data_9NHR
# 
_entry.id   9NHR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9NHR         pdb_00009nhr 10.2210/pdb9nhr/pdb 
WWPDB D_1000293403 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9NHR 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu Scott Lovell ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 mrivera@lsu.edu Mario Rivera ? 'principal investigator/group leader' 0000-0002-5692-5497 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lovell, S.'     1 0000-0002-3215-4472 
'Seibold, S.'    2 0000-0001-8297-229X 
'Battaile, K.P.' 3 0000-0003-0833-3259 
'Yao, H.'        4 ?                   
'Rivera, M.'     5 0000-0002-5692-5497 
# 
_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            'Acs Infect Dis.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2373-8227 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Inhibitors of the Bacterioferritin Ferredoxin Complex Dysregulate Iron Homeostasis and Kill Acinetobacter baumannii and Biofilm-Embedded Pseudomonas aeruginosa Cells.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsinfecdis.5c00209 
_citation.pdbx_database_id_PubMed   40490679 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Behm, A.M.'     1  ?                   
primary 'Yao, H.'        2  ?                   
primary 'Eze, E.C.'      3  ?                   
primary 'Alli, S.A.'     4  ?                   
primary 'Baugh, S.D.P.'  5  ?                   
primary 'Ametsetor, E.'  6  ?                   
primary 'Powell, K.M.'   7  ?                   
primary 'Battaile, K.P.' 8  0000-0003-0833-3259 
primary 'Seibold, S.'    9  ?                   
primary 'Lovell, S.'     10 ?                   
primary 'Bunce, R.A.'    11 0009-0003-7927-5655 
primary 'Reitz, A.B.'    12 ?                   
primary 'Rivera, M.'     13 0000-0002-5692-5497 
# 
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 Ferroxidase                                                              18580.168 12  1.16.3.1 ? BFRB ? 
2 non-polymer syn 'POTASSIUM ION'                                                          39.098    3   ?        ? ?    ? 
3 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                        616.487   7   ?        ? ?    ? 
4 non-polymer syn 'TETRAETHYLENE GLYCOL'                                                   194.226   8   ?        ? ?    ? 
5 non-polymer syn '4-{[(5-chloro-2-hydroxyphenyl)methyl]amino}-1H-isoindole-1,3(2H)-dione' 302.712   9   ?        ? ?    ? 
6 water       nat water                                                                    18.015    695 ?        ? ?    ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKGDKKVIQHLNKILGNELIAINQYFLHSRMWNDWGLKRLGAHEYHESIDEMKHADKLIERILFLEGLPNLQDLGKLLIG
ENTQEMLQCDLNLELKATKDLREAIVHCEQVHDYVSRDLLKDILESEEEHIDYLETQLGLIQKVGLENYLQSHMHEDD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKGDKKVIQHLNKILGNELIAINQYFLHSRMWNDWGLKRLGAHEYHESIDEMKHADKLIERILFLEGLPNLQDLGKLLIG
ENTQEMLQCDLNLELKATKDLREAIVHCEQVHDYVSRDLLKDILESEEEHIDYLETQLGLIQKVGLENYLQSHMHEDD
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F,G,H,I,J,K,L 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'POTASSIUM ION'                                                          K     
3 'PROTOPORPHYRIN IX CONTAINING FE'                                        HEM   
4 'TETRAETHYLENE GLYCOL'                                                   PG4   
5 '4-{[(5-chloro-2-hydroxyphenyl)methyl]amino}-1H-isoindole-1,3(2H)-dione' A1BYB 
6 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   LYS n 
1 3   GLY n 
1 4   ASP n 
1 5   LYS n 
1 6   LYS n 
1 7   VAL n 
1 8   ILE n 
1 9   GLN n 
1 10  HIS n 
1 11  LEU n 
1 12  ASN n 
1 13  LYS n 
1 14  ILE n 
1 15  LEU n 
1 16  GLY n 
1 17  ASN n 
1 18  GLU n 
1 19  LEU n 
1 20  ILE n 
1 21  ALA n 
1 22  ILE n 
1 23  ASN n 
1 24  GLN n 
1 25  TYR n 
1 26  PHE n 
1 27  LEU n 
1 28  HIS n 
1 29  SER n 
1 30  ARG n 
1 31  MET n 
1 32  TRP n 
1 33  ASN n 
1 34  ASP n 
1 35  TRP n 
1 36  GLY n 
1 37  LEU n 
1 38  LYS n 
1 39  ARG n 
1 40  LEU n 
1 41  GLY n 
1 42  ALA n 
1 43  HIS n 
1 44  GLU n 
1 45  TYR n 
1 46  HIS n 
1 47  GLU n 
1 48  SER n 
1 49  ILE n 
1 50  ASP n 
1 51  GLU n 
1 52  MET n 
1 53  LYS n 
1 54  HIS n 
1 55  ALA n 
1 56  ASP n 
1 57  LYS n 
1 58  LEU n 
1 59  ILE n 
1 60  GLU n 
1 61  ARG n 
1 62  ILE n 
1 63  LEU n 
1 64  PHE n 
1 65  LEU n 
1 66  GLU n 
1 67  GLY n 
1 68  LEU n 
1 69  PRO n 
1 70  ASN n 
1 71  LEU n 
1 72  GLN n 
1 73  ASP n 
1 74  LEU n 
1 75  GLY n 
1 76  LYS n 
1 77  LEU n 
1 78  LEU n 
1 79  ILE n 
1 80  GLY n 
1 81  GLU n 
1 82  ASN n 
1 83  THR n 
1 84  GLN n 
1 85  GLU n 
1 86  MET n 
1 87  LEU n 
1 88  GLN n 
1 89  CYS n 
1 90  ASP n 
1 91  LEU n 
1 92  ASN n 
1 93  LEU n 
1 94  GLU n 
1 95  LEU n 
1 96  LYS n 
1 97  ALA n 
1 98  THR n 
1 99  LYS n 
1 100 ASP n 
1 101 LEU n 
1 102 ARG n 
1 103 GLU n 
1 104 ALA n 
1 105 ILE n 
1 106 VAL n 
1 107 HIS n 
1 108 CYS n 
1 109 GLU n 
1 110 GLN n 
1 111 VAL n 
1 112 HIS n 
1 113 ASP n 
1 114 TYR n 
1 115 VAL n 
1 116 SER n 
1 117 ARG n 
1 118 ASP n 
1 119 LEU n 
1 120 LEU n 
1 121 LYS n 
1 122 ASP n 
1 123 ILE n 
1 124 LEU n 
1 125 GLU n 
1 126 SER n 
1 127 GLU n 
1 128 GLU n 
1 129 GLU n 
1 130 HIS n 
1 131 ILE n 
1 132 ASP n 
1 133 TYR n 
1 134 LEU n 
1 135 GLU n 
1 136 THR n 
1 137 GLN n 
1 138 LEU n 
1 139 GLY n 
1 140 LEU n 
1 141 ILE n 
1 142 GLN n 
1 143 LYS n 
1 144 VAL n 
1 145 GLY n 
1 146 LEU n 
1 147 GLU n 
1 148 ASN n 
1 149 TYR n 
1 150 LEU n 
1 151 GLN n 
1 152 SER n 
1 153 HIS n 
1 154 MET n 
1 155 HIS n 
1 156 GLU n 
1 157 ASP n 
1 158 ASP 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                   158 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'bfrB, PA3531' 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'ARCTIC EXPRESS RIL' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PET11A 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BYB non-polymer         . '4-{[(5-chloro-2-hydroxyphenyl)methyl]amino}-1H-isoindole-1,3(2H)-dione' ?    'C15 H11 Cl N2 O3' 
302.712 
ALA   'L-peptide linking' y ALANINE                                                                  ?    'C3 H7 N O2'       
89.093  
ARG   'L-peptide linking' y ARGININE                                                                 ?    'C6 H15 N4 O2 1'   
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                               ?    'C4 H8 N2 O3'      
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                          ?    'C4 H7 N O4'       
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                 ?    'C3 H7 N O2 S'     
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                ?    'C5 H10 N2 O3'     
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                          ?    'C5 H9 N O4'       
147.129 
GLY   'peptide linking'   y GLYCINE                                                                  ?    'C2 H5 N O2'       
75.067  
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                        HEME 'C34 H32 Fe N4 O4' 
616.487 
HIS   'L-peptide linking' y HISTIDINE                                                                ?    'C6 H10 N3 O2 1'   
156.162 
HOH   non-polymer         . WATER                                                                    ?    'H2 O'             
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                               ?    'C6 H13 N O2'      
131.173 
K     non-polymer         . 'POTASSIUM ION'                                                          ?    'K 1'              
39.098  
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 
PG4   non-polymer         . 'TETRAETHYLENE GLYCOL'                                                   ?    'C8 H18 O5'        
194.226 
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   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   GLY 3   3   3   GLY GLY A . n 
