data_9EMZ
# 
_entry.id   9EMZ 
# 
_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   9EMZ         pdb_00009emz 10.2210/pdb9emz/pdb 
WWPDB D_1292134609 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-26 ? 
2 'Structure model' 1 1 2025-04-02 ? 
3 'Structure model' 1 2 2025-05-21 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.pdbx_database_id_DOI'    
7  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 2 'Structure model' '_citation_author.identifier_ORCID' 
11 2 'Structure model' '_citation_author.name'             
12 3 'Structure model' '_citation.journal_volume'          
13 3 'Structure model' '_citation.page_first'              
14 3 'Structure model' '_citation.page_last'               
15 3 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EMZ 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        'In meso structure of unlabelled protein' 
_pdbx_database_related.db_id          5DIR 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              Chia-Ying.Huang@psi.ch 
_pdbx_contact_author.name_first         Chia-Ying 
_pdbx_contact_author.name_last          Huang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7676-0239 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bailey, J.'    1 ?                   
'Boland, C.'    2 ?                   
'Caffrey, M.'   3 0000-0002-2931-4551 
'Huang, C.-Y.'  4 0000-0002-7676-0239 
'Gawrisch, K.'  5 ?                   
'Kooshapur, H.' 6 ?                   
'Ramberg, K.O.' 7 0000-0002-3991-4809 
'Soubias, O.'   8 ?                   
'Wiktor, M.'    9 ?                   
# 
_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            Biophys.J. 
_citation.journal_id_ASTM           BIOJAU 
_citation.journal_id_CSD            0030 
_citation.journal_id_ISSN           1542-0086 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            124 
_citation.language                  ? 
_citation.page_first                1387 
_citation.page_last                 1400 
_citation.title                     'Solid-state NMR of membrane peptides and proteins in the lipid cubic phase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bpj.2025.03.012 
_citation.pdbx_database_id_PubMed   40119522 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ramberg, K.O.' 1 ? 
primary 'Boland, C.'    2 ? 
primary 'Kooshapur, H.' 3 ? 
primary 'Soubias, O.'   4 ? 
primary 'Wiktor, M.'    5 ? 
primary 'Huang, C.Y.'   6 ? 
primary 'Bailey, J.'    7 ? 
primary 'Gawrisch, K.'  8 ? 
primary 'Caffrey, M.'   9 ? 
# 
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 'Lipoprotein signal peptidase'                   19013.232 4  3.4.23.36 ? ? ?          
2 polymer     syn Globomycin                                       673.838   4  ?         ? ? Globomycin 
3 non-polymer syn '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 356.540   24 ?         ? ? ?          
4 water       nat water                                            18.015    12 ?         ? ? ?          
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'LspPae,Prolipoprotein signal peptidase,Signal peptidase II,SPase II' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;MPDVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSMYQQIVVIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVV
SASLVVWLKRLKKGETWLAIALALVLGGALGNLYDRMVLGHVVDFILVHWQNRWYFPAFNLADSAITVGAVMLALDMFRS
KKSGEAAHG
;
;MPDVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSMYQQIVVIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVV
SASLVVWLKRLKKGETWLAIALALVLGGALGNLYDRMVLGHVVDFILVHWQNRWYFPAFNLADSAITVGAVMLALDMFRS
KKSGEAAHG
;
A,B,C,D ? 
2 'polypeptide(L)' no yes '(MLE)(IIL)S(ALO)(5BV)' LISTX E,F,G,H ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' OLC 
4 water                                            HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PRO n 
1 3   ASP n 
1 4   VAL n 
1 5   ASP n 
1 6   ARG n 
1 7   PHE n 
1 8   GLY n 
1 9   ARG n 
1 10  LEU n 
1 11  PRO n 
1 12  TRP n 
1 13  LEU n 
1 14  TRP n 
1 15  ILE n 
1 16  THR n 
1 17  VAL n 
1 18  LEU n 
1 19  VAL n 
1 20  PHE n 
1 21  VAL n 
1 22  LEU n 
1 23  ASP n 
1 24  GLN n 
1 25  VAL n 
1 26  SER n 
1 27  LYS n 
1 28  ALA n 
1 29  PHE n 
1 30  PHE n 
1 31  GLN n 
1 32  ALA n 
1 33  GLU n 
1 34  LEU n 
1 35  SER n 
1 36  MET n 
1 37  TYR n 
1 38  GLN n 
1 39  GLN n 
1 40  ILE n 
1 41  VAL n 
1 42  VAL n 
1 43  ILE n 
1 44  PRO n 
1 45  ASP n 
1 46  LEU n 
1 47  PHE n 
1 48  SER n 
1 49  TRP n 
1 50  THR n 
1 51  LEU n 
1 52  ALA n 
1 53  TYR n 
1 54  ASN n 
1 55  THR n 
1 56  GLY n 
1 57  ALA n 
1 58  ALA n 
1 59  PHE n 
1 60  SER n 
1 61  PHE n 
1 62  LEU n 
1 63  ALA n 
1 64  ASP n 
1 65  SER n 
1 66  SER n 
1 67  GLY n 
1 68  TRP n 
1 69  GLN n 
1 70  ARG n 
1 71  TRP n 
1 72  LEU n 
1 73  PHE n 
1 74  ALA n 
1 75  LEU n 
1 76  ILE n 
1 77  ALA n 
1 78  ILE n 
1 79  VAL n 
1 80  VAL n 
1 81  SER n 
1 82  ALA n 
1 83  SER n 
1 84  LEU n 
1 85  VAL n 
1 86  VAL n 
1 87  TRP n 
1 88  LEU n 
1 89  LYS n 
1 90  ARG n 
1 91  LEU n 
1 92  LYS n 
1 93  LYS n 
1 94  GLY n 
1 95  GLU n 
1 96  THR n 
1 97  TRP n 
1 98  LEU n 
1 99  ALA n 
1 100 ILE n 
1 101 ALA n 
1 102 LEU n 
1 103 ALA n 
1 104 LEU n 
1 105 VAL n 
1 106 LEU n 
1 107 GLY n 
1 108 GLY n 
1 109 ALA n 
1 110 LEU n 
1 111 GLY n 
1 112 ASN n 
1 113 LEU n 
1 114 TYR n 
1 115 ASP n 
1 116 ARG n 
1 117 MET n 
1 118 VAL n 
1 119 LEU n 
1 120 GLY n 
1 121 HIS n 
1 122 VAL n 
1 123 VAL n 
1 124 ASP n 
1 125 PHE n 
1 126 ILE n 
1 127 LEU n 
1 128 VAL n 
1 129 HIS n 
1 130 TRP n 
1 131 GLN n 
1 132 ASN n 
1 133 ARG n 
1 134 TRP n 
1 135 TYR n 
1 136 PHE n 
1 137 PRO n 
1 138 ALA n 
1 139 PHE n 
1 140 ASN n 
1 141 LEU n 
1 142 ALA n 
1 143 ASP n 
1 144 SER n 
1 145 ALA n 
1 146 ILE n 
1 147 THR n 
1 148 VAL n 
1 149 GLY n 
1 150 ALA n 
1 151 VAL n 
1 152 MET n 
1 153 LEU n 
1 154 ALA n 
1 155 LEU n 
1 156 ASP n 
1 157 MET n 
1 158 PHE n 
1 159 ARG n 
1 160 SER n 
1 161 LYS n 
1 162 LYS n 
1 163 SER n 
1 164 GLY n 
1 165 GLU n 
1 166 ALA n 
1 167 ALA n 
1 168 HIS n 
1 169 GLY n 
2 1   MLE n 
2 2   IIL n 
2 3   SER n 
2 4   ALO n 
2 5   5BV 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                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'lspA, ls, PA4559' 
_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 PAO1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     208964 
_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                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       5 
_pdbx_entity_src_syn.organism_scientific    'synthetic construct' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
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 
5BV non-polymer         . '(2R,3R)-3-(glycyloxy)-2-methylnonanoic acid'    ?                   'C12 H23 N O4'   245.315 
ALA 'L-peptide linking' y ALANINE                                          ?                   'C3 H7 N O2'     89.093  
ALO 'L-peptide linking' n ALLO-THREONINE                                   ?                   'C4 H9 N O3'     119.119 
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 
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  
IIL 'L-peptide linking' n ISO-ISOLEUCINE                                   ALLO-ISOLEUCINE     'C6 H13 N O2'    131.173 
ILE 'L-peptide linking' y ISOLEUCINE                                       ?                   'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                          ?                   'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                           ?                   'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                       ?                   'C5 H11 N O2 S'  149.211 
MLE 'L-peptide linking' n N-METHYLLEUCINE                                  ?                   'C7 H15 N O2'    145.199 
OLC non-polymer         . '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 1-Oleoyl-R-glycerol 'C21 H40 O4'     356.540 
PHE 'L-peptide linking' y PHENYLALANINE                                    ?                   'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                          ?                   'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                           ?                   'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                        ?                   'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                       ?                   'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                         ?                   'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                           ?                   'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   2   PRO PRO A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   VAL 4   4   4   VAL VAL A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   ARG 6   6   6   ARG ARG A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  TRP 12  12  12  TRP TRP A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  TRP 14  14  14  TRP TRP A . n 
A 1 15  ILE 15  15  15  ILE ILE A . n 
A 1 16  THR 16  16  16  THR THR A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  GLN 24  24  24  GLN GLN A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  PHE 29  29  29  PHE PHE A . n 
A 1 30  PHE 30  30  30  PHE PHE A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  GLU 33  33  33  GLU GLU A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  MET 36  36  36  MET MET A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  GLN 39  39  39  GLN GLN A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  PHE 47  47  47  PHE PHE A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  TRP 49  49  49  TRP TRP A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  ASP 64  64  64  ASP ASP A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  TRP 68  68  68  TRP TRP A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  TRP 71  71  71  TRP TRP A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PHE 73  73  73  PHE PHE A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  TRP 87  87  87  TRP TRP A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 HIS 121 121 121 HIS HIS A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 PHE 125 125 125 PHE PHE A . n 
A 1 126 ILE 126 126 126 ILE ILE A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 HIS 129 129 129 HIS HIS A . n 
A 1 130 TRP 130 130 130 TRP TRP A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 ASN 132 132 132 ASN ASN A . n 
A 1 133 ARG 133 133 133 ARG ARG A . n 
A 1 134 TRP 134 134 134 TRP TRP A . n 
A 1 135 TYR 135 135 135 TYR TYR A . n 
A 1 136 PHE 136 136 136 PHE PHE A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 ALA 138 138 138 ALA ALA A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 MET 152 152 152 MET MET A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 ARG 159 159 ?   ?   ?   A . n 
A 1 160 SER 160 160 ?   ?   ?   A . n 
A 1 161 LYS 161 161 ?   ?   ?   A . n 
A 1 162 LYS 162 162 ?   ?   ?   A . n 
A 1 163 SER 163 163 ?   ?   ?   A . n 
A 1 164 GLY 164 164 ?   ?   ?   A . n 
A 1 165 GLU 165 165 ?   ?   ?   A . n 
A 1 166 ALA 166 166 ?   ?   ?   A . n 
A 1 167 ALA 167 167 ?   ?   ?   A . n 
A 1 168 HIS 168 168 ?   ?   ?   A . n 
A 1 169 GLY 169 169 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   2   PRO PRO B . n 
B 1 3   ASP 3   3   3   ASP ASP B . n 
B 1 4   VAL 4   4   4   VAL VAL B . n 
B 1 5   ASP 5   5   5   ASP ASP B . n 
B 1 6   ARG 6   6   6   ARG ARG B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   ARG 9   9   9   ARG ARG B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  PRO 11  11  11  PRO PRO B . n 
B 1 12  TRP 12  12  12  TRP TRP B . n 
B 1 13  LEU 13  13  13  LEU LEU B . n 
B 1 14  TRP 14  14  14  TRP TRP B . n 
B 1 15  ILE 15  15  15  ILE ILE B . n 
B 1 16  THR 16  16  16  THR THR B . n 
B 1 17  VAL 17  17  17  VAL VAL B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  VAL 21  21  21  VAL VAL B . n 
B 1 22  LEU 22  22  22  LEU LEU B . n 
B 1 23  ASP 23  23  23  ASP ASP B . n 
B 1 24  GLN 24  24  24  GLN GLN B . n 
B 1 25  VAL 25  25  25  VAL VAL B . n 
B 1 26  SER 26  26  26  SER SER B . n 
B 1 27  LYS 27  27  27  LYS LYS B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  PHE 29  29  29  PHE PHE B . n 
B 1 30  PHE 30  30  30  PHE PHE B . n 
B 1 31  GLN 31  31  31  GLN GLN B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  GLU 33  33  33  GLU GLU B . n 
B 1 34  LEU 34  34  34  LEU LEU B . n 
B 1 35  SER 35  35  35  SER SER B . n 
B 1 36  MET 36  36  36  MET MET B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  GLN 39  39  39  GLN GLN B . n 
B 1 40  ILE 40  40  40  ILE ILE B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  PRO 44  44  44  PRO PRO B . n 
B 1 45  ASP 45  45  45  ASP ASP B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  PHE 47  47  47  PHE PHE B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  TRP 49  49  49  TRP TRP B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  TYR 53  53  53  TYR TYR B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  ALA 58  58  58  ALA ALA B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  SER 60  60  60  SER SER B . n 
B 1 61  PHE 61  61  ?   ?   ?   B . n 
B 1 62  LEU 62  62  ?   ?   ?   B . n 
B 1 63  ALA 63  63  ?   ?   ?   B . n 
B 1 64  ASP 64  64  ?   ?   ?   B . n 
B 1 65  SER 65  65  ?   ?   ?   B . n 
B 1 66  SER 66  66  ?   ?   ?   B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  TRP 68  68  68  TRP TRP B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ARG 70  70  70  ARG ARG B . n 
B 1 71  TRP 71  71  71  TRP TRP B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  PHE 73  73  73  PHE PHE B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ILE 76  76  76  ILE ILE B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  TRP 87  87  87  TRP TRP B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  LEU 91  91  91  LEU LEU B . n 
B 1 92  LYS 92  92  92  LYS LYS B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  GLY 94  94  94  GLY GLY B . n 
B 1 95  GLU 95  95  95  GLU GLU B . n 
B 1 96  THR 96  96  96  THR THR B . n 
B 1 97  TRP 97  97  97  TRP TRP B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  ALA 99  99  99  ALA ALA B . n 
B 1 100 ILE 100 100 100 ILE ILE B . n 
B 1 101 ALA 101 101 101 ALA ALA B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 ALA 103 103 103 ALA ALA B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 VAL 105 105 105 VAL VAL B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 GLY 107 107 107 GLY GLY B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 GLY 111 111 111 GLY GLY B . n 
B 1 112 ASN 112 112 112 ASN ASN B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 ASP 115 115 115 ASP ASP B . n 
B 1 116 ARG 116 116 116 ARG ARG B . n 
B 1 117 MET 117 117 117 MET MET B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 HIS 121 121 121 HIS HIS B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 VAL 123 123 123 VAL VAL B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 PHE 125 125 125 PHE PHE B . n 
B 1 126 ILE 126 126 126 ILE ILE B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 HIS 129 129 129 HIS HIS B . n 
B 1 130 TRP 130 130 130 TRP TRP B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 ASN 132 132 132 ASN ASN B . n 
B 1 133 ARG 133 133 133 ARG ARG B . n 
B 1 134 TRP 134 134 134 TRP TRP B . n 
B 1 135 TYR 135 135 135 TYR TYR B . n 
B 1 136 PHE 136 136 136 PHE PHE B . n 
B 1 137 PRO 137 137 137 PRO PRO B . n 
B 1 138 ALA 138 138 138 ALA ALA B . n 
B 1 139 PHE 139 139 139 PHE PHE B . n 
B 1 140 ASN 140 140 140 ASN ASN B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ALA 142 142 142 ALA ALA B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 THR 147 147 147 THR THR B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 MET 152 152 152 MET MET B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 LEU 155 155 155 LEU LEU B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 MET 157 157 ?   ?   ?   B . n 
B 1 158 PHE 158 158 ?   ?   ?   B . n 
B 1 159 ARG 159 159 ?   ?   ?   B . n 
B 1 160 SER 160 160 ?   ?   ?   B . n 
B 1 161 LYS 161 161 ?   ?   ?   B . n 
B 1 162 LYS 162 162 ?   ?   ?   B . n 
B 1 163 SER 163 163 ?   ?   ?   B . n 
B 1 164 GLY 164 164 ?   ?   ?   B . n 
B 1 165 GLU 165 165 ?   ?   ?   B . n 
B 1 166 ALA 166 166 ?   ?   ?   B . n 
B 1 167 ALA 167 167 ?   ?   ?   B . n 
B 1 168 HIS 168 168 ?   ?   ?   B . n 
B 1 169 GLY 169 169 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   PRO 2   2   ?   ?   ?   C . n 
C 1 3   ASP 3   3   ?   ?   ?   C . n 
C 1 4   VAL 4   4   ?   ?   ?   C . n 
C 1 5   ASP 5   5   ?   ?   ?   C . n 
C 1 6   ARG 6   6   ?   ?   ?   C . n 
C 1 7   PHE 7   7   ?   ?   ?   C . n 
C 1 8   GLY 8   8   ?   ?   ?   C . n 
C 1 9   ARG 9   9   ?   ?   ?   C . n 
C 1 10  LEU 10  10  ?   ?   ?   C . n 
C 1 11  PRO 11  11  11  PRO PRO C . n 
C 1 12  TRP 12  12  12  TRP TRP C . n 
C 1 13  LEU 13  13  13  LEU LEU C . n 
C 1 14  TRP 14  14  14  TRP TRP C . n 
C 1 15  ILE 15  15  15  ILE ILE C . n 
C 1 16  THR 16  16  16  THR THR C . n 
C 1 17  VAL 17  17  17  VAL VAL C . n 
C 1 18  LEU 18  18  18  LEU LEU C . n 
C 1 19  VAL 19  19  19  VAL VAL C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  VAL 21  21  21  VAL VAL C . n 
C 1 22  LEU 22  22  22  LEU LEU C . n 
C 1 23  ASP 23  23  23  ASP ASP C . n 
C 1 24  GLN 24  24  24  GLN GLN C . n 
C 1 25  VAL 25  25  25  VAL VAL C . n 
C 1 26  SER 26  26  26  SER SER C . n 
C 1 27  LYS 27  27  27  LYS LYS C . n 
C 1 28  ALA 28  28  28  ALA ALA C . n 
C 1 29  PHE 29  29  29  PHE PHE C . n 
C 1 30  PHE 30  30  30  PHE PHE C . n 
C 1 31  GLN 31  31  31  GLN GLN C . n 
C 1 32  ALA 32  32  32  ALA ALA C . n 
C 1 33  GLU 33  33  33  GLU GLU C . n 
C 1 34  LEU 34  34  34  LEU LEU C . n 
C 1 35  SER 35  35  35  SER SER C . n 
C 1 36  MET 36  36  36  MET MET C . n 
C 1 37  TYR 37  37  37  TYR TYR C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  GLN 39  39  39  GLN GLN C . n 
C 1 40  ILE 40  40  40  ILE ILE C . n 
C 1 41  VAL 41  41  41  VAL VAL C . n 
C 1 42  VAL 42  42  42  VAL VAL C . n 
C 1 43  ILE 43  43  43  ILE ILE C . n 
C 1 44  PRO 44  44  44  PRO PRO C . n 
C 1 45  ASP 45  45  45  ASP ASP C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  PHE 47  47  47  PHE PHE C . n 
C 1 48  SER 48  48  48  SER SER C . n 
C 1 49  TRP 49  49  49  TRP TRP C . n 
C 1 50  THR 50  50  50  THR THR C . n 
C 1 51  LEU 51  51  51  LEU LEU C . n 
C 1 52  ALA 52  52  52  ALA ALA C . n 
C 1 53  TYR 53  53  53  TYR TYR C . n 
C 1 54  ASN 54  54  54  ASN ASN C . n 
C 1 55  THR 55  55  55  THR THR C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  ALA 57  57  57  ALA ALA C . n 
C 1 58  ALA 58  58  58  ALA ALA C . n 
C 1 59  PHE 59  59  59  PHE PHE C . n 
C 1 60  SER 60  60  60  SER SER C . n 
C 1 61  PHE 61  61  61  PHE PHE C . n 
C 1 62  LEU 62  62  62  LEU LEU C . n 
C 1 63  ALA 63  63  63  ALA ALA C . n 
C 1 64  ASP 64  64  64  ASP ASP C . n 
C 1 65  SER 65  65  65  SER SER C . n 
C 1 66  SER 66  66  66  SER SER C . n 
C 1 67  GLY 67  67  67  GLY GLY C . n 
C 1 68  TRP 68  68  68  TRP TRP C . n 
C 1 69  GLN 69  69  69  GLN GLN C . n 
C 1 70  ARG 70  70  70  ARG ARG C . n 
C 1 71  TRP 71  71  71  TRP TRP C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  PHE 73  73  73  PHE PHE C . n 
C 1 74  ALA 74  74  74  ALA ALA C . n 
C 1 75  LEU 75  75  75  LEU LEU C . n 
C 1 76  ILE 76  76  76  ILE ILE C . n 
C 1 77  ALA 77  77  77  ALA ALA C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  VAL 79  79  79  VAL VAL C . n 
C 1 80  VAL 80  80  80  VAL VAL C . n 
C 1 81  SER 81  81  81  SER SER C . n 
C 1 82  ALA 82  82  82  ALA ALA C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  VAL 85  85  85  VAL VAL C . n 
C 1 86  VAL 86  86  86  VAL VAL C . n 
C 1 87  TRP 87  87  87  TRP TRP C . n 
C 1 88  LEU 88  88  88  LEU LEU C . n 
C 1 89  LYS 89  89  89  LYS LYS C . n 
C 1 90  ARG 90  90  90  ARG ARG C . n 
C 1 91  LEU 91  91  91  LEU LEU C . n 
C 1 92  LYS 92  92  92  LYS LYS C . n 
C 1 93  LYS 93  93  93  LYS LYS C . n 
C 1 94  GLY 94  94  94  GLY GLY C . n 
C 1 95  GLU 95  95  95  GLU GLU C . n 
C 1 96  THR 96  96  96  THR THR C . n 
C 1 97  TRP 97  97  97  TRP TRP C . n 
C 1 98  LEU 98  98  98  LEU LEU C . n 
C 1 99  ALA 99  99  99  ALA ALA C . n 
C 1 100 ILE 100 100 100 ILE ILE C . n 
C 1 101 ALA 101 101 101 ALA ALA C . n 
C 1 102 LEU 102 102 102 LEU LEU C . n 
C 1 103 ALA 103 103 103 ALA ALA C . n 
C 1 104 LEU 104 104 104 LEU LEU C . n 
C 1 105 VAL 105 105 105 VAL VAL C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 GLY 107 107 107 GLY GLY C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 ALA 109 109 109 ALA ALA C . n 
C 1 110 LEU 110 110 110 LEU LEU C . n 
C 1 111 GLY 111 111 111 GLY GLY C . n 
C 1 112 ASN 112 112 112 ASN ASN C . n 
C 1 113 LEU 113 113 113 LEU LEU C . n 
C 1 114 TYR 114 114 114 TYR TYR C . n 
C 1 115 ASP 115 115 115 ASP ASP C . n 
C 1 116 ARG 116 116 116 ARG ARG C . n 
C 1 117 MET 117 117 117 MET MET C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 LEU 119 119 119 LEU LEU C . n 
C 1 120 GLY 120 120 120 GLY GLY C . n 
C 1 121 HIS 121 121 121 HIS HIS C . n 
C 1 122 VAL 122 122 122 VAL VAL C . n 
C 1 123 VAL 123 123 123 VAL VAL C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 PHE 125 125 125 PHE PHE C . n 
C 1 126 ILE 126 126 126 ILE ILE C . n 
C 1 127 LEU 127 127 127 LEU LEU C . n 
C 1 128 VAL 128 128 128 VAL VAL C . n 
C 1 129 HIS 129 129 129 HIS HIS C . n 
C 1 130 TRP 130 130 130 TRP TRP C . n 
C 1 131 GLN 131 131 131 GLN GLN C . n 
C 1 132 ASN 132 132 132 ASN ASN C . n 
C 1 133 ARG 133 133 133 ARG ARG C . n 
C 1 134 TRP 134 134 134 TRP TRP C . n 
C 1 135 TYR 135 135 135 TYR TYR C . n 
C 1 136 PHE 136 136 136 PHE PHE C . n 
C 1 137 PRO 137 137 137 PRO PRO C . n 
C 1 138 ALA 138 138 138 ALA ALA C . n 
C 1 139 PHE 139 139 139 PHE PHE C . n 
C 1 140 ASN 140 140 140 ASN ASN C . n 
C 1 141 LEU 141 141 141 LEU LEU C . n 
C 1 142 ALA 142 142 142 ALA ALA C . n 
C 1 143 ASP 143 143 143 ASP ASP C . n 
C 1 144 SER 144 144 144 SER SER C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 THR 147 147 147 THR THR C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 ALA 150 150 150 ALA ALA C . n 
C 1 151 VAL 151 151 151 VAL VAL C . n 
C 1 152 MET 152 152 152 MET MET C . n 
C 1 153 LEU 153 153 153 LEU LEU C . n 
C 1 154 ALA 154 154 154 ALA ALA C . n 
C 1 155 LEU 155 155 155 LEU LEU C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 MET 157 157 157 MET MET C . n 
C 1 158 PHE 158 158 158 PHE PHE C . n 
C 1 159 ARG 159 159 159 ARG ARG C . n 
C 1 160 SER 160 160 ?   ?   ?   C . n 
C 1 161 LYS 161 161 ?   ?   ?   C . n 
C 1 162 LYS 162 162 ?   ?   ?   C . n 
C 1 163 SER 163 163 ?   ?   ?   C . n 
C 1 164 GLY 164 164 ?   ?   ?   C . n 
C 1 165 GLU 165 165 ?   ?   ?   C . n 
C 1 166 ALA 166 166 ?   ?   ?   C . n 
C 1 167 ALA 167 167 ?   ?   ?   C . n 
C 1 168 HIS 168 168 ?   ?   ?   C . n 
C 1 169 GLY 169 169 ?   ?   ?   C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   PRO 2   2   ?   ?   ?   D . n 
D 1 3   ASP 3   3   ?   ?   ?   D . n 
D 1 4   VAL 4   4   ?   ?   ?   D . n 
D 1 5   ASP 5   5   ?   ?   ?   D . n 
D 1 6   ARG 6   6   ?   ?   ?   D . n 
D 1 7   PHE 7   7   ?   ?   ?   D . n 
D 1 8   GLY 8   8   ?   ?   ?   D . n 
D 1 9   ARG 9   9   ?   ?   ?   D . n 
D 1 10  LEU 10  10  ?   ?   ?   D . n 
D 1 11  PRO 11  11  11  PRO PRO D . n 
D 1 12  TRP 12  12  12  TRP TRP D . n 
D 1 13  LEU 13  13  13  LEU LEU D . n 
D 1 14  TRP 14  14  14  TRP TRP D . n 
D 1 15  ILE 15  15  15  ILE ILE D . n 
D 1 16  THR 16  16  16  THR THR D . n 
D 1 17  VAL 17  17  17  VAL VAL D . n 
D 1 18  LEU 18  18  18  LEU LEU D . n 
D 1 19  VAL 19  19  19  VAL VAL D . n 
D 1 20  PHE 20  20  20  PHE PHE D . n 
D 1 21  VAL 21  21  21  VAL VAL D . n 
D 1 22  LEU 22  22  22  LEU LEU D . n 
D 1 23  ASP 23  23  23  ASP ASP D . n 
D 1 24  GLN 24  24  24  GLN GLN D . n 
D 1 25  VAL 25  25  25  VAL VAL D . n 
D 1 26  SER 26  26  26  SER SER D . n 
D 1 27  LYS 27  27  27  LYS LYS D . n 
D 1 28  ALA 28  28  28  ALA ALA D . n 
D 1 29  PHE 29  29  29  PHE PHE D . n 
D 1 30  PHE 30  30  30  PHE PHE D . n 
D 1 31  GLN 31  31  31  GLN GLN D . n 
D 1 32  ALA 32  32  32  ALA ALA D . n 
D 1 33  GLU 33  33  33  GLU GLU D . n 
D 1 34  LEU 34  34  34  LEU LEU D . n 
D 1 35  SER 35  35  35  SER SER D . n 
D 1 36  MET 36  36  36  MET MET D . n 
D 1 37  TYR 37  37  37  TYR TYR D . n 
D 1 38  GLN 38  38  38  GLN GLN D . n 
D 1 39  GLN 39  39  39  GLN GLN D . n 
D 1 40  ILE 40  40  40  ILE ILE D . n 
D 1 41  VAL 41  41  41  VAL VAL D . n 
D 1 42  VAL 42  42  42  VAL VAL D . n 
D 1 43  ILE 43  43  43  ILE ILE D . n 
D 1 44  PRO 44  44  44  PRO PRO D . n 
D 1 45  ASP 45  45  45  ASP ASP D . n 
D 1 46  LEU 46  46  46  LEU LEU D . n 
D 1 47  PHE 47  47  47  PHE PHE D . n 
D 1 48  SER 48  48  48  SER SER D . n 
D 1 49  TRP 49  49  49  TRP TRP D . n 
D 1 50  THR 50  50  50  THR THR D . n 
D 1 51  LEU 51  51  51  LEU LEU D . n 
D 1 52  ALA 52  52  52  ALA ALA D . n 
D 1 53  TYR 53  53  53  TYR TYR D . n 
D 1 54  ASN 54  54  54  ASN ASN D . n 
D 1 55  THR 55  55  55  THR THR D . n 
D 1 56  GLY 56  56  56  GLY GLY D . n 
D 1 57  ALA 57  57  57  ALA ALA D . n 
D 1 58  ALA 58  58  58  ALA ALA D . n 
D 1 59  PHE 59  59  59  PHE PHE D . n 
D 1 60  SER 60  60  60  SER SER D . n 
D 1 61  PHE 61  61  61  PHE PHE D . n 
D 1 62  LEU 62  62  62  LEU LEU D . n 
D 1 63  ALA 63  63  63  ALA ALA D . n 
D 1 64  ASP 64  64  64  ASP ASP D . n 
D 1 65  SER 65  65  65  SER SER D . n 
D 1 66  SER 66  66  66  SER SER D . n 
D 1 67  GLY 67  67  67  GLY GLY D . n 
D 1 68  TRP 68  68  68  TRP TRP D . n 
D 1 69  GLN 69  69  69  GLN GLN D . n 
D 1 70  ARG 70  70  70  ARG ARG D . n 
D 1 71  TRP 71  71  71  TRP TRP D . n 
D 1 72  LEU 72  72  72  LEU LEU D . n 
D 1 73  PHE 73  73  73  PHE PHE D . n 
D 1 74  ALA 74  74  74  ALA ALA D . n 
D 1 75  LEU 75  75  75  LEU LEU D . n 
D 1 76  ILE 76  76  76  ILE ILE D . n 
D 1 77  ALA 77  77  77  ALA ALA D . n 
D 1 78  ILE 78  78  78  ILE ILE D . n 
D 1 79  VAL 79  79  79  VAL VAL D . n 
D 1 80  VAL 80  80  80  VAL VAL D . n 
D 1 81  SER 81  81  81  SER SER D . n 
D 1 82  ALA 82  82  82  ALA ALA D . n 
D 1 83  SER 83  83  83  SER SER D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  VAL 85  85  85  VAL VAL D . n 
D 1 86  VAL 86  86  86  VAL VAL D . n 
D 1 87  TRP 87  87  87  TRP TRP D . n 
D 1 88  LEU 88  88  88  LEU LEU D . n 
D 1 89  LYS 89  89  89  LYS LYS D . n 
D 1 90  ARG 90  90  90  ARG ARG D . n 
D 1 91  LEU 91  91  91  LEU LEU D . n 
D 1 92  LYS 92  92  92  LYS LYS D . n 
D 1 93  LYS 93  93  93  LYS LYS D . n 
D 1 94  GLY 94  94  94  GLY GLY D . n 
D 1 95  GLU 95  95  95  GLU GLU D . n 
D 1 96  THR 96  96  96  THR THR D . n 
D 1 97  TRP 97  97  97  TRP TRP D . n 
D 1 98  LEU 98  98  98  LEU LEU D . n 
D 1 99  ALA 99  99  99  ALA ALA D . n 
D 1 100 ILE 100 100 100 ILE ILE D . n 
D 1 101 ALA 101 101 101 ALA ALA D . n 
D 1 102 LEU 102 102 102 LEU LEU D . n 
D 1 103 ALA 103 103 103 ALA ALA D . n 
D 1 104 LEU 104 104 104 LEU LEU D . n 
D 1 105 VAL 105 105 105 VAL VAL D . n 
D 1 106 LEU 106 106 106 LEU LEU D . n 
D 1 107 GLY 107 107 107 GLY GLY D . n 
D 1 108 GLY 108 108 108 GLY GLY D . n 
D 1 109 ALA 109 109 109 ALA ALA D . n 
D 1 110 LEU 110 110 110 LEU LEU D . n 
D 1 111 GLY 111 111 111 GLY GLY D . n 
D 1 112 ASN 112 112 112 ASN ASN D . n 
D 1 113 LEU 113 113 113 LEU LEU D . n 
D 1 114 TYR 114 114 114 TYR TYR D . n 
D 1 115 ASP 115 115 115 ASP ASP D . n 
D 1 116 ARG 116 116 116 ARG ARG D . n 
D 1 117 MET 117 117 117 MET MET D . n 
D 1 118 VAL 118 118 118 VAL VAL D . n 
D 1 119 LEU 119 119 119 LEU LEU D . n 
D 1 120 GLY 120 120 120 GLY GLY D . n 
D 1 121 HIS 121 121 121 HIS HIS D . n 
D 1 122 VAL 122 122 122 VAL VAL D . n 
D 1 123 VAL 123 123 123 VAL VAL D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 PHE 125 125 125 PHE PHE D . n 
D 1 126 ILE 126 126 126 ILE ILE D . n 
D 1 127 LEU 127 127 127 LEU LEU D . n 
D 1 128 VAL 128 128 128 VAL VAL D . n 
D 1 129 HIS 129 129 129 HIS HIS D . n 
D 1 130 TRP 130 130 130 TRP TRP D . n 
D 1 131 GLN 131 131 131 GLN GLN D . n 
D 1 132 ASN 132 132 132 ASN ASN D . n 
D 1 133 ARG 133 133 133 ARG ARG D . n 
D 1 134 TRP 134 134 134 TRP TRP D . n 
D 1 135 TYR 135 135 135 TYR TYR D . n 
D 1 136 PHE 136 136 136 PHE PHE D . n 
D 1 137 PRO 137 137 137 PRO PRO D . n 
D 1 138 ALA 138 138 138 ALA ALA D . n 
D 1 139 PHE 139 139 139 PHE PHE D . n 
D 1 140 ASN 140 140 140 ASN ASN D . n 
D 1 141 LEU 141 141 141 LEU LEU D . n 
D 1 142 ALA 142 142 142 ALA ALA D . n 
D 1 143 ASP 143 143 143 ASP ASP D . n 
D 1 144 SER 144 144 144 SER SER D . n 
D 1 145 ALA 145 145 145 ALA ALA D . n 
D 1 146 ILE 146 146 146 ILE ILE D . n 
D 1 147 THR 147 147 147 THR THR D . n 
D 1 148 VAL 148 148 148 VAL VAL D . n 
D 1 149 GLY 149 149 149 GLY GLY D . n 
D 1 150 ALA 150 150 150 ALA ALA D . n 
D 1 151 VAL 151 151 151 VAL VAL D . n 
D 1 152 MET 152 152 152 MET MET D . n 
D 1 153 LEU 153 153 153 LEU LEU D . n 
D 1 154 ALA 154 154 154 ALA ALA D . n 
D 1 155 LEU 155 155 155 LEU LEU D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 MET 157 157 157 MET MET D . n 
D 1 158 PHE 158 158 158 PHE PHE D . n 
D 1 159 ARG 159 159 159 ARG ARG D . n 
D 1 160 SER 160 160 ?   ?   ?   D . n 
D 1 161 LYS 161 161 ?   ?   ?   D . n 
D 1 162 LYS 162 162 ?   ?   ?   D . n 
D 1 163 SER 163 163 ?   ?   ?   D . n 
D 1 164 GLY 164 164 ?   ?   ?   D . n 
D 1 165 GLU 165 165 ?   ?   ?   D . n 
D 1 166 ALA 166 166 ?   ?   ?   D . n 
D 1 167 ALA 167 167 ?   ?   ?   D . n 
D 1 168 HIS 168 168 ?   ?   ?   D . n 
D 1 169 GLY 169 169 ?   ?   ?   D . n 
E 2 1   MLE 1   201 201 MLE MLE E . n 
E 2 2   IIL 2   202 202 IIL IIL E . n 
E 2 3   SER 3   203 203 SER SER E . n 
E 2 4   ALO 4   204 204 ALO ALO E . n 
E 2 5   5BV 5   205 205 5BV 5BV E . n 
F 2 1   MLE 1   201 201 MLE MLE F . n 
F 2 2   IIL 2   202 202 IIL IIL F . n 
F 2 3   SER 3   203 203 SER SER F . n 
F 2 4   ALO 4   204 204 ALO ALO F . n 
F 2 5   5BV 5   205 205 5BV 5BV F . n 
G 2 1   MLE 1   201 201 MLE MLE G . n 
G 2 2   IIL 2   202 202 IIL IIL G . n 
G 2 3   SER 3   203 203 SER SER G . n 
G 2 4   ALO 4   204 204 ALO ALO G . n 
G 2 5   5BV 5   205 205 5BV 5BV G . n 
H 2 1   MLE 1   201 201 MLE MLE H . n 
H 2 2   IIL 2   202 202 IIL IIL H . n 
H 2 3   SER 3   203 203 SER SER H . n 
H 2 4   ALO 4   204 204 ALO ALO H . n 
H 2 5   5BV 5   205 205 5BV 5BV H . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 5BV ? ? 5BV ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ALO ? ? ALO ? ? 'SUBJECT OF INVESTIGATION' ? 
3 IIL ? ? IIL ? ? 'SUBJECT OF INVESTIGATION' ? 
4 MLE ? ? MLE ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
I  3 OLC 1 201 201 OLC OLC A . 
J  3 OLC 1 202 202 OLC OLC A . 
K  3 OLC 1 203 203 OLC OLC A . 
L  3 OLC 1 204 204 OLC OLC A . 
M  3 OLC 1 205 205 OLC OLC A . 
N  3 OLC 1 206 206 OLC OLC A . 
O  3 OLC 1 201 208 OLC OLC B . 
P  3 OLC 1 202 209 OLC OLC B . 
Q  3 OLC 1 203 210 OLC OLC B . 
R  3 OLC 1 204 211 OLC OLC B . 
S  3 OLC 1 205 212 OLC OLC B . 
T  3 OLC 1 206 213 OLC OLC B . 
U  3 OLC 1 207 207 OLC OLC B . 
V  3 OLC 1 201 214 OLC OLC C . 
W  3 OLC 1 202 215 OLC OLC C . 
X  3 OLC 1 203 216 OLC OLC C . 
Y  3 OLC 1 204 217 OLC OLC C . 
Z  3 OLC 1 205 301 OLC OLC C . 
AA 3 OLC 1 206 302 OLC OLC C . 
BA 3 OLC 1 201 218 OLC OLC D . 
CA 3 OLC 1 202 219 OLC OLC D . 
DA 3 OLC 1 203 220 OLC OLC D . 
EA 3 OLC 1 204 221 OLC OLC D . 
FA 3 OLC 1 205 222 OLC OLC D . 
GA 4 HOH 1 301 301 HOH HOH A . 
GA 4 HOH 2 302 302 HOH HOH A . 
HA 4 HOH 1 301 301 HOH HOH C . 
HA 4 HOH 2 302 305 HOH HOH C . 
HA 4 HOH 3 303 303 HOH HOH C . 
HA 4 HOH 4 304 307 HOH HOH C . 
HA 4 HOH 5 305 304 HOH HOH C . 
HA 4 HOH 6 306 306 HOH HOH C . 
IA 4 HOH 1 301 303 HOH HOH D . 
IA 4 HOH 2 302 302 HOH HOH D . 
IA 4 HOH 3 303 304 HOH HOH D . 
IA 4 HOH 4 304 301 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.19.2_4158: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.54 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EMZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.991 
_cell.length_a_esd                 ? 
_cell.length_b                     106.086 
_cell.length_b_esd                 ? 
_cell.length_c                     85.919 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         9EMZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EMZ 
_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             3.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          66.85 
_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          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM MES pH 5.6-6.0, 35-43 %(v/v) PEG400 and 60-100 mM ammonium phosphate monobasic' 
_exptl_crystal_grow.pdbx_pH_range   5.6-6.0 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-07-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00003 
_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                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00003 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EMZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.995 
_reflns.d_resolution_low                               85.176 
_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                                     10425 
_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                           72.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.121 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_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 
9.94  85.176 ? 2.3 ? ? ? ? 520 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1 1 1    ? ? ?    ? 0.028 ? ? ? ? ? ? ? ? ? 
2.995 3.307  ? 1.5 ? ? ? ? 522 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 0.57 ? ? 67.3 ? 0.769 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EMZ 
_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                            3.00 
_refine.ls_d_res_low                             60.00 
_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                     10410 
_refine.ls_number_reflns_R_free                  525 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    50.77 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2484 
_refine.ls_R_factor_R_free                       0.3033 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2453 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.39 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.69 
_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                            0.37 
_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                       3.00 
_refine_hist.d_res_low                        60.00 
_refine_hist.number_atoms_solvent             12 
_refine_hist.number_atoms_total               5649 
_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        4945 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         692 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  ? 5750 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.605  ? 7646 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.648 ? 2068 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 841  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 874  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.00 3.30  . . 29  470  10.00 . . . . 0.3345 . . . . . . . . . . . 0.3565 
'X-RAY DIFFRACTION' 3.30 3.77  . . 73  1551 32.00 . . . . 0.2853 . . . . . . . . . . . 0.3293 
'X-RAY DIFFRACTION' 3.77 4.75  . . 176 3426 70.00 . . . . 0.2513 . . . . . . . . . . . 0.3322 
'X-RAY DIFFRACTION' 4.75 60.00 . . 247 4438 90.00 . . . . 0.2283 . . . . . . . . . . . 0.2753 
# 
_struct.entry_id                     9EMZ 
_struct.title                        '13C/15N-labelled Integral Membrane Enzyme LspA in the Lipid Cubic Phase' 
_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        9EMZ 
_struct_keywords.text            'Lipid Cubic Phase, LspA, Hydrolase, Globomycin' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 2 ? 
G  N N 2 ? 
H  N N 2 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 3 ? 
S  N N 3 ? 
T  N N 3 ? 
U  N N 3 ? 
V  N N 3 ? 
W  N N 3 ? 
X  N N 3 ? 
Y  N N 3 ? 
Z  N N 3 ? 
AA N N 3 ? 
BA N N 3 ? 
CA N N 3 ? 
DA N N 3 ? 
EA N N 3 ? 
FA N N 3 ? 
GA N N 4 ? 
HA N N 4 ? 
IA N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP LSPA_PSEAE Q9HVM5 ? 1 
;MPDVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSMYQQIVVIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVV
SASLVVWLKRLKKGETWLAIALALVLGGALGNLYDRMVLGHVVDFILVHWQNRWYFPAFNLADSAITVGAVMLALDMFRS
KKSGEAAHG
;
1 
2 PDB 9EMZ       9EMZ   ? 2 ? 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 9EMZ A 1 ? 169 ? Q9HVM5 1   ? 169 ? 1   169 
2 1 9EMZ B 1 ? 169 ? Q9HVM5 1   ? 169 ? 1   169 
3 1 9EMZ C 1 ? 169 ? Q9HVM5 1   ? 169 ? 1   169 
4 1 9EMZ D 1 ? 169 ? Q9HVM5 1   ? 169 ? 1   169 
5 2 9EMZ E 1 ? 5   ? 9EMZ   201 ? 205 ? 201 205 
6 2 9EMZ F 1 ? 5   ? 9EMZ   201 ? 205 ? 201 205 
7 2 9EMZ G 1 ? 5   ? 9EMZ   201 ? 205 ? 201 205 
8 2 9EMZ H 1 ? 5   ? 9EMZ   201 ? 205 ? 201 205 
# 
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 ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
3 author_defined_assembly ? dimeric 2 
4 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,I,J,K,L,M,N,GA    
2 1 B,H,O,P,Q,R,S,T,U     
3 1 C,F,V,W,X,Y,Z,AA,HA   
4 1 D,G,BA,CA,DA,EA,FA,IA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 2   ? PHE A 7   ? PRO A 2   PHE A 7   1 ? 6  
HELX_P HELX_P2  AA2 ARG A 9   ? PRO A 11  ? ARG A 9   PRO A 11  5 ? 3  
HELX_P HELX_P3  AA3 TRP A 12  ? LEU A 34  ? TRP A 12  LEU A 34  1 ? 23 
HELX_P HELX_P4  AA4 GLY A 56  ? ALA A 63  ? GLY A 56  ALA A 63  5 ? 8  
HELX_P HELX_P5  AA5 TRP A 68  ? LEU A 91  ? TRP A 68  LEU A 91  1 ? 24 
HELX_P HELX_P6  AA6 GLU A 95  ? LEU A 119 ? GLU A 95  LEU A 119 1 ? 25 
HELX_P HELX_P7  AA7 ASN A 140 ? LEU A 155 ? ASN A 140 LEU A 155 1 ? 16 
HELX_P HELX_P8  AA8 ARG B 9   ? PRO B 11  ? ARG B 9   PRO B 11  5 ? 3  
HELX_P HELX_P9  AA9 TRP B 12  ? LEU B 34  ? TRP B 12  LEU B 34  1 ? 23 
HELX_P HELX_P10 AB1 THR B 55  ? ALA B 57  ? THR B 55  ALA B 57  5 ? 3  
HELX_P HELX_P11 AB2 TRP B 68  ? ARG B 90  ? TRP B 68  ARG B 90  1 ? 23 
HELX_P HELX_P12 AB3 GLU B 95  ? ASP B 115 ? GLU B 95  ASP B 115 1 ? 21 
HELX_P HELX_P13 AB4 ASN B 140 ? LEU B 155 ? ASN B 140 LEU B 155 1 ? 16 
HELX_P HELX_P14 AB5 LEU C 13  ? LEU C 34  ? LEU C 13  LEU C 34  1 ? 22 
HELX_P HELX_P15 AB6 GLY C 56  ? ALA C 63  ? GLY C 56  ALA C 63  5 ? 8  
HELX_P HELX_P16 AB7 GLY C 67  ? LEU C 91  ? GLY C 67  LEU C 91  1 ? 25 
HELX_P HELX_P17 AB8 GLU C 95  ? LEU C 119 ? GLU C 95  LEU C 119 1 ? 25 
HELX_P HELX_P18 AB9 ASN C 140 ? LEU C 155 ? ASN C 140 LEU C 155 1 ? 16 
HELX_P HELX_P19 AC1 TRP D 12  ? LEU D 34  ? TRP D 12  LEU D 34  1 ? 23 
HELX_P HELX_P20 AC2 GLY D 67  ? ARG D 90  ? GLY D 67  ARG D 90  1 ? 24 
HELX_P HELX_P21 AC3 GLU D 95  ? LEU D 119 ? GLU D 95  LEU D 119 1 ? 25 
HELX_P HELX_P22 AC4 ASN D 140 ? ASP D 156 ? ASN D 140 ASP D 156 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? E MLE 1 C ? ? ? 1_555 E IIL 2 N ? ? E MLE 201 E IIL 202 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale2  covale both ? E MLE 1 N ? ? ? 1_555 E 5BV 5 C ? ? E MLE 201 E 5BV 205 1_555 ? ? ? ? ? ? ? 1.592 ? ? 
covale3  covale both ? E IIL 2 C ? ? ? 1_555 E SER 3 N ? ? E IIL 202 E SER 203 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale4  covale both ? E SER 3 C ? ? ? 1_555 E ALO 4 N ? ? E SER 203 E ALO 204 1_555 ? ? ? ? ? ? ? 1.460 ? ? 
covale5  covale both ? E ALO 4 C ? ? ? 1_555 E 5BV 5 N ? ? E ALO 204 E 5BV 205 1_555 ? ? ? ? ? ? ? 1.648 ? ? 
covale6  covale both ? F MLE 1 C ? ? ? 1_555 F IIL 2 N ? ? F MLE 201 F IIL 202 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale7  covale both ? F MLE 1 N ? ? ? 1_555 F 5BV 5 C ? ? F MLE 201 F 5BV 205 1_555 ? ? ? ? ? ? ? 1.510 ? ? 
covale8  covale both ? F IIL 2 C ? ? ? 1_555 F SER 3 N ? ? F IIL 202 F SER 203 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale9  covale both ? F SER 3 C ? ? ? 1_555 F ALO 4 N ? ? F SER 203 F ALO 204 1_555 ? ? ? ? ? ? ? 1.563 ? ? 
covale10 covale both ? F ALO 4 C ? ? ? 1_555 F 5BV 5 N ? ? F ALO 204 F 5BV 205 1_555 ? ? ? ? ? ? ? 1.128 ? ? 
covale11 covale both ? G MLE 1 C ? ? ? 1_555 G IIL 2 N ? ? G MLE 201 G IIL 202 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale12 covale both ? G MLE 1 N ? ? ? 1_555 G 5BV 5 C ? ? G MLE 201 G 5BV 205 1_555 ? ? ? ? ? ? ? 1.431 ? ? 
covale13 covale both ? G IIL 2 C ? ? ? 1_555 G SER 3 N ? ? G IIL 202 G SER 203 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale14 covale both ? G SER 3 C ? ? ? 1_555 G ALO 4 N ? ? G SER 203 G ALO 204 1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale15 covale both ? G ALO 4 C ? ? ? 1_555 G 5BV 5 N ? ? G ALO 204 G 5BV 205 1_555 ? ? ? ? ? ? ? 1.579 ? ? 
covale16 covale both ? H MLE 1 C ? ? ? 1_555 H IIL 2 N ? ? H MLE 201 H IIL 202 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale17 covale both ? H MLE 1 N ? ? ? 1_555 H 5BV 5 C ? ? H MLE 201 H 5BV 205 1_555 ? ? ? ? ? ? ? 1.433 ? ? 
covale18 covale both ? H IIL 2 C ? ? ? 1_555 H SER 3 N ? ? H IIL 202 H SER 203 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale19 covale both ? H SER 3 C ? ? ? 1_555 H ALO 4 N ? ? H SER 203 H ALO 204 1_555 ? ? ? ? ? ? ? 1.471 ? ? 
covale20 covale both ? H ALO 4 C ? ? ? 1_555 H 5BV 5 N ? ? H ALO 204 H 5BV 205 1_555 ? ? ? ? ? ? ? 1.532 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  MLE E 1 ? .   . . . MLE E 201 ? 1_555 .   . .   . .     . . LEU 1 MLE Methylation         'Named protein modification' 
2  IIL E 2 ? .   . . . IIL E 202 ? 1_555 .   . .   . .     . . ILE 1 IIL Stereoisomerisation 'Named protein modification' 
3  ALO E 4 ? .   . . . ALO E 204 ? 1_555 .   . .   . .     . . THR 1 ALO Stereoisomerisation 'Named protein modification' 
4  MLE F 1 ? .   . . . MLE F 201 ? 1_555 .   . .   . .     . . LEU 1 MLE Methylation         'Named protein modification' 
5  IIL F 2 ? .   . . . IIL F 202 ? 1_555 .   . .   . .     . . ILE 1 IIL Stereoisomerisation 'Named protein modification' 
6  ALO F 4 ? .   . . . ALO F 204 ? 1_555 .   . .   . .     . . THR 1 ALO Stereoisomerisation 'Named protein modification' 
7  MLE G 1 ? .   . . . MLE G 201 ? 1_555 .   . .   . .     . . LEU 1 MLE Methylation         'Named protein modification' 
8  IIL G 2 ? .   . . . IIL G 202 ? 1_555 .   . .   . .     . . ILE 1 IIL Stereoisomerisation 'Named protein modification' 
9  ALO G 4 ? .   . . . ALO G 204 ? 1_555 .   . .   . .     . . THR 1 ALO Stereoisomerisation 'Named protein modification' 
10 MLE H 1 ? .   . . . MLE H 201 ? 1_555 .   . .   . .     . . LEU 1 MLE Methylation         'Named protein modification' 
11 IIL H 2 ? .   . . . IIL H 202 ? 1_555 .   . .   . .     . . ILE 1 IIL Stereoisomerisation 'Named protein modification' 
12 ALO H 4 ? .   . . . ALO H 204 ? 1_555 .   . .   . .     . . THR 1 ALO Stereoisomerisation 'Named protein modification' 
13 5BV E 5 ? .   . . . 5BV E 205 ? 1_555 .   . .   . .     . . ?   1 5BV None                'Non-standard residue'       
14 5BV F 5 ? .   . . . 5BV F 205 ? 1_555 .   . .   . .     . . ?   1 5BV None                'Non-standard residue'       
15 5BV G 5 ? .   . . . 5BV G 205 ? 1_555 .   . .   . .     . . ?   1 5BV None                'Non-standard residue'       
16 5BV H 5 ? .   . . . 5BV H 205 ? 1_555 .   . .   . .     . . ?   1 5BV None                'Non-standard residue'       
17 MLE E 1 ? 5BV E 5 ? MLE E 201 ? 1_555 5BV E 205 ? 1_555 N C .   . .   None                'Non-standard linkage'       
18 MLE F 1 ? 5BV F 5 ? MLE F 201 ? 1_555 5BV F 205 ? 1_555 N C .   . .   None                'Non-standard linkage'       
19 MLE G 1 ? 5BV G 5 ? MLE G 201 ? 1_555 5BV G 205 ? 1_555 N C .   . .   None                'Non-standard linkage'       
20 MLE H 1 ? 5BV H 5 ? MLE H 201 ? 1_555 5BV H 205 ? 1_555 N C .   . .   None                'Non-standard linkage'       
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? 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 ILE A 40  ? ILE A 43  ? ILE A 40  ILE A 43  
AA1 2 PHE A 47  ? ASN A 54  ? PHE A 47  ASN A 54  
AA1 3 VAL A 122 ? TRP A 130 ? VAL A 122 TRP A 130 
AA1 4 TRP A 134 ? TYR A 135 ? TRP A 134 TYR A 135 
AA2 1 ILE B 40  ? ILE B 43  ? ILE B 40  ILE B 43  
AA2 2 PHE B 47  ? TYR B 53  ? PHE B 47  TYR B 53  
AA2 3 VAL B 123 ? TRP B 130 ? VAL B 123 TRP B 130 
AA2 4 TRP B 134 ? TYR B 135 ? TRP B 134 TYR B 135 
AA3 1 ILE C 40  ? ILE C 43  ? ILE C 40  ILE C 43  
AA3 2 PHE C 47  ? TYR C 53  ? PHE C 47  TYR C 53  
AA3 3 VAL C 123 ? TRP C 130 ? VAL C 123 TRP C 130 
AA3 4 TRP C 134 ? TYR C 135 ? TRP C 134 TYR C 135 
AA4 1 ILE D 40  ? ILE D 43  ? ILE D 40  ILE D 43  
AA4 2 PHE D 47  ? ASN D 54  ? PHE D 47  ASN D 54  
AA4 3 VAL D 122 ? TRP D 130 ? VAL D 122 TRP D 130 
AA4 4 TRP D 134 ? TYR D 135 ? TRP D 134 TYR D 135 
# 
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 ILE A 40  ? N ILE A 40  O TRP A 49  ? O TRP A 49  
AA1 2 3 N ASN A 54  ? N ASN A 54  O VAL A 122 ? O VAL A 122 
AA1 3 4 N TRP A 130 ? N TRP A 130 O TRP A 134 ? O TRP A 134 
AA2 1 2 N ILE B 40  ? N ILE B 40  O TRP B 49  ? O TRP B 49  
AA2 2 3 N ALA B 52  ? N ALA B 52  O ASP B 124 ? O ASP B 124 
AA2 3 4 N TRP B 130 ? N TRP B 130 O TRP B 134 ? O TRP B 134 
AA3 1 2 N ILE C 40  ? N ILE C 40  O TRP C 49  ? O TRP C 49  
AA3 2 3 N ALA C 52  ? N ALA C 52  O ASP C 124 ? O ASP C 124 
AA3 3 4 N TRP C 130 ? N TRP C 130 O TRP C 134 ? O TRP C 134 
AA4 1 2 N ILE D 40  ? N ILE D 40  O TRP D 49  ? O TRP D 49  
AA4 2 3 N THR D 50  ? N THR D 50  O PHE D 125 ? O PHE D 125 
AA4 3 4 N TRP D 130 ? N TRP D 130 O TRP D 134 ? O TRP D 134 
# 
_pdbx_entry_details.entry_id                   9EMZ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C E ALO 204 ? ? N E 5BV 205 ? ? 1.648 1.336 0.312  0.023 Y 
2 1 C F SER 203 ? ? N F ALO 204 ? ? 1.563 1.336 0.227  0.023 Y 
3 1 C F ALO 204 ? ? N F 5BV 205 ? ? 1.128 1.336 -0.208 0.023 Y 
4 1 C G ALO 204 ? ? N G 5BV 205 ? ? 1.579 1.336 0.243  0.023 Y 
5 1 C H ALO 204 ? ? N H 5BV 205 ? ? 1.532 1.336 0.196  0.023 Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 O  E SER 203 ? ? C E SER 203 ? ? N  E ALO 204 ? ? 112.41 122.70 -10.29 1.60 Y 
2 1 O  E ALO 204 ? ? C E ALO 204 ? ? N  E 5BV 205 ? ? 111.76 122.70 -10.94 1.60 Y 
3 1 CA F SER 203 ? ? C F SER 203 ? ? N  F ALO 204 ? ? 133.58 117.20 16.38  2.20 Y 
4 1 O  F SER 203 ? ? C F SER 203 ? ? N  F ALO 204 ? ? 111.06 122.70 -11.64 1.60 Y 
5 1 C  F SER 203 ? ? N F ALO 204 ? ? CA F ALO 204 ? ? 138.97 121.70 17.27  2.50 Y 
6 1 O  G ALO 204 ? ? C G ALO 204 ? ? N  G 5BV 205 ? ? 109.75 122.70 -12.95 1.60 Y 
7 1 CA H ALO 204 ? ? C H ALO 204 ? ? N  H 5BV 205 ? ? 136.63 117.20 19.43  2.20 Y 
8 1 O  H ALO 204 ? ? C H ALO 204 ? ? N  H 5BV 205 ? ? 101.99 122.70 -20.71 1.60 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 VAL A 42  ? ? -109.43 -63.84  
2  1 LEU A 51  ? ? -141.68 48.63   
3  1 PHE A 125 ? ? -144.63 25.08   
4  1 GLN A 131 ? ? 56.56   -154.64 
5  1 THR B 55  ? ? 74.97   -9.64   
6  1 GLU B 95  ? ? -94.14  56.76   
7  1 GLN B 131 ? ? 50.52   -139.03 
8  1 VAL C 42  ? ? -104.78 -61.86  
9  1 GLN C 131 ? ? 57.42   -142.84 
10 1 PHE C 158 ? ? -94.65  30.31   
11 1 ARG D 90  ? ? -96.55  31.61   
12 1 PHE D 125 ? ? -142.45 -4.03   
13 1 GLN D 131 ? ? 52.40   -109.27 
14 1 IIL E 202 ? ? -66.17  -175.12 
15 1 IIL F 202 ? ? -68.70  -176.47 
16 1 ALO H 204 ? ? -66.55  62.82   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   SER 
_pdbx_validate_peptide_omega.auth_asym_id_1   F 
_pdbx_validate_peptide_omega.auth_seq_id_1    203 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   ALO 
_pdbx_validate_peptide_omega.auth_asym_id_2   F 
_pdbx_validate_peptide_omega.auth_seq_id_2    204 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -137.71 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 SER E 203 ? ? 22.11  
2 1 ALO G 204 ? ? -29.12 
3 1 SER H 203 ? ? 10.40  
4 1 ALO H 204 ? ? -28.76 
# 
loop_
_pdbx_validate_polymer_linkage.id 
_pdbx_validate_polymer_linkage.PDB_model_num 
_pdbx_validate_polymer_linkage.auth_atom_id_1 
_pdbx_validate_polymer_linkage.auth_asym_id_1 
_pdbx_validate_polymer_linkage.auth_comp_id_1 
_pdbx_validate_polymer_linkage.auth_seq_id_1 
_pdbx_validate_polymer_linkage.PDB_ins_code_1 
_pdbx_validate_polymer_linkage.label_alt_id_1 
_pdbx_validate_polymer_linkage.auth_atom_id_2 
_pdbx_validate_polymer_linkage.auth_asym_id_2 
_pdbx_validate_polymer_linkage.auth_comp_id_2 
_pdbx_validate_polymer_linkage.auth_seq_id_2 
_pdbx_validate_polymer_linkage.PDB_ins_code_2 
_pdbx_validate_polymer_linkage.label_alt_id_2 
_pdbx_validate_polymer_linkage.dist 
1 1 C E ALO 204 ? ? N E 5BV 205 ? ? 1.65 
2 1 C F ALO 204 ? ? N F 5BV 205 ? ? 1.13 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ARG 159 ? A ARG 159 
3  1 Y 1 A SER 160 ? A SER 160 
4  1 Y 1 A LYS 161 ? A LYS 161 
5  1 Y 1 A LYS 162 ? A LYS 162 
6  1 Y 1 A SER 163 ? A SER 163 
7  1 Y 1 A GLY 164 ? A GLY 164 
8  1 Y 1 A GLU 165 ? A GLU 165 
9  1 Y 1 A ALA 166 ? A ALA 166 
10 1 Y 1 A ALA 167 ? A ALA 167 
11 1 Y 1 A HIS 168 ? A HIS 168 
12 1 Y 1 A GLY 169 ? A GLY 169 
13 1 Y 1 B MET 1   ? B MET 1   
14 1 Y 1 B PHE 61  ? B PHE 61  
15 1 Y 1 B LEU 62  ? B LEU 62  
16 1 Y 1 B ALA 63  ? B ALA 63  
17 1 Y 1 B ASP 64  ? B ASP 64  
18 1 Y 1 B SER 65  ? B SER 65  
19 1 Y 1 B SER 66  ? B SER 66  
20 1 Y 1 B MET 157 ? B MET 157 
21 1 Y 1 B PHE 158 ? B PHE 158 
22 1 Y 1 B ARG 159 ? B ARG 159 
23 1 Y 1 B SER 160 ? B SER 160 
24 1 Y 1 B LYS 161 ? B LYS 161 
25 1 Y 1 B LYS 162 ? B LYS 162 
26 1 Y 1 B SER 163 ? B SER 163 
27 1 Y 1 B GLY 164 ? B GLY 164 
28 1 Y 1 B GLU 165 ? B GLU 165 
29 1 Y 1 B ALA 166 ? B ALA 166 
30 1 Y 1 B ALA 167 ? B ALA 167 
31 1 Y 1 B HIS 168 ? B HIS 168 
32 1 Y 1 B GLY 169 ? B GLY 169 
33 1 Y 1 C MET 1   ? C MET 1   
34 1 Y 1 C PRO 2   ? C PRO 2   
35 1 Y 1 C ASP 3   ? C ASP 3   
36 1 Y 1 C VAL 4   ? C VAL 4   
37 1 Y 1 C ASP 5   ? C ASP 5   
38 1 Y 1 C ARG 6   ? C ARG 6   
39 1 Y 1 C PHE 7   ? C PHE 7   
40 1 Y 1 C GLY 8   ? C GLY 8   
41 1 Y 1 C ARG 9   ? C ARG 9   
42 1 Y 1 C LEU 10  ? C LEU 10  
43 1 Y 1 C SER 160 ? C SER 160 
44 1 Y 1 C LYS 161 ? C LYS 161 
45 1 Y 1 C LYS 162 ? C LYS 162 
46 1 Y 1 C SER 163 ? C SER 163 
47 1 Y 1 C GLY 164 ? C GLY 164 
48 1 Y 1 C GLU 165 ? C GLU 165 
49 1 Y 1 C ALA 166 ? C ALA 166 
50 1 Y 1 C ALA 167 ? C ALA 167 
51 1 Y 1 C HIS 168 ? C HIS 168 
52 1 Y 1 C GLY 169 ? C GLY 169 
53 1 Y 1 D MET 1   ? D MET 1   
54 1 Y 1 D PRO 2   ? D PRO 2   
55 1 Y 1 D ASP 3   ? D ASP 3   
56 1 Y 1 D VAL 4   ? D VAL 4   
57 1 Y 1 D ASP 5   ? D ASP 5   
58 1 Y 1 D ARG 6   ? D ARG 6   
59 1 Y 1 D PHE 7   ? D PHE 7   
60 1 Y 1 D GLY 8   ? D GLY 8   
61 1 Y 1 D ARG 9   ? D ARG 9   
62 1 Y 1 D LEU 10  ? D LEU 10  
63 1 Y 1 D SER 160 ? D SER 160 
64 1 Y 1 D LYS 161 ? D LYS 161 
65 1 Y 1 D LYS 162 ? D LYS 162 
66 1 Y 1 D SER 163 ? D SER 163 
67 1 Y 1 D GLY 164 ? D GLY 164 
68 1 Y 1 D GLU 165 ? D GLU 165 
69 1 Y 1 D ALA 166 ? D ALA 166 
70 1 Y 1 D ALA 167 ? D ALA 167 
71 1 Y 1 D HIS 168 ? D HIS 168 
72 1 Y 1 D GLY 169 ? D GLY 169 
# 
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 
5BV O34  O N N 1   
5BV O35  O N N 2   
5BV O    O N N 3   
5BV N    N N N 4   
5BV C32  C N N 5   
5BV C33  C N N 6   
5BV C36  C N R 7   
5BV C37  C N N 8   
5BV C38  C N N 9   
5BV C39  C N N 10  
5BV C40  C N N 11  
5BV C41  C N N 12  
5BV C42  C N N 13  
5BV C43  C N R 14  
5BV C44  C N N 15  
5BV C    C N N 16  
5BV H    H N N 17  
5BV H2   H N N 18  
5BV H4   H N N 19  
5BV H5   H N N 20  
5BV H6   H N N 21  
5BV H7   H N N 22  
5BV H8   H N N 23  
5BV H9   H N N 24  
5BV H10  H N N 25  
5BV H11  H N N 26  
5BV H12  H N N 27  
5BV H13  H N N 28  
5BV H14  H N N 29  
5BV H15  H N N 30  
5BV H16  H N N 31  
5BV H17  H N N 32  
5BV H18  H N N 33  
5BV H19  H N N 34  
5BV H20  H N N 35  
5BV H21  H N N 36  
5BV H22  H N N 37  
5BV H23  H N N 38  
5BV OXT  O N N 39  
5BV HXT  H N N 40  
ALA N    N N N 41  
ALA CA   C N S 42  
ALA C    C N N 43  
ALA O    O N N 44  
ALA CB   C N N 45  
ALA OXT  O N N 46  
ALA H    H N N 47  
ALA H2   H N N 48  
ALA HA   H N N 49  
ALA HB1  H N N 50  
ALA HB2  H N N 51  
ALA HB3  H N N 52  
ALA HXT  H N N 53  
ALO N    N N N 54  
ALO CA   C N S 55  
ALO CB   C N S 56  
ALO CG2  C N N 57  
ALO OG1  O N N 58  
ALO C    C N N 59  
ALO O    O N N 60  
ALO OXT  O N N 61  
ALO H    H N N 62  
ALO H2   H N N 63  
ALO HA   H N N 64  
ALO HB   H N N 65  
ALO HG21 H N N 66  
ALO HG22 H N N 67  
ALO HG23 H N N 68  
ALO HG1  H N N 69  
ALO HXT  H N N 70  
ARG N    N N N 71  
ARG CA   C N S 72  
ARG C    C N N 73  
ARG O    O N N 74  
ARG CB   C N N 75  
ARG CG   C N N 76  
ARG CD   C N N 77  
ARG NE   N N N 78  
ARG CZ   C N N 79  
ARG NH1  N N N 80  
ARG NH2  N N N 81  
ARG OXT  O N N 82  
ARG H    H N N 83  
ARG H2   H N N 84  
ARG HA   H N N 85  
ARG HB2  H N N 86  
ARG HB3  H N N 87  
ARG HG2  H N N 88  
ARG HG3  H N N 89  
ARG HD2  H N N 90  
ARG HD3  H N N 91  
ARG HE   H N N 92  
ARG HH11 H N N 93  
ARG HH12 H N N 94  
ARG HH21 H N N 95  
ARG HH22 H N N 96  
ARG HXT  H N N 97  
ASN N    N N N 98  
ASN CA   C N S 99  
ASN C    C N N 100 
ASN O    O N N 101 
ASN CB   C N N 102 
ASN CG   C N N 103 
ASN OD1  O N N 104 
ASN ND2  N N N 105 
ASN OXT  O N N 106 
ASN H    H N N 107 
ASN H2   H N N 108 
ASN HA   H N N 109 
ASN HB2  H N N 110 
ASN HB3  H N N 111 
ASN HD21 H N N 112 
ASN HD22 H N N 113 
ASN HXT  H N N 114 
ASP N    N N N 115 
ASP CA   C N S 116 
ASP C    C N N 117 
ASP O    O N N 118 
ASP CB   C N N 119 
ASP CG   C N N 120 
ASP OD1  O N N 121 
ASP OD2  O N N 122 
ASP OXT  O N N 123 
ASP H    H N N 124 
ASP H2   H N N 125 
ASP HA   H N N 126 
ASP HB2  H N N 127 
ASP HB3  H N N 128 
ASP HD2  H N N 129 
ASP HXT  H N N 130 
GLN N    N N N 131 
GLN CA   C N S 132 
GLN C    C N N 133 
GLN O    O N N 134 
GLN CB   C N N 135 
GLN CG   C N N 136 
GLN CD   C N N 137 
GLN OE1  O N N 138 
GLN NE2  N N N 139 
GLN OXT  O N N 140 
GLN H    H N N 141 
GLN H2   H N N 142 
GLN HA   H N N 143 
GLN HB2  H N N 144 
GLN HB3  H N N 145 
GLN HG2  H N N 146 
GLN HG3  H N N 147 
GLN HE21 H N N 148 
GLN HE22 H N N 149 
GLN HXT  H N N 150 
GLU N    N N N 151 
GLU CA   C N S 152 
GLU C    C N N 153 
GLU O    O N N 154 
GLU CB   C N N 155 
GLU CG   C N N 156 
GLU CD   C N N 157 
GLU OE1  O N N 158 
GLU OE2  O N N 159 
GLU OXT  O N N 160 
GLU H    H N N 161 
GLU H2   H N N 162 
GLU HA   H N N 163 
GLU HB2  H N N 164 
GLU HB3  H N N 165 
GLU HG2  H N N 166 
GLU HG3  H N N 167 
GLU HE2  H N N 168 
GLU HXT  H N N 169 
GLY N    N N N 170 
GLY CA   C N N 171 
GLY C    C N N 172 
GLY O    O N N 173 
GLY OXT  O N N 174 
GLY H    H N N 175 
GLY H2   H N N 176 
GLY HA2  H N N 177 
GLY HA3  H N N 178 
GLY HXT  H N N 179 
HIS N    N N N 180 
HIS CA   C N S 181 
HIS C    C N N 182 
HIS O    O N N 183 
HIS CB   C N N 184 
HIS CG   C Y N 185 
HIS ND1  N Y N 186 
HIS CD2  C Y N 187 
HIS CE1  C Y N 188 
HIS NE2  N Y N 189 
HIS OXT  O N N 190 
HIS H    H N N 191 
HIS H2   H N N 192 
HIS HA   H N N 193 
HIS HB2  H N N 194 
HIS HB3  H N N 195 
HIS HD1  H N N 196 
HIS HD2  H N N 197 
HIS HE1  H N N 198 
HIS HE2  H N N 199 
HIS HXT  H N N 200 
HOH O    O N N 201 
HOH H1   H N N 202 
HOH H2   H N N 203 
IIL N    N N N 204 
IIL CA   C N S 205 
IIL C    C N N 206 
IIL O    O N N 207 
IIL CB   C N R 208 
IIL CG2  C N N 209 
IIL CG1  C N N 210 
IIL CD1  C N N 211 
IIL OXT  O N N 212 
IIL H    H N N 213 
IIL H2   H N N 214 
IIL HA   H N N 215 
IIL HB   H N N 216 
IIL HG21 H N N 217 
IIL HG22 H N N 218 
IIL HG23 H N N 219 
IIL HG12 H N N 220 
IIL HG13 H N N 221 
IIL HD11 H N N 222 
IIL HD12 H N N 223 
IIL HD13 H N N 224 
IIL HXT  H N N 225 
ILE N    N N N 226 
ILE CA   C N S 227 
ILE C    C N N 228 
ILE O    O N N 229 
ILE CB   C N S 230 
ILE CG1  C N N 231 
ILE CG2  C N N 232 
ILE CD1  C N N 233 
ILE OXT  O N N 234 
ILE H    H N N 235 
ILE H2   H N N 236 
ILE HA   H N N 237 
ILE HB   H N N 238 
ILE HG12 H N N 239 
ILE HG13 H N N 240 
ILE HG21 H N N 241 
ILE HG22 H N N 242 
ILE HG23 H N N 243 
ILE HD11 H N N 244 
ILE HD12 H N N 245 
ILE HD13 H N N 246 
ILE HXT  H N N 247 
LEU N    N N N 248 
LEU CA   C N S 249 
LEU C    C N N 250 
LEU O    O N N 251 
LEU CB   C N N 252 
LEU CG   C N N 253 
LEU CD1  C N N 254 
LEU CD2  C N N 255 
LEU OXT  O N N 256 
LEU H    H N N 257 
LEU H2   H N N 258 
LEU HA   H N N 259 
LEU HB2  H N N 260 
LEU HB3  H N N 261 
LEU HG   H N N 262 
LEU HD11 H N N 263 
LEU HD12 H N N 264 
LEU HD13 H N N 265 
LEU HD21 H N N 266 
LEU HD22 H N N 267 
LEU HD23 H N N 268 
LEU HXT  H N N 269 
LYS N    N N N 270 
LYS CA   C N S 271 
LYS C    C N N 272 
LYS O    O N N 273 
LYS CB   C N N 274 
LYS CG   C N N 275 
LYS CD   C N N 276 
LYS CE   C N N 277 
LYS NZ   N N N 278 
LYS OXT  O N N 279 
LYS H    H N N 280 
LYS H2   H N N 281 
LYS HA   H N N 282 
LYS HB2  H N N 283 
LYS HB3  H N N 284 
LYS HG2  H N N 285 
LYS HG3  H N N 286 
LYS HD2  H N N 287 
LYS HD3  H N N 288 
LYS HE2  H N N 289 
LYS HE3  H N N 290 
LYS HZ1  H N N 291 
LYS HZ2  H N N 292 
LYS HZ3  H N N 293 
LYS HXT  H N N 294 
MET N    N N N 295 
MET CA   C N S 296 
MET C    C N N 297 
MET O    O N N 298 
MET CB   C N N 299 
MET CG   C N N 300 
MET SD   S N N 301 
MET CE   C N N 302 
MET OXT  O N N 303 
MET H    H N N 304 
MET H2   H N N 305 
MET HA   H N N 306 
MET HB2  H N N 307 
MET HB3  H N N 308 
MET HG2  H N N 309 
MET HG3  H N N 310 
MET HE1  H N N 311 
MET HE2  H N N 312 
MET HE3  H N N 313 
MET HXT  H N N 314 
MLE N    N N N 315 
MLE CN   C N N 316 
MLE CA   C N S 317 
MLE CB   C N N 318 
MLE CG   C N N 319 
MLE CD1  C N N 320 
MLE CD2  C N N 321 
MLE C    C N N 322 
MLE O    O N N 323 
MLE OXT  O N N 324 
MLE H    H N N 325 
MLE HN1  H N N 326 
MLE HN2  H N N 327 
MLE HN3  H N N 328 
MLE HA   H N N 329 
MLE HB2  H N N 330 
MLE HB3  H N N 331 
MLE HG   H N N 332 
MLE HD11 H N N 333 
MLE HD12 H N N 334 
MLE HD13 H N N 335 
MLE HD21 H N N 336 
MLE HD22 H N N 337 
MLE HD23 H N N 338 
MLE HXT  H N N 339 
OLC C18  C N N 340 
OLC C10  C N N 341 
OLC C9   C N N 342 
OLC C17  C N N 343 
OLC C11  C N N 344 
OLC C8   C N N 345 
OLC C24  C N N 346 
OLC C16  C N N 347 
OLC C12  C N N 348 
OLC C7   C N N 349 
OLC C15  C N N 350 
OLC C13  C N N 351 
OLC C6   C N N 352 
OLC C14  C N N 353 
OLC C5   C N N 354 
OLC C4   C N N 355 
OLC C3   C N N 356 
OLC C2   C N N 357 
OLC C21  C N N 358 
OLC C1   C N N 359 
OLC C22  C N R 360 
OLC O19  O N N 361 
OLC O25  O N N 362 
OLC O23  O N N 363 
OLC O20  O N N 364 
OLC H18  H N N 365 
OLC H18A H N N 366 
OLC H18B H N N 367 
OLC H10  H N N 368 
OLC H9   H N N 369 
OLC H17  H N N 370 
OLC H17A H N N 371 
OLC H11  H N N 372 
OLC H11A H N N 373 
OLC H8   H N N 374 
OLC H8A  H N N 375 
OLC H24  H N N 376 
OLC H24A H N N 377 
OLC H16  H N N 378 
OLC H16A H N N 379 
OLC H12  H N N 380 
OLC H12A H N N 381 
OLC H7   H N N 382 
OLC H7A  H N N 383 
OLC H15  H N N 384 
OLC H15A H N N 385 
OLC H13  H N N 386 
OLC H13A H N N 387 
OLC H6   H N N 388 
OLC H6A  H N N 389 
OLC H14  H N N 390 
OLC H14A H N N 391 
OLC H5   H N N 392 
OLC H5A  H N N 393 
OLC H4   H N N 394 
OLC H4A  H N N 395 
OLC H3   H N N 396 
OLC H3A  H N N 397 
OLC H2   H N N 398 
OLC H2A  H N N 399 
OLC H21  H N N 400 
OLC H21A H N N 401 
OLC H22  H N N 402 
OLC HO25 H N N 403 
OLC HO23 H N N 404 
PHE N    N N N 405 
PHE CA   C N S 406 
PHE C    C N N 407 
PHE O    O N N 408 
PHE CB   C N N 409 
PHE CG   C Y N 410 
PHE CD1  C Y N 411 
PHE CD2  C Y N 412 
PHE CE1  C Y N 413 
PHE CE2  C Y N 414 
PHE CZ   C Y N 415 
PHE OXT  O N N 416 
PHE H    H N N 417 
PHE H2   H N N 418 
PHE HA   H N N 419 
PHE HB2  H N N 420 
PHE HB3  H N N 421 
PHE HD1  H N N 422 
PHE HD2  H N N 423 
PHE HE1  H N N 424 
PHE HE2  H N N 425 
PHE HZ   H N N 426 
PHE HXT  H N N 427 
PRO N    N N N 428 
PRO CA   C N S 429 
PRO C    C N N 430 
PRO O    O N N 431 
PRO CB   C N N 432 
PRO CG   C N N 433 
PRO CD   C N N 434 
PRO OXT  O N N 435 
PRO H    H N N 436 
PRO HA   H N N 437 
PRO HB2  H N N 438 
PRO HB3  H N N 439 
PRO HG2  H N N 440 
PRO HG3  H N N 441 
PRO HD2  H N N 442 
PRO HD3  H N N 443 
PRO HXT  H N N 444 
SER N    N N N 445 
SER CA   C N S 446 
SER C    C N N 447 
SER O    O N N 448 
SER CB   C N N 449 
SER OG   O N N 450 
SER OXT  O N N 451 
SER H    H N N 452 
SER H2   H N N 453 
SER HA   H N N 454 
SER HB2  H N N 455 
SER HB3  H N N 456 
SER HG   H N N 457 
SER HXT  H N N 458 
THR N    N N N 459 
THR CA   C N S 460 
THR C    C N N 461 
THR O    O N N 462 
THR CB   C N R 463 
THR OG1  O N N 464 
THR CG2  C N N 465 
THR OXT  O N N 466 
THR H    H N N 467 
THR H2   H N N 468 
THR HA   H N N 469 
THR HB   H N N 470 
THR HG1  H N N 471 
THR HG21 H N N 472 
THR HG22 H N N 473 
THR HG23 H N N 474 
THR HXT  H N N 475 
TRP N    N N N 476 
TRP CA   C N S 477 
TRP C    C N N 478 
TRP O    O N N 479 
TRP CB   C N N 480 
TRP CG   C Y N 481 
TRP CD1  C Y N 482 
TRP CD2  C Y N 483 
TRP NE1  N Y N 484 
TRP CE2  C Y N 485 
TRP CE3  C Y N 486 
TRP CZ2  C Y N 487 
TRP CZ3  C Y N 488 
TRP CH2  C Y N 489 
TRP OXT  O N N 490 
TRP H    H N N 491 
TRP H2   H N N 492 
TRP HA   H N N 493 
TRP HB2  H N N 494 
TRP HB3  H N N 495 
TRP HD1  H N N 496 
TRP HE1  H N N 497 
TRP HE3  H N N 498 
TRP HZ2  H N N 499 
TRP HZ3  H N N 500 
TRP HH2  H N N 501 
TRP HXT  H N N 502 
TYR N    N N N 503 
TYR CA   C N S 504 
TYR C    C N N 505 
TYR O    O N N 506 
TYR CB   C N N 507 
TYR CG   C Y N 508 
TYR CD1  C Y N 509 
TYR CD2  C Y N 510 
TYR CE1  C Y N 511 
TYR CE2  C Y N 512 
TYR CZ   C Y N 513 
TYR OH   O N N 514 
TYR OXT  O N N 515 
TYR H    H N N 516 
TYR H2   H N N 517 
TYR HA   H N N 518 
TYR HB2  H N N 519 
TYR HB3  H N N 520 
TYR HD1  H N N 521 
TYR HD2  H N N 522 
TYR HE1  H N N 523 
TYR HE2  H N N 524 
TYR HH   H N N 525 
TYR HXT  H N N 526 
VAL N    N N N 527 
VAL CA   C N S 528 
VAL C    C N N 529 
VAL O    O N N 530 
VAL CB   C N N 531 
VAL CG1  C N N 532 
VAL CG2  C N N 533 
VAL OXT  O N N 534 
VAL H    H N N 535 
VAL H2   H N N 536 
VAL HA   H N N 537 
VAL HB   H N N 538 
VAL HG11 H N N 539 
VAL HG12 H N N 540 
VAL HG13 H N N 541 
VAL HG21 H N N 542 
VAL HG22 H N N 543 
VAL HG23 H N N 544 
VAL HXT  H N N 545 
# 
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 
5BV N   C32  sing N N 1   
5BV O34 C33  doub N N 2   
5BV O   C    doub N N 3   
5BV C33 C32  sing N N 4   
5BV C33 O35  sing N N 5   
5BV C   C43  sing N N 6   
5BV O35 C36  sing N N 7   
5BV C36 C43  sing N N 8   
5BV C36 C37  sing N N 9   
5BV C38 C37  sing N N 10  
5BV C38 C39  sing N N 11  
5BV C43 C44  sing N N 12  
5BV C39 C40  sing N N 13  
5BV C40 C41  sing N N 14  
5BV C41 C42  sing N N 15  
5BV N   H    sing N N 16  
5BV N   H2   sing N N 17  
5BV C32 H4   sing N N 18  
5BV C32 H5   sing N N 19  
5BV C36 H6   sing N N 20  
5BV C37 H7   sing N N 21  
5BV C37 H8   sing N N 22  
5BV C38 H9   sing N N 23  
5BV C38 H10  sing N N 24  
5BV C39 H11  sing N N 25  
5BV C39 H12  sing N N 26  
5BV C40 H13  sing N N 27  
5BV C40 H14  sing N N 28  
5BV C41 H15  sing N N 29  
5BV C41 H16  sing N N 30  
5BV C42 H17  sing N N 31  
5BV C42 H18  sing N N 32  
5BV C42 H19  sing N N 33  
5BV C43 H20  sing N N 34  
5BV C44 H21  sing N N 35  
5BV C44 H22  sing N N 36  
5BV C44 H23  sing N N 37  
5BV C   OXT  sing N N 38  
5BV OXT HXT  sing N N 39  
ALA N   CA   sing N N 40  
ALA N   H    sing N N 41  
ALA N   H2   sing N N 42  
ALA CA  C    sing N N 43  
ALA CA  CB   sing N N 44  
ALA CA  HA   sing N N 45  
ALA C   O    doub N N 46  
ALA C   OXT  sing N N 47  
ALA CB  HB1  sing N N 48  
ALA CB  HB2  sing N N 49  
ALA CB  HB3  sing N N 50  
ALA OXT HXT  sing N N 51  
ALO N   CA   sing N N 52  
ALO N   H    sing N N 53  
ALO N   H2   sing N N 54  
ALO CA  CB   sing N N 55  
ALO CA  C    sing N N 56  
ALO CA  HA   sing N N 57  
ALO CB  CG2  sing N N 58  
ALO CB  OG1  sing N N 59  
ALO CB  HB   sing N N 60  
ALO CG2 HG21 sing N N 61  
ALO CG2 HG22 sing N N 62  
ALO CG2 HG23 sing N N 63  
ALO OG1 HG1  sing N N 64  
ALO C   O    doub N N 65  
ALO C   OXT  sing N N 66  
ALO OXT HXT  sing N N 67  
ARG N   CA   sing N N 68  
ARG N   H    sing N N 69  
ARG N   H2   sing N N 70  
ARG CA  C    sing N N 71  
ARG CA  CB   sing N N 72  
ARG CA  HA   sing N N 73  
ARG C   O    doub N N 74  
ARG C   OXT  sing N N 75  
ARG CB  CG   sing N N 76  
ARG CB  HB2  sing N N 77  
ARG CB  HB3  sing N N 78  
ARG CG  CD   sing N N 79  
ARG CG  HG2  sing N N 80  
ARG CG  HG3  sing N N 81  
ARG CD  NE   sing N N 82  
ARG CD  HD2  sing N N 83  
ARG CD  HD3  sing N N 84  
ARG NE  CZ   sing N N 85  
ARG NE  HE   sing N N 86  
ARG CZ  NH1  sing N N 87  
ARG CZ  NH2  doub N N 88  
ARG NH1 HH11 sing N N 89  
ARG NH1 HH12 sing N N 90  
ARG NH2 HH21 sing N N 91  
ARG NH2 HH22 sing N N 92  
ARG OXT HXT  sing N N 93  
ASN N   CA   sing N N 94  
ASN N   H    sing N N 95  
ASN N   H2   sing N N 96  
ASN CA  C    sing N N 97  
ASN CA  CB   sing N N 98  
ASN CA  HA   sing N N 99  
ASN C   O    doub N N 100 
ASN C   OXT  sing N N 101 
ASN CB  CG   sing N N 102 
ASN CB  HB2  sing N N 103 
ASN CB  HB3  sing N N 104 
ASN CG  OD1  doub N N 105 
ASN CG  ND2  sing N N 106 
ASN ND2 HD21 sing N N 107 
ASN ND2 HD22 sing N N 108 
ASN OXT HXT  sing N N 109 
ASP N   CA   sing N N 110 
ASP N   H    sing N N 111 
ASP N   H2   sing N N 112 
ASP CA  C    sing N N 113 
ASP CA  CB   sing N N 114 
ASP CA  HA   sing N N 115 
ASP C   O    doub N N 116 
ASP C   OXT  sing N N 117 
ASP CB  CG   sing N N 118 
ASP CB  HB2  sing N N 119 
ASP CB  HB3  sing N N 120 
ASP CG  OD1  doub N N 121 
ASP CG  OD2  sing N N 122 
ASP OD2 HD2  sing N N 123 
ASP OXT HXT  sing N N 124 
GLN N   CA   sing N N 125 
GLN N   H    sing N N 126 
GLN N   H2   sing N N 127 
GLN CA  C    sing N N 128 
GLN CA  CB   sing N N 129 
GLN CA  HA   sing N N 130 
GLN C   O    doub N N 131 
GLN C   OXT  sing N N 132 
GLN CB  CG   sing N N 133 
GLN CB  HB2  sing N N 134 
GLN CB  HB3  sing N N 135 
GLN CG  CD   sing N N 136 
GLN CG  HG2  sing N N 137 
GLN CG  HG3  sing N N 138 
GLN CD  OE1  doub N N 139 
GLN CD  NE2  sing N N 140 
GLN NE2 HE21 sing N N 141 
GLN NE2 HE22 sing N N 142 
GLN OXT HXT  sing N N 143 
GLU N   CA   sing N N 144 
GLU N   H    sing N N 145 
GLU N   H2   sing N N 146 
GLU CA  C    sing N N 147 
GLU CA  CB   sing N N 148 
GLU CA  HA   sing N N 149 
GLU C   O    doub N N 150 
GLU C   OXT  sing N N 151 
GLU CB  CG   sing N N 152 
GLU CB  HB2  sing N N 153 
GLU CB  HB3  sing N N 154 
GLU CG  CD   sing N N 155 
GLU CG  HG2  sing N N 156 
GLU CG  HG3  sing N N 157 
GLU CD  OE1  doub N N 158 
GLU CD  OE2  sing N N 159 
GLU OE2 HE2  sing N N 160 
GLU OXT HXT  sing N N 161 
GLY N   CA   sing N N 162 
GLY N   H    sing N N 163 
GLY N   H2   sing N N 164 
GLY CA  C    sing N N 165 
GLY CA  HA2  sing N N 166 
GLY CA  HA3  sing N N 167 
GLY C   O    doub N N 168 
GLY C   OXT  sing N N 169 
GLY OXT HXT  sing N N 170 
HIS N   CA   sing N N 171 
HIS N   H    sing N N 172 
HIS N   H2   sing N N 173 
HIS CA  C    sing N N 174 
HIS CA  CB   sing N N 175 
HIS CA  HA   sing N N 176 
HIS C   O    doub N N 177 
HIS C   OXT  sing N N 178 
HIS CB  CG   sing N N 179 
HIS CB  HB2  sing N N 180 
HIS CB  HB3  sing N N 181 
HIS CG  ND1  sing Y N 182 
HIS CG  CD2  doub Y N 183 
HIS ND1 CE1  doub Y N 184 
HIS ND1 HD1  sing N N 185 
HIS CD2 NE2  sing Y N 186 
HIS CD2 HD2  sing N N 187 
HIS CE1 NE2  sing Y N 188 
HIS CE1 HE1  sing N N 189 
HIS NE2 HE2  sing N N 190 
HIS OXT HXT  sing N N 191 
HOH O   H1   sing N N 192 
HOH O   H2   sing N N 193 
IIL N   CA   sing N N 194 
IIL N   H    sing N N 195 
IIL N   H2   sing N N 196 
IIL CA  C    sing N N 197 
IIL CA  CB   sing N N 198 
IIL CA  HA   sing N N 199 
IIL C   O    doub N N 200 
IIL C   OXT  sing N N 201 
IIL CB  CG2  sing N N 202 
IIL CB  CG1  sing N N 203 
IIL CB  HB   sing N N 204 
IIL CG2 HG21 sing N N 205 
IIL CG2 HG22 sing N N 206 
IIL CG2 HG23 sing N N 207 
IIL CG1 CD1  sing N N 208 
IIL CG1 HG12 sing N N 209 
IIL CG1 HG13 sing N N 210 
IIL CD1 HD11 sing N N 211 
IIL CD1 HD12 sing N N 212 
IIL CD1 HD13 sing N N 213 
IIL OXT HXT  sing N N 214 
ILE N   CA   sing N N 215 
ILE N   H    sing N N 216 
ILE N   H2   sing N N 217 
ILE CA  C    sing N N 218 
ILE CA  CB   sing N N 219 
ILE CA  HA   sing N N 220 
ILE C   O    doub N N 221 
ILE C   OXT  sing N N 222 
ILE CB  CG1  sing N N 223 
ILE CB  CG2  sing N N 224 
ILE CB  HB   sing N N 225 
ILE CG1 CD1  sing N N 226 
ILE CG1 HG12 sing N N 227 
ILE CG1 HG13 sing N N 228 
ILE CG2 HG21 sing N N 229 
ILE CG2 HG22 sing N N 230 
ILE CG2 HG23 sing N N 231 
ILE CD1 HD11 sing N N 232 
ILE CD1 HD12 sing N N 233 
ILE CD1 HD13 sing N N 234 
ILE OXT HXT  sing N N 235 
LEU N   CA   sing N N 236 
LEU N   H    sing N N 237 
LEU N   H2   sing N N 238 
LEU CA  C    sing N N 239 
LEU CA  CB   sing N N 240 
LEU CA  HA   sing N N 241 
LEU C   O    doub N N 242 
LEU C   OXT  sing N N 243 
LEU CB  CG   sing N N 244 
LEU CB  HB2  sing N N 245 
LEU CB  HB3  sing N N 246 
LEU CG  CD1  sing N N 247 
LEU CG  CD2  sing N N 248 
LEU CG  HG   sing N N 249 
LEU CD1 HD11 sing N N 250 
LEU CD1 HD12 sing N N 251 
LEU CD1 HD13 sing N N 252 
LEU CD2 HD21 sing N N 253 
LEU CD2 HD22 sing N N 254 
LEU CD2 HD23 sing N N 255 
LEU OXT HXT  sing N N 256 
LYS N   CA   sing N N 257 
LYS N   H    sing N N 258 
LYS N   H2   sing N N 259 
LYS CA  C    sing N N 260 
LYS CA  CB   sing N N 261 
LYS CA  HA   sing N N 262 
LYS C   O    doub N N 263 
LYS C   OXT  sing N N 264 
LYS CB  CG   sing N N 265 
LYS CB  HB2  sing N N 266 
LYS CB  HB3  sing N N 267 
LYS CG  CD   sing N N 268 
LYS CG  HG2  sing N N 269 
LYS CG  HG3  sing N N 270 
LYS CD  CE   sing N N 271 
LYS CD  HD2  sing N N 272 
LYS CD  HD3  sing N N 273 
LYS CE  NZ   sing N N 274 
LYS CE  HE2  sing N N 275 
LYS CE  HE3  sing N N 276 
LYS NZ  HZ1  sing N N 277 
LYS NZ  HZ2  sing N N 278 
LYS NZ  HZ3  sing N N 279 
LYS OXT HXT  sing N N 280 
MET N   CA   sing N N 281 
MET N   H    sing N N 282 
MET N   H2   sing N N 283 
MET CA  C    sing N N 284 
MET CA  CB   sing N N 285 
MET CA  HA   sing N N 286 
MET C   O    doub N N 287 
MET C   OXT  sing N N 288 
MET CB  CG   sing N N 289 
MET CB  HB2  sing N N 290 
MET CB  HB3  sing N N 291 
MET CG  SD   sing N N 292 
MET CG  HG2  sing N N 293 
MET CG  HG3  sing N N 294 
MET SD  CE   sing N N 295 
MET CE  HE1  sing N N 296 
MET CE  HE2  sing N N 297 
MET CE  HE3  sing N N 298 
MET OXT HXT  sing N N 299 
MLE N   CN   sing N N 300 
MLE N   CA   sing N N 301 
MLE N   H    sing N N 302 
MLE CN  HN1  sing N N 303 
MLE CN  HN2  sing N N 304 
MLE CN  HN3  sing N N 305 
MLE CA  CB   sing N N 306 
MLE CA  C    sing N N 307 
MLE CA  HA   sing N N 308 
MLE CB  CG   sing N N 309 
MLE CB  HB2  sing N N 310 
MLE CB  HB3  sing N N 311 
MLE CG  CD1  sing N N 312 
MLE CG  CD2  sing N N 313 
MLE CG  HG   sing N N 314 
MLE CD1 HD11 sing N N 315 
MLE CD1 HD12 sing N N 316 
MLE CD1 HD13 sing N N 317 
MLE CD2 HD21 sing N N 318 
MLE CD2 HD22 sing N N 319 
MLE CD2 HD23 sing N N 320 
MLE C   O    doub N N 321 
MLE C   OXT  sing N N 322 
MLE OXT HXT  sing N N 323 
OLC C18 C17  sing N N 324 
OLC C10 C9   doub N N 325 
OLC C10 C11  sing N N 326 
OLC C9  C8   sing N N 327 
OLC C17 C16  sing N Z 328 
OLC C11 C12  sing N N 329 
OLC C8  C7   sing N N 330 
OLC C24 C22  sing N N 331 
OLC C24 O25  sing N N 332 
OLC C16 C15  sing N N 333 
OLC C12 C13  sing N N 334 
OLC C7  C6   sing N N 335 
OLC C15 C14  sing N N 336 
OLC C13 C14  sing N N 337 
OLC C6  C5   sing N N 338 
OLC C5  C4   sing N N 339 
OLC C4  C3   sing N N 340 
OLC C3  C2   sing N N 341 
OLC C2  C1   sing N N 342 
OLC C21 C22  sing N N 343 
OLC C21 O20  sing N N 344 
OLC C1  O19  doub N N 345 
OLC C1  O20  sing N N 346 
OLC C22 O23  sing N N 347 
OLC C18 H18  sing N N 348 
OLC C18 H18A sing N N 349 
OLC C18 H18B sing N N 350 
OLC C10 H10  sing N N 351 
OLC C9  H9   sing N N 352 
OLC C17 H17  sing N N 353 
OLC C17 H17A sing N N 354 
OLC C11 H11  sing N N 355 
OLC C11 H11A sing N N 356 
OLC C8  H8   sing N N 357 
OLC C8  H8A  sing N N 358 
OLC C24 H24  sing N N 359 
OLC C24 H24A sing N N 360 
OLC C16 H16  sing N N 361 
OLC C16 H16A sing N N 362 
OLC C12 H12  sing N N 363 
OLC C12 H12A sing N N 364 
OLC C7  H7   sing N N 365 
OLC C7  H7A  sing N N 366 
OLC C15 H15  sing N N 367 
OLC C15 H15A sing N N 368 
OLC C13 H13  sing N N 369 
OLC C13 H13A sing N N 370 
OLC C6  H6   sing N N 371 
OLC C6  H6A  sing N N 372 
OLC C14 H14  sing N N 373 
OLC C14 H14A sing N N 374 
OLC C5  H5   sing N N 375 
OLC C5  H5A  sing N N 376 
OLC C4  H4   sing N N 377 
OLC C4  H4A  sing N N 378 
OLC C3  H3   sing N N 379 
OLC C3  H3A  sing N N 380 
OLC C2  H2   sing N N 381 
OLC C2  H2A  sing N N 382 
OLC C21 H21  sing N N 383 
OLC C21 H21A sing N N 384 
OLC C22 H22  sing N N 385 
OLC O25 HO25 sing N N 386 
OLC O23 HO23 sing N N 387 
PHE N   CA   sing N N 388 
PHE N   H    sing N N 389 
PHE N   H2   sing N N 390 
PHE CA  C    sing N N 391 
PHE CA  CB   sing N N 392 
