GLU A N   1 
ATOM   1218 C  CA  . GLU A 1 146 ? -59.02300 4.42500  2.73500   1.000 38.82122 ? 145 GLU A CA  1 
ATOM   1219 C  C   . GLU A 1 146 ? -57.76600 4.29900  1.87400   1.000 35.11607 ? 145 GLU A C   1 
ATOM   1220 O  O   . GLU A 1 146 ? -56.81100 3.61100  2.25700   1.000 32.19223 ? 145 GLU A O   1 
ATOM   1221 C  CB  . GLU A 1 146 ? -60.14300 3.54800  2.17400   1.000 40.99231 ? 145 GLU A CB  1 
ATOM   1222 C  CG  . GLU A 1 146 ? -60.49200 2.35800  3.07300   1.000 54.54810 ? 145 GLU A CG  1 
ATOM   1223 C  CD  . GLU A 1 146 ? -61.25800 1.26800  2.35100   1.000 65.92652 ? 145 GLU A CD  1 
ATOM   1224 O  OE1 . GLU A 1 146 ? -60.63600 0.25300  1.96100   1.000 68.98874 ? 145 GLU A OE1 1 
ATOM   1225 O  OE2 . GLU A 1 146 ? -62.48500 1.42100  2.18100   1.000 73.86726 ? 145 GLU A OE2 1 
ATOM   1226 N  N   . ARG A 1 147 ? -57.73200 4.96300  0.71000   1.000 34.31958 ? 146 ARG A N   1 
ATOM   1227 C  CA  . ARG A 1 147 ? -56.59000 4.78900  -0.19500  1.000 30.80940 ? 146 ARG A CA  1 
ATOM   1228 C  C   . ARG A 1 147 ? -55.28800 5.24800  0.45500   1.000 26.75064 ? 146 ARG A C   1 
ATOM   1229 O  O   . ARG A 1 147 ? -54.27400 4.54100  0.42900   1.000 27.01904 ? 146 ARG A O   1 
ATOM   1230 C  CB  . ARG A 1 147 ? -56.82200 5.54500  -1.51400  1.000 30.50781 ? 146 ARG A CB  1 
ATOM   1231 C  CG  . ARG A 1 147 ? -55.72500 5.33600  -2.56700  1.000 27.20137 ? 146 ARG A CG  1 
ATOM   1232 C  CD  . ARG A 1 147 ? -56.07300 6.06400  -3.88900  1.000 27.74102 ? 146 ARG A CD  1 
ATOM   1233 N  NE  . ARG A 1 147 ? -56.19000 7.52900  -3.71900  1.000 27.68830 ? 146 ARG A NE  1 
ATOM   1234 C  CZ  . ARG A 1 147 ? -55.16700 8.38000  -3.65300  1.000 24.72795 ? 146 ARG A CZ  1 
ATOM   1235 N  NH1 . ARG A 1 147 ? -53.90600 7.98600  -3.71900  1.000 25.37090 ? 146 ARG A NH1 1 
ATOM   1236 N  NH2 . ARG A 1 147 ? -55.40900 9.68300  -3.50100  1.000 27.22412 ? 146 ARG A NH2 1 
ATOM   1237 N  N   . LEU A 1 148 ? -55.28900 6.44800  1.03000   1.000 24.32615 ? 147 LEU A N   1 
ATOM   1238 C  CA  . LEU A 1 148 ? -54.06500 6.95400  1.62600   1.000 23.15682 ? 147 LEU A CA  1 
ATOM   1239 C  C   . LEU A 1 148 ? -53.70300 6.20200  2.90100   1.000 26.91112 ? 147 LEU A C   1 
ATOM   1240 O  O   . LEU A 1 148 ? -52.51100 6.04200  3.19300   1.000 24.59883 ? 147 LEU A O   1 
ATOM   1241 C  CB  . LEU A 1 148 ? -54.19700 8.46300  1.90500   1.000 24.82954 ? 147 LEU A CB  1 
ATOM   1242 C  CG  . LEU A 1 148 ? -54.24500 9.32400  0.63800   1.000 25.69024 ? 147 LEU A CG  1 
ATOM   1243 C  CD1 . LEU A 1 148 ? -54.67400 10.78300 0.97500   1.000 26.65196 ? 147 LEU A CD1 1 
ATOM   1244 C  CD2 . LEU A 1 148 ? -52.93900 9.32400  -0.14900  1.000 24.37598 ? 147 LEU A CD2 1 
ATOM   1245 N  N   . ARG A 1 149 ? -54.70000 5.76300  3.67400   1.000 26.62312 ? 148 ARG A N   1 
ATOM   1246 C  CA  . ARG A 1 149 ? -54.41500 4.94600  4.85400   1.000 29.56699 ? 148 ARG A CA  1 
ATOM   1247 C  C   . ARG A 1 149 ? -53.69100 3.66400  4.46000   1.000 30.41293 ? 148 ARG A C   1 
ATOM   1248 O  O   . ARG A 1 149 ? -52.76900 3.22600  5.15400   1.000 30.14802 ? 148 ARG A O   1 
ATOM   1249 C  CB  . ARG A 1 149 ? -55.70100 4.62700  5.62800   1.000 31.32403 ? 148 ARG A CB  1 
ATOM   1250 C  CG  . ARG A 1 149 ? -56.13200 5.75500  6.56900   1.000 35.52984 ? 148 ARG A CG  1 
ATOM   1251 C  CD  . ARG A 1 149 ? -57.22400 5.32600  7.54200   1.000 43.47039 ? 148 ARG A CD  1 
ATOM   1252 N  NE  . ARG A 1 149 ? -58.46600 4.97800  6.86400   1.000 44.28633 ? 148 ARG A NE  1 
ATOM   1253 C  CZ  . ARG A 1 149 ? -59.50200 5.80300  6.72400   1.000 47.70612 ? 148 ARG A CZ  1 
ATOM   1254 N  NH1 . ARG A 1 149 ? -60.59800 5.39500  6.10200   1.000 44.11060 ? 148 ARG A NH1 1 
ATOM   1255 N  NH2 . ARG A 1 149 ? -59.44200 7.03100  7.21000   1.000 47.35558 ? 148 ARG A NH2 1 
ATOM   1256 N  N   . ALA A 1 150 ? -54.10100 3.04800  3.35500   1.000 32.59202 ? 149 ALA A N   1 
ATOM   1257 C  CA  . ALA A 1 150 ? -53.43300 1.83000  2.90900   1.000 28.48582 ? 149 ALA A CA  1 
ATOM   1258 C  C   . ALA A 1 150 ? -51.96300 2.08200  2.57300   1.000 27.57072 ? 149 ALA A C   1 
ATOM   1259 O  O   . ALA A 1 150 ? -51.09700 1.25000  2.86800   1.000 27.23252 ? 149 ALA A O   1 
ATOM   1260 C  CB  . ALA A 1 150 ? -54.18000 1.25100  1.71200   1.000 27.78340 ? 149 ALA A CB  1 
ATOM   1261 N  N   . ILE A 1 151 ? -51.66200 3.19900  1.91200   1.000 24.35900 ? 150 ILE A N   1 
ATOM   1262 C  CA  . ILE A 1 151 ? -50.27400 3.52000  1.60400   1.000 21.29137 ? 150 ILE A CA  1 
ATOM   1263 C  C   . ILE A 1 151 ? -49.48000 3.71400  2.88700   1.000 23.05705 ? 150 ILE A C   1 
ATOM   1264 O  O   . ILE A 1 151 ? -48.36100 3.20600  3.03600   1.000 23.80526 ? 150 ILE A O   1 
ATOM   1265 C  CB  . ILE A 1 151 ? -50.22900 4.78400  0.72300   1.000 22.64202 ? 150 ILE A CB  1 
ATOM   1266 C  CG1 . ILE A 1 151 ? -50.91700 4.49800  -0.60200  1.000 23.73533 ? 150 ILE A CG1 1 
ATOM   1267 C  CG2 . ILE A 1 151 ? -48.79500 5.31100  0.53200   1.000 20.94586 ? 150 ILE A CG2 1 
ATOM   1268 C  CD1 . ILE A 1 151 ? -51.24400 5.81500  -1.35400  1.000 24.92327 ? 150 ILE A CD1 1 
ATOM   1269 N  N   . LEU A 1 152 ? -50.01400 4.51500  3.81500   1.000 22.78308 ? 151 LEU A N   1 
ATOM   1270 C  CA  . LEU A 1 152 ? -49.28700 4.76200  5.05600   1.000 22.07777 ? 151 LEU A CA  1 
ATOM   1271 C  C   . LEU A 1 152 ? -49.02900 3.45200  5.80800   1.000 25.41359 ? 151 LEU A C   1 
ATOM   1272 O  O   . LEU A 1 152 ? -47.93700 3.25600  6.35900   1.000 25.23711 ? 151 LEU A O   1 
ATOM   1273 C  CB  . LEU A 1 152 ? -50.07000 5.73500  5.93200   1.000 23.85061 ? 151 LEU A CB  1 
ATOM   1274 C  CG  . LEU A 1 152 ? -50.20300 7.19000  5.43700   1.000 23.26113 ? 151 LEU A CG  1 
ATOM   1275 C  CD1 . LEU A 1 152 ? -51.14700 7.95700  6.38100   1.000 25.38840 ? 151 LEU A CD1 1 
ATOM   1276 C  CD2 . LEU A 1 152 ? -48.84700 7.86500  5.34800   1.000 25.90225 ? 151 LEU A CD2 1 
ATOM   1277 N  N   . GLY A 1 153 ? -50.02500 2.56400  5.84100   1.000 25.91021 ? 152 GLY A N   1 
ATOM   1278 C  CA  . GLY A 1 153 ? -49.84800 1.25800  6.47400   1.000 25.44314 ? 152 GLY A CA  1 
ATOM   1279 C  C   . GLY A 1 153 ? -48.73700 0.44300  5.83800   1.000 28.05047 ? 152 GLY A C   1 
ATOM   1280 O  O   . GLY A 1 153 ? -47.90800 -0.14900 6.53500   1.000 28.71478 ? 152 GLY A O   1 
ATOM   1281 N  N   . HIS A 1 154 ? -48.66500 0.43800  4.50900   1.000 24.29571 ? 153 HIS A N   1 
ATOM   1282 C  CA  . HIS A 1 154 ? -47.62800 -0.36500 3.87700   1.000 25.11977 ? 153 HIS A CA  1 
ATOM   1283 C  C   . HIS A 1 154 ? -46.24700 0.25700  4.05400   1.000 24.66389 ? 153 HIS A C   1 
ATOM   1284 O  O   . HIS A 1 154 ? -45.25200 -0.46400 4.20300   1.000 25.23251 ? 153 HIS A O   1 
ATOM   1285 C  CB  . HIS A 1 154 ? -47.95300 -0.57500 2.40300   1.000 27.33356 ? 153 HIS A CB  1 
ATOM   1286 C  CG  . HIS A 1 154 ? -47.04600 -1.55600 1.72700   1.000 24.08565 ? 153 HIS A CG  1 
ATOM   1287 N  ND1 . HIS A 1 154 ? -46.20600 -1.18700 0.69800   1.000 28.58940 ? 153 HIS A ND1 1 
ATOM   1288 C  CD2 . HIS A 1 154 ? -46.79300 -2.86300 1.97100   1.000 29.89024 ? 153 HIS A CD2 1 
ATOM   1289 C  CE1 . HIS A 1 154 ? -45.51200 -2.24200 0.30200   1.000 31.16395 ? 153 HIS A CE1 1 
ATOM   1290 N  NE2 . HIS A 1 154 ? -45.84500 -3.27000 1.06200   1.000 29.72766 ? 153 HIS A NE2 1 
ATOM   1291 N  N   . GLU A 1 155 ? -46.16200 1.59400  4.01000   1.000 22.33079 ? 154 GLU A N   1 
ATOM   1292 C  CA  . GLU A 1 155 ? -44.92900 2.29800  4.35400   1.000 22.82998 ? 154 GLU A CA  1 
ATOM   1293 C  C   . GLU A 1 155 ? -44.37000 1.83100  5.69300   1.000 24.64607 ? 154 GLU A C   1 
ATOM   1294 O  O   . GLU A 1 155 ? -43.15700 1.60500  5.81800   1.000 24.05811 ? 154 GLU A O   1 
ATOM   1295 C  CB  . GLU A 1 155 ? -45.19000 3.80400  4.39800   1.000 24.12947 ? 154 GLU A CB  1 
ATOM   1296 C  CG  . GLU A 1 155 ? -45.22500 4.45200  3.05100   1.000 21.43309 ? 154 GLU A CG  1 
ATOM   1297 C  CD  . GLU A 1 155 ? -45.54600 5.94300  3.14200   1.000 24.75351 ? 154 GLU A CD  1 
ATOM   1298 O  OE1 . GLU A 1 155 ? -45.68500 6.50300  4.26200   1.000 27.12927 ? 154 GLU A OE1 1 
ATOM   1299 O  OE2 . GLU A 1 155 ? -45.65300 6.51400  2.06400   1.000 24.57695 ? 154 GLU A OE2 1 
ATOM   1300 N  N   . GLN A 1 156 ? -45.24100 1.62300  6.69500   1.000 24.29791 ? 155 GLN A N   1 
ATOM   1301 C  CA  . GLN A 1 156 ? -44.74300 1.21100  7.99900   1.000 26.41957 ? 155 GLN A CA  1 
ATOM   1302 C  C   . GLN A 1 156 ? -44.16700 -0.20500 7.98300   1.000 29.58173 ? 155 GLN A C   1 
ATOM   1303 O  O   . GLN A 1 156 ? -43.38300 -0.55300 8.87300   1.000 39.58402 ? 155 GLN A O   1 
ATOM   1304 C  CB  . GLN A 1 156 ? -45.84800 1.29800  9.04500   1.000 35.79811 ? 155 GLN A CB  1 
ATOM   1305 C  CG  . GLN A 1 156 ? -45.31500 1.37200  10.46300  1.000 48.13232 ? 155 GLN A CG  1 
ATOM   1306 C  CD  . GLN A 1 156 ? -46.32500 0.91400  11.48600  1.000 51.95905 ? 155 GLN A CD  1 
ATOM   1307 O  OE1 . GLN A 1 156 ? -47.32600 0.28700  11.14500  1.000 53.56788 ? 155 GLN A OE1 1 
ATOM   1308 N  NE2 . GLN A 1 156 ? -46.06200 1.21400  12.75100  1.000 47.34422 ? 155 GLN A NE2 1 
ATOM   1309 N  N   . GLU A 1 157 ? -44.51100 -1.01300 6.99000   1.000 23.73631 ? 156 GLU A N   1 
ATOM   1310 C  CA  . GLU A 1 157 ? -43.94600 -2.35800 6.89300   1.000 27.43886 ? 156 GLU A CA  1 
ATOM   1311 C  C   . GLU A 1 157 ? -42.56000 -2.39300 6.25000   1.000 26.95477 ? 156 GLU A C   1 
ATOM   1312 O  O   . GLU A 1 157 ? -41.82600 -3.38900 6.44300   1.000 31.12787 ? 156 GLU A O   1 
ATOM   1313 C  CB  . GLU A 1 157 ? -44.89100 -3.26800 6.10400   1.000 30.02598 ? 156 GLU A CB  1 
ATOM   1314 C  CG  . GLU A 1 157 ? -46.28300 -3.32600 6.71300   1.000 36.35770 ? 156 GLU A CG  1 
ATOM   1315 C  CD  . GLU A 1 157 ? -47.19100 -4.35200 6.07900   1.000 41.75541 ? 156 GLU A CD  1 
ATOM   1316 O  OE1 . GLU A 1 157 ? -46.70800 -5.19800 5.28400   1.000 33.60710 ? 156 GLU A OE1 1 
ATOM   1317 O  OE2 . GLU A 1 157 ? -48.40400 -4.30000 6.39100   1.000 42.19743 ? 156 GLU A OE2 1 
ATOM   1318 N  N   . ILE A 1 158 ? -42.19600 -1.35600 5.49500   1.000 27.34289 ? 157 ILE A N   1 
ATOM   1319 C  CA  . ILE A 1 158 ? -40.98300 -1.36400 4.69400   1.000 25.18419 ? 157 ILE A CA  1 
ATOM   1320 C  C   . ILE A 1 158 ? -39.93300 -0.41700 5.23300   1.000 27.07515 ? 157 ILE A C   1 
ATOM   1321 O  O   . ILE A 1 158 ? -38.94500 -0.14200 4.54400   1.000 28.57800 ? 157 ILE A O   1 
ATOM   1322 C  CB  . ILE A 1 158 ? -41.27300 -1.07600 3.21700   1.000 24.22435 ? 157 ILE A CB  1 
ATOM   1323 C  CG1 . ILE A 1 158 ? -41.87300 0.32700  3.04500   1.000 25.04396 ? 157 ILE A CG1 1 
ATOM   1324 C  CG2 . ILE A 1 158 ? -42.18300 -2.18200 2.63100   1.000 28.83251 ? 157 ILE A CG2 1 
ATOM   1325 C  CD1 . ILE A 1 158 ? -42.20300 0.65100  1.61300   1.000 28.19942 ? 157 ILE A CD1 1 
ATOM   1326 N  N   . GLY A 1 159 ? -40.08900 0.07000  6.46100   1.000 26.06393 ? 158 GLY A N   1 
ATOM   1327 C  CA  . GLY A 1 159 ? -39.02700 0.89600  6.99800   1.000 26.54829 ? 158 GLY A CA  1 
ATOM   1328 C  C   . GLY A 1 159 ? -39.38100 2.24900  7.53600   1.000 28.15657 ? 158 GLY A C   1 
ATOM   1329 O  O   . GLY A 1 159 ? -38.61700 2.80900  8.33700   1.000 30.71856 ? 158 GLY A O   1 
ATOM   1330 N  N   . PHE A 1 160 ? -40.47800 2.82800  7.06100   1.000 22.87974 ? 159 PHE A N   1 
ATOM   1331 C  CA  . PHE A 1 160 ? -40.88400 4.11400  7.58100   1.000 26.84617 ? 159 PHE A CA  1 
ATOM   1332 C  C   . PHE A 1 160 ? -41.44900 3.90900  8.97900   1.000 31.85496 ? 159 PHE A C   1 
ATOM   1333 O  O   . PHE A 1 160 ? -41.93200 2.81900  9.33100   1.000 34.19279 ? 159 PHE A O   1 
ATOM   1334 C  CB  . PHE A 1 160 ? -41.88600 4.78100  6.63500   1.000 24.75325 ? 159 PHE A CB  1 
ATOM   1335 C  CG  . PHE A 1 160 ? -41.36600 4.97400  5.22800   1.000 24.66396 ? 159 PHE A CG  1 
ATOM   1336 C  CD1 . PHE A 1 160 ? -41.52000 3.99400  4.26600   1.000 24.86810 ? 159 PHE A CD1 1 
ATOM   1337 C  CD2 . PHE A 1 160 ? -40.71200 6.13600  4.87400   1.000 27.19249 ? 159 PHE A CD2 1 
ATOM   1338 C  CE1 . PHE A 1 160 ? -41.02400 4.17400  2.97000   1.000 28.07534 ? 159 PHE A CE1 1 
ATOM   1339 C  CE2 . PHE A 1 160 ? -40.25100 6.34100  3.59000   1.000 29.53368 ? 159 PHE A CE2 1 
ATOM   1340 C  CZ  . PHE A 1 160 ? -40.39600 5.36400  2.62900   1.000 28.24239 ? 159 PHE A CZ  1 
ATOM   1341 N  N   . ALA A 1 161 ? -41.26200 4.90800  9.81300   1.000 27.20040 ? 160 ALA A N   1 
ATOM   1342 C  CA  . ALA A 1 161 ? -41.87600 4.92700  11.12500  1.000 28.99067 ? 160 ALA A CA  1 
ATOM   1343 C  C   . ALA A 1 161 ? -43.16700 5.71800  10.99800  1.000 30.24421 ? 160 ALA A C   1 
ATOM   1344 O  O   . ALA A 1 161 ? -43.15900 6.82400  10.45800  1.000 29.82834 ? 160 ALA A O   1 
ATOM   1345 C  CB  . ALA A 1 161 ? -40.93500 5.56300  12.14800  1.000 29.88732 ? 160 ALA A CB  1 
ATOM   1346 N  N   . ALA A 1 162 ? -44.27600 5.12400  11.44300  1.000 35.73186 ? 161 ALA A N   1 
ATOM   1347 C  CA  . ALA A 1 162 ? -45.57300 5.78900  11.36400  1.000 31.89500 ? 161 ALA A CA  1 
ATOM   1348 C  C   . ALA A 1 162 ? -45.50100 7.21900  11.87700  1.000 31.67140 ? 161 ALA A C   1 
ATOM   1349 O  O   . ALA A 1 162 ? -46.02100 8.13300  11.22500  1.000 34.04924 ? 161 ALA A O   1 
ATOM   1350 C  CB  . ALA A 1 162 ? -46.61500 5.00900  12.17100  1.000 35.13094 ? 161 ALA A CB  1 
ATOM   1351 N  N   . ASP A 1 163 ? -44.84200 7.42900  13.02900  1.000 32.98688 ? 162 ASP A N   1 
ATOM   1352 C  CA  . ASP A 1 163 ? -44.73800 8.74300  13.66800  1.000 32.72451 ? 162 ASP A CA  1 
ATOM   1353 C  C   . ASP A 1 163 ? -43.95600 9.76800  12.85100  1.000 33.40348 ? 162 ASP A C   1 
ATOM   1354 O  O   . ASP A 1 163 ? -43.89600 10.93800 13.25000  1.000 38.95130 ? 162 ASP A O   1 
ATOM   1355 C  CB  . ASP A 1 163 ? -44.08200 8.60700  15.04200  1.000 44.02064 ? 162 ASP A CB  1 
ATOM   1356 C  CG  . ASP A 1 163 ? -45.04100 8.08700  16.09300  1.000 61.98446 ? 162 ASP A CG  1 
ATOM   1357 O  OD1 . ASP A 1 163 ? -46.25200 8.01000  15.78800  1.000 65.95325 ? 162 ASP A OD1 1 
ATOM   1358 O  OD2 . ASP A 1 163 ? -44.58900 7.74800  17.21600  1.000 66.58604 ? 162 ASP A OD2 1 
ATOM   1359 N  N   . SER A 1 164 ? -43.35800 9.37700  11.73300  1.000 33.39497 ? 163 SER A N   1 
ATOM   1360 C  CA  . SER A 1 164 ? -42.57500 10.29400 10.90800  1.000 28.81340 ? 163 SER A CA  1 
ATOM   1361 C  C   . SER A 1 164 ? -43.22100 10.60200 9.57000   1.000 25.79741 ? 163 SER A C   1 
ATOM   1362 O  O   . SER A 1 164 ? -42.67900 11.41800 8.82300   1.000 25.31558 ? 163 SER A O   1 
ATOM   1363 C  CB  . SER A 1 164 ? -41.17600 9.73200  10.63900  1.000 30.47235 ? 163 SER A CB  1 
ATOM   1364 O  OG  . SER A 1 164 ? -41.24600 8.63300  9.73200   1.000 41.83506 ? 163 SER A OG  1 
ATOM   1365 N  N   . ARG A 1 165 ? -44.36500 10.00400 9.25400   1.000 22.64855 ? 164 ARG A N   1 
ATOM   1366 C  CA  . ARG A 1 165 ? -44.99900 10.12800 7.94800   1.000 22.13708 ? 164 ARG A CA  1 
ATOM   1367 C  C   . ARG A 1 165 ? -46.39300 10.73600 8.07500   1.000 25.96343 ? 164 ARG A C   1 
ATOM   1368 O  O   . ARG A 1 165 ? -47.06100 10.58700 9.10900   1.000 29.63149 ? 164 ARG A O   1 
ATOM   1369 C  CB  . ARG A 1 165 ? -45.15300 8.74800  7.28000   1.000 23.02833 ? 164 ARG A CB  1 
ATOM   1370 C  CG  . ARG A 1 165 ? -43.85700 7.98900  7.01100   1.000 26.38596 ? 164 ARG A CG  1 
ATOM   1371 C  CD  . ARG A 1 165 ? -43.06400 8.65200  5.90000   1.000 23.52702 ? 164 ARG A CD  1 
ATOM   1372 N  NE  . ARG A 1 165 ? -43.61500 8.43500  4.56000   1.000 21.73072 ? 164 ARG A NE  1 
ATOM   1373 C  CZ  . ARG A 1 165 ? -43.02300 8.84700  3.43200   1.000 20.56667 ? 164 ARG A CZ  1 
ATOM   1374 N  NH1 . ARG A 1 165 ? -41.86000 9.51000  3.48600   1.000 21.49225 ? 164 ARG A NH1 1 
ATOM   1375 N  NH2 . ARG A 1 165 ? -43.57400 8.60600  2.24500   1.000 24.41671 ? 164 ARG A NH2 1 
ATOM   1376 N  N   . CYS A 1 166 ? -46.86000 11.35400 6.98400   1.000 23.50090 ? 165 CYS A N   1 
ATOM   1377 C  CA  . CYS A 1 166 ? -48.23400 11.84200 6.93100   1.000 26.52343 ? 165 CYS A CA  1 
ATOM   1378 C  C   . CYS A 1 166 ? -48.74400 11.83000 5.49000   1.000 27.28060 ? 165 CYS A C   1 
ATOM   1379 O  O   . CYS A 1 166 ? -47.97000 11.90300 4.53300   1.000 23.82081 ? 165 CYS A O   1 
ATOM   1380 C  CB  . CYS A 1 166 ? -48.35800 13.24900 7.53900   1.000 30.42610 ? 165 CYS A CB  1 
ATOM   1381 S  SG  . CYS A 1 166 ? -47.44700 14.55400 6.63200   1.000 31.91872 ? 165 CYS A SG  1 
ATOM   1382 N  N   . ALA A 1 167 ? -50.06000 11.73800 5.35100   1.000 25.28325 ? 166 ALA A N   1 
ATOM   1383 C  CA  . ALA A 1 167 ? -50.73200 12.00900 4.09100   1.000 24.28397 ? 166 ALA A CA  1 
ATOM   1384 C  C   . ALA A 1 167 ? -51.12500 13.47700 4.04600   1.000 20.45856 ? 166 ALA A C   1 
ATOM   1385 O  O   . ALA A 1 167 ? -51.37100 14.11200 5.08400   1.000 24.26753 ? 166 ALA A O   1 
ATOM   1386 C  CB  . ALA A 1 167 ? -52.00300 11.16600 3.93100   1.000 25.45627 ? 166 ALA A CB  1 
HETATM 1387 N  N   . MSE A 1 168 ? -51.12800 14.03500 2.83600   1.000 21.81724 ? 167 MSE A N   1 
HETATM 1388 C  CA  . MSE A 1 168 ? -51.54400 15.43400 2.65300   1.000 21.69527 ? 167 MSE A CA  1 
HETATM 1389 C  C   . MSE A 1 168 ? -52.47300 15.59500 1.45900   1.000 24.08950 ? 167 MSE A C   1 
HETATM 1390 O  O   . MSE A 1 168 ? -52.38700 14.84600 0.49100   1.000 24.26040 ? 167 MSE A O   1 
HETATM 1391 C  CB  . MSE A 1 168 ? -50.31500 16.38900 2.47500   1.000 24.19547 ? 167 MSE A CB  1 
HETATM 1392 C  CG  . MSE A 1 168 ? -49.22500 16.22300 3.52700   1.000 22.54348 ? 167 MSE A CG  1 
HETATM 1393 SE SE  . MSE A 1 168 ? -47.70000 17.41200 3.28400   1.000 28.62761 ? 167 MSE A SE  1 
HETATM 1394 C  CE  . MSE A 1 168 ? -48.45900 18.99400 4.15800   1.000 25.59096 ? 167 MSE A CE  1 
ATOM   1395 N  N   . ARG A 1 169 ? -53.32700 16.63100 1.49800   1.000 23.69443 ? 168 ARG A N   1 
ATOM   1396 C  CA  . ARG A 1 169 ? -54.23400 16.90000 0.39400   1.000 25.65282 ? 168 ARG A CA  1 
ATOM   1397 C  C   . ARG A 1 169 ? -54.28100 18.39700 0.11100   1.000 27.60867 ? 168 ARG A C   1 
ATOM   1398 O  O   . ARG A 1 169 ? -54.34400 19.20800 1.03500   1.000 26.04167 ? 168 ARG A O   1 
ATOM   1399 C  CB  . ARG A 1 169 ? -55.65700 16.36300 0.69000   1.000 24.47766 ? 168 ARG A CB  1 
ATOM   1400 C  CG  . ARG A 1 169 ? -56.66500 16.49300 -0.45000  1.000 26.17280 ? 168 ARG A CG  1 
ATOM   1401 C  CD  . ARG A 1 169 ? -58.05800 15.90400 -0.10400  1.000 28.23321 ? 168 ARG A CD  1 
ATOM   1402 N  NE  . ARG A 1 169 ? -58.00600 14.46200 0.17900   1.000 31.35509 ? 168 ARG A NE  1 
ATOM   1403 C  CZ  . ARG A 1 169 ? -58.24400 13.92200 1.37200   1.000 34.92064 ? 168 ARG A CZ  1 
ATOM   1404 N  NH1 . ARG A 1 169 ? -58.56400 14.68500 2.41300   1.000 37.45427 ? 168 ARG A NH1 1 
ATOM   1405 N  NH2 . ARG A 1 169 ? -58.19300 12.60000 1.51900   1.000 34.49786 ? 168 ARG A NH2 1 
ATOM   1406 N  N   A LEU A 1 170 ? -54.23400 18.74800 -1.17100  0.600 25.84879 ? 169 LEU A N   1 
ATOM   1407 N  N   B LEU A 1 170 ? -54.26100 18.73800 -1.17200  0.400 25.77252 ? 169 LEU A N   1 
ATOM   1408 C  CA  A LEU A 1 170 ? -54.48900 20.10400 -1.65800  0.600 25.06457 ? 169 LEU A CA  1 
ATOM   1409 C  CA  B LEU A 1 170 ? -54.49400 20.09200 -1.66300  0.400 25.17486 ? 169 LEU A CA  1 
ATOM   1410 C  C   A LEU A 1 170 ? -55.81500 20.07600 -2.39800  0.600 27.27227 ? 169 LEU A C   1 
ATOM   1411 C  C   B LEU A 1 170 ? -55.82500 20.06800 -2.39700  0.400 27.35017 ? 169 LEU A C   1 
ATOM   1412 O  O   A LEU A 1 170 ? -55.90500 19.48100 -3.47500  0.600 27.90371 ? 169 LEU A O   1 
ATOM   1413 O  O   B LEU A 1 170 ? -55.92600 19.46800 -3.47000  0.400 28.13610 ? 169 LEU A O   1 
ATOM   1414 C  CB  A LEU A 1 170 ? -53.36800 20.57800 -2.58800  0.600 24.55312 ? 169 LEU A CB  1 
ATOM   1415 C  CB  B LEU A 1 170 ? -53.36100 20.53100 -2.59300  0.400 24.51140 ? 169 LEU A CB  1 
ATOM   1416 C  CG  A LEU A 1 170 ? -53.61900 21.93600 -3.27700  0.600 26.09085 ? 169 LEU A CG  1 
ATOM   1417 C  CG  B LEU A 1 170 ? -53.12600 22.02400 -2.87200  0.400 30.83896 ? 169 LEU A CG  1 
ATOM   1418 C  CD1 A LEU A 1 170 ? -53.54500 23.05000 -2.27500  0.600 26.86931 ? 169 LEU A CD1 1 
ATOM   1419 C  CD1 B LEU A 1 170 ? -52.04100 22.20100 -3.94700  0.400 26.02104 ? 169 LEU A CD1 1 
ATOM   1420 C  CD2 A LEU A 1 170 ? -52.61300 22.17000 -4.40000  0.600 27.77552 ? 169 LEU A CD2 1 
ATOM   1421 C  CD2 B LEU A 1 170 ? -54.37300 22.77500 -3.24600  0.400 33.13389 ? 169 LEU A CD2 1 
ATOM   1422 N  N   . VAL A 1 171 ? -56.83300 20.74700 -1.84200  1.000 28.24618 ? 170 VAL A N   1 
ATOM   1423 C  CA  . VAL A 1 171 ? -58.16200 20.79700 -2.44100  1.000 30.20214 ? 170 VAL A CA  1 
ATOM   1424 C  C   . VAL A 1 171 ? -58.21000 21.96300 -3.41000  1.000 31.34119 ? 170 VAL A C   1 
ATOM   1425 O  O   . VAL A 1 171 ? -57.83400 23.09500 -3.06000  1.000 31.88122 ? 170 VAL A O   1 
ATOM   1426 C  CB  . VAL A 1 171 ? -59.24700 20.93100 -1.36500  1.000 34.72201 ? 170 VAL A CB  1 
ATOM   1427 C  CG1 . VAL A 1 171 ? -60.58300 21.13400 -2.02500  1.000 36.09409 ? 170 VAL A CG1 1 
ATOM   1428 C  CG2 . VAL A 1 171 ? -59.24900 19.67100 -0.49800  1.000 32.59044 ? 170 VAL A CG2 1 
ATOM   1429 N  N   . LEU A 1 172 ? -58.67200 21.70600 -4.62600  1.000 32.29388 ? 171 LEU A N   1 
ATOM   1430 C  CA  . LEU A 1 172 ? -58.80700 22.76800 -5.61900  1.000 33.85600 ? 171 LEU A CA  1 
ATOM   1431 C  C   . LEU A 1 172 ? -60.18500 23.39400 -5.44800  1.000 41.10776 ? 171 LEU A C   1 
ATOM   1432 O  O   . LEU A 1 172 ? -61.20200 22.76600 -5.75600  1.000 41.69590 ? 171 LEU A O   1 
ATOM   1433 C  CB  . LEU A 1 172 ? -58.59900 22.23900 -7.03300  1.000 37.31393 ? 171 LEU A CB  1 
ATOM   1434 C  CG  . LEU A 1 172 ? -57.24400 21.54800 -7.24900  1.000 39.54474 ? 171 LEU A CG  1 
ATOM   1435 C  CD1 . LEU A 1 172 ? -57.02600 21.22600 -8.73200  1.000 41.19620 ? 171 LEU A CD1 1 
ATOM   1436 C  CD2 . LEU A 1 172 ? -56.11400 22.40600 -6.69400  1.000 43.79897 ? 171 LEU A CD2 1 
ATOM   1437 N  N   . GLY A 1 173 ? -60.21300 24.61900 -4.93700  1.000 45.17862 ? 172 GLY A N   1 
ATOM   1438 C  CA  . GLY A 1 173 ? -61.45900 25.30600 -4.63200  1.000 48.16444 ? 172 GLY A CA  1 
ATOM   1439 C  C   . GLY A 1 173 ? -62.24900 25.74300 -5.84200  1.000 57.10424 ? 172 GLY A C   1 
ATOM   1440 O  O   . GLY A 1 173 ? -63.42500 26.09800 -5.71200  1.000 60.67904 ? 172 GLY A O   1 
HETATM 1441 N  N   . MSE B 1 2   ? -28.24000 34.84900 -5.37000  1.000 76.60016 ? 1   MSE B N   1 
HETATM 1442 C  CA  . MSE B 1 2   ? -29.33500 34.14200 -4.72000  1.000 77.72193 ? 1   MSE B CA  1 
HETATM 1443 C  C   . MSE B 1 2   ? -29.22000 32.63800 -4.96100  1.000 77.48909 ? 1   MSE B C   1 
HETATM 1444 O  O   . MSE B 1 2   ? -29.27100 31.84700 -4.01500  1.000 80.27145 ? 1   MSE B O   1 
HETATM 1445 C  CB  . MSE B 1 2   ? -30.69000 34.66200 -5.21500  1.000 82.37657 ? 1   MSE B CB  1 
ATOM   1446 N  N   . ASP B 1 3   ? -29.05100 32.24400 -6.22300  1.000 69.48016 ? 2   ASP B N   1 
ATOM   1447 C  CA  . ASP B 1 3   ? -28.96600 30.83800 -6.59300  1.000 62.53216 ? 2   ASP B CA  1 
ATOM   1448 C  C   . ASP B 1 3   ? -27.52000 30.42400 -6.84400  1.000 57.29145 ? 2   ASP B C   1 
ATOM   1449 O  O   . ASP B 1 3   ? -26.73900 31.15200 -7.46500  1.000 53.89337 ? 2   ASP B O   1 
ATOM   1450 C  CB  . ASP B 1 3   ? -29.82300 30.53900 -7.82000  1.000 65.59669 ? 2   ASP B CB  1 
ATOM   1451 C  CG  . ASP B 1 3   ? -31.28100 30.29500 -7.46000  1.000 78.43425 ? 2   ASP B CG  1 
ATOM   1452 O  OD1 . ASP B 1 3   ? -31.92700 29.44500 -8.11100  1.000 81.97794 ? 2   ASP B OD1 1 
ATOM   1453 O  OD2 . ASP B 1 3   ? -31.77500 30.94000 -6.50800  1.000 79.82039 ? 2   ASP B OD2 1 
ATOM   1454 N  N   . TYR B 1 4   ? -27.18100 29.24200 -6.35800  1.000 45.17566 ? 3   TYR B N   1 
ATOM   1455 C  CA  . TYR B 1 4   ? -25.82600 28.73100 -6.37000  1.000 34.87333 ? 3   TYR B CA  1 
ATOM   1456 C  C   . TYR B 1 4   ? -25.82800 27.34600 -6.99400  1.000 34.43412 ? 3   TYR B C   1 
ATOM   1457 O  O   . TYR B 1 4   ? -26.85700 26.67700 -7.03700  1.000 37.71668 ? 3   TYR B O   1 
ATOM   1458 C  CB  . TYR B 1 4   ? -25.27600 28.65300 -4.95200  1.000 32.89794 ? 3   TYR B CB  1 
ATOM   1459 C  CG  . TYR B 1 4   ? -25.14300 29.97600 -4.21100  1.000 32.44543 ? 3   TYR B CG  1 
ATOM   1460 C  CD1 . TYR B 1 4   ? -23.98300 30.74000 -4.31700  1.000 35.35048 ? 3   TYR B CD1 1 
ATOM   1461 C  CD2 . TYR B 1 4   ? -26.15600 30.42800 -3.36600  1.000 37.04833 ? 3   TYR B CD2 1 
ATOM   1462 C  CE1 . TYR B 1 4   ? -23.85300 31.94200 -3.62300  1.000 35.54890 ? 3   TYR B CE1 1 
ATOM   1463 C  CE2 . TYR B 1 4   ? -26.02400 31.60900 -2.66900  1.000 39.59129 ? 3   TYR B CE2 1 
ATOM   1464 C  CZ  . TYR B 1 4   ? -24.86900 32.36100 -2.79900  1.000 35.73994 ? 3   TYR B CZ  1 
ATOM   1465 O  OH  . TYR B 1 4   ? -24.74700 33.55300 -2.10400  1.000 41.00307 ? 3   TYR B OH  1 
ATOM   1466 N  N   . ARG B 1 5   ? -24.65900 26.89500 -7.45100  1.000 32.95260 ? 4   ARG B N   1 
ATOM   1467 C  CA  . ARG B 1 5   ? -24.50100 25.51300 -7.89000  1.000 34.64697 ? 4   ARG B CA  1 
ATOM   1468 C  C   . ARG B 1 5   ? -23.27600 24.92600 -7.21000  1.000 28.17227 ? 4   ARG B C   1 
ATOM   1469 O  O   . ARG B 1 5   ? -22.29500 25.62800 -6.98400  1.000 28.69334 ? 4   ARG B O   1 
ATOM   1470 C  CB  . ARG B 1 5   ? -24.34700 25.40100 -9.41600  1.000 36.22576 ? 4   ARG B CB  1 
ATOM   1471 C  CG  . ARG B 1 5   ? -25.51500 25.94500 -10.20500 1.000 43.21416 ? 4   ARG B CG  1 
ATOM   1472 C  CD  . ARG B 1 5   ? -25.33100 25.67700 -11.68500 1.000 54.07768 ? 4   ARG B CD  1 
ATOM   1473 N  NE  . ARG B 1 5   ? -26.53600 26.00000 -12.44200 1.000 65.99026 ? 4   ARG B NE  1 
ATOM   1474 C  CZ  . ARG B 1 5   ? -27.54200 25.15200 -12.62300 1.000 70.72531 ? 4   ARG B CZ  1 
ATOM   1475 N  NH1 . ARG B 1 5   ? -27.47900 23.93200 -12.09900 1.000 69.52602 ? 4   ARG B NH1 1 
ATOM   1476 N  NH2 . ARG B 1 5   ? -28.60600 25.52500 -13.32200 1.000 77.62549 ? 4   ARG B NH2 1 
ATOM   1477 N  N   . ILE B 1 6   ? -23.32800 23.64300 -6.86700  1.000 30.30822 ? 5   ILE B N   1 
ATOM   1478 C  CA  . ILE B 1 6   ? -22.15900 22.92200 -6.38300  1.000 27.00853 ? 5   ILE B CA  1 
ATOM   1479 C  C   . ILE B 1 6   ? -21.69000 22.00100 -7.51100  1.000 27.32877 ? 5   ILE B C   1 
ATOM   1480 O  O   . ILE B 1 6   ? -22.51400 21.35900 -8.17600  1.000 30.13305 ? 5   ILE B O   1 
ATOM   1481 C  CB  . ILE B 1 6   ? -22.47600 22.14100 -5.09100  1.000 27.66313 ? 5   ILE B CB  1 
ATOM   1482 C  CG1 . ILE B 1 6   ? -22.25900 23.03800 -3.85200  1.000 30.49693 ? 5   ILE B CG1 1 
ATOM   1483 C  CG2 . ILE B 1 6   ? -21.54800 20.93700 -4.97400  1.000 29.32405 ? 5   ILE B CG2 1 
ATOM   1484 C  CD1 . ILE B 1 6   ? -23.24700 24.17400 -3.65700  1.000 32.04596 ? 5   ILE B CD1 1 
ATOM   1485 N  N   . ARG B 1 7   ? -20.37400 21.97900 -7.75200  1.000 27.34668 ? 6   ARG B N   1 
ATOM   1486 C  CA  . ARG B 1 7   ? -19.79400 21.19500 -8.82600  1.000 28.60939 ? 6   ARG B CA  1 
ATOM   1487 C  C   . ARG B 1 7   ? -18.40700 20.72100 -8.42500  1.000 27.77163 ? 6   ARG B C   1 
ATOM   1488 O  O   . ARG B 1 7   ? -17.79600 21.22600 -7.47300  1.000 26.05638 ? 6   ARG B O   1 
ATOM   1489 C  CB  . ARG B 1 7   ? -19.72100 21.99300 -10.12600 1.000 29.42806 ? 6   ARG B CB  1 
ATOM   1490 C  CG  . ARG B 1 7   ? -18.87900 23.23800 -10.05600 1.000 27.79522 ? 6   ARG B CG  1 
ATOM   1491 C  CD  . ARG B 1 7   ? -18.52800 23.64300 -11.46900 1.000 30.66603 ? 6   ARG B CD  1 
ATOM   1492 N  NE  . ARG B 1 7   ? -17.83800 24.93200 -11.50800 1.000 29.32538 ? 6   ARG B NE  1 
ATOM   1493 C  CZ  . ARG B 1 7   ? -16.52700 25.08800 -11.37000 1.000 32.32732 ? 6   ARG B CZ  1 
ATOM   1494 N  NH1 . ARG B 1 7   ? -15.74300 24.04400 -11.16000 1.000 29.28602 ? 6   ARG B NH1 1 
ATOM   1495 N  NH2 . ARG B 1 7   ? -16.00000 26.30200 -11.43600 1.000 33.86737 ? 6   ARG B NH2 1 
ATOM   1496 N  N   A THR B 1 8   ? -17.92400 19.71300 -9.15400  0.780 30.70104 ? 7   THR B N   1 
ATOM   1497 N  N   B THR B 1 8   ? -17.91800 19.73600 -9.17600  0.220 30.07770 ? 7   THR B N   1 
ATOM   1498 C  CA  A THR B 1 8   ? -16.54600 19.28100 -8.98200  0.780 28.02306 ? 7   THR B CA  1 
ATOM   1499 C  CA  B THR B 1 8   ? -16.54500 19.27700 -9.03700  0.220 28.95988 ? 7   THR B CA  1 
ATOM   1500 C  C   A THR B 1 8   ? -15.60400 20.41400 -9.36600  0.780 26.39144 ? 7   THR B C   1 
ATOM   1501 C  C   B THR B 1 8   ? -15.57800 20.39700 -9.40300  0.220 28.43904 ? 7   THR B C   1 
ATOM   1502 O  O   A THR B 1 8   ? -15.81100 21.10400 -10.36800 0.780 32.97434 ? 7   THR B O   1 
ATOM   1503 O  O   B THR B 1 8   ? -15.75100 21.07000 -10.42300 0.220 30.99549 ? 7   THR B O   1 
ATOM   1504 C  CB  A THR B 1 8   ? -16.26300 18.04400 -9.83800  0.780 31.50451 ? 7   THR B CB  1 
ATOM   1505 C  CB  B THR B 1 8   ? -16.32100 18.06700 -9.94400  0.220 32.13906 ? 7   THR B CB  1 
ATOM   1506 O  OG1 A THR B 1 8   ? -16.40300 18.37700 -11.22400 0.780 36.46063 ? 7   THR B OG1 1 
ATOM   1507 O  OG1 B THR B 1 8   ? -17.19200 17.00400 -9.54500  0.220 33.39512 ? 7   THR B OG1 1 
ATOM   1508 C  CG2 A THR B 1 8   ? -17.25900 16.97200 -9.51900  0.780 33.35461 ? 7   THR B CG2 1 
ATOM   1509 C  CG2 B THR B 1 8   ? -14.89100 17.59800 -9.88300  0.220 31.06984 ? 7   THR B CG2 1 
ATOM   1510 N  N   . SER B 1 9   ? -14.55500 20.59400 -8.57500  1.000 28.26926 ? 8   SER B N   1 
ATOM   1511 C  CA  . SER B 1 9   ? -13.56500 21.62200 -8.87900  1.000 24.63654 ? 8   SER B CA  1 
ATOM   1512 C  C   . SER B 1 9   ? -12.71100 21.18800 -10.07000 1.000 29.05417 ? 8   SER B C   1 
ATOM   1513 O  O   . SER B 1 9   ? -12.53700 19.99700 -10.34000 1.000 32.86263 ? 8   SER B O   1 
ATOM   1514 C  CB  . SER B 1 9   ? -12.67200 21.88600 -7.67500  1.000 27.81603 ? 8   SER B CB  1 
ATOM   1515 O  OG  . SER B 1 9   ? -13.46200 22.11700 -6.51500  1.000 26.64440 ? 8   SER B OG  1 
ATOM   1516 N  N   . ARG B 1 10  ? -12.17600 22.17500 -10.78600 1.000 32.28663 ? 9   ARG B N   1 
ATOM   1517 C  CA  . ARG B 1 10  ? -11.30600 21.96000 -11.93300 1.000 33.74929 ? 9   ARG B CA  1 
ATOM   1518 C  C   . ARG B 1 10  ? -9.97100  22.65700 -11.70500 1.000 31.03729 ? 9   ARG B C   1 
ATOM   1519 O  O   . ARG B 1 10  ? -9.85500  23.56500 -10.88000 1.000 30.40393 ? 9   ARG B O   1 
ATOM   1520 C  CB  . ARG B 1 10  ? -11.95500 22.47400 -13.23600 1.000 34.34901 ? 9   ARG B CB  1 
ATOM   1521 C  CG  . ARG B 1 10  ? -13.31800 21.88400 -13.49100 1.000 32.85975 ? 9   ARG B CG  1 
ATOM   1522 C  CD  . ARG B 1 10  ? -13.91700 22.34400 -14.79500 1.000 45.73914 ? 9   ARG B CD  1 
ATOM   1523 N  NE  . ARG B 1 10  ? -14.41900 23.71800 -14.74900 1.000 58.03199 ? 9   ARG B NE  1 
ATOM   1524 C  CZ  . ARG B 1 10  ? -15.70000 24.04200 -14.57800 1.000 57.46157 ? 9   ARG B CZ  1 
ATOM   1525 N  NH1 . ARG B 1 10  ? -16.60600 23.08200 -14.42300 1.000 56.34314 ? 9   ARG B NH1 1 
ATOM   1526 N  NH2 . ARG B 1 10  ? -16.07800 25.32200 -14.57500 1.000 50.64991 ? 9   ARG B NH2 1 
ATOM   1527 N  N   . ASP B 1 11  ? -8.96700  22.24400 -12.48200 1.000 37.49982 ? 10  ASP B N   1 
ATOM   1528 C  CA  . ASP B 1 11  ? -7.62200  22.77100 -12.28300 1.000 38.35191 ? 10  ASP B CA  1 
ATOM   1529 C  C   . ASP B 1 11  ? -7.60900  24.29000 -12.36200 1.000 40.79401 ? 10  ASP B C   1 
ATOM   1530 O  O   . ASP B 1 11  ? -6.94800  24.95600 -11.55500 1.000 42.00942 ? 10  ASP B O   1 
ATOM   1531 C  CB  . ASP B 1 11  ? -6.66300  22.16300 -13.30800 1.000 48.44692 ? 10  ASP B CB  1 
ATOM   1532 C  CG  . ASP B 1 11  ? -5.22100  22.54100 -13.03800 1.000 59.32515 ? 10  ASP B CG  1 
ATOM   1533 O  OD1 . ASP B 1 11  ? -4.63200  23.29100 -13.85600 1.000 65.92824 ? 10  ASP B OD1 1 
ATOM   1534 O  OD2 . ASP B 1 11  ? -4.69400  22.11200 -11.98200 1.000 56.93969 ? 10  ASP B OD2 1 
ATOM   1535 N  N   . GLU B 1 12  ? -8.37000  24.85900 -13.29700 1.000 40.99274 ? 11  GLU B N   1 
ATOM   1536 C  CA  . GLU B 1 12  ? -8.39700  26.30700 -13.45200 1.000 39.52975 ? 11  GLU B CA  1 
ATOM   1537 C  C   . GLU B 1 12  ? -8.99900  27.01900 -12.25000 1.000 36.43329 ? 11  GLU B C   1 
ATOM   1538 O  O   . GLU B 1 12  ? -8.81100  28.23200 -12.12200 1.000 39.76667 ? 11  GLU B O   1 
ATOM   1539 C  CB  . GLU B 1 12  ? -9.16300  26.69800 -14.71700 1.000 42.41955 ? 11  GLU B CB  1 
ATOM   1540 C  CG  . GLU B 1 12  ? -10.64000 26.41000 -14.67600 1.000 50.66969 ? 11  GLU B CG  1 
ATOM   1541 C  CD  . GLU B 1 12  ? -11.31700 26.70600 -15.99900 1.000 60.83893 ? 11  GLU B CD  1 
ATOM   1542 O  OE1 . GLU B 1 12  ? -10.61700 27.11300 -16.94900 1.000 68.20991 ? 11  GLU B OE1 1 
ATOM   1543 O  OE2 . GLU B 1 12  ? -12.54900 26.52400 -16.09900 1.000 66.28517 ? 11  GLU B OE2 1 
ATOM   1544 N  N   . ASP B 1 13  ? -9.70500  26.30500 -11.36500 1.000 29.97867 ? 12  ASP B N   1 
ATOM   1545 C  CA  . ASP B 1 13  ? -10.26700 26.95000 -10.18800 1.000 28.58758 ? 12  ASP B CA  1 
ATOM   1546 C  C   . ASP B 1 13  ? -9.25700  27.09900 -9.05100  1.000 30.36628 ? 12  ASP B C   1 
ATOM   1547 O  O   . ASP B 1 13  ? -9.45900  27.93900 -8.16500  1.000 31.44500 ? 12  ASP B O   1 
ATOM   1548 C  CB  . ASP B 1 13  ? -11.48000 26.15700 -9.68800  1.000 32.87358 ? 12  ASP B CB  1 
ATOM   1549 C  CG  . ASP B 1 13  ? -12.56700 26.02300 -10.73100 1.000 33.39656 ? 12  ASP B CG  1 
ATOM   1550 O  OD1 . ASP B 1 13  ? -12.99600 27.05100 -11.30200 1.000 35.57527 ? 12  ASP B OD1 1 
ATOM   1551 O  OD2 . ASP B 1 13  ? -12.98800 24.87000 -10.99500 1.000 33.32199 ? 12  ASP B OD2 1 
ATOM   1552 N  N   . ALA B 1 14  ? -8.15800  26.34600 -9.08100  1.000 28.92738 ? 13  ALA B N   1 
ATOM   1553 C  CA  . ALA B 1 14  ? -7.30700  26.22200 -7.89900  1.000 27.93217 ? 13  ALA B CA  1 
ATOM   1554 C  C   . ALA B 1 14  ? -6.74300  27.56400 -7.44400  1.000 29.85194 ? 13  ALA B C   1 
ATOM   1555 O  O   . ALA B 1 14  ? -6.70100  27.84600 -6.24400  1.000 27.96412 ? 13  ALA B O   1 
ATOM   1556 C  CB  . ALA B 1 14  ? -6.17200  25.24700 -8.18700  1.000 31.13366 ? 13  ALA B CB  1 
ATOM   1557 N  N   . ALA B 1 15  ? -6.28700  28.39900 -8.38500  1.000 33.96113 ? 14  ALA B N   1 
ATOM   1558 C  CA  . ALA B 1 15  ? -5.65600  29.66100 -8.00800  1.000 32.31201 ? 14  ALA B CA  1 
ATOM   1559 C  C   . ALA B 1 15  ? -6.56700  30.56000 -7.18600  1.000 30.05634 ? 14  ALA B C   1 
ATOM   1560 O  O   . ALA B 1 15  ? -6.06600  31.40800 -6.43900  1.000 32.80226 ? 14  ALA B O   1 
ATOM   1561 C  CB  . ALA B 1 15  ? -5.19300  30.40800 -9.26600  1.000 37.53984 ? 14  ALA B CB  1 
ATOM   1562 N  N   . LEU B 1 16  ? -7.88300  30.41000 -7.31200  1.000 29.91063 ? 15  LEU B N   1 
ATOM   1563 C  CA  . LEU B 1 16  ? -8.84900  31.25200 -6.60200  1.000 29.79756 ? 15  LEU B CA  1 
ATOM   1564 C  C   . LEU B 1 16  ? -9.15200  30.78900 -5.18300  1.000 28.57898 ? 15  LEU B C   1 
ATOM   1565 O  O   . LEU B 1 16  ? -9.80300  31.53400 -4.42700  1.000 26.68201 ? 15  LEU B O   1 
ATOM   1566 C  CB  . LEU B 1 16  ? -10.16200 31.31700 -7.38300  1.000 30.27453 ? 15  LEU B CB  1 
ATOM   1567 C  CG  . LEU B 1 16  ? -10.08400 31.89800 -8.80000  1.000 39.22700 ? 15  LEU B CG  1 
ATOM   1568 C  CD1 . LEU B 1 16  ? -11.33400 31.52800 -9.60400  1.000 40.28264 ? 15  LEU B CD1 1 
ATOM   1569 C  CD2 . LEU B 1 16  ? -9.88400  33.41200 -8.77800  1.000 39.99838 ? 15  LEU B CD2 1 
ATOM   1570 N  N   . LEU B 1 17  ? -8.73600  29.58600 -4.80100  1.000 24.60723 ? 16  LEU B N   1 
ATOM   1571 C  CA  . LEU B 1 17  ? -9.26600  29.04600 -3.55900  1.000 25.13391 ? 16  LEU B CA  1 
ATOM   1572 C  C   . LEU B 1 17  ? -8.59300  29.58400 -2.29000  1.000 24.35653 ? 16  LEU B C   1 
ATOM   1573 O  O   . LEU B 1 17  ? -9.28400  29.70800 -1.25900  1.000 21.12591 ? 16  LEU B O   1 
ATOM   1574 C  CB  . LEU B 1 17  ? -9.19000  27.51400 -3.59900  1.000 24.06159 ? 16  LEU B CB  1 
ATOM   1575 C  CG  . LEU B 1 17  ? -9.90700  26.85600 -4.78300  1.000 26.85790 ? 16  LEU B CG  1 
ATOM   1576 C  CD1 . LEU B 1 17  ? -9.79200  25.32600 -4.65600  1.000 28.56211 ? 16  LEU B CD1 1 
ATOM   1577 C  CD2 . LEU B 1 17  ? -11.38500 27.28700 -4.89400  1.000 26.43569 ? 16  LEU B CD2 1 
ATOM   1578 N  N   . PRO B 1 18  ? -7.27600  29.88400 -2.29000  1.000 24.01197 ? 17  PRO B N   1 
ATOM   1579 C  CA  . PRO B 1 18  ? -6.69300  30.44800 -1.06000  1.000 24.59486 ? 17  PRO B CA  1 
ATOM   1580 C  C   . PRO B 1 18  ? -7.38900  31.71300 -0.59200  1.000 25.77307 ? 17  PRO B C   1 
ATOM   1581 O  O   . PRO B 1 18  ? -7.57600  31.87400 0.61500   1.000 24.32122 ? 17  PRO B O   1 
ATOM   1582 C  CB  . PRO B 1 18  ? -5.22400  30.69000 -1.44600  1.000 26.75809 ? 17  PRO B CB  1 
ATOM   1583 C  CG  . PRO B 1 18  ? -4.90200  29.57100 -2.43100  1.000 26.86192 ? 17  PRO B CG  1 
ATOM   1584 C  CD  . PRO B 1 18  ? -6.21900  29.49100 -3.25000  1.000 25.18619 ? 17  PRO B CD  1 
ATOM   1585 N  N   . ALA B 1 19  ? -7.80000  32.60800 -1.50400  1.000 24.04495 ? 18  ALA B N   1 
ATOM   1586 C  CA  . ALA B 1 19  ? -8.53600  33.79800 -1.08000  1.000 26.31532 ? 18  ALA B CA  1 
ATOM   1587 C  C   . ALA B 1 19  ? -9.87900  33.44600 -0.43300  1.000 23.86944 ? 18  ALA B C   1 
ATOM   1588 O  O   . ALA B 1 19  ? -10.34100 34.15600 0.47100   1.000 25.43894 ? 18  ALA B O   1 
ATOM   1589 C  CB  . ALA B 1 19  ? -8.74100  34.73100 -2.27700  1.000 25.76796 ? 18  ALA B CB  1 
ATOM   1590 N  N   . ILE B 1 20  ? -10.52800 32.36300 -0.87400  1.000 22.69338 ? 19  ILE B N   1 
ATOM   1591 C  CA  . ILE B 1 20  ? -11.77600 31.95000 -0.24500  1.000 22.93473 ? 19  ILE B CA  1 
ATOM   1592 C  C   . ILE B 1 20  ? -11.51700 31.41000 1.16100   1.000 23.16123 ? 19  ILE B C   1 
ATOM   1593 O  O   . ILE B 1 20  ? -12.27900 31.69000 2.09700   1.000 23.01941 ? 19  ILE B O   1 
ATOM   1594 C  CB  . ILE B 1 20  ? -12.48700 30.89600 -1.12700  1.000 23.83472 ? 19  ILE B CB  1 
ATOM   1595 C  CG1 . ILE B 1 20  ? -12.97900 31.53600 -2.42200  1.000 25.44819 ? 19  ILE B CG1 1 
ATOM   1596 C  CG2 . ILE B 1 20  ? -13.62100 30.15200 -0.35400  1.000 22.65923 ? 19  ILE B CG2 1 
ATOM   1597 C  CD1 . ILE B 1 20  ? -13.45400 30.50200 -3.45100  1.000 26.99324 ? 19  ILE B CD1 1 
ATOM   1598 N  N   . GLU B 1 21  ? -10.44600 30.63400 1.34200   1.000 21.34422 ? 20  GLU B N   1 
ATOM   1599 C  CA  . GLU B 1 21  ? -10.13700 30.13500 2.68100   1.000 21.95637 ? 20  GLU B CA  1 
ATOM   1600 C  C   . GLU B 1 21  ? -9.79100  31.28800 3.62400   1.000 23.55316 ? 20  GLU B C   1 
ATOM   1601 O  O   . GLU B 1 21  ? -10.21700 31.29500 4.79300   1.000 23.11606 ? 20  GLU B O   1 
ATOM   1602 C  CB  . GLU B 1 21  ? -8.99500  29.10600 2.62800   1.000 23.69900 ? 20  GLU B CB  1 
ATOM   1603 C  CG  . GLU B 1 21  ? -8.83200  28.37400 3.98700   1.000 23.85206 ? 20  GLU B CG  1 
ATOM   1604 C  CD  . GLU B 1 21  ? -7.77800  27.26100 4.03000   1.000 25.92938 ? 20  GLU B CD  1 
ATOM   1605 O  OE1 . GLU B 1 21  ? -7.38300  26.90200 5.15600   1.000 32.23244 ? 20  GLU B OE1 1 
ATOM   1606 O  OE2 . GLU B 1 21  ? -7.33300  26.74700 2.98500   1.000 27.97677 ? 20  GLU B OE2 1 
ATOM   1607 N  N   . ARG B 1 22  ? -9.05800  32.28300 3.12800   1.000 24.15459 ? 21  ARG B N   1 
ATOM   1608 C  CA  . ARG B 1 22  ? -8.78800  33.46500 3.95100   1.000 21.00928 ? 21  ARG B CA  1 
ATOM   1609 C  C   . ARG B 1 22  ? -10.07600 34.19500 4.30800   1.000 24.36399 ? 21  ARG B C   1 
ATOM   1610 O  O   . ARG B 1 22  ? -10.24400 34.64900 5.45000   1.000 27.77413 ? 21  ARG B O   1 
ATOM   1611 C  CB  . ARG B 1 22  ? -7.80900  34.40600 3.23300   1.000 23.25843 ? 21  ARG B CB  1 
ATOM   1612 C  CG  . ARG B 1 22  ? -6.37600  33.95200 3.36400   1.000 29.73732 ? 21  ARG B CG  1 
ATOM   1613 C  CD  . ARG B 1 22  ? -5.37600  35.00900 2.87500   1.000 35.33664 ? 21  ARG B CD  1 
ATOM   1614 N  NE  . ARG B 1 22  ? -5.47200  35.19200 1.43400   1.000 38.93788 ? 21  ARG B NE  1 
ATOM   1615 C  CZ  . ARG B 1 22  ? -4.79400  34.47700 0.54200   1.000 43.33919 ? 21  ARG B CZ  1 
ATOM   1616 N  NH1 . ARG B 1 22  ? -3.95500  33.52600 0.94500   1.000 47.46694 ? 21  ARG B NH1 1 
ATOM   1617 N  NH2 . ARG B 1 22  ? -4.94900  34.71700 -0.75400  1.000 40.73912 ? 21  ARG B NH2 1 
ATOM   1618 N  N   . SER B 1 23  ? -10.98800 34.35900 3.34600   1.000 21.34847 ? 22  SER B N   1 
ATOM   1619 C  CA  . SER B 1 23  ? -12.23900 35.05700 3.64900   1.000 24.02892 ? 22  SER B CA  1 
ATOM   1620 C  C   . SER B 1 23  ? -13.02000 34.30900 4.71400   1.000 22.80227 ? 22  SER B C   1 
ATOM   1621 O  O   . SER B 1 23  ? -13.53300 34.92000 5.66300   1.000 25.49104 ? 22  SER B O   1 
ATOM   1622 C  CB  . SER B 1 23  ? -13.09100 35.21000 2.38800   1.000 26.74331 ? 22  SER B CB  1 
ATOM   1623 O  OG  . SER B 1 23  ? -14.33000 35.85500 2.69300   1.000 27.73011 ? 22  SER B OG  1 
ATOM   1624 N  N   . ALA B 1 24  ? -13.11200 32.97800 4.57100   1.000 20.50503 ? 23  ALA B N   1 
ATOM   1625 C  CA  . ALA B 1 24  ? -13.83200 32.16900 5.55200   1.000 22.01099 ? 23  ALA B CA  1 
ATOM   1626 C  C   . ALA B 1 24  ? -13.24800 32.35800 6.94600   1.000 20.48431 ? 23  ALA B C   1 
ATOM   1627 O  O   . ALA B 1 24  ? -13.99500 32.52000 7.92200   1.000 22.66171 ? 23  ALA B O   1 
ATOM   1628 C  CB  . ALA B 1 24  ? -13.83400 30.70800 5.13200   1.000 22.65471 ? 23  ALA B CB  1 
ATOM   1629 N  N   . GLY B 1 25  ? -11.92000 32.40700 7.04500   1.000 23.43531 ? 24  GLY B N   1 
ATOM   1630 C  CA  . GLY B 1 25  ? -11.25200 32.55900 8.33300   1.000 24.41175 ? 24  GLY B CA  1 
ATOM   1631 C  C   . GLY B 1 25  ? -11.59600 33.84800 9.05800   1.000 22.87611 ? 24  GLY B C   1 
ATOM   1632 O  O   . GLY B 1 25  ? -11.38500 33.94200 10.26700  1.000 24.16313 ? 24  GLY B O   1 
ATOM   1633 N  N   . GLU B 1 26  ? -12.12400 34.85200 8.34500   1.000 21.93993 ? 25  GLU B N   1 
ATOM   1634 C  CA  . GLU B 1 26  ? -12.50900 36.09100 9.00200   1.000 23.74900 ? 25  GLU B CA  1 
ATOM   1635 C  C   . GLU B 1 26  ? -13.59200 35.85900 10.04300  1.000 25.76373 ? 25  GLU B C   1 
ATOM   1636 O  O   . GLU B 1 26  ? -13.72100 36.67700 10.95900  1.000 27.03120 ? 25  GLU B O   1 
ATOM   1637 C  CB  . GLU B 1 26  ? -12.97700 37.12700 7.96900   1.000 25.78887 ? 25  GLU B CB  1 
ATOM   1638 C  CG  . GLU B 1 26  ? -11.86400 37.65100 7.03900   1.000 26.95083 ? 25  GLU B CG  1 
ATOM   1639 C  CD  . GLU B 1 26  ? -10.80800 38.47100 7.77700   1.000 31.87784 ? 25  GLU B CD  1 
ATOM   1640 O  OE1 . GLU B 1 26  ? -11.14400 39.24300 8.69600   1.000 31.59094 ? 25  GLU B OE1 1 
ATOM   1641 O  OE2 . GLU B 1 26  ? -9.60600  38.31400 7.47100   1.000 38.76048 ? 25  GLU B OE2 1 
ATOM   1642 N  N   . SER B 1 27  ? -14.32100 34.72700 9.95700   1.000 24.42166 ? 26  SER B N   1 
ATOM   1643 C  CA  . SER B 1 27  ? -15.37300 34.41100 10.92500  1.000 22.76743 ? 26  SER B CA  1 
ATOM   1644 C  C   . SER B 1 27  ? -14.84000 34.22200 12.32900  1.000 22.90308 ? 26  SER B C   1 
ATOM   1645 O  O   . SER B 1 27  ? -15.63300 34.22900 13.27200  1.000 27.10090 ? 26  SER B O   1 
ATOM   1646 C  CB  . SER B 1 27  ? -16.13000 33.12700 10.51900  1.000 27.77915 ? 26  SER B CB  1 
ATOM   1647 O  OG  . SER B 1 27  ? -16.82700 33.31900 9.29700   1.000 28.51699 ? 26  SER B OG  1 
ATOM   1648 N  N   . PHE B 1 28  ? -13.52100 34.09100 12.50000  1.000 22.72187 ? 27  PHE B N   1 
ATOM   1649 C  CA  . PHE B 1 28  ? -12.95600 33.87700 13.82000  1.000 24.12044 ? 27  PHE B CA  1 
ATOM   1650 C  C   . PHE B 1 28  ? -12.44400 35.13500 14.49900  1.000 25.87980 ? 27  PHE B C   1 
ATOM   1651 O  O   . PHE B 1 28  ? -12.10200 35.06100 15.68000  1.000 27.88221 ? 27  PHE B O   1 
ATOM   1652 C  CB  . PHE B 1 28  ? -11.79700 32.85100 13.72200  1.000 23.82645 ? 27  PHE B CB  1 
ATOM   1653 C  CG  . PHE B 1 28  ? -12.25800 31.43800 13.45700  1.000 23.18930 ? 27  PHE B CG  1 
ATOM   1654 C  CD1 . PHE B 1 28  ? -12.54400 30.62100 14.51800  1.000 25.24051 ? 27  PHE B CD1 1 
ATOM   1655 C  CD2 . PHE B 1 28  ? -12.42600 30.94800 12.17600  1.000 23.31492 ? 27  PHE B CD2 1 
ATOM   1656 C  CE1 . PHE B 1 28  ? -12.99500 29.31000 14.31700  1.000 25.22272 ? 27  PHE B CE1 1 
ATOM   1657 C  CE2 . PHE B 1 28  ? -12.86200 29.62400 11.97500  1.000 21.15694 ? 27  PHE B CE2 1 
ATOM   1658 C  CZ  . PHE B 1 28  ? -13.14000 28.83200 13.06600  1.000 24.11787 ? 27  PHE B CZ  1 
ATOM   1659 N  N   . ARG B 1 29  ? -12.43600 36.29600 13.82900  1.000 25.62770 ? 28  ARG B N   1 
ATOM   1660 C  CA  . ARG B 1 29  ? -11.76600 37.45300 14.43800  1.000 24.48650 ? 28  ARG B CA  1 
ATOM   1661 C  C   . ARG B 1 29  ? -12.46300 37.92000 15.72500  1.000 27.31113 ? 28  ARG B C   1 
ATOM   1662 O  O   . ARG B 1 29  ? -11.80300 38.47500 16.60400  1.000 26.62635 ? 28  ARG B O   1 
ATOM   1663 C  CB  . ARG B 1 29  ? -11.66700 38.60700 13.43800  1.000 30.17526 ? 28  ARG B CB  1 
ATOM   1664 C  CG  . ARG B 1 29  ? -10.59800 38.39000 12.35400  1.000 31.83364 ? 28  ARG B CG  1 
ATOM   1665 C  CD  . ARG B 1 29  ? -10.02800 39.67700 11.72400  1.000 38.08695 ? 28  ARG B CD  1 
ATOM   1666 N  NE  . ARG B 1 29  ? -9.29200  39.34600 10.50100  1.000 32.84644 ? 28  ARG B NE  1 
ATOM   1667 C  CZ  . ARG B 1 29  ? -8.03100  38.92700 10.47800  1.000 38.33291 ? 28  ARG B CZ  1 
ATOM   1668 N  NH1 . ARG B 1 29  ? -7.35000  38.80500 11.61100  1.000 36.19389 ? 28  ARG B NH1 1 
ATOM   1669 N  NH2 . ARG B 1 29  ? -7.46600  38.59500 9.32600   1.000 37.25706 ? 28  ARG B NH2 1 
ATOM   1670 N  N   . LEU B 1 30  ? -13.77500 37.71400 15.86600  1.000 22.67895 ? 29  LEU B N   1 
ATOM   1671 C  CA  . LEU B 1 30  ? -14.48200 38.16100 17.06600  1.000 21.58562 ? 29  LEU B CA  1 
ATOM   1672 C  C   . LEU B 1 30  ? -14.75600 37.02800 18.04600  1.000 25.33400 ? 29  LEU B C   1 
ATOM   1673 O  O   . LEU B 1 30  ? -15.64300 37.13600 18.90100  1.000 25.04953 ? 29  LEU B O   1 
ATOM   1674 C  CB  . LEU B 1 30  ? -15.75800 38.91000 16.68400  1.000 26.08734 ? 29  LEU B CB  1 
ATOM   1675 C  CG  . LEU B 1 30  ? -15.44100 40.18600 15.90600  1.000 25.80610 ? 29  LEU B CG  1 
ATOM   1676 C  CD1 . LEU B 1 30  ? -16.73000 40.97300 15.61200  1.000 29.55965 ? 29  LEU B CD1 1 
ATOM   1677 C  CD2 . LEU B 1 30  ? -14.43500 41.09700 16.65700  1.000 30.66152 ? 29  LEU B CD2 1 
ATOM   1678 N  N   A LEU B 1 31  ? -14.00900 35.92700 17.93000  0.570 22.77982 ? 30  LEU B N   1 
ATOM   1679 N  N   B LEU B 1 31  ? -14.01800 35.92400 17.92400  0.430 22.95910 ? 30  LEU B N   1 
ATOM   1680 C  CA  A LEU B 1 31  ? -13.98200 34.89000 18.95000  0.570 23.29852 ? 30  LEU B CA  1 
ATOM   1681 C  CA  B LEU B 1 31  ? -13.98800 34.89300 18.94900  0.430 23.17266 ? 30  LEU B CA  1 
ATOM   1682 C  C   A LEU B 1 31  ? -12.67800 35.04100 19.71200  0.570 23.48932 ? 30  LEU B C   1 
ATOM   1683 C  C   B LEU B 1 31  ? -12.68000 35.04600 19.70800  0.430 23.79174 ? 30  LEU B C   1 
ATOM   1684 O  O   A LEU B 1 31  ? -11.63500 34.58800 19.22500  0.570 25.93599 ? 30  LEU B O   1 
ATOM   1685 O  O   B LEU B 1 31  ? -11.63600 34.60000 19.21400  0.430 25.85201 ? 30  LEU B O   1 
ATOM   1686 C  CB  A LEU B 1 31  ? -14.06800 33.49700 18.31900  0.570 22.94667 ? 30  LEU B CB  1 
ATOM   1687 C  CB  B LEU B 1 31  ? -14.08100 33.50000 18.32300  0.430 23.36487 ? 30  LEU B CB  1 
ATOM   1688 C  CG  A LEU B 1 31  ? -15.46500 32.93300 18.08400  0.570 27.12343 ? 30  LEU B CG  1 
ATOM   1689 C  CG  B LEU B 1 31  ? -15.36000 33.14400 17.57300  0.430 26.74205 ? 30  LEU B CG  1 
ATOM   1690 C  CD1 A LEU B 1 31  ? -16.20800 33.81100 17.08300  0.570 27.08021 ? 30  LEU B CD1 1 
ATOM   1691 C  CD1 B LEU B 1 31  ? -15.27600 31.69600 17.09000  0.430 26.73014 ? 30  LEU B CD1 1 
ATOM   1692 C  CD2 A LEU B 1 31  ? -15.39800 31.47400 17.61100  0.570 25.31851 ? 30  LEU B CD2 1 
ATOM   1693 C  CD2 B LEU B 1 31  ? -16.59300 33.35900 18.45500  0.430 30.14126 ? 30  LEU B CD2 1 
ATOM   1694 N  N   . PRO B 1 32  ? -12.67000 35.67600 20.88700  1.000 25.83105 ? 31  PRO B N   1 
ATOM   1695 C  CA  . PRO B 1 32  ? -11.38000 35.99000 21.54300  1.000 26.77828 ? 31  PRO B CA  1 
ATOM   1696 C  C   . PRO B 1 32  ? -10.44400 34.80000 21.74600  1.000 24.87755 ? 31  PRO B C   1 
ATOM   1697 O  O   . PRO B 1 32  ? -9.23000  34.95600 21.57900  1.000 32.11921 ? 31  PRO B O   1 
ATOM   1698 C  CB  . PRO B 1 32  ? -11.81000 36.59400 22.88600  1.000 30.36698 ? 31  PRO B CB  1 
ATOM   1699 C  CG  . PRO B 1 32  ? -13.17500 37.13100 22.64900  1.000 29.56808 ? 31  PRO B CG  1 
ATOM   1700 C  CD  . PRO B 1 32  ? -13.82400 36.23500 21.61500  1.000 28.13460 ? 31  PRO B CD  1 
ATOM   1701 N  N   . GLU B 1 33  ? -10.95400 33.61400 22.08300  1.000 28.15795 ? 32  GLU B N   1 
ATOM   1702 C  CA  . GLU B 1 33  ? -10.02900 32.50400 22.29900  1.000 30.15318 ? 32  GLU B CA  1 
ATOM   1703 C  C   . GLU B 1 33  ? -9.38200  32.02900 21.00100  1.000 30.88615 ? 32  GLU B C   1 
ATOM   1704 O  O   . GLU B 1 33  ? -8.29300  31.44500 21.03400  1.000 30.79973 ? 32  GLU B O   1 
ATOM   1705 C  CB  . GLU B 1 33  ? -10.75200 31.34100 22.98800  1.000 36.02594 ? 32  GLU B CB  1 
ATOM   1706 C  CG  . GLU B 1 33  ? -11.32700 31.72000 24.35100  1.000 44.45166 ? 32  GLU B CG  1 
ATOM   1707 C  CD  . GLU B 1 33  ? -12.01000 30.56900 25.08100  1.000 61.14211 ? 32  GLU B CD  1 
ATOM   1708 O  OE1 . GLU B 1 33  ? -11.85800 29.39700 24.66200  1.000 62.35745 ? 32  GLU B OE1 1 
ATOM   1709 O  OE2 . GLU B 1 33  ? -12.69900 30.84900 26.08800  1.000 67.82181 ? 32  GLU B OE2 1 
ATOM   1710 N  N   . LEU B 1 34  ? -10.00700 32.30700 19.85700  1.000 25.88184 ? 33  LEU B N   1 
ATOM   1711 C  CA  . LEU B 1 34  ? -9.60200  31.72800 18.58200  1.000 22.60079 ? 33  LEU B CA  1 
ATOM   1712 C  C   . LEU B 1 34  ? -9.30600  32.78600 17.53600  1.000 22.67097 ? 33  LEU B C   1 
ATOM   1713 O  O   . LEU B 1 34  ? -9.20600  32.45000 16.35100  1.000 26.13537 ? 33  LEU B O   1 
ATOM   1714 C  CB  . LEU B 1 34  ? -10.68000 30.77700 18.04900  1.000 23.55932 ? 33  LEU B CB  1 
ATOM   1715 C  CG  . LEU B 1 34  ? -11.02900 29.61100 18.96400  1.000 24.61647 ? 33  LEU B CG  1 
ATOM   1716 C  CD1 . LEU B 1 34  ? -12.17800 28.76300 18.40200  1.000 28.71654 ? 33  LEU B CD1 1 
ATOM   1717 C  CD2 . LEU B 1 34  ? -9.79900  28.74700 19.24100  1.000 29.94328 ? 33  LEU B CD2 1 
ATOM   1718 N  N   . ALA B 1 35  ? -9.15100  34.05800 17.94500  1.000 23.84378 ? 34  ALA B N   1 
ATOM   1719 C  CA  . ALA B 1 35  ? -8.97200  35.12600 16.95500  1.000 24.43714 ? 34  ALA B CA  1 
ATOM   1720 C  C   . ALA B 1 35  ? -7.75600  34.87900 16.06600  1.000 27.53338 ? 34  ALA B C   1 
ATOM   1721 O  O   . ALA B 1 35  ? -7.75200  35.28600 14.89500  1.000 31.21944 ? 34  ALA B O   1 
ATOM   1722 C  CB  . ALA B 1 35  ? -8.85000  36.47900 17.64900  1.000 30.00686 ? 34  ALA B CB  1 
ATOM   1723 N  N   . TRP B 1 36  ? -6.71600  34.23400 16.60900  1.000 24.91397 ? 35  TRP B N   1 
ATOM   1724 C  CA  . TRP B 1 36  ? -5.48200  33.98200 15.86900  1.000 26.16505 ? 35  TRP B CA  1 
ATOM   1725 C  C   . TRP B 1 36  ? -5.71700  33.12100 14.63200  1.000 25.18665 ? 35  TRP B C   1 
ATOM   1726 O  O   . TRP B 1 36  ? -4.91600  33.17500 13.69500  1.000 28.10457 ? 35  TRP B O   1 
ATOM   1727 C  CB  . TRP B 1 36  ? -4.44400  33.31800 16.77600  1.000 28.90112 ? 35  TRP B CB  1 
ATOM   1728 C  CG  . TRP B 1 36  ? -4.87000  31.93200 17.27600  1.000 28.14104 ? 35  TRP B CG  1 
ATOM   1729 C  CD1 . TRP B 1 36  ? -5.70400  31.65900 18.33600  1.000 30.50030 ? 35  TRP B CD1 1 
ATOM   1730 C  CD2 . TRP B 1 36  ? -4.48000  30.65900 16.73700  1.000 31.94982 ? 35  TRP B CD2 1 
ATOM   1731 N  NE1 . TRP B 1 36  ? -5.85300  30.29400 18.47700  1.000 30.05141 ? 35  TRP B NE1 1 
ATOM   1732 C  CE2 . TRP B 1 36  ? -5.11200  29.66200 17.51400  1.000 29.52012 ? 35  TRP B CE2 1 
ATOM   1733 C  CE3 . TRP B 1 36  ? -3.66100  30.26900 15.67500  1.000 34.30970 ? 35  TRP B CE3 1 
ATOM   1734 C  CZ2 . TRP B 1 36  ? -4.94900  28.30300 17.25800  1.000 34.69338 ? 35  TRP B CZ2 1 
ATOM   1735 C  CZ3 . TRP B 1 36  ? -3.48500  28.92400 15.43400  1.000 38.25099 ? 35  TRP B CZ3 1 
ATOM   1736 C  CH2 . TRP B 1 36  ? -4.12700  27.95100 16.22000  1.000 37.32028 ? 35  TRP B CH2 1 
ATOM   1737 N  N   . ILE B 1 37  ? -6.78100  32.31600 14.62200  1.000 25.06560 ? 36  ILE B N   1 
ATOM   1738 C  CA  . ILE B 1 37  ? -7.09400  31.45800 13.48000  1.000 27.22087 ? 36  ILE B CA  1 
ATOM   1739 C  C   . ILE B 1 37  ? -7.26300  32.26600 12.20200  1.000 24.20893 ? 36  ILE B C   1 
ATOM   1740 O  O   . ILE B 1 37  ? -6.93500  31.78600 11.11000  1.000 29.31524 ? 36  ILE B O   1 
ATOM   1741 C  CB  . ILE B 1 37  ? -8.37300  30.65300 13.78800  1.000 25.08915 ? 36  ILE B CB  1 
ATOM   1742 C  CG1 . ILE B 1 37  ? -8.09700  29.64000 14.88500  1.000 27.85269 ? 36  ILE B CG1 1 
ATOM   1743 C  CG2 . ILE B 1 37  ? -8.96100  30.02900 12.52300  1.000 28.56361 ? 36  ILE B CG2 1 
ATOM   1744 C  CD1 . ILE B 1 37  ? -7.10600  28.56300 14.48500  1.000 33.77757 ? 36  ILE B CD1 1 
ATOM   1745 N  N   . ALA B 1 38  ? -7.78600  33.49300 12.30100  1.000 24.20481 ? 37  ALA B N   1 
ATOM   1746 C  CA  . ALA B 1 38  ? -8.00200  34.27500 11.09800  1.000 26.67570 ? 37  ALA B CA  1 
ATOM   1747 C  C   . ALA B 1 38  ? -6.69600  34.63100 10.39100  1.000 33.16531 ? 37  ALA B C   1 
ATOM   1748 O  O   . ALA B 1 38  ? -6.72400  35.07600 9.23300   1.000 35.28322 ? 37  ALA B O   1 
ATOM   1749 C  CB  . ALA B 1 38  ? -8.76400  35.54200 11.45400  1.000 30.72630 ? 37  ALA B CB  1 
ATOM   1750 N  N   . ASP B 1 39  ? -5.55300  34.47600 11.06000  1.000 33.80950 ? 38  ASP B N   1 
ATOM   1751 C  CA  . ASP B 1 39  ? -4.25700  34.79100 10.47200  1.000 33.41661 ? 38  ASP B CA  1 
ATOM   1752 C  C   . ASP B 1 39  ? -3.38000  33.55300 10.34400  1.000 32.82195 ? 38  ASP B C   1 
ATOM   1753 O  O   . ASP B 1 39  ? -2.18800  33.66200 10.03200  1.000 35.91571 ? 38  ASP B O   1 
ATOM   1754 C  CB  . ASP B 1 39  ? -3.54200  35.87100 11.29000  1.000 38.05609 ? 38  ASP B CB  1 
ATOM   1755 C  CG  . ASP B 1 39  ? -4.34700  37.16400 11.37200  1.000 48.16969 ? 38  ASP B CG  1 
ATOM   1756 O  OD1 . ASP B 1 39  ? -4.82000  37.64700 10.31600  1.000 41.61587 ? 38  ASP B OD1 1 
ATOM   1757 O  OD2 . ASP B 1 39  ? -4.50400  37.68600 12.49400  1.000 46.68582 ? 38  ASP B OD2 1 
ATOM   1758 N  N   . ALA B 1 40  ? -3.95200  32.38000 10.56100  1.000 35.74022 ? 39  ALA B N   1 
ATOM   1759 C  CA  . ALA B 1 40  ? -3.20700  31.16600 10.31600  1.000 34.14161 ? 39  ALA B CA  1 
ATOM   1760 C  C   . ALA B 1 40  ? -3.09800  30.92800 8.81100   1.000 34.68685 ? 39  ALA B C   1 
ATOM   1761 O  O   . ALA B 1 40  ? -3.85200  31.48300 8.00300   1.000 40.46203 ? 39  ALA B O   1 
ATOM   1762 C  CB  . ALA B 1 40  ? -3.87800  29.99400 11.02800  1.000 36.26279 ? 39  ALA B CB  1 
ATOM   1763 N  N   . GLY B 1 41  ? -2.13200  30.10400 8.43000   1.000 40.15309 ? 40  GLY B N   1 
ATOM   1764 C  CA  . GLY B 1 41  ? -1.93500  29.82700 7.02100   1.000 35.30125 ? 40  GLY B CA  1 
ATOM   1765 C  C   . GLY B 1 41  ? -3.13400  29.13600 6.40500   1.000 33.51051 ? 40  GLY B C   1 
ATOM   1766 O  O   . GLY B 1 41  ? -3.94300  28.50400 7.07800   1.000 36.04747 ? 40  GLY B O   1 
ATOM   1767 N  N   . VAL B 1 42  ? -3.24600  29.26900 5.09200   1.000 30.68858 ? 41  VAL B N   1 
ATOM   1768 C  CA  . VAL B 1 42  ? -4.22100  28.51100 4.32400   1.000 29.65872 ? 41  VAL B CA  1 
ATOM   1769 C  C   . VAL B 1 42  ? -3.45000  27.62700 3.36000   1.000 28.68923 ? 41  VAL B C   1 
ATOM   1770 O  O   . VAL B 1 42  ? -2.26400  27.84700 3.10500   1.000 32.26169 ? 41  VAL B O   1 
ATOM   1771 C  CB  . VAL B 1 42  ? -5.20100  29.42300 3.56200   1.000 29.10504 ? 41  VAL B CB  1 
ATOM   1772 C  CG1 . VAL B 1 42  ? -5.87600  30.38200 4.52900   1.000 30.77590 ? 41  VAL B CG1 1 
ATOM   1773 C  CG2 . VAL B 1 42  ? -4.47400  30.17300 2.44200   1.000 29.16808 ? 41  VAL B CG2 1 
ATOM   1774 N  N   . ALA B 1 43  ? -4.13700  26.62500 2.81700   1.000 27.26484 ? 42  ALA B N   1 
ATOM   1775 C  CA  . ALA B 1 43  ? -3.48600  25.71100 1.88700   1.000 31.07338 ? 42  ALA B CA  1 
ATOM   1776 C  C   . ALA B 1 43  ? -3.07500  26.44200 0.61100   1.000 34.97816 ? 42  ALA B C   1 
ATOM   1777 O  O   . ALA B 1 43  ? -3.79500  27.31500 0.11900   1.000 34.85071 ? 42  ALA B O   1 
ATOM   1778 C  CB  . ALA B 1 43  ? -4.41300  24.54800 1.54900   1.000 28.77048 ? 42  ALA B CB  1 
ATOM   1779 N  N   . GLY B 1 44  ? -1.89500  26.07300 0.06100   1.000 30.00783 ? 43  GLY B N   1 
ATOM   1780 C  CA  . GLY B 1 44  ? -1.45300  26.63900 -1.20100  1.000 30.21160 ? 43  GLY B CA  1 
ATOM   1781 C  C   . GLY B 1 44  ? -2.15200  26.04400 -2.41600  1.000 29.60976 ? 43  GLY B C   1 
ATOM   1782 O  O   . GLY B 1 44  ? -2.88600  25.05900 -2.33300  1.000 29.40347 ? 43  GLY B O   1 
ATOM   1783 N  N   . VAL B 1 45  ? -1.89900  26.65700 -3.58000  1.000 31.60155 ? 44  VAL B N   1 
ATOM   1784 C  CA  . VAL B 1 45  ? -2.58900  26.24200 -4.80600  1.000 32.26345 ? 44  VAL B CA  1 
ATOM   1785 C  C   . VAL B 1 45  ? -2.23700  24.80200 -5.17900  1.000 29.09750 ? 44  VAL B C   1 
ATOM   1786 O  O   . VAL B 1 45  ? -3.09600  24.04400 -5.64700  1.000 29.62334 ? 44  VAL B O   1 
ATOM   1787 C  CB  . VAL B 1 45  ? -2.27900  27.21500 -5.95600  1.000 34.84006 ? 44  VAL B CB  1 
ATOM   1788 C  CG1 . VAL B 1 45  ? -2.97000  26.76400 -7.26100  1.000 32.98391 ? 44  VAL B CG1 1 
ATOM   1789 C  CG2 . VAL B 1 45  ? -2.70200  28.62000 -5.58200  1.000 40.11453 ? 44  VAL B CG2 1 
ATOM   1790 N  N   . ASP B 1 46  ? -0.98500  24.39000 -4.95200  1.000 31.57141 ? 45  ASP B N   1 
ATOM   1791 C  CA  . ASP B 1 46  ? -0.58100  23.04500 -5.36000  1.000 37.85263 ? 45  ASP B CA  1 
ATOM   1792 C  C   . ASP B 1 46  ? -1.26500  21.96400 -4.53000  1.000 35.78850 ? 45  ASP B C   1 
ATOM   1793 O  O   . ASP B 1 46  ? -1.49900  20.85800 -5.03200  1.000 36.42073 ? 45  ASP B O   1 
ATOM   1794 C  CB  . ASP B 1 46  ? 0.94100   22.91900 -5.29000  1.000 39.76143 ? 45  ASP B CB  1 
ATOM   1795 C  CG  . ASP B 1 46  ? 1.63100   23.75100 -6.36000  1.000 54.14190 ? 45  ASP B CG  1 
ATOM   1796 O  OD1 . ASP B 1 46  ? 1.00700   23.97000 -7.42100  1.000 56.62579 ? 45  ASP B OD1 1 
ATOM   1797 O  OD2 . ASP B 1 46  ? 2.78600   24.18500 -6.15400  1.000 58.45297 ? 45  ASP B OD2 1 
ATOM   1798 N  N   . PHE B 1 47  ? -1.59100  22.25800 -3.27200  1.000 30.70795 ? 46  PHE B N   1 
ATOM   1799 C  CA  . PHE B 1 47  ? -2.40800  21.34200 -2.48500  1.000 31.18398 ? 46  PHE B CA  1 
ATOM   1800 C  C   . PHE B 1 47  ? -3.75900  21.09300 -3.15700  1.000 31.23847 ? 46  PHE B C   1 
ATOM   1801 O  O   . PHE B 1 47  ? -4.16900  19.93900 -3.36800  1.000 28.99021 ? 46  PHE B O   1 
ATOM   1802 C  CB  . PHE B 1 47  ? -2.60500  21.91700 -1.08000  1.000 30.48094 ? 46  PHE B CB  1 
ATOM   1803 C  CG  . PHE B 1 47  ? -3.57800  21.14100 -0.24200  1.000 31.25831 ? 46  PHE B CG  1 
ATOM   1804 C  CD1 . PHE B 1 47  ? -3.19300  19.96000 0.36600   1.000 35.55831 ? 46  PHE B CD1 1 
ATOM   1805 C  CD2 . PHE B 1 47  ? -4.86800  21.60600 -0.05100  1.000 29.17151 ? 46  PHE B CD2 1 
ATOM   1806 C  CE1 . PHE B 1 47  ? -4.08700  19.23800 1.13600   1.000 33.24072 ? 46  PHE B CE1 1 
ATOM   1807 C  CE2 . PHE B 1 47  ? -5.77000  20.86900 0.73400   1.000 30.30013 ? 46  PHE B CE2 1 
ATOM   1808 C  CZ  . PHE B 1 47  ? -5.37500  19.71700 1.32800   1.000 29.20753 ? 46  PHE B CZ  1 
ATOM   1809 N  N   . HIS B 1 48  ? -4.45800  22.17100 -3.52500  1.000 29.51220 ? 47  HIS B N   1 
ATOM   1810 C  CA  . HIS B 1 48  ? -5.73800  22.01200 -4.20500  1.000 26.92816 ? 47  HIS B CA  1 
ATOM   1811 C  C   . HIS B 1 48  ? -5.57500  21.28800 -5.52700  1.000 27.22992 ? 47  HIS B C   1 
ATOM   1812 O  O   . HIS B 1 48  ? -6.39300  20.42100 -5.86300  1.000 28.18308 ? 47  HIS B O   1 
ATOM   1813 C  CB  . HIS B 1 48  ? -6.40300  23.36900 -4.44300  1.000 26.42612 ? 47  HIS B CB  1 
ATOM   1814 C  CG  . HIS B 1 48  ? -6.76800  24.07100 -3.17600  1.000 23.96726 ? 47  HIS B CG  1 
ATOM   1815 N  ND1 . HIS B 1 48  ? -7.82400  23.67400 -2.39300  1.000 26.69376 ? 47  HIS B ND1 1 
ATOM   1816 C  CD2 . HIS B 1 48  ? -6.20700  25.13200 -2.55000  1.000 28.33533 ? 47  HIS B CD2 1 
ATOM   1817 C  CE1 . HIS B 1 48  ? -7.89600  24.45300 -1.32700  1.000 26.04219 ? 47  HIS B CE1 1 
ATOM   1818 N  NE2 . HIS B 1 48  ? -6.92400  25.34500 -1.39900  1.000 25.27553 ? 47  HIS B NE2 1 
ATOM   1819 N  N   . ARG B 1 49  ? -4.52600  21.62700 -6.28500  1.000 27.19267 ? 48  ARG B N   1 
ATOM   1820 C  CA  A ARG B 1 49  ? -4.30600  20.97600 -7.57200  0.590 33.75489 ? 48  ARG B CA  1 
ATOM   1821 C  CA  B ARG B 1 49  ? -4.30500  20.97600 -7.57200  0.410 33.70371 ? 48  ARG B CA  1 
ATOM   1822 C  C   . ARG B 1 49  ? -4.17600  19.46900 -7.41000  1.000 36.04624 ? 48  ARG B C   1 
ATOM   1823 O  O   . ARG B 1 49  ? -4.68300  18.70800 -8.23600  1.000 33.19579 ? 48  ARG B O   1 
ATOM   1824 C  CB  A ARG B 1 49  ? -3.06000  21.53800 -8.25400  0.590 38.09817 ? 48  ARG B CB  1 
ATOM   1825 C  CB  B ARG B 1 49  ? -3.05700  21.53800 -8.25200  0.410 38.01719 ? 48  ARG B CB  1 
ATOM   1826 C  CG  A ARG B 1 49  ? -3.21800  22.93200 -8.84600  0.590 39.71646 ? 48  ARG B CG  1 
ATOM   1827 C  CG  B ARG B 1 49  ? -3.17800  22.97500 -8.73800  0.410 39.83168 ? 48  ARG B CG  1 
ATOM   1828 C  CD  A ARG B 1 49  ? -2.09500  23.20800 -9.83500  0.590 46.09578 ? 48  ARG B CD  1 
ATOM   1829 C  CD  B ARG B 1 49  ? -1.99100  23.33100 -9.61800  0.410 45.28058 ? 48  ARG B CD  1 
ATOM   1830 N  NE  A ARG B 1 49  ? -2.06500  24.59900 -10.27100 0.590 48.09482 ? 48  ARG B NE  1 
ATOM   1831 N  NE  B ARG B 1 49  ? -1.77600  24.77200 -9.71700  0.410 46.75598 ? 48  ARG B NE  1 
ATOM   1832 C  CZ  A ARG B 1 49  ? -1.13300  25.47600 -9.91100  0.590 47.16335 ? 48  ARG B CZ  1 
ATOM   1833 C  CZ  B ARG B 1 49  ? -2.34600  25.56000 -10.62400 0.410 48.17277 ? 48  ARG B CZ  1 