A 1 4   ASP 4   4   4   ASP ASP A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   GLN 9   9   9   GLN GLN A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  ASN 12  12  12  ASN ASN A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  ILE 14  14  14  ILE ILE A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ASN 17  17  17  ASN ASN A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  ILE 20  20  20  ILE ILE A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  GLN 24  24  24  GLN GLN A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  HIS 28  28  28  HIS HIS A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  MET 31  31  31  MET MET A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  ASN 33  33  33  ASN ASN A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  TRP 35  35  35  TRP TRP A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  TYR 45  45  45  TYR TYR A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  MET 52  52  52  MET MET A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  HIS 54  54  54  HIS HIS A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  GLN 72  72  72  GLN GLN A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  GLN 84  84  84  GLN GLN A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  MET 86  86  86  MET MET A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLN 88  88  88  GLN GLN A . n 
A 1 89  CYS 89  89  89  CYS CYS A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 ASP 100 100 100 ASP ASP A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 CYS 108 108 108 CYS CYS A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 HIS 112 112 112 HIS HIS A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 ASP 118 118 118 ASP ASP A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 TYR 133 133 133 TYR TYR A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 GLN 137 137 137 GLN GLN A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 GLN 142 142 142 GLN GLN A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 ASN 148 148 148 ASN ASN A . n 
A 1 149 TYR 149 149 149 TYR TYR A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 GLN 151 151 151 GLN GLN A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 HIS 153 153 153 HIS HIS A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 HIS 155 155 155 HIS HIS A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 ASP 157 157 ?   ?   ?   A . n 
A 1 158 ASP 158 158 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   LYS 2   2   2   LYS LYS B . n 
B 1 3   GLY 3   3   3   GLY GLY B . n 
B 1 4   ASP 4   4   4   ASP ASP B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   LYS 6   6   6   LYS LYS B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   ILE 8   8   8   ILE ILE B . n 
B 1 9   GLN 9   9   9   GLN GLN B . n 
B 1 10  HIS 10  10  10  HIS HIS B . n 
B 1 11  LEU 11  11  11  LEU LEU B . n 
B 1 12  ASN 12  12  12  ASN ASN B . n 
B 1 13  LYS 13  13  13  LYS LYS B . n 
B 1 14  ILE 14  14  14  ILE ILE B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ASN 17  17  17  ASN ASN B . n 
B 1 18  GLU 18  18  18  GLU GLU B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  ILE 20  20  20  ILE ILE B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  ASN 23  23  23  ASN ASN B . n 
B 1 24  GLN 24  24  24  GLN GLN B . n 
B 1 25  TYR 25  25  25  TYR TYR B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  HIS 28  28  28  HIS HIS B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  ARG 30  30  30  ARG ARG B . n 
B 1 31  MET 31  31  31  MET MET B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  ASN 33  33  33  ASN ASN B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  TRP 35  35  35  TRP TRP B . n 
B 1 36  GLY 36  36  36  GLY GLY B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  LYS 38  38  38  LYS LYS B . n 
B 1 39  ARG 39  39  39  ARG ARG B . n 
B 1 40  LEU 40  40  40  LEU LEU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLU 44  44  44  GLU GLU B . n 
B 1 45  TYR 45  45  45  TYR TYR B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  ILE 49  49  49  ILE ILE B . n 
B 1 50  ASP 50  50  50  ASP ASP B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  MET 52  52  52  MET MET B . n 
B 1 53  LYS 53  53  53  LYS LYS B . n 
B 1 54  HIS 54  54  54  HIS HIS B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  ARG 61  61  61  ARG ARG B . n 
B 1 62  ILE 62  62  62  ILE ILE B . n 
B 1 63  LEU 63  63  63  LEU LEU B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  LEU 65  65  65  LEU LEU B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  LEU 68  68  68  LEU LEU B . n 
B 1 69  PRO 69  69  69  PRO PRO B . n 
B 1 70  ASN 70  70  70  ASN ASN B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  GLN 72  72  72  GLN GLN B . n 
B 1 73  ASP 73  73  73  ASP ASP B . n 
B 1 74  LEU 74  74  74  LEU LEU B . n 
B 1 75  GLY 75  75  75  GLY GLY B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  GLU 81  81  81  GLU GLU B . n 
B 1 82  ASN 82  82  82  ASN ASN B . n 
B 1 83  THR 83  83  83  THR THR B . n 
B 1 84  GLN 84  84  84  GLN GLN B . n 
B 1 85  GLU 85  85  85  GLU GLU B . n 
B 1 86  MET 86  86  86  MET MET B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  GLN 88  88  88  GLN GLN B . n 
B 1 89  CYS 89  89  89  CYS CYS B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LEU 91  91  91  LEU LEU B . n 
B 1 92  ASN 92  92  92  ASN ASN B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  GLU 94  94  94  GLU GLU B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  LYS 96  96  96  LYS LYS B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 ASP 100 100 100 ASP ASP B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 ARG 102 102 102 ARG ARG B . n 
B 1 103 GLU 103 103 103 GLU GLU B . n 
B 1 104 ALA 104 104 104 ALA ALA B . n 
B 1 105 ILE 105 105 105 ILE ILE B . n 
B 1 106 VAL 106 106 106 VAL VAL B . n 
B 1 107 HIS 107 107 107 HIS HIS B . n 
B 1 108 CYS 108 108 108 CYS CYS B . n 
B 1 109 GLU 109 109 109 GLU GLU B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 VAL 111 111 111 VAL VAL B . n 
B 1 112 HIS 112 112 112 HIS HIS B . n 
B 1 113 ASP 113 113 113 ASP ASP B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 VAL 115 115 115 VAL VAL B . n 
B 1 116 SER 116 116 116 SER SER B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 ASP 118 118 118 ASP ASP B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 ILE 123 123 123 ILE ILE B . n 
B 1 124 LEU 124 124 124 LEU LEU B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 SER 126 126 126 SER SER B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 GLU 128 128 128 GLU GLU B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 HIS 130 130 130 HIS HIS B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 ASP 132 132 132 ASP ASP B . n 
B 1 133 TYR 133 133 133 TYR TYR B . n 
B 1 134 LEU 134 134 134 LEU LEU B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 THR 136 136 136 THR THR B . n 
B 1 137 GLN 137 137 137 GLN GLN B . n 
B 1 138 LEU 138 138 138 LEU LEU B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ILE 141 141 141 ILE ILE B . n 
B 1 142 GLN 142 142 142 GLN GLN B . n 
B 1 143 LYS 143 143 143 LYS LYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 GLY 145 145 145 GLY GLY B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 ASN 148 148 148 ASN ASN B . n 
B 1 149 TYR 149 149 149 TYR TYR B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 GLN 151 151 151 GLN GLN B . n 
B 1 152 SER 152 152 152 SER SER B . n 
B 1 153 HIS 153 153 153 HIS HIS B . n 
B 1 154 MET 154 154 154 MET MET B . n 
B 1 155 HIS 155 155 155 HIS HIS B . n 
B 1 156 GLU 156 156 156 GLU GLU B . n 
B 1 157 ASP 157 157 ?   ?   ?   B . n 
B 1 158 ASP 158 158 ?   ?   ?   B . n 
C 1 1   MET 1   1   1   MET MET C . n 
C 1 2   LYS 2   2   2   LYS LYS C . n 
C 1 3   GLY 3   3   3   GLY GLY C . n 
C 1 4   ASP 4   4   4   ASP ASP C . n 
C 1 5   LYS 5   5   5   LYS LYS C . n 
C 1 6   LYS 6   6   6   LYS LYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   ILE 8   8   8   ILE ILE C . n 
C 1 9   GLN 9   9   9   GLN GLN C . n 
C 1 10  HIS 10  10  10  HIS HIS C . n 
C 1 11  LEU 11  11  11  LEU LEU C . n 
C 1 12  ASN 12  12  12  ASN ASN C . n 
C 1 13  LYS 13  13  13  LYS LYS C . n 
C 1 14  ILE 14  14  14  ILE ILE C . n 
C 1 15  LEU 15  15  15  LEU LEU C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  ASN 17  17  17  ASN ASN C . n 
C 1 18  GLU 18  18  18  GLU GLU C . n 
C 1 19  LEU 19  19  19  LEU LEU C . n 
C 1 20  ILE 20  20  20  ILE ILE C . n 
C 1 21  ALA 21  21  21  ALA ALA C . n 
C 1 22  ILE 22  22  22  ILE ILE C . n 