PHE CA  HA   sing N N 393 
PHE C   O    doub N N 394 
PHE C   OXT  sing N N 395 
PHE CB  CG   sing N N 396 
PHE CB  HB2  sing N N 397 
PHE CB  HB3  sing N N 398 
PHE CG  CD1  doub Y N 399 
PHE CG  CD2  sing Y N 400 
PHE CD1 CE1  sing Y N 401 
PHE CD1 HD1  sing N N 402 
PHE CD2 CE2  doub Y N 403 
PHE CD2 HD2  sing N N 404 
PHE CE1 CZ   doub Y N 405 
PHE CE1 HE1  sing N N 406 
PHE CE2 CZ   sing Y N 407 
PHE CE2 HE2  sing N N 408 
PHE CZ  HZ   sing N N 409 
PHE OXT HXT  sing N N 410 
PRO N   CA   sing N N 411 
PRO N   CD   sing N N 412 
PRO N   H    sing N N 413 
PRO CA  C    sing N N 414 
PRO CA  CB   sing N N 415 
PRO CA  HA   sing N N 416 
PRO C   O    doub N N 417 
PRO C   OXT  sing N N 418 
PRO CB  CG   sing N N 419 
PRO CB  HB2  sing N N 420 
PRO CB  HB3  sing N N 421 
PRO CG  CD   sing N N 422 
PRO CG  HG2  sing N N 423 
PRO CG  HG3  sing N N 424 
PRO CD  HD2  sing N N 425 
PRO CD  HD3  sing N N 426 
PRO OXT HXT  sing N N 427 
SER N   CA   sing N N 428 
SER N   H    sing N N 429 
SER N   H2   sing N N 430 
SER CA  C    sing N N 431 
SER CA  CB   sing N N 432 
SER CA  HA   sing N N 433 
SER C   O    doub N N 434 
SER C   OXT  sing N N 435 
SER CB  OG   sing N N 436 
SER CB  HB2  sing N N 437 
SER CB  HB3  sing N N 438 
SER OG  HG   sing N N 439 
SER OXT HXT  sing N N 440 
THR N   CA   sing N N 441 
THR N   H    sing N N 442 
THR N   H2   sing N N 443 
THR CA  C    sing N N 444 
THR CA  CB   sing N N 445 
THR CA  HA   sing N N 446 
THR C   O    doub N N 447 
THR C   OXT  sing N N 448 
THR CB  OG1  sing N N 449 
THR CB  CG2  sing N N 450 
THR CB  HB   sing N N 451 
THR OG1 HG1  sing N N 452 
THR CG2 HG21 sing N N 453 
THR CG2 HG22 sing N N 454 
THR CG2 HG23 sing N N 455 
THR OXT HXT  sing N N 456 
TRP N   CA   sing N N 457 
TRP N   H    sing N N 458 
TRP N   H2   sing N N 459 
TRP CA  C    sing N N 460 
TRP CA  CB   sing N N 461 
TRP CA  HA   sing N N 462 
TRP C   O    doub N N 463 
TRP C   OXT  sing N N 464 
TRP CB  CG   sing N N 465 
TRP CB  HB2  sing N N 466 
TRP CB  HB3  sing N N 467 
TRP CG  CD1  doub Y N 468 
TRP CG  CD2  sing Y N 469 
TRP CD1 NE1  sing Y N 470 
TRP CD1 HD1  sing N N 471 
TRP CD2 CE2  doub Y N 472 
TRP CD2 CE3  sing Y N 473 
TRP NE1 CE2  sing Y N 474 
TRP NE1 HE1  sing N N 475 
TRP CE2 CZ2  sing Y N 476 
TRP CE3 CZ3  doub Y N 477 
TRP CE3 HE3  sing N N 478 
TRP CZ2 CH2  doub Y N 479 
TRP CZ2 HZ2  sing N N 480 
TRP CZ3 CH2  sing Y N 481 
TRP CZ3 HZ3  sing N N 482 
TRP CH2 HH2  sing N N 483 
TRP OXT HXT  sing N N 484 
TYR N   CA   sing N N 485 
TYR N   H    sing N N 486 
TYR N   H2   sing N N 487 
TYR CA  C    sing N N 488 
TYR CA  CB   sing N N 489 
TYR CA  HA   sing N N 490 
TYR C   O    doub N N 491 
TYR C   OXT  sing N N 492 
TYR CB  CG   sing N N 493 
TYR CB  HB2  sing N N 494 
TYR CB  HB3  sing N N 495 
TYR CG  CD1  doub Y N 496 
TYR CG  CD2  sing Y N 497 
TYR CD1 CE1  sing Y N 498 
TYR CD1 HD1  sing N N 499 
TYR CD2 CE2  doub Y N 500 
TYR CD2 HD2  sing N N 501 
TYR CE1 CZ   doub Y N 502 
TYR CE1 HE1  sing N N 503 
TYR CE2 CZ   sing Y N 504 
TYR CE2 HE2  sing N N 505 
TYR CZ  OH   sing N N 506 
TYR OH  HH   sing N N 507 
TYR OXT HXT  sing N N 508 
VAL N   CA   sing N N 509 
VAL N   H    sing N N 510 
VAL N   H2   sing N N 511 
VAL CA  C    sing N N 512 
VAL CA  CB   sing N N 513 
VAL CA  HA   sing N N 514 
VAL C   O    doub N N 515 
VAL C   OXT  sing N N 516 
VAL CB  CG1  sing N N 517 
VAL CB  CG2  sing N N 518 
VAL CB  HB   sing N N 519 
VAL CG1 HG11 sing N N 520 
VAL CG1 HG12 sing N N 521 
VAL CG1 HG13 sing N N 522 
VAL CG2 HG21 sing N N 523 
VAL CG2 HG22 sing N N 524 
VAL CG2 HG23 sing N N 525 
VAL OXT HXT  sing N N 526 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Science Foundation Ireland'        Ireland     '16/IA/4435 and 22/FFP-A/10278' 1 
'Swiss National Science Foundation' Switzerland P2BSP3_15254                    2 
# 
_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   5DIR 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EMZ 
_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]   0.008773 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001161 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009426 
_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]   0.011740 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . PRO A  1 2   ? -31.594 -33.607 16.667  1.00 54.89 ? 2   PRO A N   1 
ATOM   2    C CA  . PRO A  1 2   ? -30.716 -32.542 16.173  1.00 52.24 ? 2   PRO A CA  1 
ATOM   3    C C   . PRO A  1 2   ? -31.036 -31.194 16.811  1.00 49.16 ? 2   PRO A C   1 
ATOM   4    O O   . PRO A  1 2   ? -31.996 -31.083 17.575  1.00 48.63 ? 2   PRO A O   1 
ATOM   5    C CB  . PRO A  1 2   ? -31.008 -32.525 14.671  1.00 53.17 ? 2   PRO A CB  1 
ATOM   6    C CG  . PRO A  1 2   ? -32.434 -32.938 14.582  1.00 54.87 ? 2   PRO A CG  1 
ATOM   7    C CD  . PRO A  1 2   ? -32.659 -33.932 15.701  1.00 56.29 ? 2   PRO A CD  1 
ATOM   8    N N   . ASP A  1 3   ? -30.231 -30.177 16.499  1.00 47.03 ? 3   ASP A N   1 
ATOM   9    C CA  . ASP A  1 3   ? -30.440 -28.866 17.102  1.00 44.52 ? 3   ASP A CA  1 
ATOM   10   C C   . ASP A  1 3   ? -31.703 -28.195 16.591  1.00 44.87 ? 3   ASP A C   1 
ATOM   11   O O   . ASP A  1 3   ? -32.291 -27.374 17.301  1.00 45.28 ? 3   ASP A O   1 
ATOM   12   C CB  . ASP A  1 3   ? -29.240 -27.962 16.840  1.00 43.83 ? 3   ASP A CB  1 
ATOM   13   C CG  . ASP A  1 3   ? -28.119 -28.192 17.823  1.00 44.17 ? 3   ASP A CG  1 
ATOM   14   O OD1 . ASP A  1 3   ? -28.327 -28.952 18.794  1.00 44.83 ? 3   ASP A OD1 1 
ATOM   15   O OD2 . ASP A  1 3   ? -27.030 -27.614 17.623  1.00 43.62 ? 3   ASP A OD2 1 
ATOM   16   N N   . VAL A  1 4   ? -32.124 -28.514 15.368  1.00 45.64 ? 4   VAL A N   1 
ATOM   17   C CA  . VAL A  1 4   ? -33.231 -27.786 14.754  1.00 46.54 ? 4   VAL A CA  1 
ATOM   18   C C   . VAL A  1 4   ? -34.522 -27.980 15.547  1.00 46.28 ? 4   VAL A C   1 
ATOM   19   O O   . VAL A  1 4   ? -35.333 -27.052 15.674  1.00 44.28 ? 4   VAL A O   1 
ATOM   20   C CB  . VAL A  1 4   ? -33.390 -28.204 13.280  1.00 46.82 ? 4   VAL A CB  1 
ATOM   21   C CG1 . VAL A  1 4   ? -33.452 -29.722 13.152  1.00 47.88 ? 4   VAL A CG1 1 
ATOM   22   C CG2 . VAL A  1 4   ? -34.626 -27.549 12.672  1.00 45.28 ? 4   VAL A CG2 1 
ATOM   23   N N   . ASP A  1 5   ? -34.734 -29.178 16.092  1.00 47.10 ? 5   ASP A N   1 
ATOM   24   C CA  . ASP A  1 5   ? -35.971 -29.481 16.804  1.00 46.66 ? 5   ASP A CA  1 
ATOM   25   C C   . ASP A  1 5   ? -35.919 -29.156 18.291  1.00 44.20 ? 5   ASP A C   1 
ATOM   26   O O   . ASP A  1 5   ? -36.977 -28.997 18.911  1.00 42.63 ? 5   ASP A O   1 
ATOM   27   C CB  . ASP A  1 5   ? -36.333 -30.961 16.633  1.00 48.71 ? 5   ASP A CB  1 
ATOM   28   C CG  . ASP A  1 5   ? -36.638 -31.326 15.191  1.00 50.75 ? 5   ASP A CG  1 
ATOM   29   O OD1 . ASP A  1 5   ? -35.684 -31.585 14.424  1.00 50.78 ? 5   ASP A OD1 1 
ATOM   30   O OD2 . ASP A  1 5   ? -37.836 -31.346 14.827  1.00 51.08 ? 5   ASP A OD2 1 
ATOM   31   N N   . ARG A  1 6   ? -34.729 -29.059 18.883  1.00 44.09 ? 6   ARG A N   1 
ATOM   32   C CA  . ARG A  1 6   ? -34.645 -28.828 20.320  1.00 43.11 ? 6   ARG A CA  1 
ATOM   33   C C   . ARG A  1 6   ? -34.938 -27.385 20.708  1.00 41.94 ? 6   ARG A C   1 
ATOM   34   O O   . ARG A  1 6   ? -35.181 -27.113 21.889  1.00 41.83 ? 6   ARG A O   1 
ATOM   35   C CB  . ARG A  1 6   ? -33.268 -29.243 20.843  1.00 43.18 ? 6   ARG A CB  1 
ATOM   36   C CG  . ARG A  1 6   ? -32.125 -28.383 20.355  1.00 43.06 ? 6   ARG A CG  1 
ATOM   37   C CD  . ARG A  1 6   ? -30.809 -28.881 20.917  1.00 44.38 ? 6   ARG A CD  1 
ATOM   38   N NE  . ARG A  1 6   ? -30.833 -28.945 22.373  1.00 46.52 ? 6   ARG A NE  1 
ATOM   39   C CZ  . ARG A  1 6   ? -30.499 -27.940 23.172  1.00 49.51 ? 6   ARG A CZ  1 
ATOM   40   N NH1 . ARG A  1 6   ? -30.114 -26.770 22.688  1.00 47.99 ? 6   ARG A NH1 1 
ATOM   41   N NH2 . ARG A  1 6   ? -30.552 -28.114 24.490  1.00 51.76 ? 6   ARG A NH2 1 
ATOM   42   N N   . PHE A  1 7   ? -34.920 -26.459 19.748  1.00 41.49 ? 7   PHE A N   1 
ATOM   43   C CA  . PHE A  1 7   ? -35.354 -25.092 19.995  1.00 38.99 ? 7   PHE A CA  1 
ATOM   44   C C   . PHE A  1 7   ? -36.807 -24.860 19.616  1.00 37.95 ? 7   PHE A C   1 
ATOM   45   O O   . PHE A  1 7   ? -37.414 -23.905 20.113  1.00 36.69 ? 7   PHE A O   1 
ATOM   46   C CB  . PHE A  1 7   ? -34.470 -24.099 19.237  1.00 39.47 ? 7   PHE A CB  1 
ATOM   47   C CG  . PHE A  1 7   ? -33.033 -24.128 19.667  1.00 41.43 ? 7   PHE A CG  1 
ATOM   48   C CD1 . PHE A  1 7   ? -32.631 -23.503 20.838  1.00 41.93 ? 7   PHE A CD1 1 
ATOM   49   C CD2 . PHE A  1 7   ? -32.079 -24.774 18.895  1.00 41.65 ? 7   PHE A CD2 1 
ATOM   50   C CE1 . PHE A  1 7   ? -31.304 -23.527 21.231  1.00 41.90 ? 7   PHE A CE1 1 
ATOM   51   C CE2 . PHE A  1 7   ? -30.753 -24.800 19.285  1.00 41.39 ? 7   PHE A CE2 1 
ATOM   52   C CZ  . PHE A  1 7   ? -30.367 -24.177 20.452  1.00 41.22 ? 7   PHE A CZ  1 
ATOM   53   N N   . GLY A  1 8   ? -37.370 -25.704 18.756  1.00 39.10 ? 8   GLY A N   1 
ATOM   54   C CA  . GLY A  1 8   ? -38.777 -25.606 18.400  1.00 38.94 ? 8   GLY A CA  1 
ATOM   55   C C   . GLY A  1 8   ? -38.987 -24.669 17.230  1.00 38.39 ? 8   GLY A C   1 
ATOM   56   O O   . GLY A  1 8   ? -38.331 -24.803 16.196  1.00 38.94 ? 8   GLY A O   1 
ATOM   57   N N   . ARG A  1 9   ? -39.907 -23.721 17.393  1.00 37.53 ? 9   ARG A N   1 
ATOM   58   C CA  . ARG A  1 9   ? -40.155 -22.700 16.385  1.00 37.13 ? 9   ARG A CA  1 
ATOM   59   C C   . ARG A  1 9   ? -39.450 -21.393 16.718  1.00 35.64 ? 9   ARG A C   1 
ATOM   60   O O   . ARG A  1 9   ? -39.713 -20.370 16.078  1.00 34.98 ? 9   ARG A O   1 
ATOM   61   C CB  . ARG A  1 9   ? -41.659 -22.464 16.218  1.00 37.60 ? 9   ARG A CB  1 
ATOM   62   C CG  . ARG A  1 9   ? -42.496 -23.733 16.222  1.00 40.24 ? 9   ARG A CG  1 
ATOM   63   C CD  . ARG A  1 9   ? -41.930 -24.799 15.283  1.00 40.44 ? 9   ARG A CD  1 
ATOM   64   N NE  . ARG A  1 9   ? -42.664 -26.056 15.381  1.00 42.35 ? 9   ARG A NE  1 
ATOM   65   C CZ  . ARG A  1 9   ? -42.559 -26.913 16.389  1.00 43.28 ? 9   ARG A CZ  1 
ATOM   66   N NH1 . ARG A  1 9   ? -41.765 -26.674 17.422  1.00 42.43 ? 9   ARG A NH1 1 
ATOM   67   N NH2 . ARG A  1 9   ? -43.269 -28.039 16.361  1.00 44.45 ? 9   ARG A NH2 1 
ATOM   68   N N   . LEU A  1 10  ? -38.565 -21.410 17.710  1.00 35.44 ? 10  LEU A N   1 
ATOM   69   C CA  . LEU A  1 10  ? -37.783 -20.257 18.137  1.00 34.85 ? 10  LEU A CA  1 
ATOM   70   C C   . LEU A  1 10  ? -36.762 -19.790 17.097  1.00 34.50 ? 10  LEU A C   1 
ATOM   71   O O   . LEU A  1 10  ? -36.555 -18.577 16.969  1.00 34.24 ? 10  LEU A O   1 
ATOM   72   C CB  . LEU A  1 10  ? -37.081 -20.562 19.464  1.00 35.83 ? 10  LEU A CB  1 
ATOM   73   C CG  . LEU A  1 10  ? -37.729 -19.954 20.712  1.00 35.43 ? 10  LEU A CG  1 
ATOM   74   C CD1 . LEU A  1 10  ? -39.126 -20.525 20.921  1.00 37.02 ? 10  LEU A CD1 1 
ATOM   75   C CD2 . LEU A  1 10  ? -36.859 -20.168 21.947  1.00 34.03 ? 10  LEU A CD2 1 
ATOM   76   N N   . PRO A  1 11  ? -36.091 -20.680 16.350  1.00 34.94 ? 11  PRO A N   1 
ATOM   77   C CA  . PRO A  1 11  ? -35.162 -20.196 15.309  1.00 34.48 ? 11  PRO A CA  1 
ATOM   78   C C   . PRO A  1 11  ? -35.800 -19.261 14.295  1.00 33.41 ? 11  PRO A C   1 
ATOM   79   O O   . PRO A  1 11  ? -35.066 -18.588 13.560  1.00 32.92 ? 11  PRO A O   1 
ATOM   80   C CB  . PRO A  1 11  ? -34.677 -21.487 14.640  1.00 35.02 ? 11  PRO A CB  1 
ATOM   81   C CG  . PRO A  1 11  ? -34.753 -22.497 15.707  1.00 36.79 ? 11  PRO A CG  1 
ATOM   82   C CD  . PRO A  1 11  ? -35.959 -22.139 16.536  1.00 36.47 ? 11  PRO A CD  1 
ATOM   83   N N   . TRP A  1 12  ? -37.132 -19.200 14.226  1.00 33.92 ? 12  TRP A N   1 
ATOM   84   C CA  . TRP A  1 12  ? -37.795 -18.189 13.410  1.00 33.63 ? 12  TRP A CA  1 
ATOM   85   C C   . TRP A  1 12  ? -37.568 -16.778 13.935  1.00 32.20 ? 12  TRP A C   1 
ATOM   86   O O   . TRP A  1 12  ? -37.773 -15.813 13.191  1.00 31.15 ? 12  TRP A O   1 
ATOM   87   C CB  . TRP A  1 12  ? -39.294 -18.467 13.337  1.00 33.85 ? 12  TRP A CB  1 
ATOM   88   C CG  . TRP A  1 12  ? -39.640 -19.658 12.520  1.00 34.15 ? 12  TRP A CG  1 
ATOM   89   C CD1 . TRP A  1 12  ? -39.955 -20.905 12.977  1.00 34.76 ? 12  TRP A CD1 1 
ATOM   90   C CD2 . TRP A  1 12  ? -39.709 -19.723 11.092  1.00 34.60 ? 12  TRP A CD2 1 
ATOM   91   N NE1 . TRP A  1 12  ? -40.221 -21.742 11.920  1.00 35.86 ? 12  TRP A NE1 1 
ATOM   92   C CE2 . TRP A  1 12  ? -40.072 -21.042 10.751  1.00 36.08 ? 12  TRP A CE2 1 
ATOM   93   C CE3 . TRP A  1 12  ? -39.498 -18.794 10.067  1.00 33.99 ? 12  TRP A CE3 1 
ATOM   94   C CZ2 . TRP A  1 12  ? -40.234 -21.454 9.428   1.00 36.51 ? 12  TRP A CZ2 1 
ATOM   95   C CZ3 . TRP A  1 12  ? -39.657 -19.202 8.756   1.00 34.34 ? 12  TRP A CZ3 1 
ATOM   96   C CH2 . TRP A  1 12  ? -40.022 -20.522 8.447   1.00 35.87 ? 12  TRP A CH2 1 
ATOM   97   N N   . LEU A  1 13  ? -37.161 -16.635 15.199  1.00 33.09 ? 13  LEU A N   1 
ATOM   98   C CA  . LEU A  1 13  ? -36.919 -15.311 15.756  1.00 31.54 ? 13  LEU A CA  1 
ATOM   99   C C   . LEU A  1 13  ? -35.784 -14.592 15.051  1.00 30.90 ? 13  LEU A C   1 
ATOM   100  O O   . LEU A  1 13  ? -35.691 -13.366 15.147  1.00 30.39 ? 13  LEU A O   1 
ATOM   101  C CB  . LEU A  1 13  ? -36.603 -15.402 17.247  1.00 31.96 ? 13  LEU A CB  1 
ATOM   102  C CG  . LEU A  1 13  ? -37.720 -15.893 18.164  1.00 32.28 ? 13  LEU A CG  1 
ATOM   103  C CD1 . LEU A  1 13  ? -37.213 -15.967 19.593  1.00 33.40 ? 13  LEU A CD1 1 
ATOM   104  C CD2 . LEU A  1 13  ? -38.942 -14.991 18.063  1.00 30.78 ? 13  LEU A CD2 1 
ATOM   105  N N   . TRP A  1 14  ? -34.909 -15.322 14.361  1.00 31.49 ? 14  TRP A N   1 
ATOM   106  C CA  . TRP A  1 14  ? -33.798 -14.667 13.686  1.00 30.81 ? 14  TRP A CA  1 
ATOM   107  C C   . TRP A  1 14  ? -34.280 -13.767 12.557  1.00 30.42 ? 14  TRP A C   1 
ATOM   108  O O   . TRP A  1 14  ? -33.622 -12.770 12.236  1.00 30.47 ? 14  TRP A O   1 
ATOM   109  C CB  . TRP A  1 14  ? -32.806 -15.713 13.181  1.00 31.54 ? 14  TRP A CB  1 
ATOM   110  C CG  . TRP A  1 14  ? -31.980 -16.291 14.286  1.00 32.18 ? 14  TRP A CG  1 
ATOM   111  C CD1 . TRP A  1 14  ? -31.983 -17.581 14.729  1.00 33.21 ? 14  TRP A CD1 1 
ATOM   112  C CD2 . TRP A  1 14  ? -31.041 -15.587 15.106  1.00 32.49 ? 14  TRP A CD2 1 
ATOM   113  N NE1 . TRP A  1 14  ? -31.095 -17.726 15.768  1.00 33.94 ? 14  TRP A NE1 1 
ATOM   114  C CE2 . TRP A  1 14  ? -30.504 -16.515 16.019  1.00 33.53 ? 14  TRP A CE2 1 
ATOM   115  C CE3 . TRP A  1 14  ? -30.597 -14.262 15.151  1.00 33.15 ? 14  TRP A CE3 1 
ATOM   116  C CZ2 . TRP A  1 14  ? -29.547 -16.160 16.968  1.00 33.77 ? 14  TRP A CZ2 1 
ATOM   117  C CZ3 . TRP A  1 14  ? -29.646 -13.912 16.093  1.00 33.96 ? 14  TRP A CZ3 1 
ATOM   118  C CH2 . TRP A  1 14  ? -29.131 -14.858 16.988  1.00 33.88 ? 14  TRP A CH2 1 
ATOM   119  N N   . ILE A  1 15  ? -35.427 -14.087 11.955  1.00 30.00 ? 15  ILE A N   1 
ATOM   120  C CA  . ILE A  1 15  ? -36.043 -13.161 11.012  1.00 30.65 ? 15  ILE A CA  1 
ATOM   121  C C   . ILE A  1 15  ? -36.518 -11.907 11.736  1.00 29.70 ? 15  ILE A C   1 
ATOM   122  O O   . ILE A  1 15  ? -36.389 -10.789 11.223  1.00 28.55 ? 15  ILE A O   1 
ATOM   123  C CB  . ILE A  1 15  ? -37.190 -13.857 10.258  1.00 30.76 ? 15  ILE A CB  1 
ATOM   124  C CG1 . ILE A  1 15  ? -36.674 -15.126 9.575   1.00 32.18 ? 15  ILE A CG1 1 
ATOM   125  C CG2 . ILE A  1 15  ? -37.819 -12.911 9.242   1.00 31.00 ? 15  ILE A CG2 1 
ATOM   126  C CD1 . ILE A  1 15  ? -37.766 -16.009 9.027   1.00 32.98 ? 15  ILE A CD1 1 
ATOM   127  N N   . THR A  1 16  ? -37.081 -12.072 12.936  1.00 29.53 ? 16  THR A N   1 
ATOM   128  C CA  . THR A  1 16  ? -37.413 -10.916 13.763  1.00 28.55 ? 16  THR A CA  1 
ATOM   129  C C   . THR A  1 16  ? -36.160 -10.126 14.115  1.00 29.54 ? 16  THR A C   1 
ATOM   130  O O   . THR A  1 16  ? -36.158 -8.890  14.056  1.00 28.25 ? 16  THR A O   1 
ATOM   131  C CB  . THR A  1 16  ? -38.139 -11.369 15.033  1.00 27.92 ? 16  THR A CB  1 
ATOM   132  O OG1 . THR A  1 16  ? -39.460 -11.814 14.705  1.00 28.50 ? 16  THR A OG1 1 
ATOM   133  C CG2 . THR A  1 16  ? -38.215 -10.244 16.051  1.00 26.50 ? 16  THR A CG2 1 
ATOM   134  N N   . VAL A  1 17  ? -35.081 -10.825 14.478  1.00 28.97 ? 17  VAL A N   1 
ATOM   135  C CA  . VAL A  1 17  ? -33.827 -10.153 14.807  1.00 27.87 ? 17  VAL A CA  1 
ATOM   136  C C   . VAL A  1 17  ? -33.278 -9.425  13.589  1.00 27.47 ? 17  VAL A C   1 
ATOM   137  O O   . VAL A  1 17  ? -32.740 -8.316  13.699  1.00 27.19 ? 17  VAL A O   1 
ATOM   138  C CB  . VAL A  1 17  ? -32.813 -11.164 15.374  1.00 29.30 ? 17  VAL A CB  1 
ATOM   139  C CG1 . VAL A  1 17  ? -31.459 -10.503 15.594  1.00 30.29 ? 17  VAL A CG1 1 
ATOM   140  C CG2 . VAL A  1 17  ? -33.333 -11.761 16.671  1.00 30.70 ? 17  VAL A CG2 1 
ATOM   141  N N   . LEU A  1 18  ? -33.415 -10.029 12.408  1.00 26.91 ? 18  LEU A N   1 
ATOM   142  C CA  . LEU A  1 18  ? -32.897 -9.412  11.191  1.00 26.73 ? 18  LEU A CA  1 
ATOM   143  C C   . LEU A  1 18  ? -33.657 -8.138  10.834  1.00 28.37 ? 18  LEU A C   1 
ATOM   144  O O   . LEU A  1 18  ? -33.044 -7.129  10.461  1.00 27.64 ? 18  LEU A O   1 
ATOM   145  C CB  . LEU A  1 18  ? -32.951 -10.417 10.042  1.00 26.68 ? 18  LEU A CB  1 
ATOM   146  C CG  . LEU A  1 18  ? -32.524 -9.923  8.663   1.00 25.75 ? 18  LEU A CG  1 
ATOM   147  C CD1 . LEU A  1 18  ? -31.147 -9.294  8.725   1.00 26.70 ? 18  LEU A CD1 1 
ATOM   148  C CD2 . LEU A  1 18  ? -32.539 -11.076 7.682   1.00 26.44 ? 18  LEU A CD2 1 
ATOM   149  N N   . VAL A  1 19  ? -34.989 -8.163  10.933  1.00 27.62 ? 19  VAL A N   1 
ATOM   150  C CA  . VAL A  1 19  ? -35.785 -6.981  10.605  1.00 27.15 ? 19  VAL A CA  1 
ATOM   151  C C   . VAL A  1 19  ? -35.452 -5.836  11.552  1.00 26.02 ? 19  VAL A C   1 
ATOM   152  O O   . VAL A  1 19  ? -35.276 -4.687  11.127  1.00 26.64 ? 19  VAL A O   1 
ATOM   153  C CB  . VAL A  1 19  ? -37.289 -7.319  10.634  1.00 27.37 ? 19  VAL A CB  1 
ATOM   154  C CG1 . VAL A  1 19  ? -38.124 -6.049  10.533  1.00 26.99 ? 19  VAL A CG1 1 
ATOM   155  C CG2 . VAL A  1 19  ? -37.645 -8.290  9.513   1.00 28.20 ? 19  VAL A CG2 1 
ATOM   156  N N   . PHE A  1 20  ? -35.349 -6.135  12.848  1.00 26.86 ? 20  PHE A N   1 
ATOM   157  C CA  . PHE A  1 20  ? -35.004 -5.118  13.836  1.00 26.07 ? 20  PHE A CA  1 
ATOM   158  C C   . PHE A  1 20  ? -33.679 -4.447  13.494  1.00 26.67 ? 20  PHE A C   1 
ATOM   159  O O   . PHE A  1 20  ? -33.567 -3.217  13.522  1.00 27.41 ? 20  PHE A O   1 
ATOM   160  C CB  . PHE A  1 20  ? -34.953 -5.763  15.223  1.00 27.16 ? 20  PHE A CB  1 
ATOM   161  C CG  . PHE A  1 20  ? -34.621 -4.813  16.333  1.00 26.94 ? 20  PHE A CG  1 
ATOM   162  C CD1 . PHE A  1 20  ? -33.303 -4.566  16.684  1.00 27.96 ? 20  PHE A CD1 1 
ATOM   163  C CD2 . PHE A  1 20  ? -35.630 -4.192  17.047  1.00 26.93 ? 20  PHE A CD2 1 
ATOM   164  C CE1 . PHE A  1 20  ? -32.999 -3.700  17.714  1.00 29.29 ? 20  PHE A CE1 1 
ATOM   165  C CE2 . PHE A  1 20  ? -35.336 -3.329  18.078  1.00 27.80 ? 20  PHE A CE2 1 
ATOM   166  C CZ  . PHE A  1 20  ? -34.018 -3.080  18.413  1.00 29.54 ? 20  PHE A CZ  1 
ATOM   167  N N   . VAL A  1 21  ? -32.663 -5.245  13.157  1.00 27.07 ? 21  VAL A N   1 
ATOM   168  C CA  . VAL A  1 21  ? -31.349 -4.697  12.826  1.00 26.63 ? 21  VAL A CA  1 
ATOM   169  C C   . VAL A  1 21  ? -31.414 -3.870  11.549  1.00 26.76 ? 21  VAL A C   1 
ATOM   170  O O   . VAL A  1 21  ? -30.900 -2.747  11.490  1.00 27.08 ? 21  VAL A O   1 
ATOM   171  C CB  . VAL A  1 21  ? -30.314 -5.827  12.706  1.00 26.08 ? 21  VAL A CB  1 
ATOM   172  C CG1 . VAL A  1 21  ? -29.065 -5.320  12.005  1.00 28.74 ? 21  VAL A CG1 1 
ATOM   173  C CG2 . VAL A  1 21  ? -29.978 -6.372  14.074  1.00 28.13 ? 21  VAL A CG2 1 
ATOM   174  N N   . LEU A  1 22  ? -32.033 -4.424  10.502  1.00 26.82 ? 22  LEU A N   1 
ATOM   175  C CA  . LEU A  1 22  ? -32.180 -3.700  9.242   1.00 27.02 ? 22  LEU A CA  1 
ATOM   176  C C   . LEU A  1 22  ? -32.874 -2.364  9.448   1.00 27.25 ? 22  LEU A C   1 
ATOM   177  O O   . LEU A  1 22  ? -32.467 -1.342  8.883   1.00 27.55 ? 22  LEU A O   1 
ATOM   178  C CB  . LEU A  1 22  ? -32.970 -4.548  8.246   1.00 26.77 ? 22  LEU A CB  1 
ATOM   179  C CG  . LEU A  1 22  ? -32.199 -5.585  7.439   1.00 27.60 ? 22  LEU A CG  1 
ATOM   180  C CD1 . LEU A  1 22  ? -33.148 -6.657  6.942   1.00 28.91 ? 22  LEU A CD1 1 
ATOM   181  C CD2 . LEU A  1 22  ? -31.505 -4.905  6.273   1.00 29.13 ? 22  LEU A CD2 1 
ATOM   182  N N   . ASP A  1 23  ? -33.930 -2.356  10.256  1.00 28.84 ? 23  ASP A N   1 
ATOM   183  C CA  . ASP A  1 23  ? -34.678 -1.131  10.490  1.00 27.13 ? 23  ASP A CA  1 
ATOM   184  C C   . ASP A  1 23  ? -33.888 -0.132  11.330  1.00 27.60 ? 23  ASP A C   1 
ATOM   185  O O   . ASP A  1 23  ? -34.027 1.081   11.133  1.00 28.51 ? 23  ASP A O   1 
ATOM   186  C CB  . ASP A  1 23  ? -36.012 -1.481  11.149  1.00 28.01 ? 23  ASP A CB  1 
ATOM   187  C CG  . ASP A  1 23  ? -36.707 -0.281  11.738  1.00 29.00 ? 23  ASP A CG  1 
ATOM   188  O OD1 . ASP A  1 23  ? -36.963 0.689   10.990  1.00 29.48 ? 23  ASP A OD1 1 
ATOM   189  O OD2 . ASP A  1 23  ? -37.004 -0.320  12.953  1.00 29.04 ? 23  ASP A OD2 1 
ATOM   190  N N   . GLN A  1 24  ? -33.049 -0.609  12.253  1.00 27.45 ? 24  GLN A N   1 
ATOM   191  C CA  . GLN A  1 24  ? -32.299 0.310   13.105  1.00 27.99 ? 24  GLN A CA  1 
ATOM   192  C C   . GLN A  1 24  ? -31.174 1.001   12.344  1.00 28.22 ? 24  GLN A C   1 
ATOM   193  O O   . GLN A  1 24  ? -30.891 2.178   12.594  1.00 28.50 ? 24  GLN A O   1 
ATOM   194  C CB  . GLN A  1 24  ? -31.753 -0.429  14.326  1.00 28.20 ? 24  GLN A CB  1 
ATOM   195  C CG  . GLN A  1 24  ? -32.825 -0.793  15.336  1.00 27.75 ? 24  GLN A CG  1 
ATOM   196  C CD  . GLN A  1 24  ? -33.659 0.406   15.751  1.00 28.04 ? 24  GLN A CD  1 
ATOM   197  O OE1 . GLN A  1 24  ? -33.124 1.479   16.026  1.00 29.07 ? 24  GLN A OE1 1 
ATOM   198  N NE2 . GLN A  1 24  ? -34.977 0.232   15.789  1.00 27.59 ? 24  GLN A NE2 1 
ATOM   199  N N   . VAL A  1 25  ? -30.514 0.288   11.425  1.00 28.21 ? 25  VAL A N   1 
ATOM   200  C CA  . VAL A  1 25  ? -29.509 0.929   10.580  1.00 28.78 ? 25  VAL A CA  1 
ATOM   201  C C   . VAL A  1 25  ? -30.173 1.828   9.547   1.00 28.02 ? 25  VAL A C   1 
ATOM   202  O O   . VAL A  1 25  ? -29.604 2.850   9.144   1.00 28.16 ? 25  VAL A O   1 
ATOM   203  C CB  . VAL A  1 25  ? -28.602 -0.122  9.915   1.00 28.56 ? 25  VAL A CB  1 
ATOM   204  C CG1 . VAL A  1 25  ? -27.383 0.549   9.296   1.00 29.47 ? 25  VAL A CG1 1 
ATOM   205  C CG2 . VAL A  1 25  ? -28.174 -1.155  10.930  1.00 31.31 ? 25  VAL A CG2 1 
ATOM   206  N N   . SER A  1 26  ? -31.374 1.465   9.095   1.00 28.38 ? 26  SER A N   1 
ATOM   207  C CA  . SER A  1 26  ? -32.131 2.332   8.199   1.00 27.43 ? 26  SER A CA  1 
ATOM   208  C C   . SER A  1 26  ? -32.381 3.695   8.834   1.00 27.95 ? 26  SER A C   1 
ATOM   209  O O   . SER A  1 26  ? -32.136 4.736   8.215   1.00 28.89 ? 26  SER A O   1 
ATOM   210  C CB  . SER A  1 26  ? -33.452 1.661   7.827   1.00 27.80 ? 26  SER A CB  1 
ATOM   211  O OG  . SER A  1 26  ? -33.373 1.055   6.552   1.00 30.36 ? 26  SER A OG  1 
ATOM   212  N N   . LYS A  1 27  ? -32.865 3.706   10.079  1.00 28.57 ? 27  LYS A N   1 
ATOM   213  C CA  . LYS A  1 27  ? -33.082 4.970   10.777  1.00 28.26 ? 27  LYS A CA  1 
ATOM   214  C C   . LYS A  1 27  ? -31.768 5.704   11.016  1.00 29.44 ? 27  LYS A C   1 
ATOM   215  O O   . LYS A  1 27  ? -31.681 6.919   10.803  1.00 29.48 ? 27  LYS A O   1 
ATOM   216  C CB  . LYS A  1 27  ? -33.801 4.721   12.104  1.00 27.85 ? 27  LYS A CB  1 
ATOM   217  C CG  . LYS A  1 27  ? -35.181 4.108   11.961  1.00 28.72 ? 27  LYS A CG  1 
ATOM   218  C CD  . LYS A  1 27  ? -35.658 3.532   13.285  1.00 29.39 ? 27  LYS A CD  1 
ATOM   219  C CE  . LYS A  1 27  ? -37.087 3.023   13.185  1.00 29.42 ? 27  LYS A CE  1 
ATOM   220  N NZ  . LYS A  1 27  ? -37.541 2.323   14.422  1.00 28.75 ? 27  LYS A NZ  1 
ATOM   221  N N   . ALA A  1 28  ? -30.732 4.983   11.454  1.00 29.18 ? 28  ALA A N   1 
ATOM   222  C CA  . ALA A  1 28  ? -29.478 5.640   11.813  1.00 29.18 ? 28  ALA A CA  1 
ATOM   223  C C   . ALA A  1 28  ? -28.818 6.301   10.608  1.00 29.30 ? 28  ALA A C   1 
ATOM   224  O O   . ALA A  1 28  ? -28.104 7.299   10.763  1.00 29.04 ? 28  ALA A O   1 
ATOM   225  C CB  . ALA A  1 28  ? -28.527 4.638   12.469  1.00 30.25 ? 28  ALA A CB  1 
ATOM   226  N N   . PHE A  1 29  ? -29.044 5.771   9.404   1.00 28.88 ? 29  PHE A N   1 
ATOM   227  C CA  . PHE A  1 29  ? -28.493 6.408   8.213   1.00 29.67 ? 29  PHE A CA  1 
ATOM   228  C C   . PHE A  1 29  ? -29.201 7.723   7.923   1.00 30.64 ? 29  PHE A C   1 
ATOM   229  O O   . PHE A  1 29  ? -28.586 8.795   7.950   1.00 31.55 ? 29  PHE A O   1 
ATOM   230  C CB  . PHE A  1 29  ? -28.593 5.476   7.004   1.00 30.21 ? 29  PHE A CB  1 
ATOM   231  C CG  . PHE A  1 29  ? -28.247 6.146   5.703   1.00 31.62 ? 29  PHE A CG  1 
ATOM   232  C CD1 . PHE A  1 29  ? -26.924 6.334   5.338   1.00 32.77 ? 29  PHE A CD1 1 
ATOM   233  C CD2 . PHE A  1 29  ? -29.242 6.603   4.852   1.00 32.71 ? 29  PHE A CD2 1 
ATOM   234  C CE1 . PHE A  1 29  ? -26.598 6.960   4.148   1.00 34.26 ? 29  PHE A CE1 1 
ATOM   235  C CE2 . PHE A  1 29  ? -28.923 7.229   3.660   1.00 33.77 ? 29  PHE A CE2 1 
ATOM   236  C CZ  . PHE A  1 29  ? -27.600 7.407   3.308   1.00 34.46 ? 29  PHE A CZ  1 
ATOM   237  N N   . PHE A  1 30  ? -30.508 7.659   7.658   1.00 31.08 ? 30  PHE A N   1 
ATOM   238  C CA  . PHE A  1 30  ? -31.244 8.846   7.245   1.00 30.96 ? 30  PHE A CA  1 
ATOM   239  C C   . PHE A  1 30  ? -31.314 9.898   8.341   1.00 31.03 ? 30  PHE A C   1 
ATOM   240  O O   . PHE A  1 30  ? -31.526 11.076  8.034   1.00 31.63 ? 30  PHE A O   1 
ATOM   241  C CB  . PHE A  1 30  ? -32.647 8.457   6.785   1.00 30.71 ? 30  PHE A CB  1 
ATOM   242  C CG  . PHE A  1 30  ? -32.664 7.722   5.476   1.00 30.92 ? 30  PHE A CG  1 
ATOM   243  C CD1 . PHE A  1 30  ? -32.364 8.381   4.294   1.00 31.29 ? 30  PHE A CD1 1 
ATOM   244  C CD2 . PHE A  1 30  ? -32.969 6.372   5.427   1.00 31.48 ? 30  PHE A CD2 1 
ATOM   245  C CE1 . PHE A  1 30  ? -32.370 7.707   3.088   1.00 32.19 ? 30  PHE A CE1 1 
ATOM   246  C CE2 . PHE A  1 30  ? -32.977 5.694   4.225   1.00 32.16 ? 30  PHE A CE2 1 
ATOM   247  C CZ  . PHE A  1 30  ? -32.678 6.361   3.054   1.00 33.21 ? 30  PHE A CZ  1 
ATOM   248  N N   . GLN A  1 31  ? -31.127 9.510   9.603   1.00 30.38 ? 31  GLN A N   1 
ATOM   249  C CA  . GLN A  1 31  ? -31.014 10.502  10.667  1.00 30.18 ? 31  GLN A CA  1 
ATOM   250  C C   . GLN A  1 31  ? -29.761 11.346  10.485  1.00 30.21 ? 31  GLN A C   1 
ATOM   251  O O   . GLN A  1 31  ? -29.838 12.566  10.294  1.00 29.92 ? 31  GLN A O   1 
ATOM   252  C CB  . GLN A  1 31  ? -31.005 9.815   12.034  1.00 29.97 ? 31  GLN A CB  1 
ATOM   253  C CG  . GLN A  1 31  ? -32.385 9.535   12.597  1.00 29.68 ? 31  GLN A CG  1 
ATOM   254  C CD  . GLN A  1 31  ? -32.344 9.181   14.066  1.00 29.40 ? 31  GLN A CD  1 
ATOM   255  O OE1 . GLN A  1 31  ? -32.083 8.036   14.434  1.00 28.43 ? 31  GLN A OE1 1 
ATOM   256  N NE2 . GLN A  1 31  ? -32.598 10.167  14.919  1.00 30.13 ? 31  GLN A NE2 1 
ATOM   257  N N   . ALA A  1 32  ? -28.595 10.707  10.519  1.00 30.25 ? 32  ALA A N   1 
ATOM   258  C CA  . ALA A  1 32  ? -27.323 11.404  10.411  1.00 30.53 ? 32  ALA A CA  1 
ATOM   259  C C   . ALA A  1 32  ? -26.989 11.812  8.981   1.00 31.25 ? 32  ALA A C   1 
ATOM   260  O O   . ALA A  1 32  ? -25.887 12.315  8.741   1.00 32.01 ? 32  ALA A O   1 
ATOM   261  C CB  . ALA A  1 32  ? -26.200 10.534  10.985  1.00 30.53 ? 32  ALA A CB  1 
ATOM   262  N N   . GLU A  1 33  ? -27.906 11.612  8.034   1.00 31.39 ? 33  GLU A N   1 
ATOM   263  C CA  . GLU A  1 33  ? -27.684 12.007  6.651   1.00 32.58 ? 33  GLU A CA  1 
ATOM   264  C C   . GLU A  1 33  ? -28.584 13.140  6.186   1.00 33.28 ? 33  GLU A C   1 
ATOM   265  O O   . GLU A  1 33  ? -28.158 13.942  5.351   1.00 35.31 ? 33  GLU A O   1 
ATOM   266  C CB  . GLU A  1 33  ? -27.877 10.809  5.712   1.00 33.66 ? 33  GLU A CB  1 
ATOM   267  C CG  . GLU A  1 33  ? -27.363 11.048  4.304   1.00 35.51 ? 33  GLU A CG  1 
ATOM   268  C CD  . GLU A  1 33  ? -25.859 11.254  4.268   1.00 38.06 ? 33  GLU A CD  1 
ATOM   269  O OE1 . GLU A  1 33  ? -25.145 10.525  4.992   1.00 37.59 ? 33  GLU A OE1 1 
ATOM   270  O OE2 . GLU A  1 33  ? -25.392 12.146  3.523   1.00 40.40 ? 33  GLU A OE2 1 
ATOM   271  N N   . LEU A  1 34  ? -29.806 13.234  6.703   1.00 32.27 ? 34  LEU A N   1 
ATOM   272  C CA  . LEU A  1 34  ? -30.775 14.223  6.252   1.00 32.18 ? 34  LEU A CA  1 
ATOM   273  C C   . LEU A  1 34  ? -31.084 15.227  7.355   1.00 31.68 ? 34  LEU A C   1 
ATOM   274  O O   . LEU A  1 34  ? -30.707 15.056  8.516   1.00 31.32 ? 34  LEU A O   1 
ATOM   275  C CB  . LEU A  1 34  ? -32.070 13.546  5.783   1.00 32.23 ? 34  LEU A CB  1 
ATOM   276  C CG  . LEU A  1 34  ? -32.122 12.971  4.366   1.00 32.28 ? 34  LEU A CG  1 
ATOM   277  C CD1 . LEU A  1 34  ? -31.180 11.785  4.216   1.00 33.10 ? 34  LEU A CD1 1 
ATOM   278  C CD2 . LEU A  1 34  ? -33.547 12.576  4.011   1.00 31.61 ? 34  LEU A CD2 1 
ATOM   279  N N   . SER A  1 35  ? -31.767 16.298  6.966   1.00 31.88 ? 35  SER A N   1 
ATOM   280  C CA  . SER A  1 35  ? -32.345 17.250  7.901   1.00 32.02 ? 35  SER A CA  1 
ATOM   281  C C   . SER A  1 35  ? -33.839 16.982  8.027   1.00 32.02 ? 35  SER A C   1 
ATOM   282  O O   . SER A  1 35  ? -34.451 16.353  7.159   1.00 32.58 ? 35  SER A O   1 
ATOM   283  C CB  . SER A  1 35  ? -32.104 18.692  7.446   1.00 32.89 ? 35  SER A CB  1 
ATOM   284  O OG  . SER A  1 35  ? -30.749 18.896  7.089   1.00 32.76 ? 35  SER A OG  1 
ATOM   285  N N   . MET A  1 36  ? -34.424 17.462  9.123   1.00 31.05 ? 36  MET A N   1 
ATOM   286  C CA  . MET A  1 36  ? -35.817 17.143  9.411   1.00 31.92 ? 36  MET A CA  1 
ATOM   287  C C   . MET A  1 36  ? -36.717 17.674  8.302   1.00 32.88 ? 36  MET A C   1 
ATOM   288  O O   . MET A  1 36  ? -36.750 18.882  8.045   1.00 34.66 ? 36  MET A O   1 
ATOM   289  C CB  . MET A  1 36  ? -36.237 17.722  10.763  1.00 34.08 ? 36  MET A CB  1 
ATOM   290  C CG  . MET A  1 36  ? -37.322 16.904  11.480  1.00 36.00 ? 36  MET A CG  1 
ATOM   291  S SD  . MET A  1 36  ? -38.499 17.896  12.436  1.00 39.99 ? 36  MET A SD  1 
ATOM   292  C CE  . MET A  1 36  ? -39.552 16.622  13.136  1.00 38.47 ? 36  MET A CE  1 
ATOM   293  N N   . TYR A  1 37  ? -37.424 16.759  7.636   1.00 32.34 ? 37  TYR A N   1 
ATOM   294  C CA  . TYR A  1 37  ? -38.368 16.992  6.537   1.00 33.15 ? 37  TYR A CA  1 
ATOM   295  C C   . TYR A  1 37  ? -37.664 17.321  5.224   1.00 32.98 ? 37  TYR A C   1 
ATOM   296  O O   . TYR A  1 37  ? -38.348 17.596  4.226   1.00 33.70 ? 37  TYR A O   1 
ATOM   297  C CB  . TYR A  1 37  ? -39.392 18.087  6.872   1.00 34.05 ? 37  TYR A CB  1 
ATOM   298  C CG  . TYR A  1 37  ? -40.219 17.781  8.109   1.00 34.66 ? 37  TYR A CG  1 
ATOM   299  C CD1 . TYR A  1 37  ? -40.676 16.494  8.356   1.00 34.77 ? 37  TYR A CD1 1 
ATOM   300  C CD2 . TYR A  1 37  ? -40.518 18.769  9.039   1.00 35.66 ? 37  TYR A CD2 1 
ATOM   301  C CE1 . TYR A  1 37  ? -41.418 16.201  9.483   1.00 35.20 ? 37  TYR A CE1 1 
ATOM   302  C CE2 . TYR A  1 37  ? -41.260 18.485  10.172  1.00 36.30 ? 37  TYR A CE2 1 
ATOM   303  C CZ  . TYR A  1 37  ? -41.708 17.197  10.389  1.00 36.32 ? 37  TYR A CZ  1 
ATOM   304  O OH  . TYR A  1 37  ? -42.448 16.900  11.512  1.00 38.09 ? 37  TYR A OH  1 
ATOM   305  N N   . GLN A  1 38  ? -36.331 17.306  5.184   1.00 32.61 ? 38  GLN A N   1 
ATOM   306  C CA  . GLN A  1 38  ? -35.611 17.404  3.920   1.00 32.76 ? 38  GLN A CA  1 
ATOM   307  C C   . GLN A  1 38  ? -35.839 16.139  3.106   1.00 33.48 ? 38  GLN A C   1 
ATOM   308  O O   . GLN A  1 38  ? -35.806 15.028  3.641   1.00 34.12 ? 38  GLN A O   1 
ATOM   309  C CB  . GLN A  1 38  ? -34.116 17.606  4.173   1.00 32.29 ? 38  GLN A CB  1 
ATOM   310  C CG  . GLN A  1 38  ? -33.222 17.459  2.953   1.00 33.19 ? 38  GLN A CG  1 
ATOM   311  C CD  . GLN A  1 38  ? -31.761 17.366  3.339   1.00 33.73 ? 38  GLN A CD  1 
ATOM   312  O OE1 . GLN A  1 38  ? -31.424 17.407  4.522   1.00 33.09 ? 38  GLN A OE1 1 
ATOM   313  N NE2 . GLN A  1 38  ? -30.884 17.234  2.347   1.00 35.02 ? 38  GLN A NE2 1 
ATOM   314  N N   . GLN A  1 39  ? -36.080 16.297  1.806   1.00 33.36 ? 39  GLN A N   1 
ATOM   315  C CA  . GLN A  1 39  ? -36.426 15.147  0.985   1.00 34.11 ? 39  GLN A CA  1 
ATOM   316  C C   . GLN A  1 39  ? -35.455 15.002  -0.180  1.00 34.57 ? 39  GLN A C   1 
ATOM   317  O O   . GLN A  1 39  ? -35.141 15.978  -0.867  1.00 33.45 ? 39  GLN A O   1 
ATOM   318  C CB  . GLN A  1 39  ? -37.887 15.215  0.509   1.00 34.72 ? 39  GLN A CB  1 
ATOM   319  C CG  . GLN A  1 39  ? -38.208 16.051  -0.707  1.00 35.63 ? 39  GLN A CG  1 
ATOM   320  C CD  . GLN A  1 39  ? -39.685 15.966  -1.036  1.00 34.31 ? 39  GLN A CD  1 
ATOM   321  O OE1 . GLN A  1 39  ? -40.519 15.861  -0.136  1.00 33.89 ? 39  GLN A OE1 1 
ATOM   322  N NE2 . GLN A  1 39  ? -40.016 15.981  -2.321  1.00 33.59 ? 39  GLN A NE2 1 
ATOM   323  N N   . ILE A  1 40  ? -34.962 13.780  -0.369  1.00 35.26 ? 40  ILE A N   1 
ATOM   324  C CA  . ILE A  1 40  ? -34.028 13.440  -1.436  1.00 35.11 ? 40  ILE A CA  1 
ATOM   325  C C   . ILE A  1 40  ? -34.839 12.753  -2.527  1.00 35.58 ? 40  ILE A C   1 
ATOM   326  O O   . ILE A  1 40  ? -35.225 11.590  -2.391  1.00 36.16 ? 40  ILE A O   1 
ATOM   327  C CB  . ILE A  1 40  ? -32.892 12.550  -0.927  1.00 33.73 ? 40  ILE A CB  1 
ATOM   328  C CG1 . ILE A  1 40  ? -31.974 13.340  0.004   1.00 34.26 ? 40  ILE A CG1 1 
ATOM   329  C CG2 . ILE A  1 40  ? -32.111 11.977  -2.088  1.00 35.04 ? 40  ILE A CG2 1 
ATOM   330  C CD1 . ILE A  1 40  ? -30.889 12.512  0.640   1.00 36.17 ? 40  ILE A CD1 1 
ATOM   331  N N   . VAL A  1 41  ? -35.088 13.472  -3.620  1.00 36.09 ? 41  VAL A N   1 
ATOM   332  C CA  . VAL A  1 41  ? -35.990 12.981  -4.652  1.00 36.51 ? 41  VAL A CA  1 
ATOM   333  C C   . VAL A  1 41  ? -35.345 11.814  -5.388  1.00 36.65 ? 41  VAL A C   1 
ATOM   334  O O   . VAL A  1 41  ? -34.192 11.898  -5.831  1.00 36.77 ? 41  VAL A O   1 
ATOM   335  C CB  . VAL A  1 41  ? -36.365 14.118  -5.612  1.00 37.24 ? 41  VAL A CB  1 
ATOM   336  C CG1 . VAL A  1 41  ? -37.205 13.579  -6.734  1.00 38.78 ? 41  VAL A CG1 1 
ATOM   337  C CG2 . VAL A  1 41  ? -37.109 15.211  -4.865  1.00 36.65 ? 41  VAL A CG2 1 
ATOM   338  N N   . VAL A  1 42  ? -36.089 10.710  -5.514  1.00 37.47 ? 42  VAL A N   1 
ATOM   339  C CA  . VAL A  1 42  ? -35.649 9.528   -6.263  1.00 37.55 ? 42  VAL A CA  1 
ATOM   340  C C   . VAL A  1 42  ? -36.443 9.358   -7.563  1.00 38.89 ? 42  VAL A C   1 
ATOM   341  O O   . VAL A  1 42  ? -35.880 9.424   -8.656  1.00 40.41 ? 42  VAL A O   1 
ATOM   342  C CB  . VAL A  1 42  ? -35.723 8.255   -5.392  1.00 37.67 ? 42  VAL A CB  1 
ATOM   343  C CG1 . VAL A  1 42  ? -35.391 7.030   -6.226  1.00 38.65 ? 42  VAL A CG1 1 
ATOM   344  C CG2 . VAL A  1 42  ? -34.784 8.366   -4.201  1.00 37.30 ? 42  VAL A CG2 1 
ATOM   345  N N   . ILE A  1 43  ? -37.748 9.127   -7.460  1.00 39.09 ? 43  ILE A N   1 
ATOM   346  C CA  . ILE A  1 43  ? -38.655 9.241   -8.603  1.00 39.19 ? 43  ILE A CA  1 
ATOM   347  C C   . ILE A  1 43  ? -39.363 10.588  -8.475  1.00 39.54 ? 43  ILE A C   1 
ATOM   348  O O   . ILE A  1 43  ? -40.113 10.791  -7.504  1.00 39.50 ? 43  ILE A O   1 
ATOM   349  C CB  . ILE A  1 43  ? -39.665 8.087   -8.670  1.00 38.26 ? 43  ILE A CB  1 
ATOM   350  C CG1 . ILE A  1 43  ? -38.976 6.753   -8.975  1.00 37.99 ? 43  ILE A CG1 1 
ATOM   351  C CG2 . ILE A  1 43  ? -40.716 8.364   -9.724  1.00 38.62 ? 43  ILE A CG2 1 
ATOM   352  C CD1 . ILE A  1 43  ? -38.624 5.932   -7.760  1.00 38.99 ? 43  ILE A CD1 1 
ATOM   353  N N   . PRO A  1 44  ? -39.162 11.522  -9.411  1.00 40.25 ? 44  PRO A N   1 
ATOM   354  C CA  . PRO A  1 44  ? -39.554 12.921  -9.165  1.00 40.38 ? 44  PRO A CA  1 
ATOM   355  C C   . PRO A  1 44  ? -41.000 13.124  -8.745  1.00 39.76 ? 44  PRO A C   1 
ATOM   356  O O   . PRO A  1 44  ? -41.273 13.994  -7.909  1.00 40.59 ? 44  PRO A O   1 
ATOM   357  C CB  . PRO A  1 44  ? -39.256 13.593  -10.510 1.00 42.19 ? 44  PRO A CB  1 
ATOM   358  C CG  . PRO A  1 44  ? -38.141 12.789  -11.075 1.00 42.01 ? 44  PRO A CG  1 
ATOM   359  C CD  . PRO A  1 44  ? -38.419 11.369  -10.672 1.00 40.68 ? 44  PRO A CD  1 
ATOM   360  N N   . ASP A  1 45  ? -41.938 12.365  -9.306  1.00 39.22 ? 45  ASP A N   1 
ATOM   361  C CA  . ASP A  1 45  ? -43.347 12.530  -8.981  1.00 38.85 ? 45  ASP A CA  1 
ATOM   362  C C   . ASP A  1 45  ? -43.917 11.369  -8.174  1.00 39.33 ? 45  ASP A C   1 
ATOM   363  O O   . ASP A  1 45  ? -45.133 11.327  -7.963  1.00 39.84 ? 45  ASP A O   1 
ATOM   364  C CB  . ASP A  1 45  ? -44.170 12.729  -10.262 1.00 40.59 ? 45  ASP A CB  1 
ATOM   365  C CG  . ASP A  1 45  ? -43.941 14.089  -10.911 1.00 40.42 ? 45  ASP A CG  1 
ATOM   366  O OD1 . ASP A  1 45  ? -43.713 15.068  -10.167 1.00 40.65 ? 45  ASP A OD1 1 
ATOM   367  O OD2 . ASP A  1 45  ? -43.998 14.180  -12.160 1.00 37.97 ? 45  ASP A OD2 1 
ATOM   368  N N   . LEU A  1 46  ? -43.091 10.417  -7.727  1.00 39.46 ? 46  LEU A N   1 
ATOM   369  C CA  . LEU A  1 46  ? -43.657 9.283   -6.998  1.00 38.78 ? 46  LEU A CA  1 
ATOM   370  C C   . LEU A  1 46  ? -42.941 8.912   -5.698  1.00 38.32 ? 46  LEU A C   1 
ATOM   371  O O   . LEU A  1 46  ? -43.586 8.380   -4.788  1.00 39.02 ? 46  LEU A O   1 
ATOM   372  C CB  . LEU A  1 46  ? -43.724 8.050   -7.914  1.00 37.97 ? 46  LEU A CB  1 
ATOM   373  C CG  . LEU A  1 46  ? -44.258 6.732   -7.337  1.00 36.49 ? 46  LEU A CG  1 
ATOM   374  C CD1 . LEU A  1 46  ? -45.712 6.853   -6.907  1.00 37.45 ? 46  LEU A CD1 1 
ATOM   375  C CD2 . LEU A  1 46  ? -44.087 5.596   -8.333  1.00 34.85 ? 46  LEU A CD2 1 
ATOM   376  N N   . PHE A  1 47  ? -41.639 9.179   -5.567  1.00 38.63 ? 47  PHE A N   1 
ATOM   377  C CA  . PHE A  1 47  ? -40.905 8.619   -4.435  1.00 38.91 ? 47  PHE A CA  1 
ATOM   378  C C   . PHE A  1 47  ? -39.692 9.473   -4.088  1.00 39.16 ? 47  PHE A C   1 
ATOM   379  O O   . PHE A  1 47  ? -39.044 10.049  -4.966  1.00 39.21 ? 47  PHE A O   1 
ATOM   380  C CB  . PHE A  1 47  ? -40.486 7.172   -4.735  1.00 38.99 ? 47  PHE A CB  1 
ATOM   381  C CG  . PHE A  1 47  ? -39.498 6.584   -3.754  1.00 38.97 ? 47  PHE A CG  1 
ATOM   382  C CD1 . PHE A  1 47  ? -39.819 6.434   -2.414  1.00 38.96 ? 47  PHE A CD1 1 
ATOM   383  C CD2 . PHE A  1 47  ? -38.261 6.133   -4.190  1.00 38.59 ? 47  PHE A CD2 1 
ATOM   384  C CE1 . PHE A  1 47  ? -38.910 5.875   -1.524  1.00 37.74 ? 47  PHE A CE1 1 
ATOM   385  C CE2 . PHE A  1 47  ? -37.351 5.573   -3.307  1.00 37.92 ? 47  PHE A CE2 1 
ATOM   386  C CZ  . PHE A  1 47  ? -37.677 5.444   -1.973  1.00 37.54 ? 47  PHE A CZ  1 
ATOM   387  N N   . SER A  1 48  ? -39.392 9.541   -2.789  1.00 38.07 ? 48  SER A N   1 
ATOM   388  C CA  . SER A  1 48  ? -38.250 10.296  -2.290  1.00 37.35 ? 48  SER A CA  1 
ATOM   389  C C   . SER A  1 48  ? -37.887 9.781   -0.903  1.00 36.78 ? 48  SER A C   1 
ATOM   390  O O   . SER A  1 48  ? -38.695 9.137   -0.230  1.00 37.11 ? 48  SER A O   1 
ATOM   391  C CB  . SER A  1 48  ? -38.552 11.798  -2.242  1.00 36.94 ? 48  SER A CB  1 
ATOM   392  O OG  . SER A  1 48  ? -38.995 12.276  -3.500  1.00 38.77 ? 48  SER A OG  1 
ATOM   393  N N   . TRP A  1 49  ? -36.655 10.064  -0.488  1.00 35.42 ? 49  TRP A N   1 
ATOM   394  C CA  . TRP A  1 49  ? -36.251 9.842   0.893   1.00 34.41 ? 49  TRP A CA  1 
ATOM   395  C C   . TRP A  1 49  ? -36.556 11.094  1.711   1.00 33.87 ? 49  TRP A C   1 
ATOM   396  O O   . TRP A  1 49  ? -36.540 12.206  1.186   1.00 34.18 ? 49  TRP A O   1 
ATOM   397  C CB  . TRP A  1 49  ? -34.760 9.505   0.984   1.00 34.84 ? 49  TRP A CB  1 
ATOM   398  C CG  . TRP A  1 49  ? -34.279 8.370   0.103   1.00 34.77 ? 49  TRP A CG  1 
ATOM   399  C CD1 . TRP A  1 49  ? -33.404 8.462   -0.942  1.00 34.75 ? 49  TRP A CD1 1 
ATOM   400  C CD2 . TRP A  1 49  ? -34.624 6.980   0.213   1.00 34.67 ? 49  TRP A CD2 1 
ATOM   401  N NE1 . TRP A  1 49  ? -33.188 7.222   -1.492  1.00 34.63 ? 49  TRP A NE1 1 
ATOM   402  C CE2 . TRP A  1 49  ? -33.926 6.295   -0.803  1.00 34.86 ? 49  TRP A CE2 1 
ATOM   403  C CE3 . TRP A  1 49  ? -35.457 6.251   1.065   1.00 34.40 ? 49  TRP A CE3 1 
ATOM   404  C CZ2 . TRP A  1 49  ? -34.035 4.917   -0.988  1.00 35.59 ? 49  TRP A CZ2 1 
ATOM   405  C CZ3 . TRP A  1 49  ? -35.565 4.881   0.878   1.00 34.46 ? 49  TRP A CZ3 1 
ATOM   406  C CH2 . TRP A  1 49  ? -34.857 4.230   -0.140  1.00 34.67 ? 49  TRP A CH2 1 
ATOM   407  N N   . THR A  1 50  ? -36.847 10.910  3.001   1.00 32.99 ? 50  THR A N   1 
ATOM   408  C CA  . THR A  1 50  ? -37.172 12.034  3.877   1.00 31.93 ? 50  THR A CA  1 
ATOM   409  C C   . THR A  1 50  ? -36.762 11.689  5.308   1.00 31.47 ? 50  THR A C   1 
ATOM   410  O O   . THR A  1 50  ? -36.162 10.643  5.563   1.00 31.75 ? 50  THR A O   1 
ATOM   411  C CB  . THR A  1 50  ? -38.658 12.396  3.778   1.00 31.91 ? 50  THR A CB  1 
ATOM   412  O OG1 . THR A  1 50  ? -38.975 13.397  4.752   1.00 31.96 ? 50  THR A OG1 1 
ATOM   413  C CG2 . THR A  1 50  ? -39.529 11.169  4.007   1.00 32.81 ? 50  THR A CG2 1 
ATOM   414  N N   . LEU A  1 51  ? -37.046 12.598  6.243   1.00 30.95 ? 51  LEU A N   1 
ATOM   415  C CA  . LEU A  1 51  ? -36.650 12.412  7.642   1.00 30.32 ? 51  LEU A CA  1 
ATOM   416  C C   . LEU A  1 51  ? -37.728 12.914  8.609   1.00 30.50 ? 51  LEU A C   1 
ATOM   417  O O   . LEU A  1 51  ? -37.456 13.673  9.540   1.00 31.32 ? 51  LEU A O   1 
ATOM   418  C CB  . LEU A  1 51  ? -35.301 13.078  7.912   1.00 29.98 ? 51  LEU A CB  1 
ATOM   419  C CG  . LEU A  1 51  ? -34.635 12.728  9.249   1.00 29.92 ? 51  LEU A CG  1 
ATOM   420  C CD1 . LEU A  1 51  ? -34.505 11.225  9.404   1.00 30.77 ? 51  LEU A CD1 1 
ATOM   421  C CD2 . LEU A  1 51  ? -33.287 13.407  9.402   1.00 31.70 ? 51  LEU A CD2 1 
ATOM   422  N N   . ALA A  1 52  ? -38.981 12.522  8.392   1.00 29.82 ? 52  ALA A N   1 
ATOM   423  C CA  . ALA A  1 52  ? -40.049 12.910  9.308   1.00 29.81 ? 52  ALA A CA  1 
ATOM   424  C C   . ALA A  1 52  ? -40.008 12.082  10.589  1.00 30.46 ? 52  ALA A C   1 
ATOM   425  O O   . ALA A  1 52  ? -39.778 10.870  10.559  1.00 31.19 ? 52  ALA A O   1 
ATOM   426  C CB  . ALA A  1 52  ? -41.414 12.753  8.639   1.00 31.30 ? 52  ALA A CB  1 
ATOM   427  N N   . TYR A  1 53  ? -40.253 12.743  11.719  1.00 31.31 ? 53  TYR A N   1 
ATOM   428  C CA  . TYR A  1 53  ? -40.348 12.091  13.025  1.00 31.71 ? 53  TYR A CA  1 
ATOM   429  C C   . TYR A  1 53  ? -41.812 12.097  13.445  1.00 32.36 ? 53  TYR A C   1 
ATOM   430  O O   . TYR A  1 53  ? -42.345 13.135  13.845  1.00 34.13 ? 53  TYR A O   1 
ATOM   431  C CB  . TYR A  1 53  ? -39.494 12.799  14.072  1.00 32.75 ? 53  TYR A CB  1 
ATOM   432  C CG  . TYR A  1 53  ? -38.008 12.704  13.849  1.00 33.81 ? 53  TYR A CG  1 
ATOM   433  C CD1 . TYR A  1 53  ? -37.447 11.596  13.233  1.00 33.06 ? 53  TYR A CD1 1 
ATOM   434  C CD2 . TYR A  1 53  ? -37.163 13.727  14.259  1.00 34.61 ? 53  TYR A CD2 1 
ATOM   435  C CE1 . TYR A  1 53  ? -36.084 11.508  13.030  1.00 33.24 ? 53  TYR A CE1 1 
ATOM   436  C CE2 . TYR A  1 53  ? -35.801 13.650  14.061  1.00 34.47 ? 53  TYR A CE2 1 
ATOM   437  C CZ  . TYR A  1 53  ? -35.264 12.538  13.445  1.00 33.84 ? 53  TYR A CZ  1 
ATOM   438  O OH  . TYR A  1 53  ? -33.904 12.453  13.244  1.00 34.23 ? 53  TYR A OH  1 
ATOM   439  N N   . ASN A  1 54  ? -42.461 10.941  13.361  1.00 32.62 ? 54  ASN A N   1 
ATOM   440  C CA  . ASN A  1 54  ? -43.855 10.836  13.772  1.00 33.09 ? 54  ASN A CA  1 
ATOM   441  C C   . ASN A  1 54  ? -43.908 10.533  15.264  1.00 33.65 ? 54  ASN A C   1 
ATOM   442  O O   . ASN A  1 54  ? -43.518 9.445   15.703  1.00 33.66 ? 54  ASN A O   1 
ATOM   443  C CB  . ASN A  1 54  ? -44.583 9.766   12.964  1.00 32.57 ? 54  ASN A CB  1 
ATOM   444  C CG  . ASN A  1 54  ? -46.094 9.919   13.026  1.00 33.22 ? 54  ASN A CG  1 
ATOM   445  O OD1 . ASN A  1 54  ? -46.609 10.977  13.399  1.00 34.03 ? 54  ASN A OD1 1 
ATOM   446  N ND2 . ASN A  1 54  ? -46.813 8.863   12.658  1.00 32.45 ? 54  ASN A ND2 1 
ATOM   447  N N   . THR A  1 55  ? -44.394 11.494  16.043  1.00 34.61 ? 55  THR A N   1 
ATOM   448  C CA  . THR A  1 55  ? -44.607 11.316  17.471  1.00 34.53 ? 55  THR A CA  1 
ATOM   449  C C   . THR A  1 55  ? -45.891 10.560  17.783  1.00 33.99 ? 55  THR A C   1 
ATOM   450  O O   . THR A  1 55  ? -46.344 10.593  18.933  1.00 34.20 ? 55  THR A O   1 
ATOM   451  C CB  . THR A  1 55  ? -44.637 12.676  18.171  1.00 35.44 ? 55  THR A CB  1 
ATOM   452  O OG1 . THR A  1 55  ? -45.605 13.518  17.528  1.00 34.32 ? 55  THR A OG1 1 
ATOM   453  C CG2 . THR A  1 55  ? -43.269 13.342  18.106  1.00 36.70 ? 55  THR A CG2 1 
ATOM   454  N N   . GLY A  1 56  ? -46.478 9.885   16.800  1.00 33.70 ? 56  GLY A N   1 
ATOM   455  C CA  . GLY A  1 56  ? -47.793 9.297   16.981  1.00 32.85 ? 56  GLY A CA  1 
ATOM   456  C C   . GLY A  1 56  ? -48.892 10.328  17.122  1.00 31.98 ? 56  GLY A C   1 
ATOM   457  O O   . GLY A  1 56  ? -49.798 10.152  17.945  1.00 31.80 ? 56  GLY A O   1 
ATOM   458  N N   . ALA A  1 57  ? -48.837 11.402  16.336  1.00 32.41 ? 57  ALA A N   1 
ATOM   459  C CA  . ALA A  1 57  ? -49.820 12.475  16.413  1.00 33.43 ? 57  ALA A CA  1 
ATOM   460  C C   . ALA A  1 57  ? -51.071 12.204  15.584  1.00 32.88 ? 57  ALA A C   1 
ATOM   461  O O   . ALA A  1 57  ? -51.848 13.136  15.343  1.00 32.60 ? 57  ALA A O   1 
ATOM   462  C CB  . ALA A  1 57  ? -49.189 13.801  15.979  1.00 35.00 ? 57  ALA A CB  1 
ATOM   463  N N   . ALA A  1 58  ? -51.282 10.965  15.133  1.00 33.16 ? 58  ALA A N   1 
ATOM   464  C CA  . ALA A  1 58  ? -52.524 10.640  14.436  1.00 31.91 ? 58  ALA A CA  1 
ATOM   465  C C   . ALA A  1 58  ? -53.694 10.566  15.408  1.00 31.75 ? 58  ALA A C   1 
ATOM   466  O O   . ALA A  1 58  ? -54.787 11.060  15.112  1.00 32.02 ? 58  ALA A O   1 
ATOM   467  C CB  . ALA A  1 58  ? -52.374 9.321   13.676  1.00 30.90 ? 58  ALA A CB  1 
ATOM   468  N N   . PHE A  1 59  ? -53.473 9.970   16.582  1.00 31.37 ? 59  PHE A N   1 
ATOM   469  C CA  . PHE A  1 59  ? -54.502 9.800   17.601  1.00 30.86 ? 59  PHE A CA  1 
ATOM   470  C C   . PHE A  1 59  ? -54.511 10.932  18.623  1.00 31.68 ? 59  PHE A C   1 
ATOM   471  O O   . PHE A  1 59  ? -54.886 10.714  19.783  1.00 31.83 ? 59  PHE A O   1 
ATOM   472  C CB  . PHE A  1 59  ? -54.329 8.451   18.303  1.00 30.61 ? 59  PHE A CB  1 
ATOM   473  C CG  . PHE A  1 59  ? -54.441 7.265   17.383  1.00 29.92 ? 59  PHE A CG  1 
ATOM   474  C CD1 . PHE A  1 59  ? -53.373 6.889   16.584  1.00 30.49 ? 59  PHE A CD1 1 
ATOM   475  C CD2 . PHE A  1 59  ? -55.607 6.519   17.327  1.00 29.60 ? 59  PHE A CD2 1 
ATOM   476  C CE1 . PHE A  1 59  ? -53.469 5.801   15.740  1.00 30.49 ? 59  PHE A CE1 1 
ATOM   477  C CE2 . PHE A  1 59  ? -55.707 5.427   16.484  1.00 29.30 ? 59  PHE A CE2 1 
ATOM   478  C CZ  . PHE A  1 59  ? -54.636 5.069   15.690  1.00 29.68 ? 59  PHE A CZ  1 
ATOM   479  N N   . SER A  1 60  ? -54.106 12.140  18.221  1.00 32.56 ? 60  SER A N   1 
ATOM   480  C CA  . SER A  1 60  ? -54.121 13.283  19.127  1.00 32.51 ? 60  SER A CA  1 
ATOM   481  C C   . SER A  1 60  ? -55.531 13.688  19.531  1.00 33.72 ? 60  SER A C   1 
ATOM   482  O O   . SER A  1 60  ? -55.690 14.447  20.492  1.00 35.07 ? 60  SER A O   1 
ATOM   483  C CB  . SER A  1 60  ? -53.422 14.475  18.480  1.00 33.52 ? 60  SER A CB  1 
ATOM   484  O OG  . SER A  1 60  ? -54.113 14.878  17.308  1.00 34.95 ? 60  SER A OG  1 
ATOM   485  N N   . PHE A  1 61  ? -56.554 13.210  18.817  1.00 33.06 ? 61  PHE A N   1 
ATOM   486  C CA  . PHE A  1 61  ? -57.934 13.572  19.119  1.00 32.65 ? 61  PHE A CA  1 
ATOM   487  C C   . PHE A  1 61  ? -58.443 12.969  20.425  1.00 33.20 ? 61  PHE A C   1 
ATOM   488  O O   . PHE A  1 61  ? -59.495 13.394  20.913  1.00 33.86 ? 61  PHE A O   1 
ATOM   489  C CB  . PHE A  1 61  ? -58.848 13.161  17.957  1.00 30.28 ? 61  PHE A CB  1 
ATOM   490  C CG  . PHE A  1 61  ? -58.702 11.722  17.545  1.00 30.07 ? 61  PHE A CG  1 
ATOM   491  C CD1 . PHE A  1 61  ? -59.447 10.732  18.163  1.00 29.73 ? 61  PHE A CD1 1 
ATOM   492  C CD2 . PHE A  1 61  ? -57.825 11.360  16.534  1.00 30.36 ? 61  PHE A CD2 1 
ATOM   493  C CE1 . PHE A  1 61  ? -59.316 9.409   17.788  1.00 28.42 ? 61  PHE A CE1 1 
ATOM   494  C CE2 . PHE A  1 61  ? -57.690 10.037  16.155  1.00 29.19 ? 61  PHE A CE2 1 
ATOM   495  C CZ  . PHE A  1 61  ? -58.437 9.062   16.783  1.00 27.88 ? 61  PHE A CZ  1 
ATOM   496  N N   . LEU A  1 62  ? -57.728 12.007  21.009  1.00 33.09 ? 62  LEU A N   1 
ATOM   497  C CA  . LEU A  1 62  ? -58.209 11.326  22.205  1.00 33.23 ? 62  LEU A CA  1 
ATOM   498  C C   . LEU A  1 62  ? -57.889 12.067  23.495  1.00 35.46 ? 62  LEU A C   1 
ATOM   499  O O   . LEU A  1 62  ? -58.385 11.666  24.553  1.00 36.25 ? 62  LEU A O   1 
ATOM   500  C CB  . LEU A  1 62  ? -57.623 9.915   22.275  1.00 31.32 ? 62  LEU A CB  1 
ATOM   501  C CG  . LEU A  1 62  ? -58.002 8.996   21.115  1.00 29.85 ? 62  LEU A CG  1 
ATOM   502  C CD1 . LEU A  1 62  ? -57.083 7.790   21.056  1.00 29.27 ? 62  LEU A CD1 1 
ATOM   503  C CD2 . LEU A  1 62  ? -59.461 8.562   21.212  1.00 27.25 ? 62  LEU A CD2 1 
ATOM   504  N N   . ALA A  1 63  ? -57.076 13.120  23.445  1.00 37.41 ? 63  ALA A N   1 
ATOM   505  C CA  . ALA A  1 63  ? -56.677 13.800  24.669  1.00 40.46 ? 63  ALA A CA  1 
ATOM   506  C C   . ALA A  1 63  ? -56.162 15.197  24.346  1.00 42.89 ? 63  ALA A C   1 
ATOM   507  O O   . ALA A  1 63  ? -55.690 15.461  23.237  1.00 40.75 ? 63  ALA A O   1 
ATOM   508  C CB  . ALA A  1 63  ? -55.610 12.998  25.423  1.00 40.07 ? 63  ALA A CB  1 
ATOM   509  N N   . ASP A  1 64  ? -56.264 16.093  25.332  1.00 45.08 ? 64  ASP A N   1 
ATOM   510  C CA  . ASP A  1 64  ? -55.725 17.443  25.221  1.00 45.26 ? 64  ASP A CA  1 
ATOM   511  C C   . ASP A  1 64  ? -54.307 17.544  25.778  1.00 45.64 ? 64  ASP A C   1 
ATOM   512  O O   . ASP A  1 64  ? -53.890 18.618  26.241  1.00 45.29 ? 64  ASP A O   1 
ATOM   513  C CB  . ASP A  1 64  ? -56.658 18.453  25.900  1.00 47.52 ? 64  ASP A CB  1 
ATOM   514  C CG  . ASP A  1 64  ? -56.838 18.193  27.385  1.00 49.93 ? 64  ASP A CG  1 
ATOM   515  O OD1 . ASP A  1 64  ? -56.364 17.147  27.875  1.00 48.21 ? 64  ASP A OD1 1 
ATOM   516  O OD2 . ASP A  1 64  ? -57.456 19.046  28.062  1.00 52.11 ? 64  ASP A OD2 1 
ATOM   517  N N   . SER A  1 65  ? -53.568 16.438  25.770  1.00 44.80 ? 65  SER A N   1 
ATOM   518  C CA  . SER A  1 65  ? -52.159 16.404  26.125  1.00 42.43 ? 65  SER A CA  1 
ATOM   519  C C   . SER A  1 65  ? -51.347 15.900  24.937  1.00 40.06 ? 65  SER A C   1 
ATOM   520  O O   . SER A  1 65  ? -51.889 15.411  23.941  1.00 39.14 ? 65  SER A O   1 
ATOM   521  C CB  . SER A  1 65  ? -51.909 15.514  27.351  1.00 41.51 ? 65  SER A CB  1 
ATOM   522  O OG  . SER A  1 65  ? -52.623 15.973  28.482  1.00 43.38 ? 65  SER A OG  1 
ATOM   523  N N   . SER A  1 66  ? -50.026 16.025  25.050  1.00 39.16 ? 66  SER A N   1 
ATOM   524  C CA  . SER A  1 66  ? -49.108 15.516  24.036  1.00 37.18 ? 66  SER A CA  1 
ATOM   525  C C   . SER A  1 66  ? -47.949 14.827  24.735  1.00 35.21 ? 66  SER A C   1 
ATOM   526  O O   . SER A  1 66  ? -47.267 15.441  25.561  1.00 34.53 ? 66  SER A O   1 
ATOM   527  C CB  . SER A  1 66  ? -48.600 16.637  23.123  1.00 36.67 ? 66  SER A CB  1 
ATOM   528  O OG  . SER A  1 66  ? -49.587 17.003  22.171  1.00 38.00 ? 66  SER A OG  1 
ATOM   529  N N   . GLY A  1 67  ? -47.729 13.557  24.405  1.00 34.73 ? 67  GLY A N   1 
ATOM   530  C CA  . GLY A  1 67  ? -46.644 12.798  24.993  1.00 34.76 ? 67  GLY A CA  1 
ATOM   531  C C   . GLY A  1 67  ? -47.052 11.401  25.412  1.00 33.36 ? 67  GLY A C   1 
ATOM   532  O O   . GLY A  1 67  ? -46.210 10.505  25.507  1.00 33.43 ? 67  GLY A O   1 
ATOM   533  N N   . TRP A  1 68  ? -48.348 11.200  25.659  1.00 33.65 ? 68  TRP A N   1 
ATOM   534  C CA  . TRP A  1 68  ? -48.816 9.904   26.133  1.00 33.54 ? 68  TRP A CA  1 
ATOM   535  C C   . TRP A  1 68  ? -48.779 8.833   25.053  1.00 33.13 ? 68  TRP A C   1 
ATOM   536  O O   . TRP A  1 68  ? -48.793 7.643   25.385  1.00 32.21 ? 68  TRP A O   1 
ATOM   537  C CB  . TRP A  1 68  ? -50.231 10.027  26.692  1.00 34.49 ? 68  TRP A CB  1 
ATOM   538  C CG  . TRP A  1 68  ? -51.166 10.756  25.789  1.00 35.36 ? 68  TRP A CG  1 
ATOM   539  C CD1 . TRP A  1 68  ? -51.490 12.077  25.847  1.00 36.93 ? 68  TRP A CD1 1 
ATOM   540  C CD2 . TRP A  1 68  ? -51.906 10.208  24.691  1.00 34.83 ? 68  TRP A CD2 1 
ATOM   541  N NE1 . TRP A  1 68  ? -52.385 12.389  24.853  1.00 37.35 ? 68  TRP A NE1 1 
ATOM   542  C CE2 . TRP A  1 68  ? -52.658 11.258  24.129  1.00 35.33 ? 68  TRP A CE2 1 
ATOM   543  C CE3 . TRP A  1 68  ? -52.005 8.931   24.127  1.00 34.28 ? 68  TRP A CE3 1 
ATOM   544  C CZ2 . TRP A  1 68  ? -53.499 11.073  23.035  1.00 34.69 ? 68  TRP A CZ2 1 
ATOM   545  C CZ3 . TRP A  1 68  ? -52.840 8.749   23.040  1.00 33.93 ? 68  TRP A CZ3 1 
ATOM   546  C CH2 . TRP A  1 68  ? -53.575 9.816   22.504  1.00 33.92 ? 68  TRP A CH2 1 
ATOM   547  N N   . GLN A  1 69  ? -48.741 9.221   23.774  1.00 33.36 ? 69  GLN A N   1 
ATOM   548  C CA  . GLN A  1 69  ? -48.620 8.226   22.712  1.00 32.92 ? 69  GLN A CA  1 
ATOM   549  C C   . GLN A  1 69  ? -47.309 7.462   22.830  1.00 33.07 ? 69  GLN A C   1 
ATOM   550  O O   . GLN A  1 69  ? -47.247 6.264   22.524  1.00 32.67 ? 69  GLN A O   1 
ATOM   551  C CB  . GLN A  1 69  ? -48.727 8.890   21.340  1.00 32.62 ? 69  GLN A CB  1 
ATOM   552  C CG  . GLN A  1 69  ? -50.102 9.423   21.004  1.00 31.91 ? 69  GLN A CG  1 
ATOM   553  C CD  . GLN A  1 69  ? -50.268 10.871  21.391  1.00 32.64 ? 69  GLN A CD  1 
ATOM   554  O OE1 . GLN A  1 69  ? -49.498 11.403  22.189  1.00 33.48 ? 69  GLN A OE1 1 
ATOM   555  N NE2 . GLN A  1 69  ? -51.270 11.524  20.818  1.00 32.96 ? 69  GLN A NE2 1 
ATOM   556  N N   . ARG A  1 70  ? -46.252 8.140   23.283  1.00 33.40 ? 70  ARG A N   1 
ATOM   557  C CA  . ARG A  1 70  ? -44.973 7.473   23.493  1.00 33.49 ? 70  ARG A CA  1 
ATOM   558  C C   . ARG A  1 70  ? -45.107 6.305   24.460  1.00 33.33 ? 70  ARG A C   1 
ATOM   559  O O   . ARG A  1 70  ? -44.330 5.346   24.387  1.00 33.53 ? 70  ARG A O   1 
ATOM   560  C CB  . ARG A  1 70  ? -43.943 8.480   24.012  1.00 33.90 ? 70  ARG A CB  1 
ATOM   561  C CG  . ARG A  1 70  ? -42.510 7.972   24.043  1.00 34.51 ? 70  ARG A CG  1 
ATOM   562  C CD  . ARG A  1 70  ? -41.669 8.788   25.005  1.00 34.36 ? 70  ARG A CD  1 
ATOM   563  N NE  . ARG A  1 70  ? -40.250 8.473   24.899  1.00 35.91 ? 70  ARG A NE  1 
ATOM   564  C CZ  . ARG A  1 70  ? -39.313 8.970   25.695  1.00 37.35 ? 70  ARG A CZ  1 
ATOM   565  N NH1 . ARG A  1 70  ? -39.615 9.781   26.697  1.00 37.30 ? 70  ARG A NH1 1 
ATOM   566  N NH2 . ARG A  1 70  ? -38.040 8.649   25.479  1.00 38.76 ? 70  ARG A NH2 1 
ATOM   567  N N   . TRP A  1 71  ? -46.087 6.356   25.362  1.00 32.93 ? 71  TRP A N   1 
ATOM   568  C CA  . TRP A  1 71  ? -46.261 5.320   26.371  1.00 32.97 ? 71  TRP A CA  1 
ATOM   569  C C   . TRP A  1 71  ? -47.393 4.356   26.039  1.00 32.00 ? 71  TRP A C   1 
ATOM   570  O O   . TRP A  1 71  ? -47.205 3.137   26.113  1.00 32.08 ? 71  TRP A O   1 
ATOM   571  C CB  . TRP A  1 71  ? -46.503 5.963   27.740  1.00 32.47 ? 71  TRP A CB  1 
ATOM   572  C CG  . TRP A  1 71  ? -45.501 7.020   28.081  1.00 32.65 ? 71  TRP A CG  1 
ATOM   573  C CD1 . TRP A  1 71  ? -45.744 8.349   28.257  1.00 33.38 ? 71  TRP A CD1 1 
ATOM   574  C CD2 . TRP A  1 71  ? -44.092 6.841   28.274  1.00 32.73 ? 71  TRP A CD2 1 
ATOM   575  N NE1 . TRP A  1 71  ? -44.577 9.009   28.555  1.00 33.06 ? 71  TRP A NE1 1 
ATOM   576  C CE2 . TRP A  1 71  ? -43.548 8.105   28.571  1.00 33.07 ? 71  TRP A CE2 1 
ATOM   577  C CE3 . TRP A  1 71  ? -43.240 5.735   28.228  1.00 32.79 ? 71  TRP A CE3 1 
ATOM   578  C CZ2 . TRP A  1 71  ? -42.192 8.295   28.820  1.00 33.46 ? 71  TRP A CZ2 1 
ATOM   579  C CZ3 . TRP A  1 71  ? -41.893 5.927   28.477  1.00 34.55 ? 71  TRP A CZ3 1 
ATOM   580  C CH2 . TRP A  1 71  ? -41.383 7.197   28.769  1.00 35.00 ? 71  TRP A CH2 1 
ATOM   581  N N   . LEU A  1 72  ? -48.567 4.878   25.677  1.00 32.45 ? 72  LEU A N   1 
ATOM   582  C CA  . LEU A  1 72  ? -49.690 4.010   25.339  1.00 31.38 ? 72  LEU A CA  1 
ATOM   583  C C   . LEU A  1 72  ? -49.337 3.074   24.192  1.00 31.52 ? 72  LEU A C   1 
ATOM   584  O O   . LEU A  1 72  ? -49.657 1.879   24.234  1.00 31.22 ? 72  LEU A O   1 
ATOM   585  C CB  . LEU A  1 72  ? -50.914 4.855   24.987  1.00 31.04 ? 72  LEU A CB  1 
ATOM   586  C CG  . LEU A  1 72  ? -52.012 4.203   24.145  1.00 30.48 ? 72  LEU A CG  1 
ATOM   587  C CD1 . LEU A  1 72  ? -52.674 3.048   24.884  1.00 30.56 ? 72  LEU A CD1 1 
ATOM   588  C CD2 . LEU A  1 72  ? -53.040 5.242   23.735  1.00 29.93 ? 72  LEU A CD2 1 
ATOM   589  N N   . PHE A  1 73  ? -48.662 3.594   23.164  1.00 31.28 ? 73  PHE A N   1 
ATOM   590  C CA  . PHE A  1 73  ? -48.283 2.764   22.025  1.00 31.19 ? 73  PHE A CA  1 
ATOM   591  C C   . PHE A  1 73  ? -47.113 1.845   22.357  1.00 31.11 ? 73  PHE A C   1 
ATOM   592  O O   . PHE A  1 73  ? -47.076 0.698   21.898  1.00 29.88 ? 73  PHE A O   1 
ATOM   593  C CB  . PHE A  1 73  ? -47.958 3.649   20.824  1.00 31.18 ? 73  PHE A CB  1 
ATOM   594  C CG  . PHE A  1 73  ? -49.143 4.403   20.306  1.00 31.12 ? 73  PHE A CG  1 
ATOM   595  C CD1 . PHE A  1 73  ? -50.414 3.869   20.422  1.00 30.71 ? 73  PHE A CD1 1 
ATOM   596  C CD2 . PHE A  1 73  ? -48.996 5.647   19.721  1.00 31.89 ? 73  PHE A CD2 1 
ATOM   597  C CE1 . PHE A  1 73  ? -51.515 4.553   19.955  1.00 30.70 ? 73  PHE A CE1 1 
ATOM   598  C CE2 . PHE A  1 73  ? -50.097 6.340   19.251  1.00 31.79 ? 73  PHE A CE2 1 
ATOM   599  C CZ  . PHE A  1 73  ? -51.359 5.791   19.369  1.00 31.09 ? 73  PHE A CZ  1 
ATOM   600  N N   . ALA A  1 74  ? -46.150 2.322   23.150  1.00 31.69 ? 74  ALA A N   1 
ATOM   601  C CA  . ALA A  1 74  ? -45.068 1.444   23.579  1.00 30.82 ? 74  ALA A CA  1 
ATOM   602  C C   . ALA A  1 74  ? -45.607 0.276   24.390  1.00 30.20 ? 74  ALA A C   1 
ATOM   603  O O   . ALA A  1 74  ? -45.195 -0.872  24.186  1.00 30.06 ? 74  ALA A O   1 
ATOM   604  C CB  . ALA A  1 74  ? -44.031 2.223   24.387  1.00 32.34 ? 74  ALA A CB  1 
ATOM   605  N N   . LEU A  1 75  ? -46.551 0.543   25.298  1.00 29.36 ? 75  LEU A N   1 
ATOM   606  C CA  . LEU A  1 75  ? -47.158 -0.544  26.058  1.00 30.60 ? 75  LEU A CA  1 
ATOM   607  C C   . LEU A  1 75  ? -47.890 -1.508  25.137  1.00 30.48 ? 75  LEU A C   1 
ATOM   608  O O   . LEU A  1 75  ? -47.836 -2.726  25.335  1.00 28.65 ? 75  LEU A O   1 
ATOM   609  C CB  . LEU A  1 75  ? -48.108 0.008   27.122  1.00 29.50 ? 75  LEU A CB  1 
ATOM   610  C CG  . LEU A  1 75  ? -48.606 -1.008  28.158  1.00 28.73 ? 75  LEU A CG  1 
ATOM   611  C CD1 . LEU A  1 75  ? -48.657 -0.367  29.531  1.00 29.61 ? 75  LEU A CD1 1 
ATOM   612  C CD2 . LEU A  1 75  ? -49.975 -1.592  27.793  1.00 29.44 ? 75  LEU A CD2 1 
ATOM   613  N N   . ILE A  1 76  ? -48.579 -0.980  24.122  1.00 29.30 ? 76  ILE A N   1 
ATOM   614  C CA  . ILE A  1 76  ? -49.254 -1.839  23.153  1.00 28.44 ? 76  ILE A CA  1 
ATOM   615  C C   . ILE A  1 76  ? -48.258 -2.802  22.524  1.00 28.20 ? 76  ILE A C   1 
ATOM   616  O O   . ILE A  1 76  ? -48.477 -4.018  22.496  1.00 27.49 ? 76  ILE A O   1 
ATOM   617  C CB  . ILE A  1 76  ? -49.969 -0.993  22.083  1.00 28.57 ? 76  ILE A CB  1 
ATOM   618  C CG1 . ILE A  1 76  ? -51.276 -0.431  22.632  1.00 29.25 ? 76  ILE A CG1 1 
ATOM   619  C CG2 . ILE A  1 76  ? -50.226 -1.816  20.823  1.00 28.18 ? 76  ILE A CG2 1 
ATOM   620  C CD1 . ILE A  1 76  ? -52.038 0.407   21.642  1.00 30.66 ? 76  ILE A CD1 1 
ATOM   621  N N   . ALA A  1 77  ? -47.132 -2.273  22.044  1.00 28.21 ? 77  ALA A N   1 
ATOM   622  C CA  . ALA A  1 77  ? -46.126 -3.126  21.423  1.00 28.02 ? 77  ALA A CA  1 
ATOM   623  C C   . ALA A  1 77  ? -45.576 -4.139  22.416  1.00 27.73 ? 77  ALA A C   1 
ATOM   624  O O   . ALA A  1 77  ? -45.312 -5.290  22.054  1.00 27.91 ? 77  ALA A O   1 
ATOM   625  C CB  . ALA A  1 77  ? -44.998 -2.277  20.839  1.00 27.84 ? 77  ALA A CB  1 
ATOM   626  N N   . ILE A  1 78  ? -45.395 -3.727  23.674  1.00 28.40 ? 78  ILE A N   1 
ATOM   627  C CA  . ILE A  1 78  ? -44.855 -4.631  24.689  1.00 27.84 ? 78  ILE A CA  1 
ATOM   628  C C   . ILE A  1 78  ? -45.786 -5.820  24.900  1.00 27.60 ? 78  ILE A C   1 
ATOM   629  O O   . ILE A  1 78  ? -45.357 -6.981  24.869  1.00 28.21 ? 78  ILE A O   1 
ATOM   630  C CB  . ILE A  1 78  ? -44.602 -3.870  26.005  1.00 27.30 ? 78  ILE A CB  1 
ATOM   631  C CG1 . ILE A  1 78  ? -43.429 -2.903  25.847  1.00 27.55 ? 78  ILE A CG1 1 
ATOM   632  C CG2 . ILE A  1 78  ? -44.335 -4.841  27.141  1.00 25.64 ? 78  ILE A CG2 1 
ATOM   633  C CD1 . ILE A  1 78  ? -43.284 -1.922  26.984  1.00 27.98 ? 78  ILE A CD1 1 
ATOM   634  N N   . VAL A  1 79  ? -47.077 -5.551  25.111  1.00 27.51 ? 79  VAL A N   1 
ATOM   635  C CA  . VAL A  1 79  ? -48.030 -6.630  25.353  1.00 26.79 ? 79  VAL A CA  1 
ATOM   636  C C   . VAL A  1 79  ? -48.283 -7.425  24.079  1.00 26.90 ? 79  VAL A C   1 
ATOM   637  O O   . VAL A  1 79  ? -48.338 -8.660  24.106  1.00 27.02 ? 79  VAL A O   1 
ATOM   638  C CB  . VAL A  1 79  ? -49.335 -6.070  25.947  1.00 26.61 ? 79  VAL A CB  1 
ATOM   639  C CG1 . VAL A  1 79  ? -50.491 -7.032  25.711  1.00 27.06 ? 79  VAL A CG1 1 
ATOM   640  C CG2 . VAL A  1 79  ? -49.163 -5.813  27.437  1.00 26.43 ? 79  VAL A CG2 1 
ATOM   641  N N   . VAL A  1 80  ? -48.437 -6.738  22.945  1.00 26.93 ? 80  VAL A N   1 
ATOM   642  C CA  . VAL A  1 80  ? -48.690 -7.435  21.686  1.00 27.11 ? 80  VAL A CA  1 
ATOM   643  C C   . VAL A  1 80  ? -47.536 -8.370  21.354  1.00 29.05 ? 80  VAL A C   1 
ATOM   644  O O   . VAL A  1 80  ? -47.745 -9.488  20.867  1.00 29.03 ? 80  VAL A O   1 
ATOM   645  C CB  . VAL A  1 80  ? -48.950 -6.425  20.552  1.00 26.89 ? 80  VAL A CB  1 
ATOM   646  C CG1 . VAL A  1 80  ? -48.782 -7.085  19.195  1.00 27.41 ? 80  VAL A CG1 1 
ATOM   647  C CG2 . VAL A  1 80  ? -50.344 -5.844  20.677  1.00 27.48 ? 80  VAL A CG2 1 
ATOM   648  N N   . SER A  1 81  ? -46.303 -7.937  21.625  1.00 28.05 ? 81  SER A N   1 
ATOM   649  C CA  . SER A  1 81  ? -45.142 -8.774  21.339  1.00 28.05 ? 81  SER A CA  1 
ATOM   650  C C   . SER A  1 81  ? -45.158 -10.052 22.170  1.00 28.81 ? 81  SER A C   1 
ATOM   651  O O   . SER A  1 81  ? -44.779 -11.125 21.681  1.00 29.01 ? 81  SER A O   1 
ATOM   652  C CB  . SER A  1 81  ? -43.858 -7.986  21.591  1.00 28.08 ? 81  SER A CB  1 
ATOM   653  O OG  . SER A  1 81  ? -43.847 -6.784  20.838  1.00 28.04 ? 81  SER A OG  1 
ATOM   654  N N   . ALA A  1 82  ? -45.585 -9.957  23.433  1.00 28.36 ? 82  ALA A N   1 
ATOM   655  C CA  . ALA A  1 82  ? -45.635 -11.138 24.290  1.00 29.19 ? 82  ALA A CA  1 
ATOM   656  C C   . ALA A  1 82  ? -46.631 -12.167 23.765  1.00 30.15 ? 82  ALA A C   1 
ATOM   657  O O   . ALA A  1 82  ? -46.342 -13.370 23.751  1.00 30.57 ? 82  ALA A O   1 
ATOM   658  C CB  . ALA A  1 82  ? -45.982 -10.735 25.723  1.00 29.09 ? 82  ALA A CB  1 
ATOM   659  N N   . SER A  1 83  ? -47.814 -11.716 23.335  1.00 30.12 ? 83  SER A N   1 
ATOM   660  C CA  . SER A  1 83  ? -48.806 -12.642 22.792  1.00 30.59 ? 83  SER A CA  1 
ATOM   661  C C   . SER A  1 83  ? -48.385 -13.192 21.435  1.00 31.42 ? 83  SER A C   1 
ATOM   662  O O   . SER A  1 83  ? -48.845 -14.268 21.034  1.00 33.08 ? 83  SER A O   1 
ATOM   663  C CB  . SER A  1 83  ? -50.166 -11.957 22.677  1.00 30.89 ? 83  SER A CB  1 
ATOM   664  O OG  . SER A  1 83  ? -50.139 -10.949 21.682  1.00 30.70 ? 83  SER A OG  1 
ATOM   665  N N   . LEU A  1 84  ? -47.537 -12.466 20.708  1.00 31.16 ? 84  LEU A N   1 
ATOM   666  C CA  . LEU A  1 84  ? -47.018 -12.939 19.434  1.00 31.38 ? 84  LEU A CA  1 
ATOM   667  C C   . LEU A  1 84  ? -45.746 -13.759 19.584  1.00 31.86 ? 84  LEU A C   1 
ATOM   668  O O   . LEU A  1 84  ? -45.293 -14.353 18.600  1.00 32.72 ? 84  LEU A O   1 
ATOM   669  C CB  . LEU A  1 84  ? -46.764 -11.757 18.495  1.00 30.28 ? 84  LEU A CB  1 
ATOM   670  C CG  . LEU A  1 84  ? -47.866 -11.466 17.475  1.00 30.24 ? 84  LEU A CG  1 
ATOM   671  C CD1 . LEU A  1 84  ? -49.239 -11.484 18.126  1.00 32.32 ? 84  LEU A CD1 1 
ATOM   672  C CD2 . LEU A  1 84  ? -47.613 -10.129 16.811  1.00 28.71 ? 84  LEU A CD2 1 
ATOM   673  N N   . VAL A  1 85  ? -45.162 -13.805 20.778  1.00 31.33 ? 85  VAL A N   1 
ATOM   674  C CA  . VAL A  1 85  ? -44.065 -14.728 21.047  1.00 31.39 ? 85  VAL A CA  1 
ATOM   675  C C   . VAL A  1 85  ? -44.591 -16.107 21.420  1.00 33.25 ? 85  VAL A C   1 
ATOM   676  O O   . VAL A  1 85  ? -44.097 -17.120 20.919  1.00 33.62 ? 85  VAL A O   1 
ATOM   677  C CB  . VAL A  1 85  ? -43.140 -14.160 22.144  1.00 30.70 ? 85  VAL A CB  1 
ATOM   678  C CG1 . VAL A  1 85  ? -42.353 -15.277 22.819  1.00 30.97 ? 85  VAL A CG1 1 
ATOM   679  C CG2 . VAL A  1 85  ? -42.183 -13.145 21.546  1.00 30.28 ? 85  VAL A CG2 1 
ATOM   680  N N   . VAL A  1 86  ? -45.599 -16.167 22.293  1.00 33.73 ? 86  VAL A N   1 
ATOM   681  C CA  . VAL A  1 86  ? -46.202 -17.453 22.623  1.00 34.15 ? 86  VAL A CA  1 
ATOM   682  C C   . VAL A  1 86  ? -46.917 -18.031 21.410  1.00 35.30 ? 86  VAL A C   1 
ATOM   683  O O   . VAL A  1 86  ? -46.973 -19.255 21.240  1.00 36.98 ? 86  VAL A O   1 
ATOM   684  C CB  . VAL A  1 86  ? -47.149 -17.321 23.830  1.00 32.03 ? 86  VAL A CB  1 
ATOM   685  C CG1 . VAL A  1 86  ? -46.376 -16.904 25.067  1.00 32.82 ? 86  VAL A CG1 1 
ATOM   686  C CG2 . VAL A  1 86  ? -48.253 -16.327 23.536  1.00 32.53 ? 86  VAL A CG2 1 
ATOM   687  N N   . TRP A  1 87  ? -47.476 -17.170 20.555  1.00 34.71 ? 87  TRP A N   1 
ATOM   688  C CA  . TRP A  1 87  ? -48.155 -17.645 19.354  1.00 36.33 ? 87  TRP A CA  1 
ATOM   689  C C   . TRP A  1 87  ? -47.189 -18.383 18.435  1.00 37.34 ? 87  TRP A C   1 
ATOM   690  O O   . TRP A  1 87  ? -47.530 -19.438 17.886  1.00 38.87 ? 87  TRP A O   1 
ATOM   691  C CB  . TRP A  1 87  ? -48.811 -16.466 18.632  1.00 37.55 ? 87  TRP A CB  1 
ATOM   692  C CG  . TRP A  1 87  ? -49.824 -16.855 17.581  1.00 41.55 ? 87  TRP A CG  1 
ATOM   693  C CD1 . TRP A  1 87  ? -50.102 -18.115 17.123  1.00 42.25 ? 87  TRP A CD1 1 
ATOM   694  C CD2 . TRP A  1 87  ? -50.699 -15.969 16.866  1.00 43.30 ? 87  TRP A CD2 1 
ATOM   695  N NE1 . TRP A  1 87  ? -51.088 -18.065 16.165  1.00 44.19 ? 87  TRP A NE1 1 
ATOM   696  C CE2 . TRP A  1 87  ? -51.473 -16.761 15.989  1.00 44.45 ? 87  TRP A CE2 1 
ATOM   697  C CE3 . TRP A  1 87  ? -50.900 -14.584 16.880  1.00 42.49 ? 87  TRP A CE3 1 
ATOM   698  C CZ2 . TRP A  1 87  ? -52.431 -16.212 15.136  1.00 45.49 ? 87  TRP A CZ2 1 
ATOM   699  C CZ3 . TRP A  1 87  ? -51.852 -14.042 16.034  1.00 44.14 ? 87  TRP A CZ3 1 
ATOM   700  C CH2 . TRP A  1 87  ? -52.605 -14.854 15.174  1.00 45.60 ? 87  TRP A CH2 1 
ATOM   701  N N   . LEU A  1 88  ? -45.975 -17.850 18.261  1.00 36.53 ? 88  LEU A N   1 
ATOM   702  C CA  . LEU A  1 88  ? -44.979 -18.524 17.431  1.00 36.71 ? 88  LEU A CA  1 
ATOM   703  C C   . LEU A  1 88  ? -44.491 -19.812 18.083  1.00 37.24 ? 88  LEU A C   1 
ATOM   704  O O   . LEU A  1 88  ? -44.207 -20.795 17.388  1.00 38.20 ? 88  LEU A O   1 
ATOM   705  C CB  . LEU A  1 88  ? -43.802 -17.592 17.149  1.00 35.74 ? 88  LEU A CB  1 
ATOM   706  C CG  . LEU A  1 88  ? -42.655 -18.158 16.308  1.00 34.45 ? 88  LEU A CG  1 
ATOM   707  C CD1 . LEU A  1 88  ? -43.129 -18.505 14.904  1.00 34.50 ? 88  LEU A CD1 1 
ATOM   708  C CD2 . LEU A  1 88  ? -41.495 -17.176 16.261  1.00 33.64 ? 88  LEU A CD2 1 
ATOM   709  N N   . LYS A  1 89  ? -44.379 -19.827 19.414  1.00 36.76 ? 89  LYS A N   1 
ATOM   710  C CA  . LYS A  1 89  ? -43.981 -21.054 20.097  1.00 37.91 ? 89  LYS A CA  1 
ATOM   711  C C   . LYS A  1 89  ? -44.996 -22.167 19.860  1.00 38.73 ? 89  LYS A C   1 
ATOM   712  O O   . LYS A  1 89  ? -44.621 -23.325 19.644  1.00 38.94 ? 89  LYS A O   1 
ATOM   713  C CB  . LYS A  1 89  ? -43.805 -20.792 21.596  1.00 38.90 ? 89  LYS A CB  1 
ATOM   714  C CG  . LYS A  1 89  ? -42.660 -19.838 21.940  1.00 39.30 ? 89  LYS A CG  1 
ATOM   715  C CD  . LYS A  1 89  ? -42.606 -19.524 23.436  1.00 41.26 ? 89  LYS A CD  1 
ATOM   716  C CE  . LYS A  1 89  ? -42.319 -20.775 24.269  1.00 45.02 ? 89  LYS A CE  1 
ATOM   717  N NZ  . LYS A  1 89  ? -42.160 -20.464 25.722  1.00 47.30 ? 89  LYS A NZ  1 
ATOM   718  N N   . ARG A  1 90  ? -46.288 -21.829 19.876  1.00 38.59 ? 90  ARG A N   1 
ATOM   719  C CA  . ARG A  1 90  ? -47.337 -22.829 19.697  1.00 38.47 ? 90  ARG A CA  1 
ATOM   720  C C   . ARG A  1 90  ? -47.371 -23.430 18.295  1.00 39.76 ? 90  ARG A C   1 
ATOM   721  O O   . ARG A  1 90  ? -47.913 -24.529 18.130  1.00 41.74 ? 90  ARG A O   1 
ATOM   722  C CB  . ARG A  1 90  ? -48.705 -22.230 20.025  1.00 37.49 ? 90  ARG A CB  1 
ATOM   723  C CG  . ARG A  1 90  ? -48.914 -21.921 21.498  1.00 37.43 ? 90  ARG A CG  1 
ATOM   724  C CD  . ARG A  1 90  ? -50.385 -21.635 21.794  1.00 38.71 ? 90  ARG A CD  1 
ATOM   725  N NE  . ARG A  1 90  ? -50.857 -20.424 21.131  1.00 39.89 ? 90  ARG A NE  1 
ATOM   726  C CZ  . ARG A  1 90  ? -52.095 -19.955 21.219  1.00 38.63 ? 90  ARG A CZ  1 
ATOM   727  N NH1 . ARG A  1 90  ? -53.026 -20.589 21.914  1.00 37.47 ? 90  ARG A NH1 1 
ATOM   728  N NH2 . ARG A  1 90  ? -52.405 -18.821 20.596  1.00 36.23 ? 90  ARG A NH2 1 
ATOM   729  N N   . LEU A  1 91  ? -46.817 -22.751 17.290  1.00 39.21 ? 91  LEU A N   1 
ATOM   730  C CA  . LEU A  1 91  ? -46.954 -23.207 15.912  1.00 40.61 ? 91  LEU A CA  1 
ATOM   731  C C   . LEU A  1 91  ? -46.224 -24.534 15.689  1.00 42.43 ? 91  LEU A C   1 
ATOM   732  O O   . LEU A  1 91  ? -45.487 -25.026 16.546  1.00 42.97 ? 91  LEU A O   1 
ATOM   733  C CB  . LEU A  1 91  ? -46.431 -22.145 14.951  1.00 40.67 ? 91  LEU A CB  1 
ATOM   734  C CG  . LEU A  1 91  ? -47.175 -20.811 14.957  1.00 40.76 ? 91  LEU A CG  1 
ATOM   735  C CD1 . LEU A  1 91  ? -46.512 -19.834 13.996  1.00 39.27 ? 91  LEU A CD1 1 
ATOM   736  C CD2 . LEU A  1 91  ? -48.640 -21.010 14.606  1.00 41.89 ? 91  LEU A CD2 1 
ATOM   737  N N   . LYS A  1 92  ? -46.441 -25.116 14.509  1.00 43.75 ? 92  LYS A N   1 
ATOM   738  C CA  . LYS A  1 92  ? -45.850 -26.397 14.139  1.00 44.20 ? 92  LYS A CA  1 
ATOM   739  C C   . LYS A  1 92  ? -44.945 -26.246 12.922  1.00 44.72 ? 92  LYS A C   1 
ATOM   740  O O   . LYS A  1 92  ? -44.887 -25.197 12.272  1.00 45.45 ? 92  LYS A O   1 
ATOM   741  C CB  . LYS A  1 92  ? -46.924 -27.454 13.837  1.00 45.38 ? 92  LYS A CB  1 
ATOM   742  C CG  . LYS A  1 92  ? -47.746 -27.913 15.030  1.00 46.03 ? 92  LYS A CG  1 
ATOM   743  C CD  . LYS A  1 92  ? -48.738 -28.990 14.608  1.00 47.29 ? 92  LYS A CD  1 
ATOM   744  C CE  . LYS A  1 92  ? -49.570 -29.492 15.780  1.00 50.81 ? 92  LYS A CE  1 
ATOM   745  N NZ  . LYS A  1 92  ? -50.513 -30.585 15.394  1.00 54.08 ? 92  LYS A NZ  1 
ATOM   746  N N   . LYS A  1 93  ? -44.219 -27.325 12.636  1.00 44.03 ? 93  LYS A N   1 
ATOM   747  C CA  . LYS A  1 93  ? -43.430 -27.408 11.416  1.00 43.76 ? 93  LYS A CA  1 
ATOM   748  C C   . LYS A  1 93  ? -44.351 -27.480 10.210  1.00 44.16 ? 93  LYS A C   1 
ATOM   749  O O   . LYS A  1 93  ? -45.378 -28.162 10.232  1.00 44.82 ? 93  LYS A O   1 
ATOM   750  C CB  . LYS A  1 93  ? -42.525 -28.637 11.446  1.00 43.25 ? 93  LYS A CB  1 
ATOM   751  C CG  . LYS A  1 93  ? -41.732 -28.794 12.726  1.00 41.84 ? 93  LYS A CG  1 
ATOM   752  C CD  . LYS A  1 93  ? -41.409 -30.256 12.966  1.00 40.69 ? 93  LYS A CD  1 
ATOM   753  C CE  . LYS A  1 93  ? -42.685 -31.077 13.125  1.00 39.74 ? 93  LYS A CE  1 
ATOM   754  N NZ  . LYS A  1 93  ? -43.469 -30.685 14.333  1.00 38.61 ? 93  LYS A NZ  1 
ATOM   755  N N   . GLY A  1 94  ? -43.980 -26.774 9.151   1.00 45.34 ? 94  GLY A N   1 
ATOM   756  C CA  . GLY A  1 94  ? -44.820 -26.658 7.985   1.00 46.37 ? 94  GLY A CA  1 
ATOM   757  C C   . GLY A  1 94  ? -45.749 -25.464 7.999   1.00 46.53 ? 94  GLY A C   1 
ATOM   758  O O   . GLY A  1 94  ? -46.192 -25.027 6.931   1.00 46.48 ? 94  GLY A O   1 
ATOM   759  N N   . GLU A  1 95  ? -46.053 -24.916 9.175   1.00 46.20 ? 95  GLU A N   1 
ATOM   760  C CA  . GLU A  1 95  ? -46.771 -23.650 9.239   1.00 45.60 ? 95  GLU A CA  1 
ATOM   761  C C   . GLU A  1 95  ? -45.775 -22.518 9.053   1.00 43.14 ? 95  GLU A C   1 
ATOM   762  O O   . GLU A  1 95  ? -45.699 -21.597 9.873   1.00 41.68 ? 95  GLU A O   1 
ATOM   763  C CB  . GLU A  1 95  ? -47.516 -23.493 10.564  1.00 46.61 ? 95  GLU A CB  1 
ATOM   764  C CG  . GLU A  1 95  ? -48.713 -24.405 10.715  1.00 48.45 ? 95  GLU A CG  1 
ATOM   765  C CD  . GLU A  1 95  ? -49.638 -23.961 11.835  1.00 49.55 ? 95  GLU A CD  1 
ATOM   766  O OE1 . GLU A  1 95  ? -49.245 -24.072 13.020  1.00 48.68 ? 95  GLU A OE1 1 