ATOM   1834 N  NH1 A ARG B 1 49  ? -1.19200  26.72500 -10.35500 0.590 51.32739 ? 48  ARG B NH1 1 
ATOM   1835 N  NH1 B ARG B 1 49  ? -2.08200  26.85800 -10.62900 0.410 50.15243 ? 48  ARG B NH1 1 
ATOM   1836 N  NH2 A ARG B 1 49  ? -0.13800  25.10500 -9.11600  0.590 42.29845 ? 48  ARG B NH2 1 
ATOM   1837 N  NH2 B ARG B 1 49  ? -3.18400  25.05900 -11.52300 0.410 47.13833 ? 48  ARG B NH2 1 
ATOM   1838 N  N   A ARG B 1 50  ? -3.50100  19.02100 -6.34600  0.520 33.50507 ? 49  ARG B N   1 
ATOM   1839 N  N   B ARG B 1 50  ? -3.50000  19.01900 -6.34800  0.480 33.62131 ? 49  ARG B N   1 
ATOM   1840 C  CA  A ARG B 1 50  ? -3.27300  17.59300 -6.15100  0.520 36.42574 ? 49  ARG B CA  1 
ATOM   1841 C  CA  B ARG B 1 50  ? -3.28200  17.58700 -6.16500  0.480 36.40683 ? 49  ARG B CA  1 
ATOM   1842 C  C   A ARG B 1 50  ? -4.57700  16.85300 -5.87200  0.520 33.58323 ? 49  ARG B C   1 
ATOM   1843 C  C   B ARG B 1 50  ? -4.59000  16.85700 -5.88600  0.480 33.58340 ? 49  ARG B C   1 
ATOM   1844 O  O   A ARG B 1 50  ? -4.80900  15.76900 -6.42100  0.520 35.24802 ? 49  ARG B O   1 
ATOM   1845 O  O   B ARG B 1 50  ? -4.83400  15.78000 -6.44300  0.480 35.41564 ? 49  ARG B O   1 
ATOM   1846 C  CB  A ARG B 1 50  ? -2.27500  17.37800 -5.01200  0.520 39.89650 ? 49  ARG B CB  1 
ATOM   1847 C  CB  B ARG B 1 50  ? -2.28500  17.34500 -5.03200  0.480 39.84477 ? 49  ARG B CB  1 
ATOM   1848 C  CG  A ARG B 1 50  ? -1.88900  15.93100 -4.77300  0.520 45.55185 ? 49  ARG B CG  1 
ATOM   1849 C  CG  B ARG B 1 50  ? -1.74700  15.92700 -4.99100  0.480 46.62439 ? 49  ARG B CG  1 
ATOM   1850 C  CD  A ARG B 1 50  ? -0.80000  15.81000 -3.70200  0.520 47.99576 ? 49  ARG B CD  1 
ATOM   1851 C  CD  B ARG B 1 50  ? -0.82000  15.68400 -3.80400  0.480 48.29237 ? 49  ARG B CD  1 
ATOM   1852 N  NE  A ARG B 1 50  ? -1.27300  16.28000 -2.40500  0.520 42.68583 ? 49  ARG B NE  1 
ATOM   1853 N  NE  B ARG B 1 50  ? -1.53900  15.16200 -2.64500  0.480 46.89598 ? 49  ARG B NE  1 
ATOM   1854 C  CZ  A ARG B 1 50  ? -2.01500  15.55000 -1.57500  0.520 42.76257 ? 49  ARG B CZ  1 
ATOM   1855 C  CZ  B ARG B 1 50  ? -1.78300  15.85500 -1.53800  0.480 43.79670 ? 49  ARG B CZ  1 
ATOM   1856 N  NH1 A ARG B 1 50  ? -2.35700  14.31200 -1.90400  0.520 43.20060 ? 49  ARG B NH1 1 
ATOM   1857 N  NH1 B ARG B 1 50  ? -1.36200  17.11100 -1.42600  0.480 43.24488 ? 49  ARG B NH1 1 
ATOM   1858 N  NH2 A ARG B 1 50  ? -2.42100  16.06100 -0.42100  0.520 44.14075 ? 49  ARG B NH2 1 
ATOM   1859 N  NH2 B ARG B 1 50  ? -2.44700  15.28700 -0.54200  0.480 42.64563 ? 49  ARG B NH2 1 
ATOM   1860 N  N   . LEU B 1 51  ? -5.43700  17.42500 -5.02200  1.000 31.50449 ? 50  LEU B N   1 
ATOM   1861 C  CA  . LEU B 1 51  ? -6.71300  16.79000 -4.69100  1.000 28.45840 ? 50  LEU B CA  1 
ATOM   1862 C  C   . LEU B 1 51  ? -7.69400  16.87100 -5.85400  1.000 25.96875 ? 50  LEU B C   1 
ATOM   1863 O  O   . LEU B 1 51  ? -8.45200  15.92900 -6.08200  1.000 30.27594 ? 50  LEU B O   1 
ATOM   1864 C  CB  . LEU B 1 51  ? -7.30300  17.42200 -3.42800  1.000 24.48785 ? 50  LEU B CB  1 
ATOM   1865 C  CG  . LEU B 1 51  ? -6.39800  17.13500 -2.22500  1.000 27.71240 ? 50  LEU B CG  1 
ATOM   1866 C  CD1 . LEU B 1 51  ? -6.98700  17.77300 -0.95700  1.000 26.22042 ? 50  LEU B CD1 1 
ATOM   1867 C  CD2 . LEU B 1 51  ? -6.19700  15.64400 -2.01600  1.000 30.42972 ? 50  LEU B CD2 1 
ATOM   1868 N  N   . ILE B 1 52  ? -7.66500  17.96500 -6.62200  1.000 25.78224 ? 51  ILE B N   1 
ATOM   1869 C  CA  . ILE B 1 52  ? -8.46600  18.03500 -7.84400  1.000 31.26612 ? 51  ILE B CA  1 
ATOM   1870 C  C   . ILE B 1 52  ? -8.08800  16.91200 -8.80300  1.000 35.68235 ? 51  ILE B C   1 
ATOM   1871 O  O   . ILE B 1 52  ? -8.95700  16.29400 -9.43600  1.000 35.99153 ? 51  ILE B O   1 
ATOM   1872 C  CB  . ILE B 1 52  ? -8.31300  19.42300 -8.49300  1.000 28.90668 ? 51  ILE B CB  1 
ATOM   1873 C  CG1 . ILE B 1 52  ? -9.09300  20.46800 -7.67900  1.000 29.56437 ? 51  ILE B CG1 1 
ATOM   1874 C  CG2 . ILE B 1 52  ? -8.75500  19.38200 -9.96100  1.000 36.54314 ? 51  ILE B CG2 1 
ATOM   1875 C  CD1 . ILE B 1 52  ? -8.72800  21.91600 -8.00900  1.000 32.04517 ? 51  ILE B CD1 1 
ATOM   1876 N  N   . GLU B 1 53  ? -6.78700  16.62700 -8.93200  1.000 33.15112 ? 52  GLU B N   1 
ATOM   1877 C  CA  . GLU B 1 53  ? -6.36000  15.54900 -9.81600  1.000 38.29633 ? 52  GLU B CA  1 
ATOM   1878 C  C   . GLU B 1 53  ? -6.91300  14.20200 -9.36200  1.000 38.51490 ? 52  GLU B C   1 
ATOM   1879 O  O   . GLU B 1 53  ? -7.20900  13.33700 -10.19600 1.000 41.19146 ? 52  GLU B O   1 
ATOM   1880 C  CB  . GLU B 1 53  ? -4.83200  15.50900 -9.89500  1.000 40.42023 ? 52  GLU B CB  1 
ATOM   1881 C  CG  . GLU B 1 53  ? -4.28900  14.40300 -10.79100 1.000 51.46535 ? 52  GLU B CG  1 
ATOM   1882 C  CD  . GLU B 1 53  ? -4.29200  14.76800 -12.26800 1.000 65.01565 ? 52  GLU B CD  1 
ATOM   1883 O  OE1 . GLU B 1 53  ? -3.51700  14.15000 -13.03100 1.000 73.36318 ? 52  GLU B OE1 1 
ATOM   1884 O  OE2 . GLU B 1 53  ? -5.05200  15.67600 -12.67000 1.000 68.02632 ? 52  GLU B OE2 1 
ATOM   1885 N  N   . ARG B 1 54  ? -7.07100  14.01200 -8.05200  1.000 40.82877 ? 53  ARG B N   1 
ATOM   1886 C  CA  . ARG B 1 54  ? -7.66900  12.79400 -7.52300  1.000 38.32389 ? 53  ARG B CA  1 
ATOM   1887 C  C   . ARG B 1 54  ? -9.18300  12.75900 -7.68100  1.000 37.81389 ? 53  ARG B C   1 
ATOM   1888 O  O   . ARG B 1 54  ? -9.77400  11.67200 -7.62200  1.000 40.58361 ? 53  ARG B O   1 
ATOM   1889 C  CB  . ARG B 1 54  ? -7.30200  12.62800 -6.04700  1.000 41.25908 ? 53  ARG B CB  1 
ATOM   1890 C  CG  . ARG B 1 54  ? -5.81200  12.42000 -5.82000  1.000 48.44989 ? 53  ARG B CG  1 
ATOM   1891 C  CD  . ARG B 1 54  ? -5.54600  11.81500 -4.45500  1.000 52.83861 ? 53  ARG B CD  1 
ATOM   1892 N  NE  . ARG B 1 54  ? -5.91300  10.40100 -4.42200  1.000 56.84848 ? 53  ARG B NE  1 
ATOM   1893 C  CZ  . ARG B 1 54  ? -5.89900  9.65600  -3.32100  1.000 54.77212 ? 53  ARG B CZ  1 
ATOM   1894 N  NH1 . ARG B 1 54  ? -5.53600  10.19500 -2.16400  1.000 51.79954 ? 53  ARG B NH1 1 
ATOM   1895 N  NH2 . ARG B 1 54  ? -6.26200  8.38300  -3.37100  1.000 52.53037 ? 53  ARG B NH2 1 
ATOM   1896 N  N   . GLY B 1 55  ? -9.81700  13.90600 -7.89200  1.000 33.70778 ? 54  GLY B N   1 
ATOM   1897 C  CA  . GLY B 1 55  ? -11.25200 13.97200 -8.07400  1.000 36.74056 ? 54  GLY B CA  1 
ATOM   1898 C  C   . GLY B 1 55  ? -12.05800 14.31800 -6.83600  1.000 37.04120 ? 54  GLY B C   1 
ATOM   1899 O  O   . GLY B 1 55  ? -13.27900 14.49800 -6.94400  1.000 35.48553 ? 54  GLY B O   1 
ATOM   1900 N  N   . SER B 1 56  ? -11.42300 14.44200 -5.67500  1.000 28.75361 ? 55  SER B N   1 
ATOM   1901 C  CA  . SER B 1 56  ? -12.14100 14.54700 -4.40300  1.000 27.37560 ? 55  SER B CA  1 
ATOM   1902 C  C   . SER B 1 56  ? -12.20400 15.98400 -3.90300  1.000 25.39283 ? 55  SER B C   1 
ATOM   1903 O  O   . SER B 1 56  ? -11.81900 16.27800 -2.76900  1.000 26.51511 ? 55  SER B O   1 
ATOM   1904 C  CB  . SER B 1 56  ? -11.48500 13.63200 -3.37000  1.000 28.84626 ? 55  SER B CB  1 
ATOM   1905 O  OG  . SER B 1 56  ? -10.07700 13.86600 -3.25900  1.000 30.05800 ? 55  SER B OG  1 
ATOM   1906 N  N   . HIS B 1 57  ? -12.70500 16.89300 -4.74500  1.000 23.17397 ? 56  HIS B N   1 
ATOM   1907 C  CA  . HIS B 1 57  ? -12.63700 18.32300 -4.46200  1.000 22.91556 ? 56  HIS B CA  1 
ATOM   1908 C  C   . HIS B 1 57  ? -13.82100 18.99300 -5.15300  1.000 21.57706 ? 56  HIS B C   1 
ATOM   1909 O  O   . HIS B 1 57  ? -14.02800 18.78700 -6.35200  1.000 26.94444 ? 56  HIS B O   1 
ATOM   1910 C  CB  . HIS B 1 57  ? -11.30100 18.87100 -4.97500  1.000 24.69700 ? 56  HIS B CB  1 
ATOM   1911 C  CG  . HIS B 1 57  ? -10.89300 20.18200 -4.37800  1.000 23.92805 ? 56  HIS B CG  1 
ATOM   1912 N  ND1 . HIS B 1 57  ? -11.65500 21.32600 -4.50100  1.000 24.33299 ? 56  HIS B ND1 1 
ATOM   1913 C  CD2 . HIS B 1 57  ? -9.78300  20.53700 -3.68800  1.000 23.77611 ? 56  HIS B CD2 1 
ATOM   1914 C  CE1 . HIS B 1 57  ? -11.02300 22.33300 -3.91600  1.000 24.11165 ? 56  HIS B CE1 1 
ATOM   1915 N  NE2 . HIS B 1 57  ? -9.89200  21.87600 -3.40500  1.000 24.59707 ? 56  HIS B NE2 1 
ATOM   1916 N  N   . TRP B 1 58  ? -14.59800 19.76800 -4.39700  1.000 22.82305 ? 57  TRP B N   1 
ATOM   1917 C  CA  . TRP B 1 58  ? -15.82400 20.37700 -4.91100  1.000 20.70789 ? 57  TRP B CA  1 
ATOM   1918 C  C   . TRP B 1 58  ? -15.86600 21.84600 -4.51900  1.000 21.09479 ? 57  TRP B C   1 
ATOM   1919 O  O   . TRP B 1 58  ? -15.27600 22.25600 -3.52200  1.000 23.04898 ? 57  TRP B O   1 
ATOM   1920 C  CB  . TRP B 1 58  ? -17.07100 19.68000 -4.36000  1.000 23.17783 ? 57  TRP B CB  1 
ATOM   1921 C  CG  . TRP B 1 58  ? -17.04500 18.21800 -4.65300  1.000 24.58221 ? 57  TRP B CG  1 
ATOM   1922 C  CD1 . TRP B 1 58  ? -17.56100 17.59700 -5.75600  1.000 28.36210 ? 57  TRP B CD1 1 
ATOM   1923 C  CD2 . TRP B 1 58  ? -16.43800 17.19100 -3.85800  1.000 22.50090 ? 57  TRP B CD2 1 
ATOM   1924 N  NE1 . TRP B 1 58  ? -17.33000 16.24000 -5.68800  1.000 29.40349 ? 57  TRP B NE1 1 
ATOM   1925 C  CE2 . TRP B 1 58  ? -16.62900 15.96800 -4.54300  1.000 23.20428 ? 57  TRP B CE2 1 
ATOM   1926 C  CE3 . TRP B 1 58  ? -15.75000 17.18100 -2.63900  1.000 22.33190 ? 57  TRP B CE3 1 
ATOM   1927 C  CZ2 . TRP B 1 58  ? -16.15800 14.75000 -4.04700  1.000 25.88401 ? 57  TRP B CZ2 1 
ATOM   1928 C  CZ3 . TRP B 1 58  ? -15.25700 15.96700 -2.15700  1.000 24.15326 ? 57  TRP B CZ3 1 
ATOM   1929 C  CH2 . TRP B 1 58  ? -15.47700 14.76600 -2.85800  1.000 26.29303 ? 57  TRP B CH2 1 
ATOM   1930 N  N   . LEU B 1 59  ? -16.63900 22.61300 -5.26500  1.000 21.66717 ? 58  LEU B N   1 
ATOM   1931 C  CA  . LEU B 1 59  ? -16.80000 24.01600 -4.90600  1.000 23.43797 ? 58  LEU B CA  1 
ATOM   1932 C  C   . LEU B 1 59  ? -18.23600 24.45200 -5.14300  1.000 25.20812 ? 58  LEU B C   1 
ATOM   1933 O  O   . LEU B 1 59  ? -19.01700 23.81400 -5.87000  1.000 24.30740 ? 58  LEU B O   1 
ATOM   1934 C  CB  . LEU B 1 59  ? -15.81600 24.89400 -5.67700  1.000 22.10852 ? 58  LEU B CB  1 
ATOM   1935 C  CG  . LEU B 1 59  ? -15.87500 24.95400 -7.21700  1.000 21.84327 ? 58  LEU B CG  1 
ATOM   1936 C  CD1 . LEU B 1 59  ? -17.01300 25.80800 -7.83800  1.000 24.66145 ? 58  LEU B CD1 1 
ATOM   1937 C  CD2 . LEU B 1 59  ? -14.51900 25.47600 -7.79800  1.000 29.32832 ? 58  LEU B CD2 1 
ATOM   1938 N  N   . ALA B 1 60  ? -18.57800 25.56900 -4.50500  1.000 23.28719 ? 59  ALA B N   1 
ATOM   1939 C  CA  . ALA B 1 60  ? -19.83000 26.26800 -4.74200  1.000 23.26341 ? 59  ALA B CA  1 
ATOM   1940 C  C   . ALA B 1 60  ? -19.55900 27.49100 -5.60200  1.000 26.25198 ? 59  ALA B C   1 
ATOM   1941 O  O   . ALA B 1 60  ? -18.61400 28.23900 -5.32800  1.000 28.43651 ? 59  ALA B O   1 
ATOM   1942 C  CB  . ALA B 1 60  ? -20.46200 26.71200 -3.41900  1.000 28.23818 ? 59  ALA B CB  1 
ATOM   1943 N  N   . GLU B 1 61  ? -20.38000 27.70000 -6.62100  1.000 28.96202 ? 60  GLU B N   1 
ATOM   1944 C  CA  . GLU B 1 61  ? -20.23200 28.86200 -7.48900  1.000 28.91339 ? 60  GLU B CA  1 
ATOM   1945 C  C   . GLU B 1 61  ? -21.50900 29.68800 -7.48300  1.000 32.10344 ? 60  GLU B C   1 
ATOM   1946 O  O   . GLU B 1 61  ? -22.60900 29.15800 -7.32900  1.000 36.09576 ? 60  GLU B O   1 
ATOM   1947 C  CB  . GLU B 1 61  ? -19.88300 28.46100 -8.93800  1.000 32.11552 ? 60  GLU B CB  1 
ATOM   1948 C  CG  . GLU B 1 61  ? -20.93400 27.62200 -9.64200  1.000 34.46180 ? 60  GLU B CG  1 
ATOM   1949 C  CD  . GLU B 1 61  ? -20.50400 27.24100 -11.04400 1.000 41.66460 ? 60  GLU B CD  1 
ATOM   1950 O  OE1 . GLU B 1 61  ? -19.30900 27.39900 -11.36600 1.000 46.84129 ? 60  GLU B OE1 1 
ATOM   1951 O  OE2 . GLU B 1 61  ? -21.35500 26.79800 -11.82800 1.000 48.64631 ? 60  GLU B OE2 1 
ATOM   1952 N  N   . ASP B 1 62  ? -21.35600 30.99900 -7.66600  1.000 34.06748 ? 61  ASP B N   1 
ATOM   1953 C  CA  . ASP B 1 62  ? -22.50400 31.89300 -7.72700  1.000 38.88800 ? 61  ASP B CA  1 
ATOM   1954 C  C   . ASP B 1 62  ? -23.12700 31.86100 -9.12800  1.000 41.18815 ? 61  ASP B C   1 
ATOM   1955 O  O   . ASP B 1 62  ? -22.72900 31.08800 -10.00600 1.000 40.75162 ? 61  ASP B O   1 
ATOM   1956 C  CB  . ASP B 1 62  ? -22.10200 33.30200 -7.26800  1.000 43.68161 ? 61  ASP B CB  1 
ATOM   1957 C  CG  . ASP B 1 62  ? -21.21200 34.06600 -8.27400  1.000 48.78740 ? 61  ASP B CG  1 
ATOM   1958 O  OD1 . ASP B 1 62  ? -21.10100 33.68300 -9.45800  1.000 46.53209 ? 61  ASP B OD1 1 
ATOM   1959 O  OD2 . ASP B 1 62  ? -20.61500 35.09200 -7.85700  1.000 52.10604 ? 61  ASP B OD2 1 
ATOM   1960 N  N   . ALA B 1 63  ? -24.11400 32.73500 -9.34700  1.000 44.12269 ? 62  ALA B N   1 
ATOM   1961 C  CA  . ALA B 1 63  ? -24.81300 32.80200 -10.62800 1.000 55.47486 ? 62  ALA B CA  1 
ATOM   1962 C  C   . ALA B 1 63  ? -23.87800 33.14700 -11.78000 1.000 57.83713 ? 62  ALA B C   1 
ATOM   1963 O  O   . ALA B 1 63  ? -24.12600 32.73600 -12.91900 1.000 61.49769 ? 62  ALA B O   1 
ATOM   1964 C  CB  . ALA B 1 63  ? -25.94200 33.82700 -10.54800 1.000 57.01188 ? 62  ALA B CB  1 
ATOM   1965 N  N   . ASP B 1 64  ? -22.81700 33.90600 -11.51400 1.000 60.71682 ? 63  ASP B N   1 
ATOM   1966 C  CA  . ASP B 1 64  ? -21.85400 34.29200 -12.53700 1.000 57.83812 ? 63  ASP B CA  1 
ATOM   1967 C  C   . ASP B 1 64  ? -20.78300 33.23900 -12.78700 1.000 51.97826 ? 63  ASP B C   1 
ATOM   1968 O  O   . ASP B 1 64  ? -19.88500 33.47700 -13.59700 1.000 52.60033 ? 63  ASP B O   1 
ATOM   1969 C  CB  . ASP B 1 64  ? -21.17800 35.61200 -12.15400 1.000 66.55340 ? 63  ASP B CB  1 
ATOM   1970 C  CG  . ASP B 1 64  ? -22.17600 36.72900 -11.90300 1.000 75.32794 ? 63  ASP B CG  1 
ATOM   1971 O  OD1 . ASP B 1 64  ? -22.33200 37.13700 -10.73300 1.000 79.14084 ? 63  ASP B OD1 1 
ATOM   1972 O  OD2 . ASP B 1 64  ? -22.81300 37.19100 -12.87300 1.000 78.96711 ? 63  ASP B OD2 1 
ATOM   1973 N  N   . GLY B 1 65  ? -20.84600 32.08800 -12.12500 1.000 41.88403 ? 64  GLY B N   1 
ATOM   1974 C  CA  . GLY B 1 65  ? -19.79000 31.11000 -12.25700 1.000 42.38702 ? 64  GLY B CA  1 
ATOM   1975 C  C   . GLY B 1 65  ? -18.58900 31.33800 -11.36900 1.000 46.01824 ? 64  GLY B C   1 
ATOM   1976 O  O   . GLY B 1 65  ? -17.59400 30.61400 -11.50200 1.000 43.48313 ? 64  GLY B O   1 
ATOM   1977 N  N   . GLN B 1 66  ? -18.64900 32.29300 -10.44600 1.000 44.38191 ? 65  GLN B N   1 
ATOM   1978 C  CA  . GLN B 1 66  ? -17.45600 32.53600 -9.63100  1.000 40.45491 ? 65  GLN B CA  1 
ATOM   1979 C  C   . GLN B 1 66  ? -17.47800 31.67000 -8.37500  1.000 37.84895 ? 65  GLN B C   1 
ATOM   1980 O  O   . GLN B 1 66  ? -18.49400 31.64200 -7.67200  1.000 36.69936 ? 65  GLN B O   1 
ATOM   1981 C  CB  . GLN B 1 66  ? -17.36600 33.99600 -9.22100  1.000 43.91037 ? 65  GLN B CB  1 
ATOM   1982 C  CG  . GLN B 1 66  ? -17.54900 34.98500 -10.37000 1.000 55.87779 ? 65  GLN B CG  1 
ATOM   1983 C  CD  . GLN B 1 66  ? -16.43100 34.92800 -11.40400 1.000 63.37103 ? 65  GLN B CD  1 
ATOM   1984 O  OE1 . GLN B 1 66  ? -15.36000 34.35500 -11.16300 1.000 58.28799 ? 65  GLN B OE1 1 
ATOM   1985 N  NE2 . GLN B 1 66  ? -16.67200 35.54600 -12.56400 1.000 68.84360 ? 65  GLN B NE2 1 
ATOM   1986 N  N   . PRO B 1 67  ? -16.38500 30.96700 -8.06600  1.000 29.36211 ? 66  PRO B N   1 
ATOM   1987 C  CA  . PRO B 1 67  ? -16.32400 30.19100 -6.81800  1.000 25.91538 ? 66  PRO B CA  1 
ATOM   1988 C  C   . PRO B 1 67  ? -16.47100 31.07300 -5.58600  1.000 27.34627 ? 66  PRO B C   1 
ATOM   1989 O  O   . PRO B 1 67  ? -15.90300 32.16900 -5.51600  1.000 27.16810 ? 66  PRO B O   1 
ATOM   1990 C  CB  . PRO B 1 67  ? -14.93300 29.54300 -6.88000  1.000 28.02562 ? 66  PRO B CB  1 
ATOM   1991 C  CG  . PRO B 1 67  ? -14.65600 29.42800 -8.34700  1.000 33.93725 ? 66  PRO B CG  1 
ATOM   1992 C  CD  . PRO B 1 67  ? -15.22500 30.69700 -8.93400  1.000 32.12072 ? 66  PRO B CD  1 
ATOM   1993 N  N   . VAL B 1 68  ? -17.28200 30.59400 -4.63500  1.000 26.05434 ? 67  VAL B N   1 
ATOM   1994 C  CA  . VAL B 1 68  ? -17.49500 31.26100 -3.35200  1.000 22.74529 ? 67  VAL B CA  1 
ATOM   1995 C  C   . VAL B 1 68  ? -17.22600 30.35400 -2.15400  1.000 25.35195 ? 67  VAL B C   1 
ATOM   1996 O  O   . VAL B 1 68  ? -17.34500 30.81000 -1.01600  1.000 25.69162 ? 67  VAL B O   1 
ATOM   1997 C  CB  . VAL B 1 68  ? -18.92400 31.83700 -3.25900  1.000 22.42411 ? 67  VAL B CB  1 
ATOM   1998 C  CG1 . VAL B 1 68  ? -19.17700 32.83000 -4.35600  1.000 25.97342 ? 67  VAL B CG1 1 
ATOM   1999 C  CG2 . VAL B 1 68  ? -19.97200 30.71900 -3.28200  1.000 26.72913 ? 67  VAL B CG2 1 
ATOM   2000 N  N   . GLY B 1 69  ? -16.89100 29.07600 -2.35600  1.000 21.70200 ? 68  GLY B N   1 
ATOM   2001 C  CA  . GLY B 1 69  ? -16.68300 28.16000 -1.24900  1.000 19.63786 ? 68  GLY B CA  1 
ATOM   2002 C  C   . GLY B 1 69  ? -16.19000 26.84600 -1.80100  1.000 19.22437 ? 68  GLY B C   1 
ATOM   2003 O  O   . GLY B 1 69  ? -16.27100 26.60800 -3.01100  1.000 21.30530 ? 68  GLY B O   1 
ATOM   2004 N  N   . PHE B 1 70  ? -15.60200 26.03000 -0.92100  1.000 21.29735 ? 69  PHE B N   1 
ATOM   2005 C  CA  . PHE B 1 70  ? -15.05900 24.76900 -1.42100  1.000 20.90477 ? 69  PHE B CA  1 
ATOM   2006 C  C   . PHE B 1 70  ? -14.92700 23.74300 -0.29900  1.000 21.74581 ? 69  PHE B C   1 
ATOM   2007 O  O   . PHE B 1 70  ? -14.91500 24.07800 0.89100   1.000 20.10303 ? 69  PHE B O   1 
ATOM   2008 C  CB  . PHE B 1 70  ? -13.69300 24.99200 -2.10700  1.000 20.26378 ? 69  PHE B CB  1 
ATOM   2009 C  CG  . PHE B 1 70  ? -12.56700 25.33200 -1.14400  1.000 20.16529 ? 69  PHE B CG  1 
ATOM   2010 C  CD1 . PHE B 1 70  ? -11.87600 24.33500 -0.46700  1.000 19.91166 ? 69  PHE B CD1 1 
ATOM   2011 C  CD2 . PHE B 1 70  ? -12.18500 26.64700 -0.94000  1.000 21.47605 ? 69  PHE B CD2 1 
ATOM   2012 C  CE1 . PHE B 1 70  ? -10.83400 24.63100 0.40500   1.000 20.50128 ? 69  PHE B CE1 1 
ATOM   2013 C  CE2 . PHE B 1 70  ? -11.14500 26.94100 -0.04600  1.000 22.17307 ? 69  PHE B CE2 1 
ATOM   2014 C  CZ  . PHE B 1 70  ? -10.47800 25.95900 0.61400   1.000 23.78621 ? 69  PHE B CZ  1 
ATOM   2015 N  N   . LEU B 1 71  ? -14.80600 22.48100 -0.71900  1.000 19.41716 ? 70  LEU B N   1 
ATOM   2016 C  CA  . LEU B 1 71  ? -14.54000 21.35400 0.17400   1.000 19.59495 ? 70  LEU B CA  1 
ATOM   2017 C  C   . LEU B 1 71  ? -13.43700 20.51100 -0.45500  1.000 20.28791 ? 70  LEU B C   1 
ATOM   2018 O  O   . LEU B 1 71  ? -13.61300 19.97100 -1.55000  1.000 19.90600 ? 70  LEU B O   1 
ATOM   2019 C  CB  . LEU B 1 71  ? -15.79000 20.50000 0.40500   1.000 19.52303 ? 70  LEU B CB  1 
ATOM   2020 C  CG  . LEU B 1 71  ? -15.69600 19.43400 1.51500   1.000 18.97995 ? 70  LEU B CG  1 
ATOM   2021 C  CD1 . LEU B 1 71  ? -17.09700 18.98300 1.91800   1.000 22.62329 ? 70  LEU B CD1 1 
ATOM   2022 C  CD2 . LEU B 1 71  ? -14.86000 18.20100 1.12300   1.000 20.46964 ? 70  LEU B CD2 1 
ATOM   2023 N  N   . ALA B 1 72  ? -12.29700 20.42200 0.22400   1.000 20.21952 ? 71  ALA B N   1 
ATOM   2024 C  CA  . ALA B 1 72  ? -11.14300 19.65300 -0.23000  1.000 20.06014 ? 71  ALA B CA  1 
ATOM   2025 C  C   . ALA B 1 72  ? -11.05800 18.38600 0.60200   1.000 20.61702 ? 71  ALA B C   1 
ATOM   2026 O  O   . ALA B 1 72  ? -10.99800 18.46600 1.83600   1.000 20.39187 ? 71  ALA B O   1 
ATOM   2027 C  CB  . ALA B 1 72  ? -9.86800  20.47400 -0.05400  1.000 19.55666 ? 71  ALA B CB  1 
ATOM   2028 N  N   . ALA B 1 73  ? -11.03200 17.22100 -0.07100  1.000 20.32194 ? 72  ALA B N   1 
ATOM   2029 C  CA  . ALA B 1 73  ? -11.00900 15.95500 0.65500   1.000 20.70783 ? 72  ALA B CA  1 
ATOM   2030 C  C   . ALA B 1 73  ? -9.94200  15.02300 0.10500   1.000 22.49893 ? 72  ALA B C   1 
ATOM   2031 O  O   . ALA B 1 73  ? -9.43200  15.20100 -1.00100  1.000 24.49419 ? 72  ALA B O   1 
ATOM   2032 C  CB  . ALA B 1 73  ? -12.36300 15.25500 0.60000   1.000 20.30077 ? 72  ALA B CB  1 
ATOM   2033 N  N   . GLU B 1 74  ? -9.57500  14.02100 0.90000   1.000 21.47432 ? 73  GLU B N   1 
ATOM   2034 C  CA  . GLU B 1 74  ? -8.49000  13.13100 0.48300   1.000 22.26895 ? 73  GLU B CA  1 
ATOM   2035 C  C   . GLU B 1 74  ? -8.80200  11.71200 0.92500   1.000 22.72749 ? 73  GLU B C   1 
ATOM   2036 O  O   . GLU B 1 74  ? -9.08700  11.48200 2.09900   1.000 25.78971 ? 73  GLU B O   1 
ATOM   2037 C  CB  . GLU B 1 74  ? -7.13700  13.56800 1.06200   1.000 28.82467 ? 73  GLU B CB  1 
ATOM   2038 C  CG  . GLU B 1 74  ? -5.99400  12.78200 0.45600   1.000 30.84110 ? 73  GLU B CG  1 
ATOM   2039 C  CD  . GLU B 1 74  ? -4.62700  13.28500 0.86700   1.000 35.54519 ? 73  GLU B CD  1 
ATOM   2040 O  OE1 . GLU B 1 74  ? -4.56000  14.13700 1.76400   1.000 38.50640 ? 73  GLU B OE1 1 
ATOM   2041 O  OE2 . GLU B 1 74  ? -3.62700  12.82000 0.29600   1.000 42.99249 ? 73  GLU B OE2 1 
ATOM   2042 N  N   . ARG B 1 75  ? -8.73500  10.75900 -0.00700  1.000 22.71691 ? 74  ARG B N   1 
ATOM   2043 C  CA  . ARG B 1 75  ? -8.89800  9.35800  0.36500   1.000 24.10946 ? 74  ARG B CA  1 
ATOM   2044 C  C   . ARG B 1 75  ? -7.63500  8.85700  1.07200   1.000 26.29671 ? 74  ARG B C   1 
ATOM   2045 O  O   . ARG B 1 75  ? -6.52500  8.93300  0.53100   1.000 28.65723 ? 74  ARG B O   1 
ATOM   2046 C  CB  . ARG B 1 75  ? -9.21700  8.53200  -0.87700  1.000 25.60960 ? 74  ARG B CB  1 
ATOM   2047 C  CG  . ARG B 1 75  ? -9.23800  7.00300  -0.69500  1.000 31.01607 ? 74  ARG B CG  1 
ATOM   2048 C  CD  . ARG B 1 75  ? -10.51400 6.54000  -0.05600  1.000 31.91227 ? 74  ARG B CD  1 
ATOM   2049 N  NE  . ARG B 1 75  ? -10.66700 5.08600  -0.06000  1.000 33.40536 ? 74  ARG B NE  1 
ATOM   2050 C  CZ  . ARG B 1 75  ? -11.43000 4.40800  -0.91600  1.000 32.52771 ? 74  ARG B CZ  1 
ATOM   2051 N  NH1 . ARG B 1 75  ? -12.13800 5.04100  -1.85800  1.000 32.27258 ? 74  ARG B NH1 1 
ATOM   2052 N  NH2 . ARG B 1 75  ? -11.50200 3.09500  -0.80300  1.000 33.07408 ? 74  ARG B NH2 1 
ATOM   2053 N  N   . CYS B 1 76  ? -7.81200  8.32900  2.28400   1.000 25.92103 ? 75  CYS B N   1 
ATOM   2054 C  CA  . CYS B 1 76  ? -6.72400  7.86100  3.13500   1.000 27.98442 ? 75  CYS B CA  1 
ATOM   2055 C  C   . CYS B 1 76  ? -7.13200  6.48000  3.62100   1.000 28.53690 ? 75  CYS B C   1 
ATOM   2056 O  O   . CYS B 1 76  ? -8.03400  6.35400  4.45300   1.000 28.68929 ? 75  CYS B O   1 
ATOM   2057 C  CB  . CYS B 1 76  ? -6.47800  8.79700  4.32100   1.000 27.27922 ? 75  CYS B CB  1 
ATOM   2058 S  SG  . CYS B 1 76  ? -6.05700  10.48600 3.90800   1.000 31.45783 ? 75  CYS B SG  1 
ATOM   2059 N  N   . ALA B 1 77  ? -6.48000  5.44800  3.09800   1.000 29.47561 ? 76  ALA B N   1 
ATOM   2060 C  CA  . ALA B 1 77  ? -6.90800  4.07300  3.35000   1.000 33.22510 ? 76  ALA B CA  1 
ATOM   2061 C  C   . ALA B 1 77  ? -8.38800  3.88900  3.01900   1.000 34.11639 ? 76  ALA B C   1 
ATOM   2062 O  O   . ALA B 1 77  ? -8.77400  4.08700  1.86600   1.000 35.24100 ? 76  ALA B O   1 
ATOM   2063 C  CB  . ALA B 1 77  ? -6.60500  3.65500  4.79600   1.000 36.43393 ? 76  ALA B CB  1 
ATOM   2064 N  N   . ASP B 1 78  ? -9.23000  3.49300  3.97700   1.000 28.48089 ? 77  ASP B N   1 
ATOM   2065 C  CA  . ASP B 1 78  ? -10.62800 3.25800  3.63600   1.000 30.95106 ? 77  ASP B CA  1 
ATOM   2066 C  C   . ASP B 1 78  ? -11.53900 4.42500  3.98600   1.000 28.94036 ? 77  ASP B C   1 
ATOM   2067 O  O   . ASP B 1 78  ? -12.76200 4.25400  4.04600   1.000 27.94062 ? 77  ASP B O   1 
ATOM   2068 C  CB  . ASP B 1 78  ? -11.15400 1.97500  4.28400   1.000 37.93184 ? 77  ASP B CB  1 
ATOM   2069 C  CG  . ASP B 1 78  ? -11.13800 2.01700  5.81200   1.000 46.76330 ? 77  ASP B CG  1 
ATOM   2070 O  OD1 . ASP B 1 78  ? -10.47600 2.89900  6.39900   1.000 40.93669 ? 77  ASP B OD1 1 
ATOM   2071 O  OD2 . ASP B 1 78  ? -11.76400 1.10200  6.41400   1.000 55.40295 ? 77  ASP B OD2 1 
ATOM   2072 N  N   . GLU B 1 79  ? -10.97900 5.60600  4.18900   1.000 23.79523 ? 78  GLU B N   1 
ATOM   2073 C  CA  . GLU B 1 79  ? -11.76900 6.74500  4.64600   1.000 23.12607 ? 78  GLU B CA  1 
ATOM   2074 C  C   . GLU B 1 79  ? -11.56800 7.94700  3.73800   1.000 24.76966 ? 78  GLU B C   1 
ATOM   2075 O  O   . GLU B 1 79  ? -10.49100 8.14000  3.17400   1.000 27.18400 ? 78  GLU B O   1 
ATOM   2076 C  CB  . GLU B 1 79  ? -11.40300 7.15000  6.06500   1.000 23.38163 ? 78  GLU B CB  1 
ATOM   2077 C  CG  . GLU B 1 79  ? -11.69300 6.06300  7.09800   1.000 25.83571 ? 78  GLU B CG  1 
ATOM   2078 C  CD  . GLU B 1 79  ? -11.28600 6.42300  8.52400   1.000 28.79044 ? 78  GLU B CD  1 
ATOM   2079 O  OE1 . GLU B 1 79  ? -10.15400 6.92400  8.73900   1.000 28.97257 ? 78  GLU B OE1 1 
ATOM   2080 O  OE2 . GLU B 1 79  ? -12.08200 6.13200  9.44200   1.000 30.03379 ? 78  GLU B OE2 1 
ATOM   2081 N  N   . LEU B 1 80  ? -12.62200 8.77600  3.61800   1.000 21.55977 ? 79  LEU B N   1 
ATOM   2082 C  CA  . LEU B 1 80  ? -12.51300 10.08300 2.95100   1.000 21.53848 ? 79  LEU B CA  1 
ATOM   2083 C  C   . LEU B 1 80  ? -12.32300 11.16500 4.01800   1.000 23.39255 ? 79  LEU B C   1 
ATOM   2084 O  O   . LEU B 1 80  ? -13.22300 11.41500 4.82500   1.000 22.72553 ? 79  LEU B O   1 
ATOM   2085 C  CB  . LEU B 1 80  ? -13.72800 10.37500 2.07600   1.000 19.73170 ? 79  LEU B CB  1 
ATOM   2086 C  CG  . LEU B 1 80  ? -13.50100 11.59300 1.15300   1.000 21.56837 ? 79  LEU B CG  1 
ATOM   2087 C  CD1 . LEU B 1 80  ? -12.47200 11.27900 0.05800   1.000 22.90353 ? 79  LEU B CD1 1 
ATOM   2088 C  CD2 . LEU B 1 80  ? -14.82900 12.07800 0.57800   1.000 23.95393 ? 79  LEU B CD2 1 
ATOM   2089 N  N   . HIS B 1 81  ? -11.12600 11.72100 4.08400   1.000 20.73700 ? 80  HIS B N   1 
ATOM   2090 C  CA  . HIS B 1 81  ? -10.82200 12.76900 5.05900   1.000 22.07574 ? 80  HIS B CA  1 
ATOM   2091 C  C   . HIS B 1 81  ? -11.20900 14.13100 4.49800   1.000 23.81567 ? 80  HIS B C   1 
ATOM   2092 O  O   . HIS B 1 81  ? -10.80300 14.48300 3.38500   1.000 22.71463 ? 80  HIS B O   1 
ATOM   2093 C  CB  . HIS B 1 81  ? -9.33300  12.77300 5.40200   1.000 22.92208 ? 80  HIS B CB  1 
ATOM   2094 C  CG  . HIS B 1 81  ? -8.98300  13.72800 6.48900   1.000 23.91260 ? 80  HIS B CG  1 
ATOM   2095 N  ND1 . HIS B 1 81  ? -9.38600  13.54400 7.79000   1.000 21.70897 ? 80  HIS B ND1 1 
ATOM   2096 C  CD2 . HIS B 1 81  ? -8.27300  14.87800 6.47200   1.000 22.29982 ? 80  HIS B CD2 1 
ATOM   2097 C  CE1 . HIS B 1 81  ? -8.92900  14.53600 8.53700   1.000 21.47372 ? 80  HIS B CE1 1 
ATOM   2098 N  NE2 . HIS B 1 81  ? -8.24900  15.36800 7.76200   1.000 23.01862 ? 80  HIS B NE2 1 
ATOM   2099 N  N   . ILE B 1 82  ? -11.94500 14.92000 5.29000   1.000 18.79270 ? 81  ILE B N   1 
ATOM   2100 C  CA  . ILE B 1 82  ? -12.32600 16.28200 4.89400   1.000 19.98533 ? 81  ILE B CA  1 
ATOM   2101 C  C   . ILE B 1 82  ? -11.24500 17.19100 5.46600   1.000 20.11010 ? 81  ILE B C   1 
ATOM   2102 O  O   . ILE B 1 82  ? -11.21000 17.46400 6.67100   1.000 22.73682 ? 81  ILE B O   1 
ATOM   2103 C  CB  . ILE B 1 82  ? -13.72800 16.65900 5.37300   1.000 21.49621 ? 81  ILE B CB  1 
ATOM   2104 C  CG1 . ILE B 1 82  ? -14.76700 15.71800 4.74100   1.000 22.00603 ? 81  ILE B CG1 1 
ATOM   2105 C  CG2 . ILE B 1 82  ? -14.04700 18.13900 5.02600   1.000 22.37328 ? 81  ILE B CG2 1 
ATOM   2106 C  CD1 . ILE B 1 82  ? -16.07300 15.68300 5.52800   1.000 27.25288 ? 81  ILE B CD1 1 
ATOM   2107 N  N   . ALA B 1 83  ? -10.33400 17.63700 4.58700   1.000 19.63554 ? 82  ALA B N   1 
ATOM   2108 C  CA  . ALA B 1 83  ? -9.20300  18.45900 4.99500   1.000 25.20094 ? 82  ALA B CA  1 
ATOM   2109 C  C   . ALA B 1 83  ? -9.60800  19.91400 5.27600   1.000 23.36750 ? 82  ALA B C   1 
ATOM   2110 O  O   . ALA B 1 83  ? -9.12100  20.52900 6.23900   1.000 24.24921 ? 82  ALA B O   1 
ATOM   2111 C  CB  . ALA B 1 83  ? -8.11500  18.41700 3.91600   1.000 22.77504 ? 82  ALA B CB  1 
ATOM   2112 N  N   . GLU B 1 84  ? -10.47700 20.47300 4.43600   1.000 22.01354 ? 83  GLU B N   1 
ATOM   2113 C  CA  . GLU B 1 84  ? -10.86300 21.87300 4.54800   1.000 22.94076 ? 83  GLU B CA  1 
ATOM   2114 C  C   . GLU B 1 84  ? -12.24100 22.07200 3.93500   1.000 22.21337 ? 83  GLU B C   1 
ATOM   2115 O  O   . GLU B 1 84  ? -12.54200 21.54900 2.86100   1.000 22.51918 ? 83  GLU B O   1 
ATOM   2116 C  CB  . GLU B 1 84  ? -9.84700  22.79000 3.85500   1.000 22.81624 ? 83  GLU B CB  1 
ATOM   2117 C  CG  . GLU B 1 84  ? -10.16000 24.27500 4.03300   1.000 22.98461 ? 83  GLU B CG  1 
ATOM   2118 C  CD  . GLU B 1 84  ? -10.27000 24.65000 5.49400   1.000 28.11388 ? 83  GLU B CD  1 
ATOM   2119 O  OE1 . GLU B 1 84  ? -9.32500  24.36600 6.27900   1.000 29.40956 ? 83  GLU B OE1 1 
ATOM   2120 O  OE2 . GLU B 1 84  ? -11.30400 25.25900 5.86100   1.000 30.74393 ? 83  GLU B OE2 1 
ATOM   2121 N  N   . LEU B 1 85  ? -13.07600 22.83400 4.63700   1.000 21.51454 ? 84  LEU B N   1 
ATOM   2122 C  CA  . LEU B 1 85  ? -14.38300 23.25700 4.15300   1.000 20.35402 ? 84  LEU B CA  1 
ATOM   2123 C  C   . LEU B 1 85  ? -14.49700 24.74400 4.48600   1.000 21.02200 ? 84  LEU B C   1 
ATOM   2124 O  O   . LEU B 1 85  ? -14.46000 25.11600 5.66200   1.000 22.07425 ? 84  LEU B O   1 
ATOM   2125 C  CB  . LEU B 1 85  ? -15.50900 22.43300 4.81900   1.000 18.40047 ? 84  LEU B CB  1 
ATOM   2126 C  CG  . LEU B 1 85  ? -16.94600 22.95800 4.64200   1.000 21.09154 ? 84  LEU B CG  1 
ATOM   2127 C  CD1 . LEU B 1 85  ? -17.41600 22.88000 3.21100   1.000 21.62969 ? 84  LEU B CD1 1 
ATOM   2128 C  CD2 . LEU B 1 85  ? -17.89700 22.22000 5.58400   1.000 23.28463 ? 84  LEU B CD2 1 
ATOM   2129 N  N   . SER B 1 86  ? -14.63500 25.58500 3.44900   1.000 18.98605 ? 85  SER B N   1 
ATOM   2130 C  CA  . SER B 1 86  ? -14.62300 27.02900 3.65500   1.000 21.29973 ? 85  SER B CA  1 
ATOM   2131 C  C   . SER B 1 86  ? -15.59100 27.73100 2.71100   1.000 22.51867 ? 85  SER B C   1 
ATOM   2132 O  O   . SER B 1 86  ? -15.59600 27.43100 1.51000   1.000 22.53882 ? 85  SER B O   1 
ATOM   2133 C  CB  . SER B 1 86  ? -13.20400 27.58200 3.44000   1.000 27.29063 ? 85  SER B CB  1 
ATOM   2134 O  OG  . SER B 1 86  ? -12.38800 27.48100 4.60700   1.000 28.27707 ? 85  SER B OG  1 
ATOM   2135 N  N   . ILE B 1 87  ? -16.39900 28.65700 3.25200   1.000 20.63387 ? 86  ILE B N   1 
ATOM   2136 C  CA  . ILE B 1 87  ? -17.29600 29.50500 2.45800   1.000 22.84994 ? 86  ILE B CA  1 
ATOM   2137 C  C   . ILE B 1 87  ? -16.93300 30.96800 2.74100   1.000 22.02069 ? 86  ILE B C   1 
ATOM   2138 O  O   . ILE B 1 87  ? -16.82800 31.36500 3.91100   1.000 24.40169 ? 86  ILE B O   1 
ATOM   2139 C  CB  . ILE B 1 87  ? -18.78600 29.24000 2.77900   1.000 23.21912 ? 86  ILE B CB  1 
ATOM   2140 C  CG1 . ILE B 1 87  ? -19.19900 27.76700 2.55900   1.000 26.75016 ? 86  ILE B CG1 1 
ATOM   2141 C  CG2 . ILE B 1 87  ? -19.68900 30.24200 1.99700   1.000 22.63900 ? 86  ILE B CG2 1 
ATOM   2142 C  CD1 . ILE B 1 87  ? -19.14700 27.24500 1.13100   1.000 31.01089 ? 86  ILE B CD1 1 
ATOM   2143 N  N   . ALA B 1 88  ? -16.75500 31.77200 1.68000   1.000 23.84569 ? 87  ALA B N   1 
ATOM   2144 C  CA  . ALA B 1 88  ? -16.45000 33.20100 1.81500   1.000 24.73450 ? 87  ALA B CA  1 
ATOM   2145 C  C   . ALA B 1 88  ? -17.55900 33.97600 2.54600   1.000 25.49682 ? 87  ALA B C   1 
ATOM   2146 O  O   . ALA B 1 88  ? -18.73700 33.60800 2.51300   1.000 26.37409 ? 87  ALA B O   1 
ATOM   2147 C  CB  . ALA B 1 88  ? -16.22300 33.82700 0.42900   1.000 28.53166 ? 87  ALA B CB  1 
ATOM   2148 N  N   . GLN B 1 89  ? -17.15800 35.06500 3.21200   1.000 28.79746 ? 88  GLN B N   1 
ATOM   2149 C  CA  . GLN B 1 89  ? -18.05300 35.82100 4.09500   1.000 30.87079 ? 88  GLN B CA  1 
ATOM   2150 C  C   . GLN B 1 89  ? -19.37700 36.19100 3.44300   1.000 32.82901 ? 88  GLN B C   1 
ATOM   2151 O  O   . GLN B 1 89  ? -20.44200 36.02300 4.04400   1.000 34.75431 ? 88  GLN B O   1 
ATOM   2152 C  CB  . GLN B 1 89  ? -17.36400 37.09900 4.57800   1.000 33.73974 ? 88  GLN B CB  1 
ATOM   2153 C  CG  . GLN B 1 89  ? -16.30400 36.82200 5.61700   1.000 35.24231 ? 88  GLN B CG  1 
ATOM   2154 C  CD  . GLN B 1 89  ? -16.83400 35.95600 6.74300   1.000 33.06074 ? 88  GLN B CD  1 
ATOM   2155 O  OE1 . GLN B 1 89  ? -17.89300 36.23100 7.30900   1.000 40.30006 ? 88  GLN B OE1 1 
ATOM   2156 N  NE2 . GLN B 1 89  ? -16.08000 34.93800 7.10100   1.000 31.27414 ? 88  GLN B NE2 1 
ATOM   2157 N  N   . ALA B 1 90  ? -19.33700 36.72900 2.22900   1.000 32.99554 ? 89  ALA B N   1 
ATOM   2158 C  CA  . ALA B 1 90  ? -20.57100 37.24100 1.64500   1.000 32.54068 ? 89  ALA B CA  1 
ATOM   2159 C  C   . ALA B 1 90  ? -21.58000 36.14500 1.30600   1.000 34.29418 ? 89  ALA B C   1 
ATOM   2160 O  O   . ALA B 1 90  ? -22.73300 36.47300 0.97600   1.000 37.86928 ? 89  ALA B O   1 
ATOM   2161 C  CB  . ALA B 1 90  ? -20.25400 38.07100 0.39800   1.000 34.75184 ? 89  ALA B CB  1 
ATOM   2162 N  N   . HIS B 1 91  ? -21.19700 34.86500 1.41500   1.000 31.94971 ? 90  HIS B N   1 
ATOM   2163 C  CA  . HIS B 1 91  ? -22.04800 33.76600 0.99200   1.000 30.88640 ? 90  HIS B CA  1 
ATOM   2164 C  C   . HIS B 1 91  ? -22.27800 32.73100 2.09000   1.000 29.49198 ? 90  HIS B C   1 
ATOM   2165 O  O   . HIS B 1 91  ? -22.87300 31.68100 1.82400   1.000 28.94094 ? 90  HIS B O   1 
ATOM   2166 C  CB  . HIS B 1 91  ? -21.44400 33.13000 -0.26900  1.000 28.97319 ? 90  HIS B CB  1 
ATOM   2167 C  CG  . HIS B 1 91  ? -21.18900 34.15600 -1.33900  1.000 27.28985 ? 90  HIS B CG  1 
ATOM   2168 N  ND1 . HIS B 1 91  ? -22.19700 34.64600 -2.14500  1.000 30.39536 ? 90  HIS B ND1 1 
ATOM   2169 C  CD2 . HIS B 1 91  ? -20.06700 34.83100 -1.68100  1.000 29.95528 ? 90  HIS B CD2 1 
ATOM   2170 C  CE1 . HIS B 1 91  ? -21.69700 35.56300 -2.95500  1.000 30.56093 ? 90  HIS B CE1 1 
ATOM   2171 N  NE2 . HIS B 1 91  ? -20.40300 35.68100 -2.70700  1.000 30.28055 ? 90  HIS B NE2 1 
ATOM   2172 N  N   . GLN B 1 92  ? -21.88700 33.02200 3.32400   1.000 31.01944 ? 91  GLN B N   1 
ATOM   2173 C  CA  . GLN B 1 92  ? -22.15200 32.11800 4.43500   1.000 32.66447 ? 91  GLN B CA  1 
ATOM   2174 C  C   . GLN B 1 92  ? -23.64000 32.10500 4.79000   1.000 32.91392 ? 91  GLN B C   1 
ATOM   2175 O  O   . GLN B 1 92  ? -24.39000 33.02800 4.46800   1.000 33.20245 ? 91  GLN B O   1 
ATOM   2176 C  CB  . GLN B 1 92  ? -21.33500 32.54000 5.65600   1.000 31.53410 ? 91  GLN B CB  1 
ATOM   2177 C  CG  . GLN B 1 92  ? -19.87500 32.15700 5.50200   1.000 28.66510 ? 91  GLN B CG  1 
ATOM   2178 C  CD  . GLN B 1 92  ? -19.04000 32.51500 6.70400   1.000 25.90559 ? 91  GLN B CD  1 
ATOM   2179 O  OE1 . GLN B 1 92  ? -19.48000 33.28600 7.57700   1.000 28.40387 ? 91  GLN B OE1 1 
ATOM   2180 N  NE2 . GLN B 1 92  ? -17.81000 31.97300 6.74400   1.000 25.88164 ? 91  GLN B NE2 1 
ATOM   2181 N  N   . GLN B 1 93  ? -24.05200 31.02500 5.46400   1.000 31.96010 ? 92  GLN B N   1 
ATOM   2182 C  CA  . GLN B 1 93  ? -25.41100 30.87000 5.99900   1.000 35.84979 ? 92  GLN B CA  1 
ATOM   2183 C  C   . GLN B 1 93  ? -26.47300 30.93500 4.90600   1.000 35.19383 ? 92  GLN B C   1 
ATOM   2184 O  O   . GLN B 1 93  ? -27.60400 31.37900 5.13600   1.000 36.20313 ? 92  GLN B O   1 
ATOM   2185 C  CB  . GLN B 1 93  ? -25.66900 31.86300 7.13100   1.000 39.74834 ? 92  GLN B CB  1 
ATOM   2186 C  CG  . GLN B 1 93  ? -24.92200 31.41400 8.38700   1.000 40.09732 ? 92  GLN B CG  1 
ATOM   2187 C  CD  . GLN B 1 93  ? -25.29900 32.17500 9.64000   1.000 50.13536 ? 92  GLN B CD  1 
ATOM   2188 O  OE1 . GLN B 1 93  ? -26.36600 31.96300 10.22200  1.000 59.03904 ? 92  GLN B OE1 1 
ATOM   2189 N  NE2 . GLN B 1 93  ? -24.41600 33.06200 10.07300  1.000 56.10684 ? 92  GLN B NE2 1 
ATOM   2190 N  N   . GLN B 1 94  ? -26.11200 30.42800 3.72700   1.000 32.42509 ? 93  GLN B N   1 
ATOM   2191 C  CA  . GLN B 1 94  ? -27.01400 30.20500 2.60400   1.000 33.10996 ? 93  GLN B CA  1 
ATOM   2192 C  C   . GLN B 1 94  ? -27.20300 28.72400 2.31500   1.000 31.39118 ? 93  GLN B C   1 
ATOM   2193 O  O   . GLN B 1 94  ? -27.72200 28.38000 1.24700   1.000 34.21257 ? 93  GLN B O   1 
ATOM   2194 C  CB  . GLN B 1 94  ? -26.48300 30.88400 1.33700   1.000 36.06574 ? 93  GLN B CB  1 
ATOM   2195 C  CG  . GLN B 1 94  ? -26.10900 32.36100 1.48700   1.000 34.06822 ? 93  GLN B CG  1 
ATOM   2196 C  CD  . GLN B 1 94  ? -27.23700 33.28800 1.13300   1.000 47.37211 ? 93  GLN B CD  1 
ATOM   2197 O  OE1 . GLN B 1 94  ? -28.20900 32.88000 0.51700   1.000 49.98862 ? 93  GLN B OE1 1 
ATOM   2198 N  NE2 . GLN B 1 94  ? -27.10800 34.55000 1.50900   1.000 51.32125 ? 93  GLN B NE2 1 
ATOM   2199 N  N   . GLY B 1 95  ? -26.75200 27.84400 3.21500   1.000 28.40215 ? 94  GLY B N   1 
ATOM   2200 C  CA  . GLY B 1 95  ? -26.85900 26.40200 3.04700   1.000 29.66798 ? 94  GLY B CA  1 
ATOM   2201 C  C   . GLY B 1 95  ? -25.78900 25.76000 2.20000   1.000 30.78839 ? 94  GLY B C   1 
ATOM   2202 O  O   . GLY B 1 95  ? -25.87000 24.55600 1.91100   1.000 28.23699 ? 94  GLY B O   1 
ATOM   2203 N  N   . LEU B 1 96  ? -24.77400 26.51500 1.79200   1.000 26.30095 ? 95  LEU B N   1 
ATOM   2204 C  CA  . LEU B 1 96  ? -23.79000 25.95800 0.87300   1.000 23.73780 ? 95  LEU B CA  1 
ATOM   2205 C  C   . LEU B 1 96  ? -22.85900 24.96200 1.54700   1.000 24.13970 ? 95  LEU B C   1 
ATOM   2206 O  O   . LEU B 1 96  ? -22.37500 24.03900 0.88600   1.000 24.43805 ? 95  LEU B O   1 
ATOM   2207 C  CB  . LEU B 1 96  ? -22.97900 27.08700 0.23200   1.000 25.77912 ? 95  LEU B CB  1 
ATOM   2208 C  CG  . LEU B 1 96  ? -23.82800 28.08600 -0.55900  1.000 27.14066 ? 95  LEU B CG  1 
ATOM   2209 C  CD1 . LEU B 1 96  ? -22.91000 29.21000 -1.05200  1.000 26.07803 ? 95  LEU B CD1 1 
ATOM   2210 C  CD2 . LEU B 1 96  ? -24.56400 27.39100 -1.71900  1.000 26.76450 ? 95  LEU B CD2 1 
ATOM   2211 N  N   . GLY B 1 97  ? -22.56200 25.14200 2.83700   1.000 25.26384 ? 96  GLY B N   1 
ATOM   2212 C  CA  . GLY B 1 97  ? -21.69000 24.18700 3.50700   1.000 22.01316 ? 96  GLY B CA  1 
ATOM   2213 C  C   . GLY B 1 97  ? -22.32300 22.80900 3.54600   1.000 21.42724 ? 96  GLY B C   1 
ATOM   2214 O  O   . GLY B 1 97  ? -21.65400 21.80000 3.28900   1.000 23.76556 ? 96  GLY B O   1 
ATOM   2215 N  N   A ARG B 1 98  ? -23.62500 22.77600 3.77700   0.610 22.38999 ? 97  ARG B N   1 
ATOM   2216 N  N   B ARG B 1 98  ? -23.63000 22.77200 3.77100   0.390 22.94875 ? 97  ARG B N   1 
ATOM   2217 C  CA  A ARG B 1 98  ? -24.35700 21.52500 3.83100   0.610 26.23444 ? 97  ARG B CA  1 
ATOM   2218 C  CA  B ARG B 1 98  ? -24.35200 21.51100 3.82600   0.390 25.84028 ? 97  ARG B CA  1 
ATOM   2219 C  C   A ARG B 1 98  ? -24.39700 20.86300 2.45800   0.610 27.38688 ? 97  ARG B C   1 
ATOM   2220 C  C   B ARG B 1 98  ? -24.38200 20.85800 2.45200   0.390 26.81050 ? 97  ARG B C   1 
ATOM   2221 O  O   A ARG B 1 98  ? -24.18200 19.66200 2.34000   0.610 25.31649 ? 97  ARG B O   1 
ATOM   2222 O  O   B ARG B 1 98  ? -24.18400 19.65300 2.33000   0.390 25.32487 ? 97  ARG B O   1 
ATOM   2223 C  CB  A ARG B 1 98  ? -25.77000 21.77500 4.35300   0.610 28.10023 ? 97  ARG B CB  1 
ATOM   2224 C  CB  B ARG B 1 98  ? -25.77700 21.72600 4.33300   0.390 28.10012 ? 97  ARG B CB  1 
ATOM   2225 C  CG  A ARG B 1 98  ? -26.70000 20.58600 4.24800   0.610 28.93112 ? 97  ARG B CG  1 
ATOM   2226 C  CG  B ARG B 1 98  ? -26.43400 20.47600 4.89200   0.390 29.91529 ? 97  ARG B CG  1 
ATOM   2227 C  CD  A ARG B 1 98  ? -26.36900 19.51600 5.26700   0.610 29.28686 ? 97  ARG B CD  1 
ATOM   2228 C  CD  B ARG B 1 98  ? -27.86800 20.75900 5.30800   0.390 30.28847 ? 97  ARG B CD  1 
ATOM   2229 N  NE  A ARG B 1 98  ? -27.42900 18.51800 5.33100   0.610 35.40456 ? 97  ARG B NE  1 
ATOM   2230 N  NE  B ARG B 1 98  ? -28.22800 20.06500 6.54000   0.390 41.02900 ? 97  ARG B NE  1 
ATOM   2231 C  CZ  A ARG B 1 98  ? -28.40900 18.52600 6.22800   0.610 37.49782 ? 97  ARG B CZ  1 
ATOM   2232 C  CZ  B ARG B 1 98  ? -28.00300 20.55500 7.75400   0.390 42.76477 ? 97  ARG B CZ  1 
ATOM   2233 N  NH1 A ARG B 1 98  ? -28.45900 19.47500 7.15200   0.610 36.22415 ? 97  ARG B NH1 1 
ATOM   2234 N  NH1 B ARG B 1 98  ? -27.41700 21.73400 7.89200   0.390 46.34163 ? 97  ARG B NH1 1 
ATOM   2235 N  NH2 A ARG B 1 98  ? -29.33600 17.58100 6.20500   0.610 34.18854 ? 97  ARG B NH2 1 
ATOM   2236 N  NH2 B ARG B 1 98  ? -28.36000 19.86700 8.82800   0.390 42.00573 ? 97  ARG B NH2 1 
ATOM   2237 N  N   . ARG B 1 99  ? -24.53200 21.66900 1.41100   1.000 25.15149 ? 98  ARG B N   1 
ATOM   2238 C  CA  . ARG B 1 99  ? -24.57300 21.12300 0.05800   1.000 21.93287 ? 98  ARG B CA  1 
ATOM   2239 C  C   . ARG B 1 99  ? -23.22000 20.56300 -0.37200  1.000 25.05492 ? 98  ARG B C   1 
ATOM   2240 O  O   . ARG B 1 99  ? -23.17300 19.55300 -1.09800  1.000 24.33283 ? 98  ARG B O   1 
ATOM   2241 C  CB  . ARG B 1 99  ? -25.08400 22.18200 -0.92200  1.000 25.97890 ? 98  ARG B CB  1 
ATOM   2242 C  CG  . ARG B 1 99  ? -26.55300 22.52600 -0.66600  1.000 26.08720 ? 98  ARG B CG  1 
ATOM   2243 C  CD  . ARG B 1 99  ? -27.04500 23.79200 -1.35000  1.000 30.82926 ? 98  ARG B CD  1 
ATOM   2244 N  NE  . ARG B 1 99  ? -27.04000 23.69500 -2.80800  1.000 35.24548 ? 98  ARG B NE  1 
ATOM   2245 C  CZ  . ARG B 1 99  ? -27.44700 24.66800 -3.62800  1.000 28.85788 ? 98  ARG B CZ  1 
ATOM   2246 N  NH1 . ARG B 1 99  ? -27.91500 25.83300 -3.16500  1.000 30.97282 ? 98  ARG B NH1 1 
ATOM   2247 N  NH2 . ARG B 1 99  ? -27.39300 24.46900 -4.93900  1.000 35.15257 ? 98  ARG B NH2 1 
ATOM   2248 N  N   . LEU B 1 100 ? -22.11300 21.18700 0.06400   1.000 20.49412 ? 99  LEU B N   1 
ATOM   2249 C  CA  . LEU B 1 100 ? -20.78600 20.65200 -0.21000  1.000 19.06407 ? 99  LEU B CA  1 
ATOM   2250 C  C   . LEU B 1 100 ? -20.55700 19.34400 0.53100   1.000 20.72391 ? 99  LEU B C   1 
ATOM   2251 O  O   . LEU B 1 100 ? -20.00800 18.39100 -0.04500  1.000 21.50996 ? 99  LEU B O   1 
ATOM   2252 C  CB  . LEU B 1 100 ? -19.69900 21.67800 0.16800   1.000 19.60833 ? 99  LEU B CB  1 
ATOM   2253 C  CG  . LEU B 1 100 ? -19.58400 22.81500 -0.84400  1.000 18.62288 ? 99  LEU B CG  1 
ATOM   2254 C  CD1 . LEU B 1 100 ? -18.76100 23.95800 -0.20500  1.000 21.88246 ? 99  LEU B CD1 1 
ATOM   2255 C  CD2 . LEU B 1 100 ? -18.89600 22.33800 -2.08800  1.000 24.53795 ? 99  LEU B CD2 1 
ATOM   2256 N  N   . LEU B 1 101 ? -20.95000 19.28900 1.80500   1.000 20.23834 ? 100 LEU B N   1 
ATOM   2257 C  CA  . LEU B 1 101 ? -20.78700 18.05600 2.57300   1.000 21.72989 ? 100 LEU B CA  1 
ATOM   2258 C  C   . LEU B 1 101 ? -21.58600 16.92600 1.94800   1.000 22.40260 ? 100 LEU B C   1 
ATOM   2259 O  O   . LEU B 1 101 ? -21.12300 15.77300 1.93000   1.000 21.47328 ? 100 LEU B O   1 
ATOM   2260 C  CB  . LEU B 1 101 ? -21.21900 18.27800 4.01200   1.000 19.92885 ? 100 LEU B CB  1 
ATOM   2261 C  CG  . LEU B 1 101 ? -20.18600 19.03100 4.84800   1.000 21.50360 ? 100 LEU B CG  1 
ATOM   2262 C  CD1 . LEU B 1 101 ? -20.80200 19.73100 6.06600   1.000 27.26713 ? 100 LEU B CD1 1 
ATOM   2263 C  CD2 . LEU B 1 101 ? -19.02500 18.11300 5.27500   1.000 24.96056 ? 100 LEU B CD2 1 
ATOM   2264 N  N   . GLU B 1 102 ? -22.76900 17.23200 1.42500   1.000 22.23142 ? 101 GLU B N   1 
ATOM   2265 C  CA  . GLU B 1 102 ? -23.57800 16.19400 0.79000   1.000 22.99856 ? 101 GLU B CA  1 
ATOM   2266 C  C   . GLU B 1 102 ? -22.85900 15.61000 -0.41700  1.000 23.11756 ? 101 GLU B C   1 
ATOM   2267 O  O   . GLU B 1 102 ? -22.89800 14.38600 -0.64500  1.000 23.39784 ? 101 GLU B O   1 
ATOM   2268 C  CB  . GLU B 1 102 ? -24.94500 16.75100 0.40500   1.000 29.09596 ? 101 GLU B CB  1 
ATOM   2269 C  CG  . GLU B 1 102 ? -25.79300 16.98000 1.64400   1.000 40.59647 ? 101 GLU B CG  1 
ATOM   2270 C  CD  . GLU B 1 102 ? -27.23000 17.31400 1.35700   1.000 52.59460 ? 101 GLU B CD  1 
ATOM   2271 O  OE1 . GLU B 1 102 ? -28.06400 17.06200 2.26200   1.000 60.53127 ? 101 GLU B OE1 1 
ATOM   2272 O  OE2 . GLU B 1 102 ? -27.52600 17.82600 0.24900   1.000 52.06315 ? 101 GLU B OE2 1 
ATOM   2273 N  N   . ARG B 1 103 ? -22.14900 16.44600 -1.17400  1.000 20.78105 ? 102 ARG B N   1 
ATOM   2274 C  CA  A ARG B 1 103 ? -21.43000 15.94100 -2.33900  0.290 20.58637 ? 102 ARG B CA  1 
ATOM   2275 C  CA  B ARG B 1 103 ? -21.43800 15.93000 -2.34200  0.710 18.81603 ? 102 ARG B CA  1 
ATOM   2276 C  C   . ARG B 1 103 ? -20.27700 15.03700 -1.91800  1.000 21.32978 ? 102 ARG B C   1 
ATOM   2277 O  O   . ARG B 1 103 ? -20.01600 14.00000 -2.56500  1.000 21.87174 ? 102 ARG B O   1 
ATOM   2278 C  CB  A ARG B 1 103 ? -20.93000 17.11400 -3.18600  0.290 24.65986 ? 102 ARG B CB  1 
ATOM   2279 C  CB  B ARG B 1 103 ? -20.95800 17.09500 -3.22200  0.710 23.99012 ? 102 ARG B CB  1 
ATOM   2280 C  CG  A ARG B 1 103 ? -20.50000 16.75200 -4.58700  0.290 30.45412 ? 102 ARG B CG  1 
ATOM   2281 C  CG  B ARG B 1 103 ? -20.67000 16.76100 -4.67700  0.710 33.73798 ? 102 ARG B CG  1 
ATOM   2282 C  CD  A ARG B 1 103 ? -21.68300 16.36300 -5.48000  0.290 35.41154 ? 102 ARG B CD  1 
ATOM   2283 C  CD  B ARG B 1 103 ? -21.93100 16.28900 -5.46100  0.710 32.04543 ? 102 ARG B CD  1 
ATOM   2284 N  NE  A ARG B 1 103 ? -21.23900 16.10200 -6.84500  0.290 42.69226 ? 102 ARG B NE  1 
ATOM   2285 N  NE  B ARG B 1 103 ? -22.95900 17.32500 -5.55300  0.710 39.68107 ? 102 ARG B NE  1 
ATOM   2286 C  CZ  A ARG B 1 103 ? -21.30800 16.98500 -7.83600  0.290 44.03880 ? 102 ARG B CZ  1 
ATOM   2287 C  CZ  B ARG B 1 103 ? -23.09300 18.15700 -6.58300  0.710 42.52642 ? 102 ARG B CZ  1 
ATOM   2288 N  NH1 A ARG B 1 103 ? -20.87400 16.66400 -9.04700  0.290 48.92979 ? 102 ARG B NH1 1 
ATOM   2289 N  NH1 B ARG B 1 103 ? -22.26500 18.06600 -7.61900  0.710 38.04674 ? 102 ARG B NH1 1 
ATOM   2290 N  NH2 A ARG B 1 103 ? -21.82100 18.18600 -7.61900  0.290 41.36401 ? 102 ARG B NH2 1 
ATOM   2291 N  NH2 B ARG B 1 103 ? -24.06200 19.06800 -6.58600  0.710 38.78343 ? 102 ARG B NH2 1 
ATOM   2292 N  N   . ALA B 1 104 ? -19.58300 15.40400 -0.82400  1.000 21.65340 ? 103 ALA B N   1 
ATOM   2293 C  CA  . ALA B 1 104 ? -18.47200 14.58800 -0.33100  1.000 19.19686 ? 103 ALA B CA  1 
ATOM   2294 C  C   . ALA B 1 104 ? -18.96300 13.23800 0.18300   1.000 21.08897 ? 103 ALA B C   1 
ATOM   2295 O  O   . ALA B 1 104 ? -18.32400 12.21000 -0.08400  1.000 20.29933 ? 103 ALA B O   1 
ATOM   2296 C  CB  . ALA B 1 104 ? -17.70000 15.32900 0.77000   1.000 21.14027 ? 103 ALA B CB  1 
ATOM   2297 N  N   . VAL B 1 105 ? -20.08600 13.22200 0.91300   1.000 21.84859 ? 104 VAL B N   1 
ATOM   2298 C  CA  . VAL B 1 105 ? -20.62500 11.96500 1.41000   1.000 20.86109 ? 104 VAL B CA  1 
ATOM   2299 C  C   . VAL B 1 105 ? -21.08200 11.07400 0.25300   1.000 21.04538 ? 104 VAL B C   1 
ATOM   2300 O  O   . VAL B 1 105 ? -20.86600 9.84300  0.28000   1.000 21.62046 ? 104 VAL B O   1 
ATOM   2301 C  CB  . VAL B 1 105 ? -21.74100 12.20200 2.43900   1.000 21.50590 ? 104 VAL B CB  1 
ATOM   2302 C  CG1 . VAL B 1 105 ? -22.31000 10.87600 2.93700   1.000 21.81621 ? 104 VAL B CG1 1 
ATOM   2303 C  CG2 . VAL B 1 105 ? -21.18200 12.94600 3.67700   1.000 24.23116 ? 104 VAL B CG2 1 
ATOM   2304 N  N   . THR B 1 106 ? -21.71600 11.65500 -0.78100  1.000 21.47499 ? 105 THR B N   1 
ATOM   2305 C  CA  . THR B 1 106 ? -22.12000 10.87100 -1.95800  1.000 20.18541 ? 105 THR B CA  1 
ATOM   2306 C  C   . THR B 1 106 ? -20.91400 10.22800 -2.62300  1.000 20.55743 ? 105 THR B C   1 
ATOM   2307 O  O   . THR B 1 106 ? -20.96100 9.04400  -2.99900  1.000 22.17552 ? 105 THR B O   1 
ATOM   2308 C  CB  . THR B 1 106 ? -22.87300 11.78500 -2.94300  1.000 22.54590 ? 105 THR B CB  1 
ATOM   2309 O  OG1 . THR B 1 106 ? -24.12400 12.15500 -2.36800  1.000 21.38061 ? 105 THR B OG1 1 
ATOM   2310 C  CG2 . THR B 1 106 ? -23.10700 11.15200 -4.30400  1.000 24.98499 ? 105 THR B CG2 1 
ATOM   2311 N  N   . TYR B 1 107 ? -19.83200 10.99400 -2.75500  1.000 21.79651 ? 106 TYR B N   1 
ATOM   2312 C  CA  . TYR B 1 107 ? -18.59200 10.52100 -3.36600  1.000 19.97191 ? 106 TYR B CA  1 
ATOM   2313 C  C   . TYR B 1 107 ? -17.94400 9.44200  -2.51200  1.000 21.68062 ? 106 TYR B C   1 
ATOM   2314 O  O   . TYR B 1 107 ? -17.44700 8.44100  -3.05000  1.000 23.26890 ? 106 TYR B O   1 
ATOM   2315 C  CB  . TYR B 1 107 ? -17.62400 11.70100 -3.54900  1.000 22.16563 ? 106 TYR B CB  1 
ATOM   2316 C  CG  . TYR B 1 107 ? -16.28900 11.33800 -4.17000  1.000 22.96609 ? 106 TYR B CG  1 
ATOM   2317 C  CD1 . TYR B 1 107 ? -16.12200 11.28900 -5.54600  1.000 27.35727 ? 106 TYR B CD1 1 
ATOM   2318 C  CD2 . TYR B 1 107 ? -15.18800 11.05400 -3.36200  1.000 24.57153 ? 106 TYR B CD2 1 
ATOM   2319 C  CE1 . TYR B 1 107 ? -14.89200 10.94700 -6.10500  1.000 36.74423 ? 106 TYR B CE1 1 
ATOM   2320 C  CE2 . TYR B 1 107 ? -13.95400 10.70400 -3.91500  1.000 27.12356 ? 106 TYR B CE2 1 
ATOM   2321 C  CZ  . TYR B 1 107 ? -13.81800 10.66700 -5.27600  1.000 32.86258 ? 106 TYR B CZ  1 
ATOM   2322 O  OH  . TYR B 1 107 ? -12.60800 10.34600 -5.82400  1.000 35.79326 ? 106 TYR B OH  1 
ATOM   2323 N  N   . ALA B 1 108 ? -17.93800 9.63200  -1.18900  1.000 21.15191 ? 107 ALA B N   1 
ATOM   2324 C  CA  . ALA B 1 108 ? -17.37900 8.60600  -0.30700  1.000 24.30267 ? 107 ALA B CA  1 
ATOM   2325 C  C   . ALA B 1 108 ? -18.12000 7.28500  -0.47100  1.000 23.26375 ? 107 ALA B C   1 
ATOM   2326 O  O   . ALA B 1 108 ? -17.49600 6.21500  -0.59600  1.000 24.99364 ? 107 ALA B O   1 
ATOM   2327 C  CB  . ALA B 1 108 ? -17.44700 9.07100  1.14100   1.000 24.19500 ? 107 ALA B CB  1 
ATOM   2328 N  N   . HIS B 1 109 ? -19.45400 7.33800  -0.47700  1.000 25.08007 ? 108 HIS B N   1 
ATOM   2329 C  CA  . HIS B 1 109 ? -20.23800 6.11800  -0.62200  1.000 24.55600 ? 108 HIS B CA  1 
ATOM   2330 C  C   . HIS B 1 109 ? -20.01200 5.46900  -1.98400  1.000 24.57303 ? 108 HIS B C   1 
ATOM   2331 O  O   . HIS B 1 109 ? -19.82400 4.23800  -2.07500  1.000 27.64333 ? 108 HIS B O   1 
ATOM   2332 C  CB  . HIS B 1 109 ? -21.71900 6.42300  -0.39600  1.000 26.31331 ? 108 HIS B CB  1 
ATOM   2333 C  CG  . HIS B 1 109 ? -22.58800 5.20800  -0.41200  1.000 27.84089 ? 108 HIS B CG  1 
ATOM   2334 N  ND1 . HIS B 1 109 ? -22.84600 4.46400  0.72000   1.000 32.34630 ? 108 HIS B ND1 1 
ATOM   2335 C  CD2 . HIS B 1 109 ? -23.22500 4.59000  -1.42900  1.000 29.13834 ? 108 HIS B CD2 1 
ATOM   2336 C  CE1 . HIS B 1 109 ? -23.62000 3.43900  0.40000   1.000 36.89955 ? 108 HIS B CE1 1 
ATOM   2337 N  NE2 . HIS B 1 109 ? -23.85800 3.48700  -0.90100  1.000 38.02852 ? 108 HIS B NE2 1 
ATOM   2338 N  N   . ALA B 1 110 ? -19.98700 6.28000  -3.05300  1.000 24.60836 ? 109 ALA B N   1 
ATOM   2339 C  CA  . ALA B 1 110 ? -19.85200 5.71500  -4.39400  1.000 27.00959 ? 109 ALA B CA  1 
ATOM   2340 C  C   . ALA B 1 110 ? -18.47200 5.12100  -4.62600  1.000 26.59110 ? 109 ALA B C   1 
ATOM   2341 O  O   . ALA B 1 110 ? -18.33700 4.21400  -5.46900  1.000 29.70080 ? 109 ALA B O   1 
ATOM   2342 C  CB  . ALA B 1 110 ? -20.15400 6.76800  -5.47600  1.000 28.96273 ? 109 ALA B CB  1 
ATOM   2343 N  N   . SER B 1 111 ? -17.45500 5.59500  -3.89100  1.000 24.48008 ? 110 SER B N   1 
ATOM   2344 C  CA  . SER B 1 111 ? -16.09900 5.05400  -3.99800  1.000 26.29069 ? 110 SER B CA  1 
ATOM   2345 C  C   . SER B 1 111 ? -15.78000 4.02900  -2.90600  1.000 27.27029 ? 110 SER B C   1 
ATOM   2346 O  O   . SER B 1 111 ? -14.60900 3.68200  -2.69700  1.000 27.50196 ? 110 SER B O   1 
ATOM   2347 C  CB  . SER B 1 111 ? -15.07200 6.18700  -4.02100  1.000 26.31192 ? 110 SER B CB  1 
ATOM   2348 O  OG  . SER B 1 111 ? -15.10300 7.00500  -2.86100  1.000 24.58111 ? 110 SER B OG  1 
ATOM   2349 N  N   . HIS B 1 112 ? -16.81000 3.50600  -2.24400  1.000 25.12095 ? 111 HIS B N   1 
ATOM   2350 C  CA  . HIS B 1 112 ? -16.66100 2.37900  -1.31800  1.000 25.28781 ? 111 HIS B CA  1 
ATOM   2351 C  C   . HIS B 1 112 ? -15.77700 2.71500  -0.11700  1.000 27.17169 ? 111 HIS B C   1 
ATOM   2352 O  O   . HIS B 1 112 ? -15.04400 1.86200  0.39400   1.000 29.68431 ? 111 HIS B O   1 
ATOM   2353 C  CB  . HIS B 1 112 ? -16.14300 1.13000  -2.06400  1.000 27.21696 ? 111 HIS B CB  1 
ATOM   2354 C  CG  . HIS B 1 112 ? -17.04500 0.68200  -3.17600  1.000 27.77440 ? 111 HIS B CG  1 
ATOM   2355 N  ND1 . HIS B 1 112 ? -18.15700 -0.10500 -2.96100  1.000 34.01206 ? 111 HIS B ND1 1 
ATOM   2356 C  CD2 . HIS B 1 112 ? -17.03800 0.96600  -4.50000  1.000 30.23014 ? 111 HIS B CD2 1 
ATOM   2357 C  CE1 . HIS B 1 112 ? -18.76500 -0.33300 -4.11400  1.000 32.74823 ? 111 HIS B CE1 1 
ATOM   2358 N  NE2 . HIS B 1 112 ? -18.12000 0.33200  -5.05800  1.000 35.25602 ? 111 HIS B NE2 1 
ATOM   2359 N  N   . CYS B 1 113 ? -15.84500 3.96300  0.35800   1.000 25.35153 ? 112 CYS B N   1 
ATOM   2360 C  CA  . CYS B 1 113 ? -15.24500 4.30000  1.63900   1.000 25.90851 ? 112 CYS B CA  1 
ATOM   2361 C  C   . CYS B 1 113 ? -16.07300 3.73300  2.77800   1.000 28.50489 ? 112 CYS B C   1 
ATOM   2362 O  O   . CYS B 1 113 ? -17.30400 3.65600  2.69900   1.000 28.92233 ? 112 CYS B O   1 
ATOM   2363 C  CB  . CYS B 1 113 ? -15.15200 5.81300  1.81300   1.000 21.17258 ? 112 CYS B CB  1 
ATOM   2364 S  SG  . CYS B 1 113 ? -14.06500 6.64700  0.66900   1.000 25.66282 ? 112 CYS B SG  1 
ATOM   2365 N  N   . ARG B 1 114 ? -15.38600 3.35400  3.85900   1.000 26.03316 ? 113 ARG B N   1 
ATOM   2366 C  CA  . ARG B 1 114 ? -16.07700 2.95400  5.08000   1.000 29.13997 ? 113 ARG B CA  1 
ATOM   2367 C  C   . ARG B 1 114 ? -16.58200 4.14900  5.89400   1.000 28.16453 ? 113 ARG B C   1 
ATOM   2368 O  O   . ARG B 1 114 ? -17.52600 3.99300  6.67400   1.000 30.34595 ? 113 ARG B O   1 
ATOM   2369 C  CB  . ARG B 1 114 ? -15.15700 2.13300  5.97900   1.000 35.29308 ? 113 ARG B CB  1 
ATOM   2370 C  CG  . ARG B 1 114 ? -15.89300 1.49400  7.16200   1.000 47.36099 ? 113 ARG B CG  1 
ATOM   2371 C  CD  . ARG B 1 114 ? -14.94200 0.90700  8.18900   1.000 53.16583 ? 113 ARG B CD  1 
ATOM   2372 N  NE  . ARG B 1 114 ? -15.60500 0.69100  9.47700   1.000 61.46227 ? 113 ARG B NE  1 
ATOM   2373 C  CZ  . ARG B 1 114 ? -15.66500 1.60100  10.45200  1.000 59.55719 ? 113 ARG B CZ  1 
ATOM   2374 N  NH1 . ARG B 1 114 ? -15.09600 2.78800  10.29800  1.000 51.77246 ? 113 ARG B NH1 1 
ATOM   2375 N  NH2 . ARG B 1 114 ? -16.28400 1.32000  11.59300  1.000 64.17470 ? 113 ARG B NH2 1 
ATOM   2376 N  N   . ALA B 1 115 ? -15.95100 5.31400  5.78100   1.000 24.99690 ? 114 ALA B N   1 
ATOM   2377 C  CA  . ALA B 1 115 ? -16.29000 6.42600  6.66800   1.000 26.01188 ? 114 ALA B CA  1 
ATOM   2378 C  C   . ALA B 1 115 ? -15.72500 7.70800  6.09500   1.000 23.90229 ? 114 ALA B C   1 
ATOM   2379 O  O   . ALA B 1 115 ? -14.82300 7.68400  5.25300   1.000 24.14223 ? 114 ALA B O   1 
ATOM   2380 C  CB  . ALA B 1 115 ? -15.72300 6.23900  8.07500   1.000 30.52659 ? 114 ALA B CB  1 
ATOM   2381 N  N   . LEU B 1 116 ? -16.22000 8.83800  6.62300   1.000 22.75920 ? 115 LEU B N   1 
ATOM   2382 C  CA  . LEU B 1 116 ? -15.57700 10.13700 6.46200   1.000 20.46837 ? 115 LEU B CA  1 
ATOM   2383 C  C   . LEU B 1 116 ? -14.98300 10.58800 7.79500   1.000 19.80553 ? 115 LEU B C   1 
ATOM   2384 O  O   . LEU B 1 116 ? -15.51300 10.26400 8.85400   1.000 23.83769 ? 115 LEU B O   1 
ATOM   2385 C  CB  . LEU B 1 116 ? -16.57100 11.18900 5.96300   1.000 21.61730 ? 115 LEU B CB  1 
ATOM   2386 C  CG  . LEU B 1 116 ? -17.15900 10.91200 4.55800   1.000 24.56731 ? 115 LEU B CG  1 
ATOM   2387 C  CD1 . LEU B 1 116 ? -18.46700 10.14900 4.57200   1.000 23.59037 ? 115 LEU B CD1 1 
ATOM   2388 C  CD2 . LEU B 1 116 ? -17.36600 12.23100 3.82300   1.000 23.55088 ? 115 LEU B CD2 1 
ATOM   2389 N  N   . THR B 1 117 ? -13.90800 11.38200 7.74300   1.000 21.83251 ? 116 THR B N   1 
ATOM   2390 C  CA  . THR B 1 117 ? -13.26800 11.88000 8.95900   1.000 21.62712 ? 116 THR B CA  1 
ATOM   2391 C  C   . THR B 1 117 ? -12.94500 13.36400 8.82200   1.000 20.61968 ? 116 THR B C   1 
ATOM   2392 O  O   . THR B 1 117 ? -12.88700 13.90400 7.71500   1.000 19.55574 ? 116 THR B O   1 
ATOM   2393 C  CB  . THR B 1 117 ? -11.96600 11.13600 9.29700   1.000 20.98506 ? 116 THR B CB  1 
ATOM   2394 O  OG1 . THR B 1 117 ? -11.02000 11.26000 8.22900   1.000 23.01505 ? 116 THR B OG1 1 
ATOM   2395 C  CG2 . THR B 1 117 ? -12.24500 9.61500  9.52600   1.000 22.59914 ? 116 THR B CG2 1 
ATOM   2396 N  N   . LEU B 1 118 ? -12.69400 13.99600 9.97100   1.000 21.26613 ? 117 LEU B N   1 
ATOM   2397 C  CA  . LEU B 1 118 ? -12.23800 15.39200 10.05800  1.000 19.09816 ? 117 LEU B CA  1 
ATOM   2398 C  C   . LEU B 1 118 ? -11.69600 15.66400 11.46000  1.000 20.24330 ? 117 LEU B C   1 
ATOM   2399 O  O   . LEU B 1 118 ? -11.88800 14.87200 12.38700  1.000 20.39579 ? 117 LEU B O   1 
ATOM   2400 C  CB  . LEU B 1 118 ? -13.37800 16.38600 9.72600   1.000 18.52744 ? 117 LEU B CB  1 
ATOM   2401 C  CG  . LEU B 1 118 ? -14.67200 16.29300 10.54100  1.000 20.10833 ? 117 LEU B CG  1 
ATOM   2402 C  CD1 . LEU B 1 118 ? -14.57200 17.05900 11.89800  1.000 22.38302 ? 117 LEU B CD1 1 
ATOM   2403 C  CD2 . LEU B 1 118 ? -15.85700 16.82600 9.74400   1.000 23.09581 ? 117 LEU B CD2 1 
ATOM   2404 N  N   . THR B 1 119 ? -10.97700 16.78900 11.60100  1.000 17.84187 ? 118 THR B N   1 
ATOM   2405 C  CA  . THR B 1 119 ? -10.70500 17.36200 12.91700  1.000 20.28190 ? 118 THR B CA  1 
ATOM   2406 C  C   . THR B 1 119 ? -11.24200 18.78400 12.89900  1.000 20.01971 ? 118 THR B C   1 
ATOM   2407 O  O   . THR B 1 119 ? -11.27600 19.43700 11.83900  1.000 21.26139 ? 118 THR B O   1 
ATOM   2408 C  CB  . THR B 1 119 ? -9.20100  17.33000 13.30000  1.000 23.08703 ? 118 THR B CB  1 
ATOM   2409 O  OG1 . THR B 1 119 ? -8.43900  18.20300 12.45000  1.000 23.81309 ? 118 THR B OG1 1 
ATOM   2410 C  CG2 . THR B 1 119 ? -8.65400  15.89700 13.19800  1.000 22.81175 ? 118 THR B CG2 1 
ATOM   2411 N  N   . THR B 1 120 ? -11.67500 19.26600 14.06000  1.000 20.58855 ? 119 THR B N   1 
ATOM   2412 C  CA  . THR B 1 120 ? -12.30000 20.59600 14.09900  1.000 21.48915 ? 119 THR B CA  1 
ATOM   2413 C  C   . THR B 1 120 ? -12.39200 21.09400 15.54200  1.000 20.28636 ? 119 THR B C   1 
ATOM   2414 O  O   . THR B 1 120 ? -11.96700 20.42200 16.48400  1.000 22.84758 ? 119 THR B O   1 
ATOM   2415 C  CB  . THR B 1 120 ? -13.67300 20.54400 13.44700  1.000 19.62038 ? 119 THR B CB  1 
ATOM   2416 O  OG1 . THR B 1 120 ? -14.13900 21.90200 13.21000  1.000 22.61605 ? 119 THR B OG1 1 
ATOM   2417 C  CG2 . THR B 1 120 ? -14.62300 19.81100 14.37700  1.000 20.67184 ? 119 THR B CG2 1 
ATOM   2418 N  N   . PHE B 1 121 ? -12.95400 22.29500 15.71600  1.000 20.25506 ? 120 PHE B N   1 
ATOM   2419 C  CA  . PHE B 1 121 ? -13.13000 22.85300 17.05400  1.000 21.27943 ? 120 PHE B CA  1 
ATOM   2420 C  C   . PHE B 1 121 ? -14.36600 22.24100 17.70700  1.000 23.49248 ? 120 PHE B C   1 
ATOM   2421 O  O   . PHE B 1 121 ? -15.43400 22.14700 17.08800  1.000 23.22007 ? 120 PHE B O   1 
ATOM   2422 C  CB  . PHE B 1 121 ? -13.29000 24.39100 17.01400  1.000 23.93571 ? 120 PHE B CB  1 
ATOM   2423 C  CG  . PHE B 1 121 ? -12.02900 25.13100 16.71200  1.000 26.02276 ? 120 PHE B CG  1 
ATOM   2424 C  CD1 . PHE B 1 121 ? -10.97700 25.12400 17.62800  1.000 23.44951 ? 120 PHE B CD1 1 
ATOM   2425 C  CD2 . PHE B 1 121 ? -11.88100 25.83600 15.51300  1.000 24.48878 ? 120 PHE B CD2 1 
ATOM   2426 C  CE1 . PHE B 1 121 ? -9.80000  25.77500 17.34400  1.000 24.33074 ? 120 PHE B CE1 1 
ATOM   2427 C  CE2 . PHE B 1 121 ? -10.70300 26.49100 15.22600  1.000 23.18831 ? 120 PHE B CE2 1 
ATOM   2428 C  CZ  . PHE B 1 121 ? -9.66600  26.47100 16.14500  1.000 25.94434 ? 120 PHE B CZ  1 
ATOM   2429 N  N   . CYS B 1 122 ? -14.23100 21.86100 18.97900  1.000 23.90157 ? 121 CYS B N   1 
ATOM   2430 C  CA  . CYS B 1 122 ? -15.35500 21.29500 19.73800  1.000 26.22519 ? 121 CYS B CA  1 
ATOM   2431 C  C   . CYS B 1 122 ? -16.49600 22.29200 19.96600  1.000 29.48496 ? 121 CYS B C   1 
ATOM   2432 O  O   . CYS B 1 122 ? -17.67000 21.90400 19.95800  1.000 32.13487 ? 121 CYS B O   1 
ATOM   2433 C  CB  . CYS B 1 122 ? -14.86800 20.83000 21.10700  1.000 31.06790 ? 121 CYS B CB  1 
ATOM   2434 S  SG  . CYS B 1 122 ? -13.59800 19.56900 21.03000  1.000 32.49639 ? 121 CYS B SG  1 
ATOM   2435 N  N   . ASP B 1 123 ? -16.17400 23.55300 20.26200  1.000 29.60296 ? 122 ASP B N   1 
ATOM   2436 C  CA  . ASP B 1 123 ? -17.11600 24.49300 20.86700  1.000 31.24562 ? 122 ASP B CA  1 
ATOM   2437 C  C   . ASP B 1 123 ? -17.48900 25.66000 19.96100  1.000 35.11092 ? 122 ASP B C   1 
ATOM   2438 O  O   . ASP B 1 123 ? -18.04200 26.65900 20.44300  1.000 49.23749 ? 122 ASP B O   1 
ATOM   2439 C  CB  . ASP B 1 123 ? -16.54200 25.04900 22.16500  1.000 37.89482 ? 122 ASP B CB  1 
ATOM   2440 C  CG  . ASP B 1 123 ? -16.34900 23.98900 23.22200  1.000 43.38909 ? 122 ASP B CG  1 
ATOM   2441 O  OD1 . ASP B 1 123 ? -17.16100 23.04900 23.27900  1.000 45.23749 ? 122 ASP B OD1 1 
ATOM   2442 O  OD2 . ASP B 1 123 ? -15.38700 24.11100 24.00300  1.000 47.28420 ? 122 ASP B OD2 1 
ATOM   2443 N  N   . VAL B 1 124 ? -17.18300 25.58100 18.68000  1.000 27.11804 ? 123 VAL B N   1 
ATOM   2444 C  CA  . VAL B 1 124 ? -17.54100 26.61600 17.71400  1.000 27.14683 ? 123 VAL B CA  1 
ATOM   2445 C  C   . VAL B 1 124 ? -18.84000 26.18500 17.02900  1.000 27.61273 ? 123 VAL B C   1 
ATOM   2446 O  O   . VAL B 1 124 ? -18.91300 25.05000 16.55000  1.000 26.13058 ? 123 VAL B O   1 
ATOM   2447 C  CB  . VAL B 1 124 ? -16.40600 26.79800 16.69000  1.000 26.30058 ? 123 VAL B CB  1 
ATOM   2448 C  CG1 . VAL B 1 124 ? -16.87100 27.69800 15.51900  1.000 29.98126 ? 123 VAL B CG1 1 
ATOM   2449 C  CG2 . VAL B 1 124 ? -15.19400 27.42400 17.36500  1.000 25.53734 ? 123 VAL B CG2 1 