C 1 23  ASN 23  23  23  ASN ASN C . n 
C 1 24  GLN 24  24  24  GLN GLN C . n 
C 1 25  TYR 25  25  25  TYR TYR C . n 
C 1 26  PHE 26  26  26  PHE PHE C . n 
C 1 27  LEU 27  27  27  LEU LEU C . n 
C 1 28  HIS 28  28  28  HIS HIS C . n 
C 1 29  SER 29  29  29  SER SER C . n 
C 1 30  ARG 30  30  30  ARG ARG C . n 
C 1 31  MET 31  31  31  MET MET C . n 
C 1 32  TRP 32  32  32  TRP TRP C . n 
C 1 33  ASN 33  33  33  ASN ASN C . n 
C 1 34  ASP 34  34  34  ASP ASP C . n 
C 1 35  TRP 35  35  35  TRP TRP C . n 
C 1 36  GLY 36  36  36  GLY GLY C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  LYS 38  38  38  LYS LYS C . n 
C 1 39  ARG 39  39  39  ARG ARG C . n 
C 1 40  LEU 40  40  40  LEU LEU C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  ALA 42  42  42  ALA ALA C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  GLU 44  44  44  GLU GLU C . n 
C 1 45  TYR 45  45  45  TYR TYR C . n 
C 1 46  HIS 46  46  46  HIS HIS C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  SER 48  48  48  SER SER C . n 
C 1 49  ILE 49  49  49  ILE ILE C . n 
C 1 50  ASP 50  50  50  ASP ASP C . n 
C 1 51  GLU 51  51  51  GLU GLU C . n 
C 1 52  MET 52  52  52  MET MET C . n 
C 1 53  LYS 53  53  53  LYS LYS C . n 
C 1 54  HIS 54  54  54  HIS HIS C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  ASP 56  56  56  ASP ASP C . n 
C 1 57  LYS 57  57  57  LYS LYS C . n 
C 1 58  LEU 58  58  58  LEU LEU C . n 
C 1 59  ILE 59  59  59  ILE ILE C . n 
C 1 60  GLU 60  60  60  GLU GLU C . n 
C 1 61  ARG 61  61  61  ARG ARG C . n 
C 1 62  ILE 62  62  62  ILE ILE C . n 
C 1 63  LEU 63  63  63  LEU LEU C . n 
C 1 64  PHE 64  64  64  PHE PHE C . n 
C 1 65  LEU 65  65  65  LEU LEU C . n 
C 1 66  GLU 66  66  66  GLU GLU C . n 
C 1 67  GLY 67  67  67  GLY GLY C . n 
C 1 68  LEU 68  68  68  LEU LEU C . n 
C 1 69  PRO 69  69  69  PRO PRO C . n 
C 1 70  ASN 70  70  70  ASN ASN C . n 
C 1 71  LEU 71  71  71  LEU LEU C . n 
C 1 72  GLN 72  72  72  GLN GLN C . n 
C 1 73  ASP 73  73  73  ASP ASP C . n 
C 1 74  LEU 74  74  74  LEU LEU C . n 
C 1 75  GLY 75  75  75  GLY GLY C . n 
C 1 76  LYS 76  76  76  LYS LYS C . n 
C 1 77  LEU 77  77  77  LEU LEU C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  ILE 79  79  79  ILE ILE C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  GLU 81  81  81  GLU GLU C . n 
C 1 82  ASN 82  82  82  ASN ASN C . n 
C 1 83  THR 83  83  83  THR THR C . n 
C 1 84  GLN 84  84  84  GLN GLN C . n 
C 1 85  GLU 85  85  85  GLU GLU C . n 
C 1 86  MET 86  86  86  MET MET C . n 
C 1 87  LEU 87  87  87  LEU LEU C . n 
C 1 88  GLN 88  88  88  GLN GLN C . n 
C 1 89  CYS 89  89  89  CYS CYS C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  LEU 91  91  91  LEU LEU C . n 
C 1 92  ASN 92  92  92  ASN ASN C . n 
C 1 93  LEU 93  93  93  LEU LEU C . n 
C 1 94  GLU 94  94  94  GLU GLU C . n 
C 1 95  LEU 95  95  95  LEU LEU C . n 
C 1 96  LYS 96  96  96  LYS LYS C . n 
C 1 97  ALA 97  97  97  ALA ALA C . n 
C 1 98  THR 98  98  98  THR THR C . n 
C 1 99  LYS 99  99  99  LYS LYS C . n 
C 1 100 ASP 100 100 100 ASP ASP C . n 
C 1 101 LEU 101 101 101 LEU LEU C . n 
C 1 102 ARG 102 102 102 ARG ARG C . n 
C 1 103 GLU 103 103 103 GLU GLU C . n 
C 1 104 ALA 104 104 104 ALA ALA C . n 
C 1 105 ILE 105 105 105 ILE ILE C . n 
C 1 106 VAL 106 106 106 VAL VAL C . n 
C 1 107 HIS 107 107 107 HIS HIS C . n 
C 1 108 CYS 108 108 108 CYS CYS C . n 
C 1 109 GLU 109 109 109 GLU GLU C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 VAL 111 111 111 VAL VAL C . n 
C 1 112 HIS 112 112 112 HIS HIS C . n 
C 1 113 ASP 113 113 113 ASP ASP C . n 
C 1 114 TYR 114 114 114 TYR TYR C . n 
C 1 115 VAL 115 115 115 VAL VAL C . n 
C 1 116 SER 116 116 116 SER SER C . n 
C 1 117 ARG 117 117 117 ARG ARG C . n 
C 1 118 ASP 118 118 118 ASP ASP C . n 
C 1 119 LEU 119 119 119 LEU LEU C . n 
C 1 120 LEU 120 120 120 LEU LEU C . n 
C 1 121 LYS 121 121 121 LYS LYS C . n 
C 1 122 ASP 122 122 122 ASP ASP C . n 
C 1 123 ILE 123 123 123 ILE ILE C . n 
C 1 124 LEU 124 124 124 LEU LEU C . n 
C 1 125 GLU 125 125 125 GLU GLU C . n 
C 1 126 SER 126 126 126 SER SER C . n 
C 1 127 GLU 127 127 127 GLU GLU C . n 
C 1 128 GLU 128 128 128 GLU GLU C . n 
C 1 129 GLU 129 129 129 GLU GLU C . n 
C 1 130 HIS 130 130 130 HIS HIS C . n 
C 1 131 ILE 131 131 131 ILE ILE C . n 
C 1 132 ASP 132 132 132 ASP ASP C . n 
C 1 133 TYR 133 133 133 TYR TYR C . n 
C 1 134 LEU 134 134 134 LEU LEU C . n 
C 1 135 GLU 135 135 135 GLU GLU C . n 
C 1 136 THR 136 136 136 THR THR C . n 
C 1 137 GLN 137 137 137 GLN GLN C . n 
C 1 138 LEU 138 138 138 LEU LEU C . n 
C 1 139 GLY 139 139 139 GLY GLY C . n 
C 1 140 LEU 140 140 140 LEU LEU C . n 
C 1 141 ILE 141 141 141 ILE ILE C . n 
C 1 142 GLN 142 142 142 GLN GLN C . n 
C 1 143 LYS 143 143 143 LYS LYS C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 GLY 145 145 145 GLY GLY C . n 
C 1 146 LEU 146 146 146 LEU LEU C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 ASN 148 148 148 ASN ASN C . n 
C 1 149 TYR 149 149 149 TYR TYR C . n 
C 1 150 LEU 150 150 150 LEU LEU C . n 
C 1 151 GLN 151 151 151 GLN GLN C . n 
C 1 152 SER 152 152 152 SER SER C . n 
C 1 153 HIS 153 153 153 HIS HIS C . n 
C 1 154 MET 154 154 154 MET MET C . n 
C 1 155 HIS 155 155 155 HIS HIS C . n 
C 1 156 GLU 156 156 156 GLU GLU C . n 
C 1 157 ASP 157 157 ?   ?   ?   C . n 
C 1 158 ASP 158 158 ?   ?   ?   C . n 
D 1 1   MET 1   1   1   MET MET D . n 
D 1 2   LYS 2   2   2   LYS LYS D . n 
D 1 3   GLY 3   3   3   GLY GLY D . n 
D 1 4   ASP 4   4   4   ASP ASP D . n 
D 1 5   LYS 5   5   5   LYS LYS D . n 
D 1 6   LYS 6   6   6   LYS LYS D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   ILE 8   8   8   ILE ILE D . n 
D 1 9   GLN 9   9   9   GLN GLN D . n 
D 1 10  HIS 10  10  10  HIS HIS D . n 
D 1 11  LEU 11  11  11  LEU LEU D . n 
D 1 12  ASN 12  12  12  ASN ASN D . n 
D 1 13  LYS 13  13  13  LYS LYS D . n 
D 1 14  ILE 14  14  14  ILE ILE D . n 
D 1 15  LEU 15  15  15  LEU LEU D . n 
D 1 16  GLY 16  16  16  GLY GLY D . n 
D 1 17  ASN 17  17  17  ASN ASN D . n 
D 1 18  GLU 18  18  18  GLU GLU D . n 
D 1 19  LEU 19  19  19  LEU LEU D . n 
D 1 20  ILE 20  20  20  ILE ILE D . n 
D 1 21  ALA 21  21  21  ALA ALA D . n 
D 1 22  ILE 22  22  22  ILE ILE D . n 
D 1 23  ASN 23  23  23  ASN ASN D . n 
D 1 24  GLN 24  24  24  GLN GLN D . n 
D 1 25  TYR 25  25  25  TYR TYR D . n 
D 1 26  PHE 26  26  26  PHE PHE D . n 
D 1 27  LEU 27  27  27  LEU LEU D . n 
D 1 28  HIS 28  28  28  HIS HIS D . n 
D 1 29  SER 29  29  29  SER SER D . n 
D 1 30  ARG 30  30  30  ARG ARG D . n 
D 1 31  MET 31  31  31  MET MET D . n 
D 1 32  TRP 32  32  32  TRP TRP D . n 
D 1 33  ASN 33  33  33  ASN ASN D . n 
D 1 34  ASP 34  34  34  ASP ASP D . n 
D 1 35  TRP 35  35  35  TRP TRP D . n 
D 1 36  GLY 36  36  36  GLY GLY D . n 
D 1 37  LEU 37  37  37  LEU LEU D . n 
D 1 38  LYS 38  38  38  LYS LYS D . n 
D 1 39  ARG 39  39  39  ARG ARG D . n 
D 1 40  LEU 40  40  40  LEU LEU D . n 
D 1 41  GLY 41  41  41  GLY GLY D . n 
D 1 42  ALA 42  42  42  ALA ALA D . n 
D 1 43  HIS 43  43  43  HIS HIS D . n 
D 1 44  GLU 44  44  44  GLU GLU D . n 
D 1 45  TYR 45  45  45  TYR TYR D . n 
D 1 46  HIS 46  46  46  HIS HIS D . n 
D 1 47  GLU 47  47  47  GLU GLU D . n 
D 1 48  SER 48  48  48  SER SER D . n 
D 1 49  ILE 49  49  49  ILE ILE D . n 
D 1 50  ASP 50  50  50  ASP ASP D . n 
D 1 51  GLU 51  51  51  GLU GLU D . n 
D 1 52  MET 52  52  52  MET MET D . n 
D 1 53  LYS 53  53  53  LYS LYS D . n 
D 1 54  HIS 54  54  54  HIS HIS D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  ASP 56  56  56  ASP ASP D . n 
D 1 57  LYS 57  57  57  LYS LYS D . n 
D 1 58  LEU 58  58  58  LEU LEU D . n 
D 1 59  ILE 59  59  59  ILE ILE D . n 
D 1 60  GLU 60  60  60  GLU GLU D . n 
D 1 61  ARG 61  61  61  ARG ARG D . n 
D 1 62  ILE 62  62  62  ILE ILE D . n 
D 1 63  LEU 63  63  63  LEU LEU D . n 
D 1 64  PHE 64  64  64  PHE PHE D . n 
D 1 65  LEU 65  65  65  LEU LEU D . n 
D 1 66  GLU 66  66  66  GLU GLU D . n 
D 1 67  GLY 67  67  67  GLY GLY D . n 
D 1 68  LEU 68  68  68  LEU LEU D . n 
D 1 69  PRO 69  69  69  PRO PRO D . n 
D 1 70  ASN 70  70  70  ASN ASN D . n 
D 1 71  LEU 71  71  71  LEU LEU D . n 
D 1 72  GLN 72  72  72  GLN GLN D . n 
D 1 73  ASP 73  73  73  ASP ASP D . n 
D 1 74  LEU 74  74  74  LEU LEU D . n 