ATOM   767  O OE2 . GLU A  1 95  ? -50.756 -23.488 11.524  1.00 51.34 ? 95  GLU A OE2 1 
ATOM   768  N N   . THR A  1 96  ? -44.999 -22.595 7.973   1.00 42.96 ? 96  THR A N   1 
ATOM   769  C CA  . THR A  1 96  ? -43.973 -21.605 7.692   1.00 41.30 ? 96  THR A CA  1 
ATOM   770  C C   . THR A  1 96  ? -44.556 -20.297 7.180   1.00 39.16 ? 96  THR A C   1 
ATOM   771  O O   . THR A  1 96  ? -43.865 -19.274 7.201   1.00 38.17 ? 96  THR A O   1 
ATOM   772  C CB  . THR A  1 96  ? -42.974 -22.179 6.686   1.00 41.26 ? 96  THR A CB  1 
ATOM   773  O OG1 . THR A  1 96  ? -43.662 -22.553 5.487   1.00 41.42 ? 96  THR A OG1 1 
ATOM   774  C CG2 . THR A  1 96  ? -42.296 -23.417 7.273   1.00 41.73 ? 96  THR A CG2 1 
ATOM   775  N N   . TRP A  1 97  ? -45.807 -20.307 6.719   1.00 39.55 ? 97  TRP A N   1 
ATOM   776  C CA  . TRP A  1 97  ? -46.470 -19.060 6.357   1.00 39.36 ? 97  TRP A CA  1 
ATOM   777  C C   . TRP A  1 97  ? -46.750 -18.220 7.599   1.00 38.13 ? 97  TRP A C   1 
ATOM   778  O O   . TRP A  1 97  ? -46.421 -17.028 7.645   1.00 37.10 ? 97  TRP A O   1 
ATOM   779  C CB  . TRP A  1 97  ? -47.758 -19.369 5.589   1.00 40.15 ? 97  TRP A CB  1 
ATOM   780  C CG  . TRP A  1 97  ? -48.576 -18.169 5.216   1.00 40.13 ? 97  TRP A CG  1 
ATOM   781  C CD1 . TRP A  1 97  ? -49.510 -17.546 5.990   1.00 40.16 ? 97  TRP A CD1 1 
ATOM   782  C CD2 . TRP A  1 97  ? -48.551 -17.458 3.969   1.00 39.92 ? 97  TRP A CD2 1 
ATOM   783  N NE1 . TRP A  1 97  ? -50.061 -16.488 5.310   1.00 40.03 ? 97  TRP A NE1 1 
ATOM   784  C CE2 . TRP A  1 97  ? -49.490 -16.411 4.067   1.00 40.15 ? 97  TRP A CE2 1 
ATOM   785  C CE3 . TRP A  1 97  ? -47.822 -17.602 2.784   1.00 39.90 ? 97  TRP A CE3 1 
ATOM   786  C CZ2 . TRP A  1 97  ? -49.720 -15.512 3.024   1.00 39.48 ? 97  TRP A CZ2 1 
ATOM   787  C CZ3 . TRP A  1 97  ? -48.052 -16.709 1.750   1.00 39.91 ? 97  TRP A CZ3 1 
ATOM   788  C CH2 . TRP A  1 97  ? -48.994 -15.677 1.878   1.00 39.87 ? 97  TRP A CH2 1 
ATOM   789  N N   . LEU A  1 98  ? -47.334 -18.839 8.630   1.00 38.76 ? 98  LEU A N   1 
ATOM   790  C CA  . LEU A  1 98  ? -47.615 -18.142 9.880   1.00 38.09 ? 98  LEU A CA  1 
ATOM   791  C C   . LEU A  1 98  ? -46.367 -17.911 10.720  1.00 36.95 ? 98  LEU A C   1 
ATOM   792  O O   . LEU A  1 98  ? -46.369 -17.017 11.575  1.00 36.18 ? 98  LEU A O   1 
ATOM   793  C CB  . LEU A  1 98  ? -48.643 -18.920 10.707  1.00 39.04 ? 98  LEU A CB  1 
ATOM   794  C CG  . LEU A  1 98  ? -50.033 -19.100 10.092  1.00 40.43 ? 98  LEU A CG  1 
ATOM   795  C CD1 . LEU A  1 98  ? -50.244 -20.533 9.611   1.00 43.06 ? 98  LEU A CD1 1 
ATOM   796  C CD2 . LEU A  1 98  ? -51.121 -18.692 11.076  1.00 41.84 ? 98  LEU A CD2 1 
ATOM   797  N N   . ALA A  1 99  ? -45.312 -18.704 10.515  1.00 36.91 ? 99  ALA A N   1 
ATOM   798  C CA  . ALA A  1 99  ? -44.064 -18.456 11.228  1.00 35.25 ? 99  ALA A CA  1 
ATOM   799  C C   . ALA A  1 99  ? -43.349 -17.227 10.683  1.00 33.41 ? 99  ALA A C   1 
ATOM   800  O O   . ALA A  1 99  ? -42.761 -16.462 11.455  1.00 31.71 ? 99  ALA A O   1 
ATOM   801  C CB  . ALA A  1 99  ? -43.161 -19.686 11.150  1.00 36.05 ? 99  ALA A CB  1 
ATOM   802  N N   . ILE A  1 100 ? -43.407 -17.012 9.367   1.00 34.27 ? 100 ILE A N   1 
ATOM   803  C CA  . ILE A  1 100 ? -42.849 -15.796 8.787   1.00 32.85 ? 100 ILE A CA  1 
ATOM   804  C C   . ILE A  1 100 ? -43.696 -14.592 9.165   1.00 31.45 ? 100 ILE A C   1 
ATOM   805  O O   . ILE A  1 100 ? -43.168 -13.529 9.509   1.00 30.07 ? 100 ILE A O   1 
ATOM   806  C CB  . ILE A  1 100 ? -42.730 -15.933 7.258   1.00 33.04 ? 100 ILE A CB  1 
ATOM   807  C CG1 . ILE A  1 100 ? -41.751 -17.046 6.889   1.00 33.18 ? 100 ILE A CG1 1 
ATOM   808  C CG2 . ILE A  1 100 ? -42.300 -14.608 6.631   1.00 31.90 ? 100 ILE A CG2 1 
ATOM   809  C CD1 . ILE A  1 100 ? -41.802 -17.442 5.440   1.00 34.13 ? 100 ILE A CD1 1 
ATOM   810  N N   . ALA A  1 101 ? -45.021 -14.740 9.104   1.00 32.13 ? 101 ALA A N   1 
ATOM   811  C CA  . ALA A  1 101 ? -45.909 -13.616 9.371   1.00 31.63 ? 101 ALA A CA  1 
ATOM   812  C C   . ALA A  1 101 ? -45.753 -13.107 10.798  1.00 31.18 ? 101 ALA A C   1 
ATOM   813  O O   . ALA A  1 101 ? -45.685 -11.894 11.027  1.00 31.28 ? 101 ALA A O   1 
ATOM   814  C CB  . ALA A  1 101 ? -47.357 -14.021 9.102   1.00 32.72 ? 101 ALA A CB  1 
ATOM   815  N N   . LEU A  1 102 ? -45.692 -14.017 11.772  1.00 31.21 ? 102 LEU A N   1 
ATOM   816  C CA  . LEU A  1 102 ? -45.509 -13.593 13.155  1.00 30.14 ? 102 LEU A CA  1 
ATOM   817  C C   . LEU A  1 102 ? -44.140 -12.958 13.362  1.00 29.68 ? 102 LEU A C   1 
ATOM   818  O O   . LEU A  1 102 ? -44.017 -11.956 14.076  1.00 28.82 ? 102 LEU A O   1 
ATOM   819  C CB  . LEU A  1 102 ? -45.708 -14.776 14.099  1.00 31.62 ? 102 LEU A CB  1 
ATOM   820  C CG  . LEU A  1 102 ? -47.163 -15.213 14.265  1.00 34.16 ? 102 LEU A CG  1 
ATOM   821  C CD1 . LEU A  1 102 ? -47.255 -16.411 15.194  1.00 37.40 ? 102 LEU A CD1 1 
ATOM   822  C CD2 . LEU A  1 102 ? -48.014 -14.061 14.780  1.00 34.12 ? 102 LEU A CD2 1 
ATOM   823  N N   . ALA A  1 103 ? -43.100 -13.523 12.745  1.00 29.83 ? 103 ALA A N   1 
ATOM   824  C CA  . ALA A  1 103 ? -41.768 -12.939 12.867  1.00 29.02 ? 103 ALA A CA  1 
ATOM   825  C C   . ALA A  1 103 ? -41.704 -11.557 12.223  1.00 28.04 ? 103 ALA A C   1 
ATOM   826  O O   . ALA A  1 103 ? -41.032 -10.656 12.739  1.00 27.63 ? 103 ALA A O   1 
ATOM   827  C CB  . ALA A  1 103 ? -40.723 -13.871 12.253  1.00 29.61 ? 103 ALA A CB  1 
ATOM   828  N N   . LEU A  1 104 ? -42.384 -11.375 11.087  1.00 28.67 ? 104 LEU A N   1 
ATOM   829  C CA  . LEU A  1 104 ? -42.392 -10.073 10.426  1.00 27.53 ? 104 LEU A CA  1 
ATOM   830  C C   . LEU A  1 104 ? -43.067 -9.018  11.292  1.00 26.84 ? 104 LEU A C   1 
ATOM   831  O O   . LEU A  1 104 ? -42.516 -7.933  11.507  1.00 26.90 ? 104 LEU A O   1 
ATOM   832  C CB  . LEU A  1 104 ? -43.086 -10.174 9.069   1.00 27.63 ? 104 LEU A CB  1 
ATOM   833  C CG  . LEU A  1 104 ? -42.253 -10.805 7.957   1.00 28.79 ? 104 LEU A CG  1 
ATOM   834  C CD1 . LEU A  1 104 ? -43.103 -11.019 6.726   1.00 30.97 ? 104 LEU A CD1 1 
ATOM   835  C CD2 . LEU A  1 104 ? -41.057 -9.927  7.635   1.00 29.76 ? 104 LEU A CD2 1 
ATOM   836  N N   . VAL A  1 105 ? -44.265 -9.318  11.797  1.00 27.68 ? 105 VAL A N   1 
ATOM   837  C CA  . VAL A  1 105 ? -44.992 -8.341  12.605  1.00 27.37 ? 105 VAL A CA  1 
ATOM   838  C C   . VAL A  1 105 ? -44.254 -8.063  13.906  1.00 26.95 ? 105 VAL A C   1 
ATOM   839  O O   . VAL A  1 105 ? -44.185 -6.915  14.364  1.00 27.52 ? 105 VAL A O   1 
ATOM   840  C CB  . VAL A  1 105 ? -46.433 -8.818  12.865  1.00 27.85 ? 105 VAL A CB  1 
ATOM   841  C CG1 . VAL A  1 105 ? -47.100 -7.935  13.908  1.00 28.23 ? 105 VAL A CG1 1 
ATOM   842  C CG2 . VAL A  1 105 ? -47.231 -8.797  11.581  1.00 29.57 ? 105 VAL A CG2 1 
ATOM   843  N N   . LEU A  1 106 ? -43.698 -9.106  14.526  1.00 26.99 ? 106 LEU A N   1 
ATOM   844  C CA  . LEU A  1 106 ? -42.974 -8.925  15.782  1.00 26.11 ? 106 LEU A CA  1 
ATOM   845  C C   . LEU A  1 106 ? -41.736 -8.059  15.586  1.00 25.82 ? 106 LEU A C   1 
ATOM   846  O O   . LEU A  1 106 ? -41.480 -7.136  16.368  1.00 25.32 ? 106 LEU A O   1 
ATOM   847  C CB  . LEU A  1 106 ? -42.591 -10.285 16.365  1.00 26.22 ? 106 LEU A CB  1 
ATOM   848  C CG  . LEU A  1 106 ? -41.736 -10.246 17.630  1.00 25.82 ? 106 LEU A CG  1 
ATOM   849  C CD1 . LEU A  1 106 ? -42.422 -9.436  18.712  1.00 24.79 ? 106 LEU A CD1 1 
ATOM   850  C CD2 . LEU A  1 106 ? -41.448 -11.656 18.119  1.00 28.09 ? 106 LEU A CD2 1 
ATOM   851  N N   . GLY A  1 107 ? -40.962 -8.337  14.535  1.00 25.68 ? 107 GLY A N   1 
ATOM   852  C CA  . GLY A  1 107 ? -39.724 -7.605  14.325  1.00 25.91 ? 107 GLY A CA  1 
ATOM   853  C C   . GLY A  1 107 ? -39.940 -6.118  14.128  1.00 25.01 ? 107 GLY A C   1 
ATOM   854  O O   . GLY A  1 107 ? -39.213 -5.298  14.692  1.00 25.73 ? 107 GLY A O   1 
ATOM   855  N N   . GLY A  1 108 ? -40.943 -5.750  13.331  1.00 25.23 ? 108 GLY A N   1 
ATOM   856  C CA  . GLY A  1 108 ? -41.213 -4.339  13.100  1.00 25.33 ? 108 GLY A CA  1 
ATOM   857  C C   . GLY A  1 108 ? -41.647 -3.611  14.358  1.00 24.81 ? 108 GLY A C   1 
ATOM   858  O O   . GLY A  1 108 ? -41.149 -2.526  14.666  1.00 25.39 ? 108 GLY A O   1 
ATOM   859  N N   . ALA A  1 109 ? -42.577 -4.206  15.111  1.00 24.68 ? 109 ALA A N   1 
ATOM   860  C CA  . ALA A  1 109 ? -43.091 -3.549  16.309  1.00 24.54 ? 109 ALA A CA  1 
ATOM   861  C C   . ALA A  1 109 ? -42.009 -3.373  17.367  1.00 24.16 ? 109 ALA A C   1 
ATOM   862  O O   . ALA A  1 109 ? -42.046 -2.403  18.131  1.00 25.11 ? 109 ALA A O   1 
ATOM   863  C CB  . ALA A  1 109 ? -44.271 -4.338  16.877  1.00 25.02 ? 109 ALA A CB  1 
ATOM   864  N N   . LEU A  1 110 ? -41.045 -4.295  17.432  1.00 25.25 ? 110 LEU A N   1 
ATOM   865  C CA  . LEU A  1 110 ? -39.943 -4.142  18.377  1.00 24.68 ? 110 LEU A CA  1 
ATOM   866  C C   . LEU A  1 110 ? -38.985 -3.041  17.946  1.00 25.42 ? 110 LEU A C   1 
ATOM   867  O O   . LEU A  1 110 ? -38.350 -2.407  18.797  1.00 26.30 ? 110 LEU A O   1 
ATOM   868  C CB  . LEU A  1 110 ? -39.189 -5.461  18.529  1.00 24.65 ? 110 LEU A CB  1 
ATOM   869  C CG  . LEU A  1 110 ? -39.987 -6.638  19.090  1.00 24.78 ? 110 LEU A CG  1 
ATOM   870  C CD1 . LEU A  1 110 ? -39.109 -7.880  19.178  1.00 25.07 ? 110 LEU A CD1 1 
ATOM   871  C CD2 . LEU A  1 110 ? -40.584 -6.293  20.445  1.00 24.87 ? 110 LEU A CD2 1 
ATOM   872  N N   . GLY A  1 111 ? -38.855 -2.816  16.636  1.00 25.76 ? 111 GLY A N   1 
ATOM   873  C CA  . GLY A  1 111 ? -38.018 -1.733  16.148  1.00 26.38 ? 111 GLY A CA  1 
ATOM   874  C C   . GLY A  1 111 ? -38.611 -0.362  16.394  1.00 26.81 ? 111 GLY A C   1 
ATOM   875  O O   . GLY A  1 111 ? -37.875 0.609   16.591  1.00 27.66 ? 111 GLY A O   1 
ATOM   876  N N   . ASN A  1 112 ? -39.938 -0.257  16.379  1.00 26.31 ? 112 ASN A N   1 
ATOM   877  C CA  . ASN A  1 112 ? -40.600 0.989   16.735  1.00 26.62 ? 112 ASN A CA  1 
ATOM   878  C C   . ASN A  1 112 ? -40.791 1.139   18.237  1.00 27.51 ? 112 ASN A C   1 
ATOM   879  O O   . ASN A  1 112 ? -40.812 2.268   18.739  1.00 29.59 ? 112 ASN A O   1 
ATOM   880  C CB  . ASN A  1 112 ? -41.949 1.093   16.021  1.00 26.02 ? 112 ASN A CB  1 
ATOM   881  C CG  . ASN A  1 112 ? -41.800 1.441   14.555  1.00 26.20 ? 112 ASN A CG  1 
ATOM   882  O OD1 . ASN A  1 112 ? -40.774 1.976   14.135  1.00 26.09 ? 112 ASN A OD1 1 
ATOM   883  N ND2 . ASN A  1 112 ? -42.829 1.147   13.769  1.00 27.00 ? 112 ASN A ND2 1 
ATOM   884  N N   . LEU A  1 113 ? -40.937 0.032   18.969  1.00 27.03 ? 113 LEU A N   1 
ATOM   885  C CA  . LEU A  1 113 ? -40.909 0.113   20.425  1.00 27.55 ? 113 LEU A CA  1 
ATOM   886  C C   . LEU A  1 113 ? -39.555 0.609   20.911  1.00 28.63 ? 113 LEU A C   1 
ATOM   887  O O   . LEU A  1 113 ? -39.474 1.368   21.882  1.00 30.40 ? 113 LEU A O   1 
ATOM   888  C CB  . LEU A  1 113 ? -41.235 -1.247  21.039  1.00 27.25 ? 113 LEU A CB  1 
ATOM   889  C CG  . LEU A  1 113 ? -40.881 -1.427  22.517  1.00 27.65 ? 113 LEU A CG  1 
ATOM   890  C CD1 . LEU A  1 113 ? -41.706 -0.499  23.398  1.00 28.86 ? 113 LEU A CD1 1 
ATOM   891  C CD2 . LEU A  1 113 ? -41.068 -2.879  22.927  1.00 27.13 ? 113 LEU A CD2 1 
ATOM   892  N N   . TYR A  1 114 ? -38.478 0.190   20.239  1.00 28.37 ? 114 TYR A N   1 
ATOM   893  C CA  . TYR A  1 114 ? -37.148 0.678   20.586  1.00 29.72 ? 114 TYR A CA  1 
ATOM   894  C C   . TYR A  1 114 ? -37.057 2.188   20.422  1.00 31.19 ? 114 TYR A C   1 
ATOM   895  O O   . TYR A  1 114 ? -36.448 2.873   21.251  1.00 32.89 ? 114 TYR A O   1 
ATOM   896  C CB  . TYR A  1 114 ? -36.091 -0.017  19.725  1.00 28.90 ? 114 TYR A CB  1 
ATOM   897  C CG  . TYR A  1 114 ? -34.687 0.520   19.925  1.00 29.71 ? 114 TYR A CG  1 
ATOM   898  C CD1 . TYR A  1 114 ? -33.874 0.034   20.941  1.00 30.13 ? 114 TYR A CD1 1 
ATOM   899  C CD2 . TYR A  1 114 ? -34.175 1.512   19.095  1.00 30.24 ? 114 TYR A CD2 1 
ATOM   900  C CE1 . TYR A  1 114 ? -32.593 0.521   21.127  1.00 30.01 ? 114 TYR A CE1 1 
ATOM   901  C CE2 . TYR A  1 114 ? -32.896 2.006   19.275  1.00 30.95 ? 114 TYR A CE2 1 
ATOM   902  C CZ  . TYR A  1 114 ? -32.109 1.506   20.292  1.00 30.75 ? 114 TYR A CZ  1 
ATOM   903  O OH  . TYR A  1 114 ? -30.834 1.994   20.474  1.00 31.86 ? 114 TYR A OH  1 
ATOM   904  N N   . ASP A  1 115 ? -37.641 2.724   19.349  1.00 30.99 ? 115 ASP A N   1 
ATOM   905  C CA  . ASP A  1 115 ? -37.664 4.170   19.166  1.00 32.55 ? 115 ASP A CA  1 
ATOM   906  C C   . ASP A  1 115 ? -38.312 4.854   20.361  1.00 34.33 ? 115 ASP A C   1 
ATOM   907  O O   . ASP A  1 115 ? -37.656 5.599   21.096  1.00 35.99 ? 115 ASP A O   1 
ATOM   908  C CB  . ASP A  1 115 ? -38.399 4.529   17.873  1.00 32.96 ? 115 ASP A CB  1 
ATOM   909  C CG  . ASP A  1 115 ? -37.453 4.752   16.709  1.00 33.27 ? 115 ASP A CG  1 
ATOM   910  O OD1 . ASP A  1 115 ? -36.575 3.889   16.487  1.00 33.79 ? 115 ASP A OD1 1 
ATOM   911  O OD2 . ASP A  1 115 ? -37.589 5.784   16.015  1.00 33.09 ? 115 ASP A OD2 1 
ATOM   912  N N   . ARG A  1 116 ? -39.592 4.558   20.604  1.00 33.46 ? 116 ARG A N   1 
ATOM   913  C CA  . ARG A  1 116 ? -40.356 5.259   21.631  1.00 34.53 ? 116 ARG A CA  1 
ATOM   914  C C   . ARG A  1 116 ? -39.732 5.140   23.020  1.00 35.96 ? 116 ARG A C   1 
ATOM   915  O O   . ARG A  1 116 ? -39.959 6.014   23.866  1.00 36.35 ? 116 ARG A O   1 
ATOM   916  C CB  . ARG A  1 116 ? -41.793 4.730   21.647  1.00 33.47 ? 116 ARG A CB  1 
ATOM   917  C CG  . ARG A  1 116 ? -42.531 4.885   20.319  1.00 32.04 ? 116 ARG A CG  1 
ATOM   918  C CD  . ARG A  1 116 ? -44.006 4.553   20.479  1.00 32.48 ? 116 ARG A CD  1 
ATOM   919  N NE  . ARG A  1 116 ? -44.813 5.015   19.355  1.00 32.65 ? 116 ARG A NE  1 
ATOM   920  C CZ  . ARG A  1 116 ? -45.213 4.246   18.351  1.00 32.11 ? 116 ARG A CZ  1 
ATOM   921  N NH1 . ARG A  1 116 ? -44.900 2.961   18.298  1.00 31.36 ? 116 ARG A NH1 1 
ATOM   922  N NH2 . ARG A  1 116 ? -45.949 4.779   17.378  1.00 31.27 ? 116 ARG A NH2 1 
ATOM   923  N N   . MET A  1 117 ? -38.949 4.090   23.275  1.00 36.64 ? 117 MET A N   1 
ATOM   924  C CA  . MET A  1 117 ? -38.264 3.935   24.554  1.00 37.95 ? 117 MET A CA  1 
ATOM   925  C C   . MET A  1 117 ? -36.945 4.692   24.618  1.00 37.61 ? 117 MET A C   1 
ATOM   926  O O   . MET A  1 117 ? -36.498 5.050   25.714  1.00 38.98 ? 117 MET A O   1 
ATOM   927  C CB  . MET A  1 117 ? -37.992 2.455   24.837  1.00 37.92 ? 117 MET A CB  1 
ATOM   928  C CG  . MET A  1 117 ? -39.229 1.594   25.020  1.00 37.79 ? 117 MET A CG  1 
ATOM   929  S SD  . MET A  1 117 ? -39.843 1.576   26.714  1.00 41.27 ? 117 MET A SD  1 
ATOM   930  C CE  . MET A  1 117 ? -40.974 2.969   26.684  1.00 38.83 ? 117 MET A CE  1 
ATOM   931  N N   . VAL A  1 118 ? -36.305 4.932   23.472  1.00 36.82 ? 118 VAL A N   1 
ATOM   932  C CA  . VAL A  1 118 ? -35.019 5.621   23.427  1.00 37.33 ? 118 VAL A CA  1 
ATOM   933  C C   . VAL A  1 118 ? -35.225 7.090   23.076  1.00 38.01 ? 118 VAL A C   1 
ATOM   934  O O   . VAL A  1 118 ? -34.782 7.983   23.808  1.00 38.60 ? 118 VAL A O   1 
ATOM   935  C CB  . VAL A  1 118 ? -34.063 4.945   22.426  1.00 35.86 ? 118 VAL A CB  1 
ATOM   936  C CG1 . VAL A  1 118 ? -32.796 5.777   22.253  1.00 36.49 ? 118 VAL A CG1 1 
ATOM   937  C CG2 . VAL A  1 118 ? -33.724 3.535   22.889  1.00 34.77 ? 118 VAL A CG2 1 
ATOM   938  N N   . LEU A  1 119 ? -35.887 7.350   21.951  1.00 37.82 ? 119 LEU A N   1 
ATOM   939  C CA  . LEU A  1 119 ? -36.184 8.700   21.489  1.00 37.94 ? 119 LEU A CA  1 
ATOM   940  C C   . LEU A  1 119 ? -37.691 8.849   21.343  1.00 37.44 ? 119 LEU A C   1 
ATOM   941  O O   . LEU A  1 119 ? -38.333 8.048   20.655  1.00 37.25 ? 119 LEU A O   1 
ATOM   942  C CB  . LEU A  1 119 ? -35.484 8.989   20.159  1.00 37.64 ? 119 LEU A CB  1 
ATOM   943  C CG  . LEU A  1 119 ? -35.485 7.798   19.197  1.00 37.25 ? 119 LEU A CG  1 
ATOM   944  C CD1 . LEU A  1 119 ? -35.968 8.221   17.821  1.00 36.52 ? 119 LEU A CD1 1 
ATOM   945  C CD2 . LEU A  1 119 ? -34.095 7.191   19.125  1.00 37.81 ? 119 LEU A CD2 1 
ATOM   946  N N   . GLY A  1 120 ? -38.244 9.885   21.966  1.00 36.75 ? 120 GLY A N   1 
ATOM   947  C CA  . GLY A  1 120 ? -39.683 10.066  22.057  1.00 36.65 ? 120 GLY A CA  1 
ATOM   948  C C   . GLY A  1 120 ? -40.507 9.810   20.807  1.00 35.71 ? 120 GLY A C   1 
ATOM   949  O O   . GLY A  1 120 ? -41.692 9.476   20.917  1.00 35.36 ? 120 GLY A O   1 
ATOM   950  N N   . HIS A  1 121 ? -39.911 9.938   19.622  1.00 35.85 ? 121 HIS A N   1 
ATOM   951  C CA  . HIS A  1 121 ? -40.643 9.818   18.366  1.00 35.40 ? 121 HIS A CA  1 
ATOM   952  C C   . HIS A  1 121 ? -40.260 8.546   17.611  1.00 34.81 ? 121 HIS A C   1 
ATOM   953  O O   . HIS A  1 121 ? -39.508 7.690   18.091  1.00 35.30 ? 121 HIS A O   1 
ATOM   954  C CB  . HIS A  1 121 ? -40.402 11.048  17.490  1.00 35.65 ? 121 HIS A CB  1 
ATOM   955  C CG  . HIS A  1 121 ? -38.975 11.489  17.462  1.00 35.64 ? 121 HIS A CG  1 
ATOM   956  N ND1 . HIS A  1 121 ? -38.009 10.845  16.719  1.00 35.49 ? 121 HIS A ND1 1 
ATOM   957  C CD2 . HIS A  1 121 ? -38.345 12.501  18.105  1.00 35.90 ? 121 HIS A CD2 1 
ATOM   958  C CE1 . HIS A  1 121 ? -36.847 11.449  16.896  1.00 35.81 ? 121 HIS A CE1 1 
ATOM   959  N NE2 . HIS A  1 121 ? -37.023 12.456  17.734  1.00 36.59 ? 121 HIS A NE2 1 
ATOM   960  N N   . VAL A  1 122 ? -40.805 8.439   16.400  1.00 33.92 ? 122 VAL A N   1 
ATOM   961  C CA  . VAL A  1 122 ? -40.547 7.327   15.493  1.00 32.76 ? 122 VAL A CA  1 
ATOM   962  C C   . VAL A  1 122 ? -39.997 7.885   14.186  1.00 31.67 ? 122 VAL A C   1 
ATOM   963  O O   . VAL A  1 122 ? -40.629 8.741   13.550  1.00 32.07 ? 122 VAL A O   1 
ATOM   964  C CB  . VAL A  1 122 ? -41.812 6.494   15.242  1.00 31.25 ? 122 VAL A CB  1 
ATOM   965  C CG1 . VAL A  1 122 ? -41.567 5.480   14.150  1.00 30.57 ? 122 VAL A CG1 1 
ATOM   966  C CG2 . VAL A  1 122 ? -42.252 5.799   16.524  1.00 30.47 ? 122 VAL A CG2 1 
ATOM   967  N N   . VAL A  1 123 ? -38.834 7.385   13.780  1.00 31.41 ? 123 VAL A N   1 
ATOM   968  C CA  . VAL A  1 123 ? -38.168 7.839   12.565  1.00 30.53 ? 123 VAL A CA  1 
ATOM   969  C C   . VAL A  1 123 ? -38.827 7.197   11.348  1.00 30.66 ? 123 VAL A C   1 
ATOM   970  O O   . VAL A  1 123 ? -39.072 5.985   11.325  1.00 30.78 ? 123 VAL A O   1 
ATOM   971  C CB  . VAL A  1 123 ? -36.667 7.521   12.629  1.00 28.66 ? 123 VAL A CB  1 
ATOM   972  C CG1 . VAL A  1 123 ? -35.943 8.164   11.466  1.00 28.81 ? 123 VAL A CG1 1 
ATOM   973  C CG2 . VAL A  1 123 ? -36.094 7.988   13.967  1.00 28.58 ? 123 VAL A CG2 1 
ATOM   974  N N   . ASP A  1 124 ? -39.117 8.019   10.335  1.00 30.33 ? 124 ASP A N   1 
ATOM   975  C CA  . ASP A  1 124 ? -39.749 7.603   9.090   1.00 30.43 ? 124 ASP A CA  1 
ATOM   976  C C   . ASP A  1 124 ? -39.064 8.311   7.929   1.00 30.34 ? 124 ASP A C   1 
ATOM   977  O O   . ASP A  1 124 ? -38.757 9.501   8.030   1.00 31.06 ? 124 ASP A O   1 
ATOM   978  C CB  . ASP A  1 124 ? -41.244 7.937   9.106   1.00 30.96 ? 124 ASP A CB  1 
ATOM   979  C CG  . ASP A  1 124 ? -41.975 7.292   10.270  1.00 31.10 ? 124 ASP A CG  1 
ATOM   980  O OD1 . ASP A  1 124 ? -41.731 6.098   10.535  1.00 30.48 ? 124 ASP A OD1 1 
ATOM   981  O OD2 . ASP A  1 124 ? -42.788 7.981   10.926  1.00 31.33 ? 124 ASP A OD2 1 
ATOM   982  N N   . PHE A  1 125 ? -38.825 7.578   6.821   1.00 30.51 ? 125 PHE A N   1 
ATOM   983  C CA  . PHE A  1 125 ? -37.944 8.079   5.766   1.00 30.63 ? 125 PHE A CA  1 
ATOM   984  C C   . PHE A  1 125 ? -38.375 7.685   4.346   1.00 31.85 ? 125 PHE A C   1 
ATOM   985  O O   . PHE A  1 125 ? -37.535 7.639   3.442   1.00 32.30 ? 125 PHE A O   1 
ATOM   986  C CB  . PHE A  1 125 ? -36.505 7.609   6.015   1.00 30.19 ? 125 PHE A CB  1 
ATOM   987  C CG  . PHE A  1 125 ? -36.380 6.131   6.271   1.00 30.41 ? 125 PHE A CG  1 
ATOM   988  C CD1 . PHE A  1 125 ? -36.438 5.228   5.221   1.00 30.69 ? 125 PHE A CD1 1 
ATOM   989  C CD2 . PHE A  1 125 ? -36.190 5.638   7.555   1.00 30.38 ? 125 PHE A CD2 1 
ATOM   990  C CE1 . PHE A  1 125 ? -36.313 3.870   5.436   1.00 30.04 ? 125 PHE A CE1 1 
ATOM   991  C CE2 . PHE A  1 125 ? -36.060 4.268   7.780   1.00 30.07 ? 125 PHE A CE2 1 
ATOM   992  C CZ  . PHE A  1 125 ? -36.126 3.387   6.713   1.00 29.88 ? 125 PHE A CZ  1 
ATOM   993  N N   . ILE A  1 126 ? -39.657 7.412   4.110   1.00 32.38 ? 126 ILE A N   1 
ATOM   994  C CA  . ILE A  1 126 ? -40.136 6.986   2.790   1.00 33.18 ? 126 ILE A CA  1 
ATOM   995  C C   . ILE A  1 126 ? -41.407 7.766   2.463   1.00 34.75 ? 126 ILE A C   1 
ATOM   996  O O   . ILE A  1 126 ? -42.501 7.401   2.910   1.00 34.79 ? 126 ILE A O   1 
ATOM   997  C CB  . ILE A  1 126 ? -40.385 5.474   2.715   1.00 32.18 ? 126 ILE A CB  1 
ATOM   998  C CG1 . ILE A  1 126 ? -39.076 4.706   2.937   1.00 31.41 ? 126 ILE A CG1 1 
ATOM   999  C CG2 . ILE A  1 126 ? -40.973 5.108   1.359   1.00 33.75 ? 126 ILE A CG2 1 
ATOM   1000 C CD1 . ILE A  1 126 ? -39.246 3.225   3.184   1.00 29.50 ? 126 ILE A CD1 1 
ATOM   1001 N N   . LEU A  1 127 ? -41.268 8.825   1.661   1.00 35.77 ? 127 LEU A N   1 
ATOM   1002 C CA  . LEU A  1 127 ? -42.387 9.663   1.228   1.00 36.85 ? 127 LEU A CA  1 
ATOM   1003 C C   . LEU A  1 127 ? -42.825 9.210   -0.162  1.00 38.04 ? 127 LEU A C   1 
ATOM   1004 O O   . LEU A  1 127 ? -42.231 9.601   -1.170  1.00 39.01 ? 127 LEU A O   1 
ATOM   1005 C CB  . LEU A  1 127 ? -41.996 11.139  1.223   1.00 36.08 ? 127 LEU A CB  1 
ATOM   1006 C CG  . LEU A  1 127 ? -43.115 12.107  0.816   1.00 36.70 ? 127 LEU A CG  1 
ATOM   1007 C CD1 . LEU A  1 127 ? -44.093 12.295  1.962   1.00 37.74 ? 127 LEU A CD1 1 
ATOM   1008 C CD2 . LEU A  1 127 ? -42.571 13.446  0.337   1.00 37.01 ? 127 LEU A CD2 1 
ATOM   1009 N N   . VAL A  1 128 ? -43.865 8.383   -0.214  1.00 38.14 ? 128 VAL A N   1 
ATOM   1010 C CA  . VAL A  1 128 ? -44.500 8.000   -1.470  1.00 38.97 ? 128 VAL A CA  1 
ATOM   1011 C C   . VAL A  1 128 ? -45.581 9.025   -1.785  1.00 39.42 ? 128 VAL A C   1 
ATOM   1012 O O   . VAL A  1 128 ? -46.457 9.283   -0.953  1.00 40.37 ? 128 VAL A O   1 
ATOM   1013 C CB  . VAL A  1 128 ? -45.093 6.584   -1.376  1.00 39.11 ? 128 VAL A CB  1 
ATOM   1014 C CG1 . VAL A  1 128 ? -45.855 6.234   -2.646  1.00 38.58 ? 128 VAL A CG1 1 
ATOM   1015 C CG2 . VAL A  1 128 ? -43.998 5.560   -1.091  1.00 37.81 ? 128 VAL A CG2 1 
ATOM   1016 N N   . HIS A  1 129 ? -45.527 9.616   -2.979  1.00 38.98 ? 129 HIS A N   1 
ATOM   1017 C CA  . HIS A  1 129 ? -46.453 10.684  -3.342  1.00 39.45 ? 129 HIS A CA  1 
ATOM   1018 C C   . HIS A  1 129 ? -46.829 10.549  -4.814  1.00 39.70 ? 129 HIS A C   1 
ATOM   1019 O O   . HIS A  1 129 ? -46.424 9.603   -5.497  1.00 39.67 ? 129 HIS A O   1 
ATOM   1020 C CB  . HIS A  1 129 ? -45.851 12.065  -3.026  1.00 39.74 ? 129 HIS A CB  1 
ATOM   1021 C CG  . HIS A  1 129 ? -44.599 12.378  -3.791  1.00 38.80 ? 129 HIS A CG  1 
ATOM   1022 N ND1 . HIS A  1 129 ? -44.536 13.384  -4.731  1.00 37.78 ? 129 HIS A ND1 1 
ATOM   1023 C CD2 . HIS A  1 129 ? -43.363 11.826  -3.747  1.00 38.70 ? 129 HIS A CD2 1 
ATOM   1024 C CE1 . HIS A  1 129 ? -43.316 13.434  -5.236  1.00 37.16 ? 129 HIS A CE1 1 
ATOM   1025 N NE2 . HIS A  1 129 ? -42.585 12.500  -4.657  1.00 37.22 ? 129 HIS A NE2 1 
ATOM   1026 N N   . TRP A  1 130 ? -47.657 11.484  -5.293  1.00 40.16 ? 130 TRP A N   1 
ATOM   1027 C CA  . TRP A  1 130 ? -47.972 11.625  -6.720  1.00 40.21 ? 130 TRP A CA  1 
ATOM   1028 C C   . TRP A  1 130 ? -48.083 13.123  -6.993  1.00 40.32 ? 130 TRP A C   1 
ATOM   1029 O O   . TRP A  1 130 ? -49.158 13.708  -6.827  1.00 40.44 ? 130 TRP A O   1 
ATOM   1030 C CB  . TRP A  1 130 ? -49.247 10.887  -7.117  1.00 40.12 ? 130 TRP A CB  1 
ATOM   1031 C CG  . TRP A  1 130 ? -49.631 11.133  -8.559  1.00 41.83 ? 130 TRP A CG  1 
ATOM   1032 C CD1 . TRP A  1 130 ? -50.692 11.867  -9.017  1.00 42.49 ? 130 TRP A CD1 1 
ATOM   1033 C CD2 . TRP A  1 130 ? -48.934 10.669  -9.725  1.00 42.62 ? 130 TRP A CD2 1 
ATOM   1034 N NE1 . TRP A  1 130 ? -50.704 11.874  -10.394 1.00 42.65 ? 130 TRP A NE1 1 
ATOM   1035 C CE2 . TRP A  1 130 ? -49.636 11.147  -10.852 1.00 42.30 ? 130 TRP A CE2 1 
ATOM   1036 C CE3 . TRP A  1 130 ? -47.789 9.889   -9.925  1.00 42.20 ? 130 TRP A CE3 1 
ATOM   1037 C CZ2 . TRP A  1 130 ? -49.228 10.871  -12.158 1.00 42.24 ? 130 TRP A CZ2 1 
ATOM   1038 C CZ3 . TRP A  1 130 ? -47.387 9.617   -11.222 1.00 41.34 ? 130 TRP A CZ3 1 
ATOM   1039 C CH2 . TRP A  1 130 ? -48.105 10.107  -12.321 1.00 41.44 ? 130 TRP A CH2 1 
ATOM   1040 N N   . GLN A  1 131 ? -46.966 13.731  -7.408  1.00 39.92 ? 131 GLN A N   1 
ATOM   1041 C CA  . GLN A  1 131 ? -46.903 15.171  -7.640  1.00 40.01 ? 131 GLN A CA  1 
ATOM   1042 C C   . GLN A  1 131 ? -47.308 15.918  -6.376  1.00 40.33 ? 131 GLN A C   1 
ATOM   1043 O O   . GLN A  1 131 ? -47.172 15.387  -5.268  1.00 40.39 ? 131 GLN A O   1 
ATOM   1044 C CB  . GLN A  1 131 ? -47.797 15.564  -8.821  1.00 41.22 ? 131 GLN A CB  1 
ATOM   1045 C CG  . GLN A  1 131 ? -47.475 14.814  -10.107 1.00 41.08 ? 131 GLN A CG  1 
ATOM   1046 C CD  . GLN A  1 131 ? -48.524 15.001  -11.191 1.00 40.91 ? 131 GLN A CD  1 
ATOM   1047 O OE1 . GLN A  1 131 ? -49.689 15.286  -10.909 1.00 41.16 ? 131 GLN A OE1 1 
ATOM   1048 N NE2 . GLN A  1 131 ? -48.110 14.836  -12.441 1.00 40.60 ? 131 GLN A NE2 1 
ATOM   1049 N N   . ASN A  1 132 ? -47.802 17.146  -6.521  1.00 40.04 ? 132 ASN A N   1 
ATOM   1050 C CA  . ASN A  1 132 ? -48.359 17.868  -5.384  1.00 39.97 ? 132 ASN A CA  1 
ATOM   1051 C C   . ASN A  1 132 ? -49.801 17.461  -5.079  1.00 41.01 ? 132 ASN A C   1 
ATOM   1052 O O   . ASN A  1 132 ? -50.453 18.103  -4.247  1.00 41.27 ? 132 ASN A O   1 
ATOM   1053 C CB  . ASN A  1 132 ? -48.280 19.378  -5.625  1.00 39.78 ? 132 ASN A CB  1 
ATOM   1054 C CG  . ASN A  1 132 ? -48.441 20.184  -4.344  1.00 39.72 ? 132 ASN A CG  1 
ATOM   1055 O OD1 . ASN A  1 132 ? -48.224 19.672  -3.245  1.00 38.57 ? 132 ASN A OD1 1 
ATOM   1056 N ND2 . ASN A  1 132 ? -48.831 21.447  -4.481  1.00 39.60 ? 132 ASN A ND2 1 
ATOM   1057 N N   . ARG A  1 133 ? -50.310 16.412  -5.733  1.00 41.39 ? 133 ARG A N   1 
ATOM   1058 C CA  . ARG A  1 133 ? -51.702 16.021  -5.535  1.00 41.00 ? 133 ARG A CA  1 
ATOM   1059 C C   . ARG A  1 133 ? -51.918 15.398  -4.158  1.00 39.45 ? 133 ARG A C   1 
ATOM   1060 O O   . ARG A  1 133 ? -52.842 15.787  -3.435  1.00 39.03 ? 133 ARG A O   1 
ATOM   1061 C CB  . ARG A  1 133 ? -52.140 15.078  -6.657  1.00 42.74 ? 133 ARG A CB  1 
ATOM   1062 C CG  . ARG A  1 133 ? -51.884 15.652  -8.049  1.00 43.68 ? 133 ARG A CG  1 
ATOM   1063 C CD  . ARG A  1 133 ? -52.856 15.124  -9.098  1.00 46.52 ? 133 ARG A CD  1 
ATOM   1064 N NE  . ARG A  1 133 ? -54.236 15.478  -8.788  1.00 49.15 ? 133 ARG A NE  1 
ATOM   1065 C CZ  . ARG A  1 133 ? -55.152 14.618  -8.362  1.00 49.71 ? 133 ARG A CZ  1 
ATOM   1066 N NH1 . ARG A  1 133 ? -54.878 13.329  -8.224  1.00 48.20 ? 133 ARG A NH1 1 
ATOM   1067 N NH2 . ARG A  1 133 ? -56.372 15.061  -8.071  1.00 49.90 ? 133 ARG A NH2 1 
ATOM   1068 N N   . TRP A  1 134 ? -51.073 14.442  -3.766  1.00 39.95 ? 134 TRP A N   1 
ATOM   1069 C CA  . TRP A  1 134 ? -51.142 13.895  -2.413  1.00 40.03 ? 134 TRP A CA  1 
ATOM   1070 C C   . TRP A  1 134 ? -49.808 13.263  -2.028  1.00 40.05 ? 134 TRP A C   1 
ATOM   1071 O O   . TRP A  1 134 ? -49.005 12.883  -2.885  1.00 39.40 ? 134 TRP A O   1 
ATOM   1072 C CB  . TRP A  1 134 ? -52.290 12.885  -2.260  1.00 39.20 ? 134 TRP A CB  1 
ATOM   1073 C CG  . TRP A  1 134 ? -52.222 11.667  -3.140  1.00 38.43 ? 134 TRP A CG  1 
ATOM   1074 C CD1 . TRP A  1 134 ? -52.481 11.607  -4.477  1.00 39.19 ? 134 TRP A CD1 1 
ATOM   1075 C CD2 . TRP A  1 134 ? -51.920 10.323  -2.730  1.00 38.26 ? 134 TRP A CD2 1 
ATOM   1076 N NE1 . TRP A  1 134 ? -52.340 10.316  -4.931  1.00 39.31 ? 134 TRP A NE1 1 
ATOM   1077 C CE2 . TRP A  1 134 ? -51.997 9.508   -3.878  1.00 38.30 ? 134 TRP A CE2 1 
ATOM   1078 C CE3 . TRP A  1 134 ? -51.583 9.732   -1.507  1.00 38.98 ? 134 TRP A CE3 1 
ATOM   1079 C CZ2 . TRP A  1 134 ? -51.748 8.135   -3.840  1.00 37.67 ? 134 TRP A CZ2 1 
ATOM   1080 C CZ3 . TRP A  1 134 ? -51.336 8.366   -1.472  1.00 38.80 ? 134 TRP A CZ3 1 
ATOM   1081 C CH2 . TRP A  1 134 ? -51.420 7.585   -2.631  1.00 37.86 ? 134 TRP A CH2 1 
ATOM   1082 N N   . TYR A  1 135 ? -49.589 13.160  -0.714  1.00 39.94 ? 135 TYR A N   1 
ATOM   1083 C CA  . TYR A  1 135 ? -48.340 12.656  -0.143  1.00 39.98 ? 135 TYR A CA  1 
ATOM   1084 C C   . TYR A  1 135 ? -48.665 11.632  0.940   1.00 40.53 ? 135 TYR A C   1 
ATOM   1085 O O   . TYR A  1 135 ? -49.172 11.996  2.006   1.00 41.83 ? 135 TYR A O   1 
ATOM   1086 C CB  . TYR A  1 135 ? -47.498 13.790  0.449   1.00 40.52 ? 135 TYR A CB  1 
ATOM   1087 C CG  . TYR A  1 135 ? -47.034 14.859  -0.519  1.00 40.31 ? 135 TYR A CG  1 
ATOM   1088 C CD1 . TYR A  1 135 ? -47.913 15.824  -1.002  1.00 40.25 ? 135 TYR A CD1 1 
ATOM   1089 C CD2 . TYR A  1 135 ? -45.704 14.934  -0.908  1.00 39.92 ? 135 TYR A CD2 1 
ATOM   1090 C CE1 . TYR A  1 135 ? -47.484 16.812  -1.870  1.00 39.86 ? 135 TYR A CE1 1 
ATOM   1091 C CE2 . TYR A  1 135 ? -45.264 15.917  -1.775  1.00 40.10 ? 135 TYR A CE2 1 
ATOM   1092 C CZ  . TYR A  1 135 ? -46.157 16.853  -2.253  1.00 39.85 ? 135 TYR A CZ  1 
ATOM   1093 O OH  . TYR A  1 135 ? -45.716 17.831  -3.118  1.00 40.33 ? 135 TYR A OH  1 
ATOM   1094 N N   . PHE A  1 136 ? -48.367 10.359  0.679   1.00 40.42 ? 136 PHE A N   1 
ATOM   1095 C CA  . PHE A  1 136 ? -48.523 9.329   1.701   1.00 40.13 ? 136 PHE A CA  1 
ATOM   1096 C C   . PHE A  1 136 ? -47.538 9.579   2.843   1.00 40.23 ? 136 PHE A C   1 
ATOM   1097 O O   . PHE A  1 136 ? -46.412 10.030  2.605   1.00 39.88 ? 136 PHE A O   1 
ATOM   1098 C CB  . PHE A  1 136 ? -48.289 7.940   1.099   1.00 40.58 ? 136 PHE A CB  1 
ATOM   1099 C CG  . PHE A  1 136 ? -48.887 6.807   1.895   1.00 41.30 ? 136 PHE A CG  1 
ATOM   1100 C CD1 . PHE A  1 136 ? -50.246 6.537   1.822   1.00 41.64 ? 136 PHE A CD1 1 
ATOM   1101 C CD2 . PHE A  1 136 ? -48.087 5.990   2.684   1.00 40.71 ? 136 PHE A CD2 1 
ATOM   1102 C CE1 . PHE A  1 136 ? -50.801 5.491   2.537   1.00 41.71 ? 136 PHE A CE1 1 
ATOM   1103 C CE2 . PHE A  1 136 ? -48.638 4.938   3.402   1.00 40.23 ? 136 PHE A CE2 1 
ATOM   1104 C CZ  . PHE A  1 136 ? -49.997 4.690   3.328   1.00 41.09 ? 136 PHE A CZ  1 
ATOM   1105 N N   . PRO A  1 137 ? -47.933 9.308   4.087   1.00 40.40 ? 137 PRO A N   1 
ATOM   1106 C CA  . PRO A  1 137 ? -47.024 9.541   5.216   1.00 40.08 ? 137 PRO A CA  1 
ATOM   1107 C C   . PRO A  1 137 ? -45.776 8.676   5.131   1.00 37.97 ? 137 PRO A C   1 
ATOM   1108 O O   . PRO A  1 137 ? -45.796 7.561   4.604   1.00 37.62 ? 137 PRO A O   1 
ATOM   1109 C CB  . PRO A  1 137 ? -47.875 9.170   6.437   1.00 39.36 ? 137 PRO A CB  1 
ATOM   1110 C CG  . PRO A  1 137 ? -49.285 9.316   5.973   1.00 40.02 ? 137 PRO A CG  1 
ATOM   1111 C CD  . PRO A  1 137 ? -49.272 8.897   4.537   1.00 40.91 ? 137 PRO A CD  1 
ATOM   1112 N N   . ALA A  1 138 ? -44.677 9.213   5.653   1.00 35.97 ? 138 ALA A N   1 
ATOM   1113 C CA  . ALA A  1 138 ? -43.425 8.478   5.664   1.00 33.87 ? 138 ALA A CA  1 
ATOM   1114 C C   . ALA A  1 138 ? -43.509 7.302   6.629   1.00 32.62 ? 138 ALA A C   1 
ATOM   1115 O O   . ALA A  1 138 ? -44.249 7.328   7.616   1.00 33.06 ? 138 ALA A O   1 
ATOM   1116 C CB  . ALA A  1 138 ? -42.264 9.398   6.041   1.00 33.26 ? 138 ALA A CB  1 
ATOM   1117 N N   . PHE A  1 139 ? -42.756 6.253   6.317   1.00 32.02 ? 139 PHE A N   1 
ATOM   1118 C CA  . PHE A  1 139 ? -42.698 5.062   7.150   1.00 31.15 ? 139 PHE A CA  1 
ATOM   1119 C C   . PHE A  1 139 ? -41.277 4.521   7.083   1.00 31.03 ? 139 PHE A C   1 
ATOM   1120 O O   . PHE A  1 139 ? -40.359 5.197   6.610   1.00 30.74 ? 139 PHE A O   1 
ATOM   1121 C CB  . PHE A  1 139 ? -43.761 4.045   6.715   1.00 31.64 ? 139 PHE A CB  1 
ATOM   1122 C CG  . PHE A  1 139 ? -43.774 3.769   5.238   1.00 32.33 ? 139 PHE A CG  1 
ATOM   1123 C CD1 . PHE A  1 139 ? -43.011 2.741   4.705   1.00 31.85 ? 139 PHE A CD1 1 
ATOM   1124 C CD2 . PHE A  1 139 ? -44.560 4.530   4.385   1.00 33.47 ? 139 PHE A CD2 1 
ATOM   1125 C CE1 . PHE A  1 139 ? -43.028 2.480   3.348   1.00 32.02 ? 139 PHE A CE1 1 
ATOM   1126 C CE2 . PHE A  1 139 ? -44.580 4.275   3.028   1.00 33.49 ? 139 PHE A CE2 1 
ATOM   1127 C CZ  . PHE A  1 139 ? -43.813 3.248   2.509   1.00 32.97 ? 139 PHE A CZ  1 
ATOM   1128 N N   . ASN A  1 140 ? -41.081 3.301   7.570   1.00 28.99 ? 140 ASN A N   1 
ATOM   1129 C CA  . ASN A  1 140 ? -39.738 2.748   7.662   1.00 28.72 ? 140 ASN A CA  1 
ATOM   1130 C C   . ASN A  1 140 ? -39.792 1.253   7.372   1.00 28.36 ? 140 ASN A C   1 
ATOM   1131 O O   . ASN A  1 140 ? -40.829 0.713   6.972   1.00 27.80 ? 140 ASN A O   1 
ATOM   1132 C CB  . ASN A  1 140 ? -39.128 3.050   9.037   1.00 28.41 ? 140 ASN A CB  1 
ATOM   1133 C CG  . ASN A  1 140 ? -40.115 2.847   10.171  1.00 28.39 ? 140 ASN A CG  1 
ATOM   1134 O OD1 . ASN A  1 140 ? -41.149 2.200   10.001  1.00 28.09 ? 140 ASN A OD1 1 
ATOM   1135 N ND2 . ASN A  1 140 ? -39.802 3.402   11.334  1.00 28.13 ? 140 ASN A ND2 1 
ATOM   1136 N N   . LEU A  1 141 ? -38.651 0.589   7.561   1.00 27.80 ? 141 LEU A N   1 
ATOM   1137 C CA  . LEU A  1 141 ? -38.582 -0.853  7.365   1.00 27.58 ? 141 LEU A CA  1 
ATOM   1138 C C   . LEU A  1 141 ? -39.441 -1.601  8.374   1.00 28.11 ? 141 LEU A C   1 
ATOM   1139 O O   . LEU A  1 141 ? -39.928 -2.698  8.077   1.00 28.79 ? 141 LEU A O   1 
ATOM   1140 C CB  . LEU A  1 141 ? -37.128 -1.312  7.458   1.00 27.58 ? 141 LEU A CB  1 
ATOM   1141 C CG  . LEU A  1 141 ? -36.548 -1.976  6.210   1.00 28.90 ? 141 LEU A CG  1 
ATOM   1142 C CD1 . LEU A  1 141 ? -36.858 -1.152  4.965   1.00 29.98 ? 141 LEU A CD1 1 
ATOM   1143 C CD2 . LEU A  1 141 ? -35.047 -2.166  6.378   1.00 30.33 ? 141 LEU A CD2 1 
ATOM   1144 N N   . ALA A  1 142 ? -39.628 -1.033  9.567   1.00 27.65 ? 142 ALA A N   1 
ATOM   1145 C CA  . ALA A  1 142 ? -40.463 -1.680  10.571  1.00 27.54 ? 142 ALA A CA  1 
ATOM   1146 C C   . ALA A  1 142 ? -41.926 -1.682  10.143  1.00 27.96 ? 142 ALA A C   1 
ATOM   1147 O O   . ALA A  1 142 ? -42.605 -2.711  10.232  1.00 28.38 ? 142 ALA A O   1 
ATOM   1148 C CB  . ALA A  1 142 ? -40.288 -0.987  11.922  1.00 27.20 ? 142 ALA A CB  1 
ATOM   1149 N N   . ASP A  1 143 ? -42.427 -0.537  9.669   1.00 28.07 ? 143 ASP A N   1 
ATOM   1150 C CA  . ASP A  1 143 ? -43.794 -0.489  9.157   1.00 29.01 ? 143 ASP A CA  1 
ATOM   1151 C C   . ASP A  1 143 ? -43.962 -1.426  7.972   1.00 27.89 ? 143 ASP A C   1 
ATOM   1152 O O   . ASP A  1 143 ? -45.002 -2.079  7.828   1.00 29.90 ? 143 ASP A O   1 
ATOM   1153 C CB  . ASP A  1 143 ? -44.164 0.938   8.754   1.00 29.30 ? 143 ASP A CB  1 
ATOM   1154 C CG  . ASP A  1 143 ? -44.404 1.835   9.946   1.00 29.87 ? 143 ASP A CG  1 
ATOM   1155 O OD1 . ASP A  1 143 ? -43.970 1.474   11.062  1.00 28.90 ? 143 ASP A OD1 1 
ATOM   1156 O OD2 . ASP A  1 143 ? -45.036 2.897   9.766   1.00 30.37 ? 143 ASP A OD2 1 
ATOM   1157 N N   . SER A  1 144 ? -42.947 -1.498  7.109   1.00 29.31 ? 144 SER A N   1 
ATOM   1158 C CA  . SER A  1 144 ? -43.005 -2.409  5.974   1.00 28.39 ? 144 SER A CA  1 
ATOM   1159 C C   . SER A  1 144 ? -43.110 -3.858  6.435   1.00 29.30 ? 144 SER A C   1 
ATOM   1160 O O   . SER A  1 144 ? -43.852 -4.651  5.844   1.00 30.01 ? 144 SER A O   1 
ATOM   1161 C CB  . SER A  1 144 ? -41.779 -2.203  5.086   1.00 27.61 ? 144 SER A CB  1 
ATOM   1162 O OG  . SER A  1 144 ? -41.617 -0.830  4.774   1.00 27.07 ? 144 SER A OG  1 
ATOM   1163 N N   . ALA A  1 145 ? -42.378 -4.223  7.492   1.00 28.64 ? 145 ALA A N   1 
ATOM   1164 C CA  . ALA A  1 145 ? -42.460 -5.586  8.009   1.00 28.56 ? 145 ALA A CA  1 
ATOM   1165 C C   . ALA A  1 145 ? -43.791 -5.839  8.704   1.00 28.72 ? 145 ALA A C   1 
ATOM   1166 O O   . ALA A  1 145 ? -44.362 -6.929  8.584   1.00 29.32 ? 145 ALA A O   1 
ATOM   1167 C CB  . ALA A  1 145 ? -41.299 -5.857  8.962   1.00 27.81 ? 145 ALA A CB  1 
ATOM   1168 N N   . ILE A  1 146 ? -44.298 -4.850  9.440   1.00 28.34 ? 146 ILE A N   1 
ATOM   1169 C CA  . ILE A  1 146 ? -45.589 -5.004  10.106  1.00 29.41 ? 146 ILE A CA  1 
ATOM   1170 C C   . ILE A  1 146 ? -46.700 -5.191  9.080   1.00 30.01 ? 146 ILE A C   1 
ATOM   1171 O O   . ILE A  1 146 ? -47.540 -6.092  9.202   1.00 30.02 ? 146 ILE A O   1 
ATOM   1172 C CB  . ILE A  1 146 ? -45.864 -3.796  11.020  1.00 29.35 ? 146 ILE A CB  1 
ATOM   1173 C CG1 . ILE A  1 146 ? -44.881 -3.779  12.191  1.00 27.67 ? 146 ILE A CG1 1 
ATOM   1174 C CG2 . ILE A  1 146 ? -47.311 -3.802  11.509  1.00 29.67 ? 146 ILE A CG2 1 
ATOM   1175 C CD1 . ILE A  1 146 ? -45.030 -2.582  13.093  1.00 27.36 ? 146 ILE A CD1 1 
ATOM   1176 N N   . THR A  1 147 ? -46.716 -4.341  8.049   1.00 30.06 ? 147 THR A N   1 
ATOM   1177 C CA  . THR A  1 147 ? -47.794 -4.371  7.065   1.00 30.33 ? 147 THR A CA  1 
ATOM   1178 C C   . THR A  1 147 ? -47.797 -5.673  6.270   1.00 30.60 ? 147 THR A C   1 
ATOM   1179 O O   . THR A  1 147 ? -48.866 -6.213  5.958   1.00 31.13 ? 147 THR A O   1 
ATOM   1180 C CB  . THR A  1 147 ? -47.673 -3.170  6.128   1.00 30.19 ? 147 THR A CB  1 
ATOM   1181 O OG1 . THR A  1 147 ? -47.641 -1.965  6.902   1.00 30.02 ? 147 THR A OG1 1 
ATOM   1182 C CG2 . THR A  1 147 ? -48.853 -3.114  5.177   1.00 30.41 ? 147 THR A CG2 1 
ATOM   1183 N N   . VAL A  1 148 ? -46.615 -6.190  5.928   1.00 30.69 ? 148 VAL A N   1 
ATOM   1184 C CA  . VAL A  1 148 ? -46.544 -7.454  5.199   1.00 31.62 ? 148 VAL A CA  1 
ATOM   1185 C C   . VAL A  1 148 ? -47.080 -8.595  6.053   1.00 31.88 ? 148 VAL A C   1 
ATOM   1186 O O   . VAL A  1 148 ? -47.851 -9.437  5.576   1.00 32.20 ? 148 VAL A O   1 
ATOM   1187 C CB  . VAL A  1 148 ? -45.103 -7.728  4.731   1.00 31.79 ? 148 VAL A CB  1 
ATOM   1188 C CG1 . VAL A  1 148 ? -44.963 -9.164  4.246   1.00 32.01 ? 148 VAL A CG1 1 
ATOM   1189 C CG2 . VAL A  1 148 ? -44.709 -6.755  3.628   1.00 32.99 ? 148 VAL A CG2 1 
ATOM   1190 N N   . GLY A  1 149 ? -46.686 -8.639  7.328   1.00 31.44 ? 149 GLY A N   1 
ATOM   1191 C CA  . GLY A  1 149 ? -47.147 -9.703  8.202   1.00 31.40 ? 149 GLY A CA  1 
ATOM   1192 C C   . GLY A  1 149 ? -48.645 -9.684  8.431   1.00 31.71 ? 149 GLY A C   1 
ATOM   1193 O O   . GLY A  1 149 ? -49.267 -10.740 8.578   1.00 32.82 ? 149 GLY A O   1 
ATOM   1194 N N   . ALA A  1 150 ? -49.242 -8.490  8.476   1.00 30.95 ? 150 ALA A N   1 
ATOM   1195 C CA  . ALA A  1 150 ? -50.695 -8.399  8.557   1.00 30.87 ? 150 ALA A CA  1 
ATOM   1196 C C   . ALA A  1 150 ? -51.350 -8.997  7.318   1.00 31.59 ? 150 ALA A C   1 
ATOM   1197 O O   . ALA A  1 150 ? -52.369 -9.691  7.419   1.00 32.07 ? 150 ALA A O   1 
ATOM   1198 C CB  . ALA A  1 150 ? -51.122 -6.943  8.741   1.00 30.47 ? 150 ALA A CB  1 
ATOM   1199 N N   . VAL A  1 151 ? -50.777 -8.736  6.138   1.00 31.56 ? 151 VAL A N   1 
ATOM   1200 C CA  . VAL A  1 151 ? -51.310 -9.293  4.896   1.00 31.03 ? 151 VAL A CA  1 
ATOM   1201 C C   . VAL A  1 151 ? -51.202 -10.811 4.897   1.00 32.59 ? 151 VAL A C   1 
ATOM   1202 O O   . VAL A  1 151 ? -52.135 -11.516 4.489   1.00 33.43 ? 151 VAL A O   1 
ATOM   1203 C CB  . VAL A  1 151 ? -50.587 -8.674  3.687   1.00 29.37 ? 151 VAL A CB  1 
ATOM   1204 C CG1 . VAL A  1 151 ? -50.835 -9.499  2.435   1.00 28.87 ? 151 VAL A CG1 1 
ATOM   1205 C CG2 . VAL A  1 151 ? -51.049 -7.243  3.480   1.00 29.40 ? 151 VAL A CG2 1 
ATOM   1206 N N   . MET A  1 152 ? -50.065 -11.339 5.357   1.00 33.52 ? 152 MET A N   1 
ATOM   1207 C CA  . MET A  1 152 ? -49.889 -12.785 5.417   1.00 34.63 ? 152 MET A CA  1 
ATOM   1208 C C   . MET A  1 152 ? -50.873 -13.435 6.386   1.00 35.19 ? 152 MET A C   1 
ATOM   1209 O O   . MET A  1 152 ? -51.355 -14.543 6.123   1.00 37.12 ? 152 MET A O   1 
ATOM   1210 C CB  . MET A  1 152 ? -48.447 -13.117 5.804   1.00 35.23 ? 152 MET A CB  1 
ATOM   1211 C CG  . MET A  1 152 ? -47.407 -12.555 4.836   1.00 35.09 ? 152 MET A CG  1 
ATOM   1212 S SD  . MET A  1 152 ? -45.724 -13.119 5.168   1.00 35.64 ? 152 MET A SD  1 
ATOM   1213 C CE  . MET A  1 152 ? -45.935 -14.897 5.039   1.00 36.78 ? 152 MET A CE  1 
ATOM   1214 N N   . LEU A  1 153 ? -51.190 -12.768 7.498   1.00 34.06 ? 153 LEU A N   1 
ATOM   1215 C CA  . LEU A  1 153 ? -52.178 -13.312 8.424   1.00 34.09 ? 153 LEU A CA  1 
ATOM   1216 C C   . LEU A  1 153 ? -53.599 -13.155 7.892   1.00 34.46 ? 153 LEU A C   1 
ATOM   1217 O O   . LEU A  1 153 ? -54.436 -14.045 8.082   1.00 35.87 ? 153 LEU A O   1 
ATOM   1218 C CB  . LEU A  1 153 ? -52.045 -12.639 9.788   1.00 32.98 ? 153 LEU A CB  1 
ATOM   1219 C CG  . LEU A  1 153 ? -50.775 -12.990 10.561  1.00 33.16 ? 153 LEU A CG  1 
ATOM   1220 C CD1 . LEU A  1 153 ? -50.776 -12.338 11.934  1.00 34.22 ? 153 LEU A CD1 1 
ATOM   1221 C CD2 . LEU A  1 153 ? -50.637 -14.497 10.682  1.00 34.71 ? 153 LEU A CD2 1 
ATOM   1222 N N   . ALA A  1 154 ? -53.892 -12.033 7.232   1.00 33.85 ? 154 ALA A N   1 
ATOM   1223 C CA  . ALA A  1 154 ? -55.220 -11.834 6.667   1.00 33.69 ? 154 ALA A CA  1 
ATOM   1224 C C   . ALA A  1 154 ? -55.487 -12.753 5.482   1.00 35.45 ? 154 ALA A C   1 
ATOM   1225 O O   . ALA A  1 154 ? -56.653 -13.038 5.184   1.00 37.26 ? 154 ALA A O   1 
ATOM   1226 C CB  . ALA A  1 154 ? -55.405 -10.373 6.256   1.00 33.67 ? 154 ALA A CB  1 
ATOM   1227 N N   . LEU A  1 155 ? -54.441 -13.223 4.801   1.00 35.71 ? 155 LEU A N   1 
ATOM   1228 C CA  . LEU A  1 155 ? -54.572 -14.213 3.742   1.00 36.61 ? 155 LEU A CA  1 
ATOM   1229 C C   . LEU A  1 155 ? -54.314 -15.626 4.250   1.00 39.02 ? 155 LEU A C   1 
ATOM   1230 O O   . LEU A  1 155 ? -54.081 -16.539 3.449   1.00 40.54 ? 155 LEU A O   1 
ATOM   1231 C CB  . LEU A  1 155 ? -53.636 -13.880 2.578   1.00 34.71 ? 155 LEU A CB  1 
ATOM   1232 C CG  . LEU A  1 155 ? -54.034 -12.640 1.771   1.00 32.38 ? 155 LEU A CG  1 
ATOM   1233 C CD1 . LEU A  1 155 ? -53.333 -12.620 0.420   1.00 30.70 ? 155 LEU A CD1 1 
ATOM   1234 C CD2 . LEU A  1 155 ? -55.545 -12.567 1.600   1.00 30.15 ? 155 LEU A CD2 1 
ATOM   1235 N N   . ASP A  1 156 ? -54.325 -15.815 5.569   1.00 39.24 ? 156 ASP A N   1 
ATOM   1236 C CA  . ASP A  1 156 ? -54.310 -17.144 6.157   1.00 40.28 ? 156 ASP A CA  1 
ATOM   1237 C C   . ASP A  1 156 ? -55.686 -17.576 6.642   1.00 41.86 ? 156 ASP A C   1 
ATOM   1238 O O   . ASP A  1 156 ? -55.930 -18.778 6.782   1.00 43.42 ? 156 ASP A O   1 
ATOM   1239 C CB  . ASP A  1 156 ? -53.313 -17.198 7.320   1.00 40.64 ? 156 ASP A CB  1 
ATOM   1240 C CG  . ASP A  1 156 ? -52.817 -18.600 7.589   1.00 43.04 ? 156 ASP A CG  1 
ATOM   1241 O OD1 . ASP A  1 156 ? -51.970 -19.088 6.811   1.00 43.10 ? 156 ASP A OD1 1 
ATOM   1242 O OD2 . ASP A  1 156 ? -53.290 -19.220 8.565   1.00 46.04 ? 156 ASP A OD2 1 
ATOM   1243 N N   . MET A  1 157 ? -56.586 -16.627 6.895   1.00 41.60 ? 157 MET A N   1 
ATOM   1244 C CA  . MET A  1 157 ? -58.001 -16.929 7.054   1.00 43.09 ? 157 MET A CA  1 
ATOM   1245 C C   . MET A  1 157 ? -58.732 -16.985 5.720   1.00 42.82 ? 157 MET A C   1 
ATOM   1246 O O   . MET A  1 157 ? -59.885 -17.431 5.682   1.00 42.17 ? 157 MET A O   1 
ATOM   1247 C CB  . MET A  1 157 ? -58.673 -15.886 7.954   1.00 42.82 ? 157 MET A CB  1 
ATOM   1248 C CG  . MET A  1 157 ? -58.689 -14.495 7.356   1.00 42.89 ? 157 MET A CG  1 
ATOM   1249 S SD  . MET A  1 157 ? -59.961 -13.434 8.065   1.00 50.26 ? 157 MET A SD  1 
ATOM   1250 C CE  . MET A  1 157 ? -59.446 -13.372 9.782   1.00 43.71 ? 157 MET A CE  1 
ATOM   1251 N N   . PHE A  1 158 ? -58.085 -16.549 4.639   1.00 42.33 ? 158 PHE A N   1 
ATOM   1252 C CA  . PHE A  1 158 ? -58.645 -16.589 3.292   1.00 41.60 ? 158 PHE A CA  1 
ATOM   1253 C C   . PHE A  1 158 ? -59.956 -15.806 3.212   1.00 40.46 ? 158 PHE A C   1 
ATOM   1254 O O   . PHE A  1 158 ? -59.957 -14.574 3.188   1.00 39.43 ? 158 PHE A O   1 
ATOM   1255 C CB  . PHE A  1 158 ? -58.862 -18.039 2.837   1.00 42.65 ? 158 PHE A CB  1 
ATOM   1256 C CG  . PHE A  1 158 ? -57.856 -19.015 3.396   1.00 43.65 ? 158 PHE A CG  1 
ATOM   1257 C CD1 . PHE A  1 158 ? -56.503 -18.878 3.121   1.00 43.39 ? 158 PHE A CD1 1 
ATOM   1258 C CD2 . PHE A  1 158 ? -58.268 -20.081 4.186   1.00 45.14 ? 158 PHE A CD2 1 
ATOM   1259 C CE1 . PHE A  1 158 ? -55.579 -19.777 3.634   1.00 44.25 ? 158 PHE A CE1 1 
ATOM   1260 C CE2 . PHE A  1 158 ? -57.350 -20.986 4.700   1.00 44.59 ? 158 PHE A CE2 1 
ATOM   1261 C CZ  . PHE A  1 158 ? -56.005 -20.834 4.423   1.00 44.16 ? 158 PHE A CZ  1 
ATOM   1262 N N   . PRO B  1 2   ? -89.248 -33.745 25.922  1.00 46.23 ? 2   PRO B N   1 
ATOM   1263 C CA  . PRO B  1 2   ? -89.803 -32.518 26.501  1.00 45.74 ? 2   PRO B CA  1 
ATOM   1264 C C   . PRO B  1 2   ? -89.369 -31.274 25.739  1.00 46.05 ? 2   PRO B C   1 
ATOM   1265 O O   . PRO B  1 2   ? -88.483 -31.348 24.889  1.00 47.19 ? 2   PRO B O   1 
ATOM   1266 C CB  . PRO B  1 2   ? -89.226 -32.513 27.917  1.00 46.49 ? 2   PRO B CB  1 
ATOM   1267 C CG  . PRO B  1 2   ? -87.913 -33.195 27.767  1.00 46.57 ? 2   PRO B CG  1 
ATOM   1268 C CD  . PRO B  1 2   ? -88.135 -34.275 26.730  1.00 46.56 ? 2   PRO B CD  1 
ATOM   1269 N N   . ASP B  1 3   ? -89.993 -30.141 26.048  1.00 45.81 ? 3   ASP B N   1 
ATOM   1270 C CA  . ASP B  1 3   ? -89.641 -28.871 25.430  1.00 45.57 ? 3   ASP B CA  1 
ATOM   1271 C C   . ASP B  1 3   ? -88.582 -28.106 26.209  1.00 47.25 ? 3   ASP B C   1 
ATOM   1272 O O   . ASP B  1 3   ? -88.019 -27.142 25.677  1.00 48.10 ? 3   ASP B O   1 
ATOM   1273 C CB  . ASP B  1 3   ? -90.893 -28.009 25.284  1.00 43.10 ? 3   ASP B CB  1 
ATOM   1274 C CG  . ASP B  1 3   ? -92.139 -28.842 25.097  1.00 42.57 ? 3   ASP B CG  1 
ATOM   1275 O OD1 . ASP B  1 3   ? -92.104 -29.779 24.270  1.00 43.73 ? 3   ASP B OD1 1 
ATOM   1276 O OD2 . ASP B  1 3   ? -93.138 -28.583 25.797  1.00 39.76 ? 3   ASP B OD2 1 
ATOM   1277 N N   . VAL B  1 4   ? -88.311 -28.504 27.454  1.00 48.20 ? 4   VAL B N   1 
ATOM   1278 C CA  . VAL B  1 4   ? -87.267 -27.856 28.240  1.00 49.10 ? 4   VAL B CA  1 
ATOM   1279 C C   . VAL B  1 4   ? -85.898 -28.131 27.630  1.00 50.07 ? 4   VAL B C   1 
ATOM   1280 O O   . VAL B  1 4   ? -85.006 -27.272 27.648  1.00 50.35 ? 4   VAL B O   1 
ATOM   1281 C CB  . VAL B  1 4   ? -87.350 -28.315 29.708  1.00 48.98 ? 4   VAL B CB  1 
ATOM   1282 C CG1 . VAL B  1 4   ? -87.307 -29.841 29.798  1.00 50.35 ? 4   VAL B CG1 1 
ATOM   1283 C CG2 . VAL B  1 4   ? -86.235 -27.692 30.532  1.00 48.40 ? 4   VAL B CG2 1 
ATOM   1284 N N   . ASP B  1 5   ? -85.713 -29.328 27.079  1.00 50.28 ? 5   ASP B N   1 
ATOM   1285 C CA  . ASP B  1 5   ? -84.475 -29.694 26.408  1.00 52.12 ? 5   ASP B CA  1 
ATOM   1286 C C   . ASP B  1 5   ? -84.392 -29.158 24.982  1.00 50.63 ? 5   ASP B C   1 
ATOM   1287 O O   . ASP B  1 5   ? -83.310 -29.200 24.385  1.00 49.69 ? 5   ASP B O   1 
ATOM   1288 C CB  . ASP B  1 5   ? -84.329 -31.221 26.399  1.00 52.24 ? 5   ASP B CB  1 
ATOM   1289 C CG  . ASP B  1 5   ? -82.894 -31.678 26.621  1.00 52.76 ? 5   ASP B CG  1 
ATOM   1290 O OD1 . ASP B  1 5   ? -82.250 -31.184 27.574  1.00 52.51 ? 5   ASP B OD1 1 
ATOM   1291 O OD2 . ASP B  1 5   ? -82.417 -32.544 25.854  1.00 52.84 ? 5   ASP B OD2 1 
ATOM   1292 N N   . ARG B  1 6   ? -85.498 -28.655 24.425  1.00 48.98 ? 6   ARG B N   1 
ATOM   1293 C CA  . ARG B  1 6   ? -85.506 -28.298 23.012  1.00 47.85 ? 6   ARG B CA  1 
ATOM   1294 C C   . ARG B  1 6   ? -84.777 -26.992 22.724  1.00 47.56 ? 6   ARG B C   1 
ATOM   1295 O O   . ARG B  1 6   ? -84.245 -26.823 21.622  1.00 49.66 ? 6   ARG B O   1 
ATOM   1296 C CB  . ARG B  1 6   ? -86.940 -28.210 22.486  1.00 47.63 ? 6   ARG B CB  1 
ATOM   1297 C CG  . ARG B  1 6   ? -87.003 -28.296 20.968  1.00 49.52 ? 6   ARG B CG  1 
ATOM   1298 C CD  . ARG B  1 6   ? -88.305 -27.778 20.385  1.00 51.49 ? 6   ARG B CD  1 
ATOM   1299 N NE  . ARG B  1 6   ? -88.147 -27.494 18.962  1.00 55.11 ? 6   ARG B NE  1 
ATOM   1300 C CZ  . ARG B  1 6   ? -89.145 -27.292 18.112  1.00 57.17 ? 6   ARG B CZ  1 
ATOM   1301 N NH1 . ARG B  1 6   ? -90.408 -27.344 18.502  1.00 55.79 ? 6   ARG B NH1 1 
ATOM   1302 N NH2 . ARG B  1 6   ? -88.868 -27.043 16.834  1.00 59.65 ? 6   ARG B NH2 1 
ATOM   1303 N N   . PHE B  1 7   ? -84.745 -26.055 23.672  1.00 45.88 ? 7   PHE B N   1 
ATOM   1304 C CA  . PHE B  1 7   ? -84.173 -24.738 23.415  1.00 44.01 ? 7   PHE B CA  1 
ATOM   1305 C C   . PHE B  1 7   ? -82.922 -24.465 24.238  1.00 44.45 ? 7   PHE B C   1 
ATOM   1306 O O   . PHE B  1 7   ? -82.397 -23.345 24.196  1.00 43.92 ? 7   PHE B O   1 
ATOM   1307 C CB  . PHE B  1 7   ? -85.224 -23.651 23.664  1.00 43.62 ? 7   PHE B CB  1 
ATOM   1308 C CG  . PHE B  1 7   ? -86.506 -23.874 22.911  1.00 45.68 ? 7   PHE B CG  1 
ATOM   1309 C CD1 . PHE B  1 7   ? -86.630 -23.472 21.591  1.00 46.00 ? 7   PHE B CD1 1 
ATOM   1310 C CD2 . PHE B  1 7   ? -87.585 -24.498 23.521  1.00 45.90 ? 7   PHE B CD2 1 
ATOM   1311 C CE1 . PHE B  1 7   ? -87.809 -23.685 20.890  1.00 47.23 ? 7   PHE B CE1 1 
ATOM   1312 C CE2 . PHE B  1 7   ? -88.768 -24.713 22.828  1.00 45.78 ? 7   PHE B CE2 1 
ATOM   1313 C CZ  . PHE B  1 7   ? -88.880 -24.306 21.509  1.00 46.71 ? 7   PHE B CZ  1 
ATOM   1314 N N   . GLY B  1 8   ? -82.424 -25.460 24.971  1.00 45.90 ? 8   GLY B N   1 
ATOM   1315 C CA  . GLY B  1 8   ? -81.219 -25.302 25.764  1.00 45.40 ? 8   GLY B CA  1 
ATOM   1316 C C   . GLY B  1 8   ? -81.387 -24.288 26.875  1.00 44.04 ? 8   GLY B C   1 
ATOM   1317 O O   . GLY B  1 8   ? -82.177 -24.488 27.802  1.00 44.13 ? 8   GLY B O   1 
ATOM   1318 N N   . ARG B  1 9   ? -80.659 -23.179 26.785  1.00 42.76 ? 9   ARG B N   1 
ATOM   1319 C CA  . ARG B  1 9   ? -80.767 -22.100 27.755  1.00 42.81 ? 9   ARG B CA  1 
ATOM   1320 C C   . ARG B  1 9   ? -81.392 -20.844 27.155  1.00 40.56 ? 9   ARG B C   1 
ATOM   1321 O O   . ARG B  1 9   ? -81.340 -19.778 27.779  1.00 39.13 ? 9   ARG B O   1 
ATOM   1322 C CB  . ARG B  1 9   ? -79.387 -21.789 28.338  1.00 44.72 ? 9   ARG B CB  1 
ATOM   1323 C CG  . ARG B  1 9   ? -78.447 -23.002 28.412  1.00 46.53 ? 9   ARG B CG  1 
ATOM   1324 C CD  . ARG B  1 9   ? -78.969 -24.095 29.342  1.00 47.09 ? 9   ARG B CD  1 
ATOM   1325 N NE  . ARG B  1 9   ? -78.099 -25.267 29.336  1.00 49.20 ? 9   ARG B NE  1 
ATOM   1326 C CZ  . ARG B  1 9   ? -78.399 -26.433 28.780  1.00 51.06 ? 9   ARG B CZ  1 
ATOM   1327 N NH1 . ARG B  1 9   ? -79.571 -26.643 28.201  1.00 50.83 ? 9   ARG B NH1 1 
ATOM   1328 N NH2 . ARG B  1 9   ? -77.502 -27.417 28.812  1.00 51.58 ? 9   ARG B NH2 1 
ATOM   1329 N N   . LEU B  1 10  ? -81.980 -20.940 25.962  1.00 39.91 ? 10  LEU B N   1 
ATOM   1330 C CA  . LEU B  1 10  ? -82.659 -19.781 25.391  1.00 38.24 ? 10  LEU B CA  1 
ATOM   1331 C C   . LEU B  1 10  ? -83.822 -19.259 26.237  1.00 38.16 ? 10  LEU B C   1 
ATOM   1332 O O   . LEU B  1 10  ? -83.938 -18.027 26.358  1.00 38.34 ? 10  LEU B O   1 
ATOM   1333 C CB  . LEU B  1 10  ? -83.118 -20.090 23.961  1.00 38.12 ? 10  LEU B CB  1 
ATOM   1334 C CG  . LEU B  1 10  ? -82.154 -19.704 22.832  1.00 36.38 ? 10  LEU B CG  1 
ATOM   1335 C CD1 . LEU B  1 10  ? -80.827 -20.430 22.973  1.00 38.53 ? 10  LEU B CD1 1 
ATOM   1336 C CD2 . LEU B  1 10  ? -82.776 -20.000 21.487  1.00 35.27 ? 10  LEU B CD2 1 
ATOM   1337 N N   . PRO B  1 11  ? -84.688 -20.088 26.851  1.00 38.46 ? 11  PRO B N   1 
ATOM   1338 C CA  . PRO B  1 11  ? -85.822 -19.510 27.603  1.00 38.34 ? 11  PRO B CA  1 
ATOM   1339 C C   . PRO B  1 11  ? -85.411 -18.517 28.676  1.00 38.45 ? 11  PRO B C   1 
ATOM   1340 O O   . PRO B  1 11  ? -86.260 -17.742 29.135  1.00 37.92 ? 11  PRO B O   1 
ATOM   1341 C CB  . PRO B  1 11  ? -86.513 -20.740 28.215  1.00 38.57 ? 11  PRO B CB  1 
ATOM   1342 C CG  . PRO B  1 11  ? -85.520 -21.843 28.118  1.00 39.87 ? 11  PRO B CG  1 
ATOM   1343 C CD  . PRO B  1 11  ? -84.761 -21.562 26.861  1.00 39.71 ? 11  PRO B CD  1 
ATOM   1344 N N   . TRP B  1 12  ? -84.139 -18.512 29.083  1.00 38.69 ? 12  TRP B N   1 
ATOM   1345 C CA  . TRP B  1 12  ? -83.647 -17.493 30.003  1.00 37.88 ? 12  TRP B CA  1 
ATOM   1346 C C   . TRP B  1 12  ? -83.804 -16.087 29.436  1.00 36.52 ? 12  TRP B C   1 
ATOM   1347 O O   . TRP B  1 12  ? -83.930 -15.121 30.197  1.00 36.52 ? 12  TRP B O   1 
ATOM   1348 C CB  . TRP B  1 12  ? -82.185 -17.771 30.337  1.00 38.79 ? 12  TRP B CB  1 
ATOM   1349 C CG  . TRP B  1 12  ? -81.999 -18.955 31.216  1.00 39.98 ? 12  TRP B CG  1 
ATOM   1350 C CD1 . TRP B  1 12  ? -81.609 -20.207 30.841  1.00 40.92 ? 12  TRP B CD1 1 
ATOM   1351 C CD2 . TRP B  1 12  ? -82.203 -19.002 32.632  1.00 40.84 ? 12  TRP B CD2 1 
ATOM   1352 N NE1 . TRP B  1 12  ? -81.551 -21.032 31.940  1.00 42.24 ? 12  TRP B NE1 1 
ATOM   1353 C CE2 . TRP B  1 12  ? -81.913 -20.316 33.051  1.00 42.24 ? 12  TRP B CE2 1 
ATOM   1354 C CE3 . TRP B  1 12  ? -82.597 -18.059 33.586  1.00 39.84 ? 12  TRP B CE3 1 
ATOM   1355 C CZ2 . TRP B  1 12  ? -82.008 -20.711 34.385  1.00 43.41 ? 12  TRP B CZ2 1 
ATOM   1356 C CZ3 . TRP B  1 12  ? -82.692 -18.450 34.908  1.00 40.49 ? 12  TRP B CZ3 1 
ATOM   1357 C CH2 . TRP B  1 12  ? -82.399 -19.765 35.296  1.00 43.17 ? 12  TRP B CH2 1 
ATOM   1358 N N   . LEU B  1 13  ? -83.810 -15.950 28.108  1.00 35.70 ? 13  LEU B N   1 
ATOM   1359 C CA  . LEU B  1 13  ? -83.925 -14.636 27.488  1.00 34.77 ? 13  LEU B CA  1 
ATOM   1360 C C   . LEU B  1 13  ? -85.243 -13.948 27.815  1.00 34.91 ? 13  LEU B C   1 
ATOM   1361 O O   . LEU B  1 13  ? -85.383 -12.752 27.541  1.00 34.22 ? 13  LEU B O   1 
ATOM   1362 C CB  . LEU B  1 13  ? -83.759 -14.763 25.974  1.00 35.22 ? 13  LEU B CB  1 
ATOM   1363 C CG  . LEU B  1 13  ? -82.414 -15.333 25.523  1.00 34.07 ? 13  LEU B CG  1 
ATOM   1364 C CD1 . LEU B  1 13  ? -82.430 -15.617 24.036  1.00 32.74 ? 13  LEU B CD1 1 
ATOM   1365 C CD2 . LEU B  1 13  ? -81.290 -14.376 25.879  1.00 33.79 ? 13  LEU B CD2 1 
ATOM   1366 N N   . TRP B  1 14  ? -86.213 -14.674 28.374  1.00 35.57 ? 14  TRP B N   1 
ATOM   1367 C CA  . TRP B  1 14  ? -87.439 -14.032 28.831  1.00 35.63 ? 14  TRP B CA  1 
ATOM   1368 C C   . TRP B  1 14  ? -87.174 -13.089 29.995  1.00 34.42 ? 14  TRP B C   1 
ATOM   1369 O O   . TRP B  1 14  ? -87.886 -12.091 30.156  1.00 34.52 ? 14  TRP B O   1 
ATOM   1370 C CB  . TRP B  1 14  ? -88.474 -15.089 29.214  1.00 36.30 ? 14  TRP B CB  1 
ATOM   1371 C CG  . TRP B  1 14  ? -89.125 -15.702 28.021  1.00 37.16 ? 14  TRP B CG  1 
ATOM   1372 C CD1 . TRP B  1 14  ? -88.986 -16.983 27.575  1.00 37.79 ? 14  TRP B CD1 1 
ATOM   1373 C CD2 . TRP B  1 14  ? -90.002 -15.047 27.098  1.00 37.63 ? 14  TRP B CD2 1 
ATOM   1374 N NE1 . TRP B  1 14  ? -89.734 -17.170 26.436  1.00 38.44 ? 14  TRP B NE1 1 
ATOM   1375 C CE2 . TRP B  1 14  ? -90.366 -15.995 26.122  1.00 38.26 ? 14  TRP B CE2 1 
ATOM   1376 C CE3 . TRP B  1 14  ? -90.520 -13.751 27.008  1.00 37.19 ? 14  TRP B CE3 1 
ATOM   1377 C CZ2 . TRP B  1 14  ? -91.223 -15.689 25.068  1.00 39.02 ? 14  TRP B CZ2 1 
ATOM   1378 C CZ3 . TRP B  1 14  ? -91.369 -13.449 25.962  1.00 38.63 ? 14  TRP B CZ3 1 
ATOM   1379 C CH2 . TRP B  1 14  ? -91.713 -14.414 25.006  1.00 39.85 ? 14  TRP B CH2 1 
ATOM   1380 N N   . ILE B  1 15  ? -86.164 -13.387 30.816  1.00 33.87 ? 15  ILE B N   1 
ATOM   1381 C CA  . ILE B  1 15  ? -85.723 -12.427 31.823  1.00 33.71 ? 15  ILE B CA  1 
ATOM   1382 C C   . ILE B  1 15  ? -85.235 -11.153 31.149  1.00 33.98 ? 15  ILE B C   1 
ATOM   1383 O O   . ILE B  1 15  ? -85.518 -10.039 31.608  1.00 33.58 ? 15  ILE B O   1 
ATOM   1384 C CB  . ILE B  1 15  ? -84.633 -13.046 32.714  1.00 33.49 ? 15  ILE B CB  1 
ATOM   1385 C CG1 . ILE B  1 15  ? -85.172 -14.285 33.428  1.00 35.31 ? 15  ILE B CG1 1 
ATOM   1386 C CG2 . ILE B  1 15  ? -84.116 -12.024 33.712  1.00 33.99 ? 15  ILE B CG2 1 
ATOM   1387 C CD1 . ILE B  1 15  ? -84.135 -15.009 34.250  1.00 37.48 ? 15  ILE B CD1 1 
ATOM   1388 N N   . THR B  1 16  ? -84.496 -11.301 30.045  1.00 34.25 ? 16  THR B N   1 
ATOM   1389 C CA  . THR B  1 16  ? -84.053 -10.144 29.273  1.00 33.83 ? 16  THR B CA  1 
ATOM   1390 C C   . THR B  1 16  ? -85.240 -9.349  28.746  1.00 33.79 ? 16  THR B C   1 
ATOM   1391 O O   . THR B  1 16  ? -85.229 -8.112  28.767  1.00 33.73 ? 16  THR B O   1 
ATOM   1392 C CB  . THR B  1 16  ? -83.158 -10.604 28.120  1.00 33.35 ? 16  THR B CB  1 
ATOM   1393 O OG1 . THR B  1 16  ? -81.882 -11.001 28.632  1.00 34.37 ? 16  THR B OG1 1 
ATOM   1394 C CG2 . THR B  1 16  ? -82.965 -9.499  27.096  1.00 33.98 ? 16  THR B CG2 1 
ATOM   1395 N N   . VAL B  1 17  ? -86.272 -10.045 28.265  1.00 34.09 ? 17  VAL B N   1 
ATOM   1396 C CA  . VAL B  1 17  ? -87.476 -9.367  27.794  1.00 33.34 ? 17  VAL B CA  1 
ATOM   1397 C C   . VAL B  1 17  ? -88.151 -8.624  28.938  1.00 33.07 ? 17  VAL B C   1 
ATOM   1398 O O   . VAL B  1 17  ? -88.602 -7.484  28.776  1.00 33.07 ? 17  VAL B O   1 
ATOM   1399 C CB  . VAL B  1 17  ? -88.431 -10.374 27.130  1.00 34.19 ? 17  VAL B CB  1 
ATOM   1400 C CG1 . VAL B  1 17  ? -89.695 -9.678  26.661  1.00 35.33 ? 17  VAL B CG1 1 
ATOM   1401 C CG2 . VAL B  1 17  ? -87.742 -11.062 25.967  1.00 36.08 ? 17  VAL B CG2 1 
ATOM   1402 N N   . LEU B  1 18  ? -88.228 -9.255  30.112  1.00 33.25 ? 18  LEU B N   1 
ATOM   1403 C CA  . LEU B  1 18  ? -88.879 -8.619  31.254  1.00 33.53 ? 18  LEU B CA  1 
ATOM   1404 C C   . LEU B  1 18  ? -88.137 -7.358  31.688  1.00 34.08 ? 18  LEU B C   1 
ATOM   1405 O O   . LEU B  1 18  ? -88.754 -6.313  31.918  1.00 34.33 ? 18  LEU B O   1 
ATOM   1406 C CB  . LEU B  1 18  ? -88.991 -9.607  32.414  1.00 34.14 ? 18  LEU B CB  1 
ATOM   1407 C CG  . LEU B  1 18  ? -89.654 -9.034  33.668  1.00 34.72 ? 18  LEU B CG  1 
ATOM   1408 C CD1 . LEU B  1 18  ? -91.079 -8.610  33.357  1.00 35.92 ? 18  LEU B CD1 1 
ATOM   1409 C CD2 . LEU B  1 18  ? -89.621 -10.036 34.816  1.00 35.52 ? 18  LEU B CD2 1 
ATOM   1410 N N   . VAL B  1 19  ? -86.807 -7.437  31.806  1.00 34.05 ? 19  VAL B N   1 
ATOM   1411 C CA  . VAL B  1 19  ? -86.019 -6.279  32.237  1.00 33.39 ? 19  VAL B CA  1 
ATOM   1412 C C   . VAL B  1 19  ? -86.156 -5.139  31.235  1.00 32.29 ? 19  VAL B C   1 
ATOM   1413 O O   . VAL B  1 19  ? -86.332 -3.973  31.608  1.00 31.97 ? 19  VAL B O   1 
ATOM   1414 C CB  . VAL B  1 19  ? -84.545 -6.673  32.444  1.00 32.04 ? 19  VAL B CB  1 
ATOM   1415 C CG1 . VAL B  1 19  ? -83.713 -5.452  32.801  1.00 31.74 ? 19  VAL B CG1 1 
ATOM   1416 C CG2 . VAL B  1 19  ? -84.422 -7.735  33.520  1.00 32.15 ? 19  VAL B CG2 1 
ATOM   1417 N N   . PHE B  1 20  ? -86.073 -5.465  29.944  1.00 32.01 ? 20  PHE B N   1 
ATOM   1418 C CA  . PHE B  1 20  ? -86.240 -4.461  28.900  1.00 31.70 ? 20  PHE B CA  1 
ATOM   1419 C C   . PHE B  1 20  ? -87.633 -3.838  28.943  1.00 32.66 ? 20  PHE B C   1 
ATOM   1420 O O   . PHE B  1 20  ? -87.778 -2.615  28.826  1.00 32.89 ? 20  PHE B O   1 
ATOM   1421 C CB  . PHE B  1 20  ? -85.957 -5.103  27.541  1.00 31.02 ? 20  PHE B CB  1 
ATOM   1422 C CG  . PHE B  1 20  ? -86.288 -4.233  26.372  1.00 31.80 ? 20  PHE B CG  1 
ATOM   1423 C CD1 . PHE B  1 20  ? -85.417 -3.243  25.959  1.00 32.81 ? 20  PHE B CD1 1 
ATOM   1424 C CD2 . PHE B  1 20  ? -87.464 -4.422  25.669  1.00 32.80 ? 20  PHE B CD2 1 
ATOM   1425 C CE1 . PHE B  1 20  ? -85.723 -2.445  24.875  1.00 34.06 ? 20  PHE B CE1 1 
ATOM   1426 C CE2 . PHE B  1 20  ? -87.776 -3.628  24.586  1.00 33.07 ? 20  PHE B CE2 1 
ATOM   1427 C CZ  . PHE B  1 20  ? -86.905 -2.639  24.188  1.00 34.13 ? 20  PHE B CZ  1 
ATOM   1428 N N   . VAL B  1 21  ? -88.670 -4.663  29.121  1.00 33.02 ? 21  VAL B N   1 
ATOM   1429 C CA  . VAL B  1 21  ? -90.037 -4.149  29.198  1.00 33.12 ? 21  VAL B CA  1 
ATOM   1430 C C   . VAL B  1 21  ? -90.240 -3.325  30.464  1.00 33.38 ? 21  VAL B C   1 
ATOM   1431 O O   . VAL B  1 21  ? -90.830 -2.240  30.419  1.00 33.92 ? 21  VAL B O   1 
ATOM   1432 C CB  . VAL B  1 21  ? -91.053 -5.303  29.108  1.00 34.29 ? 21  VAL B CB  1 
ATOM   1433 C CG1 . VAL B  1 21  ? -92.388 -4.891  29.715  1.00 35.68 ? 21  VAL B CG1 1 
ATOM   1434 C CG2 . VAL B  1 21  ? -91.239 -5.728  27.663  1.00 35.24 ? 21  VAL B CG2 1 
ATOM   1435 N N   . LEU B  1 22  ? -89.766 -3.827  31.609  1.00 33.40 ? 22  LEU B N   1 
ATOM   1436 C CA  . LEU B  1 22  ? -89.863 -3.065  32.852  1.00 33.26 ? 22  LEU B CA  1 
ATOM   1437 C C   . LEU B  1 22  ? -89.160 -1.723  32.727  1.00 32.91 ? 22  LEU B C   1 
ATOM   1438 O O   . LEU B  1 22  ? -89.598 -0.722  33.305  1.00 33.31 ? 22  LEU B O   1 
ATOM   1439 C CB  . LEU B  1 22  ? -89.256 -3.855  34.010  1.00 34.05 ? 22  LEU B CB  1 
ATOM   1440 C CG  . LEU B  1 22  ? -89.952 -5.114  34.521  1.00 34.98 ? 22  LEU B CG  1 
ATOM   1441 C CD1 . LEU B  1 22  ? -89.094 -5.761  35.594  1.00 34.55 ? 22  LEU B CD1 1 
ATOM   1442 C CD2 . LEU B  1 22  ? -91.343 -4.801  35.051  1.00 36.04 ? 22  LEU B CD2 1 
ATOM   1443 N N   . ASP B  1 23  ? -88.057 -1.688  31.983  1.00 32.59 ? 23  ASP B N   1 
ATOM   1444 C CA  . ASP B  1 23  ? -87.290 -0.458  31.864  1.00 32.68 ? 23  ASP B CA  1 
ATOM   1445 C C   . ASP B  1 23  ? -88.033 0.596   31.048  1.00 33.04 ? 23  ASP B C   1 
ATOM   1446 O O   . ASP B  1 23  ? -88.066 1.771   31.432  1.00 33.07 ? 23  ASP B O   1 
ATOM   1447 C CB  . ASP B  1 23  ? -85.928 -0.766  31.250  1.00 32.86 ? 23  ASP B CB  1 
ATOM   1448 C CG  . ASP B  1 23  ? -85.149 0.480   30.914  1.00 34.87 ? 23  ASP B CG  1 
ATOM   1449 O OD1 . ASP B  1 23  ? -85.089 1.391   31.770  1.00 35.41 ? 23  ASP B OD1 1 
ATOM   1450 O OD2 . ASP B  1 23  ? -84.593 0.538   29.795  1.00 35.22 ? 23  ASP B OD2 1 
ATOM   1451 N N   . GLN B  1 24  ? -88.647 0.200   29.929  1.00 32.94 ? 24  GLN B N   1 
ATOM   1452 C CA  . GLN B  1 24  ? -89.229 1.175   29.014  1.00 32.96 ? 24  GLN B CA  1 
ATOM   1453 C C   . GLN B  1 24  ? -90.603 1.667   29.447  1.00 33.03 ? 24  GLN B C   1 
ATOM   1454 O O   . GLN B  1 24  ? -91.039 2.721   28.973  1.00 33.02 ? 24  GLN B O   1 
ATOM   1455 C CB  . GLN B  1 24  ? -89.311 0.592   27.602  1.00 34.31 ? 24  GLN B CB  1 
ATOM   1456 C CG  . GLN B  1 24  ? -87.966 0.126   27.051  1.00 35.10 ? 24  GLN B CG  1 
ATOM   1457 C CD  . GLN B  1 24  ? -86.895 1.212   27.076  1.00 36.19 ? 24  GLN B CD  1 
ATOM   1458 O OE1 . GLN B  1 24  ? -87.180 2.397   26.879  1.00 37.06 ? 24  GLN B OE1 1 
ATOM   1459 N NE2 . GLN B  1 24  ? -85.652 0.805   27.318  1.00 35.82 ? 24  GLN B NE2 1 
ATOM   1460 N N   . VAL B  1 25  ? -91.301 0.935   30.317  1.00 33.19 ? 25  VAL B N   1 
ATOM   1461 C CA  . VAL B  1 25  ? -92.530 1.475   30.893  1.00 33.49 ? 25  VAL B CA  1 
ATOM   1462 C C   . VAL B  1 25  ? -92.208 2.502   31.971  1.00 32.56 ? 25  VAL B C   1 
ATOM   1463 O O   . VAL B  1 25  ? -92.852 3.555   32.054  1.00 32.79 ? 25  VAL B O   1 
ATOM   1464 C CB  . VAL B  1 25  ? -93.435 0.348   31.430  1.00 33.31 ? 25  VAL B CB  1 
ATOM   1465 C CG1 . VAL B  1 25  ? -94.018 -0.456  30.285  1.00 36.75 ? 25  VAL B CG1 1 
ATOM   1466 C CG2 . VAL B  1 25  ? -92.684 -0.557  32.393  1.00 33.17 ? 25  VAL B CG2 1 
ATOM   1467 N N   . SER B  1 26  ? -91.208 2.217   32.809  1.00 32.21 ? 26  SER B N   1 
ATOM   1468 C CA  . SER B  1 26  ? -90.802 3.176   33.829  1.00 31.99 ? 26  SER B CA  1 
ATOM   1469 C C   . SER B  1 26  ? -90.275 4.462   33.201  1.00 32.12 ? 26  SER B C   1 
ATOM   1470 O O   . SER B  1 26  ? -90.600 5.564   33.660  1.00 31.93 ? 26  SER B O   1 
ATOM   1471 C CB  . SER B  1 26  ? -89.755 2.542   34.744  1.00 32.60 ? 26  SER B CB  1 
ATOM   1472 O OG  . SER B  1 26  ? -88.888 1.698   34.006  1.00 32.22 ? 26  SER B OG  1 
ATOM   1473 N N   . LYS B  1 27  ? -89.465 4.345   32.143  1.00 32.68 ? 27  LYS B N   1 
ATOM   1474 C CA  . LYS B  1 27  ? -88.937 5.536   31.482  1.00 32.26 ? 27  LYS B CA  1 
ATOM   1475 C C   . LYS B  1 27  ? -90.054 6.389   30.893  1.00 32.46 ? 27  LYS B C   1 
ATOM   1476 O O   . LYS B  1 27  ? -90.049 7.617   31.037  1.00 32.35 ? 27  LYS B O   1 
ATOM   1477 C CB  . LYS B  1 27  ? -87.940 5.139   30.395  1.00 32.38 ? 27  LYS B CB  1 
ATOM   1478 C CG  . LYS B  1 27  ? -86.591 4.705   30.931  1.00 34.00 ? 27  LYS B CG  1 
ATOM   1479 C CD  . LYS B  1 27  ? -85.675 4.273   29.807  1.00 36.24 ? 27  LYS B CD  1 
ATOM   1480 C CE  . LYS B  1 27  ? -84.255 4.066   30.299  1.00 36.58 ? 27  LYS B CE  1 
ATOM   1481 N NZ  . LYS B  1 27  ? -83.352 3.641   29.192  1.00 36.72 ? 27  LYS B NZ  1 
ATOM   1482 N N   . ALA B  1 28  ? -91.030 5.755   30.238  1.00 32.69 ? 28  ALA B N   1 
ATOM   1483 C CA  . ALA B  1 28  ? -92.139 6.512   29.668  1.00 32.14 ? 28  ALA B CA  1 
ATOM   1484 C C   . ALA B  1 28  ? -93.038 7.094   30.751  1.00 31.22 ? 28  ALA B C   1 
ATOM   1485 O O   . ALA B  1 28  ? -93.593 8.185   30.572  1.00 31.68 ? 28  ALA B O   1 
ATOM   1486 C CB  . ALA B  1 28  ? -92.946 5.627   28.716  1.00 31.94 ? 28  ALA B CB  1 
ATOM   1487 N N   . PHE B  1 29  ? -93.199 6.390   31.873  1.00 30.77 ? 29  PHE B N   1 
ATOM   1488 C CA  . PHE B  1 29  ? -94.003 6.929   32.963  1.00 30.40 ? 29  PHE B CA  1 
ATOM   1489 C C   . PHE B  1 29  ? -93.376 8.193   33.531  1.00 31.51 ? 29  PHE B C   1 
ATOM   1490 O O   . PHE B  1 29  ? -94.033 9.235   33.629  1.00 31.84 ? 29  PHE B O   1 
ATOM   1491 C CB  . PHE B  1 29  ? -94.182 5.879   34.059  1.00 31.50 ? 29  PHE B CB  1 
ATOM   1492 C CG  . PHE B  1 29  ? -94.641 6.448   35.375  1.00 33.02 ? 29  PHE B CG  1 
ATOM   1493 C CD1 . PHE B  1 29  ? -95.895 7.028   35.500  1.00 33.35 ? 29  PHE B CD1 1 
ATOM   1494 C CD2 . PHE B  1 29  ? -93.820 6.397   36.489  1.00 34.26 ? 29  PHE B CD2 1 
ATOM   1495 C CE1 . PHE B  1 29  ? -96.315 7.551   36.710  1.00 33.67 ? 29  PHE B CE1 1 
ATOM   1496 C CE2 . PHE B  1 29  ? -94.235 6.918   37.701  1.00 34.79 ? 29  PHE B CE2 1 
ATOM   1497 C CZ  . PHE B  1 29  ? -95.484 7.495   37.810  1.00 34.81 ? 29  PHE B CZ  1 
ATOM   1498 N N   . PHE B  1 30  ? -92.095 8.126   33.891  1.00 31.51 ? 30  PHE B N   1 
ATOM   1499 C CA  . PHE B  1 30  ? -91.450 9.285   34.490  1.00 31.94 ? 30  PHE B CA  1 
ATOM   1500 C C   . PHE B  1 30  ? -91.177 10.379  33.469  1.00 32.25 ? 30  PHE B C   1 
ATOM   1501 O O   . PHE B  1 30  ? -91.012 11.541  33.855  1.00 32.76 ? 30  PHE B O   1 
ATOM   1502 C CB  . PHE B  1 30  ? -90.158 8.869   35.191  1.00 32.18 ? 30  PHE B CB  1 
ATOM   1503 C CG  . PHE B  1 30  ? -90.386 8.225   36.528  1.00 32.91 ? 30  PHE B CG  1 
ATOM   1504 C CD1 . PHE B  1 30  ? -90.957 8.941   37.567  1.00 32.89 ? 30  PHE B CD1 1 
ATOM   1505 C CD2 . PHE B  1 30  ? -90.040 6.903   36.746  1.00 33.70 ? 30  PHE B CD2 1 
ATOM   1506 C CE1 . PHE B  1 30  ? -91.181 8.354   38.799  1.00 34.59 ? 30  PHE B CE1 1 
ATOM   1507 C CE2 . PHE B  1 30  ? -90.260 6.309   37.978  1.00 34.38 ? 30  PHE B CE2 1 
ATOM   1508 C CZ  . PHE B  1 30  ? -90.830 7.035   39.003  1.00 35.55 ? 30  PHE B CZ  1 
ATOM   1509 N N   . GLN B  1 31  ? -91.144 10.038  32.180  1.00 32.25 ? 31  GLN B N   1 
ATOM   1510 C CA  . GLN B  1 31  ? -91.004 11.062  31.151  1.00 32.29 ? 31  GLN B CA  1 
ATOM   1511 C C   . GLN B  1 31  ? -92.254 11.926  31.068  1.00 31.59 ? 31  GLN B C   1 
ATOM   1512 O O   . GLN B  1 31  ? -92.163 13.140  30.853  1.00 31.97 ? 31  GLN B O   1 
ATOM   1513 C CB  . GLN B  1 31  ? -90.707 10.407  29.804  1.00 31.99 ? 31  GLN B CB  1 
ATOM   1514 C CG  . GLN B  1 31  ? -89.653 11.114  28.972  1.00 31.81 ? 31  GLN B CG  1 
ATOM   1515 C CD  . GLN B  1 31  ? -89.169 10.256  27.823  1.00 33.79 ? 31  GLN B CD  1 
ATOM   1516 O OE1 . GLN B  1 31  ? -89.364 9.039   27.821  1.00 34.44 ? 31  GLN B OE1 1 
ATOM   1517 N NE2 . GLN B  1 31  ? -88.537 10.882  26.837  1.00 34.60 ? 31  GLN B NE2 1 
ATOM   1518 N N   . ALA B  1 32  ? -93.429 11.321  31.235  1.00 30.92 ? 32  ALA B N   1 
ATOM   1519 C CA  . ALA B  1 32  ? -94.680 12.061  31.150  1.00 30.66 ? 32  ALA B CA  1 
ATOM   1520 C C   . ALA B  1 32  ? -95.081 12.687  32.479  1.00 32.26 ? 32  ALA B C   1 
ATOM   1521 O O   . ALA B  1 32  ? -95.589 13.813  32.501  1.00 32.73 ? 32  ALA B O   1 
ATOM   1522 C CB  . ALA B  1 32  ? -95.798 11.146  30.651  1.00 30.76 ? 32  ALA B CB  1 
ATOM   1523 N N   . GLU B  1 33  ? -94.867 11.977  33.591  1.00 33.46 ? 33  GLU B N   1 
ATOM   1524 C CA  . GLU B  1 33  ? -95.266 12.498  34.894  1.00 35.34 ? 33  GLU B CA  1 
ATOM   1525 C C   . GLU B  1 33  ? -94.351 13.612  35.388  1.00 36.07 ? 33  GLU B C   1 
ATOM   1526 O O   . GLU B  1 33  ? -94.768 14.405  36.240  1.00 36.99 ? 33  GLU B O   1 
ATOM   1527 C CB  . GLU B  1 33  ? -95.312 11.368  35.925  1.00 36.27 ? 33  GLU B CB  1 
ATOM   1528 C CG  . GLU B  1 33  ? -96.709 11.068  36.440  1.00 39.81 ? 33  GLU B CG  1 
ATOM   1529 C CD  . GLU B  1 33  ? -97.340 12.257  37.145  1.00 44.91 ? 33  GLU B CD  1 
ATOM   1530 O OE1 . GLU B  1 33  ? -96.625 12.951  37.901  1.00 44.36 ? 33  GLU B OE1 1 
ATOM   1531 O OE2 . GLU B  1 33  ? -98.552 12.498  36.938  1.00 48.22 ? 33  GLU B OE2 1 
ATOM   1532 N N   . LEU B  1 34  ? -93.128 13.698  34.877  1.00 35.04 ? 34  LEU B N   1 
ATOM   1533 C CA  . LEU B  1 34  ? -92.172 14.713  35.296  1.00 34.92 ? 34  LEU B CA  1 
ATOM   1534 C C   . LEU B  1 34  ? -91.743 15.570  34.109  1.00 35.01 ? 34  LEU B C   1 
ATOM   1535 O O   . LEU B  1 34  ? -92.158 15.360  32.966  1.00 34.81 ? 34  LEU B O   1 
ATOM   1536 C CB  . LEU B  1 34  ? -90.943 14.081  35.956  1.00 34.58 ? 34  LEU B CB  1 
ATOM   1537 C CG  . LEU B  1 34  ? -91.037 13.695  37.431  1.00 34.04 ? 34  LEU B CG  1 
ATOM   1538 C CD1 . LEU B  1 34  ? -91.574 12.291  37.568  1.00 33.88 ? 34  LEU B CD1 1 
ATOM   1539 C CD2 . LEU B  1 34  ? -89.682 13.826  38.108  1.00 34.94 ? 34  LEU B CD2 1 
ATOM   1540 N N   . SER B  1 35  ? -90.898 16.555  34.410  1.00 35.56 ? 35  SER B N   1 
ATOM   1541 C CA  . SER B  1 35  ? -90.285 17.411  33.404  1.00 36.15 ? 35  SER B CA  1 
ATOM   1542 C C   . SER B  1 35  ? -88.781 17.442  33.631  1.00 37.77 ? 35  SER B C   1 
ATOM   1543 O O   . SER B  1 35  ? -88.279 16.743  34.516  1.00 38.30 ? 35  SER B O   1 
ATOM   1544 C CB  . SER B  1 35  ? -90.874 18.819  33.463  1.00 37.00 ? 35  SER B CB  1 
ATOM   1545 O OG  . SER B  1 35  ? -90.880 19.297  34.795  1.00 37.45 ? 35  SER B OG  1 
ATOM   1546 N N   . MET B  1 36  ? -88.054 18.240  32.850  1.00 38.56 ? 36  MET B N   1 
ATOM   1547 C CA  . MET B  1 36  ? -86.601 18.271  32.968  1.00 39.78 ? 36  MET B CA  1 
ATOM   1548 C C   . MET B  1 36  ? -86.179 18.652  34.380  1.00 40.08 ? 36  MET B C   1 
ATOM   1549 O O   . MET B  1 36  ? -86.637 19.656  34.931  1.00 41.27 ? 36  MET B O   1 
ATOM   1550 C CB  . MET B  1 36  ? -86.010 19.264  31.968  1.00 42.08 ? 36  MET B CB  1 
ATOM   1551 C CG  . MET B  1 36  ? -85.318 18.627  30.770  1.00 45.58 ? 36  MET B CG  1 
ATOM   1552 S SD  . MET B  1 36  ? -83.508 18.691  30.853  1.00 49.47 ? 36  MET B SD  1 
ATOM   1553 C CE  . MET B  1 36  ? -83.099 16.952  31.040  1.00 42.37 ? 36  MET B CE  1 
ATOM   1554 N N   . TYR B  1 37  ? -85.307 17.838  34.967  1.00 39.32 ? 37  TYR B N   1 
ATOM   1555 C CA  . TYR B  1 37  ? -84.648 18.114  36.241  1.00 39.38 ? 37  TYR B CA  1 
ATOM   1556 C C   . TYR B  1 37  ? -85.618 18.232  37.415  1.00 36.97 ? 37  TYR B C   1 
ATOM   1557 O O   . TYR B  1 37  ? -85.193 18.572  38.525  1.00 36.87 ? 37  TYR B O   1 
ATOM   1558 C CB  . TYR B  1 37  ? -83.788 19.387  36.152  1.00 40.65 ? 37  TYR B CB  1 
ATOM   1559 C CG  . TYR B  1 37  ? -82.709 19.358  35.087  1.00 42.96 ? 37  TYR B CG  1 
ATOM   1560 C CD1 . TYR B  1 37  ? -82.144 18.155  34.660  1.00 44.15 ? 37  TYR B CD1 1 
ATOM   1561 C CD2 . TYR B  1 37  ? -82.247 20.535  34.519  1.00 44.35 ? 37  TYR B CD2 1 
ATOM   1562 C CE1 . TYR B  1 37  ? -81.148 18.137  33.689  1.00 45.32 ? 37  TYR B CE1 1 
ATOM   1563 C CE2 . TYR B  1 37  ? -81.255 20.528  33.552  1.00 45.51 ? 37  TYR B CE2 1 
ATOM   1564 C CZ  . TYR B  1 37  ? -80.710 19.328  33.139  1.00 46.39 ? 37  TYR B CZ  1 
ATOM   1565 O OH  . TYR B  1 37  ? -79.725 19.322  32.176  1.00 47.06 ? 37  TYR B OH  1 
ATOM   1566 N N   . GLN B  1 38  ? -86.903 17.957  37.212  1.00 35.80 ? 38  GLN B N   1 
ATOM   1567 C CA  . GLN B  1 38  ? -87.867 18.083  38.294  1.00 35.07 ? 38  GLN B CA  1 
ATOM   1568 C C   . GLN B  1 38  ? -87.572 17.060  39.387  1.00 34.97 ? 38  GLN B C   1 
ATOM   1569 O O   . GLN B  1 38  ? -87.102 15.952  39.120  1.00 36.17 ? 38  GLN B O   1 
ATOM   1570 C CB  . GLN B  1 38  ? -89.289 17.905  37.764  1.00 34.99 ? 38  GLN B CB  1 
ATOM   1571 C CG  . GLN B  1 38  ? -90.372 18.269  38.764  1.00 35.43 ? 38  GLN B CG  1 
ATOM   1572 C CD  . GLN B  1 38  ? -91.763 17.986  38.241  1.00 36.26 ? 38  GLN B CD  1 
ATOM   1573 O OE1 . GLN B  1 38  ? -91.981 17.909  37.031  1.00 36.85 ? 38  GLN B OE1 1 
ATOM   1574 N NE2 . GLN B  1 38  ? -92.715 17.817  39.153  1.00 36.11 ? 38  GLN B NE2 1 
ATOM   1575 N N   . GLN B  1 39  ? -87.834 17.448  40.633  1.00 34.66 ? 39  GLN B N   1 
ATOM   1576 C CA  . GLN B  1 39  ? -87.520 16.614  41.787  1.00 34.72 ? 39  GLN B CA  1 
ATOM   1577 C C   . GLN B  1 39  ? -88.796 16.258  42.534  1.00 34.93 ? 39  GLN B C   1 
ATOM   1578 O O   . GLN B  1 39  ? -89.533 17.145  42.978  1.00 34.41 ? 39  GLN B O   1 
ATOM   1579 C CB  . GLN B  1 39  ? -86.524 17.312  42.713  1.00 34.01 ? 39  GLN B CB  1 
ATOM   1580 C CG  . GLN B  1 39  ? -85.129 17.423  42.122  1.00 32.82 ? 39  GLN B CG  1 