ATOM   2450 N  N   . PRO B 1 125 ? -19.86600 27.03300 16.97700  1.000 30.87192 ? 124 PRO B N   1 
ATOM   2451 C  CA  . PRO B 1 125 ? -21.19200 26.54000 16.54900  1.000 34.65112 ? 124 PRO B CA  1 
ATOM   2452 C  C   . PRO B 1 125 ? -21.22800 25.97800 15.13700  1.000 29.93874 ? 124 PRO B C   1 
ATOM   2453 O  O   . PRO B 1 125 ? -22.04700 25.09300 14.85100  1.000 32.97065 ? 124 PRO B O   1 
ATOM   2454 C  CB  . PRO B 1 125 ? -22.08500 27.78600 16.66800  1.000 37.26695 ? 124 PRO B CB  1 
ATOM   2455 C  CG  . PRO B 1 125 ? -21.39600 28.69500 17.61100  1.000 38.95268 ? 124 PRO B CG  1 
ATOM   2456 C  CD  . PRO B 1 125 ? -19.90800 28.42000 17.47600  1.000 34.67951 ? 124 PRO B CD  1 
ATOM   2457 N  N   . TRP B 1 126 ? -20.39400 26.48100 14.23300  1.000 29.16910 ? 125 TRP B N   1 
ATOM   2458 C  CA  . TRP B 1 126 ? -20.41000 26.02300 12.85400  1.000 29.41586 ? 125 TRP B CA  1 
ATOM   2459 C  C   . TRP B 1 126 ? -19.39200 24.94200 12.63300  1.000 26.64848 ? 125 TRP B C   1 
ATOM   2460 O  O   . TRP B 1 126 ? -19.10900 24.59000 11.47900  1.000 26.37809 ? 125 TRP B O   1 
ATOM   2461 C  CB  . TRP B 1 126 ? -20.18200 27.19200 11.87200  1.000 30.93413 ? 125 TRP B CB  1 
ATOM   2462 C  CG  . TRP B 1 126 ? -18.84300 27.93500 12.05100  1.000 31.76642 ? 125 TRP B CG  1 
ATOM   2463 C  CD1 . TRP B 1 126 ? -17.63300 27.61300 11.47600  1.000 30.43083 ? 125 TRP B CD1 1 
ATOM   2464 C  CD2 . TRP B 1 126 ? -18.61100 29.10000 12.83400  1.000 30.71421 ? 125 TRP B CD2 1 
ATOM   2465 N  NE1 . TRP B 1 126 ? -16.66100 28.53200 11.86100  1.000 26.71361 ? 125 TRP B NE1 1 
ATOM   2466 C  CE2 . TRP B 1 126 ? -17.23300 29.43700 12.71000  1.000 28.66162 ? 125 TRP B CE2 1 
ATOM   2467 C  CE3 . TRP B 1 126 ? -19.43300 29.90900 13.63600  1.000 32.22275 ? 125 TRP B CE3 1 
ATOM   2468 C  CZ2 . TRP B 1 126 ? -16.67300 30.56200 13.34500  1.000 31.13163 ? 125 TRP B CZ2 1 
ATOM   2469 C  CZ3 . TRP B 1 126 ? -18.86300 31.01500 14.29200  1.000 36.74010 ? 125 TRP B CZ3 1 
ATOM   2470 C  CH2 . TRP B 1 126 ? -17.49700 31.32300 14.13800  1.000 36.69101 ? 125 TRP B CH2 1 
ATOM   2471 N  N   . ASN B 1 127 ? -18.82600 24.40500 13.72100  1.000 23.73669 ? 126 ASN B N   1 
ATOM   2472 C  CA  . ASN B 1 127 ? -17.89400 23.29100 13.63000  1.000 22.46475 ? 126 ASN B CA  1 
ATOM   2473 C  C   . ASN B 1 127 ? -18.52600 22.04900 14.26100  1.000 23.95830 ? 126 ASN B C   1 
ATOM   2474 O  O   . ASN B 1 127 ? -19.53600 21.56900 13.74200  1.000 23.99743 ? 126 ASN B O   1 
ATOM   2475 C  CB  . ASN B 1 127 ? -16.53500 23.64400 14.26200  1.000 22.65749 ? 126 ASN B CB  1 
ATOM   2476 C  CG  . ASN B 1 127 ? -15.69600 24.63700 13.41000  1.000 25.53632 ? 126 ASN B CG  1 
ATOM   2477 O  OD1 . ASN B 1 127 ? -14.72600 25.20800 13.90800  1.000 28.46696 ? 126 ASN B OD1 1 
ATOM   2478 N  ND2 . ASN B 1 127 ? -16.05000 24.81300 12.13900  1.000 25.32734 ? 126 ASN B ND2 1 
ATOM   2479 N  N   . ALA B 1 128 ? -17.97600 21.51200 15.35400  1.000 24.43260 ? 127 ALA B N   1 
ATOM   2480 C  CA  . ALA B 1 128 ? -18.38800 20.16000 15.75700  1.000 23.65412 ? 127 ALA B CA  1 
ATOM   2481 C  C   . ALA B 1 128 ? -19.88900 20.01100 16.00600  1.000 24.72457 ? 127 ALA B C   1 
ATOM   2482 O  O   . ALA B 1 128 ? -20.45000 18.99800 15.55800  1.000 25.65401 ? 127 ALA B O   1 
ATOM   2483 C  CB  . ALA B 1 128 ? -17.59000 19.72300 17.00100  1.000 25.42237 ? 127 ALA B CB  1 
ATOM   2484 N  N   . PRO B 1 129 ? -20.59200 20.95600 16.65300  1.000 26.26860 ? 128 PRO B N   1 
ATOM   2485 C  CA  . PRO B 1 129 ? -22.04900 20.74900 16.84700  1.000 29.21762 ? 128 PRO B CA  1 
ATOM   2486 C  C   . PRO B 1 129 ? -22.82300 20.62900 15.53900  1.000 29.95265 ? 128 PRO B C   1 
ATOM   2487 O  O   . PRO B 1 129 ? -23.80800 19.87600 15.46300  1.000 28.31941 ? 128 PRO B O   1 
ATOM   2488 C  CB  . PRO B 1 129 ? -22.47800 21.98000 17.65800  1.000 30.38896 ? 128 PRO B CB  1 
ATOM   2489 C  CG  . PRO B 1 129 ? -21.19500 22.45000 18.35700  1.000 35.28059 ? 128 PRO B CG  1 
ATOM   2490 C  CD  . PRO B 1 129 ? -20.09600 22.15100 17.36900  1.000 29.10697 ? 128 PRO B CD  1 
ATOM   2491 N  N   . PHE B 1 130 ? -22.41000 21.36300 14.50600  1.000 27.32009 ? 129 PHE B N   1 
ATOM   2492 C  CA  . PHE B 1 130 ? -23.01300 21.24400 13.18000  1.000 24.56284 ? 129 PHE B CA  1 
ATOM   2493 C  C   . PHE B 1 130 ? -22.74000 19.87300 12.57300  1.000 23.70812 ? 129 PHE B C   1 
ATOM   2494 O  O   . PHE B 1 130 ? -23.67100 19.15300 12.17400  1.000 24.17947 ? 129 PHE B O   1 
ATOM   2495 C  CB  . PHE B 1 130 ? -22.47500 22.39100 12.29000  1.000 24.64702 ? 129 PHE B CB  1 
ATOM   2496 C  CG  . PHE B 1 130 ? -22.69400 22.19700 10.79300  1.000 22.92559 ? 129 PHE B CG  1 
ATOM   2497 C  CD1 . PHE B 1 130 ? -23.91000 21.75500 10.30500  1.000 24.87371 ? 129 PHE B CD1 1 
ATOM   2498 C  CD2 . PHE B 1 130 ? -21.68600 22.51700 9.88200   1.000 28.48877 ? 129 PHE B CD2 1 
ATOM   2499 C  CE1 . PHE B 1 130 ? -24.12200 21.58300 8.92600   1.000 25.25396 ? 129 PHE B CE1 1 
ATOM   2500 C  CE2 . PHE B 1 130 ? -21.89200 22.36200 8.47900   1.000 27.81486 ? 129 PHE B CE2 1 
ATOM   2501 C  CZ  . PHE B 1 130 ? -23.12000 21.89200 8.02500   1.000 27.26262 ? 129 PHE B CZ  1 
ATOM   2502 N  N   . TYR B 1 131 ? -21.46800 19.47000 12.52000  1.000 22.96900 ? 130 TYR B N   1 
ATOM   2503 C  CA  . TYR B 1 131 ? -21.13600 18.15300 11.97000  1.000 20.89569 ? 130 TYR B CA  1 
ATOM   2504 C  C   . TYR B 1 131 ? -21.83800 17.03700 12.74000  1.000 21.69932 ? 130 TYR B C   1 
ATOM   2505 O  O   . TYR B 1 131 ? -22.24700 16.01700 12.15300  1.000 23.01778 ? 130 TYR B O   1 
ATOM   2506 C  CB  . TYR B 1 131 ? -19.61300 17.94600 12.00000  1.000 20.19031 ? 130 TYR B CB  1 
ATOM   2507 C  CG  . TYR B 1 131 ? -18.82100 18.98700 11.26600  1.000 25.44786 ? 130 TYR B CG  1 
ATOM   2508 C  CD1 . TYR B 1 131 ? -19.20300 19.40100 10.00900  1.000 29.74234 ? 130 TYR B CD1 1 
ATOM   2509 C  CD2 . TYR B 1 131 ? -17.68300 19.54200 11.82400  1.000 24.38539 ? 130 TYR B CD2 1 
ATOM   2510 C  CE1 . TYR B 1 131 ? -18.47000 20.34200 9.31700   1.000 33.71967 ? 130 TYR B CE1 1 
ATOM   2511 C  CE2 . TYR B 1 131 ? -16.95000 20.49700 11.13400  1.000 24.33373 ? 130 TYR B CE2 1 
ATOM   2512 C  CZ  . TYR B 1 131 ? -17.34700 20.88400 9.88500   1.000 31.80638 ? 130 TYR B CZ  1 
ATOM   2513 O  OH  . TYR B 1 131 ? -16.62400 21.83200 9.18500   1.000 32.51341 ? 130 TYR B OH  1 
ATOM   2514 N  N   . ALA B 1 132 ? -21.99400 17.20300 14.05100  1.000 24.63701 ? 131 ALA B N   1 
ATOM   2515 C  CA  . ALA B 1 132 ? -22.64700 16.15200 14.82800  1.000 25.41603 ? 131 ALA B CA  1 
ATOM   2516 C  C   . ALA B 1 132 ? -24.11700 16.00500 14.44300  1.000 25.36442 ? 131 ALA B C   1 
ATOM   2517 O  O   . ALA B 1 132 ? -24.65800 14.89000 14.47500  1.000 28.53100 ? 131 ALA B O   1 
ATOM   2518 C  CB  . ALA B 1 132 ? -22.49800 16.42400 16.32800  1.000 26.34877 ? 131 ALA B CB  1 
ATOM   2519 N  N   . ARG B 1 133 ? -24.78100 17.09500 14.03300  1.000 25.32858 ? 132 ARG B N   1 
ATOM   2520 C  CA  . ARG B 1 133 ? -26.16200 16.93300 13.57200  1.000 24.56810 ? 132 ARG B CA  1 
ATOM   2521 C  C   . ARG B 1 133 ? -26.25900 16.12800 12.27700  1.000 23.01977 ? 132 ARG B C   1 
ATOM   2522 O  O   . ARG B 1 133 ? -27.34000 15.56700 11.99300  1.000 28.98599 ? 132 ARG B O   1 
ATOM   2523 C  CB  . ARG B 1 133 ? -26.83300 18.28600 13.35500  1.000 24.03709 ? 132 ARG B CB  1 
ATOM   2524 C  CG  . ARG B 1 133 ? -27.01200 19.10000 14.63500  1.000 26.54028 ? 132 ARG B CG  1 
ATOM   2525 C  CD  . ARG B 1 133 ? -27.91400 20.34200 14.44400  1.000 29.93869 ? 132 ARG B CD  1 
ATOM   2526 N  NE  . ARG B 1 133 ? -27.27800 21.38300 13.62800  1.000 31.54791 ? 132 ARG B NE  1 
ATOM   2527 C  CZ  . ARG B 1 133 ? -26.49800 22.35100 14.11800  1.000 32.79585 ? 132 ARG B CZ  1 
ATOM   2528 N  NH1 . ARG B 1 133 ? -26.21900 22.43400 15.41600  1.000 31.84414 ? 132 ARG B NH1 1 
ATOM   2529 N  NH2 . ARG B 1 133 ? -25.97700 23.23900 13.27700  1.000 33.81449 ? 132 ARG B NH2 1 
ATOM   2530 N  N   . LEU B 1 134 ? -25.18100 16.06300 11.50700  1.000 23.59849 ? 133 LEU B N   1 
ATOM   2531 C  CA  . LEU B 1 134 ? -25.13800 15.28900 10.26900  1.000 23.36700 ? 133 LEU B CA  1 
ATOM   2532 C  C   . LEU B 1 134 ? -24.77700 13.83500 10.47600  1.000 26.35041 ? 133 LEU B C   1 
ATOM   2533 O  O   . LEU B 1 134 ? -24.79500 13.06900 9.50600   1.000 25.21124 ? 133 LEU B O   1 
ATOM   2534 C  CB  . LEU B 1 134 ? -24.12800 15.88800 9.29200   1.000 22.95132 ? 133 LEU B CB  1 
ATOM   2535 C  CG  . LEU B 1 134 ? -24.21600 17.40700 9.15500   1.000 20.67551 ? 133 LEU B CG  1 
ATOM   2536 C  CD1 . LEU B 1 134 ? -23.15300 17.95100 8.20700   1.000 22.09869 ? 133 LEU B CD1 1 
ATOM   2537 C  CD2 . LEU B 1 134 ? -25.64100 17.75800 8.67600   1.000 26.07040 ? 133 LEU B CD2 1 
ATOM   2538 N  N   . GLY B 1 135 ? -24.42100 13.44000 11.69400  1.000 23.75173 ? 134 GLY B N   1 
ATOM   2539 C  CA  . GLY B 1 135 ? -24.05300 12.06300 11.98200  1.000 24.23596 ? 134 GLY B CA  1 
ATOM   2540 C  C   . GLY B 1 135 ? -22.58700 11.87300 12.32800  1.000 25.45685 ? 134 GLY B C   1 
ATOM   2541 O  O   . GLY B 1 135 ? -22.20800 10.74800 12.68200  1.000 27.41429 ? 134 GLY B O   1 
ATOM   2542 N  N   . PHE B 1 136 ? -21.74300 12.90700 12.22900  1.000 23.19112 ? 135 PHE B N   1 
ATOM   2543 C  CA  . PHE B 1 136 ? -20.36500 12.73900 12.68100  1.000 22.40258 ? 135 PHE B CA  1 
ATOM   2544 C  C   . PHE B 1 136 ? -20.32300 12.52200 14.18500  1.000 29.52324 ? 135 PHE B C   1 
ATOM   2545 O  O   . PHE B 1 136 ? -21.03900 13.18500 14.94600  1.000 30.05397 ? 135 PHE B O   1 
ATOM   2546 C  CB  . PHE B 1 136 ? -19.50500 13.95800 12.32900  1.000 21.98472 ? 135 PHE B CB  1 
ATOM   2547 C  CG  . PHE B 1 136 ? -19.08800 13.99500 10.88900  1.000 22.30441 ? 135 PHE B CG  1 
ATOM   2548 C  CD1 . PHE B 1 136 ? -19.90400 14.60700 9.93400   1.000 23.23971 ? 135 PHE B CD1 1 
ATOM   2549 C  CD2 . PHE B 1 136 ? -17.88700 13.42400 10.48600  1.000 23.47935 ? 135 PHE B CD2 1 
ATOM   2550 C  CE1 . PHE B 1 136 ? -19.54200 14.64500 8.59300   1.000 19.52128 ? 135 PHE B CE1 1 
ATOM   2551 C  CE2 . PHE B 1 136 ? -17.50200 13.46200 9.16800   1.000 21.47022 ? 135 PHE B CE2 1 
ATOM   2552 C  CZ  . PHE B 1 136 ? -18.32600 14.08200 8.21000   1.000 21.55186 ? 135 PHE B CZ  1 
ATOM   2553 N  N   . GLN B 1 137 ? -19.46300 11.60800 14.62200  1.000 26.75547 ? 136 GLN B N   1 
ATOM   2554 C  CA  A GLN B 1 137 ? -19.33500 11.27700 16.03300  0.580 29.85635 ? 136 GLN B CA  1 
ATOM   2555 C  CA  B GLN B 1 137 ? -19.33100 11.26000 16.03100  0.420 30.12963 ? 136 GLN B CA  1 
ATOM   2556 C  C   . GLN B 1 137 ? -17.98500 11.72800 16.56800  1.000 28.36572 ? 136 GLN B C   1 
ATOM   2557 O  O   . GLN B 1 137 ? -16.94700 11.49400 15.93900  1.000 26.60757 ? 136 GLN B O   1 
ATOM   2558 C  CB  A GLN B 1 137 ? -19.53200 9.78000  16.24800  0.580 35.02790 ? 136 GLN B CB  1 
ATOM   2559 C  CB  B GLN B 1 137 ? -19.48700 9.75200  16.22400  0.420 34.78017 ? 136 GLN B CB  1 
ATOM   2560 C  CG  A GLN B 1 137 ? -20.97200 9.38700  16.01200  0.580 40.48506 ? 136 GLN B CG  1 
ATOM   2561 C  CG  B GLN B 1 137 ? -20.85500 9.23100  15.80700  0.420 40.33701 ? 136 GLN B CG  1 
ATOM   2562 C  CD  A GLN B 1 137 ? -21.29400 7.99200  16.48200  0.580 46.05188 ? 136 GLN B CD  1 
ATOM   2563 C  CD  B GLN B 1 137 ? -21.97600 9.74800  16.69000  0.420 42.79248 ? 136 GLN B CD  1 
ATOM   2564 O  OE1 A GLN B 1 137 ? -20.54600 7.38800  17.25400  0.580 51.66953 ? 136 GLN B OE1 1 
ATOM   2565 O  OE1 B GLN B 1 137 ? -21.86300 9.74700  17.91700  0.420 46.87136 ? 136 GLN B OE1 1 
ATOM   2566 N  NE2 A GLN B 1 137 ? -22.41900 7.47000  16.02000  0.580 49.90184 ? 136 GLN B NE2 1 
ATOM   2567 N  NE2 B GLN B 1 137 ? -23.06200 10.19700 16.07000  0.420 40.75830 ? 136 GLN B NE2 1 
ATOM   2568 N  N   . ARG B 1 138 ? -18.01200 12.39300 17.72400  1.000 26.07180 ? 137 ARG B N   1 
ATOM   2569 C  CA  . ARG B 1 138 ? -16.78200 12.78400 18.39700  1.000 27.76618 ? 137 ARG B CA  1 
ATOM   2570 C  C   . ARG B 1 138 ? -16.06500 11.53600 18.89600  1.000 30.17126 ? 137 ARG B C   1 
ATOM   2571 O  O   . ARG B 1 138 ? -16.68900 10.65400 19.49300  1.000 32.66214 ? 137 ARG B O   1 
ATOM   2572 C  CB  . ARG B 1 138 ? -17.08900 13.71400 19.56200  1.000 33.40582 ? 137 ARG B CB  1 
ATOM   2573 C  CG  . ARG B 1 138 ? -15.81700 14.23300 20.20300  1.000 41.14203 ? 137 ARG B CG  1 
ATOM   2574 C  CD  . ARG B 1 138 ? -16.08600 15.28000 21.28300  1.000 44.19947 ? 137 ARG B CD  1 
ATOM   2575 N  NE  . ARG B 1 138 ? -14.87800 15.54700 22.05300  1.000 49.92364 ? 137 ARG B NE  1 
ATOM   2576 C  CZ  . ARG B 1 138 ? -14.76400 16.50900 22.96500  1.000 53.18472 ? 137 ARG B CZ  1 
ATOM   2577 N  NH1 . ARG B 1 138 ? -15.78600 17.31400 23.21800  1.000 54.89832 ? 137 ARG B NH1 1 
ATOM   2578 N  NH2 . ARG B 1 138 ? -13.62000 16.67000 23.61400  1.000 53.13336 ? 137 ARG B NH2 1 
ATOM   2579 N  N   . LEU B 1 139 ? -14.76200 11.45900 18.63900  1.000 29.24210 ? 138 LEU B N   1 
ATOM   2580 C  CA  . LEU B 1 139 ? -13.95100 10.28300 18.93500  1.000 32.55529 ? 138 LEU B CA  1 
ATOM   2581 C  C   . LEU B 1 139 ? -13.09900 10.51200 20.17700  1.000 32.58888 ? 138 LEU B C   1 
ATOM   2582 O  O   . LEU B 1 139 ? -12.52900 11.59200 20.36200  1.000 29.88338 ? 138 LEU B O   1 
ATOM   2583 C  CB  . LEU B 1 139 ? -13.03300 9.96700  17.74900  1.000 29.15245 ? 138 LEU B CB  1 
ATOM   2584 C  CG  . LEU B 1 139 ? -13.70100 9.81700  16.39400  1.000 28.52588 ? 138 LEU B CG  1 
ATOM   2585 C  CD1 . LEU B 1 139 ? -12.68800 9.57000  15.27400  1.000 29.04673 ? 138 LEU B CD1 1 
ATOM   2586 C  CD2 . LEU B 1 139 ? -14.71000 8.66700  16.49500  1.000 27.71365 ? 138 LEU B CD2 1 
ATOM   2587 N  N   . THR B 1 140 ? -12.98900 9.48600  21.02000  1.000 32.76538 ? 139 THR B N   1 
ATOM   2588 C  CA  . THR B 1 140 ? -11.95900 9.52800  22.04500  1.000 31.99540 ? 139 THR B CA  1 
ATOM   2589 C  C   . THR B 1 140 ? -10.58700 9.40700  21.39200  1.000 38.35441 ? 139 THR B C   1 
ATOM   2590 O  O   . THR B 1 140 ? -10.45500 9.03000  20.22700  1.000 34.26085 ? 139 THR B O   1 
ATOM   2591 C  CB  . THR B 1 140 ? -12.13300 8.39900  23.05900  1.000 40.22239 ? 139 THR B CB  1 
ATOM   2592 O  OG1 . THR B 1 140 ? -11.83000 7.14900  22.42100  1.000 45.75493 ? 139 THR B OG1 1 
ATOM   2593 C  CG2 . THR B 1 140 ? -13.55700 8.37000  23.58900  1.000 43.42061 ? 139 THR B CG2 1 
ATOM   2594 N  N   . TRP B 1 141 ? -9.54600  9.71700  22.17200  1.000 40.15275 ? 140 TRP B N   1 
ATOM   2595 C  CA  . TRP B 1 141 ? -8.18100  9.59500  21.67100  1.000 38.98641 ? 140 TRP B CA  1 
ATOM   2596 C  C   . TRP B 1 141 ? -7.91500  8.18800  21.14700  1.000 43.96362 ? 140 TRP B C   1 
ATOM   2597 O  O   . TRP B 1 141 ? -7.29900  8.01500  20.08700  1.000 41.49757 ? 140 TRP B O   1 
ATOM   2598 C  CB  . TRP B 1 141 ? -7.20100  9.96300  22.78500  1.000 44.87710 ? 140 TRP B CB  1 
ATOM   2599 C  CG  . TRP B 1 141 ? -5.74300  10.03300 22.39800  1.000 43.10823 ? 140 TRP B CG  1 
ATOM   2600 C  CD1 . TRP B 1 141 ? -4.76000  9.14400  22.74900  1.000 41.39325 ? 140 TRP B CD1 1 
ATOM   2601 C  CD2 . TRP B 1 141 ? -5.09300  11.07600 21.65200  1.000 41.39560 ? 140 TRP B CD2 1 
ATOM   2602 N  NE1 . TRP B 1 141 ? -3.54800  9.56200  22.25200  1.000 45.50499 ? 140 TRP B NE1 1 
ATOM   2603 C  CE2 . TRP B 1 141 ? -3.72100  10.74400 21.57900  1.000 41.83403 ? 140 TRP B CE2 1 
ATOM   2604 C  CE3 . TRP B 1 141 ? -5.53400  12.25200 21.03900  1.000 35.74593 ? 140 TRP B CE3 1 
ATOM   2605 C  CZ2 . TRP B 1 141 ? -2.79200  11.53700 20.90500  1.000 36.11128 ? 140 TRP B CZ2 1 
ATOM   2606 C  CZ3 . TRP B 1 141 ? -4.60300  13.04100 20.36800  1.000 37.68265 ? 140 TRP B CZ3 1 
ATOM   2607 C  CH2 . TRP B 1 141 ? -3.24900  12.67500 20.30600  1.000 34.65481 ? 140 TRP B CH2 1 
ATOM   2608 N  N   . GLN B 1 142 ? -8.41800  7.17000  21.85100  1.000 46.95917 ? 141 GLN B N   1 
ATOM   2609 C  CA  . GLN B 1 142 ? -8.23200  5.79900  21.39200  1.000 52.04053 ? 141 GLN B CA  1 
ATOM   2610 C  C   . GLN B 1 142 ? -8.98600  5.53500  20.09000  1.000 46.16927 ? 141 GLN B C   1 
ATOM   2611 O  O   . GLN B 1 142 ? -8.43400  4.92900  19.16700  1.000 50.47565 ? 141 GLN B O   1 
ATOM   2612 C  CB  . GLN B 1 142 ? -8.66700  4.81700  22.48500  1.000 62.97288 ? 141 GLN B CB  1 
ATOM   2613 C  CG  . GLN B 1 142 ? -7.97600  3.45200  22.42400  1.000 74.87567 ? 141 GLN B CG  1 
ATOM   2614 C  CD  . GLN B 1 142 ? -8.75300  2.42600  21.61600  1.000 78.28974 ? 141 GLN B CD  1 
ATOM   2615 O  OE1 . GLN B 1 142 ? -9.95200  2.58200  21.37300  1.000 77.44867 ? 141 GLN B OE1 1 
ATOM   2616 N  NE2 . GLN B 1 142 ? -8.07000  1.36500  21.19800  1.000 80.60430 ? 141 GLN B NE2 1 
ATOM   2617 N  N   . GLU B 1 143 ? -10.24100 5.98700  19.99100  1.000 39.24169 ? 142 GLU B N   1 
ATOM   2618 C  CA  . GLU B 1 143 ? -11.06100 5.76100  18.79900  1.000 42.56080 ? 142 GLU B CA  1 
ATOM   2619 C  C   . GLU B 1 143 ? -10.54600 6.49200  17.56700  1.000 41.86225 ? 142 GLU B C   1 
ATOM   2620 O  O   . GLU B 1 143 ? -10.94600 6.15300  16.44600  1.000 36.55692 ? 142 GLU B O   1 
ATOM   2621 C  CB  . GLU B 1 143 ? -12.51100 6.19400  19.05700  1.000 43.55163 ? 142 GLU B CB  1 
ATOM   2622 C  CG  . GLU B 1 143 ? -13.27200 5.27100  20.01100  1.000 48.85708 ? 142 GLU B CG  1 
ATOM   2623 C  CD  . GLU B 1 143 ? -14.49700 5.92200  20.63500  1.000 51.34868 ? 142 GLU B CD  1 
ATOM   2624 O  OE1 . GLU B 1 143 ? -14.72000 7.13800  20.43900  1.000 44.47129 ? 142 GLU B OE1 1 
ATOM   2625 O  OE2 . GLU B 1 143 ? -15.24200 5.20800  21.33600  1.000 53.84143 ? 142 GLU B OE2 1 
ATOM   2626 N  N   . ALA B 1 144 ? -9.68900  7.49500  17.74200  1.000 39.01966 ? 143 ALA B N   1 
ATOM   2627 C  CA  . ALA B 1 144 ? -9.25600  8.29600  16.60600  1.000 37.45472 ? 143 ALA B CA  1 
ATOM   2628 C  C   . ALA B 1 144 ? -8.35100  7.50900  15.66000  1.000 33.59098 ? 143 ALA B C   1 
ATOM   2629 O  O   . ALA B 1 144 ? -8.38000  7.74100  14.45000  1.000 30.41678 ? 143 ALA B O   1 
ATOM   2630 C  CB  . ALA B 1 144 ? -8.54200  9.56200  17.09600  1.000 31.20217 ? 143 ALA B CB  1 
ATOM   2631 N  N   . GLY B 1 145 ? -7.51500  6.61600  16.18500  1.000 36.42619 ? 144 GLY B N   1 
ATOM   2632 C  CA  . GLY B 1 145 ? -6.58200  5.86700  15.36300  1.000 34.91546 ? 144 GLY B CA  1 
ATOM   2633 C  C   . GLY B 1 145 ? -5.31600  6.65600  15.07700  1.000 36.14642 ? 144 GLY B C   1 
ATOM   2634 O  O   . GLY B 1 145 ? -5.19600  7.83500  15.40400  1.000 32.65125 ? 144 GLY B O   1 
ATOM   2635 N  N   . GLU B 1 146 ? -4.36100  5.99500  14.40800  1.000 39.89893 ? 145 GLU B N   1 
ATOM   2636 C  CA  . GLU B 1 146 ? -3.01100  6.55800  14.25600  1.000 34.74589 ? 145 GLU B CA  1 
ATOM   2637 C  C   . GLU B 1 146 ? -3.00100  7.84900  13.42800  1.000 34.20503 ? 145 GLU B C   1 
ATOM   2638 O  O   . GLU B 1 146 ? -2.35100  8.83200  13.81200  1.000 31.92674 ? 145 GLU B O   1 
ATOM   2639 C  CB  . GLU B 1 146 ? -2.07500  5.52900  13.61700  1.000 37.09973 ? 145 GLU B CB  1 
ATOM   2640 C  CG  . GLU B 1 146 ? -1.67700  4.37000  14.52000  1.000 55.99150 ? 145 GLU B CG  1 
ATOM   2641 C  CD  . GLU B 1 146 ? -0.84700  4.81000  15.71900  1.000 69.37677 ? 145 GLU B CD  1 
ATOM   2642 O  OE1 . GLU B 1 146 ? -1.34000  4.67700  16.86200  1.000 72.84558 ? 145 GLU B OE1 1 
ATOM   2643 O  OE2 . GLU B 1 146 ? 0.29100   5.29400  15.51800  1.000 73.34390 ? 145 GLU B OE2 1 
ATOM   2644 N  N   . ARG B 1 147 ? -3.69100  7.85600  12.27700  1.000 32.46022 ? 146 ARG B N   1 
ATOM   2645 C  CA  . ARG B 1 147 ? -3.66900  9.02800  11.39300  1.000 30.33956 ? 146 ARG B CA  1 
ATOM   2646 C  C   . ARG B 1 147 ? -4.27600  10.25100 12.06700  1.000 28.62129 ? 146 ARG B C   1 
ATOM   2647 O  O   . ARG B 1 147 ? -3.66500  11.33100 12.09100  1.000 26.77584 ? 146 ARG B O   1 
ATOM   2648 C  CB  . ARG B 1 147 ? -4.41500  8.72000  10.08000  1.000 30.04287 ? 146 ARG B CB  1 
ATOM   2649 C  CG  . ARG B 1 147 ? -4.34700  9.86400  9.04400   1.000 29.08982 ? 146 ARG B CG  1 
ATOM   2650 C  CD  . ARG B 1 147 ? -4.98700  9.47200  7.70100   1.000 32.57421 ? 146 ARG B CD  1 
ATOM   2651 N  NE  . ARG B 1 147 ? -6.39700  9.11700  7.85900   1.000 29.92871 ? 146 ARG B NE  1 
ATOM   2652 C  CZ  . ARG B 1 147 ? -7.37400  10.00700 8.01500   1.000 26.83203 ? 146 ARG B CZ  1 
ATOM   2653 N  NH1 . ARG B 1 147 ? -7.09000  11.31200 8.00700   1.000 25.29364 ? 146 ARG B NH1 1 
ATOM   2654 N  NH2 . ARG B 1 147 ? -8.61800  9.60000  8.18600   1.000 27.32003 ? 146 ARG B NH2 1 
ATOM   2655 N  N   . LEU B 1 148 ? -5.48300  10.10500 12.61400  1.000 26.17092 ? 147 LEU B N   1 
ATOM   2656 C  CA  . LEU B 1 148 ? -6.11800  11.25700 13.24900  1.000 24.28747 ? 147 LEU B CA  1 
ATOM   2657 C  C   . LEU B 1 148 ? -5.37800  11.68100 14.51100  1.000 26.80360 ? 147 LEU B C   1 
ATOM   2658 O  O   . LEU B 1 148 ? -5.30800  12.88100 14.80100  1.000 25.82162 ? 147 LEU B O   1 
ATOM   2659 C  CB  . LEU B 1 148 ? -7.58400  10.95800 13.54500  1.000 27.54019 ? 147 LEU B CB  1 
ATOM   2660 C  CG  . LEU B 1 148 ? -8.41200  10.79300 12.26200  1.000 27.36326 ? 147 LEU B CG  1 
ATOM   2661 C  CD1 . LEU B 1 148 ? -9.82800  10.35100 12.55400  1.000 27.90476 ? 147 LEU B CD1 1 
ATOM   2662 C  CD2 . LEU B 1 148 ? -8.41400  12.07100 11.37800  1.000 29.26288 ? 147 LEU B CD2 1 
ATOM   2663 N  N   . ARG B 1 149 ? -4.82600  10.73800 15.27600  1.000 26.58749 ? 148 ARG B N   1 
ATOM   2664 C  CA  . ARG B 1 149 ? -4.01300  11.12000 16.43600  1.000 29.84113 ? 148 ARG B CA  1 
ATOM   2665 C  C   . ARG B 1 149 ? -2.81100  11.94700 16.01200  1.000 30.52244 ? 148 ARG B C   1 
ATOM   2666 O  O   . ARG B 1 149 ? -2.42700  12.90500 16.70100  1.000 29.37910 ? 148 ARG B O   1 
ATOM   2667 C  CB  . ARG B 1 149 ? -3.55400  9.87500  17.21000  1.000 31.60679 ? 148 ARG B CB  1 
ATOM   2668 C  CG  . ARG B 1 149 ? -4.60300  9.37700  18.17900  1.000 30.55709 ? 148 ARG B CG  1 
ATOM   2669 C  CD  . ARG B 1 149 ? -4.05900  8.38500  19.18100  1.000 36.96290 ? 148 ARG B CD  1 
ATOM   2670 N  NE  . ARG B 1 149 ? -3.61900  7.11400  18.61000  1.000 42.33361 ? 148 ARG B NE  1 
ATOM   2671 C  CZ  . ARG B 1 149 ? -4.39200  6.03900  18.47600  1.000 43.32100 ? 148 ARG B CZ  1 
ATOM   2672 N  NH1 . ARG B 1 149 ? -3.87800  4.91200  17.98100  1.000 41.48613 ? 148 ARG B NH1 1 
ATOM   2673 N  NH2 . ARG B 1 149 ? -5.67100  6.09400  18.82400  1.000 39.90086 ? 148 ARG B NH2 1 
ATOM   2674 N  N   . ALA B 1 150 ? -2.18000  11.57100 14.89800  1.000 29.93161 ? 149 ALA B N   1 
ATOM   2675 C  CA  . ALA B 1 150 ? -1.02700  12.31900 14.41300  1.000 28.95007 ? 149 ALA B CA  1 
ATOM   2676 C  C   . ALA B 1 150 ? -1.41500  13.74500 14.02100  1.000 28.87175 ? 149 ALA B C   1 
ATOM   2677 O  O   . ALA B 1 150 ? -0.63700  14.67600 14.25400  1.000 26.60044 ? 149 ALA B O   1 
ATOM   2678 C  CB  . ALA B 1 150 ? -0.38500  11.58000 13.23400  1.000 30.96854 ? 149 ALA B CB  1 
ATOM   2679 N  N   . ILE B 1 151 ? -2.58300  13.92400 13.39200  1.000 23.78394 ? 150 ILE B N   1 
ATOM   2680 C  CA  . ILE B 1 151 ? -3.05700  15.26600 13.03900  1.000 21.28173 ? 150 ILE B CA  1 
ATOM   2681 C  C   . ILE B 1 151 ? -3.32100  16.09200 14.29900  1.000 22.24547 ? 150 ILE B C   1 
ATOM   2682 O  O   . ILE B 1 151 ? -2.93400  17.26500 14.38300  1.000 23.61049 ? 150 ILE B O   1 
ATOM   2683 C  CB  . ILE B 1 151 ? -4.31300  15.17800 12.14900  1.000 21.51851 ? 150 ILE B CB  1 
ATOM   2684 C  CG1 . ILE B 1 151 ? -3.97300  14.53900 10.79900  1.000 27.96525 ? 150 ILE B CG1 1 
ATOM   2685 C  CG2 . ILE B 1 151 ? -4.94600  16.59100 11.92400  1.000 23.69866 ? 150 ILE B CG2 1 
ATOM   2686 C  CD1 . ILE B 1 151 ? -5.21000  14.13700 10.01000  1.000 28.27545 ? 150 ILE B CD1 1 
ATOM   2687 N  N   . LEU B 1 152 ? -4.02400  15.52000 15.27500  1.000 22.18426 ? 151 LEU B N   1 
ATOM   2688 C  CA  . LEU B 1 152 ? -4.31100  16.26100 16.50600  1.000 21.11559 ? 151 LEU B CA  1 
ATOM   2689 C  C   . LEU B 1 152 ? -3.02900  16.63200 17.23700  1.000 22.53568 ? 151 LEU B C   1 
ATOM   2690 O  O   . LEU B 1 152 ? -2.90800  17.73700 17.78600  1.000 22.56455 ? 151 LEU B O   1 
ATOM   2691 C  CB  . LEU B 1 152 ? -5.21600  15.43800 17.42200  1.000 23.91573 ? 151 LEU B CB  1 
ATOM   2692 C  CG  . LEU B 1 152 ? -6.62100  15.23900 16.85600  1.000 24.96017 ? 151 LEU B CG  1 
ATOM   2693 C  CD1 . LEU B 1 152 ? -7.31400  14.15300 17.70200  1.000 25.01807 ? 151 LEU B CD1 1 
ATOM   2694 C  CD2 . LEU B 1 152 ? -7.43300  16.56000 16.85400  1.000 21.85789 ? 151 LEU B CD2 1 
ATOM   2695 N  N   . GLY B 1 153 ? -2.06700  15.71600 17.27900  1.000 25.13897 ? 152 GLY B N   1 
ATOM   2696 C  CA  . GLY B 1 153 ? -0.80800  16.05300 17.91900  1.000 24.79389 ? 152 GLY B CA  1 
ATOM   2697 C  C   . GLY B 1 153 ? -0.07200  17.15200 17.18400  1.000 23.24955 ? 152 GLY B C   1 
ATOM   2698 O  O   . GLY B 1 153 ? 0.48300   18.05900 17.81000  1.000 26.08720 ? 152 GLY B O   1 
ATOM   2699 N  N   . HIS B 1 154 ? -0.08000  17.11000 15.84800  1.000 22.40366 ? 153 HIS B N   1 
ATOM   2700 C  CA  . HIS B 1 154 ? 0.64800   18.14600 15.11900  1.000 26.56557 ? 153 HIS B CA  1 
ATOM   2701 C  C   . HIS B 1 154 ? -0.02900  19.49900 15.30100  1.000 24.11695 ? 153 HIS B C   1 
ATOM   2702 O  O   . HIS B 1 154 ? 0.64700   20.53000 15.43800  1.000 26.56163 ? 153 HIS B O   1 
ATOM   2703 C  CB  . HIS B 1 154 ? 0.79400   17.76700 13.63800  1.000 26.40521 ? 153 HIS B CB  1 
ATOM   2704 C  CG  . HIS B 1 154 ? 1.69600   18.68600 12.86800  1.000 24.11833 ? 153 HIS B CG  1 
ATOM   2705 N  ND1 . HIS B 1 154 ? 1.26200   19.41000 11.78100  1.000 26.00566 ? 153 HIS B ND1 1 
ATOM   2706 C  CD2 . HIS B 1 154 ? 3.00300   19.00400 13.03500  1.000 28.94144 ? 153 HIS B CD2 1 
ATOM   2707 C  CE1 . HIS B 1 154 ? 2.26000   20.13600 11.30800  1.000 28.59565 ? 153 HIS B CE1 1 
ATOM   2708 N  NE2 . HIS B 1 154 ? 3.33100   19.90000 12.04400  1.000 27.71570 ? 153 HIS B NE2 1 
ATOM   2709 N  N   . GLU B 1 155 ? -1.37100  19.51300 15.36200  1.000 20.41115 ? 154 GLU B N   1 
ATOM   2710 C  CA  . GLU B 1 155 ? -2.08700  20.74400 15.70200  1.000 22.79127 ? 154 GLU B CA  1 
ATOM   2711 C  C   . GLU B 1 155 ? -1.56100  21.32700 17.00700  1.000 22.52867 ? 154 GLU B C   1 
ATOM   2712 O  O   . GLU B 1 155 ? -1.35300  22.54300 17.12200  1.000 24.75262 ? 154 GLU B O   1 
ATOM   2713 C  CB  . GLU B 1 155 ? -3.59500  20.47400 15.81200  1.000 21.12081 ? 154 GLU B CB  1 
ATOM   2714 C  CG  . GLU B 1 155 ? -4.28100  20.22300 14.45700  1.000 21.06767 ? 154 GLU B CG  1 
ATOM   2715 C  CD  . GLU B 1 155 ? -5.77200  19.87800 14.58200  1.000 21.96485 ? 154 GLU B CD  1 
ATOM   2716 O  OE1 . GLU B 1 155 ? -6.29700  19.79800 15.71600  1.000 22.53344 ? 154 GLU B OE1 1 
ATOM   2717 O  OE2 . GLU B 1 155 ? -6.41400  19.69800 13.53200  1.000 23.17424 ? 154 GLU B OE2 1 
ATOM   2718 N  N   . GLN B 1 156 ? -1.36700  20.49000 18.02200  1.000 23.07926 ? 155 GLN B N   1 
ATOM   2719 C  CA  . GLN B 1 156 ? -0.91000  21.05300 19.28800  1.000 25.43199 ? 155 GLN B CA  1 
ATOM   2720 C  C   . GLN B 1 156 ? 0.47900   21.66100 19.14700  1.000 29.93731 ? 155 GLN B C   1 
ATOM   2721 O  O   . GLN B 1 156 ? 0.78600   22.67100 19.79700  1.000 32.30724 ? 155 GLN B O   1 
ATOM   2722 C  CB  . GLN B 1 156 ? -0.92700  19.98000 20.37300  1.000 30.02780 ? 155 GLN B CB  1 
ATOM   2723 C  CG  . GLN B 1 156 ? -2.33400  19.41900 20.63100  1.000 31.35099 ? 155 GLN B CG  1 
ATOM   2724 C  CD  . GLN B 1 156 ? -2.33000  18.11700 21.43300  1.000 48.78240 ? 155 GLN B CD  1 
ATOM   2725 O  OE1 . GLN B 1 156 ? -1.32800  17.74300 22.05800  1.000 56.34871 ? 155 GLN B OE1 1 
ATOM   2726 N  NE2 . GLN B 1 156 ? -3.46000  17.42100 21.41600  1.000 49.71913 ? 155 GLN B NE2 1 
ATOM   2727 N  N   . GLU B 1 157 ? 1.30100   21.10200 18.26500  1.000 26.16092 ? 156 GLU B N   1 
ATOM   2728 C  CA  . GLU B 1 157 ? 2.66600   21.59100 18.12100  1.000 23.91610 ? 156 GLU B CA  1 
ATOM   2729 C  C   . GLU B 1 157 ? 2.70200   22.97500 17.49600  1.000 28.22053 ? 156 GLU B C   1 
ATOM   2730 O  O   . GLU B 1 157 ? 3.66500   23.72400 17.71800  1.000 30.76903 ? 156 GLU B O   1 
ATOM   2731 C  CB  . GLU B 1 157 ? 3.49100   20.62300 17.26900  1.000 27.05542 ? 156 GLU B CB  1 
ATOM   2732 C  CG  . GLU B 1 157 ? 3.64100   19.23200 17.87000  1.000 39.07968 ? 156 GLU B CG  1 
ATOM   2733 C  CD  . GLU B 1 157 ? 4.46200   18.29600 16.99100  1.000 40.75264 ? 156 GLU B CD  1 
ATOM   2734 O  OE1 . GLU B 1 157 ? 5.19400   18.77500 16.08900  1.000 34.87456 ? 156 GLU B OE1 1 
ATOM   2735 O  OE2 . GLU B 1 157 ? 4.36600   17.06800 17.21000  1.000 38.40398 ? 156 GLU B OE2 1 
ATOM   2736 N  N   . ILE B 1 158 ? 1.67700   23.31700 16.71300  1.000 27.82996 ? 157 ILE B N   1 
ATOM   2737 C  CA  . ILE B 1 158 ? 1.69500   24.51800 15.89600  1.000 27.46713 ? 157 ILE B CA  1 
ATOM   2738 C  C   . ILE B 1 158 ? 0.77200   25.60700 16.44400  1.000 30.06221 ? 157 ILE B C   1 
ATOM   2739 O  O   . ILE B 1 158 ? 0.52300   26.60000 15.75300  1.000 30.44126 ? 157 ILE B O   1 
ATOM   2740 C  CB  . ILE B 1 158 ? 1.37100   24.20500 14.42800  1.000 26.27405 ? 157 ILE B CB  1 
ATOM   2741 C  CG1 . ILE B 1 158 ? -0.06000  23.65900 14.30600  1.000 26.50274 ? 157 ILE B CG1 1 
ATOM   2742 C  CG2 . ILE B 1 158 ? 2.41900   23.26700 13.82500  1.000 29.02712 ? 157 ILE B CG2 1 
ATOM   2743 C  CD1 . ILE B 1 158 ? -0.51500  23.45400 12.86400  1.000 30.48411 ? 157 ILE B CD1 1 
ATOM   2744 N  N   . GLY B 1 159 ? 0.26400   25.46500 17.67300  1.000 28.72615 ? 158 GLY B N   1 
ATOM   2745 C  CA  . GLY B 1 159 ? -0.43700  26.55300 18.35100  1.000 28.68930 ? 158 GLY B CA  1 
ATOM   2746 C  C   . GLY B 1 159 ? -1.86200  26.27900 18.79800  1.000 24.64591 ? 158 GLY B C   1 
ATOM   2747 O  O   . GLY B 1 159 ? -2.45100  27.12500 19.49400  1.000 30.12397 ? 158 GLY B O   1 
ATOM   2748 N  N   . PHE B 1 160 ? -2.47200  25.13700 18.43900  1.000 23.33805 ? 159 PHE B N   1 
ATOM   2749 C  CA  . PHE B 1 160 ? -3.82600  24.84000 18.90800  1.000 23.89559 ? 159 PHE B CA  1 
ATOM   2750 C  C   . PHE B 1 160 ? -3.79900  24.37400 20.36400  1.000 30.84556 ? 159 PHE B C   1 
ATOM   2751 O  O   . PHE B 1 160 ? -2.84400  23.73600 20.81400  1.000 33.86220 ? 159 PHE B O   1 
ATOM   2752 C  CB  . PHE B 1 160 ? -4.48100  23.74500 18.05100  1.000 24.63513 ? 159 PHE B CB  1 
ATOM   2753 C  CG  . PHE B 1 160 ? -4.82100  24.16100 16.62700  1.000 23.62716 ? 159 PHE B CG  1 
ATOM   2754 C  CD1 . PHE B 1 160 ? -3.85900  24.07300 15.63100  1.000 24.49571 ? 159 PHE B CD1 1 
ATOM   2755 C  CD2 . PHE B 1 160 ? -6.11100  24.58400 16.29100  1.000 26.48943 ? 159 PHE B CD2 1 
ATOM   2756 C  CE1 . PHE B 1 160 ? -4.16700  24.43100 14.29600  1.000 27.34672 ? 159 PHE B CE1 1 
ATOM   2757 C  CE2 . PHE B 1 160 ? -6.44700  24.92300 14.96600  1.000 28.01142 ? 159 PHE B CE2 1 
ATOM   2758 C  CZ  . PHE B 1 160 ? -5.46000  24.85300 13.96800  1.000 25.60154 ? 159 PHE B CZ  1 
ATOM   2759 N  N   . ALA B 1 161 ? -4.85000  24.72000 21.10000  1.000 29.93285 ? 160 ALA B N   1 
ATOM   2760 C  CA  . ALA B 1 161 ? -5.04600  24.23000 22.46200  1.000 31.18552 ? 160 ALA B CA  1 
ATOM   2761 C  C   . ALA B 1 161 ? -5.65900  22.83400 22.38500  1.000 32.68841 ? 160 ALA B C   1 
ATOM   2762 O  O   . ALA B 1 161 ? -6.67600  22.64600 21.72300  1.000 30.36312 ? 160 ALA B O   1 
ATOM   2763 C  CB  . ALA B 1 161 ? -5.96000  25.17100 23.25000  1.000 34.19696 ? 160 ALA B CB  1 
ATOM   2764 N  N   . ALA B 1 162 ? -5.05300  21.86700 23.08000  1.000 40.87580 ? 161 ALA B N   1 
ATOM   2765 C  CA  . ALA B 1 162 ? -5.46500  20.47000 22.94200  1.000 42.80807 ? 161 ALA B CA  1 
ATOM   2766 C  C   . ALA B 1 162 ? -6.95400  20.28900 23.21400  1.000 36.88616 ? 161 ALA B C   1 
ATOM   2767 O  O   . ALA B 1 162 ? -7.67000  19.67800 22.40500  1.000 34.31195 ? 161 ALA B O   1 
ATOM   2768 C  CB  . ALA B 1 162 ? -4.63800  19.58700 23.88300  1.000 42.50497 ? 161 ALA B CB  1 
ATOM   2769 N  N   . ASP B 1 163 ? -7.44200  20.82000 24.35000  1.000 38.33528 ? 162 ASP B N   1 
ATOM   2770 C  CA  . ASP B 1 163 ? -8.84000  20.62100 24.73500  1.000 36.86793 ? 162 ASP B CA  1 
ATOM   2771 C  C   . ASP B 1 163 ? -9.82800  21.29700 23.79200  1.000 40.58576 ? 162 ASP B C   1 
ATOM   2772 O  O   . ASP B 1 163 ? -11.03100 21.04400 23.90300  1.000 44.26591 ? 162 ASP B O   1 
ATOM   2773 C  CB  . ASP B 1 163 ? -9.09000  21.12100 26.15800  1.000 48.06701 ? 162 ASP B CB  1 
ATOM   2774 C  CG  . ASP B 1 163 ? -8.57000  20.16600 27.21200  1.000 56.30874 ? 162 ASP B CG  1 
ATOM   2775 O  OD1 . ASP B 1 163 ? -8.21600  19.02300 26.86000  1.000 50.70038 ? 162 ASP B OD1 1 
ATOM   2776 O  OD2 . ASP B 1 163 ? -8.50100  20.56800 28.40000  1.000 59.83201 ? 162 ASP B OD2 1 
ATOM   2777 N  N   . SER B 1 164 ? -9.36200  22.12800 22.86000  1.000 32.07456 ? 163 SER B N   1 
ATOM   2778 C  CA  . SER B 1 164 ? -10.27900 22.84300 21.99900  1.000 30.65901 ? 163 SER B CA  1 
ATOM   2779 C  C   . SER B 1 164 ? -10.62100 22.07200 20.73700  1.000 28.14653 ? 163 SER B C   1 
ATOM   2780 O  O   . SER B 1 164 ? -11.51200 22.49900 20.01200  1.000 28.24847 ? 163 SER B O   1 
ATOM   2781 C  CB  . SER B 1 164 ? -9.69200  24.21500 21.61300  1.000 31.13281 ? 163 SER B CB  1 
ATOM   2782 O  OG  . SER B 1 164 ? -8.59400  24.06600 20.74400  1.000 32.61961 ? 163 SER B OG  1 
ATOM   2783 N  N   . ARG B 1 165 ? -9.94500  20.95400 20.47000  1.000 26.35434 ? 164 ARG B N   1 
ATOM   2784 C  CA  . ARG B 1 165 ? -10.05400 20.25300 19.19400  1.000 24.19101 ? 164 ARG B CA  1 
ATOM   2785 C  C   . ARG B 1 165 ? -10.51700 18.82400 19.41700  1.000 24.23579 ? 164 ARG B C   1 
ATOM   2786 O  O   . ARG B 1 165 ? -10.29400 18.25600 20.48900  1.000 27.21351 ? 164 ARG B O   1 
ATOM   2787 C  CB  . ARG B 1 165 ? -8.70100  20.20800 18.47600  1.000 22.42327 ? 164 ARG B CB  1 
ATOM   2788 C  CG  . ARG B 1 165 ? -8.09500  21.60200 18.18600  1.000 24.72263 ? 164 ARG B CG  1 
ATOM   2789 C  CD  . ARG B 1 165 ? -8.86200  22.28000 17.07400  1.000 24.82130 ? 164 ARG B CD  1 
ATOM   2790 N  NE  . ARG B 1 165 ? -8.54600  21.68100 15.77200  1.000 23.01162 ? 164 ARG B NE  1 
ATOM   2791 C  CZ  . ARG B 1 165 ? -8.99200  22.18800 14.61800  1.000 21.04286 ? 164 ARG B CZ  1 
ATOM   2792 N  NH1 . ARG B 1 165 ? -9.78100  23.24400 14.61600  1.000 23.76614 ? 164 ARG B NH1 1 
ATOM   2793 N  NH2 . ARG B 1 165 ? -8.67400  21.62000 13.46100  1.000 23.03453 ? 164 ARG B NH2 1 
ATOM   2794 N  N   . CYS B 1 166 ? -11.10100 18.22000 18.37200  1.000 24.26652 ? 165 CYS B N   1 
ATOM   2795 C  CA  . CYS B 1 166 ? -11.48300 16.81100 18.38900  1.000 25.44845 ? 165 CYS B CA  1 
ATOM   2796 C  C   . CYS B 1 166 ? -11.41600 16.24700 16.97700  1.000 23.44791 ? 165 CYS B C   1 
ATOM   2797 O  O   . CYS B 1 166 ? -11.53600 16.97600 15.99100  1.000 23.89296 ? 165 CYS B O   1 
ATOM   2798 C  CB  . CYS B 1 166 ? -12.90300 16.58100 18.94900  1.000 37.79756 ? 165 CYS B CB  1 
ATOM   2799 S  SG  . CYS B 1 166 ? -14.30500 17.51400 18.11200  1.000 38.58069 ? 165 CYS B SG  1 
ATOM   2800 N  N   . ALA B 1 167 ? -11.23000 14.93500 16.89600  1.000 24.49132 ? 166 ALA B N   1 
ATOM   2801 C  CA  . ALA B 1 167 ? -11.43900 14.18400 15.66600  1.000 20.57747 ? 166 ALA B CA  1 
ATOM   2802 C  C   . ALA B 1 167 ? -12.86000 13.63000 15.65000  1.000 21.36836 ? 166 ALA B C   1 
ATOM   2803 O  O   . ALA B 1 167 ? -13.42800 13.31600 16.69400  1.000 23.29309 ? 166 ALA B O   1 
ATOM   2804 C  CB  . ALA B 1 167 ? -10.45200 13.00500 15.55600  1.000 25.70295 ? 166 ALA B CB  1 
HETATM 2805 N  N   . MSE B 1 168 ? -13.41600 13.49700 14.44800  1.000 20.70788 ? 167 MSE B N   1 
HETATM 2806 C  CA  . MSE B 1 168 ? -14.77200 12.96800 14.28300  1.000 22.54044 ? 167 MSE B CA  1 
HETATM 2807 C  C   . MSE B 1 168 ? -14.84700 11.98900 13.11000  1.000 21.63548 ? 167 MSE B C   1 
HETATM 2808 O  O   . MSE B 1 168 ? -14.10700 12.11300 12.14600  1.000 22.23220 ? 167 MSE B O   1 
HETATM 2809 C  CB  . MSE B 1 168 ? -15.77100 14.09900 14.04000  1.000 23.85058 ? 167 MSE B CB  1 
HETATM 2810 C  CG  . MSE B 1 168 ? -15.75700 15.22000 15.10200  1.000 23.61985 ? 167 MSE B CG  1 
HETATM 2811 SE SE  . MSE B 1 168 ? -17.11500 16.61500 14.82400  1.000 29.42716 ? 167 MSE B SE  1 
HETATM 2812 C  CE  . MSE B 1 168 ? -18.56800 15.85400 15.81900  1.000 26.72126 ? 167 MSE B CE  1 
ATOM   2813 N  N   . ARG B 1 169 ? -15.79300 11.06000 13.17800  1.000 22.71784 ? 168 ARG B N   1 
ATOM   2814 C  CA  . ARG B 1 169 ? -15.96900 10.08900 12.11000  1.000 23.06803 ? 168 ARG B CA  1 
ATOM   2815 C  C   . ARG B 1 169 ? -17.45600 9.91500  11.82900  1.000 24.36266 ? 168 ARG B C   1 
ATOM   2816 O  O   . ARG B 1 169 ? -18.26000 9.79800  12.76400  1.000 26.14442 ? 168 ARG B O   1 
ATOM   2817 C  CB  . ARG B 1 169 ? -15.33400 8.73100  12.48800  1.000 24.93820 ? 168 ARG B CB  1 
ATOM   2818 C  CG  . ARG B 1 169 ? -15.29800 7.74800  11.31400  1.000 24.02554 ? 168 ARG B CG  1 
ATOM   2819 C  CD  . ARG B 1 169 ? -14.62100 6.45100  11.73200  1.000 26.19609 ? 168 ARG B CD  1 
ATOM   2820 N  NE  . ARG B 1 169 ? -13.19700 6.60600  11.99700  1.000 26.31533 ? 168 ARG B NE  1 
ATOM   2821 C  CZ  . ARG B 1 169 ? -12.63000 6.43200  13.19000  1.000 29.33368 ? 168 ARG B CZ  1 
ATOM   2822 N  NH1 . ARG B 1 169 ? -13.36900 6.13300  14.24900  1.000 29.95075 ? 168 ARG B NH1 1 
ATOM   2823 N  NH2 . ARG B 1 169 ? -11.31600 6.56900  13.33700  1.000 32.92846 ? 168 ARG B NH2 1 
ATOM   2824 N  N   . LEU B 1 170 ? -17.80700 9.87300  10.53600  1.000 25.00738 ? 169 LEU B N   1 
ATOM   2825 C  CA  . LEU B 1 170 ? -19.13800 9.48000  10.06300  1.000 23.87154 ? 169 LEU B CA  1 
ATOM   2826 C  C   . LEU B 1 170 ? -18.98200 8.12400  9.38400   1.000 24.67836 ? 169 LEU B C   1 
ATOM   2827 O  O   . LEU B 1 170 ? -18.40700 8.04100  8.29700   1.000 25.34745 ? 169 LEU B O   1 
ATOM   2828 C  CB  . LEU B 1 170 ? -19.71400 10.53300 9.09900   1.000 23.66783 ? 169 LEU B CB  1 
ATOM   2829 C  CG  . LEU B 1 170 ? -21.03600 10.12700 8.39300   1.000 24.84888 ? 169 LEU B CG  1 
ATOM   2830 C  CD1 . LEU B 1 170 ? -22.15900 9.91100  9.36400   1.000 28.36306 ? 169 LEU B CD1 1 
ATOM   2831 C  CD2 . LEU B 1 170 ? -21.43700 11.18700 7.37400   1.000 25.35684 ? 169 LEU B CD2 1 
ATOM   2832 N  N   . VAL B 1 171 ? -19.48400 7.05500  10.02000  1.000 26.01022 ? 170 VAL B N   1 
ATOM   2833 C  CA  . VAL B 1 171 ? -19.38200 5.70600  9.45400   1.000 27.35291 ? 170 VAL B CA  1 
ATOM   2834 C  C   . VAL B 1 171 ? -20.49300 5.49800  8.43200   1.000 28.04065 ? 170 VAL B C   1 
ATOM   2835 O  O   . VAL B 1 171 ? -21.66900 5.76000  8.71100   1.000 28.76205 ? 170 VAL B O   1 
ATOM   2836 C  CB  . VAL B 1 171 ? -19.44600 4.63400  10.55300  1.000 29.07411 ? 170 VAL B CB  1 
ATOM   2837 C  CG1 . VAL B 1 171 ? -19.49800 3.22500  9.92000   1.000 31.04108 ? 170 VAL B CG1 1 
ATOM   2838 C  CG2 . VAL B 1 171 ? -18.23300 4.75200  11.47200  1.000 29.05217 ? 170 VAL B CG2 1 
ATOM   2839 N  N   . LEU B 1 172 ? -20.11000 4.99900  7.26500   1.000 28.61881 ? 171 LEU B N   1 
ATOM   2840 C  CA  . LEU B 1 172 ? -21.05700 4.71300  6.20500   1.000 29.67895 ? 171 LEU B CA  1 
ATOM   2841 C  C   . LEU B 1 172 ? -21.44700 3.24800  6.29400   1.000 35.05529 ? 171 LEU B C   1 
ATOM   2842 O  O   . LEU B 1 172 ? -20.62300 2.36500  6.08200   1.000 36.62438 ? 171 LEU B O   1 
ATOM   2843 C  CB  . LEU B 1 172 ? -20.44400 4.99400  4.84100   1.000 30.31795 ? 171 LEU B CB  1 
ATOM   2844 C  CG  . LEU B 1 172 ? -20.01800 6.43300  4.56400   1.000 30.26516 ? 171 LEU B CG  1 
ATOM   2845 C  CD1 . LEU B 1 172 ? -19.32400 6.52700  3.21600   1.000 30.42735 ? 171 LEU B CD1 1 
ATOM   2846 C  CD2 . LEU B 1 172 ? -21.21300 7.36300  4.62500   1.000 28.48622 ? 171 LEU B CD2 1 
ATOM   2847 N  N   . GLY B 1 173 ? -22.69400 3.00200  6.65700   1.000 33.83778 ? 172 GLY B N   1 
ATOM   2848 C  CA  . GLY B 1 173 ? -23.20900 1.65200  6.76700   1.000 41.54293 ? 172 GLY B CA  1 
ATOM   2849 C  C   . GLY B 1 173 ? -23.40300 0.98700  5.41800   1.000 49.76343 ? 172 GLY B C   1 
ATOM   2850 O  O   . GLY B 1 173 ? -23.69400 1.65000  4.42500   1.000 50.65292 ? 172 GLY B O   1 
ATOM   2851 N  N   . SER B 1 174 ? -23.24700 -0.33200 5.38500   1.000 50.19295 ? 173 SER B N   1 
ATOM   2852 C  CA  . SER B 1 174 ? -23.41600 -1.08300 4.15000   1.000 54.05943 ? 173 SER B CA  1 
ATOM   2853 C  C   . SER B 1 174 ? -24.84000 -1.61700 4.00100   1.000 55.09851 ? 173 SER B C   1 
ATOM   2854 O  O   . SER B 1 174 ? -25.65800 -1.55100 4.91600   1.000 48.95527 ? 173 SER B O   1 
ATOM   2855 C  CB  . SER B 1 174 ? -22.40900 -2.23100 4.07800   1.000 59.81385 ? 173 SER B CB  1 
ATOM   2856 O  OG  . SER B 1 174 ? -22.62600 -3.16400 5.11800   1.000 63.95238 ? 173 SER B OG  1 
ATOM   2857 O  OXT . SER B 1 174 ? -25.21000 -2.12600 2.95000   1.000 50.89966 ? 173 SER B OXT 1 
HETATM 2858 N  N1A . ACO C 2 .   ? -32.88900 21.84600 2.64000   1.000 38.69611 ? 201 ACO A N1A 1 
HETATM 2859 C  C2A . ACO C 2 .   ? -33.81000 22.75500 2.98700   1.000 41.83956 ? 201 ACO A C2A 1 
HETATM 2860 N  N3A . ACO C 2 .   ? -34.73200 23.22900 2.14500   1.000 49.88890 ? 201 ACO A N3A 1 
HETATM 2861 C  C4A . ACO C 2 .   ? -34.77500 22.79600 0.86800   1.000 42.55271 ? 201 ACO A C4A 1 
HETATM 2862 C  C5A . ACO C 2 .   ? -33.80200 21.80200 0.41600   1.000 36.18060 ? 201 ACO A C5A 1 
HETATM 2863 C  C6A . ACO C 2 .   ? -32.81900 21.33300 1.40200   1.000 41.14347 ? 201 ACO A C6A 1 
HETATM 2864 N  N6A . ACO C 2 .   ? -31.88400 20.41600 1.07000   1.000 39.36217 ? 201 ACO A N6A 1 
HETATM 2865 N  N7A . ACO C 2 .   ? -34.07300 21.55100 -0.87100  1.000 40.79852 ? 201 ACO A N7A 1 
HETATM 2866 C  C8A . ACO C 2 .   ? -35.12300 22.32400 -1.21500  1.000 39.85110 ? 201 ACO A C8A 1 
HETATM 2867 N  N9A . ACO C 2 .   ? -35.53800 23.06500 -0.18200  1.000 40.88695 ? 201 ACO A N9A 1 
HETATM 2868 C  C1B . ACO C 2 .   ? -36.66800 24.01100 -0.18000  1.000 47.75509 ? 201 ACO A C1B 1 
HETATM 2869 C  C2B . ACO C 2 .   ? -36.28400 25.34200 -0.78700  1.000 48.45432 ? 201 ACO A C2B 1 
HETATM 2870 O  O2B . ACO C 2 .   ? -35.74800 26.21700 0.20000   1.000 56.57712 ? 201 ACO A O2B 1 
HETATM 2871 C  C3B . ACO C 2 .   ? -37.59100 25.85400 -1.33900  1.000 48.54526 ? 201 ACO A C3B 1 
HETATM 2872 O  O3B . ACO C 2 .   ? -38.29700 26.58900 -0.35400  1.000 55.99301 ? 201 ACO A O3B 1 
HETATM 2873 P  P3B . ACO C 2 .   ? -38.44900 28.17200 -0.48900  1.000 70.61368 ? 201 ACO A P3B 1 
HETATM 2874 O  O7A . ACO C 2 .   ? -39.61100 28.35000 -1.42300  1.000 72.80688 ? 201 ACO A O7A 1 
HETATM 2875 O  O8A . ACO C 2 .   ? -38.71100 28.62300 0.92300   1.000 74.79349 ? 201 ACO A O8A 1 
HETATM 2876 O  O9A . ACO C 2 .   ? -37.12000 28.59600 -1.04200  1.000 66.84783 ? 201 ACO A O9A 1 
HETATM 2877 C  C4B . ACO C 2 .   ? -38.38700 24.60100 -1.63100  1.000 37.72125 ? 201 ACO A C4B 1 
HETATM 2878 O  O4B . ACO C 2 .   ? -37.70700 23.51700 -1.01100  1.000 43.77710 ? 201 ACO A O4B 1 
HETATM 2879 C  C5B . ACO C 2 .   ? -38.47400 24.37100 -3.12100  1.000 39.10378 ? 201 ACO A C5B 1 
HETATM 2880 O  O5B . ACO C 2 .   ? -37.16300 24.30700 -3.64900  1.000 30.05634 ? 201 ACO A O5B 1 
HETATM 2881 P  P1A . ACO C 2 .   ? -36.99600 23.88000 -5.16900  1.000 25.16962 ? 201 ACO A P1A 1 
HETATM 2882 O  O1A . ACO C 2 .   ? -35.65900 24.34000 -5.65300  1.000 26.81229 ? 201 ACO A O1A 1 
HETATM 2883 O  O2A . ACO C 2 .   ? -38.24300 24.28100 -5.88800  1.000 25.25860 ? 201 ACO A O2A 1 
HETATM 2884 O  O3A . ACO C 2 .   ? -37.00100 22.29800 -4.96900  1.000 25.56061 ? 201 ACO A O3A 1 
HETATM 2885 P  P2A . ACO C 2 .   ? -36.05200 21.24100 -5.68900  1.000 24.08738 ? 201 ACO A P2A 1 
HETATM 2886 O  O4A . ACO C 2 .   ? -34.81400 21.04700 -4.87700  1.000 24.04086 ? 201 ACO A O4A 1 
HETATM 2887 O  O5A . ACO C 2 .   ? -35.95800 21.53100 -7.15400  1.000 24.35071 ? 201 ACO A O5A 1 
HETATM 2888 O  O6A . ACO C 2 .   ? -37.01400 19.97400 -5.50500  1.000 23.90911 ? 201 ACO A O6A 1 
HETATM 2889 C  CBP . ACO C 2 .   ? -37.35500 18.04600 -4.11500  1.000 21.27107 ? 201 ACO A CBP 1 
HETATM 2890 C  CCP . ACO C 2 .   ? -37.37700 19.56100 -4.19900  1.000 26.14304 ? 201 ACO A CCP 1 
HETATM 2891 C  CDP . ACO C 2 .   ? -38.10100 17.41800 -5.27800  1.000 25.30166 ? 201 ACO A CDP 1 
HETATM 2892 C  CEP . ACO C 2 .   ? -37.98800 17.62100 -2.79900  1.000 27.11194 ? 201 ACO A CEP 1 
HETATM 2893 C  CAP . ACO C 2 .   ? -35.88400 17.65500 -4.14900  1.000 23.30909 ? 201 ACO A CAP 1 
HETATM 2894 O  OAP . ACO C 2 .   ? -35.23400 18.32800 -3.07600  1.000 27.90111 ? 201 ACO A OAP 1 
HETATM 2895 C  C9P . ACO C 2 .   ? -35.66700 16.17600 -4.00600  1.000 20.31783 ? 201 ACO A C9P 1 
HETATM 2896 O  O9P . ACO C 2 .   ? -35.66400 15.46000 -4.98000  1.000 21.84567 ? 201 ACO A O9P 1 
HETATM 2897 N  N8P . ACO C 2 .   ? -35.47600 15.71700 -2.77900  1.000 21.77997 ? 201 ACO A N8P 1 
HETATM 2898 C  C7P . ACO C 2 .   ? -35.12500 14.34000 -2.50400  1.000 22.48775 ? 201 ACO A C7P 1 
HETATM 2899 C  C6P . ACO C 2 .   ? -36.23100 13.35900 -2.88200  1.000 22.87008 ? 201 ACO A C6P 1 
HETATM 2900 C  C5P . ACO C 2 .   ? -37.51700 13.72000 -2.18300  1.000 22.31472 ? 201 ACO A C5P 1 
HETATM 2901 O  O5P . ACO C 2 .   ? -37.54700 13.94500 -0.99400  1.000 25.24669 ? 201 ACO A O5P 1 
HETATM 2902 N  N4P . ACO C 2 .   ? -38.60200 13.77100 -2.93800  1.000 22.63098 ? 201 ACO A N4P 1 
HETATM 2903 C  C3P . ACO C 2 .   ? -39.89900 14.05600 -2.36600  1.000 23.26534 ? 201 ACO A C3P 1 
HETATM 2904 C  C2P . ACO C 2 .   ? -40.67300 12.78900 -2.04600  1.000 27.56431 ? 201 ACO A C2P 1 
HETATM 2905 S  S1P . ACO C 2 .   ? -42.27200 13.18300 -1.42000  1.000 27.27156 ? 201 ACO A S1P 1 
HETATM 2906 C  C   . ACO C 2 .   ? -43.21000 12.82300 -2.74500  1.000 29.24498 ? 201 ACO A C   1 
HETATM 2907 O  O   . ACO C 2 .   ? -42.67500 12.46600 -3.77000  1.000 26.57855 ? 201 ACO A O   1 
HETATM 2908 C  CH3 . ACO C 2 .   ? -44.69500 12.96200 -2.63200  1.000 28.90144 ? 201 ACO A CH3 1 
HETATM 2909 NA NA  . NA  D 3 .   ? -64.21700 16.19400 -11.18900 0.500 18.78488 ? 202 NA  A NA  1 
HETATM 2910 NA NA  . NA  E 3 .   ? -39.92800 6.57100  -4.56000  1.000 25.56873 ? 203 NA  A NA  1 
HETATM 2911 NA NA  . NA  F 3 .   ? -27.45400 2.63000  -3.62700  1.000 25.56195 ? 204 NA  A NA  1 
HETATM 2912 CL CL  . CL  G 4 .   ? -32.40400 12.50500 11.06000  1.000 45.42307 ? 205 CL  A CL  1 
HETATM 2913 N  N1A . ACO H 2 .   ? -23.32100 30.79700 14.13800  1.000 35.20623 ? 201 ACO B N1A 1 
HETATM 2914 C  C2A . ACO H 2 .   ? -24.02500 29.70200 14.47200  1.000 32.97133 ? 201 ACO B C2A 1 
HETATM 2915 N  N3A . ACO H 2 .   ? -24.35100 28.73400 13.60300  1.000 32.80089 ? 201 ACO B N3A 1 
HETATM 2916 C  C4A . ACO H 2 .   ? -23.96800 28.81900 12.31200  1.000 29.04672 ? 201 ACO B C4A 1 
HETATM 2917 C  C5A . ACO H 2 .   ? -23.19600 29.98200 11.87200  1.000 32.64386 ? 201 ACO B C5A 1 
HETATM 2918 C  C6A . ACO H 2 .   ? -22.88600 31.00500 12.88200  1.000 33.35722 ? 201 ACO B C6A 1 
HETATM 2919 N  N6A . ACO H 2 .   ? -22.18000 32.10000 12.53300  1.000 35.04357 ? 201 ACO B N6A 1 
HETATM 2920 N  N7A . ACO H 2 .   ? -22.95200 29.82500 10.56500  1.000 32.74188 ? 201 ACO B N7A 1 
HETATM 2921 C  C8A . ACO H 2 .   ? -23.51500 28.65800 10.19600  1.000 30.06790 ? 201 ACO B C8A 1 
HETATM 2922 N  N9A . ACO H 2 .   ? -24.11900 28.06600 11.23300  1.000 32.65700 ? 201 ACO B N9A 1 
HETATM 2923 C  C1B . ACO H 2 .   ? -24.82800 26.78000 11.17800  1.000 37.63625 ? 201 ACO B C1B 1 
HETATM 2924 C  C2B . ACO H 2 .   ? -26.13300 26.93300 10.42700  1.000 35.62166 ? 201 ACO B C2B 1 
HETATM 2925 O  O2B . ACO H 2 .   ? -27.19400 27.36700 11.27800  1.000 40.36985 ? 201 ACO B O2B 1 
HETATM 2926 C  C3B . ACO H 2 .   ? -26.35900 25.54000 9.88800   1.000 35.23882 ? 201 ACO B C3B 1 
HETATM 2927 O  O3B . ACO H 2 .   ? -27.04000 24.77000 10.85800  1.000 40.28863 ? 201 ACO B O3B 1 
HETATM 2928 P  P3B . ACO H 2 .   ? -28.31800 23.91000 10.44900  1.000 53.22206 ? 201 ACO B P3B 1 
HETATM 2929 O  O7A . ACO H 2 .   ? -28.06800 22.56700 11.07100  1.000 59.46657 ? 201 ACO B O7A 1 
HETATM 2930 O  O8A . ACO H 2 .   ? -29.44600 24.71800 11.01400  1.000 60.98149 ? 201 ACO B O8A 1 
HETATM 2931 O  O9A . ACO H 2 .   ? -28.28200 23.87800 8.95100   1.000 61.98596 ? 201 ACO B O9A 1 
HETATM 2932 C  C4B . ACO H 2 .   ? -24.96300 24.97500 9.72200   1.000 32.05026 ? 201 ACO B C4B 1 
HETATM 2933 O  O4B . ACO H 2 .   ? -24.07600 25.85700 10.40100  1.000 35.58308 ? 201 ACO B O4B 1 
HETATM 2934 C  C5B . ACO H 2 .   ? -24.60800 24.92100 8.25300   1.000 32.67697 ? 201 ACO B C5B 1 
HETATM 2935 O  O5B . ACO H 2 .   ? -24.94200 26.17700 7.69000   1.000 28.79261 ? 201 ACO B O5B 1 
HETATM 2936 P  P1A . ACO H 2 .   ? -24.69300 26.43600 6.14100   1.000 31.67689 ? 201 ACO B P1A 1 
HETATM 2937 O  O1A . ACO H 2 .   ? -25.24100 27.78100 5.79600   1.000 32.29270 ? 201 ACO B O1A 1 
HETATM 2938 O  O2A . ACO H 2 .   ? -25.09600 25.20800 5.37300   1.000 34.02462 ? 201 ACO B O2A 1 
HETATM 2939 O  O3A . ACO H 2 .   ? -23.10300 26.50100 6.21400   1.000 35.91344 ? 201 ACO B O3A 1 
HETATM 2940 P  P2A . ACO H 2 .   ? -22.20400 27.62900 5.54000   1.000 29.27311 ? 201 ACO B P2A 1 
HETATM 2941 O  O4A . ACO H 2 .   ? -22.23000 28.88800 6.34600   1.000 26.31816 ? 201 ACO B O4A 1 
HETATM 2942 O  O5A . ACO H 2 .   ? -22.50700 27.64900 4.07400   1.000 31.57516 ? 201 ACO B O5A 1 
HETATM 2943 O  O6A . ACO H 2 .   ? -20.78800 26.93000 5.75300   1.000 32.86901 ? 201 ACO B O6A 1 
HETATM 2944 C  CBP . ACO H 2 .   ? -18.83900 26.82700 7.11800   1.000 26.79688 ? 201 ACO B CBP 1 
HETATM 2945 C  CCP . ACO H 2 .   ? -20.34500 26.65400 7.07000   1.000 28.37107 ? 201 ACO B CCP 1 
HETATM 2946 C  CDP . ACO H 2 .   ? -18.19600 26.32400 5.83800   1.000 28.23053 ? 201 ACO B CDP 1 
HETATM 2947 C  CEP . ACO H 2 .   ? -18.26500 26.05400 8.29400   1.000 26.18626 ? 201 ACO B CEP 1 
HETATM 2948 C  CAP . ACO H 2 .   ? -18.61100 28.32600 7.28500   1.000 26.34130 ? 201 ACO B CAP 1 
HETATM 2949 O  OAP . ACO H 2 .   ? -19.25200 28.76100 8.48100   1.000 27.84310 ? 201 ACO B OAP 1 
HETATM 2950 C  C9P . ACO H 2 .   ? -17.15300 28.67600 7.32300   1.000 25.34961 ? 201 ACO B C9P 1 
HETATM 2951 O  O9P . ACO H 2 .   ? -16.53100 28.75900 6.29000   1.000 23.79907 ? 201 ACO B O9P 1 
HETATM 2952 N  N8P . ACO H 2 .   ? -16.61500 28.87600 8.51700   1.000 21.59958 ? 201 ACO B N8P 1 
HETATM 2953 C  C7P . ACO H 2 .   ? -15.25600 29.33900 8.69700   1.000 22.43322 ? 201 ACO B C7P 1 
HETATM 2954 C  C6P . ACO H 2 .   ? -14.22800 28.29000 8.30300   1.000 26.09018 ? 201 ACO B C6P 1 
HETATM 2955 C  C5P . ACO H 2 .   ? -14.48200 27.00200 9.04800   1.000 28.25038 ? 201 ACO B C5P 1 
HETATM 2956 O  O5P . ACO H 2 .   ? -14.66200 26.99800 10.24900  1.000 24.01188 ? 201 ACO B O5P 1 
HETATM 2957 N  N4P . ACO H 2 .   ? -14.48500 25.90000 8.31000   1.000 25.52536 ? 201 ACO B N4P 1 
HETATM 2958 C  C3P . ACO H 2 .   ? -14.62300 24.58400 8.89500   1.000 24.14963 ? 201 ACO B C3P 1 
HETATM 2959 C  C2P . ACO H 2 .   ? -13.28100 23.92300 9.16700   1.000 24.40886 ? 201 ACO B C2P 1 
HETATM 2960 S  S1P . ACO H 2 .   ? -13.52600 22.32300 9.87100   1.000 27.56504 ? 201 ACO B S1P 1 
HETATM 2961 C  C   . ACO H 2 .   ? -13.09500 21.37600 8.57700   1.000 31.42585 ? 201 ACO B C   1 
HETATM 2962 O  O   . ACO H 2 .   ? -12.80300 21.90800 7.53000   1.000 27.93681 ? 201 ACO B O   1 
HETATM 2963 C  CH3 . ACO H 2 .   ? -13.08600 19.89100 8.74200   1.000 28.60818 ? 201 ACO B CH3 1 
HETATM 2964 NA NA  . NA  I 3 .   ? -7.06600  25.21900 6.64500   1.000 23.69485 ? 202 NA  B NA  1 
HETATM 2965 NA NA  . NA  J 3 .   ? -20.55700 34.91900 8.70400   1.000 35.37998 ? 203 NA  B NA  1 
HETATM 2966 CL CL  . CL  K 4 .   ? -13.92200 32.50800 21.93300  1.000 36.82863 ? 204 CL  B CL  1 
HETATM 2967 O  O   . HOH L 5 .   ? -41.60500 27.60100 -0.70600  1.000 57.88076 ? 301 HOH A O   1 
HETATM 2968 O  O   . HOH L 5 .   ? -46.54100 5.43500  -26.57500 1.000 43.44166 ? 302 HOH A O   1 
HETATM 2969 O  O   . HOH L 5 .   ? -34.73700 15.23300 -23.89000 1.000 47.37647 ? 303 HOH A O   1 
HETATM 2970 O  O   A HOH L 5 .   ? -37.72500 12.38600 -25.36900 0.710 44.44913 ? 304 HOH A O   1 
HETATM 2971 O  O   . HOH L 5 .   ? -31.09800 18.70400 -0.30300  1.000 54.80207 ? 305 HOH A O   1 
HETATM 2972 O  O   . HOH L 5 .   ? -36.95200 27.65400 2.20400   1.000 46.98462 ? 306 HOH A O   1 
HETATM 2973 O  O   . HOH L 5 .   ? -31.83300 3.90500  -4.16600  1.000 49.95129 ? 307 HOH A O   1 
HETATM 2974 O  O   . HOH L 5 .   ? -65.37100 14.34200 -6.79600  1.000 38.38753 ? 308 HOH A O   1 
HETATM 2975 O  O   . HOH L 5 .   ? -33.42300 20.08300 -2.72500  1.000 50.25203 ? 309 HOH A O   1 
HETATM 2976 O  O   . HOH L 5 .   ? -41.36400 0.51200  9.96300   1.000 38.21305 ? 310 HOH A O   1 
HETATM 2977 O  O   . HOH L 5 .   ? -48.55500 4.06000  -25.91500 1.000 58.55302 ? 311 HOH A O   1 
HETATM 2978 O  O   . HOH L 5 .   ? -44.94400 8.32200  -25.03300 1.000 45.14677 ? 312 HOH A O   1 
HETATM 2979 O  O   . HOH L 5 .   ? -34.88300 11.73500 -23.33200 1.000 47.13542 ? 313 HOH A O   1 
HETATM 2980 O  O   . HOH L 5 .   ? -29.24000 4.29300  -3.97500  1.000 47.74297 ? 314 HOH A O   1 
HETATM 2981 O  O   . HOH L 5 .   ? -37.21700 28.32200 -3.55500  1.000 42.09729 ? 315 HOH A O   1 
HETATM 2982 O  O   . HOH L 5 .   ? -34.24200 22.63700 -8.65200  1.000 24.54259 ? 316 HOH A O   1 
HETATM 2983 O  O   . HOH L 5 .   ? -41.553   -5.912   6.344     1.000 41.77175 ? 317 HOH A O   1 
HETATM 2984 O  O   . HOH L 5 .   ? -27.30000 6.85600  -5.31600  1.000 44.85300 ? 318 HOH A O   1 
HETATM 2985 O  O   . HOH L 5 .   ? -29.39400 14.50900 -16.51200 1.000 50.02545 ? 319 HOH A O   1 
HETATM 2986 O  O   . HOH L 5 .   ? -31.17100 7.22600  -3.56900  1.000 36.82259 ? 320 HOH A O   1 
HETATM 2987 O  O   . HOH L 5 .   ? -60.32300 21.15900 -10.37500 1.000 37.49681 ? 321 HOH A O   1 
HETATM 2988 O  O   . HOH L 5 .   ? -47.99500 -6.31300 3.37000   1.000 32.15954 ? 322 HOH A O   1 
HETATM 2989 O  O   . HOH L 5 .   ? -42.88600 16.00100 -24.56700 1.000 36.14479 ? 323 HOH A O   1 
HETATM 2990 O  O   . HOH L 5 .   ? -45.62500 30.80400 -9.32300  1.000 34.56882 ? 324 HOH A O   1 
HETATM 2991 O  O   . HOH L 5 .   ? -48.679   1.127    -9.166    1.000 42.22808 ? 325 HOH A O   1 
HETATM 2992 O  O   . HOH L 5 .   ? -57.59900 8.30100  0.62700   1.000 28.60365 ? 326 HOH A O   1 
HETATM 2993 O  O   . HOH L 5 .   ? -44.555   -6.286   4.277     1.000 42.22209 ? 327 HOH A O   1 
HETATM 2994 O  O   . HOH L 5 .   ? -44.303   -4.977   -14.657   1.000 32.26341 ? 328 HOH A O   1 
HETATM 2995 O  O   . HOH L 5 .   ? -36.37200 -0.24600 -9.80200  1.000 49.11529 ? 329 HOH A O   1 
HETATM 2996 O  O   . HOH L 5 .   ? -26.47400 16.91500 -15.01000 1.000 50.94216 ? 330 HOH A O   1 
HETATM 2997 O  O   . HOH L 5 .   ? -62.73200 19.99700 1.21500   1.000 51.34568 ? 331 HOH A O   1 
HETATM 2998 O  O   . HOH L 5 .   ? -27.75500 4.71600  3.62900   1.000 45.76848 ? 332 HOH A O   1 
HETATM 2999 O  O   . HOH L 5 .   ? -54.91600 24.78400 0.53800   1.000 34.50780 ? 333 HOH A O   1 
HETATM 3000 O  O   . HOH L 5 .   ? -29.23200 11.87700 -19.81400 1.000 40.21861 ? 334 HOH A O   1 
HETATM 3001 O  O   . HOH L 5 .   ? -50.08600 -6.09800 7.41500   1.000 33.13738 ? 335 HOH A O   1 
HETATM 3002 O  O   . HOH L 5 .   ? -54.84600 17.69100 10.20800  1.000 52.39344 ? 336 HOH A O   1 
HETATM 3003 O  O   . HOH L 5 .   ? -27.46300 6.71000  10.44100  1.000 41.02482 ? 337 HOH A O   1 
HETATM 3004 O  O   . HOH L 5 .   ? -31.504   -1.080   -2.770    1.000 42.06667 ? 338 HOH A O   1 
HETATM 3005 O  O   . HOH L 5 .   ? -26.17200 12.08900 -7.26800  1.000 30.25667 ? 339 HOH A O   1 
HETATM 3006 O  O   . HOH L 5 .   ? -46.90700 10.30900 -2.40300  1.000 22.80498 ? 340 HOH A O   1 
HETATM 3007 O  O   . HOH L 5 .   ? -51.56000 3.34700  -18.35900 1.000 45.21591 ? 341 HOH A O   1 
HETATM 3008 O  O   . HOH L 5 .   ? -29.49600 14.75600 -3.70500  1.000 35.69445 ? 342 HOH A O   1 
HETATM 3009 O  O   . HOH L 5 .   ? -38.77700 23.85600 4.73600   1.000 37.81234 ? 343 HOH A O   1 
HETATM 3010 O  O   . HOH L 5 .   ? -55.75400 4.87600  -10.47600 1.000 36.65940 ? 344 HOH A O   1 
HETATM 3011 O  O   . HOH L 5 .   ? -51.06200 24.37000 4.03000   1.000 47.58616 ? 345 HOH A O   1 
HETATM 3012 O  O   . HOH L 5 .   ? -44.54600 5.57400  -0.21600  1.000 31.81281 ? 346 HOH A O   1 
HETATM 3013 O  O   . HOH L 5 .   ? -29.03300 16.23000 9.72200   1.000 34.81573 ? 347 HOH A O   1 
HETATM 3014 O  O   . HOH L 5 .   ? -58.17600 10.62600 -0.34100  1.000 32.83361 ? 348 HOH A O   1 
HETATM 3015 O  O   . HOH L 5 .   ? -30.18000 25.17600 1.35100   1.000 42.30876 ? 349 HOH A O   1 
HETATM 3016 O  O   . HOH L 5 .   ? -56.64700 22.46000 0.25500   1.000 55.64206 ? 350 HOH A O   1 
HETATM 3017 O  O   . HOH L 5 .   ? -25.89700 1.39100  2.20800   1.000 41.48640 ? 351 HOH A O   1 
HETATM 3018 O  O   . HOH L 5 .   ? -31.90300 5.26600  -15.26400 1.000 26.62844 ? 352 HOH A O   1 
HETATM 3019 O  O   . HOH L 5 .   ? -55.35100 9.36100  -19.00700 1.000 54.81433 ? 353 HOH A O   1 
HETATM 3020 O  O   . HOH L 5 .   ? -28.09400 23.07800 -8.24000  1.000 34.67939 ? 354 HOH A O   1 
HETATM 3021 O  O   . HOH L 5 .   ? -51.23500 13.68900 10.63900  1.000 48.90336 ? 355 HOH A O   1 
HETATM 3022 O  O   . HOH L 5 .   ? -46.03700 -0.49200 -17.81300 1.000 43.15929 ? 356 HOH A O   1 
HETATM 3023 O  O   . HOH L 5 .   ? -27.24700 14.01700 2.61000   1.000 47.22750 ? 357 HOH A O   1 
HETATM 3024 O  O   . HOH L 5 .   ? -58.68900 9.10000  -4.57400  1.000 35.16408 ? 358 HOH A O   1 
HETATM 3025 O  O   . HOH L 5 .   ? -26.85100 20.62600 -17.15900 0.500 41.63181 ? 359 HOH A O   1 
HETATM 3026 O  O   . HOH L 5 .   ? -59.78700 5.68800  -10.32000 1.000 48.15364 ? 360 HOH A O   1 
HETATM 3027 O  O   . HOH L 5 .   ? -60.92200 8.58000  -12.34900 1.000 44.34636 ? 361 HOH A O   1 
HETATM 3028 O  O   . HOH L 5 .   ? -26.57100 18.24500 -20.73600 1.000 51.60051 ? 362 HOH A O   1 
HETATM 3029 O  O   . HOH L 5 .   ? -56.27100 25.26800 -3.67300  1.000 33.60422 ? 363 HOH A O   1 
HETATM 3030 O  O   . HOH L 5 .   ? -37.55600 5.68700  -10.71700 1.000 25.08272 ? 364 HOH A O   1 
HETATM 3031 O  O   . HOH L 5 .   ? -51.81600 11.29200 7.55100   1.000 28.63217 ? 365 HOH A O   1 
HETATM 3032 O  O   . HOH L 5 .   ? -38.54700 10.05500 -2.88200  1.000 44.44205 ? 366 HOH A O   1 
HETATM 3033 O  O   . HOH L 5 .   ? -46.94500 29.57000 -1.46800  1.000 34.47809 ? 367 HOH A O   1 
HETATM 3034 O  O   . HOH L 5 .   ? -40.01200 -2.28600 -14.40600 1.000 32.84568 ? 368 HOH A O   1 
HETATM 3035 O  O   . HOH L 5 .   ? -29.59800 19.82300 -2.26900  1.000 36.82689 ? 369 HOH A O   1 
HETATM 3036 O  O   . HOH L 5 .   ? -36.21100 27.34200 -12.12600 1.000 33.79463 ? 370 HOH A O   1 
HETATM 3037 O  O   . HOH L 5 .   ? -62.64200 25.97300 -12.28800 1.000 42.72266 ? 371 HOH A O   1 
HETATM 3038 O  O   . HOH L 5 .   ? -30.74500 9.78500  -15.95800 1.000 27.75251 ? 372 HOH A O   1 
HETATM 3039 O  O   . HOH L 5 .   ? -33.09900 1.95800  -17.31900 1.000 35.00205 ? 373 HOH A O   1 
HETATM 3040 O  O   . HOH L 5 .   ? -61.00900 14.63300 -2.61700  1.000 38.70634 ? 374 HOH A O   1 
HETATM 3041 O  O   . HOH L 5 .   ? -61.37400 21.52900 -12.73300 1.000 41.58559 ? 375 HOH A O   1 
HETATM 3042 O  O   . HOH L 5 .   ? -47.41600 16.20800 -24.79400 1.000 60.56449 ? 376 HOH A O   1 
HETATM 3043 O  O   . HOH L 5 .   ? -55.50200 24.26800 -15.75700 1.000 40.16790 ? 377 HOH A O   1 
HETATM 3044 O  O   . HOH L 5 .   ? -47.89200 29.75200 2.38700   1.000 37.25150 ? 378 HOH A O   1 
HETATM 3045 O  O   . HOH L 5 .   ? -48.538   25.158   -15.242   1.000 40.26416 ? 379 HOH A O   1 
HETATM 3046 O  O   . HOH L 5 .   ? -34.88300 26.79300 -4.54500  1.000 32.69903 ? 380 HOH A O   1 
HETATM 3047 O  O   . HOH L 5 .   ? -37.52400 4.23400  -22.03300 1.000 30.77453 ? 381 HOH A O   1 
HETATM 3048 O  O   . HOH L 5 .   ? -53.96600 2.40500  -1.36800  1.000 33.12773 ? 382 HOH A O   1 
HETATM 3049 O  O   . HOH L 5 .   ? -29.25800 27.28300 -5.25900  1.000 39.39657 ? 383 HOH A O   1 
HETATM 3050 O  O   . HOH L 5 .   ? -46.51600 5.60500  6.97100   1.000 30.72254 ? 384 HOH A O   1 
HETATM 3051 O  O   . HOH L 5 .   ? -52.46700 26.81700 -2.89200  1.000 23.65152 ? 385 HOH A O   1 
HETATM 3052 O  O   . HOH L 5 .   ? -39.57500 27.73400 -9.21600  1.000 27.98821 ? 386 HOH A O   1 
HETATM 3053 O  O   . HOH L 5 .   ? -50.15500 -4.52600 4.19400   1.000 56.47356 ? 387 HOH A O   1 
HETATM 3054 O  O   . HOH L 5 .   ? -42.34400 9.23100  -2.72600  1.000 45.15329 ? 388 HOH A O   1 
HETATM 3055 O  O   . HOH L 5 .   ? -24.74300 8.45500  5.52000   1.000 28.97820 ? 389 HOH A O   1 
HETATM 3056 O  O   . HOH L 5 .   ? -44.23300 25.02000 -14.35600 1.000 31.12163 ? 390 HOH A O   1 
HETATM 3057 O  O   . HOH L 5 .   ? -54.98600 11.21300 -15.89600 1.000 36.50989 ? 391 HOH A O   1 
HETATM 3058 O  O   . HOH L 5 .   ? -46.47300 12.00300 -19.84200 1.000 32.13124 ? 392 HOH A O   1 
HETATM 3059 O  O   . HOH L 5 .   ? -46.15500 11.63000 -23.79500 1.000 57.34169 ? 393 HOH A O   1 
HETATM 3060 O  O   . HOH L 5 .   ? -37.05800 27.91100 -20.04800 1.000 50.01242 ? 394 HOH A O   1 
HETATM 3061 O  O   . HOH L 5 .   ? -36.56600 25.02900 3.32200   1.000 52.81312 ? 395 HOH A O   1 
HETATM 3062 O  O   . HOH L 5 .   ? -57.26000 1.51300  4.10400   1.000 38.73640 ? 396 HOH A O   1 
HETATM 3063 O  O   . HOH L 5 .   ? -33.48400 17.57200 -0.97900  1.000 42.04045 ? 397 HOH A O   1 
HETATM 3064 O  O   . HOH L 5 .   ? -42.06100 26.34500 -15.62900 1.000 34.61388 ? 398 HOH A O   1 
HETATM 3065 O  O   . HOH L 5 .   ? -35.09400 27.98800 -16.20700 1.000 37.57015 ? 399 HOH A O   1 