D 1 75  GLY 75  75  75  GLY GLY D . n 
D 1 76  LYS 76  76  76  LYS LYS D . n 
D 1 77  LEU 77  77  77  LEU LEU D . n 
D 1 78  LEU 78  78  78  LEU LEU D . n 
D 1 79  ILE 79  79  79  ILE ILE D . n 
D 1 80  GLY 80  80  80  GLY GLY D . n 
D 1 81  GLU 81  81  81  GLU GLU D . n 
D 1 82  ASN 82  82  82  ASN ASN D . n 
D 1 83  THR 83  83  83  THR THR D . n 
D 1 84  GLN 84  84  84  GLN GLN D . n 
D 1 85  GLU 85  85  85  GLU GLU D . n 
D 1 86  MET 86  86  86  MET MET D . n 
D 1 87  LEU 87  87  87  LEU LEU D . n 
D 1 88  GLN 88  88  88  GLN GLN D . n 
D 1 89  CYS 89  89  89  CYS CYS D . n 
D 1 90  ASP 90  90  90  ASP ASP D . n 
D 1 91  LEU 91  91  91  LEU LEU D . n 
D 1 92  ASN 92  92  92  ASN ASN D . n 
D 1 93  LEU 93  93  93  LEU LEU D . n 
D 1 94  GLU 94  94  94  GLU GLU D . n 
D 1 95  LEU 95  95  95  LEU LEU D . n 
D 1 96  LYS 96  96  96  LYS LYS D . n 
D 1 97  ALA 97  97  97  ALA ALA D . n 
D 1 98  THR 98  98  98  THR THR D . n 
D 1 99  LYS 99  99  99  LYS LYS D . n 
D 1 100 ASP 100 100 100 ASP ASP D . n 
D 1 101 LEU 101 101 101 LEU LEU D . n 
D 1 102 ARG 102 102 102 ARG ARG D . n 
D 1 103 GLU 103 103 103 GLU GLU D . n 
D 1 104 ALA 104 104 104 ALA ALA D . n 
D 1 105 ILE 105 105 105 ILE ILE D . n 
D 1 106 VAL 106 106 106 VAL VAL D . n 
D 1 107 HIS 107 107 107 HIS HIS D . n 
D 1 108 CYS 108 108 108 CYS CYS D . n 
D 1 109 GLU 109 109 109 GLU GLU D . n 
D 1 110 GLN 110 110 110 GLN GLN D . n 
D 1 111 VAL 111 111 111 VAL VAL D . n 
D 1 112 HIS 112 112 112 HIS HIS D . n 
D 1 113 ASP 113 113 113 ASP ASP D . n 
D 1 114 TYR 114 114 114 TYR TYR D . n 
D 1 115 VAL 115 115 115 VAL VAL D . n 
D 1 116 SER 116 116 116 SER SER D . n 
D 1 117 ARG 117 117 117 ARG ARG D . n 
D 1 118 ASP 118 118 118 ASP ASP D . n 
D 1 119 LEU 119 119 119 LEU LEU D . n 
D 1 120 LEU 120 120 120 LEU LEU D . n 
D 1 121 LYS 121 121 121 LYS LYS D . n 
D 1 122 ASP 122 122 122 ASP ASP D . n 
D 1 123 ILE 123 123 123 ILE ILE D . n 
D 1 124 LEU 124 124 124 LEU LEU D . n 
D 1 125 GLU 125 125 125 GLU GLU D . n 
D 1 126 SER 126 126 126 SER SER D . n 
D 1 127 GLU 127 127 127 GLU GLU D . n 
D 1 128 GLU 128 128 128 GLU GLU D . n 
D 1 129 GLU 129 129 129 GLU GLU D . n 
D 1 130 HIS 130 130 130 HIS HIS D . n 
D 1 131 ILE 131 131 131 ILE ILE D . n 
D 1 132 ASP 132 132 132 ASP ASP D . n 
D 1 133 TYR 133 133 133 TYR TYR D . n 
D 1 134 LEU 134 134 134 LEU LEU D . n 
D 1 135 GLU 135 135 135 GLU GLU D . n 
D 1 136 THR 136 136 136 THR THR D . n 
D 1 137 GLN 137 137 137 GLN GLN D . n 
D 1 138 LEU 138 138 138 LEU LEU D . n 
D 1 139 GLY 139 139 139 GLY GLY D . n 
D 1 140 LEU 140 140 140 LEU LEU D . n 
D 1 141 ILE 141 141 141 ILE ILE D . n 
D 1 142 GLN 142 142 142 GLN GLN D . n 
D 1 143 LYS 143 143 143 LYS LYS D . n 
D 1 144 VAL 144 144 144 VAL VAL D . n 
D 1 145 GLY 145 145 145 GLY GLY D . n 
D 1 146 LEU 146 146 146 LEU LEU D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 ASN 148 148 148 ASN ASN D . n 
D 1 149 TYR 149 149 149 TYR TYR D . n 
D 1 150 LEU 150 150 150 LEU LEU D . n 
D 1 151 GLN 151 151 151 GLN GLN D . n 
D 1 152 SER 152 152 152 SER SER D . n 
D 1 153 HIS 153 153 153 HIS HIS D . n 
D 1 154 MET 154 154 154 MET MET D . n 
D 1 155 HIS 155 155 155 HIS HIS D . n 
D 1 156 GLU 156 156 156 GLU GLU D . n 
D 1 157 ASP 157 157 ?   ?   ?   D . n 
D 1 158 ASP 158 158 ?   ?   ?   D . n 
E 1 1   MET 1   1   1   MET MET E . n 
E 1 2   LYS 2   2   2   LYS LYS E . n 
E 1 3   GLY 3   3   3   GLY GLY E . n 
E 1 4   ASP 4   4   4   ASP ASP E . n 
E 1 5   LYS 5   5   5   LYS LYS E . n 
E 1 6   LYS 6   6   6   LYS LYS E . n 
E 1 7   VAL 7   7   7   VAL VAL E . n 
E 1 8   ILE 8   8   8   ILE ILE E . n 
E 1 9   GLN 9   9   9   GLN GLN E . n 
E 1 10  HIS 10  10  10  HIS HIS E . n 
E 1 11  LEU 11  11  11  LEU LEU E . n 
E 1 12  ASN 12  12  12  ASN ASN E . n 
E 1 13  LYS 13  13  13  LYS LYS E . n 
E 1 14  ILE 14  14  14  ILE ILE E . n 
E 1 15  LEU 15  15  15  LEU LEU E . n 
E 1 16  GLY 16  16  16  GLY GLY E . n 
E 1 17  ASN 17  17  17  ASN ASN E . n 
E 1 18  GLU 18  18  18  GLU GLU E . n 
E 1 19  LEU 19  19  19  LEU LEU E . n 
E 1 20  ILE 20  20  20  ILE ILE E . n 
E 1 21  ALA 21  21  21  ALA ALA E . n 
E 1 22  ILE 22  22  22  ILE ILE E . n 
E 1 23  ASN 23  23  23  ASN ASN E . n 
E 1 24  GLN 24  24  24  GLN GLN E . n 
E 1 25  TYR 25  25  25  TYR TYR E . n 
E 1 26  PHE 26  26  26  PHE PHE E . n 
E 1 27  LEU 27  27  27  LEU LEU E . n 
E 1 28  HIS 28  28  28  HIS HIS E . n 
E 1 29  SER 29  29  29  SER SER E . n 
E 1 30  ARG 30  30  30  ARG ARG E . n 
E 1 31  MET 31  31  31  MET MET E . n 
E 1 32  TRP 32  32  32  TRP TRP E . n 
E 1 33  ASN 33  33  33  ASN ASN E . n 
E 1 34  ASP 34  34  34  ASP ASP E . n 
E 1 35  TRP 35  35  35  TRP TRP E . n 
E 1 36  GLY 36  36  36  GLY GLY E . n 
E 1 37  LEU 37  37  37  LEU LEU E . n 
E 1 38  LYS 38  38  38  LYS LYS E . n 
E 1 39  ARG 39  39  39  ARG ARG E . n 
E 1 40  LEU 40  40  40  LEU LEU E . n 
E 1 41  GLY 41  41  41  GLY GLY E . n 
E 1 42  ALA 42  42  42  ALA ALA E . n 
E 1 43  HIS 43  43  43  HIS HIS E . n 
E 1 44  GLU 44  44  44  GLU GLU E . n 
E 1 45  TYR 45  45  45  TYR TYR E . n 
E 1 46  HIS 46  46  46  HIS HIS E . n 
E 1 47  GLU 47  47  47  GLU GLU E . n 
E 1 48  SER 48  48  48  SER SER E . n 
E 1 49  ILE 49  49  49  ILE ILE E . n 
E 1 50  ASP 50  50  50  ASP ASP E . n 
E 1 51  GLU 51  51  51  GLU GLU E . n 
E 1 52  MET 52  52  52  MET MET E . n 
E 1 53  LYS 53  53  53  LYS LYS E . n 
E 1 54  HIS 54  54  54  HIS HIS E . n 
E 1 55  ALA 55  55  55  ALA ALA E . n 
E 1 56  ASP 56  56  56  ASP ASP E . n 
E 1 57  LYS 57  57  57  LYS LYS E . n 
E 1 58  LEU 58  58  58  LEU LEU E . n 
E 1 59  ILE 59  59  59  ILE ILE E . n 
E 1 60  GLU 60  60  60  GLU GLU E . n 
E 1 61  ARG 61  61  61  ARG ARG E . n 
E 1 62  ILE 62  62  62  ILE ILE E . n 
E 1 63  LEU 63  63  63  LEU LEU E . n 
E 1 64  PHE 64  64  64  PHE PHE E . n 
E 1 65  LEU 65  65  65  LEU LEU E . n 
E 1 66  GLU 66  66  66  GLU GLU E . n 
E 1 67  GLY 67  67  67  GLY GLY E . n 
E 1 68  LEU 68  68  68  LEU LEU E . n 
E 1 69  PRO 69  69  69  PRO PRO E . n 
E 1 70  ASN 70  70  70  ASN ASN E . n 
E 1 71  LEU 71  71  71  LEU LEU E . n 
E 1 72  GLN 72  72  72  GLN GLN E . n 
E 1 73  ASP 73  73  73  ASP ASP E . n 
E 1 74  LEU 74  74  74  LEU LEU E . n 
E 1 75  GLY 75  75  75  GLY GLY E . n 
E 1 76  LYS 76  76  76  LYS LYS E . n 
E 1 77  LEU 77  77  77  LEU LEU E . n 
E 1 78  LEU 78  78  78  LEU LEU E . n 
E 1 79  ILE 79  79  79  ILE ILE E . n 
E 1 80  GLY 80  80  80  GLY GLY E . n 
E 1 81  GLU 81  81  81  GLU GLU E . n 
E 1 82  ASN 82  82  82  ASN ASN E . n 
E 1 83  THR 83  83  83  THR THR E . n 
E 1 84  GLN 84  84  84  GLN GLN E . n 
E 1 85  GLU 85  85  85  GLU GLU E . n 
E 1 86  MET 86  86  86  MET MET E . n 
E 1 87  LEU 87  87  87  LEU LEU E . n 
E 1 88  GLN 88  88  88  GLN GLN E . n 
E 1 89  CYS 89  89  89  CYS CYS E . n 
E 1 90  ASP 90  90  90  ASP ASP E . n 
E 1 91  LEU 91  91  91  LEU LEU E . n 
E 1 92  ASN 92  92  92  ASN ASN E . n 
E 1 93  LEU 93  93  93  LEU LEU E . n 
E 1 94  GLU 94  94  94  GLU GLU E . n 
E 1 95  LEU 95  95  95  LEU LEU E . n 
E 1 96  LYS 96  96  96  LYS LYS E . n 
E 1 97  ALA 97  97  97  ALA ALA E . n 
E 1 98  THR 98  98  98  THR THR E . n 
E 1 99  LYS 99  99  99  LYS LYS E . n 
E 1 100 ASP 100 100 100 ASP ASP E . n 
E 1 101 LEU 101 101 101 LEU LEU E . n 
E 1 102 ARG 102 102 102 ARG ARG E . n 
E 1 103 GLU 103 103 103 GLU GLU E . n 
E 1 104 ALA 104 104 104 ALA ALA E . n 
E 1 105 ILE 105 105 105 ILE ILE E . n 
E 1 106 VAL 106 106 106 VAL VAL E . n 
E 1 107 HIS 107 107 107 HIS HIS E . n 
E 1 108 CYS 108 108 108 CYS CYS E . n 
E 1 109 GLU 109 109 109 GLU GLU E . n 
E 1 110 GLN 110 110 110 GLN GLN E . n 
E 1 111 VAL 111 111 111 VAL VAL E . n 
E 1 112 HIS 112 112 112 HIS HIS E . n 
E 1 113 ASP 113 113 113 ASP ASP E . n 
E 1 114 TYR 114 114 114 TYR TYR E . n 
E 1 115 VAL 115 115 115 VAL VAL E . n 
E 1 116 SER 116 116 116 SER SER E . n 
E 1 117 ARG 117 117 117 ARG ARG E . n 
E 1 118 ASP 118 118 118 ASP ASP E . n 
E 1 119 LEU 119 119 119 LEU LEU E . n 
E 1 120 LEU 120 120 120 LEU LEU E . n 
E 1 121 LYS 121 121 121 LYS LYS E . n 
E 1 122 ASP 122 122 122 ASP ASP E . n 
E 1 123 ILE 123 123 123 ILE ILE E . n 
E 1 124 LEU 124 124 124 LEU LEU E . n 
E 1 125 GLU 125 125 125 GLU GLU E . n 
E 1 126 SER 126 126 126 SER SER E . n 
E 1 127 GLU 127 127 127 GLU GLU E . n 