ATOM   1581 C CD  . GLN B  1 39  ? -84.059 16.951  43.084  1.00 31.91 ? 39  GLN B CD  1 
ATOM   1582 O OE1 . GLN B  1 39  ? -84.360 16.454  44.170  1.00 31.64 ? 39  GLN B OE1 1 
ATOM   1583 N NE2 . GLN B  1 39  ? -82.801 17.102  42.692  1.00 33.23 ? 39  GLN B NE2 1 
ATOM   1584 N N   . ILE B  1 40  ? -89.045 14.962  42.677  1.00 36.03 ? 40  ILE B N   1 
ATOM   1585 C CA  . ILE B  1 40  ? -90.178 14.440  43.429  1.00 37.63 ? 40  ILE B CA  1 
ATOM   1586 C C   . ILE B  1 40  ? -89.595 13.664  44.603  1.00 37.89 ? 40  ILE B C   1 
ATOM   1587 O O   . ILE B  1 40  ? -89.118 12.538  44.436  1.00 37.87 ? 40  ILE B O   1 
ATOM   1588 C CB  . ILE B  1 40  ? -91.094 13.569  42.563  1.00 38.58 ? 40  ILE B CB  1 
ATOM   1589 C CG1 . ILE B  1 40  ? -91.712 14.407  41.441  1.00 38.59 ? 40  ILE B CG1 1 
ATOM   1590 C CG2 . ILE B  1 40  ? -92.177 12.927  43.405  1.00 42.00 ? 40  ILE B CG2 1 
ATOM   1591 C CD1 . ILE B  1 40  ? -92.787 13.686  40.656  1.00 40.60 ? 40  ILE B CD1 1 
ATOM   1592 N N   . VAL B  1 41  ? -89.646 14.254  45.793  1.00 38.46 ? 41  VAL B N   1 
ATOM   1593 C CA  . VAL B  1 41  ? -88.869 13.767  46.929  1.00 37.81 ? 41  VAL B CA  1 
ATOM   1594 C C   . VAL B  1 41  ? -89.584 12.612  47.625  1.00 38.10 ? 41  VAL B C   1 
ATOM   1595 O O   . VAL B  1 41  ? -90.702 12.768  48.127  1.00 38.76 ? 41  VAL B O   1 
ATOM   1596 C CB  . VAL B  1 41  ? -88.568 14.907  47.911  1.00 36.12 ? 41  VAL B CB  1 
ATOM   1597 C CG1 . VAL B  1 41  ? -87.806 14.383  49.103  1.00 36.03 ? 41  VAL B CG1 1 
ATOM   1598 C CG2 . VAL B  1 41  ? -87.778 16.015  47.213  1.00 35.00 ? 41  VAL B CG2 1 
ATOM   1599 N N   . VAL B  1 42  ? -88.927 11.456  47.664  1.00 37.29 ? 42  VAL B N   1 
ATOM   1600 C CA  . VAL B  1 42  ? -89.371 10.308  48.449  1.00 37.97 ? 42  VAL B CA  1 
ATOM   1601 C C   . VAL B  1 42  ? -88.683 10.265  49.806  1.00 38.00 ? 42  VAL B C   1 
ATOM   1602 O O   . VAL B  1 42  ? -89.342 10.170  50.841  1.00 39.17 ? 42  VAL B O   1 
ATOM   1603 C CB  . VAL B  1 42  ? -89.131 8.998   47.668  1.00 37.76 ? 42  VAL B CB  1 
ATOM   1604 C CG1 . VAL B  1 42  ? -89.436 7.797   48.551  1.00 38.19 ? 42  VAL B CG1 1 
ATOM   1605 C CG2 . VAL B  1 42  ? -89.976 8.965   46.408  1.00 39.36 ? 42  VAL B CG2 1 
ATOM   1606 N N   . ILE B  1 43  ? -87.354 10.330  49.816  1.00 37.02 ? 43  ILE B N   1 
ATOM   1607 C CA  . ILE B  1 43  ? -86.575 10.419  51.050  1.00 35.86 ? 43  ILE B CA  1 
ATOM   1608 C C   . ILE B  1 43  ? -85.676 11.644  50.931  1.00 35.62 ? 43  ILE B C   1 
ATOM   1609 O O   . ILE B  1 43  ? -84.760 11.660  50.098  1.00 36.01 ? 43  ILE B O   1 
ATOM   1610 C CB  . ILE B  1 43  ? -85.763 9.137   51.306  1.00 35.15 ? 43  ILE B CB  1 
ATOM   1611 C CG1 . ILE B  1 43  ? -86.685 7.921   51.324  1.00 34.88 ? 43  ILE B CG1 1 
ATOM   1612 C CG2 . ILE B  1 43  ? -85.021 9.224   52.628  1.00 34.96 ? 43  ILE B CG2 1 
ATOM   1613 C CD1 . ILE B  1 43  ? -85.960 6.598   51.433  1.00 36.17 ? 43  ILE B CD1 1 
ATOM   1614 N N   . PRO B  1 44  ? -85.912 12.695  51.719  1.00 34.84 ? 44  PRO B N   1 
ATOM   1615 C CA  . PRO B  1 44  ? -85.082 13.902  51.574  1.00 34.22 ? 44  PRO B CA  1 
ATOM   1616 C C   . PRO B  1 44  ? -83.621 13.658  51.887  1.00 34.39 ? 44  PRO B C   1 
ATOM   1617 O O   . PRO B  1 44  ? -82.747 14.236  51.230  1.00 34.49 ? 44  PRO B O   1 
ATOM   1618 C CB  . PRO B  1 44  ? -85.717 14.885  52.569  1.00 33.56 ? 44  PRO B CB  1 
ATOM   1619 C CG  . PRO B  1 44  ? -87.063 14.306  52.902  1.00 33.06 ? 44  PRO B CG  1 
ATOM   1620 C CD  . PRO B  1 44  ? -86.897 12.830  52.801  1.00 34.84 ? 44  PRO B CD  1 
ATOM   1621 N N   . ASP B  1 45  ? -83.324 12.817  52.878  1.00 34.22 ? 45  ASP B N   1 
ATOM   1622 C CA  . ASP B  1 45  ? -81.927 12.553  53.195  1.00 34.16 ? 45  ASP B CA  1 
ATOM   1623 C C   . ASP B  1 45  ? -81.251 11.761  52.087  1.00 34.79 ? 45  ASP B C   1 
ATOM   1624 O O   . ASP B  1 45  ? -80.098 12.038  51.734  1.00 35.60 ? 45  ASP B O   1 
ATOM   1625 C CB  . ASP B  1 45  ? -81.811 11.812  54.529  1.00 34.92 ? 45  ASP B CB  1 
ATOM   1626 C CG  . ASP B  1 45  ? -81.589 12.751  55.701  1.00 34.97 ? 45  ASP B CG  1 
ATOM   1627 O OD1 . ASP B  1 45  ? -82.305 13.771  55.779  1.00 36.21 ? 45  ASP B OD1 1 
ATOM   1628 O OD2 . ASP B  1 45  ? -80.711 12.470  56.549  1.00 33.99 ? 45  ASP B OD2 1 
ATOM   1629 N N   . LEU B  1 46  ? -81.957 10.791  51.508  1.00 34.60 ? 46  LEU B N   1 
ATOM   1630 C CA  . LEU B  1 46  ? -81.311 9.746   50.726  1.00 34.23 ? 46  LEU B CA  1 
ATOM   1631 C C   . LEU B  1 46  ? -81.610 9.812   49.233  1.00 34.76 ? 46  LEU B C   1 
ATOM   1632 O O   . LEU B  1 46  ? -80.674 9.892   48.435  1.00 35.40 ? 46  LEU B O   1 
ATOM   1633 C CB  . LEU B  1 46  ? -81.697 8.371   51.295  1.00 33.83 ? 46  LEU B CB  1 
ATOM   1634 C CG  . LEU B  1 46  ? -81.019 7.988   52.613  1.00 34.03 ? 46  LEU B CG  1 
ATOM   1635 C CD1 . LEU B  1 46  ? -81.419 6.582   53.051  1.00 34.80 ? 46  LEU B CD1 1 
ATOM   1636 C CD2 . LEU B  1 46  ? -79.500 8.106   52.511  1.00 33.77 ? 46  LEU B CD2 1 
ATOM   1637 N N   . PHE B  1 47  ? -82.874 9.772   48.811  1.00 35.04 ? 47  PHE B N   1 
ATOM   1638 C CA  . PHE B  1 47  ? -83.125 9.576   47.387  1.00 35.56 ? 47  PHE B CA  1 
ATOM   1639 C C   . PHE B  1 47  ? -84.490 10.134  47.000  1.00 35.20 ? 47  PHE B C   1 
ATOM   1640 O O   . PHE B  1 47  ? -85.417 10.165  47.813  1.00 35.86 ? 47  PHE B O   1 
ATOM   1641 C CB  . PHE B  1 47  ? -82.985 8.083   47.031  1.00 37.45 ? 47  PHE B CB  1 
ATOM   1642 C CG  . PHE B  1 47  ? -84.214 7.454   46.429  1.00 37.39 ? 47  PHE B CG  1 
ATOM   1643 C CD1 . PHE B  1 47  ? -85.250 6.998   47.231  1.00 37.10 ? 47  PHE B CD1 1 
ATOM   1644 C CD2 . PHE B  1 47  ? -84.299 7.260   45.061  1.00 36.17 ? 47  PHE B CD2 1 
ATOM   1645 C CE1 . PHE B  1 47  ? -86.361 6.402   46.672  1.00 37.78 ? 47  PHE B CE1 1 
ATOM   1646 C CE2 . PHE B  1 47  ? -85.402 6.664   44.499  1.00 35.23 ? 47  PHE B CE2 1 
ATOM   1647 C CZ  . PHE B  1 47  ? -86.435 6.235   45.303  1.00 36.91 ? 47  PHE B CZ  1 
ATOM   1648 N N   . SER B  1 48  ? -84.593 10.583  45.747  1.00 34.07 ? 48  SER B N   1 
ATOM   1649 C CA  . SER B  1 48  ? -85.801 11.226  45.246  1.00 34.36 ? 48  SER B CA  1 
ATOM   1650 C C   . SER B  1 48  ? -85.892 11.021  43.739  1.00 34.41 ? 48  SER B C   1 
ATOM   1651 O O   . SER B  1 48  ? -84.900 10.711  43.076  1.00 34.43 ? 48  SER B O   1 
ATOM   1652 C CB  . SER B  1 48  ? -85.820 12.721  45.587  1.00 34.68 ? 48  SER B CB  1 
ATOM   1653 O OG  . SER B  1 48  ? -84.834 13.423  44.855  1.00 34.53 ? 48  SER B OG  1 
ATOM   1654 N N   . TRP B  1 49  ? -87.101 11.192  43.202  1.00 35.10 ? 49  TRP B N   1 
ATOM   1655 C CA  . TRP B  1 49  ? -87.334 10.987  41.777  1.00 34.50 ? 49  TRP B CA  1 
ATOM   1656 C C   . TRP B  1 49  ? -86.910 12.215  40.981  1.00 34.22 ? 49  TRP B C   1 
ATOM   1657 O O   . TRP B  1 49  ? -87.088 13.351  41.428  1.00 34.41 ? 49  TRP B O   1 
ATOM   1658 C CB  . TRP B  1 49  ? -88.810 10.686  41.506  1.00 35.03 ? 49  TRP B CB  1 
ATOM   1659 C CG  . TRP B  1 49  ? -89.327 9.412   42.118  1.00 35.39 ? 49  TRP B CG  1 
ATOM   1660 C CD1 . TRP B  1 49  ? -90.357 9.294   43.005  1.00 37.32 ? 49  TRP B CD1 1 
ATOM   1661 C CD2 . TRP B  1 49  ? -88.847 8.080   41.882  1.00 35.21 ? 49  TRP B CD2 1 
ATOM   1662 N NE1 . TRP B  1 49  ? -90.549 7.975   43.338  1.00 38.48 ? 49  TRP B NE1 1 
ATOM   1663 C CE2 . TRP B  1 49  ? -89.635 7.209   42.664  1.00 36.58 ? 49  TRP B CE2 1 
ATOM   1664 C CE3 . TRP B  1 49  ? -87.832 7.540   41.086  1.00 34.32 ? 49  TRP B CE3 1 
ATOM   1665 C CZ2 . TRP B  1 49  ? -89.439 5.830   42.676  1.00 35.99 ? 49  TRP B CZ2 1 
ATOM   1666 C CZ3 . TRP B  1 49  ? -87.638 6.168   41.100  1.00 34.31 ? 49  TRP B CZ3 1 
ATOM   1667 C CH2 . TRP B  1 49  ? -88.439 5.330   41.890  1.00 35.51 ? 49  TRP B CH2 1 
ATOM   1668 N N   . THR B  1 50  ? -86.357 11.982  39.791  1.00 33.89 ? 50  THR B N   1 
ATOM   1669 C CA  . THR B  1 50  ? -85.931 13.062  38.911  1.00 33.75 ? 50  THR B CA  1 
ATOM   1670 C C   . THR B  1 50  ? -86.199 12.644  37.468  1.00 33.46 ? 50  THR B C   1 
ATOM   1671 O O   . THR B  1 50  ? -86.784 11.590  37.211  1.00 33.88 ? 50  THR B O   1 
ATOM   1672 C CB  . THR B  1 50  ? -84.460 13.410  39.155  1.00 33.75 ? 50  THR B CB  1 
ATOM   1673 O OG1 . THR B  1 50  ? -84.132 14.623  38.469  1.00 33.56 ? 50  THR B OG1 1 
ATOM   1674 C CG2 . THR B  1 50  ? -83.552 12.288  38.670  1.00 33.95 ? 50  THR B CG2 1 
ATOM   1675 N N   . LEU B  1 51  ? -85.826 13.501  36.517  1.00 33.41 ? 51  LEU B N   1 
ATOM   1676 C CA  . LEU B  1 51  ? -85.979 13.177  35.094  1.00 33.04 ? 51  LEU B CA  1 
ATOM   1677 C C   . LEU B  1 51  ? -84.761 13.641  34.287  1.00 34.23 ? 51  LEU B C   1 
ATOM   1678 O O   . LEU B  1 51  ? -84.880 14.317  33.264  1.00 35.78 ? 51  LEU B O   1 
ATOM   1679 C CB  . LEU B  1 51  ? -87.277 13.756  34.535  1.00 33.50 ? 51  LEU B CB  1 
ATOM   1680 C CG  . LEU B  1 51  ? -87.717 13.217  33.168  1.00 34.47 ? 51  LEU B CG  1 
ATOM   1681 C CD1 . LEU B  1 51  ? -87.781 11.693  33.178  1.00 34.70 ? 51  LEU B CD1 1 
ATOM   1682 C CD2 . LEU B  1 51  ? -89.046 13.815  32.717  1.00 34.72 ? 51  LEU B CD2 1 
ATOM   1683 N N   . ALA B  1 52  ? -83.563 13.296  34.745  1.00 33.96 ? 52  ALA B N   1 
ATOM   1684 C CA  . ALA B  1 52  ? -82.361 13.741  34.053  1.00 36.01 ? 52  ALA B CA  1 
ATOM   1685 C C   . ALA B  1 52  ? -82.061 12.862  32.838  1.00 36.29 ? 52  ALA B C   1 
ATOM   1686 O O   . ALA B  1 52  ? -82.457 11.695  32.769  1.00 36.36 ? 52  ALA B O   1 
ATOM   1687 C CB  . ALA B  1 52  ? -81.167 13.756  35.006  1.00 37.03 ? 52  ALA B CB  1 
ATOM   1688 N N   . TYR B  1 53  ? -81.361 13.448  31.865  1.00 36.76 ? 53  TYR B N   1 
ATOM   1689 C CA  . TYR B  1 53  ? -80.970 12.770  30.633  1.00 37.26 ? 53  TYR B CA  1 
ATOM   1690 C C   . TYR B  1 53  ? -79.451 12.677  30.536  1.00 37.63 ? 53  TYR B C   1 
ATOM   1691 O O   . TYR B  1 53  ? -78.741 13.647  30.819  1.00 39.31 ? 53  TYR B O   1 
ATOM   1692 C CB  . TYR B  1 53  ? -81.513 13.495  29.398  1.00 37.64 ? 53  TYR B CB  1 
ATOM   1693 C CG  . TYR B  1 53  ? -83.017 13.473  29.272  1.00 36.96 ? 53  TYR B CG  1 
ATOM   1694 C CD1 . TYR B  1 53  ? -83.778 12.530  29.945  1.00 36.91 ? 53  TYR B CD1 1 
ATOM   1695 C CD2 . TYR B  1 53  ? -83.675 14.399  28.475  1.00 36.90 ? 53  TYR B CD2 1 
ATOM   1696 C CE1 . TYR B  1 53  ? -85.153 12.507  29.831  1.00 37.06 ? 53  TYR B CE1 1 
ATOM   1697 C CE2 . TYR B  1 53  ? -85.049 14.387  28.354  1.00 37.75 ? 53  TYR B CE2 1 
ATOM   1698 C CZ  . TYR B  1 53  ? -85.785 13.439  29.034  1.00 37.38 ? 53  TYR B CZ  1 
ATOM   1699 O OH  . TYR B  1 53  ? -87.158 13.421  28.917  1.00 35.83 ? 53  TYR B OH  1 
ATOM   1700 N N   . ASN B  1 54  ? -78.963 11.512  30.105  1.00 37.20 ? 54  ASN B N   1 
ATOM   1701 C CA  . ASN B  1 54  ? -77.531 11.205  30.086  1.00 37.94 ? 54  ASN B CA  1 
ATOM   1702 C C   . ASN B  1 54  ? -76.921 11.417  31.464  1.00 39.39 ? 54  ASN B C   1 
ATOM   1703 O O   . ASN B  1 54  ? -75.789 11.890  31.599  1.00 39.83 ? 54  ASN B O   1 
ATOM   1704 C CB  . ASN B  1 54  ? -76.781 12.002  29.021  1.00 37.65 ? 54  ASN B CB  1 
ATOM   1705 C CG  . ASN B  1 54  ? -76.992 11.431  27.633  1.00 36.46 ? 54  ASN B CG  1 
ATOM   1706 O OD1 . ASN B  1 54  ? -77.152 10.220  27.462  1.00 35.85 ? 54  ASN B OD1 1 
ATOM   1707 N ND2 . ASN B  1 54  ? -76.981 12.296  26.633  1.00 36.54 ? 54  ASN B ND2 1 
ATOM   1708 N N   . THR B  1 55  ? -77.685 11.033  32.492  1.00 39.04 ? 55  THR B N   1 
ATOM   1709 C CA  . THR B  1 55  ? -77.380 11.213  33.915  1.00 38.69 ? 55  THR B CA  1 
ATOM   1710 C C   . THR B  1 55  ? -77.582 12.667  34.352  1.00 40.04 ? 55  THR B C   1 
ATOM   1711 O O   . THR B  1 55  ? -77.508 13.002  35.539  1.00 41.01 ? 55  THR B O   1 
ATOM   1712 C CB  . THR B  1 55  ? -75.949 10.754  34.251  1.00 39.28 ? 55  THR B CB  1 
ATOM   1713 O OG1 . THR B  1 55  ? -74.996 11.518  33.494  1.00 41.05 ? 55  THR B OG1 1 
ATOM   1714 C CG2 . THR B  1 55  ? -75.772 9.288   33.933  1.00 38.84 ? 55  THR B CG2 1 
ATOM   1715 N N   . GLY B  1 56  ? -77.793 13.554  33.393  1.00 41.34 ? 56  GLY B N   1 
ATOM   1716 C CA  . GLY B  1 56  ? -78.201 14.914  33.672  1.00 43.20 ? 56  GLY B CA  1 
ATOM   1717 C C   . GLY B  1 56  ? -77.153 15.996  33.491  1.00 46.81 ? 56  GLY B C   1 
ATOM   1718 O O   . GLY B  1 56  ? -77.510 17.171  33.580  1.00 46.86 ? 56  GLY B O   1 
ATOM   1719 N N   . ALA B  1 57  ? -75.890 15.675  33.248  1.00 47.42 ? 57  ALA B N   1 
ATOM   1720 C CA  . ALA B  1 57  ? -74.883 16.718  33.101  1.00 49.44 ? 57  ALA B CA  1 
ATOM   1721 C C   . ALA B  1 57  ? -75.121 17.498  31.812  1.00 50.99 ? 57  ALA B C   1 
ATOM   1722 O O   . ALA B  1 57  ? -75.093 16.926  30.715  1.00 51.69 ? 57  ALA B O   1 
ATOM   1723 C CB  . ALA B  1 57  ? -73.494 16.091  33.116  1.00 48.25 ? 57  ALA B CB  1 
ATOM   1724 N N   . ALA B  1 58  ? -75.350 18.806  31.952  1.00 51.23 ? 58  ALA B N   1 
ATOM   1725 C CA  . ALA B  1 58  ? -75.516 19.705  30.818  1.00 50.87 ? 58  ALA B CA  1 
ATOM   1726 C C   . ALA B  1 58  ? -74.330 20.639  30.613  1.00 49.52 ? 58  ALA B C   1 
ATOM   1727 O O   . ALA B  1 58  ? -74.379 21.492  29.717  1.00 49.77 ? 58  ALA B O   1 
ATOM   1728 C CB  . ALA B  1 58  ? -76.800 20.526  30.973  1.00 51.20 ? 58  ALA B CB  1 
ATOM   1729 N N   . PHE B  1 59  ? -73.271 20.505  31.416  1.00 49.25 ? 59  PHE B N   1 
ATOM   1730 C CA  . PHE B  1 59  ? -72.008 21.204  31.199  1.00 49.16 ? 59  PHE B CA  1 
ATOM   1731 C C   . PHE B  1 59  ? -70.871 20.246  30.865  1.00 50.07 ? 59  PHE B C   1 
ATOM   1732 O O   . PHE B  1 59  ? -69.708 20.666  30.828  1.00 49.94 ? 59  PHE B O   1 
ATOM   1733 C CB  . PHE B  1 59  ? -71.618 22.030  32.430  1.00 48.63 ? 59  PHE B CB  1 
ATOM   1734 C CG  . PHE B  1 59  ? -72.158 23.434  32.433  1.00 48.20 ? 59  PHE B CG  1 
ATOM   1735 C CD1 . PHE B  1 59  ? -73.088 23.839  31.491  1.00 47.48 ? 59  PHE B CD1 1 
ATOM   1736 C CD2 . PHE B  1 59  ? -71.723 24.356  33.379  1.00 47.45 ? 59  PHE B CD2 1 
ATOM   1737 C CE1 . PHE B  1 59  ? -73.584 25.130  31.496  1.00 46.55 ? 59  PHE B CE1 1 
ATOM   1738 C CE2 . PHE B  1 59  ? -72.216 25.654  33.388  1.00 45.16 ? 59  PHE B CE2 1 
ATOM   1739 C CZ  . PHE B  1 59  ? -73.148 26.039  32.446  1.00 45.66 ? 59  PHE B CZ  1 
ATOM   1740 N N   . SER B  1 60  ? -71.172 18.967  30.651  1.00 50.90 ? 60  SER B N   1 
ATOM   1741 C CA  . SER B  1 60  ? -70.144 17.962  30.403  1.00 51.24 ? 60  SER B CA  1 
ATOM   1742 C C   . SER B  1 60  ? -70.186 17.463  28.958  1.00 51.62 ? 60  SER B C   1 
ATOM   1743 O O   . SER B  1 60  ? -70.104 16.263  28.696  1.00 52.93 ? 60  SER B O   1 
ATOM   1744 C CB  . SER B  1 60  ? -70.309 16.789  31.375  1.00 51.68 ? 60  SER B CB  1 
ATOM   1745 O OG  . SER B  1 60  ? -70.435 17.257  32.707  1.00 50.06 ? 60  SER B OG  1 
ATOM   1746 N N   . GLY B  1 67  ? -75.508 13.135  18.444  1.00 41.00 ? 67  GLY B N   1 
ATOM   1747 C CA  . GLY B  1 67  ? -74.189 13.247  19.041  1.00 40.05 ? 67  GLY B CA  1 
ATOM   1748 C C   . GLY B  1 67  ? -73.295 12.061  18.738  1.00 42.15 ? 67  GLY B C   1 
ATOM   1749 O O   . GLY B  1 67  ? -73.778 10.952  18.505  1.00 43.58 ? 67  GLY B O   1 
ATOM   1750 N N   . TRP B  1 68  ? -71.981 12.296  18.746  1.00 41.38 ? 68  TRP B N   1 
ATOM   1751 C CA  . TRP B  1 68  ? -71.030 11.227  18.464  1.00 40.61 ? 68  TRP B CA  1 
ATOM   1752 C C   . TRP B  1 68  ? -71.006 10.164  19.555  1.00 41.14 ? 68  TRP B C   1 
ATOM   1753 O O   . TRP B  1 68  ? -70.555 9.043   19.297  1.00 41.41 ? 68  TRP B O   1 
ATOM   1754 C CB  . TRP B  1 68  ? -69.629 11.811  18.272  1.00 41.86 ? 68  TRP B CB  1 
ATOM   1755 C CG  . TRP B  1 68  ? -69.114 12.551  19.471  1.00 43.22 ? 68  TRP B CG  1 
ATOM   1756 C CD1 . TRP B  1 68  ? -69.244 13.887  19.734  1.00 41.71 ? 68  TRP B CD1 1 
ATOM   1757 C CD2 . TRP B  1 68  ? -68.384 11.994  20.573  1.00 43.55 ? 68  TRP B CD2 1 
ATOM   1758 N NE1 . TRP B  1 68  ? -68.640 14.194  20.931  1.00 42.24 ? 68  TRP B NE1 1 
ATOM   1759 C CE2 . TRP B  1 68  ? -68.105 13.050  21.466  1.00 43.10 ? 68  TRP B CE2 1 
ATOM   1760 C CE3 . TRP B  1 68  ? -67.941 10.704  20.891  1.00 41.87 ? 68  TRP B CE3 1 
ATOM   1761 C CZ2 . TRP B  1 68  ? -67.402 12.855  22.656  1.00 42.80 ? 68  TRP B CZ2 1 
ATOM   1762 C CZ3 . TRP B  1 68  ? -67.243 10.513  22.070  1.00 41.10 ? 68  TRP B CZ3 1 
ATOM   1763 C CH2 . TRP B  1 68  ? -66.980 11.582  22.938  1.00 41.36 ? 68  TRP B CH2 1 
ATOM   1764 N N   . GLN B  1 69  ? -71.469 10.488  20.767  1.00 42.01 ? 69  GLN B N   1 
ATOM   1765 C CA  . GLN B  1 69  ? -71.496 9.509   21.852  1.00 42.09 ? 69  GLN B CA  1 
ATOM   1766 C C   . GLN B  1 69  ? -72.634 8.509   21.700  1.00 42.42 ? 69  GLN B C   1 
ATOM   1767 O O   . GLN B  1 69  ? -72.496 7.352   22.117  1.00 42.98 ? 69  GLN B O   1 
ATOM   1768 C CB  . GLN B  1 69  ? -71.616 10.214  23.203  1.00 41.55 ? 69  GLN B CB  1 
ATOM   1769 C CG  . GLN B  1 69  ? -70.415 11.051  23.582  1.00 42.12 ? 69  GLN B CG  1 
ATOM   1770 C CD  . GLN B  1 69  ? -70.665 11.874  24.828  1.00 43.78 ? 69  GLN B CD  1 
ATOM   1771 O OE1 . GLN B  1 69  ? -71.503 11.521  25.660  1.00 44.88 ? 69  GLN B OE1 1 
ATOM   1772 N NE2 . GLN B  1 69  ? -69.946 12.985  24.959  1.00 43.74 ? 69  GLN B NE2 1 
ATOM   1773 N N   . ARG B  1 70  ? -73.762 8.940   21.130  1.00 41.84 ? 70  ARG B N   1 
ATOM   1774 C CA  . ARG B  1 70  ? -74.901 8.044   20.956  1.00 42.43 ? 70  ARG B CA  1 
ATOM   1775 C C   . ARG B  1 70  ? -74.541 6.862   20.062  1.00 43.10 ? 70  ARG B C   1 
ATOM   1776 O O   . ARG B  1 70  ? -74.902 5.717   20.360  1.00 42.32 ? 70  ARG B O   1 
ATOM   1777 C CB  . ARG B  1 70  ? -76.090 8.837   20.404  1.00 43.51 ? 70  ARG B CB  1 
ATOM   1778 C CG  . ARG B  1 70  ? -76.886 8.186   19.278  1.00 44.56 ? 70  ARG B CG  1 
ATOM   1779 C CD  . ARG B  1 70  ? -78.012 9.119   18.834  1.00 45.44 ? 70  ARG B CD  1 
ATOM   1780 N NE  . ARG B  1 70  ? -78.770 8.605   17.698  1.00 46.43 ? 70  ARG B NE  1 
ATOM   1781 C CZ  . ARG B  1 70  ? -79.806 9.224   17.147  1.00 47.06 ? 70  ARG B CZ  1 
ATOM   1782 N NH1 . ARG B  1 70  ? -80.241 10.389  17.603  1.00 47.03 ? 70  ARG B NH1 1 
ATOM   1783 N NH2 . ARG B  1 70  ? -80.423 8.660   16.111  1.00 47.47 ? 70  ARG B NH2 1 
ATOM   1784 N N   . TRP B  1 71  ? -73.807 7.113   18.976  1.00 43.98 ? 71  TRP B N   1 
ATOM   1785 C CA  . TRP B  1 71  ? -73.400 6.029   18.086  1.00 43.63 ? 71  TRP B CA  1 
ATOM   1786 C C   . TRP B  1 71  ? -72.218 5.238   18.645  1.00 42.37 ? 71  TRP B C   1 
ATOM   1787 O O   . TRP B  1 71  ? -72.127 4.024   18.431  1.00 42.80 ? 71  TRP B O   1 
ATOM   1788 C CB  . TRP B  1 71  ? -73.064 6.594   16.706  1.00 44.45 ? 71  TRP B CB  1 
ATOM   1789 C CG  . TRP B  1 71  ? -74.152 7.442   16.137  1.00 45.53 ? 71  TRP B CG  1 
ATOM   1790 C CD1 . TRP B  1 71  ? -74.291 8.790   16.276  1.00 46.03 ? 71  TRP B CD1 1 
ATOM   1791 C CD2 . TRP B  1 71  ? -75.263 7.001   15.348  1.00 47.33 ? 71  TRP B CD2 1 
ATOM   1792 N NE1 . TRP B  1 71  ? -75.418 9.220   15.621  1.00 47.13 ? 71  TRP B NE1 1 
ATOM   1793 C CE2 . TRP B  1 71  ? -76.034 8.142   15.042  1.00 48.34 ? 71  TRP B CE2 1 
ATOM   1794 C CE3 . TRP B  1 71  ? -75.682 5.754   14.869  1.00 49.14 ? 71  TRP B CE3 1 
ATOM   1795 C CZ2 . TRP B  1 71  ? -77.201 8.076   14.278  1.00 49.36 ? 71  TRP B CZ2 1 
ATOM   1796 C CZ3 . TRP B  1 71  ? -76.843 5.689   14.109  1.00 51.63 ? 71  TRP B CZ3 1 
ATOM   1797 C CH2 . TRP B  1 71  ? -77.589 6.846   13.821  1.00 50.50 ? 71  TRP B CH2 1 
ATOM   1798 N N   . LEU B  1 72  ? -71.297 5.904   19.345  1.00 41.07 ? 72  LEU B N   1 
ATOM   1799 C CA  . LEU B  1 72  ? -70.190 5.186   19.970  1.00 40.94 ? 72  LEU B CA  1 
ATOM   1800 C C   . LEU B  1 72  ? -70.689 4.241   21.056  1.00 41.50 ? 72  LEU B C   1 
ATOM   1801 O O   . LEU B  1 72  ? -70.205 3.109   21.176  1.00 41.22 ? 72  LEU B O   1 
ATOM   1802 C CB  . LEU B  1 72  ? -69.177 6.175   20.546  1.00 40.20 ? 72  LEU B CB  1 
ATOM   1803 C CG  . LEU B  1 72  ? -68.183 5.586   21.548  1.00 38.12 ? 72  LEU B CG  1 
ATOM   1804 C CD1 . LEU B  1 72  ? -67.249 4.592   20.874  1.00 36.09 ? 72  LEU B CD1 1 
ATOM   1805 C CD2 . LEU B  1 72  ? -67.398 6.689   22.238  1.00 39.06 ? 72  LEU B CD2 1 
ATOM   1806 N N   . PHE B  1 73  ? -71.654 4.691   21.861  1.00 41.81 ? 73  PHE B N   1 
ATOM   1807 C CA  . PHE B  1 73  ? -72.186 3.882   22.951  1.00 42.09 ? 73  PHE B CA  1 
ATOM   1808 C C   . PHE B  1 73  ? -73.258 2.894   22.502  1.00 42.78 ? 73  PHE B C   1 
ATOM   1809 O O   . PHE B  1 73  ? -73.583 1.972   23.260  1.00 43.08 ? 73  PHE B O   1 
ATOM   1810 C CB  . PHE B  1 73  ? -72.723 4.793   24.060  1.00 40.84 ? 73  PHE B CB  1 
ATOM   1811 C CG  . PHE B  1 73  ? -71.639 5.405   24.913  1.00 40.41 ? 73  PHE B CG  1 
ATOM   1812 C CD1 . PHE B  1 73  ? -70.466 4.707   25.171  1.00 41.19 ? 73  PHE B CD1 1 
ATOM   1813 C CD2 . PHE B  1 73  ? -71.786 6.676   25.448  1.00 39.77 ? 73  PHE B CD2 1 
ATOM   1814 C CE1 . PHE B  1 73  ? -69.465 5.262   25.950  1.00 41.21 ? 73  PHE B CE1 1 
ATOM   1815 C CE2 . PHE B  1 73  ? -70.786 7.237   26.227  1.00 39.51 ? 73  PHE B CE2 1 
ATOM   1816 C CZ  . PHE B  1 73  ? -69.626 6.529   26.477  1.00 39.08 ? 73  PHE B CZ  1 
ATOM   1817 N N   . ALA B  1 74  ? -73.817 3.057   21.302  1.00 42.33 ? 74  ALA B N   1 
ATOM   1818 C CA  . ALA B  1 74  ? -74.634 1.995   20.727  1.00 41.51 ? 74  ALA B CA  1 
ATOM   1819 C C   . ALA B  1 74  ? -73.775 0.845   20.218  1.00 41.49 ? 74  ALA B C   1 
ATOM   1820 O O   . ALA B  1 74  ? -74.228 -0.305  20.205  1.00 41.13 ? 74  ALA B O   1 
ATOM   1821 C CB  . ALA B  1 74  ? -75.504 2.545   19.597  1.00 42.43 ? 74  ALA B CB  1 
ATOM   1822 N N   . LEU B  1 75  ? -72.537 1.133   19.807  1.00 42.12 ? 75  LEU B N   1 
ATOM   1823 C CA  . LEU B  1 75  ? -71.666 0.086   19.282  1.00 41.65 ? 75  LEU B CA  1 
ATOM   1824 C C   . LEU B  1 75  ? -71.216 -0.870  20.380  1.00 41.85 ? 75  LEU B C   1 
ATOM   1825 O O   . LEU B  1 75  ? -71.204 -2.092  20.182  1.00 41.67 ? 75  LEU B O   1 
ATOM   1826 C CB  . LEU B  1 75  ? -70.455 0.711   18.589  1.00 41.50 ? 75  LEU B CB  1 
ATOM   1827 C CG  . LEU B  1 75  ? -69.351 -0.253  18.134  1.00 42.21 ? 75  LEU B CG  1 
ATOM   1828 C CD1 . LEU B  1 75  ? -69.864 -1.205  17.063  1.00 43.65 ? 75  LEU B CD1 1 
ATOM   1829 C CD2 . LEU B  1 75  ? -68.119 0.498   17.646  1.00 42.18 ? 75  LEU B CD2 1 
ATOM   1830 N N   . ILE B  1 76  ? -70.840 -0.332  21.542  1.00 42.02 ? 76  ILE B N   1 
ATOM   1831 C CA  . ILE B  1 76  ? -70.383 -1.177  22.642  1.00 42.91 ? 76  ILE B CA  1 
ATOM   1832 C C   . ILE B  1 76  ? -71.517 -2.056  23.151  1.00 43.37 ? 76  ILE B C   1 
ATOM   1833 O O   . ILE B  1 76  ? -71.323 -3.249  23.415  1.00 42.92 ? 76  ILE B O   1 
ATOM   1834 C CB  . ILE B  1 76  ? -69.777 -0.315  23.767  1.00 44.91 ? 76  ILE B CB  1 
ATOM   1835 C CG1 . ILE B  1 76  ? -69.523 -1.155  25.025  1.00 45.93 ? 76  ILE B CG1 1 
ATOM   1836 C CG2 . ILE B  1 76  ? -70.668 0.878   24.074  1.00 43.13 ? 76  ILE B CG2 1 
ATOM   1837 C CD1 . ILE B  1 76  ? -68.732 -0.431  26.102  1.00 47.28 ? 76  ILE B CD1 1 
ATOM   1838 N N   . ALA B  1 77  ? -72.719 -1.494  23.285  1.00 43.69 ? 77  ALA B N   1 
ATOM   1839 C CA  . ALA B  1 77  ? -73.845 -2.304  23.734  1.00 42.38 ? 77  ALA B CA  1 
ATOM   1840 C C   . ALA B  1 77  ? -74.195 -3.381  22.712  1.00 41.04 ? 77  ALA B C   1 
ATOM   1841 O O   . ALA B  1 77  ? -74.508 -4.514  23.088  1.00 40.54 ? 77  ALA B O   1 
ATOM   1842 C CB  . ALA B  1 77  ? -75.052 -1.415  24.032  1.00 41.38 ? 77  ALA B CB  1 
ATOM   1843 N N   . ILE B  1 78  ? -74.127 -3.058  21.417  1.00 40.99 ? 78  ILE B N   1 
ATOM   1844 C CA  . ILE B  1 78  ? -74.439 -4.053  20.391  1.00 40.19 ? 78  ILE B CA  1 
ATOM   1845 C C   . ILE B  1 78  ? -73.397 -5.170  20.376  1.00 40.34 ? 78  ILE B C   1 
ATOM   1846 O O   . ILE B  1 78  ? -73.737 -6.352  20.242  1.00 39.75 ? 78  ILE B O   1 
ATOM   1847 C CB  . ILE B  1 78  ? -74.572 -3.384  19.011  1.00 38.37 ? 78  ILE B CB  1 
ATOM   1848 C CG1 . ILE B  1 78  ? -75.892 -2.623  18.914  1.00 36.90 ? 78  ILE B CG1 1 
ATOM   1849 C CG2 . ILE B  1 78  ? -74.489 -4.419  17.897  1.00 37.72 ? 78  ILE B CG2 1 
ATOM   1850 C CD1 . ILE B  1 78  ? -76.091 -1.927  17.593  1.00 35.75 ? 78  ILE B CD1 1 
ATOM   1851 N N   . VAL B  1 79  ? -72.115 -4.819  20.501  1.00 40.37 ? 79  VAL B N   1 
ATOM   1852 C CA  . VAL B  1 79  ? -71.060 -5.832  20.494  1.00 40.72 ? 79  VAL B CA  1 
ATOM   1853 C C   . VAL B  1 79  ? -71.104 -6.666  21.770  1.00 41.64 ? 79  VAL B C   1 
ATOM   1854 O O   . VAL B  1 79  ? -71.012 -7.899  21.728  1.00 41.94 ? 79  VAL B O   1 
ATOM   1855 C CB  . VAL B  1 79  ? -69.684 -5.172  20.302  1.00 41.60 ? 79  VAL B CB  1 
ATOM   1856 C CG1 . VAL B  1 79  ? -68.568 -6.122  20.738  1.00 40.24 ? 79  VAL B CG1 1 
ATOM   1857 C CG2 . VAL B  1 79  ? -69.499 -4.755  18.849  1.00 42.44 ? 79  VAL B CG2 1 
ATOM   1858 N N   . VAL B  1 80  ? -71.235 -6.006  22.924  1.00 42.10 ? 80  VAL B N   1 
ATOM   1859 C CA  . VAL B  1 80  ? -71.281 -6.723  24.196  1.00 41.84 ? 80  VAL B CA  1 
ATOM   1860 C C   . VAL B  1 80  ? -72.506 -7.626  24.258  1.00 42.18 ? 80  VAL B C   1 
ATOM   1861 O O   . VAL B  1 80  ? -72.437 -8.756  24.759  1.00 42.77 ? 80  VAL B O   1 
ATOM   1862 C CB  . VAL B  1 80  ? -71.247 -5.731  25.374  1.00 41.51 ? 80  VAL B CB  1 
ATOM   1863 C CG1 . VAL B  1 80  ? -71.621 -6.430  26.670  1.00 42.00 ? 80  VAL B CG1 1 
ATOM   1864 C CG2 . VAL B  1 80  ? -69.869 -5.114  25.497  1.00 43.21 ? 80  VAL B CG2 1 
ATOM   1865 N N   . SER B  1 81  ? -73.646 -7.143  23.755  1.00 42.05 ? 81  SER B N   1 
ATOM   1866 C CA  . SER B  1 81  ? -74.855 -7.962  23.743  1.00 41.38 ? 81  SER B CA  1 
ATOM   1867 C C   . SER B  1 81  ? -74.661 -9.218  22.904  1.00 41.24 ? 81  SER B C   1 
ATOM   1868 O O   . SER B  1 81  ? -75.065 -10.313 23.311  1.00 40.57 ? 81  SER B O   1 
ATOM   1869 C CB  . SER B  1 81  ? -76.039 -7.147  23.220  1.00 41.03 ? 81  SER B CB  1 
ATOM   1870 O OG  . SER B  1 81  ? -76.167 -5.921  23.924  1.00 40.81 ? 81  SER B OG  1 
ATOM   1871 N N   . ALA B  1 82  ? -74.031 -9.080  21.735  1.00 41.65 ? 82  ALA B N   1 
ATOM   1872 C CA  . ALA B  1 82  ? -73.825 -10.233 20.864  1.00 42.12 ? 82  ALA B CA  1 
ATOM   1873 C C   . ALA B  1 82  ? -72.949 -11.282 21.539  1.00 43.13 ? 82  ALA B C   1 
ATOM   1874 O O   . ALA B  1 82  ? -73.248 -12.481 21.490  1.00 43.44 ? 82  ALA B O   1 
ATOM   1875 C CB  . ALA B  1 82  ? -73.218 -9.782  19.534  1.00 41.54 ? 82  ALA B CB  1 
ATOM   1876 N N   . SER B  1 83  ? -71.861 -10.850 22.183  1.00 43.29 ? 83  SER B N   1 
ATOM   1877 C CA  . SER B  1 83  ? -71.022 -11.796 22.911  1.00 43.47 ? 83  SER B CA  1 
ATOM   1878 C C   . SER B  1 83  ? -71.766 -12.406 24.092  1.00 43.32 ? 83  SER B C   1 
ATOM   1879 O O   . SER B  1 83  ? -71.439 -13.518 24.523  1.00 44.79 ? 83  SER B O   1 
ATOM   1880 C CB  . SER B  1 83  ? -69.737 -11.116 23.383  1.00 43.63 ? 83  SER B CB  1 
ATOM   1881 O OG  . SER B  1 83  ? -70.014 -10.115 24.344  1.00 43.73 ? 83  SER B OG  1 
ATOM   1882 N N   . LEU B  1 84  ? -72.757 -11.693 24.632  1.00 42.61 ? 84  LEU B N   1 
ATOM   1883 C CA  . LEU B  1 84  ? -73.536 -12.224 25.746  1.00 42.19 ? 84  LEU B CA  1 
ATOM   1884 C C   . LEU B  1 84  ? -74.475 -13.329 25.283  1.00 42.27 ? 84  LEU B C   1 
ATOM   1885 O O   . LEU B  1 84  ? -74.724 -14.290 26.020  1.00 42.28 ? 84  LEU B O   1 
ATOM   1886 C CB  . LEU B  1 84  ? -74.314 -11.094 26.420  1.00 41.45 ? 84  LEU B CB  1 
ATOM   1887 C CG  . LEU B  1 84  ? -74.114 -10.963 27.930  1.00 40.02 ? 84  LEU B CG  1 
ATOM   1888 C CD1 . LEU B  1 84  ? -72.695 -11.341 28.305  1.00 40.57 ? 84  LEU B CD1 1 
ATOM   1889 C CD2 . LEU B  1 84  ? -74.429 -9.547  28.404  1.00 39.71 ? 84  LEU B CD2 1 
ATOM   1890 N N   . VAL B  1 85  ? -75.023 -13.194 24.074  1.00 42.26 ? 85  VAL B N   1 
ATOM   1891 C CA  . VAL B  1 85  ? -75.849 -14.253 23.504  1.00 41.93 ? 85  VAL B CA  1 
ATOM   1892 C C   . VAL B  1 85  ? -75.019 -15.511 23.289  1.00 43.11 ? 85  VAL B C   1 
ATOM   1893 O O   . VAL B  1 85  ? -75.463 -16.624 23.595  1.00 43.14 ? 85  VAL B O   1 
ATOM   1894 C CB  . VAL B  1 85  ? -76.505 -13.770 22.196  1.00 40.31 ? 85  VAL B CB  1 
ATOM   1895 C CG1 . VAL B  1 85  ? -77.378 -14.859 21.593  1.00 40.44 ? 85  VAL B CG1 1 
ATOM   1896 C CG2 . VAL B  1 85  ? -77.314 -12.512 22.445  1.00 40.52 ? 85  VAL B CG2 1 
ATOM   1897 N N   . VAL B  1 86  ? -73.796 -15.355 22.771  1.00 43.48 ? 86  VAL B N   1 
ATOM   1898 C CA  . VAL B  1 86  ? -72.906 -16.501 22.589  1.00 43.51 ? 86  VAL B CA  1 
ATOM   1899 C C   . VAL B  1 86  ? -72.590 -17.147 23.933  1.00 44.18 ? 86  VAL B C   1 
ATOM   1900 O O   . VAL B  1 86  ? -72.638 -18.372 24.076  1.00 45.74 ? 86  VAL B O   1 
ATOM   1901 C CB  . VAL B  1 86  ? -71.623 -16.081 21.848  1.00 44.45 ? 86  VAL B CB  1 
ATOM   1902 C CG1 . VAL B  1 86  ? -70.665 -17.265 21.718  1.00 45.48 ? 86  VAL B CG1 1 
ATOM   1903 C CG2 . VAL B  1 86  ? -71.964 -15.518 20.481  1.00 45.27 ? 86  VAL B CG2 1 
ATOM   1904 N N   . TRP B  1 87  ? -72.276 -16.328 24.940  1.00 43.89 ? 87  TRP B N   1 
ATOM   1905 C CA  . TRP B  1 87  ? -71.956 -16.853 26.267  1.00 44.23 ? 87  TRP B CA  1 
ATOM   1906 C C   . TRP B  1 87  ? -73.143 -17.605 26.864  1.00 44.11 ? 87  TRP B C   1 
ATOM   1907 O O   . TRP B  1 87  ? -72.987 -18.701 27.417  1.00 43.80 ? 87  TRP B O   1 
ATOM   1908 C CB  . TRP B  1 87  ? -71.519 -15.701 27.177  1.00 44.60 ? 87  TRP B CB  1 
ATOM   1909 C CG  . TRP B  1 87  ? -70.941 -16.099 28.511  1.00 46.41 ? 87  TRP B CG  1 
ATOM   1910 C CD1 . TRP B  1 87  ? -70.895 -17.353 29.058  1.00 46.76 ? 87  TRP B CD1 1 
ATOM   1911 C CD2 . TRP B  1 87  ? -70.322 -15.225 29.463  1.00 48.13 ? 87  TRP B CD2 1 
ATOM   1912 N NE1 . TRP B  1 87  ? -70.289 -17.310 30.293  1.00 47.25 ? 87  TRP B NE1 1 
ATOM   1913 C CE2 . TRP B  1 87  ? -69.928 -16.016 30.564  1.00 48.17 ? 87  TRP B CE2 1 
ATOM   1914 C CE3 . TRP B  1 87  ? -70.064 -13.850 29.493  1.00 48.22 ? 87  TRP B CE3 1 
ATOM   1915 C CZ2 . TRP B  1 87  ? -69.290 -15.476 31.683  1.00 48.49 ? 87  TRP B CZ2 1 
ATOM   1916 C CZ3 . TRP B  1 87  ? -69.430 -13.315 30.604  1.00 47.93 ? 87  TRP B CZ3 1 
ATOM   1917 C CH2 . TRP B  1 87  ? -69.050 -14.127 31.682  1.00 48.48 ? 87  TRP B CH2 1 
ATOM   1918 N N   . LEU B  1 88  ? -74.345 -17.037 26.746  1.00 44.34 ? 88  LEU B N   1 
ATOM   1919 C CA  . LEU B  1 88  ? -75.520 -17.680 27.325  1.00 44.98 ? 88  LEU B CA  1 
ATOM   1920 C C   . LEU B  1 88  ? -75.944 -18.911 26.530  1.00 44.09 ? 88  LEU B C   1 
ATOM   1921 O O   . LEU B  1 88  ? -76.495 -19.857 27.105  1.00 44.27 ? 88  LEU B O   1 
ATOM   1922 C CB  . LEU B  1 88  ? -76.668 -16.674 27.427  1.00 43.66 ? 88  LEU B CB  1 
ATOM   1923 C CG  . LEU B  1 88  ? -77.899 -17.113 28.222  1.00 41.83 ? 88  LEU B CG  1 
ATOM   1924 C CD1 . LEU B  1 88  ? -78.398 -15.968 29.082  1.00 39.98 ? 88  LEU B CD1 1 
ATOM   1925 C CD2 . LEU B  1 88  ? -78.992 -17.596 27.279  1.00 42.42 ? 88  LEU B CD2 1 
ATOM   1926 N N   . LYS B  1 89  ? -75.704 -18.923 25.217  1.00 43.54 ? 89  LYS B N   1 
ATOM   1927 C CA  . LYS B  1 89  ? -75.990 -20.120 24.432  1.00 44.29 ? 89  LYS B CA  1 
ATOM   1928 C C   . LYS B  1 89  ? -75.109 -21.286 24.870  1.00 45.68 ? 89  LYS B C   1 
ATOM   1929 O O   . LYS B  1 89  ? -75.603 -22.395 25.107  1.00 45.72 ? 89  LYS B O   1 
ATOM   1930 C CB  . LYS B  1 89  ? -75.805 -19.834 22.939  1.00 43.92 ? 89  LYS B CB  1 
ATOM   1931 C CG  . LYS B  1 89  ? -76.996 -19.163 22.268  1.00 41.54 ? 89  LYS B CG  1 
ATOM   1932 C CD  . LYS B  1 89  ? -76.845 -19.184 20.755  1.00 41.88 ? 89  LYS B CD  1 
ATOM   1933 C CE  . LYS B  1 89  ? -78.114 -18.714 20.059  1.00 42.56 ? 89  LYS B CE  1 
ATOM   1934 N NZ  . LYS B  1 89  ? -78.034 -18.858 18.576  1.00 44.51 ? 89  LYS B NZ  1 
ATOM   1935 N N   . ARG B  1 90  ? -73.796 -21.046 25.017  1.00 45.60 ? 90  ARG B N   1 
ATOM   1936 C CA  . ARG B  1 90  ? -72.870 -22.119 25.387  1.00 46.44 ? 90  ARG B CA  1 
ATOM   1937 C C   . ARG B  1 90  ? -72.997 -22.524 26.857  1.00 46.95 ? 90  ARG B C   1 
ATOM   1938 O O   . ARG B  1 90  ? -72.140 -23.274 27.348  1.00 48.47 ? 90  ARG B O   1 
ATOM   1939 C CB  . ARG B  1 90  ? -71.419 -21.716 25.098  1.00 46.83 ? 90  ARG B CB  1 
ATOM   1940 C CG  . ARG B  1 90  ? -71.167 -20.966 23.788  1.00 46.22 ? 90  ARG B CG  1 
ATOM   1941 C CD  . ARG B  1 90  ? -71.186 -21.851 22.549  1.00 48.35 ? 90  ARG B CD  1 
ATOM   1942 N NE  . ARG B  1 90  ? -70.816 -21.104 21.349  1.00 49.59 ? 90  ARG B NE  1 
ATOM   1943 C CZ  . ARG B  1 90  ? -71.680 -20.488 20.550  1.00 48.31 ? 90  ARG B CZ  1 
ATOM   1944 N NH1 . ARG B  1 90  ? -72.981 -20.513 20.789  1.00 46.63 ? 90  ARG B NH1 1 
ATOM   1945 N NH2 . ARG B  1 90  ? -71.226 -19.831 19.485  1.00 47.96 ? 90  ARG B NH2 1 
ATOM   1946 N N   . LEU B  1 91  ? -74.020 -22.044 27.561  1.00 46.35 ? 91  LEU B N   1 
ATOM   1947 C CA  . LEU B  1 91  ? -74.211 -22.370 28.964  1.00 47.37 ? 91  LEU B CA  1 
ATOM   1948 C C   . LEU B  1 91  ? -74.814 -23.764 29.119  1.00 48.71 ? 91  LEU B C   1 
ATOM   1949 O O   . LEU B  1 91  ? -75.349 -24.352 28.175  1.00 48.68 ? 91  LEU B O   1 
ATOM   1950 C CB  . LEU B  1 91  ? -75.117 -21.339 29.639  1.00 46.36 ? 91  LEU B CB  1 
ATOM   1951 C CG  . LEU B  1 91  ? -74.573 -20.594 30.860  1.00 45.93 ? 91  LEU B CG  1 
ATOM   1952 C CD1 . LEU B  1 91  ? -73.574 -19.530 30.439  1.00 44.64 ? 91  LEU B CD1 1 
ATOM   1953 C CD2 . LEU B  1 91  ? -75.706 -19.982 31.674  1.00 44.49 ? 91  LEU B CD2 1 
ATOM   1954 N N   . LYS B  1 92  ? -74.725 -24.288 30.340  1.00 49.65 ? 92  LYS B N   1 
ATOM   1955 C CA  . LYS B  1 92  ? -75.304 -25.576 30.687  1.00 51.36 ? 92  LYS B CA  1 
ATOM   1956 C C   . LYS B  1 92  ? -76.146 -25.427 31.948  1.00 52.52 ? 92  LYS B C   1 
ATOM   1957 O O   . LYS B  1 92  ? -76.024 -24.447 32.689  1.00 52.60 ? 92  LYS B O   1 
ATOM   1958 C CB  . LYS B  1 92  ? -74.224 -26.647 30.889  1.00 52.95 ? 92  LYS B CB  1 
ATOM   1959 C CG  . LYS B  1 92  ? -73.398 -26.474 32.152  1.00 53.53 ? 92  LYS B CG  1 
ATOM   1960 C CD  . LYS B  1 92  ? -72.339 -27.559 32.263  1.00 53.39 ? 92  LYS B CD  1 
ATOM   1961 C CE  . LYS B  1 92  ? -71.328 -27.447 31.129  1.00 53.70 ? 92  LYS B CE  1 
ATOM   1962 N NZ  . LYS B  1 92  ? -70.305 -28.532 31.160  1.00 52.50 ? 92  LYS B NZ  1 
ATOM   1963 N N   . LYS B  1 93  ? -77.021 -26.406 32.177  1.00 53.20 ? 93  LYS B N   1 
ATOM   1964 C CA  . LYS B  1 93  ? -77.852 -26.410 33.373  1.00 53.39 ? 93  LYS B CA  1 
ATOM   1965 C C   . LYS B  1 93  ? -77.003 -26.672 34.616  1.00 54.17 ? 93  LYS B C   1 
ATOM   1966 O O   . LYS B  1 93  ? -75.931 -27.282 34.557  1.00 54.80 ? 93  LYS B O   1 
ATOM   1967 C CB  . LYS B  1 93  ? -78.961 -27.455 33.256  1.00 52.60 ? 93  LYS B CB  1 
ATOM   1968 C CG  . LYS B  1 93  ? -80.042 -27.095 32.258  1.00 52.45 ? 93  LYS B CG  1 
ATOM   1969 C CD  . LYS B  1 93  ? -81.128 -28.155 32.225  1.00 52.61 ? 93  LYS B CD  1 
ATOM   1970 C CE  . LYS B  1 93  ? -82.116 -27.892 31.100  1.00 50.74 ? 93  LYS B CE  1 
ATOM   1971 N NZ  . LYS B  1 93  ? -83.056 -29.033 30.928  1.00 50.85 ? 93  LYS B NZ  1 
ATOM   1972 N N   . GLY B  1 94  ? -77.510 -26.212 35.761  1.00 53.55 ? 94  GLY B N   1 
ATOM   1973 C CA  . GLY B  1 94  ? -76.735 -26.151 36.978  1.00 52.40 ? 94  GLY B CA  1 
ATOM   1974 C C   . GLY B  1 94  ? -75.967 -24.862 37.146  1.00 51.50 ? 94  GLY B C   1 
ATOM   1975 O O   . GLY B  1 94  ? -75.576 -24.527 38.270  1.00 51.60 ? 94  GLY B O   1 
ATOM   1976 N N   . GLU B  1 95  ? -75.747 -24.135 36.056  1.00 51.19 ? 95  GLU B N   1 
ATOM   1977 C CA  . GLU B  1 95  ? -75.212 -22.780 36.097  1.00 49.61 ? 95  GLU B CA  1 
ATOM   1978 C C   . GLU B  1 95  ? -76.363 -21.782 36.088  1.00 46.43 ? 95  GLU B C   1 
ATOM   1979 O O   . GLU B  1 95  ? -76.462 -20.916 35.223  1.00 45.89 ? 95  GLU B O   1 
ATOM   1980 C CB  . GLU B  1 95  ? -74.279 -22.547 34.912  1.00 50.16 ? 95  GLU B CB  1 
ATOM   1981 C CG  . GLU B  1 95  ? -73.105 -23.500 34.845  1.00 50.92 ? 95  GLU B CG  1 
ATOM   1982 C CD  . GLU B  1 95  ? -72.354 -23.416 33.529  1.00 51.28 ? 95  GLU B CD  1 
ATOM   1983 O OE1 . GLU B  1 95  ? -72.987 -23.156 32.483  1.00 49.89 ? 95  GLU B OE1 1 
ATOM   1984 O OE2 . GLU B  1 95  ? -71.120 -23.602 33.545  1.00 52.91 ? 95  GLU B OE2 1 
ATOM   1985 N N   . THR B  1 96  ? -77.254 -21.924 37.069  1.00 45.93 ? 96  THR B N   1 
ATOM   1986 C CA  . THR B  1 96  ? -78.412 -21.044 37.125  1.00 45.05 ? 96  THR B CA  1 
ATOM   1987 C C   . THR B  1 96  ? -78.034 -19.636 37.568  1.00 43.74 ? 96  THR B C   1 
ATOM   1988 O O   . THR B  1 96  ? -78.771 -18.687 37.279  1.00 42.45 ? 96  THR B O   1 
ATOM   1989 C CB  . THR B  1 96  ? -79.483 -21.631 38.054  1.00 44.85 ? 96  THR B CB  1 
ATOM   1990 O OG1 . THR B  1 96  ? -78.911 -21.907 39.337  1.00 45.34 ? 96  THR B OG1 1 
ATOM   1991 C CG2 . THR B  1 96  ? -80.040 -22.926 37.466  1.00 43.85 ? 96  THR B CG2 1 
ATOM   1992 N N   . TRP B  1 97  ? -76.899 -19.477 38.254  1.00 44.48 ? 97  TRP B N   1 
ATOM   1993 C CA  . TRP B  1 97  ? -76.481 -18.148 38.687  1.00 43.88 ? 97  TRP B CA  1 
ATOM   1994 C C   . TRP B  1 97  ? -75.933 -17.331 37.523  1.00 42.65 ? 97  TRP B C   1 
ATOM   1995 O O   . TRP B  1 97  ? -76.193 -16.125 37.430  1.00 42.06 ? 97  TRP B O   1 
ATOM   1996 C CB  . TRP B  1 97  ? -75.444 -18.266 39.804  1.00 45.88 ? 97  TRP B CB  1 
ATOM   1997 C CG  . TRP B  1 97  ? -75.220 -16.992 40.577  1.00 46.06 ? 97  TRP B CG  1 
ATOM   1998 C CD1 . TRP B  1 97  ? -74.438 -15.934 40.209  1.00 44.32 ? 97  TRP B CD1 1 
ATOM   1999 C CD2 . TRP B  1 97  ? -75.771 -16.654 41.860  1.00 46.03 ? 97  TRP B CD2 1 
ATOM   2000 N NE1 . TRP B  1 97  ? -74.474 -14.959 41.177  1.00 44.16 ? 97  TRP B NE1 1 
ATOM   2001 C CE2 . TRP B  1 97  ? -75.284 -15.376 42.200  1.00 45.33 ? 97  TRP B CE2 1 
ATOM   2002 C CE3 . TRP B  1 97  ? -76.633 -17.307 42.750  1.00 46.82 ? 97  TRP B CE3 1 
ATOM   2003 C CZ2 . TRP B  1 97  ? -75.629 -14.737 43.390  1.00 46.94 ? 97  TRP B CZ2 1 
ATOM   2004 C CZ3 . TRP B  1 97  ? -76.973 -16.671 43.932  1.00 47.94 ? 97  TRP B CZ3 1 
ATOM   2005 C CH2 . TRP B  1 97  ? -76.471 -15.399 44.241  1.00 47.63 ? 97  TRP B CH2 1 
ATOM   2006 N N   . LEU B  1 98  ? -75.162 -17.963 36.631  1.00 42.96 ? 98  LEU B N   1 
ATOM   2007 C CA  . LEU B  1 98  ? -74.670 -17.250 35.456  1.00 41.74 ? 98  LEU B CA  1 
ATOM   2008 C C   . LEU B  1 98  ? -75.795 -16.926 34.481  1.00 40.31 ? 98  LEU B C   1 
ATOM   2009 O O   . LEU B  1 98  ? -75.737 -15.901 33.793  1.00 39.94 ? 98  LEU B O   1 
ATOM   2010 C CB  . LEU B  1 98  ? -73.577 -18.059 34.758  1.00 41.68 ? 98  LEU B CB  1 
ATOM   2011 C CG  . LEU B  1 98  ? -72.142 -17.687 35.139  1.00 41.74 ? 98  LEU B CG  1 
ATOM   2012 C CD1 . LEU B  1 98  ? -71.765 -18.270 36.497  1.00 41.97 ? 98  LEU B CD1 1 
ATOM   2013 C CD2 . LEU B  1 98  ? -71.157 -18.118 34.059  1.00 41.34 ? 98  LEU B CD2 1 
ATOM   2014 N N   . ALA B  1 99  ? -76.821 -17.777 34.406  1.00 39.87 ? 99  ALA B N   1 
ATOM   2015 C CA  . ALA B  1 99  ? -77.970 -17.465 33.565  1.00 38.90 ? 99  ALA B CA  1 
ATOM   2016 C C   . ALA B  1 99  ? -78.683 -16.213 34.056  1.00 39.66 ? 99  ALA B C   1 
ATOM   2017 O O   . ALA B  1 99  ? -79.092 -15.365 33.253  1.00 38.97 ? 99  ALA B O   1 
ATOM   2018 C CB  . ALA B  1 99  ? -78.930 -18.652 33.528  1.00 40.43 ? 99  ALA B CB  1 
ATOM   2019 N N   . ILE B  1 100 ? -78.840 -16.077 35.375  1.00 40.75 ? 100 ILE B N   1 
ATOM   2020 C CA  . ILE B  1 100 ? -79.432 -14.865 35.934  1.00 39.54 ? 100 ILE B CA  1 
ATOM   2021 C C   . ILE B  1 100 ? -78.509 -13.670 35.722  1.00 38.71 ? 100 ILE B C   1 
ATOM   2022 O O   . ILE B  1 100 ? -78.959 -12.580 35.349  1.00 38.12 ? 100 ILE B O   1 
ATOM   2023 C CB  . ILE B  1 100 ? -79.763 -15.067 37.424  1.00 39.02 ? 100 ILE B CB  1 
ATOM   2024 C CG1 . ILE B  1 100 ? -80.756 -16.216 37.597  1.00 39.87 ? 100 ILE B CG1 1 
ATOM   2025 C CG2 . ILE B  1 100 ? -80.337 -13.792 38.024  1.00 38.98 ? 100 ILE B CG2 1 
ATOM   2026 C CD1 . ILE B  1 100 ? -80.968 -16.625 39.031  1.00 39.62 ? 100 ILE B CD1 1 
ATOM   2027 N N   . ALA B  1 101 ? -77.206 -13.852 35.957  1.00 38.96 ? 101 ALA B N   1 
ATOM   2028 C CA  . ALA B  1 101 ? -76.264 -12.744 35.821  1.00 37.50 ? 101 ALA B CA  1 
ATOM   2029 C C   . ALA B  1 101 ? -76.208 -12.228 34.389  1.00 37.05 ? 101 ALA B C   1 
ATOM   2030 O O   . ALA B  1 101 ? -76.188 -11.012 34.160  1.00 36.95 ? 101 ALA B O   1 
ATOM   2031 C CB  . ALA B  1 101 ? -74.875 -13.179 36.285  1.00 39.09 ? 101 ALA B CB  1 
ATOM   2032 N N   . LEU B  1 102 ? -76.178 -13.135 33.410  1.00 37.43 ? 102 LEU B N   1 
ATOM   2033 C CA  . LEU B  1 102 ? -76.081 -12.716 32.014  1.00 37.80 ? 102 LEU B CA  1 
ATOM   2034 C C   . LEU B  1 102 ? -77.363 -12.039 31.544  1.00 37.09 ? 102 LEU B C   1 
ATOM   2035 O O   . LEU B  1 102 ? -77.319 -10.976 30.913  1.00 36.91 ? 102 LEU B O   1 
ATOM   2036 C CB  . LEU B  1 102 ? -75.759 -13.914 31.122  1.00 39.96 ? 102 LEU B CB  1 
ATOM   2037 C CG  . LEU B  1 102 ? -74.376 -14.549 31.257  1.00 41.46 ? 102 LEU B CG  1 
ATOM   2038 C CD1 . LEU B  1 102 ? -74.192 -15.613 30.188  1.00 43.44 ? 102 LEU B CD1 1 
ATOM   2039 C CD2 . LEU B  1 102 ? -73.291 -13.498 31.166  1.00 42.30 ? 102 LEU B CD2 1 
ATOM   2040 N N   . ALA B  1 103 ? -78.517 -12.648 31.834  1.00 36.58 ? 103 ALA B N   1 
ATOM   2041 C CA  . ALA B  1 103 ? -79.783 -12.106 31.351  1.00 34.91 ? 103 ALA B CA  1 
ATOM   2042 C C   . ALA B  1 103 ? -80.032 -10.703 31.894  1.00 34.56 ? 103 ALA B C   1 
ATOM   2043 O O   . ALA B  1 103 ? -80.505 -9.823  31.165  1.00 33.43 ? 103 ALA B O   1 
ATOM   2044 C CB  . ALA B  1 103 ? -80.930 -13.044 31.726  1.00 34.29 ? 103 ALA B CB  1 
ATOM   2045 N N   . LEU B  1 104 ? -79.710 -10.473 33.170  1.00 35.56 ? 104 LEU B N   1 
ATOM   2046 C CA  . LEU B  1 104 ? -79.886 -9.147  33.757  1.00 34.52 ? 104 LEU B CA  1 
ATOM   2047 C C   . LEU B  1 104 ? -79.043 -8.104  33.031  1.00 34.55 ? 104 LEU B C   1 
ATOM   2048 O O   . LEU B  1 104 ? -79.539 -7.032  32.667  1.00 34.35 ? 104 LEU B O   1 
ATOM   2049 C CB  . LEU B  1 104 ? -79.529 -9.177  35.243  1.00 34.27 ? 104 LEU B CB  1 
ATOM   2050 C CG  . LEU B  1 104 ? -80.580 -9.725  36.204  1.00 33.24 ? 104 LEU B CG  1 
ATOM   2051 C CD1 . LEU B  1 104 ? -79.995 -9.818  37.597  1.00 35.55 ? 104 LEU B CD1 1 
ATOM   2052 C CD2 . LEU B  1 104 ? -81.809 -8.836  36.200  1.00 34.00 ? 104 LEU B CD2 1 
ATOM   2053 N N   . VAL B  1 105 ? -77.758 -8.399  32.820  1.00 35.07 ? 105 VAL B N   1 
ATOM   2054 C CA  . VAL B  1 105 ? -76.888 -7.453  32.125  1.00 35.47 ? 105 VAL B CA  1 
ATOM   2055 C C   . VAL B  1 105 ? -77.355 -7.255  30.690  1.00 35.50 ? 105 VAL B C   1 
ATOM   2056 O O   . VAL B  1 105 ? -77.365 -6.130  30.173  1.00 35.59 ? 105 VAL B O   1 
ATOM   2057 C CB  . VAL B  1 105 ? -75.426 -7.926  32.176  1.00 35.85 ? 105 VAL B CB  1 
ATOM   2058 C CG1 . VAL B  1 105 ? -74.554 -7.025  31.311  1.00 36.62 ? 105 VAL B CG1 1 
ATOM   2059 C CG2 . VAL B  1 105 ? -74.926 -7.938  33.603  1.00 35.97 ? 105 VAL B CG2 1 
ATOM   2060 N N   . LEU B  1 106 ? -77.734 -8.347  30.023  1.00 35.37 ? 106 LEU B N   1 
ATOM   2061 C CA  . LEU B  1 106 ? -78.180 -8.261  28.637  1.00 35.16 ? 106 LEU B CA  1 
ATOM   2062 C C   . LEU B  1 106 ? -79.446 -7.420  28.509  1.00 34.45 ? 106 LEU B C   1 
ATOM   2063 O O   . LEU B  1 106 ? -79.555 -6.582  27.604  1.00 34.04 ? 106 LEU B O   1 
ATOM   2064 C CB  . LEU B  1 106 ? -78.404 -9.667  28.086  1.00 35.24 ? 106 LEU B CB  1 
ATOM   2065 C CG  . LEU B  1 106 ? -78.732 -9.789  26.602  1.00 35.95 ? 106 LEU B CG  1 
ATOM   2066 C CD1 . LEU B  1 106 ? -77.680 -9.076  25.771  1.00 37.12 ? 106 LEU B CD1 1 
ATOM   2067 C CD2 . LEU B  1 106 ? -78.827 -11.253 26.212  1.00 36.11 ? 106 LEU B CD2 1 
ATOM   2068 N N   . GLY B  1 107 ? -80.410 -7.622  29.412  1.00 34.15 ? 107 GLY B N   1 
ATOM   2069 C CA  . GLY B  1 107 ? -81.646 -6.860  29.339  1.00 32.41 ? 107 GLY B CA  1 
ATOM   2070 C C   . GLY B  1 107 ? -81.438 -5.379  29.582  1.00 31.99 ? 107 GLY B C   1 
ATOM   2071 O O   . GLY B  1 107 ? -82.077 -4.542  28.941  1.00 31.64 ? 107 GLY B O   1 
ATOM   2072 N N   . GLY B  1 108 ? -80.539 -5.034  30.510  1.00 32.49 ? 108 GLY B N   1 
ATOM   2073 C CA  . GLY B  1 108 ? -80.226 -3.637  30.748  1.00 32.46 ? 108 GLY B CA  1 
ATOM   2074 C C   . GLY B  1 108 ? -79.368 -3.018  29.669  1.00 32.62 ? 108 GLY B C   1 
ATOM   2075 O O   . GLY B  1 108 ? -79.504 -1.826  29.379  1.00 32.89 ? 108 GLY B O   1 
ATOM   2076 N N   . ALA B  1 109 ? -78.470 -3.802  29.068  1.00 32.23 ? 109 ALA B N   1 
ATOM   2077 C CA  . ALA B  1 109 ? -77.718 -3.300  27.924  1.00 32.01 ? 109 ALA B CA  1 
ATOM   2078 C C   . ALA B  1 109 ? -78.645 -2.998  26.754  1.00 32.89 ? 109 ALA B C   1 
ATOM   2079 O O   . ALA B  1 109 ? -78.468 -1.992  26.056  1.00 33.02 ? 109 ALA B O   1 
ATOM   2080 C CB  . ALA B  1 109 ? -76.643 -4.305  27.518  1.00 33.67 ? 109 ALA B CB  1 
ATOM   2081 N N   . LEU B  1 110 ? -79.647 -3.852  26.530  1.00 33.18 ? 110 LEU B N   1 
ATOM   2082 C CA  . LEU B  1 110 ? -80.592 -3.607  25.444  1.00 32.69 ? 110 LEU B CA  1 
ATOM   2083 C C   . LEU B  1 110 ? -81.544 -2.462  25.764  1.00 32.82 ? 110 LEU B C   1 
ATOM   2084 O O   . LEU B  1 110 ? -81.986 -1.757  24.852  1.00 33.68 ? 110 LEU B O   1 
ATOM   2085 C CB  . LEU B  1 110 ? -81.379 -4.878  25.136  1.00 30.91 ? 110 LEU B CB  1 
ATOM   2086 C CG  . LEU B  1 110 ? -80.563 -6.038  24.571  1.00 31.20 ? 110 LEU B CG  1 
ATOM   2087 C CD1 . LEU B  1 110 ? -81.404 -7.292  24.579  1.00 31.37 ? 110 LEU B CD1 1 
ATOM   2088 C CD2 . LEU B  1 110 ? -80.063 -5.729  23.163  1.00 32.28 ? 110 LEU B CD2 1 
ATOM   2089 N N   . GLY B  1 111 ? -81.873 -2.263  27.042  1.00 32.89 ? 111 GLY B N   1 
ATOM   2090 C CA  . GLY B  1 111 ? -82.782 -1.186  27.401  1.00 33.40 ? 111 GLY B CA  1 
ATOM   2091 C C   . GLY B  1 111 ? -82.211 0.183   27.088  1.00 34.58 ? 111 GLY B C   1 
ATOM   2092 O O   . GLY B  1 111 ? -82.887 1.034   26.507  1.00 35.41 ? 111 GLY B O   1 
ATOM   2093 N N   . ASN B  1 112 ? -80.952 0.413   27.469  1.00 34.65 ? 112 ASN B N   1 
ATOM   2094 C CA  . ASN B  1 112 ? -80.273 1.652   27.109  1.00 35.02 ? 112 ASN B CA  1 
ATOM   2095 C C   . ASN B  1 112 ? -79.905 1.692   25.632  1.00 37.24 ? 112 ASN B C   1 
ATOM   2096 O O   . ASN B  1 112 ? -79.746 2.783   25.074  1.00 38.87 ? 112 ASN B O   1 
ATOM   2097 C CB  . ASN B  1 112 ? -79.025 1.828   27.972  1.00 33.94 ? 112 ASN B CB  1 
ATOM   2098 C CG  . ASN B  1 112 ? -79.360 2.047   29.428  1.00 33.95 ? 112 ASN B CG  1 
ATOM   2099 O OD1 . ASN B  1 112 ? -80.249 2.830   29.755  1.00 34.67 ? 112 ASN B OD1 1 
ATOM   2100 N ND2 . ASN B  1 112 ? -78.660 1.350   30.312  1.00 33.75 ? 112 ASN B ND2 1 
ATOM   2101 N N   . LEU B  1 113 ? -79.755 0.526   24.998  1.00 37.40 ? 113 LEU B N   1 
ATOM   2102 C CA  . LEU B  1 113 ? -79.534 0.476   23.556  1.00 37.92 ? 113 LEU B CA  1 
ATOM   2103 C C   . LEU B  1 113 ? -80.738 1.026   22.803  1.00 38.26 ? 113 LEU B C   1 
ATOM   2104 O O   . LEU B  1 113 ? -80.595 1.849   21.891  1.00 39.58 ? 113 LEU B O   1 
ATOM   2105 C CB  . LEU B  1 113 ? -79.247 -0.963  23.128  1.00 37.23 ? 113 LEU B CB  1 
ATOM   2106 C CG  . LEU B  1 113 ? -78.755 -1.181  21.699  1.00 38.22 ? 113 LEU B CG  1 
ATOM   2107 C CD1 . LEU B  1 113 ? -77.377 -0.548  21.533  1.00 39.70 ? 113 LEU B CD1 1 
ATOM   2108 C CD2 . LEU B  1 113 ? -78.714 -2.656  21.384  1.00 37.79 ? 113 LEU B CD2 1 
ATOM   2109 N N   . TYR B  1 114 ? -81.939 0.576   23.175  1.00 37.36 ? 114 TYR B N   1 
ATOM   2110 C CA  . TYR B  1 114 ? -83.151 1.134   22.590  1.00 38.60 ? 114 TYR B CA  1 
ATOM   2111 C C   . TYR B  1 114 ? -83.288 2.612   22.915  1.00 40.61 ? 114 TYR B C   1 
ATOM   2112 O O   . TYR B  1 114 ? -83.895 3.364   22.144  1.00 42.92 ? 114 TYR B O   1 
ATOM   2113 C CB  . TYR B  1 114 ? -84.378 0.366   23.089  1.00 38.19 ? 114 TYR B CB  1 
ATOM   2114 C CG  . TYR B  1 114 ? -85.717 0.971   22.702  1.00 39.17 ? 114 TYR B CG  1 
ATOM   2115 C CD1 . TYR B  1 114 ? -86.353 1.890   23.531  1.00 39.71 ? 114 TYR B CD1 1 
ATOM   2116 C CD2 . TYR B  1 114 ? -86.351 0.608   21.520  1.00 39.44 ? 114 TYR B CD2 1 
ATOM   2117 C CE1 . TYR B  1 114 ? -87.568 2.440   23.188  1.00 41.27 ? 114 TYR B CE1 1 
ATOM   2118 C CE2 . TYR B  1 114 ? -87.574 1.150   21.170  1.00 40.86 ? 114 TYR B CE2 1 
ATOM   2119 C CZ  . TYR B  1 114 ? -88.178 2.067   22.008  1.00 42.33 ? 114 TYR B CZ  1 
ATOM   2120 O OH  . TYR B  1 114 ? -89.396 2.616   21.668  1.00 43.30 ? 114 TYR B OH  1 
ATOM   2121 N N   . ASP B  1 115 ? -82.750 3.046   24.047  1.00 39.93 ? 115 ASP B N   1 
ATOM   2122 C CA  . ASP B  1 115 ? -82.874 4.437   24.449  1.00 40.96 ? 115 ASP B CA  1 
ATOM   2123 C C   . ASP B  1 115 ? -81.716 5.301   23.965  1.00 42.10 ? 115 ASP B C   1 
ATOM   2124 O O   . ASP B  1 115 ? -81.697 6.498   24.256  1.00 43.25 ? 115 ASP B O   1 
ATOM   2125 C CB  . ASP B  1 115 ? -83.011 4.531   25.973  1.00 41.31 ? 115 ASP B CB  1 
ATOM   2126 C CG  . ASP B  1 115 ? -84.044 5.565   26.403  1.00 44.10 ? 115 ASP B CG  1 
ATOM   2127 O OD1 . ASP B  1 115 ? -83.741 6.779   26.318  1.00 44.84 ? 115 ASP B OD1 1 
ATOM   2128 O OD2 . ASP B  1 115 ? -85.166 5.163   26.803  1.00 43.92 ? 115 ASP B OD2 1 
ATOM   2129 N N   . ARG B  1 116 ? -80.763 4.738   23.219  1.00 41.74 ? 116 ARG B N   1 
ATOM   2130 C CA  . ARG B  1 116 ? -79.697 5.520   22.602  1.00 41.56 ? 116 ARG B CA  1 
ATOM   2131 C C   . ARG B  1 116 ? -79.784 5.525   21.079  1.00 43.20 ? 116 ARG B C   1 
ATOM   2132 O O   . ARG B  1 116 ? -78.823 5.931   20.420  1.00 43.71 ? 116 ARG B O   1 
ATOM   2133 C CB  . ARG B  1 116 ? -78.323 5.009   23.052  1.00 39.76 ? 116 ARG B CB  1 
ATOM   2134 C CG  . ARG B  1 116 ? -77.815 5.674   24.327  1.00 39.11 ? 116 ARG B CG  1 
ATOM   2135 C CD  . ARG B  1 116 ? -76.738 4.868   25.035  1.00 37.64 ? 116 ARG B CD  1 
ATOM   2136 N NE  . ARG B  1 116 ? -76.126 5.669   26.088  1.00 35.58 ? 116 ARG B NE  1 
ATOM   2137 C CZ  . ARG B  1 116 ? -75.504 5.181   27.152  1.00 36.68 ? 116 ARG B CZ  1 
ATOM   2138 N NH1 . ARG B  1 116 ? -75.382 3.877   27.346  1.00 38.86 ? 116 ARG B NH1 1 
ATOM   2139 N NH2 . ARG B  1 116 ? -75.001 6.023   28.050  1.00 37.05 ? 116 ARG B NH2 1 
ATOM   2140 N N   . MET B  1 117 ? -80.894 5.066   20.505  1.00 43.85 ? 117 MET B N   1 
ATOM   2141 C CA  . MET B  1 117 ? -81.197 5.201   19.083  1.00 44.33 ? 117 MET B CA  1 
ATOM   2142 C C   . MET B  1 117 ? -82.543 5.851   18.848  1.00 44.23 ? 117 MET B C   1 
ATOM   2143 O O   . MET B  1 117 ? -82.666 6.700   17.961  1.00 45.69 ? 117 MET B O   1 
ATOM   2144 C CB  . MET B  1 117 ? -81.195 3.833   18.406  1.00 45.97 ? 117 MET B CB  1 
ATOM   2145 C CG  . MET B  1 117 ? -80.019 2.980   18.774  1.00 46.10 ? 117 MET B CG  1 
ATOM   2146 S SD  . MET B  1 117 ? -80.462 1.242   18.797  1.00 48.33 ? 117 MET B SD  1 
ATOM   2147 C CE  . MET B  1 117 ? -78.900 0.507   18.350  1.00 45.35 ? 117 MET B CE  1 
ATOM   2148 N N   . VAL B  1 118 ? -83.555 5.464   19.621  1.00 44.62 ? 118 VAL B N   1 
ATOM   2149 C CA  . VAL B  1 118 ? -84.847 6.126   19.546  1.00 46.58 ? 118 VAL B CA  1 
ATOM   2150 C C   . VAL B  1 118 ? -84.755 7.519   20.150  1.00 47.63 ? 118 VAL B C   1 
ATOM   2151 O O   . VAL B  1 118 ? -85.291 8.482   19.595  1.00 47.66 ? 118 VAL B O   1 
ATOM   2152 C CB  . VAL B  1 118 ? -85.922 5.261   20.227  1.00 45.82 ? 118 VAL B CB  1 
ATOM   2153 C CG1 . VAL B  1 118 ? -87.301 5.929   20.135  1.00 46.12 ? 118 VAL B CG1 1 
ATOM   2154 C CG2 . VAL B  1 118 ? -85.946 3.880   19.597  1.00 44.82 ? 118 VAL B CG2 1 
ATOM   2155 N N   . LEU B  1 119 ? -84.064 7.652   21.281  1.00 46.97 ? 119 LEU B N   1 
ATOM   2156 C CA  . LEU B  1 119 ? -83.735 8.943   21.867  1.00 46.09 ? 119 LEU B CA  1 
ATOM   2157 C C   . LEU B  1 119 ? -82.218 9.079   21.879  1.00 45.47 ? 119 LEU B C   1 
ATOM   2158 O O   . LEU B  1 119 ? -81.504 8.105   22.138  1.00 45.25 ? 119 LEU B O   1 
ATOM   2159 C CB  . LEU B  1 119 ? -84.313 9.079   23.288  1.00 44.68 ? 119 LEU B CB  1 
ATOM   2160 C CG  . LEU B  1 119 ? -85.682 8.429   23.552  1.00 44.80 ? 119 LEU B CG  1 
ATOM   2161 C CD1 . LEU B  1 119 ? -86.072 8.569   25.015  1.00 42.06 ? 119 LEU B CD1 1 
ATOM   2162 C CD2 . LEU B  1 119 ? -86.779 8.998   22.656  1.00 46.41 ? 119 LEU B CD2 1 
ATOM   2163 N N   . GLY B  1 120 ? -81.717 10.275  21.569  1.00 45.06 ? 120 GLY B N   1 
ATOM   2164 C CA  . GLY B  1 120 ? -80.275 10.471  21.532  1.00 44.62 ? 120 GLY B CA  1 
ATOM   2165 C C   . GLY B  1 120 ? -79.605 10.327  22.881  1.00 42.55 ? 120 GLY B C   1 
ATOM   2166 O O   . GLY B  1 120 ? -78.383 10.141  22.946  1.00 41.26 ? 120 GLY B O   1 
ATOM   2167 N N   . HIS B  1 121 ? -80.383 10.373  23.954  1.00 42.89 ? 121 HIS B N   1 
ATOM   2168 C CA  . HIS B  1 121 ? -79.904 10.381  25.325  1.00 41.95 ? 121 HIS B CA  1 
ATOM   2169 C C   . HIS B  1 121 ? -80.582 9.270   26.117  1.00 41.32 ? 121 HIS B C   1 
ATOM   2170 O O   . HIS B  1 121 ? -81.597 8.708   25.700  1.00 42.70 ? 121 HIS B O   1 
ATOM   2171 C CB  . HIS B  1 121 ? -80.194 11.734  25.974  1.00 40.26 ? 121 HIS B CB  1 
ATOM   2172 C CG  . HIS B  1 121 ? -81.604 12.188  25.775  1.00 39.82 ? 121 HIS B CG  1 
ATOM   2173 N ND1 . HIS B  1 121 ? -82.671 11.595  26.416  1.00 39.17 ? 121 HIS B ND1 1 
ATOM   2174 C CD2 . HIS B  1 121 ? -82.130 13.145  24.974  1.00 40.54 ? 121 HIS B CD2 1 
ATOM   2175 C CE1 . HIS B  1 121 ? -83.790 12.184  26.035  1.00 39.76 ? 121 HIS B CE1 1 
ATOM   2176 N NE2 . HIS B  1 121 ? -83.490 13.128  25.162  1.00 40.58 ? 121 HIS B NE2 1 
ATOM   2177 N N   . VAL B  1 122 ? -80.030 8.969   27.288  1.00 39.29 ? 122 VAL B N   1 
ATOM   2178 C CA  . VAL B  1 122 ? -80.601 7.971   28.183  1.00 38.10 ? 122 VAL B CA  1 
ATOM   2179 C C   . VAL B  1 122 ? -81.497 8.671   29.192  1.00 37.53 ? 122 VAL B C   1 
ATOM   2180 O O   . VAL B  1 122 ? -81.073 9.626   29.854  1.00 37.59 ? 122 VAL B O   1 
ATOM   2181 C CB  . VAL B  1 122 ? -79.507 7.162   28.894  1.00 37.49 ? 122 VAL B CB  1 
ATOM   2182 C CG1 . VAL B  1 122 ? -80.137 6.182   29.861  1.00 36.81 ? 122 VAL B CG1 1 
ATOM   2183 C CG2 . VAL B  1 122 ? -78.665 6.431   27.877  1.00 38.23 ? 122 VAL B CG2 1 
ATOM   2184 N N   . VAL B  1 123 ? -82.731 8.200   29.310  1.00 37.03 ? 123 VAL B N   1 
ATOM   2185 C CA  . VAL B  1 123 ? -83.654 8.731   30.304  1.00 36.01 ? 123 VAL B CA  1 
ATOM   2186 C C   . VAL B  1 123 ? -83.365 8.079   31.650  1.00 35.53 ? 123 VAL B C   1 
ATOM   2187 O O   . VAL B  1 123 ? -83.319 6.848   31.763  1.00 36.06 ? 123 VAL B O   1 
ATOM   2188 C CB  . VAL B  1 123 ? -85.110 8.501   29.872  1.00 36.08 ? 123 VAL B CB  1 
ATOM   2189 C CG1 . VAL B  1 123 ? -86.064 9.049   30.918  1.00 34.38 ? 123 VAL B CG1 1 
ATOM   2190 C CG2 . VAL B  1 123 ? -85.361 9.143   28.521  1.00 36.96 ? 123 VAL B CG2 1 
ATOM   2191 N N   . ASP B  1 124 ? -83.164 8.905   32.674  1.00 34.63 ? 124 ASP B N   1 
ATOM   2192 C CA  . ASP B  1 124 ? -82.869 8.440   34.021  1.00 34.54 ? 124 ASP B CA  1 
ATOM   2193 C C   . ASP B  1 124 ? -83.762 9.168   35.017  1.00 34.79 ? 124 ASP B C   1 
ATOM   2194 O O   . ASP B  1 124 ? -84.096 10.341  34.830  1.00 36.01 ? 124 ASP B O   1 
ATOM   2195 C CB  . ASP B  1 124 ? -81.399 8.659   34.361  1.00 34.94 ? 124 ASP B CB  1 
ATOM   2196 C CG  . ASP B  1 124 ? -80.475 8.007   33.358  1.00 35.90 ? 124 ASP B CG  1 
ATOM   2197 O OD1 . ASP B  1 124 ? -80.752 6.858   32.954  1.00 35.21 ? 124 ASP B OD1 1 
ATOM   2198 O OD2 . ASP B  1 124 ? -79.478 8.647   32.962  1.00 37.23 ? 124 ASP B OD2 1 
ATOM   2199 N N   . PHE B  1 125 ? -84.157 8.460   36.082  1.00 33.77 ? 125 PHE B N   1 
ATOM   2200 C CA  . PHE B  1 125 ? -85.096 9.029   37.039  1.00 32.94 ? 125 PHE B CA  1 
ATOM   2201 C C   . PHE B  1 125 ? -84.826 8.698   38.504  1.00 33.30 ? 125 PHE B C   1 
ATOM   2202 O O   . PHE B  1 125 ? -85.593 9.148   39.363  1.00 33.59 ? 125 PHE B O   1 
ATOM   2203 C CB  . PHE B  1 125 ? -86.538 8.604   36.681  1.00 32.59 ? 125 PHE B CB  1 
ATOM   2204 C CG  . PHE B  1 125 ? -86.673 7.164   36.252  1.00 32.42 ? 125 PHE B CG  1 
ATOM   2205 C CD1 . PHE B  1 125 ? -86.601 6.139   37.180  1.00 32.55 ? 125 PHE B CD1 1 
ATOM   2206 C CD2 . PHE B  1 125 ? -86.906 6.840   34.925  1.00 32.41 ? 125 PHE B CD2 1 
ATOM   2207 C CE1 . PHE B  1 125 ? -86.733 4.821   36.793  1.00 32.11 ? 125 PHE B CE1 1 
ATOM   2208 C CE2 . PHE B  1 125 ? -87.041 5.523   34.533  1.00 32.36 ? 125 PHE B CE2 1 
ATOM   2209 C CZ  . PHE B  1 125 ? -86.954 4.512   35.468  1.00 32.26 ? 125 PHE B CZ  1 
ATOM   2210 N N   . ILE B  1 126 ? -83.765 7.964   38.827  1.00 33.64 ? 126 ILE B N   1 
ATOM   2211 C CA  . ILE B  1 126 ? -83.479 7.555   40.200  1.00 33.43 ? 126 ILE B CA  1 
ATOM   2212 C C   . ILE B  1 126 ? -82.271 8.346   40.684  1.00 34.60 ? 126 ILE B C   1 
ATOM   2213 O O   . ILE B  1 126 ? -81.134 8.067   40.284  1.00 36.07 ? 126 ILE B O   1 
ATOM   2214 C CB  . ILE B  1 126 ? -83.235 6.042   40.310  1.00 34.00 ? 126 ILE B CB  1 
ATOM   2215 C CG1 . ILE B  1 126 ? -84.413 5.261   39.724  1.00 33.86 ? 126 ILE B CG1 1 
ATOM   2216 C CG2 . ILE B  1 126 ? -83.013 5.647   41.759  1.00 35.10 ? 126 ILE B CG2 1 
ATOM   2217 C CD1 . ILE B  1 126 ? -84.183 3.760   39.646  1.00 33.09 ? 126 ILE B CD1 1 
ATOM   2218 N N   . LEU B  1 127 ? -82.512 9.319   41.566  1.00 34.35 ? 127 LEU B N   1 
ATOM   2219 C CA  . LEU B  1 127 ? -81.465 10.193  42.096  1.00 34.55 ? 127 LEU B CA  1 
ATOM   2220 C C   . LEU B  1 127 ? -81.122 9.763   43.520  1.00 35.45 ? 127 LEU B C   1 
ATOM   2221 O O   . LEU B  1 127 ? -81.832 10.100  44.471  1.00 35.67 ? 127 LEU B O   1 
ATOM   2222 C CB  . LEU B  1 127 ? -81.908 11.652  42.048  1.00 33.83 ? 127 LEU B CB  1 
ATOM   2223 C CG  . LEU B  1 127 ? -80.987 12.683  42.704  1.00 34.07 ? 127 LEU B CG  1 
ATOM   2224 C CD1 . LEU B  1 127 ? -79.600 12.635  42.093  1.00 35.15 ? 127 LEU B CD1 1 
ATOM   2225 C CD2 . LEU B  1 127 ? -81.570 14.080  42.593  1.00 33.20 ? 127 LEU B CD2 1 
ATOM   2226 N N   . VAL B  1 128 ? -80.032 9.016   43.664  1.00 35.64 ? 128 VAL B N   1 
ATOM   2227 C CA  . VAL B  1 128 ? -79.465 8.733   44.978  1.00 34.90 ? 128 VAL B CA  1 
ATOM   2228 C C   . VAL B  1 128 ? -78.557 9.891   45.363  1.00 36.11 ? 128 VAL B C   1 
ATOM   2229 O O   . VAL B  1 128 ? -77.739 10.345  44.555  1.00 37.09 ? 128 VAL B O   1 
ATOM   2230 C CB  . VAL B  1 128 ? -78.702 7.399   44.966  1.00 33.88 ? 128 VAL B CB  1 
ATOM   2231 C CG1 . VAL B  1 128 ? -77.821 7.274   46.199  1.00 33.98 ? 128 VAL B CG1 1 
ATOM   2232 C CG2 . VAL B  1 128 ? -79.678 6.232   44.878  1.00 34.05 ? 128 VAL B CG2 1 
ATOM   2233 N N   . HIS B  1 129 ? -78.709 10.395  46.584  1.00 36.16 ? 129 HIS B N   1 
ATOM   2234 C CA  . HIS B  1 129 ? -77.877 11.505  47.035  1.00 36.76 ? 129 HIS B CA  1 
ATOM   2235 C C   . HIS B  1 129 ? -77.767 11.460  48.556  1.00 36.69 ? 129 HIS B C   1 
ATOM   2236 O O   . HIS B  1 129 ? -78.124 10.466  49.197  1.00 36.82 ? 129 HIS B O   1 
ATOM   2237 C CB  . HIS B  1 129 ? -78.436 12.846  46.544  1.00 36.82 ? 129 HIS B CB  1 
ATOM   2238 C CG  . HIS B  1 129 ? -79.760 13.209  47.141  1.00 35.95 ? 129 HIS B CG  1 
ATOM   2239 N ND1 . HIS B  1 129 ? -79.973 14.393  47.814  1.00 35.50 ? 129 HIS B ND1 1 
ATOM   2240 C CD2 . HIS B  1 129 ? -80.942 12.547  47.159  1.00 35.89 ? 129 HIS B CD2 1 
ATOM   2241 C CE1 . HIS B  1 129 ? -81.228 14.441  48.227  1.00 35.19 ? 129 HIS B CE1 1 
ATOM   2242 N NE2 . HIS B  1 129 ? -81.837 13.334  47.842  1.00 35.59 ? 129 HIS B NE2 1 
ATOM   2243 N N   . TRP B  1 130 ? -77.244 12.538  49.133  1.00 36.78 ? 130 TRP B N   1 
ATOM   2244 C CA  . TRP B  1 130 ? -77.175 12.678  50.585  1.00 36.17 ? 130 TRP B CA  1 
ATOM   2245 C C   . TRP B  1 130 ? -77.246 14.170  50.893  1.00 36.28 ? 130 TRP B C   1 
ATOM   2246 O O   . TRP B  1 130 ? -76.227 14.865  50.823  1.00 36.88 ? 130 TRP B O   1 
ATOM   2247 C CB  . TRP B  1 130 ? -75.909 12.048  51.146  1.00 37.04 ? 130 TRP B CB  1 
ATOM   2248 C CG  . TRP B  1 130 ? -75.641 12.466  52.551  1.00 36.83 ? 130 TRP B CG  1 
ATOM   2249 C CD1 . TRP B  1 130 ? -74.653 13.303  52.987  1.00 37.24 ? 130 TRP B CD1 1 
ATOM   2250 C CD2 . TRP B  1 130 ? -76.390 12.091  53.710  1.00 36.49 ? 130 TRP B CD2 1 
ATOM   2251 N NE1 . TRP B  1 130 ? -74.735 13.462  54.349  1.00 37.14 ? 130 TRP B NE1 1 
ATOM   2252 C CE2 . TRP B  1 130 ? -75.793 12.727  54.817  1.00 36.54 ? 130 TRP B CE2 1 
ATOM   2253 C CE3 . TRP B  1 130 ? -77.502 11.271  53.921  1.00 35.99 ? 130 TRP B CE3 1 
ATOM   2254 C CZ2 . TRP B  1 130 ? -76.274 12.571  56.115  1.00 36.51 ? 130 TRP B CZ2 1 
ATOM   2255 C CZ3 . TRP B  1 130 ? -77.978 11.118  55.209  1.00 35.55 ? 130 TRP B CZ3 1 
ATOM   2256 C CH2 . TRP B  1 130 ? -77.365 11.764  56.289  1.00 36.03 ? 130 TRP B CH2 1 
ATOM   2257 N N   . GLN B  1 131 ? -78.445 14.647  51.232  1.00 35.60 ? 131 GLN B N   1 
ATOM   2258 C CA  . GLN B  1 131 ? -78.673 16.063  51.506  1.00 34.67 ? 131 GLN B CA  1 
ATOM   2259 C C   . GLN B  1 131 ? -78.114 16.918  50.377  1.00 35.33 ? 131 GLN B C   1 
ATOM   2260 O O   . GLN B  1 131 ? -78.237 16.558  49.203  1.00 35.94 ? 131 GLN B O   1 
ATOM   2261 C CB  . GLN B  1 131 ? -78.048 16.466  52.843  1.00 34.85 ? 131 GLN B CB  1 
ATOM   2262 C CG  . GLN B  1 131 ? -78.721 15.841  54.052  1.00 34.76 ? 131 GLN B CG  1 
ATOM   2263 C CD  . GLN B  1 131 ? -77.918 16.010  55.326  1.00 34.10 ? 131 GLN B CD  1 
ATOM   2264 O OE1 . GLN B  1 131 ? -76.932 16.746  55.363  1.00 34.53 ? 131 GLN B OE1 1 
ATOM   2265 N NE2 . GLN B  1 131 ? -78.334 15.321  56.379  1.00 34.23 ? 131 GLN B NE2 1 
ATOM   2266 N N   . ASN B  1 132 ? -77.478 18.038  50.720  1.00 36.07 ? 132 ASN B N   1 
ATOM   2267 C CA  . ASN B  1 132 ? -76.892 18.944  49.740  1.00 35.89 ? 132 ASN B CA  1 
ATOM   2268 C C   . ASN B  1 132 ? -75.369 18.845  49.710  1.00 35.99 ? 132 ASN B C   1 
ATOM   2269 O O   . ASN B  1 132 ? -74.682 19.816  49.381  1.00 36.32 ? 132 ASN B O   1 
ATOM   2270 C CB  . ASN B  1 132 ? -77.324 20.382  50.017  1.00 35.54 ? 132 ASN B CB  1 
ATOM   2271 C CG  . ASN B  1 132 ? -78.833 20.577  49.896  1.00 34.82 ? 132 ASN B CG  1 
ATOM   2272 O OD1 . ASN B  1 132 ? -79.475 20.038  48.990  1.00 34.63 ? 132 ASN B OD1 1 
ATOM   2273 N ND2 . ASN B  1 132 ? -79.406 21.342  50.821  1.00 33.27 ? 132 ASN B ND2 1 
ATOM   2274 N N   . ARG B  1 133 ? -74.826 17.678  50.049  1.00 37.14 ? 133 ARG B N   1 
ATOM   2275 C CA  . ARG B  1 133 ? -73.386 17.456  50.003  1.00 38.83 ? 133 ARG B CA  1 
ATOM   2276 C C   . ARG B  1 133 ? -72.946 16.798  48.703  1.00 39.00 ? 133 ARG B C   1 
ATOM   2277 O O   . ARG B  1 133 ? -72.001 17.265  48.064  1.00 39.09 ? 133 ARG B O   1 
ATOM   2278 C CB  . ARG B  1 133 ? -72.939 16.600  51.194  1.00 41.39 ? 133 ARG B CB  1 
ATOM   2279 C CG  . ARG B  1 133 ? -73.144 17.246  52.558  1.00 42.08 ? 133 ARG B CG  1 
ATOM   2280 C CD  . ARG B  1 133 ? -72.201 18.419  52.762  1.00 45.16 ? 133 ARG B CD  1 
ATOM   2281 N NE  . ARG B  1 133 ? -72.394 19.069  54.054  1.00 49.57 ? 133 ARG B NE  1 
ATOM   2282 C CZ  . ARG B  1 133 ? -71.649 18.844  55.129  1.00 50.47 ? 133 ARG B CZ  1 
ATOM   2283 N NH1 . ARG B  1 133 ? -70.647 17.978  55.108  1.00 49.38 ? 133 ARG B NH1 1 
ATOM   2284 N NH2 . ARG B  1 133 ? -71.915 19.506  56.254  1.00 50.28 ? 133 ARG B NH2 1 
ATOM   2285 N N   . TRP B  1 134 ? -73.609 15.717  48.295  1.00 39.28 ? 134 TRP B N   1 
ATOM   2286 C CA  . TRP B  1 134 ? -73.246 15.042  47.058  1.00 39.94 ? 134 TRP B CA  1 
ATOM   2287 C C   . TRP B  1 134 ? -74.475 14.387  46.446  1.00 39.54 ? 134 TRP B C   1 
ATOM   2288 O O   . TRP B  1 134 ? -75.368 13.925  47.160  1.00 38.76 ? 134 TRP B O   1 
ATOM   2289 C CB  . TRP B  1 134 ? -72.153 13.993  47.288  1.00 41.34 ? 134 TRP B CB  1 
ATOM   2290 C CG  . TRP B  1 134 ? -72.529 12.914  48.257  1.00 41.36 ? 134 TRP B CG  1 
ATOM   2291 C CD1 . TRP B  1 134 ? -72.354 12.932  49.610  1.00 41.62 ? 134 TRP B CD1 1 
ATOM   2292 C CD2 . TRP B  1 134 ? -73.125 11.645  47.946  1.00 41.23 ? 134 TRP B CD2 1 
ATOM   2293 N NE1 . TRP B  1 134 ? -72.808 11.758  50.164  1.00 42.19 ? 134 TRP B NE1 1 
ATOM   2294 C CE2 . TRP B  1 134 ? -73.288 10.952  49.164  1.00 42.01 ? 134 TRP B CE2 1 
ATOM   2295 C CE3 . TRP B  1 134 ? -73.539 11.031  46.759  1.00 40.18 ? 134 TRP B CE3 1 
ATOM   2296 C CZ2 . TRP B  1 134 ? -73.847 9.674   49.230  1.00 41.58 ? 134 TRP B CZ2 1 
ATOM   2297 C CZ3 . TRP B  1 134 ? -74.094 9.761   46.826  1.00 40.24 ? 134 TRP B CZ3 1 
ATOM   2298 C CH2 . TRP B  1 134 ? -74.243 9.098   48.053  1.00 41.78 ? 134 TRP B CH2 1 
ATOM   2299 N N   . TYR B  1 135 ? -74.503 14.344  45.113  1.00 39.53 ? 135 TYR B N   1 
ATOM   2300 C CA  . TYR B  1 135 ? -75.599 13.742  44.357  1.00 38.41 ? 135 TYR B CA  1 
ATOM   2301 C C   . TYR B  1 135 ? -75.025 12.706  43.399  1.00 38.91 ? 135 TYR B C   1 
ATOM   2302 O O   . TYR B  1 135 ? -74.373 13.062  42.411  1.00 40.67 ? 135 TYR B O   1 
ATOM   2303 C CB  . TYR B  1 135 ? -76.391 14.800  43.588  1.00 37.29 ? 135 TYR B CB  1 
ATOM   2304 C CG  . TYR B  1 135 ? -77.281 15.680  44.436  1.00 37.35 ? 135 TYR B CG  1 
ATOM   2305 C CD1 . TYR B  1 135 ? -76.745 16.683  45.233  1.00 37.75 ? 135 TYR B CD1 1 
ATOM   2306 C CD2 . TYR B  1 135 ? -78.662 15.532  44.410  1.00 36.86 ? 135 TYR B CD2 1 
ATOM   2307 C CE1 . TYR B  1 135 ? -77.559 17.501  45.999  1.00 36.79 ? 135 TYR B CE1 1 
ATOM   2308 C CE2 . TYR B  1 135 ? -79.486 16.344  45.171  1.00 35.99 ? 135 TYR B CE2 1 
ATOM   2309 C CZ  . TYR B  1 135 ? -78.929 17.328  45.963  1.00 35.91 ? 135 TYR B CZ  1 
ATOM   2310 O OH  . TYR B  1 135 ? -79.742 18.139  46.721  1.00 34.94 ? 135 TYR B OH  1 
ATOM   2311 N N   . PHE B  1 136 ? -75.264 11.430  43.694  1.00 37.82 ? 136 PHE B N   1 
ATOM   2312 C CA  . PHE B  1 136 ? -74.945 10.369  42.746  1.00 37.29 ? 136 PHE B CA  1 
ATOM   2313 C C   . PHE B  1 136 ? -75.828 10.515  41.504  1.00 38.17 ? 136 PHE B C   1 
ATOM   2314 O O   . PHE B  1 136 ? -77.027 10.791  41.621  1.00 38.58 ? 136 PHE B O   1 
ATOM   2315 C CB  . PHE B  1 136 ? -75.140 8.995   43.405  1.00 37.00 ? 136 PHE B CB  1 
ATOM   2316 C CG  . PHE B  1 136 ? -74.661 7.821   42.576  1.00 35.53 ? 136 PHE B CG  1 
ATOM   2317 C CD1 . PHE B  1 136 ? -73.326 7.680   42.242  1.00 34.95 ? 136 PHE B CD1 1 
ATOM   2318 C CD2 . PHE B  1 136 ? -75.547 6.825   42.192  1.00 35.14 ? 136 PHE B CD2 1 
ATOM   2319 C CE1 . PHE B  1 136 ? -72.892 6.600   41.499  1.00 34.28 ? 136 PHE B CE1 1 
ATOM   2320 C CE2 . PHE B  1 136 ? -75.117 5.737   41.453  1.00 34.22 ? 136 PHE B CE2 1 
ATOM   2321 C CZ  . PHE B  1 136 ? -73.788 5.625   41.108  1.00 34.55 ? 136 PHE B CZ  1 
ATOM   2322 N N   . PRO B  1 137 ? -75.262 10.357  40.308  1.00 38.37 ? 137 PRO B N   1 
ATOM   2323 C CA  . PRO B  1 137 ? -76.016 10.654  39.083  1.00 38.39 ? 137 PRO B CA  1 
ATOM   2324 C C   . PRO B  1 137 ? -77.279 9.815   38.937  1.00 37.47 ? 137 PRO B C   1 
ATOM   2325 O O   . PRO B  1 137 ? -77.356 8.669   39.388  1.00 37.21 ? 137 PRO B O   1 
ATOM   2326 C CB  . PRO B  1 137 ? -75.008 10.343  37.971  1.00 37.44 ? 137 PRO B CB  1 
ATOM   2327 C CG  . PRO B  1 137 ? -73.679 10.556  38.607  1.00 37.55 ? 137 PRO B CG  1 
ATOM   2328 C CD  . PRO B  1 137 ? -73.839 10.108  40.031  1.00 37.59 ? 137 PRO B CD  1 
ATOM   2329 N N   . ALA B  1 138 ? -78.277 10.410  38.286  1.00 36.21 ? 138 ALA B N   1 
ATOM   2330 C CA  . ALA B  1 138 ? -79.526 9.711   38.030  1.00 35.63 ? 138 ALA B CA  1 
ATOM   2331 C C   . ALA B  1 138 ? -79.284 8.517   37.118  1.00 36.38 ? 138 ALA B C   1 
ATOM   2332 O O   . ALA B  1 138 ? -78.435 8.560   36.222  1.00 37.55 ? 138 ALA B O   1 
ATOM   2333 C CB  . ALA B  1 138 ? -80.556 10.653  37.404  1.00 35.40 ? 138 ALA B CB  1 
ATOM   2334 N N   . PHE B  1 139 ? -80.025 7.440   37.366  1.00 35.55 ? 139 PHE B N   1 
ATOM   2335 C CA  . PHE B  1 139 ? -79.942 6.222   36.574  1.00 34.76 ? 139 PHE B CA  1 
ATOM   2336 C C   . PHE B  1 139 ? -81.350 5.657   36.448  1.00 33.97 ? 139 PHE B C   1 
ATOM   2337 O O   . PHE B  1 139 ? -82.334 6.308   36.812  1.00 33.89 ? 139 PHE B O   1 
ATOM   2338 C CB  . PHE B  1 139 ? -78.952 5.230   37.199  1.00 34.95 ? 139 PHE B CB  1 
ATOM   2339 C CG  . PHE B  1 139 ? -79.235 4.911   38.641  1.00 35.49 ? 139 PHE B CG  1 
ATOM   2340 C CD1 . PHE B  1 139 ? -80.085 3.869   38.979  1.00 35.16 ? 139 PHE B CD1 1 
ATOM   2341 C CD2 . PHE B  1 139 ? -78.644 5.647   39.658  1.00 34.92 ? 139 PHE B CD2 1 
ATOM   2342 C CE1 . PHE B  1 139 ? -80.344 3.570   40.303  1.00 34.74 ? 139 PHE B CE1 1 
ATOM   2343 C CE2 . PHE B  1 139 ? -78.899 5.353   40.984  1.00 33.97 ? 139 PHE B CE2 1 
ATOM   2344 C CZ  . PHE B  1 139 ? -79.750 4.313   41.306  1.00 34.24 ? 139 PHE B CZ  1 
ATOM   2345 N N   . ASN B  1 140 ? -81.454 4.435   35.932  1.00 33.41 ? 140 ASN B N   1 
ATOM   2346 C CA  . ASN B  1 140 ? -82.752 3.827   35.665  1.00 33.24 ? 140 ASN B CA  1 
ATOM   2347 C C   . ASN B  1 140 ? -82.687 2.349   36.037  1.00 32.71 ? 140 ASN B C   1 
ATOM   2348 O O   . ASN B  1 140 ? -81.731 1.884   36.667  1.00 32.73 ? 140 ASN B O   1 
ATOM   2349 C CB  . ASN B  1 140 ? -83.158 4.045   34.201  1.00 33.45 ? 140 ASN B CB  1 
ATOM   2350 C CG  . ASN B  1 140 ? -82.081 3.612   33.231  1.00 33.46 ? 140 ASN B CG  1 
ATOM   2351 O OD1 . ASN B  1 140 ? -82.017 2.450   32.840  1.00 33.54 ? 140 ASN B OD1 1 
ATOM   2352 N ND2 . ASN B  1 140 ? -81.224 4.548   32.837  1.00 34.00 ? 140 ASN B ND2 1 
ATOM   2353 N N   . LEU B  1 141 ? -83.731 1.609   35.654  1.00 32.51 ? 141 LEU B N   1 
ATOM   2354 C CA  . LEU B  1 141 ? -83.810 0.198   36.012  1.00 32.30 ? 141 LEU B CA  1 
ATOM   2355 C C   . LEU B  1 141 ? -82.853 -0.651  35.186  1.00 32.07 ? 141 LEU B C   1 
ATOM   2356 O O   . LEU B  1 141 ? -82.312 -1.638  35.695  1.00 32.52 ? 141 LEU B O   1 
ATOM   2357 C CB  . LEU B  1 141 ? -85.245 -0.306  35.847  1.00 32.86 ? 141 LEU B CB  1 
ATOM   2358 C CG  . LEU B  1 141 ? -86.364 0.532   36.479  1.00 33.52 ? 141 LEU B CG  1 
ATOM   2359 C CD1 . LEU B  1 141 ? -87.690 -0.210  36.403  1.00 33.77 ? 141 LEU B CD1 1 
ATOM   2360 C CD2 . LEU B  1 141 ? -86.034 0.921   37.917  1.00 32.84 ? 141 LEU B CD2 1 
ATOM   2361 N N   . ALA B  1 142 ? -82.631 -0.289  33.919  1.00 31.63 ? 142 ALA B N   1 
ATOM   2362 C CA  . ALA B  1 142 ? -81.682 -1.035  33.100  1.00 31.47 ? 142 ALA B CA  1 
ATOM   2363 C C   . ALA B  1 142 ? -80.282 -0.968  33.694  1.00 32.62 ? 142 ALA B C   1 
ATOM   2364 O O   . ALA B  1 142 ? -79.563 -1.973  33.722  1.00 33.75 ? 142 ALA B O   1 
ATOM   2365 C CB  . ALA B  1 142 ? -81.689 -0.506  31.666  1.00 31.51 ? 142 ALA B CB  1 
ATOM   2366 N N   . ASP B  1 143 ? -79.879 0.208   34.182  1.00 32.67 ? 143 ASP B N   1 
ATOM   2367 C CA  . ASP B  1 143 ? -78.609 0.315   34.893  1.00 32.45 ? 143 ASP B CA  1 
ATOM   2368 C C   . ASP B  1 143 ? -78.622 -0.531  36.156  1.00 32.25 ? 143 ASP B C   1 
ATOM   2369 O O   . ASP B  1 143 ? -77.604 -1.128  36.524  1.00 32.44 ? 143 ASP B O   1 
ATOM   2370 C CB  . ASP B  1 143 ? -78.319 1.773   35.238  1.00 33.51 ? 143 ASP B CB  1 
ATOM   2371 C CG  . ASP B  1 143 ? -78.574 2.705   34.076  1.00 34.66 ? 143 ASP B CG  1 
ATOM   2372 O OD1 . ASP B  1 143 ? -78.147 2.383   32.946  1.00 35.73 ? 143 ASP B OD1 1 
ATOM   2373 O OD2 . ASP B  1 143 ? -79.212 3.757   34.294  1.00 34.51 ? 143 ASP B OD2 1 
ATOM   2374 N N   . SER B  1 144 ? -79.765 -0.580  36.845  1.00 31.66 ? 144 SER B N   1 
ATOM   2375 C CA  . SER B  1 144 ? -79.880 -1.420  38.030  1.00 31.93 ? 144 SER B CA  1 
ATOM   2376 C C   . SER B  1 144 ? -79.680 -2.890  37.691  1.00 33.54 ? 144 SER B C   1 
ATOM   2377 O O   . SER B  1 144 ? -79.111 -3.639  38.491  1.00 35.12 ? 144 SER B O   1 
ATOM   2378 C CB  . SER B  1 144 ? -81.238 -1.200  38.693  1.00 31.55 ? 144 SER B CB  1 
ATOM   2379 O OG  . SER B  1 144 ? -81.520 0.183   38.803  1.00 31.48 ? 144 SER B OG  1 
ATOM   2380 N N   . ALA B  1 145 ? -80.130 -3.320  36.511  1.00 33.16 ? 145 ALA B N   1 
ATOM   2381 C CA  . ALA B  1 145 ? -79.904 -4.698  36.091  1.00 32.67 ? 145 ALA B CA  1 
ATOM   2382 C C   . ALA B  1 145 ? -78.455 -4.931  35.686  1.00 33.54 ? 145 ALA B C   1 
ATOM   2383 O O   . ALA B  1 145 ? -77.879 -5.974  36.013  1.00 34.20 ? 145 ALA B O   1 
ATOM   2384 C CB  . ALA B  1 145 ? -80.836 -5.052  34.935  1.00 32.39 ? 145 ALA B CB  1 
ATOM   2385 N N   . ILE B  1 146 ? -77.854 -3.977  34.973  1.00 33.71 ? 146 ILE B N   1 
ATOM   2386 C CA  . ILE B  1 146 ? -76.476 -4.140  34.515  1.00 34.72 ? 146 ILE B CA  1 
ATOM   2387 C C   . ILE B  1 146 ? -75.521 -4.221  35.699  1.00 35.13 ? 146 ILE B C   1 
ATOM   2388 O O   . ILE B  1 146 ? -74.652 -5.098  35.759  1.00 35.17 ? 146 ILE B O   1 
ATOM   2389 C CB  . ILE B  1 146 ? -76.089 -2.995  33.564  1.00 34.80 ? 146 ILE B CB  1 
ATOM   2390 C CG1 . ILE B  1 146 ? -76.836 -3.134  32.239  1.00 33.87 ? 146 ILE B CG1 1 
ATOM   2391 C CG2 . ILE B  1 146 ? -74.577 -2.957  33.357  1.00 36.53 ? 146 ILE B CG2 1 
ATOM   2392 C CD1 . ILE B  1 146 ? -76.480 -2.074  31.236  1.00 34.84 ? 146 ILE B CD1 1 
ATOM   2393 N N   . THR B  1 147 ? -75.661 -3.295  36.651  1.00 35.56 ? 147 THR B N   1 
ATOM   2394 C CA  . THR B  1 147 ? -74.758 -3.260  37.798  1.00 35.34 ? 147 THR B CA  1 