HETATM 3066 O  O   . HOH L 5 .   ? -36.72700 11.99100 15.35900  1.000 58.17794 ? 400 HOH A O   1 
HETATM 3067 O  O   . HOH L 5 .   ? -37.73400 0.04200  -1.91600  1.000 31.44030 ? 401 HOH A O   1 
HETATM 3068 O  O   . HOH L 5 .   ? -45.15500 18.71300 9.21200   1.000 39.77533 ? 402 HOH A O   1 
HETATM 3069 O  O   . HOH L 5 .   ? -57.97200 10.20200 12.94000  1.000 53.27364 ? 403 HOH A O   1 
HETATM 3070 O  O   . HOH L 5 .   ? -31.28200 11.87200 -17.74200 1.000 30.76684 ? 404 HOH A O   1 
HETATM 3071 O  O   . HOH L 5 .   ? -62.21700 11.10800 -5.48900  1.000 31.12103 ? 405 HOH A O   1 
HETATM 3072 O  O   . HOH L 5 .   ? -35.28900 15.86800 9.44800   1.000 49.91374 ? 406 HOH A O   1 
HETATM 3073 O  O   . HOH L 5 .   ? -53.42800 9.36200  -14.47100 1.000 29.86867 ? 407 HOH A O   1 
HETATM 3074 O  O   . HOH L 5 .   ? -27.98300 7.83400  -10.24300 1.000 31.31843 ? 408 HOH A O   1 
HETATM 3075 O  O   . HOH L 5 .   ? -44.72900 25.03700 6.30400   1.000 32.18529 ? 409 HOH A O   1 
HETATM 3076 O  O   . HOH L 5 .   ? -25.20900 12.98200 0.56500   1.000 33.29579 ? 410 HOH A O   1 
HETATM 3077 O  O   . HOH L 5 .   ? -59.38900 24.65000 -1.20900  1.000 42.55620 ? 411 HOH A O   1 
HETATM 3078 O  O   . HOH L 5 .   ? -66.45800 22.83900 -13.68000 1.000 37.73183 ? 412 HOH A O   1 
HETATM 3079 O  O   . HOH L 5 .   ? -50.18100 15.53900 -20.48900 1.000 49.73369 ? 413 HOH A O   1 
HETATM 3080 O  O   . HOH L 5 .   ? -40.22200 13.19100 9.33500   1.000 28.37978 ? 414 HOH A O   1 
HETATM 3081 O  O   . HOH L 5 .   ? -53.62300 13.33600 -20.26900 1.000 43.79379 ? 415 HOH A O   1 
HETATM 3082 O  O   . HOH L 5 .   ? -38.99000 26.96300 -5.10800  1.000 32.68483 ? 416 HOH A O   1 
HETATM 3083 O  O   . HOH L 5 .   ? -47.84100 6.87700  9.35900   1.000 47.13319 ? 417 HOH A O   1 
HETATM 3084 O  O   . HOH L 5 .   ? -39.12100 6.76400  9.10500   1.000 31.20395 ? 418 HOH A O   1 
HETATM 3085 O  O   . HOH L 5 .   ? -45.26300 23.88700 -17.21900 1.000 46.55849 ? 419 HOH A O   1 
HETATM 3086 O  O   . HOH L 5 .   ? -49.782   25.948   -11.181   1.000 33.03048 ? 420 HOH A O   1 
HETATM 3087 O  O   . HOH L 5 .   ? -56.32600 13.39600 -14.15300 1.000 37.95569 ? 421 HOH A O   1 
HETATM 3088 O  O   . HOH L 5 .   ? -39.06100 4.38500  -3.68800  1.000 32.67951 ? 422 HOH A O   1 
HETATM 3089 O  O   . HOH L 5 .   ? -59.03200 17.53900 2.75900   1.000 33.57970 ? 423 HOH A O   1 
HETATM 3090 O  O   . HOH L 5 .   ? -51.68100 -1.53000 3.51400   1.000 39.95304 ? 424 HOH A O   1 
HETATM 3091 O  O   . HOH L 5 .   ? -36.53300 16.85000 -25.72000 1.000 56.43033 ? 425 HOH A O   1 
HETATM 3092 O  O   . HOH L 5 .   ? -58.75400 2.16100  6.14900   1.000 42.89369 ? 426 HOH A O   1 
HETATM 3093 O  O   . HOH L 5 .   ? -25.05600 6.53400  3.73500   1.000 26.01109 ? 427 HOH A O   1 
HETATM 3094 O  O   . HOH L 5 .   ? -36.58900 -0.72900 -14.29800 1.000 33.81743 ? 428 HOH A O   1 
HETATM 3095 O  O   . HOH L 5 .   ? -35.64300 10.04500 -4.50500  1.000 31.17337 ? 429 HOH A O   1 
HETATM 3096 O  O   . HOH L 5 .   ? -47.71500 1.98800  15.07200  1.000 41.30143 ? 430 HOH A O   1 
HETATM 3097 O  O   . HOH L 5 .   ? -42.38000 26.69500 6.50200   1.000 42.95605 ? 431 HOH A O   1 
HETATM 3098 O  O   . HOH L 5 .   ? -61.69900 17.94300 -18.28300 1.000 45.72219 ? 432 HOH A O   1 
HETATM 3099 O  O   . HOH L 5 .   ? -50.89100 21.30400 7.33000   1.000 39.25323 ? 433 HOH A O   1 
HETATM 3100 O  O   . HOH L 5 .   ? -29.19100 24.11200 -18.36000 1.000 45.75422 ? 434 HOH A O   1 
HETATM 3101 O  O   . HOH L 5 .   ? -44.36300 9.61100  -1.74400  1.000 48.96935 ? 435 HOH A O   1 
HETATM 3102 O  O   . HOH L 5 .   ? -41.16300 11.48500 1.28700   1.000 32.25116 ? 436 HOH A O   1 
HETATM 3103 O  O   . HOH L 5 .   ? -63.85600 21.60600 -4.96200  1.000 48.42754 ? 437 HOH A O   1 
HETATM 3104 O  O   . HOH L 5 .   ? -31.05200 2.95200  -13.87900 1.000 34.90646 ? 438 HOH A O   1 
HETATM 3105 O  O   . HOH L 5 .   ? -37.95400 1.64200  -20.90600 1.000 32.17994 ? 439 HOH A O   1 
HETATM 3106 O  O   . HOH L 5 .   ? -41.33400 27.03600 -3.70300  1.000 33.40344 ? 440 HOH A O   1 
HETATM 3107 O  O   . HOH L 5 .   ? -51.462   -1.042   0.936     1.000 41.17006 ? 441 HOH A O   1 
HETATM 3108 O  O   . HOH L 5 .   ? -37.07300 5.27900  9.33500   1.000 35.89502 ? 442 HOH A O   1 
HETATM 3109 O  O   . HOH L 5 .   ? -26.85700 14.68000 -9.88700  1.000 31.63225 ? 443 HOH A O   1 
HETATM 3110 O  O   . HOH L 5 .   ? -27.60500 16.37800 -17.65500 1.000 58.56053 ? 444 HOH A O   1 
HETATM 3111 O  O   . HOH L 5 .   ? -24.03100 14.93700 -8.23300  1.000 48.36945 ? 445 HOH A O   1 
HETATM 3112 O  O   . HOH L 5 .   ? -39.16500 3.61500  -25.94900 1.000 63.86135 ? 446 HOH A O   1 
HETATM 3113 O  O   . HOH L 5 .   ? -53.76800 0.87400  6.83000   1.000 41.36676 ? 447 HOH A O   1 
HETATM 3114 O  O   A HOH L 5 .   ? -32.34300 0.28900  -7.38300  0.910 40.41759 ? 448 HOH A O   1 
HETATM 3115 O  O   . HOH L 5 .   ? -29.74600 19.57300 -27.32300 1.000 67.22138 ? 449 HOH A O   1 
HETATM 3116 O  O   . HOH L 5 .   ? -38.94800 7.53300  -2.70800  1.000 37.84534 ? 450 HOH A O   1 
HETATM 3117 O  O   . HOH L 5 .   ? -58.94900 6.90400  -13.01300 1.000 54.47913 ? 451 HOH A O   1 
HETATM 3118 O  O   . HOH L 5 .   ? -28.83100 20.70000 1.47400   1.000 39.32344 ? 452 HOH A O   1 
HETATM 3119 O  O   . HOH L 5 .   ? -59.93300 6.83700  -0.41200  1.000 30.59496 ? 453 HOH A O   1 
HETATM 3120 O  O   . HOH L 5 .   ? -42.09600 28.90600 -9.95700  1.000 36.11648 ? 454 HOH A O   1 
HETATM 3121 O  O   . HOH L 5 .   ? -30.65700 5.03800  8.62800   1.000 34.76223 ? 455 HOH A O   1 
HETATM 3122 O  O   . HOH L 5 .   ? -41.38200 8.30600  0.02700   1.000 49.55150 ? 456 HOH A O   1 
HETATM 3123 O  O   . HOH L 5 .   ? -34.91100 -0.42600 -7.00700  1.000 29.39997 ? 457 HOH A O   1 
HETATM 3124 O  O   . HOH L 5 .   ? -49.75300 18.65600 -19.25900 1.000 28.56760 ? 458 HOH A O   1 
HETATM 3125 O  O   . HOH L 5 .   ? -64.20300 11.46500 -11.18000 0.830 59.49244 ? 459 HOH A O   1 
HETATM 3126 O  O   . HOH L 5 .   ? -52.47600 5.49200  -4.99000  1.000 31.58878 ? 460 HOH A O   1 
HETATM 3127 O  O   . HOH L 5 .   ? -33.34700 28.77900 -14.16400 1.000 50.81858 ? 461 HOH A O   1 
HETATM 3128 O  O   . HOH L 5 .   ? -40.99100 25.48000 -18.68000 1.000 30.80904 ? 462 HOH A O   1 
HETATM 3129 O  O   . HOH L 5 .   ? -45.01700 19.75600 -22.63000 1.000 34.02406 ? 463 HOH A O   1 
HETATM 3130 O  O   . HOH L 5 .   ? -44.14800 32.63800 -4.99700  1.000 41.75344 ? 464 HOH A O   1 
HETATM 3131 O  O   . HOH L 5 .   ? -29.71400 13.92100 -14.35000 1.000 44.03584 ? 465 HOH A O   1 
HETATM 3132 O  O   . HOH L 5 .   ? -38.37800 20.50400 9.18300   1.000 58.78991 ? 466 HOH A O   1 
HETATM 3133 O  O   . HOH L 5 .   ? -54.04700 11.16900 13.49500  1.000 64.36734 ? 467 HOH A O   1 
HETATM 3134 O  O   . HOH L 5 .   ? -61.35400 17.13400 1.43100   1.000 37.90948 ? 468 HOH A O   1 
HETATM 3135 O  O   . HOH L 5 .   ? -27.94800 5.18200  -11.14100 1.000 38.76884 ? 469 HOH A O   1 
HETATM 3136 O  O   . HOH L 5 .   ? -38.05800 10.60200 -0.78700  1.000 43.52693 ? 470 HOH A O   1 
HETATM 3137 O  O   . HOH L 5 .   ? -39.076   29.658   -14.661   1.000 49.11730 ? 471 HOH A O   1 
HETATM 3138 O  O   . HOH L 5 .   ? -42.227   29.430   -12.236   1.000 51.82727 ? 472 HOH A O   1 
HETATM 3139 O  O   . HOH L 5 .   ? -63.26400 23.63100 -12.77100 1.000 43.69653 ? 473 HOH A O   1 
HETATM 3140 O  O   . HOH L 5 .   ? -33.52900 34.03800 -19.33600 1.000 36.01027 ? 474 HOH A O   1 
HETATM 3141 O  O   . HOH L 5 .   ? -32.74800 12.67700 -23.46300 1.000 48.14172 ? 475 HOH A O   1 
HETATM 3142 O  O   . HOH L 5 .   ? -41.82400 6.02600  -3.18600  1.000 37.33767 ? 476 HOH A O   1 
HETATM 3143 O  O   . HOH L 5 .   ? -54.34200 26.25700 2.61000   1.000 56.95761 ? 477 HOH A O   1 
HETATM 3144 O  O   . HOH L 5 .   ? -47.27900 0.99700  -20.24700 1.000 51.21365 ? 478 HOH A O   1 
HETATM 3145 O  O   . HOH L 5 .   ? -33.03400 27.18600 -2.59700  1.000 52.25900 ? 479 HOH A O   1 
HETATM 3146 O  O   . HOH L 5 .   ? -60.32700 -1.05500 5.29100   1.000 54.35938 ? 480 HOH A O   1 
HETATM 3147 O  O   . HOH L 5 .   ? -64.53900 9.52300  -9.41400  1.000 43.07073 ? 481 HOH A O   1 
HETATM 3148 O  O   . HOH L 5 .   ? -58.98500 5.13000  -6.65200  1.000 49.29793 ? 482 HOH A O   1 
HETATM 3149 O  O   . HOH L 5 .   ? -49.63000 13.95100 -22.10500 1.000 52.18136 ? 483 HOH A O   1 
HETATM 3150 O  O   . HOH L 5 .   ? -31.57200 22.58100 5.96200   1.000 46.07227 ? 484 HOH A O   1 
HETATM 3151 O  O   . HOH L 5 .   ? -46.793   4.399    15.886    0.500 33.39338 ? 485 HOH A O   1 
HETATM 3152 O  O   . HOH L 5 .   ? -27.80500 15.07700 -13.01800 1.000 52.68302 ? 486 HOH A O   1 
HETATM 3153 O  O   . HOH L 5 .   ? -50.34900 23.02600 -19.13100 1.000 37.37977 ? 487 HOH A O   1 
HETATM 3154 O  O   . HOH L 5 .   ? -43.84600 18.45400 -24.89900 1.000 50.63239 ? 488 HOH A O   1 
HETATM 3155 O  O   . HOH L 5 .   ? -33.25500 6.43500  -3.72300  1.000 47.22665 ? 489 HOH A O   1 
HETATM 3156 O  O   . HOH L 5 .   ? -26.92400 7.97500  -7.71400  1.000 50.59754 ? 490 HOH A O   1 
HETATM 3157 O  O   . HOH L 5 .   ? -54.56400 0.95600  -13.65700 1.000 54.87429 ? 491 HOH A O   1 
HETATM 3158 O  O   . HOH L 5 .   ? -43.982   24.979   -19.049   1.000 53.12777 ? 492 HOH A O   1 
HETATM 3159 O  O   . HOH L 5 .   ? -28.53800 4.00800  8.15300   1.000 53.95673 ? 493 HOH A O   1 
HETATM 3160 O  O   . HOH L 5 .   ? -64.81600 10.05300 -6.78800  1.000 60.71392 ? 494 HOH A O   1 
HETATM 3161 O  O   . HOH L 5 .   ? -46.88000 26.58800 5.98800   1.000 48.09484 ? 495 HOH A O   1 
HETATM 3162 O  O   . HOH L 5 .   ? -40.30500 8.39600  -30.37900 1.000 50.98313 ? 496 HOH A O   1 
HETATM 3163 O  O   . HOH L 5 .   ? -33.40800 23.87200 5.82900   0.500 33.75264 ? 497 HOH A O   1 
HETATM 3164 O  O   . HOH L 5 .   ? -56.68600 1.16300  -0.66600  1.000 45.68904 ? 498 HOH A O   1 
HETATM 3165 O  O   . HOH L 5 .   ? -51.78000 20.63300 -18.30900 1.000 40.58306 ? 499 HOH A O   1 
HETATM 3166 O  O   . HOH L 5 .   ? -54.34500 5.21600  14.09100  1.000 61.99830 ? 500 HOH A O   1 
HETATM 3167 O  O   . HOH L 5 .   ? -60.97800 10.80200 -0.39200  1.000 43.17260 ? 501 HOH A O   1 
HETATM 3168 O  O   . HOH L 5 .   ? -34.86100 0.25000  -12.64300 1.000 46.76148 ? 502 HOH A O   1 
HETATM 3169 O  O   . HOH L 5 .   ? -55.73900 0.43600  5.69400   0.500 36.52446 ? 503 HOH A O   1 
HETATM 3170 O  O   . HOH L 5 .   ? -29.37700 11.23900 -13.55800 1.000 40.51584 ? 504 HOH A O   1 
HETATM 3171 O  O   . HOH L 5 .   ? -29.69100 5.59500  -16.62800 1.000 39.29177 ? 505 HOH A O   1 
HETATM 3172 O  O   . HOH L 5 .   ? -31.22700 13.35800 13.77100  1.000 49.20087 ? 506 HOH A O   1 
HETATM 3173 O  O   A HOH L 5 .   ? -40.68500 7.11500  -28.56400 0.700 31.49181 ? 507 HOH A O   1 
HETATM 3174 O  O   . HOH L 5 .   ? -27.22400 10.03200 -12.22200 1.000 45.96666 ? 508 HOH A O   1 
HETATM 3175 O  O   . HOH L 5 .   ? -60.13500 7.35500  -3.00400  1.000 47.18950 ? 509 HOH A O   1 
HETATM 3176 O  O   . HOH L 5 .   ? -51.44400 9.74500  9.74300   1.000 35.73234 ? 510 HOH A O   1 
HETATM 3177 O  O   . HOH L 5 .   ? -23.403   18.741   -25.002   1.000 38.66644 ? 511 HOH A O   1 
HETATM 3178 O  O   . HOH L 5 .   ? -61.63300 9.63800  -3.45500  1.000 59.24762 ? 512 HOH A O   1 
HETATM 3179 O  O   . HOH L 5 .   ? -62.61900 13.62500 -4.63900  1.000 37.83275 ? 513 HOH A O   1 
HETATM 3180 O  O   . HOH L 5 .   ? -32.80600 1.03400  -14.48800 1.000 49.75533 ? 514 HOH A O   1 
HETATM 3181 O  O   . HOH L 5 .   ? -38.81500 8.22900  0.91100   1.000 41.01600 ? 515 HOH A O   1 
HETATM 3182 O  O   . HOH L 5 .   ? -47.20700 20.27000 7.72700   1.000 45.66555 ? 516 HOH A O   1 
HETATM 3183 O  O   . HOH L 5 .   ? -23.56600 8.26300  -6.66600  1.000 42.07327 ? 517 HOH A O   1 
HETATM 3184 O  O   . HOH L 5 .   ? -38.83800 28.67900 -7.18900  1.000 36.76585 ? 518 HOH A O   1 
HETATM 3185 O  O   . HOH L 5 .   ? -37.67900 -2.87200 -13.09700 1.000 45.50374 ? 519 HOH A O   1 
HETATM 3186 O  O   . HOH L 5 .   ? -31.47500 3.07300  9.91700   1.000 59.46728 ? 520 HOH A O   1 
HETATM 3187 O  O   . HOH L 5 .   ? -35.838   0.032    -24.147   1.000 39.76852 ? 521 HOH A O   1 
HETATM 3188 O  O   . HOH L 5 .   ? -54.86000 24.34300 -18.63000 1.000 45.74089 ? 522 HOH A O   1 
HETATM 3189 O  O   . HOH L 5 .   ? -63.80200 22.97000 -1.66900  1.000 61.36841 ? 523 HOH A O   1 
HETATM 3190 O  O   . HOH L 5 .   ? -37.89100 12.00700 10.54700  1.000 49.32839 ? 524 HOH A O   1 
HETATM 3191 O  O   . HOH L 5 .   ? -52.69400 7.99000  -26.31900 1.000 52.07339 ? 525 HOH A O   1 
HETATM 3192 O  O   . HOH L 5 .   ? -38.35200 23.18200 7.79000   1.000 48.33754 ? 526 HOH A O   1 
HETATM 3193 O  O   . HOH L 5 .   ? -39.64000 4.10100  -0.93600  1.000 33.12317 ? 527 HOH A O   1 
HETATM 3194 O  O   . HOH L 5 .   ? -41.880   -5.442   0.619     1.000 35.52052 ? 528 HOH A O   1 
HETATM 3195 O  O   . HOH L 5 .   ? -28.805   15.916   -28.265   1.000 47.60840 ? 529 HOH A O   1 
HETATM 3196 O  O   . HOH L 5 .   ? -28.73800 8.31200  -16.59300 1.000 37.78233 ? 530 HOH A O   1 
HETATM 3197 O  O   . HOH L 5 .   ? -48.94300 25.17800 -18.20600 1.000 40.75671 ? 531 HOH A O   1 
HETATM 3198 O  O   . HOH L 5 .   ? -47.245   32.141   -0.676    1.000 44.59513 ? 532 HOH A O   1 
HETATM 3199 O  O   . HOH L 5 .   ? -25.36100 8.29500  9.80200   1.000 28.65545 ? 533 HOH A O   1 
HETATM 3200 O  O   . HOH L 5 .   ? -62.18900 24.18300 -0.78800  1.000 54.25211 ? 534 HOH A O   1 
HETATM 3201 O  O   . HOH L 5 .   ? -24.86200 9.84500  -7.78500  1.000 44.36311 ? 535 HOH A O   1 
HETATM 3202 O  O   . HOH L 5 .   ? -45.33600 23.29500 8.34500   1.000 42.90724 ? 536 HOH A O   1 
HETATM 3203 O  O   . HOH L 5 .   ? -53.46600 2.87900  -3.94200  1.000 42.30774 ? 537 HOH A O   1 
HETATM 3204 O  O   . HOH L 5 .   ? -64.48700 7.41800  -10.10800 1.000 72.98916 ? 538 HOH A O   1 
HETATM 3205 O  O   . HOH L 5 .   ? -31.34100 5.14300  -21.90500 1.000 55.15509 ? 539 HOH A O   1 
HETATM 3206 O  O   . HOH L 5 .   ? -55.22800 7.18800  14.77500  1.000 59.72950 ? 540 HOH A O   1 
HETATM 3207 O  O   . HOH L 5 .   ? -25.27500 11.85100 -11.99400 1.000 49.43724 ? 541 HOH A O   1 
HETATM 3208 O  O   . HOH L 5 .   ? -38.01800 6.41600  -0.54100  1.000 37.63311 ? 542 HOH A O   1 
HETATM 3209 O  O   . HOH L 5 .   ? -36.61000 4.06600  -26.89600 1.000 65.53500 ? 543 HOH A O   1 
HETATM 3210 O  O   . HOH L 5 .   ? -34.30300 -0.10600 -18.49500 1.000 51.97222 ? 544 HOH A O   1 
HETATM 3211 O  O   . HOH L 5 .   ? -35.45500 -1.94400 -16.75900 1.000 42.09315 ? 545 HOH A O   1 
HETATM 3212 O  O   . HOH L 5 .   ? -48.72900 25.36500 7.86700   1.000 49.05249 ? 546 HOH A O   1 
HETATM 3213 O  O   . HOH L 5 .   ? -61.10800 22.09100 2.06000   1.000 73.90701 ? 547 HOH A O   1 
HETATM 3214 O  O   . HOH L 5 .   ? -26.85000 5.39700  -13.78300 1.000 50.97312 ? 548 HOH A O   1 
HETATM 3215 O  O   . HOH L 5 .   ? -64.73000 6.14600  -7.10200  1.000 65.89445 ? 549 HOH A O   1 
HETATM 3216 O  O   . HOH L 5 .   ? -27.58100 9.17200  -19.01400 1.000 60.98072 ? 550 HOH A O   1 
HETATM 3217 O  O   . HOH L 5 .   ? -26.61500 8.17500  -14.60200 1.000 47.47224 ? 551 HOH A O   1 
HETATM 3218 O  O   . HOH L 5 .   ? -65.00100 7.59700  -5.08600  1.000 55.22588 ? 552 HOH A O   1 
HETATM 3219 O  O   . HOH M 5 .   ? -29.84200 18.44900 9.78500   1.000 59.11778 ? 301 HOH B O   1 
HETATM 3220 O  O   . HOH M 5 .   ? -21.34900 30.10500 8.09300   1.000 35.04556 ? 302 HOH B O   1 
HETATM 3221 O  O   . HOH M 5 .   ? -15.64200 2.78800  13.25600  1.000 44.05406 ? 303 HOH B O   1 
HETATM 3222 O  O   . HOH M 5 .   ? -5.50600  32.98700 7.24000   1.000 56.54220 ? 304 HOH B O   1 
HETATM 3223 O  O   . HOH M 5 .   ? -29.64400 26.82600 9.95600   1.000 65.00251 ? 305 HOH B O   1 
HETATM 3224 O  O   . HOH M 5 .   ? -27.07900 16.88300 -1.91100  1.000 56.91098 ? 306 HOH B O   1 
HETATM 3225 O  O   A HOH M 5 .   ? -27.44500 21.56800 7.76400   0.580 28.68241 ? 307 HOH B O   1 
HETATM 3226 O  O   . HOH M 5 .   ? -28.60200 26.36600 12.98500  0.500 42.73808 ? 308 HOH B O   1 
HETATM 3227 O  O   . HOH M 5 .   ? -12.09600 2.26700  22.51000  1.000 62.98347 ? 309 HOH B O   1 
HETATM 3228 O  O   . HOH M 5 .   ? 4.18500   15.69000 15.17600  1.000 44.74022 ? 310 HOH B O   1 
HETATM 3229 O  O   . HOH M 5 .   ? -23.77200 29.24200 2.67600   1.000 24.46546 ? 311 HOH B O   1 
HETATM 3230 O  O   . HOH M 5 .   ? -0.19400  24.40500 21.31300  1.000 31.99658 ? 312 HOH B O   1 
HETATM 3231 O  O   . HOH M 5 .   ? -10.90300 27.72400 23.05000  1.000 48.77869 ? 313 HOH B O   1 
HETATM 3232 O  O   . HOH M 5 .   ? -9.44400  6.70800  11.13900  1.000 31.40153 ? 314 HOH B O   1 
HETATM 3233 O  O   . HOH M 5 .   ? 6.29200   17.42700 14.25500  1.000 31.03165 ? 315 HOH B O   1 
HETATM 3234 O  O   . HOH M 5 .   ? -4.25700  33.92500 -3.10300  1.000 37.15329 ? 316 HOH B O   1 
HETATM 3235 O  O   . HOH M 5 .   ? -26.424   0.440    6.408     1.000 45.40011 ? 317 HOH B O   1 
HETATM 3236 O  O   . HOH M 5 .   ? -3.59600  28.08700 21.62600  1.000 49.08410 ? 318 HOH B O   1 
HETATM 3237 O  O   . HOH M 5 .   ? 5.79900   15.24000 18.40200  1.000 37.93284 ? 319 HOH B O   1 
HETATM 3238 O  O   . HOH M 5 .   ? -16.70500 20.72100 24.37200  1.000 49.31528 ? 320 HOH B O   1 
HETATM 3239 O  O   . HOH M 5 .   ? 6.46100   20.94100 15.34100  1.000 39.15944 ? 321 HOH B O   1 
HETATM 3240 O  O   . HOH M 5 .   ? -29.02100 25.92300 7.48900   1.000 48.96919 ? 322 HOH B O   1 
HETATM 3241 O  O   . HOH M 5 .   ? -29.20900 14.96100 13.72900  1.000 43.29781 ? 323 HOH B O   1 
HETATM 3242 O  O   . HOH M 5 .   ? -11.92400 4.96100  23.87100  1.000 60.99046 ? 324 HOH B O   1 
HETATM 3243 O  O   . HOH M 5 .   ? -5.06100  26.15400 7.46000   1.000 33.30282 ? 325 HOH B O   1 
HETATM 3244 O  O   . HOH M 5 .   ? -12.26100 18.07600 -12.11600 1.000 56.57849 ? 326 HOH B O   1 
HETATM 3245 O  O   . HOH M 5 .   ? -14.87400 13.65400 -8.86000  1.000 52.37872 ? 327 HOH B O   1 
HETATM 3246 O  O   . HOH M 5 .   ? -0.29000  27.32500 13.34800  1.000 36.72647 ? 328 HOH B O   1 
HETATM 3247 O  O   . HOH M 5 .   ? -9.228    19.842   30.835    1.000 58.00363 ? 329 HOH B O   1 
HETATM 3248 O  O   . HOH M 5 .   ? -28.134   -1.965   5.776     1.000 40.22344 ? 330 HOH B O   1 
HETATM 3249 O  O   . HOH M 5 .   ? -20.27000 2.63300  -6.38300  1.000 49.82267 ? 331 HOH B O   1 
HETATM 3250 O  O   . HOH M 5 .   ? -0.80800  7.11700  17.77900  1.000 50.66402 ? 332 HOH B O   1 
HETATM 3251 O  O   . HOH M 5 .   ? 6.307     23.813   17.410    1.000 40.03890 ? 333 HOH B O   1 
HETATM 3252 O  O   . HOH M 5 .   ? -2.95100  14.04500 -7.23700  1.000 42.67645 ? 334 HOH B O   1 
HETATM 3253 O  O   . HOH M 5 .   ? -5.78200  20.73000 11.15400  1.000 29.19588 ? 335 HOH B O   1 
HETATM 3254 O  O   . HOH M 5 .   ? -19.64700 3.28900  1.45200   1.000 36.93529 ? 336 HOH B O   1 
HETATM 3255 O  O   . HOH M 5 .   ? -24.85900 35.49700 2.61900   1.000 56.90635 ? 337 HOH B O   1 
HETATM 3256 O  O   . HOH M 5 .   ? -18.74400 19.56200 20.71700  1.000 54.52504 ? 338 HOH B O   1 
HETATM 3257 O  O   . HOH M 5 .   ? -10.14500 18.04300 9.07100   1.000 23.26591 ? 339 HOH B O   1 
HETATM 3258 O  O   . HOH M 5 .   ? -23.82000 21.51900 -10.52400 1.000 54.18318 ? 340 HOH B O   1 
HETATM 3259 O  O   . HOH M 5 .   ? -15.15600 37.53000 13.08000  1.000 44.17338 ? 341 HOH B O   1 
HETATM 3260 O  O   . HOH M 5 .   ? -12.34600 9.86900  -8.47800  1.000 45.91578 ? 342 HOH B O   1 
HETATM 3261 O  O   . HOH M 5 .   ? -6.58700  33.03600 -4.33100  1.000 28.81566 ? 343 HOH B O   1 
HETATM 3262 O  O   . HOH M 5 .   ? -6.58900  27.36300 0.44500   1.000 25.38275 ? 344 HOH B O   1 
HETATM 3263 O  O   . HOH M 5 .   ? -12.32100 17.82700 -8.23600  1.000 34.43201 ? 345 HOH B O   1 
HETATM 3264 O  O   . HOH M 5 .   ? -12.94000 0.96400  1.87300   1.000 40.63500 ? 346 HOH B O   1 
HETATM 3265 O  O   . HOH M 5 .   ? -0.94800  29.41600 1.30700   1.000 39.77276 ? 347 HOH B O   1 
HETATM 3266 O  O   . HOH M 5 .   ? -28.46400 26.47500 -0.57200  1.000 39.73560 ? 348 HOH B O   1 
HETATM 3267 O  O   . HOH M 5 .   ? -24.89200 4.53800  7.15500   1.000 37.79448 ? 349 HOH B O   1 
HETATM 3268 O  O   . HOH M 5 .   ? -20.53300 7.45300  12.52100  1.000 45.46272 ? 350 HOH B O   1 
HETATM 3269 O  O   . HOH M 5 .   ? -21.86100 18.63100 -10.68300 1.000 44.06814 ? 351 HOH B O   1 
HETATM 3270 O  O   . HOH M 5 .   ? -23.83900 8.60100  12.17900  1.000 37.79465 ? 352 HOH B O   1 
HETATM 3271 O  O   . HOH M 5 .   ? -12.90200 29.60300 -12.30300 1.000 50.49341 ? 353 HOH B O   1 
HETATM 3272 O  O   . HOH M 5 .   ? -2.19100  33.48800 13.56900  1.000 38.91023 ? 354 HOH B O   1 
HETATM 3273 O  O   . HOH M 5 .   ? -3.85800  9.54700  0.76200   1.000 45.46369 ? 355 HOH B O   1 
HETATM 3274 O  O   . HOH M 5 .   ? 0.13000   8.49300  14.95300  1.000 50.90857 ? 356 HOH B O   1 
HETATM 3275 O  O   . HOH M 5 .   ? -7.80200  37.31000 21.54500  1.000 37.72791 ? 357 HOH B O   1 
HETATM 3276 O  O   . HOH M 5 .   ? -25.10200 18.92500 17.70000  1.000 28.49140 ? 358 HOH B O   1 
HETATM 3277 O  O   . HOH M 5 .   ? -6.20800  22.54500 26.11100  1.000 51.27730 ? 359 HOH B O   1 
HETATM 3278 O  O   . HOH M 5 .   ? -7.15600  4.01100  -0.36500  1.000 51.13899 ? 360 HOH B O   1 
HETATM 3279 O  O   . HOH M 5 .   ? -16.33200 36.49200 14.68900  1.000 43.34227 ? 361 HOH B O   1 
HETATM 3280 O  O   . HOH M 5 .   ? -26.03800 10.77800 8.59200   1.000 26.17999 ? 362 HOH B O   1 
HETATM 3281 O  O   . HOH M 5 .   ? -20.35600 13.52700 -5.26700  1.000 39.99262 ? 363 HOH B O   1 
HETATM 3282 O  O   . HOH M 5 .   ? -9.79000  36.84100 0.83700   1.000 30.88230 ? 364 HOH B O   1 
HETATM 3283 O  O   . HOH M 5 .   ? -16.62800 20.65900 -13.08400 1.000 43.18394 ? 365 HOH B O   1 
HETATM 3284 O  O   . HOH M 5 .   ? -10.02200 21.69100 10.82800  1.000 41.70537 ? 366 HOH B O   1 
HETATM 3285 O  O   . HOH M 5 .   ? -3.46200  32.33100 -6.64500  1.000 39.08646 ? 367 HOH B O   1 
HETATM 3286 O  O   . HOH M 5 .   ? -21.73300 32.94800 9.38900   1.000 65.39315 ? 368 HOH B O   1 
HETATM 3287 O  O   . HOH M 5 .   ? -13.63000 38.52000 2.99800   1.000 36.29407 ? 369 HOH B O   1 
HETATM 3288 O  O   . HOH M 5 .   ? -17.39900 29.35000 20.25400  1.000 51.77594 ? 370 HOH B O   1 
HETATM 3289 O  O   . HOH M 5 .   ? -6.91800  7.69300  12.09200  1.000 29.66972 ? 371 HOH B O   1 
HETATM 3290 O  O   . HOH M 5 .   ? -24.45200 24.74900 16.19300  1.000 34.42578 ? 372 HOH B O   1 
HETATM 3291 O  O   . HOH M 5 .   ? -9.70900  22.71700 8.48100   1.000 45.49177 ? 373 HOH B O   1 
HETATM 3292 O  O   . HOH M 5 .   ? -12.62200 3.27100  9.13100   1.000 43.95088 ? 374 HOH B O   1 
HETATM 3293 O  O   . HOH M 5 .   ? -6.99100  26.15100 19.84800  1.000 28.91503 ? 375 HOH B O   1 
HETATM 3294 O  O   . HOH M 5 .   ? -9.49300  39.98600 16.25900  1.000 29.44021 ? 376 HOH B O   1 
HETATM 3295 O  O   . HOH M 5 .   ? -17.12100 8.07000  -5.80100  1.000 84.08691 ? 377 HOH B O   1 
HETATM 3296 O  O   . HOH M 5 .   ? -2.38400  33.09300 3.21600   1.000 42.80908 ? 378 HOH B O   1 
HETATM 3297 O  O   . HOH M 5 .   ? -25.11300 18.88700 -3.00500  1.000 36.24252 ? 379 HOH B O   1 
HETATM 3298 O  O   . HOH M 5 .   ? -16.89400 37.50900 1.10200   1.000 38.98052 ? 380 HOH B O   1 
HETATM 3299 O  O   . HOH M 5 .   ? 1.99300   14.27500 15.14300  1.000 35.15042 ? 381 HOH B O   1 
HETATM 3300 O  O   . HOH M 5 .   ? -6.41300  28.75700 8.38400   1.000 54.58599 ? 382 HOH B O   1 
HETATM 3301 O  O   . HOH M 5 .   ? -13.49300 27.81200 26.30200  1.000 45.01284 ? 383 HOH B O   1 
HETATM 3302 O  O   . HOH M 5 .   ? -21.203   34.250   14.051    1.000 47.12681 ? 384 HOH B O   1 
HETATM 3303 O  O   . HOH M 5 .   ? -13.47000 33.03800 -6.65000  1.000 32.78255 ? 385 HOH B O   1 
HETATM 3304 O  O   . HOH M 5 .   ? -8.70100  11.44100 -2.82200  1.000 27.04535 ? 386 HOH B O   1 
HETATM 3305 O  O   . HOH M 5 .   ? -25.78400 26.67900 14.90900  1.000 48.31674 ? 387 HOH B O   1 
HETATM 3306 O  O   . HOH M 5 .   ? -23.30500 7.62900  -3.70300  1.000 27.45847 ? 388 HOH B O   1 
HETATM 3307 O  O   . HOH M 5 .   ? -11.43000 33.79900 -4.89100  1.000 30.35492 ? 389 HOH B O   1 
HETATM 3308 O  O   . HOH M 5 .   ? -10.41800 9.47900  -4.25800  1.000 32.26349 ? 390 HOH B O   1 
HETATM 3309 O  O   . HOH M 5 .   ? -16.44300 34.89800 -4.97400  1.000 40.32689 ? 391 HOH B O   1 
HETATM 3310 O  O   . HOH M 5 .   ? -23.61100 29.05800 -11.78300 1.000 61.57720 ? 392 HOH B O   1 
HETATM 3311 O  O   . HOH M 5 .   ? -24.04900 7.04400  7.84700   1.000 26.60709 ? 393 HOH B O   1 
HETATM 3312 O  O   . HOH M 5 .   ? 0.49200   29.97800 9.50700   1.000 45.19236 ? 394 HOH B O   1 
HETATM 3313 O  O   . HOH M 5 .   ? -7.70200  6.42500  7.27300   1.000 34.81552 ? 395 HOH B O   1 
HETATM 3314 O  O   . HOH M 5 .   ? -10.67300 13.42500 19.23700  1.000 33.91500 ? 396 HOH B O   1 
HETATM 3315 O  O   . HOH M 5 .   ? -17.68700 7.99000  19.28600  1.000 61.09293 ? 397 HOH B O   1 
HETATM 3316 O  O   . HOH M 5 .   ? -5.59500  6.27700  -1.56400  1.000 48.25546 ? 398 HOH B O   1 
HETATM 3317 O  O   . HOH M 5 .   ? -18.45700 36.17600 -6.31800  1.000 58.64872 ? 399 HOH B O   1 
HETATM 3318 O  O   . HOH M 5 .   ? -12.71800 13.41600 22.56200  1.000 54.01325 ? 400 HOH B O   1 
HETATM 3319 O  O   . HOH M 5 .   ? -5.06300  12.76200 6.59500   1.000 32.25462 ? 401 HOH B O   1 
HETATM 3320 O  O   . HOH M 5 .   ? -27.94400 28.05200 6.70700   1.000 41.57890 ? 402 HOH B O   1 
HETATM 3321 O  O   . HOH M 5 .   ? -27.73900 24.28900 6.16300   1.000 36.01142 ? 403 HOH B O   1 
HETATM 3322 O  O   . HOH M 5 .   ? -5.38100  19.12600 18.35400  1.000 24.02550 ? 404 HOH B O   1 
HETATM 3323 O  O   . HOH M 5 .   ? -20.48600 1.99500  -0.38200  1.000 40.84158 ? 405 HOH B O   1 
HETATM 3324 O  O   . HOH M 5 .   ? -6.32400  17.93200 20.52800  1.000 34.37720 ? 406 HOH B O   1 
HETATM 3325 O  O   . HOH M 5 .   ? -19.44100 33.67700 10.50400  1.000 45.98816 ? 407 HOH B O   1 
HETATM 3326 O  O   . HOH M 5 .   ? -20.65100 12.88200 18.85300  1.000 44.84031 ? 408 HOH B O   1 
HETATM 3327 O  O   . HOH M 5 .   ? -11.99000 23.74600 12.51600  1.000 35.03372 ? 409 HOH B O   1 
HETATM 3328 O  O   . HOH M 5 .   ? 3.15500   5.80300  15.24700  1.000 54.00161 ? 410 HOH B O   1 
HETATM 3329 O  O   . HOH M 5 .   ? -12.39500 7.94100  -2.28900  1.000 31.76942 ? 411 HOH B O   1 
HETATM 3330 O  O   . HOH M 5 .   ? -28.51200 23.39200 2.36900   1.000 35.17410 ? 412 HOH B O   1 
HETATM 3331 O  O   . HOH M 5 .   ? -1.92500  29.93500 18.87100  1.000 40.57961 ? 413 HOH B O   1 
HETATM 3332 O  O   . HOH M 5 .   ? -16.15300 5.32100  14.64400  1.000 32.48547 ? 414 HOH B O   1 
HETATM 3333 O  O   . HOH M 5 .   ? -4.01300  5.89300  1.58600   1.000 44.56707 ? 415 HOH B O   1 
HETATM 3334 O  O   . HOH M 5 .   ? -5.65800  27.57000 -11.13100 1.000 37.40679 ? 416 HOH B O   1 
HETATM 3335 O  O   . HOH M 5 .   ? -31.77600 19.20700 5.91400   1.000 52.73293 ? 417 HOH B O   1 
HETATM 3336 O  O   . HOH M 5 .   ? -10.73900 26.78400 8.32100   1.000 42.50233 ? 418 HOH B O   1 
HETATM 3337 O  O   . HOH M 5 .   ? -5.89800  2.85100  17.35200  1.000 45.18282 ? 419 HOH B O   1 
HETATM 3338 O  O   B HOH M 5 .   ? -20.10900 16.16900 -8.31800  0.710 35.13322 ? 420 HOH B O   1 
HETATM 3339 O  O   . HOH M 5 .   ? -9.28900  23.56000 -15.78900 1.000 41.58595 ? 421 HOH B O   1 
HETATM 3340 O  O   . HOH M 5 .   ? -0.99900  19.82400 24.13300  1.000 48.64315 ? 422 HOH B O   1 
HETATM 3341 O  O   . HOH M 5 .   ? -1.93800  31.93600 -0.53000  1.000 55.80182 ? 423 HOH B O   1 
HETATM 3342 O  O   . HOH M 5 .   ? -25.78000 21.99000 -7.07600  1.000 34.41399 ? 424 HOH B O   1 
HETATM 3343 O  O   . HOH M 5 .   ? -7.15100  37.41600 0.41800   1.000 45.37136 ? 425 HOH B O   1 
HETATM 3344 O  O   . HOH M 5 .   ? -13.46100 24.73400 20.51500  1.000 28.48330 ? 426 HOH B O   1 
HETATM 3345 O  O   . HOH M 5 .   ? -21.16200 36.38100 6.91900   1.000 41.46753 ? 427 HOH B O   1 
HETATM 3346 O  O   . HOH M 5 .   ? -6.18000  29.25800 -13.09700 1.000 53.06217 ? 428 HOH B O   1 
HETATM 3347 O  O   . HOH M 5 .   ? -10.13200 1.11200  0.96700   1.000 33.65698 ? 429 HOH B O   1 
HETATM 3348 O  O   . HOH M 5 .   ? -24.20000 35.84200 5.50100   0.800 45.32147 ? 430 HOH B O   1 
HETATM 3349 O  O   . HOH M 5 .   ? -0.11000  29.06500 -3.40200  1.000 47.44323 ? 431 HOH B O   1 
HETATM 3350 O  O   . HOH M 5 .   ? -6.89400  18.05400 -12.75400 1.000 44.81958 ? 432 HOH B O   1 
HETATM 3351 O  O   . HOH M 5 .   ? -19.70700 18.43500 -11.21700 1.000 39.15712 ? 433 HOH B O   1 
HETATM 3352 O  O   . HOH M 5 .   ? -5.60600  36.06100 6.61600   1.000 49.63028 ? 434 HOH B O   1 
HETATM 3353 O  O   . HOH M 5 .   ? -7.82900  19.54200 9.81800   1.000 46.61651 ? 435 HOH B O   1 
HETATM 3354 O  O   . HOH M 5 .   ? -18.86300 31.00900 10.45400  1.000 40.29206 ? 436 HOH B O   1 
HETATM 3355 O  O   . HOH M 5 .   ? -7.57200  39.60700 14.51100  1.000 45.56674 ? 437 HOH B O   1 
HETATM 3356 O  O   . HOH M 5 .   ? -18.72400 27.05400 -14.31400 1.000 53.46900 ? 438 HOH B O   1 
HETATM 3357 O  O   . HOH M 5 .   ? -18.55300 14.19000 -7.57800  1.000 38.03384 ? 439 HOH B O   1 
HETATM 3358 O  O   . HOH M 5 .   ? -10.71000 29.21000 6.96000   1.000 36.15496 ? 440 HOH B O   1 
HETATM 3359 O  O   . HOH M 5 .   ? -23.77600 -1.40600 8.18900   1.000 58.06973 ? 441 HOH B O   1 
HETATM 3360 O  O   . HOH M 5 .   ? -8.45100  23.80400 11.34200  1.000 42.21220 ? 442 HOH B O   1 
HETATM 3361 O  O   . HOH M 5 .   ? -27.243   20.835   17.808    1.000 36.75664 ? 443 HOH B O   1 
HETATM 3362 O  O   . HOH M 5 .   ? -13.75800 34.97500 -8.62100  1.000 37.41465 ? 444 HOH B O   1 
HETATM 3363 O  O   . HOH M 5 .   ? -5.38500  5.54200  11.18600  1.000 32.95872 ? 445 HOH B O   1 
HETATM 3364 O  O   . HOH M 5 .   ? -8.77800  7.84800  -5.06500  1.000 61.34838 ? 446 HOH B O   1 
HETATM 3365 O  O   . HOH M 5 .   ? -9.23100  7.40800  24.81900  1.000 47.14500 ? 447 HOH B O   1 
HETATM 3366 O  O   . HOH M 5 .   ? -8.08200  26.15900 8.47900   1.000 41.58151 ? 448 HOH B O   1 
HETATM 3367 O  O   . HOH M 5 .   ? -26.189   -4.613   4.548     1.000 52.68330 ? 449 HOH B O   1 
HETATM 3368 O  O   . HOH M 5 .   ? -5.13900  3.05800  13.71400  1.000 41.88537 ? 450 HOH B O   1 
HETATM 3369 O  O   . HOH M 5 .   ? -0.12900  12.32300 18.72500  1.000 41.88032 ? 451 HOH B O   1 
HETATM 3370 O  O   . HOH M 5 .   ? -6.70400  28.57000 20.93400  1.000 49.84741 ? 452 HOH B O   1 
HETATM 3371 O  O   . HOH M 5 .   ? -0.87100  30.79100 3.75500   1.000 44.67366 ? 453 HOH B O   1 
HETATM 3372 O  O   . HOH M 5 .   ? -6.35700  34.68500 19.68400  1.000 36.50274 ? 454 HOH B O   1 
HETATM 3373 O  O   . HOH M 5 .   ? -12.580   1.334    -3.203    1.000 36.59470 ? 455 HOH B O   1 
HETATM 3374 O  O   . HOH M 5 .   ? -25.53200 34.46400 -6.95400  1.000 53.42255 ? 456 HOH B O   1 
HETATM 3375 O  O   . HOH M 5 .   ? -25.16800 35.52100 -4.87800  1.000 59.79029 ? 457 HOH B O   1 
HETATM 3376 O  O   . HOH M 5 .   ? -28.26200 29.56400 9.17400   1.000 52.81335 ? 458 HOH B O   1 
HETATM 3377 O  O   . HOH M 5 .   ? -12.71400 1.57700  20.01800  1.000 56.39919 ? 459 HOH B O   1 
HETATM 3378 O  O   . HOH M 5 .   ? -26.38600 20.88100 -4.29300  1.000 42.67749 ? 460 HOH B O   1 
HETATM 3379 O  O   . HOH M 5 .   ? -14.16200 31.58300 -12.37600 1.000 54.62003 ? 461 HOH B O   1 
HETATM 3380 O  O   A HOH M 5 .   ? -11.98100 23.48200 -17.19600 0.500 39.04068 ? 462 HOH B O   1 
HETATM 3381 O  O   . HOH M 5 .   ? -21.15300 25.66800 19.89200  1.000 48.22310 ? 463 HOH B O   1 
HETATM 3382 O  O   . HOH M 5 .   ? -3.55600  33.95300 5.81700   1.000 44.32304 ? 464 HOH B O   1 
HETATM 3383 O  O   . HOH M 5 .   ? -30.89400 21.90600 12.68200  0.620 36.29267 ? 465 HOH B O   1 
HETATM 3384 O  O   . HOH M 5 .   ? -28.012   -0.359   2.734     1.000 40.09284 ? 466 HOH B O   1 
HETATM 3385 O  O   . HOH M 5 .   ? -17.42900 37.03700 -1.95900  1.000 59.81757 ? 467 HOH B O   1 
HETATM 3386 O  O   . HOH M 5 .   ? -1.07900  7.61000  10.17000  1.000 42.67432 ? 468 HOH B O   1 
HETATM 3387 O  O   . HOH M 5 .   ? 0.69900   24.18600 -1.72500  1.000 46.05147 ? 469 HOH B O   1 
HETATM 3388 O  O   . HOH M 5 .   ? -10.26900 12.60300 23.79700  1.000 64.91646 ? 470 HOH B O   1 
HETATM 3389 O  O   . HOH M 5 .   ? -14.96800 5.09900  24.71600  1.000 54.24173 ? 471 HOH B O   1 
HETATM 3390 O  O   . HOH M 5 .   ? -4.58600  5.42000  22.00100  1.000 54.74784 ? 472 HOH B O   1 
HETATM 3391 O  O   . HOH M 5 .   ? 0.043     13.843   1.314     1.000 56.38384 ? 473 HOH B O   1 
HETATM 3392 O  O   . HOH M 5 .   ? -11.29200 26.52900 10.94800  1.000 49.39542 ? 474 HOH B O   1 
HETATM 3393 O  O   . HOH M 5 .   ? -32.17200 18.46900 8.00800   1.000 55.67288 ? 475 HOH B O   1 
HETATM 3394 O  O   . HOH M 5 .   ? -26.32900 32.50700 13.74300  1.000 56.47710 ? 476 HOH B O   1 
HETATM 3395 O  O   . HOH M 5 .   ? -7.84100  0.56000  2.62900   1.000 38.07172 ? 477 HOH B O   1 
HETATM 3396 O  O   . HOH M 5 .   ? -29.85900 28.65700 4.91700   1.000 54.30666 ? 478 HOH B O   1 
HETATM 3397 O  O   . HOH M 5 .   ? -13.88200 38.44600 0.31700   1.000 53.98250 ? 479 HOH B O   1 
HETATM 3398 O  O   . HOH M 5 .   ? -6.40200  23.27300 8.01600   1.000 52.66171 ? 480 HOH B O   1 
HETATM 3399 O  O   . HOH M 5 .   ? -14.18500 2.70900  -6.10900  1.000 47.91770 ? 481 HOH B O   1 
HETATM 3400 O  O   . HOH M 5 .   ? -11.74500 3.15300  12.33900  1.000 49.71246 ? 482 HOH B O   1 
HETATM 3401 O  O   . HOH M 5 .   ? -9.50200  3.97200  11.61800  1.000 46.03712 ? 483 HOH B O   1 
HETATM 3402 O  O   . HOH M 5 .   ? -15.95700 5.23600  17.60700  1.000 55.79200 ? 484 HOH B O   1 
HETATM 3403 O  O   . HOH M 5 .   ? -25.07700 0.00000  -0.00000  0.500 41.03232 ? 485 HOH B O   1 
HETATM 3404 O  O   . HOH M 5 .   ? -8.80600  25.96600 12.38600  1.000 47.97034 ? 486 HOH B O   1 
HETATM 3405 O  O   . HOH M 5 .   ? -30.37200 19.37400 11.85200  1.000 58.99067 ? 487 HOH B O   1 
HETATM 3406 O  O   . HOH M 5 .   ? -20.58800 18.19700 19.14800  1.000 38.71170 ? 488 HOH B O   1 
HETATM 3407 O  O   . HOH M 5 .   ? -8.12300  2.53800  -2.15800  1.000 58.94102 ? 489 HOH B O   1 
HETATM 3408 O  O   . HOH M 5 .   ? -4.74500  36.90800 18.21400  1.000 67.84456 ? 490 HOH B O   1 
HETATM 3409 O  O   . HOH M 5 .   ? -13.26500 35.09000 -1.58100  1.000 47.40466 ? 491 HOH B O   1 
HETATM 3410 O  O   . HOH M 5 .   ? -4.84500  1.13500  23.02100  1.000 61.38062 ? 492 HOH B O   1 
HETATM 3411 O  O   . HOH M 5 .   ? -26.37100 16.35300 17.49300  1.000 36.89623 ? 493 HOH B O   1 
HETATM 3412 O  O   . HOH M 5 .   ? -17.44700 40.02100 2.30800   1.000 41.25753 ? 494 HOH B O   1 
HETATM 3413 O  O   . HOH M 5 .   ? -32.24800 27.16100 10.07000  1.000 64.28393 ? 495 HOH B O   1 
HETATM 3414 O  O   . HOH M 5 .   ? -3.53100  7.23900  4.78300   1.000 45.08562 ? 496 HOH B O   1 
HETATM 3415 O  O   . HOH M 5 .   ? -35.71900 29.53800 -7.42100  1.000 46.16132 ? 497 HOH B O   1 
HETATM 3416 O  O   . HOH M 5 .   ? -14.784   33.804   24.710    1.000 45.32996 ? 498 HOH B O   1 
HETATM 3417 O  O   . HOH M 5 .   ? -19.91800 11.12600 -6.64700  1.000 34.02344 ? 499 HOH B O   1 
HETATM 3418 O  O   . HOH M 5 .   ? -11.66800 37.31000 -1.43100  1.000 49.79103 ? 500 HOH B O   1 
HETATM 3419 O  O   . HOH M 5 .   ? -26.418   36.218   11.264    1.000 42.52912 ? 501 HOH B O   1 
HETATM 3420 O  O   . HOH M 5 .   ? -9.01600  13.52300 21.22400  1.000 45.95768 ? 502 HOH B O   1 
HETATM 3421 O  O   . HOH M 5 .   ? -13.06200 27.04400 21.69600  1.000 42.13182 ? 503 HOH B O   1 
HETATM 3422 O  O   . HOH M 5 .   ? -8.66900  27.87400 22.81400  1.000 52.04076 ? 504 HOH B O   1 
HETATM 3423 O  O   . HOH M 5 .   ? -22.08100 0.00000  0.00000   0.610 43.44511 ? 505 HOH B O   1 
HETATM 3424 O  O   . HOH M 5 .   ? -10.82000 38.38000 3.24500   1.000 35.32502 ? 506 HOH B O   1 
HETATM 3425 O  O   . HOH M 5 .   ? -13.28100 15.05800 -10.94700 1.000 63.72924 ? 507 HOH B O   1 
HETATM 3426 O  O   . HOH M 5 .   ? -25.704   0.321    8.544     1.000 54.52197 ? 508 HOH B O   1 
HETATM 3427 O  O   . HOH M 5 .   ? -19.43900 20.06500 -13.33100 1.000 57.06550 ? 509 HOH B O   1 
HETATM 3428 O  O   A HOH M 5 .   ? -7.41000  24.52100 -17.41700 0.910 41.72011 ? 510 HOH B O   1 
HETATM 3429 O  O   . HOH M 5 .   ? -12.31500 35.01400 26.22100  1.000 56.46398 ? 511 HOH B O   1 
HETATM 3430 O  O   . HOH M 5 .   ? -15.142   31.470   29.468    1.000 61.29117 ? 512 HOH B O   1 
HETATM 3431 O  O   . HOH M 5 .   ? 0.35100   33.18100 6.69200   1.000 56.50740 ? 513 HOH B O   1 
HETATM 3432 O  O   . HOH M 5 .   ? -3.36600  34.29200 -7.97200  1.000 51.87073 ? 514 HOH B O   1 
HETATM 3433 O  O   . HOH M 5 .   ? -6.07800  23.51400 10.69800  1.000 48.07874 ? 515 HOH B O   1 
HETATM 3434 O  O   . HOH M 5 .   ? -7.63600  35.27500 -5.67700  1.000 37.92989 ? 516 HOH B O   1 
HETATM 3435 O  O   . HOH M 5 .   ? -5.93600  4.98800  8.74500   1.000 45.12687 ? 517 HOH B O   1 
HETATM 3436 O  O   . HOH M 5 .   ? -22.692   -5.909   8.417     1.000 49.83723 ? 518 HOH B O   1 
HETATM 3437 O  O   . HOH M 5 .   ? -14.59100 29.54700 21.33300  1.000 49.80909 ? 519 HOH B O   1 
HETATM 3438 O  O   . HOH M 5 .   ? -11.34400 34.06200 -12.81600 1.000 53.76367 ? 520 HOH B O   1 
HETATM 3439 O  O   . HOH M 5 .   ? -9.294    39.205   20.590    1.000 26.06943 ? 521 HOH B O   1 
HETATM 3440 O  O   . HOH M 5 .   ? -2.02600  26.63300 11.09700  1.000 35.82018 ? 522 HOH B O   1 
HETATM 3441 O  O   . HOH M 5 .   ? -10.25700 29.11100 9.41300   1.000 48.59314 ? 523 HOH B O   1 
HETATM 3442 O  O   . HOH M 5 .   ? -4.48900  25.68400 10.42400  1.000 32.07758 ? 524 HOH B O   1 
HETATM 3443 O  O   . HOH M 5 .   ? -19.78400 16.11400 19.33200  1.000 49.87355 ? 525 HOH B O   1 
HETATM 3444 O  O   . HOH M 5 .   ? -31.63100 15.36100 10.85600  1.000 60.47747 ? 526 HOH B O   1 
HETATM 3445 O  O   . HOH M 5 .   ? -6.62800  27.37800 10.60200  1.000 43.30669 ? 527 HOH B O   1 
HETATM 3446 O  O   . HOH M 5 .   ? -24.01100 25.21900 18.85700  1.000 48.87429 ? 528 HOH B O   1 
HETATM 3447 O  O   . HOH M 5 .   ? -6.41600  37.46000 -3.99500  1.000 50.97659 ? 529 HOH B O   1 
HETATM 3448 O  O   . HOH M 5 .   ? 1.882     9.436    16.400    1.000 55.18278 ? 530 HOH B O   1 
HETATM 3449 O  O   . HOH M 5 .   ? -15.36200 7.12500  -7.64900  1.000 55.49503 ? 531 HOH B O   1 
HETATM 3450 O  O   . HOH M 5 .   ? -23.61500 16.83200 -12.74100 1.000 50.83757 ? 532 HOH B O   1 
HETATM 3451 O  O   . HOH M 5 .   ? -10.02600 35.99800 -5.52900  1.000 39.59865 ? 533 HOH B O   1 
HETATM 3452 O  O   . HOH M 5 .   ? -19.72200 2.70200  14.37100  1.000 58.21881 ? 534 HOH B O   1 
HETATM 3453 O  O   . HOH M 5 .   ? -2.01700  31.92800 -3.87800  1.000 56.30075 ? 535 HOH B O   1 
HETATM 3454 O  O   . HOH M 5 .   ? -18.82200 31.42000 19.75500  1.000 47.71115 ? 536 HOH B O   1 
HETATM 3455 O  O   . HOH M 5 .   ? -1.46900  31.09300 -8.09000  1.000 53.58777 ? 537 HOH B O   1 
HETATM 3456 O  O   . HOH M 5 .   ? 0.91300   29.73200 -6.36700  1.000 54.22400 ? 538 HOH B O   1 
HETATM 3457 O  O   . HOH M 5 .   ? -18.27800 9.42500  -7.95600  1.000 46.99269 ? 539 HOH B O   1 
HETATM 3458 O  O   . HOH M 5 .   ? -12.27800 10.59400 26.70700  1.000 56.90645 ? 540 HOH B O   1 
HETATM 3459 O  O   . HOH M 5 .   ? -10.40700 37.98700 -3.62900  1.000 44.31764 ? 541 HOH B O   1 
HETATM 3460 O  O   . HOH M 5 .   ? -16.96300 10.73100 -9.38200  1.000 52.24973 ? 542 HOH B O   1 
HETATM 3461 O  O   . HOH M 5 .   ? -11.05400 36.75900 -8.28400  1.000 54.30121 ? 543 HOH B O   1 
HETATM 3462 O  O   . HOH M 5 .   ? -4.41500  1.10500  6.80000   1.000 61.42955 ? 544 HOH B O   1 
HETATM 3463 O  O   . HOH M 5 .   ? -10.58900 40.99700 -0.15600  1.000 53.50465 ? 545 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . MSE A 2   ? 1.01384 0.91298 1.31030 -0.40297 0.11131  0.12138  1   MSE A N   
2    C  CA  . MSE A 2   ? 0.94254 0.86004 1.26487 -0.38167 0.06838  0.05925  1   MSE A CA  
3    C  C   . MSE A 2   ? 0.99828 0.84953 1.22358 -0.32667 0.03656  0.04587  1   MSE A C   
4    O  O   . MSE A 2   ? 1.02260 0.86243 1.25722 -0.28293 -0.01406 0.00334  1   MSE A O   
5    C  CB  . MSE A 2   ? 1.04004 0.93113 1.43437 -0.39854 0.01413  0.02977  1   MSE A CB  
6    N  N   . ASP A 3   ? 0.92164 0.73574 1.05354 -0.32387 0.06577  0.08296  2   ASP A N   
7    C  CA  . ASP A 3   ? 0.78129 0.53212 0.82473 -0.27853 0.03564  0.07841  2   ASP A CA  
8    C  C   . ASP A 3   ? 0.69837 0.51109 0.69765 -0.23892 0.06395  0.06867  2   ASP A C   
9    O  O   . ASP A 3   ? 0.72639 0.60218 0.72828 -0.25038 0.11327  0.07871  2   ASP A O   
10   C  CB  . ASP A 3   ? 0.82735 0.46886 0.79253 -0.30151 0.03227  0.12534  2   ASP A CB  
11   C  CG  . ASP A 3   ? 1.11997 0.66518 1.10206 -0.31396 -0.02356 0.12312  2   ASP A CG  
12   O  OD1 . ASP A 3   ? 1.12689 0.66367 1.12309 -0.27188 -0.07540 0.08043  2   ASP A OD1 
13   O  OD2 . ASP A 3   ? 1.22141 0.72652 1.21085 -0.34093 -0.00975 0.15553  2   ASP A OD2 
14   N  N   . TYR A 4   ? 0.61958 0.41355 0.58176 -0.19072 0.02984  0.04952  3   TYR A N   
15   C  CA  . TYR A 4   ? 0.55391 0.39786 0.48788 -0.15267 0.04400  0.03845  3   TYR A CA  
16   C  C   . TYR A 4   ? 0.57133 0.34692 0.42385 -0.13136 0.01929  0.05455  3   TYR A C   
17   O  O   . TYR A 4   ? 0.66956 0.36917 0.49408 -0.13085 -0.01627 0.06391  3   TYR A O   
18   C  CB  . TYR A 4   ? 0.47543 0.38960 0.46925 -0.10894 0.02649  -0.00145 3   TYR A CB  
19   C  CG  . TYR A 4   ? 0.42520 0.41508 0.50019 -0.11946 0.04487  -0.02504 3   TYR A CG  
20   C  CD1 . TYR A 4   ? 0.34183 0.41035 0.43420 -0.11585 0.08765  -0.03152 3   TYR A CD1 
21   C  CD2 . TYR A 4   ? 0.41772 0.39838 0.55103 -0.12869 0.01393  -0.04439 3   TYR A CD2 
22   C  CE1 . TYR A 4   ? 0.35786 0.50200 0.52390 -0.12059 0.10318  -0.05468 3   TYR A CE1 
23   C  CE2 . TYR A 4   ? 0.44578 0.50143 0.65853 -0.13584 0.02517  -0.07001 3   TYR A CE2 
24   C  CZ  . TYR A 4   ? 0.37132 0.51313 0.60007 -0.13082 0.07185  -0.07426 3   TYR A CZ  
25   O  OH  . TYR A 4   ? 0.32819 0.55008 0.63514 -0.13440 0.08250  -0.10057 3   TYR A OH  
26   N  N   A ARG A 5   ? 0.54054 0.34141 0.35626 -0.11205 0.03418  0.05566  4   ARG A N   
27   N  N   B ARG A 5   ? 0.54217 0.34219 0.35701 -0.11287 0.03476  0.05625  4   ARG A N   
28   C  CA  A ARG A 5   ? 0.60935 0.36069 0.35816 -0.08948 0.00791  0.06630  4   ARG A CA  
29   C  CA  B ARG A 5   ? 0.59242 0.34433 0.34248 -0.08912 0.00745  0.06588  4   ARG A CA  
30   C  C   A ARG A 5   ? 0.56796 0.37758 0.34295 -0.05149 -0.00207 0.04701  4   ARG A C   
31   C  C   B ARG A 5   ? 0.56925 0.38118 0.34869 -0.05063 -0.00291 0.04585  4   ARG A C   
32   O  O   A ARG A 5   ? 0.53743 0.40964 0.34578 -0.04895 0.02555  0.03441  4   ARG A O   
33   O  O   B ARG A 5   ? 0.54193 0.42018 0.36184 -0.04670 0.02343  0.03163  4   ARG A O   
34   C  CB  A ARG A 5   ? 0.72876 0.43400 0.39453 -0.10882 0.03123  0.09392  4   ARG A CB  
35   C  CB  B ARG A 5   ? 0.73605 0.44161 0.40182 -0.10699 0.02946  0.09308  4   ARG A CB  
36   C  CG  A ARG A 5   ? 0.77797 0.43663 0.37389 -0.08319 0.00058  0.09986  4   ARG A CG  
37   C  CG  B ARG A 5   ? 0.81280 0.45125 0.44305 -0.14279 0.04130  0.12558  4   ARG A CG  
38   C  CD  A ARG A 5   ? 0.92173 0.52970 0.43551 -0.09383 0.01732  0.12416  4   ARG A CD  
39   C  CD  B ARG A 5   ? 0.90295 0.52810 0.46475 -0.14875 0.07392  0.15001  4   ARG A CD  
40   N  NE  A ARG A 5   ? 0.93107 0.53878 0.41106 -0.06385 -0.00473 0.11196  4   ARG A NE  
41   N  NE  B ARG A 5   ? 0.92506 0.63049 0.51556 -0.14796 0.11343  0.13828  4   ARG A NE  
42   C  CZ  A ARG A 5   ? 0.84357 0.48772 0.31916 -0.05369 0.00814  0.09811  4   ARG A CZ  
43   C  CZ  B ARG A 5   ? 0.92238 0.67487 0.55091 -0.16777 0.15265  0.15204  4   ARG A CZ  
44   N  NH1 A ARG A 5   ? 0.81827 0.51202 0.32195 -0.06542 0.04612  0.09316  4   ARG A NH1 
45   N  NH1 B ARG A 5   ? 0.93183 0.65648 0.57712 -0.19735 0.16146  0.18257  4   ARG A NH1 
46   N  NH2 A ARG A 5   ? 0.84384 0.47638 0.29342 -0.03062 -0.01943 0.08644  4   ARG A NH2 
47   N  NH2 B ARG A 5   ? 0.78573 0.61544 0.44184 -0.15370 0.17844  0.13721  4   ARG A NH2 
48   N  N   . ILE A 6   ? 0.52126 0.31121 0.28367 -0.02146 -0.04114 0.04790  5   ILE A N   
49   C  CA  . ILE A 6   ? 0.49976 0.34366 0.29458 0.01161  -0.05294 0.03986  5   ILE A CA  
50   C  C   . ILE A 6   ? 0.55160 0.35943 0.28842 0.00874  -0.06395 0.05165  5   ILE A C   
51   O  O   . ILE A 6   ? 0.61044 0.35278 0.28594 0.00730  -0.08700 0.06490  5   ILE A O   
52   C  CB  . ILE A 6   ? 0.49251 0.35339 0.32005 0.05200  -0.08905 0.03609  5   ILE A CB  
53   C  CG1 . ILE A 6   ? 0.51637 0.39850 0.38782 0.06187  -0.08867 0.01854  5   ILE A CG1 
54   C  CG2 . ILE A 6   ? 0.47158 0.40049 0.34665 0.08453  -0.09564 0.03788  5   ILE A CG2 
55   C  CD1 . ILE A 6   ? 0.41228 0.36770 0.34131 0.06055  -0.05444 0.00229  5   ILE A CD1 
56   N  N   . ARG A 7   ? 0.47322 0.31850 0.22716 0.01137  -0.05255 0.04492  6   ARG A N   
57   C  CA  . ARG A 7   ? 0.49979 0.31164 0.20637 0.01305  -0.07360 0.04889  6   ARG A CA  
58   C  C   . ARG A 7   ? 0.45118 0.31702 0.22039 0.02732  -0.08298 0.04164  6   ARG A C   
59   O  O   . ARG A 7   ? 0.40579 0.33231 0.24247 0.03495  -0.06256 0.03607  6   ARG A O   
60   C  CB  . ARG A 7   ? 0.61258 0.38012 0.24102 -0.00685 -0.04959 0.04957  6   ARG A CB  
61   C  CG  . ARG A 7   ? 0.55132 0.36392 0.20484 -0.01602 -0.00696 0.03750  6   ARG A CG  
62   C  CD  . ARG A 7   ? 0.64445 0.42009 0.21540 -0.02023 0.00816  0.03686  6   ARG A CD  
63   N  NE  . ARG A 7   ? 0.61231 0.43568 0.20576 -0.02352 0.04965  0.02590  6   ARG A NE  
64   C  CZ  . ARG A 7   ? 0.63285 0.48174 0.24436 -0.00973 0.05016  0.00676  6   ARG A CZ  
65   N  NH1 . ARG A 7   ? 0.60288 0.43425 0.22257 0.00268  0.01124  -0.00171 6   ARG A NH1 
66   N  NH2 . ARG A 7   ? 0.60381 0.50424 0.24632 -0.00720 0.08117  -0.00219 6   ARG A NH2 
67   N  N   . THR A 8   ? 0.51050 0.35096 0.25768 0.03104  -0.11616 0.04267  7   THR A N   
68   C  CA  A THR A 8   ? 0.49261 0.37116 0.30047 0.03560  -0.12787 0.03776  7   THR A CA  
69   C  CA  B THR A 8   ? 0.49623 0.37282 0.30185 0.03542  -0.12878 0.03765  7   THR A CA  
70   C  C   . THR A 8   ? 0.46070 0.33744 0.25355 0.02509  -0.09679 0.02167  7   THR A C   
71   O  O   . THR A 8   ? 0.53752 0.37011 0.25018 0.01623  -0.07990 0.01376  7   THR A O   
72   C  CB  A THR A 8   ? 0.51929 0.37047 0.31737 0.03654  -0.17039 0.03580  7   THR A CB  
73   C  CB  B THR A 8   ? 0.53093 0.37452 0.31787 0.03590  -0.17018 0.03505  7   THR A CB  
74   O  OG1 A THR A 8   ? 0.61215 0.39307 0.31159 0.03031  -0.17303 0.02426  7   THR A OG1 
75   O  OG1 B THR A 8   ? 0.54096 0.39642 0.34613 0.04341  -0.17480 0.04280  7   THR A OG1 
76   C  CG2 A THR A 8   ? 0.50091 0.38267 0.34253 0.04585  -0.17612 0.04530  7   THR A CG2 
77   C  CG2 B THR A 8   ? 0.51663 0.39558 0.38090 0.03604  -0.19288 0.03470  7   THR A CG2 
78   N  N   . SER A 9   ? 0.38799 0.31572 0.25713 0.03047  -0.08694 0.01988  8   SER A N   
79   C  CA  . SER A 9   ? 0.39100 0.31500 0.24736 0.02697  -0.06337 0.00296  8   SER A CA  
80   C  C   . SER A 9   ? 0.46629 0.33300 0.27868 0.02409  -0.09916 -0.01132 8   SER A C   
81   O  O   . SER A 9   ? 0.51977 0.37166 0.35390 0.02309  -0.14491 -0.00619 8   SER A O   
82   C  CB  . SER A 9   ? 0.34782 0.33666 0.29670 0.03778  -0.04451 0.00834  8   SER A CB  
83   O  OG  . SER A 9   ? 0.28697 0.32736 0.27150 0.04898  -0.02014 0.01715  8   SER A OG  
84   N  N   . ARG A 10  ? 0.48688 0.32331 0.23610 0.02664  -0.08111 -0.03143 9   ARG A N   
85   C  CA  . ARG A 10  ? 0.62770 0.40183 0.31997 0.03283  -0.11739 -0.05293 9   ARG A CA  
86   C  C   . ARG A 10  ? 0.61708 0.39600 0.33262 0.04045  -0.10603 -0.06977 9   ARG A C   
87   O  O   . ARG A 10  ? 0.50594 0.33589 0.26054 0.04299  -0.06173 -0.06511 9   ARG A O   
88   C  CB  . ARG A 10  ? 0.72677 0.44665 0.29147 0.04195  -0.11048 -0.06253 9   ARG A CB  
89   C  CG  . ARG A 10  ? 0.73841 0.44510 0.27103 0.03584  -0.11568 -0.04223 9   ARG A CG  
90   C  CD  . ARG A 10  ? 0.90263 0.58128 0.35992 0.04467  -0.09528 -0.03956 9   ARG A CD  
91   N  NE  . ARG A 10  ? 1.04454 0.75929 0.49292 0.03800  -0.03680 -0.02811 9   ARG A NE  
92   C  CZ  . ARG A 10  ? 1.01164 0.73682 0.45768 0.02399  -0.01108 -0.00488 9   ARG A CZ  
93   N  NH1 . ARG A 10  ? 0.99754 0.69387 0.43851 0.01903  -0.03583 0.00858  9   ARG A NH1 
94   N  NH2 . ARG A 10  ? 0.91028 0.67752 0.36762 0.01512  0.03560  0.00507  9   ARG A NH2 
95   N  N   . ASP A 11  ? 0.61666 0.40427 0.28549 0.01129  -0.15218 0.04666  10  ASP A N   
96   C  CA  . ASP A 11  ? 0.58998 0.39758 0.26699 0.03306  -0.14650 0.01837  10  ASP A CA  
97   C  C   . ASP A 11  ? 0.53230 0.39122 0.19050 0.02685  -0.11348 0.00488  10  ASP A C   
98   O  O   . ASP A 11  ? 0.49300 0.37416 0.19431 0.04065  -0.09914 -0.01292 10  ASP A O   
99   C  CB  . ASP A 11  ? 0.69583 0.49684 0.36185 0.04631  -0.16695 -0.00261 10  ASP A CB  
100  C  CG  . ASP A 11  ? 0.89580 0.65827 0.61209 0.05600  -0.19112 0.00134  10  ASP A CG  
101  O  OD1 . ASP A 11  ? 1.07984 0.82000 0.78004 0.05012  -0.20805 0.00640  10  ASP A OD1 
102  O  OD2 . ASP A 11  ? 0.92371 0.68389 0.69813 0.06571  -0.19005 -0.00141 10  ASP A OD2 
103  N  N   . GLU A 12  ? 0.58414 0.46415 0.17882 0.00335  -0.10345 0.01371  11  GLU A N   
104  C  CA  . GLU A 12  ? 0.60430 0.54469 0.18219 -0.00636 -0.06961 -0.00225 11  GLU A CA  
105  C  C   . GLU A 12  ? 0.58825 0.53667 0.20489 -0.01198 -0.04889 0.01132  11  GLU A C   
106  O  O   . GLU A 12  ? 0.61734 0.61520 0.24487 -0.01146 -0.02249 -0.00933 11  GLU A O   
107  C  CB  . GLU A 12  ? 0.66108 0.63377 0.18715 -0.03175 -0.05992 0.01016  11  GLU A CB  
108  C  CG  . GLU A 12  ? 0.77898 0.71286 0.30677 -0.05465 -0.07173 0.05575  11  GLU A CG  
109  C  CD  . GLU A 12  ? 0.94766 0.89408 0.42831 -0.08053 -0.07097 0.07306  11  GLU A CD  
110  O  OE1 . GLU A 12  ? 1.06694 1.05721 0.50994 -0.08063 -0.05603 0.05002  11  GLU A OE1 
111  O  OE2 . GLU A 12  ? 0.96281 0.87222 0.44562 -0.10154 -0.08805 0.10711  11  GLU A OE2 
112  N  N   . ASP A 13  ? 0.53590 0.44050 0.17898 -0.01522 -0.06198 0.04008  12  ASP A N   
113  C  CA  . ASP A 13  ? 0.49579 0.40794 0.17706 -0.01815 -0.04513 0.04927  12  ASP A CA  
114  C  C   . ASP A 13  ? 0.46744 0.38643 0.20823 0.00671  -0.03923 0.02857  12  ASP A C   
115  O  O   . ASP A 13  ? 0.42408 0.36078 0.19137 0.00583  -0.02213 0.02827  12  ASP A O   
116  C  CB  . ASP A 13  ? 0.49882 0.36703 0.19193 -0.02877 -0.06460 0.08023  12  ASP A CB  
117  C  CG  . ASP A 13  ? 0.57185 0.43368 0.23825 -0.05272 -0.07437 0.10151  12  ASP A CG  
118  O  OD1 . ASP A 13  ? 0.64842 0.54452 0.28695 -0.07187 -0.05523 0.10627  12  ASP A OD1 
119  O  OD2 . ASP A 13  ? 0.56989 0.39430 0.24883 -0.05246 -0.10179 0.11034  12  ASP A OD2 
120  N  N   . ALA A 14  ? 0.43422 0.33813 0.19566 0.02614  -0.05630 0.01348  13  ALA A N   
121  C  CA  . ALA A 14  ? 0.39952 0.29981 0.21521 0.04128  -0.05871 0.00603  13  ALA A CA  
122  C  C   . ALA A 14  ? 0.37081 0.30478 0.20521 0.04740  -0.04225 -0.01315 13  ALA A C   
123  O  O   . ALA A 14  ? 0.38662 0.32080 0.25450 0.04853  -0.03764 -0.00759 13  ALA A O   
124  C  CB  . ALA A 14  ? 0.43546 0.31521 0.26941 0.05628  -0.08337 -0.00479 13  ALA A CB  
125  N  N   . ALA A 15  ? 0.41622 0.38253 0.23120 0.05159  -0.03527 -0.03948 14  ALA A N   
126  C  CA  . ALA A 15  ? 0.39253 0.39382 0.23710 0.06200  -0.02560 -0.06745 14  ALA A CA  
127  C  C   . ALA A 15  ? 0.39388 0.41361 0.24630 0.04904  -0.00251 -0.05508 14  ALA A C   
128  O  O   . ALA A 15  ? 0.37239 0.40750 0.26243 0.05869  -0.00097 -0.07156 14  ALA A O   
129  C  CB  . ALA A 15  ? 0.39232 0.43886 0.21700 0.06856  -0.01985 -0.10660 14  ALA A CB  
130  N  N   . LEU A 16  ? 0.36578 0.38025 0.18718 0.02746  0.00982  -0.02651 15  LEU A N   
131  C  CA  . LEU A 16  ? 0.38378 0.41266 0.21362 0.01374  0.02819  -0.01333 15  LEU A CA  
132  C  C   . LEU A 16  ? 0.36798 0.36568 0.22956 0.01680  0.02051  0.00574  15  LEU A C   
133  O  O   . LEU A 16  ? 0.34715 0.35525 0.22470 0.01056  0.03192  0.01154  15  LEU A O   
134  C  CB  . LEU A 16  ? 0.36608 0.40056 0.14956 -0.01442 0.03767  0.01065  15  LEU A CB  
135  C  CG  . LEU A 16  ? 0.43582 0.51736 0.17608 -0.02812 0.05237  -0.00523 15  LEU A CG  
136  C  CD1 . LEU A 16  ? 0.48902 0.56296 0.18368 -0.06170 0.05309  0.03003  15  LEU A CD1 
137  C  CD2 . LEU A 16  ? 0.46969 0.61094 0.23726 -0.02384 0.07592  -0.03803 15  LEU A CD2 
138  N  N   . LEU A 17  ? 0.34837 0.31395 0.21967 0.02453  0.00218  0.01372  16  LEU A N   
139  C  CA  . LEU A 17  ? 0.32352 0.27216 0.21964 0.02291  -0.00167 0.02907  16  LEU A CA  
140  C  C   . LEU A 17  ? 0.32786 0.28502 0.25616 0.02954  -0.00087 0.02279  16  LEU A C   
141  O  O   . LEU A 17  ? 0.29724 0.25725 0.23870 0.02427  0.00504  0.03122  16  LEU A O   
142  C  CB  . LEU A 17  ? 0.32281 0.24537 0.22195 0.02536  -0.01945 0.03684  16  LEU A CB  
143  C  CG  . LEU A 17  ? 0.38827 0.29332 0.25523 0.01796  -0.02882 0.04588  16  LEU A CG  
144  C  CD1 . LEU A 17  ? 0.45730 0.33764 0.33913 0.02330  -0.04960 0.04873  16  LEU A CD1 
145  C  CD2 . LEU A 17  ? 0.40293 0.30505 0.25753 0.00194  -0.02456 0.06234  16  LEU A CD2 
146  N  N   . PRO A 18  ? 0.32833 0.28707 0.27114 0.04014  -0.01176 0.00844  17  PRO A N   
147  C  CA  . PRO A 18  ? 0.30644 0.26649 0.27618 0.04153  -0.01795 0.00859  17  PRO A CA  
148  C  C   . PRO A 18  ? 0.33765 0.31752 0.31333 0.03881  -0.00236 0.00422  17  PRO A C   
149  O  O   . PRO A 18  ? 0.31312 0.29118 0.30012 0.03369  -0.00295 0.01413  17  PRO A O   
150  C  CB  . PRO A 18  ? 0.33503 0.28845 0.32280 0.05431  -0.04068 -0.00916 17  PRO A CB  
151  C  CG  . PRO A 18  ? 0.33582 0.27544 0.30916 0.05701  -0.04935 -0.00849 17  PRO A CG  
152  C  CD  . PRO A 18  ? 0.29560 0.24693 0.23566 0.05084  -0.02790 -0.00600 17  PRO A CD  
153  N  N   . ALA A 19  ? 0.29983 0.30328 0.26689 0.03928  0.01240  -0.01023 18  ALA A N   
154  C  CA  . ALA A 19  ? 0.29422 0.31960 0.27352 0.03483  0.02673  -0.01459 18  ALA A CA  
155  C  C   . ALA A 19  ? 0.29125 0.30794 0.26296 0.02214  0.03537  0.00804  18  ALA A C   
156  O  O   . ALA A 19  ? 0.28472 0.30750 0.27377 0.02048  0.03857  0.00881  18  ALA A O   
157  C  CB  . ALA A 19  ? 0.29692 0.36114 0.26873 0.03178  0.04439  -0.03457 18  ALA A CB  
158  N  N   . ILE A 20  ? 0.30132 0.30253 0.25193 0.01481  0.03446  0.02325  19  ILE A N   
159  C  CA  . ILE A 20  ? 0.29458 0.28517 0.24911 0.00677  0.03418  0.03820  19  ILE A CA  
160  C  C   . ILE A 20  ? 0.28244 0.26880 0.25643 0.01208  0.02723  0.03807  19  ILE A C   
161  O  O   . ILE A 20  ? 0.27859 0.27083 0.26630 0.00989  0.02944  0.03851  19  ILE A O   
162  C  CB  . ILE A 20  ? 0.31610 0.28687 0.25094 -0.00043 0.02569  0.05101  19  ILE A CB  
163  C  CG1 . ILE A 20  ? 0.33696 0.31732 0.24317 -0.01468 0.03338  0.05703  19  ILE A CG1 
164  C  CG2 . ILE A 20  ? 0.36306 0.32057 0.31649 -0.00283 0.01599  0.05809  19  ILE A CG2 
165  C  CD1 . ILE A 20  ? 0.39865 0.35455 0.27432 -0.02456 0.01875  0.07243  19  ILE A CD1 
166  N  N   . GLU A 21  ? 0.29703 0.27696 0.27169 0.01652  0.01800  0.03737  20  GLU A N   
167  C  CA  . GLU A 21  ? 0.29727 0.28306 0.28387 0.01358  0.01376  0.04024  20  GLU A CA  
168  C  C   . GLU A 21  ? 0.29170 0.28510 0.28569 0.01292  0.01277  0.03837  20  GLU A C   
169  O  O   . GLU A 21  ? 0.30306 0.30785 0.30124 0.00764  0.01443  0.03975  20  GLU A O   
170  C  CB  . GLU A 21  ? 0.27793 0.25735 0.26429 0.01190  0.00255  0.04478  20  GLU A CB  
171  C  CG  . GLU A 21  ? 0.30600 0.30388 0.30013 0.00075  0.00230  0.04961  20  GLU A CG  
172  C  CD  . GLU A 21  ? 0.39378 0.39087 0.39094 -0.00743 -0.00845 0.05782  20  GLU A CD  
173  O  OE1 . GLU A 21  ? 0.40998 0.42659 0.40778 -0.02361 -0.00980 0.06652  20  GLU A OE1 
174  O  OE2 . GLU A 21  ? 0.34628 0.32545 0.34360 -0.00054 -0.01647 0.05674  20  GLU A OE2 
175  N  N   A ARG A 22  ? 0.27100 0.26086 0.26931 0.01925  0.00779  0.03103  21  ARG A N   
176  N  N   B ARG A 22  ? 0.27754 0.26742 0.27578 0.01928  0.00791  0.03098  21  ARG A N   
177  C  CA  A ARG A 22  ? 0.28313 0.27613 0.29548 0.02071  0.00053  0.02635  21  ARG A CA  
178  C  CA  B ARG A 22  ? 0.28470 0.27756 0.29704 0.02088  0.00045  0.02618  21  ARG A CA  
179  C  C   A ARG A 22  ? 0.29908 0.30561 0.31785 0.01918  0.01409  0.02275  21  ARG A C   
180  C  C   B ARG A 22  ? 0.28874 0.29519 0.30771 0.01936  0.01389  0.02252  21  ARG A C   
181  O  O   A ARG A 22  ? 0.28437 0.29334 0.30823 0.01602  0.00902  0.02492  21  ARG A O   
182  O  O   B ARG A 22  ? 0.29935 0.30792 0.32396 0.01646  0.00832  0.02441  21  ARG A O   
183  C  CB  A ARG A 22  ? 0.29474 0.28645 0.32321 0.03198  -0.01044 0.00924  21  ARG A CB  
184  C  CB  B ARG A 22  ? 0.30560 0.29722 0.33361 0.03222  -0.01031 0.00898  21  ARG A CB  
185  C  CG  A ARG A 22  ? 0.34101 0.31306 0.37276 0.03482  -0.03452 0.01134  21  ARG A CG  
186  C  CG  B ARG A 22  ? 0.34223 0.32246 0.39126 0.03509  -0.03606 0.00571  21  ARG A CG  
187  C  CD  A ARG A 22  ? 0.42080 0.38824 0.48324 0.04845  -0.05860 -0.01062 21  ARG A CD  
188  C  CD  B ARG A 22  ? 0.39234 0.37221 0.46872 0.05091  -0.05378 -0.02008 21  ARG A CD  
189  N  NE  A ARG A 22  ? 0.51462 0.46249 0.58344 0.05367  -0.08299 -0.01284 21  ARG A NE  
190  N  NE  B ARG A 22  ? 0.43340 0.40919 0.50058 0.05569  -0.05529 -0.02452 21  ARG A NE  
191  C  CZ  A ARG A 22  ? 0.49855 0.45619 0.56721 0.06555  -0.07822 -0.03337 21  ARG A CZ  
192  C  CZ  B ARG A 22  ? 0.49946 0.44850 0.56969 0.05472  -0.08283 -0.01488 21  ARG A CZ  
193  N  NH1 A ARG A 22  ? 0.52071 0.45699 0.59896 0.07106  -0.10528 -0.03574 21  ARG A NH1 
194  N  NH1 B ARG A 22  ? 0.49735 0.44377 0.56136 0.06086  -0.08428 -0.02208 21  ARG A NH1 
195  N  NH2 A ARG A 22  ? 0.40252 0.39242 0.46001 0.06918  -0.04846 -0.05038 21  ARG A NH2 
196  N  NH2 B ARG A 22  ? 0.57718 0.50135 0.65487 0.04461  -0.11149 0.00436  21  ARG A NH2 
197  N  N   . SER A 23  ? 0.26881 0.28357 0.28548 0.01850  0.02868  0.01940  22  SER A N   
198  C  CA  . SER A 23  ? 0.25751 0.28211 0.28445 0.01382  0.03773  0.01935  22  SER A CA  
199  C  C   . SER A 23  ? 0.28548 0.30576 0.31330 0.01101  0.03422  0.02522  22  SER A C   
200  O  O   . SER A 23  ? 0.26924 0.29580 0.31017 0.01109  0.03255  0.02109  22  SER A O   
201  C  CB  . SER A 23  ? 0.26475 0.29707 0.28365 0.00568  0.04993  0.02235  22  SER A CB  
202  O  OG  . SER A 23  ? 0.26587 0.30434 0.29819 -0.00292 0.05432  0.02673  22  SER A OG  
203  N  N   . ALA A 24  ? 0.23800 0.25157 0.25665 0.00992  0.03168  0.02980  23  ALA A N   
204  C  CA  . ALA A 24  ? 0.23424 0.25483 0.26242 0.00993  0.02783  0.02481  23  ALA A CA  
205  C  C   . ALA A 24  ? 0.24717 0.28444 0.27400 0.00826  0.02601  0.02007  23  ALA A C   
206  O  O   . ALA A 24  ? 0.25952 0.31120 0.29673 0.00913  0.02485  0.00959  23  ALA A O   
207  C  CB  . ALA A 24  ? 0.23885 0.25576 0.26470 0.01042  0.02371  0.02479  23  ALA A CB  
208  N  N   . GLY A 25  ? 0.23345 0.26830 0.24657 0.00409  0.02165  0.02802  24  GLY A N   
209  C  CA  . GLY A 25  ? 0.27118 0.31905 0.27379 -0.00504 0.01504  0.03119  24  GLY A CA  
210  C  C   . GLY A 25  ? 0.23584 0.28187 0.24366 -0.00297 0.00905  0.02754  24  GLY A C   
211  O  O   . GLY A 25  ? 0.26615 0.32375 0.26005 -0.01248 0.00163  0.03026  24  GLY A O   
212  N  N   . GLU A 26  ? 0.23765 0.27351 0.26415 0.00646  0.01187  0.02151  25  GLU A N   
213  C  CA  . GLU A 26  ? 0.23862 0.27512 0.27841 0.00926  0.00538  0.01502  25  GLU A CA  
214  C  C   . GLU A 26  ? 0.23499 0.28758 0.27534 0.00806  0.00586  0.00627  25  GLU A C   
215  O  O   . GLU A 26  ? 0.23267 0.28673 0.27536 0.00805  -0.00423 0.00203  25  GLU A O   
216  C  CB  . GLU A 26  ? 0.24225 0.27743 0.30731 0.01559  0.01290  0.00785  25  GLU A CB  
217  C  CG  . GLU A 26  ? 0.24346 0.27459 0.31533 0.01985  0.01081  0.00458  25  GLU A CG  
218  C  CD  . GLU A 26  ? 0.31765 0.34056 0.40282 0.02417  -0.01076 -0.00117 25  GLU A CD  
219  O  OE1 . GLU A 26  ? 0.32320 0.34753 0.41999 0.02456  -0.01824 -0.00533 25  GLU A OE1 
220  O  OE2 . GLU A 26  ? 0.35662 0.36875 0.44442 0.02790  -0.02494 -0.00281 25  GLU A OE2 
221  N  N   . SER A 27  ? 0.26377 0.32935 0.30557 0.00865  0.01352  -0.00063 26  SER A N   
222  C  CA  . SER A 27  ? 0.26623 0.35373 0.31638 0.01121  0.01115  -0.01879 26  SER A CA  
223  C  C   . SER A 27  ? 0.27398 0.38652 0.29626 0.00091  0.00743  -0.02108 26  SER A C   
224  O  O   . SER A 27  ? 0.32898 0.46372 0.35384 0.00301  0.00380  -0.03934 26  SER A O   
225  C  CB  . SER A 27  ? 0.29427 0.39307 0.36030 0.01609  0.01432  -0.03211 26  SER A CB  
226  O  OG  . SER A 27  ? 0.32612 0.39792 0.41160 0.02016  0.01217  -0.02465 26  SER A OG  
227  N  N   . PHE A 28  ? 0.19706 0.30726 0.19131 -0.01269 0.00542  -0.00222 27  PHE A N   
228  C  CA  . PHE A 28  ? 0.22318 0.35831 0.18264 -0.03153 -0.00023 0.00346  27  PHE A CA  
229  C  C   . PHE A 28  ? 0.22639 0.34024 0.17188 -0.03656 -0.02105 0.01489  27  PHE A C   
230  O  O   . PHE A 28  ? 0.26010 0.39330 0.17037 -0.05532 -0.02992 0.02139  27  PHE A O   
231  C  CB  . PHE A 28  ? 0.25238 0.39293 0.18865 -0.05051 0.00119  0.02429  27  PHE A CB  
232  C  CG  . PHE A 28  ? 0.21749 0.39500 0.16384 -0.05093 0.01987  0.00861  27  PHE A CG  