E 1 128 GLU 128 128 128 GLU GLU E . n 
E 1 129 GLU 129 129 129 GLU GLU E . n 
E 1 130 HIS 130 130 130 HIS HIS E . n 
E 1 131 ILE 131 131 131 ILE ILE E . n 
E 1 132 ASP 132 132 132 ASP ASP E . n 
E 1 133 TYR 133 133 133 TYR TYR E . n 
E 1 134 LEU 134 134 134 LEU LEU E . n 
E 1 135 GLU 135 135 135 GLU GLU E . n 
E 1 136 THR 136 136 136 THR THR E . n 
E 1 137 GLN 137 137 137 GLN GLN E . n 
E 1 138 LEU 138 138 138 LEU LEU E . n 
E 1 139 GLY 139 139 139 GLY GLY E . n 
E 1 140 LEU 140 140 140 LEU LEU E . n 
E 1 141 ILE 141 141 141 ILE ILE E . n 
E 1 142 GLN 142 142 142 GLN GLN E . n 
E 1 143 LYS 143 143 143 LYS LYS E . n 
E 1 144 VAL 144 144 144 VAL VAL E . n 
E 1 145 GLY 145 145 145 GLY GLY E . n 
E 1 146 LEU 146 146 146 LEU LEU E . n 
E 1 147 GLU 147 147 147 GLU GLU E . n 
E 1 148 ASN 148 148 148 ASN ASN E . n 
E 1 149 TYR 149 149 149 TYR TYR E . n 
E 1 150 LEU 150 150 150 LEU LEU E . n 
E 1 151 GLN 151 151 151 GLN GLN E . n 
E 1 152 SER 152 152 152 SER SER E . n 
E 1 153 HIS 153 153 153 HIS HIS E . n 
E 1 154 MET 154 154 154 MET MET E . n 
E 1 155 HIS 155 155 155 HIS HIS E . n 
E 1 156 GLU 156 156 156 GLU GLU E . n 
E 1 157 ASP 157 157 ?   ?   ?   E . n 
E 1 158 ASP 158 158 ?   ?   ?   E . n 
F 1 1   MET 1   1   1   MET MET F . n 
F 1 2   LYS 2   2   2   LYS LYS F . n 
F 1 3   GLY 3   3   3   GLY GLY F . n 
F 1 4   ASP 4   4   4   ASP ASP F . n 
F 1 5   LYS 5   5   5   LYS LYS F . n 
F 1 6   LYS 6   6   6   LYS LYS F . n 
F 1 7   VAL 7   7   7   VAL VAL F . n 
F 1 8   ILE 8   8   8   ILE ILE F . n 
F 1 9   GLN 9   9   9   GLN GLN F . n 
F 1 10  HIS 10  10  10  HIS HIS F . n 
F 1 11  LEU 11  11  11  LEU LEU F . n 
F 1 12  ASN 12  12  12  ASN ASN F . n 
F 1 13  LYS 13  13  13  LYS LYS F . n 
F 1 14  ILE 14  14  14  ILE ILE F . n 
F 1 15  LEU 15  15  15  LEU LEU F . n 
F 1 16  GLY 16  16  16  GLY GLY F . n 
F 1 17  ASN 17  17  17  ASN ASN F . n 
F 1 18  GLU 18  18  18  GLU GLU F . n 
F 1 19  LEU 19  19  19  LEU LEU F . n 
F 1 20  ILE 20  20  20  ILE ILE F . n 
F 1 21  ALA 21  21  21  ALA ALA F . n 
F 1 22  ILE 22  22  22  ILE ILE F . n 
F 1 23  ASN 23  23  23  ASN ASN F . n 
F 1 24  GLN 24  24  24  GLN GLN F . n 
F 1 25  TYR 25  25  25  TYR TYR F . n 
F 1 26  PHE 26  26  26  PHE PHE F . n 
F 1 27  LEU 27  27  27  LEU LEU F . n 
F 1 28  HIS 28  28  28  HIS HIS F . n 
F 1 29  SER 29  29  29  SER SER F . n 
F 1 30  ARG 30  30  30  ARG ARG F . n 
F 1 31  MET 31  31  31  MET MET F . n 
F 1 32  TRP 32  32  32  TRP TRP F . n 
F 1 33  ASN 33  33  33  ASN ASN F . n 
F 1 34  ASP 34  34  34  ASP ASP F . n 
F 1 35  TRP 35  35  35  TRP TRP F . n 
F 1 36  GLY 36  36  36  GLY GLY F . n 
F 1 37  LEU 37  37  37  LEU LEU F . n 
F 1 38  LYS 38  38  38  LYS LYS F . n 
F 1 39  ARG 39  39  39  ARG ARG F . n 
F 1 40  LEU 40  40  40  LEU LEU F . n 
F 1 41  GLY 41  41  41  GLY GLY F . n 
F 1 42  ALA 42  42  42  ALA ALA F . n 
F 1 43  HIS 43  43  43  HIS HIS F . n 
F 1 44  GLU 44  44  44  GLU GLU F . n 
F 1 45  TYR 45  45  45  TYR TYR F . n 
F 1 46  HIS 46  46  46  HIS HIS F . n 
F 1 47  GLU 47  47  47  GLU GLU F . n 
F 1 48  SER 48  48  48  SER SER F . n 
F 1 49  ILE 49  49  49  ILE ILE F . n 
F 1 50  ASP 50  50  50  ASP ASP F . n 
F 1 51  GLU 51  51  51  GLU GLU F . n 
F 1 52  MET 52  52  52  MET MET F . n 
F 1 53  LYS 53  53  53  LYS LYS F . n 
F 1 54  HIS 54  54  54  HIS HIS F . n 
F 1 55  ALA 55  55  55  ALA ALA F . n 
F 1 56  ASP 56  56  56  ASP ASP F . n 
F 1 57  LYS 57  57  57  LYS LYS F . n 
F 1 58  LEU 58  58  58  LEU LEU F . n 
F 1 59  ILE 59  59  59  ILE ILE F . n 
F 1 60  GLU 60  60  60  GLU GLU F . n 
F 1 61  ARG 61  61  61  ARG ARG F . n 
F 1 62  ILE 62  62  62  ILE ILE F . n 
F 1 63  LEU 63  63  63  LEU LEU F . n 
F 1 64  PHE 64  64  64  PHE PHE F . n 
F 1 65  LEU 65  65  65  LEU LEU F . n 
F 1 66  GLU 66  66  66  GLU GLU F . n 
F 1 67  GLY 67  67  67  GLY GLY F . n 
F 1 68  LEU 68  68  68  LEU LEU F . n 
F 1 69  PRO 69  69  69  PRO PRO F . n 
F 1 70  ASN 70  70  70  ASN ASN F . n 
F 1 71  LEU 71  71  71  LEU LEU F . n 
F 1 72  GLN 72  72  72  GLN GLN F . n 
F 1 73  ASP 73  73  73  ASP ASP F . n 
F 1 74  LEU 74  74  74  LEU LEU F . n 
F 1 75  GLY 75  75  75  GLY GLY F . n 
F 1 76  LYS 76  76  76  LYS LYS F . n 
F 1 77  LEU 77  77  77  LEU LEU F . n 
F 1 78  LEU 78  78  78  LEU LEU F . n 
F 1 79  ILE 79  79  79  ILE ILE F . n 
F 1 80  GLY 80  80  80  GLY GLY F . n 
F 1 81  GLU 81  81  81  GLU GLU F . n 
F 1 82  ASN 82  82  82  ASN ASN F . n 
F 1 83  THR 83  83  83  THR THR F . n 
F 1 84  GLN 84  84  84  GLN GLN F . n 
F 1 85  GLU 85  85  85  GLU GLU F . n 
F 1 86  MET 86  86  86  MET MET F . n 
F 1 87  LEU 87  87  87  LEU LEU F . n 
F 1 88  GLN 88  88  88  GLN GLN F . n 
F 1 89  CYS 89  89  89  CYS CYS F . n 
F 1 90  ASP 90  90  90  ASP ASP F . n 
F 1 91  LEU 91  91  91  LEU LEU F . n 
F 1 92  ASN 92  92  92  ASN ASN F . n 
F 1 93  LEU 93  93  93  LEU LEU F . n 
F 1 94  GLU 94  94  94  GLU GLU F . n 
F 1 95  LEU 95  95  95  LEU LEU F . n 
F 1 96  LYS 96  96  96  LYS LYS F . n 
F 1 97  ALA 97  97  97  ALA ALA F . n 
F 1 98  THR 98  98  98  THR THR F . n 
F 1 99  LYS 99  99  99  LYS LYS F . n 
F 1 100 ASP 100 100 100 ASP ASP F . n 
F 1 101 LEU 101 101 101 LEU LEU F . n 
F 1 102 ARG 102 102 102 ARG ARG F . n 
F 1 103 GLU 103 103 103 GLU GLU F . n 
F 1 104 ALA 104 104 104 ALA ALA F . n 
F 1 105 ILE 105 105 105 ILE ILE F . n 
F 1 106 VAL 106 106 106 VAL VAL F . n 
F 1 107 HIS 107 107 107 HIS HIS F . n 
F 1 108 CYS 108 108 108 CYS CYS F . n 
F 1 109 GLU 109 109 109 GLU GLU F . n 
F 1 110 GLN 110 110 110 GLN GLN F . n 
F 1 111 VAL 111 111 111 VAL VAL F . n 
F 1 112 HIS 112 112 112 HIS HIS F . n 
F 1 113 ASP 113 113 113 ASP ASP F . n 
F 1 114 TYR 114 114 114 TYR TYR F . n 
F 1 115 VAL 115 115 115 VAL VAL F . n 
F 1 116 SER 116 116 116 SER SER F . n 
F 1 117 ARG 117 117 117 ARG ARG F . n 
F 1 118 ASP 118 118 118 ASP ASP F . n 
F 1 119 LEU 119 119 119 LEU LEU F . n 
F 1 120 LEU 120 120 120 LEU LEU F . n 
F 1 121 LYS 121 121 121 LYS LYS F . n 
F 1 122 ASP 122 122 122 ASP ASP F . n 
F 1 123 ILE 123 123 123 ILE ILE F . n 
F 1 124 LEU 124 124 124 LEU LEU F . n 
F 1 125 GLU 125 125 125 GLU GLU F . n 
F 1 126 SER 126 126 126 SER SER F . n 
F 1 127 GLU 127 127 127 GLU GLU F . n 
F 1 128 GLU 128 128 128 GLU GLU F . n 
F 1 129 GLU 129 129 129 GLU GLU F . n 
F 1 130 HIS 130 130 130 HIS HIS F . n 
F 1 131 ILE 131 131 131 ILE ILE F . n 
F 1 132 ASP 132 132 132 ASP ASP F . n 
F 1 133 TYR 133 133 133 TYR TYR F . n 
F 1 134 LEU 134 134 134 LEU LEU F . n 
F 1 135 GLU 135 135 135 GLU GLU F . n 
F 1 136 THR 136 136 136 THR THR F . n 
F 1 137 GLN 137 137 137 GLN GLN F . n 
F 1 138 LEU 138 138 138 LEU LEU F . n 
F 1 139 GLY 139 139 139 GLY GLY F . n 
F 1 140 LEU 140 140 140 LEU LEU F . n 
F 1 141 ILE 141 141 141 ILE ILE F . n 
F 1 142 GLN 142 142 142 GLN GLN F . n 
F 1 143 LYS 143 143 143 LYS LYS F . n 
F 1 144 VAL 144 144 144 VAL VAL F . n 
F 1 145 GLY 145 145 145 GLY GLY F . n 
F 1 146 LEU 146 146 146 LEU LEU F . n 
F 1 147 GLU 147 147 147 GLU GLU F . n 
F 1 148 ASN 148 148 148 ASN ASN F . n 
F 1 149 TYR 149 149 149 TYR TYR F . n 
F 1 150 LEU 150 150 150 LEU LEU F . n 
F 1 151 GLN 151 151 151 GLN GLN F . n 
F 1 152 SER 152 152 152 SER SER F . n 
F 1 153 HIS 153 153 153 HIS HIS F . n 
F 1 154 MET 154 154 154 MET MET F . n 
F 1 155 HIS 155 155 155 HIS HIS F . n 
F 1 156 GLU 156 156 156 GLU GLU F . n 
F 1 157 ASP 157 157 ?   ?   ?   F . n 
F 1 158 ASP 158 158 ?   ?   ?   F . n 
G 1 1   MET 1   1   1   MET MET G . n 
G 1 2   LYS 2   2   2   LYS LYS G . n 
G 1 3   GLY 3   3   3   GLY GLY G . n 
G 1 4   ASP 4   4   4   ASP ASP G . n 
G 1 5   LYS 5   5   5   LYS LYS G . n 
G 1 6   LYS 6   6   6   LYS LYS G . n 
G 1 7   VAL 7   7   7   VAL VAL G . n 
G 1 8   ILE 8   8   8   ILE ILE G . n 
G 1 9   GLN 9   9   9   GLN GLN G . n 
G 1 10  HIS 10  10  10  HIS HIS G . n 
G 1 11  LEU 11  11  11  LEU LEU G . n 
G 1 12  ASN 12  12  12  ASN ASN G . n 
G 1 13  LYS 13  13  13  LYS LYS G . n 
G 1 14  ILE 14  14  14  ILE ILE G . n 
G 1 15  LEU 15  15  15  LEU LEU G . n 
G 1 16  GLY 16  16  16  GLY GLY G . n 
G 1 17  ASN 17  17  17  ASN ASN G . n 
G 1 18  GLU 18  18  18  GLU GLU G . n 
G 1 19  LEU 19  19  19  LEU LEU G . n 
G 1 20  ILE 20  20  20  ILE ILE G . n 
G 1 21  ALA 21  21  21  ALA ALA G . n 
G 1 22  ILE 22  22  22  ILE ILE G . n 