ATOM   2395 C C   . THR B  1 147 ? -74.930 -4.488  38.684  1.00 35.80 ? 147 THR B C   1 
ATOM   2396 O O   . THR B  1 147 ? -73.941 -5.062  39.155  1.00 36.48 ? 147 THR B O   1 
ATOM   2397 C CB  . THR B  1 147 ? -74.990 -1.984  38.605  1.00 35.75 ? 147 THR B CB  1 
ATOM   2398 O OG1 . THR B  1 147 ? -74.654 -0.844  37.803  1.00 36.76 ? 147 THR B OG1 1 
ATOM   2399 C CG2 . THR B  1 147 ? -74.132 -1.979  39.856  1.00 36.55 ? 147 THR B CG2 1 
ATOM   2400 N N   . VAL B  1 148 ? -76.176 -4.899  38.930  1.00 36.15 ? 148 VAL B N   1 
ATOM   2401 C CA  . VAL B  1 148 ? -76.425 -6.076  39.757  1.00 37.09 ? 148 VAL B CA  1 
ATOM   2402 C C   . VAL B  1 148 ? -75.921 -7.336  39.065  1.00 37.79 ? 148 VAL B C   1 
ATOM   2403 O O   . VAL B  1 148 ? -75.299 -8.201  39.696  1.00 38.48 ? 148 VAL B O   1 
ATOM   2404 C CB  . VAL B  1 148 ? -77.922 -6.171  40.105  1.00 36.70 ? 148 VAL B CB  1 
ATOM   2405 C CG1 . VAL B  1 148 ? -78.273 -7.564  40.598  1.00 37.69 ? 148 VAL B CG1 1 
ATOM   2406 C CG2 . VAL B  1 148 ? -78.275 -5.139  41.154  1.00 38.33 ? 148 VAL B CG2 1 
ATOM   2407 N N   . GLY B  1 149 ? -76.168 -7.457  37.759  1.00 37.24 ? 149 GLY B N   1 
ATOM   2408 C CA  . GLY B  1 149 ? -75.686 -8.614  37.028  1.00 37.11 ? 149 GLY B CA  1 
ATOM   2409 C C   . GLY B  1 149 ? -74.179 -8.647  36.872  1.00 37.91 ? 149 GLY B C   1 
ATOM   2410 O O   . GLY B  1 149 ? -73.592 -9.723  36.727  1.00 38.79 ? 149 GLY B O   1 
ATOM   2411 N N   . ALA B  1 150 ? -73.532 -7.480  36.880  1.00 38.14 ? 150 ALA B N   1 
ATOM   2412 C CA  . ALA B  1 150 ? -72.076 -7.454  36.786  1.00 38.19 ? 150 ALA B CA  1 
ATOM   2413 C C   . ALA B  1 150 ? -71.423 -7.966  38.063  1.00 38.11 ? 150 ALA B C   1 
ATOM   2414 O O   . ALA B  1 150 ? -70.346 -8.569  38.006  1.00 38.71 ? 150 ALA B O   1 
ATOM   2415 C CB  . ALA B  1 150 ? -71.586 -6.041  36.469  1.00 37.66 ? 150 ALA B CB  1 
ATOM   2416 N N   . VAL B  1 151 ? -72.050 -7.727  39.218  1.00 37.83 ? 151 VAL B N   1 
ATOM   2417 C CA  . VAL B  1 151 ? -71.533 -8.273  40.469  1.00 38.22 ? 151 VAL B CA  1 
ATOM   2418 C C   . VAL B  1 151 ? -71.683 -9.788  40.487  1.00 38.68 ? 151 VAL B C   1 
ATOM   2419 O O   . VAL B  1 151 ? -70.733 -10.520 40.793  1.00 39.30 ? 151 VAL B O   1 
ATOM   2420 C CB  . VAL B  1 151 ? -72.240 -7.627  41.672  1.00 37.05 ? 151 VAL B CB  1 
ATOM   2421 C CG1 . VAL B  1 151 ? -71.718 -8.225  42.971  1.00 38.25 ? 151 VAL B CG1 1 
ATOM   2422 C CG2 . VAL B  1 151 ? -72.036 -6.125  41.655  1.00 37.07 ? 151 VAL B CG2 1 
ATOM   2423 N N   . MET B  1 152 ? -72.879 -10.279 40.150  1.00 38.66 ? 152 MET B N   1 
ATOM   2424 C CA  . MET B  1 152 ? -73.103 -11.719 40.070  1.00 39.38 ? 152 MET B CA  1 
ATOM   2425 C C   . MET B  1 152 ? -72.192 -12.368 39.037  1.00 39.49 ? 152 MET B C   1 
ATOM   2426 O O   . MET B  1 152 ? -71.800 -13.530 39.196  1.00 40.88 ? 152 MET B O   1 
ATOM   2427 C CB  . MET B  1 152 ? -74.566 -12.004 39.735  1.00 40.26 ? 152 MET B CB  1 
ATOM   2428 C CG  . MET B  1 152 ? -75.566 -11.282 40.619  1.00 40.17 ? 152 MET B CG  1 
ATOM   2429 S SD  . MET B  1 152 ? -77.266 -11.510 40.055  1.00 39.33 ? 152 MET B SD  1 
ATOM   2430 C CE  . MET B  1 152 ? -77.446 -13.283 40.228  1.00 41.35 ? 152 MET B CE  1 
ATOM   2431 N N   . LEU B  1 153 ? -71.860 -11.642 37.969  1.00 38.69 ? 153 LEU B N   1 
ATOM   2432 C CA  . LEU B  1 153 ? -70.868 -12.126 37.018  1.00 38.89 ? 153 LEU B CA  1 
ATOM   2433 C C   . LEU B  1 153 ? -69.512 -12.293 37.692  1.00 39.67 ? 153 LEU B C   1 
ATOM   2434 O O   . LEU B  1 153 ? -68.818 -13.295 37.487  1.00 40.40 ? 153 LEU B O   1 
ATOM   2435 C CB  . LEU B  1 153 ? -70.774 -11.159 35.838  1.00 39.42 ? 153 LEU B CB  1 
ATOM   2436 C CG  . LEU B  1 153 ? -70.326 -11.724 34.492  1.00 40.34 ? 153 LEU B CG  1 
ATOM   2437 C CD1 . LEU B  1 153 ? -71.294 -12.799 34.033  1.00 40.68 ? 153 LEU B CD1 1 
ATOM   2438 C CD2 . LEU B  1 153 ? -70.233 -10.604 33.468  1.00 39.49 ? 153 LEU B CD2 1 
ATOM   2439 N N   . ALA B  1 154 ? -69.126 -11.318 38.513  1.00 40.06 ? 154 ALA B N   1 
ATOM   2440 C CA  . ALA B  1 154 ? -67.845 -11.354 39.203  1.00 40.99 ? 154 ALA B CA  1 
ATOM   2441 C C   . ALA B  1 154 ? -67.862 -12.228 40.450  1.00 41.10 ? 154 ALA B C   1 
ATOM   2442 O O   . ALA B  1 154 ? -66.814 -12.381 41.088  1.00 42.49 ? 154 ALA B O   1 
ATOM   2443 C CB  . ALA B  1 154 ? -67.407 -9.939  39.575  1.00 41.78 ? 154 ALA B CB  1 
ATOM   2444 N N   . LEU B  1 155 ? -69.008 -12.798 40.822  1.00 40.21 ? 155 LEU B N   1 
ATOM   2445 C CA  . LEU B  1 155 ? -69.030 -13.724 41.948  1.00 40.93 ? 155 LEU B CA  1 
ATOM   2446 C C   . LEU B  1 155 ? -68.593 -15.112 41.491  1.00 43.11 ? 155 LEU B C   1 
ATOM   2447 O O   . LEU B  1 155 ? -69.282 -16.107 41.746  1.00 43.30 ? 155 LEU B O   1 
ATOM   2448 C CB  . LEU B  1 155 ? -70.420 -13.777 42.586  1.00 39.64 ? 155 LEU B CB  1 
ATOM   2449 C CG  . LEU B  1 155 ? -70.951 -12.484 43.209  1.00 37.32 ? 155 LEU B CG  1 
ATOM   2450 C CD1 . LEU B  1 155 ? -72.355 -12.708 43.741  1.00 36.90 ? 155 LEU B CD1 1 
ATOM   2451 C CD2 . LEU B  1 155 ? -70.027 -11.968 44.304  1.00 32.92 ? 155 LEU B CD2 1 
ATOM   2452 N N   . ASP B  1 156 ? -67.442 -15.184 40.828  1.00 43.29 ? 156 ASP B N   1 
ATOM   2453 C CA  . ASP B  1 156 ? -66.880 -16.445 40.365  1.00 43.73 ? 156 ASP B CA  1 
ATOM   2454 C C   . ASP B  1 156 ? -65.417 -16.546 40.774  1.00 42.27 ? 156 ASP B C   1 
ATOM   2455 O O   . ASP B  1 156 ? -65.027 -16.052 41.831  1.00 39.92 ? 156 ASP B O   1 
ATOM   2456 C CB  . ASP B  1 156 ? -67.018 -16.581 38.845  1.00 44.97 ? 156 ASP B CB  1 
ATOM   2457 C CG  . ASP B  1 156 ? -68.335 -17.223 38.428  1.00 45.56 ? 156 ASP B CG  1 
ATOM   2458 O OD1 . ASP B  1 156 ? -69.320 -17.137 39.193  1.00 43.77 ? 156 ASP B OD1 1 
ATOM   2459 O OD2 . ASP B  1 156 ? -68.378 -17.833 37.337  1.00 46.30 ? 156 ASP B OD2 1 
ATOM   2460 N N   . PRO C  1 11  ? -43.377 55.687  21.142  1.00 47.60 ? 11  PRO C N   1 
ATOM   2461 C CA  . PRO C  1 11  ? -43.744 56.716  22.122  1.00 49.47 ? 11  PRO C CA  1 
ATOM   2462 C C   . PRO C  1 11  ? -44.406 56.132  23.372  1.00 49.80 ? 11  PRO C C   1 
ATOM   2463 O O   . PRO C  1 11  ? -45.524 55.614  23.270  1.00 50.72 ? 11  PRO C O   1 
ATOM   2464 C CB  . PRO C  1 11  ? -44.728 57.604  21.345  1.00 50.67 ? 11  PRO C CB  1 
ATOM   2465 C CG  . PRO C  1 11  ? -45.268 56.720  20.265  1.00 49.45 ? 11  PRO C CG  1 
ATOM   2466 C CD  . PRO C  1 11  ? -44.130 55.826  19.882  1.00 47.70 ? 11  PRO C CD  1 
ATOM   2467 N N   . TRP C  1 12  ? -43.728 56.220  24.524  1.00 48.82 ? 12  TRP C N   1 
ATOM   2468 C CA  . TRP C  1 12  ? -44.270 55.745  25.799  1.00 48.66 ? 12  TRP C CA  1 
ATOM   2469 C C   . TRP C  1 12  ? -44.637 54.262  25.705  1.00 47.23 ? 12  TRP C C   1 
ATOM   2470 O O   . TRP C  1 12  ? -45.759 53.848  26.004  1.00 46.66 ? 12  TRP C O   1 
ATOM   2471 C CB  . TRP C  1 12  ? -45.468 56.611  26.221  1.00 53.01 ? 12  TRP C CB  1 
ATOM   2472 C CG  . TRP C  1 12  ? -46.107 56.298  27.554  1.00 55.68 ? 12  TRP C CG  1 
ATOM   2473 C CD1 . TRP C  1 12  ? -47.338 55.740  27.761  1.00 56.12 ? 12  TRP C CD1 1 
ATOM   2474 C CD2 . TRP C  1 12  ? -45.562 56.555  28.856  1.00 57.41 ? 12  TRP C CD2 1 
ATOM   2475 N NE1 . TRP C  1 12  ? -47.588 55.620  29.107  1.00 56.35 ? 12  TRP C NE1 1 
ATOM   2476 C CE2 . TRP C  1 12  ? -46.514 56.112  29.802  1.00 58.25 ? 12  TRP C CE2 1 
ATOM   2477 C CE3 . TRP C  1 12  ? -44.361 57.107  29.314  1.00 57.34 ? 12  TRP C CE3 1 
ATOM   2478 C CZ2 . TRP C  1 12  ? -46.299 56.204  31.178  1.00 59.73 ? 12  TRP C CZ2 1 
ATOM   2479 C CZ3 . TRP C  1 12  ? -44.150 57.199  30.680  1.00 58.83 ? 12  TRP C CZ3 1 
ATOM   2480 C CH2 . TRP C  1 12  ? -45.114 56.749  31.596  1.00 59.08 ? 12  TRP C CH2 1 
ATOM   2481 N N   . LEU C  1 13  ? -43.671 53.457  25.255  1.00 44.75 ? 13  LEU C N   1 
ATOM   2482 C CA  . LEU C  1 13  ? -43.847 52.013  25.140  1.00 41.06 ? 13  LEU C CA  1 
ATOM   2483 C C   . LEU C  1 13  ? -42.836 51.242  25.979  1.00 39.83 ? 13  LEU C C   1 
ATOM   2484 O O   . LEU C  1 13  ? -42.576 50.066  25.703  1.00 39.24 ? 13  LEU C O   1 
ATOM   2485 C CB  . LEU C  1 13  ? -43.766 51.572  23.677  1.00 39.82 ? 13  LEU C CB  1 
ATOM   2486 C CG  . LEU C  1 13  ? -42.651 52.112  22.775  1.00 39.11 ? 13  LEU C CG  1 
ATOM   2487 C CD1 . LEU C  1 13  ? -41.259 51.644  23.181  1.00 36.73 ? 13  LEU C CD1 1 
ATOM   2488 C CD2 . LEU C  1 13  ? -42.937 51.708  21.340  1.00 37.02 ? 13  LEU C CD2 1 
ATOM   2489 N N   . TRP C  1 14  ? -42.228 51.888  26.975  1.00 40.70 ? 14  TRP C N   1 
ATOM   2490 C CA  . TRP C  1 14  ? -41.304 51.183  27.853  1.00 40.39 ? 14  TRP C CA  1 
ATOM   2491 C C   . TRP C  1 14  ? -42.000 50.133  28.702  1.00 40.67 ? 14  TRP C C   1 
ATOM   2492 O O   . TRP C  1 14  ? -41.319 49.287  29.288  1.00 40.91 ? 14  TRP C O   1 
ATOM   2493 C CB  . TRP C  1 14  ? -40.563 52.175  28.750  1.00 41.77 ? 14  TRP C CB  1 
ATOM   2494 C CG  . TRP C  1 14  ? -39.717 53.139  27.979  1.00 43.60 ? 14  TRP C CG  1 
ATOM   2495 C CD1 . TRP C  1 14  ? -39.915 54.483  27.848  1.00 43.79 ? 14  TRP C CD1 1 
ATOM   2496 C CD2 . TRP C  1 14  ? -38.543 52.830  27.213  1.00 44.67 ? 14  TRP C CD2 1 
ATOM   2497 N NE1 . TRP C  1 14  ? -38.933 55.032  27.058  1.00 44.91 ? 14  TRP C NE1 1 
ATOM   2498 C CE2 . TRP C  1 14  ? -38.079 54.039  26.655  1.00 44.94 ? 14  TRP C CE2 1 
ATOM   2499 C CE3 . TRP C  1 14  ? -37.836 51.650  26.952  1.00 44.23 ? 14  TRP C CE3 1 
ATOM   2500 C CZ2 . TRP C  1 14  ? -36.941 54.102  25.848  1.00 45.17 ? 14  TRP C CZ2 1 
ATOM   2501 C CZ3 . TRP C  1 14  ? -36.707 51.714  26.150  1.00 43.27 ? 14  TRP C CZ3 1 
ATOM   2502 C CH2 . TRP C  1 14  ? -36.271 52.932  25.609  1.00 43.73 ? 14  TRP C CH2 1 
ATOM   2503 N N   . ILE C  1 15  ? -43.331 50.181  28.789  1.00 40.98 ? 15  ILE C N   1 
ATOM   2504 C CA  . ILE C  1 15  ? -44.090 49.090  29.396  1.00 40.54 ? 15  ILE C CA  1 
ATOM   2505 C C   . ILE C  1 15  ? -43.971 47.830  28.546  1.00 40.76 ? 15  ILE C C   1 
ATOM   2506 O O   . ILE C  1 15  ? -43.780 46.724  29.066  1.00 41.14 ? 15  ILE C O   1 
ATOM   2507 C CB  . ILE C  1 15  ? -45.564 49.495  29.583  1.00 38.86 ? 15  ILE C CB  1 
ATOM   2508 C CG1 . ILE C  1 15  ? -45.700 51.010  29.764  1.00 39.66 ? 15  ILE C CG1 1 
ATOM   2509 C CG2 . ILE C  1 15  ? -46.181 48.744  30.755  1.00 37.86 ? 15  ILE C CG2 1 
ATOM   2510 C CD1 . ILE C  1 15  ? -46.049 51.762  28.483  1.00 42.67 ? 15  ILE C CD1 1 
ATOM   2511 N N   . THR C  1 16  ? -44.101 47.977  27.225  1.00 40.48 ? 16  THR C N   1 
ATOM   2512 C CA  . THR C  1 16  ? -43.978 46.828  26.334  1.00 40.17 ? 16  THR C CA  1 
ATOM   2513 C C   . THR C  1 16  ? -42.576 46.238  26.389  1.00 41.19 ? 16  THR C C   1 
ATOM   2514 O O   . THR C  1 16  ? -42.412 45.013  26.433  1.00 41.27 ? 16  THR C O   1 
ATOM   2515 C CB  . THR C  1 16  ? -44.337 47.236  24.904  1.00 40.64 ? 16  THR C CB  1 
ATOM   2516 O OG1 . THR C  1 16  ? -45.723 47.591  24.843  1.00 40.56 ? 16  THR C OG1 1 
ATOM   2517 C CG2 . THR C  1 16  ? -44.071 46.098  23.932  1.00 41.34 ? 16  THR C CG2 1 
ATOM   2518 N N   . VAL C  1 17  ? -41.554 47.094  26.390  1.00 41.42 ? 17  VAL C N   1 
ATOM   2519 C CA  . VAL C  1 17  ? -40.178 46.613  26.432  1.00 42.04 ? 17  VAL C CA  1 
ATOM   2520 C C   . VAL C  1 17  ? -39.878 45.962  27.776  1.00 40.69 ? 17  VAL C C   1 
ATOM   2521 O O   . VAL C  1 17  ? -39.308 44.868  27.837  1.00 39.95 ? 17  VAL C O   1 
ATOM   2522 C CB  . VAL C  1 17  ? -39.198 47.762  26.138  1.00 42.31 ? 17  VAL C CB  1 
ATOM   2523 C CG1 . VAL C  1 17  ? -37.779 47.224  25.981  1.00 41.89 ? 17  VAL C CG1 1 
ATOM   2524 C CG2 . VAL C  1 17  ? -39.629 48.527  24.902  1.00 42.92 ? 17  VAL C CG2 1 
ATOM   2525 N N   . LEU C  1 18  ? -40.264 46.624  28.872  1.00 41.02 ? 18  LEU C N   1 
ATOM   2526 C CA  . LEU C  1 18  ? -39.886 46.144  30.199  1.00 40.42 ? 18  LEU C CA  1 
ATOM   2527 C C   . LEU C  1 18  ? -40.577 44.836  30.561  1.00 40.14 ? 18  LEU C C   1 
ATOM   2528 O O   . LEU C  1 18  ? -40.006 44.025  31.298  1.00 40.19 ? 18  LEU C O   1 
ATOM   2529 C CB  . LEU C  1 18  ? -40.175 47.215  31.251  1.00 40.21 ? 18  LEU C CB  1 
ATOM   2530 C CG  . LEU C  1 18  ? -39.028 48.208  31.462  1.00 40.70 ? 18  LEU C CG  1 
ATOM   2531 C CD1 . LEU C  1 18  ? -39.515 49.494  32.107  1.00 40.36 ? 18  LEU C CD1 1 
ATOM   2532 C CD2 . LEU C  1 18  ? -37.929 47.565  32.303  1.00 41.69 ? 18  LEU C CD2 1 
ATOM   2533 N N   . VAL C  1 19  ? -41.796 44.612  30.072  1.00 39.96 ? 19  VAL C N   1 
ATOM   2534 C CA  . VAL C  1 19  ? -42.449 43.323  30.286  1.00 40.05 ? 19  VAL C CA  1 
ATOM   2535 C C   . VAL C  1 19  ? -41.735 42.229  29.503  1.00 39.07 ? 19  VAL C C   1 
ATOM   2536 O O   . VAL C  1 19  ? -41.425 41.158  30.038  1.00 37.42 ? 19  VAL C O   1 
ATOM   2537 C CB  . VAL C  1 19  ? -43.937 43.401  29.904  1.00 41.49 ? 19  VAL C CB  1 
ATOM   2538 C CG1 . VAL C  1 19  ? -44.534 42.001  29.809  1.00 40.76 ? 19  VAL C CG1 1 
ATOM   2539 C CG2 . VAL C  1 19  ? -44.693 44.242  30.920  1.00 42.03 ? 19  VAL C CG2 1 
ATOM   2540 N N   . PHE C  1 20  ? -41.451 42.492  28.228  1.00 39.82 ? 20  PHE C N   1 
ATOM   2541 C CA  . PHE C  1 20  ? -40.847 41.484  27.364  1.00 38.65 ? 20  PHE C CA  1 
ATOM   2542 C C   . PHE C  1 20  ? -39.453 41.089  27.843  1.00 37.71 ? 20  PHE C C   1 
ATOM   2543 O O   . PHE C  1 20  ? -39.075 39.915  27.764  1.00 37.28 ? 20  PHE C O   1 
ATOM   2544 C CB  . PHE C  1 20  ? -40.818 42.005  25.927  1.00 39.05 ? 20  PHE C CB  1 
ATOM   2545 C CG  . PHE C  1 20  ? -39.779 41.362  25.069  1.00 39.21 ? 20  PHE C CG  1 
ATOM   2546 C CD1 . PHE C  1 20  ? -40.016 40.144  24.460  1.00 39.39 ? 20  PHE C CD1 1 
ATOM   2547 C CD2 . PHE C  1 20  ? -38.566 41.989  24.855  1.00 41.60 ? 20  PHE C CD2 1 
ATOM   2548 C CE1 . PHE C  1 20  ? -39.054 39.560  23.667  1.00 41.27 ? 20  PHE C CE1 1 
ATOM   2549 C CE2 . PHE C  1 20  ? -37.606 41.414  24.068  1.00 43.09 ? 20  PHE C CE2 1 
ATOM   2550 C CZ  . PHE C  1 20  ? -37.846 40.197  23.472  1.00 42.78 ? 20  PHE C CZ  1 
ATOM   2551 N N   . VAL C  1 21  ? -38.670 42.048  28.341  1.00 38.15 ? 21  VAL C N   1 
ATOM   2552 C CA  . VAL C  1 21  ? -37.314 41.719  28.770  1.00 37.18 ? 21  VAL C CA  1 
ATOM   2553 C C   . VAL C  1 21  ? -37.312 41.119  30.171  1.00 37.40 ? 21  VAL C C   1 
ATOM   2554 O O   . VAL C  1 21  ? -36.509 40.228  30.466  1.00 38.58 ? 21  VAL C O   1 
ATOM   2555 C CB  . VAL C  1 21  ? -36.390 42.947  28.675  1.00 37.10 ? 21  VAL C CB  1 
ATOM   2556 C CG1 . VAL C  1 21  ? -36.336 43.451  27.244  1.00 38.18 ? 21  VAL C CG1 1 
ATOM   2557 C CG2 . VAL C  1 21  ? -36.837 44.045  29.629  1.00 39.14 ? 21  VAL C CG2 1 
ATOM   2558 N N   . LEU C  1 22  ? -38.190 41.592  31.060  1.00 37.19 ? 22  LEU C N   1 
ATOM   2559 C CA  . LEU C  1 22  ? -38.340 40.934  32.354  1.00 36.85 ? 22  LEU C CA  1 
ATOM   2560 C C   . LEU C  1 22  ? -38.814 39.500  32.175  1.00 36.34 ? 22  LEU C C   1 
ATOM   2561 O O   . LEU C  1 22  ? -38.354 38.588  32.873  1.00 35.50 ? 22  LEU C O   1 
ATOM   2562 C CB  . LEU C  1 22  ? -39.319 41.709  33.235  1.00 38.47 ? 22  LEU C CB  1 
ATOM   2563 C CG  . LEU C  1 22  ? -38.739 42.696  34.247  1.00 40.00 ? 22  LEU C CG  1 
ATOM   2564 C CD1 . LEU C  1 22  ? -39.837 43.585  34.810  1.00 42.28 ? 22  LEU C CD1 1 
ATOM   2565 C CD2 . LEU C  1 22  ? -38.037 41.948  35.368  1.00 41.00 ? 22  LEU C CD2 1 
ATOM   2566 N N   . ASP C  1 23  ? -39.733 39.287  31.234  1.00 36.72 ? 23  ASP C N   1 
ATOM   2567 C CA  . ASP C  1 23  ? -40.216 37.943  30.941  1.00 36.36 ? 23  ASP C CA  1 
ATOM   2568 C C   . ASP C  1 23  ? -39.079 37.040  30.471  1.00 35.15 ? 23  ASP C C   1 
ATOM   2569 O O   . ASP C  1 23  ? -38.900 35.930  30.985  1.00 34.40 ? 23  ASP C O   1 
ATOM   2570 C CB  . ASP C  1 23  ? -41.330 38.031  29.896  1.00 36.16 ? 23  ASP C CB  1 
ATOM   2571 C CG  . ASP C  1 23  ? -41.779 36.681  29.403  1.00 35.31 ? 23  ASP C CG  1 
ATOM   2572 O OD1 . ASP C  1 23  ? -42.204 35.857  30.240  1.00 35.73 ? 23  ASP C OD1 1 
ATOM   2573 O OD2 . ASP C  1 23  ? -41.717 36.454  28.175  1.00 35.90 ? 23  ASP C OD2 1 
ATOM   2574 N N   . GLN C  1 24  ? -38.276 37.520  29.516  1.00 35.57 ? 24  GLN C N   1 
ATOM   2575 C CA  . GLN C  1 24  ? -37.188 36.711  28.973  1.00 35.33 ? 24  GLN C CA  1 
ATOM   2576 C C   . GLN C  1 24  ? -36.072 36.492  29.985  1.00 35.76 ? 24  GLN C C   1 
ATOM   2577 O O   . GLN C  1 24  ? -35.402 35.455  29.944  1.00 36.12 ? 24  GLN C O   1 
ATOM   2578 C CB  . GLN C  1 24  ? -36.628 37.363  27.711  1.00 35.57 ? 24  GLN C CB  1 
ATOM   2579 C CG  . GLN C  1 24  ? -37.595 37.346  26.552  1.00 37.22 ? 24  GLN C CG  1 
ATOM   2580 C CD  . GLN C  1 24  ? -37.992 35.941  26.158  1.00 37.20 ? 24  GLN C CD  1 
ATOM   2581 O OE1 . GLN C  1 24  ? -37.179 35.016  26.209  1.00 37.57 ? 24  GLN C OE1 1 
ATOM   2582 N NE2 . GLN C  1 24  ? -39.250 35.769  25.766  1.00 37.09 ? 24  GLN C NE2 1 
ATOM   2583 N N   . VAL C  1 25  ? -35.845 37.454  30.882  1.00 35.60 ? 25  VAL C N   1 
ATOM   2584 C CA  . VAL C  1 25  ? -34.853 37.262  31.936  1.00 34.58 ? 25  VAL C CA  1 
ATOM   2585 C C   . VAL C  1 25  ? -35.275 36.125  32.857  1.00 35.43 ? 25  VAL C C   1 
ATOM   2586 O O   . VAL C  1 25  ? -34.457 35.278  33.237  1.00 37.09 ? 25  VAL C O   1 
ATOM   2587 C CB  . VAL C  1 25  ? -34.634 38.573  32.716  1.00 33.83 ? 25  VAL C CB  1 
ATOM   2588 C CG1 . VAL C  1 25  ? -33.974 38.292  34.055  1.00 34.57 ? 25  VAL C CG1 1 
ATOM   2589 C CG2 . VAL C  1 25  ? -33.779 39.536  31.907  1.00 33.81 ? 25  VAL C CG2 1 
ATOM   2590 N N   . SER C  1 26  ? -36.558 36.084  33.224  1.00 34.59 ? 26  SER C N   1 
ATOM   2591 C CA  . SER C  1 26  ? -37.038 35.039  34.123  1.00 34.48 ? 26  SER C CA  1 
ATOM   2592 C C   . SER C  1 26  ? -36.999 33.668  33.461  1.00 34.44 ? 26  SER C C   1 
ATOM   2593 O O   . SER C  1 26  ? -36.637 32.675  34.103  1.00 34.16 ? 26  SER C O   1 
ATOM   2594 C CB  . SER C  1 26  ? -38.453 35.368  34.591  1.00 34.56 ? 26  SER C CB  1 
ATOM   2595 O OG  . SER C  1 26  ? -38.448 36.510  35.426  1.00 36.91 ? 26  SER C OG  1 
ATOM   2596 N N   . LYS C  1 27  ? -37.372 33.591  32.183  1.00 34.18 ? 27  LYS C N   1 
ATOM   2597 C CA  . LYS C  1 27  ? -37.397 32.303  31.498  1.00 33.80 ? 27  LYS C CA  1 
ATOM   2598 C C   . LYS C  1 27  ? -36.011 31.679  31.436  1.00 35.35 ? 27  LYS C C   1 
ATOM   2599 O O   . LYS C  1 27  ? -35.853 30.476  31.673  1.00 36.17 ? 27  LYS C O   1 
ATOM   2600 C CB  . LYS C  1 27  ? -37.963 32.470  30.092  1.00 33.75 ? 27  LYS C CB  1 
ATOM   2601 C CG  . LYS C  1 27  ? -39.437 32.780  30.062  1.00 33.31 ? 27  LYS C CG  1 
ATOM   2602 C CD  . LYS C  1 27  ? -39.866 33.150  28.666  1.00 32.71 ? 27  LYS C CD  1 
ATOM   2603 C CE  . LYS C  1 27  ? -41.364 33.282  28.591  1.00 33.43 ? 27  LYS C CE  1 
ATOM   2604 N NZ  . LYS C  1 27  ? -41.799 33.949  27.338  1.00 34.86 ? 27  LYS C NZ  1 
ATOM   2605 N N   . ALA C  1 28  ? -34.993 32.480  31.117  1.00 35.33 ? 28  ALA C N   1 
ATOM   2606 C CA  . ALA C  1 28  ? -33.637 31.949  31.064  1.00 35.65 ? 28  ALA C CA  1 
ATOM   2607 C C   . ALA C  1 28  ? -33.147 31.520  32.442  1.00 36.73 ? 28  ALA C C   1 
ATOM   2608 O O   . ALA C  1 28  ? -32.309 30.617  32.544  1.00 37.50 ? 28  ALA C O   1 
ATOM   2609 C CB  . ALA C  1 28  ? -32.689 32.982  30.456  1.00 37.08 ? 28  ALA C CB  1 
ATOM   2610 N N   . PHE C  1 29  ? -33.645 32.155  33.506  1.00 36.15 ? 29  PHE C N   1 
ATOM   2611 C CA  . PHE C  1 29  ? -33.255 31.750  34.853  1.00 36.20 ? 29  PHE C CA  1 
ATOM   2612 C C   . PHE C  1 29  ? -33.826 30.381  35.203  1.00 36.91 ? 29  PHE C C   1 
ATOM   2613 O O   . PHE C  1 29  ? -33.114 29.517  35.729  1.00 38.38 ? 29  PHE C O   1 
ATOM   2614 C CB  . PHE C  1 29  ? -33.705 32.798  35.871  1.00 35.86 ? 29  PHE C CB  1 
ATOM   2615 C CG  . PHE C  1 29  ? -33.695 32.301  37.291  1.00 37.10 ? 29  PHE C CG  1 
ATOM   2616 C CD1 . PHE C  1 29  ? -32.504 32.174  37.989  1.00 38.44 ? 29  PHE C CD1 1 
ATOM   2617 C CD2 . PHE C  1 29  ? -34.878 31.953  37.925  1.00 37.73 ? 29  PHE C CD2 1 
ATOM   2618 C CE1 . PHE C  1 29  ? -32.495 31.709  39.293  1.00 39.85 ? 29  PHE C CE1 1 
ATOM   2619 C CE2 . PHE C  1 29  ? -34.875 31.489  39.228  1.00 37.82 ? 29  PHE C CE2 1 
ATOM   2620 C CZ  . PHE C  1 29  ? -33.682 31.367  39.912  1.00 39.77 ? 29  PHE C CZ  1 
ATOM   2621 N N   . PHE C  1 30  ? -35.116 30.168  34.926  1.00 36.23 ? 30  PHE C N   1 
ATOM   2622 C CA  . PHE C  1 30  ? -35.759 28.900  35.254  1.00 35.70 ? 30  PHE C CA  1 
ATOM   2623 C C   . PHE C  1 30  ? -35.411 27.794  34.265  1.00 36.06 ? 30  PHE C C   1 
ATOM   2624 O O   . PHE C  1 30  ? -35.439 26.614  34.633  1.00 35.82 ? 30  PHE C O   1 
ATOM   2625 C CB  . PHE C  1 30  ? -37.275 29.083  35.325  1.00 34.76 ? 30  PHE C CB  1 
ATOM   2626 C CG  . PHE C  1 30  ? -37.755 29.643  36.633  1.00 33.68 ? 30  PHE C CG  1 
ATOM   2627 C CD1 . PHE C  1 30  ? -37.826 28.838  37.758  1.00 32.25 ? 30  PHE C CD1 1 
ATOM   2628 C CD2 . PHE C  1 30  ? -38.136 30.970  36.738  1.00 33.31 ? 30  PHE C CD2 1 
ATOM   2629 C CE1 . PHE C  1 30  ? -38.265 29.348  38.961  1.00 32.16 ? 30  PHE C CE1 1 
ATOM   2630 C CE2 . PHE C  1 30  ? -38.578 31.484  37.940  1.00 32.39 ? 30  PHE C CE2 1 
ATOM   2631 C CZ  . PHE C  1 30  ? -38.641 30.672  39.052  1.00 32.55 ? 30  PHE C CZ  1 
ATOM   2632 N N   . GLN C  1 31  ? -35.104 28.146  33.014  1.00 36.46 ? 31  GLN C N   1 
ATOM   2633 C CA  . GLN C  1 31  ? -34.641 27.145  32.056  1.00 37.12 ? 31  GLN C CA  1 
ATOM   2634 C C   . GLN C  1 31  ? -33.319 26.528  32.495  1.00 38.92 ? 31  GLN C C   1 
ATOM   2635 O O   . GLN C  1 31  ? -33.093 25.326  32.308  1.00 40.02 ? 31  GLN C O   1 
ATOM   2636 C CB  . GLN C  1 31  ? -34.491 27.768  30.670  1.00 36.97 ? 31  GLN C CB  1 
ATOM   2637 C CG  . GLN C  1 31  ? -35.744 27.730  29.819  1.00 36.16 ? 31  GLN C CG  1 
ATOM   2638 C CD  . GLN C  1 31  ? -35.517 27.007  28.505  1.00 37.64 ? 31  GLN C CD  1 
ATOM   2639 O OE1 . GLN C  1 31  ? -35.040 25.870  28.483  1.00 38.73 ? 31  GLN C OE1 1 
ATOM   2640 N NE2 . GLN C  1 31  ? -35.843 27.672  27.400  1.00 37.93 ? 31  GLN C NE2 1 
ATOM   2641 N N   . ALA C  1 32  ? -32.425 27.339  33.063  1.00 39.31 ? 32  ALA C N   1 
ATOM   2642 C CA  . ALA C  1 32  ? -31.137 26.826  33.515  1.00 39.86 ? 32  ALA C CA  1 
ATOM   2643 C C   . ALA C  1 32  ? -31.215 26.208  34.905  1.00 40.29 ? 32  ALA C C   1 
ATOM   2644 O O   . ALA C  1 32  ? -30.423 25.313  35.225  1.00 41.27 ? 32  ALA C O   1 
ATOM   2645 C CB  . ALA C  1 32  ? -30.094 27.941  33.500  1.00 41.73 ? 32  ALA C CB  1 
ATOM   2646 N N   . GLU C  1 33  ? -32.152 26.664  35.740  1.00 40.04 ? 33  GLU C N   1 
ATOM   2647 C CA  . GLU C  1 33  ? -32.218 26.192  37.118  1.00 39.64 ? 33  GLU C CA  1 
ATOM   2648 C C   . GLU C  1 33  ? -32.955 24.864  37.247  1.00 38.26 ? 33  GLU C C   1 
ATOM   2649 O O   . GLU C  1 33  ? -32.622 24.064  38.128  1.00 39.30 ? 33  GLU C O   1 
ATOM   2650 C CB  . GLU C  1 33  ? -32.886 27.249  38.000  1.00 40.26 ? 33  GLU C CB  1 
ATOM   2651 C CG  . GLU C  1 33  ? -32.664 27.064  39.497  1.00 43.63 ? 33  GLU C CG  1 
ATOM   2652 C CD  . GLU C  1 33  ? -31.315 27.589  39.974  1.00 48.49 ? 33  GLU C CD  1 
ATOM   2653 O OE1 . GLU C  1 33  ? -30.520 28.073  39.137  1.00 48.29 ? 33  GLU C OE1 1 
ATOM   2654 O OE2 . GLU C  1 33  ? -31.055 27.524  41.197  1.00 51.52 ? 33  GLU C OE2 1 
ATOM   2655 N N   . LEU C  1 34  ? -33.933 24.600  36.386  1.00 36.82 ? 34  LEU C N   1 
ATOM   2656 C CA  . LEU C  1 34  ? -34.831 23.470  36.564  1.00 35.35 ? 34  LEU C CA  1 
ATOM   2657 C C   . LEU C  1 34  ? -34.680 22.443  35.448  1.00 34.81 ? 34  LEU C C   1 
ATOM   2658 O O   . LEU C  1 34  ? -33.990 22.657  34.447  1.00 35.36 ? 34  LEU C O   1 
ATOM   2659 C CB  . LEU C  1 34  ? -36.286 23.941  36.638  1.00 33.60 ? 34  LEU C CB  1 
ATOM   2660 C CG  . LEU C  1 34  ? -36.611 24.779  37.869  1.00 33.34 ? 34  LEU C CG  1 
ATOM   2661 C CD1 . LEU C  1 34  ? -38.111 24.969  37.996  1.00 30.70 ? 34  LEU C CD1 1 
ATOM   2662 C CD2 . LEU C  1 34  ? -36.035 24.102  39.098  1.00 34.37 ? 34  LEU C CD2 1 
ATOM   2663 N N   . SER C  1 35  ? -35.348 21.313  35.651  1.00 33.87 ? 35  SER C N   1 
ATOM   2664 C CA  . SER C  1 35  ? -35.455 20.239  34.677  1.00 32.81 ? 35  SER C CA  1 
ATOM   2665 C C   . SER C  1 35  ? -36.875 20.194  34.132  1.00 31.71 ? 35  SER C C   1 
ATOM   2666 O O   . SER C  1 35  ? -37.775 20.881  34.622  1.00 32.30 ? 35  SER C O   1 
ATOM   2667 C CB  . SER C  1 35  ? -35.082 18.894  35.310  1.00 33.20 ? 35  SER C CB  1 
ATOM   2668 O OG  . SER C  1 35  ? -34.020 19.048  36.237  1.00 34.36 ? 35  SER C OG  1 
ATOM   2669 N N   . MET C  1 36  ? -37.066 19.375  33.100  1.00 31.07 ? 36  MET C N   1 
ATOM   2670 C CA  . MET C  1 36  ? -38.384 19.220  32.493  1.00 32.14 ? 36  MET C CA  1 
ATOM   2671 C C   . MET C  1 36  ? -39.405 18.761  33.529  1.00 32.01 ? 36  MET C C   1 
ATOM   2672 O O   . MET C  1 36  ? -39.248 17.704  34.150  1.00 32.53 ? 36  MET C O   1 
ATOM   2673 C CB  . MET C  1 36  ? -38.315 18.230  31.329  1.00 33.13 ? 36  MET C CB  1 
ATOM   2674 C CG  . MET C  1 36  ? -38.270 18.875  29.941  1.00 32.83 ? 36  MET C CG  1 
ATOM   2675 S SD  . MET C  1 36  ? -39.843 19.608  29.445  1.00 34.57 ? 36  MET C SD  1 
ATOM   2676 C CE  . MET C  1 36  ? -40.005 18.984  27.773  1.00 35.59 ? 36  MET C CE  1 
ATOM   2677 N N   . TYR C  1 37  ? -40.441 19.576  33.724  1.00 31.34 ? 37  TYR C N   1 
ATOM   2678 C CA  . TYR C  1 37  ? -41.534 19.341  34.665  1.00 31.15 ? 37  TYR C CA  1 
ATOM   2679 C C   . TYR C  1 37  ? -41.063 19.223  36.112  1.00 31.06 ? 37  TYR C C   1 
ATOM   2680 O O   . TYR C  1 37  ? -41.841 18.804  36.977  1.00 31.00 ? 37  TYR C O   1 
ATOM   2681 C CB  . TYR C  1 37  ? -42.353 18.102  34.273  1.00 31.86 ? 37  TYR C CB  1 
ATOM   2682 C CG  . TYR C  1 37  ? -42.888 18.144  32.853  1.00 32.93 ? 37  TYR C CG  1 
ATOM   2683 C CD1 . TYR C  1 37  ? -44.053 18.840  32.541  1.00 33.05 ? 37  TYR C CD1 1 
ATOM   2684 C CD2 . TYR C  1 37  ? -42.227 17.488  31.823  1.00 33.80 ? 37  TYR C CD2 1 
ATOM   2685 C CE1 . TYR C  1 37  ? -44.541 18.879  31.239  1.00 32.82 ? 37  TYR C CE1 1 
ATOM   2686 C CE2 . TYR C  1 37  ? -42.707 17.520  30.523  1.00 34.41 ? 37  TYR C CE2 1 
ATOM   2687 C CZ  . TYR C  1 37  ? -43.861 18.216  30.237  1.00 33.46 ? 37  TYR C CZ  1 
ATOM   2688 O OH  . TYR C  1 37  ? -44.328 18.243  28.943  1.00 33.78 ? 37  TYR C OH  1 
ATOM   2689 N N   . GLN C  1 38  ? -39.813 19.583  36.401  1.00 31.35 ? 38  GLN C N   1 
ATOM   2690 C CA  . GLN C  1 38  ? -39.322 19.578  37.774  1.00 31.07 ? 38  GLN C CA  1 
ATOM   2691 C C   . GLN C  1 38  ? -40.016 20.676  38.570  1.00 30.67 ? 38  GLN C C   1 
ATOM   2692 O O   . GLN C  1 38  ? -40.131 21.813  38.106  1.00 31.15 ? 38  GLN C O   1 
ATOM   2693 C CB  . GLN C  1 38  ? -37.807 19.778  37.794  1.00 31.51 ? 38  GLN C CB  1 
ATOM   2694 C CG  . GLN C  1 38  ? -37.189 19.659  39.174  1.00 32.35 ? 38  GLN C CG  1 
ATOM   2695 C CD  . GLN C  1 38  ? -35.749 20.129  39.210  1.00 33.09 ? 38  GLN C CD  1 
ATOM   2696 O OE1 . GLN C  1 38  ? -35.256 20.733  38.258  1.00 33.22 ? 38  GLN C OE1 1 
ATOM   2697 N NE2 . GLN C  1 38  ? -35.066 19.855  40.317  1.00 33.06 ? 38  GLN C NE2 1 
ATOM   2698 N N   . GLN C  1 39  ? -40.478 20.338  39.771  1.00 31.02 ? 39  GLN C N   1 
ATOM   2699 C CA  . GLN C  1 39  ? -41.346 21.209  40.556  1.00 31.52 ? 39  GLN C CA  1 
ATOM   2700 C C   . GLN C  1 39  ? -40.613 21.697  41.798  1.00 32.19 ? 39  GLN C C   1 
ATOM   2701 O O   . GLN C  1 39  ? -40.142 20.885  42.601  1.00 32.35 ? 39  GLN C O   1 
ATOM   2702 C CB  . GLN C  1 39  ? -42.631 20.478  40.949  1.00 31.73 ? 39  GLN C CB  1 
ATOM   2703 C CG  . GLN C  1 39  ? -43.563 21.299  41.827  1.00 31.57 ? 39  GLN C CG  1 
ATOM   2704 C CD  . GLN C  1 39  ? -44.948 20.687  41.963  1.00 31.83 ? 39  GLN C CD  1 
ATOM   2705 O OE1 . GLN C  1 39  ? -45.566 20.752  43.024  1.00 31.09 ? 39  GLN C OE1 1 
ATOM   2706 N NE2 . GLN C  1 39  ? -45.445 20.096  40.882  1.00 32.69 ? 39  GLN C NE2 1 
ATOM   2707 N N   . ILE C  1 40  ? -40.531 23.015  41.966  1.00 32.59 ? 40  ILE C N   1 
ATOM   2708 C CA  . ILE C  1 40  ? -39.999 23.618  43.185  1.00 33.39 ? 40  ILE C CA  1 
ATOM   2709 C C   . ILE C  1 40  ? -41.196 24.065  44.016  1.00 33.23 ? 40  ILE C C   1 
ATOM   2710 O O   . ILE C  1 40  ? -41.800 25.112  43.758  1.00 32.93 ? 40  ILE C O   1 
ATOM   2711 C CB  . ILE C  1 40  ? -39.041 24.776  42.896  1.00 31.80 ? 40  ILE C CB  1 
ATOM   2712 C CG1 . ILE C  1 40  ? -37.759 24.253  42.249  1.00 31.82 ? 40  ILE C CG1 1 
ATOM   2713 C CG2 . ILE C  1 40  ? -38.713 25.516  44.183  1.00 33.55 ? 40  ILE C CG2 1 
ATOM   2714 C CD1 . ILE C  1 40  ? -36.540 25.124  42.484  1.00 32.79 ? 40  ILE C CD1 1 
ATOM   2715 N N   . VAL C  1 41  ? -41.543 23.267  45.021  1.00 33.25 ? 41  VAL C N   1 
ATOM   2716 C CA  . VAL C  1 41  ? -42.702 23.578  45.845  1.00 33.51 ? 41  VAL C CA  1 
ATOM   2717 C C   . VAL C  1 41  ? -42.411 24.836  46.650  1.00 33.58 ? 41  VAL C C   1 
ATOM   2718 O O   . VAL C  1 41  ? -41.395 24.923  47.351  1.00 34.65 ? 41  VAL C O   1 
ATOM   2719 C CB  . VAL C  1 41  ? -43.061 22.400  46.757  1.00 33.67 ? 41  VAL C CB  1 
ATOM   2720 C CG1 . VAL C  1 41  ? -44.108 22.827  47.762  1.00 35.56 ? 41  VAL C CG1 1 
ATOM   2721 C CG2 . VAL C  1 41  ? -43.570 21.231  45.936  1.00 32.89 ? 41  VAL C CG2 1 
ATOM   2722 N N   . VAL C  1 42  ? -43.303 25.817  46.551  1.00 32.84 ? 42  VAL C N   1 
ATOM   2723 C CA  . VAL C  1 42  ? -43.183 27.028  47.352  1.00 33.79 ? 42  VAL C CA  1 
ATOM   2724 C C   . VAL C  1 42  ? -44.212 26.973  48.473  1.00 34.85 ? 42  VAL C C   1 
ATOM   2725 O O   . VAL C  1 42  ? -43.859 26.962  49.658  1.00 35.33 ? 42  VAL C O   1 
ATOM   2726 C CB  . VAL C  1 42  ? -43.369 28.293  46.497  1.00 33.04 ? 42  VAL C CB  1 
ATOM   2727 C CG1 . VAL C  1 42  ? -43.131 29.536  47.338  1.00 32.72 ? 42  VAL C CG1 1 
ATOM   2728 C CG2 . VAL C  1 42  ? -42.432 28.270  45.308  1.00 33.39 ? 42  VAL C CG2 1 
ATOM   2729 N N   . ILE C  1 43  ? -45.488 26.931  48.103  1.00 34.87 ? 43  ILE C N   1 
ATOM   2730 C CA  . ILE C  1 43  ? -46.612 26.806  49.021  1.00 35.07 ? 43  ILE C CA  1 
ATOM   2731 C C   . ILE C  1 43  ? -47.154 25.385  48.875  1.00 36.65 ? 43  ILE C C   1 
ATOM   2732 O O   . ILE C  1 43  ? -47.812 25.080  47.870  1.00 37.52 ? 43  ILE C O   1 
ATOM   2733 C CB  . ILE C  1 43  ? -47.691 27.859  48.732  1.00 34.03 ? 43  ILE C CB  1 
ATOM   2734 C CG1 . ILE C  1 43  ? -47.107 29.273  48.817  1.00 34.56 ? 43  ILE C CG1 1 
ATOM   2735 C CG2 . ILE C  1 43  ? -48.859 27.699  49.687  1.00 34.48 ? 43  ILE C CG2 1 
ATOM   2736 C CD1 . ILE C  1 43  ? -48.030 30.359  48.282  1.00 34.81 ? 43  ILE C CD1 1 
ATOM   2737 N N   . PRO C  1 44  ? -46.920 24.499  49.858  1.00 37.00 ? 44  PRO C N   1 
ATOM   2738 C CA  . PRO C  1 44  ? -47.102 23.050  49.658  1.00 38.81 ? 44  PRO C CA  1 
ATOM   2739 C C   . PRO C  1 44  ? -48.327 22.597  48.873  1.00 39.43 ? 44  PRO C C   1 
ATOM   2740 O O   . PRO C  1 44  ? -48.199 21.713  48.020  1.00 41.19 ? 44  PRO C O   1 
ATOM   2741 C CB  . PRO C  1 44  ? -47.148 22.518  51.095  1.00 40.28 ? 44  PRO C CB  1 
ATOM   2742 C CG  . PRO C  1 44  ? -46.249 23.454  51.848  1.00 40.52 ? 44  PRO C CG  1 
ATOM   2743 C CD  . PRO C  1 44  ? -46.316 24.805  51.169  1.00 37.76 ? 44  PRO C CD  1 
ATOM   2744 N N   . ASP C  1 45  ? -49.506 23.167  49.117  1.00 38.70 ? 45  ASP C N   1 
ATOM   2745 C CA  . ASP C  1 45  ? -50.703 22.701  48.425  1.00 40.65 ? 45  ASP C CA  1 
ATOM   2746 C C   . ASP C  1 45  ? -51.351 23.758  47.541  1.00 39.83 ? 45  ASP C C   1 
ATOM   2747 O O   . ASP C  1 45  ? -52.478 23.550  47.080  1.00 40.96 ? 45  ASP C O   1 
ATOM   2748 C CB  . ASP C  1 45  ? -51.721 22.157  49.431  1.00 44.05 ? 45  ASP C CB  1 
ATOM   2749 C CG  . ASP C  1 45  ? -51.483 20.693  49.755  1.00 46.34 ? 45  ASP C CG  1 
ATOM   2750 O OD1 . ASP C  1 45  ? -50.883 19.985  48.915  1.00 46.38 ? 45  ASP C OD1 1 
ATOM   2751 O OD2 . ASP C  1 45  ? -51.893 20.243  50.844  1.00 48.19 ? 45  ASP C OD2 1 
ATOM   2752 N N   . LEU C  1 46  ? -50.679 24.867  47.274  1.00 38.03 ? 46  LEU C N   1 
ATOM   2753 C CA  . LEU C  1 46  ? -51.288 25.874  46.410  1.00 37.35 ? 46  LEU C CA  1 
ATOM   2754 C C   . LEU C  1 46  ? -50.399 26.328  45.258  1.00 35.82 ? 46  LEU C C   1 
ATOM   2755 O O   . LEU C  1 46  ? -50.904 26.571  44.157  1.00 35.50 ? 46  LEU C O   1 
ATOM   2756 C CB  . LEU C  1 46  ? -51.696 27.088  47.257  1.00 37.35 ? 46  LEU C CB  1 
ATOM   2757 C CG  . LEU C  1 46  ? -52.323 28.255  46.497  1.00 38.33 ? 46  LEU C CG  1 
ATOM   2758 C CD1 . LEU C  1 46  ? -53.642 27.832  45.861  1.00 41.00 ? 46  LEU C CD1 1 
ATOM   2759 C CD2 . LEU C  1 46  ? -52.525 29.443  47.418  1.00 39.15 ? 46  LEU C CD2 1 
ATOM   2760 N N   . PHE C  1 47  ? -49.092 26.457  45.481  1.00 35.06 ? 47  PHE C N   1 
ATOM   2761 C CA  . PHE C  1 47  ? -48.211 27.137  44.540  1.00 33.43 ? 47  PHE C CA  1 
ATOM   2762 C C   . PHE C  1 47  ? -46.896 26.385  44.409  1.00 32.85 ? 47  PHE C C   1 
ATOM   2763 O O   . PHE C  1 47  ? -46.414 25.773  45.365  1.00 33.47 ? 47  PHE C O   1 
ATOM   2764 C CB  . PHE C  1 47  ? -47.958 28.585  44.989  1.00 32.89 ? 47  PHE C CB  1 
ATOM   2765 C CG  . PHE C  1 47  ? -47.032 29.359  44.088  1.00 32.10 ? 47  PHE C CG  1 
ATOM   2766 C CD1 . PHE C  1 47  ? -47.333 29.551  42.750  1.00 32.03 ? 47  PHE C CD1 1 
ATOM   2767 C CD2 . PHE C  1 47  ? -45.872 29.921  44.592  1.00 31.76 ? 47  PHE C CD2 1 
ATOM   2768 C CE1 . PHE C  1 47  ? -46.485 30.273  41.928  1.00 31.01 ? 47  PHE C CE1 1 
ATOM   2769 C CE2 . PHE C  1 47  ? -45.023 30.642  43.777  1.00 31.86 ? 47  PHE C CE2 1 
ATOM   2770 C CZ  . PHE C  1 47  ? -45.329 30.819  42.443  1.00 31.27 ? 47  PHE C CZ  1 
ATOM   2771 N N   . SER C  1 48  ? -46.311 26.449  43.213  1.00 31.65 ? 48  SER C N   1 
ATOM   2772 C CA  . SER C  1 48  ? -45.066 25.749  42.934  1.00 31.11 ? 48  SER C CA  1 
ATOM   2773 C C   . SER C  1 48  ? -44.400 26.380  41.723  1.00 30.70 ? 48  SER C C   1 
ATOM   2774 O O   . SER C  1 48  ? -45.071 26.957  40.863  1.00 31.53 ? 48  SER C O   1 
ATOM   2775 C CB  . SER C  1 48  ? -45.306 24.259  42.673  1.00 31.44 ? 48  SER C CB  1 
ATOM   2776 O OG  . SER C  1 48  ? -46.172 23.689  43.638  1.00 33.24 ? 48  SER C OG  1 
ATOM   2777 N N   . TRP C  1 49  ? -43.074 26.284  41.675  1.00 30.16 ? 49  TRP C N   1 
ATOM   2778 C CA  . TRP C  1 49  ? -42.332 26.559  40.453  1.00 29.41 ? 49  TRP C CA  1 
ATOM   2779 C C   . TRP C  1 49  ? -42.211 25.268  39.658  1.00 29.88 ? 49  TRP C C   1 
ATOM   2780 O O   . TRP C  1 49  ? -42.130 24.180  40.230  1.00 30.40 ? 49  TRP C O   1 
ATOM   2781 C CB  . TRP C  1 49  ? -40.927 27.095  40.731  1.00 29.93 ? 49  TRP C CB  1 
ATOM   2782 C CG  . TRP C  1 49  ? -40.834 28.376  41.490  1.00 30.34 ? 49  TRP C CG  1 
ATOM   2783 C CD1 . TRP C  1 49  ? -40.247 28.554  42.707  1.00 31.78 ? 49  TRP C CD1 1 
ATOM   2784 C CD2 . TRP C  1 49  ? -41.296 29.667  41.075  1.00 30.25 ? 49  TRP C CD2 1 
ATOM   2785 N NE1 . TRP C  1 49  ? -40.329 29.870  43.085  1.00 32.62 ? 49  TRP C NE1 1 
ATOM   2786 C CE2 . TRP C  1 49  ? -40.969 30.575  42.101  1.00 31.18 ? 49  TRP C CE2 1 
ATOM   2787 C CE3 . TRP C  1 49  ? -41.962 30.143  39.943  1.00 30.84 ? 49  TRP C CE3 1 
ATOM   2788 C CZ2 . TRP C  1 49  ? -41.284 31.931  42.030  1.00 31.49 ? 49  TRP C CZ2 1 
ATOM   2789 C CZ3 . TRP C  1 49  ? -42.275 31.494  39.875  1.00 31.21 ? 49  TRP C CZ3 1 
ATOM   2790 C CH2 . TRP C  1 49  ? -41.935 32.369  40.913  1.00 30.93 ? 49  TRP C CH2 1 
ATOM   2791 N N   . THR C  1 50  ? -42.201 25.391  38.335  1.00 29.39 ? 50  THR C N   1 
ATOM   2792 C CA  . THR C  1 50  ? -42.019 24.223  37.479  1.00 30.07 ? 50  THR C CA  1 
ATOM   2793 C C   . THR C  1 50  ? -41.322 24.665  36.197  1.00 29.76 ? 50  THR C C   1 
ATOM   2794 O O   . THR C  1 50  ? -40.838 25.796  36.091  1.00 30.12 ? 50  THR C O   1 
ATOM   2795 C CB  . THR C  1 50  ? -43.360 23.522  37.211  1.00 30.88 ? 50  THR C CB  1 
ATOM   2796 O OG1 . THR C  1 50  ? -43.125 22.239  36.613  1.00 31.81 ? 50  THR C OG1 1 
ATOM   2797 C CG2 . THR C  1 50  ? -44.240 24.355  36.287  1.00 30.94 ? 50  THR C CG2 1 
ATOM   2798 N N   . LEU C  1 51  ? -41.251 23.759  35.221  1.00 29.41 ? 51  LEU C N   1 
ATOM   2799 C CA  . LEU C  1 51  ? -40.597 24.069  33.950  1.00 29.33 ? 51  LEU C CA  1 
ATOM   2800 C C   . LEU C  1 51  ? -41.228 23.194  32.869  1.00 29.23 ? 51  LEU C C   1 
ATOM   2801 O O   . LEU C  1 51  ? -40.860 22.025  32.723  1.00 30.19 ? 51  LEU C O   1 
ATOM   2802 C CB  . LEU C  1 51  ? -39.092 23.855  34.042  1.00 30.31 ? 51  LEU C CB  1 
ATOM   2803 C CG  . LEU C  1 51  ? -38.278 24.209  32.795  1.00 31.15 ? 51  LEU C CG  1 
ATOM   2804 C CD1 . LEU C  1 51  ? -38.411 25.688  32.480  1.00 32.24 ? 51  LEU C CD1 1 
ATOM   2805 C CD2 . LEU C  1 51  ? -36.818 23.824  32.979  1.00 32.48 ? 51  LEU C CD2 1 
ATOM   2806 N N   . ALA C  1 52  ? -42.172 23.766  32.126  1.00 28.83 ? 52  ALA C N   1 
ATOM   2807 C CA  . ALA C  1 52  ? -42.854 23.104  31.024  1.00 29.09 ? 52  ALA C CA  1 
ATOM   2808 C C   . ALA C  1 52  ? -42.558 23.842  29.724  1.00 30.13 ? 52  ALA C C   1 
ATOM   2809 O O   . ALA C  1 52  ? -42.002 24.942  29.721  1.00 31.40 ? 52  ALA C O   1 
ATOM   2810 C CB  . ALA C  1 52  ? -44.369 23.038  31.266  1.00 29.15 ? 52  ALA C CB  1 
ATOM   2811 N N   . TYR C  1 53  ? -42.931 23.222  28.606  1.00 29.66 ? 53  TYR C N   1 
ATOM   2812 C CA  . TYR C  1 53  ? -42.793 23.828  27.284  1.00 30.96 ? 53  TYR C CA  1 
ATOM   2813 C C   . TYR C  1 53  ? -44.115 23.652  26.550  1.00 31.41 ? 53  TYR C C   1 
ATOM   2814 O O   . TYR C  1 53  ? -44.440 22.545  26.111  1.00 31.53 ? 53  TYR C O   1 
ATOM   2815 C CB  . TYR C  1 53  ? -41.640 23.203  26.496  1.00 33.44 ? 53  TYR C CB  1 
ATOM   2816 C CG  . TYR C  1 53  ? -40.274 23.419  27.109  1.00 33.23 ? 53  TYR C CG  1 
ATOM   2817 C CD1 . TYR C  1 53  ? -39.900 24.659  27.610  1.00 32.42 ? 53  TYR C CD1 1 
ATOM   2818 C CD2 . TYR C  1 53  ? -39.361 22.378  27.193  1.00 33.86 ? 53  TYR C CD2 1 
ATOM   2819 C CE1 . TYR C  1 53  ? -38.654 24.853  28.174  1.00 33.74 ? 53  TYR C CE1 1 
ATOM   2820 C CE2 . TYR C  1 53  ? -38.115 22.564  27.754  1.00 34.83 ? 53  TYR C CE2 1 
ATOM   2821 C CZ  . TYR C  1 53  ? -37.767 23.802  28.244  1.00 35.17 ? 53  TYR C CZ  1 
ATOM   2822 O OH  . TYR C  1 53  ? -36.524 23.993  28.803  1.00 36.33 ? 53  TYR C OH  1 
ATOM   2823 N N   . ASN C  1 54  ? -44.867 24.743  26.403  1.00 32.44 ? 54  ASN C N   1 
ATOM   2824 C CA  . ASN C  1 54  ? -46.225 24.684  25.857  1.00 33.75 ? 54  ASN C CA  1 
ATOM   2825 C C   . ASN C  1 54  ? -46.159 24.524  24.344  1.00 34.31 ? 54  ASN C C   1 
ATOM   2826 O O   . ASN C  1 54  ? -46.069 25.498  23.593  1.00 33.57 ? 54  ASN C O   1 
ATOM   2827 C CB  . ASN C  1 54  ? -47.015 25.930  26.240  1.00 33.48 ? 54  ASN C CB  1 
ATOM   2828 C CG  . ASN C  1 54  ? -48.311 25.604  26.957  1.00 33.43 ? 54  ASN C CG  1 
ATOM   2829 O OD1 . ASN C  1 54  ? -49.315 25.264  26.328  1.00 33.87 ? 54  ASN C OD1 1 
ATOM   2830 N ND2 . ASN C  1 54  ? -48.297 25.711  28.283  1.00 32.56 ? 54  ASN C ND2 1 
ATOM   2831 N N   . THR C  1 55  ? -46.221 23.273  23.888  1.00 35.23 ? 55  THR C N   1 
ATOM   2832 C CA  . THR C  1 55  ? -46.248 23.021  22.453  1.00 35.28 ? 55  THR C CA  1 
ATOM   2833 C C   . THR C  1 55  ? -47.565 23.466  21.829  1.00 35.78 ? 55  THR C C   1 
ATOM   2834 O O   . THR C  1 55  ? -47.594 23.853  20.656  1.00 36.34 ? 55  THR C O   1 
ATOM   2835 C CB  . THR C  1 55  ? -46.004 21.538  22.181  1.00 36.01 ? 55  THR C CB  1 
ATOM   2836 O OG1 . THR C  1 55  ? -46.993 20.754  22.862  1.00 35.98 ? 55  THR C OG1 1 
ATOM   2837 C CG2 . THR C  1 55  ? -44.621 21.137  22.674  1.00 36.67 ? 55  THR C CG2 1 
ATOM   2838 N N   . GLY C  1 56  ? -48.650 23.434  22.596  1.00 36.31 ? 56  GLY C N   1 
ATOM   2839 C CA  . GLY C  1 56  ? -49.976 23.657  22.058  1.00 36.79 ? 56  GLY C CA  1 
ATOM   2840 C C   . GLY C  1 56  ? -50.836 22.416  22.176  1.00 38.00 ? 56  GLY C C   1 
ATOM   2841 O O   . GLY C  1 56  ? -51.723 22.185  21.350  1.00 38.61 ? 56  GLY C O   1 
ATOM   2842 N N   . ALA C  1 57  ? -50.575 21.606  23.206  1.00 38.82 ? 57  ALA C N   1 
ATOM   2843 C CA  . ALA C  1 57  ? -51.277 20.336  23.353  1.00 38.62 ? 57  ALA C CA  1 
ATOM   2844 C C   . ALA C  1 57  ? -52.758 20.529  23.655  1.00 39.61 ? 57  ALA C C   1 
ATOM   2845 O O   . ALA C  1 57  ? -53.576 19.678  23.286  1.00 40.33 ? 57  ALA C O   1 
ATOM   2846 C CB  . ALA C  1 57  ? -50.617 19.496  24.445  1.00 39.69 ? 57  ALA C CB  1 
ATOM   2847 N N   . ALA C  1 58  ? -53.128 21.633  24.311  1.00 39.40 ? 58  ALA C N   1 
ATOM   2848 C CA  . ALA C  1 58  ? -54.530 21.862  24.651  1.00 41.00 ? 58  ALA C CA  1 
ATOM   2849 C C   . ALA C  1 58  ? -55.412 22.002  23.415  1.00 40.19 ? 58  ALA C C   1 
ATOM   2850 O O   . ALA C  1 58  ? -56.638 21.884  23.524  1.00 40.14 ? 58  ALA C O   1 
ATOM   2851 C CB  . ALA C  1 58  ? -54.663 23.107  25.533  1.00 41.05 ? 58  ALA C CB  1 
ATOM   2852 N N   . PHE C  1 59  ? -54.814 22.253  22.248  1.00 39.39 ? 59  PHE C N   1 
ATOM   2853 C CA  . PHE C  1 59  ? -55.536 22.356  20.985  1.00 38.78 ? 59  PHE C CA  1 
ATOM   2854 C C   . PHE C  1 59  ? -55.117 21.290  19.978  1.00 39.45 ? 59  PHE C C   1 
ATOM   2855 O O   . PHE C  1 59  ? -55.456 21.413  18.796  1.00 40.13 ? 59  PHE C O   1 
ATOM   2856 C CB  . PHE C  1 59  ? -55.327 23.737  20.354  1.00 37.90 ? 59  PHE C CB  1 
ATOM   2857 C CG  . PHE C  1 59  ? -56.026 24.856  21.063  1.00 36.86 ? 59  PHE C CG  1 
ATOM   2858 C CD1 . PHE C  1 59  ? -55.591 25.294  22.301  1.00 37.11 ? 59  PHE C CD1 1 
ATOM   2859 C CD2 . PHE C  1 59  ? -57.093 25.502  20.465  1.00 38.16 ? 59  PHE C CD2 1 
ATOM   2860 C CE1 . PHE C  1 59  ? -56.228 26.337  22.943  1.00 38.33 ? 59  PHE C CE1 1 
ATOM   2861 C CE2 . PHE C  1 59  ? -57.733 26.547  21.099  1.00 39.11 ? 59  PHE C CE2 1 
ATOM   2862 C CZ  . PHE C  1 59  ? -57.301 26.965  22.339  1.00 39.38 ? 59  PHE C CZ  1 
ATOM   2863 N N   . SER C  1 60  ? -54.375 20.260  20.403  1.00 39.53 ? 60  SER C N   1 
ATOM   2864 C CA  . SER C  1 60  ? -53.804 19.310  19.449  1.00 39.04 ? 60  SER C CA  1 
ATOM   2865 C C   . SER C  1 60  ? -54.875 18.529  18.702  1.00 39.44 ? 60  SER C C   1 
ATOM   2866 O O   . SER C  1 60  ? -54.673 18.154  17.542  1.00 40.43 ? 60  SER C O   1 
ATOM   2867 C CB  . SER C  1 60  ? -52.857 18.343  20.161  1.00 39.22 ? 60  SER C CB  1 
ATOM   2868 O OG  . SER C  1 60  ? -51.534 18.850  20.205  1.00 39.20 ? 60  SER C OG  1 
ATOM   2869 N N   . PHE C  1 61  ? -56.017 18.277  19.343  1.00 39.89 ? 61  PHE C N   1 
ATOM   2870 C CA  . PHE C  1 61  ? -57.056 17.441  18.749  1.00 40.03 ? 61  PHE C CA  1 
ATOM   2871 C C   . PHE C  1 61  ? -57.619 18.015  17.448  1.00 41.33 ? 61  PHE C C   1 
ATOM   2872 O O   . PHE C  1 61  ? -58.172 17.258  16.643  1.00 41.20 ? 61  PHE C O   1 
ATOM   2873 C CB  . PHE C  1 61  ? -58.183 17.231  19.765  1.00 40.49 ? 61  PHE C CB  1 
ATOM   2874 C CG  . PHE C  1 61  ? -58.786 18.510  20.266  1.00 43.41 ? 61  PHE C CG  1 
ATOM   2875 C CD1 . PHE C  1 61  ? -58.196 19.215  21.306  1.00 43.44 ? 61  PHE C CD1 1 
ATOM   2876 C CD2 . PHE C  1 61  ? -59.934 19.017  19.687  1.00 44.73 ? 61  PHE C CD2 1 
ATOM   2877 C CE1 . PHE C  1 61  ? -58.740 20.396  21.753  1.00 42.84 ? 61  PHE C CE1 1 
ATOM   2878 C CE2 . PHE C  1 61  ? -60.482 20.193  20.133  1.00 44.31 ? 61  PHE C CE2 1 
ATOM   2879 C CZ  . PHE C  1 61  ? -59.886 20.886  21.168  1.00 43.61 ? 61  PHE C CZ  1 
ATOM   2880 N N   . LEU C  1 62  ? -57.488 19.327  17.220  1.00 41.87 ? 62  LEU C N   1 
ATOM   2881 C CA  . LEU C  1 62  ? -58.128 19.953  16.063  1.00 41.60 ? 62  LEU C CA  1 
ATOM   2882 C C   . LEU C  1 62  ? -57.539 19.443  14.751  1.00 42.66 ? 62  LEU C C   1 
ATOM   2883 O O   . LEU C  1 62  ? -58.277 19.037  13.847  1.00 43.62 ? 62  LEU C O   1 
ATOM   2884 C CB  . LEU C  1 62  ? -58.003 21.475  16.156  1.00 39.99 ? 62  LEU C CB  1 
ATOM   2885 C CG  . LEU C  1 62  ? -58.801 22.105  17.299  1.00 40.59 ? 62  LEU C CG  1 
ATOM   2886 C CD1 . LEU C  1 62  ? -58.270 23.484  17.650  1.00 40.51 ? 62  LEU C CD1 1 
ATOM   2887 C CD2 . LEU C  1 62  ? -60.282 22.171  16.943  1.00 42.49 ? 62  LEU C CD2 1 
ATOM   2888 N N   . ALA C  1 63  ? -56.213 19.450  14.631  1.00 42.82 ? 63  ALA C N   1 
ATOM   2889 C CA  . ALA C  1 63  ? -55.536 19.066  13.400  1.00 43.67 ? 63  ALA C CA  1 
ATOM   2890 C C   . ALA C  1 63  ? -54.676 17.829  13.638  1.00 45.08 ? 63  ALA C C   1 
ATOM   2891 O O   . ALA C  1 63  ? -54.327 17.497  14.773  1.00 44.53 ? 63  ALA C O   1 
ATOM   2892 C CB  . ALA C  1 63  ? -54.677 20.218  12.853  1.00 43.10 ? 63  ALA C CB  1 
ATOM   2893 N N   . ASP C  1 64  ? -54.340 17.133  12.548  1.00 47.26 ? 64  ASP C N   1 
ATOM   2894 C CA  . ASP C  1 64  ? -53.527 15.923  12.650  1.00 46.11 ? 64  ASP C CA  1 
ATOM   2895 C C   . ASP C  1 64  ? -52.032 16.192  12.534  1.00 45.94 ? 64  ASP C C   1 
ATOM   2896 O O   . ASP C  1 64  ? -51.230 15.307  12.854  1.00 45.51 ? 64  ASP C O   1 
ATOM   2897 C CB  . ASP C  1 64  ? -53.940 14.898  11.584  1.00 45.55 ? 64  ASP C CB  1 
ATOM   2898 C CG  . ASP C  1 64  ? -53.883 15.459  10.175  1.00 46.34 ? 64  ASP C CG  1 
ATOM   2899 O OD1 . ASP C  1 64  ? -53.734 16.691  10.032  1.00 47.03 ? 64  ASP C OD1 1 
ATOM   2900 O OD2 . ASP C  1 64  ? -53.987 14.663  9.215   1.00 45.46 ? 64  ASP C OD2 1 
ATOM   2901 N N   . SER C  1 65  ? -51.639 17.378  12.081  1.00 44.91 ? 65  SER C N   1 
ATOM   2902 C CA  . SER C  1 65  ? -50.226 17.717  12.032  1.00 43.70 ? 65  SER C CA  1 
ATOM   2903 C C   . SER C  1 65  ? -49.692 17.943  13.444  1.00 42.24 ? 65  SER C C   1 
ATOM   2904 O O   . SER C  1 65  ? -50.415 18.372  14.349  1.00 41.41 ? 65  SER C O   1 
ATOM   2905 C CB  . SER C  1 65  ? -49.996 18.957  11.161  1.00 45.09 ? 65  SER C CB  1 
ATOM   2906 O OG  . SER C  1 65  ? -48.616 19.166  10.890  1.00 44.63 ? 65  SER C OG  1 
ATOM   2907 N N   . SER C  1 66  ? -48.419 17.615  13.634  1.00 43.08 ? 66  SER C N   1 
ATOM   2908 C CA  . SER C  1 66  ? -47.719 17.844  14.895  1.00 42.68 ? 66  SER C CA  1 
ATOM   2909 C C   . SER C  1 66  ? -46.722 18.975  14.656  1.00 41.61 ? 66  SER C C   1 
ATOM   2910 O O   . SER C  1 66  ? -45.578 18.746  14.257  1.00 41.13 ? 66  SER C O   1 
ATOM   2911 C CB  . SER C  1 66  ? -47.026 16.564  15.391  1.00 42.66 ? 66  SER C CB  1 
ATOM   2912 O OG  . SER C  1 66  ? -46.002 16.149  14.499  1.00 42.91 ? 66  SER C OG  1 
ATOM   2913 N N   . GLY C  1 67  ? -47.169 20.206  14.889  1.00 40.22 ? 67  GLY C N   1 
ATOM   2914 C CA  . GLY C  1 67  ? -46.278 21.337  14.727  1.00 40.26 ? 67  GLY C CA  1 
ATOM   2915 C C   . GLY C  1 67  ? -46.911 22.580  14.142  1.00 38.92 ? 67  GLY C C   1 
ATOM   2916 O O   . GLY C  1 67  ? -46.248 23.612  14.039  1.00 38.94 ? 67  GLY C O   1 
ATOM   2917 N N   . TRP C  1 68  ? -48.178 22.498  13.730  1.00 39.29 ? 68  TRP C N   1 
ATOM   2918 C CA  . TRP C  1 68  ? -48.855 23.679  13.205  1.00 39.57 ? 68  TRP C CA  1 
ATOM   2919 C C   . TRP C  1 68  ? -49.008 24.774  14.252  1.00 39.48 ? 68  TRP C C   1 
ATOM   2920 O O   . TRP C  1 68  ? -49.158 25.945  13.888  1.00 39.29 ? 68  TRP C O   1 
ATOM   2921 C CB  . TRP C  1 68  ? -50.228 23.305  12.650  1.00 40.76 ? 68  TRP C CB  1 
ATOM   2922 C CG  . TRP C  1 68  ? -51.089 22.580  13.634  1.00 39.97 ? 68  TRP C CG  1 
ATOM   2923 C CD1 . TRP C  1 68  ? -51.174 21.234  13.801  1.00 40.61 ? 68  TRP C CD1 1 
ATOM   2924 C CD2 . TRP C  1 68  ? -51.991 23.161  14.587  1.00 39.18 ? 68  TRP C CD2 1 
ATOM   2925 N NE1 . TRP C  1 68  ? -52.068 20.934  14.800  1.00 40.64 ? 68  TRP C NE1 1 
ATOM   2926 C CE2 . TRP C  1 68  ? -52.586 22.100  15.298  1.00 39.83 ? 68  TRP C CE2 1 
ATOM   2927 C CE3 . TRP C  1 68  ? -52.351 24.471  14.908  1.00 38.62 ? 68  TRP C CE3 1 
ATOM   2928 C CZ2 . TRP C  1 68  ? -53.523 22.310  16.311  1.00 39.74 ? 68  TRP C CZ2 1 
ATOM   2929 C CZ3 . TRP C  1 68  ? -53.282 24.677  15.913  1.00 38.26 ? 68  TRP C CZ3 1 
ATOM   2930 C CH2 . TRP C  1 68  ? -53.856 23.602  16.602  1.00 38.59 ? 68  TRP C CH2 1 
ATOM   2931 N N   . GLN C  1 69  ? -48.979 24.420  15.540  1.00 39.95 ? 69  GLN C N   1 
ATOM   2932 C CA  . GLN C  1 69  ? -49.238 25.401  16.592  1.00 39.58 ? 69  GLN C CA  1 
ATOM   2933 C C   . GLN C  1 69  ? -48.160 26.480  16.638  1.00 38.96 ? 69  GLN C C   1 
ATOM   2934 O O   . GLN C  1 69  ? -48.467 27.673  16.752  1.00 38.10 ? 69  GLN C O   1 
ATOM   2935 C CB  . GLN C  1 69  ? -49.352 24.696  17.946  1.00 39.06 ? 69  GLN C CB  1 
ATOM   2936 C CG  . GLN C  1 69  ? -50.537 23.768  18.072  1.00 38.04 ? 69  GLN C CG  1 
ATOM   2937 C CD  . GLN C  1 69  ? -50.131 22.311  18.085  1.00 38.13 ? 69  GLN C CD  1 
ATOM   2938 O OE1 . GLN C  1 69  ? -49.056 21.946  17.605  1.00 39.03 ? 69  GLN C OE1 1 
ATOM   2939 N NE2 . GLN C  1 69  ? -50.990 21.466  18.643  1.00 38.78 ? 69  GLN C NE2 1 
ATOM   2940 N N   . ARG C  1 70  ? -46.887 26.074  16.561  1.00 39.22 ? 70  ARG C N   1 
ATOM   2941 C CA  . ARG C  1 70  ? -45.781 27.021  16.693  1.00 37.87 ? 70  ARG C CA  1 
ATOM   2942 C C   . ARG C  1 70  ? -45.917 28.174  15.709  1.00 37.97 ? 70  ARG C C   1 
ATOM   2943 O O   . ARG C  1 70  ? -45.737 29.343  16.074  1.00 38.16 ? 70  ARG C O   1 
ATOM   2944 C CB  . ARG C  1 70  ? -44.447 26.295  16.485  1.00 37.82 ? 70  ARG C CB  1 
ATOM   2945 C CG  . ARG C  1 70  ? -43.226 27.205  16.389  1.00 37.57 ? 70  ARG C CG  1 
ATOM   2946 C CD  . ARG C  1 70  ? -42.110 26.549  15.588  1.00 38.28 ? 70  ARG C CD  1 
ATOM   2947 N NE  . ARG C  1 70  ? -40.800 27.084  15.937  1.00 39.62 ? 70  ARG C NE  1 
ATOM   2948 C CZ  . ARG C  1 70  ? -39.648 26.587  15.507  1.00 40.86 ? 70  ARG C CZ  1 
ATOM   2949 N NH1 . ARG C  1 70  ? -39.607 25.574  14.656  1.00 39.72 ? 70  ARG C NH1 1 
ATOM   2950 N NH2 . ARG C  1 70  ? -38.509 27.113  15.949  1.00 42.09 ? 70  ARG C NH2 1 
ATOM   2951 N N   . TRP C  1 71  ? -46.263 27.865  14.461  1.00 37.74 ? 71  TRP C N   1 
ATOM   2952 C CA  . TRP C  1 71  ? -46.343 28.868  13.410  1.00 37.64 ? 71  TRP C CA  1 
ATOM   2953 C C   . TRP C  1 71  ? -47.703 29.550  13.362  1.00 37.60 ? 71  TRP C C   1 
ATOM   2954 O O   . TRP C  1 71  ? -47.777 30.756  13.100  1.00 37.89 ? 71  TRP C O   1 
ATOM   2955 C CB  . TRP C  1 71  ? -46.012 28.231  12.058  1.00 37.25 ? 71  TRP C CB  1 
ATOM   2956 C CG  . TRP C  1 71  ? -44.667 27.565  12.061  1.00 36.86 ? 71  TRP C CG  1 
ATOM   2957 C CD1 . TRP C  1 71  ? -44.413 26.225  12.047  1.00 36.62 ? 71  TRP C CD1 1 
ATOM   2958 C CD2 . TRP C  1 71  ? -43.390 28.214  12.101  1.00 37.07 ? 71  TRP C CD2 1 
ATOM   2959 N NE1 . TRP C  1 71  ? -43.057 26.000  12.067  1.00 36.65 ? 71  TRP C NE1 1 
ATOM   2960 C CE2 . TRP C  1 71  ? -42.408 27.207  12.101  1.00 36.55 ? 71  TRP C CE2 1 
ATOM   2961 C CE3 . TRP C  1 71  ? -42.983 29.551  12.134  1.00 38.37 ? 71  TRP C CE3 1 
ATOM   2962 C CZ2 . TRP C  1 71  ? -41.046 27.494  12.131  1.00 37.31 ? 71  TRP C CZ2 1 
ATOM   2963 C CZ3 . TRP C  1 71  ? -41.633 29.833  12.161  1.00 39.79 ? 71  TRP C CZ3 1 
ATOM   2964 C CH2 . TRP C  1 71  ? -40.680 28.810  12.160  1.00 38.90 ? 71  TRP C CH2 1 
ATOM   2965 N N   . LEU C  1 72  ? -48.783 28.803  13.605  1.00 37.47 ? 72  LEU C N   1 
ATOM   2966 C CA  . LEU C  1 72  ? -50.108 29.415  13.606  1.00 37.55 ? 72  LEU C CA  1 
ATOM   2967 C C   . LEU C  1 72  ? -50.244 30.435  14.728  1.00 38.49 ? 72  LEU C C   1 
ATOM   2968 O O   . LEU C  1 72  ? -50.756 31.541  14.514  1.00 38.23 ? 72  LEU C O   1 
ATOM   2969 C CB  . LEU C  1 72  ? -51.190 28.348  13.735  1.00 36.28 ? 72  LEU C CB  1 
ATOM   2970 C CG  . LEU C  1 72  ? -52.605 28.922  13.698  1.00 35.08 ? 72  LEU C CG  1 
ATOM   2971 C CD1 . LEU C  1 72  ? -53.009 29.203  12.260  1.00 32.48 ? 72  LEU C CD1 1 
ATOM   2972 C CD2 . LEU C  1 72  ? -53.604 28.001  14.386  1.00 36.36 ? 72  LEU C CD2 1 
ATOM   2973 N N   . PHE C  1 73  ? -49.791 30.082  15.935  1.00 39.00 ? 73  PHE C N   1 
ATOM   2974 C CA  . PHE C  1 73  ? -49.854 31.006  17.060  1.00 38.85 ? 73  PHE C CA  1 
ATOM   2975 C C   . PHE C  1 73  ? -48.783 32.082  16.978  1.00 38.29 ? 73  PHE C C   1 
ATOM   2976 O O   . PHE C  1 73  ? -48.910 33.118  17.641  1.00 38.17 ? 73  PHE C O   1 
ATOM   2977 C CB  . PHE C  1 73  ? -49.759 30.234  18.379  1.00 36.85 ? 73  PHE C CB  1 
ATOM   2978 C CG  . PHE C  1 73  ? -50.876 29.257  18.570  1.00 35.89 ? 73  PHE C CG  1 
ATOM   2979 C CD1 . PHE C  1 73  ? -52.151 29.559  18.121  1.00 36.42 ? 73  PHE C CD1 1 
ATOM   2980 C CD2 . PHE C  1 73  ? -50.651 28.027  19.159  1.00 36.17 ? 73  PHE C CD2 1 
ATOM   2981 C CE1 . PHE C  1 73  ? -53.187 28.664  18.275  1.00 37.14 ? 73  PHE C CE1 1 
ATOM   2982 C CE2 . PHE C  1 73  ? -51.682 27.123  19.315  1.00 37.03 ? 73  PHE C CE2 1 
ATOM   2983 C CZ  . PHE C  1 73  ? -52.953 27.441  18.873  1.00 37.68 ? 73  PHE C CZ  1 
ATOM   2984 N N   . ALA C  1 74  ? -47.735 31.862  16.181  1.00 37.84 ? 74  ALA C N   1 
ATOM   2985 C CA  . ALA C  1 74  ? -46.884 32.974  15.780  1.00 38.39 ? 74  ALA C CA  1 
ATOM   2986 C C   . ALA C  1 74  ? -47.631 33.909  14.837  1.00 38.23 ? 74  ALA C C   1 
ATOM   2987 O O   . ALA C  1 74  ? -47.489 35.134  14.923  1.00 38.62 ? 74  ALA C O   1 
ATOM   2988 C CB  . ALA C  1 74  ? -45.608 32.449  15.125  1.00 38.97 ? 74  ALA C CB  1 
ATOM   2989 N N   . LEU C  1 75  ? -48.447 33.346  13.945  1.00 37.01 ? 75  LEU C N   1 
ATOM   2990 C CA  . LEU C  1 75  ? -49.221 34.173  13.030  1.00 36.13 ? 75  LEU C CA  1 
ATOM   2991 C C   . LEU C  1 75  ? -50.266 34.988  13.781  1.00 37.17 ? 75  LEU C C   1 
ATOM   2992 O O   . LEU C  1 75  ? -50.524 36.146  13.433  1.00 37.53 ? 75  LEU C O   1 
ATOM   2993 C CB  . LEU C  1 75  ? -49.871 33.294  11.965  1.00 34.72 ? 75  LEU C CB  1 
ATOM   2994 C CG  . LEU C  1 75  ? -50.459 34.000  10.747  1.00 32.21 ? 75  LEU C CG  1 
ATOM   2995 C CD1 . LEU C  1 75  ? -49.512 35.071  10.245  1.00 30.72 ? 75  LEU C CD1 1 
ATOM   2996 C CD2 . LEU C  1 75  ? -50.728 32.982  9.661   1.00 30.11 ? 75  LEU C CD2 1 
ATOM   2997 N N   . ILE C  1 76  ? -50.881 34.403  14.811  1.00 37.77 ? 76  ILE C N   1 
ATOM   2998 C CA  . ILE C  1 76  ? -51.839 35.153  15.619  1.00 38.08 ? 76  ILE C CA  1 
ATOM   2999 C C   . ILE C  1 76  ? -51.136 36.266  16.382  1.00 38.37 ? 76  ILE C C   1 
ATOM   3000 O O   . ILE C  1 76  ? -51.629 37.398  16.450  1.00 37.46 ? 76  ILE C O   1 
ATOM   3001 C CB  . ILE C  1 76  ? -52.596 34.218  16.578  1.00 38.52 ? 76  ILE C CB  1 
ATOM   3002 C CG1 . ILE C  1 76  ? -53.365 33.149  15.802  1.00 39.40 ? 76  ILE C CG1 1 
ATOM   3003 C CG2 . ILE C  1 76  ? -53.541 35.023  17.465  1.00 38.21 ? 76  ILE C CG2 1 
ATOM   3004 C CD1 . ILE C  1 76  ? -54.162 32.213  16.683  1.00 38.68 ? 76  ILE C CD1 1 
ATOM   3005 N N   . ALA C  1 77  ? -49.975 35.963  16.969  1.00 39.47 ? 77  ALA C N   1 
ATOM   3006 C CA  . ALA C  1 77  ? -49.252 36.951  17.761  1.00 39.58 ? 77  ALA C CA  1 
ATOM   3007 C C   . ALA C  1 77  ? -48.598 38.022  16.895  1.00 38.86 ? 77  ALA C C   1 
ATOM   3008 O O   . ALA C  1 77  ? -48.502 39.176  17.322  1.00 38.62 ? 77  ALA C O   1 
ATOM   3009 C CB  . ALA C  1 77  ? -48.201 36.259  18.632  1.00 39.17 ? 77  ALA C CB  1 
ATOM   3010 N N   . ILE C  1 78  ? -48.142 37.671  15.690  1.00 38.35 ? 78  ILE C N   1 
ATOM   3011 C CA  . ILE C  1 78  ? -47.571 38.678  14.799  1.00 38.39 ? 78  ILE C CA  1 
ATOM   3012 C C   . ILE C  1 78  ? -48.639 39.672  14.367  1.00 38.69 ? 78  ILE C C   1 
ATOM   3013 O O   . ILE C  1 78  ? -48.439 40.891  14.424  1.00 39.36 ? 78  ILE C O   1 
ATOM   3014 C CB  . ILE C  1 78  ? -46.908 38.010  13.581  1.00 38.41 ? 78  ILE C CB  1 
ATOM   3015 C CG1 . ILE C  1 78  ? -45.563 37.402  13.971  1.00 40.75 ? 78  ILE C CG1 1 
ATOM   3016 C CG2 . ILE C  1 78  ? -46.738 39.013  12.443  1.00 38.06 ? 78  ILE C CG2 1 
ATOM   3017 C CD1 . ILE C  1 78  ? -44.856 36.709  12.828  1.00 41.79 ? 78  ILE C CD1 1 
ATOM   3018 N N   . VAL C  1 79  ? -49.796 39.166  13.940  1.00 38.21 ? 79  VAL C N   1 
ATOM   3019 C CA  . VAL C  1 79  ? -50.835 40.039  13.403  1.00 37.23 ? 79  VAL C CA  1 
ATOM   3020 C C   . VAL C  1 79  ? -51.365 40.965  14.486  1.00 37.56 ? 79  VAL C C   1 
ATOM   3021 O O   . VAL C  1 79  ? -51.462 42.181  14.294  1.00 38.41 ? 79  VAL C O   1 
ATOM   3022 C CB  . VAL C  1 79  ? -51.967 39.205  12.778  1.00 36.62 ? 79  VAL C CB  1 
ATOM   3023 C CG1 . VAL C  1 79  ? -53.156 40.096  12.452  1.00 36.88 ? 79  VAL C CG1 1 
ATOM   3024 C CG2 . VAL C  1 79  ? -51.472 38.499  11.532  1.00 35.47 ? 79  VAL C CG2 1 
ATOM   3025 N N   . VAL C  1 80  ? -51.709 40.405  15.645  1.00 37.31 ? 80  VAL C N   1 
ATOM   3026 C CA  . VAL C  1 80  ? -52.334 41.212  16.683  1.00 37.46 ? 80  VAL C CA  1 
ATOM   3027 C C   . VAL C  1 80  ? -51.340 42.192  17.295  1.00 39.11 ? 80  VAL C C   1 
ATOM   3028 O O   . VAL C  1 80  ? -51.709 43.323  17.632  1.00 40.09 ? 80  VAL C O   1 
ATOM   3029 C CB  . VAL C  1 80  ? -52.979 40.302  17.741  1.00 37.26 ? 80  VAL C CB  1 
ATOM   3030 C CG1 . VAL C  1 80  ? -53.670 41.131  18.804  1.00 36.75 ? 80  VAL C CG1 1 
ATOM   3031 C CG2 . VAL C  1 80  ? -53.976 39.372  17.074  1.00 37.31 ? 80  VAL C CG2 1 
ATOM   3032 N N   . SER C  1 81  ? -50.074 41.791  17.448  1.00 39.67 ? 81  SER C N   1 
ATOM   3033 C CA  . SER C  1 81  ? -49.070 42.715  17.974  1.00 40.65 ? 81  SER C CA  1 
ATOM   3034 C C   . SER C  1 81  ? -48.865 43.901  17.039  1.00 40.14 ? 81  SER C C   1 
ATOM   3035 O O   . SER C  1 81  ? -48.656 45.028  17.499  1.00 39.69 ? 81  SER C O   1 
ATOM   3036 C CB  . SER C  1 81  ? -47.746 41.986  18.219  1.00 41.53 ? 81  SER C CB  1 
ATOM   3037 O OG  . SER C  1 81  ? -47.887 40.971  19.204  1.00 40.75 ? 81  SER C OG  1 
ATOM   3038 N N   . ALA C  1 82  ? -48.919 43.669  15.725  1.00 39.84 ? 82  ALA C N   1 
ATOM   3039 C CA  . ALA C  1 82  ? -48.899 44.788  14.790  1.00 39.74 ? 82  ALA C CA  1 
ATOM   3040 C C   . ALA C  1 82  ? -50.219 45.549  14.819  1.00 39.71 ? 82  ALA C C   1 
ATOM   3041 O O   . ALA C  1 82  ? -50.237 46.774  14.663  1.00 40.36 ? 82  ALA C O   1 
ATOM   3042 C CB  . ALA C  1 82  ? -48.584 44.292  13.379  1.00 38.99 ? 82  ALA C CB  1 
ATOM   3043 N N   . SER C  1 83  ? -51.335 44.840  15.004  1.00 39.95 ? 83  SER C N   1 
ATOM   3044 C CA  . SER C  1 83  ? -52.633 45.506  15.083  1.00 40.63 ? 83  SER C CA  1 
ATOM   3045 C C   . SER C  1 83  ? -52.744 46.364  16.339  1.00 40.95 ? 83  SER C C   1 
ATOM   3046 O O   . SER C  1 83  ? -53.353 47.441  16.309  1.00 41.03 ? 83  SER C O   1 
ATOM   3047 C CB  . SER C  1 83  ? -53.754 44.468  15.036  1.00 40.01 ? 83  SER C CB  1 
ATOM   3048 O OG  . SER C  1 83  ? -55.004 45.050  15.355  1.00 41.08 ? 83  SER C OG  1 
ATOM   3049 N N   . LEU C  1 84  ? -52.169 45.897  17.451  1.00 40.94 ? 84  LEU C N   1 
ATOM   3050 C CA  . LEU C  1 84  ? -52.203 46.651  18.703  1.00 41.10 ? 84  LEU C CA  1 
ATOM   3051 C C   . LEU C  1 84  ? -51.375 47.932  18.623  1.00 41.96 ? 84  LEU C C   1 
ATOM   3052 O O   . LEU C  1 84  ? -51.697 48.917  19.298  1.00 42.43 ? 84  LEU C O   1 
ATOM   3053 C CB  . LEU C  1 84  ? -51.714 45.763  19.853  1.00 40.52 ? 84  LEU C CB  1 
ATOM   3054 C CG  . LEU C  1 84  ? -52.693 44.768  20.492  1.00 39.54 ? 84  LEU C CG  1 
ATOM   3055 C CD1 . LEU C  1 84  ? -52.017 43.467  20.941  1.00 38.07 ? 84  LEU C CD1 1 
ATOM   3056 C CD2 . LEU C  1 84  ? -53.407 45.412  21.666  1.00 38.70 ? 84  LEU C CD2 1 
ATOM   3057 N N   . VAL C  1 85  ? -50.306 47.932  17.822  1.00 41.88 ? 85  VAL C N   1 
ATOM   3058 C CA  . VAL C  1 85  ? -49.501 49.141  17.634  1.00 41.26 ? 85  VAL C CA  1 
ATOM   3059 C C   . VAL C  1 85  ? -50.340 50.249  17.008  1.00 42.05 ? 85  VAL C C   1 
ATOM   3060 O O   . VAL C  1 85  ? -50.301 51.405  17.448  1.00 42.60 ? 85  VAL C O   1 
ATOM   3061 C CB  . VAL C  1 85  ? -48.253 48.827  16.787  1.00 40.70 ? 85  VAL C CB  1 
ATOM   3062 C CG1 . VAL C  1 85  ? -47.564 50.118  16.331  1.00 38.82 ? 85  VAL C CG1 1 
ATOM   3063 C CG2 . VAL C  1 85  ? -47.299 47.954  17.572  1.00 41.18 ? 85  VAL C CG2 1 
ATOM   3064 N N   . VAL C  1 86  ? -51.122 49.900  15.978  1.00 43.03 ? 86  VAL C N   1 
ATOM   3065 C CA  . VAL C  1 86  ? -51.957 50.872  15.266  1.00 43.01 ? 86  VAL C CA  1 
ATOM   3066 C C   . VAL C  1 86  ? -52.904 51.582  16.228  1.00 43.73 ? 86  VAL C C   1 
ATOM   3067 O O   . VAL C  1 86  ? -53.040 52.812  16.195  1.00 44.21 ? 86  VAL C O   1 
ATOM   3068 C CB  . VAL C  1 86  ? -52.732 50.184  14.123  1.00 41.67 ? 86  VAL C CB  1 
ATOM   3069 C CG1 . VAL C  1 86  ? -53.665 51.176  13.441  1.00 42.52 ? 86  VAL C CG1 1 
ATOM   3070 C CG2 . VAL C  1 86  ? -51.766 49.564  13.140  1.00 41.72 ? 86  VAL C CG2 1 
ATOM   3071 N N   . TRP C  1 87  ? -53.595 50.820  17.081  1.00 43.86 ? 87  TRP C N   1 
ATOM   3072 C CA  . TRP C  1 87  ? -54.482 51.455  18.052  1.00 45.52 ? 87  TRP C CA  1 
ATOM   3073 C C   . TRP C  1 87  ? -53.697 52.344  19.016  1.00 45.38 ? 87  TRP C C   1 
ATOM   3074 O O   . TRP C  1 87  ? -54.110 53.475  19.296  1.00 46.52 ? 87  TRP C O   1 
ATOM   3075 C CB  . TRP C  1 87  ? -55.303 50.402  18.813  1.00 46.69 ? 87  TRP C CB  1 
ATOM   3076 C CG  . TRP C  1 87  ? -56.488 50.968  19.563  1.00 49.63 ? 87  TRP C CG  1 
ATOM   3077 C CD1 . TRP C  1 87  ? -57.011 52.224  19.440  1.00 51.19 ? 87  TRP C CD1 1 
ATOM   3078 C CD2 . TRP C  1 87  ? -57.287 50.299  20.551  1.00 50.33 ? 87  TRP C CD2 1 
ATOM   3079 N NE1 . TRP C  1 87  ? -58.084 52.377  20.282  1.00 51.60 ? 87  TRP C NE1 1 
ATOM   3080 C CE2 . TRP C  1 87  ? -58.274 51.212  20.977  1.00 51.93 ? 87  TRP C CE2 1 
ATOM   3081 C CE3 . TRP C  1 87  ? -57.264 49.019  21.115  1.00 50.99 ? 87  TRP C CE3 1 
ATOM   3082 C CZ2 . TRP C  1 87  ? -59.228 50.889  21.940  1.00 52.49 ? 87  TRP C CZ2 1 
ATOM   3083 C CZ3 . TRP C  1 87  ? -58.216 48.699  22.074  1.00 51.56 ? 87  TRP C CZ3 1 
ATOM   3084 C CH2 . TRP C  1 87  ? -59.183 49.632  22.475  1.00 52.40 ? 87  TRP C CH2 1 
ATOM   3085 N N   . LEU C  1 88  ? -52.538 51.873  19.498  1.00 43.26 ? 88  LEU C N   1 
ATOM   3086 C CA  . LEU C  1 88  ? -51.792 52.636  20.502  1.00 43.48 ? 88  LEU C CA  1 
ATOM   3087 C C   . LEU C  1 88  ? -51.397 54.012  19.978  1.00 44.33 ? 88  LEU C C   1 
ATOM   3088 O O   . LEU C  1 88  ? -51.479 55.009  20.706  1.00 45.16 ? 88  LEU C O   1 
ATOM   3089 C CB  . LEU C  1 88  ? -50.552 51.861  20.962  1.00 42.82 ? 88  LEU C CB  1 
ATOM   3090 C CG  . LEU C  1 88  ? -49.746 52.429  22.147  1.00 43.50 ? 88  LEU C CG  1 
ATOM   3091 C CD1 . LEU C  1 88  ? -49.263 51.309  23.059  1.00 42.63 ? 88  LEU C CD1 1 
ATOM   3092 C CD2 . LEU C  1 88  ? -48.556 53.298  21.707  1.00 42.39 ? 88  LEU C CD2 1 
ATOM   3093 N N   . LYS C  1 89  ? -50.965 54.089  18.719  1.00 43.71 ? 89  LYS C N   1 
ATOM   3094 C CA  . LYS C  1 89  ? -50.678 55.391  18.127  1.00 43.15 ? 89  LYS C CA  1 
ATOM   3095 C C   . LYS C  1 89  ? -51.945 56.231  18.002  1.00 45.25 ? 89  LYS C C   1 
ATOM   3096 O O   . LYS C  1 89  ? -51.922 57.437  18.272  1.00 46.10 ? 89  LYS C O   1 
ATOM   3097 C CB  . LYS C  1 89  ? -49.997 55.212  16.770  1.00 40.30 ? 89  LYS C CB  1 
ATOM   3098 C CG  . LYS C  1 89  ? -48.651 54.503  16.857  1.00 38.02 ? 89  LYS C CG  1 
ATOM   3099 C CD  . LYS C  1 89  ? -48.035 54.297  15.489  1.00 36.20 ? 89  LYS C CD  1 
ATOM   3100 C CE  . LYS C  1 89  ? -46.636 53.717  15.607  1.00 35.45 ? 89  LYS C CE  1 
ATOM   3101 N NZ  . LYS C  1 89  ? -45.752 54.570  16.454  1.00 37.12 ? 89  LYS C NZ  1 
ATOM   3102 N N   . ARG C  1 90  ? -53.065 55.614  17.614  1.00 45.70 ? 90  ARG C N   1 
ATOM   3103 C CA  . ARG C  1 90  ? -54.313 56.359  17.466  1.00 47.07 ? 90  ARG C CA  1 
ATOM   3104 C C   . ARG C  1 90  ? -54.881 56.839  18.799  1.00 49.36 ? 90  ARG C C   1 
ATOM   3105 O O   . ARG C  1 90  ? -55.801 57.667  18.797  1.00 51.33 ? 90  ARG C O   1 
ATOM   3106 C CB  . ARG C  1 90  ? -55.357 55.512  16.725  1.00 46.32 ? 90  ARG C CB  1 
ATOM   3107 C CG  . ARG C  1 90  ? -54.986 55.172  15.280  1.00 46.40 ? 90  ARG C CG  1 
ATOM   3108 C CD  . ARG C  1 90  ? -56.124 54.458  14.548  1.00 47.07 ? 90  ARG C CD  1 
ATOM   3109 N NE  . ARG C  1 90  ? -55.735 54.044  13.203  1.00 46.52 ? 90  ARG C NE  1 
ATOM   3110 C CZ  . ARG C  1 90  ? -56.577 53.617  12.270  1.00 46.90 ? 90  ARG C CZ  1 
ATOM   3111 N NH1 . ARG C  1 90  ? -57.880 53.543  12.493  1.00 47.07 ? 90  ARG C NH1 1 
ATOM   3112 N NH2 . ARG C  1 90  ? -56.099 53.259  11.080  1.00 46.37 ? 90  ARG C NH2 1 
ATOM   3113 N N   . LEU C  1 91  ? -54.363 56.354  19.927  1.00 48.53 ? 91  LEU C N   1 
ATOM   3114 C CA  . LEU C  1 91  ? -54.842 56.800  21.228  1.00 49.47 ? 91  LEU C CA  1 
ATOM   3115 C C   . LEU C  1 91  ? -54.289 58.175  21.574  1.00 51.34 ? 91  LEU C C   1 
ATOM   3116 O O   . LEU C  1 91  ? -53.146 58.507  21.243  1.00 50.95 ? 91  LEU C O   1 
ATOM   3117 C CB  . LEU C  1 91  ? -54.444 55.817  22.320  1.00 49.00 ? 91  LEU C CB  1 
ATOM   3118 C CG  . LEU C  1 91  ? -54.966 54.405  22.175  1.00 48.29 ? 91  LEU C CG  1 
ATOM   3119 C CD1 . LEU C  1 91  ? -54.217 53.558  23.160  1.00 47.30 ? 91  LEU C CD1 1 
ATOM   3120 C CD2 . LEU C  1 91  ? -56.469 54.381  22.430  1.00 49.66 ? 91  LEU C CD2 1 
ATOM   3121 N N   . LYS C  1 92  ? -55.099 58.961  22.272  1.00 52.95 ? 92  LYS C N   1 
ATOM   3122 C CA  . LYS C  1 92  ? -54.737 60.320  22.629  1.00 53.51 ? 92  LYS C CA  1 
ATOM   3123 C C   . LYS C  1 92  ? -54.163 60.377  24.045  1.00 54.64 ? 92  LYS C C   1 
ATOM   3124 O O   . LYS C  1 92  ? -54.000 59.361  24.727  1.00 54.54 ? 92  LYS C O   1 
ATOM   3125 C CB  . LYS C  1 92  ? -55.953 61.232  22.474  1.00 54.70 ? 92  LYS C CB  1 
ATOM   3126 C CG  . LYS C  1 92  ? -57.259 60.605  22.949  1.00 55.77 ? 92  LYS C CG  1 
ATOM   3127 C CD  . LYS C  1 92  ? -57.744 61.229  24.250  1.00 55.98 ? 92  LYS C CD  1 
ATOM   3128 C CE  . LYS C  1 92  ? -59.045 60.594  24.722  1.00 55.27 ? 92  LYS C CE  1 
ATOM   3129 N NZ  . LYS C  1 92  ? -59.568 61.210  25.976  1.00 55.28 ? 92  LYS C NZ  1 
ATOM   3130 N N   . LYS C  1 93  ? -53.824 61.590  24.478  1.00 54.90 ? 93  LYS C N   1 
ATOM   3131 C CA  . LYS C  1 93  ? -53.289 61.824  25.808  1.00 54.58 ? 93  LYS C CA  1 
ATOM   3132 C C   . LYS C  1 93  ? -54.410 61.777  26.844  1.00 55.03 ? 93  LYS C C   1 
ATOM   3133 O O   . LYS C  1 93  ? -55.598 61.824  26.520  1.00 54.95 ? 93  LYS C O   1 
ATOM   3134 C CB  . LYS C  1 93  ? -52.573 63.174  25.875  1.00 53.26 ? 93  LYS C CB  1 
ATOM   3135 C CG  . LYS C  1 93  ? -51.575 63.430  24.751  1.00 53.14 ? 93  LYS C CG  1 
ATOM   3136 C CD  . LYS C  1 93  ? -50.937 64.808  24.904  1.00 52.15 ? 93  LYS C CD  1 
ATOM   3137 C CE  . LYS C  1 93  ? -50.251 65.260  23.623  1.00 50.70 ? 93  LYS C CE  1 
ATOM   3138 N NZ  . LYS C  1 93  ? -49.226 64.283  23.159  1.00 49.51 ? 93  LYS C NZ  1 
ATOM   3139 N N   . GLY C  1 94  ? -54.016 61.690  28.111  1.00 55.58 ? 94  GLY C N   1 
ATOM   3140 C CA  . GLY C  1 94  ? -54.975 61.614  29.195  1.00 55.69 ? 94  GLY C CA  1 
ATOM   3141 C C   . GLY C  1 94  ? -55.503 60.212  29.412  1.00 55.24 ? 94  GLY C C   1 
ATOM   3142 O O   . GLY C  1 94  ? -55.662 59.774  30.555  1.00 56.11 ? 94  GLY C O   1 
ATOM   3143 N N   . GLU C  1 95  ? -55.774 59.494  28.319  1.00 54.84 ? 95  GLU C N   1 
ATOM   3144 C CA  . GLU C  1 95  ? -56.296 58.128  28.386  1.00 52.96 ? 95  GLU C CA  1 
ATOM   3145 C C   . GLU C  1 95  ? -55.148 57.178  28.729  1.00 51.26 ? 95  GLU C C   1 
ATOM   3146 O O   . GLU C  1 95  ? -54.733 56.324  27.942  1.00 50.58 ? 95  GLU C O   1 
ATOM   3147 C CB  . GLU C  1 95  ? -56.976 57.752  27.076  1.00 53.66 ? 95  GLU C CB  1 
ATOM   3148 C CG  . GLU C  1 95  ? -58.000 56.637  27.212  1.00 54.15 ? 95  GLU C CG  1 
ATOM   3149 C CD  . GLU C  1 95  ? -59.077 56.696  26.140  1.00 55.12 ? 95  GLU C CD  1 
ATOM   3150 O OE1 . GLU C  1 95  ? -58.791 57.206  25.034  1.00 55.13 ? 95  GLU C OE1 1 
ATOM   3151 O OE2 . GLU C  1 95  ? -60.214 56.243  26.409  1.00 54.54 ? 95  GLU C OE2 1 
ATOM   3152 N N   . THR C  1 96  ? -54.630 57.352  29.949  1.00 51.20 ? 96  THR C N   1 
ATOM   3153 C CA  . THR C  1 96  ? -53.475 56.578  30.394  1.00 49.19 ? 96  THR C CA  1 
ATOM   3154 C C   . THR C  1 96  ? -53.834 55.111  30.596  1.00 47.03 ? 96  THR C C   1 
ATOM   3155 O O   . THR C  1 96  ? -53.124 54.220  30.117  1.00 45.86 ? 96  THR C O   1 
ATOM   3156 C CB  . THR C  1 96  ? -52.911 57.177  31.684  1.00 48.22 ? 96  THR C CB  1 
ATOM   3157 O OG1 . THR C  1 96  ? -53.889 57.078  32.727  1.00 47.78 ? 96  THR C OG1 1 
ATOM   3158 C CG2 . THR C  1 96  ? -52.544 58.640  31.476  1.00 48.27 ? 96  THR C CG2 1 
ATOM   3159 N N   . TRP C  1 97  ? -54.953 54.846  31.280  1.00 47.88 ? 97  TRP C N   1 
ATOM   3160 C CA  . TRP C  1 97  ? -55.331 53.476  31.623  1.00 47.02 ? 97  TRP C CA  1 
ATOM   3161 C C   . TRP C  1 97  ? -55.436 52.596  30.382  1.00 46.56 ? 97  TRP C C   1 
ATOM   3162 O O   . TRP C  1 97  ? -54.981 51.446  30.384  1.00 45.96 ? 97  TRP C O   1 
ATOM   3163 C CB  . TRP C  1 97  ? -56.654 53.485  32.391  1.00 47.11 ? 97  TRP C CB  1 
ATOM   3164 C CG  . TRP C  1 97  ? -57.226 52.125  32.684  1.00 47.17 ? 97  TRP C CG  1 
ATOM   3165 C CD1 . TRP C  1 97  ? -57.794 51.258  31.792  1.00 47.00 ? 97  TRP C CD1 1 
ATOM   3166 C CD2 . TRP C  1 97  ? -57.320 51.494  33.967  1.00 47.79 ? 97  TRP C CD2 1 
ATOM   3167 N NE1 . TRP C  1 97  ? -58.217 50.122  32.437  1.00 48.35 ? 97  TRP C NE1 1 
ATOM   3168 C CE2 . TRP C  1 97  ? -57.939 50.242  33.773  1.00 48.17 ? 97  TRP C CE2 1 
ATOM   3169 C CE3 . TRP C  1 97  ? -56.934 51.863  35.259  1.00 48.05 ? 97  TRP C CE3 1 
ATOM   3170 C CZ2 . TRP C  1 97  ? -58.181 49.357  34.824  1.00 47.31 ? 97  TRP C CZ2 1 
ATOM   3171 C CZ3 . TRP C  1 97  ? -57.175 50.984  36.300  1.00 48.32 ? 97  TRP C CZ3 1 
ATOM   3172 C CH2 . TRP C  1 97  ? -57.792 49.745  36.076  1.00 47.42 ? 97  TRP C CH2 1 
ATOM   3173 N N   . LEU C  1 98  ? -56.057 53.107  29.317  1.00 47.55 ? 98  LEU C N   1 
ATOM   3174 C CA  . LEU C  1 98  ? -56.170 52.322  28.091  1.00 46.67 ? 98  LEU C CA  1 
ATOM   3175 C C   . LEU C  1 98  ? -54.796 52.042  27.489  1.00 45.43 ? 98  LEU C C   1 
ATOM   3176 O O   . LEU C  1 98  ? -54.549 50.945  26.976  1.00 45.22 ? 98  LEU C O   1 
ATOM   3177 C CB  . LEU C  1 98  ? -57.081 53.034  27.088  1.00 48.68 ? 98  LEU C CB  1 
ATOM   3178 C CG  . LEU C  1 98  ? -57.651 52.236  25.906  1.00 48.38 ? 98  LEU C CG  1 
ATOM   3179 C CD1 . LEU C  1 98  ? -58.336 50.958  26.362  1.00 47.75 ? 98  LEU C CD1 1 
ATOM   3180 C CD2 . LEU C  1 98  ? -58.624 53.093  25.112  1.00 49.88 ? 98  LEU C CD2 1 
ATOM   3181 N N   . ALA C  1 99  ? -53.881 53.013  27.556  1.00 45.92 ? 99  ALA C N   1 
ATOM   3182 C CA  . ALA C  1 99  ? -52.531 52.772  27.054  1.00 45.49 ? 99  ALA C CA  1 
ATOM   3183 C C   . ALA C  1 99  ? -51.767 51.782  27.929  1.00 43.69 ? 99  ALA C C   1 
ATOM   3184 O O   . ALA C  1 99  ? -50.912 51.045  27.421  1.00 42.72 ? 99  ALA C O   1 
ATOM   3185 C CB  . ALA C  1 99  ? -51.762 54.092  26.942  1.00 46.70 ? 99  ALA C CB  1 
ATOM   3186 N N   . ILE C  1 100 ? -52.046 51.752  29.236  1.00 43.28 ? 100 ILE C N   1 
ATOM   3187 C CA  . ILE C  1 100 ? -51.406 50.767  30.105  1.00 41.83 ? 100 ILE C CA  1 
ATOM   3188 C C   . ILE C  1 100 ? -51.896 49.367  29.768  1.00 40.87 ? 100 ILE C C   1 
ATOM   3189 O O   . ILE C  1 100 ? -51.106 48.419  29.683  1.00 39.89 ? 100 ILE C O   1 
ATOM   3190 C CB  . ILE C  1 100 ? -51.659 51.097  31.587  1.00 41.74 ? 100 ILE C CB  1 
ATOM   3191 C CG1 . ILE C  1 100 ? -51.334 52.557  31.886  1.00 42.54 ? 100 ILE C CG1 1 
ATOM   3192 C CG2 . ILE C  1 100 ? -50.816 50.197  32.476  1.00 41.71 ? 100 ILE C CG2 1 
ATOM   3193 C CD1 . ILE C  1 100 ? -51.891 53.026  33.208  1.00 43.85 ? 100 ILE C CD1 1 
ATOM   3194 N N   . ALA C  1 101 ? -53.209 49.214  29.582  1.00 41.26 ? 101 ALA C N   1 
ATOM   3195 C CA  . ALA C  1 101 ? -53.763 47.915  29.225  1.00 39.43 ? 101 ALA C CA  1 
ATOM   3196 C C   . ALA C  1 101 ? -53.210 47.430  27.894  1.00 39.97 ? 101 ALA C C   1 
ATOM   3197 O O   . ALA C  1 101 ? -52.918 46.240  27.730  1.00 41.38 ? 101 ALA C O   1 
ATOM   3198 C CB  . ALA C  1 101 ? -55.288 47.989  29.174  1.00 40.41 ? 101 ALA C CB  1 
ATOM   3199 N N   . LEU C  1 102 ? -53.067 48.332  26.925  1.00 40.06 ? 102 LEU C N   1 
ATOM   3200 C CA  . LEU C  1 102 ? -52.639 47.904  25.598  1.00 39.94 ? 102 LEU C CA  1 
ATOM   3201 C C   . LEU C  1 102 ? -51.143 47.619  25.552  1.00 39.73 ? 102 LEU C C   1 
ATOM   3202 O O   . LEU C  1 102 ? -50.704 46.712  24.836  1.00 39.61 ? 102 LEU C O   1 
ATOM   3203 C CB  . LEU C  1 102 ? -53.039 48.948  24.565  1.00 41.16 ? 102 LEU C CB  1 
ATOM   3204 C CG  . LEU C  1 102 ? -54.561 48.977  24.456  1.00 44.21 ? 102 LEU C CG  1 
ATOM   3205 C CD1 . LEU C  1 102 ? -55.030 50.277  23.841  1.00 47.53 ? 102 LEU C CD1 1 
ATOM   3206 C CD2 . LEU C  1 102 ? -55.050 47.757  23.670  1.00 44.74 ? 102 LEU C CD2 1 
ATOM   3207 N N   . ALA C  1 103 ? -50.341 48.375  26.303  1.00 39.79 ? 103 ALA C N   1 
ATOM   3208 C CA  . ALA C  1 103 ? -48.907 48.103  26.333  1.00 38.45 ? 103 ALA C CA  1 