233  C  CD1 . PHE A 28  ? 0.24805 0.48460 0.17997 -0.06594 0.03064  -0.00691 27  PHE A CD1 
234  C  CD2 . PHE A 28  ? 0.28790 0.44493 0.26065 -0.03609 0.02521  0.00563  27  PHE A CD2 
235  C  CE1 . PHE A 28  ? 0.26203 0.53899 0.21502 -0.06383 0.04593  -0.02916 27  PHE A CE1 
236  C  CE2 . PHE A 28  ? 0.24127 0.42851 0.23035 -0.03452 0.03634  -0.01130 27  PHE A CE2 
237  C  CZ  . PHE A 28  ? 0.24193 0.48898 0.22667 -0.04640 0.04623  -0.03095 27  PHE A CZ  
238  N  N   . ARG A 29  ? 0.27005 0.34947 0.24256 -0.02213 -0.03022 0.01556  28  ARG A N   
239  C  CA  . ARG A 29  ? 0.25535 0.31314 0.22250 -0.02540 -0.05563 0.02329  28  ARG A CA  
240  C  C   . ARG A 29  ? 0.25460 0.33130 0.21204 -0.02615 -0.06125 0.00914  28  ARG A C   
241  O  O   . ARG A 29  ? 0.29882 0.36280 0.23491 -0.03642 -0.08599 0.01950  28  ARG A O   
242  C  CB  . ARG A 29  ? 0.30193 0.33150 0.31107 -0.00814 -0.06234 0.01755  28  ARG A CB  
243  C  CG  . ARG A 29  ? 0.26463 0.27729 0.28401 -0.00545 -0.06253 0.02558  28  ARG A CG  
244  C  CD  . ARG A 29  ? 0.25892 0.25400 0.31916 0.00879  -0.07615 0.01391  28  ARG A CD  
245  N  NE  . ARG A 29  ? 0.27775 0.26630 0.34907 0.01398  -0.07302 0.01332  28  ARG A NE  
246  C  CZ  . ARG A 29  ? 0.27436 0.24070 0.33776 0.00877  -0.09788 0.02528  28  ARG A CZ  
247  N  NH1 . ARG A 29  ? 0.33499 0.27964 0.37699 -0.00609 -0.13099 0.04452  28  ARG A NH1 
248  N  NH2 . ARG A 29  ? 0.29101 0.25512 0.36724 0.01641  -0.09364 0.01928  28  ARG A NH2 
249  N  N   . LEU A 30  ? 0.25532 0.35888 0.22985 -0.01516 -0.04445 -0.01525 29  LEU A N   
250  C  CA  . LEU A 30  ? 0.25671 0.38104 0.22645 -0.01275 -0.05201 -0.03518 29  LEU A CA  
251  C  C   . LEU A 30  ? 0.27567 0.45231 0.20689 -0.02756 -0.04287 -0.04722 29  LEU A C   
252  O  O   . LEU A 30  ? 0.28858 0.49490 0.21863 -0.02261 -0.04562 -0.07400 29  LEU A O   
253  C  CB  . LEU A 30  ? 0.36670 0.48681 0.38841 0.00914  -0.04801 -0.05859 29  LEU A CB  
254  C  CG  . LEU A 30  ? 0.38826 0.47167 0.44409 0.01738  -0.05783 -0.04974 29  LEU A CG  
255  C  CD1 . LEU A 30  ? 0.42152 0.50270 0.52576 0.03115  -0.05919 -0.06782 29  LEU A CD1 
256  C  CD2 . LEU A 30  ? 0.49031 0.55679 0.52724 0.01077  -0.08234 -0.03987 29  LEU A CD2 
257  N  N   . LEU A 31  ? 0.24865 0.38030 0.23529 -0.03689 -0.08221 0.00963  30  LEU A N   
258  C  CA  . LEU A 31  ? 0.28911 0.42295 0.21628 -0.04918 -0.07548 -0.00033 30  LEU A CA  
259  C  C   . LEU A 31  ? 0.29592 0.40766 0.18677 -0.06575 -0.08429 0.01639  30  LEU A C   
260  O  O   . LEU A 31  ? 0.32656 0.44179 0.21631 -0.07348 -0.07276 0.02652  30  LEU A O   
261  C  CB  . LEU A 31  ? 0.31788 0.48622 0.24120 -0.05020 -0.04538 -0.01023 30  LEU A CB  
262  C  CG  . LEU A 31  ? 0.32984 0.52312 0.29131 -0.03522 -0.03392 -0.02573 30  LEU A CG  
263  C  CD1 . LEU A 31  ? 0.29908 0.52591 0.25296 -0.03946 -0.00596 -0.03187 30  LEU A CD1 
264  C  CD2 . LEU A 31  ? 0.40626 0.59216 0.35753 -0.02550 -0.04834 -0.04251 30  LEU A CD2 
265  N  N   . PRO A 32  ? 0.34131 0.42711 0.19931 -0.07263 -0.10718 0.02004  31  PRO A N   
266  C  CA  . PRO A 32  ? 0.40336 0.46438 0.23496 -0.08865 -0.12079 0.03947  31  PRO A CA  
267  C  C   . PRO A 32  ? 0.47517 0.54976 0.27196 -0.10532 -0.10233 0.04624  31  PRO A C   
268  O  O   . PRO A 32  ? 0.47871 0.53755 0.28135 -0.11355 -0.10726 0.06253  31  PRO A O   
269  C  CB  . PRO A 32  ? 0.44314 0.47741 0.24002 -0.09182 -0.14431 0.03721  31  PRO A CB  
270  C  CG  . PRO A 32  ? 0.40989 0.44295 0.23892 -0.07621 -0.15860 0.02518  31  PRO A CG  
271  C  CD  . PRO A 32  ? 0.36442 0.43422 0.21559 -0.06499 -0.12895 0.00898  31  PRO A CD  
272  N  N   . GLU A 33  ? 0.43549 0.53619 0.20860 -0.10583 -0.07917 0.03456  32  GLU A N   
273  C  CA  . GLU A 33  ? 0.48828 0.60361 0.24840 -0.11939 -0.06054 0.04479  32  GLU A CA  
274  C  C   . GLU A 33  ? 0.42780 0.55750 0.21853 -0.12268 -0.04888 0.05057  32  GLU A C   
275  O  O   . GLU A 33  ? 0.44926 0.57680 0.23725 -0.13750 -0.04666 0.06487  32  GLU A O   
276  C  CB  . GLU A 33  ? 0.50019 0.64340 0.23846 -0.11411 -0.03910 0.03319  32  GLU A CB  
277  C  CG  . GLU A 33  ? 0.74427 0.86870 0.43820 -0.11012 -0.04992 0.02825  32  GLU A CG  
278  C  CD  . GLU A 33  ? 0.94244 1.09134 0.60980 -0.09907 -0.02761 0.01671  32  GLU A CD  
279  O  OE1 . GLU A 33  ? 1.01609 1.14709 0.64428 -0.08612 -0.03541 0.00352  32  GLU A OE1 
280  O  OE2 . GLU A 33  ? 0.93865 1.12151 0.62425 -0.10192 -0.00458 0.02139  32  GLU A OE2 
281  N  N   . LEU A 34  ? 0.35123 0.49469 0.17093 -0.10953 -0.04417 0.04002  33  LEU A N   
282  C  CA  . LEU A 34  ? 0.30338 0.45831 0.14962 -0.10920 -0.03156 0.04285  33  LEU A CA  
283  C  C   . LEU A 34  ? 0.32849 0.45558 0.21078 -0.09501 -0.04228 0.04594  33  LEU A C   
284  O  O   . LEU A 34  ? 0.31059 0.44319 0.21624 -0.08816 -0.03151 0.04393  33  LEU A O   
285  C  CB  . LEU A 34  ? 0.32304 0.51728 0.18981 -0.09895 -0.00820 0.02609  33  LEU A CB  
286  C  CG  . LEU A 34  ? 0.34881 0.56340 0.20374 -0.10042 0.00611  0.02030  33  LEU A CG  
287  C  CD1 . LEU A 34  ? 0.35797 0.60159 0.24321 -0.08572 0.02346  0.00412  33  LEU A CD1 
288  C  CD2 . LEU A 34  ? 0.36864 0.58340 0.21383 -0.11866 0.00715  0.03804  33  LEU A CD2 
289  N  N   . ALA A 35  ? 0.34987 0.44831 0.23699 -0.08907 -0.06292 0.05200  34  ALA A N   
290  C  CA  . ALA A 35  ? 0.32192 0.40373 0.24912 -0.06986 -0.06844 0.05575  34  ALA A CA  
291  C  C   . ALA A 35  ? 0.36263 0.42310 0.28316 -0.07148 -0.06815 0.06459  34  ALA A C   
292  O  O   . ALA A 35  ? 0.31484 0.37078 0.26309 -0.05206 -0.06198 0.06286  34  ALA A O   
293  C  CB  . ALA A 35  ? 0.33284 0.39128 0.27075 -0.06411 -0.09172 0.06500  34  ALA A CB  
294  N  N   . TRP A 36  ? 0.38790 0.43381 0.26959 -0.09400 -0.07617 0.07493  35  TRP A N   
295  C  CA  . TRP A 36  ? 0.40151 0.41989 0.27248 -0.09758 -0.08173 0.08298  35  TRP A CA  
296  C  C   . TRP A 36  ? 0.38920 0.42301 0.27427 -0.09005 -0.06359 0.07351  35  TRP A C   
297  O  O   . TRP A 36  ? 0.40610 0.40930 0.28691 -0.08268 -0.06962 0.07569  35  TRP A O   
298  C  CB  . TRP A 36  ? 0.41939 0.42621 0.24927 -0.12854 -0.09520 0.09924  35  TRP A CB  
299  C  CG  . TRP A 36  ? 0.37290 0.42053 0.19593 -0.14629 -0.07637 0.09718  35  TRP A CG  
300  C  CD1 . TRP A 36  ? 0.41887 0.49734 0.23577 -0.15219 -0.06529 0.09247  35  TRP A CD1 
301  C  CD2 . TRP A 36  ? 0.39754 0.45754 0.22612 -0.15598 -0.06729 0.09891  35  TRP A CD2 
302  N  NE1 . TRP A 36  ? 0.46941 0.58267 0.29217 -0.16165 -0.04828 0.09131  35  TRP A NE1 
303  C  CE2 . TRP A 36  ? 0.41458 0.51901 0.24789 -0.16590 -0.05049 0.09618  35  TRP A CE2 
304  C  CE3 . TRP A 36  ? 0.40428 0.43909 0.23346 -0.15520 -0.07448 0.10232  35  TRP A CE3 
305  C  CZ2 . TRP A 36  ? 0.47507 0.60469 0.32134 -0.17538 -0.04219 0.09870  35  TRP A CZ2 
306  C  CZ3 . TRP A 36  ? 0.44547 0.50120 0.28296 -0.16867 -0.06701 0.10479  35  TRP A CZ3 
307  C  CH2 . TRP A 36  ? 0.44767 0.55343 0.29726 -0.17893 -0.05179 0.10394  35  TRP A CH2 
308  N  N   . ILE A 37  ? 0.33146 0.40788 0.22980 -0.09108 -0.04377 0.06271  36  ILE A N   
309  C  CA  . ILE A 37  ? 0.36367 0.45606 0.27611 -0.08693 -0.02828 0.05548  36  ILE A CA  
310  C  C   . ILE A 37  ? 0.33435 0.41016 0.27174 -0.05915 -0.02582 0.04922  36  ILE A C   
311  O  O   . ILE A 37  ? 0.35314 0.41632 0.28725 -0.05462 -0.02276 0.04747  36  ILE A O   
312  C  CB  . ILE A 37  ? 0.32282 0.46479 0.25100 -0.08871 -0.00832 0.04410  36  ILE A CB  
313  C  CG1 . ILE A 37  ? 0.35738 0.52356 0.25807 -0.11276 -0.00459 0.05136  36  ILE A CG1 
314  C  CG2 . ILE A 37  ? 0.35781 0.51653 0.30896 -0.08150 0.00623  0.03649  36  ILE A CG2 
315  C  CD1 . ILE A 37  ? 0.41230 0.57840 0.31366 -0.12705 -0.00525 0.05904  36  ILE A CD1 
316  N  N   . ALA A 38  ? 0.28375 0.35943 0.24544 -0.03994 -0.02816 0.04802  37  ALA A N   
317  C  CA  . ALA A 38  ? 0.30599 0.37848 0.29711 -0.01128 -0.02130 0.04578  37  ALA A CA  
318  C  C   . ALA A 38  ? 0.31276 0.34152 0.28269 0.00084  -0.02935 0.05034  37  ALA A C   
319  O  O   . ALA A 38  ? 0.34048 0.36653 0.32234 0.02483  -0.01911 0.04668  37  ALA A O   
320  C  CB  . ALA A 38  ? 0.26923 0.35274 0.29512 0.00393  -0.02583 0.05047  37  ALA A CB  
321  N  N   . ASP A 39  ? 0.35358 0.34595 0.28928 -0.01412 -0.04864 0.05833  38  ASP A N   
322  C  CA  . ASP A 39  ? 0.40993 0.35091 0.31911 -0.00274 -0.06213 0.06107  38  ASP A CA  
323  C  C   . ASP A 39  ? 0.45405 0.36976 0.32414 -0.02917 -0.07500 0.06392  38  ASP A C   
324  O  O   . ASP A 39  ? 0.56924 0.43258 0.40918 -0.02683 -0.09525 0.06769  38  ASP A O   
325  C  CB  . ASP A 39  ? 0.45468 0.36740 0.36345 0.00572  -0.08008 0.07106  38  ASP A CB  
326  C  CG  . ASP A 39  ? 0.45502 0.39427 0.41032 0.03321  -0.06930 0.07313  38  ASP A CG  
327  O  OD1 . ASP A 39  ? 0.42206 0.37302 0.39811 0.06156  -0.05236 0.06850  38  ASP A OD1 
328  O  OD2 . ASP A 39  ? 0.42578 0.37461 0.39665 0.02547  -0.07911 0.08164  38  ASP A OD2 
329  N  N   . ALA A 40  ? 0.50641 0.45848 0.37913 -0.05297 -0.06496 0.06339  39  ALA A N   
330  C  CA  . ALA A 40  ? 0.59731 0.53649 0.44428 -0.07864 -0.07508 0.07015  39  ALA A CA  
331  C  C   . ALA A 40  ? 0.45876 0.37245 0.29758 -0.06252 -0.07402 0.06109  39  ALA A C   
332  O  O   . ALA A 40  ? 0.51664 0.43584 0.37200 -0.03235 -0.05865 0.04911  39  ALA A O   
333  C  CB  . ALA A 40  ? 0.56958 0.56458 0.42922 -0.10365 -0.06015 0.07350  39  ALA A CB  
334  N  N   . GLY A 41  ? 0.55431 0.44114 0.36711 -0.08406 -0.09169 0.06908  40  GLY A N   
335  C  CA  . GLY A 41  ? 0.49042 0.34373 0.28646 -0.07071 -0.09627 0.06054  40  GLY A CA  
336  C  C   . GLY A 41  ? 0.43974 0.34216 0.26571 -0.06458 -0.06954 0.05087  40  GLY A C   
337  O  O   . GLY A 41  ? 0.42822 0.38922 0.28664 -0.07548 -0.05060 0.05184  40  GLY A O   
338  N  N   . VAL A 42  ? 0.41179 0.28639 0.22357 -0.04383 -0.06908 0.04043  41  VAL A N   
339  C  CA  . VAL A 42  ? 0.37430 0.28530 0.20842 -0.04199 -0.05041 0.03375  41  VAL A CA  
340  C  C   . VAL A 42  ? 0.43471 0.29882 0.23380 -0.05143 -0.07177 0.03518  41  VAL A C   
341  O  O   . VAL A 42  ? 0.53090 0.32709 0.28503 -0.04692 -0.09859 0.03567  41  VAL A O   
342  C  CB  . VAL A 42  ? 0.38472 0.31728 0.24128 -0.00516 -0.02564 0.02106  41  VAL A CB  
343  C  CG1 . VAL A 42  ? 0.37625 0.34918 0.26886 0.00220  -0.01139 0.02244  41  VAL A CG1 
344  C  CG2 . VAL A 42  ? 0.46829 0.34386 0.28646 0.02791  -0.03273 0.01318  41  VAL A CG2 
345  N  N   . ALA A 43  ? 0.40393 0.30102 0.22332 -0.06522 -0.06330 0.03628  42  ALA A N   
346  C  CA  . ALA A 43  ? 0.52110 0.37432 0.31002 -0.07886 -0.08763 0.04055  42  ALA A CA  
347  C  C   . ALA A 43  ? 0.52220 0.31089 0.26427 -0.04422 -0.09606 0.02507  42  ALA A C   
348  O  O   . ALA A 43  ? 0.52005 0.32449 0.27031 -0.01023 -0.07167 0.01210  42  ALA A O   
349  C  CB  . ALA A 43  ? 0.46042 0.36497 0.28566 -0.09698 -0.07541 0.04491  42  ALA A CB  
350  N  N   . GLY A 44  ? 0.56509 0.28213 0.25764 -0.05240 -0.13127 0.02791  43  GLY A N   
351  C  CA  . GLY A 44  ? 0.66864 0.31658 0.30525 -0.01771 -0.14186 0.01138  43  GLY A CA  
352  C  C   . GLY A 44  ? 0.69117 0.34059 0.32095 -0.01475 -0.13777 0.00568  43  GLY A C   
353  O  O   . GLY A 44  ? 0.58972 0.29212 0.26182 -0.04161 -0.12944 0.01549  43  GLY A O   
354  N  N   . VAL A 45  ? 0.53503 0.27306 0.31478 0.06790  0.05801  0.06530  44  VAL A N   
355  C  CA  . VAL A 45  ? 0.50278 0.23063 0.26877 0.05648  0.03803  0.04570  44  VAL A CA  
356  C  C   . VAL A 45  ? 0.52510 0.25005 0.30226 0.03622  0.02743  0.02762  44  VAL A C   
357  O  O   . VAL A 45  ? 0.56454 0.30370 0.34087 0.02973  0.00356  0.01377  44  VAL A O   
358  C  CB  . VAL A 45  ? 0.62538 0.31023 0.35833 0.06034  0.04719  0.04366  44  VAL A CB  
359  C  CG1 . VAL A 45  ? 0.62729 0.34551 0.37630 0.07455  0.05386  0.05265  44  VAL A CG1 
360  C  CG2 . VAL A 45  ? 0.66581 0.30437 0.38631 0.05262  0.06988  0.04152  44  VAL A CG2 
361  N  N   A ASP A 46  ? 0.58069 0.28868 0.37124 0.02688  0.04608  0.02785  45  ASP A N   
362  N  N   B ASP A 46  ? 0.56917 0.27785 0.35995 0.02654  0.04522  0.02733  45  ASP A N   
363  C  CA  A ASP A 46  ? 0.54282 0.25198 0.35509 0.00457  0.03822  0.00864  45  ASP A CA  
364  C  CA  B ASP A 46  ? 0.56318 0.27353 0.37306 0.00416  0.03413  0.00658  45  ASP A CA  
365  C  C   A ASP A 46  ? 0.52298 0.28069 0.36736 0.00280  0.01903  0.00736  45  ASP A C   
366  C  C   B ASP A 46  ? 0.51570 0.27343 0.36171 0.00194  0.01945  0.00696  45  ASP A C   
367  O  O   A ASP A 46  ? 0.49327 0.26740 0.35124 -0.01042 -0.00351 -0.01017 45  ASP A O   
368  O  O   B ASP A 46  ? 0.50037 0.27393 0.36560 -0.01338 0.00030  -0.01059 45  ASP A O   
369  C  CB  A ASP A 46  ? 0.58741 0.26696 0.41395 -0.00414 0.07025  0.01155  45  ASP A CB  
370  C  CB  B ASP A 46  ? 0.58438 0.25804 0.40230 -0.00869 0.06221  0.00314  45  ASP A CB  
371  C  CG  A ASP A 46  ? 0.63742 0.33542 0.48598 0.01020  0.09200  0.03571  45  ASP A CG  
372  C  CG  B ASP A 46  ? 0.63114 0.25149 0.41094 -0.01010 0.07672  -0.00236 45  ASP A CG  
373  O  OD1 A ASP A 46  ? 0.59484 0.31989 0.43685 0.03070  0.08765  0.05351  45  ASP A OD1 
374  O  OD1 B ASP A 46  ? 0.59048 0.18335 0.36018 0.00288  0.10775  0.01622  45  ASP A OD1 
375  O  OD2 A ASP A 46  ? 0.62501 0.30891 0.49678 0.00068  0.11505  0.03587  45  ASP A OD2 
376  O  OD2 B ASP A 46  ? 0.62577 0.23144 0.38260 -0.02173 0.05743  -0.02410 45  ASP A OD2 
377  N  N   . PHE A 47  ? 0.46393 0.24590 0.31886 0.01758  0.02729  0.02595  46  PHE A N   
378  C  CA  . PHE A 47  ? 0.45222 0.27458 0.33415 0.01769  0.01491  0.02646  46  PHE A CA  
379  C  C   . PHE A 47  ? 0.42074 0.26305 0.29451 0.01992  -0.01260 0.01755  46  PHE A C   
380  O  O   . PHE A 47  ? 0.41263 0.27814 0.30875 0.01210  -0.02911 0.00787  46  PHE A O   
381  C  CB  . PHE A 47  ? 0.45678 0.29479 0.33827 0.03506  0.02975  0.04690  46  PHE A CB  
382  C  CG  . PHE A 47  ? 0.41860 0.29240 0.31767 0.03805  0.01993  0.04812  46  PHE A CG  
383  C  CD1 . PHE A 47  ? 0.46621 0.35092 0.39739 0.02967  0.02715  0.04700  46  PHE A CD1 
384  C  CD2 . PHE A 47  ? 0.46405 0.35767 0.34956 0.04883  0.00763  0.05016  46  PHE A CD2 
385  C  CE1 . PHE A 47  ? 0.51895 0.43289 0.46491 0.03383  0.02193  0.04930  46  PHE A CE1 
386  C  CE2 . PHE A 47  ? 0.50065 0.42210 0.39998 0.05110  0.00239  0.05024  46  PHE A CE2 
387  C  CZ  . PHE A 47  ? 0.44442 0.37454 0.37195 0.04447  0.00996  0.05069  46  PHE A CZ  
388  N  N   . HIS A 48  ? 0.43832 0.27132 0.28242 0.03205  -0.01520 0.02205  47  HIS A N   
389  C  CA  . HIS A 48  ? 0.41138 0.25539 0.24361 0.03724  -0.03455 0.01615  47  HIS A CA  
390  C  C   . HIS A 48  ? 0.41338 0.24628 0.23545 0.02770  -0.05307 -0.00037 47  HIS A C   
391  O  O   . HIS A 48  ? 0.41014 0.26526 0.24029 0.02874  -0.07146 -0.00577 47  HIS A O   
392  C  CB  . HIS A 48  ? 0.49949 0.33065 0.30574 0.05089  -0.02801 0.02377  47  HIS A CB  
393  C  CG  . HIS A 48  ? 0.41628 0.27023 0.23350 0.06085  -0.01797 0.03638  47  HIS A CG  
394  N  ND1 . HIS A 48  ? 0.40575 0.29067 0.23826 0.06332  -0.02399 0.03654  47  HIS A ND1 
395  C  CD2 . HIS A 48  ? 0.42885 0.28059 0.24233 0.06976  -0.00328 0.04845  47  HIS A CD2 
396  C  CE1 . HIS A 48  ? 0.40890 0.30972 0.24391 0.07135  -0.01546 0.04532  47  HIS A CE1 
397  N  NE2 . HIS A 48  ? 0.42830 0.31292 0.25338 0.07649  -0.00440 0.05358  47  HIS A NE2 
398  N  N   . ARG A 49  ? 0.44774 0.24600 0.25010 0.01956  -0.04775 -0.00836 48  ARG A N   
399  C  CA  . ARG A 49  ? 0.47673 0.26332 0.26297 0.00932  -0.06737 -0.02754 48  ARG A CA  
400  C  C   . ARG A 49  ? 0.46751 0.28805 0.29603 -0.00597 -0.08297 -0.03929 48  ARG A C   
401  O  O   . ARG A 49  ? 0.49555 0.33566 0.32393 -0.00712 -0.10908 -0.05044 48  ARG A O   
402  C  CB  . ARG A 49  ? 0.53034 0.26875 0.28737 0.00052  -0.05428 -0.03639 48  ARG A CB  
403  C  CG  . ARG A 49  ? 0.58111 0.28270 0.29248 0.01573  -0.04271 -0.02835 48  ARG A CG  
404  C  CD  . ARG A 49  ? 0.66948 0.31875 0.35037 0.00659  -0.02708 -0.03805 48  ARG A CD  
405  N  NE  . ARG A 49  ? 0.70444 0.31523 0.34066 0.02176  -0.01484 -0.03089 48  ARG A NE  
406  C  CZ  . ARG A 49  ? 0.80075 0.38477 0.39081 0.02490  -0.02701 -0.04276 48  ARG A CZ  
407  N  NH1 . ARG A 49  ? 0.75855 0.35536 0.34042 0.01446  -0.05602 -0.06291 48  ARG A NH1 
408  N  NH2 . ARG A 49  ? 0.90270 0.44859 0.45522 0.03991  -0.00976 -0.03375 48  ARG A NH2 
409  N  N   A ARG A 50  ? 0.45521 0.28741 0.32289 -0.01463 -0.06673 -0.03448 49  ARG A N   
410  N  N   B ARG A 50  ? 0.45468 0.28721 0.32257 -0.01448 -0.06666 -0.03428 49  ARG A N   
411  C  CA  A ARG A 50  ? 0.43143 0.29703 0.34769 -0.02976 -0.07801 -0.04528 49  ARG A CA  
412  C  CA  B ARG A 50  ? 0.45341 0.31921 0.36972 -0.02971 -0.07814 -0.04527 49  ARG A CA  
413  C  C   A ARG A 50  ? 0.40527 0.31489 0.34121 -0.01890 -0.09734 -0.03986 49  ARG A C   
414  C  C   B ARG A 50  ? 0.41209 0.32188 0.34825 -0.01893 -0.09735 -0.03985 49  ARG A C   
415  O  O   A ARG A 50  ? 0.41073 0.34830 0.36797 -0.02559 -0.12138 -0.05238 49  ARG A O   
416  O  O   B ARG A 50  ? 0.41740 0.35546 0.37559 -0.02577 -0.12129 -0.05239 49  ARG A O   
417  C  CB  A ARG A 50  ? 0.46395 0.32775 0.41756 -0.03839 -0.04963 -0.03798 49  ARG A CB  
418  C  CB  B ARG A 50  ? 0.48170 0.34611 0.43639 -0.03910 -0.05031 -0.03875 49  ARG A CB  
419  C  CG  A ARG A 50  ? 0.52615 0.42412 0.53897 -0.05459 -0.05535 -0.04794 49  ARG A CG  
420  C  CG  B ARG A 50  ? 0.54608 0.43870 0.55682 -0.05950 -0.05791 -0.05391 49  ARG A CG  
421  C  CD  A ARG A 50  ? 0.57902 0.46236 0.62415 -0.06403 -0.02057 -0.04187 49  ARG A CD  
422  C  CD  B ARG A 50  ? 0.58070 0.46507 0.62925 -0.06779 -0.02389 -0.04626 49  ARG A CD  
423  N  NE  A ARG A 50  ? 0.58779 0.47566 0.63127 -0.04495 0.00118  -0.01660 49  ARG A NE  
424  N  NE  B ARG A 50  ? 0.58143 0.49569 0.65756 -0.05570 -0.01529 -0.02860 49  ARG A NE  
425  C  CZ  A ARG A 50  ? 0.55113 0.47146 0.62837 -0.04045 0.00267  -0.00853 49  ARG A CZ  
426  C  CZ  B ARG A 50  ? 0.56963 0.47241 0.62806 -0.03829 0.00888  -0.00639 49  ARG A CZ  
427  N  NH1 A ARG A 50  ? 0.53070 0.45031 0.59644 -0.02302 0.02228  0.01218  49  ARG A NH1 
428  N  NH1 B ARG A 50  ? 0.52304 0.45052 0.60190 -0.02849 0.01596  0.00648  49  ARG A NH1 
429  N  NH2 A ARG A 50  ? 0.54080 0.49541 0.66273 -0.05254 -0.01575 -0.02145 49  ARG A NH2 
430  N  NH2 B ARG A 50  ? 0.59337 0.46061 0.61266 -0.02964 0.02602  0.00292  49  ARG A NH2 
431  N  N   . LEU A 51  ? 0.40155 0.31593 0.32576 -0.00092 -0.08810 -0.02232 50  LEU A N   
432  C  CA  . LEU A 51  ? 0.37600 0.32464 0.31661 0.01030  -0.09916 -0.01590 50  LEU A CA  
433  C  C   . LEU A 51  ? 0.40083 0.34670 0.30716 0.02300  -0.11937 -0.01886 50  LEU A C   
434  O  O   . LEU A 51  ? 0.37592 0.35094 0.29821 0.02965  -0.13569 -0.01880 50  LEU A O   
435  C  CB  . LEU A 51  ? 0.33124 0.28472 0.27419 0.02172  -0.07871 0.00068  50  LEU A CB  
436  C  CG  . LEU A 51  ? 0.33745 0.29230 0.30794 0.01421  -0.05685 0.00680  50  LEU A CG  
437  C  CD1 . LEU A 51  ? 0.37419 0.33473 0.33681 0.02744  -0.04065 0.02126  50  LEU A CD1 
438  C  CD2 . LEU A 51  ? 0.37489 0.35471 0.39640 0.00139  -0.05986 0.00057  50  LEU A CD2 
439  N  N   . ILE A 52  ? 0.42145 0.33116 0.28097 0.02844  -0.11625 -0.01990 51  ILE A N   
440  C  CA  . ILE A 52  ? 0.47711 0.37605 0.29779 0.04189  -0.13185 -0.02236 51  ILE A CA  
441  C  C   . ILE A 52  ? 0.50769 0.42243 0.33061 0.03501  -0.16084 -0.03814 51  ILE A C   
442  O  O   . ILE A 52  ? 0.52214 0.45284 0.33332 0.04947  -0.17942 -0.03674 51  ILE A O   
443  C  CB  . ILE A 52  ? 0.53177 0.38432 0.30406 0.04776  -0.11841 -0.02069 51  ILE A CB  
444  C  CG1 . ILE A 52  ? 0.45440 0.30342 0.22816 0.05823  -0.09612 -0.00575 51  ILE A CG1 
445  C  CG2 . ILE A 52  ? 0.55379 0.38658 0.28022 0.06018  -0.13223 -0.02549 51  ILE A CG2 
446  C  CD1 . ILE A 52  ? 0.48654 0.29792 0.23158 0.06102  -0.07768 -0.00195 51  ILE A CD1 
447  N  N   A GLU A 53  ? 0.49816 0.40970 0.33667 0.01342  -0.16476 -0.05386 52  GLU A N   
448  N  N   B GLU A 53  ? 0.49880 0.41044 0.33756 0.01338  -0.16466 -0.05382 52  GLU A N   
449  C  CA  A GLU A 53  ? 0.52222 0.45592 0.36967 0.00272  -0.19546 -0.07373 52  GLU A CA  
450  C  CA  B GLU A 53  ? 0.52544 0.45904 0.37335 0.00241  -0.19522 -0.07382 52  GLU A CA  
451  C  C   A GLU A 53  ? 0.51534 0.50734 0.41809 0.00526  -0.21174 -0.07026 52  GLU A C   
452  C  C   B GLU A 53  ? 0.51467 0.50656 0.41802 0.00467  -0.21164 -0.07061 52  GLU A C   
453  O  O   A GLU A 53  ? 0.58123 0.60252 0.48365 0.01110  -0.24236 -0.07810 52  GLU A O   
454  O  O   B GLU A 53  ? 0.57516 0.59636 0.47897 0.00941  -0.24257 -0.07937 52  GLU A O   
455  C  CB  A GLU A 53  ? 0.55727 0.47423 0.41850 -0.02514 -0.19091 -0.09395 52  GLU A CB  
456  C  CB  B GLU A 53  ? 0.55949 0.47617 0.42148 -0.02544 -0.19019 -0.09381 52  GLU A CB  
457  C  CG  A GLU A 53  ? 0.63585 0.58727 0.52548 -0.04334 -0.22313 -0.11941 52  GLU A CG  
458  C  CG  B GLU A 53  ? 0.66460 0.59154 0.51867 -0.03994 -0.22299 -0.12181 52  GLU A CG  
459  C  CD  A GLU A 53  ? 0.71669 0.65116 0.54767 -0.04038 -0.24870 -0.13676 52  GLU A CD  
460  C  CD  B GLU A 53  ? 0.67682 0.66659 0.59960 -0.05266 -0.24664 -0.13279 52  GLU A CD  
461  O  OE1 A GLU A 53  ? 0.73508 0.64213 0.51175 -0.01785 -0.23828 -0.12165 52  GLU A OE1 
462  O  OE1 B GLU A 53  ? 0.70084 0.72350 0.61857 -0.04869 -0.27619 -0.14207 52  GLU A OE1 
463  O  OE2 A GLU A 53  ? 0.75638 0.71140 0.60532 -0.06093 -0.26450 -0.15999 52  GLU A OE2 
464  O  OE2 B GLU A 53  ? 0.61264 0.62115 0.59641 -0.06520 -0.22791 -0.12807 52  GLU A OE2 
465  N  N   . ARG A 54  ? 0.44838 0.45807 0.39701 0.00339  -0.19101 -0.05724 53  ARG A N   
466  C  CA  . ARG A 54  ? 0.40427 0.46477 0.40584 0.00850  -0.19967 -0.05039 53  ARG A CA  
467  C  C   . ARG A 54  ? 0.45653 0.52549 0.43595 0.03655  -0.20345 -0.03354 53  ARG A C   
468  O  O   . ARG A 54  ? 0.41238 0.52322 0.42692 0.04570  -0.21609 -0.02803 53  ARG A O   
469  C  CB  . ARG A 54  ? 0.44731 0.51536 0.49636 -0.00041 -0.17138 -0.04102 53  ARG A CB  
470  C  CG  . ARG A 54  ? 0.53256 0.58822 0.60840 -0.02649 -0.15919 -0.05449 53  ARG A CG  
471  C  CD  . ARG A 54  ? 0.55895 0.63356 0.69253 -0.03272 -0.13514 -0.04501 53  ARG A CD  
472  N  NE  . ARG A 54  ? 0.64114 0.76761 0.83766 -0.03892 -0.15255 -0.05134 53  ARG A NE  
473  C  CZ  . ARG A 54  ? 0.56111 0.71242 0.81466 -0.04077 -0.13468 -0.04197 53  ARG A CZ  
474  N  NH1 . ARG A 54  ? 0.60699 0.80920 0.92288 -0.04580 -0.15159 -0.04769 53  ARG A NH1 
475  N  NH2 . ARG A 54  ? 0.48479 0.61104 0.73218 -0.03601 -0.09985 -0.02636 53  ARG A NH2 
476  N  N   . GLY A 55  ? 0.53231 0.38991 0.39057 -0.03453 -0.23790 0.00063  54  GLY A N   
477  C  CA  . GLY A 55  ? 0.50874 0.37578 0.36747 -0.02273 -0.23480 0.01639  54  GLY A CA  
478  C  C   . GLY A 55  ? 0.48445 0.36993 0.38526 -0.00955 -0.21818 0.02189  54  GLY A C   
479  O  O   . GLY A 55  ? 0.50914 0.39776 0.41695 0.00004  -0.21564 0.03358  54  GLY A O   
480  N  N   . SER A 56  ? 0.43789 0.33449 0.36519 -0.01164 -0.20858 0.01420  55  SER A N   
481  C  CA  . SER A 56  ? 0.37975 0.30093 0.34800 -0.00422 -0.18920 0.01555  55  SER A CA  
482  C  C   . SER A 56  ? 0.36455 0.27214 0.29189 -0.00063 -0.16004 0.01358  55  SER A C   
483  O  O   . SER A 56  ? 0.35484 0.27595 0.29494 -0.00675 -0.13984 0.01117  55  SER A O   
484  C  CB  . SER A 56  ? 0.37892 0.33341 0.40901 -0.01522 -0.18068 0.00951  55  SER A CB  
485  O  OG  . SER A 56  ? 0.39268 0.33267 0.40140 -0.02961 -0.17969 0.00621  55  SER A OG  
486  N  N   . HIS A 57  ? 0.37977 0.26373 0.25897 0.00674  -0.15935 0.01765  56  HIS A N   
487  C  CA  . HIS A 57  ? 0.38560 0.25989 0.23417 0.01037  -0.13542 0.01648  56  HIS A CA  
488  C  C   . HIS A 57  ? 0.36708 0.23244 0.19101 0.01631  -0.12736 0.02294  56  HIS A C   
489  O  O   . HIS A 57  ? 0.41854 0.27103 0.21758 0.01388  -0.13493 0.02545  56  HIS A O   
490  C  CB  . HIS A 57  ? 0.45297 0.30303 0.27208 0.00746  -0.13513 0.00800  56  HIS A CB  
491  C  CG  . HIS A 57  ? 0.41428 0.26249 0.23213 0.01296  -0.11297 0.00900  56  HIS A CG  
492  N  ND1 . HIS A 57  ? 0.42739 0.27912 0.23234 0.02066  -0.09643 0.01271  56  HIS A ND1 
493  C  CD2 . HIS A 57  ? 0.42302 0.26813 0.25985 0.01117  -0.10810 0.01113  56  HIS A CD2 
494  C  CE1 . HIS A 57  ? 0.39179 0.24779 0.21339 0.02491  -0.08408 0.01595  56  HIS A CE1 
495  N  NE2 . HIS A 57  ? 0.41359 0.26332 0.25359 0.02012  -0.09225 0.01715  56  HIS A NE2 
496  N  N   . TRP A 58  ? 0.42743 0.30192 0.25879 0.01945  -0.11116 0.02632  57  TRP A N   
497  C  CA  . TRP A 58  ? 0.38973 0.25420 0.20457 0.02186  -0.10530 0.03560  57  TRP A CA  
498  C  C   . TRP A 58  ? 0.38982 0.26204 0.19722 0.02122  -0.08182 0.03435  57  TRP A C   
499  O  O   . TRP A 58  ? 0.40572 0.29551 0.23115 0.01969  -0.07441 0.02968  57  TRP A O   
500  C  CB  . TRP A 58  ? 0.41668 0.28733 0.27391 0.02370  -0.10877 0.03937  57  TRP A CB  
501  C  CG  . TRP A 58  ? 0.37796 0.25015 0.26598 0.02726  -0.13321 0.04245  57  TRP A CG  
502  C  CD1 . TRP A 58  ? 0.40480 0.26321 0.28776 0.02866  -0.15583 0.05843  57  TRP A CD1 
503  C  CD2 . TRP A 58  ? 0.34200 0.23856 0.27649 0.02603  -0.13536 0.03044  57  TRP A CD2 
504  N  NE1 . TRP A 58  ? 0.43301 0.30631 0.36419 0.03124  -0.17748 0.05813  57  TRP A NE1 
505  C  CE2 . TRP A 58  ? 0.35217 0.24884 0.31642 0.03018  -0.16474 0.04002  57  TRP A CE2 
506  C  CE3 . TRP A 58  ? 0.33970 0.26022 0.29222 0.01863  -0.11602 0.01580  57  TRP A CE3 
507  C  CZ2 . TRP A 58  ? 0.37367 0.29806 0.39874 0.02922  -0.17161 0.03186  57  TRP A CZ2 
508  C  CZ3 . TRP A 58  ? 0.32435 0.26845 0.32461 0.01472  -0.11943 0.00829  57  TRP A CZ3 
509  C  CH2 . TRP A 58  ? 0.30688 0.25465 0.34805 0.02085  -0.14526 0.01450  57  TRP A CH2 
510  N  N   . LEU A 59  ? 0.40451 0.26602 0.18811 0.02018  -0.07207 0.04242  58  LEU A N   
511  C  CA  . LEU A 59  ? 0.41482 0.29173 0.20689 0.01845  -0.05040 0.04245  58  LEU A CA  
512  C  C   . LEU A 59  ? 0.41739 0.28945 0.21070 0.01121  -0.04268 0.05344  58  LEU A C   
513  O  O   . LEU A 59  ? 0.46635 0.31540 0.24248 0.00918  -0.05273 0.06530  58  LEU A O   
514  C  CB  . LEU A 59  ? 0.41527 0.28825 0.18598 0.02356  -0.03531 0.03634  58  LEU A CB  
515  C  CG  . LEU A 59  ? 0.42824 0.27591 0.14275 0.02057  -0.02797 0.03522  58  LEU A CG  
516  C  CD1 . LEU A 59  ? 0.54438 0.39385 0.24418 0.01206  -0.00820 0.04736  58  LEU A CD1 
517  C  CD2 . LEU A 59  ? 0.46416 0.30392 0.16669 0.02732  -0.01286 0.01543  58  LEU A CD2 
518  N  N   . ALA A 60  ? 0.40652 0.30042 0.22516 0.00530  -0.02837 0.05255  59  ALA A N   
519  C  CA  . ALA A 60  ? 0.43896 0.33059 0.26386 -0.00561 -0.01655 0.06207  59  ALA A CA  
520  C  C   . ALA A 60  ? 0.42138 0.32386 0.23449 -0.00722 0.00651  0.06688  59  ALA A C   
521  O  O   . ALA A 60  ? 0.40585 0.33295 0.23902 -0.00025 0.01467  0.05917  59  ALA A O   
522  C  CB  . ALA A 60  ? 0.41884 0.33225 0.28375 -0.01648 -0.01664 0.05380  59  ALA A CB  
523  N  N   . GLU A 61  ? 0.45247 0.33705 0.23780 -0.01689 0.01863  0.08105  60  GLU A N   
524  C  CA  . GLU A 61  ? 0.47048 0.36943 0.24587 -0.02224 0.04990  0.08303  60  GLU A CA  
525  C  C   . GLU A 61  ? 0.46730 0.37496 0.26792 -0.04123 0.06433  0.09765  60  GLU A C   
526  O  O   . GLU A 61  ? 0.51697 0.39967 0.31850 -0.05124 0.05008  0.11053  60  GLU A O   
527  C  CB  . GLU A 61  ? 0.56244 0.43389 0.26433 -0.02439 0.05923  0.08581  60  GLU A CB  
528  C  CG  . GLU A 61  ? 0.61544 0.44889 0.27127 -0.03586 0.03840  0.11027  60  GLU A CG  
529  C  CD  . GLU A 61  ? 0.76907 0.58841 0.35518 -0.04394 0.04183  0.11403  60  GLU A CD  
530  O  OE1 . GLU A 61  ? 0.83938 0.66136 0.39832 -0.03745 0.04801  0.09099  60  GLU A OE1 
531  O  OE2 . GLU A 61  ? 0.83433 0.64448 0.40354 -0.05671 0.03655  0.13785  60  GLU A OE2 
532  N  N   . ASP A 62  ? 0.46174 0.40514 0.29376 -0.04613 0.09327  0.09494  61  ASP A N   
533  C  CA  . ASP A 62  ? 0.47765 0.43413 0.33948 -0.06855 0.10969  0.10912  61  ASP A CA  
534  C  C   . ASP A 62  ? 0.57235 0.50121 0.37473 -0.08512 0.13291  0.12904  61  ASP A C   
535  O  O   . ASP A 62  ? 0.60650 0.50505 0.33810 -0.08078 0.13076  0.13191  61  ASP A O   
536  C  CB  . ASP A 62  ? 0.56996 0.58521 0.50587 -0.06928 0.12763  0.10093  61  ASP A CB  
537  C  CG  . ASP A 62  ? 0.60183 0.64142 0.53995 -0.06030 0.16758  0.09246  61  ASP A CG  
538  O  OD1 . ASP A 62  ? 0.55792 0.56788 0.42593 -0.06102 0.18709  0.09147  61  ASP A OD1 
539  O  OD2 . ASP A 62  ? 0.56066 0.65140 0.57544 -0.05324 0.17923  0.08533  61  ASP A OD2 
540  N  N   . ALA A 63  ? 0.58491 0.52522 0.41285 -0.10918 0.15405  0.14503  62  ALA A N   
541  C  CA  . ALA A 63  ? 0.67691 0.58616 0.44525 -0.13259 0.17286  0.17314  62  ALA A CA  
542  C  C   . ALA A 63  ? 0.75100 0.67460 0.46579 -0.13100 0.20763  0.16461  62  ALA A C   
543  O  O   . ALA A 63  ? 0.86256 0.76681 0.51896 -0.13790 0.20404  0.18083  62  ALA A O   
544  C  CB  . ALA A 63  ? 0.67018 0.59274 0.48871 -0.16182 0.19064  0.19127  62  ALA A CB  
545  N  N   . ASP A 64  ? 0.67317 0.63854 0.42531 -0.11641 0.23550  0.13573  63  ASP A N   
546  C  CA  . ASP A 64  ? 0.72028 0.70049 0.43602 -0.11007 0.26988  0.11428  63  ASP A CA  
547  C  C   . ASP A 64  ? 0.75960 0.70895 0.41936 -0.08919 0.24940  0.09326  63  ASP A C   
548  O  O   . ASP A 64  ? 0.81707 0.77559 0.45680 -0.08062 0.27500  0.06524  63  ASP A O   
549  C  CB  . ASP A 64  ? 0.74014 0.78077 0.54563 -0.10183 0.31353  0.09212  63  ASP A CB  
550  C  CG  . ASP A 64  ? 0.80006 0.88109 0.67418 -0.12468 0.33000  0.11100  63  ASP A CG  
551  O  OD1 . ASP A 64  ? 0.88473 0.95173 0.71567 -0.14858 0.33258  0.13453  63  ASP A OD1 
552  O  OD2 . ASP A 64  ? 0.81111 0.94064 0.78920 -0.11869 0.33617  0.10533  63  ASP A OD2 
553  N  N   . GLY A 65  ? 0.68649 0.60142 0.33005 -0.08098 0.20277  0.10305  64  GLY A N   
554  C  CA  . GLY A 65  ? 0.68468 0.57386 0.28561 -0.06359 0.17739  0.08530  64  GLY A CA  
555  C  C   . GLY A 65  ? 0.72488 0.63823 0.38890 -0.03614 0.17700  0.05495  64  GLY A C   
556  O  O   . GLY A 65  ? 0.72392 0.61531 0.35313 -0.02462 0.16490  0.03609  64  GLY A O   
557  N  N   . GLN A 66  ? 0.58871 0.54589 0.34756 -0.02749 0.18515  0.05293  65  GLN A N   
558  C  CA  . GLN A 66  ? 0.52428 0.50102 0.34446 -0.00191 0.17822  0.03302  65  GLN A CA  
559  C  C   . GLN A 66  ? 0.50360 0.47298 0.34273 0.00519  0.12934  0.04190  65  GLN A C   
560  O  O   . GLN A 66  ? 0.44410 0.42304 0.30532 -0.00628 0.11140  0.05805  65  GLN A O   
561  C  CB  . GLN A 66  ? 0.53902 0.57094 0.45721 0.00458  0.20433  0.03021  65  GLN A CB  
562  C  CG  . GLN A 66  ? 0.68150 0.73205 0.60115 -0.00103 0.26355  0.01582  65  GLN A CG  
563  C  CD  . GLN A 66  ? 0.78406 0.80579 0.65489 0.01150  0.29077  -0.01775 65  GLN A CD  
564  O  OE1 . GLN A 66  ? 0.80339 0.80595 0.68563 0.03257  0.26865  -0.03223 65  GLN A OE1 
565  N  NE2 . GLN A 66  ? 0.83592 0.85200 0.64705 -0.00560 0.34032  -0.03133 65  GLN A NE2 
566  N  N   . PRO A 67  ? 0.39273 0.55072 0.19925 -0.01837 0.07189  -0.00420 66  PRO A N   
567  C  CA  . PRO A 67  ? 0.35046 0.46437 0.17516 -0.01603 0.05257  -0.00076 66  PRO A CA  
568  C  C   . PRO A 67  ? 0.35150 0.44236 0.21703 -0.01535 0.05333  0.00342  66  PRO A C   
569  O  O   . PRO A 67  ? 0.35384 0.45463 0.24326 -0.01238 0.06447  -0.01120 66  PRO A O   
570  C  CB  . PRO A 67  ? 0.38787 0.49777 0.21260 -0.00845 0.04466  -0.03499 66  PRO A CB  
571  C  CG  . PRO A 67  ? 0.39645 0.54425 0.18967 -0.00813 0.05162  -0.05017 66  PRO A CG  
572  C  CD  . PRO A 67  ? 0.43028 0.60441 0.22613 -0.01134 0.07221  -0.04039 66  PRO A CD  
573  N  N   . VAL A 68  ? 0.30455 0.36889 0.18017 -0.01796 0.04068  0.02213  67  VAL A N   
574  C  CA  . VAL A 68  ? 0.32230 0.36944 0.23104 -0.01771 0.03719  0.02477  67  VAL A CA  
575  C  C   . VAL A 68  ? 0.31601 0.33883 0.23004 -0.01459 0.02154  0.02185  67  VAL A C   
576  O  O   . VAL A 68  ? 0.30091 0.31573 0.23596 -0.01424 0.01654  0.02260  67  VAL A O   
577  C  CB  . VAL A 68  ? 0.30951 0.35893 0.23487 -0.02516 0.04000  0.04737  67  VAL A CB  
578  C  CG1 . VAL A 68  ? 0.36592 0.44628 0.29225 -0.02965 0.05920  0.05526  67  VAL A CG1 
579  C  CG2 . VAL A 68  ? 0.32806 0.36452 0.24791 -0.02913 0.02838  0.06603  67  VAL A CG2 
580  N  N   . GLY A 69  ? 0.30220 0.31815 0.19802 -0.01265 0.01359  0.01862  68  GLY A N   
581  C  CA  . GLY A 69  ? 0.29701 0.29682 0.19928 -0.01008 0.00221  0.01664  68  GLY A CA  
582  C  C   . GLY A 69  ? 0.29038 0.28782 0.17741 -0.00820 -0.00424 0.01137  68  GLY A C   
583  O  O   . GLY A 69  ? 0.32369 0.33191 0.19075 -0.00949 -0.00311 0.01151  68  GLY A O   
584  N  N   . PHE A 70  ? 0.29804 0.28637 0.19549 -0.00562 -0.01124 0.00765  69  PHE A N   
585  C  CA  . PHE A 70  ? 0.31326 0.29954 0.20507 -0.00420 -0.01868 0.00190  69  PHE A CA  
586  C  C   . PHE A 70  ? 0.29121 0.27030 0.19665 -0.00328 -0.02462 0.00610  69  PHE A C   
587  O  O   . PHE A 70  ? 0.27668 0.25705 0.19307 -0.00316 -0.02224 0.01044  69  PHE A O   
588  C  CB  . PHE A 70  ? 0.32254 0.31426 0.22288 -0.00149 -0.01788 -0.01634 69  PHE A CB  
589  C  CG  . PHE A 70  ? 0.28367 0.26983 0.21774 0.00054  -0.01763 -0.01792 69  PHE A CG  
590  C  CD1 . PHE A 70  ? 0.30466 0.28470 0.25905 0.00059  -0.02464 -0.01285 69  PHE A CD1 
591  C  CD2 . PHE A 70  ? 0.26608 0.25620 0.21707 0.00190  -0.01086 -0.02067 69  PHE A CD2 
592  C  CE1 . PHE A 70  ? 0.27220 0.25143 0.26106 0.00099  -0.02513 -0.00495 69  PHE A CE1 
593  C  CE2 . PHE A 70  ? 0.30179 0.28848 0.28868 0.00327  -0.01364 -0.01488 69  PHE A CE2 
594  C  CZ  . PHE A 70  ? 0.26252 0.24441 0.26705 0.00238  -0.02099 -0.00479 69  PHE A CZ  
595  N  N   . LEU A 71  ? 0.28915 0.26623 0.19378 -0.00273 -0.03246 0.00431  70  LEU A N   
596  C  CA  . LEU A 71  ? 0.26610 0.24187 0.18810 -0.00184 -0.03592 0.00661  70  LEU A CA  
597  C  C   . LEU A 71  ? 0.27232 0.24774 0.20649 -0.00132 -0.04315 -0.00169 70  LEU A C   
598  O  O   . LEU A 71  ? 0.29369 0.27045 0.21575 -0.00126 -0.05134 -0.00761 70  LEU A O   
599  C  CB  . LEU A 71  ? 0.28431 0.25851 0.20717 -0.00138 -0.03974 0.01145  70  LEU A CB  
600  C  CG  . LEU A 71  ? 0.28719 0.26803 0.22982 0.00018  -0.03844 0.01057  70  LEU A CG  
601  C  CD1 . LEU A 71  ? 0.27178 0.25290 0.22379 0.00214  -0.03998 0.00814  70  LEU A CD1 
602  C  CD2 . LEU A 71  ? 0.32368 0.30513 0.28223 0.00047  -0.04508 0.00917  70  LEU A CD2 
603  N  N   . ALA A 72  ? 0.26965 0.24608 0.23112 -0.00155 -0.04166 -0.00076 71  ALA A N   
604  C  CA  . ALA A 72  ? 0.26664 0.24155 0.25602 -0.00177 -0.04972 -0.00953 71  ALA A CA  
605  C  C   . ALA A 72  ? 0.28793 0.26733 0.30061 -0.00325 -0.05084 0.00157  71  ALA A C   
606  O  O   . ALA A 72  ? 0.27861 0.26688 0.30108 -0.00466 -0.04220 0.01693  71  ALA A O   
607  C  CB  . ALA A 72  ? 0.28064 0.25361 0.30120 -0.00169 -0.04779 -0.01276 71  ALA A CB  
608  N  N   . ALA A 73  ? 0.28748 0.26622 0.30890 -0.00312 -0.06130 -0.00580 72  ALA A N   
609  C  CA  . ALA A 73  ? 0.26060 0.24666 0.30859 -0.00421 -0.06144 0.00296  72  ALA A CA  
610  C  C   . ALA A 73  ? 0.27123 0.25613 0.35937 -0.00608 -0.07360 -0.00513 72  ALA A C   
611  O  O   . ALA A 73  ? 0.28069 0.25982 0.36875 -0.00546 -0.08534 -0.02384 72  ALA A O   
612  C  CB  . ALA A 73  ? 0.25870 0.24638 0.29089 -0.00169 -0.06475 0.00283  72  ALA A CB  
613  N  N   . GLU A 74  ? 0.22602 0.22071 0.35111 -0.00843 -0.07086 0.00628  73  GLU A N   
614  C  CA  . GLU A 74  ? 0.26442 0.25856 0.44066 -0.01141 -0.08287 0.00046  73  GLU A CA  
615  C  C   . GLU A 74  ? 0.27310 0.28022 0.47608 -0.01227 -0.08227 0.00856  73  GLU A C   
616  O  O   . GLU A 74  ? 0.24697 0.27064 0.45416 -0.01320 -0.06516 0.02605  73  GLU A O   
617  C  CB  . GLU A 74  ? 0.27848 0.27270 0.50193 -0.01601 -0.07823 0.01267  73  GLU A CB  
618  C  CG  . GLU A 74  ? 0.25703 0.24812 0.54467 -0.01952 -0.09328 0.00330  73  GLU A CG  
619  C  CD  . GLU A 74  ? 0.33903 0.32586 0.68856 -0.02415 -0.09312 0.01472  73  GLU A CD  
620  O  OE1 . GLU A 74  ? 0.37183 0.36113 0.71225 -0.02483 -0.08076 0.03549  73  GLU A OE1 
621  O  OE2 . GLU A 74  ? 0.39927 0.38052 0.81164 -0.02705 -0.10790 0.00237  73  GLU A OE2 
622  N  N   . ARG A 75  ? 0.24784 0.25234 0.46896 -0.01165 -0.10104 -0.00605 74  ARG A N   
623  C  CA  . ARG A 75  ? 0.25456 0.27203 0.51538 -0.01242 -0.10280 -0.00008 74  ARG A CA  
624  C  C   . ARG A 75  ? 0.25603 0.28410 0.58199 -0.01919 -0.09590 0.01424  74  ARG A C   
625  O  O   . ARG A 75  ? 0.26305 0.28177 0.62637 -0.02287 -0.10862 0.00604  74  ARG A O   
626  C  CB  . ARG A 75  ? 0.29399 0.30744 0.55842 -0.01025 -0.12917 -0.01811 74  ARG A CB  
627  C  CG  . ARG A 75  ? 0.30403 0.33076 0.61886 -0.01028 -0.13595 -0.01430 74  ARG A CG  
628  C  CD  . ARG A 75  ? 0.34068 0.37791 0.64727 -0.00573 -0.12008 -0.00325 74  ARG A CD  
629  N  NE  . ARG A 75  ? 0.30242 0.35274 0.65748 -0.00365 -0.12781 -0.00338 74  ARG A NE  
630  C  CZ  . ARG A 75  ? 0.35284 0.39869 0.70582 0.00091  -0.15002 -0.00902 74  ARG A CZ  
631  N  NH1 . ARG A 75  ? 0.38678 0.41913 0.68839 0.00273  -0.16685 -0.01278 74  ARG A NH1 
632  N  NH2 . ARG A 75  ? 0.29485 0.34683 0.68724 0.00320  -0.15035 -0.00797 74  ARG A NH2 
633  N  N   . CYS A 76  ? 0.26082 0.31198 0.60594 -0.02098 -0.07601 0.03467  75  CYS A N   
634  C  CA  . CYS A 76  ? 0.23127 0.30253 0.63835 -0.02887 -0.06432 0.05871  75  CYS A CA  
635  C  C   . CYS A 76  ? 0.23693 0.33359 0.67930 -0.02876 -0.05684 0.06279  75  CYS A C   
636  O  O   . CYS A 76  ? 0.22691 0.34645 0.64513 -0.02514 -0.03724 0.06696  75  CYS A O   
637  C  CB  . CYS A 76  ? 0.26675 0.35512 0.65459 -0.03209 -0.04129 0.08567  75  CYS A CB  
638  S  SG  . CYS A 76  ? 0.29573 0.35816 0.65070 -0.03152 -0.04755 0.08408  75  CYS A SG  
639  N  N   . ALA A 77  ? 0.19677 0.28528 0.68718 -0.03042 -0.07095 0.05687  76  ALA A N   
640  C  CA  . ALA A 77  ? 0.21187 0.31551 0.72903 -0.02799 -0.06686 0.05507  76  ALA A CA  
641  C  C   . ALA A 77  ? 0.23655 0.34165 0.72213 -0.01971 -0.07471 0.03632  76  ALA A C   
642  O  O   . ALA A 77  ? 0.24749 0.32817 0.70301 -0.01613 -0.09893 0.01906  76  ALA A O   
643  C  CB  . ALA A 77  ? 0.25343 0.39327 0.79520 -0.03271 -0.03608 0.08276  76  ALA A CB  
644  N  N   . ASP A 78  ? 0.22606 0.35963 0.71618 -0.01551 -0.05535 0.03819  77  ASP A N   
645  C  CA  . ASP A 78  ? 0.21440 0.34128 0.67927 -0.00567 -0.06329 0.02059  77  ASP A CA  
646  C  C   . ASP A 78  ? 0.18831 0.31222 0.58876 -0.00139 -0.04799 0.01766  77  ASP A C   
647  O  O   . ASP A 78  ? 0.24596 0.37160 0.63666 0.00653  -0.04610 0.00483  77  ASP A O   
648  C  CB  . ASP A 78  ? 0.21005 0.35980 0.71878 -0.00123 -0.05317 0.01535  77  ASP A CB  
649  C  CG  . ASP A 78  ? 0.25122 0.37735 0.76110 0.00640  -0.07838 0.00066  77  ASP A CG  
650  O  OD1 . ASP A 78  ? 0.27117 0.36835 0.75070 0.00681  -0.10517 -0.00228 77  ASP A OD1 
651  O  OD2 . ASP A 78  ? 0.22998 0.36941 0.77169 0.01133  -0.07047 -0.00625 77  ASP A OD2 
652  N  N   . GLU A 79  ? 0.19445 0.31306 0.55867 -0.00629 -0.03955 0.02840  78  GLU A N   
653  C  CA  . GLU A 79  ? 0.20002 0.31673 0.50639 -0.00292 -0.02768 0.02523  78  GLU A CA  
654  C  C   . GLU A 79  ? 0.24643 0.32899 0.50910 -0.00376 -0.04374 0.02324  78  GLU A C   
655  O  O   . GLU A 79  ? 0.23149 0.29993 0.50698 -0.00852 -0.05637 0.02675  78  GLU A O   
656  C  CB  . GLU A 79  ? 0.17242 0.32430 0.47220 -0.00749 -0.00008 0.04176  78  GLU A CB  
657  C  CG  . GLU A 79  ? 0.19517 0.39248 0.52720 -0.00591 0.02199  0.04014  78  GLU A CG  
658  C  CD  . GLU A 79  ? 0.27146 0.51485 0.58900 -0.01133 0.04959  0.05966  78  GLU A CD  
659  O  OE1 . GLU A 79  ? 0.23226 0.47521 0.55204 -0.02016 0.04982  0.08848  78  GLU A OE1 
660  O  OE2 . GLU A 79  ? 0.22529 0.50972 0.53415 -0.00682 0.07048  0.04639  78  GLU A OE2 
661  N  N   . LEU A 80  ? 0.20740 0.27924 0.42390 0.00091  -0.04257 0.01514  79  LEU A N   
662  C  CA  . LEU A 80  ? 0.22177 0.26939 0.39539 -0.00016 -0.05113 0.01470  79  LEU A CA  
663  C  C   . LEU A 80  ? 0.21928 0.27982 0.36890 -0.00236 -0.03236 0.02394  79  LEU A C   
664  O  O   . LEU A 80  ? 0.21246 0.28735 0.34412 0.00094  -0.02023 0.01880  79  LEU A O   
665  C  CB  . LEU A 80  ? 0.22896 0.25810 0.37364 0.00489  -0.06377 0.00528  79  LEU A CB  
666  C  CG  . LEU A 80  ? 0.23078 0.24081 0.33415 0.00301  -0.07130 0.00514  79  LEU A CG  
667  C  CD1 . LEU A 80  ? 0.27644 0.27890 0.38955 0.00025  -0.08864 0.00017  79  LEU A CD1 
668  C  CD2 . LEU A 80  ? 0.29356 0.29198 0.36885 0.00632  -0.07839 0.00395  79  LEU A CD2 
669  N  N   . HIS A 81  ? 0.23201 0.29023 0.38817 -0.00782 -0.03169 0.03672  80  HIS A N   
670  C  CA  . HIS A 81  ? 0.18825 0.26066 0.32589 -0.01053 -0.01775 0.05143  80  HIS A CA  
671  C  C   . HIS A 81  ? 0.22340 0.27376 0.32047 -0.00827 -0.02371 0.04356  80  HIS A C   
672  O  O   . HIS A 81  ? 0.25094 0.27753 0.34671 -0.00805 -0.03692 0.03513  80  HIS A O   
673  C  CB  . HIS A 81  ? 0.21057 0.29152 0.38889 -0.01785 -0.01574 0.07498  80  HIS A CB  
674  C  CG  . HIS A 81  ? 0.23803 0.33808 0.40315 -0.02142 -0.00430 0.09822  80  HIS A CG  
675  N  ND1 . HIS A 81  ? 0.21502 0.35657 0.36449 -0.02276 0.01368  0.11190  80  HIS A ND1 
676  C  CD2 . HIS A 81  ? 0.22146 0.30930 0.39001 -0.02380 -0.00960 0.11038  80  HIS A CD2 
677  C  CE1 . HIS A 81  ? 0.21887 0.37377 0.35719 -0.02643 0.01710  0.13481  80  HIS A CE1 
678  N  NE2 . HIS A 81  ? 0.25896 0.37919 0.41267 -0.02692 0.00280  0.13548  80  HIS A NE2 
679  N  N   . ILE A 82  ? 0.22032 0.28242 0.28566 -0.00642 -0.01407 0.04293  81  ILE A N   
680  C  CA  . ILE A 82  ? 0.23870 0.28357 0.27218 -0.00507 -0.01818 0.03773  81  ILE A CA  
681  C  C   . ILE A 82  ? 0.23646 0.28802 0.27569 -0.00910 -0.01498 0.05632  81  ILE A C   
682  O  O   . ILE A 82  ? 0.27059 0.34924 0.30269 -0.01103 -0.00551 0.07026  81  ILE A O   
683  C  CB  . ILE A 82  ? 0.24414 0.29662 0.25155 -0.00138 -0.01319 0.02569  81  ILE A CB  
684  C  CG1 . ILE A 82  ? 0.26967 0.31343 0.28735 0.00279  -0.01897 0.01101  81  ILE A CG1 
685  C  CG2 . ILE A 82  ? 0.30452 0.34119 0.28643 -0.00122 -0.01698 0.02329  81  ILE A CG2 
686  C  CD1 . ILE A 82  ? 0.33000 0.38255 0.34126 0.00687  -0.01481 -0.00440 81  ILE A CD1 
687  N  N   . ALA A 83  ? 0.24681 0.27708 0.30252 -0.01011 -0.02417 0.05560  82  ALA A N   
688  C  CA  . ALA A 83  ? 0.22536 0.25886 0.30524 -0.01345 -0.02405 0.07438  82  ALA A CA  
689  C  C   . ALA A 83  ? 0.25542 0.28811 0.30885 -0.01180 -0.02258 0.07526  82  ALA A C   
690  O  O   . ALA A 83  ? 0.26693 0.31601 0.33074 -0.01454 -0.02026 0.09812  82  ALA A O   
691  C  CB  . ALA A 83  ? 0.29519 0.30748 0.41589 -0.01399 -0.03536 0.06562  82  ALA A CB  
692  N  N   . GLU A 84  ? 0.27527 0.29202 0.29904 -0.00808 -0.02487 0.05439  83  GLU A N   
693  C  CA  . GLU A 84  ? 0.27292 0.28904 0.27852 -0.00691 -0.02356 0.05395  83  GLU A CA  
694  C  C   . GLU A 84  ? 0.29701 0.30388 0.26974 -0.00441 -0.02312 0.03622  83  GLU A C   
695  O  O   . GLU A 84  ? 0.31993 0.31375 0.28723 -0.00320 -0.02696 0.02409  83  GLU A O   
696  C  CB  . GLU A 84  ? 0.29083 0.29390 0.32405 -0.00619 -0.02810 0.05236  83  GLU A CB  
697  C  CG  . GLU A 84  ? 0.28200 0.28645 0.30591 -0.00482 -0.02669 0.05300  83  GLU A CG  
698  C  CD  . GLU A 84  ? 0.31041 0.33765 0.32932 -0.00717 -0.02587 0.07552  83  GLU A CD  
699  O  OE1 . GLU A 84  ? 0.34842 0.38988 0.39336 -0.01018 -0.02774 0.09995  83  GLU A OE1 
700  O  OE2 . GLU A 84  ? 0.37666 0.41156 0.36707 -0.00662 -0.02430 0.06998  83  GLU A OE2 
701  N  N   . LEU A 85  ? 0.24321 0.25957 0.19817 -0.00427 -0.02023 0.03678  84  LEU A N   
702  C  CA  . LEU A 85  ? 0.25452 0.26220 0.19107 -0.00313 -0.02056 0.02443  84  LEU A CA  
703  C  C   . LEU A 85  ? 0.25449 0.26628 0.18879 -0.00382 -0.01994 0.02675  84  LEU A C   
704  O  O   . LEU A 85  ? 0.27666 0.30733 0.20985 -0.00455 -0.02034 0.03270  84  LEU A O   
705  C  CB  . LEU A 85  ? 0.26970 0.28704 0.20129 -0.00201 -0.01972 0.01689  84  LEU A CB  
706  C  CG  . LEU A 85  ? 0.27111 0.28125 0.19873 -0.00156 -0.02192 0.00670  84  LEU A CG  
707  C  CD1 . LEU A 85  ? 0.27790 0.26746 0.20440 -0.00223 -0.02544 0.00880  84  LEU A CD1 
708  C  CD2 . LEU A 85  ? 0.30772 0.33157 0.24305 0.00084  -0.02163 -0.00726 84  LEU A CD2 
709  N  N   . SER A 86  ? 0.25951 0.25928 0.19402 -0.00375 -0.01895 0.02256  85  SER A N   
710  C  CA  . SER A 86  ? 0.25273 0.25702 0.19467 -0.00418 -0.01799 0.02486  85  SER A CA  
711  C  C   . SER A 86  ? 0.25907 0.25665 0.19484 -0.00543 -0.01429 0.01868  85  SER A C   
712  O  O   . SER A 86  ? 0.29747 0.28866 0.22558 -0.00548 -0.01090 0.01504  85  SER A O   
713  C  CB  . SER A 86  ? 0.28602 0.28948 0.25226 -0.00267 -0.01799 0.02910  85  SER A CB  
714  O  OG  . SER A 86  ? 0.30423 0.32007 0.28546 -0.00335 -0.02281 0.04558  85  SER A OG  
715  N  N   . ILE A 87  ? 0.26526 0.26857 0.20593 -0.00717 -0.01556 0.01870  86  ILE A N   
716  C  CA  . ILE A 87  ? 0.26316 0.26336 0.20890 -0.00993 -0.01117 0.01842  86  ILE A CA  
717  C  C   . ILE A 87  ? 0.24999 0.25893 0.21449 -0.01005 -0.00927 0.01954  86  ILE A C   
718  O  O   . ILE A 87  ? 0.27049 0.28893 0.24380 -0.00964 -0.01690 0.02065  86  ILE A O   
719  C  CB  . ILE A 87  ? 0.28410 0.28181 0.23618 -0.01252 -0.01630 0.01599  86  ILE A CB  
720  C  CG1 . ILE A 87  ? 0.33803 0.32777 0.28145 -0.01121 -0.01946 0.01445  86  ILE A CG1 
721  C  CG2 . ILE A 87  ? 0.28148 0.27749 0.24899 -0.01718 -0.01154 0.02293  86  ILE A CG2 
722  C  CD1 . ILE A 87  ? 0.33749 0.31980 0.26988 -0.01232 -0.01601 0.02357  86  ILE A CD1 
723  N  N   . ALA A 88  ? 0.25335 0.26427 0.22456 -0.01054 0.00067  0.01903  87  ALA A N   
724  C  CA  . ALA A 88  ? 0.29429 0.31504 0.29230 -0.00990 0.00356  0.01850  87  ALA A CA  
725  C  C   . ALA A 88  ? 0.27711 0.30314 0.29153 -0.01362 -0.00359 0.02155  87  ALA A C   
726  O  O   . ALA A 88  ? 0.28802 0.30987 0.30056 -0.01769 -0.00527 0.02243  87  ALA A O   
727  C  CB  . ALA A 88  ? 0.32808 0.35733 0.33071 -0.01006 0.01921  0.01378  87  ALA A CB  
728  N  N   . GLN A 89  ? 0.27032 0.30648 0.30817 -0.01205 -0.01021 0.02278  88  GLN A N   
729  C  CA  . GLN A 89  ? 0.25225 0.29828 0.30676 -0.01496 -0.02217 0.02201  88  GLN A CA  
730  C  C   . GLN A 89  ? 0.28146 0.32517 0.35303 -0.02077 -0.01728 0.02014  88  GLN A C   
731  O  O   . GLN A 89  ? 0.27381 0.31747 0.35222 -0.02393 -0.02784 0.01355  88  GLN A O   
732  C  CB  . GLN A 89  ? 0.26303 0.32246 0.34831 -0.01247 -0.02828 0.02719  88  GLN A CB  
733  C  CG  . GLN A 89  ? 0.27976 0.35494 0.38552 -0.01530 -0.04412 0.02560  88  GLN A CG  
734  C  CD  . GLN A 89  ? 0.28016 0.36998 0.42022 -0.01236 -0.05303 0.03515  88  GLN A CD  
735  O  OE1 . GLN A 89  ? 0.41422 0.50168 0.58516 -0.00987 -0.04161 0.03626  88  GLN A OE1 
736  N  NE2 . GLN A 89  ? 0.26522 0.37458 0.40257 -0.01241 -0.07378 0.04152  88  GLN A NE2 
737  N  N   . ALA A 90  ? 0.28871 0.33453 0.37344 -0.02246 -0.00120 0.02531  89  ALA A N   
738  C  CA  . ALA A 90  ? 0.30301 0.35218 0.41308 -0.02958 0.00548  0.03180  89  ALA A CA  
739  C  C   . ALA A 90  ? 0.25644 0.29333 0.35375 -0.03393 0.00541  0.03840  89  ALA A C   
740  O  O   . ALA A 90  ? 0.31919 0.35645 0.44761 -0.04098 0.00603  0.04748  89  ALA A O   
741  C  CB  . ALA A 90  ? 0.34916 0.41345 0.47257 -0.03035 0.02655  0.03739  89  ALA A CB  
742  N  N   . HIS A 91  ? 0.28489 0.31105 0.34626 -0.03013 0.00291  0.03575  90  HIS A N   
743  C  CA  . HIS A 91  ? 0.28923 0.30413 0.34350 -0.03325 0.00157  0.04405  90  HIS A CA  
744  C  C   . HIS A 91  ? 0.32182 0.32603 0.37047 -0.02987 -0.01361 0.03006  90  HIS A C   
745  O  O   . HIS A 91  ? 0.30132 0.29483 0.34960 -0.03064 -0.01688 0.03405  90  HIS A O   
746  C  CB  . HIS A 91  ? 0.31054 0.32848 0.33079 -0.03222 0.01380  0.05369  90  HIS A CB  
747  C  CG  . HIS A 91  ? 0.34867 0.38671 0.37269 -0.03558 0.03162  0.06358  90  HIS A CG  
748  N  ND1 . HIS A 91  ? 0.38263 0.43126 0.42431 -0.04408 0.03983  0.08633  90  HIS A ND1 
749  C  CD2 . HIS A 91  ? 0.35324 0.40686 0.37216 -0.03165 0.04380  0.05341  90  HIS A CD2 
750  C  CE1 . HIS A 91  ? 0.38514 0.45958 0.42522 -0.04550 0.05871  0.08963  90  HIS A CE1 
751  N  NE2 . HIS A 91  ? 0.40713 0.48421 0.43515 -0.03726 0.06130  0.06625  90  HIS A NE2 
752  N  N   . GLN A 92  ? 0.28921 0.30084 0.33626 -0.02620 -0.02309 0.01454  91  GLN A N   
753  C  CA  . GLN A 92  ? 0.29824 0.31076 0.33932 -0.02313 -0.03500 -0.00246 91  GLN A CA  
754  C  C   . GLN A 92  ? 0.28551 0.29433 0.36644 -0.02642 -0.04520 -0.01526 91  GLN A C   
755  O  O   . GLN A 92  ? 0.26919 0.27622 0.38810 -0.03206 -0.04616 -0.00985 91  GLN A O   
756  C  CB  . GLN A 92  ? 0.26285 0.29480 0.28884 -0.01955 -0.04236 -0.01134 91  GLN A CB  
757  C  CG  . GLN A 92  ? 0.26744 0.30007 0.26557 -0.01588 -0.03530 0.00083  91  GLN A CG  
758  C  CD  . GLN A 92  ? 0.27559 0.32993 0.26560 -0.01362 -0.04362 0.00301  91  GLN A CD  
759  O  OE1 . GLN A 92  ? 0.32199 0.39504 0.32085 -0.01473 -0.05514 -0.00510 91  GLN A OE1 
760  N  NE2 . GLN A 92  ? 0.28454 0.33868 0.26262 -0.01103 -0.03954 0.01594  91  GLN A NE2 
761  N  N   . GLN A 93  ? 0.29414 0.30318 0.37400 -0.02279 -0.05262 -0.03401 92  GLN A N   
762  C  CA  . GLN A 93  ? 0.27604 0.28352 0.40189 -0.02377 -0.06487 -0.05694 92  GLN A CA  
763  C  C   . GLN A 93  ? 0.23981 0.22502 0.41354 -0.02980 -0.06422 -0.03795 92  GLN A C   
764  O  O   . GLN A 93  ? 0.30427 0.28590 0.53499 -0.03378 -0.07431 -0.04825 92  GLN A O   
765  C  CB  . GLN A 93  ? 0.28701 0.31547 0.43074 -0.02479 -0.07720 -0.08023 92  GLN A CB  
766  C  CG  . GLN A 93  ? 0.32619 0.38318 0.41991 -0.02011 -0.07874 -0.08810 92  GLN A CG  
767  C  CD  . GLN A 93  ? 0.36559 0.45395 0.46799 -0.01945 -0.09535 -0.11920 92  GLN A CD  
768  O  OE1 . GLN A 93  ? 0.44479 0.53839 0.58041 -0.01872 -0.10581 -0.15216 92  GLN A OE1 
769  N  NE2 . GLN A 93  ? 0.38159 0.49362 0.45766 -0.01939 -0.09963 -0.11019 92  GLN A NE2 
770  N  N   . GLN A 94  ? 0.28599 0.25946 0.43907 -0.03099 -0.05369 -0.00871 93  GLN A N   
771  C  CA  . GLN A 94  ? 0.28311 0.24175 0.47295 -0.03714 -0.05308 0.01903  93  GLN A CA  
772  C  C   . GLN A 94  ? 0.31853 0.26564 0.50467 -0.03336 -0.05657 0.02439  93  GLN A C   
773  O  O   . GLN A 94  ? 0.36255 0.30069 0.57070 -0.03833 -0.05713 0.05541  93  GLN A O   
774  C  CB  . GLN A 94  ? 0.34494 0.30993 0.51243 -0.04312 -0.03789 0.05382  93  GLN A CB  
775  C  CG  . GLN A 94  ? 0.33547 0.31415 0.50849 -0.04666 -0.03097 0.05347  93  GLN A CG  
776  C  CD  . GLN A 94  ? 0.49028 0.46660 0.73233 -0.05406 -0.03871 0.05549  93  GLN A CD  
777  O  OE1 . GLN A 94  ? 0.52057 0.48667 0.80699 -0.05990 -0.04256 0.07558  93  GLN A OE1 
778  N  NE2 . GLN A 94  ? 0.51829 0.50473 0.77706 -0.05426 -0.04341 0.03626  93  GLN A NE2 
779  N  N   . GLY A 95  ? 0.31039 0.26164 0.46896 -0.02521 -0.05853 -0.00063 94  GLY A N   
780  C  CA  . GLY A 95  ? 0.29956 0.24165 0.46369 -0.02089 -0.06282 0.00069  94  GLY A CA  
781  C  C   . GLY A 95  ? 0.28967 0.23382 0.39874 -0.01905 -0.05478 0.01857  94  GLY A C   
782  O  O   . GLY A 95  ? 0.33933 0.27775 0.45221 -0.01539 -0.05942 0.02049  94  GLY A O   
783  N  N   . LEU A 96  ? 0.30827 0.26108 0.37435 -0.02111 -0.04434 0.02896  95  LEU A N   
784  C  CA  . LEU A 96  ? 0.25986 0.21509 0.28287 -0.01992 -0.03866 0.04283  95  LEU A CA  
785  C  C   . LEU A 96  ? 0.32185 0.28054 0.32282 -0.01320 -0.03911 0.02453  95  LEU A C   
786  O  O   . LEU A 96  ? 0.32265 0.27890 0.30961 -0.01143 -0.04106 0.03165  95  LEU A O   
787  C  CB  . LEU A 96  ? 0.30645 0.27222 0.30064 -0.02306 -0.02702 0.05264  95  LEU A CB  
788  C  CG  . LEU A 96  ? 0.30032 0.27020 0.31558 -0.03081 -0.02247 0.07488  95  LEU A CG  
789  C  CD1 . LEU A 96  ? 0.33936 0.32540 0.33000 -0.03238 -0.00812 0.07736  95  LEU A CD1 
790  C  CD2 . LEU A 96  ? 0.34384 0.31219 0.36839 -0.03535 -0.02715 0.10463  95  LEU A CD2 
791  N  N   . GLY A 97  ? 0.29639 0.26539 0.29343 -0.01021 -0.03749 0.00384  96  GLY A N   
792  C  CA  . GLY A 97  ? 0.26862 0.24697 0.24988 -0.00529 -0.03612 -0.00793 96  GLY A CA  
793  C  C   . GLY A 97  ? 0.28157 0.25534 0.28595 -0.00174 -0.04167 -0.01522 96  GLY A C   
794  O  O   . GLY A 97  ? 0.28326 0.25719 0.27746 0.00051  -0.04110 -0.01113 96  GLY A O   
795  N  N   A ARG A 98  ? 0.27370 0.24321 0.31859 -0.00104 -0.04841 -0.02742 97  ARG A N   
796  N  N   B ARG A 98  ? 0.26875 0.23802 0.31364 -0.00106 -0.04845 -0.02707 97  ARG A N   
797  C  CA  A ARG A 98  ? 0.25308 0.21719 0.33567 0.00335  -0.05520 -0.03648 97  ARG A CA  
798  C  CA  B ARG A 98  ? 0.27693 0.24138 0.35781 0.00346  -0.05492 -0.03619 97  ARG A CA  
799  C  C   A ARG A 98  ? 0.31282 0.26106 0.39680 0.00144  -0.06116 -0.00702 97  ARG A C   
800  C  C   B ARG A 98  ? 0.29865 0.24681 0.38254 0.00146  -0.06122 -0.00680 97  ARG A C   
801  O  O   A ARG A 98  ? 0.28729 0.23609 0.37830 0.00548  -0.06430 -0.00832 97  ARG A O   
802  O  O   B ARG A 98  ? 0.29582 0.24407 0.38846 0.00549  -0.06477 -0.00784 97  ARG A O   
803  C  CB  A ARG A 98  ? 0.29164 0.25117 0.43144 0.00411  -0.06369 -0.05567 97  ARG A CB  
804  C  CB  B ARG A 98  ? 0.29888 0.26003 0.43685 0.00486  -0.06314 -0.05754 97  ARG A CB  
805  C  CG  A ARG A 98  ? 0.32899 0.27620 0.52806 0.00825  -0.07408 -0.05936 97  ARG A CG  
806  C  CG  B ARG A 98  ? 0.33106 0.28814 0.51937 0.01113  -0.07026 -0.07164 97  ARG A CG  
807  C  CD  A ARG A 98  ? 0.30776 0.27360 0.51147 0.01684  -0.06944 -0.08975 97  ARG A CD  
808  C  CD  B ARG A 98  ? 0.26260 0.21134 0.52488 0.01253  -0.08139 -0.09255 97  ARG A CD  
809  N  NE  A ARG A 98  ? 0.30348 0.25950 0.57968 0.02243  -0.08014 -0.10173 97  ARG A NE  
810  N  NE  B ARG A 98  ? 0.36403 0.30614 0.68696 0.01922  -0.08972 -0.10372 97  ARG A NE  
811  C  CZ  A ARG A 98  ? 0.33225 0.29605 0.66671 0.02815  -0.08413 -0.14237 97  ARG A CZ  
812  C  CZ  B ARG A 98  ? 0.38125 0.34488 0.73886 0.02779  -0.08770 -0.14836 97  ARG A CZ  
813  N  NH1 A ARG A 98  ? 0.39016 0.37654 0.71084 0.02846  -0.07881 -0.17446 97  ARG A NH1 
814  N  NH1 B ARG A 98  ? 0.35249 0.34736 0.68375 0.03015  -0.07853 -0.18451 97  ARG A NH1 
815  N  NH2 A ARG A 98  ? 0.37263 0.33634 0.77375 0.03229  -0.09279 -0.14456 97  ARG A NH2 
816  N  NH2 B ARG A 98  ? 0.36479 0.33256 0.77696 0.03265  -0.09351 -0.15059 97  ARG A NH2 
817  N  N   . ARG A 99  ? 0.28998 0.22941 0.36683 -0.00500 -0.06281 0.02032  98  ARG A N   
818  C  CA  . ARG A 99  ? 0.30283 0.23643 0.37503 -0.00762 -0.07000 0.05041  98  ARG A CA  
819  C  C   . ARG A 99  ? 0.30320 0.24499 0.32837 -0.00595 -0.06647 0.05112  98  ARG A C   
820  O  O   . ARG A 99  ? 0.33624 0.27706 0.36424 -0.00490 -0.07609 0.06292  98  ARG A O   
821  C  CB  . ARG A 99  ? 0.29657 0.22964 0.36761 -0.01582 -0.06954 0.08087  98  ARG A CB  
822  C  CG  . ARG A 99  ? 0.33441 0.25600 0.47126 -0.01886 -0.07858 0.09029  98  ARG A CG  
823  C  CD  . ARG A 99  ? 0.37527 0.30173 0.51364 -0.02844 -0.07323 0.11936  98  ARG A CD  
824  N  NE  . ARG A 99  ? 0.42243 0.36084 0.53484 -0.03440 -0.07421 0.16060  98  ARG A NE  
825  C  CZ  . ARG A 99  ? 0.44792 0.40428 0.54925 -0.04240 -0.06451 0.18547  98  ARG A CZ  
826  N  NH1 . ARG A 99  ? 0.46366 0.41800 0.58711 -0.04684 -0.05655 0.18292  98  ARG A NH1 
827  N  NH2 . ARG A 99  ? 0.42519 0.40597 0.49562 -0.04534 -0.06201 0.20752  98  ARG A NH2 
828  N  N   . LEU A 100 ? 0.27149 0.22150 0.26147 -0.00582 -0.05536 0.03941  99  LEU A N   
829  C  CA  . LEU A 100 ? 0.27941 0.23528 0.24019 -0.00423 -0.05404 0.03711  99  LEU A CA  
830  C  C   . LEU A 100 ? 0.31481 0.27287 0.29361 0.00084  -0.05662 0.02346  99  LEU A C   
831  O  O   . LEU A 100 ? 0.30419 0.26301 0.28115 0.00192  -0.06336 0.02734  99  LEU A O   
832  C  CB  . LEU A 100 ? 0.29072 0.25347 0.22504 -0.00515 -0.04311 0.02967  99  LEU A CB  
833  C  CG  . LEU A 100 ? 0.32646 0.29343 0.24027 -0.00926 -0.03796 0.03979  99  LEU A CG  
834  C  CD1 . LEU A 100 ? 0.36584 0.33762 0.27388 -0.00879 -0.02810 0.02947  99  LEU A CD1 
835  C  CD2 . LEU A 100 ? 0.38754 0.36213 0.27721 -0.00979 -0.04167 0.04371  99  LEU A CD2 
836  N  N   . LEU A 101 ? 0.27186 0.23583 0.26998 0.00389  -0.05147 0.00583  100 LEU A N   
837  C  CA  . LEU A 101 ? 0.26956 0.24369 0.28721 0.00875  -0.05032 -0.00816 100 LEU A CA  
838  C  C   . LEU A 101 ? 0.28455 0.24950 0.33846 0.01153  -0.06271 -0.00348 100 LEU A C   
839  O  O   . LEU A 101 ? 0.30245 0.27255 0.36847 0.01430  -0.06547 -0.00522 100 LEU A O   
840  C  CB  . LEU A 101 ? 0.27538 0.26713 0.30441 0.01173  -0.04182 -0.03174 100 LEU A CB  
841  C  CG  . LEU A 101 ? 0.28289 0.29196 0.27831 0.00934  -0.03142 -0.03209 100 LEU A CG  
842  C  CD1 . LEU A 101 ? 0.32867 0.35858 0.32814 0.01102  -0.02729 -0.05402 100 LEU A CD1 
843  C  CD2 . LEU A 101 ? 0.33583 0.36122 0.32398 0.00963  -0.02450 -0.02744 100 LEU A CD2 
844  N  N   . GLU A 102 ? 0.27762 0.22981 0.35761 0.01051  -0.07152 0.00487  101 GLU A N   
845  C  CA  . GLU A 102 ? 0.28515 0.22800 0.40842 0.01278  -0.08680 0.01643  101 GLU A CA  
846  C  C   . GLU A 102 ? 0.30244 0.24511 0.40117 0.01027  -0.09693 0.03992  101 GLU A C   
847  O  O   . GLU A 102 ? 0.31607 0.26017 0.44127 0.01392  -0.10714 0.04114  101 GLU A O   
848  C  CB  . GLU A 102 ? 0.29860 0.22774 0.45956 0.01007  -0.09570 0.02991  101 GLU A CB  
849  C  CG  . GLU A 102 ? 0.37504 0.30517 0.58694 0.01526  -0.09262 -0.00349 101 GLU A CG  
850  C  CD  . GLU A 102 ? 0.46351 0.37853 0.72775 0.01214  -0.10224 0.00527  101 GLU A CD  
851  O  OE1 . GLU A 102 ? 0.51532 0.42275 0.76401 0.00411  -0.10573 0.04001  101 GLU A OE1 
852  O  OE2 . GLU A 102 ? 0.43224 0.34632 0.75757 0.01761  -0.10558 -0.02486 101 GLU A OE2 
853  N  N   . ARG A 103 ? 0.30073 0.24578 0.35062 0.00454  -0.09433 0.05435  102 ARG A N   
854  C  CA  . ARG A 103 ? 0.32932 0.28121 0.35083 0.00235  -0.10435 0.06863  102 ARG A CA  
855  C  C   . ARG A 103 ? 0.29892 0.25700 0.31875 0.00575  -0.10292 0.05042  102 ARG A C   
856  O  O   . ARG A 103 ? 0.35169 0.31387 0.38026 0.00668  -0.11746 0.05622  102 ARG A O   
857  C  CB  . ARG A 103 ? 0.37241 0.33195 0.34472 -0.00325 -0.09767 0.07717  102 ARG A CB  
858  C  CG  . ARG A 103 ? 0.40992 0.38384 0.35004 -0.00543 -0.10858 0.08606  102 ARG A CG  
859  C  CD  . ARG A 103 ? 0.44616 0.42530 0.40417 -0.00670 -0.12670 0.11266  102 ARG A CD  
860  N  NE  . ARG A 103 ? 0.54216 0.54414 0.46007 -0.00818 -0.12902 0.11225  102 ARG A NE  
861  C  CZ  . ARG A 103 ? 0.54567 0.56594 0.43024 -0.01140 -0.12135 0.12299  102 ARG A CZ  
862  N  NH1 . ARG A 103 ? 0.49378 0.53656 0.34212 -0.00998 -0.12513 0.11447  102 ARG A NH1 
863  N  NH2 . ARG A 103 ? 0.49374 0.51120 0.38576 -0.01569 -0.11131 0.14075  102 ARG A NH2 
864  N  N   . ALA A 104 ? 0.29828 0.25976 0.31062 0.00684  -0.08690 0.03164  103 ALA A N   
865  C  CA  . ALA A 104 ? 0.28053 0.25022 0.29818 0.00831  -0.08386 0.02023  103 ALA A CA  
866  C  C   . ALA A 104 ? 0.25140 0.22556 0.31418 0.01304  -0.08841 0.01460  103 ALA A C   
867  O  O   . ALA A 104 ? 0.29090 0.27048 0.36823 0.01355  -0.09569 0.01398  103 ALA A O   
868  C  CB  . ALA A 104 ? 0.32316 0.30001 0.32867 0.00749  -0.06618 0.00993  103 ALA A CB  
869  N  N   A VAL A 105 ? 0.26936 0.24309 0.36183 0.01691  -0.08462 0.00700  104 VAL A N   
870  N  N   B VAL A 105 ? 0.26809 0.24177 0.36030 0.01688  -0.08461 0.00707  104 VAL A N   
871  C  CA  A VAL A 105 ? 0.27629 0.25774 0.41966 0.02277  -0.08738 -0.00337 104 VAL A CA  
872  C  CA  B VAL A 105 ? 0.26786 0.24895 0.41152 0.02283  -0.08733 -0.00349 104 VAL A CA  
873  C  C   A VAL A 105 ? 0.28544 0.25696 0.45570 0.02376  -0.11087 0.01441  104 VAL A C   
874  C  C   B VAL A 105 ? 0.28371 0.25521 0.45355 0.02372  -0.11075 0.01440  104 VAL A C   
875  O  O   A VAL A 105 ? 0.26301 0.24180 0.46861 0.02715  -0.11788 0.01131  104 VAL A O   
876  O  O   B VAL A 105 ? 0.25885 0.23779 0.46265 0.02696  -0.11761 0.01136  104 VAL A O   
877  C  CB  A VAL A 105 ? 0.26855 0.25733 0.44376 0.02803  -0.07664 -0.02566 104 VAL A CB  
878  C  CB  B VAL A 105 ? 0.26011 0.24634 0.43476 0.02777  -0.07790 -0.02425 104 VAL A CB  
879  C  CG1 A VAL A 105 ? 0.29663 0.26686 0.48954 0.02788  -0.08746 -0.01835 104 VAL A CG1 
880  C  CG1 B VAL A 105 ? 0.28043 0.27662 0.51749 0.03538  -0.08035 -0.03995 104 VAL A CG1 
881  C  CG2 A VAL A 105 ? 0.25952 0.26438 0.48972 0.03518  -0.07432 -0.04363 104 VAL A CG2 
882  C  CG2 B VAL A 105 ? 0.21096 0.21666 0.35482 0.02660  -0.05678 -0.04074 104 VAL A CG2 
883  N  N   . THR A 106 ? 0.30304 0.26208 0.45983 0.02032  -0.12388 0.03643  105 THR A N   
884  C  CA  . THR A 106 ? 0.27342 0.22970 0.44883 0.01985  -0.14876 0.06125  105 THR A CA  
885  C  C   . THR A 106 ? 0.30448 0.27149 0.45155 0.01744  -0.15829 0.06349  105 THR A C   
886  O  O   . THR A 106 ? 0.35729 0.32886 0.53259 0.01853  -0.17304 0.06845  105 THR A O   
887  C  CB  . THR A 106 ? 0.33692 0.28627 0.49397 0.01416  -0.15668 0.08975  105 THR A CB  
888  O  OG1 . THR A 106 ? 0.36398 0.30179 0.56952 0.01619  -0.15286 0.08668  105 THR A OG1 