G 1 23  ASN 23  23  23  ASN ASN G . n 
G 1 24  GLN 24  24  24  GLN GLN G . n 
G 1 25  TYR 25  25  25  TYR TYR G . n 
G 1 26  PHE 26  26  26  PHE PHE G . n 
G 1 27  LEU 27  27  27  LEU LEU G . n 
G 1 28  HIS 28  28  28  HIS HIS G . n 
G 1 29  SER 29  29  29  SER SER G . n 
G 1 30  ARG 30  30  30  ARG ARG G . n 
G 1 31  MET 31  31  31  MET MET G . n 
G 1 32  TRP 32  32  32  TRP TRP G . n 
G 1 33  ASN 33  33  33  ASN ASN G . n 
G 1 34  ASP 34  34  34  ASP ASP G . n 
G 1 35  TRP 35  35  35  TRP TRP G . n 
G 1 36  GLY 36  36  36  GLY GLY G . n 
G 1 37  LEU 37  37  37  LEU LEU G . n 
G 1 38  LYS 38  38  38  LYS LYS G . n 
G 1 39  ARG 39  39  39  ARG ARG G . n 
G 1 40  LEU 40  40  40  LEU LEU G . n 
G 1 41  GLY 41  41  41  GLY GLY G . n 
G 1 42  ALA 42  42  42  ALA ALA G . n 
G 1 43  HIS 43  43  43  HIS HIS G . n 
G 1 44  GLU 44  44  44  GLU GLU G . n 
G 1 45  TYR 45  45  45  TYR TYR G . n 
G 1 46  HIS 46  46  46  HIS HIS G . n 
G 1 47  GLU 47  47  47  GLU GLU G . n 
G 1 48  SER 48  48  48  SER SER G . n 
G 1 49  ILE 49  49  49  ILE ILE G . n 
G 1 50  ASP 50  50  50  ASP ASP G . n 
G 1 51  GLU 51  51  51  GLU GLU G . n 
G 1 52  MET 52  52  52  MET MET G . n 
G 1 53  LYS 53  53  53  LYS LYS G . n 
G 1 54  HIS 54  54  54  HIS HIS G . n 
G 1 55  ALA 55  55  55  ALA ALA G . n 
G 1 56  ASP 56  56  56  ASP ASP G . n 
G 1 57  LYS 57  57  57  LYS LYS G . n 
G 1 58  LEU 58  58  58  LEU LEU G . n 
G 1 59  ILE 59  59  59  ILE ILE G . n 
G 1 60  GLU 60  60  60  GLU GLU G . n 
G 1 61  ARG 61  61  61  ARG ARG G . n 
G 1 62  ILE 62  62  62  ILE ILE G . n 
G 1 63  LEU 63  63  63  LEU LEU G . n 
G 1 64  PHE 64  64  64  PHE PHE G . n 
G 1 65  LEU 65  65  65  LEU LEU G . n 
G 1 66  GLU 66  66  66  GLU GLU G . n 
G 1 67  GLY 67  67  67  GLY GLY G . n 
G 1 68  LEU 68  68  68  LEU LEU G . n 
G 1 69  PRO 69  69  69  PRO PRO G . n 
G 1 70  ASN 70  70  70  ASN ASN G . n 
G 1 71  LEU 71  71  71  LEU LEU G . n 
G 1 72  GLN 72  72  72  GLN GLN G . n 
G 1 73  ASP 73  73  73  ASP ASP G . n 
G 1 74  LEU 74  74  74  LEU LEU G . n 
G 1 75  GLY 75  75  75  GLY GLY G . n 
G 1 76  LYS 76  76  76  LYS LYS G . n 
G 1 77  LEU 77  77  77  LEU LEU G . n 
G 1 78  LEU 78  78  78  LEU LEU G . n 
G 1 79  ILE 79  79  79  ILE ILE G . n 
G 1 80  GLY 80  80  80  GLY GLY G . n 
G 1 81  GLU 81  81  81  GLU GLU G . n 
G 1 82  ASN 82  82  82  ASN ASN G . n 
G 1 83  THR 83  83  83  THR THR G . n 
G 1 84  GLN 84  84  84  GLN GLN G . n 
G 1 85  GLU 85  85  85  GLU GLU G . n 
G 1 86  MET 86  86  86  MET MET G . n 
G 1 87  LEU 87  87  87  LEU LEU G . n 
G 1 88  GLN 88  88  88  GLN GLN G . n 
G 1 89  CYS 89  89  89  CYS CYS G . n 
G 1 90  ASP 90  90  90  ASP ASP G . n 
G 1 91  LEU 91  91  91  LEU LEU G . n 
G 1 92  ASN 92  92  92  ASN ASN G . n 
G 1 93  LEU 93  93  93  LEU LEU G . n 
G 1 94  GLU 94  94  94  GLU GLU G . n 
G 1 95  LEU 95  95  95  LEU LEU G . n 
G 1 96  LYS 96  96  96  LYS LYS G . n 
G 1 97  ALA 97  97  97  ALA ALA G . n 
G 1 98  THR 98  98  98  THR THR G . n 
G 1 99  LYS 99  99  99  LYS LYS G . n 
G 1 100 ASP 100 100 100 ASP ASP G . n 
G 1 101 LEU 101 101 101 LEU LEU G . n 
G 1 102 ARG 102 102 102 ARG ARG G . n 
G 1 103 GLU 103 103 103 GLU GLU G . n 
G 1 104 ALA 104 104 104 ALA ALA G . n 
G 1 105 ILE 105 105 105 ILE ILE G . n 
G 1 106 VAL 106 106 106 VAL VAL G . n 
G 1 107 HIS 107 107 107 HIS HIS G . n 
G 1 108 CYS 108 108 108 CYS CYS G . n 
G 1 109 GLU 109 109 109 GLU GLU G . n 
G 1 110 GLN 110 110 110 GLN GLN G . n 
G 1 111 VAL 111 111 111 VAL VAL G . n 
G 1 112 HIS 112 112 112 HIS HIS G . n 
G 1 113 ASP 113 113 113 ASP ASP G . n 
G 1 114 TYR 114 114 114 TYR TYR G . n 
G 1 115 VAL 115 115 115 VAL VAL G . n 
G 1 116 SER 116 116 116 SER SER G . n 
G 1 117 ARG 117 117 117 ARG ARG G . n 
G 1 118 ASP 118 118 118 ASP ASP G . n 
G 1 119 LEU 119 119 119 LEU LEU G . n 
G 1 120 LEU 120 120 120 LEU LEU G . n 
G 1 121 LYS 121 121 121 LYS LYS G . n 
G 1 122 ASP 122 122 122 ASP ASP G . n 
G 1 123 ILE 123 123 123 ILE ILE G . n 
G 1 124 LEU 124 124 124 LEU LEU G . n 
G 1 125 GLU 125 125 125 GLU GLU G . n 
G 1 126 SER 126 126 126 SER SER G . n 
G 1 127 GLU 127 127 127 GLU GLU G . n 
G 1 128 GLU 128 128 128 GLU GLU G . n 
G 1 129 GLU 129 129 129 GLU GLU G . n 
G 1 130 HIS 130 130 130 HIS HIS G . n 
G 1 131 ILE 131 131 131 ILE ILE G . n 
G 1 132 ASP 132 132 132 ASP ASP G . n 
G 1 133 TYR 133 133 133 TYR TYR G . n 
G 1 134 LEU 134 134 134 LEU LEU G . n 
G 1 135 GLU 135 135 135 GLU GLU G . n 
G 1 136 THR 136 136 136 THR THR G . n 
G 1 137 GLN 137 137 137 GLN GLN G . n 
G 1 138 LEU 138 138 138 LEU LEU G . n 
G 1 139 GLY 139 139 139 GLY GLY G . n 
G 1 140 LEU 140 140 140 LEU LEU G . n 
G 1 141 ILE 141 141 141 ILE ILE G . n 
G 1 142 GLN 142 142 142 GLN GLN G . n 
G 1 143 LYS 143 143 143 LYS LYS G . n 
G 1 144 VAL 144 144 144 VAL VAL G . n 
G 1 145 GLY 145 145 145 GLY GLY G . n 
G 1 146 LEU 146 146 146 LEU LEU G . n 
G 1 147 GLU 147 147 147 GLU GLU G . n 
G 1 148 ASN 148 148 148 ASN ASN G . n 
G 1 149 TYR 149 149 149 TYR TYR G . n 
G 1 150 LEU 150 150 150 LEU LEU G . n 
G 1 151 GLN 151 151 151 GLN GLN G . n 
G 1 152 SER 152 152 152 SER SER G . n 
G 1 153 HIS 153 153 153 HIS HIS G . n 
G 1 154 MET 154 154 154 MET MET G . n 
G 1 155 HIS 155 155 155 HIS HIS G . n 
G 1 156 GLU 156 156 156 GLU GLU G . n 
G 1 157 ASP 157 157 ?   ?   ?   G . n 
G 1 158 ASP 158 158 ?   ?   ?   G . n 
H 1 1   MET 1   1   1   MET MET H . n 
H 1 2   LYS 2   2   2   LYS LYS H . n 
H 1 3   GLY 3   3   3   GLY GLY H . n 
H 1 4   ASP 4   4   4   ASP ASP H . n 
H 1 5   LYS 5   5   5   LYS LYS H . n 
H 1 6   LYS 6   6   6   LYS LYS H . n 
H 1 7   VAL 7   7   7   VAL VAL H . n 
H 1 8   ILE 8   8   8   ILE ILE H . n 
H 1 9   GLN 9   9   9   GLN GLN H . n 
H 1 10  HIS 10  10  10  HIS HIS H . n 
H 1 11  LEU 11  11  11  LEU LEU H . n 
H 1 12  ASN 12  12  12  ASN ASN H . n 
H 1 13  LYS 13  13  13  LYS LYS H . n 
H 1 14  ILE 14  14  14  ILE ILE H . n 
H 1 15  LEU 15  15  15  LEU LEU H . n 
H 1 16  GLY 16  16  16  GLY GLY H . n 
H 1 17  ASN 17  17  17  ASN ASN H . n 
H 1 18  GLU 18  18  18  GLU GLU H . n 
H 1 19  LEU 19  19  19  LEU LEU H . n 
H 1 20  ILE 20  20  20  ILE ILE H . n 
H 1 21  ALA 21  21  21  ALA ALA H . n 
H 1 22  ILE 22  22  22  ILE ILE H . n 
H 1 23  ASN 23  23  23  ASN ASN H . n 
H 1 24  GLN 24  24  24  GLN GLN H . n 
H 1 25  TYR 25  25  25  TYR TYR H . n 
H 1 26  PHE 26  26  26  PHE PHE H . n 
H 1 27  LEU 27  27  27  LEU LEU H . n 
H 1 28  HIS 28  28  28  HIS HIS H . n 
H 1 29  SER 29  29  29  SER SER H . n 
H 1 30  ARG 30  30  30  ARG ARG H . n 
H 1 31  MET 31  31  31  MET MET H . n 
H 1 32  TRP 32  32  32  TRP TRP H . n 
H 1 33  ASN 33  33  33  ASN ASN H . n 
H 1 34  ASP 34  34  34  ASP ASP H . n 
H 1 35  TRP 35  35  35  TRP TRP H . n 
H 1 36  GLY 36  36  36  GLY GLY H . n 
H 1 37  LEU 37  37  37  LEU LEU H . n 
H 1 38  LYS 38  38  38  LYS LYS H . n 
H 1 39  ARG 39  39  39  ARG ARG H . n 
H 1 40  LEU 40  40  40  LEU LEU H . n 
H 1 41  GLY 41  41  41  GLY GLY H . n 
H 1 42  ALA 42  42  42  ALA ALA H . n 
H 1 43  HIS 43  43  43  HIS HIS H . n 
H 1 44  GLU 44  44  44  GLU GLU H . n 
H 1 45  TYR 45  45  45  TYR TYR H . n 
H 1 46  HIS 46  46  ?   ?   ?   H . n 
H 1 47  GLU 47  47  47  GLU GLU H . n 
H 1 48  SER 48  48  48  SER SER H . n 
H 1 49  ILE 49  49  49  ILE ILE H . n 
H 1 50  ASP 50  50  50  ASP ASP H . n 
H 1 51  GLU 51  51  51  GLU GLU H . n 
H 1 52  MET 52  52  52  MET MET H . n 
H 1 53  LYS 53  53  53  LYS LYS H . n 
H 1 54  HIS 54  54  54  HIS HIS H . n 
H 1 55  ALA 55  55  55  ALA ALA H . n 
H 1 56  ASP 56  56  56  ASP ASP H . n 
H 1 57  LYS 57  57  57  LYS LYS H . n 
H 1 58  LEU 58  58  58  LEU LEU H . n 
H 1 59  ILE 59  59  59  ILE ILE H . n 
H 1 60  GLU 60  60  60  GLU GLU H . n 
H 1 61  ARG 61  61  61  ARG ARG H . n 
H 1 62  ILE 62  62  62  ILE ILE H . n 
H 1 63  LEU 63  63  63  LEU LEU H . n 
H 1 64  PHE 64  64  64  PHE PHE H . n 
H 1 65  LEU 65  65  65  LEU LEU H . n 
H 1 66  GLU 66  66  66  GLU GLU H . n 
H 1 67  GLY 67  67  67  GLY GLY H . n 
H 1 68  LEU 68  68  68  LEU LEU H . n 
H 1 69  PRO 69  69  69  PRO PRO H . n 
H 1 70  ASN 70  70  70  ASN ASN H . n 
H 1 71  LEU 71  71  71  LEU LEU H . n 
H 1 72  GLN 72  72  72  GLN GLN H . n 
H 1 73  ASP 73  73  73  ASP ASP H . n 
H 1 74  LEU 74  74  74  LEU LEU H . n 
H 1 75  GLY 75  75  75  GLY GLY H . n 