ATOM   3209 C C   . ALA C  1 103 ? -48.587 46.820  27.096  1.00 38.40 ? 103 ALA C C   1 
ATOM   3210 O O   . ALA C  1 103 ? -47.594 46.150  26.787  1.00 38.63 ? 103 ALA C O   1 
ATOM   3211 C CB  . ALA C  1 103 ? -48.158 49.290  26.941  1.00 38.50 ? 103 ALA C CB  1 
ATOM   3212 N N   . LEU C  1 104 ? -49.402 46.466  28.097  1.00 38.10 ? 104 LEU C N   1 
ATOM   3213 C CA  . LEU C  1 104 ? -49.207 45.199  28.798  1.00 37.12 ? 104 LEU C CA  1 
ATOM   3214 C C   . LEU C  1 104 ? -49.413 44.012  27.865  1.00 36.94 ? 104 LEU C C   1 
ATOM   3215 O O   . LEU C  1 104 ? -48.626 43.057  27.882  1.00 36.85 ? 104 LEU C O   1 
ATOM   3216 C CB  . LEU C  1 104 ? -50.155 45.104  29.994  1.00 36.66 ? 104 LEU C CB  1 
ATOM   3217 C CG  . LEU C  1 104 ? -49.748 45.872  31.251  1.00 36.25 ? 104 LEU C CG  1 
ATOM   3218 C CD1 . LEU C  1 104 ? -50.854 45.799  32.286  1.00 37.93 ? 104 LEU C CD1 1 
ATOM   3219 C CD2 . LEU C  1 104 ? -48.452 45.317  31.815  1.00 36.61 ? 104 LEU C CD2 1 
ATOM   3220 N N   . VAL C  1 105 ? -50.462 44.057  27.042  1.00 36.81 ? 105 VAL C N   1 
ATOM   3221 C CA  . VAL C  1 105 ? -50.719 42.973  26.099  1.00 36.96 ? 105 VAL C CA  1 
ATOM   3222 C C   . VAL C  1 105 ? -49.643 42.935  25.017  1.00 36.80 ? 105 VAL C C   1 
ATOM   3223 O O   . VAL C  1 105 ? -49.234 41.859  24.561  1.00 35.98 ? 105 VAL C O   1 
ATOM   3224 C CB  . VAL C  1 105 ? -52.131 43.117  25.504  1.00 35.79 ? 105 VAL C CB  1 
ATOM   3225 C CG1 . VAL C  1 105 ? -52.378 42.053  24.453  1.00 35.76 ? 105 VAL C CG1 1 
ATOM   3226 C CG2 . VAL C  1 105 ? -53.171 43.030  26.611  1.00 35.83 ? 105 VAL C CG2 1 
ATOM   3227 N N   . LEU C  1 106 ? -49.172 44.106  24.588  1.00 36.92 ? 106 LEU C N   1 
ATOM   3228 C CA  . LEU C  1 106 ? -48.093 44.166  23.608  1.00 36.97 ? 106 LEU C CA  1 
ATOM   3229 C C   . LEU C  1 106 ? -46.850 43.454  24.115  1.00 38.25 ? 106 LEU C C   1 
ATOM   3230 O O   . LEU C  1 106 ? -46.286 42.593  23.430  1.00 38.44 ? 106 LEU C O   1 
ATOM   3231 C CB  . LEU C  1 106 ? -47.767 45.622  23.291  1.00 38.99 ? 106 LEU C CB  1 
ATOM   3232 C CG  . LEU C  1 106 ? -48.585 46.298  22.200  1.00 41.12 ? 106 LEU C CG  1 
ATOM   3233 C CD1 . LEU C  1 106 ? -48.318 47.799  22.217  1.00 39.93 ? 106 LEU C CD1 1 
ATOM   3234 C CD2 . LEU C  1 106 ? -48.216 45.692  20.867  1.00 40.56 ? 106 LEU C CD2 1 
ATOM   3235 N N   . GLY C  1 107 ? -46.407 43.810  25.323  1.00 38.95 ? 107 GLY C N   1 
ATOM   3236 C CA  . GLY C  1 107 ? -45.213 43.206  25.880  1.00 38.90 ? 107 GLY C CA  1 
ATOM   3237 C C   . GLY C  1 107 ? -45.376 41.735  26.190  1.00 38.73 ? 107 GLY C C   1 
ATOM   3238 O O   . GLY C  1 107 ? -44.425 40.962  26.048  1.00 39.36 ? 107 GLY C O   1 
ATOM   3239 N N   . GLY C  1 108 ? -46.573 41.329  26.619  1.00 38.28 ? 108 GLY C N   1 
ATOM   3240 C CA  . GLY C  1 108 ? -46.791 39.935  26.969  1.00 37.12 ? 108 GLY C CA  1 
ATOM   3241 C C   . GLY C  1 108 ? -46.781 39.013  25.764  1.00 36.23 ? 108 GLY C C   1 
ATOM   3242 O O   . GLY C  1 108 ? -46.148 37.956  25.787  1.00 36.16 ? 108 GLY C O   1 
ATOM   3243 N N   . ALA C  1 109 ? -47.470 39.405  24.691  1.00 36.45 ? 109 ALA C N   1 
ATOM   3244 C CA  . ALA C  1 109 ? -47.582 38.572  23.501  1.00 35.92 ? 109 ALA C CA  1 
ATOM   3245 C C   . ALA C  1 109 ? -46.351 38.642  22.610  1.00 36.21 ? 109 ALA C C   1 
ATOM   3246 O O   . ALA C  1 109 ? -46.286 37.910  21.619  1.00 36.16 ? 109 ALA C O   1 
ATOM   3247 C CB  . ALA C  1 109 ? -48.826 38.972  22.702  1.00 36.64 ? 109 ALA C CB  1 
ATOM   3248 N N   . LEU C  1 110 ? -45.386 39.503  22.929  1.00 37.17 ? 110 LEU C N   1 
ATOM   3249 C CA  . LEU C  1 110 ? -44.120 39.548  22.206  1.00 37.90 ? 110 LEU C CA  1 
ATOM   3250 C C   . LEU C  1 110 ? -43.112 38.548  22.755  1.00 37.48 ? 110 LEU C C   1 
ATOM   3251 O O   . LEU C  1 110 ? -42.365 37.935  21.985  1.00 38.66 ? 110 LEU C O   1 
ATOM   3252 C CB  . LEU C  1 110 ? -43.531 40.960  22.257  1.00 38.97 ? 110 LEU C CB  1 
ATOM   3253 C CG  . LEU C  1 110 ? -44.054 41.950  21.216  1.00 38.60 ? 110 LEU C CG  1 
ATOM   3254 C CD1 . LEU C  1 110 ? -43.528 43.344  21.505  1.00 41.53 ? 110 LEU C CD1 1 
ATOM   3255 C CD2 . LEU C  1 110 ? -43.665 41.505  19.814  1.00 39.80 ? 110 LEU C CD2 1 
ATOM   3256 N N   . GLY C  1 111 ? -43.074 38.375  24.077  1.00 36.70 ? 111 GLY C N   1 
ATOM   3257 C CA  . GLY C  1 111 ? -42.178 37.388  24.652  1.00 36.51 ? 111 GLY C CA  1 
ATOM   3258 C C   . GLY C  1 111 ? -42.524 35.978  24.221  1.00 35.97 ? 111 GLY C C   1 
ATOM   3259 O O   . GLY C  1 111 ? -41.643 35.195  23.857  1.00 36.57 ? 111 GLY C O   1 
ATOM   3260 N N   . ASN C  1 112 ? -43.814 35.640  24.242  1.00 35.02 ? 112 ASN C N   1 
ATOM   3261 C CA  . ASN C  1 112 ? -44.238 34.322  23.788  1.00 34.66 ? 112 ASN C CA  1 
ATOM   3262 C C   . ASN C  1 112 ? -43.971 34.140  22.301  1.00 36.04 ? 112 ASN C C   1 
ATOM   3263 O O   . ASN C  1 112 ? -43.526 33.069  21.873  1.00 37.70 ? 112 ASN C O   1 
ATOM   3264 C CB  . ASN C  1 112 ? -45.715 34.110  24.105  1.00 33.74 ? 112 ASN C CB  1 
ATOM   3265 C CG  . ASN C  1 112 ? -45.996 34.144  25.591  1.00 33.39 ? 112 ASN C CG  1 
ATOM   3266 O OD1 . ASN C  1 112 ? -45.089 33.981  26.409  1.00 32.79 ? 112 ASN C OD1 1 
ATOM   3267 N ND2 . ASN C  1 112 ? -47.256 34.353  25.951  1.00 32.90 ? 112 ASN C ND2 1 
ATOM   3268 N N   . LEU C  1 113 ? -44.230 35.173  21.497  1.00 36.10 ? 113 LEU C N   1 
ATOM   3269 C CA  . LEU C  1 113 ? -43.893 35.100  20.079  1.00 36.78 ? 113 LEU C CA  1 
ATOM   3270 C C   . LEU C  1 113 ? -42.396 34.901  19.887  1.00 38.30 ? 113 LEU C C   1 
ATOM   3271 O O   . LEU C  1 113 ? -41.968 34.120  19.029  1.00 38.74 ? 113 LEU C O   1 
ATOM   3272 C CB  . LEU C  1 113 ? -44.355 36.365  19.360  1.00 37.17 ? 113 LEU C CB  1 
ATOM   3273 C CG  . LEU C  1 113 ? -43.827 36.525  17.936  1.00 37.82 ? 113 LEU C CG  1 
ATOM   3274 C CD1 . LEU C  1 113 ? -44.454 35.493  17.016  1.00 37.90 ? 113 LEU C CD1 1 
ATOM   3275 C CD2 . LEU C  1 113 ? -44.079 37.931  17.431  1.00 39.01 ? 113 LEU C CD2 1 
ATOM   3276 N N   . TYR C  1 114 ? -41.587 35.605  20.682  1.00 40.06 ? 114 TYR C N   1 
ATOM   3277 C CA  . TYR C  1 114 ? -40.142 35.421  20.635  1.00 41.22 ? 114 TYR C CA  1 
ATOM   3278 C C   . TYR C  1 114 ? -39.770 33.971  20.914  1.00 40.65 ? 114 TYR C C   1 
ATOM   3279 O O   . TYR C  1 114 ? -38.874 33.415  20.268  1.00 42.16 ? 114 TYR C O   1 
ATOM   3280 C CB  . TYR C  1 114 ? -39.477 36.365  21.638  1.00 41.79 ? 114 TYR C CB  1 
ATOM   3281 C CG  . TYR C  1 114 ? -37.979 36.208  21.786  1.00 42.73 ? 114 TYR C CG  1 
ATOM   3282 C CD1 . TYR C  1 114 ? -37.103 36.848  20.919  1.00 44.74 ? 114 TYR C CD1 1 
ATOM   3283 C CD2 . TYR C  1 114 ? -37.443 35.443  22.814  1.00 41.58 ? 114 TYR C CD2 1 
ATOM   3284 C CE1 . TYR C  1 114 ? -35.735 36.716  21.064  1.00 43.96 ? 114 TYR C CE1 1 
ATOM   3285 C CE2 . TYR C  1 114 ? -36.080 35.305  22.966  1.00 41.52 ? 114 TYR C CE2 1 
ATOM   3286 C CZ  . TYR C  1 114 ? -35.230 35.943  22.091  1.00 42.40 ? 114 TYR C CZ  1 
ATOM   3287 O OH  . TYR C  1 114 ? -33.871 35.800  22.249  1.00 42.80 ? 114 TYR C OH  1 
ATOM   3288 N N   . ASP C  1 115 ? -40.454 33.339  21.869  1.00 38.90 ? 115 ASP C N   1 
ATOM   3289 C CA  . ASP C  1 115 ? -40.205 31.927  22.138  1.00 38.68 ? 115 ASP C CA  1 
ATOM   3290 C C   . ASP C  1 115 ? -40.649 31.052  20.974  1.00 38.14 ? 115 ASP C C   1 
ATOM   3291 O O   . ASP C  1 115 ? -39.960 30.090  20.619  1.00 39.25 ? 115 ASP C O   1 
ATOM   3292 C CB  . ASP C  1 115 ? -40.905 31.505  23.427  1.00 37.98 ? 115 ASP C CB  1 
ATOM   3293 C CG  . ASP C  1 115 ? -40.318 32.181  24.649  1.00 38.22 ? 115 ASP C CG  1 
ATOM   3294 O OD1 . ASP C  1 115 ? -39.409 33.024  24.482  1.00 38.93 ? 115 ASP C OD1 1 
ATOM   3295 O OD2 . ASP C  1 115 ? -40.761 31.869  25.775  1.00 36.52 ? 115 ASP C OD2 1 
ATOM   3296 N N   . ARG C  1 116 ? -41.785 31.378  20.355  1.00 36.83 ? 116 ARG C N   1 
ATOM   3297 C CA  . ARG C  1 116 ? -42.284 30.569  19.249  1.00 38.63 ? 116 ARG C CA  1 
ATOM   3298 C C   . ARG C  1 116 ? -41.449 30.722  17.981  1.00 40.82 ? 116 ARG C C   1 
ATOM   3299 O O   . ARG C  1 116 ? -41.695 30.005  17.005  1.00 40.90 ? 116 ARG C O   1 
ATOM   3300 C CB  . ARG C  1 116 ? -43.749 30.909  18.965  1.00 37.73 ? 116 ARG C CB  1 
ATOM   3301 C CG  . ARG C  1 116 ? -44.714 30.351  20.006  1.00 36.60 ? 116 ARG C CG  1 
ATOM   3302 C CD  . ARG C  1 116 ? -46.163 30.463  19.551  1.00 36.55 ? 116 ARG C CD  1 
ATOM   3303 N NE  . ARG C  1 116 ? -47.085 29.885  20.523  1.00 33.94 ? 116 ARG C NE  1 
ATOM   3304 C CZ  . ARG C  1 116 ? -47.720 30.579  21.457  1.00 33.44 ? 116 ARG C CZ  1 
ATOM   3305 N NH1 . ARG C  1 116 ? -47.579 31.890  21.558  1.00 34.38 ? 116 ARG C NH1 1 
ATOM   3306 N NH2 . ARG C  1 116 ? -48.515 29.942  22.311  1.00 32.79 ? 116 ARG C NH2 1 
ATOM   3307 N N   . MET C  1 117 ? -40.485 31.640  17.961  1.00 40.93 ? 117 MET C N   1 
ATOM   3308 C CA  . MET C  1 117 ? -39.495 31.693  16.892  1.00 41.90 ? 117 MET C CA  1 
ATOM   3309 C C   . MET C  1 117 ? -38.178 31.064  17.330  1.00 43.14 ? 117 MET C C   1 
ATOM   3310 O O   . MET C  1 117 ? -37.699 30.111  16.707  1.00 45.11 ? 117 MET C O   1 
ATOM   3311 C CB  . MET C  1 117 ? -39.264 33.142  16.448  1.00 45.22 ? 117 MET C CB  1 
ATOM   3312 C CG  . MET C  1 117 ? -40.509 33.862  15.989  1.00 45.04 ? 117 MET C CG  1 
ATOM   3313 S SD  . MET C  1 117 ? -41.316 32.999  14.633  1.00 45.72 ? 117 MET C SD  1 
ATOM   3314 C CE  . MET C  1 117 ? -42.528 34.222  14.136  1.00 45.35 ? 117 MET C CE  1 
ATOM   3315 N N   . VAL C  1 118 ? -37.601 31.578  18.419  1.00 43.46 ? 118 VAL C N   1 
ATOM   3316 C CA  . VAL C  1 118 ? -36.269 31.157  18.854  1.00 44.67 ? 118 VAL C CA  1 
ATOM   3317 C C   . VAL C  1 118 ? -36.253 29.670  19.198  1.00 44.01 ? 118 VAL C C   1 
ATOM   3318 O O   . VAL C  1 118 ? -35.403 28.909  18.715  1.00 45.41 ? 118 VAL C O   1 
ATOM   3319 C CB  . VAL C  1 118 ? -35.805 32.022  20.042  1.00 43.78 ? 118 VAL C CB  1 
ATOM   3320 C CG1 . VAL C  1 118 ? -34.465 31.530  20.573  1.00 43.70 ? 118 VAL C CG1 1 
ATOM   3321 C CG2 . VAL C  1 118 ? -35.737 33.482  19.628  1.00 45.30 ? 118 VAL C CG2 1 
ATOM   3322 N N   . LEU C  1 119 ? -37.187 29.238  20.042  1.00 41.96 ? 119 LEU C N   1 
ATOM   3323 C CA  . LEU C  1 119 ? -37.228 27.880  20.567  1.00 41.19 ? 119 LEU C CA  1 
ATOM   3324 C C   . LEU C  1 119 ? -38.165 26.969  19.783  1.00 40.55 ? 119 LEU C C   1 
ATOM   3325 O O   . LEU C  1 119 ? -37.780 25.863  19.390  1.00 40.81 ? 119 LEU C O   1 
ATOM   3326 C CB  . LEU C  1 119 ? -37.666 27.898  22.037  1.00 39.63 ? 119 LEU C CB  1 
ATOM   3327 C CG  . LEU C  1 119 ? -37.353 29.141  22.862  1.00 38.90 ? 119 LEU C CG  1 
ATOM   3328 C CD1 . LEU C  1 119 ? -38.169 29.095  24.135  1.00 36.89 ? 119 LEU C CD1 1 
ATOM   3329 C CD2 . LEU C  1 119 ? -35.874 29.214  23.177  1.00 39.62 ? 119 LEU C CD2 1 
ATOM   3330 N N   . GLY C  1 120 ? -39.399 27.419  19.551  1.00 40.64 ? 120 GLY C N   1 
ATOM   3331 C CA  . GLY C  1 120 ? -40.464 26.600  18.999  1.00 39.40 ? 120 GLY C CA  1 
ATOM   3332 C C   . GLY C  1 120 ? -41.601 26.372  19.976  1.00 37.45 ? 120 GLY C C   1 
ATOM   3333 O O   . GLY C  1 120 ? -42.759 26.253  19.561  1.00 37.85 ? 120 GLY C O   1 
ATOM   3334 N N   . HIS C  1 121 ? -41.290 26.322  21.264  1.00 36.35 ? 121 HIS C N   1 
ATOM   3335 C CA  . HIS C  1 121 ? -42.263 26.187  22.335  1.00 35.43 ? 121 HIS C CA  1 
ATOM   3336 C C   . HIS C  1 121 ? -42.266 27.458  23.179  1.00 34.97 ? 121 HIS C C   1 
ATOM   3337 O O   . HIS C  1 121 ? -41.512 28.403  22.928  1.00 36.38 ? 121 HIS C O   1 
ATOM   3338 C CB  . HIS C  1 121 ? -41.941 24.956  23.182  1.00 35.01 ? 121 HIS C CB  1 
ATOM   3339 C CG  . HIS C  1 121 ? -40.485 24.822  23.501  1.00 36.24 ? 121 HIS C CG  1 
ATOM   3340 N ND1 . HIS C  1 121 ? -39.861 25.591  24.459  1.00 35.79 ? 121 HIS C ND1 1 
ATOM   3341 C CD2 . HIS C  1 121 ? -39.523 24.035  22.963  1.00 36.68 ? 121 HIS C CD2 1 
ATOM   3342 C CE1 . HIS C  1 121 ? -38.581 25.270  24.508  1.00 35.81 ? 121 HIS C CE1 1 
ATOM   3343 N NE2 . HIS C  1 121 ? -38.350 24.327  23.613  1.00 35.76 ? 121 HIS C NE2 1 
ATOM   3344 N N   . VAL C  1 122 ? -43.134 27.477  24.187  1.00 32.88 ? 122 VAL C N   1 
ATOM   3345 C CA  . VAL C  1 122 ? -43.251 28.591  25.120  1.00 31.74 ? 122 VAL C CA  1 
ATOM   3346 C C   . VAL C  1 122 ? -42.942 28.081  26.520  1.00 31.28 ? 122 VAL C C   1 
ATOM   3347 O O   . VAL C  1 122 ? -43.532 27.094  26.973  1.00 31.34 ? 122 VAL C O   1 
ATOM   3348 C CB  . VAL C  1 122 ? -44.646 29.235  25.068  1.00 31.06 ? 122 VAL C CB  1 
ATOM   3349 C CG1 . VAL C  1 122 ? -44.855 30.140  26.260  1.00 31.37 ? 122 VAL C CG1 1 
ATOM   3350 C CG2 . VAL C  1 122 ? -44.813 30.014  23.776  1.00 32.27 ? 122 VAL C CG2 1 
ATOM   3351 N N   . VAL C  1 123 ? -42.031 28.763  27.204  1.00 31.09 ? 123 VAL C N   1 
ATOM   3352 C CA  . VAL C  1 123 ? -41.508 28.307  28.486  1.00 29.74 ? 123 VAL C CA  1 
ATOM   3353 C C   . VAL C  1 123 ? -42.383 28.860  29.606  1.00 30.09 ? 123 VAL C C   1 
ATOM   3354 O O   . VAL C  1 123 ? -42.393 30.065  29.865  1.00 31.08 ? 123 VAL C O   1 
ATOM   3355 C CB  . VAL C  1 123 ? -40.044 28.724  28.657  1.00 30.57 ? 123 VAL C CB  1 
ATOM   3356 C CG1 . VAL C  1 123 ? -39.474 28.136  29.930  1.00 31.72 ? 123 VAL C CG1 1 
ATOM   3357 C CG2 . VAL C  1 123 ? -39.242 28.275  27.446  1.00 32.15 ? 123 VAL C CG2 1 
ATOM   3358 N N   . ASP C  1 124 ? -43.127 27.976  30.261  1.00 29.41 ? 124 ASP C N   1 
ATOM   3359 C CA  . ASP C  1 124 ? -43.945 28.314  31.416  1.00 29.63 ? 124 ASP C CA  1 
ATOM   3360 C C   . ASP C  1 124 ? -43.295 27.760  32.679  1.00 29.88 ? 124 ASP C C   1 
ATOM   3361 O O   . ASP C  1 124 ? -42.644 26.713  32.645  1.00 30.42 ? 124 ASP C O   1 
ATOM   3362 C CB  . ASP C  1 124 ? -45.359 27.748  31.275  1.00 30.12 ? 124 ASP C CB  1 
ATOM   3363 C CG  . ASP C  1 124 ? -45.985 28.038  29.921  1.00 30.87 ? 124 ASP C CG  1 
ATOM   3364 O OD1 . ASP C  1 124 ? -45.662 29.079  29.311  1.00 30.92 ? 124 ASP C OD1 1 
ATOM   3365 O OD2 . ASP C  1 124 ? -46.808 27.212  29.472  1.00 31.82 ? 124 ASP C OD2 1 
ATOM   3366 N N   . PHE C  1 125 ? -43.462 28.482  33.802  1.00 30.12 ? 125 PHE C N   1 
ATOM   3367 C CA  . PHE C  1 125 ? -42.831 28.066  35.052  1.00 30.10 ? 125 PHE C CA  1 
ATOM   3368 C C   . PHE C  1 125 ? -43.665 28.328  36.308  1.00 30.04 ? 125 PHE C C   1 
ATOM   3369 O O   . PHE C  1 125 ? -43.163 28.107  37.416  1.00 30.30 ? 125 PHE C O   1 
ATOM   3370 C CB  . PHE C  1 125 ? -41.453 28.735  35.194  1.00 29.91 ? 125 PHE C CB  1 
ATOM   3371 C CG  . PHE C  1 125 ? -41.484 30.233  35.069  1.00 30.39 ? 125 PHE C CG  1 
ATOM   3372 C CD1 . PHE C  1 125 ? -41.782 31.024  36.166  1.00 30.53 ? 125 PHE C CD1 1 
ATOM   3373 C CD2 . PHE C  1 125 ? -41.196 30.855  33.863  1.00 30.70 ? 125 PHE C CD2 1 
ATOM   3374 C CE1 . PHE C  1 125 ? -41.806 32.398  36.064  1.00 30.63 ? 125 PHE C CE1 1 
ATOM   3375 C CE2 . PHE C  1 125 ? -41.217 32.235  33.754  1.00 31.17 ? 125 PHE C CE2 1 
ATOM   3376 C CZ  . PHE C  1 125 ? -41.523 33.006  34.857  1.00 31.91 ? 125 PHE C CZ  1 
ATOM   3377 N N   . ILE C  1 126 ? -44.912 28.779  36.189  1.00 29.55 ? 126 ILE C N   1 
ATOM   3378 C CA  . ILE C  1 126 ? -45.753 29.096  37.341  1.00 29.17 ? 126 ILE C CA  1 
ATOM   3379 C C   . ILE C  1 126 ? -46.877 28.067  37.400  1.00 29.95 ? 126 ILE C C   1 
ATOM   3380 O O   . ILE C  1 126 ? -47.838 28.140  36.625  1.00 30.80 ? 126 ILE C O   1 
ATOM   3381 C CB  . ILE C  1 126 ? -46.313 30.525  37.268  1.00 29.49 ? 126 ILE C CB  1 
ATOM   3382 C CG1 . ILE C  1 126 ? -45.187 31.557  37.193  1.00 29.84 ? 126 ILE C CG1 1 
ATOM   3383 C CG2 . ILE C  1 126 ? -47.180 30.825  38.475  1.00 29.50 ? 126 ILE C CG2 1 
ATOM   3384 C CD1 . ILE C  1 126 ? -45.679 32.991  37.214  1.00 30.81 ? 126 ILE C CD1 1 
ATOM   3385 N N   . LEU C  1 127 ? -46.769 27.122  38.336  1.00 30.05 ? 127 LEU C N   1 
ATOM   3386 C CA  . LEU C  1 127 ? -47.757 26.064  38.542  1.00 30.46 ? 127 LEU C CA  1 
ATOM   3387 C C   . LEU C  1 127 ? -48.498 26.333  39.850  1.00 31.97 ? 127 LEU C C   1 
ATOM   3388 O O   . LEU C  1 127 ? -47.957 26.111  40.937  1.00 32.68 ? 127 LEU C O   1 
ATOM   3389 C CB  . LEU C  1 127 ? -47.089 24.690  38.564  1.00 29.53 ? 127 LEU C CB  1 
ATOM   3390 C CG  . LEU C  1 127 ? -47.990 23.477  38.823  1.00 31.06 ? 127 LEU C CG  1 
ATOM   3391 C CD1 . LEU C  1 127 ? -49.121 23.444  37.819  1.00 31.92 ? 127 LEU C CD1 1 
ATOM   3392 C CD2 . LEU C  1 127 ? -47.189 22.187  38.771  1.00 32.50 ? 127 LEU C CD2 1 
ATOM   3393 N N   . VAL C  1 128 ? -49.738 26.808  39.744  1.00 32.49 ? 128 VAL C N   1 
ATOM   3394 C CA  . VAL C  1 128 ? -50.630 26.955  40.889  1.00 32.60 ? 128 VAL C CA  1 
ATOM   3395 C C   . VAL C  1 128 ? -51.671 25.846  40.811  1.00 33.60 ? 128 VAL C C   1 
ATOM   3396 O O   . VAL C  1 128 ? -52.073 25.431  39.716  1.00 33.47 ? 128 VAL C O   1 
ATOM   3397 C CB  . VAL C  1 128 ? -51.289 28.349  40.948  1.00 30.91 ? 128 VAL C CB  1 
ATOM   3398 C CG1 . VAL C  1 128 ? -50.233 29.435  40.845  1.00 31.41 ? 128 VAL C CG1 1 
ATOM   3399 C CG2 . VAL C  1 128 ? -52.308 28.520  39.858  1.00 31.65 ? 128 VAL C CG2 1 
ATOM   3400 N N   . HIS C  1 129 ? -52.072 25.339  41.970  1.00 35.12 ? 129 HIS C N   1 
ATOM   3401 C CA  . HIS C  1 129 ? -52.926 24.160  42.036  1.00 36.85 ? 129 HIS C CA  1 
ATOM   3402 C C   . HIS C  1 129 ? -53.655 24.168  43.376  1.00 39.82 ? 129 HIS C C   1 
ATOM   3403 O O   . HIS C  1 129 ? -53.627 25.160  44.111  1.00 40.31 ? 129 HIS C O   1 
ATOM   3404 C CB  . HIS C  1 129 ? -52.095 22.887  41.843  1.00 37.17 ? 129 HIS C CB  1 
ATOM   3405 C CG  . HIS C  1 129 ? -51.127 22.622  42.956  1.00 37.15 ? 129 HIS C CG  1 
ATOM   3406 N ND1 . HIS C  1 129 ? -51.411 21.770  44.002  1.00 38.28 ? 129 HIS C ND1 1 
ATOM   3407 C CD2 . HIS C  1 129 ? -49.882 23.102  43.191  1.00 35.94 ? 129 HIS C CD2 1 
ATOM   3408 C CE1 . HIS C  1 129 ? -50.381 21.734  44.829  1.00 38.01 ? 129 HIS C CE1 1 
ATOM   3409 N NE2 . HIS C  1 129 ? -49.440 22.533  44.360  1.00 36.23 ? 129 HIS C NE2 1 
ATOM   3410 N N   . TRP C  1 130 ? -54.315 23.054  43.694  1.00 41.45 ? 130 TRP C N   1 
ATOM   3411 C CA  . TRP C  1 130 ? -54.948 22.862  45.001  1.00 43.02 ? 130 TRP C CA  1 
ATOM   3412 C C   . TRP C  1 130 ? -54.806 21.389  45.368  1.00 42.81 ? 130 TRP C C   1 
ATOM   3413 O O   . TRP C  1 130 ? -55.604 20.556  44.928  1.00 42.68 ? 130 TRP C O   1 
ATOM   3414 C CB  . TRP C  1 130 ? -56.408 23.298  44.992  1.00 44.03 ? 130 TRP C CB  1 
ATOM   3415 C CG  . TRP C  1 130 ? -57.100 23.122  46.314  1.00 46.36 ? 130 TRP C CG  1 
ATOM   3416 C CD1 . TRP C  1 130 ? -58.175 22.321  46.578  1.00 45.72 ? 130 TRP C CD1 1 
ATOM   3417 C CD2 . TRP C  1 130 ? -56.759 23.758  47.555  1.00 48.35 ? 130 TRP C CD2 1 
ATOM   3418 N NE1 . TRP C  1 130 ? -58.526 22.422  47.903  1.00 47.67 ? 130 TRP C NE1 1 
ATOM   3419 C CE2 . TRP C  1 130 ? -57.672 23.297  48.525  1.00 49.18 ? 130 TRP C CE2 1 
ATOM   3420 C CE3 . TRP C  1 130 ? -55.770 24.673  47.939  1.00 46.37 ? 130 TRP C CE3 1 
ATOM   3421 C CZ2 . TRP C  1 130 ? -57.627 23.719  49.857  1.00 49.96 ? 130 TRP C CZ2 1 
ATOM   3422 C CZ3 . TRP C  1 130 ? -55.726 25.090  49.261  1.00 46.03 ? 130 TRP C CZ3 1 
ATOM   3423 C CH2 . TRP C  1 130 ? -56.649 24.613  50.203  1.00 47.83 ? 130 TRP C CH2 1 
ATOM   3424 N N   . GLN C  1 131 ? -53.788 21.081  46.163  1.00 43.32 ? 131 GLN C N   1 
ATOM   3425 C CA  . GLN C  1 131 ? -53.513 19.716  46.639  1.00 45.24 ? 131 GLN C CA  1 
ATOM   3426 C C   . GLN C  1 131 ? -53.342 18.815  45.411  1.00 44.52 ? 131 GLN C C   1 
ATOM   3427 O O   . GLN C  1 131 ? -52.774 19.247  44.396  1.00 43.43 ? 131 GLN C O   1 
ATOM   3428 C CB  . GLN C  1 131 ? -54.607 19.286  47.599  1.00 46.67 ? 131 GLN C CB  1 
ATOM   3429 C CG  . GLN C  1 131 ? -54.866 20.264  48.734  1.00 47.13 ? 131 GLN C CG  1 
ATOM   3430 C CD  . GLN C  1 131 ? -56.068 19.873  49.567  1.00 47.96 ? 131 GLN C CD  1 
ATOM   3431 O OE1 . GLN C  1 131 ? -56.833 18.984  49.193  1.00 48.67 ? 131 GLN C OE1 1 
ATOM   3432 N NE2 . GLN C  1 131 ? -56.241 20.536  50.705  1.00 48.83 ? 131 GLN C NE2 1 
ATOM   3433 N N   . ASN C  1 132 ? -53.815 17.572  45.466  1.00 44.86 ? 132 ASN C N   1 
ATOM   3434 C CA  . ASN C  1 132 ? -53.807 16.664  44.323  1.00 43.52 ? 132 ASN C CA  1 
ATOM   3435 C C   . ASN C  1 132 ? -55.186 16.576  43.691  1.00 42.83 ? 132 ASN C C   1 
ATOM   3436 O O   . ASN C  1 132 ? -55.611 15.511  43.236  1.00 43.05 ? 132 ASN C O   1 
ATOM   3437 C CB  . ASN C  1 132 ? -53.313 15.287  44.751  1.00 44.93 ? 132 ASN C CB  1 
ATOM   3438 C CG  . ASN C  1 132 ? -52.030 15.358  45.557  1.00 46.14 ? 132 ASN C CG  1 
ATOM   3439 O OD1 . ASN C  1 132 ? -50.953 15.600  45.010  1.00 46.63 ? 132 ASN C OD1 1 
ATOM   3440 N ND2 . ASN C  1 132 ? -52.138 15.147  46.866  1.00 46.70 ? 132 ASN C ND2 1 
ATOM   3441 N N   . ARG C  1 133 ? -55.908 17.694  43.669  1.00 41.91 ? 133 ARG C N   1 
ATOM   3442 C CA  . ARG C  1 133 ? -57.282 17.745  43.187  1.00 40.98 ? 133 ARG C CA  1 
ATOM   3443 C C   . ARG C  1 133 ? -57.433 18.428  41.838  1.00 39.27 ? 133 ARG C C   1 
ATOM   3444 O O   . ARG C  1 133 ? -58.262 18.001  41.034  1.00 39.26 ? 133 ARG C O   1 
ATOM   3445 C CB  . ARG C  1 133 ? -58.171 18.464  44.207  1.00 42.92 ? 133 ARG C CB  1 
ATOM   3446 C CG  . ARG C  1 133 ? -58.169 17.840  45.596  1.00 44.72 ? 133 ARG C CG  1 
ATOM   3447 C CD  . ARG C  1 133 ? -58.966 16.549  45.626  1.00 47.11 ? 133 ARG C CD  1 
ATOM   3448 N NE  . ARG C  1 133 ? -59.451 16.244  46.967  1.00 48.75 ? 133 ARG C NE  1 
ATOM   3449 C CZ  . ARG C  1 133 ? -60.562 16.745  47.491  1.00 49.71 ? 133 ARG C CZ  1 
ATOM   3450 N NH1 . ARG C  1 133 ? -61.325 17.590  46.817  1.00 48.94 ? 133 ARG C NH1 1 
ATOM   3451 N NH2 . ARG C  1 133 ? -60.916 16.388  48.723  1.00 52.67 ? 133 ARG C NH2 1 
ATOM   3452 N N   . TRP C  1 134 ? -56.671 19.489  41.574  1.00 39.47 ? 134 TRP C N   1 
ATOM   3453 C CA  . TRP C  1 134 ? -56.717 20.152  40.276  1.00 39.26 ? 134 TRP C CA  1 
ATOM   3454 C C   . TRP C  1 134 ? -55.482 21.028  40.110  1.00 38.27 ? 134 TRP C C   1 
ATOM   3455 O O   . TRP C  1 134 ? -54.967 21.586  41.082  1.00 38.40 ? 134 TRP C O   1 
ATOM   3456 C CB  . TRP C  1 134 ? -57.996 20.989  40.111  1.00 39.54 ? 134 TRP C CB  1 
ATOM   3457 C CG  . TRP C  1 134 ? -58.020 22.289  40.877  1.00 38.71 ? 134 TRP C CG  1 
ATOM   3458 C CD1 . TRP C  1 134 ? -58.385 22.469  42.180  1.00 39.21 ? 134 TRP C CD1 1 
ATOM   3459 C CD2 . TRP C  1 134 ? -57.696 23.593  40.370  1.00 37.89 ? 134 TRP C CD2 1 
ATOM   3460 N NE1 . TRP C  1 134 ? -58.298 23.798  42.518  1.00 38.99 ? 134 TRP C NE1 1 
ATOM   3461 C CE2 . TRP C  1 134 ? -57.872 24.509  41.426  1.00 38.54 ? 134 TRP C CE2 1 
ATOM   3462 C CE3 . TRP C  1 134 ? -57.265 24.072  39.128  1.00 37.23 ? 134 TRP C CE3 1 
ATOM   3463 C CZ2 . TRP C  1 134 ? -57.633 25.877  41.279  1.00 37.71 ? 134 TRP C CZ2 1 
ATOM   3464 C CZ3 . TRP C  1 134 ? -57.027 25.432  38.984  1.00 36.78 ? 134 TRP C CZ3 1 
ATOM   3465 C CH2 . TRP C  1 134 ? -57.212 26.317  40.053  1.00 35.99 ? 134 TRP C CH2 1 
ATOM   3466 N N   . TYR C  1 135 ? -55.019 21.148  38.864  1.00 37.30 ? 135 TYR C N   1 
ATOM   3467 C CA  . TYR C  1 135 ? -53.838 21.937  38.535  1.00 36.11 ? 135 TYR C CA  1 
ATOM   3468 C C   . TYR C  1 135 ? -54.173 22.954  37.455  1.00 35.95 ? 135 TYR C C   1 
ATOM   3469 O O   . TYR C  1 135 ? -54.713 22.595  36.403  1.00 35.71 ? 135 TYR C O   1 
ATOM   3470 C CB  . TYR C  1 135 ? -52.689 21.043  38.063  1.00 35.69 ? 135 TYR C CB  1 
ATOM   3471 C CG  . TYR C  1 135 ? -52.007 20.283  39.174  1.00 37.75 ? 135 TYR C CG  1 
ATOM   3472 C CD1 . TYR C  1 135 ? -52.610 19.172  39.753  1.00 39.27 ? 135 TYR C CD1 1 
ATOM   3473 C CD2 . TYR C  1 135 ? -50.753 20.667  39.638  1.00 37.72 ? 135 TYR C CD2 1 
ATOM   3474 C CE1 . TYR C  1 135 ? -51.987 18.467  40.774  1.00 39.85 ? 135 TYR C CE1 1 
ATOM   3475 C CE2 . TYR C  1 135 ? -50.121 19.970  40.660  1.00 38.23 ? 135 TYR C CE2 1 
ATOM   3476 C CZ  . TYR C  1 135 ? -50.744 18.870  41.222  1.00 39.64 ? 135 TYR C CZ  1 
ATOM   3477 O OH  . TYR C  1 135 ? -50.127 18.169  42.234  1.00 40.10 ? 135 TYR C OH  1 
ATOM   3478 N N   . PHE C  1 136 ? -53.847 24.216  37.723  1.00 34.31 ? 136 PHE C N   1 
ATOM   3479 C CA  . PHE C  1 136 ? -53.900 25.290  36.738  1.00 32.62 ? 136 PHE C CA  1 
ATOM   3480 C C   . PHE C  1 136 ? -52.724 25.139  35.781  1.00 32.48 ? 136 PHE C C   1 
ATOM   3481 O O   . PHE C  1 136 ? -51.583 25.013  36.234  1.00 32.75 ? 136 PHE C O   1 
ATOM   3482 C CB  . PHE C  1 136 ? -53.823 26.632  37.447  1.00 32.46 ? 136 PHE C CB  1 
ATOM   3483 C CG  . PHE C  1 136 ? -54.434 27.781  36.696  1.00 33.50 ? 136 PHE C CG  1 
ATOM   3484 C CD1 . PHE C  1 136 ? -53.911 28.217  35.491  1.00 34.04 ? 136 PHE C CD1 1 
ATOM   3485 C CD2 . PHE C  1 136 ? -55.498 28.474  37.247  1.00 33.42 ? 136 PHE C CD2 1 
ATOM   3486 C CE1 . PHE C  1 136 ? -54.471 29.298  34.829  1.00 34.11 ? 136 PHE C CE1 1 
ATOM   3487 C CE2 . PHE C  1 136 ? -56.057 29.550  36.596  1.00 33.13 ? 136 PHE C CE2 1 
ATOM   3488 C CZ  . PHE C  1 136 ? -55.545 29.964  35.386  1.00 33.10 ? 136 PHE C CZ  1 
ATOM   3489 N N   . PRO C  1 137 ? -52.955 25.134  34.468  1.00 32.55 ? 137 PRO C N   1 
ATOM   3490 C CA  . PRO C  1 137 ? -51.840 24.959  33.528  1.00 31.80 ? 137 PRO C CA  1 
ATOM   3491 C C   . PRO C  1 137 ? -50.777 26.030  33.723  1.00 31.56 ? 137 PRO C C   1 
ATOM   3492 O O   . PRO C  1 137 ? -51.082 27.208  33.918  1.00 32.20 ? 137 PRO C O   1 
ATOM   3493 C CB  . PRO C  1 137 ? -52.514 25.065  32.154  1.00 32.13 ? 137 PRO C CB  1 
ATOM   3494 C CG  . PRO C  1 137 ? -53.817 25.745  32.407  1.00 33.14 ? 137 PRO C CG  1 
ATOM   3495 C CD  . PRO C  1 137 ? -54.239 25.309  33.772  1.00 33.10 ? 137 PRO C CD  1 
ATOM   3496 N N   . ALA C  1 138 ? -49.519 25.599  33.675  1.00 30.82 ? 138 ALA C N   1 
ATOM   3497 C CA  . ALA C  1 138 ? -48.406 26.479  34.002  1.00 30.36 ? 138 ALA C CA  1 
ATOM   3498 C C   . ALA C  1 138 ? -48.310 27.624  33.005  1.00 30.49 ? 138 ALA C C   1 
ATOM   3499 O O   . ALA C  1 138 ? -48.577 27.455  31.813  1.00 31.33 ? 138 ALA C O   1 
ATOM   3500 C CB  . ALA C  1 138 ? -47.095 25.691  34.031  1.00 30.22 ? 138 ALA C CB  1 
ATOM   3501 N N   . PHE C  1 139 ? -47.933 28.800  33.504  1.00 30.40 ? 139 PHE C N   1 
ATOM   3502 C CA  . PHE C  1 139 ? -47.795 29.988  32.669  1.00 30.86 ? 139 PHE C CA  1 
ATOM   3503 C C   . PHE C  1 139 ? -46.558 30.759  33.124  1.00 30.51 ? 139 PHE C C   1 
ATOM   3504 O O   . PHE C  1 139 ? -45.783 30.295  33.966  1.00 32.54 ? 139 PHE C O   1 
ATOM   3505 C CB  . PHE C  1 139 ? -49.075 30.836  32.704  1.00 31.79 ? 139 PHE C CB  1 
ATOM   3506 C CG  . PHE C  1 139 ? -49.504 31.254  34.083  1.00 31.60 ? 139 PHE C CG  1 
ATOM   3507 C CD1 . PHE C  1 139 ? -50.297 30.425  34.859  1.00 31.54 ? 139 PHE C CD1 1 
ATOM   3508 C CD2 . PHE C  1 139 ? -49.142 32.491  34.590  1.00 31.22 ? 139 PHE C CD2 1 
ATOM   3509 C CE1 . PHE C  1 139 ? -50.702 30.812  36.120  1.00 30.88 ? 139 PHE C CE1 1 
ATOM   3510 C CE2 . PHE C  1 139 ? -49.545 32.883  35.851  1.00 30.66 ? 139 PHE C CE2 1 
ATOM   3511 C CZ  . PHE C  1 139 ? -50.326 32.043  36.616  1.00 30.20 ? 139 PHE C CZ  1 
ATOM   3512 N N   . ASN C  1 140 ? -46.371 31.949  32.559  1.00 29.98 ? 140 ASN C N   1 
ATOM   3513 C CA  . ASN C  1 140 ? -45.157 32.723  32.786  1.00 30.44 ? 140 ASN C CA  1 
ATOM   3514 C C   . ASN C  1 140 ? -45.484 34.169  33.126  1.00 32.12 ? 140 ASN C C   1 
ATOM   3515 O O   . ASN C  1 140 ? -46.647 34.511  33.362  1.00 32.99 ? 140 ASN C O   1 
ATOM   3516 C CB  . ASN C  1 140 ? -44.267 32.668  31.547  1.00 31.15 ? 140 ASN C CB  1 
ATOM   3517 C CG  . ASN C  1 140 ? -45.050 32.884  30.273  1.00 31.29 ? 140 ASN C CG  1 
ATOM   3518 O OD1 . ASN C  1 140 ? -46.204 33.301  30.310  1.00 31.33 ? 140 ASN C OD1 1 
ATOM   3519 N ND2 . ASN C  1 140 ? -44.432 32.593  29.138  1.00 31.88 ? 140 ASN C ND2 1 
ATOM   3520 N N   . LEU C  1 141 ? -44.458 35.023  33.150  1.00 32.14 ? 141 LEU C N   1 
ATOM   3521 C CA  . LEU C  1 141 ? -44.687 36.449  33.354  1.00 32.38 ? 141 LEU C CA  1 
ATOM   3522 C C   . LEU C  1 141 ? -45.515 37.042  32.223  1.00 32.29 ? 141 LEU C C   1 
ATOM   3523 O O   . LEU C  1 141 ? -46.424 37.844  32.465  1.00 32.30 ? 141 LEU C O   1 
ATOM   3524 C CB  . LEU C  1 141 ? -43.354 37.183  33.470  1.00 33.32 ? 141 LEU C CB  1 
ATOM   3525 C CG  . LEU C  1 141 ? -42.479 36.858  34.678  1.00 35.24 ? 141 LEU C CG  1 
ATOM   3526 C CD1 . LEU C  1 141 ? -41.232 37.710  34.635  1.00 37.02 ? 141 LEU C CD1 1 
ATOM   3527 C CD2 . LEU C  1 141 ? -43.242 37.091  35.973  1.00 37.65 ? 141 LEU C CD2 1 
ATOM   3528 N N   . ALA C  1 142 ? -45.216 36.655  30.981  1.00 32.55 ? 142 ALA C N   1 
ATOM   3529 C CA  . ALA C  1 142 ? -45.906 37.234  29.833  1.00 33.33 ? 142 ALA C CA  1 
ATOM   3530 C C   . ALA C  1 142 ? -47.403 36.955  29.884  1.00 33.43 ? 142 ALA C C   1 
ATOM   3531 O O   . ALA C  1 142 ? -48.213 37.833  29.569  1.00 34.10 ? 142 ALA C O   1 
ATOM   3532 C CB  . ALA C  1 142 ? -45.301 36.702  28.534  1.00 32.94 ? 142 ALA C CB  1 
ATOM   3533 N N   . ASP C  1 143 ? -47.790 35.739  30.279  1.00 33.17 ? 143 ASP C N   1 
ATOM   3534 C CA  . ASP C  1 143 ? -49.209 35.415  30.379  1.00 33.50 ? 143 ASP C CA  1 
ATOM   3535 C C   . ASP C  1 143 ? -49.914 36.330  31.371  1.00 33.33 ? 143 ASP C C   1 
ATOM   3536 O O   . ASP C  1 143 ? -51.074 36.706  31.166  1.00 33.96 ? 143 ASP C O   1 
ATOM   3537 C CB  . ASP C  1 143 ? -49.392 33.949  30.777  1.00 33.63 ? 143 ASP C CB  1 
ATOM   3538 C CG  . ASP C  1 143 ? -49.119 32.998  29.629  1.00 32.93 ? 143 ASP C CG  1 
ATOM   3539 O OD1 . ASP C  1 143 ? -48.441 33.413  28.666  1.00 32.63 ? 143 ASP C OD1 1 
ATOM   3540 O OD2 . ASP C  1 143 ? -49.590 31.841  29.686  1.00 32.58 ? 143 ASP C OD2 1 
ATOM   3541 N N   . SER C  1 144 ? -49.228 36.697  32.453  1.00 33.25 ? 144 SER C N   1 
ATOM   3542 C CA  . SER C  1 144 ? -49.818 37.611  33.423  1.00 34.60 ? 144 SER C CA  1 
ATOM   3543 C C   . SER C  1 144 ? -50.099 38.979  32.804  1.00 36.29 ? 144 SER C C   1 
ATOM   3544 O O   . SER C  1 144 ? -51.171 39.558  33.020  1.00 35.94 ? 144 SER C O   1 
ATOM   3545 C CB  . SER C  1 144 ? -48.895 37.734  34.633  1.00 34.93 ? 144 SER C CB  1 
ATOM   3546 O OG  . SER C  1 144 ? -48.656 36.463  35.212  1.00 32.98 ? 144 SER C OG  1 
ATOM   3547 N N   . ALA C  1 145 ? -49.151 39.508  32.021  1.00 36.55 ? 145 ALA C N   1 
ATOM   3548 C CA  . ALA C  1 145 ? -49.355 40.807  31.385  1.00 35.71 ? 145 ALA C CA  1 
ATOM   3549 C C   . ALA C  1 145 ? -50.435 40.747  30.312  1.00 36.10 ? 145 ALA C C   1 
ATOM   3550 O O   . ALA C  1 145 ? -51.165 41.725  30.115  1.00 36.92 ? 145 ALA C O   1 
ATOM   3551 C CB  . ALA C  1 145 ? -48.042 41.320  30.792  1.00 35.74 ? 145 ALA C CB  1 
ATOM   3552 N N   . ILE C  1 146 ? -50.546 39.622  29.601  1.00 35.76 ? 146 ILE C N   1 
ATOM   3553 C CA  . ILE C  1 146 ? -51.622 39.470  28.627  1.00 35.67 ? 146 ILE C CA  1 
ATOM   3554 C C   . ILE C  1 146 ? -52.972 39.408  29.328  1.00 36.06 ? 146 ILE C C   1 
ATOM   3555 O O   . ILE C  1 146 ? -53.959 39.982  28.854  1.00 36.67 ? 146 ILE C O   1 
ATOM   3556 C CB  . ILE C  1 146 ? -51.386 38.227  27.752  1.00 35.16 ? 146 ILE C CB  1 
ATOM   3557 C CG1 . ILE C  1 146 ? -50.020 38.308  27.077  1.00 34.83 ? 146 ILE C CG1 1 
ATOM   3558 C CG2 . ILE C  1 146 ? -52.489 38.098  26.706  1.00 35.80 ? 146 ILE C CG2 1 
ATOM   3559 C CD1 . ILE C  1 146 ? -49.626 37.045  26.365  1.00 34.17 ? 146 ILE C CD1 1 
ATOM   3560 N N   . THR C  1 147 ? -53.045 38.699  30.455  1.00 36.71 ? 147 THR C N   1 
ATOM   3561 C CA  . THR C  1 147 ? -54.306 38.603  31.181  1.00 36.00 ? 147 THR C CA  1 
ATOM   3562 C C   . THR C  1 147 ? -54.688 39.941  31.800  1.00 37.33 ? 147 THR C C   1 
ATOM   3563 O O   . THR C  1 147 ? -55.811 40.423  31.610  1.00 38.82 ? 147 THR C O   1 
ATOM   3564 C CB  . THR C  1 147 ? -54.210 37.520  32.252  1.00 34.79 ? 147 THR C CB  1 
ATOM   3565 O OG1 . THR C  1 147 ? -53.972 36.257  31.623  1.00 35.08 ? 147 THR C OG1 1 
ATOM   3566 C CG2 . THR C  1 147 ? -55.496 37.441  33.045  1.00 33.54 ? 147 THR C CG2 1 
ATOM   3567 N N   . VAL C  1 148 ? -53.755 40.571  32.521  1.00 36.60 ? 148 VAL C N   1 
ATOM   3568 C CA  . VAL C  1 148 ? -54.064 41.826  33.205  1.00 36.79 ? 148 VAL C CA  1 
ATOM   3569 C C   . VAL C  1 148 ? -54.392 42.924  32.200  1.00 37.83 ? 148 VAL C C   1 
ATOM   3570 O O   . VAL C  1 148 ? -55.327 43.708  32.401  1.00 38.59 ? 148 VAL C O   1 
ATOM   3571 C CB  . VAL C  1 148 ? -52.904 42.230  34.133  1.00 36.10 ? 148 VAL C CB  1 
ATOM   3572 C CG1 . VAL C  1 148 ? -53.161 43.602  34.736  1.00 36.65 ? 148 VAL C CG1 1 
ATOM   3573 C CG2 . VAL C  1 148 ? -52.729 41.199  35.229  1.00 35.64 ? 148 VAL C CG2 1 
ATOM   3574 N N   . GLY C  1 149 ? -53.627 43.000  31.107  1.00 37.95 ? 149 GLY C N   1 
ATOM   3575 C CA  . GLY C  1 149 ? -53.942 43.956  30.057  1.00 38.12 ? 149 GLY C CA  1 
ATOM   3576 C C   . GLY C  1 149 ? -55.311 43.718  29.447  1.00 39.45 ? 149 GLY C C   1 
ATOM   3577 O O   . GLY C  1 149 ? -56.026 44.665  29.108  1.00 40.81 ? 149 GLY C O   1 
ATOM   3578 N N   . ALA C  1 150 ? -55.689 42.447  29.285  1.00 38.68 ? 150 ALA C N   1 
ATOM   3579 C CA  . ALA C  1 150 ? -57.047 42.133  28.861  1.00 39.05 ? 150 ALA C CA  1 
ATOM   3580 C C   . ALA C  1 150 ? -58.062 42.465  29.949  1.00 39.51 ? 150 ALA C C   1 
ATOM   3581 O O   . ALA C  1 150 ? -59.206 42.815  29.637  1.00 40.08 ? 150 ALA C O   1 
ATOM   3582 C CB  . ALA C  1 150 ? -57.151 40.660  28.469  1.00 39.51 ? 150 ALA C CB  1 
ATOM   3583 N N   . VAL C  1 151 ? -57.672 42.356  31.222  1.00 38.63 ? 151 VAL C N   1 
ATOM   3584 C CA  . VAL C  1 151 ? -58.590 42.686  32.310  1.00 39.52 ? 151 VAL C CA  1 
ATOM   3585 C C   . VAL C  1 151 ? -58.877 44.183  32.335  1.00 42.03 ? 151 VAL C C   1 
ATOM   3586 O O   . VAL C  1 151 ? -60.031 44.605  32.471  1.00 43.76 ? 151 VAL C O   1 
ATOM   3587 C CB  . VAL C  1 151 ? -58.033 42.197  33.658  1.00 38.93 ? 151 VAL C CB  1 
ATOM   3588 C CG1 . VAL C  1 151 ? -58.775 42.871  34.806  1.00 41.00 ? 151 VAL C CG1 1 
ATOM   3589 C CG2 . VAL C  1 151 ? -58.161 40.687  33.772  1.00 37.60 ? 151 VAL C CG2 1 
ATOM   3590 N N   . MET C  1 152 ? -57.830 45.007  32.213  1.00 41.81 ? 152 MET C N   1 
ATOM   3591 C CA  . MET C  1 152 ? -58.015 46.455  32.204  1.00 42.55 ? 152 MET C CA  1 
ATOM   3592 C C   . MET C  1 152 ? -58.743 46.923  30.951  1.00 42.73 ? 152 MET C C   1 
ATOM   3593 O O   . MET C  1 152 ? -59.465 47.925  30.994  1.00 44.35 ? 152 MET C O   1 
ATOM   3594 C CB  . MET C  1 152 ? -56.664 47.159  32.323  1.00 42.35 ? 152 MET C CB  1 
ATOM   3595 C CG  . MET C  1 152 ? -55.864 46.780  33.554  1.00 42.08 ? 152 MET C CG  1 
ATOM   3596 S SD  . MET C  1 152 ? -54.140 47.292  33.438  1.00 41.12 ? 152 MET C SD  1 
ATOM   3597 C CE  . MET C  1 152 ? -54.307 49.073  33.360  1.00 44.19 ? 152 MET C CE  1 
ATOM   3598 N N   . LEU C  1 153 ? -58.553 46.227  29.828  1.00 41.65 ? 153 LEU C N   1 
ATOM   3599 C CA  . LEU C  1 153 ? -59.324 46.537  28.628  1.00 42.39 ? 153 LEU C CA  1 
ATOM   3600 C C   . LEU C  1 153 ? -60.816 46.351  28.876  1.00 44.52 ? 153 LEU C C   1 
ATOM   3601 O O   . LEU C  1 153 ? -61.641 47.125  28.376  1.00 45.11 ? 153 LEU C O   1 
ATOM   3602 C CB  . LEU C  1 153 ? -58.859 45.656  27.469  1.00 42.19 ? 153 LEU C CB  1 
ATOM   3603 C CG  . LEU C  1 153 ? -58.637 46.348  26.125  1.00 43.51 ? 153 LEU C CG  1 
ATOM   3604 C CD1 . LEU C  1 153 ? -57.551 47.400  26.255  1.00 44.49 ? 153 LEU C CD1 1 
ATOM   3605 C CD2 . LEU C  1 153 ? -58.276 45.330  25.053  1.00 42.82 ? 153 LEU C CD2 1 
ATOM   3606 N N   . ALA C  1 154 ? -61.180 45.320  29.643  1.00 45.09 ? 154 ALA C N   1 
ATOM   3607 C CA  . ALA C  1 154 ? -62.566 45.113  30.040  1.00 44.64 ? 154 ALA C CA  1 
ATOM   3608 C C   . ALA C  1 154 ? -62.999 46.044  31.165  1.00 46.23 ? 154 ALA C C   1 
ATOM   3609 O O   . ALA C  1 154 ? -64.204 46.228  31.365  1.00 48.05 ? 154 ALA C O   1 
ATOM   3610 C CB  . ALA C  1 154 ? -62.782 43.658  30.461  1.00 43.08 ? 154 ALA C CB  1 
ATOM   3611 N N   . LEU C  1 155 ? -62.053 46.635  31.896  1.00 46.25 ? 155 LEU C N   1 
ATOM   3612 C CA  . LEU C  1 155 ? -62.353 47.563  32.978  1.00 47.58 ? 155 LEU C CA  1 
ATOM   3613 C C   . LEU C  1 155 ? -62.485 48.999  32.494  1.00 49.53 ? 155 LEU C C   1 
ATOM   3614 O O   . LEU C  1 155 ? -62.659 49.906  33.315  1.00 51.16 ? 155 LEU C O   1 
ATOM   3615 C CB  . LEU C  1 155 ? -61.276 47.481  34.063  1.00 46.77 ? 155 LEU C CB  1 
ATOM   3616 C CG  . LEU C  1 155 ? -61.256 46.202  34.900  1.00 46.54 ? 155 LEU C CG  1 
ATOM   3617 C CD1 . LEU C  1 155 ? -60.035 46.187  35.805  1.00 45.89 ? 155 LEU C CD1 1 
ATOM   3618 C CD2 . LEU C  1 155 ? -62.535 46.070  35.711  1.00 47.84 ? 155 LEU C CD2 1 
ATOM   3619 N N   . ASP C  1 156 ? -62.405 49.225  31.182  1.00 49.60 ? 156 ASP C N   1 
ATOM   3620 C CA  . ASP C  1 156 ? -62.577 50.547  30.597  1.00 50.75 ? 156 ASP C CA  1 
ATOM   3621 C C   . ASP C  1 156 ? -64.039 50.861  30.296  1.00 52.68 ? 156 ASP C C   1 
ATOM   3622 O O   . ASP C  1 156 ? -64.331 51.703  29.435  1.00 52.95 ? 156 ASP C O   1 
ATOM   3623 C CB  . ASP C  1 156 ? -61.729 50.667  29.332  1.00 49.64 ? 156 ASP C CB  1 
ATOM   3624 C CG  . ASP C  1 156 ? -60.895 51.928  29.311  1.00 50.00 ? 156 ASP C CG  1 
ATOM   3625 O OD1 . ASP C  1 156 ? -61.479 53.027  29.413  1.00 51.33 ? 156 ASP C OD1 1 
ATOM   3626 O OD2 . ASP C  1 156 ? -59.655 51.817  29.212  1.00 49.31 ? 156 ASP C OD2 1 
ATOM   3627 N N   . MET C  1 157 ? -64.968 50.197  30.984  1.00 53.90 ? 157 MET C N   1 
ATOM   3628 C CA  . MET C  1 157 ? -66.390 50.441  30.813  1.00 55.61 ? 157 MET C CA  1 
ATOM   3629 C C   . MET C  1 157 ? -67.021 51.179  31.983  1.00 56.56 ? 157 MET C C   1 
ATOM   3630 O O   . MET C  1 157 ? -68.210 51.507  31.911  1.00 57.89 ? 157 MET C O   1 
ATOM   3631 C CB  . MET C  1 157 ? -67.139 49.117  30.610  1.00 55.78 ? 157 MET C CB  1 
ATOM   3632 C CG  . MET C  1 157 ? -66.614 48.270  29.472  1.00 54.97 ? 157 MET C CG  1 
ATOM   3633 S SD  . MET C  1 157 ? -67.647 46.822  29.191  1.00 56.84 ? 157 MET C SD  1 
ATOM   3634 C CE  . MET C  1 157 ? -69.238 47.601  28.918  1.00 51.07 ? 157 MET C CE  1 
ATOM   3635 N N   . PHE C  1 158 ? -66.268 51.455  33.051  1.00 56.08 ? 158 PHE C N   1 
ATOM   3636 C CA  . PHE C  1 158 ? -66.834 52.027  34.267  1.00 57.92 ? 158 PHE C CA  1 
ATOM   3637 C C   . PHE C  1 158 ? -66.722 53.548  34.301  1.00 57.93 ? 158 PHE C C   1 
ATOM   3638 O O   . PHE C  1 158 ? -66.607 54.141  35.385  1.00 58.96 ? 158 PHE C O   1 
ATOM   3639 C CB  . PHE C  1 158 ? -66.170 51.413  35.502  1.00 59.33 ? 158 PHE C CB  1 
ATOM   3640 C CG  . PHE C  1 158 ? -66.452 49.938  35.690  1.00 58.80 ? 158 PHE C CG  1 
ATOM   3641 C CD1 . PHE C  1 158 ? -67.196 49.223  34.759  1.00 57.22 ? 158 PHE C CD1 1 
ATOM   3642 C CD2 . PHE C  1 158 ? -65.975 49.271  36.811  1.00 57.97 ? 158 PHE C CD2 1 
ATOM   3643 C CE1 . PHE C  1 158 ? -67.445 47.876  34.936  1.00 56.45 ? 158 PHE C CE1 1 
ATOM   3644 C CE2 . PHE C  1 158 ? -66.226 47.924  36.993  1.00 55.87 ? 158 PHE C CE2 1 
ATOM   3645 C CZ  . PHE C  1 158 ? -66.960 47.228  36.056  1.00 55.67 ? 158 PHE C CZ  1 
ATOM   3646 N N   . ARG C  1 159 ? -66.748 54.194  33.139  1.00 56.06 ? 159 ARG C N   1 
ATOM   3647 C CA  . ARG C  1 159 ? -66.674 55.642  33.056  1.00 54.22 ? 159 ARG C CA  1 
ATOM   3648 C C   . ARG C  1 159 ? -68.052 56.243  32.791  1.00 53.63 ? 159 ARG C C   1 
ATOM   3649 O O   . ARG C  1 159 ? -68.211 57.463  32.752  1.00 53.34 ? 159 ARG C O   1 
ATOM   3650 C CB  . ARG C  1 159 ? -65.697 56.054  31.959  1.00 51.84 ? 159 ARG C CB  1 
ATOM   3651 C CG  . ARG C  1 159 ? -64.334 55.393  32.070  1.00 50.91 ? 159 ARG C CG  1 
ATOM   3652 C CD  . ARG C  1 159 ? -63.760 55.119  30.694  1.00 51.42 ? 159 ARG C CD  1 
ATOM   3653 N NE  . ARG C  1 159 ? -63.518 56.344  29.940  1.00 53.61 ? 159 ARG C NE  1 
ATOM   3654 C CZ  . ARG C  1 159 ? -63.446 56.406  28.617  1.00 54.24 ? 159 ARG C CZ  1 
ATOM   3655 N NH1 . ARG C  1 159 ? -63.636 55.334  27.864  1.00 53.07 ? 159 ARG C NH1 1 
ATOM   3656 N NH2 . ARG C  1 159 ? -63.186 57.573  28.034  1.00 54.58 ? 159 ARG C NH2 1 
ATOM   3657 N N   . PRO D  1 11  ? -76.785 56.866  15.773  1.00 45.53 ? 11  PRO D N   1 
ATOM   3658 C CA  . PRO D  1 11  ? -77.426 56.861  14.455  1.00 45.40 ? 11  PRO D CA  1 
ATOM   3659 C C   . PRO D  1 11  ? -77.094 55.605  13.665  1.00 46.23 ? 11  PRO D C   1 
ATOM   3660 O O   . PRO D  1 11  ? -77.968 55.021  13.028  1.00 45.34 ? 11  PRO D O   1 
ATOM   3661 C CB  . PRO D  1 11  ? -76.845 58.104  13.776  1.00 47.19 ? 11  PRO D CB  1 
ATOM   3662 C CG  . PRO D  1 11  ? -75.519 58.302  14.425  1.00 48.08 ? 11  PRO D CG  1 
ATOM   3663 C CD  . PRO D  1 11  ? -75.677 57.835  15.848  1.00 47.97 ? 11  PRO D CD  1 
ATOM   3664 N N   . TRP D  1 12  ? -75.827 55.191  13.720  1.00 49.08 ? 12  TRP D N   1 
ATOM   3665 C CA  . TRP D  1 12  ? -75.388 54.007  12.992  1.00 48.91 ? 12  TRP D CA  1 
ATOM   3666 C C   . TRP D  1 12  ? -75.919 52.714  13.594  1.00 46.00 ? 12  TRP D C   1 
ATOM   3667 O O   . TRP D  1 12  ? -75.820 51.665  12.948  1.00 44.39 ? 12  TRP D O   1 
ATOM   3668 C CB  . TRP D  1 12  ? -73.860 53.968  12.930  1.00 49.29 ? 12  TRP D CB  1 
ATOM   3669 C CG  . TRP D  1 12  ? -73.271 55.228  12.373  1.00 50.94 ? 12  TRP D CG  1 
ATOM   3670 C CD1 . TRP D  1 12  ? -72.549 56.167  13.052  1.00 51.68 ? 12  TRP D CD1 1 
ATOM   3671 C CD2 . TRP D  1 12  ? -73.379 55.702  11.025  1.00 51.53 ? 12  TRP D CD2 1 
ATOM   3672 N NE1 . TRP D  1 12  ? -72.190 57.189  12.206  1.00 52.76 ? 12  TRP D NE1 1 
ATOM   3673 C CE2 . TRP D  1 12  ? -72.688 56.928  10.957  1.00 52.24 ? 12  TRP D CE2 1 
ATOM   3674 C CE3 . TRP D  1 12  ? -73.988 55.205  9.868   1.00 51.50 ? 12  TRP D CE3 1 
ATOM   3675 C CZ2 . TRP D  1 12  ? -72.590 57.665  9.779   1.00 53.27 ? 12  TRP D CZ2 1 
ATOM   3676 C CZ3 . TRP D  1 12  ? -73.888 55.938  8.699   1.00 51.95 ? 12  TRP D CZ3 1 
ATOM   3677 C CH2 . TRP D  1 12  ? -73.195 57.154  8.663   1.00 52.94 ? 12  TRP D CH2 1 
ATOM   3678 N N   . LEU D  1 13  ? -76.479 52.759  14.806  1.00 45.83 ? 13  LEU D N   1 
ATOM   3679 C CA  . LEU D  1 13  ? -77.040 51.558  15.411  1.00 44.18 ? 13  LEU D CA  1 
ATOM   3680 C C   . LEU D  1 13  ? -78.265 51.044  14.668  1.00 42.09 ? 13  LEU D C   1 
ATOM   3681 O O   . LEU D  1 13  ? -78.683 49.907  14.916  1.00 41.41 ? 13  LEU D O   1 
ATOM   3682 C CB  . LEU D  1 13  ? -77.386 51.815  16.878  1.00 44.43 ? 13  LEU D CB  1 
ATOM   3683 C CG  . LEU D  1 13  ? -76.201 52.115  17.798  1.00 42.99 ? 13  LEU D CG  1 
ATOM   3684 C CD1 . LEU D  1 13  ? -76.662 52.128  19.242  1.00 42.08 ? 13  LEU D CD1 1 
ATOM   3685 C CD2 . LEU D  1 13  ? -75.078 51.105  17.592  1.00 41.70 ? 13  LEU D CD2 1 
ATOM   3686 N N   . TRP D  1 14  ? -78.857 51.847  13.778  1.00 41.83 ? 14  TRP D N   1 
ATOM   3687 C CA  . TRP D  1 14  ? -79.929 51.329  12.936  1.00 40.48 ? 14  TRP D CA  1 
ATOM   3688 C C   . TRP D  1 14  ? -79.420 50.236  12.005  1.00 40.90 ? 14  TRP D C   1 
ATOM   3689 O O   . TRP D  1 14  ? -80.193 49.362  11.595  1.00 41.23 ? 14  TRP D O   1 
ATOM   3690 C CB  . TRP D  1 14  ? -80.585 52.456  12.129  1.00 39.83 ? 14  TRP D CB  1 
ATOM   3691 C CG  . TRP D  1 14  ? -81.707 53.190  12.844  1.00 38.49 ? 14  TRP D CG  1 
ATOM   3692 C CD1 . TRP D  1 14  ? -81.875 54.543  12.928  1.00 38.05 ? 14  TRP D CD1 1 
ATOM   3693 C CD2 . TRP D  1 14  ? -82.808 52.608  13.564  1.00 37.33 ? 14  TRP D CD2 1 
ATOM   3694 N NE1 . TRP D  1 14  ? -83.006 54.839  13.652  1.00 36.08 ? 14  TRP D NE1 1 
ATOM   3695 C CE2 . TRP D  1 14  ? -83.596 53.670  14.054  1.00 35.33 ? 14  TRP D CE2 1 
ATOM   3696 C CE3 . TRP D  1 14  ? -83.204 51.294  13.841  1.00 37.66 ? 14  TRP D CE3 1 
ATOM   3697 C CZ2 . TRP D  1 14  ? -84.751 53.459  14.806  1.00 34.22 ? 14  TRP D CZ2 1 
ATOM   3698 C CZ3 . TRP D  1 14  ? -84.353 51.089  14.590  1.00 35.30 ? 14  TRP D CZ3 1 
ATOM   3699 C CH2 . TRP D  1 14  ? -85.111 52.165  15.062  1.00 33.35 ? 14  TRP D CH2 1 
ATOM   3700 N N   . ILE D  1 15  ? -78.131 50.270  11.653  1.00 41.23 ? 15  ILE D N   1 
ATOM   3701 C CA  . ILE D  1 15  ? -77.537 49.156  10.918  1.00 41.33 ? 15  ILE D CA  1 
ATOM   3702 C C   . ILE D  1 15  ? -77.531 47.903  11.781  1.00 40.12 ? 15  ILE D C   1 
ATOM   3703 O O   . ILE D  1 15  ? -77.814 46.797  11.304  1.00 39.80 ? 15  ILE D O   1 
ATOM   3704 C CB  . ILE D  1 15  ? -76.115 49.509  10.447  1.00 41.12 ? 15  ILE D CB  1 
ATOM   3705 C CG1 . ILE D  1 15  ? -76.088 50.885  9.782   1.00 42.90 ? 15  ILE D CG1 1 
ATOM   3706 C CG2 . ILE D  1 15  ? -75.587 48.435  9.497   1.00 38.32 ? 15  ILE D CG2 1 
ATOM   3707 C CD1 . ILE D  1 15  ? -74.691 51.373  9.474   1.00 44.33 ? 15  ILE D CD1 1 
ATOM   3708 N N   . THR D  1 16  ? -77.182 48.055  13.060  1.00 39.76 ? 16  THR D N   1 
ATOM   3709 C CA  . THR D  1 16  ? -77.181 46.917  13.972  1.00 38.62 ? 16  THR D CA  1 
ATOM   3710 C C   . THR D  1 16  ? -78.578 46.323  14.113  1.00 38.36 ? 16  THR D C   1 
ATOM   3711 O O   . THR D  1 16  ? -78.747 45.098  14.059  1.00 37.33 ? 16  THR D O   1 
ATOM   3712 C CB  . THR D  1 16  ? -76.635 47.349  15.336  1.00 38.04 ? 16  THR D CB  1 
ATOM   3713 O OG1 . THR D  1 16  ? -75.220 47.551  15.244  1.00 37.60 ? 16  THR D OG1 1 
ATOM   3714 C CG2 . THR D  1 16  ? -76.926 46.307  16.399  1.00 37.31 ? 16  THR D CG2 1 
ATOM   3715 N N   . VAL D  1 17  ? -79.593 47.178  14.278  1.00 38.98 ? 17  VAL D N   1 
ATOM   3716 C CA  . VAL D  1 17  ? -80.955 46.690  14.488  1.00 38.51 ? 17  VAL D CA  1 
ATOM   3717 C C   . VAL D  1 17  ? -81.472 45.977  13.244  1.00 38.00 ? 17  VAL D C   1 
ATOM   3718 O O   . VAL D  1 17  ? -82.121 44.927  13.339  1.00 37.44 ? 17  VAL D O   1 
ATOM   3719 C CB  . VAL D  1 17  ? -81.882 47.846  14.911  1.00 36.54 ? 17  VAL D CB  1 
ATOM   3720 C CG1 . VAL D  1 17  ? -83.325 47.372  15.004  1.00 33.77 ? 17  VAL D CG1 1 
ATOM   3721 C CG2 . VAL D  1 17  ? -81.426 48.429  16.243  1.00 36.18 ? 17  VAL D CG2 1 
ATOM   3722 N N   . LEU D  1 18  ? -81.185 46.524  12.060  1.00 38.33 ? 18  LEU D N   1 
ATOM   3723 C CA  . LEU D  1 18  ? -81.663 45.912  10.824  1.00 37.61 ? 18  LEU D CA  1 
ATOM   3724 C C   . LEU D  1 18  ? -81.007 44.559  10.571  1.00 37.49 ? 18  LEU D C   1 
ATOM   3725 O O   . LEU D  1 18  ? -81.679 43.610  10.150  1.00 37.34 ? 18  LEU D O   1 
ATOM   3726 C CB  . LEU D  1 18  ? -81.426 46.858  9.650   1.00 38.56 ? 18  LEU D CB  1 
ATOM   3727 C CG  . LEU D  1 18  ? -82.487 47.953  9.549   1.00 40.12 ? 18  LEU D CG  1 
ATOM   3728 C CD1 . LEU D  1 18  ? -82.036 49.070  8.622   1.00 42.82 ? 18  LEU D CD1 1 
ATOM   3729 C CD2 . LEU D  1 18  ? -83.795 47.345  9.069   1.00 42.15 ? 18  LEU D CD2 1 
ATOM   3730 N N   . VAL D  1 19  ? -79.698 44.450  10.820  1.00 37.64 ? 19  VAL D N   1 
ATOM   3731 C CA  . VAL D  1 19  ? -79.000 43.181  10.617  1.00 37.63 ? 19  VAL D CA  1 
ATOM   3732 C C   . VAL D  1 19  ? -79.539 42.114  11.562  1.00 35.35 ? 19  VAL D C   1 
ATOM   3733 O O   . VAL D  1 19  ? -79.766 40.965  11.163  1.00 33.99 ? 19  VAL D O   1 
ATOM   3734 C CB  . VAL D  1 19  ? -77.481 43.372  10.784  1.00 38.37 ? 19  VAL D CB  1 
ATOM   3735 C CG1 . VAL D  1 19  ? -76.773 42.019  10.861  1.00 37.15 ? 19  VAL D CG1 1 
ATOM   3736 C CG2 . VAL D  1 19  ? -76.922 44.213  9.643   1.00 38.20 ? 19  VAL D CG2 1 
ATOM   3737 N N   . PHE D  1 20  ? -79.755 42.476  12.827  1.00 35.12 ? 20  PHE D N   1 
ATOM   3738 C CA  . PHE D  1 20  ? -80.295 41.527  13.792  1.00 33.62 ? 20  PHE D CA  1 
ATOM   3739 C C   . PHE D  1 20  ? -81.669 41.031  13.364  1.00 32.92 ? 20  PHE D C   1 
ATOM   3740 O O   . PHE D  1 20  ? -81.944 39.827  13.389  1.00 32.70 ? 20  PHE D O   1 
ATOM   3741 C CB  . PHE D  1 20  ? -80.360 42.183  15.172  1.00 34.14 ? 20  PHE D CB  1 
ATOM   3742 C CG  . PHE D  1 20  ? -81.044 41.348  16.217  1.00 32.48 ? 20  PHE D CG  1 
ATOM   3743 C CD1 . PHE D  1 20  ? -80.360 40.338  16.870  1.00 32.08 ? 20  PHE D CD1 1 
ATOM   3744 C CD2 . PHE D  1 20  ? -82.366 41.582  16.558  1.00 32.52 ? 20  PHE D CD2 1 
ATOM   3745 C CE1 . PHE D  1 20  ? -80.982 39.572  17.832  1.00 31.79 ? 20  PHE D CE1 1 
ATOM   3746 C CE2 . PHE D  1 20  ? -82.992 40.818  17.520  1.00 32.85 ? 20  PHE D CE2 1 
ATOM   3747 C CZ  . PHE D  1 20  ? -82.299 39.812  18.158  1.00 31.99 ? 20  PHE D CZ  1 
ATOM   3748 N N   . VAL D  1 21  ? -82.542 41.948  12.953  1.00 33.50 ? 21  VAL D N   1 
ATOM   3749 C CA  . VAL D  1 21  ? -83.911 41.578  12.609  1.00 32.63 ? 21  VAL D CA  1 
ATOM   3750 C C   . VAL D  1 21  ? -83.944 40.753  11.329  1.00 33.32 ? 21  VAL D C   1 
ATOM   3751 O O   . VAL D  1 21  ? -84.604 39.709  11.266  1.00 33.25 ? 21  VAL D O   1 
ATOM   3752 C CB  . VAL D  1 21  ? -84.787 42.835  12.492  1.00 31.97 ? 21  VAL D CB  1 
ATOM   3753 C CG1 . VAL D  1 21  ? -86.057 42.519  11.721  1.00 31.37 ? 21  VAL D CG1 1 
ATOM   3754 C CG2 . VAL D  1 21  ? -85.121 43.369  13.871  1.00 31.10 ? 21  VAL D CG2 1 
ATOM   3755 N N   . LEU D  1 22  ? -83.246 41.214  10.286  1.00 34.09 ? 22  LEU D N   1 
ATOM   3756 C CA  . LEU D  1 22  ? -83.250 40.492  9.016   1.00 33.69 ? 22  LEU D CA  1 
ATOM   3757 C C   . LEU D  1 22  ? -82.686 39.090  9.170   1.00 32.97 ? 22  LEU D C   1 
ATOM   3758 O O   . LEU D  1 22  ? -83.147 38.154  8.506   1.00 32.09 ? 22  LEU D O   1 
ATOM   3759 C CB  . LEU D  1 22  ? -82.452 41.263  7.967   1.00 36.04 ? 22  LEU D CB  1 
ATOM   3760 C CG  . LEU D  1 22  ? -83.174 42.413  7.268   1.00 39.61 ? 22  LEU D CG  1 
ATOM   3761 C CD1 . LEU D  1 22  ? -82.173 43.318  6.566   1.00 41.30 ? 22  LEU D CD1 1 
ATOM   3762 C CD2 . LEU D  1 22  ? -84.192 41.871  6.275   1.00 41.13 ? 22  LEU D CD2 1 
ATOM   3763 N N   . ASP D  1 23  ? -81.689 38.928  10.037  1.00 33.22 ? 23  ASP D N   1 
ATOM   3764 C CA  . ASP D  1 23  ? -81.140 37.603  10.292  1.00 32.86 ? 23  ASP D CA  1 
ATOM   3765 C C   . ASP D  1 23  ? -82.145 36.714  11.015  1.00 32.74 ? 23  ASP D C   1 
ATOM   3766 O O   . ASP D  1 23  ? -82.324 35.547  10.647  1.00 33.31 ? 23  ASP D O   1 
ATOM   3767 C CB  . ASP D  1 23  ? -79.851 37.729  11.099  1.00 33.26 ? 23  ASP D CB  1 
ATOM   3768 C CG  . ASP D  1 23  ? -79.442 36.430  11.731  1.00 33.57 ? 23  ASP D CG  1 
ATOM   3769 O OD1 . ASP D  1 23  ? -79.043 35.513  10.984  1.00 33.84 ? 23  ASP D OD1 1 
ATOM   3770 O OD2 . ASP D  1 23  ? -79.521 36.330  12.974  1.00 32.71 ? 23  ASP D OD2 1 
ATOM   3771 N N   . GLN D  1 24  ? -82.816 37.249  12.041  1.00 32.31 ? 24  GLN D N   1 
ATOM   3772 C CA  . GLN D  1 24  ? -83.786 36.454  12.792  1.00 32.32 ? 24  GLN D CA  1 
ATOM   3773 C C   . GLN D  1 24  ? -84.970 36.046  11.924  1.00 32.93 ? 24  GLN D C   1 
ATOM   3774 O O   . GLN D  1 24  ? -85.490 34.931  12.061  1.00 33.44 ? 24  GLN D O   1 
ATOM   3775 C CB  . GLN D  1 24  ? -84.266 37.225  14.020  1.00 31.94 ? 24  GLN D CB  1 
ATOM   3776 C CG  . GLN D  1 24  ? -83.175 37.496  15.034  1.00 32.51 ? 24  GLN D CG  1 
ATOM   3777 C CD  . GLN D  1 24  ? -82.529 36.229  15.556  1.00 32.90 ? 24  GLN D CD  1 
ATOM   3778 O OE1 . GLN D  1 24  ? -83.139 35.159  15.557  1.00 33.30 ? 24  GLN D OE1 1 
ATOM   3779 N NE2 . GLN D  1 24  ? -81.285 36.345  16.005  1.00 32.49 ? 24  GLN D NE2 1 
ATOM   3780 N N   . VAL D  1 25  ? -85.424 36.941  11.044  1.00 32.68 ? 25  VAL D N   1 
ATOM   3781 C CA  . VAL D  1 25  ? -86.472 36.580  10.091  1.00 32.09 ? 25  VAL D CA  1 
ATOM   3782 C C   . VAL D  1 25  ? -85.968 35.516  9.124   1.00 32.51 ? 25  VAL D C   1 
ATOM   3783 O O   . VAL D  1 25  ? -86.696 34.578  8.775   1.00 33.26 ? 25  VAL D O   1 
ATOM   3784 C CB  . VAL D  1 25  ? -86.980 37.826  9.343   1.00 31.48 ? 25  VAL D CB  1 
ATOM   3785 C CG1 . VAL D  1 25  ? -87.984 37.422  8.279   1.00 32.23 ? 25  VAL D CG1 1 
ATOM   3786 C CG2 . VAL D  1 25  ? -87.605 38.809  10.317  1.00 31.69 ? 25  VAL D CG2 1 
ATOM   3787 N N   . SER D  1 26  ? -84.720 35.648  8.667   1.00 32.37 ? 26  SER D N   1 
ATOM   3788 C CA  . SER D  1 26  ? -84.141 34.651  7.771   1.00 32.69 ? 26  SER D CA  1 
ATOM   3789 C C   . SER D  1 26  ? -84.070 33.285  8.441   1.00 33.51 ? 26  SER D C   1 
ATOM   3790 O O   . SER D  1 26  ? -84.483 32.273  7.863   1.00 33.71 ? 26  SER D O   1 
ATOM   3791 C CB  . SER D  1 26  ? -82.749 35.094  7.325   1.00 32.85 ? 26  SER D CB  1 
ATOM   3792 O OG  . SER D  1 26  ? -82.790 36.350  6.678   1.00 35.94 ? 26  SER D OG  1 
ATOM   3793 N N   . LYS D  1 27  ? -83.546 33.239  9.668   1.00 33.78 ? 27  LYS D N   1 
ATOM   3794 C CA  . LYS D  1 27  ? -83.447 31.972  10.385  1.00 34.24 ? 27  LYS D CA  1 
ATOM   3795 C C   . LYS D  1 27  ? -84.822 31.361  10.616  1.00 35.30 ? 27  LYS D C   1 
ATOM   3796 O O   . LYS D  1 27  ? -85.018 30.157  10.411  1.00 37.14 ? 27  LYS D O   1 
ATOM   3797 C CB  . LYS D  1 27  ? -82.727 32.177  11.719  1.00 33.87 ? 27  LYS D CB  1 
ATOM   3798 C CG  . LYS D  1 27  ? -81.254 32.517  11.600  1.00 33.84 ? 27  LYS D CG  1 
ATOM   3799 C CD  . LYS D  1 27  ? -80.687 32.866  12.962  1.00 33.21 ? 27  LYS D CD  1 
ATOM   3800 C CE  . LYS D  1 27  ? -79.173 32.934  12.936  1.00 33.29 ? 27  LYS D CE  1 
ATOM   3801 N NZ  . LYS D  1 27  ? -78.616 33.311  14.267  1.00 33.46 ? 27  LYS D NZ  1 
ATOM   3802 N N   . ALA D  1 28  ? -85.792 32.177  11.033  1.00 34.61 ? 28  ALA D N   1 
ATOM   3803 C CA  . ALA D  1 28  ? -87.119 31.649  11.323  1.00 34.38 ? 28  ALA D CA  1 
ATOM   3804 C C   . ALA D  1 28  ? -87.844 31.209  10.058  1.00 34.68 ? 28  ALA D C   1 
ATOM   3805 O O   . ALA D  1 28  ? -88.718 30.339  10.123  1.00 35.09 ? 28  ALA D O   1 
ATOM   3806 C CB  . ALA D  1 28  ? -87.944 32.690  12.078  1.00 34.46 ? 28  ALA D CB  1 
ATOM   3807 N N   . PHE D  1 29  ? -87.508 31.798  8.906   1.00 34.57 ? 29  PHE D N   1 
ATOM   3808 C CA  . PHE D  1 29  ? -88.153 31.399  7.658   1.00 35.43 ? 29  PHE D CA  1 
ATOM   3809 C C   . PHE D  1 29  ? -87.656 30.040  7.180   1.00 36.50 ? 29  PHE D C   1 
ATOM   3810 O O   . PHE D  1 29  ? -88.450 29.208  6.724   1.00 37.75 ? 29  PHE D O   1 
ATOM   3811 C CB  . PHE D  1 29  ? -87.929 32.458  6.580   1.00 35.85 ? 29  PHE D CB  1 
ATOM   3812 C CG  . PHE D  1 29  ? -88.188 31.961  5.187   1.00 36.61 ? 29  PHE D CG  1 
ATOM   3813 C CD1 . PHE D  1 29  ? -89.482 31.776  4.731   1.00 37.41 ? 29  PHE D CD1 1 
ATOM   3814 C CD2 . PHE D  1 29  ? -87.135 31.673  4.335   1.00 38.39 ? 29  PHE D CD2 1 
ATOM   3815 C CE1 . PHE D  1 29  ? -89.720 31.312  3.449   1.00 39.92 ? 29  PHE D CE1 1 
ATOM   3816 C CE2 . PHE D  1 29  ? -87.366 31.210  3.053   1.00 40.21 ? 29  PHE D CE2 1 
ATOM   3817 C CZ  . PHE D  1 29  ? -88.660 31.028  2.609   1.00 41.31 ? 29  PHE D CZ  1 
ATOM   3818 N N   . PHE D  1 30  ? -86.346 29.802  7.258   1.00 35.99 ? 30  PHE D N   1 
ATOM   3819 C CA  . PHE D  1 30  ? -85.806 28.513  6.838   1.00 35.68 ? 30  PHE D CA  1 
ATOM   3820 C C   . PHE D  1 30  ? -86.053 27.424  7.874   1.00 36.13 ? 30  PHE D C   1 
ATOM   3821 O O   . PHE D  1 30  ? -86.158 26.246  7.513   1.00 36.34 ? 30  PHE D O   1 
ATOM   3822 C CB  . PHE D  1 30  ? -84.313 28.635  6.537   1.00 34.33 ? 30  PHE D CB  1 
ATOM   3823 C CG  . PHE D  1 30  ? -84.020 29.330  5.239   1.00 34.82 ? 30  PHE D CG  1 
ATOM   3824 C CD1 . PHE D  1 30  ? -84.181 28.673  4.030   1.00 34.32 ? 30  PHE D CD1 1 
ATOM   3825 C CD2 . PHE D  1 30  ? -83.586 30.645  5.229   1.00 35.72 ? 30  PHE D CD2 1 
ATOM   3826 C CE1 . PHE D  1 30  ? -83.917 29.317  2.836   1.00 35.77 ? 30  PHE D CE1 1 
ATOM   3827 C CE2 . PHE D  1 30  ? -83.320 31.292  4.040   1.00 35.59 ? 30  PHE D CE2 1 
ATOM   3828 C CZ  . PHE D  1 30  ? -83.486 30.628  2.844   1.00 36.86 ? 30  PHE D CZ  1 
ATOM   3829 N N   . GLN D  1 31  ? -86.145 27.789  9.155   1.00 36.19 ? 31  GLN D N   1 
ATOM   3830 C CA  . GLN D  1 31  ? -86.472 26.802  10.178  1.00 36.47 ? 31  GLN D CA  1 
ATOM   3831 C C   . GLN D  1 31  ? -87.886 26.264  10.011  1.00 37.97 ? 31  GLN D C   1 
ATOM   3832 O O   . GLN D  1 31  ? -88.134 25.086  10.291  1.00 40.03 ? 31  GLN D O   1 
ATOM   3833 C CB  . GLN D  1 31  ? -86.304 27.406  11.571  1.00 36.03 ? 31  GLN D CB  1 
ATOM   3834 C CG  . GLN D  1 31  ? -85.042 26.971  12.293  1.00 36.74 ? 31  GLN D CG  1 
ATOM   3835 C CD  . GLN D  1 31  ? -85.011 27.446  13.731  1.00 37.96 ? 31  GLN D CD  1 
ATOM   3836 O OE1 . GLN D  1 31  ? -85.590 28.478  14.069  1.00 38.00 ? 31  GLN D OE1 1 
ATOM   3837 N NE2 . GLN D  1 31  ? -84.341 26.687  14.590  1.00 39.13 ? 31  GLN D NE2 1 
ATOM   3838 N N   . ALA D  1 32  ? -88.822 27.103  9.564   1.00 38.16 ? 32  ALA D N   1 
ATOM   3839 C CA  . ALA D  1 32  ? -90.217 26.694  9.440   1.00 38.46 ? 32  ALA D CA  1 
ATOM   3840 C C   . ALA D  1 32  ? -90.553 26.091  8.080   1.00 38.82 ? 32  ALA D C   1 
ATOM   3841 O O   . ALA D  1 32  ? -91.462 25.257  7.994   1.00 39.48 ? 32  ALA D O   1 
ATOM   3842 C CB  . ALA D  1 32  ? -91.139 27.885  9.713   1.00 38.57 ? 32  ALA D CB  1 
ATOM   3843 N N   . GLU D  1 33  ? -89.850 26.492  7.018   1.00 38.66 ? 33  GLU D N   1 
ATOM   3844 C CA  . GLU D  1 33  ? -90.108 25.958  5.685   1.00 38.62 ? 33  GLU D CA  1 
ATOM   3845 C C   . GLU D  1 33  ? -89.368 24.649  5.424   1.00 38.63 ? 33  GLU D C   1 
ATOM   3846 O O   . GLU D  1 33  ? -89.928 23.737  4.808   1.00 39.11 ? 33  GLU D O   1 
ATOM   3847 C CB  . GLU D  1 33  ? -89.726 26.989  4.618   1.00 39.22 ? 33  GLU D CB  1 
ATOM   3848 C CG  . GLU D  1 33  ? -90.394 26.779  3.263   1.00 41.45 ? 33  GLU D CG  1 
ATOM   3849 C CD  . GLU D  1 33  ? -91.821 27.309  3.214   1.00 43.55 ? 33  GLU D CD  1 
ATOM   3850 O OE1 . GLU D  1 33  ? -92.389 27.619  4.284   1.00 43.15 ? 33  GLU D OE1 1 
ATOM   3851 O OE2 . GLU D  1 33  ? -92.373 27.424  2.098   1.00 44.74 ? 33  GLU D OE2 1 
ATOM   3852 N N   . LEU D  1 34  ? -88.124 24.533  5.880   1.00 37.91 ? 34  LEU D N   1 
ATOM   3853 C CA  . LEU D  1 34  ? -87.316 23.349  5.641   1.00 36.48 ? 34  LEU D CA  1 
ATOM   3854 C C   . LEU D  1 34  ? -87.412 22.368  6.810   1.00 35.94 ? 34  LEU D C   1 
ATOM   3855 O O   . LEU D  1 34  ? -88.119 22.586  7.797   1.00 36.44 ? 34  LEU D O   1 
ATOM   3856 C CB  . LEU D  1 34  ? -85.857 23.740  5.407   1.00 37.00 ? 34  LEU D CB  1 
ATOM   3857 C CG  . LEU D  1 34  ? -85.287 23.725  3.991   1.00 35.39 ? 34  LEU D CG  1 
ATOM   3858 C CD1 . LEU D  1 34  ? -86.032 24.708  3.120   1.00 36.39 ? 34  LEU D CD1 1 
ATOM   3859 C CD2 . LEU D  1 34  ? -83.805 24.058  4.039   1.00 33.90 ? 34  LEU D CD2 1 
ATOM   3860 N N   . SER D  1 35  ? -86.683 21.264  6.680   1.00 35.99 ? 35  SER D N   1 
ATOM   3861 C CA  . SER D  1 35  ? -86.451 20.305  7.749   1.00 36.04 ? 35  SER D CA  1 
ATOM   3862 C C   . SER D  1 35  ? -84.948 20.149  7.940   1.00 36.94 ? 35  SER D C   1 
ATOM   3863 O O   . SER D  1 35  ? -84.165 20.397  7.018   1.00 37.73 ? 35  SER D O   1 
ATOM   3864 C CB  . SER D  1 35  ? -87.099 18.953  7.436   1.00 33.86 ? 35  SER D CB  1 
ATOM   3865 O OG  . SER D  1 35  ? -86.977 18.642  6.061   1.00 33.67 ? 35  SER D OG  1 
ATOM   3866 N N   . MET D  1 36  ? -84.548 19.765  9.150   1.00 36.39 ? 36  MET D N   1 
ATOM   3867 C CA  . MET D  1 36  ? -83.132 19.778  9.494   1.00 38.09 ? 36  MET D CA  1 
ATOM   3868 C C   . MET D  1 36  ? -82.344 18.868  8.563   1.00 39.66 ? 36  MET D C   1 
ATOM   3869 O O   . MET D  1 36  ? -82.742 17.729  8.306   1.00 40.40 ? 36  MET D O   1 
ATOM   3870 C CB  . MET D  1 36  ? -82.928 19.343  10.942  1.00 39.82 ? 36  MET D CB  1 
ATOM   3871 C CG  . MET D  1 36  ? -81.534 19.641  11.476  1.00 43.58 ? 36  MET D CG  1 
ATOM   3872 S SD  . MET D  1 36  ? -80.991 18.462  12.732  1.00 55.27 ? 36  MET D SD  1 
ATOM   3873 C CE  . MET D  1 36  ? -79.381 19.131  13.168  1.00 50.98 ? 36  MET D CE  1 
ATOM   3874 N N   . TYR D  1 37  ? -81.231 19.388  8.046   1.00 39.81 ? 37  TYR D N   1 
ATOM   3875 C CA  . TYR D  1 37  ? -80.315 18.728  7.119   1.00 40.30 ? 37  TYR D CA  1 
ATOM   3876 C C   . TYR D  1 37  ? -80.883 18.579  5.710   1.00 38.47 ? 37  TYR D C   1 
ATOM   3877 O O   . TYR D  1 37  ? -80.223 17.973  4.854   1.00 38.41 ? 37  TYR D O   1 
ATOM   3878 C CB  . TYR D  1 37  ? -79.862 17.346  7.616   1.00 41.74 ? 37  TYR D CB  1 
ATOM   3879 C CG  . TYR D  1 37  ? -78.871 17.393  8.757   1.00 44.70 ? 37  TYR D CG  1 
ATOM   3880 C CD1 . TYR D  1 37  ? -78.349 18.604  9.206   1.00 45.89 ? 37  TYR D CD1 1 
ATOM   3881 C CD2 . TYR D  1 37  ? -78.443 16.224  9.376   1.00 46.75 ? 37  TYR D CD2 1 
ATOM   3882 C CE1 . TYR D  1 37  ? -77.436 18.647  10.246  1.00 48.82 ? 37  TYR D CE1 1 
ATOM   3883 C CE2 . TYR D  1 37  ? -77.528 16.258  10.417  1.00 49.72 ? 37  TYR D CE2 1 
ATOM   3884 C CZ  . TYR D  1 37  ? -77.032 17.468  10.846  1.00 51.25 ? 37  TYR D CZ  1 
ATOM   3885 O OH  . TYR D  1 37  ? -76.125 17.501  11.877  1.00 52.99 ? 37  TYR D OH  1 
ATOM   3886 N N   . GLN D  1 38  ? -82.071 19.107  5.436   1.00 36.74 ? 38  GLN D N   1 
ATOM   3887 C CA  . GLN D  1 38  ? -82.629 19.061  4.095   1.00 36.04 ? 38  GLN D CA  1 
ATOM   3888 C C   . GLN D  1 38  ? -82.031 20.180  3.249   1.00 36.26 ? 38  GLN D C   1 
ATOM   3889 O O   . GLN D  1 38  ? -81.603 21.215  3.767   1.00 36.64 ? 38  GLN D O   1 
ATOM   3890 C CB  . GLN D  1 38  ? -84.154 19.184  4.153   1.00 35.18 ? 38  GLN D CB  1 
ATOM   3891 C CG  . GLN D  1 38  ? -84.857 19.084  2.812   1.00 34.31 ? 38  GLN D CG  1 
ATOM   3892 C CD  . GLN D  1 38  ? -86.067 19.988  2.727   1.00 34.49 ? 38  GLN D CD  1 
ATOM   3893 O OE1 . GLN D  1 38  ? -86.273 20.675  1.728   1.00 35.65 ? 38  GLN D OE1 1 
ATOM   3894 N NE2 . GLN D  1 38  ? -86.874 19.997  3.780   1.00 34.59 ? 38  GLN D NE2 1 
ATOM   3895 N N   . GLN D  1 39  ? -81.992 19.959  1.935   1.00 36.35 ? 39  GLN D N   1 
ATOM   3896 C CA  . GLN D  1 39  ? -81.394 20.901  0.995   1.00 35.98 ? 39  GLN D CA  1 
ATOM   3897 C C   . GLN D  1 39  ? -82.408 21.322  -0.062  1.00 35.92 ? 39  GLN D C   1 
ATOM   3898 O O   . GLN D  1 39  ? -83.121 20.478  -0.613  1.00 35.88 ? 39  GLN D O   1 
ATOM   3899 C CB  . GLN D  1 39  ? -80.158 20.291  0.324   1.00 35.81 ? 39  GLN D CB  1 
ATOM   3900 C CG  . GLN D  1 39  ? -79.202 19.635  1.306   1.00 35.73 ? 39  GLN D CG  1 
ATOM   3901 C CD  . GLN D  1 39  ? -77.827 19.396  0.723   1.00 35.81 ? 39  GLN D CD  1 
ATOM   3902 O OE1 . GLN D  1 39  ? -77.588 19.631  -0.462  1.00 34.89 ? 39  GLN D OE1 1 
ATOM   3903 N NE2 . GLN D  1 39  ? -76.908 18.936  1.562   1.00 35.93 ? 39  GLN D NE2 1 
ATOM   3904 N N   . ILE D  1 40  ? -82.466 22.622  -0.345  1.00 35.74 ? 40  ILE D N   1 
ATOM   3905 C CA  . ILE D  1 40  ? -83.193 23.154  -1.496  1.00 36.72 ? 40  ILE D CA  1 
ATOM   3906 C C   . ILE D  1 40  ? -82.167 23.775  -2.433  1.00 36.93 ? 40  ILE D C   1 
ATOM   3907 O O   . ILE D  1 40  ? -81.616 24.845  -2.147  1.00 37.43 ? 40  ILE D O   1 
ATOM   3908 C CB  . ILE D  1 40  ? -84.268 24.176  -1.097  1.00 37.41 ? 40  ILE D CB  1 
ATOM   3909 C CG1 . ILE D  1 40  ? -85.454 23.480  -0.429  1.00 38.59 ? 40  ILE D CG1 1 
ATOM   3910 C CG2 . ILE D  1 40  ? -84.747 24.948  -2.321  1.00 40.19 ? 40  ILE D CG2 1 
ATOM   3911 C CD1 . ILE D  1 40  ? -86.711 24.322  -0.385  1.00 42.24 ? 40  ILE D CD1 1 
ATOM   3912 N N   . VAL D  1 41  ? -81.930 23.118  -3.567  1.00 36.42 ? 41  VAL D N   1 
ATOM   3913 C CA  . VAL D  1 41  ? -80.841 23.506  -4.454  1.00 36.19 ? 41  VAL D CA  1 
ATOM   3914 C C   . VAL D  1 41  ? -81.181 24.795  -5.190  1.00 36.03 ? 41  VAL D C   1 
ATOM   3915 O O   . VAL D  1 41  ? -82.321 25.009  -5.615  1.00 38.75 ? 41  VAL D O   1 
ATOM   3916 C CB  . VAL D  1 41  ? -80.539 22.362  -5.434  1.00 35.20 ? 41  VAL D CB  1 
ATOM   3917 C CG1 . VAL D  1 41  ? -79.250 22.630  -6.178  1.00 36.04 ? 41  VAL D CG1 1 
ATOM   3918 C CG2 . VAL D  1 41  ? -80.469 21.042  -4.687  1.00 33.79 ? 41  VAL D CG2 1 
ATOM   3919 N N   . VAL D  1 42  ? -80.184 25.666  -5.339  1.00 34.27 ? 42  VAL D N   1 
ATOM   3920 C CA  . VAL D  1 42  ? -80.293 26.869  -6.162  1.00 35.72 ? 42  VAL D CA  1 
ATOM   3921 C C   . VAL D  1 42  ? -79.377 26.785  -7.382  1.00 36.86 ? 42  VAL D C   1 
ATOM   3922 O O   . VAL D  1 42  ? -79.841 26.838  -8.523  1.00 37.81 ? 42  VAL D O   1 
ATOM   3923 C CB  . VAL D  1 42  ? -80.007 28.142  -5.334  1.00 36.77 ? 42  VAL D CB  1 
ATOM   3924 C CG1 . VAL D  1 42  ? -80.068 29.373  -6.222  1.00 37.44 ? 42  VAL D CG1 1 
ATOM   3925 C CG2 . VAL D  1 42  ? -80.999 28.260  -4.198  1.00 39.01 ? 42  VAL D CG2 1 
ATOM   3926 N N   . ILE D  1 43  ? -78.073 26.674  -7.159  1.00 35.93 ? 43  ILE D N   1 
ATOM   3927 C CA  . ILE D  1 43  ? -77.112 26.392  -8.220  1.00 34.44 ? 43  ILE D CA  1 
ATOM   3928 C C   . ILE D  1 43  ? -76.525 25.013  -7.941  1.00 35.23 ? 43  ILE D C   1 
ATOM   3929 O O   . ILE D  1 43  ? -75.836 24.833  -6.926  1.00 36.59 ? 43  ILE D O   1 
ATOM   3930 C CB  . ILE D  1 43  ? -76.012 27.456  -8.296  1.00 34.03 ? 43  ILE D CB  1 
ATOM   3931 C CG1 . ILE D  1 43  ? -76.619 28.842  -8.503  1.00 35.40 ? 43  ILE D CG1 1 
ATOM   3932 C CG2 . ILE D  1 43  ? -75.049 27.121  -9.410  1.00 34.60 ? 43  ILE D CG2 1 
ATOM   3933 C CD1 . ILE D  1 43  ? -75.689 29.981  -8.139  1.00 37.77 ? 43  ILE D CD1 1 
ATOM   3934 N N   . PRO D  1 44  ? -76.762 24.017  -8.798  1.00 34.80 ? 44  PRO D N   1 
ATOM   3935 C CA  . PRO D  1 44  ? -76.353 22.647  -8.451  1.00 34.89 ? 44  PRO D CA  1 
ATOM   3936 C C   . PRO D  1 44  ? -74.873 22.512  -8.141  1.00 35.99 ? 44  PRO D C   1 
ATOM   3937 O O   . PRO D  1 44  ? -74.501 21.706  -7.278  1.00 36.43 ? 44  PRO D O   1 
ATOM   3938 C CB  . PRO D  1 44  ? -76.755 21.841  -9.694  1.00 34.57 ? 44  PRO D CB  1 
ATOM   3939 C CG  . PRO D  1 44  ? -77.824 22.655  -10.347 1.00 35.21 ? 44  PRO D CG  1 
ATOM   3940 C CD  . PRO D  1 44  ? -77.445 24.082  -10.099 1.00 36.15 ? 44  PRO D CD  1 
ATOM   3941 N N   . ASP D  1 45  ? -74.012 23.284  -8.809  1.00 35.29 ? 45  ASP D N   1 
ATOM   3942 C CA  . ASP D  1 45  ? -72.578 23.113  -8.605  1.00 34.96 ? 45  ASP D CA  1 
ATOM   3943 C C   . ASP D  1 45  ? -72.133 23.618  -7.236  1.00 34.70 ? 45  ASP D C   1 
ATOM   3944 O O   . ASP D  1 45  ? -71.312 22.970  -6.575  1.00 35.07 ? 45  ASP D O   1 
ATOM   3945 C CB  . ASP D  1 45  ? -71.797 23.815  -9.718  1.00 36.41 ? 45  ASP D CB  1 
ATOM   3946 C CG  . ASP D  1 45  ? -71.671 22.966  -10.974 1.00 36.03 ? 45  ASP D CG  1 
ATOM   3947 O OD1 . ASP D  1 45  ? -71.418 21.749  -10.850 1.00 36.56 ? 45  ASP D OD1 1 
ATOM   3948 O OD2 . ASP D  1 45  ? -71.824 23.516  -12.087 1.00 35.68 ? 45  ASP D OD2 1 
ATOM   3949 N N   . LEU D  1 46  ? -72.645 24.770  -6.789  1.00 34.62 ? 46  LEU D N   1 
ATOM   3950 C CA  . LEU D  1 46  ? -72.012 25.424  -5.644  1.00 34.80 ? 46  LEU D CA  1 
ATOM   3951 C C   . LEU D  1 46  ? -72.933 25.965  -4.550  1.00 33.57 ? 46  LEU D C   1 
ATOM   3952 O O   . LEU D  1 46  ? -72.461 26.103  -3.418  1.00 33.23 ? 46  LEU D O   1 
ATOM   3953 C CB  . LEU D  1 46  ? -71.111 26.564  -6.138  1.00 34.43 ? 46  LEU D CB  1 
ATOM   3954 C CG  . LEU D  1 46  ? -71.532 27.339  -7.381  1.00 33.48 ? 46  LEU D CG  1 
ATOM   3955 C CD1 . LEU D  1 46  ? -72.602 28.329  -7.020  1.00 35.41 ? 46  LEU D CD1 1 
ATOM   3956 C CD2 . LEU D  1 46  ? -70.346 28.034  -8.002  1.00 35.24 ? 46  LEU D CD2 1 
ATOM   3957 N N   . PHE D  1 47  ? -74.213 26.254  -4.794  1.00 33.04 ? 47  PHE D N   1 
ATOM   3958 C CA  . PHE D  1 47  ? -75.031 26.940  -3.793  1.00 32.77 ? 47  PHE D CA  1 
ATOM   3959 C C   . PHE D  1 47  ? -76.359 26.229  -3.567  1.00 33.48 ? 47  PHE D C   1 
ATOM   3960 O O   . PHE D  1 47  ? -77.060 25.895  -4.526  1.00 34.36 ? 47  PHE D O   1 
ATOM   3961 C CB  . PHE D  1 47  ? -75.288 28.401  -4.191  1.00 33.73 ? 47  PHE D CB  1 
ATOM   3962 C CG  . PHE D  1 47  ? -76.157 29.154  -3.210  1.00 34.94 ? 47  PHE D CG  1 
ATOM   3963 C CD1 . PHE D  1 47  ? -75.834 29.198  -1.862  1.00 34.56 ? 47  PHE D CD1 1 
ATOM   3964 C CD2 . PHE D  1 47  ? -77.291 29.823  -3.640  1.00 35.54 ? 47  PHE D CD2 1 
ATOM   3965 C CE1 . PHE D  1 47  ? -76.631 29.889  -0.963  1.00 32.98 ? 47  PHE D CE1 1 
ATOM   3966 C CE2 . PHE D  1 47  ? -78.089 30.514  -2.744  1.00 36.45 ? 47  PHE D CE2 1 
ATOM   3967 C CZ  . PHE D  1 47  ? -77.758 30.546  -1.405  1.00 34.55 ? 47  PHE D CZ  1 
ATOM   3968 N N   . SER D  1 48  ? -76.713 26.033  -2.296  1.00 32.47 ? 48  SER D N   1 
ATOM   3969 C CA  . SER D  1 48  ? -77.983 25.427  -1.919  1.00 32.38 ? 48  SER D CA  1 
ATOM   3970 C C   . SER D  1 48  ? -78.456 26.046  -0.611  1.00 32.97 ? 48  SER D C   1 
ATOM   3971 O O   . SER D  1 48  ? -77.665 26.608  0.150   1.00 33.32 ? 48  SER D O   1 
ATOM   3972 C CB  . SER D  1 48  ? -77.861 23.905  -1.764  1.00 33.38 ? 48  SER D CB  1 
ATOM   3973 O OG  . SER D  1 48  ? -77.093 23.330  -2.809  1.00 34.87 ? 48  SER D OG  1 
ATOM   3974 N N   . TRP D  1 49  ? -79.761 25.947  -0.360  1.00 34.16 ? 49  TRP D N   1 
ATOM   3975 C CA  . TRP D  1 49  ? -80.318 26.262  0.948   1.00 33.63 ? 49  TRP D CA  1 
ATOM   3976 C C   . TRP D  1 49  ? -80.323 25.000  1.798   1.00 33.96 ? 49  TRP D C   1 
ATOM   3977 O O   . TRP D  1 49  ? -80.582 23.906  1.292   1.00 34.11 ? 49  TRP D O   1 
ATOM   3978 C CB  . TRP D  1 49  ? -81.744 26.808  0.840   1.00 34.29 ? 49  TRP D CB  1 
ATOM   3979 C CG  . TRP D  1 49  ? -81.887 28.073  0.051   1.00 37.03 ? 49  TRP D CG  1 
ATOM   3980 C CD1 . TRP D  1 49  ? -82.584 28.237  -1.109  1.00 39.84 ? 49  TRP D CD1 1 
ATOM   3981 C CD2 . TRP D  1 49  ? -81.332 29.356  0.369   1.00 37.19 ? 49  TRP D CD2 1 
ATOM   3982 N NE1 . TRP D  1 49  ? -82.495 29.538  -1.537  1.00 42.48 ? 49  TRP D NE1 1 
ATOM   3983 C CE2 . TRP D  1 49  ? -81.729 30.245  -0.648  1.00 41.63 ? 49  TRP D CE2 1 
ATOM   3984 C CE3 . TRP D  1 49  ? -80.534 29.837  1.410   1.00 36.41 ? 49  TRP D CE3 1 
ATOM   3985 C CZ2 . TRP D  1 49  ? -81.359 31.587  -0.652  1.00 44.05 ? 49  TRP D CZ2 1 
ATOM   3986 C CZ3 . TRP D  1 49  ? -80.167 31.170  1.402   1.00 36.48 ? 49  TRP D CZ3 1 
ATOM   3987 C CH2 . TRP D  1 49  ? -80.579 32.029  0.379   1.00 40.13 ? 49  TRP D CH2 1 
ATOM   3988 N N   . THR D  1 50  ? -80.039 25.155  3.093   1.00 34.02 ? 50  THR D N   1 
ATOM   3989 C CA  . THR D  1 50  ? -80.016 24.027  4.019   1.00 34.24 ? 50  THR D CA  1 
ATOM   3990 C C   . THR D  1 50  ? -80.583 24.461  5.370   1.00 33.81 ? 50  THR D C   1 
ATOM   3991 O O   . THR D  1 50  ? -81.057 25.588  5.537   1.00 33.47 ? 50  THR D O   1 
ATOM   3992 C CB  . THR D  1 50  ? -78.598 23.462  4.169   1.00 33.02 ? 50  THR D CB  1 
ATOM   3993 O OG1 . THR D  1 50  ? -78.640 22.251  4.933   1.00 34.60 ? 50  THR D OG1 1 
ATOM   3994 C CG2 . THR D  1 50  ? -77.690 24.461  4.865   1.00 32.91 ? 50  THR D CG2 1 
ATOM   3995 N N   . LEU D  1 51  ? -80.561 23.542  6.340   1.00 34.06 ? 51  LEU D N   1 
ATOM   3996 C CA  . LEU D  1 51  ? -81.037 23.825  7.700   1.00 34.92 ? 51  LEU D CA  1 
ATOM   3997 C C   . LEU D  1 51  ? -80.169 23.037  8.684   1.00 36.21 ? 51  LEU D C   1 
ATOM   3998 O O   . LEU D  1 51  ? -80.443 21.870  8.982   1.00 38.99 ? 51  LEU D O   1 
ATOM   3999 C CB  . LEU D  1 51  ? -82.522 23.494  7.847   1.00 35.77 ? 51  LEU D CB  1 
ATOM   4000 C CG  . LEU D  1 51  ? -83.139 23.656  9.240   1.00 35.74 ? 51  LEU D CG  1 
ATOM   4001 C CD1 . LEU D  1 51  ? -82.906 25.058  9.777   1.00 36.33 ? 51  LEU D CD1 1 
ATOM   4002 C CD2 . LEU D  1 51  ? -84.621 23.335  9.206   1.00 35.73 ? 51  LEU D CD2 1 
ATOM   4003 N N   . ALA D  1 52  ? -79.120 23.681  9.184   1.00 33.86 ? 52  ALA D N   1 
ATOM   4004 C CA  . ALA D  1 52  ? -78.214 23.068  10.141  1.00 35.37 ? 52  ALA D CA  1 
ATOM   4005 C C   . ALA D  1 52  ? -78.351 23.755  11.490  1.00 36.96 ? 52  ALA D C   1 
ATOM   4006 O O   . ALA D  1 52  ? -78.848 24.878  11.592  1.00 37.19 ? 52  ALA D O   1 
ATOM   4007 C CB  . ALA D  1 52  ? -76.762 23.137  9.657   1.00 36.74 ? 52  ALA D CB  1 
ATOM   4008 N N   . TYR D  1 53  ? -77.929 23.051  12.534  1.00 38.67 ? 53  TYR D N   1 
ATOM   4009 C CA  . TYR D  1 53  ? -77.891 23.581  13.895  1.00 38.93 ? 53  TYR D CA  1 
ATOM   4010 C C   . TYR D  1 53  ? -76.435 23.500  14.346  1.00 39.93 ? 53  TYR D C   1 
ATOM   4011 O O   . TYR D  1 53  ? -76.011 22.498  14.924  1.00 41.81 ? 53  TYR D O   1 
ATOM   4012 C CB  . TYR D  1 53  ? -78.819 22.802  14.825  1.00 40.15 ? 53  TYR D CB  1 
ATOM   4013 C CG  . TYR D  1 53  ? -80.302 23.030  14.598  1.00 40.89 ? 53  TYR D CG  1 
ATOM   4014 C CD1 . TYR D  1 53  ? -80.768 24.162  13.933  1.00 39.66 ? 53  TYR D CD1 1 
ATOM   4015 C CD2 . TYR D  1 53  ? -81.239 22.112  15.060  1.00 41.72 ? 53  TYR D CD2 1 
ATOM   4016 C CE1 . TYR D  1 53  ? -82.128 24.367  13.734  1.00 39.43 ? 53  TYR D CE1 1 
ATOM   4017 C CE2 . TYR D  1 53  ? -82.596 22.311  14.865  1.00 41.11 ? 53  TYR D CE2 1 
ATOM   4018 C CZ  . TYR D  1 53  ? -83.034 23.437  14.203  1.00 40.37 ? 53  TYR D CZ  1 
ATOM   4019 O OH  . TYR D  1 53  ? -84.382 23.632  14.009  1.00 40.79 ? 53  TYR D OH  1 
ATOM   4020 N N   . ASN D  1 54  ? -75.665 24.550  14.066  1.00 40.20 ? 54  ASN D N   1 
ATOM   4021 C CA  . ASN D  1 54  ? -74.227 24.521  14.321  1.00 42.30 ? 54  ASN D CA  1 