889  C  CG2 . THR A 106 ? 0.38356 0.34138 0.53250 0.00768  -0.17042 0.11432  105 THR A CG2 
890  N  N   . TYR A 107 ? 0.33348 0.30467 0.42968 0.01326  -0.14725 0.05510  106 TYR A N   
891  C  CA  . TYR A 107 ? 0.30799 0.28922 0.38630 0.01114  -0.15677 0.04964  106 TYR A CA  
892  C  C   . TYR A 107 ? 0.32896 0.31525 0.44949 0.01431  -0.15233 0.03334  106 TYR A C   
893  O  O   . TYR A 107 ? 0.32375 0.31757 0.46285 0.01426  -0.16928 0.03279  106 TYR A O   
894  C  CB  . TYR A 107 ? 0.31636 0.29985 0.34396 0.00686  -0.14513 0.04046  106 TYR A CB  
895  C  CG  . TYR A 107 ? 0.30467 0.29756 0.32369 0.00504  -0.15373 0.02608  106 TYR A CG  
896  C  CD1 . TYR A 107 ? 0.32074 0.32723 0.31082 0.00270  -0.17318 0.02842  106 TYR A CD1 
897  C  CD2 . TYR A 107 ? 0.27462 0.26639 0.31665 0.00511  -0.14228 0.01017  106 TYR A CD2 
898  C  CE1 . TYR A 107 ? 0.38356 0.40023 0.37240 0.00143  -0.18044 0.00648  106 TYR A CE1 
899  C  CE2 . TYR A 107 ? 0.33102 0.32894 0.37937 0.00301  -0.15162 -0.00453 106 TYR A CE2 
900  C  CZ  . TYR A 107 ? 0.39515 0.40401 0.41884 0.00169  -0.17248 -0.00993 106 TYR A CZ  
901  O  OH  . TYR A 107 ? 0.44040 0.45653 0.47766 0.00005  -0.18366 -0.03216 106 TYR A OH  
902  N  N   . ALA A 108 ? 0.27386 0.26123 0.40963 0.01642  -0.12958 0.02040  107 ALA A N   
903  C  CA  . ALA A 108 ? 0.30095 0.30129 0.47874 0.01866  -0.12125 0.00881  107 ALA A CA  
904  C  C   . ALA A 108 ? 0.28441 0.28832 0.51711 0.02392  -0.13639 0.01084  107 ALA A C   
905  O  O   . ALA A 108 ? 0.29288 0.30699 0.55925 0.02411  -0.14355 0.00803  107 ALA A O   
906  C  CB  . ALA A 108 ? 0.25680 0.26779 0.43653 0.02008  -0.09398 -0.00306 107 ALA A CB  
907  N  N   . HIS A 109 ? 0.26691 0.26239 0.51919 0.02819  -0.14304 0.01649  108 HIS A N   
908  C  CA  . HIS A 109 ? 0.26742 0.26370 0.57826 0.03274  -0.15868 0.02021  108 HIS A CA  
909  C  C   . HIS A 109 ? 0.31348 0.30529 0.60522 0.02621  -0.18058 0.03793  108 HIS A C   
910  O  O   . HIS A 109 ? 0.32289 0.31949 0.64906 0.02631  -0.18780 0.03528  108 HIS A O   
911  C  CB  . HIS A 109 ? 0.32225 0.30606 0.65971 0.03513  -0.15854 0.02232  108 HIS A CB  
912  C  CG  . HIS A 109 ? 0.35724 0.33872 0.75166 0.03538  -0.16704 0.02192  108 HIS A CG  
913  N  ND1 . HIS A 109 ? 0.42415 0.39605 0.82112 0.02915  -0.18862 0.04747  108 HIS A ND1 
914  C  CD2 . HIS A 109 ? 0.39032 0.38202 0.84133 0.04058  -0.15644 -0.00107 108 HIS A CD2 
915  C  CE1 . HIS A 109 ? 0.44638 0.41809 0.90465 0.03049  -0.19344 0.04143  108 HIS A CE1 
916  N  NE2 . HIS A 109 ? 0.42649 0.40940 0.91763 0.03735  -0.17371 0.01054  108 HIS A NE2 
917  N  N   . ALA A 110 ? 0.31209 0.29941 0.54893 0.02080  -0.19004 0.05433  109 ALA A N   
918  C  CA  . ALA A 110 ? 0.36784 0.36111 0.58340 0.01611  -0.20937 0.06802  109 ALA A CA  
919  C  C   . ALA A 110 ? 0.34317 0.34671 0.55772 0.01518  -0.21435 0.05232  109 ALA A C   
920  O  O   . ALA A 110 ? 0.41069 0.42143 0.63355 0.01386  -0.23132 0.05677  109 ALA A O   
921  C  CB  . ALA A 110 ? 0.43929 0.43687 0.59322 0.01126  -0.21243 0.08432  109 ALA A CB  
922  N  N   . SER A 111 ? 0.35921 0.46287 0.49919 0.05475  -0.20927 0.06766  110 SER A N   
923  C  CA  . SER A 111 ? 0.33932 0.43762 0.48330 0.05764  -0.21862 0.04235  110 SER A CA  
924  C  C   . SER A 111 ? 0.35610 0.43730 0.55588 0.04801  -0.21489 0.03377  110 SER A C   
925  O  O   . SER A 111 ? 0.35364 0.42670 0.56716 0.04330  -0.22285 0.01909  110 SER A O   
926  C  CB  . SER A 111 ? 0.33523 0.43584 0.44515 0.06373  -0.21422 0.02634  110 SER A CB  
927  O  OG  . SER A 111 ? 0.32098 0.41106 0.44678 0.05679  -0.19516 0.02826  110 SER A OG  
928  N  N   . HIS A 112 ? 0.32301 0.40257 0.55568 0.04588  -0.20530 0.04370  111 HIS A N   
929  C  CA  . HIS A 112 ? 0.28615 0.37209 0.57127 0.04305  -0.19926 0.03745  111 HIS A CA  
930  C  C   . HIS A 112 ? 0.25798 0.35151 0.56097 0.03562  -0.18224 0.03030  111 HIS A C   
931  O  O   . HIS A 112 ? 0.25844 0.37087 0.59886 0.02841  -0.18096 0.02883  111 HIS A O   
932  C  CB  . HIS A 112 ? 0.30819 0.40256 0.61572 0.04154  -0.21822 0.03457  111 HIS A CB  
933  C  CG  . HIS A 112 ? 0.30752 0.41962 0.66149 0.04698  -0.21556 0.03590  111 HIS A CG  
934  N  ND1 . HIS A 112 ? 0.29681 0.44133 0.69637 0.04389  -0.20410 0.03246  111 HIS A ND1 
935  C  CD2 . HIS A 112 ? 0.32609 0.43357 0.68759 0.05770  -0.22362 0.04054  111 HIS A CD2 
936  C  CE1 . HIS A 112 ? 0.29933 0.46512 0.72996 0.05744  -0.20312 0.03059  111 HIS A CE1 
937  N  NE2 . HIS A 112 ? 0.32167 0.45763 0.73062 0.06605  -0.21714 0.03366  111 HIS A NE2 
938  N  N   . CYS A 113 ? 0.26581 0.35071 0.54483 0.03565  -0.16908 0.03040  112 CYS A N   
939  C  CA  . CYS A 113 ? 0.29938 0.39397 0.59651 0.02909  -0.15107 0.02685  112 CYS A CA  
940  C  C   . CYS A 113 ? 0.26523 0.38114 0.59427 0.03678  -0.13243 0.02543  112 CYS A C   
941  O  O   . CYS A 113 ? 0.28676 0.38976 0.60936 0.04835  -0.13322 0.02464  112 CYS A O   
942  C  CB  . CYS A 113 ? 0.27166 0.35152 0.53226 0.02925  -0.14424 0.02573  112 CYS A CB  
943  S  SG  . CYS A 113 ? 0.31817 0.38167 0.53076 0.03219  -0.16570 0.01628  112 CYS A SG  
944  N  N   . ARG A 114 ? 0.18850 0.33894 0.54914 0.03088  -0.11787 0.02551  113 ARG A N   
945  C  CA  . ARG A 114 ? 0.18397 0.37162 0.56880 0.04492  -0.09776 0.01867  113 ARG A CA  
946  C  C   . ARG A 114 ? 0.21894 0.39323 0.58237 0.05236  -0.08210 0.01120  113 ARG A C   
947  O  O   . ARG A 114 ? 0.24436 0.42317 0.60996 0.07285  -0.07625 -0.00260 113 ARG A O   
948  C  CB  . ARG A 114 ? 0.22457 0.47338 0.64629 0.03460  -0.08485 0.02737  113 ARG A CB  
949  C  CG  . ARG A 114 ? 0.31178 0.62130 0.75340 0.05717  -0.06269 0.01662  113 ARG A CG  
950  C  CD  . ARG A 114 ? 0.47916 0.86995 0.95553 0.04566  -0.04772 0.02893  113 ARG A CD  
951  N  NE  . ARG A 114 ? 0.48853 0.94989 0.97585 0.07498  -0.02585 0.00983  113 ARG A NE  
952  C  CZ  . ARG A 114 ? 0.40593 0.86701 0.88094 0.08120  -0.00628 -0.00307 113 ARG A CZ  
953  N  NH1 . ARG A 114 ? 0.28794 0.70972 0.72883 0.06226  -0.00285 0.01134  113 ARG A NH1 
954  N  NH2 . ARG A 114 ? 0.43253 0.92616 0.92409 0.10682  0.01431  -0.00507 113 ARG A NH2 
955  N  N   . ALA A 115 ? 0.19502 0.35094 0.53732 0.03839  -0.07877 0.01741  114 ALA A N   
956  C  CA  . ALA A 115 ? 0.19733 0.34200 0.51166 0.04148  -0.06004 0.01140  114 ALA A CA  
957  C  C   . ALA A 115 ? 0.17924 0.28622 0.44923 0.02782  -0.06262 0.01737  114 ALA A C   
958  O  O   . ALA A 115 ? 0.22665 0.32252 0.48983 0.01891  -0.07829 0.02202  114 ALA A O   
959  C  CB  . ALA A 115 ? 0.20826 0.40336 0.54038 0.03987  -0.03613 0.01177  114 ALA A CB  
960  N  N   . LEU A 116 ? 0.18128 0.27139 0.42191 0.03011  -0.05026 0.01366  115 LEU A N   
961  C  CA  . LEU A 116 ? 0.19226 0.26012 0.39381 0.02156  -0.04775 0.01703  115 LEU A CA  
962  C  C   . LEU A 116 ? 0.19949 0.27694 0.39553 0.01585  -0.02898 0.01573  115 LEU A C   
963  O  O   . LEU A 116 ? 0.21353 0.31268 0.42197 0.02290  -0.01514 0.01008  115 LEU A O   
964  C  CB  . LEU A 116 ? 0.24425 0.29210 0.41842 0.02501  -0.05202 0.02150  115 LEU A CB  
965  C  CG  . LEU A 116 ? 0.26313 0.30795 0.43438 0.02707  -0.07175 0.03267  115 LEU A CG  
966  C  CD1 . LEU A 116 ? 0.30745 0.34652 0.51068 0.03438  -0.08362 0.03357  115 LEU A CD1 
967  C  CD2 . LEU A 116 ? 0.30399 0.34962 0.44181 0.02303  -0.07298 0.04732  115 LEU A CD2 
968  N  N   . THR A 117 ? 0.20368 0.26754 0.38020 0.00647  -0.03184 0.01923  116 THR A N   
969  C  CA  . THR A 117 ? 0.16863 0.23869 0.33915 -0.00185 -0.01883 0.02372  116 THR A CA  
970  C  C   . THR A 117 ? 0.25610 0.29896 0.38926 -0.00029 -0.02074 0.01985  116 THR A C   
971  O  O   . THR A 117 ? 0.22858 0.25684 0.34232 0.00704  -0.03320 0.01417  116 THR A O   
972  C  CB  . THR A 117 ? 0.19878 0.28344 0.39798 -0.01958 -0.02761 0.03918  116 THR A CB  
973  O  OG1 . THR A 117 ? 0.21836 0.26894 0.41246 -0.02286 -0.05596 0.03634  116 THR A OG1 
974  C  CG2 . THR A 117 ? 0.19374 0.32399 0.43762 -0.02187 -0.02418 0.04709  116 THR A CG2 
975  N  N   . LEU A 118 ? 0.21582 0.26180 0.33891 -0.00498 -0.00842 0.02327  117 LEU A N   
976  C  CA  . LEU A 118 ? 0.21677 0.24209 0.31038 -0.00309 -0.01120 0.02036  117 LEU A CA  
977  C  C   . LEU A 118 ? 0.21562 0.24819 0.30717 -0.01290 -0.00175 0.03023  117 LEU A C   
978  O  O   . LEU A 118 ? 0.21987 0.28368 0.32812 -0.01902 0.01103  0.03917  117 LEU A O   
979  C  CB  . LEU A 118 ? 0.21066 0.23464 0.28350 0.00681  -0.00534 0.01420  117 LEU A CB  
980  C  CG  . LEU A 118 ? 0.28703 0.31801 0.36421 0.00836  0.00623  0.01235  117 LEU A CG  
981  C  CD1 . LEU A 118 ? 0.24438 0.27619 0.30613 0.00642  0.01613  0.01101  117 LEU A CD1 
982  C  CD2 . LEU A 118 ? 0.24861 0.27432 0.32190 0.01107  -0.00134 0.01570  117 LEU A CD2 
983  N  N   . THR A 119 ? 0.22024 0.23171 0.29097 -0.01205 -0.00936 0.02936  118 THR A N   
984  C  CA  . THR A 119 ? 0.24622 0.26267 0.30671 -0.01949 -0.00136 0.03953  118 THR A CA  
985  C  C   . THR A 119 ? 0.24693 0.25299 0.27996 -0.00782 0.00219  0.02779  118 THR A C   
986  O  O   . THR A 119 ? 0.27105 0.26744 0.29472 0.00365  -0.00694 0.01730  118 THR A O   
987  C  CB  . THR A 119 ? 0.27927 0.27752 0.34943 -0.03490 -0.02261 0.05832  118 THR A CB  
988  O  OG1 . THR A 119 ? 0.30921 0.26623 0.36795 -0.02310 -0.04957 0.04425  118 THR A OG1 
989  C  CG2 . THR A 119 ? 0.28280 0.29786 0.38977 -0.05417 -0.03109 0.07974  118 THR A CG2 
990  N  N   . THR A 120 ? 0.23256 0.24979 0.25314 -0.00955 0.01459  0.03022  119 THR A N   
991  C  CA  . THR A 120 ? 0.24943 0.26132 0.25122 -0.00139 0.01591  0.02130  119 THR A CA  
992  C  C   . THR A 120 ? 0.28720 0.30706 0.27344 -0.00434 0.02311  0.02445  119 THR A C   
993  O  O   . THR A 120 ? 0.29488 0.33248 0.28181 -0.01137 0.02968  0.03515  119 THR A O   
994  C  CB  . THR A 120 ? 0.27157 0.28878 0.27945 0.00381  0.01871  0.01355  119 THR A CB  
995  O  OG1 . THR A 120 ? 0.29809 0.31674 0.29650 0.00630  0.01444  0.01386  119 THR A OG1 
996  C  CG2 . THR A 120 ? 0.26796 0.29375 0.28042 0.00597  0.02620  0.00625  119 THR A CG2 
997  N  N   . PHE A 121 ? 0.25889 0.27370 0.23166 0.00036  0.02043  0.01838  120 PHE A N   
998  C  CA  . PHE A 121 ? 0.27282 0.29348 0.22716 0.00007  0.02316  0.01760  120 PHE A CA  
999  C  C   . PHE A 121 ? 0.31644 0.34817 0.26872 0.00701  0.02849  0.00271  120 PHE A C   
1000 O  O   . PHE A 121 ? 0.31176 0.33290 0.27713 0.01064  0.02179  -0.00701 120 PHE A O   
1001 C  CB  . PHE A 121 ? 0.30126 0.31435 0.24712 0.00264  0.01374  0.01581  120 PHE A CB  
1002 C  CG  . PHE A 121 ? 0.27123 0.27568 0.21400 0.00497  0.00401  0.02302  120 PHE A CG  
1003 C  CD1 . PHE A 121 ? 0.28623 0.28196 0.21844 -0.00041 -0.00189 0.03530  120 PHE A CD1 
1004 C  CD2 . PHE A 121 ? 0.27158 0.28095 0.22242 0.01505  -0.00303 0.01821  120 PHE A CD2 
1005 C  CE1 . PHE A 121 ? 0.32157 0.29754 0.25485 0.00487  -0.02088 0.03924  120 PHE A CE1 
1006 C  CE2 . PHE A 121 ? 0.29596 0.29634 0.24349 0.02670  -0.01789 0.01583  120 PHE A CE2 
1007 C  CZ  . PHE A 121 ? 0.33098 0.30675 0.27152 0.02178  -0.02977 0.02477  120 PHE A CZ  
1008 N  N   . CYS A 122 ? 0.28137 0.33646 0.21625 0.01099  0.03622  0.00092  121 CYS A N   
1009 C  CA  . CYS A 122 ? 0.30717 0.37909 0.23474 0.02818  0.03781  -0.02281 121 CYS A CA  
1010 C  C   . CYS A 122 ? 0.39481 0.43773 0.31478 0.03574  0.01806  -0.04303 121 CYS A C   
1011 O  O   . CYS A 122 ? 0.40689 0.43632 0.33623 0.04906  0.00468  -0.06566 121 CYS A O   
1012 C  CB  . CYS A 122 ? 0.37810 0.50020 0.28238 0.03454  0.05187  -0.01894 121 CYS A CB  
1013 S  SG  . CYS A 122 ? 0.37048 0.54066 0.29369 0.01958  0.06999  0.01413  121 CYS A SG  
1014 N  N   . ASP A 123 ? 0.36577 0.39757 0.27227 0.02780  0.01054  -0.03510 122 ASP A N   
1015 C  CA  . ASP A 123 ? 0.44171 0.45326 0.34055 0.03262  -0.01156 -0.05160 122 ASP A CA  
1016 C  C   . ASP A 123 ? 0.47680 0.46833 0.39766 0.01615  -0.02589 -0.03577 122 ASP A C   
1017 O  O   . ASP A 123 ? 0.64391 0.62553 0.56160 0.01329  -0.04454 -0.03916 122 ASP A O   
1018 C  CB  . ASP A 123 ? 0.54958 0.57932 0.41203 0.03985  -0.01101 -0.05666 122 ASP A CB  
1019 C  CG  . ASP A 123 ? 0.65651 0.73085 0.49363 0.05724  0.00581  -0.06692 122 ASP A CG  
1020 O  OD1 . ASP A 123 ? 0.71426 0.79791 0.55679 0.07607  0.00529  -0.09109 122 ASP A OD1 
1021 O  OD2 . ASP A 123 ? 0.74468 0.85152 0.55777 0.05279  0.01802  -0.04832 122 ASP A OD2 
1022 N  N   . VAL A 124 ? 0.35876 0.35396 0.30134 0.00659  -0.01814 -0.01779 123 VAL A N   
1023 C  CA  . VAL A 124 ? 0.33457 0.33361 0.30056 -0.00579 -0.02876 -0.00046 123 VAL A CA  
1024 C  C   . VAL A 124 ? 0.36704 0.35145 0.35989 -0.01252 -0.04530 0.00159  123 VAL A C   
1025 O  O   . VAL A 124 ? 0.35390 0.33299 0.35220 -0.00740 -0.03868 -0.00293 123 VAL A O   
1026 C  CB  . VAL A 124 ? 0.29191 0.31266 0.26065 -0.00531 -0.01415 0.01395  123 VAL A CB  
1027 C  CG1 . VAL A 124 ? 0.29359 0.34237 0.28586 -0.01277 -0.02031 0.03223  123 VAL A CG1 
1028 C  CG2 . VAL A 124 ? 0.31723 0.34096 0.26555 0.00046  -0.01056 0.01386  123 VAL A CG2 
1029 N  N   . PRO A 125 ? 0.37561 0.35123 0.39001 -0.02586 -0.07193 0.01122  124 PRO A N   
1030 C  CA  . PRO A 125 ? 0.38842 0.33501 0.43071 -0.03342 -0.09964 0.01333  124 PRO A CA  
1031 C  C   . PRO A 125 ? 0.36051 0.32422 0.42392 -0.04280 -0.09215 0.03782  124 PRO A C   
1032 O  O   . PRO A 125 ? 0.37154 0.30682 0.45098 -0.04191 -0.10938 0.03407  124 PRO A O   
1033 C  CB  . PRO A 125 ? 0.39422 0.33181 0.46283 -0.05391 -0.13527 0.02996  124 PRO A CB  
1034 C  CG  . PRO A 125 ? 0.40845 0.36517 0.45538 -0.04984 -0.12553 0.02409  124 PRO A CG  
1035 C  CD  . PRO A 125 ? 0.37946 0.36651 0.39711 -0.03517 -0.08458 0.02047  124 PRO A CD  
1036 N  N   . TRP A 126 ? 0.34194 0.35290 0.40460 -0.04785 -0.07035 0.06023  125 TRP A N   
1037 C  CA  . TRP A 126 ? 0.29851 0.33504 0.37373 -0.05282 -0.06312 0.08151  125 TRP A CA  
1038 C  C   . TRP A 126 ? 0.26299 0.29741 0.31592 -0.03384 -0.03890 0.06165  125 TRP A C   
1039 O  O   . TRP A 126 ? 0.29708 0.35710 0.35244 -0.03292 -0.03092 0.07410  125 TRP A O   
1040 C  CB  . TRP A 126 ? 0.26275 0.36652 0.34952 -0.06365 -0.05680 0.11521  125 TRP A CB  
1041 C  CG  . TRP A 126 ? 0.25245 0.38794 0.31469 -0.04507 -0.03461 0.10109  125 TRP A CG  
1042 C  CD1 . TRP A 126 ? 0.23556 0.38694 0.27574 -0.02395 -0.01544 0.08658  125 TRP A CD1 
1043 C  CD2 . TRP A 126 ? 0.26808 0.41663 0.32886 -0.04475 -0.03736 0.09932  125 TRP A CD2 
1044 N  NE1 . TRP A 126 ? 0.22840 0.39608 0.25429 -0.00909 -0.00897 0.07471  125 TRP A NE1 
1045 C  CE2 . TRP A 126 ? 0.22532 0.39552 0.26297 -0.02125 -0.01964 0.08330  125 TRP A CE2 
1046 C  CE3 . TRP A 126 ? 0.31483 0.45518 0.39369 -0.06143 -0.05864 0.10876  125 TRP A CE3 
1047 C  CZ2 . TRP A 126 ? 0.25178 0.43714 0.28378 -0.01279 -0.02047 0.07752  125 TRP A CZ2 
1048 C  CZ3 . TRP A 126 ? 0.32106 0.48219 0.39316 -0.05459 -0.05648 0.10374  125 TRP A CZ3 
1049 C  CH2 . TRP A 126 ? 0.35570 0.54065 0.40475 -0.02995 -0.03642 0.08906  125 TRP A CH2 
1050 N  N   . ASN A 127 ? 0.25416 0.26498 0.28640 -0.01990 -0.02922 0.03414  126 ASN A N   
1051 C  CA  . ASN A 127 ? 0.26137 0.27128 0.28247 -0.00817 -0.01200 0.02183  126 ASN A CA  
1052 C  C   . ASN A 127 ? 0.28399 0.27196 0.31031 0.00057  -0.01631 0.00316  126 ASN A C   
1053 O  O   . ASN A 127 ? 0.27001 0.24333 0.31672 -0.00140 -0.03261 0.00591  126 ASN A O   
1054 C  CB  . ASN A 127 ? 0.26698 0.28415 0.26605 -0.00169 0.00191  0.01549  126 ASN A CB  
1055 C  CG  . ASN A 127 ? 0.29408 0.33460 0.28927 0.00082  0.00374  0.02523  126 ASN A CG  
1056 O  OD1 . ASN A 127 ? 0.29958 0.33886 0.28101 0.00669  0.00557  0.02092  126 ASN A OD1 
1057 N  ND2 . ASN A 127 ? 0.26267 0.32945 0.26915 -0.00048 0.00115  0.03799  126 ASN A ND2 
1058 N  N   . ALA A 128 ? 0.33828 0.33024 0.29058 0.06897  -0.02124 0.01917  127 ALA A N   
1059 C  CA  . ALA A 128 ? 0.32827 0.28694 0.25156 0.05875  -0.00832 0.00907  127 ALA A CA  
1060 C  C   . ALA A 128 ? 0.35968 0.31556 0.26889 0.04270  -0.01452 0.00080  127 ALA A C   
1061 O  O   . ALA A 128 ? 0.33601 0.28171 0.25980 0.03917  -0.00034 -0.00650 127 ALA A O   
1062 C  CB  . ALA A 128 ? 0.35328 0.27393 0.23550 0.06113  -0.00053 0.01582  127 ALA A CB  
1063 N  N   . PRO A 129 ? 0.35722 0.31973 0.24187 0.03035  -0.03515 0.00433  128 PRO A N   
1064 C  CA  . PRO A 129 ? 0.38231 0.32675 0.24592 0.01051  -0.03560 -0.00778 128 PRO A CA  
1065 C  C   . PRO A 129 ? 0.37222 0.33968 0.28079 0.00905  -0.03585 -0.01084 128 PRO A C   
1066 O  O   . PRO A 129 ? 0.35972 0.29914 0.26911 0.00256  -0.02371 -0.01833 128 PRO A O   
1067 C  CB  . PRO A 129 ? 0.39912 0.35680 0.22816 -0.01014 -0.06523 0.00091  128 PRO A CB  
1068 C  CG  . PRO A 129 ? 0.44656 0.41044 0.26300 -0.00055 -0.07570 0.02029  128 PRO A CG  
1069 C  CD  . PRO A 129 ? 0.37478 0.35897 0.25008 0.02976  -0.06046 0.02339  128 PRO A CD  
1070 N  N   . PHE A 130 ? 0.33752 0.35223 0.28289 0.01301  -0.04737 -0.00361 129 PHE A N   
1071 C  CA  . PHE A 130 ? 0.27779 0.31511 0.25554 0.00485  -0.04780 -0.00413 129 PHE A CA  
1072 C  C   . PHE A 130 ? 0.31184 0.33373 0.30671 0.00894  -0.03249 -0.00281 129 PHE A C   
1073 O  O   . PHE A 130 ? 0.29919 0.31323 0.30987 0.00009  -0.03330 0.00227  129 PHE A O   
1074 C  CB  . PHE A 130 ? 0.25479 0.33983 0.26070 0.00678  -0.05173 -0.00084 129 PHE A CB  
1075 C  CG  . PHE A 130 ? 0.23933 0.34429 0.26384 -0.00765 -0.04660 -0.00290 129 PHE A CG  
1076 C  CD1 . PHE A 130 ? 0.34676 0.44922 0.37047 -0.02815 -0.05676 0.00116  129 PHE A CD1 
1077 C  CD2 . PHE A 130 ? 0.32125 0.44178 0.35806 -0.00497 -0.03007 -0.00822 129 PHE A CD2 
1078 C  CE1 . PHE A 130 ? 0.29219 0.41394 0.32374 -0.04905 -0.05680 0.00492  129 PHE A CE1 
1079 C  CE2 . PHE A 130 ? 0.29885 0.43290 0.33430 -0.02920 -0.02416 -0.01175 129 PHE A CE2 
1080 C  CZ  . PHE A 130 ? 0.29661 0.43519 0.32782 -0.05309 -0.04103 -0.00268 129 PHE A CZ  
1081 N  N   . TYR A 131 ? 0.26521 0.28285 0.26180 0.02060  -0.02022 -0.00267 130 TYR A N   
1082 C  CA  . TYR A 131 ? 0.22886 0.24287 0.24576 0.01698  -0.01104 0.00347  130 TYR A CA  
1083 C  C   . TYR A 131 ? 0.27027 0.25777 0.29850 0.02276  0.00032  0.00768  130 TYR A C   
1084 O  O   . TYR A 131 ? 0.27908 0.27610 0.34676 0.01802  0.00088  0.02216  130 TYR A O   
1085 C  CB  . TYR A 131 ? 0.26141 0.26889 0.27086 0.02275  0.00156  0.00122  130 TYR A CB  
1086 C  CG  . TYR A 131 ? 0.24681 0.26827 0.25143 0.02002  0.00356  -0.00608 130 TYR A CG  
1087 C  CD1 . TYR A 131 ? 0.30094 0.34629 0.31112 -0.00114 -0.00056 -0.00851 130 TYR A CD1 
1088 C  CD2 . TYR A 131 ? 0.25916 0.26563 0.25476 0.03810  0.01408  -0.00933 130 TYR A CD2 
1089 C  CE1 . TYR A 131 ? 0.41412 0.46514 0.41911 -0.00394 0.01462  -0.02094 130 TYR A CE1 
1090 C  CE2 . TYR A 131 ? 0.25397 0.26720 0.25795 0.04150  0.02632  -0.01666 130 TYR A CE2 
1091 C  CZ  . TYR A 131 ? 0.31683 0.35048 0.32473 0.02097  0.03104  -0.02580 130 TYR A CZ  
1092 O  OH  . TYR A 131 ? 0.31855 0.35217 0.33451 0.02421  0.05573  -0.03833 130 TYR A OH  
1093 N  N   . ALA A 132 ? 0.30307 0.25708 0.29884 0.03076  0.01161  -0.00261 131 ALA A N   
1094 C  CA  . ALA A 132 ? 0.33627 0.25422 0.33911 0.03623  0.03638  -0.00535 131 ALA A CA  
1095 C  C   . ALA A 132 ? 0.35354 0.26290 0.38286 0.03127  0.03406  -0.00151 131 ALA A C   
1096 O  O   . ALA A 132 ? 0.38272 0.27868 0.45899 0.04032  0.05367  0.00774  131 ALA A O   
1097 C  CB  . ALA A 132 ? 0.40198 0.27585 0.34200 0.03474  0.05195  -0.02165 131 ALA A CB  
1098 N  N   . ARG A 133 ? 0.37791 0.29491 0.38500 0.01741  0.01175  -0.00533 132 ARG A N   
1099 C  CA  . ARG A 133 ? 0.34896 0.25058 0.37738 0.00943  0.00871  0.00029  132 ARG A CA  
1100 C  C   . ARG A 133 ? 0.30576 0.24126 0.39994 0.00980  -0.00276 0.02811  132 ARG A C   
1101 O  O   . ARG A 133 ? 0.36598 0.28219 0.49851 0.01090  0.00061  0.04267  132 ARG A O   
1102 C  CB  . ARG A 133 ? 0.37719 0.28749 0.36972 -0.01185 -0.01535 -0.00648 132 ARG A CB  
1103 C  CG  . ARG A 133 ? 0.44020 0.31458 0.36625 -0.02379 -0.01174 -0.02669 132 ARG A CG  
1104 C  CD  . ARG A 133 ? 0.44505 0.33133 0.34582 -0.05117 -0.03743 -0.02836 132 ARG A CD  
1105 N  NE  . ARG A 133 ? 0.40861 0.36628 0.33330 -0.05381 -0.06342 -0.01641 132 ARG A NE  
1106 C  CZ  . ARG A 133 ? 0.42496 0.41812 0.33736 -0.05387 -0.07776 -0.01411 132 ARG A CZ  
1107 N  NH1 . ARG A 133 ? 0.46794 0.43462 0.33431 -0.05690 -0.07736 -0.01912 132 ARG A NH1 
1108 N  NH2 . ARG A 133 ? 0.42840 0.48324 0.37707 -0.05188 -0.09047 -0.00421 132 ARG A NH2 
1109 N  N   . LEU A 134 ? 0.28240 0.26319 0.38643 0.00469  -0.01704 0.03779  133 LEU A N   
1110 C  CA  . LEU A 134 ? 0.27683 0.29311 0.42786 -0.00767 -0.03430 0.06723  133 LEU A CA  
1111 C  C   . LEU A 134 ? 0.27177 0.29469 0.47912 0.00472  -0.02173 0.08760  133 LEU A C   
1112 O  O   . LEU A 134 ? 0.26853 0.32634 0.52390 -0.00932 -0.04171 0.12136  133 LEU A O   
1113 C  CB  . LEU A 134 ? 0.25890 0.31163 0.38026 -0.02910 -0.05035 0.06355  133 LEU A CB  
1114 C  CG  . LEU A 134 ? 0.30334 0.36325 0.38305 -0.03827 -0.05599 0.04402  133 LEU A CG  
1115 C  CD1 . LEU A 134 ? 0.31107 0.39793 0.37038 -0.05667 -0.05699 0.03834  133 LEU A CD1 
1116 C  CD2 . LEU A 134 ? 0.31147 0.37163 0.39635 -0.05429 -0.07157 0.05416  133 LEU A CD2 
1117 N  N   . GLY A 135 ? 0.24692 0.24295 0.44899 0.02552  0.00897  0.07141  134 GLY A N   
1118 C  CA  . GLY A 135 ? 0.25644 0.26231 0.52016 0.03839  0.02831  0.08981  134 GLY A CA  
1119 C  C   . GLY A 135 ? 0.27123 0.28806 0.51252 0.03627  0.03754  0.08108  134 GLY A C   
1120 O  O   . GLY A 135 ? 0.31327 0.34307 0.60725 0.04414  0.05607  0.09635  134 GLY A O   
1121 N  N   . PHE A 136 ? 0.24754 0.26023 0.42130 0.02648  0.02764  0.06025  135 PHE A N   
1122 C  CA  . PHE A 136 ? 0.24621 0.25523 0.39442 0.02548  0.03931  0.05209  135 PHE A CA  
1123 C  C   . PHE A 136 ? 0.30543 0.27436 0.43259 0.04428  0.07269  0.03633  135 PHE A C   
1124 O  O   . PHE A 136 ? 0.38493 0.32048 0.47638 0.05158  0.08060  0.01959  135 PHE A O   
1125 C  CB  . PHE A 136 ? 0.26007 0.26514 0.35056 0.01651  0.02631  0.03547  135 PHE A CB  
1126 C  CG  . PHE A 136 ? 0.27854 0.31296 0.37114 -0.01125 0.00586  0.04425  135 PHE A CG  
1127 C  CD1 . PHE A 136 ? 0.24431 0.29770 0.33795 -0.02567 -0.01414 0.04857  135 PHE A CD1 
1128 C  CD2 . PHE A 136 ? 0.30653 0.34307 0.38877 -0.02995 0.00875  0.04653  135 PHE A CD2 
1129 C  CE1 . PHE A 136 ? 0.26941 0.34374 0.34825 -0.06068 -0.02932 0.05445  135 PHE A CE1 
1130 C  CE2 . PHE A 136 ? 0.28153 0.33432 0.34684 -0.06617 -0.00647 0.05027  135 PHE A CE2 
1131 C  CZ  . PHE A 136 ? 0.25411 0.32535 0.31446 -0.08235 -0.02438 0.05356  135 PHE A CZ  
1132 N  N   A GLN A 137 ? 0.30022 0.27074 0.44270 0.04521  0.09291  0.04180  136 GLN A N   
1133 N  N   B GLN A 137 ? 0.29051 0.26120 0.43342 0.04521  0.09289  0.04192  136 GLN A N   
1134 C  CA  A GLN A 137 ? 0.36092 0.29280 0.47880 0.05638  0.13064  0.02779  136 GLN A CA  
1135 C  CA  B GLN A 137 ? 0.36135 0.29354 0.47933 0.05625  0.13054  0.02793  136 GLN A CA  
1136 C  C   A GLN A 137 ? 0.38797 0.30057 0.44311 0.04975  0.13061  0.01918  136 GLN A C   
1137 C  C   B GLN A 137 ? 0.39834 0.31098 0.45223 0.04964  0.12951  0.01900  136 GLN A C   
1138 O  O   A GLN A 137 ? 0.36012 0.29281 0.42640 0.03867  0.12060  0.02965  136 GLN A O   
1139 O  O   B GLN A 137 ? 0.35737 0.28979 0.42072 0.03858  0.11826  0.02901  136 GLN A O   
1140 C  CB  A GLN A 137 ? 0.38813 0.33840 0.58521 0.06357  0.16237  0.04450  136 GLN A CB  
1141 C  CB  B GLN A 137 ? 0.38065 0.33217 0.57668 0.06265  0.16179  0.04492  136 GLN A CB  
1142 C  CG  A GLN A 137 ? 0.45399 0.35643 0.62979 0.07482  0.21452  0.02488  136 GLN A CG  
1143 C  CG  B GLN A 137 ? 0.42151 0.39350 0.70407 0.07476  0.16535  0.06384  136 GLN A CG  
1144 C  CD  A GLN A 137 ? 0.59870 0.47700 0.80999 0.08902  0.23811  0.01958  136 GLN A CD  
1145 C  CD  B GLN A 137 ? 0.58265 0.49696 0.84566 0.09099  0.20328  0.04044  136 GLN A CD  
1146 O  OE1 A GLN A 137 ? 0.59712 0.51127 0.90017 0.09585  0.23289  0.04627  136 GLN A OE1 
1147 O  OE1 B GLN A 137 ? 0.64995 0.53777 0.87190 0.08868  0.18723  0.02737  136 GLN A OE1 
1148 N  NE2 A GLN A 137 ? 0.67087 0.48884 0.79683 0.08210  0.25233  -0.01018 136 GLN A NE2 
1149 N  NE2 B GLN A 137 ? 0.63118 0.52459 0.90677 0.09453  0.24690  0.03480  136 GLN A NE2 
1150 N  N   . ARG A 138 ? 0.40986 0.27959 0.39593 0.05206  0.14049  0.00281  137 ARG A N   
1151 C  CA  . ARG A 138 ? 0.46352 0.31014 0.39353 0.04696  0.14012  0.00252  137 ARG A CA  
1152 C  C   . ARG A 138 ? 0.43288 0.27598 0.37970 0.04151  0.17200  0.00856  137 ARG A C   
1153 O  O   . ARG A 138 ? 0.50325 0.33899 0.47110 0.04376  0.20761  0.00391  137 ARG A O   
1154 C  CB  . ARG A 138 ? 0.55213 0.35846 0.40412 0.04307  0.13851  -0.00774 137 ARG A CB  
1155 C  CG  . ARG A 138 ? 0.70768 0.48830 0.50311 0.03718  0.13371  0.00147  137 ARG A CG  
1156 C  CD  . ARG A 138 ? 0.77768 0.53051 0.49779 0.02631  0.11707  0.00156  137 ARG A CD  
1157 N  NE  . ARG A 138 ? 0.88283 0.60951 0.54994 0.01862  0.10967  0.01918  137 ARG A NE  
1158 C  CZ  . ARG A 138 ? 0.95774 0.67217 0.56848 0.00763  0.08010  0.03461  137 ARG A CZ  
1159 N  NH1 . ARG A 138 ? 0.96404 0.69273 0.56324 0.00044  0.05655  0.03081  137 ARG A NH1 
1160 N  NH2 . ARG A 138 ? 0.94400 0.63440 0.51274 0.00071  0.07045  0.05872  137 ARG A NH2 
1161 N  N   . LEU A 139 ? 0.45614 0.29983 0.39386 0.03323  0.16474  0.01791  138 LEU A N   
1162 C  CA  . LEU A 139 ? 0.43293 0.27949 0.38965 0.02182  0.19129  0.02667  138 LEU A CA  
1163 C  C   . LEU A 139 ? 0.53300 0.32985 0.41329 0.01481  0.20586  0.02471  138 LEU A C   
1164 O  O   . LEU A 139 ? 0.60559 0.37506 0.43428 0.01701  0.18234  0.02730  138 LEU A O   
1165 C  CB  . LEU A 139 ? 0.41889 0.29388 0.41062 0.00628  0.17325  0.03970  138 LEU A CB  
1166 C  CG  . LEU A 139 ? 0.35481 0.27798 0.40586 0.00272  0.14906  0.04736  138 LEU A CG  
1167 C  CD1 . LEU A 139 ? 0.38893 0.32783 0.44619 -0.02610 0.13109  0.05683  138 LEU A CD1 
1168 C  CD2 . LEU A 139 ? 0.37498 0.33729 0.50624 0.01016  0.16753  0.06018  138 LEU A CD2 
1169 N  N   . THR A 140 ? 0.57476 0.36187 0.45336 0.00559  0.24557  0.02432  139 THR A N   
1170 C  CA  . THR A 140 ? 0.68160 0.42381 0.48726 -0.00972 0.25754  0.02900  139 THR A CA  
1171 C  C   . THR A 140 ? 0.70077 0.44357 0.51542 -0.02012 0.24101  0.04429  139 THR A C   
1172 O  O   . THR A 140 ? 0.64923 0.42991 0.52423 -0.02298 0.22792  0.04869  139 THR A O   
1173 C  CB  . THR A 140 ? 0.73214 0.46439 0.53330 -0.02270 0.31114  0.02360  139 THR A CB  
1174 O  OG1 . THR A 140 ? 0.68247 0.46574 0.57598 -0.02656 0.32554  0.03463  139 THR A OG1 
1175 C  CG2 . THR A 140 ? 0.77166 0.49419 0.57124 -0.01477 0.32933  0.00187  139 THR A CG2 
1176 N  N   . TRP A 141 ? 0.54228 0.45434 0.49318 0.07872  0.24334  0.05536  140 TRP A N   
1177 C  CA  . TRP A 141 ? 0.57005 0.50586 0.56960 0.06317  0.24473  0.06940  140 TRP A CA  
1178 C  C   . TRP A 141 ? 0.56010 0.53331 0.65107 0.05794  0.26050  0.08073  140 TRP A C   
1179 O  O   . TRP A 141 ? 0.47426 0.47636 0.62486 0.04110  0.24035  0.08282  140 TRP A O   
1180 C  CB  . TRP A 141 ? 0.58527 0.49162 0.53648 0.06898  0.26473  0.08143  140 TRP A CB  
1181 C  CG  . TRP A 141 ? 0.56121 0.48046 0.54836 0.05309  0.26103  0.09439  140 TRP A CG  
1182 C  CD1 . TRP A 141 ? 0.56929 0.49566 0.59933 0.04969  0.27888  0.11062  140 TRP A CD1 
1183 C  CD2 . TRP A 141 ? 0.55592 0.47816 0.53900 0.03941  0.22866  0.08844  140 TRP A CD2 
1184 N  NE1 . TRP A 141 ? 0.59521 0.52708 0.64752 0.03462  0.26656  0.11703  140 TRP A NE1 
1185 C  CE2 . TRP A 141 ? 0.58936 0.51805 0.61182 0.02877  0.23792  0.10406  140 TRP A CE2 
1186 C  CE3 . TRP A 141 ? 0.53793 0.45823 0.49311 0.03543  0.19118  0.07130  140 TRP A CE3 
1187 C  CZ2 . TRP A 141 ? 0.53761 0.46748 0.56617 0.01629  0.20958  0.10013  140 TRP A CZ2 
1188 C  CZ3 . TRP A 141 ? 0.52877 0.45443 0.49255 0.02381  0.16708  0.06935  140 TRP A CZ3 
1189 C  CH2 . TRP A 141 ? 0.56573 0.49451 0.56290 0.01533  0.17579  0.08227  140 TRP A CH2 
1190 N  N   . GLN A 142 ? 0.55711 0.52528 0.65674 0.07127  0.28303  0.08502  141 GLN A N   
1191 C  CA  . GLN A 142 ? 0.54309 0.54343 0.73017 0.06643  0.28957  0.09521  141 GLN A CA  
1192 C  C   . GLN A 142 ? 0.48769 0.51903 0.72895 0.06065  0.26554  0.08627  141 GLN A C   
1193 O  O   . GLN A 142 ? 0.47915 0.54123 0.79342 0.04706  0.24860  0.09105  141 GLN A O   
1194 C  CB  . GLN A 142 ? 0.64783 0.63288 0.82692 0.08404  0.32270  0.10323  141 GLN A CB  
1195 C  CG  . GLN A 142 ? 0.75231 0.75343 0.99674 0.07949  0.34142  0.12273  141 GLN A CG  
1196 C  CD  . GLN A 142 ? 0.77865 0.81822 1.11900 0.07166  0.33021  0.12570  141 GLN A CD  
1197 O  OE1 . GLN A 142 ? 0.77625 0.82261 1.12923 0.08084  0.33045  0.11929  141 GLN A OE1 
1198 N  NE2 . GLN A 142 ? 0.77118 0.83336 1.17927 0.05519  0.31736  0.13486  141 GLN A NE2 
1199 N  N   . GLU A 143 ? 0.48838 0.50849 0.69341 0.07173  0.26042  0.07278  142 GLU A N   
1200 C  CA  . GLU A 143 ? 0.42971 0.47376 0.67833 0.06808  0.23380  0.06504  142 GLU A CA  
1201 C  C   . GLU A 143 ? 0.38673 0.44421 0.64262 0.04787  0.19131  0.06010  142 GLU A C   
1202 O  O   . GLU A 143 ? 0.33551 0.41491 0.63442 0.04172  0.16474  0.05778  142 GLU A O   
1203 C  CB  . GLU A 143 ? 0.47127 0.48684 0.66299 0.08200  0.22765  0.05035  142 GLU A CB  
1204 C  CG  . GLU A 143 ? 0.48986 0.48855 0.67279 0.10480  0.26364  0.05091  142 GLU A CG  
1205 C  CD  . GLU A 143 ? 0.57031 0.52873 0.68313 0.11999  0.25825  0.03336  142 GLU A CD  
1206 O  OE1 . GLU A 143 ? 0.55058 0.48858 0.60932 0.11096  0.22931  0.02318  142 GLU A OE1 
1207 O  OE2 . GLU A 143 ? 0.64474 0.59030 0.75686 0.13716  0.27418  0.02955  142 GLU A OE2 
1208 N  N   . ALA A 144 ? 0.34037 0.38244 0.55113 0.03976  0.18448  0.05849  143 ALA A N   
1209 C  CA  . ALA A 144 ? 0.29548 0.34589 0.50417 0.02445  0.14795  0.05216  143 ALA A CA  
1210 C  C   . ALA A 144 ? 0.28878 0.36799 0.56964 0.01208  0.13436  0.05788  143 ALA A C   
1211 O  O   . ALA A 144 ? 0.27806 0.36752 0.56753 0.00424  0.10129  0.05079  143 ALA A O   
1212 C  CB  . ALA A 144 ? 0.38412 0.41180 0.53556 0.02097  0.14658  0.05018  143 ALA A CB  
1213 N  N   . GLY A 145 ? 0.26695 0.35698 0.59894 0.01058  0.15846  0.07098  144 GLY A N   
1214 C  CA  . GLY A 145 ? 0.27001 0.38432 0.67730 -0.00298 0.14206  0.07611  144 GLY A CA  
1215 C  C   . GLY A 145 ? 0.25873 0.36170 0.64672 -0.01593 0.12397  0.07243  144 GLY A C   
1216 O  O   . GLY A 145 ? 0.30224 0.38309 0.62151 -0.01426 0.12062  0.06558  144 GLY A O   
1217 N  N   . GLU A 146 ? 0.28217 0.40010 0.73789 -0.02875 0.10965  0.07655  145 GLU A N   
1218 C  CA  . GLU A 146 ? 0.30756 0.41110 0.75637 -0.04022 0.09894  0.07541  145 GLU A CA  
1219 C  C   . GLU A 146 ? 0.28733 0.37510 0.67182 -0.04093 0.06650  0.05700  145 GLU A C   
1220 O  O   . GLU A 146 ? 0.27308 0.33991 0.61017 -0.04103 0.07049  0.05510  145 GLU A O   
1221 C  CB  . GLU A 146 ? 0.30493 0.42024 0.83235 -0.05192 0.08107  0.07916  145 GLU A CB  
1222 C  CG  . GLU A 146 ? 0.47647 0.57758 1.01853 -0.05538 0.10371  0.09346  145 GLU A CG  
1223 C  CD  . GLU A 146 ? 0.60013 0.70253 1.20225 -0.06738 0.07520  0.09176  145 GLU A CD  
1224 O  OE1 . GLU A 146 ? 0.64829 0.73422 1.23875 -0.07695 0.05578  0.08413  145 GLU A OE1 
1225 O  OE2 . GLU A 146 ? 0.67608 0.79309 1.33745 -0.06647 0.07145  0.09775  145 GLU A OE2 
1226 N  N   . ARG A 147 ? 0.27522 0.37212 0.65665 -0.03977 0.03582  0.04494  146 ARG A N   
1227 C  CA  . ARG A 147 ? 0.25472 0.33754 0.57836 -0.03898 0.00942  0.02971  146 ARG A CA  
1228 C  C   . ARG A 147 ? 0.23126 0.29980 0.48535 -0.03069 0.02582  0.02860  146 ARG A C   
1229 O  O   . ARG A 147 ? 0.25258 0.30591 0.46811 -0.03096 0.02155  0.02306  146 ARG A O   
1230 C  CB  . ARG A 147 ? 0.24717 0.33952 0.57246 -0.03653 -0.02196 0.02072  146 ARG A CB  
1231 C  CG  . ARG A 147 ? 0.23034 0.30761 0.49557 -0.03350 -0.04550 0.00682  146 ARG A CG  
1232 C  CD  . ARG A 147 ? 0.23674 0.31912 0.49817 -0.02935 -0.07583 0.00090  146 ARG A CD  
1233 N  NE  . ARG A 147 ? 0.23292 0.32680 0.49231 -0.02241 -0.06562 0.00924  146 ARG A NE  
1234 C  CZ  . ARG A 147 ? 0.21402 0.30226 0.42327 -0.01579 -0.05459 0.01080  146 ARG A CZ  
1235 N  NH1 . ARG A 147 ? 0.24294 0.31879 0.40225 -0.01437 -0.04987 0.00605  146 ARG A NH1 
1236 N  NH2 . ARG A 147 ? 0.24126 0.33652 0.45661 -0.01029 -0.04825 0.01798  146 ARG A NH2 
1237 N  N   . LEU A 148 ? 0.20391 0.27596 0.44441 -0.02263 0.04216  0.03301  147 LEU A N   
1238 C  CA  . LEU A 148 ? 0.21432 0.27117 0.39436 -0.01583 0.05112  0.03061  147 LEU A CA  
1239 C  C   . LEU A 148 ? 0.27530 0.31428 0.43292 -0.01436 0.07317  0.03705  147 LEU A C   
1240 O  O   . LEU A 148 ? 0.26639 0.29063 0.37762 -0.01171 0.06995  0.03322  147 LEU A O   
1241 C  CB  . LEU A 148 ? 0.23756 0.29678 0.40907 -0.00743 0.05887  0.03163  147 LEU A CB  
1242 C  CG  . LEU A 148 ? 0.24212 0.31314 0.42086 -0.00724 0.03547  0.02717  147 LEU A CG  
1243 C  CD1 . LEU A 148 ? 0.25188 0.32408 0.43669 0.00124  0.04439  0.03008  147 LEU A CD1 
1244 C  CD2 . LEU A 148 ? 0.24170 0.30669 0.37779 -0.00831 0.01852  0.02083  147 LEU A CD2 
1245 N  N   . ARG A 149 ? 0.26019 0.30005 0.45131 -0.01511 0.09604  0.04871  148 ARG A N   
1246 C  CA  . ARG A 149 ? 0.31296 0.33186 0.47859 -0.01291 0.11802  0.05824  148 ARG A CA  
1247 C  C   . ARG A 149 ? 0.32980 0.33878 0.48698 -0.02032 0.10118  0.05477  148 ARG A C   
1248 O  O   . ARG A 149 ? 0.34855 0.33658 0.46036 -0.01604 0.10531  0.05647  148 ARG A O   
1249 C  CB  . ARG A 149 ? 0.31852 0.34206 0.52959 -0.01277 0.14969  0.07537  148 ARG A CB  
1250 C  CG  . ARG A 149 ? 0.37928 0.39851 0.57219 0.00169  0.17886  0.08048  148 ARG A CG  
1251 C  CD  . ARG A 149 ? 0.46883 0.48793 0.69492 0.00556  0.22017  0.10102  148 ARG A CD  
1252 N  NE  . ARG A 149 ? 0.44027 0.48770 0.75471 -0.00412 0.21388  0.10662  148 ARG A NE  
1253 C  CZ  . ARG A 149 ? 0.46370 0.52885 0.82006 0.00199  0.21836  0.10730  148 ARG A CZ  
1254 N  NH1 . ARG A 149 ? 0.38530 0.47191 0.81879 -0.00662 0.20628  0.11197  148 ARG A NH1 
1255 N  NH2 . ARG A 149 ? 0.47354 0.53155 0.79420 0.01736  0.23296  0.10289  148 ARG A NH2 
1256 N  N   . ALA A 150 ? 0.33945 0.36021 0.53869 -0.02998 0.07991  0.04898  149 ALA A N   
1257 C  CA  . ALA A 150 ? 0.29498 0.30230 0.48505 -0.03485 0.06307  0.04280  149 ALA A CA  
1258 C  C   . ALA A 150 ? 0.30465 0.30447 0.43844 -0.02772 0.04944  0.03117  149 ALA A C   
1259 O  O   . ALA A 150 ? 0.31427 0.29737 0.42307 -0.02566 0.04797  0.03071  149 ALA A O   
1260 C  CB  . ALA A 150 ? 0.26646 0.28293 0.50625 -0.04457 0.03814  0.03475  149 ALA A CB  
1261 N  N   . ILE A 151 ? 0.26449 0.27717 0.38387 -0.02382 0.03929  0.02331  150 ILE A N   
1262 C  CA  . ILE A 151 ? 0.24085 0.25042 0.31770 -0.01773 0.03011  0.01585  150 ILE A CA  
1263 C  C   . ILE A 151 ? 0.27920 0.27485 0.32201 -0.01196 0.04326  0.02211  150 ILE A C   
1264 O  O   . ILE A 151 ? 0.29970 0.28601 0.31877 -0.00843 0.03759  0.01997  150 ILE A O   
1265 C  CB  . ILE A 151 ? 0.25402 0.27903 0.32725 -0.01555 0.02042  0.01103  150 ILE A CB  
1266 C  CG1 . ILE A 151 ? 0.25785 0.29065 0.35333 -0.01891 0.00181  0.00390  150 ILE A CG1 
1267 C  CG2 . ILE A 151 ? 0.24409 0.26901 0.28275 -0.01010 0.01628  0.00802  150 ILE A CG2 
1268 C  CD1 . ILE A 151 ? 0.26790 0.31413 0.36494 -0.01649 -0.00615 0.00389  150 ILE A CD1 
1269 N  N   . LEU A 152 ? 0.27849 0.27090 0.31626 -0.00894 0.05917  0.02890  151 LEU A N   
1270 C  CA  . LEU A 152 ? 0.29045 0.26274 0.28566 -0.00143 0.06721  0.03259  151 LEU A CA  
1271 C  C   . LEU A 152 ? 0.34391 0.29617 0.32551 -0.00042 0.07345  0.04034  151 LEU A C   
1272 O  O   . LEU A 152 ? 0.35837 0.29530 0.30523 0.00509  0.06571  0.03989  151 LEU A O   
1273 C  CB  . LEU A 152 ? 0.31801 0.28367 0.30454 0.00453  0.08588  0.03715  151 LEU A CB  
1274 C  CG  . LEU A 152 ? 0.30446 0.28221 0.29715 0.00618  0.07953  0.03025  151 LEU A CG  
1275 C  CD1 . LEU A 152 ? 0.33679 0.30423 0.32362 0.01491  0.10261  0.03453  151 LEU A CD1 
1276 C  CD2 . LEU A 152 ? 0.34952 0.32183 0.31282 0.00787  0.06086  0.02270  151 LEU A CD2 
1277 N  N   . GLY A 153 ? 0.33983 0.29151 0.35313 -0.00591 0.08571  0.04881  152 GLY A N   
1278 C  CA  . GLY A 153 ? 0.34352 0.27399 0.34921 -0.00604 0.09198  0.05880  152 GLY A CA  
1279 C  C   . GLY A 153 ? 0.37973 0.30670 0.37936 -0.00629 0.06998  0.05008  152 GLY A C   
1280 O  O   . GLY A 153 ? 0.40487 0.31152 0.37464 -0.00028 0.06793  0.05497  152 GLY A O   
1281 N  N   . HIS A 154 ? 0.31814 0.26296 0.34203 -0.01076 0.05314  0.03699  153 HIS A N   
1282 C  CA  . HIS A 154 ? 0.33248 0.27253 0.34943 -0.00770 0.03683  0.02812  153 HIS A CA  
1283 C  C   . HIS A 154 ? 0.33606 0.27933 0.32172 0.00100  0.02930  0.02447  153 HIS A C   
1284 O  O   . HIS A 154 ? 0.35017 0.28348 0.32507 0.00703  0.02207  0.02398  153 HIS A O   
1285 C  CB  . HIS A 154 ? 0.34826 0.30049 0.38980 -0.01177 0.02230  0.01448  153 HIS A CB  
1286 C  CG  . HIS A 154 ? 0.31299 0.25530 0.34685 -0.00608 0.00962  0.00423  153 HIS A CG  
1287 N  ND1 . HIS A 154 ? 0.37097 0.32488 0.39041 0.00125  0.00061  -0.00765 153 HIS A ND1 
1288 C  CD2 . HIS A 154 ? 0.39269 0.31297 0.43003 -0.00453 0.00710  0.00522  153 HIS A CD2 
1289 C  CE1 . HIS A 154 ? 0.40979 0.35007 0.42422 0.00836  -0.00582 -0.01533 153 HIS A CE1 
1290 N  NE2 . HIS A 154 ? 0.39493 0.31389 0.42070 0.00477  -0.00396 -0.00853 153 HIS A NE2 
1291 N  N   . GLU A 155 ? 0.30450 0.26188 0.28209 0.00160  0.02931  0.02227  154 GLU A N   
1292 C  CA  . GLU A 155 ? 0.31727 0.27652 0.27364 0.00754  0.02097  0.02100  154 GLU A CA  
1293 C  C   . GLU A 155 ? 0.35788 0.29260 0.28595 0.01373  0.02003  0.02878  154 GLU A C   
1294 O  O   . GLU A 155 ? 0.35286 0.28615 0.27509 0.01930  0.00679  0.02768  154 GLU A O   
1295 C  CB  . GLU A 155 ? 0.33175 0.30077 0.28429 0.00595  0.02242  0.01970  154 GLU A CB  
1296 C  CG  . GLU A 155 ? 0.28321 0.27545 0.25570 0.00271  0.01769  0.01371  154 GLU A CG  
1297 C  CD  . GLU A 155 ? 0.32376 0.32175 0.29501 0.00124  0.01886  0.01415  154 GLU A CD  
1298 O  OE1 . GLU A 155 ? 0.36520 0.34776 0.31783 0.00379  0.02269  0.01634  154 GLU A OE1 
1299 O  OE2 . GLU A 155 ? 0.31155 0.32577 0.29649 -0.00093 0.01557  0.01205  154 GLU A OE2 
1300 N  N   . GLN A 156 ? 0.36589 0.28033 0.27699 0.01418  0.03455  0.03826  155 GLN A N   
1301 C  CA  . GLN A 156 ? 0.41570 0.30063 0.28749 0.02244  0.03344  0.04721  155 GLN A CA  
1302 C  C   . GLN A 156 ? 0.45777 0.33111 0.33510 0.02501  0.02658  0.05188  155 GLN A C   
1303 O  O   . GLN A 156 ? 0.60190 0.45331 0.44880 0.03355  0.01682  0.05797  155 GLN A O   
1304 C  CB  . GLN A 156 ? 0.54990 0.41339 0.39688 0.02485  0.05689  0.05888  155 GLN A CB  
1305 C  CG  . GLN A 156 ? 0.73825 0.56625 0.52430 0.03708  0.05416  0.06590  155 GLN A CG  
1306 C  CD  . GLN A 156 ? 0.80517 0.60585 0.56319 0.04214  0.08344  0.08314  155 GLN A CD  
1307 O  OE1 . GLN A 156 ? 0.80966 0.61970 0.60598 0.03441  0.10437  0.09233  155 GLN A OE1 
1308 N  NE2 . GLN A 156 ? 0.78105 0.54585 0.47197 0.05576  0.08478  0.08840  155 GLN A NE2 
1309 N  N   . GLU A 157 ? 0.36801 0.25224 0.28161 0.01911  0.02826  0.04812  156 GLU A N   
1310 C  CA  . GLU A 157 ? 0.41705 0.28739 0.33811 0.02285  0.02080  0.05026  156 GLU A CA  
1311 C  C   . GLU A 157 ? 0.40342 0.28785 0.33289 0.03019  0.00281  0.03992  156 GLU A C   
1312 O  O   . GLU A 157 ? 0.46087 0.33103 0.39082 0.03777  -0.00543 0.04279  156 GLU A O   
1313 C  CB  . GLU A 157 ? 0.43833 0.30810 0.39442 0.01437  0.02711  0.04819  156 GLU A CB  
1314 C  CG  . GLU A 157 ? 0.51893 0.37926 0.48323 0.00618  0.04733  0.06174  156 GLU A CG  
1315 C  CD  . GLU A 157 ? 0.57422 0.43008 0.58222 -0.00395 0.04905  0.06196  156 GLU A CD  
1316 O  OE1 . GLU A 157 ? 0.46823 0.31878 0.48991 -0.00275 0.03352  0.05089  156 GLU A OE1 
1317 O  OE2 . GLU A 157 ? 0.57176 0.42843 0.60312 -0.01251 0.06595  0.07310  156 GLU A OE2 
1318 N  N   . ILE A 158 ? 0.39577 0.30751 0.33562 0.02892  -0.00145 0.03007  157 ILE A N   
1319 C  CA  . ILE A 158 ? 0.35619 0.28684 0.31385 0.03564  -0.01145 0.02230  157 ILE A CA  
1320 C  C   . ILE A 158 ? 0.37796 0.31866 0.33211 0.03917  -0.02345 0.02485  157 ILE A C   
1321 O  O   . ILE A 158 ? 0.38122 0.34480 0.35981 0.04316  -0.02838 0.02101  157 ILE A O   
1322 C  CB  . ILE A 158 ? 0.33061 0.28327 0.30654 0.03279  -0.00598 0.01105  157 ILE A CB  
1323 C  CG1 . ILE A 158 ? 0.33660 0.30502 0.30994 0.02478  -0.00181 0.01080  157 ILE A CG1 
1324 C  CG2 . ILE A 158 ? 0.39167 0.32958 0.37425 0.03024  -0.00242 0.00536  157 ILE A CG2 
1325 C  CD1 . ILE A 158 ? 0.36725 0.35319 0.35102 0.02322  0.00157  0.00204  157 ILE A CD1 
1326 N  N   . GLY A 159 ? 0.38108 0.30321 0.30603 0.03874  -0.02863 0.03149  158 GLY A N   
1327 C  CA  . GLY A 159 ? 0.38623 0.31272 0.30976 0.04200  -0.04755 0.03176  158 GLY A CA  
1328 C  C   . GLY A 159 ? 0.41519 0.33699 0.31765 0.03726  -0.05066 0.02984  158 GLY A C   
1329 O  O   . GLY A 159 ? 0.45532 0.36660 0.34524 0.04060  -0.07169 0.02987  158 GLY A O   
1330 N  N   . PHE A 160 ? 0.34618 0.27511 0.24804 0.03018  -0.03342 0.02690  159 PHE A N   
1331 C  CA  . PHE A 160 ? 0.40589 0.32685 0.28729 0.02771  -0.03467 0.02418  159 PHE A CA  
1332 C  C   . PHE A 160 ? 0.49968 0.38228 0.32838 0.03455  -0.03086 0.02907  159 PHE A C   
1333 O  O   . PHE A 160 ? 0.53896 0.40623 0.35398 0.03764  -0.01867 0.03721  159 PHE A O   
1334 C  CB  . PHE A 160 ? 0.36669 0.30700 0.26682 0.02016  -0.01801 0.02080  159 PHE A CB  
1335 C  CG  . PHE A 160 ? 0.34151 0.31424 0.28136 0.01594  -0.01918 0.01793  159 PHE A CG  
1336 C  CD1 . PHE A 160 ? 0.33453 0.31902 0.29133 0.01635  -0.01097 0.01687  159 PHE A CD1 
1337 C  CD2 . PHE A 160 ? 0.36274 0.35032 0.32014 0.01260  -0.02800 0.01681  159 PHE A CD2 
1338 C  CE1 . PHE A 160 ? 0.35867 0.36797 0.34009 0.01617  -0.00917 0.01439  159 PHE A CE1 
1339 C  CE2 . PHE A 160 ? 0.37258 0.38792 0.36165 0.01034  -0.02380 0.01783  159 PHE A CE2 
1340 C  CZ  . PHE A 160 ? 0.35017 0.37599 0.34692 0.01344  -0.01322 0.01652  159 PHE A CZ  
1341 N  N   . ALA A 161 ? 0.45798 0.32094 0.25456 0.03830  -0.04297 0.02476  160 ALA A N   
1342 C  CA  . ALA A 161 ? 0.51503 0.33712 0.24937 0.04800  -0.03549 0.02816  160 ALA A CA  
1343 C  C   . ALA A 161 ? 0.53128 0.35555 0.26231 0.04606  -0.00991 0.02589  160 ALA A C   
1344 O  O   . ALA A 161 ? 0.51369 0.35351 0.26614 0.04091  -0.01534 0.01714  160 ALA A O   
1345 C  CB  . ALA A 161 ? 0.55035 0.34215 0.24308 0.05623  -0.06703 0.02173  160 ALA A CB  
1346 N  N   . ALA A 162 ? 0.61161 0.42233 0.32371 0.05001  0.01901  0.03579  161 ALA A N   
1347 C  CA  . ALA A 162 ? 0.55952 0.37500 0.27735 0.04986  0.04616  0.03581  161 ALA A CA  
1348 C  C   . ALA A 162 ? 0.57383 0.37092 0.25862 0.05702  0.03800  0.02381  161 ALA A C   
1349 O  O   . ALA A 162 ? 0.58726 0.40371 0.30274 0.05235  0.04360  0.01762  161 ALA A O   
1350 C  CB  . ALA A 162 ? 0.61573 0.41031 0.30878 0.05686  0.07910  0.05114  161 ALA A CB  
1351 N  N   . ASP A 163 ? 0.62543 0.38164 0.24628 0.06908  0.02131  0.01965  162 ASP A N   
1352 C  CA  . ASP A 163 ? 0.64589 0.37291 0.22459 0.07816  0.00926  0.00537  162 ASP A CA  
1353 C  C   . ASP A 163 ? 0.63225 0.38131 0.25561 0.06683  -0.02031 -0.00726 162 ASP A C   
1354 O  O   . ASP A 163 ? 0.71854 0.44406 0.31738 0.07209  -0.03259 -0.02025 162 ASP A O   
1355 C  CB  . ASP A 163 ? 0.83431 0.50798 0.33030 0.09394  -0.01029 0.00245  162 ASP A CB  
1356 C  CG  . ASP A 163 ? 1.08961 0.73293 0.53259 0.10918  0.02509  0.01358  162 ASP A CG  
1357 O  OD1 . ASP A 163 ? 1.12652 0.78679 0.59261 0.10857  0.06502  0.02240  162 ASP A OD1 
1358 O  OD2 . ASP A 163 ? 1.17438 0.78434 0.57125 0.11994  0.01286  0.01430  162 ASP A OD2 
1359 N  N   . SER A 164 ? 0.59739 0.38765 0.28381 0.05260  -0.03055 -0.00329 163 SER A N   
1360 C  CA  . SER A 164 ? 0.51617 0.32938 0.24923 0.04170  -0.05356 -0.01026 163 SER A CA  
1361 C  C   . SER A 164 ? 0.44626 0.29918 0.23475 0.03135  -0.03531 -0.00664 163 SER A C   
1362 O  O   . SER A 164 ? 0.42163 0.29280 0.24744 0.02283  -0.04891 -0.00905 163 SER A O   
1363 C  CB  . SER A 164 ? 0.52214 0.35105 0.28462 0.03590  -0.08075 -0.00747 163 SER A CB  
1364 O  OG  . SER A 164 ? 0.64239 0.50454 0.44260 0.03060  -0.06485 0.00234  163 SER A OG  
1365 N  N   . ARG A 165 ? 0.39989 0.26479 0.19586 0.03195  -0.00655 0.00014  164 ARG A N   
1366 C  CA  . ARG A 165 ? 0.36499 0.26545 0.21067 0.02316  0.00572  0.00359  164 ARG A CA  
1367 C  C   . ARG A 165 ? 0.41536 0.31153 0.25959 0.02792  0.02802  0.00333  164 ARG A C   
1368 O  O   . ARG A 165 ? 0.48205 0.35318 0.29064 0.03837  0.04522  0.00440  164 ARG A O   
1369 C  CB  . ARG A 165 ? 0.36120 0.28298 0.23079 0.01852  0.01487  0.01118  164 ARG A CB  
1370 C  CG  . ARG A 165 ? 0.39786 0.32797 0.27671 0.01609  -0.00237 0.01228  164 ARG A CG  
1371 C  CD  . ARG A 165 ? 0.34075 0.29729 0.25589 0.00922  -0.01435 0.01073  164 ARG A CD  
1372 N  NE  . ARG A 165 ? 0.29952 0.28219 0.24396 0.00446  -0.00342 0.01282  164 ARG A NE  
1373 C  CZ  . ARG A 165 ? 0.26861 0.27382 0.23901 0.00055  -0.00756 0.01449  164 ARG A CZ  
1374 N  NH1 . ARG A 165 ? 0.27469 0.28425 0.25766 -0.00133 -0.02035 0.01618  164 ARG A NH1 
1375 N  NH2 . ARG A 165 ? 0.30725 0.32913 0.29135 -0.00104 0.00040  0.01543  164 ARG A NH2 
1376 N  N   . CYS A 166 ? 0.36238 0.28377 0.24678 0.02165  0.02983  0.00388  165 CYS A N   
1377 C  CA  . CYS A 166 ? 0.39511 0.31966 0.29299 0.02609  0.04979  0.00528  165 CYS A CA  
1378 C  C   . CYS A 166 ? 0.37676 0.33552 0.32426 0.01742  0.04850  0.00977  165 CYS A C   
1379 O  O   . CYS A 166 ? 0.32274 0.29726 0.28508 0.01000  0.03276  0.01020  165 CYS A O   
1380 C  CB  . CYS A 166 ? 0.45989 0.35983 0.33633 0.03467  0.04792  -0.00312 165 CYS A CB  
1381 S  SG  . CYS A 166 ? 0.46820 0.37573 0.36883 0.02580  0.02081  -0.00721 165 CYS A SG  
1382 N  N   . ALA A 167 ? 0.33964 0.30863 0.31237 0.01970  0.06535  0.01395  166 ALA A N   
1383 C  CA  . ALA A 167 ? 0.30391 0.29898 0.31979 0.01451  0.05989  0.01679  166 ALA A CA  
1384 C  C   . ALA A 167 ? 0.25494 0.24499 0.27740 0.02033  0.05920  0.01464  166 ALA A C   
1385 O  O   . ALA A 167 ? 0.31771 0.28536 0.31899 0.03046  0.07115  0.01061  166 ALA A O   
1386 C  CB  . ALA A 167 ? 0.30131 0.31182 0.35409 0.01317  0.07334  0.02290  166 ALA A CB  
1387 N  N   . MSE A 168 ? 0.25885 0.26522 0.30488 0.01558  0.04462  0.01717  167 MSE A N   
1388 C  CA  . MSE A 168 ? 0.25509 0.25635 0.31288 0.02095  0.04191  0.01726  167 MSE A CA  
1389 C  C   . MSE A 168 ? 0.26459 0.28855 0.36215 0.01972  0.03474  0.02390  167 MSE A C   
1390 O  O   . MSE A 168 ? 0.25852 0.29895 0.36432 0.01294  0.02380  0.02694  167 MSE A O   
1391 C  CB  . MSE A 168 ? 0.29736 0.28522 0.33674 0.01732  0.02593  0.01582  167 MSE A CB  
1392 C  CG  . MSE A 168 ? 0.29565 0.26137 0.29953 0.01702  0.02303  0.00862  167 MSE A CG  
1393 SE SE  . MSE A 168 ? 0.37771 0.33042 0.37959 0.00930  -0.00042 0.00883  167 MSE A SE  
1394 C  CE  . MSE A 168 ? 0.35456 0.27068 0.34711 0.02152  0.00103  -0.00109 167 MSE A CE  
1395 N  N   . ARG A 169 ? 0.25320 0.27455 0.37253 0.02797  0.03811  0.02529  168 ARG A N   
1396 C  CA  . ARG A 169 ? 0.25856 0.29919 0.41694 0.02855  0.02663  0.03231  168 ARG A CA  
1397 C  C   . ARG A 169 ? 0.28569 0.31458 0.44873 0.03480  0.01896  0.03528  168 ARG A C   
1398 O  O   . ARG A 169 ? 0.27522 0.28363 0.43061 0.04350  0.03034  0.02987  168 ARG A O   
1399 C  CB  . ARG A 169 ? 0.22278 0.28021 0.42705 0.03342  0.03968  0.03436  168 ARG A CB  
1400 C  CG  . ARG A 169 ? 0.22097 0.30011 0.47337 0.03364  0.02135  0.04104  168 ARG A CG  
1401 C  CD  . ARG A 169 ? 0.21977 0.31974 0.53323 0.03667  0.03376  0.04460  168 ARG A CD  
1402 N  NE  . ARG A 169 ? 0.25619 0.36304 0.57212 0.02725  0.04064  0.04361  168 ARG A NE  
1403 C  CZ  . ARG A 169 ? 0.30127 0.40468 0.62087 0.02981  0.07106  0.04507  168 ARG A CZ  
1404 N  NH1 . ARG A 169 ? 0.33833 0.43059 0.65417 0.04331  0.09886  0.04567  168 ARG A NH1 
1405 N  NH2 . ARG A 169 ? 0.29272 0.40059 0.61745 0.02029  0.07449  0.04647  168 ARG A NH2 
1406 N  N   A LEU A 170 ? 0.25801 0.29547 0.42866 0.03158  -0.00079 0.04388  169 LEU A N   
1407 N  N   B LEU A 170 ? 0.25667 0.29448 0.42809 0.03168  -0.00073 0.04389  169 LEU A N   
1408 C  CA  A LEU A 170 ? 0.24705 0.27516 0.43013 0.03775  -0.01056 0.05103  169 LEU A CA  
1409 C  CA  B LEU A 170 ? 0.24832 0.27668 0.43153 0.03771  -0.01059 0.05103  169 LEU A CA  
1410 C  C   A LEU A 170 ? 0.25451 0.30155 0.48016 0.04373  -0.02118 0.05719  169 LEU A C   
1411 C  C   B LEU A 170 ? 0.25532 0.30256 0.48130 0.04375  -0.02115 0.05717  169 LEU A C   
1412 O  O   A LEU A 170 ? 0.25832 0.31871 0.48319 0.03904  -0.03907 0.06222  169 LEU A O   
1413 O  O   B LEU A 170 ? 0.26090 0.32163 0.48651 0.03909  -0.03902 0.06214  169 LEU A O   
1414 C  CB  A LEU A 170 ? 0.25192 0.27243 0.40856 0.03046  -0.02459 0.06053  169 LEU A CB  
1415 C  CB  B LEU A 170 ? 0.25133 0.27242 0.40757 0.03024  -0.02453 0.06039  169 LEU A CB  
1416 C  CG  A LEU A 170 ? 0.27113 0.28022 0.43998 0.03589  -0.03652 0.07265  169 LEU A CG  
1417 C  CG  B LEU A 170 ? 0.33707 0.33853 0.49613 0.03335  -0.03180 0.06956  169 LEU A CG  
1418 C  CD1 A LEU A 170 ? 0.28765 0.27133 0.46194 0.04153  -0.02871 0.06674  169 LEU A CD1 
1419 C  CD1 B LEU A 170 ? 0.28404 0.28427 0.42038 0.02495  -0.04096 0.08405  169 LEU A CD1 
1420 C  CD2 A LEU A 170 ? 0.30186 0.30800 0.44549 0.02870  -0.04668 0.08740  169 LEU A CD2 
1421 C  CD2 B LEU A 170 ? 0.35470 0.35714 0.54710 0.04470  -0.03938 0.07532  169 LEU A CD2 
1422 N  N   . VAL A 171 ? 0.25483 0.30103 0.51737 0.05566  -0.01189 0.05630  170 VAL A N   
1423 C  CA  . VAL A 171 ? 0.25469 0.32140 0.57145 0.06266  -0.02313 0.06284  170 VAL A CA  
1424 C  C   . VAL A 171 ? 0.27189 0.32851 0.59042 0.06799  -0.04533 0.07384  170 VAL A C   
1425 O  O   . VAL A 171 ? 0.29063 0.32362 0.59708 0.07364  -0.03987 0.07463  170 VAL A O   
1426 C  CB  . VAL A 171 ? 0.29424 0.36785 0.65719 0.07518  0.00211  0.05880  170 VAL A CB  
1427 C  CG1 . VAL A 171 ? 0.28107 0.37815 0.71219 0.08300  -0.01238 0.06740  170 VAL A CG1 
1428 C  CG2 . VAL A 171 ? 0.26494 0.34816 0.62519 0.06953  0.02481  0.05257  170 VAL A CG2 
1429 N  N   . LEU A 172 ? 0.27528 0.34538 0.60635 0.06685  -0.07249 0.08246  171 LEU A N   
1430 C  CA  . LEU A 172 ? 0.29936 0.35803 0.62899 0.07364  -0.09549 0.09616  171 LEU A CA  
1431 C  C   . LEU A 172 ? 0.36547 0.43458 0.76186 0.08816  -0.09950 0.09922  171 LEU A C   
1432 O  O   . LEU A 172 ? 0.34882 0.44283 0.79260 0.09005  -0.11299 0.09945  171 LEU A O   
1433 C  CB  . LEU A 172 ? 0.35271 0.41402 0.65103 0.06879  -0.12456 0.10416  171 LEU A CB  
1434 C  CG  . LEU A 172 ? 0.40420 0.45775 0.64057 0.05705  -0.11687 0.10154  171 LEU A CG  
1435 C  CD1 . LEU A 172 ? 0.44097 0.48927 0.63502 0.05753  -0.14298 0.11057  171 LEU A CD1 
1436 C  CD2 . LEU A 172 ? 0.47362 0.50683 0.68371 0.05374  -0.09721 0.10498  171 LEU A CD2 
1437 N  N   . GLY A 173 ? 0.42064 0.47020 0.82574 0.09869  -0.08848 0.10105  172 GLY A N   
1438 C  CA  . GLY A 173 ? 0.43413 0.49137 0.90453 0.11587  -0.08619 0.10300  172 GLY A CA  
1439 C  C   . GLY A 173 ? 0.54057 0.60279 1.02635 0.11840  -0.11784 0.11408  172 GLY A C   
1440 O  O   . GLY A 173 ? 0.56623 0.64004 1.09926 0.12641  -0.11612 0.11261  172 GLY A O   
1441 N  N   . MSE B 2   ? 0.81560 1.04883 1.04602 0.21533  -0.21086 -0.00293 1   MSE B N   
1442 C  CA  . MSE B 2   ? 0.77384 1.10165 1.07760 0.20438  -0.20132 -0.03682 1   MSE B CA  
1443 C  C   . MSE B 2   ? 0.75563 1.12272 1.06588 0.16524  -0.19381 -0.04228 1   MSE B C   
1444 O  O   . MSE B 2   ? 0.76473 1.17469 1.11052 0.13572  -0.16593 -0.05856 1   MSE B O   
1445 C  CB  . MSE B 2   ? 0.80813 1.17765 1.14415 0.23320  -0.22773 -0.05499 1   MSE B CB  
1446 N  N   . ASP B 3   ? 0.67486 1.02127 0.94380 0.16218  -0.21709 -0.02890 2   ASP B N   
1447 C  CA  . ASP B 3   ? 0.57752 0.95283 0.84558 0.12599  -0.21433 -0.03659 2   ASP B CA  
1448 C  C   . ASP B 3   ? 0.55263 0.86555 0.75864 0.11149  -0.20715 -0.01391 2   ASP B C   
1449 O  O   . ASP B 3   ? 0.55311 0.79658 0.69801 0.12855  -0.21606 0.01282  2   ASP B O   
1450 C  CB  . ASP B 3   ? 0.60845 1.01057 0.87335 0.12971  -0.24479 -0.04409 2   ASP B CB  
1451 C  CG  . ASP B 3   ? 0.71748 1.20566 1.05700 0.12588  -0.24544 -0.07737 2   ASP B CG  
1452 O  OD1 . ASP B 3   ? 0.74444 1.27311 1.09724 0.10691  -0.25800 -0.09288 2   ASP B OD1 
1453 O  OD2 . ASP B 3   ? 0.71136 1.22671 1.09474 0.14006  -0.23168 -0.09012 2   ASP B OD2 
1454 N  N   . TYR B 4   ? 0.39499 0.71640 0.60509 0.07132  -0.18024 -0.02140 3   TYR B N   
1455 C  CA  . TYR B 4   ? 0.30724 0.55978 0.45801 0.04969  -0.15706 -0.00113 3   TYR B CA  
1456 C  C   . TYR B 4   ? 0.30583 0.56321 0.43930 0.01899  -0.15817 -0.01119 3   TYR B C   
1457 O  O   . TYR B 4   ? 0.31466 0.62907 0.48933 0.00281  -0.16660 -0.03492 3   TYR B O   
1458 C  CB  . TYR B 4   ? 0.28300 0.52097 0.44600 0.03431  -0.12093 0.00048  3   TYR B CB  
1459 C  CG  . TYR B 4   ? 0.27705 0.50264 0.45308 0.06084  -0.11578 0.00701  3   TYR B CG  
1460 C  CD1 . TYR B 4   ? 0.35134 0.51105 0.48077 0.07122  -0.11072 0.02986  3   TYR B CD1 
1461 C  CD2 . TYR B 4   ? 0.29654 0.57835 0.53278 0.07209  -0.11309 -0.01367 3   TYR B CD2 
1462 C  CE1 . TYR B 4   ? 0.35729 0.49762 0.49578 0.09205  -0.10641 0.03333  3   TYR B CE1 
1463 C  CE2 . TYR B 4   ? 0.33116 0.59640 0.57673 0.09756  -0.10839 -0.01186 3   TYR B CE2 
1464 C  CZ  . TYR B 4   ? 0.32470 0.51407 0.51919 0.10700  -0.10625 0.01236  3   TYR B CZ  
1465 O  OH  . TYR B 4   ? 0.39693 0.56259 0.59841 0.12986  -0.10265 0.01172  3   TYR B OH  
1466 N  N   . ARG B 5   ? 0.32586 0.52533 0.40085 0.00928  -0.14815 0.00310  4   ARG B N   
1467 C  CA  . ARG B 5   ? 0.35730 0.54767 0.41146 -0.01865 -0.14517 -0.00891 4   ARG B CA  
1468 C  C   . ARG B 5   ? 0.30197 0.44045 0.32801 -0.03225 -0.11585 -0.00067 4   ARG B C   
1469 O  O   . ARG B 5   ? 0.32597 0.43317 0.33108 -0.01807 -0.10425 0.01622  4   ARG B O   
1470 C  CB  . ARG B 5   ? 0.39796 0.57504 0.40340 -0.01075 -0.16966 -0.00778 4   ARG B CB  
1471 C  CG  . ARG B 5   ? 0.46456 0.68922 0.48816 0.00791  -0.20715 -0.01587 4   ARG B CG  
1472 C  CD  . ARG B 5   ? 0.62831 0.83501 0.59138 0.01134  -0.23083 -0.01575 4   ARG B CD  
1473 N  NE  . ARG B 5   ? 0.75740 1.01185 0.73808 0.02711  -0.26985 -0.02661 4   ARG B NE  
1474 C  CZ  . ARG B 5   ? 0.78776 1.09121 0.80827 0.00656  -0.28062 -0.05353 4   ARG B CZ  
1475 N  NH1 . ARG B 5   ? 0.76264 1.07561 0.80342 -0.02937 -0.26370 -0.07568 4   ARG B NH1 
1476 N  NH2 . ARG B 5   ? 0.85807 1.19600 0.89534 0.02016  -0.30721 -0.05817 4   ARG B NH2 
1477 N  N   . ILE B 6   ? 0.33329 0.46030 0.35799 -0.05965 -0.10570 -0.01378 5   ILE B N   
1478 C  CA  . ILE B 6   ? 0.32129 0.39293 0.31198 -0.06625 -0.08640 -0.00873 5   ILE B CA  
1479 C  C   . ILE B 6   ? 0.34887 0.39202 0.29748 -0.07009 -0.09588 -0.01935 5   ILE B C   
1480 O  O   . ILE B 6   ? 0.37820 0.43741 0.32931 -0.08572 -0.11126 -0.03612 5   ILE B O   
1481 C  CB  . ILE B 6   ? 0.32883 0.38842 0.33382 -0.09141 -0.06885 -0.01324 5   ILE B CB  
1482 C  CG1 . ILE B 6   ? 0.35600 0.42247 0.38028 -0.08118 -0.05219 -0.00042 5   ILE B CG1 
1483 C  CG2 . ILE B 6   ? 0.38675 0.38062 0.34681 -0.09940 -0.06212 -0.01512 5   ILE B CG2 
1484 C  CD1 . ILE B 6   ? 0.33950 0.46572 0.41239 -0.07102 -0.05640 -0.00276 5   ILE B CD1 
1485 N  N   . ARG B 7   ? 0.37264 0.38060 0.28581 -0.05563 -0.08684 -0.01366 6   ARG B N   
1486 C  CA  . ARG B 7   ? 0.41006 0.39464 0.28233 -0.05423 -0.09227 -0.02746 6   ARG B CA  
1487 C  C   . ARG B 7   ? 0.41908 0.36542 0.27069 -0.04287 -0.07625 -0.02957 6   ARG B C   
1488 O  O   . ARG B 7   ? 0.39364 0.33687 0.25951 -0.03389 -0.06335 -0.01732 6   ARG B O   
1489 C  CB  . ARG B 7   ? 0.42199 0.42715 0.26900 -0.04167 -0.10344 -0.02291 6   ARG B CB  
1490 C  CG  . ARG B 7   ? 0.40341 0.40970 0.24298 -0.02554 -0.09096 -0.00209 6   ARG B CG  
1491 C  CD  . ARG B 7   ? 0.45626 0.46246 0.24644 -0.01985 -0.09673 0.00031  6   ARG B CD  
1492 N  NE  . ARG B 7   ? 0.44587 0.44681 0.22155 -0.01199 -0.08456 0.02258  6   ARG B NE  
1493 C  CZ  . ARG B 7   ? 0.49019 0.48288 0.25522 -0.01237 -0.05966 0.02312  6   ARG B CZ  
1494 N  NH1 . ARG B 7   ? 0.45082 0.44151 0.22040 -0.01221 -0.04721 0.00203  6   ARG B NH1 
1495 N  NH2 . ARG B 7   ? 0.51680 0.50252 0.26748 -0.01272 -0.04840 0.04289  6   ARG B NH2 
1496 N  N   A THR B 8   ? 0.47586 0.39543 0.29521 -0.04115 -0.07952 -0.04939 7   THR B N   
1497 N  N   B THR B 8   ? 0.46775 0.38815 0.28691 -0.04090 -0.07952 -0.04925 7   THR B N   
1498 C  CA  A THR B 8   ? 0.45596 0.34982 0.25897 -0.02222 -0.06803 -0.05813 7   THR B CA  
1499 C  CA  B THR B 8   ? 0.46799 0.36237 0.26998 -0.02218 -0.06825 -0.05868 7   THR B CA  
1500 C  C   A THR B 8   ? 0.42381 0.35198 0.22697 -0.00774 -0.05459 -0.04913 7   THR B C   
1501 C  C   B THR B 8   ? 0.45011 0.37823 0.25221 -0.00744 -0.05449 -0.04982 7   THR B C   
1502 O  O   A THR B 8   ? 0.50457 0.45699 0.29131 -0.01096 -0.05633 -0.04412 7   THR B O   
1503 O  O   B THR B 8   ? 0.48024 0.43242 0.26503 -0.01042 -0.05587 -0.04538 7   THR B O   
1504 C  CB  A THR B 8   ? 0.52212 0.38423 0.29068 -0.01917 -0.07509 -0.08658 7   THR B CB  
1505 C  CB  B THR B 8   ? 0.52974 0.39429 0.29711 -0.02012 -0.07582 -0.08704 7   THR B CB  
1506 O  OG1 A THR B 8   ? 0.58274 0.47432 0.32829 -0.02074 -0.07927 -0.09471 7   THR B OG1 
1507 O  OG1 B THR B 8   ? 0.56107 0.38321 0.32458 -0.04008 -0.08730 -0.09518 7   THR B OG1 
1508 C  CG2 A THR B 8   ? 0.56082 0.38174 0.32476 -0.04164 -0.08785 -0.09511 7   THR B CG2 
1509 C  CG2 B THR B 8   ? 0.52582 0.37319 0.28151 0.00636  -0.06615 -0.10333 7   THR B CG2 
1510 N  N   . SER B 9   ? 0.44309 0.37063 0.26038 0.00624  -0.04206 -0.04754 8   SER B N   
1511 C  CA  . SER B 9   ? 0.38456 0.34626 0.20526 0.01300  -0.02564 -0.04278 8   SER B CA  
1512 C  C   . SER B 9   ? 0.44539 0.42012 0.23842 0.02027  -0.01696 -0.06656 8   SER B C   
1513 O  O   . SER B 9   ? 0.50539 0.45872 0.28452 0.03045  -0.02347 -0.09122 8   SER B O   
1514 C  CB  . SER B 9   ? 0.41364 0.38023 0.26301 0.02440  -0.01685 -0.04047 8   SER B CB  
1515 O  OG  . SER B 9   ? 0.39779 0.34880 0.26577 0.01784  -0.02349 -0.02274 8   SER B OG  
1516 N  N   . ARG B 10  ? 0.47996 0.48615 0.26063 0.01343  -0.00063 -0.06011 9   ARG B N   
1517 C  CA  . ARG B 10  ? 0.50025 0.52989 0.25218 0.01506  0.01541  -0.08254 9   ARG B CA  
1518 C  C   . ARG B 10  ? 0.44490 0.51562 0.21876 0.01483  0.04186  -0.08776 9   ARG B C   
1519 O  O   . ARG B 10  ? 0.42613 0.50238 0.22670 0.00810  0.04628  -0.06799 9   ARG B O   
1520 C  CB  . ARG B 10  ? 0.52535 0.55411 0.22565 -0.00160 0.01307  -0.07078 9   ARG B CB  
1521 C  CG  . ARG B 10  ? 0.52030 0.52180 0.20643 -0.00378 -0.01574 -0.06892 9   ARG B CG  
1522 C  CD  . ARG B 10  ? 0.70124 0.70401 0.33263 -0.01486 -0.02438 -0.06020 9   ARG B CD  
1523 N  NE  . ARG B 10  ? 0.86031 0.86018 0.48446 -0.02226 -0.02950 -0.02432 9   ARG B NE  
1524 C  CZ  . ARG B 10  ? 0.85247 0.84405 0.48677 -0.02116 -0.05714 -0.00790 9   ARG B CZ  
1525 N  NH1 . ARG B 10  ? 0.83148 0.82298 0.48633 -0.02038 -0.07852 -0.02416 9   ARG B NH1 
1526 N  NH2 . ARG B 10  ? 0.77229 0.75550 0.39667 -0.02118 -0.06368 0.02219  9   ARG B NH2 
1527 N  N   . ASP B 11  ? 0.51891 0.62350 0.28241 0.02017  0.06075  -0.11843 10  ASP B N   
1528 C  CA  . ASP B 11  ? 0.50124 0.66028 0.29568 0.01800  0.08793  -0.13275 10  ASP B CA  
1529 C  C   . ASP B 11  ? 0.53340 0.69959 0.31700 -0.01422 0.10528  -0.10095 10  ASP B C   
1530 O  O   . ASP B 11  ? 0.52739 0.71796 0.35082 -0.02009 0.11592  -0.09829 10  ASP B O   
1531 C  CB  . ASP B 11  ? 0.61885 0.81808 0.40383 0.02436  0.10808  -0.17030 10  ASP B CB  
1532 C  CG  . ASP B 11  ? 0.71953 0.97660 0.55796 0.02313  0.12956  -0.18538 10  ASP B CG  
1533 O  OD1 . ASP B 11  ? 0.79802 1.08254 0.62441 -0.00405 0.15540  -0.18036 10  ASP B OD1 
1534 O  OD2 . ASP B 11  ? 0.66701 0.93910 0.55734 0.04842  0.11735  -0.20106 10  ASP B OD2 
1535 N  N   . GLU B 12  ? 0.56450 0.70241 0.29063 -0.03434 0.10450  -0.07637 11  GLU B N   
1536 C  CA  . GLU B 12  ? 0.55840 0.68366 0.25990 -0.06347 0.11788  -0.04352 11  GLU B CA  
1537 C  C   . GLU B 12  ? 0.51765 0.61336 0.25329 -0.06050 0.10024  -0.01664 11  GLU B C   
1538 O  O   . GLU B 12  ? 0.56689 0.65022 0.29384 -0.08192 0.11222  0.00528  11  GLU B O   
1539 C  CB  . GLU B 12  ? 0.63198 0.71912 0.26065 -0.07574 0.11062  -0.02063 11  GLU B CB  
1540 C  CG  . GLU B 12  ? 0.75566 0.80348 0.36608 -0.06205 0.07321  -0.00458 11  GLU B CG  
1541 C  CD  . GLU B 12  ? 0.91682 0.93575 0.45903 -0.06730 0.06125  0.01181  11  GLU B CD  
1542 O  OE1 . GLU B 12  ? 1.01926 1.04201 0.53039 -0.07947 0.08297  0.01292  11  GLU B OE1 
1543 O  OE2 . GLU B 12  ? 0.99848 0.99413 0.52592 -0.05694 0.02803  0.02210  11  GLU B OE2 
1544 N  N   . ASP B 13  ? 0.42950 0.51019 0.19936 -0.03707 0.07418  -0.01904 12  ASP B N   
1545 C  CA  . ASP B 13  ? 0.40847 0.46776 0.20997 -0.03435 0.06102  0.00193  12  ASP B CA  