H 1 76  LYS 76  76  76  LYS LYS H . n 
H 1 77  LEU 77  77  77  LEU LEU H . n 
H 1 78  LEU 78  78  78  LEU LEU H . n 
H 1 79  ILE 79  79  79  ILE ILE H . n 
H 1 80  GLY 80  80  80  GLY GLY H . n 
H 1 81  GLU 81  81  81  GLU GLU H . n 
H 1 82  ASN 82  82  82  ASN ASN H . n 
H 1 83  THR 83  83  83  THR THR H . n 
H 1 84  GLN 84  84  84  GLN GLN H . n 
H 1 85  GLU 85  85  85  GLU GLU H . n 
H 1 86  MET 86  86  86  MET MET H . n 
H 1 87  LEU 87  87  87  LEU LEU H . n 
H 1 88  GLN 88  88  88  GLN GLN H . n 
H 1 89  CYS 89  89  89  CYS CYS H . n 
H 1 90  ASP 90  90  90  ASP ASP H . n 
H 1 91  LEU 91  91  91  LEU LEU H . n 
H 1 92  ASN 92  92  92  ASN ASN H . n 
H 1 93  LEU 93  93  93  LEU LEU H . n 
H 1 94  GLU 94  94  94  GLU GLU H . n 
H 1 95  LEU 95  95  95  LEU LEU H . n 
H 1 96  LYS 96  96  96  LYS LYS H . n 
H 1 97  ALA 97  97  97  ALA ALA H . n 
H 1 98  THR 98  98  98  THR THR H . n 
H 1 99  LYS 99  99  99  LYS LYS H . n 
H 1 100 ASP 100 100 100 ASP ASP H . n 
H 1 101 LEU 101 101 101 LEU LEU H . n 
H 1 102 ARG 102 102 102 ARG ARG H . n 
H 1 103 GLU 103 103 103 GLU GLU H . n 
H 1 104 ALA 104 104 104 ALA ALA H . n 
H 1 105 ILE 105 105 105 ILE ILE H . n 
H 1 106 VAL 106 106 106 VAL VAL H . n 
H 1 107 HIS 107 107 107 HIS HIS H . n 
H 1 108 CYS 108 108 108 CYS CYS H . n 
H 1 109 GLU 109 109 109 GLU GLU H . n 
H 1 110 GLN 110 110 110 GLN GLN H . n 
H 1 111 VAL 111 111 111 VAL VAL H . n 
H 1 112 HIS 112 112 112 HIS HIS H . n 
H 1 113 ASP 113 113 113 ASP ASP H . n 
H 1 114 TYR 114 114 114 TYR TYR H . n 
H 1 115 VAL 115 115 115 VAL VAL H . n 
H 1 116 SER 116 116 116 SER SER H . n 
H 1 117 ARG 117 117 117 ARG ARG H . n 
H 1 118 ASP 118 118 118 ASP ASP H . n 
H 1 119 LEU 119 119 119 LEU LEU H . n 
H 1 120 LEU 120 120 120 LEU LEU H . n 
H 1 121 LYS 121 121 121 LYS LYS H . n 
H 1 122 ASP 122 122 122 ASP ASP H . n 
H 1 123 ILE 123 123 123 ILE ILE H . n 
H 1 124 LEU 124 124 124 LEU LEU H . n 
H 1 125 GLU 125 125 125 GLU GLU H . n 
H 1 126 SER 126 126 126 SER SER H . n 
H 1 127 GLU 127 127 127 GLU GLU H . n 
H 1 128 GLU 128 128 128 GLU GLU H . n 
H 1 129 GLU 129 129 129 GLU GLU H . n 
H 1 130 HIS 130 130 130 HIS HIS H . n 
H 1 131 ILE 131 131 131 ILE ILE H . n 
H 1 132 ASP 132 132 132 ASP ASP H . n 
H 1 133 TYR 133 133 133 TYR TYR H . n 
H 1 134 LEU 134 134 134 LEU LEU H . n 
H 1 135 GLU 135 135 135 GLU GLU H . n 
H 1 136 THR 136 136 136 THR THR H . n 
H 1 137 GLN 137 137 137 GLN GLN H . n 
H 1 138 LEU 138 138 138 LEU LEU H . n 
H 1 139 GLY 139 139 139 GLY GLY H . n 
H 1 140 LEU 140 140 140 LEU LEU H . n 
H 1 141 ILE 141 141 141 ILE ILE H . n 
H 1 142 GLN 142 142 142 GLN GLN H . n 
H 1 143 LYS 143 143 143 LYS LYS H . n 
H 1 144 VAL 144 144 144 VAL VAL H . n 
H 1 145 GLY 145 145 145 GLY GLY H . n 
H 1 146 LEU 146 146 146 LEU LEU H . n 
H 1 147 GLU 147 147 147 GLU GLU H . n 
H 1 148 ASN 148 148 148 ASN ASN H . n 
H 1 149 TYR 149 149 149 TYR TYR H . n 
H 1 150 LEU 150 150 150 LEU LEU H . n 
H 1 151 GLN 151 151 151 GLN GLN H . n 
H 1 152 SER 152 152 152 SER SER H . n 
H 1 153 HIS 153 153 153 HIS HIS H . n 
H 1 154 MET 154 154 154 MET MET H . n 
H 1 155 HIS 155 155 155 HIS HIS H . n 
H 1 156 GLU 156 156 156 GLU GLU H . n 
H 1 157 ASP 157 157 ?   ?   ?   H . n 
H 1 158 ASP 158 158 ?   ?   ?   H . n 
I 1 1   MET 1   1   1   MET MET I . n 
I 1 2   LYS 2   2   2   LYS LYS I . n 
I 1 3   GLY 3   3   3   GLY GLY I . n 
I 1 4   ASP 4   4   4   ASP ASP I . n 
I 1 5   LYS 5   5   5   LYS LYS I . n 
I 1 6   LYS 6   6   6   LYS LYS I . n 
I 1 7   VAL 7   7   7   VAL VAL I . n 
I 1 8   ILE 8   8   8   ILE ILE I . n 
I 1 9   GLN 9   9   9   GLN GLN I . n 
I 1 10  HIS 10  10  10  HIS HIS I . n 
I 1 11  LEU 11  11  11  LEU LEU I . n 
I 1 12  ASN 12  12  12  ASN ASN I . n 
I 1 13  LYS 13  13  13  LYS LYS I . n 
I 1 14  ILE 14  14  14  ILE ILE I . n 
I 1 15  LEU 15  15  15  LEU LEU I . n 
I 1 16  GLY 16  16  16  GLY GLY I . n 
I 1 17  ASN 17  17  17  ASN ASN I . n 
I 1 18  GLU 18  18  18  GLU GLU I . n 
I 1 19  LEU 19  19  19  LEU LEU I . n 
I 1 20  ILE 20  20  20  ILE ILE I . n 
I 1 21  ALA 21  21  21  ALA ALA I . n 
I 1 22  ILE 22  22  22  ILE ILE I . n 
I 1 23  ASN 23  23  23  ASN ASN I . n 
I 1 24  GLN 24  24  24  GLN GLN I . n 
I 1 25  TYR 25  25  25  TYR TYR I . n 
I 1 26  PHE 26  26  26  PHE PHE I . n 
I 1 27  LEU 27  27  27  LEU LEU I . n 
I 1 28  HIS 28  28  28  HIS HIS I . n 
I 1 29  SER 29  29  29  SER SER I . n 
I 1 30  ARG 30  30  30  ARG ARG I . n 
I 1 31  MET 31  31  31  MET MET I . n 
I 1 32  TRP 32  32  32  TRP TRP I . n 
I 1 33  ASN 33  33  33  ASN ASN I . n 
I 1 34  ASP 34  34  34  ASP ASP I . n 
I 1 35  TRP 35  35  35  TRP TRP I . n 
I 1 36  GLY 36  36  36  GLY GLY I . n 
I 1 37  LEU 37  37  37  LEU LEU I . n 
I 1 38  LYS 38  38  38  LYS LYS I . n 
I 1 39  ARG 39  39  39  ARG ARG I . n 
I 1 40  LEU 40  40  40  LEU LEU I . n 
I 1 41  GLY 41  41  41  GLY GLY I . n 
I 1 42  ALA 42  42  42  ALA ALA I . n 
I 1 43  HIS 43  43  43  HIS HIS I . n 
I 1 44  GLU 44  44  44  GLU GLU I . n 
I 1 45  TYR 45  45  45  TYR TYR I . n 
I 1 46  HIS 46  46  46  HIS HIS I . n 
I 1 47  GLU 47  47  47  GLU GLU I . n 
I 1 48  SER 48  48  48  SER SER I . n 
I 1 49  ILE 49  49  49  ILE ILE I . n 
I 1 50  ASP 50  50  50  ASP ASP I . n 
I 1 51  GLU 51  51  51  GLU GLU I . n 
I 1 52  MET 52  52  52  MET MET I . n 
I 1 53  LYS 53  53  53  LYS LYS I . n 
I 1 54  HIS 54  54  54  HIS HIS I . n 
I 1 55  ALA 55  55  55  ALA ALA I . n 
I 1 56  ASP 56  56  56  ASP ASP I . n 
I 1 57  LYS 57  57  57  LYS LYS I . n 
I 1 58  LEU 58  58  58  LEU LEU I . n 
I 1 59  ILE 59  59  59  ILE ILE I . n 
I 1 60  GLU 60  60  60  GLU GLU I . n 
I 1 61  ARG 61  61  61  ARG ARG I . n 
I 1 62  ILE 62  62  62  ILE ILE I . n 
I 1 63  LEU 63  63  63  LEU LEU I . n 
I 1 64  PHE 64  64  64  PHE PHE I . n 
I 1 65  LEU 65  65  65  LEU LEU I . n 
I 1 66  GLU 66  66  66  GLU GLU I . n 
I 1 67  GLY 67  67  67  GLY GLY I . n 
I 1 68  LEU 68  68  68  LEU LEU I . n 
I 1 69  PRO 69  69  69  PRO PRO I . n 
I 1 70  ASN 70  70  70  ASN ASN I . n 
I 1 71  LEU 71  71  71  LEU LEU I . n 
I 1 72  GLN 72  72  72  GLN GLN I . n 
I 1 73  ASP 73  73  73  ASP ASP I . n 
I 1 74  LEU 74  74  74  LEU LEU I . n 
I 1 75  GLY 75  75  75  GLY GLY I . n 
I 1 76  LYS 76  76  76  LYS LYS I . n 
I 1 77  LEU 77  77  77  LEU LEU I . n 
I 1 78  LEU 78  78  78  LEU LEU I . n 
I 1 79  ILE 79  79  79  ILE ILE I . n 
I 1 80  GLY 80  80  80  GLY GLY I . n 
I 1 81  GLU 81  81  81  GLU GLU I . n 
I 1 82  ASN 82  82  82  ASN ASN I . n 
I 1 83  THR 83  83  83  THR THR I . n 
I 1 84  GLN 84  84  84  GLN GLN I . n 
I 1 85  GLU 85  85  85  GLU GLU I . n 
I 1 86  MET 86  86  86  MET MET I . n 
I 1 87  LEU 87  87  87  LEU LEU I . n 
I 1 88  GLN 88  88  88  GLN GLN I . n 
I 1 89  CYS 89  89  89  CYS CYS I . n 
I 1 90  ASP 90  90  90  ASP ASP I . n 
I 1 91  LEU 91  91  91  LEU LEU I . n 
I 1 92  ASN 92  92  92  ASN ASN I . n 
I 1 93  LEU 93  93  93  LEU LEU I . n 
I 1 94  GLU 94  94  94  GLU GLU I . n 
I 1 95  LEU 95  95  95  LEU LEU I . n 
I 1 96  LYS 96  96  96  LYS LYS I . n 
I 1 97  ALA 97  97  97  ALA ALA I . n 
I 1 98  THR 98  98  98  THR THR I . n 
I 1 99  LYS 99  99  99  LYS LYS I . n 
I 1 100 ASP 100 100 100 ASP ASP I . n 
I 1 101 LEU 101 101 101 LEU LEU I . n 
I 1 102 ARG 102 102 102 ARG ARG I . n 
I 1 103 GLU 103 103 103 GLU GLU I . n 
I 1 104 ALA 104 104 104 ALA ALA I . n 
I 1 105 ILE 105 105 105 ILE ILE I . n 
I 1 106 VAL 106 106 106 VAL VAL I . n 
I 1 107 HIS 107 107 107 HIS HIS I . n 
I 1 108 CYS 108 108 108 CYS CYS I . n 
I 1 109 GLU 109 109 109 GLU GLU I . n 
I 1 110 GLN 110 110 110 GLN GLN I . n 
I 1 111 VAL 111 111 111 VAL VAL I . n 
I 1 112 HIS 112 112 112 HIS HIS I . n 
I 1 113 ASP 113 113 113 ASP ASP I . n 
I 1 114 TYR 114 114 114 TYR TYR I . n 
I 1 115 VAL 115 115 115 VAL VAL I . n 
I 1 116 SER 116 116 116 SER SER I . n 
I 1 117 ARG 117 117 117 ARG ARG I . n 
I 1 118 ASP 118 118 118 ASP ASP I . n 
I 1 119 LEU 119 119 119 LEU LEU I . n 
I 1 120 LEU 120 120 120 LEU LEU I . n 
I 1 121 LYS 121 121 121 LYS LYS I . n 
I 1 122 ASP 122 122 122 ASP ASP I . n 
I 1 123 ILE 123 123 123 ILE ILE I . n 
I 1 124 LEU 124 124 124 LEU LEU I . n 
I 1 125 GLU 125 125 125 GLU GLU I . n 
I 1 126 SER 126 126 126 SER SER I . n 
I 1 127 GLU 127 127 127 GLU GLU I . n 
I 1 128 GLU 128 128 128 GLU GLU I . n 