ATOM   4022 C C   . ASN D  1 54  ? -73.963 24.666  15.812  1.00 42.48 ? 54  ASN D C   1 
ATOM   4023 O O   . ASN D  1 54  ? -74.163 25.742  16.385  1.00 41.48 ? 54  ASN D O   1 
ATOM   4024 C CB  . ASN D  1 54  ? -73.524 25.627  13.540  1.00 42.35 ? 54  ASN D CB  1 
ATOM   4025 C CG  . ASN D  1 54  ? -72.165 25.194  13.001  1.00 43.10 ? 54  ASN D CG  1 
ATOM   4026 O OD1 . ASN D  1 54  ? -71.518 24.298  13.550  1.00 44.30 ? 54  ASN D OD1 1 
ATOM   4027 N ND2 . ASN D  1 54  ? -71.725 25.838  11.925  1.00 40.93 ? 54  ASN D ND2 1 
ATOM   4028 N N   . THR D  1 55  ? -73.502 23.582  16.438  1.00 44.65 ? 55  THR D N   1 
ATOM   4029 C CA  . THR D  1 55  ? -73.051 23.669  17.821  1.00 45.33 ? 55  THR D CA  1 
ATOM   4030 C C   . THR D  1 55  ? -71.801 24.538  17.925  1.00 46.17 ? 55  THR D C   1 
ATOM   4031 O O   . THR D  1 55  ? -71.723 25.437  18.772  1.00 46.08 ? 55  THR D O   1 
ATOM   4032 C CB  . THR D  1 55  ? -72.785 22.267  18.382  1.00 44.99 ? 55  THR D CB  1 
ATOM   4033 O OG1 . THR D  1 55  ? -73.907 21.415  18.117  1.00 43.84 ? 55  THR D OG1 1 
ATOM   4034 C CG2 . THR D  1 55  ? -72.555 22.329  19.889  1.00 45.98 ? 55  THR D CG2 1 
ATOM   4035 N N   . GLY D  1 56  ? -70.825 24.298  17.054  1.00 46.40 ? 56  GLY D N   1 
ATOM   4036 C CA  . GLY D  1 56  ? -69.566 25.011  17.037  1.00 45.81 ? 56  GLY D CA  1 
ATOM   4037 C C   . GLY D  1 56  ? -68.398 24.053  16.973  1.00 45.86 ? 56  GLY D C   1 
ATOM   4038 O O   . GLY D  1 56  ? -68.554 22.836  16.882  1.00 46.98 ? 56  GLY D O   1 
ATOM   4039 N N   . ALA D  1 57  ? -67.201 24.628  17.021  1.00 47.14 ? 57  ALA D N   1 
ATOM   4040 C CA  . ALA D  1 57  ? -65.965 23.862  17.084  1.00 48.50 ? 57  ALA D CA  1 
ATOM   4041 C C   . ALA D  1 57  ? -65.477 23.772  18.525  1.00 47.92 ? 57  ALA D C   1 
ATOM   4042 O O   . ALA D  1 57  ? -65.839 24.581  19.384  1.00 47.79 ? 57  ALA D O   1 
ATOM   4043 C CB  . ALA D  1 57  ? -64.881 24.486  16.200  1.00 48.12 ? 57  ALA D CB  1 
ATOM   4044 N N   . ALA D  1 58  ? -64.645 22.765  18.779  1.00 47.20 ? 58  ALA D N   1 
ATOM   4045 C CA  . ALA D  1 58  ? -64.082 22.536  20.107  1.00 47.64 ? 58  ALA D CA  1 
ATOM   4046 C C   . ALA D  1 58  ? -62.783 23.327  20.231  1.00 48.93 ? 58  ALA D C   1 
ATOM   4047 O O   . ALA D  1 58  ? -61.717 22.869  19.810  1.00 47.65 ? 58  ALA D O   1 
ATOM   4048 C CB  . ALA D  1 58  ? -63.861 21.046  20.350  1.00 46.92 ? 58  ALA D CB  1 
ATOM   4049 N N   . PHE D  1 59  ? -62.873 24.532  20.797  1.00 49.21 ? 59  PHE D N   1 
ATOM   4050 C CA  . PHE D  1 59  ? -61.685 25.295  21.161  1.00 47.20 ? 59  PHE D CA  1 
ATOM   4051 C C   . PHE D  1 59  ? -61.116 24.860  22.505  1.00 46.81 ? 59  PHE D C   1 
ATOM   4052 O O   . PHE D  1 59  ? -60.026 25.309  22.883  1.00 46.39 ? 59  PHE D O   1 
ATOM   4053 C CB  . PHE D  1 59  ? -62.010 26.793  21.182  1.00 47.68 ? 59  PHE D CB  1 
ATOM   4054 C CG  . PHE D  1 59  ? -62.572 27.306  19.882  1.00 48.78 ? 59  PHE D CG  1 
ATOM   4055 C CD1 . PHE D  1 59  ? -61.750 27.493  18.780  1.00 49.42 ? 59  PHE D CD1 1 
ATOM   4056 C CD2 . PHE D  1 59  ? -63.921 27.598  19.762  1.00 47.72 ? 59  PHE D CD2 1 
ATOM   4057 C CE1 . PHE D  1 59  ? -62.265 27.961  17.582  1.00 49.52 ? 59  PHE D CE1 1 
ATOM   4058 C CE2 . PHE D  1 59  ? -64.442 28.065  18.569  1.00 47.62 ? 59  PHE D CE2 1 
ATOM   4059 C CZ  . PHE D  1 59  ? -63.613 28.247  17.477  1.00 48.06 ? 59  PHE D CZ  1 
ATOM   4060 N N   . SER D  1 60  ? -61.849 24.029  23.240  1.00 47.40 ? 60  SER D N   1 
ATOM   4061 C CA  . SER D  1 60  ? -61.353 23.330  24.414  1.00 46.86 ? 60  SER D CA  1 
ATOM   4062 C C   . SER D  1 60  ? -61.871 21.906  24.307  1.00 47.49 ? 60  SER D C   1 
ATOM   4063 O O   . SER D  1 60  ? -63.073 21.702  24.119  1.00 47.91 ? 60  SER D O   1 
ATOM   4064 C CB  . SER D  1 60  ? -61.820 23.992  25.722  1.00 48.84 ? 60  SER D CB  1 
ATOM   4065 O OG  . SER D  1 60  ? -63.230 24.127  25.771  1.00 52.20 ? 60  SER D OG  1 
ATOM   4066 N N   . PHE D  1 61  ? -60.964 20.936  24.437  1.00 46.95 ? 61  PHE D N   1 
ATOM   4067 C CA  . PHE D  1 61  ? -61.214 19.524  24.145  1.00 45.80 ? 61  PHE D CA  1 
ATOM   4068 C C   . PHE D  1 61  ? -62.558 19.015  24.667  1.00 46.49 ? 61  PHE D C   1 
ATOM   4069 O O   . PHE D  1 61  ? -62.973 19.326  25.786  1.00 46.89 ? 61  PHE D O   1 
ATOM   4070 C CB  . PHE D  1 61  ? -60.060 18.702  24.727  1.00 45.14 ? 61  PHE D CB  1 
ATOM   4071 C CG  . PHE D  1 61  ? -60.281 17.222  24.677  1.00 45.11 ? 61  PHE D CG  1 
ATOM   4072 C CD1 . PHE D  1 61  ? -60.269 16.535  23.470  1.00 43.76 ? 61  PHE D CD1 1 
ATOM   4073 C CD2 . PHE D  1 61  ? -60.500 16.516  25.846  1.00 44.95 ? 61  PHE D CD2 1 
ATOM   4074 C CE1 . PHE D  1 61  ? -60.474 15.167  23.441  1.00 42.51 ? 61  PHE D CE1 1 
ATOM   4075 C CE2 . PHE D  1 61  ? -60.700 15.159  25.823  1.00 42.94 ? 61  PHE D CE2 1 
ATOM   4076 C CZ  . PHE D  1 61  ? -60.687 14.480  24.622  1.00 42.66 ? 61  PHE D CZ  1 
ATOM   4077 N N   . LEU D  1 62  ? -63.228 18.216  23.825  1.00 46.55 ? 62  LEU D N   1 
ATOM   4078 C CA  . LEU D  1 62  ? -64.547 17.639  24.119  1.00 45.19 ? 62  LEU D CA  1 
ATOM   4079 C C   . LEU D  1 62  ? -65.591 18.723  24.398  1.00 46.67 ? 62  LEU D C   1 
ATOM   4080 O O   . LEU D  1 62  ? -66.333 18.669  25.383  1.00 46.81 ? 62  LEU D O   1 
ATOM   4081 C CB  . LEU D  1 62  ? -64.473 16.633  25.273  1.00 42.90 ? 62  LEU D CB  1 
ATOM   4082 C CG  . LEU D  1 62  ? -63.991 15.216  24.940  1.00 41.11 ? 62  LEU D CG  1 
ATOM   4083 C CD1 . LEU D  1 62  ? -64.621 14.182  25.864  1.00 39.23 ? 62  LEU D CD1 1 
ATOM   4084 C CD2 . LEU D  1 62  ? -64.220 14.853  23.479  1.00 41.89 ? 62  LEU D CD2 1 
ATOM   4085 N N   . ALA D  1 63  ? -65.648 19.711  23.498  1.00 47.81 ? 63  ALA D N   1 
ATOM   4086 C CA  . ALA D  1 63  ? -66.558 20.844  23.612  1.00 47.56 ? 63  ALA D CA  1 
ATOM   4087 C C   . ALA D  1 63  ? -67.843 20.679  22.816  1.00 48.06 ? 63  ALA D C   1 
ATOM   4088 O O   . ALA D  1 63  ? -68.832 21.348  23.133  1.00 47.71 ? 63  ALA D O   1 
ATOM   4089 C CB  . ALA D  1 63  ? -65.865 22.130  23.154  1.00 46.87 ? 63  ALA D CB  1 
ATOM   4090 N N   . ASP D  1 64  ? -67.861 19.814  21.799  1.00 48.78 ? 64  ASP D N   1 
ATOM   4091 C CA  . ASP D  1 64  ? -69.085 19.625  21.027  1.00 49.55 ? 64  ASP D CA  1 
ATOM   4092 C C   . ASP D  1 64  ? -70.159 18.892  21.819  1.00 50.93 ? 64  ASP D C   1 
ATOM   4093 O O   . ASP D  1 64  ? -71.333 18.928  21.432  1.00 50.90 ? 64  ASP D O   1 
ATOM   4094 C CB  . ASP D  1 64  ? -68.778 18.868  19.735  1.00 49.06 ? 64  ASP D CB  1 
ATOM   4095 C CG  . ASP D  1 64  ? -67.649 19.497  18.951  1.00 47.41 ? 64  ASP D CG  1 
ATOM   4096 O OD1 . ASP D  1 64  ? -66.497 19.439  19.433  1.00 47.66 ? 64  ASP D OD1 1 
ATOM   4097 O OD2 . ASP D  1 64  ? -67.910 20.045  17.860  1.00 46.11 ? 64  ASP D OD2 1 
ATOM   4098 N N   . SER D  1 65  ? -69.782 18.230  22.913  1.00 50.72 ? 65  SER D N   1 
ATOM   4099 C CA  . SER D  1 65  ? -70.729 17.531  23.773  1.00 50.15 ? 65  SER D CA  1 
ATOM   4100 C C   . SER D  1 65  ? -71.086 18.306  25.035  1.00 50.19 ? 65  SER D C   1 
ATOM   4101 O O   . SER D  1 65  ? -72.162 18.083  25.601  1.00 50.73 ? 65  SER D O   1 
ATOM   4102 C CB  . SER D  1 65  ? -70.171 16.159  24.169  1.00 48.31 ? 65  SER D CB  1 
ATOM   4103 O OG  . SER D  1 65  ? -69.820 15.400  23.023  1.00 46.78 ? 65  SER D OG  1 
ATOM   4104 N N   . SER D  1 66  ? -70.210 19.202  25.490  1.00 49.40 ? 66  SER D N   1 
ATOM   4105 C CA  . SER D  1 66  ? -70.470 19.995  26.684  1.00 48.73 ? 66  SER D CA  1 
ATOM   4106 C C   . SER D  1 66  ? -71.277 21.238  26.330  1.00 48.31 ? 66  SER D C   1 
ATOM   4107 O O   . SER D  1 66  ? -70.955 21.948  25.372  1.00 48.96 ? 66  SER D O   1 
ATOM   4108 C CB  . SER D  1 66  ? -69.156 20.398  27.356  1.00 48.90 ? 66  SER D CB  1 
ATOM   4109 O OG  . SER D  1 66  ? -68.530 21.468  26.664  1.00 47.79 ? 66  SER D OG  1 
ATOM   4110 N N   . GLY D  1 67  ? -72.315 21.509  27.114  1.00 48.17 ? 67  GLY D N   1 
ATOM   4111 C CA  . GLY D  1 67  ? -73.126 22.686  26.895  1.00 47.60 ? 67  GLY D CA  1 
ATOM   4112 C C   . GLY D  1 67  ? -72.529 23.979  27.393  1.00 46.90 ? 67  GLY D C   1 
ATOM   4113 O O   . GLY D  1 67  ? -73.190 25.020  27.333  1.00 47.12 ? 67  GLY D O   1 
ATOM   4114 N N   . TRP D  1 68  ? -71.293 23.943  27.899  1.00 47.25 ? 68  TRP D N   1 
ATOM   4115 C CA  . TRP D  1 68  ? -70.646 25.164  28.365  1.00 47.72 ? 68  TRP D CA  1 
ATOM   4116 C C   . TRP D  1 68  ? -70.203 26.043  27.203  1.00 47.27 ? 68  TRP D C   1 
ATOM   4117 O O   . TRP D  1 68  ? -70.074 27.261  27.369  1.00 47.76 ? 68  TRP D O   1 
ATOM   4118 C CB  . TRP D  1 68  ? -69.457 24.829  29.268  1.00 48.16 ? 68  TRP D CB  1 
ATOM   4119 C CG  . TRP D  1 68  ? -68.684 26.044  29.749  1.00 50.02 ? 68  TRP D CG  1 
ATOM   4120 C CD1 . TRP D  1 68  ? -67.335 26.242  29.662  1.00 50.91 ? 68  TRP D CD1 1 
ATOM   4121 C CD2 . TRP D  1 68  ? -69.220 27.225  30.377  1.00 50.34 ? 68  TRP D CD2 1 
ATOM   4122 N NE1 . TRP D  1 68  ? -66.996 27.464  30.201  1.00 51.06 ? 68  TRP D NE1 1 
ATOM   4123 C CE2 . TRP D  1 68  ? -68.134 28.087  30.645  1.00 50.79 ? 68  TRP D CE2 1 
ATOM   4124 C CE3 . TRP D  1 68  ? -70.509 27.636  30.739  1.00 49.81 ? 68  TRP D CE3 1 
ATOM   4125 C CZ2 . TRP D  1 68  ? -68.299 29.333  31.257  1.00 50.66 ? 68  TRP D CZ2 1 
ATOM   4126 C CZ3 . TRP D  1 68  ? -70.669 28.873  31.348  1.00 50.34 ? 68  TRP D CZ3 1 
ATOM   4127 C CH2 . TRP D  1 68  ? -69.570 29.705  31.600  1.00 50.86 ? 68  TRP D CH2 1 
ATOM   4128 N N   . GLN D  1 69  ? -69.971 25.452  26.027  1.00 46.41 ? 69  GLN D N   1 
ATOM   4129 C CA  . GLN D  1 69  ? -69.666 26.250  24.842  1.00 46.19 ? 69  GLN D CA  1 
ATOM   4130 C C   . GLN D  1 69  ? -70.780 27.243  24.549  1.00 46.18 ? 69  GLN D C   1 
ATOM   4131 O O   . GLN D  1 69  ? -70.519 28.396  24.179  1.00 45.27 ? 69  GLN D O   1 
ATOM   4132 C CB  . GLN D  1 69  ? -69.449 25.335  23.640  1.00 45.52 ? 69  GLN D CB  1 
ATOM   4133 C CG  . GLN D  1 69  ? -68.221 24.485  23.753  1.00 46.06 ? 69  GLN D CG  1 
ATOM   4134 C CD  . GLN D  1 69  ? -66.951 25.272  23.503  1.00 46.60 ? 69  GLN D CD  1 
ATOM   4135 O OE1 . GLN D  1 69  ? -66.251 25.662  24.439  1.00 46.32 ? 69  GLN D OE1 1 
ATOM   4136 N NE2 . GLN D  1 69  ? -66.639 25.500  22.230  1.00 46.80 ? 69  GLN D NE2 1 
ATOM   4137 N N   . ARG D  1 70  ? -72.031 26.805  24.713  1.00 45.87 ? 70  ARG D N   1 
ATOM   4138 C CA  . ARG D  1 70  ? -73.183 27.669  24.487  1.00 45.31 ? 70  ARG D CA  1 
ATOM   4139 C C   . ARG D  1 70  ? -73.056 28.967  25.273  1.00 45.74 ? 70  ARG D C   1 
ATOM   4140 O O   . ARG D  1 70  ? -73.181 30.062  24.712  1.00 45.10 ? 70  ARG D O   1 
ATOM   4141 C CB  . ARG D  1 70  ? -74.456 26.914  24.872  1.00 45.01 ? 70  ARG D CB  1 
ATOM   4142 C CG  . ARG D  1 70  ? -75.697 27.764  25.026  1.00 44.41 ? 70  ARG D CG  1 
ATOM   4143 C CD  . ARG D  1 70  ? -76.764 26.988  25.780  1.00 43.92 ? 70  ARG D CD  1 
ATOM   4144 N NE  . ARG D  1 70  ? -78.066 27.638  25.712  1.00 43.50 ? 70  ARG D NE  1 
ATOM   4145 C CZ  . ARG D  1 70  ? -79.169 27.161  26.272  1.00 42.94 ? 70  ARG D CZ  1 
ATOM   4146 N NH1 . ARG D  1 70  ? -79.159 26.037  26.970  1.00 43.76 ? 70  ARG D NH1 1 
ATOM   4147 N NH2 . ARG D  1 70  ? -80.310 27.828  26.127  1.00 41.81 ? 70  ARG D NH2 1 
ATOM   4148 N N   . TRP D  1 71  ? -72.773 28.864  26.572  1.00 46.08 ? 71  TRP D N   1 
ATOM   4149 C CA  . TRP D  1 71  ? -72.635 30.059  27.393  1.00 46.25 ? 71  TRP D CA  1 
ATOM   4150 C C   . TRP D  1 71  ? -71.264 30.706  27.266  1.00 45.65 ? 71  TRP D C   1 
ATOM   4151 O O   . TRP D  1 71  ? -71.134 31.903  27.548  1.00 45.86 ? 71  TRP D O   1 
ATOM   4152 C CB  . TRP D  1 71  ? -72.917 29.731  28.860  1.00 46.87 ? 71  TRP D CB  1 
ATOM   4153 C CG  . TRP D  1 71  ? -74.220 29.027  29.085  1.00 46.64 ? 71  TRP D CG  1 
ATOM   4154 C CD1 . TRP D  1 71  ? -74.397 27.790  29.630  1.00 46.97 ? 71  TRP D CD1 1 
ATOM   4155 C CD2 . TRP D  1 71  ? -75.531 29.515  28.763  1.00 46.49 ? 71  TRP D CD2 1 
ATOM   4156 N NE1 . TRP D  1 71  ? -75.734 27.477  29.674  1.00 47.31 ? 71  TRP D NE1 1 
ATOM   4157 C CE2 . TRP D  1 71  ? -76.453 28.518  29.147  1.00 46.51 ? 71  TRP D CE2 1 
ATOM   4158 C CE3 . TRP D  1 71  ? -76.015 30.697  28.190  1.00 46.03 ? 71  TRP D CE3 1 
ATOM   4159 C CZ2 . TRP D  1 71  ? -77.830 28.666  28.978  1.00 45.41 ? 71  TRP D CZ2 1 
ATOM   4160 C CZ3 . TRP D  1 71  ? -77.384 30.842  28.023  1.00 44.74 ? 71  TRP D CZ3 1 
ATOM   4161 C CH2 . TRP D  1 71  ? -78.275 29.832  28.416  1.00 44.46 ? 71  TRP D CH2 1 
ATOM   4162 N N   . LEU D  1 72  ? -70.242 29.947  26.865  1.00 45.53 ? 72  LEU D N   1 
ATOM   4163 C CA  . LEU D  1 72  ? -68.925 30.541  26.662  1.00 45.26 ? 72  LEU D CA  1 
ATOM   4164 C C   . LEU D  1 72  ? -68.961 31.559  25.533  1.00 43.73 ? 72  LEU D C   1 
ATOM   4165 O O   . LEU D  1 72  ? -68.446 32.674  25.667  1.00 43.34 ? 72  LEU D O   1 
ATOM   4166 C CB  . LEU D  1 72  ? -67.893 29.454  26.361  1.00 45.58 ? 72  LEU D CB  1 
ATOM   4167 C CG  . LEU D  1 72  ? -66.454 29.950  26.208  1.00 43.18 ? 72  LEU D CG  1 
ATOM   4168 C CD1 . LEU D  1 72  ? -65.865 30.286  27.571  1.00 43.99 ? 72  LEU D CD1 1 
ATOM   4169 C CD2 . LEU D  1 72  ? -65.588 28.935  25.472  1.00 42.98 ? 72  LEU D CD2 1 
ATOM   4170 N N   . PHE D  1 73  ? -69.585 31.193  24.413  1.00 44.18 ? 73  PHE D N   1 
ATOM   4171 C CA  . PHE D  1 73  ? -69.659 32.105  23.279  1.00 43.99 ? 73  PHE D CA  1 
ATOM   4172 C C   . PHE D  1 73  ? -70.557 33.298  23.576  1.00 43.05 ? 73  PHE D C   1 
ATOM   4173 O O   . PHE D  1 73  ? -70.264 34.415  23.136  1.00 42.04 ? 73  PHE D O   1 
ATOM   4174 C CB  . PHE D  1 73  ? -70.143 31.353  22.040  1.00 43.35 ? 73  PHE D CB  1 
ATOM   4175 C CG  . PHE D  1 73  ? -69.219 30.255  21.604  1.00 41.78 ? 73  PHE D CG  1 
ATOM   4176 C CD1 . PHE D  1 73  ? -67.856 30.349  21.833  1.00 42.22 ? 73  PHE D CD1 1 
ATOM   4177 C CD2 . PHE D  1 73  ? -69.713 29.127  20.975  1.00 42.50 ? 73  PHE D CD2 1 
ATOM   4178 C CE1 . PHE D  1 73  ? -67.002 29.343  21.437  1.00 43.56 ? 73  PHE D CE1 1 
ATOM   4179 C CE2 . PHE D  1 73  ? -68.865 28.115  20.579  1.00 44.18 ? 73  PHE D CE2 1 
ATOM   4180 C CZ  . PHE D  1 73  ? -67.508 28.222  20.810  1.00 44.81 ? 73  PHE D CZ  1 
ATOM   4181 N N   . ALA D  1 74  ? -71.646 33.085  24.321  1.00 43.71 ? 74  ALA D N   1 
ATOM   4182 C CA  . ALA D  1 74  ? -72.504 34.200  24.711  1.00 43.21 ? 74  ALA D CA  1 
ATOM   4183 C C   . ALA D  1 74  ? -71.755 35.174  25.607  1.00 41.84 ? 74  ALA D C   1 
ATOM   4184 O O   . ALA D  1 74  ? -71.977 36.388  25.541  1.00 40.83 ? 74  ALA D O   1 
ATOM   4185 C CB  . ALA D  1 74  ? -73.760 33.682  25.411  1.00 44.10 ? 74  ALA D CB  1 
ATOM   4186 N N   . LEU D  1 75  ? -70.873 34.655  26.464  1.00 42.36 ? 75  LEU D N   1 
ATOM   4187 C CA  . LEU D  1 75  ? -70.027 35.519  27.279  1.00 42.67 ? 75  LEU D CA  1 
ATOM   4188 C C   . LEU D  1 75  ? -69.112 36.369  26.407  1.00 41.28 ? 75  LEU D C   1 
ATOM   4189 O O   . LEU D  1 75  ? -68.929 37.566  26.663  1.00 40.87 ? 75  LEU D O   1 
ATOM   4190 C CB  . LEU D  1 75  ? -69.210 34.668  28.247  1.00 45.59 ? 75  LEU D CB  1 
ATOM   4191 C CG  . LEU D  1 75  ? -67.998 35.325  28.906  1.00 47.51 ? 75  LEU D CG  1 
ATOM   4192 C CD1 . LEU D  1 75  ? -68.431 36.462  29.821  1.00 49.45 ? 75  LEU D CD1 1 
ATOM   4193 C CD2 . LEU D  1 75  ? -67.194 34.280  29.667  1.00 48.79 ? 75  LEU D CD2 1 
ATOM   4194 N N   . ILE D  1 76  ? -68.524 35.762  25.375  1.00 41.01 ? 76  ILE D N   1 
ATOM   4195 C CA  . ILE D  1 76  ? -67.691 36.507  24.437  1.00 39.74 ? 76  ILE D CA  1 
ATOM   4196 C C   . ILE D  1 76  ? -68.525 37.527  23.672  1.00 40.28 ? 76  ILE D C   1 
ATOM   4197 O O   . ILE D  1 76  ? -68.141 38.696  23.542  1.00 40.42 ? 76  ILE D O   1 
ATOM   4198 C CB  . ILE D  1 76  ? -66.975 35.541  23.477  1.00 38.91 ? 76  ILE D CB  1 
ATOM   4199 C CG1 . ILE D  1 76  ? -65.851 34.805  24.203  1.00 38.44 ? 76  ILE D CG1 1 
ATOM   4200 C CG2 . ILE D  1 76  ? -66.456 36.281  22.249  1.00 39.70 ? 76  ILE D CG2 1 
ATOM   4201 C CD1 . ILE D  1 76  ? -65.239 33.687  23.400  1.00 39.34 ? 76  ILE D CD1 1 
ATOM   4202 N N   . ALA D  1 77  ? -69.674 37.101  23.148  1.00 41.13 ? 77  ALA D N   1 
ATOM   4203 C CA  . ALA D  1 77  ? -70.481 37.984  22.315  1.00 41.65 ? 77  ALA D CA  1 
ATOM   4204 C C   . ALA D  1 77  ? -71.279 39.006  23.120  1.00 41.04 ? 77  ALA D C   1 
ATOM   4205 O O   . ALA D  1 77  ? -71.829 39.939  22.525  1.00 40.72 ? 77  ALA D O   1 
ATOM   4206 C CB  . ALA D  1 77  ? -71.417 37.162  21.424  1.00 40.58 ? 77  ALA D CB  1 
ATOM   4207 N N   . ILE D  1 78  ? -71.376 38.850  24.444  1.00 40.59 ? 78  ILE D N   1 
ATOM   4208 C CA  . ILE D  1 78  ? -71.903 39.929  25.275  1.00 39.85 ? 78  ILE D CA  1 
ATOM   4209 C C   . ILE D  1 78  ? -70.818 40.961  25.545  1.00 40.39 ? 78  ILE D C   1 
ATOM   4210 O O   . ILE D  1 78  ? -71.069 42.171  25.508  1.00 40.45 ? 78  ILE D O   1 
ATOM   4211 C CB  . ILE D  1 78  ? -72.489 39.376  26.590  1.00 40.10 ? 78  ILE D CB  1 
ATOM   4212 C CG1 . ILE D  1 78  ? -73.878 38.786  26.364  1.00 39.76 ? 78  ILE D CG1 1 
ATOM   4213 C CG2 . ILE D  1 78  ? -72.565 40.471  27.645  1.00 40.55 ? 78  ILE D CG2 1 
ATOM   4214 C CD1 . ILE D  1 78  ? -74.298 37.786  27.420  1.00 38.84 ? 78  ILE D CD1 1 
ATOM   4215 N N   . VAL D  1 79  ? -69.601 40.497  25.834  1.00 40.33 ? 79  VAL D N   1 
ATOM   4216 C CA  . VAL D  1 79  ? -68.489 41.412  26.085  1.00 40.22 ? 79  VAL D CA  1 
ATOM   4217 C C   . VAL D  1 79  ? -68.142 42.188  24.823  1.00 40.63 ? 79  VAL D C   1 
ATOM   4218 O O   . VAL D  1 79  ? -68.007 43.418  24.844  1.00 41.47 ? 79  VAL D O   1 
ATOM   4219 C CB  . VAL D  1 79  ? -67.268 40.643  26.622  1.00 39.48 ? 79  VAL D CB  1 
ATOM   4220 C CG1 . VAL D  1 79  ? -66.017 41.509  26.554  1.00 38.12 ? 79  VAL D CG1 1 
ATOM   4221 C CG2 . VAL D  1 79  ? -67.523 40.182  28.048  1.00 40.18 ? 79  VAL D CG2 1 
ATOM   4222 N N   . VAL D  1 80  ? -67.999 41.478  23.701  1.00 40.34 ? 80  VAL D N   1 
ATOM   4223 C CA  . VAL D  1 80  ? -67.601 42.124  22.453  1.00 40.30 ? 80  VAL D CA  1 
ATOM   4224 C C   . VAL D  1 80  ? -68.681 43.081  21.956  1.00 41.54 ? 80  VAL D C   1 
ATOM   4225 O O   . VAL D  1 80  ? -68.369 44.137  21.389  1.00 41.86 ? 80  VAL D O   1 
ATOM   4226 C CB  . VAL D  1 80  ? -67.244 41.057  21.401  1.00 38.84 ? 80  VAL D CB  1 
ATOM   4227 C CG1 . VAL D  1 80  ? -67.209 41.654  20.006  1.00 38.82 ? 80  VAL D CG1 1 
ATOM   4228 C CG2 . VAL D  1 80  ? -65.894 40.431  21.734  1.00 38.69 ? 80  VAL D CG2 1 
ATOM   4229 N N   . SER D  1 81  ? -69.957 42.744  22.160  1.00 42.28 ? 81  SER D N   1 
ATOM   4230 C CA  . SER D  1 81  ? -71.027 43.675  21.811  1.00 42.31 ? 81  SER D CA  1 
ATOM   4231 C C   . SER D  1 81  ? -70.972 44.925  22.685  1.00 42.54 ? 81  SER D C   1 
ATOM   4232 O O   . SER D  1 81  ? -71.112 46.050  22.188  1.00 41.92 ? 81  SER D O   1 
ATOM   4233 C CB  . SER D  1 81  ? -72.390 42.987  21.933  1.00 42.30 ? 81  SER D CB  1 
ATOM   4234 O OG  . SER D  1 81  ? -72.490 41.870  21.061  1.00 40.62 ? 81  SER D OG  1 
ATOM   4235 N N   . ALA D  1 82  ? -70.760 44.749  23.993  1.00 43.29 ? 82  ALA D N   1 
ATOM   4236 C CA  . ALA D  1 82  ? -70.670 45.886  24.903  1.00 44.00 ? 82  ALA D CA  1 
ATOM   4237 C C   . ALA D  1 82  ? -69.355 46.645  24.775  1.00 43.70 ? 82  ALA D C   1 
ATOM   4238 O O   . ALA D  1 82  ? -69.239 47.744  25.329  1.00 44.49 ? 82  ALA D O   1 
ATOM   4239 C CB  . ALA D  1 82  ? -70.862 45.422  26.350  1.00 44.09 ? 82  ALA D CB  1 
ATOM   4240 N N   . SER D  1 83  ? -68.363 46.087  24.079  1.00 42.10 ? 83  SER D N   1 
ATOM   4241 C CA  . SER D  1 83  ? -67.146 46.825  23.765  1.00 42.15 ? 83  SER D CA  1 
ATOM   4242 C C   . SER D  1 83  ? -67.303 47.665  22.503  1.00 43.65 ? 83  SER D C   1 
ATOM   4243 O O   . SER D  1 83  ? -66.779 48.782  22.434  1.00 45.29 ? 83  SER D O   1 
ATOM   4244 C CB  . SER D  1 83  ? -65.965 45.866  23.603  1.00 43.16 ? 83  SER D CB  1 
ATOM   4245 O OG  . SER D  1 83  ? -66.030 45.196  22.356  1.00 43.56 ? 83  SER D OG  1 
ATOM   4246 N N   . LEU D  1 84  ? -68.007 47.144  21.494  1.00 43.44 ? 84  LEU D N   1 
ATOM   4247 C CA  . LEU D  1 84  ? -68.311 47.941  20.312  1.00 42.81 ? 84  LEU D CA  1 
ATOM   4248 C C   . LEU D  1 84  ? -69.330 49.032  20.602  1.00 43.62 ? 84  LEU D C   1 
ATOM   4249 O O   . LEU D  1 84  ? -69.413 50.000  19.841  1.00 43.26 ? 84  LEU D O   1 
ATOM   4250 C CB  . LEU D  1 84  ? -68.827 47.046  19.187  1.00 41.15 ? 84  LEU D CB  1 
ATOM   4251 C CG  . LEU D  1 84  ? -67.830 46.021  18.653  1.00 41.52 ? 84  LEU D CG  1 
ATOM   4252 C CD1 . LEU D  1 84  ? -68.520 45.051  17.706  1.00 39.66 ? 84  LEU D CD1 1 
ATOM   4253 C CD2 . LEU D  1 84  ? -66.673 46.728  17.960  1.00 42.56 ? 84  LEU D CD2 1 
ATOM   4254 N N   . VAL D  1 85  ? -70.121 48.881  21.667  1.00 43.86 ? 85  VAL D N   1 
ATOM   4255 C CA  . VAL D  1 85  ? -71.061 49.928  22.057  1.00 42.88 ? 85  VAL D CA  1 
ATOM   4256 C C   . VAL D  1 85  ? -70.314 51.137  22.607  1.00 43.73 ? 85  VAL D C   1 
ATOM   4257 O O   . VAL D  1 85  ? -70.566 52.280  22.206  1.00 44.12 ? 85  VAL D O   1 
ATOM   4258 C CB  . VAL D  1 85  ? -72.077 49.382  23.077  1.00 42.54 ? 85  VAL D CB  1 
ATOM   4259 C CG1 . VAL D  1 85  ? -72.718 50.522  23.855  1.00 42.83 ? 85  VAL D CG1 1 
ATOM   4260 C CG2 . VAL D  1 85  ? -73.146 48.557  22.372  1.00 41.53 ? 85  VAL D CG2 1 
ATOM   4261 N N   . VAL D  1 86  ? -69.387 50.903  23.539  1.00 43.91 ? 86  VAL D N   1 
ATOM   4262 C CA  . VAL D  1 86  ? -68.600 51.995  24.099  1.00 43.91 ? 86  VAL D CA  1 
ATOM   4263 C C   . VAL D  1 86  ? -67.625 52.534  23.061  1.00 44.86 ? 86  VAL D C   1 
ATOM   4264 O O   . VAL D  1 86  ? -67.325 53.734  23.043  1.00 46.31 ? 86  VAL D O   1 
ATOM   4265 C CB  . VAL D  1 86  ? -67.887 51.523  25.381  1.00 44.44 ? 86  VAL D CB  1 
ATOM   4266 C CG1 . VAL D  1 86  ? -67.064 52.647  25.995  1.00 46.19 ? 86  VAL D CG1 1 
ATOM   4267 C CG2 . VAL D  1 86  ? -68.905 50.990  26.384  1.00 44.43 ? 86  VAL D CG2 1 
ATOM   4268 N N   . TRP D  1 87  ? -67.116 51.665  22.183  1.00 44.79 ? 87  TRP D N   1 
ATOM   4269 C CA  . TRP D  1 87  ? -66.292 52.126  21.069  1.00 45.50 ? 87  TRP D CA  1 
ATOM   4270 C C   . TRP D  1 87  ? -67.100 53.015  20.130  1.00 46.55 ? 87  TRP D C   1 
ATOM   4271 O O   . TRP D  1 87  ? -66.590 54.021  19.620  1.00 48.53 ? 87  TRP D O   1 
ATOM   4272 C CB  . TRP D  1 87  ? -65.713 50.917  20.327  1.00 47.54 ? 87  TRP D CB  1 
ATOM   4273 C CG  . TRP D  1 87  ? -64.571 51.211  19.382  1.00 51.09 ? 87  TRP D CG  1 
ATOM   4274 C CD1 . TRP D  1 87  ? -64.402 52.325  18.601  1.00 50.38 ? 87  TRP D CD1 1 
ATOM   4275 C CD2 . TRP D  1 87  ? -63.437 50.369  19.124  1.00 54.18 ? 87  TRP D CD2 1 
ATOM   4276 N NE1 . TRP D  1 87  ? -63.240 52.225  17.875  1.00 51.97 ? 87  TRP D NE1 1 
ATOM   4277 C CE2 . TRP D  1 87  ? -62.627 51.036  18.178  1.00 55.04 ? 87  TRP D CE2 1 
ATOM   4278 C CE3 . TRP D  1 87  ? -63.028 49.117  19.602  1.00 53.55 ? 87  TRP D CE3 1 
ATOM   4279 C CZ2 . TRP D  1 87  ? -61.433 50.493  17.700  1.00 55.90 ? 87  TRP D CZ2 1 
ATOM   4280 C CZ3 . TRP D  1 87  ? -61.842 48.579  19.127  1.00 54.17 ? 87  TRP D CZ3 1 
ATOM   4281 C CH2 . TRP D  1 87  ? -61.059 49.267  18.185  1.00 54.98 ? 87  TRP D CH2 1 
ATOM   4282 N N   . LEU D  1 88  ? -68.369 52.666  19.899  1.00 46.07 ? 88  LEU D N   1 
ATOM   4283 C CA  . LEU D  1 88  ? -69.226 53.472  19.033  1.00 45.93 ? 88  LEU D CA  1 
ATOM   4284 C C   . LEU D  1 88  ? -69.600 54.802  19.678  1.00 46.14 ? 88  LEU D C   1 
ATOM   4285 O O   . LEU D  1 88  ? -69.757 55.808  18.975  1.00 46.35 ? 88  LEU D O   1 
ATOM   4286 C CB  . LEU D  1 88  ? -70.485 52.685  18.672  1.00 44.21 ? 88  LEU D CB  1 
ATOM   4287 C CG  . LEU D  1 88  ? -70.924 52.668  17.207  1.00 43.83 ? 88  LEU D CG  1 
ATOM   4288 C CD1 . LEU D  1 88  ? -71.076 51.234  16.717  1.00 42.01 ? 88  LEU D CD1 1 
ATOM   4289 C CD2 . LEU D  1 88  ? -72.226 53.438  17.035  1.00 44.20 ? 88  LEU D CD2 1 
ATOM   4290 N N   . LYS D  1 89  ? -69.754 54.828  21.005  1.00 46.16 ? 89  LYS D N   1 
ATOM   4291 C CA  . LYS D  1 89  ? -70.113 56.067  21.687  1.00 46.23 ? 89  LYS D CA  1 
ATOM   4292 C C   . LYS D  1 89  ? -68.945 57.047  21.739  1.00 47.14 ? 89  LYS D C   1 
ATOM   4293 O O   . LYS D  1 89  ? -69.161 58.266  21.761  1.00 47.05 ? 89  LYS D O   1 
ATOM   4294 C CB  . LYS D  1 89  ? -70.624 55.760  23.096  1.00 44.76 ? 89  LYS D CB  1 
ATOM   4295 C CG  . LYS D  1 89  ? -71.998 55.096  23.129  1.00 42.61 ? 89  LYS D CG  1 
ATOM   4296 C CD  . LYS D  1 89  ? -72.479 54.867  24.552  1.00 41.08 ? 89  LYS D CD  1 
ATOM   4297 C CE  . LYS D  1 89  ? -73.857 54.225  24.567  1.00 40.18 ? 89  LYS D CE  1 
ATOM   4298 N NZ  . LYS D  1 89  ? -74.314 53.934  25.953  1.00 38.11 ? 89  LYS D NZ  1 
ATOM   4299 N N   . ARG D  1 90  ? -67.709 56.544  21.751  1.00 47.35 ? 90  ARG D N   1 
ATOM   4300 C CA  . ARG D  1 90  ? -66.517 57.376  21.657  1.00 48.12 ? 90  ARG D CA  1 
ATOM   4301 C C   . ARG D  1 90  ? -65.993 57.455  20.227  1.00 48.34 ? 90  ARG D C   1 
ATOM   4302 O O   . ARG D  1 90  ? -64.782 57.570  20.013  1.00 48.57 ? 90  ARG D O   1 
ATOM   4303 C CB  . ARG D  1 90  ? -65.422 56.850  22.584  1.00 49.76 ? 90  ARG D CB  1 
ATOM   4304 C CG  . ARG D  1 90  ? -65.864 56.504  24.009  1.00 51.03 ? 90  ARG D CG  1 
ATOM   4305 C CD  . ARG D  1 90  ? -64.688 55.899  24.762  1.00 52.79 ? 90  ARG D CD  1 
ATOM   4306 N NE  . ARG D  1 90  ? -63.922 55.021  23.882  1.00 53.50 ? 90  ARG D NE  1 
ATOM   4307 C CZ  . ARG D  1 90  ? -62.769 54.451  24.203  1.00 54.96 ? 90  ARG D CZ  1 
ATOM   4308 N NH1 . ARG D  1 90  ? -62.216 54.634  25.390  1.00 56.38 ? 90  ARG D NH1 1 
ATOM   4309 N NH2 . ARG D  1 90  ? -62.155 53.682  23.307  1.00 53.15 ? 90  ARG D NH2 1 
ATOM   4310 N N   . LEU D  1 91  ? -66.882 57.386  19.241  1.00 48.51 ? 91  LEU D N   1 
ATOM   4311 C CA  . LEU D  1 91  ? -66.500 57.396  17.837  1.00 50.80 ? 91  LEU D CA  1 
ATOM   4312 C C   . LEU D  1 91  ? -66.793 58.765  17.242  1.00 54.11 ? 91  LEU D C   1 
ATOM   4313 O O   . LEU D  1 91  ? -67.931 59.243  17.304  1.00 53.75 ? 91  LEU D O   1 
ATOM   4314 C CB  . LEU D  1 91  ? -67.250 56.309  17.067  1.00 50.63 ? 91  LEU D CB  1 
ATOM   4315 C CG  . LEU D  1 91  ? -66.585 55.763  15.803  1.00 51.01 ? 91  LEU D CG  1 
ATOM   4316 C CD1 . LEU D  1 91  ? -65.189 55.248  16.119  1.00 51.40 ? 91  LEU D CD1 1 
ATOM   4317 C CD2 . LEU D  1 91  ? -67.437 54.657  15.203  1.00 47.90 ? 91  LEU D CD2 1 
ATOM   4318 N N   . LYS D  1 92  ? -65.769 59.385  16.661  1.00 56.99 ? 92  LYS D N   1 
ATOM   4319 C CA  . LYS D  1 92  ? -65.903 60.717  16.089  1.00 58.90 ? 92  LYS D CA  1 
ATOM   4320 C C   . LYS D  1 92  ? -66.682 60.681  14.778  1.00 59.44 ? 92  LYS D C   1 
ATOM   4321 O O   . LYS D  1 92  ? -66.646 59.698  14.029  1.00 58.28 ? 92  LYS D O   1 
ATOM   4322 C CB  . LYS D  1 92  ? -64.524 61.345  15.857  1.00 59.92 ? 92  LYS D CB  1 
ATOM   4323 C CG  . LYS D  1 92  ? -63.588 60.515  14.977  1.00 61.22 ? 92  LYS D CG  1 
ATOM   4324 C CD  . LYS D  1 92  ? -62.302 61.268  14.631  1.00 60.79 ? 92  LYS D CD  1 
ATOM   4325 C CE  . LYS D  1 92  ? -61.360 60.408  13.788  1.00 58.54 ? 92  LYS D CE  1 
ATOM   4326 N NZ  . LYS D  1 92  ? -60.171 61.166  13.295  1.00 54.01 ? 92  LYS D NZ  1 
ATOM   4327 N N   . LYS D  1 93  ? -67.393 61.775  14.509  1.00 59.81 ? 93  LYS D N   1 
ATOM   4328 C CA  . LYS D  1 93  ? -68.075 61.929  13.233  1.00 60.11 ? 93  LYS D CA  1 
ATOM   4329 C C   . LYS D  1 93  ? -67.058 62.061  12.103  1.00 62.08 ? 93  LYS D C   1 
ATOM   4330 O O   . LYS D  1 93  ? -65.938 62.544  12.297  1.00 62.02 ? 93  LYS D O   1 
ATOM   4331 C CB  . LYS D  1 93  ? -68.997 63.152  13.254  1.00 58.55 ? 93  LYS D CB  1 
ATOM   4332 C CG  . LYS D  1 93  ? -70.072 63.119  14.332  1.00 57.00 ? 93  LYS D CG  1 
ATOM   4333 C CD  . LYS D  1 93  ? -71.037 64.288  14.179  1.00 53.95 ? 93  LYS D CD  1 
ATOM   4334 C CE  . LYS D  1 93  ? -72.212 64.175  15.136  1.00 51.13 ? 93  LYS D CE  1 
ATOM   4335 N NZ  . LYS D  1 93  ? -73.286 65.155  14.812  1.00 50.44 ? 93  LYS D NZ  1 
ATOM   4336 N N   . GLY D  1 94  ? -67.457 61.619  10.912  1.00 62.03 ? 94  GLY D N   1 
ATOM   4337 C CA  . GLY D  1 94  ? -66.584 61.672  9.753   1.00 61.32 ? 94  GLY D CA  1 
ATOM   4338 C C   . GLY D  1 94  ? -66.015 60.318  9.376   1.00 58.24 ? 94  GLY D C   1 
ATOM   4339 O O   . GLY D  1 94  ? -65.937 59.977  8.191   1.00 57.92 ? 94  GLY D O   1 
ATOM   4340 N N   . GLU D  1 95  ? -65.625 59.527  10.379  1.00 56.94 ? 95  GLU D N   1 
ATOM   4341 C CA  . GLU D  1 95  ? -65.144 58.163  10.156  1.00 54.35 ? 95  GLU D CA  1 
ATOM   4342 C C   . GLU D  1 95  ? -66.331 57.203  10.042  1.00 51.49 ? 95  GLU D C   1 
ATOM   4343 O O   . GLU D  1 95  ? -66.472 56.224  10.775  1.00 50.21 ? 95  GLU D O   1 
ATOM   4344 C CB  . GLU D  1 95  ? -64.192 57.755  11.270  1.00 53.18 ? 95  GLU D CB  1 
ATOM   4345 C CG  . GLU D  1 95  ? -63.045 56.872  10.805  1.00 52.51 ? 95  GLU D CG  1 
ATOM   4346 C CD  . GLU D  1 95  ? -61.971 56.689  11.869  1.00 54.62 ? 95  GLU D CD  1 
ATOM   4347 O OE1 . GLU D  1 95  ? -62.203 57.116  13.024  1.00 56.59 ? 95  GLU D OE1 1 
ATOM   4348 O OE2 . GLU D  1 95  ? -60.897 56.123  11.549  1.00 52.59 ? 95  GLU D OE2 1 
ATOM   4349 N N   . THR D  1 96  ? -67.202 57.534  9.091   1.00 50.29 ? 96  THR D N   1 
ATOM   4350 C CA  . THR D  1 96  ? -68.406 56.755  8.844   1.00 48.53 ? 96  THR D CA  1 
ATOM   4351 C C   . THR D  1 96  ? -68.065 55.330  8.438   1.00 46.27 ? 96  THR D C   1 
ATOM   4352 O O   . THR D  1 96  ? -68.724 54.378  8.870   1.00 45.65 ? 96  THR D O   1 
ATOM   4353 C CB  . THR D  1 96  ? -69.227 57.446  7.753   1.00 49.31 ? 96  THR D CB  1 
ATOM   4354 O OG1 . THR D  1 96  ? -68.523 57.362  6.505   1.00 48.63 ? 96  THR D OG1 1 
ATOM   4355 C CG2 . THR D  1 96  ? -69.437 58.915  8.097   1.00 50.40 ? 96  THR D CG2 1 
ATOM   4356 N N   . TRP D  1 97  ? -67.043 55.167  7.593   1.00 46.17 ? 97  TRP D N   1 
ATOM   4357 C CA  . TRP D  1 97  ? -66.651 53.838  7.138   1.00 45.45 ? 97  TRP D CA  1 
ATOM   4358 C C   . TRP D  1 97  ? -66.317 52.922  8.308   1.00 44.64 ? 97  TRP D C   1 
ATOM   4359 O O   . TRP D  1 97  ? -66.541 51.709  8.232   1.00 43.14 ? 97  TRP D O   1 
ATOM   4360 C CB  . TRP D  1 97  ? -65.459 53.951  6.185   1.00 46.05 ? 97  TRP D CB  1 
ATOM   4361 C CG  . TRP D  1 97  ? -65.376 52.859  5.151   1.00 45.23 ? 97  TRP D CG  1 
ATOM   4362 C CD1 . TRP D  1 97  ? -65.990 52.834  3.930   1.00 44.98 ? 97  TRP D CD1 1 
ATOM   4363 C CD2 . TRP D  1 97  ? -64.620 51.645  5.242   1.00 43.90 ? 97  TRP D CD2 1 
ATOM   4364 N NE1 . TRP D  1 97  ? -65.669 51.677  3.260   1.00 43.82 ? 97  TRP D NE1 1 
ATOM   4365 C CE2 . TRP D  1 97  ? -64.831 50.930  4.043   1.00 42.81 ? 97  TRP D CE2 1 
ATOM   4366 C CE3 . TRP D  1 97  ? -63.792 51.091  6.221   1.00 42.72 ? 97  TRP D CE3 1 
ATOM   4367 C CZ2 . TRP D  1 97  ? -64.242 49.693  3.800   1.00 41.76 ? 97  TRP D CZ2 1 
ATOM   4368 C CZ3 . TRP D  1 97  ? -63.210 49.865  5.978   1.00 42.37 ? 97  TRP D CZ3 1 
ATOM   4369 C CH2 . TRP D  1 97  ? -63.436 49.178  4.777   1.00 41.77 ? 97  TRP D CH2 1 
ATOM   4370 N N   . LEU D  1 98  ? -65.780 53.483  9.394   1.00 46.17 ? 98  LEU D N   1 
ATOM   4371 C CA  . LEU D  1 98  ? -65.483 52.693  10.582  1.00 45.97 ? 98  LEU D CA  1 
ATOM   4372 C C   . LEU D  1 98  ? -66.736 52.380  11.395  1.00 44.30 ? 98  LEU D C   1 
ATOM   4373 O O   . LEU D  1 98  ? -66.805 51.322  12.031  1.00 43.64 ? 98  LEU D O   1 
ATOM   4374 C CB  . LEU D  1 98  ? -64.459 53.423  11.452  1.00 47.71 ? 98  LEU D CB  1 
ATOM   4375 C CG  . LEU D  1 98  ? -63.698 52.567  12.463  1.00 47.70 ? 98  LEU D CG  1 
ATOM   4376 C CD1 . LEU D  1 98  ? -62.823 51.553  11.743  1.00 46.30 ? 98  LEU D CD1 1 
ATOM   4377 C CD2 . LEU D  1 98  ? -62.866 53.443  13.386  1.00 50.22 ? 98  LEU D CD2 1 
ATOM   4378 N N   . ALA D  1 99  ? -67.724 53.280  11.398  1.00 44.03 ? 99  ALA D N   1 
ATOM   4379 C CA  . ALA D  1 99  ? -68.949 53.042  12.154  1.00 43.20 ? 99  ALA D CA  1 
ATOM   4380 C C   . ALA D  1 99  ? -69.852 52.012  11.490  1.00 42.11 ? 99  ALA D C   1 
ATOM   4381 O O   . ALA D  1 99  ? -70.777 51.507  12.136  1.00 41.83 ? 99  ALA D O   1 
ATOM   4382 C CB  . ALA D  1 99  ? -69.710 54.353  12.352  1.00 45.96 ? 99  ALA D CB  1 
ATOM   4383 N N   . ILE D  1 100 ? -69.622 51.704  10.217  1.00 42.50 ? 100 ILE D N   1 
ATOM   4384 C CA  . ILE D  1 100 ? -70.365 50.642  9.546   1.00 41.14 ? 100 ILE D CA  1 
ATOM   4385 C C   . ILE D  1 100 ? -69.725 49.284  9.799   1.00 39.80 ? 100 ILE D C   1 
ATOM   4386 O O   . ILE D  1 100 ? -70.425 48.284  9.975   1.00 38.72 ? 100 ILE D O   1 
ATOM   4387 C CB  . ILE D  1 100 ? -70.466 50.946  8.040   1.00 40.67 ? 100 ILE D CB  1 
ATOM   4388 C CG1 . ILE D  1 100 ? -70.893 52.398  7.823   1.00 41.99 ? 100 ILE D CG1 1 
ATOM   4389 C CG2 . ILE D  1 100 ? -71.457 50.005  7.373   1.00 39.36 ? 100 ILE D CG2 1 
ATOM   4390 C CD1 . ILE D  1 100 ? -70.586 52.919  6.445   1.00 41.64 ? 100 ILE D CD1 1 
ATOM   4391 N N   . ALA D  1 101 ? -68.389 49.231  9.810   1.00 40.10 ? 101 ALA D N   1 
ATOM   4392 C CA  . ALA D  1 101 ? -67.693 47.989  10.130  1.00 37.94 ? 101 ALA D CA  1 
ATOM   4393 C C   . ALA D  1 101 ? -67.988 47.544  11.556  1.00 38.07 ? 101 ALA D C   1 
ATOM   4394 O O   . ALA D  1 101 ? -68.164 46.348  11.818  1.00 37.83 ? 101 ALA D O   1 
ATOM   4395 C CB  . ALA D  1 101 ? -66.190 48.162  9.923   1.00 38.12 ? 101 ALA D CB  1 
ATOM   4396 N N   . LEU D  1 102 ? -68.035 48.492  12.495  1.00 39.19 ? 102 LEU D N   1 
ATOM   4397 C CA  . LEU D  1 102 ? -68.362 48.155  13.878  1.00 38.46 ? 102 LEU D CA  1 
ATOM   4398 C C   . LEU D  1 102 ? -69.811 47.695  14.008  1.00 37.43 ? 102 LEU D C   1 
ATOM   4399 O O   . LEU D  1 102 ? -70.096 46.691  14.671  1.00 37.06 ? 102 LEU D O   1 
ATOM   4400 C CB  . LEU D  1 102 ? -68.095 49.355  14.788  1.00 40.18 ? 102 LEU D CB  1 
ATOM   4401 C CG  . LEU D  1 102 ? -66.709 49.533  15.415  1.00 41.03 ? 102 LEU D CG  1 
ATOM   4402 C CD1 . LEU D  1 102 ? -65.602 49.228  14.425  1.00 40.60 ? 102 LEU D CD1 1 
ATOM   4403 C CD2 . LEU D  1 102 ? -66.569 50.953  15.934  1.00 44.99 ? 102 LEU D CD2 1 
ATOM   4404 N N   . ALA D  1 103 ? -70.742 48.422  13.381  1.00 37.92 ? 103 ALA D N   1 
ATOM   4405 C CA  . ALA D  1 103 ? -72.161 48.113  13.546  1.00 37.05 ? 103 ALA D CA  1 
ATOM   4406 C C   . ALA D  1 103 ? -72.546 46.799  12.875  1.00 36.03 ? 103 ALA D C   1 
ATOM   4407 O O   . ALA D  1 103 ? -73.432 46.091  13.370  1.00 35.60 ? 103 ALA D O   1 
ATOM   4408 C CB  . ALA D  1 103 ? -73.013 49.261  13.005  1.00 37.60 ? 103 ALA D CB  1 
ATOM   4409 N N   . LEU D  1 104 ? -71.914 46.464  11.748  1.00 36.10 ? 104 LEU D N   1 
ATOM   4410 C CA  . LEU D  1 104 ? -72.166 45.173  11.114  1.00 35.05 ? 104 LEU D CA  1 
ATOM   4411 C C   . LEU D  1 104 ? -71.802 44.031  12.050  1.00 35.52 ? 104 LEU D C   1 
ATOM   4412 O O   . LEU D  1 104 ? -72.592 43.102  12.258  1.00 35.70 ? 104 LEU D O   1 
ATOM   4413 C CB  . LEU D  1 104 ? -71.369 45.061  9.817   1.00 34.32 ? 104 LEU D CB  1 
ATOM   4414 C CG  . LEU D  1 104 ? -71.921 45.751  8.577   1.00 33.95 ? 104 LEU D CG  1 
ATOM   4415 C CD1 . LEU D  1 104 ? -70.908 45.658  7.454   1.00 35.11 ? 104 LEU D CD1 1 
ATOM   4416 C CD2 . LEU D  1 104 ? -73.229 45.105  8.175   1.00 34.94 ? 104 LEU D CD2 1 
ATOM   4417 N N   . VAL D  1 105 ? -70.599 44.088  12.623  1.00 35.81 ? 105 VAL D N   1 
ATOM   4418 C CA  . VAL D  1 105 ? -70.153 43.053  13.548  1.00 35.06 ? 105 VAL D CA  1 
ATOM   4419 C C   . VAL D  1 105 ? -71.041 43.025  14.783  1.00 34.72 ? 105 VAL D C   1 
ATOM   4420 O O   . VAL D  1 105 ? -71.442 41.954  15.255  1.00 34.86 ? 105 VAL D O   1 
ATOM   4421 C CB  . VAL D  1 105 ? -68.677 43.280  13.919  1.00 34.23 ? 105 VAL D CB  1 
ATOM   4422 C CG1 . VAL D  1 105 ? -68.252 42.323  15.022  1.00 36.61 ? 105 VAL D CG1 1 
ATOM   4423 C CG2 . VAL D  1 105 ? -67.796 43.120  12.692  1.00 33.46 ? 105 VAL D CG2 1 
ATOM   4424 N N   . LEU D  1 106 ? -71.367 44.202  15.318  1.00 34.96 ? 106 LEU D N   1 
ATOM   4425 C CA  . LEU D  1 106 ? -72.186 44.286  16.521  1.00 34.92 ? 106 LEU D CA  1 
ATOM   4426 C C   . LEU D  1 106 ? -73.547 43.635  16.309  1.00 35.10 ? 106 LEU D C   1 
ATOM   4427 O O   . LEU D  1 106 ? -73.999 42.827  17.128  1.00 34.91 ? 106 LEU D O   1 
ATOM   4428 C CB  . LEU D  1 106 ? -72.342 45.751  16.924  1.00 36.19 ? 106 LEU D CB  1 
ATOM   4429 C CG  . LEU D  1 106 ? -73.395 46.103  17.969  1.00 36.40 ? 106 LEU D CG  1 
ATOM   4430 C CD1 . LEU D  1 106 ? -73.042 45.473  19.306  1.00 37.93 ? 106 LEU D CD1 1 
ATOM   4431 C CD2 . LEU D  1 106 ? -73.529 47.615  18.094  1.00 35.81 ? 106 LEU D CD2 1 
ATOM   4432 N N   . GLY D  1 107 ? -74.213 43.974  15.206  1.00 35.62 ? 107 GLY D N   1 
ATOM   4433 C CA  . GLY D  1 107 ? -75.526 43.405  14.945  1.00 35.56 ? 107 GLY D CA  1 
ATOM   4434 C C   . GLY D  1 107 ? -75.485 41.917  14.657  1.00 34.64 ? 107 GLY D C   1 
ATOM   4435 O O   . GLY D  1 107 ? -76.337 41.162  15.132  1.00 34.22 ? 107 GLY D O   1 
ATOM   4436 N N   . GLY D  1 108 ? -74.500 41.477  13.871  1.00 34.84 ? 108 GLY D N   1 
ATOM   4437 C CA  . GLY D  1 108 ? -74.397 40.063  13.550  1.00 34.21 ? 108 GLY D CA  1 
ATOM   4438 C C   . GLY D  1 108 ? -74.110 39.201  14.764  1.00 34.03 ? 108 GLY D C   1 
ATOM   4439 O O   . GLY D  1 108 ? -74.692 38.124  14.922  1.00 34.01 ? 108 GLY D O   1 
ATOM   4440 N N   . ALA D  1 109 ? -73.211 39.660  15.638  1.00 34.31 ? 109 ALA D N   1 
ATOM   4441 C CA  . ALA D  1 109 ? -72.868 38.903  16.834  1.00 34.48 ? 109 ALA D CA  1 
ATOM   4442 C C   . ALA D  1 109 ? -73.984 38.911  17.865  1.00 33.98 ? 109 ALA D C   1 
ATOM   4443 O O   . ALA D  1 109 ? -73.970 38.077  18.773  1.00 34.75 ? 109 ALA D O   1 
ATOM   4444 C CB  . ALA D  1 109 ? -71.589 39.458  17.461  1.00 35.83 ? 109 ALA D CB  1 
ATOM   4445 N N   . LEU D  1 110 ? -74.928 39.849  17.771  1.00 33.98 ? 110 LEU D N   1 
ATOM   4446 C CA  . LEU D  1 110 ? -76.101 39.806  18.637  1.00 33.43 ? 110 LEU D CA  1 
ATOM   4447 C C   . LEU D  1 110 ? -77.103 38.763  18.163  1.00 32.98 ? 110 LEU D C   1 
ATOM   4448 O O   . LEU D  1 110 ? -77.749 38.098  18.981  1.00 33.43 ? 110 LEU D O   1 
ATOM   4449 C CB  . LEU D  1 110 ? -76.759 41.184  18.701  1.00 34.14 ? 110 LEU D CB  1 
ATOM   4450 C CG  . LEU D  1 110 ? -76.076 42.212  19.600  1.00 34.46 ? 110 LEU D CG  1 
ATOM   4451 C CD1 . LEU D  1 110 ? -76.783 43.551  19.489  1.00 35.09 ? 110 LEU D CD1 1 
ATOM   4452 C CD2 . LEU D  1 110 ? -76.054 41.724  21.042  1.00 35.09 ? 110 LEU D CD2 1 
ATOM   4453 N N   . GLY D  1 111 ? -77.246 38.619  16.845  1.00 32.84 ? 111 GLY D N   1 
ATOM   4454 C CA  . GLY D  1 111 ? -78.177 37.638  16.311  1.00 32.86 ? 111 GLY D CA  1 
ATOM   4455 C C   . GLY D  1 111 ? -77.772 36.216  16.643  1.00 32.70 ? 111 GLY D C   1 
ATOM   4456 O O   . GLY D  1 111 ? -78.600 35.405  17.066  1.00 32.84 ? 111 GLY D O   1 
ATOM   4457 N N   . ASN D  1 112 ? -76.489 35.894  16.459  1.00 32.71 ? 112 ASN D N   1 
ATOM   4458 C CA  . ASN D  1 112 ? -75.998 34.584  16.869  1.00 33.11 ? 112 ASN D CA  1 
ATOM   4459 C C   . ASN D  1 112 ? -76.121 34.402  18.374  1.00 34.37 ? 112 ASN D C   1 
ATOM   4460 O O   . ASN D  1 112 ? -76.466 33.314  18.849  1.00 36.47 ? 112 ASN D O   1 
ATOM   4461 C CB  . ASN D  1 112 ? -74.548 34.397  16.425  1.00 33.37 ? 112 ASN D CB  1 
ATOM   4462 C CG  . ASN D  1 112 ? -74.420 34.195  14.933  1.00 34.36 ? 112 ASN D CG  1 
ATOM   4463 O OD1 . ASN D  1 112 ? -75.334 33.690  14.281  1.00 33.35 ? 112 ASN D OD1 1 
ATOM   4464 N ND2 . ASN D  1 112 ? -73.278 34.583  14.381  1.00 35.38 ? 112 ASN D ND2 1 
ATOM   4465 N N   . LEU D  1 113 ? -75.837 35.454  19.142  1.00 33.73 ? 113 LEU D N   1 
ATOM   4466 C CA  . LEU D  1 113 ? -76.001 35.377  20.588  1.00 33.45 ? 113 LEU D CA  1 
ATOM   4467 C C   . LEU D  1 113 ? -77.459 35.164  20.972  1.00 33.41 ? 113 LEU D C   1 
ATOM   4468 O O   . LEU D  1 113 ? -77.758 34.387  21.886  1.00 34.20 ? 113 LEU D O   1 
ATOM   4469 C CB  . LEU D  1 113 ? -75.452 36.644  21.232  1.00 35.10 ? 113 LEU D CB  1 
ATOM   4470 C CG  . LEU D  1 113 ? -75.635 36.857  22.726  1.00 37.18 ? 113 LEU D CG  1 
ATOM   4471 C CD1 . LEU D  1 113 ? -74.455 37.659  23.202  1.00 39.63 ? 113 LEU D CD1 1 
ATOM   4472 C CD2 . LEU D  1 113 ? -76.944 37.596  23.012  1.00 36.40 ? 113 LEU D CD2 1 
ATOM   4473 N N   . TYR D  1 114 ? -78.380 35.863  20.302  1.00 33.35 ? 114 TYR D N   1 
ATOM   4474 C CA  . TYR D  1 114 ? -79.796 35.702  20.619  1.00 33.32 ? 114 TYR D CA  1 
ATOM   4475 C C   . TYR D  1 114 ? -80.237 34.263  20.418  1.00 33.77 ? 114 TYR D C   1 
ATOM   4476 O O   . TYR D  1 114 ? -80.981 33.714  21.238  1.00 34.52 ? 114 TYR D O   1 
ATOM   4477 C CB  . TYR D  1 114 ? -80.648 36.638  19.762  1.00 33.38 ? 114 TYR D CB  1 
ATOM   4478 C CG  . TYR D  1 114 ? -82.141 36.379  19.861  1.00 33.55 ? 114 TYR D CG  1 
ATOM   4479 C CD1 . TYR D  1 114 ? -82.907 36.969  20.860  1.00 33.97 ? 114 TYR D CD1 1 
ATOM   4480 C CD2 . TYR D  1 114 ? -82.785 35.552  18.946  1.00 33.81 ? 114 TYR D CD2 1 
ATOM   4481 C CE1 . TYR D  1 114 ? -84.271 36.738  20.949  1.00 34.48 ? 114 TYR D CE1 1 
ATOM   4482 C CE2 . TYR D  1 114 ? -84.144 35.314  19.028  1.00 34.24 ? 114 TYR D CE2 1 
ATOM   4483 C CZ  . TYR D  1 114 ? -84.882 35.909  20.030  1.00 34.85 ? 114 TYR D CZ  1 
ATOM   4484 O OH  . TYR D  1 114 ? -86.234 35.674  20.110  1.00 35.56 ? 114 TYR D OH  1 
ATOM   4485 N N   . ASP D  1 115 ? -79.800 33.638  19.324  1.00 33.70 ? 115 ASP D N   1 
ATOM   4486 C CA  . ASP D  1 115 ? -80.093 32.224  19.133  1.00 34.75 ? 115 ASP D CA  1 
ATOM   4487 C C   . ASP D  1 115 ? -79.537 31.402  20.287  1.00 35.76 ? 115 ASP D C   1 
ATOM   4488 O O   . ASP D  1 115 ? -80.275 30.651  20.931  1.00 36.93 ? 115 ASP D O   1 
ATOM   4489 C CB  . ASP D  1 115 ? -79.534 31.742  17.795  1.00 35.57 ? 115 ASP D CB  1 
ATOM   4490 C CG  . ASP D  1 115 ? -80.426 32.115  16.620  1.00 36.33 ? 115 ASP D CG  1 
ATOM   4491 O OD1 . ASP D  1 115 ? -80.725 33.319  16.453  1.00 35.40 ? 115 ASP D OD1 1 
ATOM   4492 O OD2 . ASP D  1 115 ? -80.827 31.203  15.862  1.00 37.52 ? 115 ASP D OD2 1 
ATOM   4493 N N   . ARG D  1 116 ? -78.254 31.594  20.614  1.00 35.17 ? 116 ARG D N   1 
ATOM   4494 C CA  . ARG D  1 116 ? -77.617 30.781  21.648  1.00 35.76 ? 116 ARG D CA  1 
ATOM   4495 C C   . ARG D  1 116 ? -78.376 30.850  22.968  1.00 36.08 ? 116 ARG D C   1 
ATOM   4496 O O   . ARG D  1 116 ? -78.581 29.825  23.628  1.00 37.82 ? 116 ARG D O   1 
ATOM   4497 C CB  . ARG D  1 116 ? -76.164 31.218  21.841  1.00 36.22 ? 116 ARG D CB  1 
ATOM   4498 C CG  . ARG D  1 116 ? -75.168 30.484  20.948  1.00 37.73 ? 116 ARG D CG  1 
ATOM   4499 C CD  . ARG D  1 116 ? -74.059 31.412  20.469  1.00 38.43 ? 116 ARG D CD  1 
ATOM   4500 N NE  . ARG D  1 116 ? -73.022 30.696  19.736  1.00 38.54 ? 116 ARG D NE  1 
ATOM   4501 C CZ  . ARG D  1 116 ? -72.125 31.275  18.951  1.00 39.70 ? 116 ARG D CZ  1 
ATOM   4502 N NH1 . ARG D  1 116 ? -72.128 32.582  18.744  1.00 38.84 ? 116 ARG D NH1 1 
ATOM   4503 N NH2 . ARG D  1 116 ? -71.203 30.524  18.355  1.00 41.52 ? 116 ARG D NH2 1 
ATOM   4504 N N   . MET D  1 117 ? -78.817 32.045  23.363  1.00 35.03 ? 117 MET D N   1 
ATOM   4505 C CA  . MET D  1 117 ? -79.584 32.165  24.599  1.00 35.31 ? 117 MET D CA  1 
ATOM   4506 C C   . MET D  1 117 ? -80.968 31.544  24.461  1.00 35.88 ? 117 MET D C   1 
ATOM   4507 O O   . MET D  1 117 ? -81.423 30.831  25.361  1.00 37.72 ? 117 MET D O   1 
ATOM   4508 C CB  . MET D  1 117 ? -79.699 33.629  25.008  1.00 35.32 ? 117 MET D CB  1 
ATOM   4509 C CG  . MET D  1 117 ? -78.373 34.324  25.184  1.00 36.19 ? 117 MET D CG  1 
ATOM   4510 S SD  . MET D  1 117 ? -78.600 35.982  25.842  1.00 38.55 ? 117 MET D SD  1 
ATOM   4511 C CE  . MET D  1 117 ? -79.944 36.563  24.804  1.00 35.30 ? 117 MET D CE  1 
ATOM   4512 N N   . VAL D  1 118 ? -81.653 31.802  23.345  1.00 35.86 ? 118 VAL D N   1 
ATOM   4513 C CA  . VAL D  1 118 ? -83.025 31.320  23.184  1.00 36.24 ? 118 VAL D CA  1 
ATOM   4514 C C   . VAL D  1 118 ? -83.047 29.816  22.928  1.00 36.15 ? 118 VAL D C   1 
ATOM   4515 O O   . VAL D  1 118 ? -83.746 29.065  23.618  1.00 35.82 ? 118 VAL D O   1 
ATOM   4516 C CB  . VAL D  1 118 ? -83.740 32.097  22.063  1.00 35.22 ? 118 VAL D CB  1 
ATOM   4517 C CG1 . VAL D  1 118 ? -85.082 31.453  21.744  1.00 36.45 ? 118 VAL D CG1 1 
ATOM   4518 C CG2 . VAL D  1 118 ? -83.936 33.546  22.472  1.00 34.46 ? 118 VAL D CG2 1 
ATOM   4519 N N   . LEU D  1 119 ? -82.300 29.357  21.928  1.00 36.69 ? 119 LEU D N   1 
ATOM   4520 C CA  . LEU D  1 119 ? -82.209 27.941  21.590  1.00 37.55 ? 119 LEU D CA  1 
ATOM   4521 C C   . LEU D  1 119 ? -80.736 27.557  21.576  1.00 38.27 ? 119 LEU D C   1 
ATOM   4522 O O   . LEU D  1 119 ? -79.951 28.147  20.832  1.00 39.13 ? 119 LEU D O   1 
ATOM   4523 C CB  . LEU D  1 119 ? -82.874 27.658  20.238  1.00 37.29 ? 119 LEU D CB  1 
ATOM   4524 C CG  . LEU D  1 119 ? -82.762 28.812  19.241  1.00 36.22 ? 119 LEU D CG  1 
ATOM   4525 C CD1 . LEU D  1 119 ? -81.962 28.409  18.012  1.00 36.40 ? 119 LEU D CD1 1 
ATOM   4526 C CD2 . LEU D  1 119 ? -84.150 29.277  18.856  1.00 37.04 ? 119 LEU D CD2 1 
ATOM   4527 N N   . GLY D  1 120 ? -80.372 26.544  22.361  1.00 37.01 ? 120 GLY D N   1 
ATOM   4528 C CA  . GLY D  1 120 ? -78.980 26.209  22.630  1.00 37.71 ? 120 GLY D CA  1 
ATOM   4529 C C   . GLY D  1 120 ? -78.008 26.276  21.462  1.00 39.44 ? 120 GLY D C   1 
ATOM   4530 O O   . GLY D  1 120 ? -76.818 26.545  21.655  1.00 39.38 ? 120 GLY D O   1 
ATOM   4531 N N   . HIS D  1 121 ? -78.504 26.059  20.248  1.00 40.21 ? 121 HIS D N   1 
ATOM   4532 C CA  . HIS D  1 121 ? -77.697 26.030  19.035  1.00 39.53 ? 121 HIS D CA  1 
ATOM   4533 C C   . HIS D  1 121 ? -77.828 27.325  18.229  1.00 38.83 ? 121 HIS D C   1 
ATOM   4534 O O   . HIS D  1 121 ? -78.602 28.230  18.554  1.00 38.30 ? 121 HIS D O   1 
ATOM   4535 C CB  . HIS D  1 121 ? -78.111 24.836  18.175  1.00 38.48 ? 121 HIS D CB  1 
ATOM   4536 C CG  . HIS D  1 121 ? -79.593 24.699  18.040  1.00 38.67 ? 121 HIS D CG  1 
ATOM   4537 N ND1 . HIS D  1 121 ? -80.351 23.950  18.913  1.00 40.57 ? 121 HIS D ND1 1 
ATOM   4538 C CD2 . HIS D  1 121 ? -80.465 25.253  17.163  1.00 39.04 ? 121 HIS D CD2 1 
ATOM   4539 C CE1 . HIS D  1 121 ? -81.623 24.030  18.566  1.00 40.54 ? 121 HIS D CE1 1 
ATOM   4540 N NE2 . HIS D  1 121 ? -81.720 24.814  17.508  1.00 39.62 ? 121 HIS D NE2 1 
ATOM   4541 N N   . VAL D  1 122 ? -77.049 27.398  17.151  1.00 39.04 ? 122 VAL D N   1 
ATOM   4542 C CA  . VAL D  1 122 ? -77.146 28.477  16.175  1.00 37.00 ? 122 VAL D CA  1 
ATOM   4543 C C   . VAL D  1 122 ? -77.667 27.904  14.864  1.00 36.25 ? 122 VAL D C   1 
ATOM   4544 O O   . VAL D  1 122 ? -77.302 26.789  14.473  1.00 37.31 ? 122 VAL D O   1 
ATOM   4545 C CB  . VAL D  1 122 ? -75.796 29.191  15.967  1.00 36.41 ? 122 VAL D CB  1 
ATOM   4546 C CG1 . VAL D  1 122 ? -76.004 30.454  15.145  1.00 36.26 ? 122 VAL D CG1 1 
ATOM   4547 C CG2 . VAL D  1 122 ? -75.151 29.515  17.304  1.00 36.82 ? 122 VAL D CG2 1 
ATOM   4548 N N   . VAL D  1 123 ? -78.513 28.670  14.183  1.00 34.37 ? 123 VAL D N   1 
ATOM   4549 C CA  . VAL D  1 123 ? -79.193 28.213  12.978  1.00 33.97 ? 123 VAL D CA  1 
ATOM   4550 C C   . VAL D  1 123 ? -78.502 28.794  11.749  1.00 33.78 ? 123 VAL D C   1 
ATOM   4551 O O   . VAL D  1 123 ? -78.314 30.013  11.648  1.00 34.08 ? 123 VAL D O   1 
ATOM   4552 C CB  . VAL D  1 123 ? -80.680 28.598  13.011  1.00 34.58 ? 123 VAL D CB  1 
ATOM   4553 C CG1 . VAL D  1 123 ? -81.404 27.990  11.826  1.00 35.21 ? 123 VAL D CG1 1 
ATOM   4554 C CG2 . VAL D  1 123 ? -81.302 28.146  14.326  1.00 35.96 ? 123 VAL D CG2 1 
ATOM   4555 N N   . ASP D  1 124 ? -78.135 27.919  10.812  1.00 33.01 ? 124 ASP D N   1 
ATOM   4556 C CA  . ASP D  1 124 ? -77.530 28.289  9.541   1.00 32.59 ? 124 ASP D CA  1 
ATOM   4557 C C   . ASP D  1 124 ? -78.343 27.700  8.396   1.00 32.51 ? 124 ASP D C   1 
ATOM   4558 O O   . ASP D  1 124 ? -79.035 26.690  8.566   1.00 33.04 ? 124 ASP D O   1 
ATOM   4559 C CB  . ASP D  1 124 ? -76.095 27.782  9.433   1.00 33.50 ? 124 ASP D CB  1 
ATOM   4560 C CG  . ASP D  1 124 ? -75.316 27.926  10.726  1.00 34.63 ? 124 ASP D CG  1 
ATOM   4561 O OD1 . ASP D  1 124 ? -75.454 28.961  11.413  1.00 33.94 ? 124 ASP D OD1 1 
ATOM   4562 O OD2 . ASP D  1 124 ? -74.569 26.981  11.059  1.00 36.29 ? 124 ASP D OD2 1 
ATOM   4563 N N   . PHE D  1 125 ? -78.260 28.345  7.222   1.00 32.24 ? 125 PHE D N   1 
ATOM   4564 C CA  . PHE D  1 125 ? -78.998 27.883  6.052   1.00 32.44 ? 125 PHE D CA  1 
ATOM   4565 C C   . PHE D  1 125 ? -78.268 28.014  4.718   1.00 32.55 ? 125 PHE D C   1 
ATOM   4566 O O   . PHE D  1 125 ? -78.802 27.552  3.705   1.00 32.83 ? 125 PHE D O   1 
ATOM   4567 C CB  . PHE D  1 125 ? -80.355 28.611  5.953   1.00 32.57 ? 125 PHE D CB  1 
ATOM   4568 C CG  . PHE D  1 125 ? -80.284 30.097  6.194   1.00 32.29 ? 125 PHE D CG  1 
ATOM   4569 C CD1 . PHE D  1 125 ? -80.034 30.973  5.152   1.00 32.37 ? 125 PHE D CD1 1 
ATOM   4570 C CD2 . PHE D  1 125 ? -80.500 30.619  7.459   1.00 32.44 ? 125 PHE D CD2 1 
ATOM   4571 C CE1 . PHE D  1 125 ? -79.982 32.336  5.371   1.00 32.53 ? 125 PHE D CE1 1 
ATOM   4572 C CE2 . PHE D  1 125 ? -80.450 31.984  7.683   1.00 32.57 ? 125 PHE D CE2 1 
ATOM   4573 C CZ  . PHE D  1 125 ? -80.188 32.841  6.637   1.00 32.89 ? 125 PHE D CZ  1 
ATOM   4574 N N   . ILE D  1 126 ? -77.074 28.597  4.677   1.00 32.11 ? 126 ILE D N   1 
ATOM   4575 C CA  . ILE D  1 126 ? -76.370 28.877  3.429   1.00 31.34 ? 126 ILE D CA  1 
ATOM   4576 C C   . ILE D  1 126 ? -75.274 27.829  3.256   1.00 32.28 ? 126 ILE D C   1 
ATOM   4577 O O   . ILE D  1 126 ? -74.276 27.837  3.983   1.00 33.45 ? 126 ILE D O   1 
ATOM   4578 C CB  . ILE D  1 126 ? -75.788 30.299  3.423   1.00 31.67 ? 126 ILE D CB  1 
ATOM   4579 C CG1 . ILE D  1 126 ? -76.869 31.333  3.739   1.00 32.04 ? 126 ILE D CG1 1 
ATOM   4580 C CG2 . ILE D  1 126 ? -75.151 30.626  2.084   1.00 30.75 ? 126 ILE D CG2 1 
ATOM   4581 C CD1 . ILE D  1 126 ? -76.356 32.762  3.797   1.00 32.76 ? 126 ILE D CD1 1 
ATOM   4582 N N   . LEU D  1 127 ? -75.442 26.932  2.283   1.00 30.82 ? 127 LEU D N   1 
ATOM   4583 C CA  . LEU D  1 127 ? -74.470 25.875  2.002   1.00 30.06 ? 127 LEU D CA  1 
ATOM   4584 C C   . LEU D  1 127 ? -73.819 26.164  0.654   1.00 31.29 ? 127 LEU D C   1 
ATOM   4585 O O   . LEU D  1 127 ? -74.378 25.842  -0.398  1.00 32.07 ? 127 LEU D O   1 
ATOM   4586 C CB  . LEU D  1 127 ? -75.128 24.495  2.015   1.00 29.22 ? 127 LEU D CB  1 
ATOM   4587 C CG  . LEU D  1 127 ? -74.196 23.313  1.726   1.00 29.22 ? 127 LEU D CG  1 
ATOM   4588 C CD1 . LEU D  1 127 ? -73.052 23.314  2.716   1.00 30.58 ? 127 LEU D CD1 1 
ATOM   4589 C CD2 . LEU D  1 127 ? -74.943 21.986  1.768   1.00 30.38 ? 127 LEU D CD2 1 
ATOM   4590 N N   . VAL D  1 128 ? -72.645 26.784  0.685   1.00 32.01 ? 128 VAL D N   1 
ATOM   4591 C CA  . VAL D  1 128 ? -71.823 26.941  -0.509  1.00 32.79 ? 128 VAL D CA  1 
ATOM   4592 C C   . VAL D  1 128 ? -70.913 25.726  -0.600  1.00 33.22 ? 128 VAL D C   1 
ATOM   4593 O O   . VAL D  1 128 ? -70.066 25.504  0.273   1.00 34.01 ? 128 VAL D O   1 
ATOM   4594 C CB  . VAL D  1 128 ? -71.010 28.244  -0.480  1.00 33.95 ? 128 VAL D CB  1 
ATOM   4595 C CG1 . VAL D  1 128 ? -69.854 28.168  -1.469  1.00 35.54 ? 128 VAL D CG1 1 
ATOM   4596 C CG2 . VAL D  1 128 ? -71.900 29.443  -0.812  1.00 33.30 ? 128 VAL D CG2 1 
ATOM   4597 N N   . HIS D  1 129 ? -71.102 24.927  -1.647  1.00 33.81 ? 129 HIS D N   1 
ATOM   4598 C CA  . HIS D  1 129 ? -70.406 23.654  -1.767  1.00 34.77 ? 129 HIS D CA  1 
ATOM   4599 C C   . HIS D  1 129 ? -69.663 23.553  -3.090  1.00 36.34 ? 129 HIS D C   1 
ATOM   4600 O O   . HIS D  1 129 ? -69.524 24.546  -3.813  1.00 37.19 ? 129 HIS D O   1 
ATOM   4601 C CB  . HIS D  1 129 ? -71.395 22.497  -1.625  1.00 34.37 ? 129 HIS D CB  1 
ATOM   4602 C CG  . HIS D  1 129 ? -72.530 22.555  -2.596  1.00 34.62 ? 129 HIS D CG  1 
ATOM   4603 N ND1 . HIS D  1 129 ? -72.587 21.761  -3.720  1.00 35.59 ? 129 HIS D ND1 1 
ATOM   4604 C CD2 . HIS D  1 129 ? -73.642 23.328  -2.623  1.00 34.40 ? 129 HIS D CD2 1 
ATOM   4605 C CE1 . HIS D  1 129 ? -73.694 22.030  -4.389  1.00 35.32 ? 129 HIS D CE1 1 
ATOM   4606 N NE2 . HIS D  1 129 ? -74.352 22.978  -3.746  1.00 34.71 ? 129 HIS D NE2 1 
ATOM   4607 N N   . TRP D  1 130 ? -69.156 22.362  -3.401  1.00 37.53 ? 130 TRP D N   1 
ATOM   4608 C CA  . TRP D  1 130 ? -68.667 22.115  -4.756  1.00 37.96 ? 130 TRP D CA  1 
ATOM   4609 C C   . TRP D  1 130 ? -68.928 20.646  -5.088  1.00 37.61 ? 130 TRP D C   1 
ATOM   4610 O O   . TRP D  1 130 ? -68.089 19.787  -4.811  1.00 38.49 ? 130 TRP D O   1 
ATOM   4611 C CB  . TRP D  1 130 ? -67.195 22.468  -4.900  1.00 39.78 ? 130 TRP D CB  1 
ATOM   4612 C CG  . TRP D  1 130 ? -66.684 22.190  -6.274  1.00 40.37 ? 130 TRP D CG  1 
ATOM   4613 C CD1 . TRP D  1 130 ? -65.759 21.255  -6.633  1.00 41.50 ? 130 TRP D CD1 1 
ATOM   4614 C CD2 . TRP D  1 130 ? -67.096 22.834  -7.482  1.00 40.15 ? 130 TRP D CD2 1 
ATOM   4615 N NE1 . TRP D  1 130 ? -65.558 21.285  -7.991  1.00 41.47 ? 130 TRP D NE1 1 
ATOM   4616 C CE2 . TRP D  1 130 ? -66.367 22.247  -8.536  1.00 41.07 ? 130 TRP D CE2 1 
ATOM   4617 C CE3 . TRP D  1 130 ? -68.004 23.854  -7.775  1.00 39.27 ? 130 TRP D CE3 1 
ATOM   4618 C CZ2 . TRP D  1 130 ? -66.519 22.645  -9.861  1.00 41.51 ? 130 TRP D CZ2 1 
ATOM   4619 C CZ3 . TRP D  1 130 ? -68.154 24.249  -9.091  1.00 39.65 ? 130 TRP D CZ3 1 
ATOM   4620 C CH2 . TRP D  1 130 ? -67.414 23.645  -10.119 1.00 40.04 ? 130 TRP D CH2 1 
ATOM   4621 N N   . GLN D  1 131 ? -70.094 20.384  -5.696  1.00 36.85 ? 131 GLN D N   1 
ATOM   4622 C CA  . GLN D  1 131 ? -70.448 19.054  -6.182  1.00 37.06 ? 131 GLN D CA  1 
ATOM   4623 C C   . GLN D  1 131 ? -70.277 18.023  -5.064  1.00 37.85 ? 131 GLN D C   1 
ATOM   4624 O O   . GLN D  1 131 ? -71.065 18.003  -4.113  1.00 37.94 ? 131 GLN D O   1 
ATOM   4625 C CB  . GLN D  1 131 ? -69.621 18.716  -7.421  1.00 38.33 ? 131 GLN D CB  1 
ATOM   4626 C CG  . GLN D  1 131 ? -69.811 19.709  -8.566  1.00 38.53 ? 131 GLN D CG  1 
ATOM   4627 C CD  . GLN D  1 131 ? -68.927 19.389  -9.776  1.00 39.75 ? 131 GLN D CD  1 
ATOM   4628 O OE1 . GLN D  1 131 ? -68.014 18.558  -9.698  1.00 40.75 ? 131 GLN D OE1 1 
ATOM   4629 N NE2 . GLN D  1 131 ? -69.200 20.049  -10.899 1.00 39.27 ? 131 GLN D NE2 1 
ATOM   4630 N N   . ASN D  1 132 ? -69.273 17.154  -5.158  1.00 38.77 ? 132 ASN D N   1 
ATOM   4631 C CA  . ASN D  1 132 ? -68.977 16.167  -4.121  1.00 38.13 ? 132 ASN D CA  1 
ATOM   4632 C C   . ASN D  1 132 ? -67.533 16.280  -3.647  1.00 39.15 ? 132 ASN D C   1 
ATOM   4633 O O   . ASN D  1 132 ? -66.881 15.281  -3.340  1.00 39.96 ? 132 ASN D O   1 
ATOM   4634 C CB  . ASN D  1 132 ? -69.257 14.750  -4.620  1.00 38.26 ? 132 ASN D CB  1 
ATOM   4635 C CG  . ASN D  1 132 ? -70.699 14.547  -5.030  1.00 37.48 ? 132 ASN D CG  1 
ATOM   4636 O OD1 . ASN D  1 132 ? -71.610 15.180  -4.486  1.00 37.05 ? 132 ASN D OD1 1 
ATOM   4637 N ND2 . ASN D  1 132 ? -70.916 13.670  -5.997  1.00 35.84 ? 132 ASN D ND2 1 
ATOM   4638 N N   . ARG D  1 133 ? -67.005 17.501  -3.613  1.00 39.29 ? 133 ARG D N   1 
ATOM   4639 C CA  . ARG D  1 133 ? -65.608 17.725  -3.257  1.00 40.77 ? 133 ARG D CA  1 
ATOM   4640 C C   . ARG D  1 133 ? -65.452 18.571  -2.001  1.00 40.59 ? 133 ARG D C   1 
ATOM   4641 O O   . ARG D  1 133 ? -64.795 18.144  -1.045  1.00 40.28 ? 133 ARG D O   1 
ATOM   4642 C CB  . ARG D  1 133 ? -64.876 18.398  -4.427  1.00 43.21 ? 133 ARG D CB  1 
ATOM   4643 C CG  . ARG D  1 133 ? -65.249 17.873  -5.801  1.00 44.28 ? 133 ARG D CG  1 
ATOM   4644 C CD  . ARG D  1 133 ? -64.891 16.406  -5.937  1.00 47.40 ? 133 ARG D CD  1 
ATOM   4645 N NE  . ARG D  1 133 ? -64.854 15.981  -7.330  1.00 50.79 ? 133 ARG D NE  1 
ATOM   4646 C CZ  . ARG D  1 133 ? -63.846 16.224  -8.157  1.00 51.40 ? 133 ARG D CZ  1 
ATOM   4647 N NH1 . ARG D  1 133 ? -62.788 16.923  -7.772  1.00 49.28 ? 133 ARG D NH1 1 
ATOM   4648 N NH2 . ARG D  1 133 ? -63.901 15.757  -9.401  1.00 52.45 ? 133 ARG D NH2 1 
ATOM   4649 N N   . TRP D  1 134 ? -66.036 19.765  -1.977  1.00 40.23 ? 134 TRP D N   1 
ATOM   4650 C CA  . TRP D  1 134 ? -65.737 20.773  -0.971  1.00 39.66 ? 134 TRP D CA  1 
ATOM   4651 C C   . TRP D  1 134 ? -67.039 21.397  -0.496  1.00 39.03 ? 134 TRP D C   1 
ATOM   4652 O O   . TRP D  1 134 ? -67.882 21.778  -1.313  1.00 38.23 ? 134 TRP D O   1 
ATOM   4653 C CB  . TRP D  1 134 ? -64.800 21.832  -1.563  1.00 40.15 ? 134 TRP D CB  1 
ATOM   4654 C CG  . TRP D  1 134 ? -64.431 22.973  -0.664  1.00 40.08 ? 134 TRP D CG  1 
ATOM   4655 C CD1 . TRP D  1 134 ? -63.361 23.041  0.180   1.00 40.51 ? 134 TRP D CD1 1 
ATOM   4656 C CD2 . TRP D  1 134 ? -65.104 24.233  -0.560  1.00 40.48 ? 134 TRP D CD2 1 
ATOM   4657 N NE1 . TRP D  1 134 ? -63.335 24.258  0.818   1.00 39.94 ? 134 TRP D NE1 1 
ATOM   4658 C CE2 . TRP D  1 134 ? -64.395 25.009  0.381   1.00 40.18 ? 134 TRP D CE2 1 
ATOM   4659 C CE3 . TRP D  1 134 ? -66.243 24.775  -1.163  1.00 39.62 ? 134 TRP D CE3 1 
ATOM   4660 C CZ2 . TRP D  1 134 ? -64.788 26.300  0.732   1.00 39.40 ? 134 TRP D CZ2 1 
ATOM   4661 C CZ3 . TRP D  1 134 ? -66.633 26.057  -0.814  1.00 39.40 ? 134 TRP D CZ3 1 
ATOM   4662 C CH2 . TRP D  1 134 ? -65.906 26.806  0.126   1.00 39.05 ? 134 TRP D CH2 1 
ATOM   4663 N N   . TYR D  1 135 ? -67.201 21.499  0.822   1.00 38.84 ? 135 TYR D N   1 
ATOM   4664 C CA  . TYR D  1 135 ? -68.412 22.049  1.424   1.00 37.11 ? 135 TYR D CA  1 
ATOM   4665 C C   . TYR D  1 135 ? -68.017 23.082  2.469   1.00 36.82 ? 135 TYR D C   1 
ATOM   4666 O O   . TYR D  1 135 ? -67.429 22.734  3.498   1.00 37.74 ? 135 TYR D O   1 
ATOM   4667 C CB  . TYR D  1 135 ? -69.268 20.947  2.052   1.00 35.90 ? 135 TYR D CB  1 
ATOM   4668 C CG  . TYR D  1 135 ? -70.184 20.255  1.071   1.00 35.70 ? 135 TYR D CG  1 
ATOM   4669 C CD1 . TYR D  1 135 ? -69.670 19.442  0.072   1.00 36.66 ? 135 TYR D CD1 1 
ATOM   4670 C CD2 . TYR D  1 135 ? -71.561 20.410  1.147   1.00 34.86 ? 135 TYR D CD2 1 
ATOM   4671 C CE1 . TYR D  1 135 ? -70.495 18.805  -0.827  1.00 36.38 ? 135 TYR D CE1 1 
ATOM   4672 C CE2 . TYR D  1 135 ? -72.401 19.774  0.248   1.00 34.94 ? 135 TYR D CE2 1 
ATOM   4673 C CZ  . TYR D  1 135 ? -71.860 18.972  -0.738  1.00 35.38 ? 135 TYR D CZ  1 
ATOM   4674 O OH  . TYR D  1 135 ? -72.684 18.334  -1.637  1.00 35.75 ? 135 TYR D OH  1 
ATOM   4675 N N   . PHE D  1 136 ? -68.325 24.346  2.200   1.00 35.34 ? 136 PHE D N   1 
ATOM   4676 C CA  . PHE D  1 136 ? -68.170 25.373  3.217   1.00 35.39 ? 136 PHE D CA  1 
ATOM   4677 C C   . PHE D  1 136 ? -69.199 25.147  4.323   1.00 35.28 ? 136 PHE D C   1 
ATOM   4678 O O   . PHE D  1 136 ? -70.345 24.789  4.035   1.00 34.67 ? 136 PHE D O   1 
ATOM   4679 C CB  . PHE D  1 136 ? -68.351 26.763  2.608   1.00 36.20 ? 136 PHE D CB  1 
ATOM   4680 C CG  . PHE D  1 136 ? -67.746 27.874  3.421   1.00 36.55 ? 136 PHE D CG  1 
ATOM   4681 C CD1 . PHE D  1 136 ? -66.408 28.196  3.283   1.00 36.77 ? 136 PHE D CD1 1 
ATOM   4682 C CD2 . PHE D  1 136 ? -68.517 28.607  4.311   1.00 36.55 ? 136 PHE D CD2 1 
ATOM   4683 C CE1 . PHE D  1 136 ? -65.846 29.215  4.020   1.00 37.12 ? 136 PHE D CE1 1 
ATOM   4684 C CE2 . PHE D  1 136 ? -67.958 29.631  5.052   1.00 36.43 ? 136 PHE D CE2 1 
ATOM   4685 C CZ  . PHE D  1 136 ? -66.621 29.934  4.905   1.00 37.03 ? 136 PHE D CZ  1 
ATOM   4686 N N   . PRO D  1 137 ? -68.821 25.327  5.588   1.00 36.41 ? 137 PRO D N   1 
ATOM   4687 C CA  . PRO D  1 137 ? -69.795 25.148  6.673   1.00 35.88 ? 137 PRO D CA  1 
ATOM   4688 C C   . PRO D  1 137 ? -70.966 26.108  6.523   1.00 34.96 ? 137 PRO D C   1 
ATOM   4689 O O   . PRO D  1 137 ? -70.794 27.276  6.170   1.00 34.62 ? 137 PRO D O   1 
ATOM   4690 C CB  . PRO D  1 137 ? -68.978 25.443  7.937   1.00 35.91 ? 137 PRO D CB  1 
ATOM   4691 C CG  . PRO D  1 137 ? -67.824 26.265  7.467   1.00 36.54 ? 137 PRO D CG  1 
ATOM   4692 C CD  . PRO D  1 137 ? -67.505 25.752  6.093   1.00 36.76 ? 137 PRO D CD  1 
ATOM   4693 N N   . ALA D  1 138 ? -72.167 25.597  6.786   1.00 34.83 ? 138 ALA D N   1 
ATOM   4694 C CA  . ALA D  1 138 ? -73.369 26.405  6.634   1.00 33.95 ? 138 ALA D CA  1 
ATOM   4695 C C   . ALA D  1 138 ? -73.322 27.603  7.571   1.00 34.52 ? 138 ALA D C   1 
ATOM   4696 O O   . ALA D  1 138 ? -72.886 27.495  8.721   1.00 36.41 ? 138 ALA D O   1 
ATOM   4697 C CB  . ALA D  1 138 ? -74.616 25.562  6.907   1.00 32.58 ? 138 ALA D CB  1 
ATOM   4698 N N   . PHE D  1 139 ? -73.758 28.759  7.070   1.00 33.91 ? 139 PHE D N   1 
ATOM   4699 C CA  . PHE D  1 139 ? -73.775 29.981  7.861   1.00 34.19 ? 139 PHE D CA  1 
ATOM   4700 C C   . PHE D  1 139 ? -75.092 30.710  7.629   1.00 33.05 ? 139 PHE D C   1 
ATOM   4701 O O   . PHE D  1 139 ? -75.933 30.293  6.827   1.00 32.88 ? 139 PHE D O   1 
ATOM   4702 C CB  . PHE D  1 139 ? -72.567 30.879  7.551   1.00 34.84 ? 139 PHE D CB  1 
ATOM   4703 C CG  . PHE D  1 139 ? -72.422 31.250  6.101   1.00 34.71 ? 139 PHE D CG  1 
ATOM   4704 C CD1 . PHE D  1 139 ? -71.746 30.417  5.225   1.00 34.49 ? 139 PHE D CD1 1 
ATOM   4705 C CD2 . PHE D  1 139 ? -72.929 32.449  5.622   1.00 34.18 ? 139 PHE D CD2 1 
ATOM   4706 C CE1 . PHE D  1 139 ? -71.596 30.759  3.897   1.00 34.04 ? 139 PHE D CE1 1 
ATOM   4707 C CE2 . PHE D  1 139 ? -72.781 32.798  4.293   1.00 33.67 ? 139 PHE D CE2 1 
ATOM   4708 C CZ  . PHE D  1 139 ? -72.112 31.951  3.430   1.00 34.01 ? 139 PHE D CZ  1 
ATOM   4709 N N   . ASN D  1 140 ? -75.273 31.800  8.357   1.00 32.48 ? 140 ASN D N   1 
ATOM   4710 C CA  . ASN D  1 140 ? -76.501 32.574  8.357   1.00 32.18 ? 140 ASN D CA  1 
ATOM   4711 C C   . ASN D  1 140 ? -76.220 33.979  7.837   1.00 32.76 ? 140 ASN D C   1 
ATOM   4712 O O   . ASN D  1 140 ? -75.086 34.330  7.503   1.00 33.49 ? 140 ASN D O   1 
ATOM   4713 C CB  . ASN D  1 140 ? -77.100 32.617  9.763   1.00 32.45 ? 140 ASN D CB  1 
ATOM   4714 C CG  . ASN D  1 140 ? -76.047 32.841  10.829  1.00 33.36 ? 140 ASN D CG  1 
ATOM   4715 O OD1 . ASN D  1 140 ? -75.613 33.967  11.059  1.00 33.69 ? 140 ASN D OD1 1 
ATOM   4716 N ND2 . ASN D  1 140 ? -75.622 31.764  11.479  1.00 34.19 ? 140 ASN D ND2 1 
ATOM   4717 N N   . LEU D  1 141 ? -77.276 34.790  7.770   1.00 32.57 ? 141 LEU D N   1 
ATOM   4718 C CA  . LEU D  1 141 ? -77.105 36.177  7.354   1.00 32.26 ? 141 LEU D CA  1 
ATOM   4719 C C   . LEU D  1 141 ? -76.220 36.934  8.334   1.00 32.50 ? 141 LEU D C   1 
ATOM   4720 O O   . LEU D  1 141 ? -75.377 37.740  7.923   1.00 33.11 ? 141 LEU D O   1 
ATOM   4721 C CB  . LEU D  1 141 ? -78.466 36.861  7.213   1.00 33.14 ? 141 LEU D CB  1 
ATOM   4722 C CG  . LEU D  1 141 ? -78.960 37.102  5.781   1.00 33.86 ? 141 LEU D CG  1 
ATOM   4723 C CD1 . LEU D  1 141 ? -79.212 35.792  5.056   1.00 33.29 ? 141 LEU D CD1 1 
ATOM   4724 C CD2 . LEU D  1 141 ? -80.209 37.971  5.771   1.00 35.04 ? 141 LEU D CD2 1 
ATOM   4725 N N   . ALA D  1 142 ? -76.382 36.675  9.635   1.00 32.22 ? 142 ALA D N   1 
ATOM   4726 C CA  . ALA D  1 142 ? -75.580 37.380  10.631  1.00 33.04 ? 142 ALA D CA  1 
ATOM   4727 C C   . ALA D  1 142 ? -74.097 37.049  10.510  1.00 33.03 ? 142 ALA D C   1 
ATOM   4728 O O   . ALA D  1 142 ? -73.251 37.904  10.796  1.00 33.42 ? 142 ALA D O   1 
ATOM   4729 C CB  . ALA D  1 142 ? -76.084 37.061  12.039  1.00 33.05 ? 142 ALA D CB  1 
ATOM   4730 N N   . ASP D  1 143 ? -73.759 35.825  10.095  1.00 32.92 ? 143 ASP D N   1 
ATOM   4731 C CA  . ASP D  1 143 ? -72.355 35.488  9.868   1.00 33.30 ? 143 ASP D CA  1 
ATOM   4732 C C   . ASP D  1 143 ? -71.764 36.335  8.752   1.00 33.07 ? 143 ASP D C   1 
ATOM   4733 O O   . ASP D  1 143 ? -70.607 36.765  8.833   1.00 33.17 ? 143 ASP D O   1 
ATOM   4734 C CB  . ASP D  1 143 ? -72.210 34.003  9.538   1.00 34.82 ? 143 ASP D CB  1 
ATOM   4735 C CG  . ASP D  1 143 ? -72.441 33.116  10.738  1.00 35.64 ? 143 ASP D CG  1 
ATOM   4736 O OD1 . ASP D  1 143 ? -72.697 33.661  11.832  1.00 36.16 ? 143 ASP D OD1 1 
ATOM   4737 O OD2 . ASP D  1 143 ? -72.364 31.879  10.586  1.00 35.78 ? 143 ASP D OD2 1 
ATOM   4738 N N   . SER D  1 144 ? -72.543 36.571  7.693   1.00 33.13 ? 144 SER D N   1 
ATOM   4739 C CA  . SER D  1 144 ? -72.086 37.435  6.613   1.00 33.78 ? 144 SER D CA  1 
ATOM   4740 C C   . SER D  1 144 ? -71.835 38.858  7.097   1.00 34.20 ? 144 SER D C   1 
ATOM   4741 O O   . SER D  1 144 ? -70.966 39.549  6.552   1.00 34.84 ? 144 SER D O   1 
ATOM   4742 C CB  . SER D  1 144 ? -73.107 37.443  5.473   1.00 33.77 ? 144 SER D CB  1 
ATOM   4743 O OG  . SER D  1 144 ? -73.484 36.131  5.100   1.00 32.43 ? 144 SER D OG  1 
ATOM   4744 N N   . ALA D  1 145 ? -72.592 39.324  8.097   1.00 34.86 ? 145 ALA D N   1 
ATOM   4745 C CA  . ALA D  1 145 ? -72.376 40.679  8.600   1.00 33.32 ? 145 ALA D CA  1 
ATOM   4746 C C   . ALA D  1 145 ? -71.119 40.759  9.458   1.00 34.42 ? 145 ALA D C   1 
ATOM   4747 O O   . ALA D  1 145 ? -70.414 41.773  9.441   1.00 35.05 ? 145 ALA D O   1 
ATOM   4748 C CB  . ALA D  1 145 ? -73.599 41.158  9.378   1.00 32.52 ? 145 ALA D CB  1 
ATOM   4749 N N   . ILE D  1 146 ? -70.818 39.700  10.212  1.00 34.56 ? 146 ILE D N   1 
ATOM   4750 C CA  . ILE D  1 146 ? -69.574 39.663  10.976  1.00 34.49 ? 146 ILE D CA  1 
ATOM   4751 C C   . ILE D  1 146 ? -68.375 39.600  10.041  1.00 33.91 ? 146 ILE D C   1 
ATOM   4752 O O   . ILE D  1 146 ? -67.378 40.303  10.240  1.00 33.53 ? 146 ILE D O   1 
ATOM   4753 C CB  . ILE D  1 146 ? -69.587 38.476  11.956  1.00 34.58 ? 146 ILE D CB  1 
ATOM   4754 C CG1 . ILE D  1 146 ? -70.644 38.705  13.039  1.00 35.11 ? 146 ILE D CG1 1 
ATOM   4755 C CG2 . ILE D  1 146 ? -68.207 38.262  12.572  1.00 34.90 ? 146 ILE D CG2 1 
ATOM   4756 C CD1 . ILE D  1 146 ? -70.800 37.556  13.980  1.00 36.72 ? 146 ILE D CD1 1 
ATOM   4757 N N   . THR D  1 147 ? -68.449 38.754  9.010   1.00 34.18 ? 147 THR D N   1 
ATOM   4758 C CA  . THR D  1 147 ? -67.343 38.621  8.066   1.00 33.64 ? 147 THR D CA  1 
ATOM   4759 C C   . THR D  1 147 ? -67.073 39.931  7.336   1.00 33.30 ? 147 THR D C   1 
ATOM   4760 O O   . THR D  1 147 ? -65.938 40.421  7.320   1.00 33.46 ? 147 THR D O   1 
ATOM   4761 C CB  . THR D  1 147 ? -67.646 37.508  7.065   1.00 33.67 ? 147 THR D CB  1 
ATOM   4762 O OG1 . THR D  1 147 ? -67.476 36.239  7.700   1.00 33.33 ? 147 THR D OG1 1 
ATOM   4763 C CG2 . THR D  1 147 ? -66.722 37.598  5.862   1.00 34.02 ? 147 THR D CG2 1 
ATOM   4764 N N   . VAL D  1 148 ? -68.109 40.521  6.735   1.00 33.49 ? 148 VAL D N   1 
ATOM   4765 C CA  . VAL D  1 148 ? -67.928 41.780  6.016   1.00 33.15 ? 148 VAL D CA  1 
ATOM   4766 C C   . VAL D  1 148 ? -67.466 42.873  6.969   1.00 33.53 ? 148 VAL D C   1 
ATOM   4767 O O   . VAL D  1 148 ? -66.571 43.662  6.644   1.00 33.86 ? 148 VAL D O   1 
ATOM   4768 C CB  . VAL D  1 148 ? -69.224 42.174  5.282   1.00 33.82 ? 148 VAL D CB  1 
ATOM   4769 C CG1 . VAL D  1 148 ? -69.145 43.613  4.799   1.00 33.70 ? 148 VAL D CG1 1 
ATOM   4770 C CG2 . VAL D  1 148 ? -69.476 41.234  4.113   1.00 35.21 ? 148 VAL D CG2 1 
ATOM   4771 N N   . GLY D  1 149 ? -68.059 42.929  8.162   1.00 33.87 ? 149 GLY D N   1 
ATOM   4772 C CA  . GLY D  1 149 ? -67.627 43.908  9.144   1.00 34.47 ? 149 GLY D CA  1 
ATOM   4773 C C   . GLY D  1 149 ? -66.176 43.726  9.552   1.00 35.11 ? 149 GLY D C   1 
ATOM   4774 O O   . GLY D  1 149 ? -65.421 44.698  9.647   1.00 36.61 ? 149 GLY D O   1 
ATOM   4775 N N   . ALA D  1 150 ? -65.761 42.478  9.788   1.00 34.25 ? 150 ALA D N   1 
ATOM   4776 C CA  . ALA D  1 150 ? -64.366 42.228  10.133  1.00 32.98 ? 150 ALA D CA  1 
ATOM   4777 C C   . ALA D  1 150 ? -63.448 42.442  8.938   1.00 32.95 ? 150 ALA D C   1 
ATOM   4778 O O   . ALA D  1 150 ? -62.289 42.835  9.111   1.00 33.68 ? 150 ALA D O   1 
ATOM   4779 C CB  . ALA D  1 150 ? -64.203 40.812  10.686  1.00 33.64 ? 150 ALA D CB  1 
ATOM   4780 N N   . VAL D  1 151 ? -63.941 42.183  7.724   1.00 32.56 ? 151 VAL D N   1 
ATOM   4781 C CA  . VAL D  1 151 ? -63.166 42.499  6.528   1.00 31.96 ? 151 VAL D CA  1 
ATOM   4782 C C   . VAL D  1 151 ? -62.922 43.998  6.443   1.00 33.58 ? 151 VAL D C   1 
ATOM   4783 O O   . VAL D  1 151 ? -61.819 44.444  6.106   1.00 33.91 ? 151 VAL D O   1 
ATOM   4784 C CB  . VAL D  1 151 ? -63.875 41.966  5.269   1.00 31.83 ? 151 VAL D CB  1 
ATOM   4785 C CG1 . VAL D  1 151 ? -63.472 42.772  4.038   1.00 32.18 ? 151 VAL D CG1 1 
ATOM   4786 C CG2 . VAL D  1 151 ? -63.551 40.497  5.066   1.00 32.02 ? 151 VAL D CG2 1 
ATOM   4787 N N   . MET D  1 152 ? -63.944 44.799  6.758   1.00 34.50 ? 152 MET D N   1 
ATOM   4788 C CA  . MET D  1 152 ? -63.807 46.251  6.687   1.00 35.25 ? 152 MET D CA  1 
ATOM   4789 C C   . MET D  1 152 ? -62.864 46.780  7.762   1.00 35.87 ? 152 MET D C   1 
ATOM   4790 O O   . MET D  1 152 ? -61.955 47.563  7.468   1.00 37.94 ? 152 MET D O   1 
ATOM   4791 C CB  . MET D  1 152 ? -65.178 46.912  6.807   1.00 35.04 ? 152 MET D CB  1 
ATOM   4792 C CG  . MET D  1 152 ? -66.107 46.630  5.650   1.00 35.93 ? 152 MET D CG  1 
ATOM   4793 S SD  . MET D  1 152 ? -67.790 47.147  6.021   1.00 37.62 ? 152 MET D SD  1 
ATOM   4794 C CE  . MET D  1 152 ? -67.531 48.885  6.377   1.00 40.13 ? 152 MET D CE  1 
ATOM   4795 N N   . LEU D  1 153 ? -63.062 46.361  9.015   1.00 34.79 ? 153 LEU D N   1 
ATOM   4796 C CA  . LEU D  1 153 ? -62.235 46.875  10.105  1.00 34.32 ? 153 LEU D CA  1 
ATOM   4797 C C   . LEU D  1 153 ? -60.764 46.548  9.886   1.00 35.36 ? 153 LEU D C   1 
ATOM   4798 O O   . LEU D  1 153 ? -59.887 47.370  10.177  1.00 37.33 ? 153 LEU D O   1 
ATOM   4799 C CB  . LEU D  1 153 ? -62.715 46.315  11.443  1.00 32.95 ? 153 LEU D CB  1 
ATOM   4800 C CG  . LEU D  1 153 ? -61.884 46.729  12.659  1.00 32.99 ? 153 LEU D CG  1 
ATOM   4801 C CD1 . LEU D  1 153 ? -62.794 47.098  13.810  1.00 32.85 ? 153 LEU D CD1 1 
ATOM   4802 C CD2 . LEU D  1 153 ? -60.921 45.622  13.079  1.00 33.77 ? 153 LEU D CD2 1 
ATOM   4803 N N   . ALA D  1 154 ? -60.473 45.341  9.396   1.00 35.61 ? 154 ALA D N   1 
ATOM   4804 C CA  . ALA D  1 154 ? -59.099 44.995  9.050   1.00 36.33 ? 154 ALA D CA  1 
ATOM   4805 C C   . ALA D  1 154 ? -58.569 45.897  7.941   1.00 38.48 ? 154 ALA D C   1 
ATOM   4806 O O   . ALA D  1 154 ? -57.420 46.351  7.994   1.00 40.26 ? 154 ALA D O   1 
ATOM   4807 C CB  . ALA D  1 154 ? -59.017 43.524  8.639   1.00 34.25 ? 154 ALA D CB  1 
ATOM   4808 N N   . LEU D  1 155 ? -59.401 46.185  6.938   1.00 38.17 ? 155 LEU D N   1 
ATOM   4809 C CA  . LEU D  1 155 ? -58.997 47.012  5.805   1.00 38.79 ? 155 LEU D CA  1 
ATOM   4810 C C   . LEU D  1 155 ? -58.824 48.482  6.162   1.00 41.51 ? 155 LEU D C   1 
ATOM   4811 O O   . LEU D  1 155 ? -58.407 49.257  5.294   1.00 44.21 ? 155 LEU D O   1 
ATOM   4812 C CB  . LEU D  1 155 ? -60.019 46.887  4.672   1.00 37.89 ? 155 LEU D CB  1 
ATOM   4813 C CG  . LEU D  1 155 ? -59.988 45.631  3.799   1.00 38.27 ? 155 LEU D CG  1 
ATOM   4814 C CD1 . LEU D  1 155 ? -61.116 45.667  2.781   1.00 36.45 ? 155 LEU D CD1 1 
ATOM   4815 C CD2 . LEU D  1 155 ? -58.640 45.489  3.106   1.00 38.24 ? 155 LEU D CD2 1 
ATOM   4816 N N   . ASP D  1 156 ? -59.127 48.893  7.392   1.00 42.33 ? 156 ASP D N   1 
ATOM   4817 C CA  . ASP D  1 156 ? -59.196 50.306  7.747   1.00 44.05 ? 156 ASP D CA  1 
ATOM   4818 C C   . ASP D  1 156 ? -57.840 50.901  8.122   1.00 46.09 ? 156 ASP D C   1 
ATOM   4819 O O   . ASP D  1 156 ? -57.791 52.026  8.627   1.00 47.27 ? 156 ASP D O   1 
ATOM   4820 C CB  . ASP D  1 156 ? -60.191 50.504  8.895   1.00 44.03 ? 156 ASP D CB  1 
ATOM   4821 C CG  . ASP D  1 156 ? -60.686 51.933  9.002   1.00 47.18 ? 156 ASP D CG  1 
ATOM   4822 O OD1 . ASP D  1 156 ? -61.477 52.361  8.130   1.00 47.16 ? 156 ASP D OD1 1 
ATOM   4823 O OD2 . ASP D  1 156 ? -60.284 52.626  9.963   1.00 48.64 ? 156 ASP D OD2 1 
ATOM   4824 N N   . MET D  1 157 ? -56.744 50.174  7.897   1.00 47.04 ? 157 MET D N   1 
ATOM   4825 C CA  . MET D  1 157 ? -55.397 50.676  8.156   1.00 47.93 ? 157 MET D CA  1 
ATOM   4826 C C   . MET D  1 157 ? -54.542 50.687  6.892   1.00 48.58 ? 157 MET D C   1 
ATOM   4827 O O   . MET D  1 157 ? -53.315 50.804  6.976   1.00 48.10 ? 157 MET D O   1 
ATOM   4828 C CB  . MET D  1 157 ? -54.728 49.848  9.256   1.00 46.77 ? 157 MET D CB  1 
ATOM   4829 C CG  . MET D  1 157 ? -55.323 48.452  9.404   1.00 46.26 ? 157 MET D CG  1 
ATOM   4830 S SD  . MET D  1 157 ? -56.179 48.128  10.966  1.00 46.78 ? 157 MET D SD  1 
ATOM   4831 C CE  . MET D  1 157 ? -57.124 49.631  11.223  1.00 45.89 ? 157 MET D CE  1 
ATOM   4832 N N   . PHE D  1 158 ? -55.174 50.585  5.715   1.00 50.01 ? 158 PHE D N   1 
ATOM   4833 C CA  . PHE D  1 158 ? -54.475 50.439  4.441   1.00 52.18 ? 158 PHE D CA  1 
ATOM   4834 C C   . PHE D  1 158 ? -54.905 51.482  3.410   1.00 53.47 ? 158 PHE D C   1 
ATOM   4835 O O   . PHE D  1 158 ? -54.675 51.289  2.209   1.00 53.55 ? 158 PHE D O   1 