1546 C  C   . ASP B 13  ? 0.40458 0.49226 0.25693 -0.03120 0.07223  -0.01124 12  ASP B C   
1547 O  O   . ASP B 13  ? 0.41612 0.49045 0.28820 -0.03580 0.06906  0.00474  12  ASP B O   
1548 C  CB  . ASP B 13  ? 0.46698 0.50201 0.28005 -0.01747 0.03279  0.00455  12  ASP B CB  
1549 C  CG  . ASP B 13  ? 0.49377 0.50950 0.26565 -0.02000 0.01612  0.01381  12  ASP B CG  
1550 O  OD1 . ASP B 13  ? 0.53718 0.53694 0.27758 -0.02924 0.01313  0.03680  12  ASP B OD1 
1551 O  OD2 . ASP B 13  ? 0.49538 0.50786 0.26285 -0.01211 0.00341  -0.00310 12  ASP B OD2 
1552 N  N   . ALA B 14  ? 0.36523 0.49466 0.23921 -0.02155 0.08371  -0.04304 13  ALA B N   
1553 C  CA  . ALA B 14  ? 0.32561 0.48424 0.25144 -0.00864 0.08327  -0.06022 13  ALA B CA  
1554 C  C   . ALA B 14  ? 0.33777 0.51376 0.28271 -0.03301 0.09971  -0.05085 13  ALA B C   
1555 O  O   . ALA B 14  ? 0.30433 0.47755 0.28063 -0.02654 0.08951  -0.04839 13  ALA B O   
1556 C  CB  . ALA B 14  ? 0.34267 0.55067 0.28959 0.01037  0.09100  -0.10060 13  ALA B CB  
1557 N  N   . ALA B 15  ? 0.39342 0.58297 0.31397 -0.06416 0.12601  -0.04633 14  ALA B N   
1558 C  CA  . ALA B 15  ? 0.36389 0.56449 0.29933 -0.09422 0.14446  -0.04033 14  ALA B CA  
1559 C  C   . ALA B 15  ? 0.35611 0.49928 0.28662 -0.09637 0.12764  -0.00995 14  ALA B C   
1560 O  O   . ALA B 15  ? 0.38021 0.52990 0.33623 -0.11208 0.13463  -0.01157 14  ALA B O   
1561 C  CB  . ALA B 15  ? 0.44485 0.64164 0.33985 -0.12872 0.17010  -0.03228 14  ALA B CB  
1562 N  N   . LEU B 16  ? 0.38084 0.47324 0.28239 -0.08126 0.10586  0.01336  15  LEU B N   
1563 C  CA  . LEU B 16  ? 0.39629 0.44021 0.29567 -0.07851 0.08995  0.03781  15  LEU B CA  
1564 C  C   . LEU B 16  ? 0.36453 0.41500 0.30634 -0.05554 0.07257  0.02907  15  LEU B C   
1565 O  O   . LEU B 16  ? 0.34828 0.36952 0.29600 -0.05363 0.06369  0.04222  15  LEU B O   
1566 C  CB  . LEU B 16  ? 0.43169 0.43094 0.28766 -0.07068 0.07287  0.06197  15  LEU B CB  
1567 C  CG  . LEU B 16  ? 0.57416 0.54825 0.36804 -0.09181 0.08418  0.07859  15  LEU B CG  
1568 C  CD1 . LEU B 16  ? 0.60900 0.55630 0.36525 -0.07517 0.05976  0.09296  15  LEU B CD1 
1569 C  CD2 . LEU B 16  ? 0.60778 0.53599 0.37599 -0.11606 0.09435  0.10012  15  LEU B CD2 
1570 N  N   . LEU B 17  ? 0.29612 0.37786 0.26098 -0.03677 0.06670  0.00735  16  LEU B N   
1571 C  CA  . LEU B 17  ? 0.30008 0.37062 0.28428 -0.01644 0.04815  0.00613  16  LEU B CA  
1572 C  C   . LEU B 17  ? 0.27480 0.36086 0.28977 -0.01688 0.04843  -0.00341 16  LEU B C   
1573 O  O   . LEU B 17  ? 0.23998 0.30408 0.25863 -0.00911 0.03723  0.00429  16  LEU B O   
1574 C  CB  . LEU B 17  ? 0.28488 0.36145 0.26790 0.00515  0.03698  -0.00945 16  LEU B CB  
1575 C  CG  . LEU B 17  ? 0.33604 0.39625 0.28819 0.00544  0.03365  -0.00501 16  LEU B CG  
1576 C  CD1 . LEU B 17  ? 0.36088 0.41404 0.31031 0.02668  0.02107  -0.02308 16  LEU B CD1 
1577 C  CD2 . LEU B 17  ? 0.34668 0.37461 0.28315 -0.00083 0.02352  0.01876  16  LEU B CD2 
1578 N  N   . PRO B 18  ? 0.24817 0.37735 0.28682 -0.02673 0.06097  -0.02346 17  PRO B N   
1579 C  CA  . PRO B 18  ? 0.24030 0.38600 0.30820 -0.02846 0.05733  -0.03486 17  PRO B CA  
1580 C  C   . PRO B 18  ? 0.27174 0.37716 0.33036 -0.04431 0.05928  -0.01641 17  PRO B C   
1581 O  O   . PRO B 18  ? 0.25246 0.35039 0.32125 -0.03528 0.04811  -0.01973 17  PRO B O   
1582 C  CB  . PRO B 18  ? 0.23679 0.44472 0.33518 -0.04451 0.07426  -0.06159 17  PRO B CB  
1583 C  CG  . PRO B 18  ? 0.23047 0.46549 0.32467 -0.02996 0.07770  -0.07478 17  PRO B CG  
1584 C  CD  . PRO B 18  ? 0.24468 0.42115 0.29113 -0.03233 0.07655  -0.04450 17  PRO B CD  
1585 N  N   . ALA B 19  ? 0.26879 0.34243 0.30237 -0.06504 0.07138  0.00244  18  ALA B N   
1586 C  CA  . ALA B 19  ? 0.31752 0.34270 0.33963 -0.07248 0.06894  0.01849  18  ALA B CA  
1587 C  C   . ALA B 19  ? 0.29588 0.29657 0.31448 -0.04690 0.05117  0.02868  18  ALA B C   
1588 O  O   . ALA B 19  ? 0.32059 0.30051 0.34545 -0.04341 0.04657  0.02890  18  ALA B O   
1589 C  CB  . ALA B 19  ? 0.33712 0.32051 0.32144 -0.09449 0.08037  0.03947  18  ALA B CB  
1590 N  N   . ILE B 20  ? 0.28252 0.28773 0.29199 -0.03143 0.04286  0.03389  19  ILE B N   
1591 C  CA  . ILE B 20  ? 0.28942 0.28180 0.30019 -0.01450 0.03023  0.03974  19  ILE B CA  
1592 C  C   . ILE B 20  ? 0.28303 0.28915 0.30784 -0.00552 0.02564  0.02629  19  ILE B C   
1593 O  O   . ILE B 20  ? 0.28362 0.27935 0.31166 -0.00031 0.02275  0.02713  19  ILE B O   
1594 C  CB  . ILE B 20  ? 0.30524 0.29863 0.30174 -0.00729 0.02313  0.04601  19  ILE B CB  
1595 C  CG1 . ILE B 20  ? 0.33952 0.31399 0.31340 -0.01267 0.02213  0.06146  19  ILE B CG1 
1596 C  CG2 . ILE B 20  ? 0.28885 0.28047 0.29162 0.00291  0.01383  0.04605  19  ILE B CG2 
1597 C  CD1 . ILE B 20  ? 0.36282 0.34352 0.31927 -0.00877 0.01470  0.06292  19  ILE B CD1 
1598 N  N   . GLU B 21  ? 0.25023 0.28023 0.28052 -0.00144 0.02387  0.01220  20  GLU B N   
1599 C  CA  . GLU B 21  ? 0.25558 0.29066 0.28800 0.01021  0.01426  0.00142  20  GLU B CA  
1600 C  C   . GLU B 21  ? 0.27028 0.30922 0.31541 0.00254  0.01681  -0.00700 20  GLU B C   
1601 O  O   . GLU B 21  ? 0.27119 0.29942 0.30770 0.00878  0.01140  -0.00884 20  GLU B O   
1602 C  CB  . GLU B 21  ? 0.26826 0.32744 0.30475 0.02380  0.00569  -0.01469 20  GLU B CB  
1603 C  CG  . GLU B 21  ? 0.27872 0.32703 0.30052 0.04184  -0.01156 -0.02059 20  GLU B CG  
1604 C  CD  . GLU B 21  ? 0.30049 0.36292 0.32178 0.06594  -0.02832 -0.03716 20  GLU B CD  
1605 O  OE1 . GLU B 21  ? 0.38718 0.44264 0.39486 0.08240  -0.04623 -0.04368 20  GLU B OE1 
1606 O  OE2 . GLU B 21  ? 0.31742 0.39680 0.34876 0.07165  -0.02572 -0.04553 20  GLU B OE2 
1607 N  N   . ARG B 22  ? 0.26891 0.31935 0.32950 -0.01461 0.02675  -0.01292 21  ARG B N   
1608 C  CA  . ARG B 22  ? 0.22747 0.27271 0.29808 -0.02620 0.02929  -0.02265 21  ARG B CA  
1609 C  C   . ARG B 22  ? 0.28739 0.29259 0.34574 -0.02293 0.03040  -0.01082 21  ARG B C   
1610 O  O   . ARG B 22  ? 0.33250 0.33159 0.39120 -0.01970 0.02737  -0.02127 21  ARG B O   
1611 C  CB  . ARG B 22  ? 0.24755 0.30390 0.33227 -0.05349 0.04303  -0.02991 21  ARG B CB  
1612 C  CG  . ARG B 22  ? 0.30025 0.41610 0.41353 -0.05734 0.04186  -0.05543 21  ARG B CG  
1613 C  CD  . ARG B 22  ? 0.35854 0.49325 0.49084 -0.09433 0.05999  -0.06812 21  ARG B CD  
1614 N  NE  . ARG B 22  ? 0.41558 0.53465 0.52923 -0.11316 0.07894  -0.05109 21  ARG B NE  
1615 C  CZ  . ARG B 22  ? 0.45290 0.61762 0.57617 -0.11576 0.08883  -0.05968 21  ARG B CZ  
1616 N  NH1 . ARG B 22  ? 0.47218 0.70151 0.62984 -0.09628 0.07901  -0.08672 21  ARG B NH1 
1617 N  NH2 . ARG B 22  ? 0.43630 0.58051 0.53109 -0.13524 0.10707  -0.04275 21  ARG B NH2 
1618 N  N   . SER B 23  ? 0.26065 0.24181 0.30868 -0.02157 0.03337  0.00753  22  SER B N   
1619 C  CA  . SER B 23  ? 0.30524 0.25770 0.35005 -0.01194 0.03152  0.01367  22  SER B CA  
1620 C  C   . SER B 23  ? 0.28439 0.25186 0.33013 0.00196  0.02817  0.00797  22  SER B C   
1621 O  O   . SER B 23  ? 0.31963 0.28044 0.36848 0.00736  0.03001  -0.00188 22  SER B O   
1622 C  CB  . SER B 23  ? 0.35005 0.28176 0.38431 -0.00738 0.02881  0.03264  22  SER B CB  
1623 O  OG  . SER B 23  ? 0.36681 0.28048 0.40632 0.00885  0.02327  0.03357  22  SER B OG  
1624 N  N   . ALA B 24  ? 0.25240 0.23607 0.29062 0.00570  0.02486  0.01291  23  ALA B N   
1625 C  CA  . ALA B 24  ? 0.27308 0.26221 0.30103 0.01111  0.02472  0.01071  23  ALA B CA  
1626 C  C   . ALA B 24  ? 0.25668 0.24741 0.27422 0.01173  0.02384  -0.00326 23  ALA B C   
1627 O  O   . ALA B 24  ? 0.28726 0.27718 0.29660 0.01308  0.02974  -0.00905 23  ALA B O   
1628 C  CB  . ALA B 24  ? 0.28590 0.27618 0.29870 0.01151  0.01982  0.01858  23  ALA B CB  
1629 N  N   . GLY B 25  ? 0.29068 0.28974 0.31002 0.01030  0.01681  -0.01217 24  GLY B N   
1630 C  CA  . GLY B 25  ? 0.30483 0.30970 0.31300 0.01255  0.01005  -0.02806 24  GLY B CA  
1631 C  C   . GLY B 25  ? 0.28617 0.28309 0.29992 0.00789  0.01703  -0.04090 24  GLY B C   
1632 O  O   . GLY B 25  ? 0.30774 0.30674 0.30361 0.01011  0.01274  -0.05466 24  GLY B O   
1633 N  N   . GLU B 26  ? 0.27300 0.25506 0.30556 0.00373  0.02551  -0.03762 25  GLU B N   
1634 C  CA  . GLU B 26  ? 0.30040 0.26521 0.33675 0.00394  0.03046  -0.05242 25  GLU B CA  
1635 C  C   . GLU B 26  ? 0.32856 0.29941 0.35093 0.01419  0.03714  -0.05932 25  GLU B C   
1636 O  O   . GLU B 26  ? 0.34828 0.31230 0.36648 0.01632  0.04063  -0.07918 25  GLU B O   
1637 C  CB  . GLU B 26  ? 0.33161 0.26599 0.38227 0.00360  0.03399  -0.04437 25  GLU B CB  
1638 C  CG  . GLU B 26  ? 0.34957 0.26957 0.40487 -0.01573 0.03356  -0.03968 25  GLU B CG  
1639 C  CD  . GLU B 26  ? 0.41198 0.32814 0.47110 -0.03292 0.03320  -0.06232 25  GLU B CD  
1640 O  OE1 . GLU B 26  ? 0.41608 0.31293 0.47131 -0.02833 0.03296  -0.07954 25  GLU B OE1 
1641 O  OE2 . GLU B 26  ? 0.48815 0.42747 0.55710 -0.05168 0.03318  -0.06742 25  GLU B OE2 
1642 N  N   . SER B 27  ? 0.31052 0.29467 0.32273 0.01691  0.04078  -0.04593 26  SER B N   
1643 C  CA  . SER B 27  ? 0.29079 0.28671 0.28756 0.01853  0.05309  -0.05265 26  SER B CA  
1644 C  C   . SER B 27  ? 0.30608 0.30025 0.26388 0.01508  0.05202  -0.06508 26  SER B C   
1645 O  O   . SER B 27  ? 0.36268 0.36535 0.30168 0.01339  0.06623  -0.07548 26  SER B O   
1646 C  CB  . SER B 27  ? 0.35342 0.35960 0.34246 0.01273  0.05804  -0.03526 26  SER B CB  
1647 O  OG  . SER B 27  ? 0.34855 0.36280 0.37217 0.01737  0.05757  -0.02741 26  SER B OG  
1648 N  N   . PHE B 28  ? 0.30987 0.29827 0.25518 0.01435  0.03529  -0.06720 27  PHE B N   
1649 C  CA  . PHE B 28  ? 0.34241 0.32881 0.24524 0.01472  0.02723  -0.07914 27  PHE B CA  
1650 C  C   . PHE B 28  ? 0.36170 0.34979 0.27182 0.01402  0.02395  -0.10684 27  PHE B C   
1651 O  O   . PHE B 28  ? 0.40017 0.38840 0.27083 0.01483  0.01696  -0.12040 27  PHE B O   
1652 C  CB  . PHE B 28  ? 0.34556 0.33032 0.22942 0.02010  0.00427  -0.06963 27  PHE B CB  
1653 C  CG  . PHE B 28  ? 0.35332 0.32046 0.20731 0.02118  0.00443  -0.04539 27  PHE B CG  
1654 C  CD1 . PHE B 28  ? 0.40867 0.35172 0.19864 0.01966  0.00339  -0.03817 27  PHE B CD1 
1655 C  CD2 . PHE B 28  ? 0.34538 0.31314 0.22733 0.02085  0.00617  -0.03036 27  PHE B CD2 
1656 C  CE1 . PHE B 28  ? 0.43052 0.34339 0.18443 0.01537  0.00447  -0.01517 27  PHE B CE1 
1657 C  CE2 . PHE B 28  ? 0.33636 0.28046 0.18704 0.01916  0.00559  -0.01104 27  PHE B CE2 
1658 C  CZ  . PHE B 28  ? 0.40517 0.31895 0.19226 0.01527  0.00497  -0.00345 27  PHE B CZ  
1659 N  N   . ARG B 29  ? 0.30879 0.31310 0.35184 0.02139  0.03532  0.00864  28  ARG B N   
1660 C  CA  . ARG B 29  ? 0.29289 0.26822 0.36926 0.01396  0.04665  0.00945  28  ARG B CA  
1661 C  C   . ARG B 29  ? 0.33109 0.30292 0.40369 0.00251  0.03373  -0.00549 28  ARG B C   
1662 O  O   . ARG B 29  ? 0.31533 0.27532 0.42103 -0.01074 0.03142  -0.01887 28  ARG B O   
1663 C  CB  . ARG B 29  ? 0.37328 0.32252 0.45073 0.03789  0.08469  0.03113  28  ARG B CB  
1664 C  CG  . ARG B 29  ? 0.39397 0.32932 0.48624 0.04502  0.10736  0.04490  28  ARG B CG  
1665 C  CD  . ARG B 29  ? 0.48742 0.36665 0.59306 0.05835  0.16316  0.06150  28  ARG B CD  
1666 N  NE  . ARG B 29  ? 0.42789 0.29128 0.52885 0.07368  0.18825  0.07904  28  ARG B NE  
1667 C  CZ  . ARG B 29  ? 0.47865 0.34468 0.63315 0.04724  0.19245  0.06492  28  ARG B CZ  
1668 N  NH1 . ARG B 29  ? 0.42335 0.31372 0.63814 0.01089  0.17051  0.02920  28  ARG B NH1 
1669 N  NH2 . ARG B 29  ? 0.47325 0.32434 0.61801 0.06291  0.21542  0.08269  28  ARG B NH2 
1670 N  N   . LEU B 30  ? 0.27812 0.26662 0.31696 0.00752  0.02592  -0.01053 29  LEU B N   
1671 C  CA  . LEU B 30  ? 0.26838 0.25034 0.30143 -0.00326 0.01662  -0.02393 29  LEU B CA  
1672 C  C   . LEU B 30  ? 0.32522 0.30270 0.33465 -0.02043 0.00073  -0.04127 29  LEU B C   
1673 O  O   . LEU B 30  ? 0.32912 0.30129 0.32136 -0.02781 -0.00219 -0.05359 29  LEU B O   
1674 C  CB  . LEU B 30  ? 0.32651 0.32496 0.33974 0.01642  0.02498  -0.02257 29  LEU B CB  
1675 C  CG  . LEU B 30  ? 0.32953 0.30463 0.34636 0.04293  0.05199  0.00027  29  LEU B CG  
1676 C  CD1 . LEU B 30  ? 0.38421 0.37316 0.36576 0.07620  0.05828  0.00154  29  LEU B CD1 
1677 C  CD2 . LEU B 30  ? 0.39035 0.32530 0.44935 0.02312  0.06621  0.00033  29  LEU B CD2 
1678 N  N   A LEU B 31  ? 0.29800 0.26839 0.29914 -0.02381 -0.00354 -0.04127 30  LEU B N   
1679 N  N   B LEU B 31  ? 0.30026 0.27081 0.30127 -0.02381 -0.00345 -0.04128 30  LEU B N   
1680 C  CA  A LEU B 31  ? 0.32702 0.26791 0.29030 -0.03015 -0.00880 -0.05211 30  LEU B CA  
1681 C  CA  B LEU B 31  ? 0.32539 0.26636 0.28870 -0.03018 -0.00875 -0.05212 30  LEU B CA  
1682 C  C   A LEU B 31  ? 0.33055 0.25890 0.30304 -0.01979 -0.02684 -0.05558 30  LEU B C   
1683 C  C   B LEU B 31  ? 0.33426 0.26275 0.30697 -0.01984 -0.02680 -0.05554 30  LEU B C   
1684 O  O   A LEU B 31  ? 0.35482 0.29055 0.34008 -0.01271 -0.03178 -0.05304 30  LEU B O   
1685 O  O   B LEU B 31  ? 0.35344 0.28951 0.33931 -0.01282 -0.03168 -0.05295 30  LEU B O   
1686 C  CB  A LEU B 31  ? 0.33231 0.26892 0.27064 -0.03401 0.00403  -0.05336 30  LEU B CB  
1687 C  CB  B LEU B 31  ? 0.33763 0.27426 0.27587 -0.03411 0.00412  -0.05348 30  LEU B CB  
1688 C  CG  A LEU B 31  ? 0.38576 0.33398 0.31083 -0.04857 0.02547  -0.07292 30  LEU B CG  
1689 C  CG  B LEU B 31  ? 0.36946 0.33716 0.30945 -0.04420 0.02205  -0.06899 30  LEU B CG  
1690 C  CD1 A LEU B 31  ? 0.35429 0.36192 0.31272 -0.04025 0.02267  -0.07754 30  LEU B CD1 
1691 C  CD1 B LEU B 31  ? 0.37824 0.33670 0.30068 -0.05274 0.04019  -0.07761 30  LEU B CD1 
1692 C  CD2 A LEU B 31  ? 0.37381 0.30896 0.27922 -0.05718 0.04627  -0.08134 30  LEU B CD2 
1693 C  CD2 B LEU B 31  ? 0.41967 0.37950 0.34606 -0.05685 0.03221  -0.08990 30  LEU B CD2 
1694 N  N   . PRO B 32  ? 0.36370 0.28296 0.33480 -0.01564 -0.03896 -0.06800 31  PRO B N   
1695 C  CA  . PRO B 32  ? 0.36225 0.29533 0.35987 -0.00059 -0.06034 -0.08697 31  PRO B CA  
1696 C  C   . PRO B 32  ? 0.35369 0.27744 0.31411 0.02358  -0.07341 -0.09247 31  PRO B C   
1697 O  O   . PRO B 32  ? 0.41905 0.37743 0.42391 0.03333  -0.08771 -0.11049 31  PRO B O   
1698 C  CB  . PRO B 32  ? 0.41587 0.33942 0.39852 0.00569  -0.07192 -0.10285 31  PRO B CB  
1699 C  CG  . PRO B 32  ? 0.41001 0.32410 0.38935 -0.01441 -0.05368 -0.08897 31  PRO B CG  
1700 C  CD  . PRO B 32  ? 0.40197 0.30987 0.35715 -0.02321 -0.03476 -0.07234 31  PRO B CD  
1701 N  N   . GLU B 33  ? 0.43809 0.31322 0.31856 0.03474  -0.06307 -0.08108 32  GLU B N   
1702 C  CA  . GLU B 33  ? 0.48665 0.34171 0.31732 0.06756  -0.07136 -0.08330 32  GLU B CA  
1703 C  C   . GLU B 33  ? 0.47658 0.35533 0.34162 0.05748  -0.06682 -0.07364 32  GLU B C   
1704 O  O   . GLU B 33  ? 0.47699 0.36343 0.32983 0.08497  -0.08216 -0.08214 32  GLU B O   
1705 C  CB  . GLU B 33  ? 0.62349 0.39706 0.34827 0.08383  -0.04507 -0.07088 32  GLU B CB  
1706 C  CG  . GLU B 33  ? 0.75802 0.49662 0.43432 0.10137  -0.04615 -0.07882 32  GLU B CG  
1707 C  CD  . GLU B 33  ? 1.04175 0.67841 0.60297 0.12037  -0.00511 -0.06607 32  GLU B CD  
1708 O  OE1 . GLU B 33  ? 1.08391 0.67972 0.60567 0.12489  0.02247  -0.05077 32  GLU B OE1 
1709 O  OE2 . GLU B 33  ? 1.14481 0.75343 0.67868 0.12477  0.00413  -0.06439 32  GLU B OE2 
1710 N  N   . LEU B 34  ? 0.39400 0.28965 0.29974 0.02517  -0.04826 -0.05898 33  LEU B N   
1711 C  CA  . LEU B 34  ? 0.34125 0.25172 0.26576 0.01792  -0.03925 -0.04678 33  LEU B CA  
1712 C  C   . LEU B 34  ? 0.30280 0.25611 0.30249 0.00369  -0.03650 -0.04274 33  LEU B C   
1713 O  O   . LEU B 34  ? 0.33861 0.30353 0.35088 -0.00116 -0.02492 -0.02934 33  LEU B O   
1714 C  CB  . LEU B 34  ? 0.37452 0.26004 0.26058 0.00278  -0.01127 -0.03686 33  LEU B CB  
1715 C  CG  . LEU B 34  ? 0.43780 0.25621 0.24130 0.01343  0.00797  -0.03900 33  LEU B CG  
1716 C  CD1 . LEU B 34  ? 0.50072 0.30136 0.28902 -0.01295 0.04762  -0.04407 33  LEU B CD1 
1717 C  CD2 . LEU B 34  ? 0.52905 0.32039 0.28827 0.04743  -0.00210 -0.03511 33  LEU B CD2 
1718 N  N   . ALA B 35  ? 0.29699 0.26667 0.34229 -0.00036 -0.04074 -0.05457 34  ALA B N   
1719 C  CA  . ALA B 35  ? 0.27999 0.26575 0.38275 -0.01090 -0.02085 -0.04694 34  ALA B CA  
1720 C  C   . ALA B 35  ? 0.30174 0.30211 0.44230 -0.00967 -0.01445 -0.04786 34  ALA B C   
1721 O  O   . ALA B 35  ? 0.34349 0.34010 0.50261 -0.01191 0.01145  -0.02939 34  ALA B O   
1722 C  CB  . ALA B 35  ? 0.33368 0.32442 0.48203 -0.01779 -0.01707 -0.06559 34  ALA B CB  
1723 N  N   . TRP B 36  ? 0.26128 0.27746 0.40788 0.00037  -0.03647 -0.07070 35  TRP B N   
1724 C  CA  . TRP B 36  ? 0.25548 0.29337 0.44531 0.00108  -0.03272 -0.08008 35  TRP B CA  
1725 C  C   . TRP B 36  ? 0.25834 0.28230 0.41634 0.00154  -0.02012 -0.04681 35  TRP B C   
1726 O  O   . TRP B 36  ? 0.27921 0.31298 0.47566 -0.00196 -0.00512 -0.04469 35  TRP B O   
1727 C  CB  . TRP B 36  ? 0.28129 0.34757 0.46925 0.02386  -0.06620 -0.11600 35  TRP B CB  
1728 C  CG  . TRP B 36  ? 0.31523 0.34881 0.40519 0.04952  -0.08380 -0.09896 35  TRP B CG  
1729 C  CD1 . TRP B 36  ? 0.37960 0.37878 0.40050 0.06380  -0.09129 -0.09485 35  TRP B CD1 
1730 C  CD2 . TRP B 36  ? 0.38229 0.40188 0.42978 0.06347  -0.08505 -0.08422 35  TRP B CD2 
1731 N  NE1 . TRP B 36  ? 0.41710 0.37222 0.35250 0.08549  -0.08905 -0.07832 35  TRP B NE1 
1732 C  CE2 . TRP B 36  ? 0.40087 0.36923 0.35153 0.08565  -0.08660 -0.07180 35  TRP B CE2 
1733 C  CE3 . TRP B 36  ? 0.39501 0.43378 0.47482 0.05931  -0.07958 -0.08033 35  TRP B CE3 
1734 C  CZ2 . TRP B 36  ? 0.50040 0.43215 0.38564 0.10314  -0.07897 -0.05606 35  TRP B CZ2 
1735 C  CZ3 . TRP B 36  ? 0.47352 0.48763 0.49222 0.07719  -0.08161 -0.06521 35  TRP B CZ3 
1736 C  CH2 . TRP B 36  ? 0.51249 0.47137 0.43414 0.09878  -0.07953 -0.05322 35  TRP B CH2 
1737 N  N   . ILE B 37  ? 0.28494 0.28863 0.37881 0.00458  -0.02231 -0.02727 36  ILE B N   
1738 C  CA  . ILE B 37  ? 0.32087 0.32267 0.39073 0.00464  -0.01071 -0.00633 36  ILE B CA  
1739 C  C   . ILE B 37  ? 0.26999 0.28121 0.36863 0.00481  0.01306  0.01106  36  ILE B C   
1740 O  O   . ILE B 37  ? 0.33209 0.35040 0.43135 0.01054  0.02210  0.02376  36  ILE B O   
1741 C  CB  . ILE B 37  ? 0.31847 0.30324 0.33156 0.00123  -0.00738 -0.00396 36  ILE B CB  
1742 C  CG1 . ILE B 37  ? 0.38195 0.33252 0.34380 0.01054  -0.01663 -0.01316 36  ILE B CG1 
1743 C  CG2 . ILE B 37  ? 0.35926 0.36111 0.36491 -0.00105 0.00763  0.00483  36  ILE B CG2 
1744 C  CD1 . ILE B 37  ? 0.46444 0.40859 0.41036 0.02287  -0.01985 -0.00963 36  ILE B CD1 
1745 N  N   . ALA B 38  ? 0.26733 0.27218 0.38016 0.00496  0.02677  0.01376  37  ALA B N   
1746 C  CA  . ALA B 38  ? 0.30005 0.29735 0.41616 0.01980  0.05667  0.03482  37  ALA B CA  
1747 C  C   . ALA B 38  ? 0.37269 0.35568 0.53176 0.01853  0.08223  0.03860  37  ALA B C   
1748 O  O   . ALA B 38  ? 0.41013 0.37308 0.55739 0.03824  0.11457  0.06149  37  ALA B O   
1749 C  CB  . ALA B 38  ? 0.35774 0.33865 0.47107 0.02544  0.07155  0.03752  37  ALA B CB  
1750 N  N   . ASP B 39  ? 0.36145 0.35494 0.56821 0.00081  0.07161  0.01224  38  ASP B N   
1751 C  CA  . ASP B 39  ? 0.33901 0.32781 0.60286 -0.00692 0.09910  0.00210  38  ASP B CA  
1752 C  C   . ASP B 39  ? 0.31992 0.33773 0.58944 -0.00720 0.07306  -0.00865 38  ASP B C   
1753 O  O   . ASP B 39  ? 0.33686 0.36457 0.66320 -0.01604 0.08836  -0.02887 38  ASP B O   
1754 C  CB  . ASP B 39  ? 0.37241 0.36349 0.71006 -0.02715 0.11620  -0.03714 38  ASP B CB  
1755 C  CG  . ASP B 39  ? 0.51622 0.46705 0.84696 -0.02664 0.15104  -0.02453 38  ASP B CG  
1756 O  OD1 . ASP B 39  ? 0.46090 0.36583 0.75449 -0.00793 0.19160  0.01244  38  ASP B OD1 
1757 O  OD2 . ASP B 39  ? 0.48486 0.44894 0.84004 -0.03835 0.13778  -0.05179 38  ASP B OD2 
1758 N  N   . ALA B 40  ? 0.56299 0.38567 0.40930 -0.06481 -0.12928 -0.09018 39  ALA B N   
1759 C  CA  . ALA B 40  ? 0.51640 0.39573 0.38510 -0.06624 -0.12323 -0.06731 39  ALA B CA  
1760 C  C   . ALA B 40  ? 0.51009 0.39853 0.40933 -0.06877 -0.11051 -0.04457 39  ALA B C   
1761 O  O   . ALA B 40  ? 0.59503 0.44925 0.49309 -0.06523 -0.10429 -0.04304 39  ALA B O   
1762 C  CB  . ALA B 40  ? 0.54110 0.44472 0.39200 -0.04340 -0.11140 -0.06748 39  ALA B CB  
1763 N  N   . GLY B 41  ? 0.55383 0.49152 0.48028 -0.07388 -0.10737 -0.02725 40  GLY B N   
1764 C  CA  . GLY B 41  ? 0.47846 0.43292 0.42991 -0.07676 -0.09323 -0.00913 40  GLY B CA  
1765 C  C   . GLY B 41  ? 0.46342 0.40516 0.40467 -0.05399 -0.07460 -0.00677 40  GLY B C   
1766 O  O   . GLY B 41  ? 0.50331 0.43940 0.42694 -0.03502 -0.07000 -0.01427 40  GLY B O   
1767 N  N   . VAL B 42  ? 0.42474 0.36535 0.37593 -0.05945 -0.06453 0.00527  41  VAL B N   
1768 C  CA  . VAL B 42  ? 0.41478 0.35250 0.35961 -0.04223 -0.04836 0.00914  41  VAL B CA  
1769 C  C   . VAL B 42  ? 0.38165 0.36166 0.34675 -0.04341 -0.03521 0.01975  41  VAL B C   
1770 O  O   . VAL B 42  ? 0.40901 0.42130 0.39548 -0.05897 -0.03691 0.02633  41  VAL B O   
1771 C  CB  . VAL B 42  ? 0.42476 0.32337 0.35773 -0.04461 -0.04913 0.01238  41  VAL B CB  
1772 C  CG1 . VAL B 42  ? 0.46521 0.32171 0.38242 -0.03914 -0.06191 -0.00298 41  VAL B CG1 
1773 C  CG2 . VAL B 42  ? 0.42108 0.32275 0.36443 -0.06933 -0.05121 0.02915  41  VAL B CG2 
1774 N  N   . ALA B 43  ? 0.36490 0.34702 0.32402 -0.02734 -0.02179 0.01956  42  ALA B N   
1775 C  CA  . ALA B 43  ? 0.39623 0.41384 0.37058 -0.02384 -0.00772 0.02307  42  ALA B CA  
1776 C  C   . ALA B 43  ? 0.43971 0.47168 0.41762 -0.04403 -0.00142 0.03332  42  ALA B C   
1777 O  O   . ALA B 43  ? 0.45355 0.45587 0.41475 -0.05471 -0.00571 0.04026  42  ALA B O   
1778 C  CB  . ALA B 43  ? 0.37525 0.38111 0.33678 -0.00581 0.00260  0.01799  42  ALA B CB  
1779 N  N   . GLY B 44  ? 0.35246 0.43428 0.35342 -0.04874 0.00887  0.03575  43  GLY B N   
1780 C  CA  . GLY B 44  ? 0.34645 0.45327 0.34818 -0.07035 0.01876  0.04728  43  GLY B CA  
1781 C  C   . GLY B 44  ? 0.34678 0.45195 0.32631 -0.06364 0.03426  0.04505  43  GLY B C   
1782 O  O   . GLY B 44  ? 0.35377 0.44118 0.32225 -0.04193 0.03823  0.03265  43  GLY B O   
1783 N  N   . VAL B 45  ? 0.36838 0.49346 0.33887 -0.08636 0.04197  0.05858  44  VAL B N   
1784 C  CA  . VAL B 45  ? 0.38658 0.51101 0.32827 -0.08510 0.05391  0.05772  44  VAL B CA  
1785 C  C   . VAL B 45  ? 0.33368 0.49119 0.28071 -0.06243 0.07358  0.03554  44  VAL B C   
1786 O  O   . VAL B 45  ? 0.35507 0.49202 0.27846 -0.05009 0.07769  0.02396  44  VAL B O   
1787 C  CB  . VAL B 45  ? 0.41748 0.56173 0.34455 -0.11741 0.05751  0.08048  44  VAL B CB  
1788 C  CG1 . VAL B 45  ? 0.40438 0.55347 0.29539 -0.11788 0.06856  0.07945  44  VAL B CG1 
1789 C  CG2 . VAL B 45  ? 0.50229 0.59826 0.42362 -0.13696 0.03421  0.10201  44  VAL B CG2 
1790 N  N   . ASP B 46  ? 0.33720 0.54480 0.31756 -0.05550 0.08411  0.02803  45  ASP B N   
1791 C  CA  . ASP B 46  ? 0.40434 0.64091 0.39297 -0.02942 0.10282  0.00439  45  ASP B CA  
1792 C  C   . ASP B 46  ? 0.39434 0.58382 0.38165 -0.00014 0.09384  -0.01105 45  ASP B C   
1793 O  O   . ASP B 46  ? 0.40846 0.59032 0.38504 0.01889  0.10438  -0.03092 45  ASP B O   
1794 C  CB  . ASP B 46  ? 0.38987 0.69835 0.42253 -0.02564 0.11516  0.00116  45  ASP B CB  
1795 C  CG  . ASP B 46  ? 0.55301 0.92002 0.58411 -0.05673 0.13078  0.01506  45  ASP B CG  
1796 O  OD1 . ASP B 46  ? 0.60119 0.95843 0.59191 -0.07156 0.13859  0.01917  45  ASP B OD1 
1797 O  OD2 . ASP B 46  ? 0.57521 1.00128 0.64446 -0.06900 0.13428  0.02401  45  ASP B OD2 
1798 N  N   . PHE B 47  ? 0.33837 0.49491 0.33348 0.00178  0.07434  -0.00257 46  PHE B N   
1799 C  CA  . PHE B 47  ? 0.36250 0.47296 0.34940 0.02221  0.06508  -0.01086 46  PHE B CA  
1800 C  C   . PHE B 47  ? 0.38817 0.46008 0.33866 0.01839  0.06599  -0.01477 46  PHE B C   
1801 O  O   . PHE B 47  ? 0.36964 0.42130 0.31056 0.03334  0.07003  -0.02945 46  PHE B O   
1802 C  CB  . PHE B 47  ? 0.35880 0.44734 0.35200 0.01902  0.04562  0.00033  46  PHE B CB  
1803 C  CG  . PHE B 47  ? 0.38777 0.43282 0.36709 0.03294  0.03664  -0.00274 46  PHE B CG  
1804 C  CD1 . PHE B 47  ? 0.43877 0.48038 0.43190 0.05452  0.03436  -0.00821 46  PHE B CD1 
1805 C  CD2 . PHE B 47  ? 0.38104 0.39151 0.33584 0.02411  0.02983  0.00198  46  PHE B CD2 
1806 C  CE1 . PHE B 47  ? 0.42776 0.42951 0.40573 0.06190  0.02570  -0.00621 46  PHE B CE1 
1807 C  CE2 . PHE B 47  ? 0.40915 0.38931 0.35280 0.03317  0.02373  0.00110  46  PHE B CE2 
1808 C  CZ  . PHE B 47  ? 0.39392 0.36891 0.34692 0.04902  0.02164  -0.00137 46  PHE B CZ  
1809 N  N   . HIS B 48  ? 0.37657 0.43694 0.30782 -0.00219 0.06003  -0.00122 47  HIS B N   
1810 C  CA  . HIS B 48  ? 0.36299 0.39626 0.26389 -0.00684 0.05809  -0.00241 47  HIS B CA  
1811 C  C   . HIS B 48  ? 0.36665 0.41847 0.24949 -0.00682 0.07358  -0.01656 47  HIS B C   
1812 O  O   . HIS B 48  ? 0.39296 0.42121 0.25666 -0.00143 0.07312  -0.02906 47  HIS B O   
1813 C  CB  . HIS B 48  ? 0.36479 0.38629 0.25299 -0.02565 0.04698  0.01681  47  HIS B CB  
1814 C  CG  . HIS B 48  ? 0.33799 0.33465 0.23801 -0.02289 0.03208  0.02402  47  HIS B CG  
1815 N  ND1 . HIS B 48  ? 0.38224 0.35299 0.27901 -0.01157 0.02490  0.01947  47  HIS B ND1 
1816 C  CD2 . HIS B 48  ? 0.38932 0.38485 0.30244 -0.03126 0.02361  0.03322  47  HIS B CD2 
1817 C  CE1 . HIS B 48  ? 0.37547 0.33303 0.28098 -0.01014 0.01474  0.02334  47  HIS B CE1 
1818 N  NE2 . HIS B 48  ? 0.35933 0.32715 0.27387 -0.02181 0.01239  0.03038  47  HIS B NE2 
1819 N  N   . ARG B 49  ? 0.34976 0.44633 0.23711 -0.01488 0.08767  -0.01596 48  ARG B N   
1820 C  CA  A ARG B 49  ? 0.43176 0.55336 0.29742 -0.01450 0.10567  -0.03324 48  ARG B CA  
1821 C  CA  B ARG B 49  ? 0.43109 0.55273 0.29677 -0.01450 0.10568  -0.03324 48  ARG B CA  
1822 C  C   . ARG B 49  ? 0.46357 0.57056 0.33546 0.01324  0.11284  -0.06260 48  ARG B C   
1823 O  O   . ARG B 49  ? 0.44173 0.53506 0.28451 0.01553  0.11843  -0.08191 48  ARG B O   
1824 C  CB  A ARG B 49  ? 0.46265 0.64672 0.33818 -0.02663 0.12319  -0.02804 48  ARG B CB  
1825 C  CB  B ARG B 49  ? 0.46156 0.64571 0.33721 -0.02660 0.12320  -0.02804 48  ARG B CB  
1826 C  CG  A ARG B 49  ? 0.48566 0.68077 0.34261 -0.06004 0.11749  0.00189  48  ARG B CG  
1827 C  CG  B ARG B 49  ? 0.48622 0.68067 0.34654 -0.05973 0.11652  0.00286  48  ARG B CG  
1828 C  CD  A ARG B 49  ? 0.54559 0.80002 0.40582 -0.07324 0.13587  0.00469  48  ARG B CD  
1829 C  CD  B ARG B 49  ? 0.53242 0.78886 0.39918 -0.07428 0.13479  0.00755  48  ARG B CD  
1830 N  NE  A ARG B 49  ? 0.57335 0.82867 0.42536 -0.10487 0.12464  0.03754  48  ARG B NE  
1831 N  NE  B ARG B 49  ? 0.54928 0.80909 0.41814 -0.10531 0.12318  0.04105  48  ARG B NE  
1832 C  CZ  A ARG B 49  ? 0.54350 0.82537 0.42312 -0.12240 0.12310  0.05607  48  ARG B CZ  
1833 C  CZ  B ARG B 49  ? 0.58319 0.82449 0.42267 -0.12563 0.11240  0.06077  48  ARG B CZ  
1834 N  NH1 A ARG B 49  ? 0.60375 0.87389 0.47257 -0.15087 0.10959  0.08500  48  ARG B NH1 
1835 N  NH1 B ARG B 49  ? 0.60792 0.84453 0.45312 -0.15131 0.09951  0.08991  48  ARG B NH1 
1836 N  NH2 A ARG B 49  ? 0.45580 0.77523 0.37611 -0.11124 0.13255  0.04574  48  ARG B NH2 
1837 N  NH2 B ARG B 49  ? 0.58650 0.81232 0.39222 -0.12043 0.11206  0.05137  48  ARG B NH2 
1838 N  N   A ARG B 50  ? 0.41963 0.52551 0.32790 0.03390  0.11009  -0.06588 49  ARG B N   
1839 N  N   B ARG B 50  ? 0.42109 0.52701 0.32935 0.03393  0.11013  -0.06594 49  ARG B N   
1840 C  CA  A ARG B 50  ? 0.45999 0.54591 0.37811 0.06292  0.11405  -0.09070 49  ARG B CA  
1841 C  CA  B ARG B 50  ? 0.45999 0.54569 0.37762 0.06285  0.11414  -0.09091 49  ARG B CA  
1842 C  C   A ARG B 50  ? 0.45343 0.47501 0.34757 0.06322  0.09978  -0.09478 49  ARG B C   
1843 C  C   B ARG B 50  ? 0.45364 0.47512 0.34725 0.06293  0.09980  -0.09481 49  ARG B C   
1844 O  O   A ARG B 50  ? 0.48852 0.48432 0.36642 0.07407  0.10425  -0.11889 49  ARG B O   
1845 O  O   B ARG B 50  ? 0.49102 0.48667 0.36795 0.07343  0.10423  -0.11885 49  ARG B O   
1846 C  CB  A ARG B 50  ? 0.48389 0.58449 0.44751 0.08372  0.10924  -0.08616 49  ARG B CB  
1847 C  CB  B ARG B 50  ? 0.48367 0.58351 0.44674 0.08415  0.10947  -0.08689 49  ARG B CB  
1848 C  CG  A ARG B 50  ? 0.55740 0.63588 0.53748 0.11797  0.11060  -0.10823 49  ARG B CG  
1849 C  CG  B ARG B 50  ? 0.56783 0.65544 0.54825 0.11890  0.11484  -0.11188 49  ARG B CG  
1850 C  CD  A ARG B 50  ? 0.56375 0.66773 0.59213 0.13894  0.10335  -0.09949 49  ARG B CD  
1851 C  CD  B ARG B 50  ? 0.56896 0.67035 0.59558 0.14103  0.10474  -0.10275 49  ARG B CD  
1852 N  NE  A ARG B 50  ? 0.50495 0.58235 0.53456 0.12754  0.08117  -0.07372 49  ARG B NE  
1853 N  NE  B ARG B 50  ? 0.57316 0.61394 0.59473 0.14563  0.08244  -0.09008 49  ARG B NE  
1854 C  CZ  A ARG B 50  ? 0.52869 0.54874 0.54736 0.13436  0.06510  -0.06819 49  ARG B CZ  
1855 C  CZ  B ARG B 50  ? 0.53434 0.57051 0.55923 0.13181  0.06597  -0.06522 49  ARG B CZ  
1856 N  NH1 A ARG B 50  ? 0.55258 0.52826 0.56058 0.15118  0.06590  -0.08518 49  ARG B NH1 
1857 N  NH1 B ARG B 50  ? 0.50945 0.58946 0.54420 0.11296  0.06663  -0.05176 49  ARG B NH1 
1858 N  NH2 A ARG B 50  ? 0.55158 0.55800 0.56757 0.12243  0.04831  -0.04626 49  ARG B NH2 
1859 N  NH2 B ARG B 50  ? 0.53925 0.52591 0.55518 0.13512  0.04874  -0.05435 49  ARG B NH2 
1860 N  N   . LEU B 51  ? 0.43604 0.43280 0.32819 0.05046  0.08284  -0.07291 50  LEU B N   
1861 C  CA  . LEU B 51  ? 0.41997 0.36717 0.29414 0.04645  0.07003  -0.07287 50  LEU B CA  
1862 C  C   . LEU B 51  ? 0.40202 0.34377 0.24091 0.02782  0.07045  -0.07883 50  LEU B C   
1863 O  O   . LEU B 51  ? 0.47385 0.38114 0.29536 0.02602  0.06527  -0.09151 50  LEU B O   
1864 C  CB  . LEU B 51  ? 0.37023 0.30560 0.25459 0.03994  0.05537  -0.04980 50  LEU B CB  
1865 C  CG  . LEU B 51  ? 0.40104 0.33806 0.31384 0.05733  0.05125  -0.04469 50  LEU B CG  
1866 C  CD1 . LEU B 51  ? 0.38420 0.31256 0.29950 0.04981  0.03817  -0.02540 50  LEU B CD1 
1867 C  CD2 . LEU B 51  ? 0.44481 0.34919 0.36219 0.07653  0.04955  -0.05720 50  LEU B CD2 
1868 N  N   . ILE B 52  ? 0.39269 0.36729 0.21963 0.01183  0.07443  -0.06854 51  ILE B N   
1869 C  CA  . ILE B 52  ? 0.47362 0.45017 0.26418 -0.00571 0.07348  -0.07292 51  ILE B CA  
1870 C  C   . ILE B 52  ? 0.53741 0.51215 0.30621 0.00177  0.08661  -0.10539 51  ILE B C   
1871 O  O   . ILE B 52  ? 0.55878 0.51085 0.29788 -0.00781 0.08037  -0.11892 51  ILE B O   
1872 C  CB  . ILE B 52  ? 0.43515 0.44677 0.21640 -0.02364 0.07443  -0.05165 51  ILE B CB  
1873 C  CG1 . ILE B 52  ? 0.44341 0.44132 0.23858 -0.03041 0.05673  -0.02475 51  ILE B CG1 
1874 C  CG2 . ILE B 52  ? 0.54142 0.56699 0.28006 -0.04047 0.07692  -0.05812 51  ILE B CG2 
1875 C  CD1 . ILE B 52  ? 0.46764 0.48709 0.26284 -0.04485 0.05437  -0.00062 51  ILE B CD1 
1876 N  N   . GLU B 53  ? 0.49147 0.49240 0.27573 0.01943  0.10461  -0.12073 52  GLU B N   
1877 C  CA  . GLU B 53  ? 0.56318 0.56228 0.32963 0.03299  0.11865  -0.15635 52  GLU B CA  
1878 C  C   . GLU B 53  ? 0.58783 0.52339 0.35217 0.04605  0.10835  -0.17734 52  GLU B C   
1879 O  O   . GLU B 53  ? 0.63738 0.55086 0.37684 0.04838  0.10512  -0.19879 52  GLU B O   
1880 C  CB  . GLU B 53  ? 0.56584 0.60758 0.36236 0.05422  0.13790  -0.16317 52  GLU B CB  
1881 C  CG  . GLU B 53  ? 0.71244 0.74542 0.49758 0.07288  0.15053  -0.19252 52  GLU B CG  
1882 C  CD  . GLU B 53  ? 0.88593 0.95029 0.63407 0.05583  0.15995  -0.19438 52  GLU B CD  
1883 O  OE1 . GLU B 53  ? 0.98853 1.06679 0.73215 0.07063  0.17708  -0.21645 52  GLU B OE1 
1884 O  OE2 . GLU B 53  ? 0.92806 1.00369 0.65295 0.02829  0.14998  -0.17305 52  GLU B OE2 
1885 N  N   . ARG B 54  ? 0.61739 0.52213 0.41179 0.05456  0.09465  -0.16031 53  ARG B N   
1886 C  CA  . ARG B 54  ? 0.60771 0.44793 0.40049 0.06096  0.08101  -0.17019 53  ARG B CA  
1887 C  C   . ARG B 54  ? 0.61964 0.43187 0.38525 0.03176  0.06446  -0.16160 53  ARG B C   
1888 O  O   . ARG B 54  ? 0.67625 0.43545 0.43029 0.02851  0.05386  -0.17477 53  ARG B O   
1889 C  CB  . ARG B 54  ? 0.63791 0.46131 0.46844 0.07685  0.07158  -0.15001 53  ARG B CB  
1890 C  CG  . ARG B 54  ? 0.70943 0.55811 0.57334 0.10895  0.08340  -0.15978 53  ARG B CG  
1891 C  CD  . ARG B 54  ? 0.76631 0.58167 0.65965 0.12683  0.06870  -0.14465 53  ARG B CD  
1892 N  NE  . ARG B 54  ? 0.84407 0.58851 0.72741 0.13712  0.05864  -0.16075 53  ARG B NE  
1893 C  CZ  . ARG B 54  ? 0.82526 0.52832 0.72751 0.14614  0.04180  -0.14402 53  ARG B CZ  
1894 N  NH1 . ARG B 54  ? 0.77368 0.49697 0.69749 0.15134  0.03416  -0.11575 53  ARG B NH1 
1895 N  NH2 . ARG B 54  ? 0.81594 0.46325 0.71672 0.14444  0.03187  -0.15212 53  ARG B NH2 
1896 N  N   . GLY B 55  ? 0.55892 0.40519 0.31663 0.01042  0.06048  -0.13946 54  GLY B N   
1897 C  CA  . GLY B 55  ? 0.60756 0.44149 0.34692 -0.01533 0.04428  -0.12961 54  GLY B CA  
1898 C  C   . GLY B 55  ? 0.60544 0.43297 0.36899 -0.02193 0.03106  -0.10087 54  GLY B C   
1899 O  O   . GLY B 55  ? 0.58710 0.41779 0.34340 -0.04225 0.01849  -0.09017 54  GLY B O   
1900 N  N   . SER B 56  ? 0.49168 0.31717 0.28366 -0.00560 0.03355  -0.08851 55  SER B N   
1901 C  CA  . SER B 56  ? 0.47110 0.28828 0.28076 -0.01070 0.02316  -0.06585 55  SER B CA  
1902 C  C   . SER B 56  ? 0.42854 0.28334 0.25293 -0.01070 0.02354  -0.04495 55  SER B C   
1903 O  O   . SER B 56  ? 0.43566 0.29327 0.27852 -0.00097 0.02339  -0.03315 55  SER B O   
1904 C  CB  . SER B 56  ? 0.49555 0.27994 0.32053 0.00551  0.02192  -0.06530 55  SER B CB  
1905 O  OG  . SER B 56  ? 0.50015 0.30078 0.34114 0.02871  0.03174  -0.07060 55  SER B OG  
1906 N  N   . HIS B 57  ? 0.39528 0.27581 0.20941 -0.02183 0.02183  -0.04037 56  HIS B N   
1907 C  CA  . HIS B 57  ? 0.37912 0.28617 0.20540 -0.01991 0.02094  -0.02321 56  HIS B CA  
1908 C  C   . HIS B 57  ? 0.35967 0.28275 0.17741 -0.03367 0.01065  -0.01337 56  HIS B C   
1909 O  O   . HIS B 57  ? 0.43351 0.36175 0.22850 -0.04472 0.00878  -0.02024 56  HIS B O   
1910 C  CB  . HIS B 57  ? 0.39625 0.32013 0.22200 -0.01349 0.03153  -0.02651 56  HIS B CB  
1911 C  CG  . HIS B 57  ? 0.37613 0.31464 0.21839 -0.01099 0.02969  -0.01033 56  HIS B CG  
1912 N  ND1 . HIS B 57  ? 0.37941 0.32393 0.22120 -0.01824 0.02006  0.00502  56  HIS B ND1 
1913 C  CD2 . HIS B 57  ? 0.36578 0.31187 0.22574 -0.00250 0.03411  -0.00822 56  HIS B CD2 
1914 C  CE1 . HIS B 57  ? 0.37094 0.31863 0.22656 -0.01498 0.01895  0.01404  56  HIS B CE1 
1915 N  NE2 . HIS B 57  ? 0.37232 0.32361 0.23864 -0.00761 0.02713  0.00642  56  HIS B NE2 
1916 N  N   . TRP B 58  ? 0.36610 0.29934 0.20174 -0.03148 0.00341  0.00135  57  TRP B N   
1917 C  CA  . TRP B 58  ? 0.33249 0.28479 0.16953 -0.03937 -0.00883 0.01215  57  TRP B CA  
1918 C  C   . TRP B 58  ? 0.32893 0.29039 0.18218 -0.02839 -0.01330 0.02641  57  TRP B C   
1919 O  O   . TRP B 58  ? 0.35226 0.30564 0.21786 -0.01713 -0.00785 0.02618  57  TRP B O   
1920 C  CB  . TRP B 58  ? 0.35735 0.31672 0.20658 -0.04644 -0.01466 0.01314  57  TRP B CB  
1921 C  CG  . TRP B 58  ? 0.38766 0.32561 0.22073 -0.05959 -0.01341 -0.00064 57  TRP B CG  
1922 C  CD1 . TRP B 58  ? 0.44251 0.37958 0.25554 -0.07718 -0.02154 -0.00908 57  TRP B CD1 
1923 C  CD2 . TRP B 58  ? 0.37123 0.27928 0.20442 -0.05607 -0.00610 -0.00836 57  TRP B CD2 
1924 N  NE1 . TRP B 58  ? 0.47116 0.37402 0.27201 -0.08473 -0.01921 -0.02459 57  TRP B NE1 
1925 C  CE2 . TRP B 58  ? 0.39472 0.27795 0.20898 -0.07070 -0.01017 -0.02261 57  TRP B CE2 
1926 C  CE3 . TRP B 58  ? 0.36834 0.26610 0.21407 -0.04228 0.00103  -0.00415 57  TRP B CE3 
1927 C  CZ2 . TRP B 58  ? 0.44356 0.28592 0.25399 -0.06953 -0.00778 -0.03149 57  TRP B CZ2 
1928 C  CZ3 . TRP B 58  ? 0.40411 0.26805 0.24556 -0.04150 0.00291  -0.00999 57  TRP B CZ3 
1929 C  CH2 . TRP B 58  ? 0.44666 0.28030 0.27205 -0.05400 -0.00171 -0.02290 57  TRP B CH2 
1930 N  N   . LEU B 59  ? 0.33139 0.30727 0.18459 -0.03150 -0.02593 0.03851  58  LEU B N   
1931 C  CA  . LEU B 59  ? 0.34832 0.32358 0.21864 -0.01845 -0.03351 0.05141  58  LEU B CA  
1932 C  C   . LEU B 59  ? 0.35750 0.35541 0.24489 -0.01406 -0.04885 0.06189  58  LEU B C   
1933 O  O   . LEU B 59  ? 0.34129 0.35947 0.22281 -0.02651 -0.05646 0.06322  58  LEU B O   
1934 C  CB  . LEU B 59  ? 0.34099 0.30367 0.19536 -0.02358 -0.03545 0.06183  58  LEU B CB  
1935 C  CG  . LEU B 59  ? 0.34329 0.31645 0.17020 -0.04018 -0.04333 0.07288  58  LEU B CG  
1936 C  CD1 . LEU B 59  ? 0.37407 0.35684 0.20611 -0.03867 -0.06565 0.09373  58  LEU B CD1 
1937 C  CD2 . LEU B 59  ? 0.44672 0.41317 0.25445 -0.05061 -0.03592 0.07993  58  LEU B CD2 
1938 N  N   . ALA B 60  ? 0.32634 0.32153 0.23694 0.00493  -0.05461 0.06775  59  ALA B N   
1939 C  CA  . ALA B 60  ? 0.31087 0.32791 0.24512 0.01709  -0.07094 0.07911  59  ALA B CA  
1940 C  C   . ALA B 60  ? 0.35869 0.35367 0.28510 0.02017  -0.08768 0.09848  59  ALA B C   
1941 O  O   . ALA B 60  ? 0.40016 0.36053 0.31977 0.02340  -0.08519 0.09985  59  ALA B O   
1942 C  CB  . ALA B 60  ? 0.35905 0.38743 0.32644 0.04128  -0.06569 0.06953  59  ALA B CB  
1943 N  N   . GLU B 61  ? 0.38624 0.40095 0.31323 0.01672  -0.10685 0.11565  60  GLU B N   
1944 C  CA  . GLU B 61  ? 0.39603 0.38879 0.31376 0.01808  -0.12691 0.14069  60  GLU B CA  
1945 C  C   . GLU B 61  ? 0.41895 0.42714 0.37369 0.04332  -0.14916 0.15390  60  GLU B C   
1946 O  O   . GLU B 61  ? 0.44567 0.49948 0.42632 0.04989  -0.15183 0.14838  60  GLU B O   
1947 C  CB  . GLU B 61  ? 0.44784 0.44897 0.32344 -0.01081 -0.13356 0.15507  60  GLU B CB  
1948 C  CG  . GLU B 61  ? 0.46385 0.50837 0.33717 -0.02160 -0.14356 0.15468  60  GLU B CG  
1949 C  CD  . GLU B 61  ? 0.56767 0.61567 0.39972 -0.04736 -0.14087 0.15510  60  GLU B CD  
1950 O  OE1 . GLU B 61  ? 0.64908 0.67535 0.45532 -0.05784 -0.12721 0.15390  60  GLU B OE1 
1951 O  OE2 . GLU B 61  ? 0.64797 0.72459 0.47577 -0.05715 -0.15225 0.15607  60  GLU B OE2 
1952 N  N   . ASP B 62  ? 0.45469 0.42539 0.41433 0.05716  -0.16425 0.17032  61  ASP B N   
1953 C  CA  . ASP B 62  ? 0.50096 0.48062 0.49598 0.08589  -0.18136 0.17773  61  ASP B CA  
1954 C  C   . ASP B 62  ? 0.52628 0.53118 0.50751 0.07230  -0.19748 0.19680  61  ASP B C   
1955 O  O   . ASP B 62  ? 0.52845 0.54635 0.47357 0.04103  -0.19361 0.20012  61  ASP B O   
1956 C  CB  . ASP B 62  ? 0.57738 0.50080 0.58153 0.10618  -0.18381 0.17827  61  ASP B CB  
1957 C  CG  . ASP B 62  ? 0.66734 0.54942 0.63693 0.08303  -0.18953 0.19907  61  ASP B CG  
1958 O  OD1 . ASP B 62  ? 0.64207 0.54250 0.58343 0.05777  -0.19366 0.21448  61  ASP B OD1 
1959 O  OD2 . ASP B 62  ? 0.72536 0.55744 0.69699 0.08887  -0.18977 0.19857  61  ASP B OD2 
1960 N  N   . ALA B 63  ? 0.55193 0.56314 0.56139 0.09787  -0.21556 0.20736  62  ALA B N   
1961 C  CA  . ALA B 63  ? 0.69074 0.72630 0.69075 0.08862  -0.23493 0.22669  62  ALA B CA  
1962 C  C   . ALA B 63  ? 0.74778 0.75012 0.69965 0.05942  -0.23711 0.24558  62  ALA B C   
1963 O  O   . ALA B 63  ? 0.79372 0.82127 0.72164 0.03790  -0.24592 0.25652  62  ALA B O   
1964 C  CB  . ALA B 63  ? 0.69419 0.73677 0.73524 0.12687  -0.25420 0.23526  62  ALA B CB  
1965 N  N   . ASP B 64  ? 0.80608 0.75618 0.74471 0.05658  -0.22922 0.24890  63  ASP B N   
1966 C  CA  . ASP B 64  ? 0.79137 0.71660 0.68962 0.02712  -0.22927 0.26714  63  ASP B CA  
1967 C  C   . ASP B 64  ? 0.72468 0.66321 0.58704 -0.00572 -0.20714 0.25494  63  ASP B C   
1968 O  O   . ASP B 64  ? 0.74672 0.67431 0.57754 -0.03077 -0.20285 0.26674  63  ASP B O   
1969 C  CB  . ASP B 64  ? 0.91959 0.78593 0.82321 0.03474  -0.23200 0.27650  63  ASP B CB  
1970 C  CG  . ASP B 64  ? 1.02605 0.87172 0.96434 0.07074  -0.25264 0.28610  63  ASP B CG  
1971 O  OD1 . ASP B 64  ? 1.07122 0.89545 1.04032 0.09874  -0.24783 0.26880  63  ASP B OD1 
1972 O  OD2 . ASP B 64  ? 1.07117 0.92342 1.00580 0.07236  -0.27331 0.30973  63  ASP B OD2 
1973 N  N   . GLY B 65  ? 0.58671 0.55068 0.45401 -0.00580 -0.19279 0.23171  64  GLY B N   
1974 C  CA  . GLY B 65  ? 0.60100 0.57274 0.43677 -0.03141 -0.17063 0.21713  64  GLY B CA  
1975 C  C   . GLY B 65  ? 0.65748 0.59738 0.49362 -0.03201 -0.15375 0.20820  64  GLY B C   
1976 O  O   . GLY B 65  ? 0.63079 0.57831 0.44306 -0.05112 -0.13459 0.19675  64  GLY B O   
1977 N  N   . GLN B 66  ? 0.63893 0.54471 0.50267 -0.01048 -0.15999 0.21016  65  GLN B N   
1978 C  CA  . GLN B 66  ? 0.59984 0.47500 0.46226 -0.01507 -0.14597 0.20113  65  GLN B CA  
1979 C  C   . GLN B 66  ? 0.55996 0.44225 0.43588 -0.00266 -0.13375 0.17775  65  GLN B C   
1980 O  O   . GLN B 66  ? 0.53352 0.42319 0.43770 0.02232  -0.14139 0.17061  65  GLN B O   
1981 C  CB  . GLN B 66  ? 0.65331 0.48102 0.53406 -0.00190 -0.15827 0.21031  65  GLN B CB  
1982 C  CG  . GLN B 66  ? 0.81241 0.62703 0.68366 -0.01027 -0.17566 0.23753  65  GLN B CG  
1983 C  CD  . GLN B 66  ? 0.91571 0.73919 0.75290 -0.04651 -0.16773 0.25110  65  GLN B CD  
1984 O  OE1 . GLN B 66  ? 0.85195 0.68556 0.67716 -0.06342 -0.14855 0.23938  65  GLN B OE1 
1985 N  NE2 . GLN B 66  ? 0.98996 0.81300 0.81279 -0.05758 -0.18265 0.27648  65  GLN B NE2 
1986 N  N   . PRO B 67  ? 0.34720 0.40635 0.36208 -0.02739 0.00065  0.10945  66  PRO B N   
1987 C  CA  . PRO B 67  ? 0.30877 0.35571 0.32019 -0.02212 0.00451  0.08770  66  PRO B CA  
1988 C  C   . PRO B 67  ? 0.33151 0.35010 0.35742 -0.01917 0.00187  0.08216  66  PRO B C   
1989 O  O   . PRO B 67  ? 0.32852 0.33575 0.36799 -0.02405 -0.00240 0.09129  66  PRO B O   
1990 C  CB  . PRO B 67  ? 0.33365 0.39402 0.33717 -0.02693 0.00976  0.08279  66  PRO B CB  
1991 C  CG  . PRO B 67  ? 0.40280 0.48976 0.39691 -0.03141 0.01193  0.09623  66  PRO B CG  
1992 C  CD  . PRO B 67  ? 0.37767 0.46009 0.38267 -0.03469 0.00547  0.11706  66  PRO B CD  
1993 N  N   . VAL B 68  ? 0.31988 0.32721 0.34286 -0.01117 0.00431  0.06727  67  VAL B N   
1994 C  CA  . VAL B 68  ? 0.28428 0.26549 0.31444 -0.00614 0.00391  0.05718  67  VAL B CA  
1995 C  C   . VAL B 68  ? 0.32413 0.29919 0.33994 -0.00330 0.00864  0.03888  67  VAL B C   
1996 O  O   . VAL B 68  ? 0.33552 0.28983 0.35082 0.00104  0.00897  0.02835  67  VAL B O   
1997 C  CB  . VAL B 68  ? 0.27872 0.25137 0.32192 0.00267  0.00355  0.05914  67  VAL B CB  
1998 C  CG1 . VAL B 68  ? 0.31730 0.29285 0.37672 -0.00003 -0.00359 0.07912  67  VAL B CG1 
1999 C  CG2 . VAL B 68  ? 0.33043 0.31756 0.36759 0.00813  0.00859  0.05369  67  VAL B CG2 
2000 N  N   . GLY B 69  ? 0.27663 0.26809 0.27987 -0.00510 0.01180  0.03449  68  GLY B N   
2001 C  CA  . GLY B 69  ? 0.25650 0.24230 0.24736 -0.00274 0.01491  0.02024  68  GLY B CA  
2002 C  C   . GLY B 69  ? 0.24773 0.25229 0.23042 -0.00535 0.01625  0.01856  68  GLY B C   
2003 O  O   . GLY B 69  ? 0.26802 0.28982 0.25166 -0.00730 0.01606  0.02587  68  GLY B O   
2004 N  N   . PHE B 70  ? 0.27824 0.27865 0.25231 -0.00521 0.01669  0.00873  69  PHE B N   
2005 C  CA  . PHE B 70  ? 0.26956 0.28547 0.23926 -0.00641 0.01723  0.00581  69  PHE B CA  
2006 C  C   . PHE B 70  ? 0.28551 0.29355 0.24718 -0.00433 0.01702  -0.00376 69  PHE B C   
2007 O  O   . PHE B 70  ? 0.27183 0.26409 0.22790 -0.00341 0.01619  -0.00781 69  PHE B O   
2008 C  CB  . PHE B 70  ? 0.25550 0.28368 0.23075 -0.01149 0.01602  0.01035  69  PHE B CB  
2009 C  CG  . PHE B 70  ? 0.25641 0.27444 0.23534 -0.01465 0.01196  0.00733  69  PHE B CG  
2010 C  CD1 . PHE B 70  ? 0.25423 0.27235 0.22998 -0.01367 0.01003  -0.00064 69  PHE B CD1 
2011 C  CD2 . PHE B 70  ? 0.27357 0.28129 0.26113 -0.01909 0.00800  0.01307  69  PHE B CD2 
2012 C  CE1 . PHE B 70  ? 0.26308 0.27304 0.24283 -0.01711 0.00376  -0.00268 69  PHE B CE1 
2013 C  CE2 . PHE B 70  ? 0.28439 0.28218 0.27591 -0.02304 0.00151  0.00948  69  PHE B CE2 
2014 C  CZ  . PHE B 70  ? 0.30560 0.30543 0.29274 -0.02219 -0.00085 0.00193  69  PHE B CZ  
2015 N  N   . LEU B 71  ? 0.25296 0.27165 0.21316 -0.00355 0.01702  -0.00733 70  LEU B N   
2016 C  CA  . LEU B 71  ? 0.25870 0.27149 0.21433 -0.00229 0.01513  -0.01381 70  LEU B CA  
2017 C  C   . LEU B 71  ? 0.26173 0.28669 0.22243 -0.00234 0.01307  -0.01737 70  LEU B C   
2018 O  O   . LEU B 71  ? 0.25216 0.28971 0.21447 -0.00098 0.01446  -0.01911 70  LEU B O   
2019 C  CB  . LEU B 71  ? 0.25920 0.26979 0.21280 -0.00011 0.01679  -0.01479 70  LEU B CB  
2020 C  CG  . LEU B 71  ? 0.25687 0.25857 0.20571 0.00023  0.01473  -0.01765 70  LEU B CG  
2021 C  CD1 . LEU B 71  ? 0.30363 0.30312 0.25283 0.00093  0.01831  -0.01462 70  LEU B CD1 
2022 C  CD2 . LEU B 71  ? 0.27225 0.27901 0.22648 0.00057  0.00962  -0.02216 70  LEU B CD2 
2023 N  N   . ALA B 72  ? 0.26099 0.28277 0.22450 -0.00334 0.00935  -0.01917 71  ALA B N   
2024 C  CA  . ALA B 72  ? 0.25157 0.28585 0.22477 -0.00188 0.00792  -0.02280 71  ALA B CA  
2025 C  C   . ALA B 72  ? 0.26170 0.28696 0.23469 0.00089  0.00270  -0.02764 71  ALA B C   
2026 O  O   . ALA B 72  ? 0.26550 0.27687 0.23243 -0.00075 -0.00208 -0.02588 71  ALA B O   
2027 C  CB  . ALA B 72  ? 0.24024 0.27942 0.22339 -0.00553 0.00566  -0.01903 71  ALA B CB  
2028 N  N   . ALA B 73  ? 0.25372 0.28593 0.23249 0.00512  0.00277  -0.03374 72  ALA B N   
2029 C  CA  . ALA B 73  ? 0.26103 0.28268 0.24310 0.00756  -0.00360 -0.03674 72  ALA B CA  
2030 C  C   . ALA B 73  ? 0.27529 0.30666 0.27291 0.01328  -0.00565 -0.04425 72  ALA B C   
2031 O  O   . ALA B 73  ? 0.29304 0.34163 0.29599 0.01613  0.00021  -0.04890 72  ALA B O   
2032 C  CB  . ALA B 73  ? 0.26028 0.27386 0.23720 0.00735  -0.00375 -0.03727 72  ALA B CB  
2033 N  N   . GLU B 74  ? 0.26311 0.28419 0.26863 0.01555  -0.01369 -0.04485 73  GLU B N   
2034 C  CA  . GLU B 74  ? 0.26392 0.29327 0.28894 0.02281  -0.01626 -0.05248 73  GLU B CA  
2035 C  C   . GLU B 74  ? 0.27263 0.28598 0.30493 0.02606  -0.02504 -0.05501 73  GLU B C   
2036 O  O   . GLU B 74  ? 0.31807 0.31610 0.34572 0.02196  -0.03239 -0.04581 73  GLU B O   
2037 C  CB  . GLU B 74  ? 0.34006 0.37690 0.37825 0.02263  -0.02004 -0.04793 73  GLU B CB  
2038 C  CG  . GLU B 74  ? 0.35243 0.40382 0.41557 0.03172  -0.01973 -0.05613 73  GLU B CG  
2039 C  CD  . GLU B 74  ? 0.40127 0.46580 0.48349 0.03117  -0.02297 -0.05068 73  GLU B CD  
2040 O  OE1 . GLU B 74  ? 0.44384 0.50132 0.51791 0.02307  -0.02880 -0.04118 73  GLU B OE1 
2041 O  OE2 . GLU B 74  ? 0.48163 0.56384 0.58804 0.03913  -0.02000 -0.05662 73  GLU B OE2 
2042 N  N   . ARG B 75  ? 0.26792 0.28420 0.31102 0.03336  -0.02466 -0.06735 74  ARG B N   
2043 C  CA  . ARG B 75  ? 0.28710 0.28604 0.34291 0.03685  -0.03500 -0.07019 74  ARG B CA  
2044 C  C   . ARG B 75  ? 0.30820 0.30600 0.38496 0.04205  -0.04304 -0.06758 74  ARG B C   
2045 O  O   . ARG B 75  ? 0.32730 0.34189 0.41966 0.04953  -0.03913 -0.07499 74  ARG B O   
2046 C  CB  . ARG B 75  ? 0.30425 0.30402 0.36478 0.04359  -0.03363 -0.08707 74  ARG B CB  
2047 C  CG  . ARG B 75  ? 0.37286 0.35316 0.45246 0.04890  -0.04560 -0.09353 74  ARG B CG  
2048 C  CD  . ARG B 75  ? 0.39260 0.35262 0.46729 0.03979  -0.05355 -0.08337 74  ARG B CD  
2049 N  NE  . ARG B 75  ? 0.41165 0.35143 0.50617 0.04341  -0.06598 -0.08950 74  ARG B NE  
2050 C  CZ  . ARG B 75  ? 0.40270 0.33389 0.49932 0.04405  -0.06997 -0.10235 74  ARG B CZ  
2051 N  NH1 . ARG B 75  ? 0.40167 0.34455 0.47999 0.04134  -0.06262 -0.10968 74  ARG B NH1 
2052 N  NH2 . ARG B 75  ? 0.40978 0.31921 0.52767 0.04678  -0.08328 -0.10698 74  ARG B NH2 
2053 N  N   . CYS B 76  ? 0.30897 0.28867 0.38724 0.03806  -0.05434 -0.05565 75  CYS B N   
2054 C  CA  . CYS B 76  ? 0.33013 0.30637 0.42678 0.04145  -0.06552 -0.04921 75  CYS B CA  
2055 C  C   . CYS B 76  ? 0.34064 0.29457 0.44906 0.04259  -0.07791 -0.04518 75  CYS B C   
2056 O  O   . CYS B 76  ? 0.35237 0.29172 0.44597 0.03386  -0.08207 -0.03196 75  CYS B O   
2057 C  CB  . CYS B 76  ? 0.32648 0.30241 0.40760 0.03309  -0.06929 -0.03440 75  CYS B CB  
2058 S  SG  . CYS B 76  ? 0.37625 0.37302 0.44599 0.02932  -0.05796 -0.03643 75  CYS B SG  
2059 N  N   . ALA B 77  ? 0.34395 0.29556 0.48042 0.05355  -0.08328 -0.05618 76  ALA B N   
2060 C  CA  . ALA B 77  ? 0.39412 0.32195 0.54634 0.05523  -0.09587 -0.05447 76  ALA B CA  
2061 C  C   . ALA B 77  ? 0.41446 0.33085 0.55096 0.04748  -0.09300 -0.05527 76  ALA B C   
2062 O  O   . ALA B 77  ? 0.42794 0.35254 0.55852 0.05036  -0.08399 -0.07151 76  ALA B O   
2063 C  CB  . ALA B 77  ? 0.43762 0.35135 0.59535 0.05054  -0.11108 -0.03304 76  ALA B CB  
2064 N  N   . ASP B 78  ? 0.35076 0.25006 0.48132 0.03749  -0.10072 -0.03734 77  ASP B N   
2065 C  CA  . ASP B 78  ? 0.38743 0.27837 0.51020 0.02989  -0.09862 -0.03717 77  ASP B CA  
2066 C  C   . ASP B 78  ? 0.36810 0.26994 0.46156 0.01961  -0.08687 -0.02678 77  ASP B C   
2067 O  O   . ASP B 78  ? 0.35881 0.25496 0.44784 0.01143  -0.08586 -0.01996 77  ASP B O   
2068 C  CB  . ASP B 78  ? 0.47806 0.34449 0.61869 0.02491  -0.11332 -0.02415 77  ASP B CB  
2069 C  CG  . ASP B 78  ? 0.59482 0.45564 0.72633 0.01651  -0.11868 0.00284  77  ASP B CG  
2070 O  OD1 . ASP B 78  ? 0.52256 0.39553 0.63732 0.01683  -0.11445 0.00832  77  ASP B OD1 
2071 O  OD2 . ASP B 78  ? 0.70657 0.54990 0.84859 0.00933  -0.12854 0.01878  77  ASP B OD2 
2072 N  N   . GLU B 79  ? 0.30333 0.22080 0.37998 0.02014  -0.07836 -0.02592 78  GLU B N   
2073 C  CA  . GLU B 79  ? 0.30110 0.22626 0.35132 0.01191  -0.06804 -0.01666 78  GLU B CA  
2074 C  C   . GLU B 79  ? 0.31940 0.26286 0.35887 0.01479  -0.05619 -0.02862 78  GLU B C   
2075 O  O   . GLU B 79  ? 0.34376 0.29732 0.39178 0.02183  -0.05531 -0.03870 78  GLU B O   
2076 C  CB  . GLU B 79  ? 0.31033 0.23245 0.34562 0.00741  -0.07104 -0.00043 78  GLU B CB  
2077 C  CG  . GLU B 79  ? 0.34514 0.25056 0.38594 0.00258  -0.08211 0.01680  78  GLU B CG  
2078 C  CD  . GLU B 79  ? 0.39013 0.29294 0.41083 -0.00181 -0.08644 0.03308  78  GLU B CD  
2079 O  OE1 . GLU B 79  ? 0.39134 0.29943 0.41005 0.00204  -0.09085 0.02964  78  GLU B OE1 
2080 O  OE2 . GLU B 79  ? 0.41247 0.30836 0.42032 -0.00945 -0.08645 0.05010  78  GLU B OE2 
2081 N  N   . LEU B 80  ? 0.28249 0.23144 0.30524 0.00918  -0.04679 -0.02568 79  LEU B N   
2082 C  CA  . LEU B 80  ? 0.28099 0.24555 0.29183 0.01017  -0.03634 -0.03201 79  LEU B CA  
2083 C  C   . LEU B 80  ? 0.31015 0.27516 0.30350 0.00626  -0.03304 -0.02236 79  LEU B C   
2084 O  O   . LEU B 80  ? 0.30804 0.26742 0.28801 0.00114  -0.02993 -0.01281 79  LEU B O   
2085 C  CB  . LEU B 80  ? 0.25783 0.22784 0.26405 0.00769  -0.03000 -0.03552 79  LEU B CB  
2086 C  CG  . LEU B 80  ? 0.27863 0.26477 0.27611 0.00956  -0.02117 -0.04182 79  LEU B CG  
2087 C  CD1 . LEU B 80  ? 0.28913 0.28542 0.29568 0.01676  -0.02136 -0.05523 79  LEU B CD1 
2088 C  CD2 . LEU B 80  ? 0.30940 0.30022 0.30052 0.00590  -0.01624 -0.04027 79  LEU B CD2 
2089 N  N   . HIS B 81  ? 0.27389 0.24528 0.26874 0.00881  -0.03449 -0.02504 80  HIS B N   
2090 C  CA  . HIS B 81  ? 0.29688 0.26651 0.27538 0.00498  -0.03426 -0.01864 80  HIS B CA  
2091 C  C   . HIS B 81  ? 0.31938 0.29746 0.28805 0.00342  -0.02420 -0.02189 80  HIS B C   
2092 O  O   . HIS B 81  ? 0.29798 0.28884 0.27623 0.00590  -0.02013 -0.02842 80  HIS B O   
2093 C  CB  . HIS B 81  ? 0.30307 0.27577 0.29209 0.00709  -0.04316 -0.01895 80  HIS B CB  
2094 C  CG  . HIS B 81  ? 0.32311 0.29076 0.29470 0.00234  -0.04702 -0.01342 80  HIS B CG  
2095 N  ND1 . HIS B 81  ? 0.30642 0.26047 0.25796 -0.00144 -0.05213 -0.00463 80  HIS B ND1 
2096 C  CD2 . HIS B 81  ? 0.30112 0.27481 0.27136 0.00034  -0.04727 -0.01578 80  HIS B CD2 
2097 C  CE1 . HIS B 81  ? 0.30980 0.26064 0.24546 -0.00474 -0.05593 -0.00417 80  HIS B CE1 
2098 N  NE2 . HIS B 81  ? 0.32148 0.28300 0.27012 -0.00415 -0.05396 -0.01088 80  HIS B NE2 
2099 N  N   . ILE B 82  ? 0.26439 0.23563 0.21402 -0.00021 -0.02010 -0.01692 81  ILE B N   
2100 C  CA  . ILE B 82  ? 0.28047 0.25615 0.22274 -0.00115 -0.01212 -0.01920 81  ILE B CA  
2101 C  C   . ILE B 82  ? 0.28451 0.25750 0.22208 -0.00299 -0.01744 -0.01991 81  ILE B C   
2102 O  O   . ILE B 82  ? 0.32726 0.28867 0.24797 -0.00504 -0.02146 -0.01759 81  ILE B O   
2103 C  CB  . ILE B 82  ? 0.30595 0.27622 0.23458 -0.00225 -0.00420 -0.01547 81  ILE B CB  
2104 C  CG1 . ILE B 82  ? 0.30749 0.28215 0.24649 -0.00195 -0.00126 -0.01371 81  ILE B CG1 
2105 C  CG2 . ILE B 82  ? 0.31791 0.29016 0.24201 -0.00195 0.00240  -0.01795 81  ILE B CG2 
2106 C  CD1 . ILE B 82  ? 0.37803 0.34902 0.30844 -0.00359 0.00551  -0.00658 81  ILE B CD1 
2107 N  N   . ALA B 83  ? 0.26959 0.25430 0.22217 -0.00270 -0.01794 -0.02290 82  ALA B N   
2108 C  CA  . ALA B 83  ? 0.33910 0.32365 0.29477 -0.00582 -0.02475 -0.02259 82  ALA B CA  
2109 C  C   . ALA B 83  ? 0.32294 0.29884 0.26608 -0.00917 -0.02219 -0.02297 82  ALA B C   
2110 O  O   . ALA B 83  ? 0.34103 0.30561 0.27472 -0.01240 -0.03023 -0.02385 82  ALA B O   
2111 C  CB  . ALA B 83  ? 0.29384 0.29758 0.27392 -0.00472 -0.02424 -0.02368 82  ALA B CB  
2112 N  N   . GLU B 84  ? 0.30422 0.28424 0.24795 -0.00818 -0.01267 -0.02281 83  GLU B N   
2113 C  CA  . GLU B 84  ? 0.32091 0.29227 0.25847 -0.01011 -0.01050 -0.02307 83  GLU B CA  
2114 C  C   . GLU B 84  ? 0.31185 0.28513 0.24702 -0.00694 -0.00043 -0.02180 83  GLU B C   
2115 O  O   . GLU B 84  ? 0.30806 0.29507 0.25250 -0.00558 0.00386  -0.01974 83  GLU B O   
2116 C  CB  . GLU B 84  ? 0.31091 0.29039 0.26561 -0.01460 -0.01372 -0.02020 83  GLU B CB  
2117 C  CG  . GLU B 84  ? 0.31852 0.28462 0.27017 -0.01716 -0.01441 -0.02016 83  GLU B CG  
2118 C  CD  . GLU B 84  ? 0.39758 0.34122 0.32940 -0.01707 -0.02092 -0.02739 83  GLU B CD  
2119 O  OE1 . GLU B 84  ? 0.41643 0.35595 0.34506 -0.02017 -0.03153 -0.02951 83  GLU B OE1 
2120 O  OE2 . GLU B 84  ? 0.43947 0.37007 0.35859 -0.01340 -0.01565 -0.03132 83  GLU B OE2 
2121 N  N   . LEU B 85  ? 0.31164 0.27134 0.23448 -0.00524 0.00273  -0.02387 84  LEU B N   
2122 C  CA  . LEU B 85  ? 0.29567 0.25706 0.22063 -0.00169 0.01142  -0.02199 84  LEU B CA  
2123 C  C   . LEU B 85  ? 0.30945 0.25677 0.23252 -0.00101 0.01099  -0.02463 84  LEU B C   
2124 O  O   . LEU B 85  ? 0.33330 0.26471 0.24071 0.00035  0.00925  -0.03145 84  LEU B O   
2125 C  CB  . LEU B 85  ? 0.27459 0.23480 0.18975 0.00191  0.01785  -0.02214 84  LEU B CB  
2126 C  CG  . LEU B 85  ? 0.30687 0.26853 0.22599 0.00647  0.02712  -0.02044 84  LEU B CG  
2127 C  CD1 . LEU B 85  ? 0.30298 0.27923 0.23962 0.00603  0.02780  -0.01486 84  LEU B CD1 
2128 C  CD2 . LEU B 85  ? 0.33793 0.29926 0.24752 0.00908  0.03435  -0.01960 84  LEU B CD2 
2129 N  N   . SER B 86  ? 0.27706 0.22922 0.21511 -0.00184 0.01177  -0.01932 85  SER B N   
2130 C  CA  . SER B 86  ? 0.31035 0.24691 0.25203 -0.00175 0.00901  -0.02086 85  SER B CA  
2131 C  C   . SER B 86  ? 0.31963 0.26051 0.27546 0.00126  0.01353  -0.01368 85  SER B C   
2132 O  O   . SER B 86  ? 0.31060 0.26909 0.27669 -0.00128 0.01421  -0.00446 85  SER B O   
2133 C  CB  . SER B 86  ? 0.38355 0.31861 0.33476 -0.00961 -0.00081 -0.01823 85  SER B CB  
2134 O  OG  . SER B 86  ? 0.40432 0.32673 0.34336 -0.01195 -0.00870 -0.02651 85  SER B OG  
2135 N  N   . ILE B 87  ? 0.30103 0.22607 0.25689 0.00732  0.01616  -0.01833 86  ILE B N   
2136 C  CA  . ILE B 87  ? 0.32296 0.24895 0.29628 0.01107  0.01823  -0.01086 86  ILE B CA  
2137 C  C   . ILE B 87  ? 0.31740 0.22055 0.29873 0.01093  0.01150  -0.01352 86  ILE B C   
2138 O  O   . ILE B 87  ? 0.35847 0.24125 0.32743 0.01449  0.01053  -0.02716 86  ILE B O   
2139 C  CB  . ILE B 87  ? 0.32626 0.25584 0.30011 0.02058  0.02826  -0.01348 86  ILE B CB  
2140 C  CG1 . ILE B 87  ? 0.36592 0.31566 0.33480 0.01944  0.03307  -0.01056 86  ILE B CG1 
2141 C  CG2 . ILE B 87  ? 0.31148 0.24086 0.30784 0.02537  0.02821  -0.00513 86  ILE B CG2 
2142 C  CD1 . ILE B 87  ? 0.40994 0.37932 0.38901 0.01429  0.02926  0.00042  86  ILE B CD1 
2143 N  N   . ALA B 88  ? 0.33316 0.23865 0.33422 0.00662  0.00607  -0.00042 87  ALA B N   
2144 C  CA  . ALA B 88  ? 0.34763 0.22989 0.36228 0.00543  -0.00223 -0.00017 87  ALA B CA  
2145 C  C   . ALA B 88  ? 0.36330 0.22469 0.38077 0.01785  0.00151  -0.01122 87  ALA B C   
2146 O  O   . ALA B 88  ? 0.37075 0.24193 0.38942 0.02687  0.01102  -0.01170 87  ALA B O   
2147 C  CB  . ALA B 88  ? 0.38506 0.27732 0.42169 -0.00165 -0.00764 0.02059  87  ALA B CB  
2148 N  N   . GLN B 89  ? 0.41366 0.24626 0.43425 0.01845  -0.00640 -0.02082 88  GLN B N   
2149 C  CA  . GLN B 89  ? 0.44799 0.25713 0.46783 0.03191  -0.00249 -0.03688 88  GLN B CA  
2150 C  C   . GLN B 89  ? 0.46299 0.27898 0.50539 0.04210  0.00408  -0.02829 88  GLN B C   
2151 O  O   . GLN B 89  ? 0.48830 0.30558 0.52662 0.05506  0.01582  -0.03875 88  GLN B O   
2152 C  CB  . GLN B 89  ? 0.49343 0.26831 0.52022 0.02956  -0.01595 -0.04606 88  GLN B CB  
2153 C  CG  . GLN B 89  ? 0.52495 0.28789 0.52621 0.02329  -0.02276 -0.06119 88  GLN B CG  
2154 C  CD  . GLN B 89  ? 0.50708 0.27399 0.47509 0.03263  -0.01057 -0.07838 88  GLN B CD  
2155 O  OE1 . GLN B 89  ? 0.60337 0.36201 0.56584 0.04676  -0.00006 -0.09073 88  GLN B OE1 
2156 N  NE2 . GLN B 89  ? 0.48712 0.26686 0.43430 0.02501  -0.01186 -0.07857 88  GLN B NE2 
2157 N  N   . ALA B 90  ? 0.45484 0.27639 0.52246 0.03652  -0.00351 -0.00813 89  ALA B N   
2158 C  CA  . ALA B 90  ? 0.43975 0.26451 0.53213 0.04646  -0.00081 0.00084  89  ALA B CA  
2159 C  C   . ALA B 90  ? 0.45279 0.30806 0.54217 0.05128  0.01053  0.00586  89  ALA B C   
2160 O  O   . ALA B 90  ? 0.48916 0.34952 0.60018 0.06108  0.01353  0.01148  89  ALA B O   
2161 C  CB  . ALA B 90  ? 0.45940 0.28342 0.57759 0.03796  -0.01344 0.02441  89  ALA B CB  
2162 N  N   . HIS B 91  ? 0.42435 0.29890 0.49069 0.04494  0.01574  0.00380  90  HIS B N   
2163 C  CA  . HIS B 91  ? 0.40185 0.30431 0.46738 0.04669  0.02345  0.00991  90  HIS B CA  
2164 C  C   . HIS B 91  ? 0.38966 0.29761 0.43329 0.05053  0.03508  -0.00476 90  HIS B C   
2165 O  O   . HIS B 91  ? 0.37560 0.30578 0.41824 0.04992  0.04052  0.00001  90  HIS B O   
2166 C  CB  . HIS B 91  ? 0.37142 0.29503 0.43440 0.03425  0.01673  0.02623  90  HIS B CB  
2167 C  CG  . HIS B 91  ? 0.34497 0.26521 0.42670 0.02936  0.00603  0.04368  90  HIS B CG  
2168 N  ND1 . HIS B 91  ? 0.37461 0.30167 0.47861 0.03405  0.00255  0.05758  90  HIS B ND1 
2169 C  CD2 . HIS B 91  ? 0.38124 0.29185 0.46508 0.01996  -0.00245 0.05113  90  HIS B CD2 
2170 C  CE1 . HIS B 91  ? 0.37456 0.29561 0.49100 0.02758  -0.00774 0.07372  90  HIS B CE1 
2171 N  NE2 . HIS B 91  ? 0.37783 0.28976 0.48293 0.01851  -0.01024 0.07057  90  HIS B NE2 
2172 N  N   . GLN B 92  ? 0.42148 0.30922 0.44790 0.05438  0.03823  -0.02185 91  GLN B N   
2173 C  CA  . GLN B 92  ? 0.44830 0.34101 0.45179 0.05826  0.04966  -0.03381 91  GLN B CA  
2174 C  C   . GLN B 92  ? 0.44387 0.34662 0.46009 0.07140  0.06380  -0.03611 91  GLN B C   
2175 O  O   . GLN B 92  ? 0.44062 0.33892 0.48200 0.08035  0.06447  -0.03409 91  GLN B O   
2176 C  CB  . GLN B 92  ? 0.45067 0.31836 0.42912 0.05899  0.04766  -0.05157 91  GLN B CB  
2177 C  CG  . GLN B 92  ? 0.41960 0.28485 0.38470 0.04524  0.03555  -0.04888 91  GLN B CG  
2178 C  CD  . GLN B 92  ? 0.40075 0.24229 0.34126 0.04450  0.03029  -0.06565 91  GLN B CD  
2179 O  OE1 . GLN B 92  ? 0.44165 0.26342 0.37416 0.05447  0.03416  -0.08114 91  GLN B OE1 
2180 N  NE2 . GLN B 92  ? 0.40366 0.24710 0.33263 0.03312  0.02060  -0.06345 91  GLN B NE2 
2181 N  N   . GLN B 93  ? 0.43182 0.34941 0.43311 0.07228  0.07504  -0.03889 92  GLN B N   
2182 C  CA  . GLN B 93  ? 0.47301 0.40424 0.48488 0.08394  0.09142  -0.04091 92  GLN B CA  
2183 C  C   . GLN B 93  ? 0.44554 0.39647 0.49519 0.08665  0.09067  -0.02586 92  GLN B C   
2184 O  O   . GLN B 93  ? 0.44865 0.40659 0.52031 0.09909  0.10124  -0.02708 92  GLN B O   
2185 C  CB  . GLN B 93  ? 0.53208 0.44339 0.53479 0.09783  0.10106  -0.05957 92  GLN B CB  
2186 C  CG  . GLN B 93  ? 0.55429 0.45468 0.51454 0.09520  0.10471  -0.07325 92  GLN B CG  
2187 C  CD  . GLN B 93  ? 0.69252 0.57700 0.63539 0.10979  0.11719  -0.09404 92  GLN B CD  
2188 O  OE1 . GLN B 93  ? 0.79918 0.69952 0.74451 0.12059  0.13618  -0.09660 92  GLN B OE1 
2189 N  NE2 . GLN B 93  ? 0.78432 0.63793 0.70955 0.11016  0.10668  -0.10958 92  GLN B NE2 
2190 N  N   . GLN B 94  ? 0.40456 0.36635 0.46109 0.07521  0.07820  -0.01189 93  GLN B N   
2191 C  CA  . GLN B 94  ? 0.39628 0.37951 0.48224 0.07429  0.07388  0.00371  93  GLN B CA  
2192 C  C   . GLN B 94  ? 0.36870 0.37382 0.45020 0.06516  0.07377  0.01075  93  GLN B C   
2193 O  O   . GLN B 94  ? 0.39269 0.41447 0.49275 0.06097  0.06573  0.02300  93  GLN B O   
2194 C  CB  . GLN B 94  ? 0.43225 0.41004 0.52804 0.06836  0.05777  0.01462  93  GLN B CB  
2195 C  CG  . GLN B 94  ? 0.41323 0.36546 0.51575 0.07438  0.05363  0.01017  93  GLN B CG  
2196 C  CD  . GLN B 94  ? 0.56937 0.52301 0.70755 0.08590  0.05352  0.01680  93  GLN B CD  
2197 O  OE1 . GLN B 94  ? 0.58787 0.56409 0.74738 0.08721  0.05318  0.02832  93  GLN B OE1 
2198 N  NE2 . GLN B 94  ? 0.62470 0.55330 0.77197 0.09433  0.05212  0.00953  93  GLN B NE2 
2199 N  N   . GLY B 95  ? 0.33954 0.34327 0.39634 0.06144  0.08035  0.00348  94  GLY B N   
2200 C  CA  . GLY B 95  ? 0.35127 0.37139 0.40459 0.05260  0.07924  0.00945  94  GLY B CA  
2201 C  C   . GLY B 95  ? 0.37054 0.38896 0.41031 0.04125  0.06561  0.01180  94  GLY B C   
2202 O  O   . GLY B 95  ? 0.33455 0.36439 0.37394 0.03428  0.06231  0.01568  94  GLY B O   
2203 N  N   . LEU B 96  ? 0.32141 0.32616 0.35174 0.03926  0.05777  0.00944  95  LEU B N   
2204 C  CA  . LEU B 96  ? 0.29123 0.29892 0.31178 0.02973  0.04687  0.01233  95  LEU B CA  
2205 C  C   . LEU B 96  ? 0.30510 0.30816 0.30394 0.02463  0.04739  0.00538  95  LEU B C   
2206 O  O   . LEU B 96  ? 0.30765 0.31837 0.30252 0.01825  0.04099  0.00689  95  LEU B O   
2207 C  CB  . LEU B 96  ? 0.32037 0.31819 0.34092 0.02829  0.03952  0.01487  95  LEU B CB  
2208 C  CG  . LEU B 96  ? 0.32874 0.33015 0.37233 0.03267  0.03609  0.02481  95  LEU B CG  
2209 C  CD1 . LEU B 96  ? 0.31952 0.30853 0.36280 0.02979  0.02877  0.02911  95  LEU B CD1 
2210 C  CD2 . LEU B 96  ? 0.31319 0.33598 0.36775 0.02907  0.02979  0.03506  95  LEU B CD2 
2211 N  N   . GLY B 97  ? 0.32865 0.31865 0.31261 0.02780  0.05391  -0.00273 96  GLY B N   
2212 C  CA  . GLY B 97  ? 0.29540 0.28118 0.25982 0.02289  0.05244  -0.00714 96  GLY B CA  
2213 C  C   . GLY B 97  ? 0.28218 0.28091 0.25105 0.01992  0.05455  -0.00231 96  GLY B C   
2214 O  O   . GLY B 97  ? 0.31285 0.31340 0.27673 0.01412  0.04792  -0.00213 96  GLY B O   
2215 N  N   A ARG B 98  ? 0.28653 0.29496 0.26922 0.02392  0.06304  0.00216  97  ARG B N   
2216 N  N   B ARG B 98  ? 0.29353 0.30206 0.27636 0.02390  0.06302  0.00221  97  ARG B N   
2217 C  CA  A ARG B 98  ? 0.32767 0.34896 0.32017 0.01991  0.06463  0.00890  97  ARG B CA  
2218 C  CA  B ARG B 98  ? 0.32267 0.34399 0.31515 0.01982  0.06453  0.00892  97  ARG B CA  
2219 C  C   A ARG B 98  ? 0.33447 0.36518 0.34093 0.01399  0.05270  0.01274  97  ARG B C   
2220 C  C   B ARG B 98  ? 0.32726 0.35788 0.33354 0.01393  0.05258  0.01268  97  ARG B C   
2221 O  O   A ARG B 98  ? 0.30796 0.34027 0.31368 0.00808  0.04703  0.01357  97  ARG B O   
2222 O  O   B ARG B 98  ? 0.30800 0.34039 0.31384 0.00802  0.04693  0.01359  97  ARG B O   
2223 C  CB  A ARG B 98  ? 0.34177 0.37486 0.35106 0.02568  0.07742  0.01407  97  ARG B CB  
2224 C  CB  B ARG B 98  ? 0.34151 0.37499 0.35118 0.02536  0.07715  0.01434  97  ARG B CB  
2225 C  CG  A ARG B 98  ? 0.34035 0.38994 0.36896 0.02018  0.07800  0.02414  97  ARG B CG  
2226 C  CG  B ARG B 98  ? 0.35850 0.40326 0.37488 0.02049  0.08208  0.02249  97  ARG B CG  
2227 C  CD  A ARG B 98  ? 0.35124 0.39727 0.36426 0.01511  0.08145  0.02658  97  ARG B CD  
2228 C  CD  B ARG B 98  ? 0.35004 0.41193 0.38885 0.02617  0.09618  0.02936  97  ARG B CD  
2229 N  NE  A ARG B 98  ? 0.41559 0.47785 0.45177 0.00982  0.08414  0.03855  97  ARG B NE  
2230 N  NE  B ARG B 98  ? 0.48665 0.55455 0.51771 0.02488  0.10901  0.03498  97  ARG B NE  
2231 C  CZ  A ARG B 98  ? 0.43469 0.51025 0.47980 0.01265  0.09990  0.04629  97  ARG B CZ  
2232 C  CZ  B ARG B 98  ? 0.51952 0.58032 0.52503 0.03127  0.12210  0.02912  97  ARG B CZ  
2233 N  NH1 A ARG B 98  ? 0.42484 0.49788 0.45363 0.02219  0.11485  0.04065  97  ARG B NH1 
2234 N  NH1 B ARG B 98  ? 0.57582 0.62096 0.56399 0.03916  0.12252  0.01601  97  ARG B NH1 
2235 N  NH2 A ARG B 98  ? 0.37877 0.47053 0.44971 0.00590  0.10085  0.05935  97  ARG B NH2 
2236 N  NH2 B ARG B 98  ? 0.51022 0.57913 0.50668 0.02922  0.13399  0.03671  97  ARG B NH2 
2237 N  N   . ARG B 99  ? 0.30163 0.33625 0.31777 0.01563  0.04754  0.01418  98  ARG B N   
2238 C  CA  . ARG B 99  ? 0.25515 0.29923 0.27897 0.01047  0.03584  0.01671  98  ARG B CA  
2239 C  C   . ARG B 99  ? 0.30261 0.34060 0.30876 0.00618  0.02869  0.01011  98  ARG B C   
2240 O  O   . ARG B 99  ? 0.29121 0.33452 0.29881 0.00187  0.02070  0.00826  98  ARG B O   
2241 C  CB  . ARG B 99  ? 0.29989 0.35079 0.33640 0.01325  0.03184  0.02242  98  ARG B CB  
2242 C  CG  . ARG B 99  ? 0.28930 0.35065 0.35124 0.01799  0.03723  0.02966  98  ARG B CG  
2243 C  CD  . ARG B 99  ? 0.34324 0.40786 0.42027 0.02314  0.03427  0.03617  98  ARG B CD  
2244 N  NE  . ARG B 99  ? 0.39559 0.46924 0.47434 0.01792  0.01988  0.04191  98  ARG B NE  
2245 C  CZ  . ARG B 99  ? 0.30903 0.38727 0.40016 0.02044  0.01339  0.05095  98  ARG B CZ  
2246 N  NH1 . ARG B 99  ? 0.33200 0.40526 0.43957 0.02896  0.01956  0.05463  98  ARG B NH1 
2247 N  NH2 . ARG B 99  ? 0.38726 0.47471 0.47367 0.01480  -0.00006 0.05628  98  ARG B NH2 
2248 N  N   . LEU B 100 ? 0.25340 0.28050 0.24478 0.00758  0.03092  0.00569  99  LEU B N   
2249 C  CA  . LEU B 100 ? 0.24047 0.26437 0.21951 0.00441  0.02571  0.00000  99  LEU B CA  
2250 C  C   . LEU B 100 ? 0.26431 0.28371 0.23940 0.00234  0.02486  -0.00331 99  LEU B C   
2251 O  O   . LEU B 100 ? 0.27371 0.29531 0.24825 0.00008  0.01843  -0.00757 99  LEU B O   
2252 C  CB  . LEU B 100 ? 0.25373 0.26814 0.22316 0.00538  0.02712  -0.00219 99  LEU B CB  
2253 C  CG  . LEU B 100 ? 0.23803 0.25703 0.21252 0.00528  0.02495  0.00290  99  LEU B CG  
2254 C  CD1 . LEU B 100 ? 0.28514 0.29096 0.25533 0.00574  0.02601  0.00173  99  LEU B CD1 
2255 C  CD2 . LEU B 100 ? 0.30982 0.34102 0.28149 0.00183  0.01983  0.00300  99  LEU B CD2 
2256 N  N   . LEU B 101 ? 0.26143 0.27429 0.23324 0.00356  0.03135  -0.00132 100 LEU B N   
2257 C  CA  . LEU B 101 ? 0.28295 0.29126 0.25142 0.00072  0.02992  -0.00074 100 LEU B CA  
2258 C  C   . LEU B 101 ? 0.28358 0.29941 0.26820 -0.00301 0.02481  0.00229  100 LEU B C   
2259 O  O   . LEU B 101 ? 0.27291 0.28419 0.25879 -0.00596 0.01786  0.00023  100 LEU B O   
2260 C  CB  . LEU B 101 ? 0.26495 0.26796 0.22429 0.00246  0.03924  0.00299  100 LEU B CB  
2261 C  CG  . LEU B 101 ? 0.29590 0.28652 0.23462 0.00465  0.03999  -0.00247 100 LEU B CG  
2262 C  CD1 . LEU B 101 ? 0.37456 0.36078 0.30069 0.00891  0.05112  -0.00224 100 LEU B CD1 
2263 C  CD2 . LEU B 101 ? 0.34527 0.32846 0.27466 0.00125  0.03161  -0.00370 100 LEU B CD2 
2264 N  N   . GLU B 102 ? 0.27295 0.29934 0.27240 -0.00293 0.02649  0.00696  101 GLU B N   
2265 C  CA  . GLU B 102 ? 0.27450 0.30781 0.29154 -0.00775 0.01896  0.00958  101 GLU B CA  
2266 C  C   . GLU B 102 ? 0.27764 0.30969 0.29103 -0.00924 0.00709  0.00025  101 GLU B C   
2267 O  O   . GLU B 102 ? 0.28000 0.30839 0.30062 -0.01304 -0.00146 -0.00276 101 GLU B O   
2268 C  CB  . GLU B 102 ? 0.34082 0.38779 0.37690 -0.00723 0.02136  0.01684  101 GLU B CB  
2269 C  CG  . GLU B 102 ? 0.48241 0.53363 0.52645 -0.00543 0.03466  0.02564  101 GLU B CG  
2270 C  CD  . GLU B 102 ? 0.61986 0.68778 0.69072 -0.00477 0.03747  0.03422  101 GLU B CD  
2271 O  OE1 . GLU B 102 ? 0.71333 0.78940 0.79718 -0.00523 0.04770  0.04291  101 GLU B OE1 
2272 O  OE2 . GLU B 102 ? 0.60799 0.68255 0.68762 -0.00384 0.02969  0.03357  101 GLU B OE2 
2273 N  N   . ARG B 103 ? 0.25097 0.28553 0.25309 -0.00612 0.00672  -0.00467 102 ARG B N   
2274 C  CA  A ARG B 103 ? 0.25001 0.28665 0.24552 -0.00632 -0.00167 -0.01417 102 ARG B CA  
2275 C  CA  B ARG B 103 ? 0.22755 0.26420 0.22317 -0.00636 -0.00175 -0.01418 102 ARG B CA  
2276 C  C   . ARG B 103 ? 0.26464 0.29141 0.25438 -0.00540 -0.00353 -0.02182 102 ARG B C   
2277 O  O   . ARG B 103 ? 0.27151 0.29636 0.26316 -0.00560 -0.01155 -0.03087 102 ARG B O   
2278 C  CB  A ARG B 103 ? 0.30241 0.34692 0.28763 -0.00389 0.00041  -0.01405 102 ARG B CB  
2279 C  CB  B ARG B 103 ? 0.29377 0.33856 0.27919 -0.00397 0.00012  -0.01411 102 ARG B CB  
2280 C  CG  A ARG B 103 ? 0.37596 0.42870 0.35246 -0.00391 -0.00641 -0.02196 102 ARG B CG  
2281 C  CG  B ARG B 103 ? 0.41691 0.47062 0.39436 -0.00423 -0.00722 -0.02138 102 ARG B CG  
2282 C  CD  A ARG B 103 ? 0.43426 0.49408 0.41714 -0.00687 -0.01608 -0.02158 102 ARG B CD  
2283 C  CD  B ARG B 103 ? 0.39062 0.45054 0.37642 -0.00751 -0.01721 -0.02074 102 ARG B CD  
2284 N  NE  A ARG B 103 ? 0.52882 0.59675 0.49654 -0.00628 -0.02235 -0.03059 102 ARG B NE  
2285 N  NE  B ARG B 103 ? 0.48154 0.54925 0.47691 -0.00811 -0.01634 -0.00839 102 ARG B NE  
2286 C  CZ  A ARG B 103 ? 0.54527 0.62552 0.50249 -0.00639 -0.02333 -0.02537 102 ARG B CZ  
2287 C  CZ  B ARG B 103 ? 0.51628 0.59442 0.50511 -0.00792 -0.01970 -0.00359 102 ARG B CZ  
2288 N  NH1 A ARG B 103 ? 0.61041 0.69934 0.54936 -0.00564 -0.02787 -0.03418 102 ARG B NH1 
2289 N  NH1 B ARG B 103 ? 0.46410 0.54802 0.43347 -0.00765 -0.02254 -0.01017 102 ARG B NH1 
2290 N  NH2 A ARG B 103 ? 0.50779 0.59152 0.47233 -0.00680 -0.01984 -0.01122 102 ARG B NH2 
2291 N  NH2 B ARG B 103 ? 0.46244 0.54632 0.46483 -0.00756 -0.01995 0.00850  102 ARG B NH2 
2292 N  N   . ALA B 104 ? 0.27327 0.29283 0.25663 -0.00390 0.00257  -0.01904 103 ALA B N   
2293 C  CA  . ALA B 104 ? 0.24592 0.25672 0.22675 -0.00278 -0.00060 -0.02411 103 ALA B CA  
2294 C  C   . ALA B 104 ? 0.26922 0.27116 0.26090 -0.00582 -0.00655 -0.02211 103 ALA B C   
2295 O  O   . ALA B 104 ? 0.25959 0.25547 0.25623 -0.00455 -0.01402 -0.02956 103 ALA B O   
2296 C  CB  . ALA B 104 ? 0.27574 0.28075 0.24674 -0.00161 0.00460  -0.02045 103 ALA B CB  
2297 N  N   . VAL B 105 ? 0.27690 0.27850 0.27474 -0.00960 -0.00306 -0.01158 104 VAL B N   
2298 C  CA  . VAL B 105 ? 0.26231 0.25673 0.27358 -0.01439 -0.00865 -0.00594 104 VAL B CA  
2299 C  C   . VAL B 105 ? 0.25974 0.25436 0.28553 -0.01673 -0.01993 -0.01343 104 VAL B C   
2300 O  O   . VAL B 105 ? 0.26734 0.25058 0.30356 -0.01864 -0.02961 -0.01640 104 VAL B O   
2301 C  CB  . VAL B 105 ? 0.26765 0.26618 0.28330 -0.01812 0.00013  0.00867  104 VAL B CB  
2302 C  CG1 . VAL B 105 ? 0.26789 0.26060 0.30043 -0.02496 -0.00571 0.01810  104 VAL B CG1 
2303 C  CG2 . VAL B 105 ? 0.31001 0.30483 0.30584 -0.01522 0.00973  0.01299  104 VAL B CG2 
2304 N  N   . THR B 106 ? 0.26108 0.26700 0.28787 -0.01666 -0.02068 -0.01687 105 THR B N   
2305 C  CA  . THR B 106 ? 0.24182 0.24766 0.27747 -0.01888 -0.03342 -0.02637 105 THR B CA  
2306 C  C   . THR B 106 ? 0.25205 0.25019 0.27885 -0.01363 -0.03961 -0.04300 105 THR B C   
2307 O  O   . THR B 106 ? 0.27271 0.26026 0.30960 -0.01491 -0.05133 -0.05189 105 THR B O   
2308 C  CB  . THR B 106 ? 0.26750 0.28837 0.30077 -0.01908 -0.03355 -0.02599 105 THR B CB  
2309 O  OG1 . THR B 106 ? 0.24473 0.27337 0.29427 -0.02333 -0.02930 -0.01139 105 THR B OG1 
2310 C  CG2 . THR B 106 ? 0.29807 0.31987 0.33137 -0.02046 -0.04768 -0.03862 105 THR B CG2 
2311 N  N   . TYR B 107 ? 0.27137 0.27479 0.28201 -0.00750 -0.03184 -0.04739 106 TYR B N   
2312 C  CA  . TYR B 107 ? 0.25118 0.25249 0.25517 -0.00092 -0.03413 -0.06249 106 TYR B CA  
2313 C  C   . TYR B 107 ? 0.27425 0.25977 0.28974 0.00058  -0.03880 -0.06368 106 TYR B C   
2314 O  O   . TYR B 107 ? 0.29501 0.27273 0.31637 0.00490  -0.04659 -0.07771 106 TYR B O   
2315 C  CB  . TYR B 107 ? 0.27975 0.29339 0.26905 0.00356  -0.02353 -0.06207 106 TYR B CB  
2316 C  CG  . TYR B 107 ? 0.29001 0.30745 0.27515 0.01096  -0.02259 -0.07585 106 TYR B CG  
2317 C  CD1 . TYR B 107 ? 0.34550 0.37394 0.32001 0.01470  -0.02298 -0.08852 106 TYR B CD1 
2318 C  CD2 . TYR B 107 ? 0.30992 0.32179 0.30189 0.01463  -0.02101 -0.07573 106 TYR B CD2 
2319 C  CE1 . TYR B 107 ? 0.46305 0.49824 0.43482 0.02285  -0.01929 -0.10167 106 TYR B CE1 
2320 C  CE2 . TYR B 107 ? 0.33953 0.35783 0.33321 0.02255  -0.01914 -0.08802 106 TYR B CE2 
2321 C  CZ  . TYR B 107 ? 0.41130 0.44205 0.39527 0.02699  -0.01690 -0.10110 106 TYR B CZ  
2322 O  OH  . TYR B 107 ? 0.44439 0.48493 0.43065 0.03597  -0.01221 -0.11349 106 TYR B OH  
2323 N  N   . ALA B 108 ? 0.26846 0.24872 0.28650 -0.00233 -0.03465 -0.04943 107 ALA B N   
2324 C  CA  . ALA B 108 ? 0.30982 0.27488 0.33870 -0.00191 -0.04085 -0.04670 107 ALA B CA  
2325 C  C   . ALA B 108 ? 0.29490 0.24651 0.34251 -0.00617 -0.05316 -0.04819 107 ALA B C   
2326 O  O   . ALA B 108 ? 0.31735 0.25559 0.37670 -0.00233 -0.06267 -0.05709 107 ALA B O   
2327 C  CB  . ALA B 108 ? 0.31102 0.27390 0.33438 -0.00570 -0.03482 -0.02953 107 ALA B CB  
2328 N  N   . HIS B 109 ? 0.31467 0.26941 0.36885 -0.01403 -0.05395 -0.03943 108 HIS B N   
2329 C  CA  . HIS B 109 ? 0.30497 0.24714 0.38090 -0.02033 -0.06720 -0.03896 108 HIS B CA  
2330 C  C   . HIS B 109 ? 0.30645 0.24273 0.38449 -0.01581 -0.07867 -0.06172 108 HIS B C   
2331 O  O   . HIS B 109 ? 0.34612 0.26378 0.44041 -0.01546 -0.09168 -0.06952 108 HIS B O   
2332 C  CB  . HIS B 109 ? 0.32077 0.27246 0.40655 -0.02989 -0.06480 -0.02396 108 HIS B CB  
2333 C  CG  . HIS B 109 ? 0.33494 0.27502 0.44786 -0.03892 -0.07882 -0.01933 108 HIS B CG  
2334 N  ND1 . HIS B 109 ? 0.38962 0.32017 0.51923 -0.04603 -0.08056 -0.00110 108 HIS B ND1 
2335 C  CD2 . HIS B 109 ? 0.34833 0.28392 0.47488 -0.04276 -0.09323 -0.03019 108 HIS B CD2 
2336 C  CE1 . HIS B 109 ? 0.44176 0.36230 0.59796 -0.05451 -0.09529 0.00027  108 HIS B CE1 
2337 N  NE2 . HIS B 109 ? 0.45588 0.37830 0.61073 -0.05259 -0.10407 -0.01858 108 HIS B NE2 
2338 N  N   . ALA B 110 ? 0.30779 0.25888 0.36834 -0.01178 -0.07434 -0.07302 109 ALA B N   
2339 C  CA  . ALA B 110 ? 0.34078 0.28840 0.39706 -0.00739 -0.08445 -0.09565 109 ALA B CA  
2340 C  C   . ALA B 110 ? 0.33915 0.27848 0.39272 0.00390  -0.08472 -0.11287 109 ALA B C   
2341 O  O   . ALA B 110 ? 0.38124 0.30958 0.43768 0.00836  -0.09558 -0.13332 109 ALA B O   
2342 C  CB  . ALA B 110 ? 0.36596 0.33361 0.40088 -0.00626 -0.07948 -0.10070 109 ALA B CB  
2343 N  N   . SER B 111 ? 0.33870 0.30395 0.28748 0.00388  -0.09403 -0.06062 110 SER B N   
2344 C  CA  . SER B 111 ? 0.35075 0.33685 0.31133 0.00411  -0.07816 -0.08448 110 SER B CA  
2345 C  C   . SER B 111 ? 0.34267 0.33534 0.35814 0.01553  -0.08980 -0.08863 110 SER B C   
2346 O  O   . SER B 111 ? 0.33135 0.34268 0.37093 0.02188  -0.08452 -0.11090 110 SER B O   
2347 C  CB  . SER B 111 ? 0.35564 0.35354 0.29055 -0.00955 -0.04909 -0.08596 110 SER B CB  
2348 O  OG  . SER B 111 ? 0.32852 0.32733 0.27812 -0.01061 -0.04580 -0.06324 110 SER B OG  
2349 N  N   . HIS B 112 ? 0.31601 0.28918 0.34929 0.01684  -0.10756 -0.07140 111 HIS B N   
2350 C  CA  . HIS B 112 ? 0.31477 0.26919 0.37686 0.02269  -0.12390 -0.07156 111 HIS B CA  
2351 C  C   . HIS B 112 ? 0.33691 0.29042 0.40507 0.02604  -0.12053 -0.06396 111 HIS B C   
2352 O  O   . HIS B 112 ? 0.36921 0.30566 0.45300 0.03833  -0.13929 -0.07573 111 HIS B O   
2353 C  CB  . HIS B 112 ? 0.33495 0.28559 0.41358 0.03552  -0.14037 -0.10281 111 HIS B CB  
2354 C  CG  . HIS B 112 ? 0.34577 0.29240 0.41713 0.03315  -0.14857 -0.11203 111 HIS B CG  
2355 N  ND1 . HIS B 112 ? 0.42895 0.34921 0.51414 0.02706  -0.16599 -0.10316 111 HIS B ND1 
2356 C  CD2 . HIS B 112 ? 0.38019 0.34223 0.42618 0.03320  -0.14184 -0.13001 111 HIS B CD2 
2357 C  CE1 . HIS B 112 ? 0.41308 0.33830 0.49291 0.02842  -0.17417 -0.11872 111 HIS B CE1 
2358 N  NE2 . HIS B 112 ? 0.44813 0.39439 0.49704 0.03293  -0.16125 -0.13301 111 HIS B NE2 
2359 N  N   . CYS B 113 ? 0.31391 0.28037 0.36896 0.01775  -0.10262 -0.04641 112 CYS B N   
2360 C  CA  . CYS B 113 ? 0.32225 0.28270 0.37945 0.01959  -0.10268 -0.03636 112 CYS B CA  
2361 C  C   . CYS B 113 ? 0.37230 0.29274 0.41802 0.01075  -0.11350 -0.01352 112 CYS B C   
2362 O  O   . CYS B 113 ? 0.38030 0.29486 0.42376 -0.00348 -0.10797 -0.00229 112 CYS B O   
2363 C  CB  . CYS B 113 ? 0.25867 0.24140 0.30439 0.01163  -0.08057 -0.02569 112 CYS B CB  
2364 S  SG  . CYS B 113 ? 0.30564 0.32241 0.34703 0.00869  -0.05887 -0.04921 112 CYS B SG  
2365 N  N   . ARG B 114 ? 0.35430 0.24478 0.39006 0.01705  -0.12922 -0.00981 113 ARG B N   
2366 C  CA  . ARG B 114 ? 0.42179 0.26192 0.42348 0.00071  -0.13404 0.01502  113 ARG B CA  
2367 C  C   . ARG B 114 ? 0.40869 0.26533 0.39611 -0.01458 -0.10885 0.03239  113 ARG B C   
2368 O  O   . ARG B 114 ? 0.45282 0.28406 0.41612 -0.03784 -0.09796 0.04853  113 ARG B O   
2369 C  CB  . ARG B 114 ? 0.52696 0.31026 0.50375 0.01404  -0.16828 0.01444  113 ARG B CB  
2370 C  CG  . ARG B 114 ? 0.72551 0.43241 0.64159 -0.01043 -0.17449 0.04268  113 ARG B CG  
2371 C  CD  . ARG B 114 ? 0.83595 0.47641 0.70770 0.00385  -0.21341 0.04494  113 ARG B CD  
2372 N  NE  . ARG B 114 ? 0.98238 0.57128 0.78163 -0.02726 -0.20185 0.06999  113 ARG B NE  
2373 C  CZ  . ARG B 114 ? 0.96753 0.55996 0.73541 -0.03852 -0.18366 0.08194  113 ARG B CZ  
2374 N  NH1 . ARG B 114 ? 0.84072 0.48287 0.64352 -0.02077 -0.17821 0.07474  113 ARG B NH1 
2375 N  NH2 . ARG B 114 ? 1.06400 0.61029 0.76406 -0.06831 -0.17020 0.09854  113 ARG B NH2 
2376 N  N   . ALA B 115 ? 0.35069 0.24717 0.35191 -0.00500 -0.09781 0.02613  114 ALA B N   
2377 C  CA  . ALA B 115 ? 0.36434 0.27113 0.35286 -0.01553 -0.07957 0.03901  114 ALA B CA  
2378 C  C   . ALA B 115 ? 0.31640 0.26647 0.32531 -0.00707 -0.06727 0.02963  114 ALA B C   
2379 O  O   . ALA B 115 ? 0.30789 0.27610 0.33331 0.00373  -0.07061 0.01259  114 ALA B O   
2380 C  CB  . ALA B 115 ? 0.44750 0.31352 0.39885 -0.01550 -0.09250 0.04835  114 ALA B CB  
2381 N  N   . LEU B 116 ? 0.29864 0.26209 0.30402 -0.01495 -0.05148 0.03796  115 LEU B N   
2382 C  CA  . LEU B 116 ? 0.25917 0.24654 0.27200 -0.01051 -0.04233 0.03292  115 LEU B CA  
2383 C  C   . LEU B 116 ? 0.25672 0.23734 0.25846 -0.00907 -0.04392 0.03539  115 LEU B C   
2384 O  O   . LEU B 116 ? 0.32316 0.28106 0.30150 -0.01666 -0.04473 0.04557  115 LEU B O   
2385 C  CB  . LEU B 116 ? 0.26789 0.26811 0.28535 -0.01569 -0.03180 0.03674  115 LEU B CB  
2386 C  CG  . LEU B 116 ? 0.30451 0.30478 0.32416 -0.01439 -0.03722 0.03277  115 LEU B CG  
2387 C  CD1 . LEU B 116 ? 0.28757 0.28660 0.32216 -0.01887 -0.04214 0.03250  115 LEU B CD1 
2388 C  CD2 . LEU B 116 ? 0.29659 0.29419 0.30404 -0.01356 -0.03670 0.03371  115 LEU B CD2 
2389 N  N   . THR B 117 ? 0.27210 0.27083 0.28661 -0.00319 -0.04212 0.02406  116 THR B N   
2390 C  CA  . THR B 117 ? 0.27303 0.26766 0.28104 0.00076  -0.04799 0.02176  116 THR B CA  
2391 C  C   . THR B 117 ? 0.24787 0.26580 0.26978 -0.00379 -0.03277 0.01631  116 THR B C   
2392 O  O   . THR B 117 ? 0.22742 0.25759 0.25801 -0.01040 -0.02025 0.01286  116 THR B O   
2393 C  CB  . THR B 117 ? 0.26323 0.25183 0.28227 0.01654  -0.07292 0.00370  116 THR B CB  
2394 O  OG1 . THR B 117 ? 0.26304 0.28796 0.32348 0.01974  -0.06660 -0.02151 116 THR B OG1 
2395 C  CG2 . THR B 117 ? 0.30621 0.25190 0.30055 0.02241  -0.09683 0.01084  116 THR B CG2 
2396 N  N   . LEU B 118 ? 0.25948 0.27427 0.27426 -0.00200 -0.03590 0.01549  117 LEU B N   
2397 C  CA  . LEU B 118 ? 0.22199 0.25282 0.25083 -0.00605 -0.02582 0.00770  117 LEU B CA  
2398 C  C   . LEU B 118 ? 0.24084 0.26612 0.26220 0.00104  -0.03863 0.00072  117 LEU B C   
2399 O  O   . LEU B 118 ? 0.26165 0.26146 0.25183 0.00638  -0.05367 0.00706  117 LEU B O   
2400 C  CB  . LEU B 118 ? 0.21827 0.24554 0.24014 -0.01387 -0.01243 0.01911  117 LEU B CB  
2401 C  CG  . LEU B 118 ? 0.24463 0.26575 0.25365 -0.01434 -0.01035 0.02702  117 LEU B CG  
2402 C  CD1 . LEU B 118 ? 0.27609 0.29767 0.27669 -0.01361 -0.00921 0.02081  117 LEU B CD1 
2403 C  CD2 . LEU B 118 ? 0.27814 0.30147 0.29793 -0.01567 -0.00614 0.02934  117 LEU B CD2 
2404 N  N   . THR B 119 ? 0.19791 0.23951 0.24049 -0.00134 -0.03407 -0.01288 118 THR B N   
2405 C  CA  . THR B 119 ? 0.23400 0.26996 0.26666 0.00428  -0.04465 -0.01957 118 THR B CA  
2406 C  C   . THR B 119 ? 0.22789 0.26797 0.26480 -0.00502 -0.02787 -0.01703 118 THR B C   
2407 O  O   . THR B 119 ? 0.23763 0.28125 0.28896 -0.01543 -0.01435 -0.01538 118 THR B O   
2408 C  CB  . THR B 119 ? 0.25397 0.30533 0.31790 0.01472  -0.06475 -0.04744 118 THR B CB  
2409 O  OG1 . THR B 119 ? 0.23735 0.32015 0.34729 0.00169  -0.04656 -0.06584 118 THR B OG1 
2410 C  CG2 . THR B 119 ? 0.25178 0.29552 0.31944 0.02993  -0.09007 -0.05604 118 THR B CG2 
2411 N  N   . THR B 120 ? 0.24446 0.27636 0.26145 -0.00196 -0.03071 -0.01784 119 THR B N   
2412 C  CA  . THR B 120 ? 0.25229 0.28620 0.27800 -0.00636 -0.01966 -0.02011 119 THR B CA  
2413 C  C   . THR B 120 ? 0.24387 0.27517 0.25175 -0.00171 -0.02445 -0.03128 119 THR B C   
2414 O  O   . THR B 120 ? 0.29002 0.31037 0.26772 0.00312  -0.03732 -0.03390 119 THR B O   
2415 C  CB  . THR B 120 ? 0.23017 0.26131 0.25400 -0.00900 -0.00926 -0.00863 119 THR B CB  
2416 O  OG1 . THR B 120 ? 0.26466 0.29050 0.30414 -0.00831 -0.00847 -0.01472 119 THR B OG1 
2417 C  CG2 . THR B 120 ? 0.25131 0.28334 0.25079 -0.01017 -0.00331 -0.00714 119 THR B CG2 
2418 N  N   . PHE B 121 ? 0.23817 0.27252 0.25891 -0.00214 -0.01790 -0.03969 120 PHE B N   
2419 C  CA  . PHE B 121 ? 0.25620 0.29160 0.26072 0.00145  -0.01913 -0.05542 120 PHE B CA  
2420 C  C   . PHE B 121 ? 0.29373 0.33161 0.26727 -0.00392 -0.00374 -0.05456 120 PHE B C   
2421 O  O   . PHE B 121 ? 0.27992 0.32954 0.27279 -0.00697 0.00877  -0.05246 120 PHE B O   
2422 C  CB  . PHE B 121 ? 0.27906 0.31612 0.31426 0.00418  -0.01965 -0.07077 120 PHE B CB  
2423 C  CG  . PHE B 121 ? 0.30004 0.33072 0.35799 0.00096  -0.02963 -0.07730 120 PHE B CG  
2424 C  CD1 . PHE B 121 ? 0.26642 0.30290 0.32166 0.00435  -0.04214 -0.09272 120 PHE B CD1 
2425 C  CD2 . PHE B 121 ? 0.27957 0.29360 0.35729 -0.00843 -0.02732 -0.07042 120 PHE B CD2 
2426 C  CE1 . PHE B 121 ? 0.26513 0.30501 0.35432 -0.00238 -0.04823 -0.10611 120 PHE B CE1 
2427 C  CE2 . PHE B 121 ? 0.25890 0.26674 0.35541 -0.02122 -0.02838 -0.07913 120 PHE B CE2 
2428 C  CZ  . PHE B 121 ? 0.28231 0.30996 0.39350 -0.01861 -0.03690 -0.09975 120 PHE B CZ  
2429 N  N   . CYS B 122 ? 0.32031 0.34478 0.24306 -0.00755 -0.00462 -0.05976 121 CYS B N   
2430 C  CA  . CYS B 122 ? 0.36481 0.38692 0.24470 -0.02342 0.01865  -0.06227 121 CYS B CA  
2431 C  C   . CYS B 122 ? 0.38221 0.43943 0.29866 -0.02576 0.04098  -0.08948 121 CYS B C   
2432 O  O   . CYS B 122 ? 0.40710 0.48399 0.32990 -0.03956 0.06621  -0.09783 121 CYS B O   
2433 C  CB  . CYS B 122 ? 0.46629 0.45065 0.26350 -0.03008 0.01064  -0.06233 121 CYS B CB  
2434 S  SG  . CYS B 122 ? 0.51565 0.45059 0.26847 -0.02091 -0.02753 -0.03924 121 CYS B SG  
2435 N  N   . ASP B 123 ? 0.37142 0.43814 0.31521 -0.01310 0.03146  -0.10956 122 ASP B N   
2436 C  CA  . ASP B 123 ? 0.37397 0.46993 0.34329 -0.01246 0.04789  -0.14473 122 ASP B CA  
2437 C  C   . ASP B 123 ? 0.39261 0.50346 0.43798 0.00622  0.03410  -0.15898 122 ASP B C   
2438 O  O   . ASP B 123 ? 0.55433 0.68490 0.63157 0.01478  0.03616  -0.19350 122 ASP B O   
2439 C  CB  . ASP B 123 ? 0.47520 0.56087 0.40376 -0.01203 0.04426  -0.16294 122 ASP B CB  
2440 C  CG  . ASP B 123 ? 0.58690 0.64202 0.41967 -0.03142 0.05394  -0.15246 122 ASP B CG  
2441 O  OD1 . ASP B 123 ? 0.62114 0.67534 0.42233 -0.05318 0.08004  -0.14542 122 ASP B OD1 
2442 O  OD2 . ASP B 123 ? 0.66196 0.68759 0.44703 -0.02594 0.03269  -0.15250 122 ASP B OD2 
2443 N  N   . VAL B 124 ? 0.28932 0.38366 0.35738 0.01262  0.01739  -0.13514 123 VAL B N   
2444 C  CA  . VAL B 124 ? 0.27618 0.36134 0.39394 0.02803  -0.00220 -0.14211 123 VAL B CA  
2445 C  C   . VAL B 124 ? 0.26414 0.37001 0.41501 0.03169  0.00203  -0.14945 123 VAL B C   
2446 O  O   . VAL B 124 ? 0.25050 0.35819 0.38415 0.02113  0.01134  -0.12785 123 VAL B O   
2447 C  CB  . VAL B 124 ? 0.28187 0.32773 0.38970 0.02619  -0.02034 -0.11289 123 VAL B CB  
2448 C  CG1 . VAL B 124 ? 0.33109 0.34440 0.46366 0.03664  -0.04289 -0.11142 123 VAL B CG1 
2449 C  CG2 . VAL B 124 ? 0.27993 0.31399 0.37638 0.02330  -0.02659 -0.11778 123 VAL B CG2 
2450 N  N   . PRO B 125 ? 0.28211 0.40493 0.48596 0.04829  -0.00815 -0.18410 124 PRO B N   
2451 C  CA  . PRO B 125 ? 0.30325 0.46134 0.55200 0.05198  -0.00289 -0.20443 124 PRO B CA  
2452 C  C   . PRO B 125 ? 0.25434 0.38447 0.49872 0.05540  -0.02214 -0.17397 124 PRO B C   
2453 O  O   . PRO B 125 ? 0.27587 0.43585 0.54101 0.04948  -0.01050 -0.18039 124 PRO B O   
2454 C  CB  . PRO B 125 ? 0.30832 0.48284 0.62482 0.07797  -0.02446 -0.25362 124 PRO B CB  
2455 C  CG  . PRO B 125 ? 0.33855 0.50255 0.63893 0.07982  -0.02399 -0.26481 124 PRO B CG  
2456 C  CD  . PRO B 125 ? 0.32259 0.44018 0.55489 0.06499  -0.02474 -0.21532 124 PRO B CD  
2457 N  N   . TRP B 126 ? 0.27320 0.34582 0.48928 0.06146  -0.04928 -0.14420 125 TRP B N   
2458 C  CA  . TRP B 126 ? 0.29291 0.33218 0.49258 0.06271  -0.06714 -0.11726 125 TRP B CA  
2459 C  C   . TRP B 126 ? 0.27593 0.30875 0.42784 0.04122  -0.04678 -0.08128 125 TRP B C   
2460 O  O   . TRP B 126 ? 0.29117 0.29248 0.41860 0.03809  -0.05747 -0.05718 125 TRP B O   
2461 C  CB  . TRP B 126 ? 0.34144 0.30965 0.52426 0.07626  -0.10759 -0.10737 125 TRP B CB  
2462 C  CG  . TRP B 126 ? 0.37939 0.30586 0.52173 0.06249  -0.10508 -0.08855 125 TRP B CG  
2463 C  CD1 . TRP B 126 ? 0.38824 0.28556 0.48243 0.03963  -0.09309 -0.05590 125 TRP B CD1 
2464 C  CD2 . TRP B 126 ? 0.36510 0.28070 0.52120 0.06915  -0.11357 -0.10839 125 TRP B CD2 
2465 N  NE1 . TRP B 126 ? 0.35422 0.22531 0.43546 0.02933  -0.09234 -0.05553 125 TRP B NE1 
2466 C  CE2 . TRP B 126 ? 0.36492 0.24374 0.48036 0.04762  -0.10602 -0.08500 125 TRP B CE2 
2467 C  CE3 . TRP B 126 ? 0.36050 0.29797 0.56585 0.09091  -0.12625 -0.14970 125 TRP B CE3 
2468 C  CZ2 . TRP B 126 ? 0.40193 0.25948 0.52144 0.04665  -0.11313 -0.09803 125 TRP B CZ2 
2469 C  CZ3 . TRP B 126 ? 0.42501 0.34032 0.63063 0.09251  -0.13403 -0.16214 125 TRP B CZ3 
2470 C  CH2 . TRP B 126 ? 0.45316 0.32650 0.61444 0.07011  -0.12834 -0.13434 125 TRP B CH2 
2471 N  N   . ASN B 127 ? 0.23642 0.29432 0.37114 0.02756  -0.02096 -0.08025 126 ASN B N   
2472 C  CA  . ASN B 127 ? 0.23463 0.28733 0.33160 0.01267  -0.00878 -0.05360 126 ASN B CA  
2473 C  C   . ASN B 127 ? 0.24664 0.32757 0.33609 0.00129  0.01288  -0.05654 126 ASN B C   
2474 O  O   . ASN B 127 ? 0.23402 0.33048 0.34730 0.00117  0.01534  -0.06260 126 ASN B O   
2475 C  CB  . ASN B 127 ? 0.24867 0.28945 0.32276 0.00761  -0.00829 -0.04868 126 ASN B CB  
2476 C  CG  . ASN B 127 ? 0.29680 0.30297 0.37049 0.00676  -0.02269 -0.04075 126 ASN B CG  
2477 O  OD1 . ASN B 127 ? 0.33658 0.33735 0.40768 0.00240  -0.02343 -0.04594 126 ASN B OD1 
2478 N  ND2 . ASN B 127 ? 0.30491 0.28275 0.37466 0.00741  -0.03381 -0.02917 126 ASN B ND2 
2479 N  N   . ALA B 128 ? 0.27825 0.34779 0.30228 -0.01292 -0.04127 -0.10473 127 ALA B N   
2480 C  CA  . ALA B 128 ? 0.28094 0.36573 0.25208 -0.01752 -0.01933 -0.09308 127 ALA B CA  
2481 C  C   . ALA B 128 ? 0.29539 0.40660 0.23743 -0.01283 0.00190  -0.10061 127 ALA B C   
2482 O  O   . ALA B 128 ? 0.30707 0.42668 0.24099 -0.02374 0.01995  -0.07754 127 ALA B O   
2483 C  CB  . ALA B 128 ? 0.31528 0.39724 0.25341 -0.01427 -0.03595 -0.09796 127 ALA B CB  
2484 N  N   . PRO B 129 ? 0.31366 0.43901 0.24542 0.00539  -0.00238 -0.13000 128 PRO B N   
2485 C  CA  . PRO B 129 ? 0.34440 0.50800 0.25774 0.01185  0.02379  -0.12817 128 PRO B CA  
2486 C  C   . PRO B 129 ? 0.34251 0.50240 0.29316 -0.00257 0.03779  -0.11183 128 PRO B C   
2487 O  O   . PRO B 129 ? 0.31407 0.49930 0.26263 -0.00969 0.05681  -0.09088 128 PRO B O   
2488 C  CB  . PRO B 129 ? 0.36066 0.53584 0.25814 0.04349  0.01177  -0.16926 128 PRO B CB  
2489 C  CG  . PRO B 129 ? 0.43746 0.57974 0.32330 0.05426  -0.02584 -0.19191 128 PRO B CG  
2490 C  CD  . PRO B 129 ? 0.35430 0.46309 0.28854 0.02558  -0.03556 -0.16585 128 PRO B CD  
2491 N  N   . PHE B 130 ? 0.30627 0.43631 0.29547 -0.00617 0.02560  -0.11692 129 PHE B N   
2492 C  CA  . PHE B 130 ? 0.26581 0.38606 0.28141 -0.01519 0.03476  -0.10199 129 PHE B CA  
2493 C  C   . PHE B 130 ? 0.26362 0.37080 0.26638 -0.02707 0.04002  -0.07289 129 PHE B C   
2494 O  O   . PHE B 130 ? 0.26877 0.37886 0.27107 -0.03330 0.04616  -0.05958 129 PHE B O   
2495 C  CB  . PHE B 130 ? 0.26046 0.35766 0.31835 -0.01258 0.02008  -0.10759 129 PHE B CB  
2496 C  CG  . PHE B 130 ? 0.23793 0.32050 0.31264 -0.01658 0.02745  -0.08685 129 PHE B CG  
2497 C  CD1 . PHE B 130 ? 0.26410 0.34922 0.33176 -0.01861 0.03719  -0.08431 129 PHE B CD1 
2498 C  CD2 . PHE B 130 ? 0.30421 0.37380 0.40444 -0.01442 0.02251  -0.06732 129 PHE B CD2 
2499 C  CE1 . PHE B 130 ? 0.27406 0.33842 0.34705 -0.01587 0.03698  -0.07022 129 PHE B CE1 
2500 C  CE2 . PHE B 130 ? 0.29832 0.35805 0.40047 -0.00806 0.03041  -0.04834 129 PHE B CE2 
2501 C  CZ  . PHE B 130 ? 0.30048 0.35246 0.38292 -0.00756 0.03492  -0.05439 129 PHE B CZ  
2502 N  N   . TYR B 131 ? 0.26176 0.35270 0.25825 -0.02824 0.03233  -0.06283 130 TYR B N   
2503 C  CA  . TYR B 131 ? 0.24668 0.32105 0.22621 -0.03193 0.03177  -0.04096 130 TYR B CA  
2504 C  C   . TYR B 131 ? 0.25939 0.34662 0.21846 -0.04276 0.03293  -0.02946 130 TYR B C   
2505 O  O   . TYR B 131 ? 0.28234 0.35260 0.23963 -0.04729 0.02512  -0.01364 130 TYR B O   
2506 C  CB  . TYR B 131 ? 0.24132 0.30552 0.22030 -0.02786 0.02484  -0.03221 130 TYR B CB  
2507 C  CG  . TYR B 131 ? 0.29607 0.35872 0.31211 -0.01911 0.02360  -0.02817 130 TYR B CG  
2508 C  CD1 . TYR B 131 ? 0.34709 0.40527 0.37771 -0.00982 0.03063  -0.02100 130 TYR B CD1 
2509 C  CD2 . TYR B 131 ? 0.27230 0.33933 0.31491 -0.02019 0.01200  -0.02593 130 TYR B CD2 
2510 C  CE1 . TYR B 131 ? 0.38076 0.44688 0.45355 -0.00229 0.03124  -0.00528 130 TYR B CE1 
2511 C  CE2 . TYR B 131 ? 0.25213 0.32430 0.34814 -0.01546 0.00784  -0.00990 130 TYR B CE2 
2512 C  CZ  . TYR B 131 ? 0.34040 0.41611 0.45198 -0.00682 0.02007  0.00355  130 TYR B CZ  
2513 O  OH  . TYR B 131 ? 0.32430 0.41446 0.49660 -0.00254 0.01788  0.03086  130 TYR B OH  
2514 N  N   . ALA B 132 ? 0.29119 0.40856 0.23635 -0.04414 0.03858  -0.03446 131 ALA B N   
2515 C  CA  . ALA B 132 ? 0.29666 0.43921 0.22982 -0.05437 0.04315  -0.01089 131 ALA B CA  
2516 C  C   . ALA B 132 ? 0.28045 0.44200 0.24128 -0.06054 0.05070  0.00323  131 ALA B C   
2517 O  O   . ALA B 132 ? 0.31399 0.48069 0.28936 -0.07497 0.04383  0.03486  131 ALA B O   
2518 C  CB  . ALA B 132 ? 0.30650 0.48559 0.20905 -0.04568 0.05104  -0.01683 131 ALA B CB  
2519 N  N   . ARG B 133 ? 0.27157 0.44095 0.24984 -0.05128 0.05918  -0.01667 132 ARG B N   
2520 C  CA  . ARG B 133 ? 0.24508 0.43006 0.25834 -0.05791 0.06300  -0.00127 132 ARG B CA  
2521 C  C   . ARG B 133 ? 0.23631 0.37182 0.26652 -0.06737 0.03926  0.01086  132 ARG B C   
2522 O  O   . ARG B 133 ? 0.29838 0.43909 0.36386 -0.07823 0.03012  0.03320  132 ARG B O   
2523 C  CB  . ARG B 133 ? 0.22812 0.42773 0.25745 -0.04412 0.07363  -0.02764 132 ARG B CB  
2524 C  CG  . ARG B 133 ? 0.25014 0.49876 0.25951 -0.02412 0.09122  -0.04552 132 ARG B CG  
2525 C  CD  . ARG B 133 ? 0.28007 0.54601 0.31146 -0.00709 0.09803  -0.07119 132 ARG B CD  
2526 N  NE  . ARG B 133 ? 0.31325 0.53170 0.35372 -0.00304 0.07955  -0.10181 132 ARG B NE  
2527 C  CZ  . ARG B 133 ? 0.33788 0.54438 0.36383 0.01328  0.06647  -0.13330 132 ARG B CZ  
2528 N  NH1 . ARG B 133 ? 0.33035 0.56167 0.31791 0.03235  0.06782  -0.14748 132 ARG B NH1 
2529 N  NH2 . ARG B 133 ? 0.35460 0.52250 0.40769 0.01174  0.04727  -0.14764 132 ARG B NH2 
2530 N  N   . LEU B 134 ? 0.26605 0.35657 0.27401 -0.05935 0.02669  -0.00173 133 LEU B N   
2531 C  CA  . LEU B 134 ? 0.28074 0.32096 0.28614 -0.05469 0.00121  0.00296  133 LEU B CA  
2532 C  C   . LEU B 134 ? 0.32876 0.34726 0.32518 -0.06172 -0.02246 0.02262  133 LEU B C   
2533 O  O   . LEU B 134 ? 0.33252 0.30276 0.32263 -0.05201 -0.05306 0.02255  133 LEU B O   
2534 C  CB  . LEU B 134 ? 0.29221 0.30494 0.27489 -0.03329 0.00275  -0.01439 133 LEU B CB  
2535 C  CG  . LEU B 134 ? 0.25152 0.28354 0.25052 -0.02821 0.02090  -0.03026 133 LEU B CG  
2536 C  CD1 . LEU B 134 ? 0.27780 0.29388 0.26797 -0.00913 0.02335  -0.03190 133 LEU B CD1 
2537 C  CD2 . LEU B 134 ? 0.31087 0.34389 0.33580 -0.03176 0.01772  -0.03323 133 LEU B CD2 
2538 N  N   . GLY B 135 ? 0.28731 0.33593 0.27922 -0.07412 -0.01390 0.03738  134 GLY B N   
2539 C  CA  . GLY B 135 ? 0.30089 0.32976 0.29021 -0.08337 -0.03943 0.05941  134 GLY B CA  
2540 C  C   . GLY B 135 ? 0.33192 0.35002 0.28530 -0.07469 -0.03769 0.05037  134 GLY B C   
2541 O  O   . GLY B 135 ? 0.36270 0.36552 0.31340 -0.08220 -0.05954 0.06781  134 GLY B O   
2542 N  N   . PHE B 136 ? 0.30713 0.33168 0.24235 -0.06036 -0.01740 0.02752  135 PHE B N   
2543 C  CA  . PHE B 136 ? 0.30525 0.32610 0.21984 -0.05495 -0.01750 0.02489  135 PHE B CA  
2544 C  C   . PHE B 136 ? 0.38688 0.44054 0.29432 -0.07093 -0.01194 0.03750  135 PHE B C   
2545 O  O   . PHE B 136 ? 0.38001 0.47227 0.28963 -0.07532 0.00562  0.03651  135 PHE B O   
2546 C  CB  . PHE B 136 ? 0.29754 0.32401 0.21378 -0.04001 -0.00184 0.00705  135 PHE B CB  
2547 C  CG  . PHE B 136 ? 0.31063 0.31210 0.22474 -0.01666 -0.00440 0.00420  135 PHE B CG  
2548 C  CD1 . PHE B 136 ? 0.32159 0.31769 0.24372 -0.00832 0.00031  -0.00254 135 PHE B CD1 
2549 C  CD2 . PHE B 136 ? 0.33436 0.32218 0.23557 0.00191  -0.01037 0.00987  135 PHE B CD2 
2550 C  CE1 . PHE B 136 ? 0.28475 0.26243 0.19453 0.02025  -0.00048 -0.00255 135 PHE B CE1 
2551 C  CE2 . PHE B 136 ? 0.31641 0.29216 0.20720 0.03350  -0.00780 0.01048  135 PHE B CE2 
2552 C  CZ  . PHE B 136 ? 0.31882 0.28986 0.21019 0.04398  -0.00237 0.00485  135 PHE B CZ  
2553 N  N   . GLN B 137 ? 0.36073 0.40101 0.25485 -0.07431 -0.02706 0.04871  136 GLN B N   
2554 C  CA  A GLN B 137 ? 0.39505 0.46414 0.27521 -0.08672 -0.02486 0.06461  136 GLN B CA  
2555 C  CA  B GLN B 137 ? 0.39861 0.46737 0.27881 -0.08682 -0.02517 0.06487  136 GLN B CA  
2556 C  C   . GLN B 137 ? 0.38387 0.44929 0.24461 -0.07800 -0.02510 0.04858  136 GLN B C   
2557 O  O   . GLN B 137 ? 0.36980 0.40644 0.23473 -0.06906 -0.03610 0.04306  136 GLN B O   
2558 C  CB  A GLN B 137 ? 0.46154 0.51825 0.35112 -0.10249 -0.04956 0.09768  136 GLN B CB  
2559 C  CB  B GLN B 137 ? 0.45914 0.51391 0.34844 -0.10219 -0.05056 0.09736  136 GLN B CB  
2560 C  CG  A GLN B 137 ? 0.51455 0.58443 0.43927 -0.11629 -0.05418 0.12315  136 GLN B CG  
2561 C  CG  B GLN B 137 ? 0.51644 0.57425 0.44193 -0.11514 -0.06073 0.12148  136 GLN B CG  
2562 C  CD  A GLN B 137 ? 0.57675 0.64518 0.52783 -0.13769 -0.08245 0.16752  136 GLN B CD  
2563 C  CD  B GLN B 137 ? 0.52187 0.64424 0.45981 -0.12441 -0.03257 0.14230  136 GLN B CD  
2564 O  OE1 A GLN B 137 ? 0.65284 0.72227 0.58810 -0.14356 -0.09146 0.18148  136 GLN B OE1 
2565 O  OE1 B GLN B 137 ? 0.56571 0.73145 0.48374 -0.12688 -0.01730 0.15912  136 GLN B OE1 
2566 N  NE2 A GLN B 137 ? 0.61065 0.67526 0.61013 -0.15097 -0.10169 0.19342  136 GLN B NE2 
2567 N  NE2 B GLN B 137 ? 0.48302 0.61497 0.45063 -0.12455 -0.02530 0.14152  136 GLN B NE2 
2568 N  N   . ARG B 138 ? 0.35135 0.44750 0.19177 -0.07606 -0.01519 0.04139  137 ARG B N   
2569 C  CA  . ARG B 138 ? 0.38064 0.46862 0.20572 -0.06874 -0.02586 0.02688  137 ARG B CA  
2570 C  C   . ARG B 138 ? 0.41946 0.49474 0.23217 -0.07838 -0.04338 0.04882  137 ARG B C   
2571 O  O   . ARG B 138 ? 0.44916 0.54197 0.24988 -0.09007 -0.04400 0.07603  137 ARG B O   
2572 C  CB  . ARG B 138 ? 0.45261 0.56933 0.24733 -0.05650 -0.02023 0.00889  137 ARG B CB  
2573 C  CG  . ARG B 138 ? 0.56043 0.65759 0.34519 -0.04698 -0.04313 -0.01102 137 ARG B CG  
2574 C  CD  . ARG B 138 ? 0.60623 0.71929 0.35386 -0.02428 -0.04893 -0.04033 137 ARG B CD  
2575 N  NE  . ARG B 138 ? 0.69160 0.77896 0.42630 -0.01557 -0.08210 -0.05656 137 ARG B NE  
2576 C  CZ  . ARG B 138 ? 0.74545 0.82723 0.44810 0.01033  -0.10501 -0.09085 137 ARG B CZ  
2577 N  NH1 . ARG B 138 ? 0.76819 0.87270 0.44500 0.03341  -0.09402 -0.11409 137 ARG B NH1 
2578 N  NH2 . ARG B 138 ? 0.75698 0.80732 0.45452 0.01665  -0.14384 -0.10408 137 ARG B NH2 
2579 N  N   . LEU B 139 ? 0.41276 0.46164 0.23667 -0.07367 -0.05840 0.04233  138 LEU B N   
2580 C  CA  . LEU B 139 ? 0.46257 0.49316 0.28123 -0.07999 -0.07848 0.05978  138 LEU B CA  
2581 C  C   . LEU B 139 ? 0.46906 0.50309 0.26607 -0.07918 -0.09217 0.05477  138 LEU B C   
2582 O  O   . LEU B 139 ? 0.43262 0.46501 0.23780 -0.06920 -0.09637 0.03297  138 LEU B O   
2583 C  CB  . LEU B 139 ? 0.41925 0.42250 0.26591 -0.06800 -0.08568 0.05756  138 LEU B CB  
2584 C  CG  . LEU B 139 ? 0.41125 0.40317 0.26944 -0.05800 -0.07786 0.05585  138 LEU B CG  
2585 C  CD1 . LEU B 139 ? 0.41872 0.39324 0.29168 -0.03293 -0.08113 0.05353  138 LEU B CD1 
2586 C  CD2 . LEU B 139 ? 0.40748 0.38865 0.25687 -0.07173 -0.09262 0.07356  138 LEU B CD2 
2587 N  N   . THR B 140 ? 0.47886 0.51364 0.25243 -0.08936 -0.10563 0.07657  139 THR B N   
2588 C  CA  . THR B 140 ? 0.47835 0.50548 0.23185 -0.08635 -0.12613 0.07194  139 THR B CA  
2589 C  C   . THR B 140 ? 0.55536 0.55269 0.34924 -0.08236 -0.14304 0.06652  139 THR B C   
2590 O  O   . THR B 140 ? 0.49688 0.48297 0.32191 -0.07850 -0.13752 0.07078  139 THR B O   
2591 C  CB  . THR B 140 ? 0.58807 0.62402 0.31618 -0.09548 -0.13339 0.10009  139 THR B CB  
2592 O  OG1 . THR B 140 ? 0.65558 0.66643 0.41647 -0.10664 -0.14662 0.11920  139 THR B OG1 
2593 C  CG2 . THR B 140 ? 0.62098 0.69877 0.33003 -0.09543 -0.10823 0.11742  139 THR B CG2 
2594 N  N   . TRP B 141 ? 0.62667 0.57064 0.32831 -0.13744 -0.11600 0.12555  140 TRP B N   
2595 C  CA  . TRP B 141 ? 0.61267 0.52887 0.33977 -0.10569 -0.13735 0.12856  140 TRP B CA  
2596 C  C   . TRP B 141 ? 0.68280 0.55125 0.43637 -0.09408 -0.16685 0.14850  140 TRP B C   
2597 O  O   . TRP B 141 ? 0.64786 0.49313 0.43573 -0.06137 -0.17574 0.13729  140 TRP B O   
2598 C  CB  . TRP B 141 ? 0.68422 0.62074 0.40017 -0.11582 -0.14389 0.13318  140 TRP B CB  
2599 C  CG  . TRP B 141 ? 0.65812 0.57768 0.40212 -0.08552 -0.16219 0.13171  140 TRP B CG  
2600 C  CD1 . TRP B 141 ? 0.63717 0.53405 0.40154 -0.08134 -0.19090 0.15105  140 TRP B CD1 
2601 C  CD2 . TRP B 141 ? 0.62637 0.55678 0.38970 -0.05751 -0.15038 0.10620  140 TRP B CD2 
2602 N  NE1 . TRP B 141 ? 0.68040 0.57546 0.47312 -0.05198 -0.19753 0.13809  140 TRP B NE1 
2603 C  CE2 . TRP B 141 ? 0.62882 0.54370 0.41698 -0.03835 -0.17498 0.11291  140 TRP B CE2 
2604 C  CE3 . TRP B 141 ? 0.54164 0.49659 0.31995 -0.04565 -0.11740 0.07512  140 TRP B CE3 
2605 C  CZ2 . TRP B 141 ? 0.54298 0.46881 0.36028 -0.01100 -0.16694 0.09029  140 TRP B CZ2 
2606 C  CZ3 . TRP B 141 ? 0.55398 0.51554 0.36225 -0.01937 -0.11167 0.05720  140 TRP B CZ3 
2607 C  CH2 . TRP B 141 ? 0.51438 0.46365 0.33870 -0.00354 -0.13435 0.06417  140 TRP B CH2 
2608 N  N   . GLN B 142 ? 0.72674 0.58500 0.47249 -0.12174 -0.18005 0.17236  141 GLN B N   
2609 C  CA  . GLN B 142 ? 0.79460 0.60794 0.57476 -0.11314 -0.20916 0.18728  141 GLN B CA  
2610 C  C   . GLN B 142 ? 0.72187 0.51351 0.51884 -0.09567 -0.20320 0.17375  141 GLN B C   
2611 O  O   . GLN B 142 ? 0.77274 0.53369 0.61141 -0.06793 -0.21941 0.16394  141 GLN B O   
2612 C  CB  . GLN B 142 ? 0.93824 0.74847 0.70598 -0.15191 -0.22725 0.21797  141 GLN B CB  
2613 C  CG  . GLN B 142 ? 1.08847 0.85625 0.90022 -0.14577 -0.26710 0.23627  141 GLN B CG  
2614 C  CD  . GLN B 142 ? 1.13384 0.86881 0.97201 -0.14266 -0.27795 0.23730  141 GLN B CD  
2615 O  OE1 . GLN B 142 ? 1.12779 0.87258 0.94233 -0.15586 -0.25837 0.23423  141 GLN B OE1 
2616 N  NE2 . GLN B 142 ? 1.15732 0.85558 1.04970 -0.12565 -0.30951 0.23874  141 GLN B NE2 
2617 N  N   . GLU B 143 ? 0.63705 0.44813 0.40582 -0.11243 -0.17951 0.16922  142 GLU B N   
2618 C  CA  . GLU B 143 ? 0.67470 0.47576 0.46665 -0.09799 -0.16751 0.15035  142 GLU B CA  
2619 C  C   . GLU B 143 ? 0.65224 0.46349 0.47484 -0.05998 -0.15118 0.11543  142 GLU B C   
2620 O  O   . GLU B 143 ? 0.58021 0.38221 0.42658 -0.04567 -0.14749 0.09907  142 GLU B O   
2621 C  CB  . GLU B 143 ? 0.68400 0.51800 0.45276 -0.12398 -0.13958 0.14535  142 GLU B CB  
2622 C  CG  . GLU B 143 ? 0.76316 0.59010 0.50309 -0.16711 -0.15355 0.17901  142 GLU B CG  
2623 C  CD  . GLU B 143 ? 0.78666 0.66487 0.49948 -0.19897 -0.12160 0.16973  142 GLU B CD  
2624 O  OE1 . GLU B 143 ? 0.68363 0.60059 0.40549 -0.18607 -0.09103 0.13677  142 GLU B OE1 
2625 O  OE2 . GLU B 143 ? 0.82142 0.70667 0.51763 -0.23503 -0.12655 0.18926  142 GLU B OE2 
2626 N  N   . ALA B 144 ? 0.60937 0.44312 0.43008 -0.04729 -0.14169 0.10439  143 ALA B N   
2627 C  CA  . ALA B 144 ? 0.57600 0.42584 0.42127 -0.01859 -0.12538 0.07599  143 ALA B CA  
2628 C  C   . ALA B 144 ? 0.52297 0.35015 0.40318 0.00623  -0.14287 0.06469  143 ALA B C   
2629 O  O   . ALA B 144 ? 0.47254 0.31227 0.37089 0.02207  -0.13059 0.04164  143 ALA B O   
2630 C  CB  . ALA B 144 ? 0.48962 0.36836 0.32756 -0.01441 -0.11273 0.06849  143 ALA B CB  
2631 N  N   . GLY B 145 ? 0.56369 0.36259 0.45775 0.00841  -0.17232 0.07870  144 GLY B N   
2632 C  CA  . GLY B 145 ? 0.53446 0.31644 0.47574 0.03352  -0.18929 0.05994  144 GLY B CA  
2633 C  C   . GLY B 145 ? 0.53603 0.34396 0.49341 0.05437  -0.18201 0.04056  144 GLY B C   
2634 O  O   . GLY B 145 ? 0.49069 0.32676 0.42315 0.05053  -0.16355 0.04188  144 GLY B O   
2635 N  N   . GLU B 146 ? 0.56936 0.37065 0.57597 0.07648  -0.19603 0.01784  145 GLU B N   
2636 C  CA  . GLU B 146 ? 0.48810 0.31429 0.51779 0.09467  -0.19396 0.00024  145 GLU B CA  
2637 C  C   . GLU B 146 ? 0.47207 0.34435 0.48322 0.09746  -0.15911 -0.01950 145 GLU B C   
2638 O  O   . GLU B 146 ? 0.43944 0.33353 0.44010 0.09830  -0.15112 -0.01599 145 GLU B O   
2639 C  CB  . GLU B 146 ? 0.49849 0.31547 0.59566 0.11735  -0.21364 -0.02882 145 GLU B CB  
2640 C  CG  . GLU B 146 ? 0.73975 0.51900 0.86867 0.11168  -0.24914 -0.00796 145 GLU B CG  
2641 C  CD  . GLU B 146 ? 0.91236 0.69662 1.02702 0.10264  -0.25899 0.01802  145 GLU B CD  
2642 O  OE1 . GLU B 146 ? 0.97416 0.74091 1.05273 0.07771  -0.27028 0.05653  145 GLU B OE1 
2643 O  OE2 . GLU B 146 ? 0.94583 0.75627 1.08463 0.11792  -0.25404 -0.00182 145 GLU B OE2 
2644 N  N   . ARG B 147 ? 0.44541 0.33329 0.45464 0.09676  -0.14127 -0.03844 146 ARG B N   
2645 C  CA  . ARG B 147 ? 0.40873 0.34029 0.40375 0.09537  -0.11447 -0.05105 146 ARG B CA  
2646 C  C   . ARG B 147 ? 0.39665 0.33457 0.35626 0.08189  -0.10199 -0.02672 146 ARG B C   
2647 O  O   . ARG B 147 ? 0.36570 0.32841 0.32324 0.08314  -0.09188 -0.02699 146 ARG B O   
2648 C  CB  . ARG B 147 ? 0.39949 0.34710 0.39490 0.09139  -0.10287 -0.07041 146 ARG B CB  
2649 C  CG  . ARG B 147 ? 0.37594 0.37195 0.35738 0.08476  -0.08093 -0.07798 146 ARG B CG  
2650 C  CD  . ARG B 147 ? 0.41317 0.43220 0.39230 0.07668  -0.07284 -0.09746 146 ARG B CD  
2651 N  NE  . ARG B 147 ? 0.39395 0.38620 0.35700 0.06708  -0.07675 -0.08156 146 ARG B NE  
2652 C  CZ  . ARG B 147 ? 0.36176 0.35590 0.30183 0.05503  -0.07020 -0.05644 146 ARG B CZ  
2653 N  NH1 . ARG B 147 ? 0.33695 0.35429 0.26980 0.05140  -0.06162 -0.04332 146 ARG B NH1 
2654 N  NH2 . ARG B 147 ? 0.37755 0.35104 0.30945 0.04656  -0.07352 -0.04599 146 ARG B NH2 
2655 N  N   . LEU B 148 ? 0.37941 0.29792 0.31705 0.06799  -0.10224 -0.00890 147 LEU B N   
2656 C  CA  . LEU B 148 ? 0.35894 0.28920 0.27467 0.05559  -0.08870 0.00476  147 LEU B CA  
2657 C  C   . LEU B 148 ? 0.39393 0.32312 0.30137 0.05295  -0.09459 0.01454  147 LEU B C   
2658 O  O   . LEU B 148 ? 0.37580 0.32559 0.27972 0.04956  -0.08190 0.01348  147 LEU B O   
2659 C  CB  . LEU B 148 ? 0.40942 0.32766 0.30933 0.03976  -0.08547 0.01546  147 LEU B CB  
2660 C  CG  . LEU B 148 ? 0.40209 0.32823 0.30936 0.04012  -0.07852 0.00622  147 LEU B CG  
2661 C  CD1 . LEU B 148 ? 0.41634 0.33047 0.31344 0.02481  -0.07734 0.01543  147 LEU B CD1 
2662 C  CD2 . LEU B 148 ? 0.41270 0.37167 0.32748 0.04214  -0.06470 0.00148  147 LEU B CD2 
2663 N  N   . ARG B 149 ? 0.39880 0.30473 0.30668 0.05286  -0.11639 0.02470  148 ARG B N   
2664 C  CA  . ARG B 149 ? 0.44196 0.35157 0.34030 0.04819  -0.12558 0.03520  148 ARG B CA  
2665 C  C   . ARG B 149 ? 0.43572 0.36916 0.35484 0.06407  -0.11949 0.01958  148 ARG B C   
2666 O  O   . ARG B 149 ? 0.41874 0.36910 0.32843 0.05852  -0.11369 0.02103  148 ARG B O   
2667 C  CB  . ARG B 149 ? 0.47333 0.35226 0.37532 0.04456  -0.15805 0.05454  148 ARG B CB  
2668 C  CG  . ARG B 149 ? 0.47648 0.34061 0.34394 0.01644  -0.16525 0.08011  148 ARG B CG  
2669 C  CD  . ARG B 149 ? 0.56689 0.40505 0.43248 0.00468  -0.20197 0.10971  148 ARG B CD  
2670 N  NE  . ARG B 149 ? 0.62934 0.43621 0.54294 0.02024  -0.22416 0.10747  148 ARG B NE  
2671 C  CZ  . ARG B 149 ? 0.64848 0.42763 0.56989 0.01044  -0.23532 0.11778  148 ARG B CZ  
2672 N  NH1 . ARG B 149 ? 0.61630 0.36940 0.59058 0.02497  -0.25693 0.10956  148 ARG B NH1 
2673 N  NH2 . ARG B 149 ? 0.61790 0.39873 0.49942 -0.01480 -0.22437 0.13258  148 ARG B NH2 
2674 N  N   . ALA B 150 ? 0.41624 0.35552 0.36550 0.08150  -0.12032 0.00167  149 ALA B N   
2675 C  CA  . ALA B 150 ? 0.38715 0.35592 0.35690 0.09283  -0.11285 -0.01395 149 ALA B CA  
2676 C  C   . ALA B 150 ? 0.38137 0.37627 0.33936 0.08490  -0.08978 -0.01460 149 ALA B C   
2677 O  O   . ALA B 150 ? 0.34411 0.35801 0.30858 0.08554  -0.08545 -0.01657 149 ALA B O   
2678 C  CB  . ALA B 150 ? 0.39714 0.37742 0.40210 0.10821  -0.11449 -0.03918 149 ALA B CB  
2679 N  N   . ILE B 151 ? 0.32019 0.31569 0.26780 0.07730  -0.07807 -0.01231 150 ILE B N   
2680 C  CA  . ILE B 151 ? 0.28199 0.29713 0.22948 0.06927  -0.06288 -0.00861 150 ILE B CA  
2681 C  C   . ILE B 151 ? 0.29757 0.30921 0.23845 0.06088  -0.06021 -0.00248 150 ILE B C   
2682 O  O   . ILE B 151 ? 0.30492 0.33275 0.25942 0.05921  -0.05402 -0.00448 150 ILE B O   
2683 C  CB  . ILE B 151 ? 0.28624 0.30164 0.22973 0.06257  -0.05648 -0.00539 150 ILE B CB  
2684 C  CG1 . ILE B 151 ? 0.36079 0.39219 0.30957 0.06646  -0.05624 -0.01722 150 ILE B CG1 
2685 C  CG2 . ILE B 151 ? 0.30526 0.33514 0.26004 0.05377  -0.04774 0.00322  150 ILE B CG2 
2686 C  CD1 . ILE B 151 ? 0.36805 0.39733 0.30895 0.05874  -0.05424 -0.01503 150 ILE B CD1 
2687 N  N   . LEU B 152 ? 0.30894 0.30340 0.23056 0.05220  -0.06424 0.00321  151 LEU B N   
2688 C  CA  . LEU B 152 ? 0.29576 0.29773 0.20881 0.03938  -0.05856 0.00182  151 LEU B CA  
2689 C  C   . LEU B 152 ? 0.31074 0.32145 0.22407 0.04146  -0.06575 -0.00065 151 LEU B C   
2690 O  O   . LEU B 152 ? 0.30267 0.33032 0.22436 0.03553  -0.05728 -0.01017 151 LEU B O   
2691 C  CB  . LEU B 152 ? 0.34425 0.33465 0.22978 0.02313  -0.06176 0.00954  151 LEU B CB  
2692 C  CG  . LEU B 152 ? 0.35760 0.34457 0.24621 0.01806  -0.05227 0.00924  151 LEU B CG  
2693 C  CD1 . LEU B 152 ? 0.37250 0.34669 0.23138 -0.00025 -0.05913 0.02114  151 LEU B CD1 
2694 C  CD2 . LEU B 152 ? 0.30265 0.31182 0.21603 0.01349  -0.03445 -0.00502 151 LEU B CD2 
2695 N  N   . GLY B 153 ? 0.34807 0.34802 0.25907 0.04989  -0.08316 0.00554  152 GLY B N   
2696 C  CA  . GLY B 153 ? 0.33849 0.34895 0.25462 0.05253  -0.09265 0.00381  152 GLY B CA  
2697 C  C   . GLY B 153 ? 0.30252 0.33482 0.24604 0.06167  -0.08171 -0.00818 152 GLY B C   
2698 O  O   . GLY B 153 ? 0.33180 0.37898 0.28041 0.05703  -0.07967 -0.01378 152 GLY B O   
2699 N  N   . HIS B 154 ? 0.28435 0.32220 0.24469 0.07077  -0.07487 -0.01191 153 HIS B N   
2700 C  CA  . HIS B 154 ? 0.32110 0.38377 0.30450 0.07304  -0.06632 -0.01775 153 HIS B CA  
2701 C  C   . HIS B 154 ? 0.28543 0.35331 0.27759 0.06240  -0.05551 -0.01630 153 HIS B C   
2702 O  O   . HIS B 154 ? 0.30519 0.38747 0.31656 0.05984  -0.05357 -0.01967 153 HIS B O   
2703 C  CB  . HIS B 154 ? 0.31087 0.38784 0.30457 0.07807  -0.06149 -0.02173 153 HIS B CB  
2704 C  CG  . HIS B 154 ? 0.26454 0.37399 0.27786 0.07475  -0.05446 -0.02457 153 HIS B CG  
2705 N  ND1 . HIS B 154 ? 0.28137 0.40810 0.29862 0.06326  -0.04595 -0.01576 153 HIS B ND1 
2706 C  CD2 . HIS B 154 ? 0.31302 0.44303 0.34359 0.07797  -0.05657 -0.03226 153 HIS B CD2 
2707 C  CE1 . HIS B 154 ? 0.29885 0.45569 0.33196 0.05701  -0.04261 -0.01600 153 HIS B CE1 
2708 N  NE2 . HIS B 154 ? 0.28341 0.44370 0.32596 0.06682  -0.04724 -0.02837 153 HIS B NE2 
2709 N  N   . GLU B 155 ? 0.24445 0.30076 0.23033 0.05611  -0.04988 -0.01355 154 GLU B N   
2710 C  CA  . GLU B 155 ? 0.26573 0.32645 0.27379 0.04784  -0.04194 -0.01852 154 GLU B CA  
2711 C  C   . GLU B 155 ? 0.25924 0.32777 0.26897 0.04236  -0.04149 -0.03230 154 GLU B C   
2712 O  O   . GLU B 155 ? 0.27331 0.35168 0.31550 0.03937  -0.03820 -0.04094 154 GLU B O   
2713 C  CB  . GLU B 155 ? 0.24912 0.30031 0.25306 0.04218  -0.03628 -0.01934 154 GLU B CB  
2714 C  CG  . GLU B 155 ? 0.24749 0.29519 0.25779 0.04446  -0.03721 -0.00657 154 GLU B CG  
2715 C  CD  . GLU B 155 ? 0.26194 0.30168 0.27094 0.03906  -0.03277 -0.00797 154 GLU B CD  
2716 O  OE1 . GLU B 155 ? 0.27143 0.31152 0.27322 0.03187  -0.02663 -0.02011 154 GLU B OE1 
2717 O  OE2 . GLU B 155 ? 0.27577 0.31426 0.29049 0.03915  -0.03519 0.00234  154 GLU B OE2 
2718 N  N   . GLN B 156 ? 0.27830 0.34349 0.25512 0.03811  -0.04703 -0.03376 155 GLN B N   
2719 C  CA  . GLN B 156 ? 0.30466 0.38439 0.27725 0.02769  -0.04708 -0.04762 155 GLN B CA  
2720 C  C   . GLN B 156 ? 0.35171 0.44186 0.34392 0.03442  -0.05331 -0.04947 155 GLN B C   
2721 O  O   . GLN B 156 ? 0.37106 0.47588 0.38059 0.02719  -0.04960 -0.06558 155 GLN B O   
2722 C  CB  . GLN B 156 ? 0.37853 0.45574 0.30665 0.01599  -0.05703 -0.04071 155 GLN B CB  
2723 C  CG  . GLN B 156 ? 0.40387 0.47622 0.31111 0.00343  -0.04932 -0.03926 155 GLN B CG  
2724 C  CD  . GLN B 156 ? 0.64262 0.70616 0.50473 -0.01028 -0.06532 -0.02004 155 GLN B CD  
2725 O  OE1 . GLN B 156 ? 0.74354 0.80778 0.58968 -0.01357 -0.08375 -0.00936 155 GLN B OE1 
2726 N  NE2 . GLN B 156 ? 0.66305 0.71801 0.50804 -0.02011 -0.06145 -0.01267 155 GLN B NE2 
2727 N  N   . GLU B 157 ? 0.30391 0.39080 0.29928 0.04708  -0.06125 -0.03749 156 GLU B N   
2728 C  CA  . GLU B 157 ? 0.26357 0.36615 0.27899 0.05190  -0.06641 -0.04031 156 GLU B CA  
2729 C  C   . GLU B 157 ? 0.30236 0.41537 0.35452 0.04823  -0.05728 -0.04360 156 GLU B C   
2730 O  O   . GLU B 157 ? 0.32317 0.45057 0.39534 0.04593  -0.05972 -0.04954 156 GLU B O   
2731 C  CB  . GLU B 157 ? 0.30174 0.40666 0.31958 0.06518  -0.07437 -0.03370 156 GLU B CB  
2732 C  CG  . GLU B 157 ? 0.46592 0.55588 0.46305 0.07056  -0.09115 -0.02821 156 GLU B CG  
2733 C  CD  . GLU B 157 ? 0.47889 0.57342 0.49610 0.08639  -0.09920 -0.03106 156 GLU B CD  
2734 O  OE1 . GLU B 157 ? 0.38773 0.50735 0.43000 0.09057  -0.09056 -0.04002 156 GLU B OE1 
2735 O  OE2 . GLU B 157 ? 0.45730 0.53275 0.46913 0.09269  -0.11469 -0.02591 156 GLU B OE2 
2736 N  N   . ILE B 158 ? 0.29574 0.40099 0.36069 0.04620  -0.05017 -0.03711 157 ILE B N   
2737 C  CA  . ILE B 158 ? 0.27593 0.38745 0.38025 0.04081  -0.04856 -0.03009 157 ILE B CA  
2738 C  C   . ILE B 158 ? 0.29958 0.40323 0.43941 0.03432  -0.04557 -0.04194 157 ILE B C   
2739 O  O   . ILE B 158 ? 0.29092 0.39235 0.47335 0.02939  -0.04941 -0.03204 157 ILE B O   
2740 C  CB  . ILE B 158 ? 0.26073 0.37498 0.36258 0.04010  -0.04843 -0.01010 157 ILE B CB  
2741 C  CG1 . ILE B 158 ? 0.27345 0.37071 0.36282 0.04152  -0.04582 -0.00741 157 ILE B CG1 
2742 C  CG2 . ILE B 158 ? 0.29666 0.42864 0.37760 0.04557  -0.04884 -0.00900 157 ILE B CG2 
2743 C  CD1 . ILE B 158 ? 0.32275 0.42554 0.40996 0.03708  -0.04737 0.01202  157 ILE B CD1 
2744 N  N   . GLY B 159 ? 0.28674 0.38959 0.41514 0.03182  -0.04017 -0.06401 158 GLY B N   
2745 C  CA  . GLY B 159 ? 0.27086 0.37638 0.44282 0.02524  -0.03472 -0.08874 158 GLY B CA  
2746 C  C   . GLY B 159 ? 0.22034 0.32479 0.39131 0.02201  -0.02502 -0.10425 158 GLY B C   
2747 O  O   . GLY B 159 ? 0.27257 0.38707 0.48493 0.01615  -0.01779 -0.13514 158 GLY B O   
2748 N  N   . PHE B 160 ? 0.21985 0.31579 0.35110 0.02458  -0.02373 -0.08845 159 PHE B N   
2749 C  CA  . PHE B 160 ? 0.22629 0.32580 0.35583 0.01857  -0.01339 -0.10362 159 PHE B CA  
2750 C  C   . PHE B 160 ? 0.32139 0.44059 0.41001 0.00395  -0.00502 -0.12537 159 PHE B C   
2751 O  O   . PHE B 160 ? 0.37400 0.49442 0.41819 0.00109  -0.01260 -0.11489 159 PHE B O   
2752 C  CB  . PHE B 160 ? 0.25048 0.33475 0.35079 0.02335  -0.01606 -0.07882 159 PHE B CB  
2753 C  CG  . PHE B 160 ? 0.22977 0.30267 0.36529 0.03078  -0.02400 -0.05770 159 PHE B CG  
2754 C  CD1 . PHE B 160 ? 0.24512 0.31454 0.37107 0.03539  -0.03345 -0.03387 159 PHE B CD1 
2755 C  CD2 . PHE B 160 ? 0.25269 0.32382 0.42997 0.03009  -0.02297 -0.06154 159 PHE B CD2 
2756 C  CE1 . PHE B 160 ? 0.27438 0.34088 0.42380 0.03476  -0.04221 -0.01046 159 PHE B CE1 
2757 C  CE2 . PHE B 160 ? 0.26531 0.32767 0.47133 0.03278  -0.03556 -0.03556 159 PHE B CE2 
2758 C  CZ  . PHE B 160 ? 0.24139 0.30251 0.42883 0.03287  -0.04537 -0.00824 159 PHE B CZ  
2759 N  N   . ALA B 161 ? 0.29686 0.43616 0.40430 -0.00777 0.00940  -0.15633 160 ALA B N   
2760 C  CA  . ALA B 161 ? 0.31832 0.48637 0.38022 -0.03021 0.01957  -0.17647 160 ALA B CA  
2761 C  C   . ALA B 161 ? 0.35878 0.51699 0.36623 -0.03684 0.01765  -0.15085 160 ALA B C   
2762 O  O   . ALA B 161 ? 0.32610 0.47492 0.35264 -0.03127 0.02222  -0.14661 160 ALA B O   
2763 C  CB  . ALA B 161 ? 0.32875 0.53267 0.43791 -0.04341 0.03948  -0.22755 160 ALA B CB  
2764 N  N   . ALA B 162 ? 0.48290 0.64281 0.42738 -0.05016 0.00787  -0.13261 161 ALA B N   
2765 C  CA  . ALA B 162 ? 0.52874 0.67081 0.42697 -0.05570 -0.00079 -0.10196 161 ALA B CA  
2766 C  C   . ALA B 162 ? 0.44754 0.60804 0.34593 -0.07259 0.01667  -0.11682 161 ALA B C   
2767 O  O   . ALA B 162 ? 0.42085 0.55979 0.32305 -0.06403 0.01501  -0.10020 161 ALA B O   
2768 C  CB  . ALA B 162 ? 0.54341 0.68834 0.38325 -0.07332 -0.01838 -0.08084 161 ALA B CB  
2769 N  N   . ASP B 163 ? 0.45133 0.65747 0.34777 -0.09855 0.03481  -0.15215 162 ASP B N   
2770 C  CA  . ASP B 163 ? 0.42291 0.65826 0.31964 -0.11957 0.05434  -0.17162 162 ASP B CA  
2771 C  C   . ASP B 163 ? 0.44774 0.67677 0.41756 -0.09851 0.06558  -0.19097 162 ASP B C   
2772 O  O   . ASP B 163 ? 0.48486 0.73402 0.46302 -0.11128 0.07981  -0.20423 162 ASP B O   
2773 C  CB  . ASP B 163 ? 0.54744 0.84156 0.43733 -0.15277 0.07317  -0.20872 162 ASP B CB  
2774 C  CG  . ASP B 163 ? 0.67210 0.97369 0.49368 -0.18170 0.05971  -0.17416 162 ASP B CG  
2775 O  OD1 . ASP B 163 ? 0.62884 0.89311 0.40443 -0.17962 0.03725  -0.12888 162 ASP B OD1 
2776 O  OD2 . ASP B 163 ? 0.70237 1.04757 0.52340 -0.20695 0.06945  -0.19225 162 ASP B OD2 
2777 N  N   . SER B 164 ? 0.33045 0.53378 0.35446 -0.06928 0.05711  -0.18968 163 SER B N   
2778 C  CA  . SER B 164 ? 0.28941 0.48738 0.38811 -0.05239 0.06135  -0.20320 163 SER B CA  
2779 C  C   . SER B 164 ? 0.27293 0.43356 0.36295 -0.03702 0.04756  -0.16322 163 SER B C   
2780 O  O   . SER B 164 ? 0.25674 0.41445 0.40213 -0.02690 0.04780  -0.16829 163 SER B O   
2781 C  CB  . SER B 164 ? 0.27463 0.46541 0.44286 -0.03410 0.05528  -0.21838 163 SER B CB  
2782 O  OG  . SER B 164 ? 0.31177 0.46637 0.46126 -0.01755 0.03548  -0.17918 163 SER B OG  
2783 N  N   . ARG B 165 ? 0.27970 0.41420 0.30745 -0.03582 0.03401  -0.12638 164 ARG B N   
2784 C  CA  . ARG B 165 ? 0.26554 0.36693 0.28668 -0.02055 0.02041  -0.09359 164 ARG B CA  
2785 C  C   . ARG B 165 ? 0.28663 0.37964 0.25457 -0.03405 0.01824  -0.07559 164 ARG B C   
2786 O  O   . ARG B 165 ? 0.33553 0.43953 0.25893 -0.05404 0.01944  -0.07460 164 ARG B O   
2787 C  CB  . ARG B 165 ? 0.25501 0.33252 0.26445 -0.00394 0.00428  -0.07048 164 ARG B CB  
2788 C  CG  . ARG B 165 ? 0.26555 0.34814 0.32566 0.00662  0.00273  -0.08100 164 ARG B CG  
2789 C  CD  . ARG B 165 ? 0.25031 0.32716 0.36563 0.01591  -0.00155 -0.07560 164 ARG B CD  
2790 N  NE  . ARG B 165 ? 0.24020 0.29841 0.33572 0.02445  -0.01440 -0.04390 164 ARG B NE  
2791 C  CZ  . ARG B 165 ? 0.20443 0.25874 0.33636 0.02879  -0.02394 -0.02871 164 ARG B CZ  
2792 N  NH1 . ARG B 165 ? 0.21531 0.27599 0.41171 0.02874  -0.02566 -0.03924 164 ARG B NH1 
2793 N  NH2 . ARG B 165 ? 0.24022 0.28736 0.34762 0.03130  -0.03340 -0.00413 164 ARG B NH2 
2794 N  N   . CYS B 166 ? 0.29241 0.36525 0.26436 -0.02534 0.01163  -0.05805 165 CYS B N   
2795 C  CA  . CYS B 166 ? 0.32688 0.38393 0.25612 -0.03569 0.00533  -0.03847 165 CYS B CA  
2796 C  C   . CYS B 166 ? 0.30932 0.33846 0.24313 -0.01805 -0.00784 -0.01921 165 CYS B C   
2797 O  O   . CYS B 166 ? 0.30248 0.33305 0.27230 -0.00453 -0.00880 -0.02068 165 CYS B O   
2798 C  CB  . CYS B 166 ? 0.47475 0.55506 0.40632 -0.05732 0.02009  -0.05142 165 CYS B CB  
2799 S  SG  . CYS B 166 ? 0.45414 0.55211 0.45964 -0.04765 0.03094  -0.07267 165 CYS B SG  
2800 N  N   . ALA B 167 ? 0.34177 0.34775 0.24104 -0.02117 -0.01987 -0.00129 166 ALA B N   
2801 C  CA  . ALA B 167 ? 0.29791 0.28369 0.20025 -0.01059 -0.02945 0.00915  166 ALA B CA  
2802 C  C   . ALA B 167 ? 0.30720 0.29486 0.20983 -0.02484 -0.02447 0.00974  166 ALA B C   
2803 O  O   . ALA B 167 ? 0.33425 0.33109 0.21969 -0.04580 -0.01821 0.00919  166 ALA B O   
2804 C  CB  . ALA B 167 ? 0.37968 0.33802 0.25890 -0.00440 -0.04734 0.02201  166 ALA B CB  
2805 N  N   . MSE B 168 ? 0.29435 0.27787 0.21458 -0.01676 -0.02767 0.01129  167 MSE B N   
2806 C  CA  . MSE B 168 ? 0.31494 0.30104 0.24045 -0.02906 -0.02458 0.01148  167 MSE B CA  
2807 C  C   . MSE B 168 ? 0.31211 0.27813 0.23181 -0.02286 -0.03742 0.01899  167 MSE B C   
2808 O  O   . MSE B 168 ? 0.31928 0.28282 0.24263 -0.00864 -0.04418 0.01869  167 MSE B O   
2809 C  CB  . MSE B 168 ? 0.30753 0.32139 0.27729 -0.02889 -0.01408 -0.00102 167 MSE B CB  
2810 C  CG  . MSE B 168 ? 0.28862 0.32845 0.28037 -0.03334 0.00039  -0.01953 167 MSE B CG  
2811 SE SE  . MSE B 168 ? 0.32336 0.39716 0.39758 -0.03049 0.00914  -0.04195 167 MSE B SE  
2812 C  CE  . MSE B 168 ? 0.28195 0.38272 0.35062 -0.05814 0.02759  -0.05891 167 MSE B CE  
2813 N  N   . ARG B 169 ? 0.33091 0.28854 0.24372 -0.03656 -0.03934 0.02271  168 ARG B N   
2814 C  CA  . ARG B 169 ? 0.34155 0.28206 0.25287 -0.03302 -0.05112 0.02432  168 ARG B CA  
2815 C  C   . ARG B 169 ? 0.34938 0.30121 0.27507 -0.04617 -0.04721 0.02307  168 ARG B C   
2816 O  O   . ARG B 169 ? 0.36981 0.32953 0.29402 -0.06405 -0.03880 0.02454  168 ARG B O   
2817 C  CB  . ARG B 169 ? 0.38343 0.28929 0.27482 -0.03569 -0.06588 0.03162  168 ARG B CB  
2818 C  CG  . ARG B 169 ? 0.37464 0.26415 0.27407 -0.02854 -0.07819 0.02338  168 ARG B CG  
2819 C  CD  . ARG B 169 ? 0.41558 0.26711 0.31264 -0.02853 -0.09710 0.02833  168 ARG B CD  
2820 N  NE  . ARG B 169 ? 0.41871 0.26394 0.31721 -0.01311 -0.10364 0.02639  168 ARG B NE  
2821 C  CZ  . ARG B 169 ? 0.46596 0.29508 0.35351 -0.01903 -0.11334 0.04370  168 ARG B CZ  
2822 N  NH1 . ARG B 169 ? 0.48258 0.30431 0.35110 -0.04368 -0.11566 0.06501  168 ARG B NH1 
2823 N  NH2 . ARG B 169 ? 0.51033 0.33583 0.40497 -0.00353 -0.12124 0.04035  168 ARG B NH2 
2824 N  N   . LEU B 170 ? 0.35128 0.30912 0.28977 -0.04039 -0.05349 0.01964  169 LEU B N   
2825 C  CA  . LEU B 170 ? 0.32972 0.29533 0.28195 -0.05213 -0.05501 0.01875  169 LEU B CA  
2826 C  C   . LEU B 170 ? 0.35294 0.29425 0.29048 -0.05366 -0.06776 0.01557  169 LEU B C   
2827 O  O   . LEU B 170 ? 0.36088 0.30593 0.29628 -0.04398 -0.07463 0.00746  169 LEU B O   
2828 C  CB  . LEU B 170 ? 0.30725 0.30217 0.28984 -0.04748 -0.05683 0.01865  169 LEU B CB  
2829 C  CG  . LEU B 170 ? 0.31278 0.31886 0.31250 -0.05862 -0.06304 0.01833  169 LEU B CG  
2830 C  CD1 . LEU B 170 ? 0.34994 0.36249 0.36524 -0.07344 -0.05263 0.01490  169 LEU B CD1 
2831 C  CD2 . LEU B 170 ? 0.29967 0.33340 0.33038 -0.05484 -0.07262 0.02506  169 LEU B CD2 
2832 N  N   . VAL B 171 ? 0.37957 0.29901 0.30970 -0.06848 -0.07128 0.02018  170 VAL B N   
2833 C  CA  . VAL B 171 ? 0.40673 0.29801 0.33455 -0.07032 -0.08618 0.01451  170 VAL B CA  
2834 C  C   . VAL B 171 ? 0.40555 0.31287 0.34700 -0.07804 -0.08842 0.00619  170 VAL B C   
2835 O  O   . VAL B 171 ? 0.40542 0.32965 0.35776 -0.09186 -0.08189 0.01214  170 VAL B O   
2836 C  CB  . VAL B 171 ? 0.44291 0.29999 0.36178 -0.08638 -0.09495 0.02909  170 VAL B CB  
2837 C  CG1 . VAL B 171 ? 0.47451 0.29905 0.40586 -0.08873 -0.11371 0.02108  170 VAL B CG1 
2838 C  CG2 . VAL B 171 ? 0.45255 0.29380 0.35750 -0.07958 -0.09880 0.03932  170 VAL B CG2 
2839 N  N   . LEU B 172 ? 0.41255 0.31917 0.35566 -0.07082 -0.09750 -0.01076 171 LEU B N   
2840 C  CA  . LEU B 172 ? 0.41712 0.34140 0.36914 -0.08028 -0.10245 -0.02065 171 LEU B CA  
2841 C  C   . LEU B 172 ? 0.49367 0.38506 0.45321 -0.09133 -0.11351 -0.02833 171 LEU B C   
2842 O  O   . LEU B 172 ? 0.52034 0.38654 0.48468 -0.08390 -0.12325 -0.04441 171 LEU B O   
2843 C  CB  . LEU B 172 ? 0.41802 0.36987 0.36405 -0.07273 -0.10544 -0.03807 171 LEU B CB  
2844 C  CG  . LEU B 172 ? 0.40823 0.39262 0.34909 -0.06556 -0.09949 -0.02645 171 LEU B CG  
2845 C  CD1 . LEU B 172 ? 0.40422 0.41997 0.33191 -0.06582 -0.10299 -0.04264 171 LEU B CD1 
2846 C  CD2 . LEU B 172 ? 0.37235 0.37900 0.33100 -0.07374 -0.09928 -0.00749 171 LEU B CD2 
2847 N  N   . GLY B 173 ? 0.47533 0.36728 0.44307 -0.10949 -0.11288 -0.01778 172 GLY B N   
2848 C  CA  . GLY B 173 ? 0.57987 0.44053 0.55804 -0.12460 -0.12496 -0.02063 172 GLY B CA  
2849 C  C   . GLY B 173 ? 0.67808 0.54509 0.66762 -0.12497 -0.13516 -0.04829 172 GLY B C   
2850 O  O   . GLY B 173 ? 0.67727 0.58417 0.66314 -0.12342 -0.13184 -0.05772 172 GLY B O   
2851 N  N   . SER B 174 ? 0.69067 0.51956 0.69687 -0.12945 -0.14999 -0.06114 173 SER B N   
2852 C  CA  . SER B 174 ? 0.73215 0.56787 0.75399 -0.13174 -0.15930 -0.09570 173 SER B CA  
2853 C  C   . SER B 174 ? 0.74081 0.57808 0.77461 -0.15498 -0.16476 -0.09204 173 SER B C   
2854 O  O   . SER B 174 ? 0.66566 0.49531 0.69911 -0.17030 -0.16161 -0.06343 173 SER B O   
2855 C  CB  . SER B 174 ? 0.80953 0.60460 0.85853 -0.12112 -0.17429 -0.12162 173 SER B CB  
2856 O  OG  . SER B 174 ? 0.87330 0.61437 0.94222 -0.13215 -0.18999 -0.09929 173 SER B OG  
2857 O  OXT . SER B 174 ? 0.67932 0.53083 0.72380 -0.16124 -0.17160 -0.12016 173 SER B OXT 
# 