ATOM   4836 C CB  . PHE D  1 158 ? -54.691 49.033  3.874   1.00 50.39 ? 158 PHE D CB  1 
ATOM   4837 C CG  . PHE D  1 158 ? -53.993 47.949  4.645   1.00 48.71 ? 158 PHE D CG  1 
ATOM   4838 C CD1 . PHE D  1 158 ? -52.867 48.228  5.401   1.00 48.00 ? 158 PHE D CD1 1 
ATOM   4839 C CD2 . PHE D  1 158 ? -54.461 46.646  4.604   1.00 47.32 ? 158 PHE D CD2 1 
ATOM   4840 C CE1 . PHE D  1 158 ? -52.224 47.232  6.105   1.00 47.03 ? 158 PHE D CE1 1 
ATOM   4841 C CE2 . PHE D  1 158 ? -53.821 45.645  5.305   1.00 47.40 ? 158 PHE D CE2 1 
ATOM   4842 C CZ  . PHE D  1 158 ? -52.701 45.938  6.057   1.00 47.86 ? 158 PHE D CZ  1 
ATOM   4843 N N   . ARG D  1 159 ? -55.525 52.577  3.844   1.00 52.87 ? 159 ARG D N   1 
ATOM   4844 C CA  . ARG D  1 159 ? -56.063 53.564  2.910   1.00 53.00 ? 159 ARG D CA  1 
ATOM   4845 C C   . ARG D  1 159 ? -55.507 54.960  3.174   1.00 53.55 ? 159 ARG D C   1 
ATOM   4846 O O   . ARG D  1 159 ? -55.188 55.697  2.240   1.00 52.24 ? 159 ARG D O   1 
ATOM   4847 C CB  . ARG D  1 159 ? -57.589 53.588  2.986   1.00 50.89 ? 159 ARG D CB  1 
ATOM   4848 C CG  . ARG D  1 159 ? -58.242 52.230  2.799   1.00 50.35 ? 159 ARG D CG  1 
ATOM   4849 C CD  . ARG D  1 159 ? -59.746 52.362  2.821   1.00 46.24 ? 159 ARG D CD  1 
ATOM   4850 N NE  . ARG D  1 159 ? -60.213 52.900  4.092   1.00 44.99 ? 159 ARG D NE  1 
ATOM   4851 C CZ  . ARG D  1 159 ? -61.291 53.658  4.228   1.00 45.63 ? 159 ARG D CZ  1 
ATOM   4852 N NH1 . ARG D  1 159 ? -62.020 54.015  3.182   1.00 45.03 ? 159 ARG D NH1 1 
ATOM   4853 N NH2 . ARG D  1 159 ? -61.641 54.077  5.440   1.00 45.81 ? 159 ARG D NH2 1 
HETATM 4854 N N   . MLE E  2 1   ? -48.624 -0.250  17.201  1.00 28.50 ? 201 MLE E N   1 
HETATM 4855 C CN  . MLE E  2 1   ? -48.319 0.463   18.175  1.00 29.49 ? 201 MLE E CN  1 
HETATM 4856 C CA  . MLE E  2 1   ? -47.500 -0.936  16.479  1.00 28.46 ? 201 MLE E CA  1 
HETATM 4857 C CB  . MLE E  2 1   ? -47.627 -2.295  15.797  1.00 28.28 ? 201 MLE E CB  1 
HETATM 4858 C CG  . MLE E  2 1   ? -48.345 -3.391  16.573  1.00 27.56 ? 201 MLE E CG  1 
HETATM 4859 C CD1 . MLE E  2 1   ? -48.071 -4.726  15.907  1.00 26.66 ? 201 MLE E CD1 1 
HETATM 4860 C CD2 . MLE E  2 1   ? -47.924 -3.446  18.028  1.00 27.19 ? 201 MLE E CD2 1 
HETATM 4861 C C   . MLE E  2 1   ? -46.795 0.006   15.449  1.00 28.77 ? 201 MLE E C   1 
HETATM 4862 O O   . MLE E  2 1   ? -45.603 0.361   15.654  1.00 29.65 ? 201 MLE E O   1 
HETATM 4863 N N   . IIL E  2 2   ? -47.513 0.397   14.400  1.00 28.42 ? 202 IIL E N   1 
HETATM 4864 C CA  . IIL E  2 2   ? -46.940 1.157   13.297  1.00 28.76 ? 202 IIL E CA  1 
HETATM 4865 C C   . IIL E  2 2   ? -46.494 2.556   13.736  1.00 29.07 ? 202 IIL E C   1 
HETATM 4866 O O   . IIL E  2 2   ? -46.557 2.882   14.949  1.00 28.85 ? 202 IIL E O   1 
HETATM 4867 C CB  . IIL E  2 2   ? -47.971 1.232   12.180  1.00 27.99 ? 202 IIL E CB  1 
HETATM 4868 C CG2 . IIL E  2 2   ? -49.296 1.652   12.802  1.00 28.47 ? 202 IIL E CG2 1 
HETATM 4869 C CG1 . IIL E  2 2   ? -48.128 -0.163  11.578  1.00 27.76 ? 202 IIL E CG1 1 
HETATM 4870 C CD1 . IIL E  2 2   ? -47.425 -0.242  10.226  1.00 29.27 ? 202 IIL E CD1 1 
ATOM   4871 N N   . SER E  2 3   ? -46.047 3.374   12.786  1.00 28.79 ? 203 SER E N   1 
ATOM   4872 C CA  . SER E  2 3   ? -45.509 4.699   13.101  1.00 29.90 ? 203 SER E CA  1 
ATOM   4873 C C   . SER E  2 3   ? -46.465 5.536   13.944  1.00 30.38 ? 203 SER E C   1 
ATOM   4874 O O   . SER E  2 3   ? -46.063 6.526   14.555  1.00 30.85 ? 203 SER E O   1 
ATOM   4875 C CB  . SER E  2 3   ? -45.169 5.457   11.819  1.00 30.48 ? 203 SER E CB  1 
ATOM   4876 O OG  . SER E  2 3   ? -44.089 4.845   11.141  1.00 30.08 ? 203 SER E OG  1 
HETATM 4877 N N   . ALO E  2 4   ? -47.727 5.783   13.253  1.00 30.40 ? 204 ALO E N   1 
HETATM 4878 C CA  . ALO E  2 4   ? -48.989 6.614   13.539  1.00 30.48 ? 204 ALO E CA  1 
HETATM 4879 C CB  . ALO E  2 4   ? -49.878 6.623   12.185  1.00 30.01 ? 204 ALO E CB  1 
HETATM 4880 C CG2 . ALO E  2 4   ? -50.205 5.201   11.988  1.00 30.09 ? 204 ALO E CG2 1 
HETATM 4881 O OG1 . ALO E  2 4   ? -48.985 7.014   11.104  1.00 30.32 ? 204 ALO E OG1 1 
HETATM 4882 C C   . ALO E  2 4   ? -49.819 6.442   14.944  1.00 30.45 ? 204 ALO E C   1 
HETATM 4883 O O   . ALO E  2 4   ? -50.835 7.306   15.523  1.00 30.14 ? 204 ALO E O   1 
HETATM 4884 O O34 . 5BV E  2 5   ? -51.534 3.012   15.163  1.00 31.22 ? 205 5BV E O34 1 
HETATM 4885 O O35 . 5BV E  2 5   ? -51.366 2.282   17.287  1.00 31.63 ? 205 5BV E O35 1 
HETATM 4886 O O   . 5BV E  2 5   ? -50.073 0.419   15.630  1.00 29.32 ? 205 5BV E O   1 
HETATM 4887 N N   . 5BV E  2 5   ? -49.654 5.039   15.793  1.00 30.79 ? 205 5BV E N   1 
HETATM 4888 C C32 . 5BV E  2 5   ? -49.527 3.657   16.217  1.00 31.05 ? 205 5BV E C32 1 
HETATM 4889 C C33 . 5BV E  2 5   ? -50.889 2.968   16.160  1.00 30.90 ? 205 5BV E C33 1 
HETATM 4890 C C36 . 5BV E  2 5   ? -52.274 1.252   17.015  1.00 31.18 ? 205 5BV E C36 1 
HETATM 4891 C C37 . 5BV E  2 5   ? -53.477 1.353   17.954  1.00 29.92 ? 205 5BV E C37 1 
HETATM 4892 C C38 . 5BV E  2 5   ? -53.859 2.812   18.176  1.00 29.52 ? 205 5BV E C38 1 
HETATM 4893 C C39 . 5BV E  2 5   ? -55.125 2.850   19.024  1.00 30.35 ? 205 5BV E C39 1 
HETATM 4894 C C40 . 5BV E  2 5   ? -55.069 4.005   20.023  1.00 30.86 ? 205 5BV E C40 1 
HETATM 4895 C C41 . 5BV E  2 5   ? -55.456 3.482   21.407  1.00 30.67 ? 205 5BV E C41 1 
HETATM 4896 C C42 . 5BV E  2 5   ? -56.341 4.504   22.118  1.00 28.69 ? 205 5BV E C42 1 
HETATM 4897 C C43 . 5BV E  2 5   ? -51.605 -0.108  17.229  1.00 30.34 ? 205 5BV E C43 1 
HETATM 4898 C C44 . 5BV E  2 5   ? -52.387 -1.175  16.464  1.00 29.58 ? 205 5BV E C44 1 
HETATM 4899 C C   . 5BV E  2 5   ? -50.155 -0.171  16.771  1.00 29.51 ? 205 5BV E C   1 
HETATM 4900 N N   . MLE F  2 1   ? -52.977 34.530  21.925  1.00 34.72 ? 201 MLE F N   1 
HETATM 4901 C CN  . MLE F  2 1   ? -52.646 34.722  20.384  1.00 36.03 ? 201 MLE F CN  1 
HETATM 4902 C CA  . MLE F  2 1   ? -51.745 34.983  22.421  1.00 34.28 ? 201 MLE F CA  1 
HETATM 4903 C CB  . MLE F  2 1   ? -52.275 36.280  23.021  1.00 35.29 ? 201 MLE F CB  1 
HETATM 4904 C CG  . MLE F  2 1   ? -52.759 37.308  22.010  1.00 34.73 ? 201 MLE F CG  1 
HETATM 4905 C CD1 . MLE F  2 1   ? -52.935 38.638  22.713  1.00 33.62 ? 201 MLE F CD1 1 
HETATM 4906 C CD2 . MLE F  2 1   ? -51.789 37.458  20.856  1.00 35.86 ? 201 MLE F CD2 1 
HETATM 4907 C C   . MLE F  2 1   ? -50.942 34.272  23.564  1.00 33.90 ? 201 MLE F C   1 
HETATM 4908 O O   . MLE F  2 1   ? -49.691 34.151  23.452  1.00 34.73 ? 201 MLE F O   1 
HETATM 4909 N N   . IIL F  2 2   ? -51.635 33.819  24.605  1.00 33.05 ? 202 IIL F N   1 
HETATM 4910 C CA  . IIL F  2 2   ? -50.984 33.255  25.781  1.00 33.18 ? 202 IIL F CA  1 
HETATM 4911 C C   . IIL F  2 2   ? -50.314 31.916  25.467  1.00 33.28 ? 202 IIL F C   1 
HETATM 4912 O O   . IIL F  2 2   ? -50.316 31.471  24.291  1.00 33.83 ? 202 IIL F O   1 
HETATM 4913 C CB  . IIL F  2 2   ? -52.006 33.092  26.902  1.00 33.22 ? 202 IIL F CB  1 
HETATM 4914 C CG2 . IIL F  2 2   ? -53.143 32.195  26.423  1.00 34.10 ? 202 IIL F CG2 1 
HETATM 4915 C CG1 . IIL F  2 2   ? -52.557 34.471  27.255  1.00 33.37 ? 202 IIL F CG1 1 
HETATM 4916 C CD1 . IIL F  2 2   ? -52.896 34.526  28.742  1.00 33.28 ? 202 IIL F CD1 1 
ATOM   4917 N N   . SER F  2 3   ? -49.750 31.276  26.489  1.00 33.18 ? 203 SER F N   1 
ATOM   4918 C CA  . SER F  2 3   ? -49.020 30.024  26.310  1.00 32.83 ? 203 SER F CA  1 
ATOM   4919 C C   . SER F  2 3   ? -49.808 29.069  25.443  1.00 33.90 ? 203 SER F C   1 
ATOM   4920 O O   . SER F  2 3   ? -49.143 28.403  24.708  1.00 34.91 ? 203 SER F O   1 
ATOM   4921 C CB  . SER F  2 3   ? -48.510 29.501  27.653  1.00 31.97 ? 203 SER F CB  1 
ATOM   4922 O OG  . SER F  2 3   ? -47.616 30.419  28.249  1.00 32.02 ? 203 SER F OG  1 
HETATM 4923 N N   . ALO F  2 4   ? -51.295 28.588  25.446  1.00 33.55 ? 204 ALO F N   1 
HETATM 4924 C CA  . ALO F  2 4   ? -52.074 27.317  25.273  1.00 34.53 ? 204 ALO F CA  1 
HETATM 4925 C CB  . ALO F  2 4   ? -53.132 27.277  26.373  1.00 37.74 ? 204 ALO F CB  1 
HETATM 4926 C CG2 . ALO F  2 4   ? -53.805 28.644  26.463  1.00 37.66 ? 204 ALO F CG2 1 
HETATM 4927 O OG1 . ALO F  2 4   ? -52.530 26.971  27.600  1.00 37.53 ? 204 ALO F OG1 1 
HETATM 4928 C C   . ALO F  2 4   ? -52.734 27.376  23.896  1.00 34.83 ? 204 ALO F C   1 
HETATM 4929 O O   . ALO F  2 4   ? -52.705 26.000  23.272  1.00 35.01 ? 204 ALO F O   1 
HETATM 4930 O O34 . 5BV F  2 5   ? -53.634 30.529  23.444  1.00 35.07 ? 205 5BV F O34 1 
HETATM 4931 O O35 . 5BV F  2 5   ? -54.136 30.403  21.260  1.00 35.74 ? 205 5BV F O35 1 
HETATM 4932 O O   . 5BV F  2 5   ? -55.108 33.950  22.608  1.00 36.36 ? 205 5BV F O   1 
HETATM 4933 N N   . 5BV F  2 5   ? -53.013 28.309  23.326  1.00 35.35 ? 205 5BV F N   1 
HETATM 4934 C C32 . 5BV F  2 5   ? -52.533 28.961  22.359  1.00 35.21 ? 205 5BV F C32 1 
HETATM 4935 C C33 . 5BV F  2 5   ? -53.352 30.094  22.377  1.00 35.30 ? 205 5BV F C33 1 
HETATM 4936 C C36 . 5BV F  2 5   ? -55.188 31.282  21.541  1.00 36.60 ? 205 5BV F C36 1 
HETATM 4937 C C37 . 5BV F  2 5   ? -56.548 30.622  21.273  1.00 38.53 ? 205 5BV F C37 1 
HETATM 4938 C C38 . 5BV F  2 5   ? -56.596 29.935  19.908  1.00 39.29 ? 205 5BV F C38 1 
HETATM 4939 C C39 . 5BV F  2 5   ? -58.038 29.963  19.399  1.00 42.12 ? 205 5BV F C39 1 
HETATM 4940 C C40 . 5BV F  2 5   ? -58.179 30.994  18.277  1.00 43.43 ? 205 5BV F C40 1 
HETATM 4941 C C41 . 5BV F  2 5   ? -59.399 31.886  18.512  1.00 42.46 ? 205 5BV F C41 1 
HETATM 4942 C C42 . 5BV F  2 5   ? -59.761 32.614  17.217  1.00 40.16 ? 205 5BV F C42 1 
HETATM 4943 C C43 . 5BV F  2 5   ? -55.023 32.567  20.723  1.00 37.02 ? 205 5BV F C43 1 
HETATM 4944 C C44 . 5BV F  2 5   ? -56.347 33.332  20.652  1.00 37.72 ? 205 5BV F C44 1 
HETATM 4945 C C   . 5BV F  2 5   ? -53.887 33.371  21.593  1.00 36.28 ? 205 5BV F C   1 
HETATM 4946 N N   . MLE G  2 1   ? -67.978 34.804  18.196  1.00 43.85 ? 201 MLE G N   1 
HETATM 4947 C CN  . MLE G  2 1   ? -68.363 34.314  19.500  1.00 42.68 ? 201 MLE G CN  1 
HETATM 4948 C CA  . MLE G  2 1   ? -69.058 35.509  17.498  1.00 43.09 ? 201 MLE G CA  1 
HETATM 4949 C CB  . MLE G  2 1   ? -68.585 36.805  16.845  1.00 42.08 ? 201 MLE G CB  1 
HETATM 4950 C CG  . MLE G  2 1   ? -67.822 37.748  17.770  1.00 42.19 ? 201 MLE G CG  1 
HETATM 4951 C CD1 . MLE G  2 1   ? -67.573 39.069  17.071  1.00 40.34 ? 201 MLE G CD1 1 
HETATM 4952 C CD2 . MLE G  2 1   ? -68.563 37.975  19.071  1.00 41.26 ? 201 MLE G CD2 1 
HETATM 4953 C C   . MLE G  2 1   ? -69.771 34.648  16.391  1.00 42.52 ? 201 MLE G C   1 
HETATM 4954 O O   . MLE G  2 1   ? -71.013 34.434  16.497  1.00 42.22 ? 201 MLE G O   1 
HETATM 4955 N N   . IIL G  2 2   ? -69.025 34.174  15.393  1.00 42.11 ? 202 IIL G N   1 
HETATM 4956 C CA  . IIL G  2 2   ? -69.598 33.383  14.307  1.00 40.22 ? 202 IIL G CA  1 
HETATM 4957 C C   . IIL G  2 2   ? -70.173 32.080  14.864  1.00 40.56 ? 202 IIL G C   1 
HETATM 4958 O O   . IIL G  2 2   ? -69.735 31.608  15.946  1.00 41.64 ? 202 IIL G O   1 
HETATM 4959 C CB  . IIL G  2 2   ? -68.550 33.091  13.230  1.00 39.58 ? 202 IIL G CB  1 
HETATM 4960 C CG2 . IIL G  2 2   ? -67.397 32.289  13.830  1.00 41.31 ? 202 IIL G CG2 1 
HETATM 4961 C CG1 . IIL G  2 2   ? -68.017 34.408  12.669  1.00 38.77 ? 202 IIL G CG1 1 
HETATM 4962 C CD1 . IIL G  2 2   ? -68.749 34.750  11.374  1.00 37.50 ? 202 IIL G CD1 1 
ATOM   4963 N N   . SER G  2 3   ? -71.133 31.499  14.148  1.00 40.04 ? 203 SER G N   1 
ATOM   4964 C CA  . SER G  2 3   ? -71.825 30.298  14.611  1.00 39.97 ? 203 SER G CA  1 
ATOM   4965 C C   . SER G  2 3   ? -70.866 29.139  14.869  1.00 41.75 ? 203 SER G C   1 
ATOM   4966 O O   . SER G  2 3   ? -70.978 28.445  15.880  1.00 42.38 ? 203 SER G O   1 
ATOM   4967 C CB  . SER G  2 3   ? -72.891 29.875  13.596  1.00 37.51 ? 203 SER G CB  1 
ATOM   4968 O OG  . SER G  2 3   ? -72.361 29.794  12.284  1.00 37.37 ? 203 SER G OG  1 
HETATM 4969 N N   . ALO G  2 4   ? -69.738 28.984  14.004  1.00 41.29 ? 204 ALO G N   1 
HETATM 4970 C CA  . ALO G  2 4   ? -68.814 27.926  14.370  1.00 42.65 ? 204 ALO G CA  1 
HETATM 4971 C CB  . ALO G  2 4   ? -68.050 27.450  13.136  1.00 42.87 ? 204 ALO G CB  1 
HETATM 4972 C CG2 . ALO G  2 4   ? -67.426 28.660  12.447  1.00 41.81 ? 204 ALO G CG2 1 
HETATM 4973 O OG1 . ALO G  2 4   ? -68.935 26.821  12.251  1.00 42.21 ? 204 ALO G OG1 1 
HETATM 4974 C C   . ALO G  2 4   ? -67.850 28.432  15.445  1.00 42.98 ? 204 ALO G C   1 
HETATM 4975 O O   . ALO G  2 4   ? -67.372 27.374  16.117  1.00 43.83 ? 204 ALO G O   1 
HETATM 4976 O O34 . 5BV G  2 5   ? -65.753 30.843  16.511  1.00 43.77 ? 205 5BV G O34 1 
HETATM 4977 O O35 . 5BV G  2 5   ? -66.514 32.018  18.277  1.00 45.33 ? 205 5BV G O35 1 
HETATM 4978 O O   . 5BV G  2 5   ? -66.397 34.477  16.600  1.00 44.20 ? 205 5BV G O   1 
HETATM 4979 N N   . 5BV G  2 5   ? -68.118 29.623  16.446  1.00 42.50 ? 205 5BV G N   1 
HETATM 4980 C C32 . 5BV G  2 5   ? -67.585 29.845  17.627  1.00 43.14 ? 205 5BV G C32 1 
HETATM 4981 C C33 . 5BV G  2 5   ? -66.532 30.926  17.404  1.00 44.34 ? 205 5BV G C33 1 
HETATM 4982 C C36 . 5BV G  2 5   ? -65.271 32.592  18.559  1.00 45.52 ? 205 5BV G C36 1 
HETATM 4983 C C37 . 5BV G  2 5   ? -64.679 31.963  19.823  1.00 46.13 ? 205 5BV G C37 1 
HETATM 4984 C C38 . 5BV G  2 5   ? -63.270 31.429  19.558  1.00 46.54 ? 205 5BV G C38 1 
HETATM 4985 C C39 . 5BV G  2 5   ? -62.382 31.715  20.770  1.00 47.57 ? 205 5BV G C39 1 
HETATM 4986 C C40 . 5BV G  2 5   ? -61.529 30.495  21.129  1.00 47.46 ? 205 5BV G C40 1 
HETATM 4987 C C41 . 5BV G  2 5   ? -60.463 30.894  22.153  1.00 44.89 ? 205 5BV G C41 1 
HETATM 4988 C C42 . 5BV G  2 5   ? -60.349 29.826  23.240  1.00 41.94 ? 205 5BV G C42 1 
HETATM 4989 C C43 . 5BV G  2 5   ? -65.535 34.076  18.814  1.00 44.41 ? 205 5BV G C43 1 
HETATM 4990 C C44 . 5BV G  2 5   ? -64.258 34.893  18.612  1.00 44.54 ? 205 5BV G C44 1 
HETATM 4991 C C   . 5BV G  2 5   ? -66.616 34.545  17.840  1.00 44.25 ? 205 5BV G C   1 
HETATM 4992 N N   . MLE H  2 1   ? -72.129 0.799   28.597  1.00 43.90 ? 201 MLE H N   1 
HETATM 4993 C CN  . MLE H  2 1   ? -71.935 1.564   27.251  1.00 43.01 ? 201 MLE H CN  1 
HETATM 4994 C CA  . MLE H  2 1   ? -73.531 0.412   28.415  1.00 41.33 ? 201 MLE H CA  1 
HETATM 4995 C CB  . MLE H  2 1   ? -73.787 -1.062  28.712  1.00 40.87 ? 201 MLE H CB  1 
HETATM 4996 C CG  . MLE H  2 1   ? -72.640 -1.988  28.327  1.00 42.09 ? 201 MLE H CG  1 
HETATM 4997 C CD1 . MLE H  2 1   ? -72.149 -2.732  29.552  1.00 42.58 ? 201 MLE H CD1 1 
HETATM 4998 C CD2 . MLE H  2 1   ? -73.056 -2.981  27.261  1.00 40.82 ? 201 MLE H CD2 1 
HETATM 4999 C C   . MLE H  2 1   ? -74.529 1.245   29.289  1.00 39.70 ? 201 MLE H C   1 
HETATM 5000 O O   . MLE H  2 1   ? -75.645 1.571   28.802  1.00 39.34 ? 201 MLE H O   1 
HETATM 5001 N N   . IIL H  2 2   ? -74.136 1.580   30.515  1.00 39.66 ? 202 IIL H N   1 
HETATM 5002 C CA  . IIL H  2 2   ? -74.990 2.340   31.415  1.00 38.46 ? 202 IIL H CA  1 
HETATM 5003 C C   . IIL H  2 2   ? -75.102 3.786   30.922  1.00 38.69 ? 202 IIL H C   1 
HETATM 5004 O O   . IIL H  2 2   ? -74.499 4.162   29.881  1.00 39.52 ? 202 IIL H O   1 
HETATM 5005 C CB  . IIL H  2 2   ? -74.437 2.277   32.838  1.00 38.11 ? 202 IIL H CB  1 
HETATM 5006 C CG2 . IIL H  2 2   ? -72.964 2.679   32.820  1.00 38.88 ? 202 IIL H CG2 1 
HETATM 5007 C CG1 . IIL H  2 2   ? -74.578 0.845   33.357  1.00 37.18 ? 202 IIL H CG1 1 
HETATM 5008 C CD1 . IIL H  2 2   ? -74.048 0.754   34.786  1.00 36.30 ? 202 IIL H CD1 1 
ATOM   5009 N N   . SER H  2 3   ? -75.860 4.601   31.645  1.00 37.59 ? 203 SER H N   1 
ATOM   5010 C CA  . SER H  2 3   ? -76.136 5.966   31.212  1.00 36.87 ? 203 SER H CA  1 
ATOM   5011 C C   . SER H  2 3   ? -74.893 6.853   31.227  1.00 37.76 ? 203 SER H C   1 
ATOM   5012 O O   . SER H  2 3   ? -74.966 7.790   30.495  1.00 38.41 ? 203 SER H O   1 
ATOM   5013 C CB  . SER H  2 3   ? -77.226 6.575   32.088  1.00 36.38 ? 203 SER H CB  1 
ATOM   5014 O OG  . SER H  2 3   ? -77.144 6.076   33.410  1.00 35.74 ? 203 SER H OG  1 
HETATM 5015 N N   . ALO H  2 4   ? -73.808 6.929   32.217  1.00 38.12 ? 204 ALO H N   1 
HETATM 5016 C CA  . ALO H  2 4   ? -72.485 7.502   32.032  1.00 37.98 ? 204 ALO H CA  1 
HETATM 5017 C CB  . ALO H  2 4   ? -71.674 7.414   33.325  1.00 37.72 ? 204 ALO H CB  1 
HETATM 5018 C CG2 . ALO H  2 4   ? -71.309 5.952   33.571  1.00 38.27 ? 204 ALO H CG2 1 
HETATM 5019 O OG1 . ALO H  2 4   ? -72.424 7.905   34.402  1.00 36.78 ? 204 ALO H OG1 1 
HETATM 5020 C C   . ALO H  2 4   ? -71.672 6.619   30.972  1.00 38.32 ? 204 ALO H C   1 
HETATM 5021 O O   . ALO H  2 4   ? -70.377 6.855   31.073  1.00 38.32 ? 204 ALO H O   1 
HETATM 5022 O O34 . 5BV H  2 5   ? -70.222 4.007   30.974  1.00 41.39 ? 205 5BV H O34 1 
HETATM 5023 O O35 . 5BV H  2 5   ? -69.493 3.220   29.012  1.00 42.01 ? 205 5BV H O35 1 
HETATM 5024 O O   . 5BV H  2 5   ? -71.385 0.635   30.771  1.00 44.29 ? 205 5BV H O   1 
HETATM 5025 N N   . 5BV H  2 5   ? -71.813 6.245   29.493  1.00 39.45 ? 205 5BV H N   1 
HETATM 5026 C C32 . 5BV H  2 5   ? -71.331 4.951   29.121  1.00 41.07 ? 205 5BV H C32 1 
HETATM 5027 C C33 . 5BV H  2 5   ? -70.315 4.033   29.793  1.00 41.45 ? 205 5BV H C33 1 
HETATM 5028 C C36 . 5BV H  2 5   ? -68.809 2.249   29.744  1.00 43.98 ? 205 5BV H C36 1 
HETATM 5029 C C37 . 5BV H  2 5   ? -67.334 2.289   29.334  1.00 44.31 ? 205 5BV H C37 1 
HETATM 5030 C C38 . 5BV H  2 5   ? -66.857 3.741   29.316  1.00 43.80 ? 205 5BV H C38 1 
HETATM 5031 C C39 . 5BV H  2 5   ? -65.400 3.816   28.859  1.00 44.35 ? 205 5BV H C39 1 
HETATM 5032 C C40 . 5BV H  2 5   ? -65.311 3.711   27.335  1.00 42.64 ? 205 5BV H C40 1 
HETATM 5033 C C41 . 5BV H  2 5   ? -65.528 5.078   26.686  1.00 39.05 ? 205 5BV H C41 1 
HETATM 5034 C C42 . 5BV H  2 5   ? -65.490 4.930   25.165  1.00 35.58 ? 205 5BV H C42 1 
HETATM 5035 C C43 . 5BV H  2 5   ? -69.413 0.863   29.478  1.00 44.71 ? 205 5BV H C43 1 
HETATM 5036 C C44 . 5BV H  2 5   ? -69.037 -0.088  30.617  1.00 45.06 ? 205 5BV H C44 1 
HETATM 5037 C C   . 5BV H  2 5   ? -70.942 0.926   29.389  1.00 44.35 ? 205 5BV H C   1 
HETATM 5038 C C18 . OLC I  3 .   ? -40.508 -13.128 3.341   1.00 32.56 ? 201 OLC A C18 1 
HETATM 5039 C C10 . OLC I  3 .   ? -42.013 -5.470  -0.335  1.00 39.42 ? 201 OLC A C10 1 
HETATM 5040 C C9  . OLC I  3 .   ? -42.651 -4.284  -0.430  1.00 38.16 ? 201 OLC A C9  1 
HETATM 5041 C C17 . OLC I  3 .   ? -40.949 -11.807 3.932   1.00 32.89 ? 201 OLC A C17 1 
HETATM 5042 C C11 . OLC I  3 .   ? -41.032 -5.748  0.787   1.00 39.96 ? 201 OLC A C11 1 
HETATM 5043 C C8  . OLC I  3 .   ? -42.412 -3.187  0.586   1.00 36.93 ? 201 OLC A C8  1 
HETATM 5044 C C24 . OLC I  3 .   ? -47.661 5.455   8.390   1.00 35.39 ? 201 OLC A C24 1 
HETATM 5045 C C16 . OLC I  3 .   ? -40.632 -10.682 2.970   1.00 34.11 ? 201 OLC A C16 1 
HETATM 5046 C C12 . OLC I  3 .   ? -40.458 -7.141  0.618   1.00 39.30 ? 201 OLC A C12 1 
HETATM 5047 C C7  . OLC I  3 .   ? -43.542 -3.178  1.597   1.00 35.17 ? 201 OLC A C7  1 
HETATM 5048 C C15 . OLC I  3 .   ? -40.825 -9.351  3.665   1.00 33.73 ? 201 OLC A C15 1 
HETATM 5049 C C13 . OLC I  3 .   ? -40.050 -7.724  1.957   1.00 38.01 ? 201 OLC A C13 1 
HETATM 5050 C C6  . OLC I  3 .   ? -43.741 -1.770  2.116   1.00 33.53 ? 201 OLC A C6  1 
HETATM 5051 C C14 . OLC I  3 .   ? -41.259 -8.314  2.652   1.00 36.14 ? 201 OLC A C14 1 
HETATM 5052 C C5  . OLC I  3 .   ? -44.991 -1.698  2.968   1.00 32.03 ? 201 OLC A C5  1 
HETATM 5053 C C4  . OLC I  3 .   ? -45.343 -0.242  3.192   1.00 31.45 ? 201 OLC A C4  1 
HETATM 5054 C C3  . OLC I  3 .   ? -46.301 -0.116  4.356   1.00 32.26 ? 201 OLC A C3  1 
HETATM 5055 C C2  . OLC I  3 .   ? -46.553 1.348   4.650   1.00 33.64 ? 201 OLC A C2  1 
HETATM 5056 C C21 . OLC I  3 .   ? -47.481 3.773   6.582   1.00 35.00 ? 201 OLC A C21 1 
HETATM 5057 C C1  . OLC I  3 .   ? -47.234 1.492   5.999   1.00 33.12 ? 201 OLC A C1  1 
HETATM 5058 C C22 . OLC I  3 .   ? -48.437 4.627   7.387   1.00 36.35 ? 201 OLC A C22 1 
HETATM 5059 O O19 . OLC I  3 .   ? -47.022 0.677   6.880   1.00 31.49 ? 201 OLC A O19 1 
HETATM 5060 O O25 . OLC I  3 .   ? -47.465 4.700   9.565   1.00 33.11 ? 201 OLC A O25 1 
HETATM 5061 O O23 . OLC I  3 .   ? -49.164 5.480   6.530   1.00 39.45 ? 201 OLC A O23 1 
HETATM 5062 O O20 . OLC I  3 .   ? -48.116 2.565   6.233   1.00 34.55 ? 201 OLC A O20 1 
HETATM 5063 C C18 . OLC J  3 .   ? -35.996 -4.516  1.203   1.00 44.86 ? 202 OLC A C18 1 
HETATM 5064 C C10 . OLC J  3 .   ? -33.930 1.350   1.960   1.00 37.99 ? 202 OLC A C10 1 
HETATM 5065 C C9  . OLC J  3 .   ? -32.872 2.169   2.147   1.00 37.67 ? 202 OLC A C9  1 
HETATM 5066 C C17 . OLC J  3 .   ? -34.866 -5.337  1.786   1.00 46.48 ? 202 OLC A C17 1 
HETATM 5067 C C11 . OLC J  3 .   ? -34.095 0.084   2.776   1.00 38.51 ? 202 OLC A C11 1 
HETATM 5068 C C8  . OLC J  3 .   ? -31.801 1.863   3.177   1.00 37.13 ? 202 OLC A C8  1 
HETATM 5069 C C24 . OLC J  3 .   ? -26.345 12.469  -1.208  1.00 41.29 ? 202 OLC A C24 1 
HETATM 5070 C C16 . OLC J  3 .   ? -33.539 -4.691  1.445   1.00 46.41 ? 202 OLC A C16 1 
HETATM 5071 C C12 . OLC J  3 .   ? -33.574 -1.111  2.001   1.00 41.45 ? 202 OLC A C12 1 
HETATM 5072 C C7  . OLC J  3 .   ? -30.731 2.938   3.128   1.00 37.41 ? 202 OLC A C7  1 
HETATM 5073 C C15 . OLC J  3 .   ? -32.775 -4.387  2.717   1.00 42.26 ? 202 OLC A C15 1 
HETATM 5074 C C13 . OLC J  3 .   ? -32.645 -1.926  2.879   1.00 39.47 ? 202 OLC A C13 1 
HETATM 5075 C C6  . OLC J  3 .   ? -30.127 3.015   1.738   1.00 37.34 ? 202 OLC A C6  1 
HETATM 5076 C C14 . OLC J  3 .   ? -33.353 -3.161  3.390   1.00 37.81 ? 202 OLC A C14 1 
HETATM 5077 C C5  . OLC J  3 .   ? -29.604 4.415   1.471   1.00 35.64 ? 202 OLC A C5  1 
HETATM 5078 C C4  . OLC J  3 .   ? -29.883 4.821   0.036   1.00 34.93 ? 202 OLC A C4  1 
HETATM 5079 C C3  . OLC J  3 .   ? -29.968 6.331   -0.085  1.00 34.31 ? 202 OLC A C3  1 
HETATM 5080 C C2  . OLC J  3 .   ? -28.587 6.955   -0.039  1.00 34.42 ? 202 OLC A C2  1 
HETATM 5081 C C21 . OLC J  3 .   ? -27.893 10.658  -0.499  1.00 37.65 ? 202 OLC A C21 1 
HETATM 5082 C C1  . OLC J  3 .   ? -28.663 8.407   -0.471  1.00 36.05 ? 202 OLC A C1  1 
HETATM 5083 C C22 . OLC J  3 .   ? -26.717 11.521  -0.084  1.00 39.56 ? 202 OLC A C22 1 
HETATM 5084 O O19 . OLC J  3 .   ? -29.518 8.750   -1.263  1.00 36.76 ? 202 OLC A O19 1 
HETATM 5085 O O25 . OLC J  3 .   ? -27.216 13.580  -1.224  1.00 40.60 ? 202 OLC A O25 1 
HETATM 5086 O O23 . OLC J  3 .   ? -27.038 12.263  1.072   1.00 39.43 ? 202 OLC A O23 1 
HETATM 5087 O O20 . OLC J  3 .   ? -27.753 9.359   0.037   1.00 37.21 ? 202 OLC A O20 1 
HETATM 5088 C C18 . OLC K  3 .   ? -39.776 -5.152  -3.134  1.00 39.57 ? 203 OLC A C18 1 
HETATM 5089 C C10 . OLC K  3 .   ? -33.516 0.361   -1.415  1.00 41.83 ? 203 OLC A C10 1 
HETATM 5090 C C9  . OLC K  3 .   ? -34.030 1.381   -2.136  1.00 42.06 ? 203 OLC A C9  1 
HETATM 5091 C C17 . OLC K  3 .   ? -38.395 -5.085  -2.518  1.00 39.77 ? 203 OLC A C17 1 
HETATM 5092 C C11 . OLC K  3 .   ? -32.702 -0.737  -2.070  1.00 43.49 ? 203 OLC A C11 1 
HETATM 5093 C C8  . OLC K  3 .   ? -33.816 1.477   -3.633  1.00 40.56 ? 203 OLC A C8  1 
HETATM 5094 C C24 . OLC K  3 .   ? -30.904 12.233  -5.493  1.00 36.78 ? 203 OLC A C24 1 
HETATM 5095 C C16 . OLC K  3 .   ? -37.956 -3.640  -2.427  1.00 40.75 ? 203 OLC A C16 1 
HETATM 5096 C C12 . OLC K  3 .   ? -33.613 -1.848  -2.549  1.00 44.78 ? 203 OLC A C12 1 
HETATM 5097 C C7  . OLC K  3 .   ? -34.263 2.838   -4.120  1.00 37.58 ? 203 OLC A C7  1 
HETATM 5098 C C15 . OLC K  3 .   ? -36.446 -3.583  -2.355  1.00 41.77 ? 203 OLC A C15 1 
HETATM 5099 C C13 . OLC K  3 .   ? -34.603 -2.201  -1.460  1.00 44.52 ? 203 OLC A C13 1 
HETATM 5100 C C6  . OLC K  3 .   ? -33.092 3.526   -4.786  1.00 37.19 ? 203 OLC A C6  1 
HETATM 5101 C C14 . OLC K  3 .   ? -36.008 -2.173  -2.025  1.00 43.06 ? 203 OLC A C14 1 
HETATM 5102 C C5  . OLC K  3 .   ? -33.098 4.996   -4.430  1.00 36.83 ? 203 OLC A C5  1 
HETATM 5103 C C4  . OLC K  3 .   ? -31.744 5.390   -3.884  1.00 36.56 ? 203 OLC A C4  1 
HETATM 5104 C C3  . OLC K  3 .   ? -31.022 6.247   -4.897  1.00 36.44 ? 203 OLC A C3  1 
HETATM 5105 C C2  . OLC K  3 .   ? -30.843 7.639   -4.333  1.00 36.44 ? 203 OLC A C2  1 
HETATM 5106 C C21 . OLC K  3 .   ? -29.576 10.522  -4.287  1.00 38.03 ? 203 OLC A C21 1 
HETATM 5107 C C1  . OLC K  3 .   ? -30.166 8.506   -5.373  1.00 37.65 ? 203 OLC A C1  1 
HETATM 5108 C C22 . OLC K  3 .   ? -29.503 11.754  -5.165  1.00 38.36 ? 203 OLC A C22 1 
HETATM 5109 O O19 . OLC K  3 .   ? -30.519 8.436   -6.534  1.00 38.44 ? 203 OLC A O19 1 
HETATM 5110 O O25 . OLC K  3 .   ? -31.239 11.887  -6.820  1.00 35.79 ? 203 OLC A O25 1 
HETATM 5111 O O23 . OLC K  3 .   ? -28.789 12.771  -4.497  1.00 39.40 ? 203 OLC A O23 1 
HETATM 5112 O O20 . OLC K  3 .   ? -29.134 9.393   -5.008  1.00 37.65 ? 203 OLC A O20 1 
HETATM 5113 C C18 . OLC L  3 .   ? -38.451 -5.635  6.449   1.00 29.78 ? 204 OLC A C18 1 
HETATM 5114 C C10 . OLC L  3 .   ? -37.050 -14.129 4.363   1.00 38.71 ? 204 OLC A C10 1 
HETATM 5115 C C9  . OLC L  3 .   ? -36.458 -15.344 4.427   1.00 39.39 ? 204 OLC A C9  1 
HETATM 5116 C C17 . OLC L  3 .   ? -37.892 -6.584  5.409   1.00 33.89 ? 204 OLC A C17 1 
HETATM 5117 C C11 . OLC L  3 .   ? -37.410 -13.366 5.623   1.00 37.44 ? 204 OLC A C11 1 
HETATM 5118 C C8  . OLC L  3 .   ? -36.128 -15.992 5.758   1.00 40.89 ? 204 OLC A C8  1 
HETATM 5119 C C24 . OLC L  3 .   ? -39.077 -24.930 11.707  1.00 37.49 ? 204 OLC A C24 1 
HETATM 5120 C C16 . OLC L  3 .   ? -36.780 -7.416  6.018   1.00 34.25 ? 204 OLC A C16 1 
HETATM 5121 C C12 . OLC L  3 .   ? -37.552 -11.882 5.344   1.00 35.81 ? 204 OLC A C12 1 
HETATM 5122 C C7  . OLC L  3 .   ? -34.719 -16.557 5.744   1.00 40.04 ? 204 OLC A C7  1 
HETATM 5123 C C15 . OLC L  3 .   ? -36.644 -8.737  5.284   1.00 34.55 ? 204 OLC A C15 1 
HETATM 5124 C C13 . OLC L  3 .   ? -36.227 -11.181 5.579   1.00 36.04 ? 204 OLC A C13 1 
HETATM 5125 C C6  . OLC L  3 .   ? -34.724 -17.980 6.270   1.00 39.66 ? 204 OLC A C6  1 
HETATM 5126 C C14 . OLC L  3 .   ? -36.434 -9.855  6.287   1.00 34.29 ? 204 OLC A C14 1 
HETATM 5127 C C5  . OLC L  3 .   ? -34.583 -18.002 7.780   1.00 38.21 ? 204 OLC A C5  1 
HETATM 5128 C C4  . OLC L  3 .   ? -35.355 -19.178 8.348   1.00 36.33 ? 204 OLC A C4  1 
HETATM 5129 C C3  . OLC L  3 .   ? -34.898 -19.483 9.760   1.00 34.72 ? 204 OLC A C3  1 
HETATM 5130 C C2  . OLC L  3 .   ? -36.078 -19.928 10.600  1.00 35.42 ? 204 OLC A C2  1 
HETATM 5131 C C21 . OLC L  3 .   ? -37.082 -23.480 11.435  1.00 36.47 ? 204 OLC A C21 1 
HETATM 5132 C C1  . OLC L  3 .   ? -36.115 -21.439 10.699  1.00 35.84 ? 204 OLC A C1  1 
HETATM 5133 C C22 . OLC L  3 .   ? -38.068 -24.060 12.430  1.00 37.48 ? 204 OLC A C22 1 
HETATM 5134 O O19 . OLC L  3 .   ? -35.382 -22.102 9.996   1.00 36.39 ? 204 OLC A O19 1 
HETATM 5135 O O25 . OLC L  3 .   ? -39.950 -25.534 12.639  1.00 38.11 ? 204 OLC A O25 1 
HETATM 5136 O O23 . OLC L  3 .   ? -37.387 -24.822 13.402  1.00 38.53 ? 204 OLC A O23 1 
HETATM 5137 O O20 . OLC L  3 .   ? -36.991 -22.080 11.598  1.00 36.44 ? 204 OLC A O20 1 
HETATM 5138 C C18 . OLC M  3 .   ? -28.979 -1.902  18.998  1.00 34.04 ? 205 OLC A C18 1 
HETATM 5139 C C10 . OLC M  3 .   ? -29.027 -11.365 19.048  1.00 39.14 ? 205 OLC A C10 1 
HETATM 5140 C C9  . OLC M  3 .   ? -28.886 -12.625 19.512  1.00 38.35 ? 205 OLC A C9  1 
HETATM 5141 C C17 . OLC M  3 .   ? -29.183 -3.150  18.166  1.00 34.13 ? 205 OLC A C17 1 
HETATM 5142 C C11 . OLC M  3 .   ? -29.404 -10.212 19.957  1.00 40.54 ? 205 OLC A C11 1 
HETATM 5143 C C8  . OLC M  3 .   ? -29.097 -12.970 20.972  1.00 38.42 ? 205 OLC A C8  1 
HETATM 5144 C C24 . OLC M  3 .   ? -31.424 -21.471 17.411  1.00 38.42 ? 205 OLC A C24 1 
HETATM 5145 C C16 . OLC M  3 .   ? -29.568 -4.298  19.075  1.00 36.56 ? 205 OLC A C16 1 
HETATM 5146 C C12 . OLC M  3 .   ? -28.621 -8.979  19.550  1.00 40.08 ? 205 OLC A C12 1 
HETATM 5147 C C7  . OLC M  3 .   ? -30.523 -13.434 21.197  1.00 39.84 ? 205 OLC A C7  1 
HETATM 5148 C C15 . OLC M  3 .   ? -29.727 -5.572  18.269  1.00 35.98 ? 205 OLC A C15 1 
HETATM 5149 C C13 . OLC M  3 .   ? -29.553 -7.800  19.361  1.00 37.84 ? 205 OLC A C13 1 
HETATM 5150 C C6  . OLC M  3 .   ? -30.977 -14.362 20.087  1.00 38.53 ? 205 OLC A C6  1 
HETATM 5151 C C14 . OLC M  3 .   ? -28.776 -6.634  18.782  1.00 36.58 ? 205 OLC A C14 1 
HETATM 5152 C C5  . OLC M  3 .   ? -32.398 -14.004 19.697  1.00 38.03 ? 205 OLC A C5  1 
HETATM 5153 C C4  . OLC M  3 .   ? -32.903 -14.936 18.617  1.00 35.10 ? 205 OLC A C4  1 
HETATM 5154 C C3  . OLC M  3 .   ? -33.404 -16.215 19.247  1.00 35.25 ? 205 OLC A C3  1 
HETATM 5155 C C2  . OLC M  3 .   ? -33.307 -17.329 18.229  1.00 36.03 ? 205 OLC A C2  1 
HETATM 5156 C C21 . OLC M  3 .   ? -32.117 -20.223 19.439  1.00 38.28 ? 205 OLC A C21 1 
HETATM 5157 C C1  . OLC M  3 .   ? -33.746 -18.626 18.870  1.00 36.85 ? 205 OLC A C1  1 
HETATM 5158 C C22 . OLC M  3 .   ? -30.949 -20.842 18.703  1.00 38.57 ? 205 OLC A C22 1 
HETATM 5159 O O19 . OLC M  3 .   ? -34.642 -18.617 19.690  1.00 37.23 ? 205 OLC A O19 1 
HETATM 5160 O O25 . OLC M  3 .   ? -31.087 -20.626 16.333  1.00 37.35 ? 205 OLC A O25 1 
HETATM 5161 O O23 . OLC M  3 .   ? -30.001 -19.839 18.417  1.00 37.13 ? 205 OLC A O23 1 
HETATM 5162 O O20 . OLC M  3 .   ? -33.115 -19.834 18.523  1.00 37.29 ? 205 OLC A O20 1 
HETATM 5163 C C18 . OLC N  3 .   ? -33.153 -7.876  19.486  1.00 33.88 ? 206 OLC A C18 1 
HETATM 5164 C C10 . OLC N  3 .   ? -35.863 -0.812  24.434  1.00 35.15 ? 206 OLC A C10 1 
HETATM 5165 C C9  . OLC N  3 .   ? -36.070 -0.691  25.763  1.00 39.54 ? 206 OLC A C9  1 
HETATM 5166 C C17 . OLC N  3 .   ? -33.104 -6.688  20.424  1.00 33.68 ? 206 OLC A C17 1 
HETATM 5167 C C11 . OLC N  3 .   ? -36.840 -1.601  23.587  1.00 33.37 ? 206 OLC A C11 1 
HETATM 5168 C C8  . OLC N  3 .   ? -37.277 -1.336  26.419  1.00 41.19 ? 206 OLC A C8  1 
HETATM 5169 C C24 . OLC N  3 .   ? -36.679 9.093   29.810  1.00 41.23 ? 206 OLC A C24 1 
HETATM 5170 C C16 . OLC N  3 .   ? -34.472 -6.474  21.037  1.00 33.23 ? 206 OLC A C16 1 
HETATM 5171 C C12 . OLC N  3 .   ? -36.294 -2.985  23.314  1.00 31.35 ? 206 OLC A C12 1 
HETATM 5172 C C7  . OLC N  3 .   ? -36.966 -1.667  27.866  1.00 42.61 ? 206 OLC A C7  1 
HETATM 5173 C C15 . OLC N  3 .   ? -34.599 -5.057  21.556  1.00 32.46 ? 206 OLC A C15 1 
HETATM 5174 C C13 . OLC N  3 .   ? -36.164 -3.163  21.818  1.00 30.74 ? 206 OLC A C13 1 
HETATM 5175 C C6  . OLC N  3 .   ? -37.735 -0.738  28.784  1.00 43.26 ? 206 OLC A C6  1 
HETATM 5176 C C14 . OLC N  3 .   ? -36.051 -4.634  21.493  1.00 30.94 ? 206 OLC A C14 1 
HETATM 5177 C C5  . OLC N  3 .   ? -36.854 -0.305  29.940  1.00 44.10 ? 206 OLC A C5  1 
HETATM 5178 C C4  . OLC N  3 .   ? -37.350 1.004   30.526  1.00 45.45 ? 206 OLC A C4  1 
HETATM 5179 C C3  . OLC N  3 .   ? -36.948 2.159   29.628  1.00 47.10 ? 206 OLC A C3  1 
HETATM 5180 C C2  . OLC N  3 .   ? -37.064 3.489   30.350  1.00 46.04 ? 206 OLC A C2  1 
HETATM 5181 C C21 . OLC N  3 .   ? -37.302 6.898   28.820  1.00 45.84 ? 206 OLC A C21 1 
HETATM 5182 C C1  . OLC N  3 .   ? -37.375 4.581   29.341  1.00 45.61 ? 206 OLC A C1  1 
HETATM 5183 C C22 . OLC N  3 .   ? -36.401 8.114   28.687  1.00 44.76 ? 206 OLC A C22 1 
HETATM 5184 O O19 . OLC N  3 .   ? -38.314 4.434   28.577  1.00 44.67 ? 206 OLC A O19 1 
HETATM 5185 O O25 . OLC N  3 .   ? -37.181 10.301  29.280  1.00 38.99 ? 206 OLC A O25 1 
HETATM 5186 O O23 . OLC N  3 .   ? -35.045 7.727   28.705  1.00 46.20 ? 206 OLC A O23 1 
HETATM 5187 O O20 . OLC N  3 .   ? -36.595 5.760   29.280  1.00 47.42 ? 206 OLC A O20 1 
HETATM 5188 C C18 . OLC O  3 .   ? -80.739 -12.604 42.189  1.00 38.13 ? 201 OLC B C18 1 
HETATM 5189 C C10 . OLC O  3 .   ? -81.322 -5.162  42.876  1.00 48.60 ? 201 OLC B C10 1 
HETATM 5190 C C9  . OLC O  3 .   ? -80.745 -4.027  43.326  1.00 46.72 ? 201 OLC B C9  1 
HETATM 5191 C C17 . OLC O  3 .   ? -82.033 -11.860 41.935  1.00 38.12 ? 201 OLC B C17 1 
HETATM 5192 C C11 . OLC O  3 .   ? -82.103 -5.192  41.576  1.00 47.71 ? 201 OLC B C11 1 
HETATM 5193 C C8  . OLC O  3 .   ? -80.854 -2.729  42.554  1.00 43.06 ? 201 OLC B C8  1 
HETATM 5194 C C24 . OLC O  3 .   ? -73.854 6.152   37.136  1.00 36.70 ? 201 OLC B C24 1 
HETATM 5195 C C16 . OLC O  3 .   ? -81.756 -10.624 41.103  1.00 38.83 ? 201 OLC B C16 1 
HETATM 5196 C C12 . OLC O  3 .   ? -82.849 -6.507  41.439  1.00 45.15 ? 201 OLC B C12 1 
HETATM 5197 C C7  . OLC O  3 .   ? -79.962 -1.690  43.199  1.00 41.74 ? 201 OLC B C7  1 
HETATM 5198 C C15 . OLC O  3 .   ? -83.030 -9.825  40.913  1.00 38.87 ? 201 OLC B C15 1 
HETATM 5199 C C13 . OLC O  3 .   ? -81.941 -7.582  40.876  1.00 40.72 ? 201 OLC B C13 1 
HETATM 5200 C C6  . OLC O  3 .   ? -79.757 -0.537  42.243  1.00 35.90 ? 201 OLC B C6  1 
HETATM 5201 C C14 . OLC O  3 .   ? -82.754 -8.586  40.083  1.00 38.13 ? 201 OLC B C14 1 
HETATM 5202 C C5  . OLC O  3 .   ? -78.449 -0.707  41.503  1.00 35.38 ? 201 OLC B C5  1 
HETATM 5203 C C4  . OLC O  3 .   ? -78.237 0.520   40.647  1.00 35.01 ? 201 OLC B C4  1 
HETATM 5204 C C3  . OLC O  3 .   ? -76.785 0.637   40.247  1.00 34.78 ? 201 OLC B C3  1 
HETATM 5205 C C2  . OLC O  3 .   ? -76.428 2.107   40.204  1.00 36.03 ? 201 OLC B C2  1 
HETATM 5206 C C21 . OLC O  3 .   ? -74.788 3.867   37.321  1.00 35.38 ? 201 OLC B C21 1 
HETATM 5207 C C1  . OLC O  3 .   ? -75.492 2.403   39.050  1.00 36.82 ? 201 OLC B C1  1 
HETATM 5208 C C22 . OLC O  3 .   ? -75.086 5.297   36.922  1.00 36.52 ? 201 OLC B C22 1 
HETATM 5209 O O19 . OLC O  3 .   ? -74.435 1.810   38.951  1.00 36.86 ? 201 OLC B O19 1 
HETATM 5210 O O25 . OLC O  3 .   ? -74.119 7.492   36.782  1.00 35.61 ? 201 OLC B O25 1 
HETATM 5211 O O23 . OLC O  3 .   ? -75.472 5.339   35.567  1.00 37.85 ? 201 OLC B O23 1 
HETATM 5212 O O20 . OLC O  3 .   ? -75.855 3.373   38.096  1.00 35.54 ? 201 OLC B O20 1 
HETATM 5213 C C18 . OLC P  3 .   ? -61.555 -11.340 34.429  1.00 32.95 ? 202 OLC B C18 1 
HETATM 5214 C C10 . OLC P  3 .   ? -66.364 -6.685  39.444  1.00 43.82 ? 202 OLC B C10 1 
HETATM 5215 C C9  . OLC P  3 .   ? -67.634 -6.373  39.781  1.00 41.85 ? 202 OLC B C9  1 
HETATM 5216 C C17 . OLC P  3 .   ? -62.450 -11.417 35.649  1.00 34.75 ? 202 OLC B C17 1 
HETATM 5217 C C11 . OLC P  3 .   ? -65.705 -6.223  38.161  1.00 43.41 ? 202 OLC B C11 1 
HETATM 5218 C C8  . OLC P  3 .   ? -68.518 -5.514  38.902  1.00 40.34 ? 202 OLC B C8  1 
HETATM 5219 C C24 . OLC P  3 .   ? -69.920 6.666   39.280  1.00 34.34 ? 202 OLC B C24 1 
HETATM 5220 C C16 . OLC P  3 .   ? -61.976 -10.443 36.710  1.00 37.86 ? 202 OLC B C16 1 
HETATM 5221 C C12 . OLC P  3 .   ? -64.208 -6.402  38.324  1.00 41.63 ? 202 OLC B C12 1 
HETATM 5222 C C7  . OLC P  3 .   ? -69.102 -4.394  39.741  1.00 38.72 ? 202 OLC B C7  1 
HETATM 5223 C C15 . OLC P  3 .   ? -62.327 -9.025  36.308  1.00 38.59 ? 202 OLC B C15 1 
HETATM 5224 C C13 . OLC P  3 .   ? -63.618 -7.079  37.106  1.00 41.16 ? 202 OLC B C13 1 
HETATM 5225 C C6  . OLC P  3 .   ? -70.267 -3.764  39.008  1.00 37.69 ? 202 OLC B C6  1 
HETATM 5226 C C14 . OLC P  3 .   ? -62.698 -8.207  37.530  1.00 38.91 ? 202 OLC B C14 1 
HETATM 5227 C C5  . OLC P  3 .   ? -70.183 -2.256  39.091  1.00 35.05 ? 202 OLC B C5  1 
HETATM 5228 C C4  . OLC P  3 .   ? -70.567 -1.678  37.747  1.00 34.90 ? 202 OLC B C4  1 
HETATM 5229 C C3  . OLC P  3 .   ? -71.171 -0.303  37.926  1.00 37.28 ? 202 OLC B C3  1 
HETATM 5230 C C2  . OLC P  3 .   ? -70.085 0.723   38.174  1.00 38.56 ? 202 OLC B C2  1 
HETATM 5231 C C21 . OLC P  3 .   ? -69.883 4.241   38.778  1.00 38.50 ? 202 OLC B C21 1 
HETATM 5232 C C1  . OLC P  3 .   ? -70.730 2.049   38.530  1.00 39.61 ? 202 OLC B C1  1 
HETATM 5233 C C22 . OLC P  3 .   ? -70.501 5.573   38.411  1.00 36.06 ? 202 OLC B C22 1 
HETATM 5234 O O19 . OLC P  3 .   ? -71.602 2.085   39.379  1.00 39.64 ? 202 OLC B O19 1 
HETATM 5235 O O25 . OLC P  3 .   ? -70.550 7.887   38.969  1.00 34.62 ? 202 OLC B O25 1 
HETATM 5236 O O23 . OLC P  3 .   ? -70.247 5.863   37.056  1.00 36.01 ? 202 OLC B O23 1 
HETATM 5237 O O20 . OLC P  3 .   ? -70.329 3.238   37.889  1.00 39.37 ? 202 OLC B O20 1 
HETATM 5238 C C18 . OLC Q  3 .   ? -82.535 -6.860  45.802  1.00 54.93 ? 203 OLC B C18 1 
HETATM 5239 C C10 . OLC Q  3 .   ? -86.343 1.039   47.018  1.00 59.22 ? 203 OLC B C10 1 
HETATM 5240 C C9  . OLC Q  3 .   ? -87.226 2.059   47.000  1.00 56.24 ? 203 OLC B C9  1 
HETATM 5241 C C17 . OLC Q  3 .   ? -83.615 -5.852  45.469  1.00 55.07 ? 203 OLC B C17 1 
HETATM 5242 C C11 . OLC Q  3 .   ? -86.733 -0.352  46.564  1.00 60.02 ? 203 OLC B C11 1 
HETATM 5243 C C8  . OLC Q  3 .   ? -88.652 1.870   46.528  1.00 57.90 ? 203 OLC B C8  1 
HETATM 5244 C C24 . OLC Q  3 .   ? -93.589 12.711  46.698  1.00 58.96 ? 203 OLC B C24 1 
HETATM 5245 C C16 . OLC Q  3 .   ? -83.156 -4.464  45.862  1.00 55.32 ? 203 OLC B C16 1 
HETATM 5246 C C12 . OLC Q  3 .   ? -85.530 -1.268  46.662  1.00 59.49 ? 203 OLC B C12 1 
HETATM 5247 C C7  . OLC Q  3 .   ? -89.510 2.977   47.107  1.00 56.12 ? 203 OLC B C7  1 
HETATM 5248 C C15 . OLC Q  3 .   ? -84.031 -3.421  45.199  1.00 55.54 ? 203 OLC B C15 1 
HETATM 5249 C C13 . OLC Q  3 .   ? -84.611 -1.027  45.483  1.00 58.80 ? 203 OLC B C13 1 
HETATM 5250 C C6  . OLC Q  3 .   ? -90.783 3.127   46.300  1.00 56.21 ? 203 OLC B C6  1 
HETATM 5251 C C14 . OLC Q  3 .   ? -83.485 -2.039  45.492  1.00 55.74 ? 203 OLC B C14 1 
HETATM 5252 C C5  . OLC Q  3 .   ? -91.658 4.200   46.913  1.00 56.31 ? 203 OLC B C5  1 
HETATM 5253 C C4  . OLC Q  3 .   ? -92.933 4.323   46.106  1.00 56.50 ? 203 OLC B C4  1 
HETATM 5254 C C3  . OLC Q  3 .   ? -93.694 5.557   46.535  1.00 56.81 ? 203 OLC B C3  1 
HETATM 5255 C C2  . OLC Q  3 .   ? -92.994 6.786   46.001  1.00 57.20 ? 203 OLC B C2  1 
HETATM 5256 C C21 . OLC Q  3 .   ? -93.402 10.273  46.280  1.00 58.49 ? 203 OLC B C21 1 
HETATM 5257 C C1  . OLC Q  3 .   ? -93.360 7.975   46.864  1.00 57.66 ? 203 OLC B C1  1 
HETATM 5258 C C22 . OLC Q  3 .   ? -94.360 11.438  46.423  1.00 58.80 ? 203 OLC B C22 1 
HETATM 5259 O O19 . OLC Q  3 .   ? -93.004 7.995   48.027  1.00 57.68 ? 203 OLC B O19 1 
HETATM 5260 O O25 . OLC Q  3 .   ? -94.115 13.770  45.926  1.00 58.98 ? 203 OLC B O25 1 
HETATM 5261 O O23 . OLC Q  3 .   ? -95.101 11.592  45.236  1.00 58.84 ? 203 OLC B O23 1 
HETATM 5262 O O20 . OLC Q  3 .   ? -94.104 9.048   46.332  1.00 58.11 ? 203 OLC B O20 1 
HETATM 5263 C C18 . OLC R  3 .   ? -84.561 -4.807  36.514  1.00 33.63 ? 204 OLC B C18 1 
HETATM 5264 C C10 . OLC R  3 .   ? -87.193 -13.108 38.599  1.00 41.86 ? 204 OLC B C10 1 
HETATM 5265 C C9  . OLC R  3 .   ? -87.909 -14.195 38.241  1.00 41.84 ? 204 OLC B C9  1 
HETATM 5266 C C17 . OLC R  3 .   ? -84.698 -5.929  37.520  1.00 35.68 ? 204 OLC B C17 1 
HETATM 5267 C C11 . OLC R  3 .   ? -85.742 -12.956 38.191  1.00 40.25 ? 204 OLC B C11 1 
HETATM 5268 C C8  . OLC R  3 .   ? -87.303 -15.310 37.412  1.00 40.69 ? 204 OLC B C8  1 
HETATM 5269 C C24 . OLC R  3 .   ? -83.106 -24.408 32.386  1.00 45.17 ? 204 OLC B C24 1 
HETATM 5270 C C16 . OLC R  3 .   ? -85.774 -6.898  37.071  1.00 35.76 ? 204 OLC B C16 1 
HETATM 5271 C C12 . OLC R  3 .   ? -85.541 -11.639 37.469  1.00 37.64 ? 204 OLC B C12 1 
HETATM 5272 C C7  . OLC R  3 .   ? -88.322 -16.423 37.262  1.00 40.50 ? 204 OLC B C7  1 
HETATM 5273 C C15 . OLC R  3 .   ? -85.889 -8.028  38.074  1.00 36.25 ? 204 OLC B C15 1 
HETATM 5274 C C13 . OLC R  3 .   ? -86.099 -10.491 38.283  1.00 37.65 ? 204 OLC B C13 1 
HETATM 5275 C C6  . OLC R  3 .   ? -88.475 -16.806 35.805  1.00 38.75 ? 204 OLC B C6  1 
HETATM 5276 C C14 . OLC R  3 .   ? -86.323 -9.299  37.374  1.00 36.24 ? 204 OLC B C14 1 
HETATM 5277 C C5  . OLC R  3 .   ? -87.532 -17.940 35.467  1.00 38.83 ? 204 OLC B C5  1 
HETATM 5278 C C4  . OLC R  3 .   ? -87.426 -18.073 33.964  1.00 38.48 ? 204 OLC B C4  1 
HETATM 5279 C C3  . OLC R  3 .   ? -86.122 -18.754 33.602  1.00 40.79 ? 204 OLC B C3  1 
HETATM 5280 C C2  . OLC R  3 .   ? -86.255 -20.259 33.717  1.00 40.95 ? 204 OLC B C2  1 
HETATM 5281 C C21 . OLC R  3 .   ? -84.927 -22.947 31.562  1.00 42.06 ? 204 OLC B C21 1 
HETATM 5282 C C1  . OLC R  3 .   ? -85.517 -20.910 32.563  1.00 42.24 ? 204 OLC B C1  1 
HETATM 5283 C C22 . OLC R  3 .   ? -83.547 -23.490 31.265  1.00 43.52 ? 204 OLC B C22 1 
HETATM 5284 O O19 . OLC R  3 .   ? -85.469 -20.356 31.482  1.00 41.74 ? 204 OLC B O19 1 
HETATM 5285 O O25 . OLC R  3 .   ? -81.758 -24.143 32.706  1.00 46.57 ? 204 OLC B O25 1 
HETATM 5286 O O23 . OLC R  3 .   ? -83.569 -24.188 30.041  1.00 45.22 ? 204 OLC B O23 1 
HETATM 5287 O O20 . OLC R  3 .   ? -84.880 -22.153 32.724  1.00 42.81 ? 204 OLC B O20 1 
HETATM 5288 C C18 . OLC S  3 .   ? -90.643 -1.568  22.632  1.00 36.32 ? 205 OLC B C18 1 
HETATM 5289 C C10 . OLC S  3 .   ? -91.570 -11.207 22.693  1.00 45.11 ? 205 OLC B C10 1 
HETATM 5290 C C9  . OLC S  3 .   ? -91.016 -12.387 22.344  1.00 43.20 ? 205 OLC B C9  1 
HETATM 5291 C C17 . OLC S  3 .   ? -91.180 -2.634  23.565  1.00 35.45 ? 205 OLC B C17 1 
HETATM 5292 C C11 . OLC S  3 .   ? -90.732 -9.965  22.932  1.00 45.45 ? 205 OLC B C11 1 
HETATM 5293 C C8  . OLC S  3 .   ? -89.517 -12.517 22.176  1.00 44.51 ? 205 OLC B C8  1 
HETATM 5294 C C24 . OLC S  3 .   ? -89.968 -20.808 26.250  1.00 38.43 ? 205 OLC B C24 1 
HETATM 5295 C C16 . OLC S  3 .   ? -91.035 -4.001  22.925  1.00 36.79 ? 205 OLC B C16 1 
HETATM 5296 C C12 . OLC S  3 .   ? -91.648 -8.784  23.205  1.00 46.66 ? 205 OLC B C12 1 
HETATM 5297 C C7  . OLC S  3 .   ? -89.043 -13.815 22.798  1.00 42.69 ? 205 OLC B C7  1 
HETATM 5298 C C15 . OLC S  3 .   ? -91.054 -5.085  23.986  1.00 37.68 ? 205 OLC B C15 1 
HETATM 5299 C C13 . OLC S  3 .   ? -90.850 -7.511  23.430  1.00 44.02 ? 205 OLC B C13 1 
HETATM 5300 C C6  . OLC S  3 .   ? -87.650 -13.622 23.359  1.00 40.56 ? 205 OLC B C6  1 
HETATM 5301 C C14 . OLC S  3 .   ? -91.781 -6.314  23.474  1.00 41.89 ? 205 OLC B C14 1 
HETATM 5302 C C5  . OLC S  3 .   ? -87.326 -14.747 24.316  1.00 38.94 ? 205 OLC B C5  1 
HETATM 5303 C C4  . OLC S  3 .   ? -86.726 -15.898 23.544  1.00 38.52 ? 205 OLC B C4  1 
HETATM 5304 C C3  . OLC S  3 .   ? -87.586 -17.127 23.735  1.00 39.86 ? 205 OLC B C3  1 
HETATM 5305 C C2  . OLC S  3 .   ? -86.713 -18.263 24.221  1.00 40.05 ? 205 OLC B C2  1 
HETATM 5306 C C21 . OLC S  3 .   ? -89.133 -20.873 23.937  1.00 41.29 ? 205 OLC B C21 1 
HETATM 5307 C C1  . OLC S  3 .   ? -87.203 -19.567 23.633  1.00 40.07 ? 205 OLC B C1  1 
HETATM 5308 C C22 . OLC S  3 .   ? -90.286 -20.448 24.816  1.00 39.56 ? 205 OLC B C22 1 
HETATM 5309 O O19 . OLC S  3 .   ? -86.419 -20.472 23.422  1.00 40.00 ? 205 OLC B O19 1 
HETATM 5310 O O25 . OLC S  3 .   ? -91.009 -20.373 27.096  1.00 37.89 ? 205 OLC B O25 1 
HETATM 5311 O O23 . OLC S  3 .   ? -90.469 -19.056 24.706  1.00 39.27 ? 205 OLC B O23 1 
HETATM 5312 O O20 . OLC S  3 .   ? -88.567 -19.731 23.337  1.00 40.86 ? 205 OLC B O20 1 
HETATM 5313 C C18 . OLC T  3 .   ? -85.729 -0.726  51.846  1.00 35.27 ? 206 OLC B C18 1 
HETATM 5314 C C10 . OLC T  3 .   ? -79.129 2.269   56.256  1.00 32.76 ? 206 OLC B C10 1 
HETATM 5315 C C9  . OLC T  3 .   ? -77.979 2.828   55.821  1.00 33.68 ? 206 OLC B C9  1 
HETATM 5316 C C17 . OLC T  3 .   ? -84.376 -0.087  52.085  1.00 33.64 ? 206 OLC B C17 1 
HETATM 5317 C C11 . OLC T  3 .   ? -80.475 2.648   55.676  1.00 32.85 ? 206 OLC B C11 1 
HETATM 5318 C C8  . OLC T  3 .   ? -77.945 3.870   54.720  1.00 33.52 ? 206 OLC B C8  1 
HETATM 5319 C C24 . OLC T  3 .   ? -69.477 12.963  56.181  1.00 42.22 ? 206 OLC B C24 1 
HETATM 5320 C C16 . OLC T  3 .   ? -83.489 -1.044  52.852  1.00 31.85 ? 206 OLC B C16 1 
HETATM 5321 C C12 . OLC T  3 .   ? -81.529 1.700   56.213  1.00 31.99 ? 206 OLC B C12 1 
HETATM 5322 C C7  . OLC T  3 .   ? -76.608 4.585   54.768  1.00 32.03 ? 206 OLC B C7  1 
HETATM 5323 C C15 . OLC T  3 .   ? -82.141 -0.400  53.095  1.00 31.78 ? 206 OLC B C15 1 
HETATM 5324 C C13 . OLC T  3 .   ? -81.588 0.456   55.351  1.00 31.76 ? 206 OLC B C13 1 
HETATM 5325 C C6  . OLC T  3 .   ? -76.778 6.025   54.330  1.00 32.50 ? 206 OLC B C6  1 
HETATM 5326 C C14 . OLC T  3 .   ? -82.296 0.765   54.049  1.00 31.59 ? 206 OLC B C14 1 
HETATM 5327 C C5  . OLC T  3 .   ? -75.720 6.890   54.988  1.00 33.04 ? 206 OLC B C5  1 
HETATM 5328 C C4  . OLC T  3 .   ? -75.735 8.272   54.368  1.00 34.26 ? 206 OLC B C4  1 
HETATM 5329 C C3  . OLC T  3 .   ? -74.566 9.101   54.867  1.00 36.04 ? 206 OLC B C3  1 
HETATM 5330 C C2  . OLC T  3 .   ? -73.587 9.329   53.731  1.00 37.89 ? 206 OLC B C2  1 
HETATM 5331 C C21 . OLC T  3 .   ? -71.162 11.250  55.609  1.00 39.90 ? 206 OLC B C21 1 
HETATM 5332 C C1  . OLC T  3 .   ? -72.694 10.531  53.982  1.00 38.64 ? 206 OLC B C1  1 
HETATM 5333 C C22 . OLC T  3 .   ? -70.946 12.604  56.255  1.00 41.64 ? 206 OLC B C22 1 
HETATM 5334 O O19 . OLC T  3 .   ? -72.113 11.051  53.048  1.00 38.21 ? 206 OLC B O19 1 
HETATM 5335 O O25 . OLC T  3 .   ? -69.273 14.231  56.763  1.00 42.68 ? 206 OLC B O25 1 
HETATM 5336 O O23 . OLC T  3 .   ? -71.700 13.593  55.588  1.00 43.43 ? 206 OLC B O23 1 
HETATM 5337 O O20 . OLC T  3 .   ? -72.520 11.055  55.276  1.00 38.87 ? 206 OLC B O20 1 
HETATM 5338 C C18 . OLC U  3 .   ? -91.054 -6.975  39.432  1.00 35.75 ? 207 OLC B C18 1 
HETATM 5339 C C10 . OLC U  3 .   ? -90.794 1.620   38.339  1.00 41.26 ? 207 OLC B C10 1 
HETATM 5340 C C9  . OLC U  3 .   ? -90.934 2.796   38.987  1.00 42.24 ? 207 OLC B C9  1 
HETATM 5341 C C17 . OLC U  3 .   ? -91.458 -5.520  39.304  1.00 37.66 ? 207 OLC B C17 1 
HETATM 5342 C C11 . OLC U  3 .   ? -91.905 0.590   38.319  1.00 42.37 ? 207 OLC B C11 1 
HETATM 5343 C C8  . OLC U  3 .   ? -92.212 3.144   39.725  1.00 44.27 ? 207 OLC B C8  1 
HETATM 5344 C C24 . OLC U  3 .   ? -96.207 13.497  42.716  1.00 48.49 ? 207 OLC B C24 1 
HETATM 5345 C C16 . OLC U  3 .   ? -90.281 -4.614  39.608  1.00 36.99 ? 207 OLC B C16 1 
HETATM 5346 C C12 . OLC U  3 .   ? -91.677 -0.435  39.413  1.00 42.83 ? 207 OLC B C12 1 
HETATM 5347 C C7  . OLC U  3 .   ? -92.062 2.824   41.199  1.00 46.54 ? 207 OLC B C7  1 
HETATM 5348 C C15 . OLC U  3 .   ? -90.726 -3.474  40.500  1.00 36.60 ? 207 OLC B C15 1 
HETATM 5349 C C13 . OLC U  3 .   ? -90.814 -1.571  38.906  1.00 40.49 ? 207 OLC B C13 1 
HETATM 5350 C C6  . OLC U  3 .   ? -92.467 4.021   42.035  1.00 46.57 ? 207 OLC B C6  1 
HETATM 5351 C C14 . OLC U  3 .   ? -90.058 -2.186  40.066  1.00 37.90 ? 207 OLC B C14 1 
HETATM 5352 C C5  . OLC U  3 .   ? -93.970 4.196   42.004  1.00 46.01 ? 207 OLC B C5  1 
HETATM 5353 C C4  . OLC U  3 .   ? -94.344 5.467   42.740  1.00 47.02 ? 207 OLC B C4  1 
HETATM 5354 C C3  . OLC U  3 .   ? -93.970 6.672   41.904  1.00 44.58 ? 207 OLC B C3  1 
HETATM 5355 C C2  . OLC U  3 .   ? -94.122 7.931   42.730  1.00 47.13 ? 207 OLC B C2  1 
HETATM 5356 C C21 . OLC U  3 .   ? -95.287 11.339  41.911  1.00 48.16 ? 207 OLC B C21 1 
HETATM 5357 C C1  . OLC U  3 .   ? -94.696 9.037   41.869  1.00 47.19 ? 207 OLC B C1  1 
HETATM 5358 C C22 . OLC U  3 .   ? -96.544 12.165  42.082  1.00 48.43 ? 207 OLC B C22 1 
HETATM 5359 O O19 . OLC U  3 .   ? -94.484 9.038   40.671  1.00 45.06 ? 207 OLC B O19 1 
HETATM 5360 O O25 . OLC U  3 .   ? -96.360 14.526  41.762  1.00 46.34 ? 207 OLC B O25 1 
HETATM 5361 O O23 . OLC U  3 .   ? -97.124 12.388  40.819  1.00 48.24 ? 207 OLC B O23 1 
HETATM 5362 O O20 . OLC U  3 .   ? -95.480 10.052  42.455  1.00 49.09 ? 207 OLC B O20 1 
HETATM 5363 C C18 . OLC V  3 .   ? -48.475 46.305  42.167  1.00 38.39 ? 201 OLC C C18 1 
HETATM 5364 C C10 . OLC V  3 .   ? -44.087 38.776  45.270  1.00 40.35 ? 201 OLC C C10 1 
HETATM 5365 C C9  . OLC V  3 .   ? -43.524 37.571  45.496  1.00 39.25 ? 201 OLC C C9  1 
HETATM 5366 C C17 . OLC V  3 .   ? -47.059 45.786  42.296  1.00 42.21 ? 201 OLC C C17 1 
HETATM 5367 C C11 . OLC V  3 .   ? -43.685 39.604  44.066  1.00 41.26 ? 201 OLC C C11 1 
HETATM 5368 C C8  . OLC V  3 .   ? -42.480 37.019  44.549  1.00 39.43 ? 201 OLC C C8  1 
HETATM 5369 C C24 . OLC V  3 .   ? -37.516 26.617  49.497  1.00 44.31 ? 201 OLC C C24 1 
HETATM 5370 C C16 . OLC V  3 .   ? -47.026 44.302  41.990  1.00 44.66 ? 201 OLC C C16 1 
HETATM 5371 C C12 . OLC V  3 .   ? -44.893 40.346  43.535  1.00 43.39 ? 201 OLC C C12 1 
HETATM 5372 C C7  . OLC V  3 .   ? -42.131 35.603  44.955  1.00 39.82 ? 201 OLC C C7  1 
HETATM 5373 C C15 . OLC V  3 .   ? -45.695 43.714  42.416  1.00 45.50 ? 201 OLC C C15 1 
HETATM 5374 C C13 . OLC V  3 .   ? -44.461 41.582  42.771  1.00 45.03 ? 201 OLC C C13 1 
HETATM 5375 C C6  . OLC V  3 .   ? -40.734 35.559  45.538  1.00 40.21 ? 201 OLC C C6  1 
HETATM 5376 C C14 . OLC V  3 .   ? -45.671 42.227  42.124  1.00 45.75 ? 201 OLC C C14 1 
HETATM 5377 C C5  . OLC V  3 .   ? -40.688 34.536  46.654  1.00 37.93 ? 201 OLC C C5  1 
HETATM 5378 C C4  . OLC V  3 .   ? -39.393 33.753  46.602  1.00 37.76 ? 201 OLC C C4  1 
HETATM 5379 C C3  . OLC V  3 .   ? -39.675 32.318  46.996  1.00 36.87 ? 201 OLC C C3  1 
HETATM 5380 C C2  . OLC V  3 .   ? -38.380 31.556  47.178  1.00 37.25 ? 201 OLC C C2  1 
HETATM 5381 C C21 . OLC V  3 .   ? -38.983 28.003  48.059  1.00 40.14 ? 201 OLC C C21 1 
HETATM 5382 C C1  . OLC V  3 .   ? -38.630 30.075  46.972  1.00 39.08 ? 201 OLC C C1  1 
HETATM 5383 C C22 . OLC V  3 .   ? -38.138 26.748  48.123  1.00 42.78 ? 201 OLC C C22 1 
HETATM 5384 O O19 . OLC V  3 .   ? -39.247 29.699  45.994  1.00 38.16 ? 201 OLC C O19 1 
HETATM 5385 O O25 . OLC V  3 .   ? -36.118 26.781  49.398  1.00 45.98 ? 201 OLC C O25 1 
HETATM 5386 O O23 . OLC V  3 .   ? -38.935 25.617  47.841  1.00 40.29 ? 201 OLC C O23 1 
HETATM 5387 O O20 . OLC V  3 .   ? -38.149 29.130  47.898  1.00 41.23 ? 201 OLC C O20 1 
HETATM 5388 C C18 . OLC W  3 .   ? -41.733 47.055  21.158  1.00 59.21 ? 202 OLC C C18 1 
HETATM 5389 C C10 . OLC W  3 .   ? -39.190 41.059  20.462  1.00 58.80 ? 202 OLC C C10 1 
HETATM 5390 C C9  . OLC W  3 .   ? -39.833 39.965  20.009  1.00 58.67 ? 202 OLC C C9  1 
HETATM 5391 C C17 . OLC W  3 .   ? -40.712 46.342  22.018  1.00 59.28 ? 202 OLC C C17 1 
HETATM 5392 C C11 . OLC W  3 .   ? -38.454 41.976  19.513  1.00 58.96 ? 202 OLC C C11 1 
HETATM 5393 C C8  . OLC W  3 .   ? -39.838 39.613  18.537  1.00 58.55 ? 202 OLC C C8  1 
HETATM 5394 C C24 . OLC W  3 .   ? -31.770 31.516  15.613  1.00 56.62 ? 202 OLC C C24 1 
HETATM 5395 C C16 . OLC W  3 .   ? -39.314 46.727  21.583  1.00 59.35 ? 202 OLC C C16 1 
HETATM 5396 C C12 . OLC W  3 .   ? -38.931 43.392  19.744  1.00 59.18 ? 202 OLC C C12 1 
HETATM 5397 C C7  . OLC W  3 .   ? -38.706 38.650  18.254  1.00 58.39 ? 202 OLC C C7  1 
HETATM 5398 C C15 . OLC W  3 .   ? -38.303 45.876  22.324  1.00 59.42 ? 202 OLC C C15 1 
HETATM 5399 C C13 . OLC W  3 .   ? -37.925 44.142  20.591  1.00 59.38 ? 202 OLC C C13 1 
HETATM 5400 C C6  . OLC W  3 .   ? -39.274 37.370  17.687  1.00 58.12 ? 202 OLC C C6  1 
HETATM 5401 C C14 . OLC W  3 .   ? -38.499 44.416  21.966  1.00 59.46 ? 202 OLC C C14 1 
HETATM 5402 C C5  . OLC W  3 .   ? -38.137 36.441  17.325  1.00 57.81 ? 202 OLC C C5  1 
HETATM 5403 C C4  . OLC W  3 .   ? -37.628 36.796  15.946  1.00 57.55 ? 202 OLC C C4  1 
HETATM 5404 C C3  . OLC W  3 .   ? -36.116 36.798  15.954  1.00 57.38 ? 202 OLC C C3  1 
HETATM 5405 C C2  . OLC W  3 .   ? -35.606 35.374  16.022  1.00 57.31 ? 202 OLC C C2  1 
HETATM 5406 C C21 . OLC W  3 .   ? -33.478 33.285  15.319  1.00 56.61 ? 202 OLC C C21 1 
HETATM 5407 C C1  . OLC W  3 .   ? -35.028 34.980  14.679  1.00 57.17 ? 202 OLC C C1  1 
HETATM 5408 C C22 . OLC W  3 .   ? -33.167 31.816  15.119  1.00 56.19 ? 202 OLC C C22 1 
HETATM 5409 O O19 . OLC W  3 .   ? -34.999 35.792  13.774  1.00 57.18 ? 202 OLC C O19 1 
HETATM 5410 O O25 . OLC W  3 .   ? -31.760 30.255  16.245  1.00 55.84 ? 202 OLC C O25 1 
HETATM 5411 O O23 . OLC W  3 .   ? -34.084 31.030  15.844  1.00 56.06 ? 202 OLC C O23 1 
HETATM 5412 O O20 . OLC W  3 .   ? -34.539 33.674  14.470  1.00 56.95 ? 202 OLC C O20 1 
HETATM 5413 C C18 . OLC X  3 .   ? -41.977 46.790  17.503  1.00 39.28 ? 203 OLC C C18 1 
HETATM 5414 C C10 . OLC X  3 .   ? -42.751 40.353  15.089  1.00 42.59 ? 203 OLC C C10 1 
HETATM 5415 C C9  . OLC X  3 .   ? -41.942 39.333  14.724  1.00 44.51 ? 203 OLC C C9  1 
HETATM 5416 C C17 . OLC X  3 .   ? -42.928 45.623  17.356  1.00 39.46 ? 203 OLC C C17 1 
HETATM 5417 C C11 . OLC X  3 .   ? -43.593 41.147  14.110  1.00 40.74 ? 203 OLC C C11 1 
HETATM 5418 C C8  . OLC X  3 .   ? -41.781 38.866  13.290  1.00 45.53 ? 203 OLC C C8  1 
HETATM 5419 C C24 . OLC X  3 .   ? -36.095 28.301  12.827  1.00 42.99 ? 203 OLC C C24 1 
HETATM 5420 C C16 . OLC X  3 .   ? -44.209 46.097  16.702  1.00 39.49 ? 203 OLC C C16 1 
HETATM 5421 C C12 . OLC X  3 .   ? -44.646 41.906  14.896  1.00 39.16 ? 203 OLC C C12 1 
HETATM 5422 C C7  . OLC X  3 .   ? -40.955 37.594  13.289  1.00 48.90 ? 203 OLC C C7  1 
HETATM 5423 C C15 . OLC X  3 .   ? -44.355 45.470  15.331  1.00 40.01 ? 203 OLC C C15 1 
HETATM 5424 C C13 . OLC X  3 .   ? -44.872 43.280  14.303  1.00 38.55 ? 203 OLC C C13 1 
HETATM 5425 C C6  . OLC X  3 .   ? -40.010 37.551  12.104  1.00 51.93 ? 203 OLC C C6  1 
HETATM 5426 C C14 . OLC X  3 .   ? -45.239 44.243  15.413  1.00 39.77 ? 203 OLC C C14 1 
HETATM 5427 C C5  . OLC X  3 .   ? -38.802 36.696  12.442  1.00 54.03 ? 203 OLC C C5  1 
HETATM 5428 C C4  . OLC X  3 .   ? -38.809 35.408  11.639  1.00 54.02 ? 203 OLC C C4  1 
HETATM 5429 C C3  . OLC X  3 .   ? -37.487 34.677  11.793  1.00 54.90 ? 203 OLC C C3  1 
HETATM 5430 C C2  . OLC X  3 .   ? -37.554 33.625  12.887  1.00 54.06 ? 203 OLC C C2  1 
HETATM 5431 C C21 . OLC X  3 .   ? -36.808 30.584  13.605  1.00 49.09 ? 203 OLC C C21 1 
HETATM 5432 C C1  . OLC X  3 .   ? -37.932 32.270  12.315  1.00 51.57 ? 203 OLC C C1  1 
HETATM 5433 C C22 . OLC X  3 .   ? -37.136 29.099  13.582  1.00 46.34 ? 203 OLC C C22 1 
HETATM 5434 O O19 . OLC X  3 .   ? -39.032 32.125  11.817  1.00 50.79 ? 203 OLC C O19 1 
HETATM 5435 O O25 . OLC X  3 .   ? -36.289 26.929  13.099  1.00 42.18 ? 203 OLC C O25 1 
HETATM 5436 O O23 . OLC X  3 .   ? -37.191 28.599  14.898  1.00 46.32 ? 203 OLC C O23 1 
HETATM 5437 O O20 . OLC X  3 .   ? -37.032 31.180  12.341  1.00 50.23 ? 203 OLC C O20 1 
HETATM 5438 C C18 . OLC Y  3 .   ? -47.775 45.954  37.019  1.00 40.59 ? 204 OLC C C18 1 
HETATM 5439 C C10 . OLC Y  3 .   ? -40.635 40.140  37.647  1.00 43.75 ? 204 OLC C C10 1 
HETATM 5440 C C9  . OLC Y  3 .   ? -40.031 38.952  37.869  1.00 44.81 ? 204 OLC C C9  1 
HETATM 5441 C C17 . OLC Y  3 .   ? -47.082 45.336  38.214  1.00 42.68 ? 204 OLC C C17 1 
HETATM 5442 C C11 . OLC Y  3 .   ? -41.505 40.787  38.703  1.00 44.50 ? 204 OLC C C11 1 
HETATM 5443 C C8  . OLC Y  3 .   ? -40.196 38.215  39.184  1.00 44.93 ? 204 OLC C C8  1 
HETATM 5444 C C24 . OLC Y  3 .   ? -34.567 29.603  43.063  1.00 40.01 ? 204 OLC C C24 1 
HETATM 5445 C C16 . OLC Y  3 .   ? -45.609 45.159  37.912  1.00 42.75 ? 204 OLC C C16 1 
HETATM 5446 C C12 . OLC Y  3 .   ? -42.037 42.102  38.176  1.00 44.52 ? 204 OLC C C12 1 
HETATM 5447 C C7  . OLC Y  3 .   ? -40.690 36.805  38.931  1.00 41.93 ? 204 OLC C C7  1 
HETATM 5448 C C15 . OLC Y  3 .   ? -45.009 44.189  38.907  1.00 44.09 ? 204 OLC C C15 1 
HETATM 5449 C C13 . OLC Y  3 .   ? -43.080 42.655  39.125  1.00 44.83 ? 204 OLC C C13 1 
HETATM 5450 C C6  . OLC Y  3 .   ? -39.879 35.823  39.751  1.00 40.50 ? 204 OLC C C6  1 
HETATM 5451 C C14 . OLC Y  3 .   ? -43.535 44.008  38.621  1.00 44.16 ? 204 OLC C C14 1 
HETATM 5452 C C5  . OLC Y  3 .   ? -40.222 35.964  41.219  1.00 40.48 ? 204 OLC C C5  1 
HETATM 5453 C C4  . OLC Y  3 .   ? -38.993 35.694  42.062  1.00 39.80 ? 204 OLC C C4  1 
HETATM 5454 C C3  . OLC Y  3 .   ? -38.413 34.339  41.712  1.00 39.77 ? 204 OLC C C3  1 
HETATM 5455 C C2  . OLC Y  3 .   ? -37.245 34.027  42.626  1.00 39.66 ? 204 OLC C C2  1 
HETATM 5456 C C21 . OLC Y  3 .   ? -36.720 30.486  42.212  1.00 37.97 ? 204 OLC C C21 1 
HETATM 5457 C C1  . OLC Y  3 .   ? -37.329 32.592  43.118  1.00 39.39 ? 204 OLC C C1  1 
HETATM 5458 C C22 . OLC Y  3 .   ? -36.037 29.302  42.861  1.00 38.38 ? 204 OLC C C22 1 
HETATM 5459 O O19 . OLC Y  3 .   ? -38.293 32.224  43.768  1.00 38.16 ? 204 OLC C O19 1 
HETATM 5460 O O25 . OLC Y  3 .   ? -33.862 28.407  43.316  1.00 40.68 ? 204 OLC C O25 1 
HETATM 5461 O O23 . OLC Y  3 .   ? -36.650 29.040  44.104  1.00 37.94 ? 204 OLC C O23 1 
HETATM 5462 O O20 . OLC Y  3 .   ? -36.292 31.681  42.829  1.00 40.15 ? 204 OLC C O20 1 
HETATM 5463 C C18 . OLC Z  3 .   ? -43.624 44.835  34.577  1.00 42.38 ? 205 OLC C C18 1 
HETATM 5464 C C10 . OLC Z  3 .   ? -49.119 38.954  37.902  1.00 39.99 ? 205 OLC C C10 1 
HETATM 5465 C C9  . OLC Z  3 .   ? -50.112 38.091  38.209  1.00 37.29 ? 205 OLC C C9  1 
HETATM 5466 C C17 . OLC Z  3 .   ? -43.677 43.341  34.344  1.00 43.09 ? 205 OLC C C17 1 
HETATM 5467 C C11 . OLC Z  3 .   ? -49.392 40.328  37.316  1.00 40.11 ? 205 OLC C C11 1 
HETATM 5468 C C8  . OLC Z  3 .   ? -51.566 38.452  37.992  1.00 36.94 ? 205 OLC C C8  1 
HETATM 5469 C C24 . OLC Z  3 .   ? -51.625 28.440  30.566  1.00 35.51 ? 205 OLC C C24 1 
HETATM 5470 C C16 . OLC Z  3 .   ? -44.652 42.694  35.306  1.00 43.21 ? 205 OLC C C16 1 
HETATM 5471 C C12 . OLC Z  3 .   ? -48.070 41.010  37.015  1.00 41.06 ? 205 OLC C C12 1 
HETATM 5472 C C7  . OLC Z  3 .   ? -52.034 38.022  36.616  1.00 36.74 ? 205 OLC C C7  1 
HETATM 5473 C C15 . OLC Z  3 .   ? -46.076 42.872  34.820  1.00 42.69 ? 205 OLC C C15 1 
HETATM 5474 C C13 . OLC Z  3 .   ? -48.129 41.752  35.694  1.00 39.56 ? 205 OLC C C13 1 
HETATM 5475 C C6  . OLC Z  3 .   ? -51.819 36.541  36.395  1.00 34.75 ? 205 OLC C C6  1 
HETATM 5476 C C14 . OLC Z  3 .   ? -46.823 41.559  34.949  1.00 39.69 ? 205 OLC C C14 1 
HETATM 5477 C C5  . OLC Z  3 .   ? -52.720 36.078  35.268  1.00 34.29 ? 205 OLC C C5  1 
HETATM 5478 C C4  . OLC Z  3 .   ? -52.083 34.900  34.565  1.00 34.14 ? 205 OLC C C4  1 
HETATM 5479 C C3  . OLC Z  3 .   ? -53.131 34.103  33.820  1.00 33.31 ? 205 OLC C C3  1 
HETATM 5480 C C2  . OLC Z  3 .   ? -52.465 32.952  33.095  1.00 33.42 ? 205 OLC C C2  1 
HETATM 5481 C C21 . OLC Z  3 .   ? -52.919 30.302  31.560  1.00 35.00 ? 205 OLC C C21 1 
HETATM 5482 C C1  . OLC Z  3 .   ? -53.257 32.624  31.847  1.00 34.67 ? 205 OLC C C1  1 
HETATM 5483 C C22 . OLC Z  3 .   ? -52.897 29.255  30.467  1.00 36.48 ? 205 OLC C C22 1 
HETATM 5484 O O19 . OLC Z  3 .   ? -54.261 33.259  31.586  1.00 35.26 ? 205 OLC C O19 1 
HETATM 5485 O O25 . OLC Z  3 .   ? -51.746 27.264  29.795  1.00 35.65 ? 205 OLC C O25 1 
HETATM 5486 O O23 . OLC Z  3 .   ? -54.012 28.404  30.600  1.00 38.46 ? 205 OLC C O23 1 
HETATM 5487 O O20 . OLC Z  3 .   ? -52.840 31.590  30.989  1.00 35.05 ? 205 OLC C O20 1 
HETATM 5488 C C18 . OLC AA 3 .   ? -63.024 43.272  25.195  1.00 38.56 ? 206 OLC C C18 1 
HETATM 5489 C C10 . OLC AA 3 .   ? -56.724 38.178  25.037  1.00 40.34 ? 206 OLC C C10 1 
HETATM 5490 C C9  . OLC AA 3 .   ? -56.609 36.856  25.271  1.00 38.76 ? 206 OLC C C9  1 
HETATM 5491 C C17 . OLC AA 3 .   ? -62.803 43.122  26.685  1.00 39.76 ? 206 OLC C C17 1 
HETATM 5492 C C11 . OLC AA 3 .   ? -58.051 38.885  25.220  1.00 42.12 ? 206 OLC C C11 1 
HETATM 5493 C C8  . OLC AA 3 .   ? -57.806 36.046  25.717  1.00 38.70 ? 206 OLC C C8  1 
HETATM 5494 C C24 . OLC AA 3 .   ? -56.267 24.489  28.866  1.00 50.54 ? 206 OLC C C24 1 
HETATM 5495 C C16 . OLC AA 3 .   ? -61.952 41.899  26.947  1.00 39.89 ? 206 OLC C C16 1 
HETATM 5496 C C12 . OLC AA 3 .   ? -58.044 40.175  24.425  1.00 42.04 ? 206 OLC C C12 1 
HETATM 5497 C C7  . OLC AA 3 .   ? -57.377 34.630  26.041  1.00 37.77 ? 206 OLC C C7  1 
HETATM 5498 C C15 . OLC AA 3 .   ? -60.527 42.180  26.523  1.00 41.44 ? 206 OLC C C15 1 
HETATM 5499 C C13 . OLC AA 3 .   ? -58.585 41.318  25.259  1.00 41.78 ? 206 OLC C C13 1 
HETATM 5500 C C6  . OLC AA 3 .   ? -56.841 33.949  24.798  1.00 36.82 ? 206 OLC C C6  1 
HETATM 5501 C C14 . OLC AA 3 .   ? -59.998 41.015  25.713  1.00 41.39 ? 206 OLC C C14 1 
HETATM 5502 C C5  . OLC AA 3 .   ? -57.470 32.579  24.651  1.00 37.46 ? 206 OLC C C5  1 
HETATM 5503 C C4  . OLC AA 3 .   ? -56.720 31.567  25.490  1.00 37.64 ? 206 OLC C C4  1 
HETATM 5504 C C3  . OLC AA 3 .   ? -57.660 30.449  25.886  1.00 39.78 ? 206 OLC C C3  1 
HETATM 5505 C C2  . OLC AA 3 .   ? -57.222 29.161  25.227  1.00 40.92 ? 206 OLC C C2  1 
HETATM 5506 C C21 . OLC AA 3 .   ? -57.108 26.175  27.236  1.00 46.01 ? 206 OLC C C21 1 
HETATM 5507 C C1  . OLC AA 3 .   ? -57.893 27.985  25.909  1.00 43.44 ? 206 OLC C C1  1 
HETATM 5508 C C22 . OLC AA 3 .   ? -57.180 25.686  28.669  1.00 48.79 ? 206 OLC C C22 1 
HETATM 5509 O O19 . OLC AA 3 .   ? -58.822 27.422  25.360  1.00 43.58 ? 206 OLC C O19 1 
HETATM 5510 O O25 . OLC AA 3 .   ? -56.860 23.318  28.344  1.00 54.79 ? 206 OLC C O25 1 
HETATM 5511 O O23 . OLC AA 3 .   ? -56.800 26.725  29.542  1.00 46.53 ? 206 OLC C O23 1 
HETATM 5512 O O20 . OLC AA 3 .   ? -57.445 27.546  27.172  1.00 44.57 ? 206 OLC C O20 1 
HETATM 5513 C C18 . OLC BA 3 .   ? -75.882 49.247  4.772   1.00 30.05 ? 201 OLC D C18 1 
HETATM 5514 C C10 . OLC BA 3 .   ? -73.881 40.471  2.666   1.00 40.07 ? 201 OLC D C10 1 
HETATM 5515 C C9  . OLC BA 3 .   ? -73.629 39.205  2.256   1.00 39.67 ? 201 OLC D C9  1 
HETATM 5516 C C17 . OLC BA 3 .   ? -76.095 47.755  4.914   1.00 33.19 ? 201 OLC D C17 1 
HETATM 5517 C C11 . OLC BA 3 .   ? -72.903 41.603  2.419   1.00 39.57 ? 201 OLC D C11 1 
HETATM 5518 C C8  . OLC BA 3 .   ? -72.357 38.822  1.520   1.00 38.11 ? 201 OLC D C8  1 
HETATM 5519 C C24 . OLC BA 3 .   ? -69.870 29.730  9.909   1.00 39.73 ? 201 OLC D C24 1 
HETATM 5520 C C16 . OLC BA 3 .   ? -74.811 47.024  4.578   1.00 34.20 ? 201 OLC D C16 1 
HETATM 5521 C C12 . OLC BA 3 .   ? -73.622 42.938  2.412   1.00 39.88 ? 201 OLC D C12 1 
HETATM 5522 C C7  . OLC BA 3 .   ? -71.262 38.454  2.503   1.00 37.00 ? 201 OLC D C7  1 
HETATM 5523 C C15 . OLC BA 3 .   ? -75.035 45.524  4.556   1.00 34.83 ? 201 OLC D C15 1 
HETATM 5524 C C13 . OLC BA 3 .   ? -74.039 43.353  3.809   1.00 37.81 ? 201 OLC D C13 1 
HETATM 5525 C C6  . OLC BA 3 .   ? -70.981 36.965  2.481   1.00 36.81 ? 201 OLC D C6  1 
HETATM 5526 C C14 . OLC BA 3 .   ? -73.812 44.844  3.971   1.00 35.65 ? 201 OLC D C14 1 
HETATM 5527 C C5  . OLC BA 3 .   ? -69.957 36.642  3.552   1.00 37.00 ? 201 OLC D C5  1 
HETATM 5528 C C4  . OLC BA 3 .   ? -69.938 35.153  3.843   1.00 38.00 ? 201 OLC D C4  1 
HETATM 5529 C C3  . OLC BA 3 .   ? -69.295 34.899  5.194   1.00 37.62 ? 201 OLC D C3  1 
HETATM 5530 C C2  . OLC BA 3 .   ? -69.141 33.411  5.458   1.00 36.99 ? 201 OLC D C2  1 
HETATM 5531 C C21 . OLC BA 3 .   ? -69.108 31.769  8.718   1.00 37.82 ? 201 OLC D C21 1 
HETATM 5532 C C1  . OLC BA 3 .   ? -68.645 33.193  6.876   1.00 36.62 ? 201 OLC D C1  1 
HETATM 5533 C C22 . OLC BA 3 .   ? -68.664 30.473  9.372   1.00 39.88 ? 201 OLC D C22 1 
HETATM 5534 O O19 . OLC BA 3 .   ? -68.310 34.150  7.549   1.00 36.48 ? 201 OLC D O19 1 
HETATM 5535 O O25 . OLC BA 3 .   ? -70.194 30.208  11.196  1.00 39.93 ? 201 OLC D O25 1 
HETATM 5536 O O23 . OLC BA 3 .   ? -67.991 29.653  8.443   1.00 39.23 ? 201 OLC D O23 1 
HETATM 5537 O O20 . OLC BA 3 .   ? -68.564 31.895  7.420   1.00 36.85 ? 201 OLC D O20 1 
HETATM 5538 C C18 . OLC CA 3 .   ? -78.375 44.912  6.220   1.00 38.62 ? 202 OLC D C18 1 
HETATM 5539 C C10 . OLC CA 3 .   ? -80.032 37.114  1.582   1.00 40.54 ? 202 OLC D C10 1 
HETATM 5540 C C9  . OLC CA 3 .   ? -80.596 35.897  1.442   1.00 40.74 ? 202 OLC D C9  1 
HETATM 5541 C C17 . OLC CA 3 .   ? -78.723 44.483  4.812   1.00 38.81 ? 202 OLC D C17 1 
HETATM 5542 C C11 . OLC CA 3 .   ? -80.828 38.280  2.133   1.00 40.31 ? 202 OLC D C11 1 
HETATM 5543 C C8  . OLC CA 3 .   ? -82.041 35.649  1.827   1.00 41.06 ? 202 OLC D C8  1 
HETATM 5544 C C24 . OLC CA 3 .   ? -89.244 26.320  -2.604  1.00 54.35 ? 202 OLC D C24 1 
HETATM 5545 C C16 . OLC CA 3 .   ? -78.465 42.999  4.664   1.00 39.11 ? 202 OLC D C16 1 
HETATM 5546 C C12 . OLC CA 3 .   ? -79.911 39.458  2.395   1.00 39.97 ? 202 OLC D C12 1 
HETATM 5547 C C7  . OLC CA 3 .   ? -82.785 35.111  0.621   1.00 44.64 ? 202 OLC D C7  1 
HETATM 5548 C C15 . OLC CA 3 .   ? -79.180 42.469  3.438   1.00 39.54 ? 202 OLC D C15 1 
HETATM 5549 C C13 . OLC CA 3 .   ? -80.736 40.705  2.640   1.00 39.67 ? 202 OLC D C13 1 
HETATM 5550 C C6  . OLC CA 3 .   ? -84.057 34.395  1.030   1.00 43.04 ? 202 OLC D C6  1 
HETATM 5551 C C14 . OLC CA 3 .   ? -80.210 41.440  3.855   1.00 39.66 ? 202 OLC D C14 1 
HETATM 5552 C C5  . OLC CA 3 .   ? -84.704 33.801  -0.206  1.00 44.29 ? 202 OLC D C5  1 
HETATM 5553 C C4  . OLC CA 3 .   ? -85.928 32.986  0.160   1.00 43.46 ? 202 OLC D C4  1 
HETATM 5554 C C3  . OLC CA 3 .   ? -85.737 31.544  -0.268  1.00 45.89 ? 202 OLC D C3  1 
HETATM 5555 C C2  . OLC CA 3 .   ? -86.909 31.075  -1.108  1.00 49.59 ? 202 OLC D C2  1 
HETATM 5556 C C21 . OLC CA 3 .   ? -89.059 28.717  -1.976  1.00 55.00 ? 202 OLC D C21 1 
HETATM 5557 C C1  . OLC CA 3 .   ? -87.247 29.635  -0.765  1.00 51.41 ? 202 OLC D C1  1 
HETATM 5558 C C22 . OLC CA 3 .   ? -89.631 27.369  -1.585  1.00 55.31 ? 202 OLC D C22 1 
HETATM 5559 O O19 . OLC CA 3 .   ? -87.159 29.252  0.387   1.00 49.61 ? 202 OLC D O19 1 
HETATM 5560 O O25 . OLC CA 3 .   ? -90.074 25.190  -2.442  1.00 53.44 ? 202 OLC D O25 1 
HETATM 5561 O O23 . OLC CA 3 .   ? -89.151 26.988  -0.315  1.00 54.41 ? 202 OLC D O23 1 
HETATM 5562 O O20 . OLC CA 3 .   ? -87.664 28.734  -1.765  1.00 54.05 ? 202 OLC D O20 1 
HETATM 5563 C C18 . OLC DA 3 .   ? -69.892 41.833  -4.735  1.00 63.13 ? 203 OLC D C18 1 
HETATM 5564 C C10 . OLC DA 3 .   ? -77.025 38.091  -4.352  1.00 60.16 ? 203 OLC D C10 1 
HETATM 5565 C C9  . OLC DA 3 .   ? -77.502 36.839  -4.199  1.00 58.29 ? 203 OLC D C9  1 
HETATM 5566 C C17 . OLC DA 3 .   ? -70.459 41.826  -3.332  1.00 62.44 ? 203 OLC D C17 1 
HETATM 5567 C C11 . OLC DA 3 .   ? -76.232 38.749  -3.246  1.00 61.90 ? 203 OLC D C11 1 
HETATM 5568 C C8  . OLC DA 3 .   ? -77.265 36.052  -2.926  1.00 56.78 ? 203 OLC D C8  1 
HETATM 5569 C C24 . OLC DA 3 .   ? -86.451 28.149  -4.968  1.00 55.28 ? 203 OLC D C24 1 
HETATM 5570 C C16 . OLC DA 3 .   ? -71.849 42.427  -3.336  1.00 64.14 ? 203 OLC D C16 1 
HETATM 5571 C C12 . OLC DA 3 .   ? -74.979 39.368  -3.829  1.00 64.23 ? 203 OLC D C12 1 
HETATM 5572 C C7  . OLC DA 3 .   ? -78.111 34.798  -2.955  1.00 54.00 ? 203 OLC D C7  1 
HETATM 5573 C C15 . OLC DA 3 .   ? -72.818 41.482  -4.017  1.00 67.90 ? 203 OLC D C15 1 
HETATM 5574 C C13 . OLC DA 3 .   ? -75.214 40.822  -4.186  1.00 63.70 ? 203 OLC D C13 1 
HETATM 5575 C C6  . OLC DA 3 .   ? -79.572 35.193  -2.943  1.00 53.88 ? 203 OLC D C6  1 
HETATM 5576 C C14 . OLC DA 3 .   ? -74.213 41.707  -3.470  1.00 66.63 ? 203 OLC D C14 1 
HETATM 5577 C C5  . OLC DA 3 .   ? -80.299 34.503  -4.078  1.00 53.87 ? 203 OLC D C5  1 
HETATM 5578 C C4  . OLC DA 3 .   ? -81.788 34.519  -3.807  1.00 53.86 ? 203 OLC D C4  1 
HETATM 5579 C C3  . OLC DA 3 .   ? -82.525 33.781  -4.904  1.00 53.97 ? 203 OLC D C3  1 
HETATM 5580 C C2  . OLC DA 3 .   ? -82.231 32.297  -4.826  1.00 54.24 ? 203 OLC D C2  1 
HETATM 5581 C C21 . OLC DA 3 .   ? -84.795 29.668  -3.921  1.00 54.98 ? 203 OLC D C21 1 
HETATM 5582 C C1  . OLC DA 3 .   ? -83.363 31.553  -4.141  1.00 54.55 ? 203 OLC D C1  1 
HETATM 5583 C C22 . OLC DA 3 .   ? -85.014 28.294  -4.516  1.00 55.26 ? 203 OLC D C22 1 
HETATM 5584 O O19 . OLC DA 3 .   ? -83.831 31.969  -3.097  1.00 54.60 ? 203 OLC D O19 1 
HETATM 5585 O O25 . OLC DA 3 .   ? -86.662 26.854  -5.488  1.00 55.25 ? 203 OLC D O25 1 
HETATM 5586 O O23 . OLC DA 3 .   ? -84.151 28.121  -5.617  1.00 55.43 ? 203 OLC D O23 1 
HETATM 5587 O O20 . OLC DA 3 .   ? -83.872 30.374  -4.720  1.00 54.76 ? 203 OLC D O20 1 
HETATM 5588 C C18 . OLC EA 3 .   ? -76.415 38.856  -7.791  1.00 58.43 ? 204 OLC D C18 1 
HETATM 5589 C C10 . OLC EA 3 .   ? -70.223 32.743  -11.076 1.00 42.53 ? 204 OLC D C10 1 
HETATM 5590 C C9  . OLC EA 3 .   ? -69.086 32.045  -10.876 1.00 40.07 ? 204 OLC D C9  1 
HETATM 5591 C C17 . OLC EA 3 .   ? -75.454 37.740  -7.442  1.00 56.46 ? 204 OLC D C17 1 
HETATM 5592 C C11 . OLC EA 3 .   ? -71.175 33.054  -9.941  1.00 46.46 ? 204 OLC D C11 1 
HETATM 5593 C C8  . OLC EA 3 .   ? -68.697 31.521  -9.507  1.00 39.24 ? 204 OLC D C8  1 
HETATM 5594 C C24 . OLC EA 3 .   ? -60.429 20.943  -9.271  1.00 44.55 ? 204 OLC D C24 1 
HETATM 5595 C C16 . OLC EA 3 .   ? -74.150 37.947  -8.179  1.00 57.62 ? 204 OLC D C16 1 
HETATM 5596 C C12 . OLC EA 3 .   ? -71.943 34.312  -10.293 1.00 50.75 ? 204 OLC D C12 1 
HETATM 5597 C C7  . OLC EA 3 .   ? -67.270 31.007  -9.552  1.00 37.16 ? 204 OLC D C7  1 
HETATM 5598 C C15 . OLC EA 3 .   ? -73.170 36.871  -7.768  1.00 56.50 ? 204 OLC D C15 1 
HETATM 5599 C C13 . OLC EA 3 .   ? -72.649 34.845  -9.066  1.00 53.54 ? 204 OLC D C13 1 
HETATM 5600 C C6  . OLC EA 3 .   ? -67.143 29.693  -8.808  1.00 35.04 ? 204 OLC D C6  1 
HETATM 5601 C C14 . OLC EA 3 .   ? -72.464 36.345  -8.997  1.00 54.96 ? 204 OLC D C14 1 
HETATM 5602 C C5  . OLC EA 3 .   ? -65.770 29.094  -9.041  1.00 35.54 ? 204 OLC D C5  1 
HETATM 5603 C C4  . OLC EA 3 .   ? -65.836 27.588  -8.870  1.00 39.22 ? 204 OLC D C4  1 
HETATM 5604 C C3  . OLC EA 3 .   ? -64.450 26.972  -8.943  1.00 41.32 ? 204 OLC D C3  1 
HETATM 5605 C C2  . OLC EA 3 .   ? -64.536 25.463  -8.795  1.00 42.69 ? 204 OLC D C2  1 
HETATM 5606 C C21 . OLC EA 3 .   ? -61.787 22.916  -8.648  1.00 45.66 ? 204 OLC D C21 1 
HETATM 5607 C C1  . OLC EA 3 .   ? -63.161 24.864  -8.547  1.00 45.11 ? 204 OLC D C1  1 
HETATM 5608 C C22 . OLC EA 3 .   ? -61.820 21.532  -9.266  1.00 44.68 ? 204 OLC D C22 1 
HETATM 5609 O O19 . OLC EA 3 .   ? -62.441 25.338  -7.685  1.00 46.71 ? 204 OLC D O19 1 
HETATM 5610 O O25 . OLC EA 3 .   ? -60.510 19.579  -9.617  1.00 44.54 ? 204 OLC D O25 1 
HETATM 5611 O O23 . OLC EA 3 .   ? -62.671 20.685  -8.528  1.00 45.65 ? 204 OLC D O23 1 
HETATM 5612 O O20 . OLC EA 3 .   ? -62.715 23.758  -9.305  1.00 45.83 ? 204 OLC D O20 1 
HETATM 5613 C C18 . OLC FA 3 .   ? -80.455 32.825  -9.042  1.00 49.58 ? 205 OLC D C18 1 
HETATM 5614 C C10 . OLC FA 3 .   ? -73.471 31.891  -5.050  1.00 41.52 ? 205 OLC D C10 1 
HETATM 5615 C C9  . OLC FA 3 .   ? -72.449 31.063  -4.752  1.00 38.67 ? 205 OLC D C9  1 
HETATM 5616 C C17 . OLC FA 3 .   ? -79.231 33.586  -9.503  1.00 50.53 ? 205 OLC D C17 1 
HETATM 5617 C C11 . OLC FA 3 .   ? -73.318 33.065  -5.995  1.00 46.35 ? 205 OLC D C11 1 
HETATM 5618 C C8  . OLC FA 3 .   ? -71.069 31.227  -5.354  1.00 39.88 ? 205 OLC D C8  1 
HETATM 5619 C C24 . OLC FA 3 .   ? -62.519 21.195  -5.195  1.00 46.85 ? 205 OLC D C24 1 
HETATM 5620 C C16 . OLC FA 3 .   ? -78.703 34.461  -8.384  1.00 51.96 ? 205 OLC D C16 1 
HETATM 5621 C C12 . OLC FA 3 .   ? -74.495 34.007  -5.822  1.00 49.06 ? 205 OLC D C12 1 
HETATM 5622 C C7  . OLC FA 3 .   ? -70.092 30.445  -4.493  1.00 41.48 ? 205 OLC D C7  1 
HETATM 5623 C C15 . OLC FA 3 .   ? -77.950 33.613  -7.381  1.00 50.95 ? 205 OLC D C15 1 
HETATM 5624 C C13 . OLC FA 3 .   ? -75.765 33.319  -6.277  1.00 49.38 ? 205 OLC D C13 1 
HETATM 5625 C C6  . OLC FA 3 .   ? -68.876 29.975  -5.273  1.00 42.16 ? 205 OLC D C6  1 
HETATM 5626 C C14 . OLC FA 3 .   ? -76.684 34.319  -6.945  1.00 51.39 ? 205 OLC D C14 1 
HETATM 5627 C C5  . OLC FA 3 .   ? -67.891 29.255  -4.365  1.00 42.89 ? 205 OLC D C5  1 
HETATM 5628 C C4  . OLC FA 3 .   ? -67.683 27.818  -4.816  1.00 41.47 ? 205 OLC D C4  1 
HETATM 5629 C C3  . OLC FA 3 .   ? -66.423 27.232  -4.202  1.00 42.28 ? 205 OLC D C3  1 
HETATM 5630 C C2  . OLC FA 3 .   ? -66.097 25.898  -4.852  1.00 43.62 ? 205 OLC D C2  1 
HETATM 5631 C C21 . OLC FA 3 .   ? -63.415 23.516  -5.099  1.00 45.94 ? 205 OLC D C21 1 
HETATM 5632 C C1  . OLC FA 3 .   ? -64.719 25.397  -4.446  1.00 45.39 ? 205 OLC D C1  1 
HETATM 5633 C C22 . OLC FA 3 .   ? -62.690 22.427  -4.336  1.00 46.01 ? 205 OLC D C22 1 
HETATM 5634 O O19 . OLC FA 3 .   ? -63.816 26.185  -4.231  1.00 45.55 ? 205 OLC D O19 1 
HETATM 5635 O O25 . OLC FA 3 .   ? -62.122 20.115  -4.379  1.00 47.13 ? 205 OLC D O25 1 
HETATM 5636 O O23 . OLC FA 3 .   ? -61.422 22.893  -3.935  1.00 48.39 ? 205 OLC D O23 1 
HETATM 5637 O O20 . OLC FA 3 .   ? -64.476 24.014  -4.312  1.00 46.01 ? 205 OLC D O20 1 
HETATM 5638 O O   . HOH GA 4 .   ? -43.432 17.524  -4.359  1.00 33.49 ? 301 HOH A O   1 
HETATM 5639 O O   . HOH GA 4 .   ? -42.547 12.725  24.514  1.00 38.14 ? 302 HOH A O   1 
HETATM 5640 O O   . HOH HA 4 .   ? -42.853 18.031  38.812  1.00 32.43 ? 301 HOH C O   1 
HETATM 5641 O O   . HOH HA 4 .   ? -51.132 17.898  16.516  1.00 34.63 ? 302 HOH C O   1 
HETATM 5642 O O   . HOH HA 4 .   ? -50.607 27.285  36.806  1.00 31.33 ? 303 HOH C O   1 
HETATM 5643 O O   . HOH HA 4 .   ? -47.113 22.162  45.667  1.00 35.74 ? 304 HOH C O   1 
HETATM 5644 O O   . HOH HA 4 .   ? -37.417 20.577  43.162  1.00 32.24 ? 305 HOH C O   1 
HETATM 5645 O O   . HOH HA 4 .   ? -31.520 21.389  35.186  1.00 36.70 ? 306 HOH C O   1 
HETATM 5646 O O   . HOH IA 4 .   ? -86.189 19.568  -0.587  1.00 32.71 ? 301 HOH D O   1 
HETATM 5647 O O   . HOH IA 4 .   ? -71.713 27.162  3.490   1.00 31.96 ? 302 HOH D O   1 
HETATM 5648 O O   . HOH IA 4 .   ? -71.455 22.544  -14.890 1.00 30.49 ? 303 HOH D O   1 
HETATM 5649 O O   . HOH IA 4 .   ? -72.543 22.523  11.226  1.00 59.42 ? 304 HOH D O   1 
# 