I 1 129 GLU 129 129 129 GLU GLU I . n 
I 1 130 HIS 130 130 130 HIS HIS I . n 
I 1 131 ILE 131 131 131 ILE ILE I . n 
I 1 132 ASP 132 132 132 ASP ASP I . n 
I 1 133 TYR 133 133 133 TYR TYR I . n 
I 1 134 LEU 134 134 134 LEU LEU I . n 
I 1 135 GLU 135 135 135 GLU GLU I . n 
I 1 136 THR 136 136 136 THR THR I . n 
I 1 137 GLN 137 137 137 GLN GLN I . n 
I 1 138 LEU 138 138 138 LEU LEU I . n 
I 1 139 GLY 139 139 139 GLY GLY I . n 
I 1 140 LEU 140 140 140 LEU LEU I . n 
I 1 141 ILE 141 141 141 ILE ILE I . n 
I 1 142 GLN 142 142 142 GLN GLN I . n 
I 1 143 LYS 143 143 143 LYS LYS I . n 
I 1 144 VAL 144 144 144 VAL VAL I . n 
I 1 145 GLY 145 145 145 GLY GLY I . n 
I 1 146 LEU 146 146 146 LEU LEU I . n 
I 1 147 GLU 147 147 147 GLU GLU I . n 
I 1 148 ASN 148 148 148 ASN ASN I . n 
I 1 149 TYR 149 149 149 TYR TYR I . n 
I 1 150 LEU 150 150 150 LEU LEU I . n 
I 1 151 GLN 151 151 151 GLN GLN I . n 
I 1 152 SER 152 152 152 SER SER I . n 
I 1 153 HIS 153 153 153 HIS HIS I . n 
I 1 154 MET 154 154 154 MET MET I . n 
I 1 155 HIS 155 155 155 HIS HIS I . n 
I 1 156 GLU 156 156 156 GLU GLU I . n 
I 1 157 ASP 157 157 ?   ?   ?   I . n 
I 1 158 ASP 158 158 ?   ?   ?   I . n 
J 1 1   MET 1   1   1   MET MET J . n 
J 1 2   LYS 2   2   2   LYS LYS J . n 
J 1 3   GLY 3   3   3   GLY GLY J . n 
J 1 4   ASP 4   4   4   ASP ASP J . n 
J 1 5   LYS 5   5   5   LYS LYS J . n 
J 1 6   LYS 6   6   6   LYS LYS J . n 
J 1 7   VAL 7   7   7   VAL VAL J . n 
J 1 8   ILE 8   8   8   ILE ILE J . n 
J 1 9   GLN 9   9   9   GLN GLN J . n 
J 1 10  HIS 10  10  10  HIS HIS J . n 
J 1 11  LEU 11  11  11  LEU LEU J . n 
J 1 12  ASN 12  12  12  ASN ASN J . n 
J 1 13  LYS 13  13  13  LYS LYS J . n 
J 1 14  ILE 14  14  14  ILE ILE J . n 
J 1 15  LEU 15  15  15  LEU LEU J . n 
J 1 16  GLY 16  16  16  GLY GLY J . n 
J 1 17  ASN 17  17  17  ASN ASN J . n 
J 1 18  GLU 18  18  18  GLU GLU J . n 
J 1 19  LEU 19  19  19  LEU LEU J . n 
J 1 20  ILE 20  20  20  ILE ILE J . n 
J 1 21  ALA 21  21  21  ALA ALA J . n 
J 1 22  ILE 22  22  22  ILE ILE J . n 
J 1 23  ASN 23  23  23  ASN ASN J . n 
J 1 24  GLN 24  24  24  GLN GLN J . n 
J 1 25  TYR 25  25  25  TYR TYR J . n 
J 1 26  PHE 26  26  26  PHE PHE J . n 
J 1 27  LEU 27  27  27  LEU LEU J . n 
J 1 28  HIS 28  28  28  HIS HIS J . n 
J 1 29  SER 29  29  29  SER SER J . n 
J 1 30  ARG 30  30  30  ARG ARG J . n 
J 1 31  MET 31  31  31  MET MET J . n 
J 1 32  TRP 32  32  32  TRP TRP J . n 
J 1 33  ASN 33  33  33  ASN ASN J . n 
J 1 34  ASP 34  34  34  ASP ASP J . n 
J 1 35  TRP 35  35  35  TRP TRP J . n 
J 1 36  GLY 36  36  36  GLY GLY J . n 
J 1 37  LEU 37  37  37  LEU LEU J . n 
J 1 38  LYS 38  38  38  LYS LYS J . n 
J 1 39  ARG 39  39  39  ARG ARG J . n 
J 1 40  LEU 40  40  40  LEU LEU J . n 
J 1 41  GLY 41  41  41  GLY GLY J . n 
J 1 42  ALA 42  42  42  ALA ALA J . n 
J 1 43  HIS 43  43  43  HIS HIS J . n 
J 1 44  GLU 44  44  44  GLU GLU J . n 
J 1 45  TYR 45  45  45  TYR TYR J . n 
J 1 46  HIS 46  46  46  HIS HIS J . n 
J 1 47  GLU 47  47  47  GLU GLU J . n 
J 1 48  SER 48  48  48  SER SER J . n 
J 1 49  ILE 49  49  49  ILE ILE J . n 
J 1 50  ASP 50  50  50  ASP ASP J . n 
J 1 51  GLU 51  51  51  GLU GLU J . n 
J 1 52  MET 52  52  52  MET MET J . n 
J 1 53  LYS 53  53  53  LYS LYS J . n 
J 1 54  HIS 54  54  54  HIS HIS J . n 
J 1 55  ALA 55  55  55  ALA ALA J . n 
J 1 56  ASP 56  56  56  ASP ASP J . n 
J 1 57  LYS 57  57  57  LYS LYS J . n 
J 1 58  LEU 58  58  58  LEU LEU J . n 
J 1 59  ILE 59  59  59  ILE ILE J . n 
J 1 60  GLU 60  60  60  GLU GLU J . n 
J 1 61  ARG 61  61  61  ARG ARG J . n 
J 1 62  ILE 62  62  62  ILE ILE J . n 
J 1 63  LEU 63  63  63  LEU LEU J . n 
J 1 64  PHE 64  64  64  PHE PHE J . n 
J 1 65  LEU 65  65  65  LEU LEU J . n 
J 1 66  GLU 66  66  66  GLU GLU J . n 
J 1 67  GLY 67  67  67  GLY GLY J . n 
J 1 68  LEU 68  68  68  LEU LEU J . n 
J 1 69  PRO 69  69  69  PRO PRO J . n 
J 1 70  ASN 70  70  70  ASN ASN J . n 
J 1 71  LEU 71  71  71  LEU LEU J . n 
J 1 72  GLN 72  72  72  GLN GLN J . n 
J 1 73  ASP 73  73  73  ASP ASP J . n 
J 1 74  LEU 74  74  74  LEU LEU J . n 
J 1 75  GLY 75  75  75  GLY GLY J . n 
J 1 76  LYS 76  76  76  LYS LYS J . n 
J 1 77  LEU 77  77  77  LEU LEU J . n 
J 1 78  LEU 78  78  78  LEU LEU J . n 
J 1 79  ILE 79  79  79  ILE ILE J . n 
J 1 80  GLY 80  80  80  GLY GLY J . n 
J 1 81  GLU 81  81  81  GLU GLU J . n 
J 1 82  ASN 82  82  82  ASN ASN J . n 
J 1 83  THR 83  83  83  THR THR J . n 
J 1 84  GLN 84  84  84  GLN GLN J . n 
J 1 85  GLU 85  85  85  GLU GLU J . n 
J 1 86  MET 86  86  86  MET MET J . n 
J 1 87  LEU 87  87  87  LEU LEU J . n 
J 1 88  GLN 88  88  88  GLN GLN J . n 
J 1 89  CYS 89  89  89  CYS CYS J . n 
J 1 90  ASP 90  90  90  ASP ASP J . n 
J 1 91  LEU 91  91  91  LEU LEU J . n 
J 1 92  ASN 92  92  92  ASN ASN J . n 
J 1 93  LEU 93  93  93  LEU LEU J . n 
J 1 94  GLU 94  94  94  GLU GLU J . n 
J 1 95  LEU 95  95  95  LEU LEU J . n 
J 1 96  LYS 96  96  96  LYS LYS J . n 
J 1 97  ALA 97  97  97  ALA ALA J . n 
J 1 98  THR 98  98  98  THR THR J . n 
J 1 99  LYS 99  99  99  LYS LYS J . n 
J 1 100 ASP 100 100 100 ASP ASP J . n 
J 1 101 LEU 101 101 101 LEU LEU J . n 
J 1 102 ARG 102 102 102 ARG ARG J . n 
J 1 103 GLU 103 103 103 GLU GLU J . n 
J 1 104 ALA 104 104 104 ALA ALA J . n 
J 1 105 ILE 105 105 105 ILE ILE J . n 
J 1 106 VAL 106 106 106 VAL VAL J . n 
J 1 107 HIS 107 107 107 HIS HIS J . n 
J 1 108 CYS 108 108 108 CYS CYS J . n 
J 1 109 GLU 109 109 109 GLU GLU J . n 
J 1 110 GLN 110 110 110 GLN GLN J . n 
J 1 111 VAL 111 111 111 VAL VAL J . n 
J 1 112 HIS 112 112 112 HIS HIS J . n 
J 1 113 ASP 113 113 113 ASP ASP J . n 
J 1 114 TYR 114 114 114 TYR TYR J . n 
J 1 115 VAL 115 115 115 VAL VAL J . n 
J 1 116 SER 116 116 116 SER SER J . n 
J 1 117 ARG 117 117 117 ARG ARG J . n 
J 1 118 ASP 118 118 118 ASP ASP J . n 
J 1 119 LEU 119 119 119 LEU LEU J . n 
J 1 120 LEU 120 120 120 LEU LEU J . n 
J 1 121 LYS 121 121 121 LYS LYS J . n 
J 1 122 ASP 122 122 122 ASP ASP J . n 
J 1 123 ILE 123 123 123 ILE ILE J . n 
J 1 124 LEU 124 124 124 LEU LEU J . n 
J 1 125 GLU 125 125 125 GLU GLU J . n 
J 1 126 SER 126 126 126 SER SER J . n 
J 1 127 GLU 127 127 127 GLU GLU J . n 
J 1 128 GLU 128 128 128 GLU GLU J . n 
J 1 129 GLU 129 129 129 GLU GLU J . n 
J 1 130 HIS 130 130 130 HIS HIS J . n 
J 1 131 ILE 131 131 131 ILE ILE J . n 
J 1 132 ASP 132 132 132 ASP ASP J . n 
J 1 133 TYR 133 133 133 TYR TYR J . n 
J 1 134 LEU 134 134 134 LEU LEU J . n 
J 1 135 GLU 135 135 135 GLU GLU J . n 
J 1 136 THR 136 136 136 THR THR J . n 
J 1 137 GLN 137 137 137 GLN GLN J . n 
J 1 138 LEU 138 138 138 LEU LEU J . n 
J 1 139 GLY 139 139 139 GLY GLY J . n 
J 1 140 LEU 140 140 140 LEU LEU J . n 
J 1 141 ILE 141 141 141 ILE ILE J . n 
J 1 142 GLN 142 142 142 GLN GLN J . n 
J 1 143 LYS 143 143 143 LYS LYS J . n 
J 1 144 VAL 144 144 144 VAL VAL J . n 
J 1 145 GLY 145 145 145 GLY GLY J . n 
J 1 146 LEU 146 146 146 LEU LEU J . n 
J 1 147 GLU 147 147 147 GLU GLU J . n 
J 1 148 ASN 148 148 148 ASN ASN J . n 
J 1 149 TYR 149 149 149 TYR TYR J . n 
J 1 150 LEU 150 150 150 LEU LEU J . n 
J 1 151 GLN 151 151 151 GLN GLN J . n 
J 1 152 SER 152 152 152 SER SER J . n 
J 1 153 HIS 153 153 153 HIS HIS J . n 
J 1 154 MET 154 154 154 MET MET J . n 
J 1 155 HIS 155 155 155 HIS HIS J . n 
J 1 156 GLU 156 156 156 GLU GLU J . n 
J 1 157 ASP 157 157 ?   ?   ?   J . n 
J 1 158 ASP 158 158 ?   ?   ?   J . n 
K 1 1   MET 1   1   1   MET MET K . n 
K 1 2   LYS 2   2   2   LYS LYS K . n 
K 1 3   GLY 3   3   3   GLY GLY K . n 
K 1 4   ASP 4   4   4   ASP ASP K . n 
K 1 5   LYS 5   5   5   LYS LYS K . n 
K 1 6   LYS 6   6   6   LYS LYS K . n 
K 1 7   VAL 7   7   7   VAL VAL K . n 
K 1 8   ILE 8   8   8   ILE ILE K . n 
K 1 9   GLN 9   9   9   GLN GLN K . n 
K 1 10  HIS 10  10  10  HIS HIS K . n 
K 1 11  LEU 11  11  11  LEU LEU K . n 
K 1 12  ASN 12  12  12  ASN ASN K . n 
K 1 13  LYS 13  13  13  LYS LYS K . n 
K 1 14  ILE 14  14  14  ILE ILE K . n 
K 1 15  LEU 15  15  15  LEU LEU K . n 
K 1 16  GLY 16  16  16  GLY GLY K . n 
K 1 17  ASN 17  17  17  ASN ASN K . n 
K 1 18  GLU 18  18  18  GLU GLU K . n 
K 1 19  LEU 19  19  19  LEU LEU K . n 
K 1 20  ILE 20  20  20  ILE ILE K . n 
K 1 21  ALA 21  21  21  ALA ALA K . n 
K 1 22  ILE 22  22  22  ILE ILE K . n 
K 1 23  ASN 23  23  23  ASN ASN K . n 
K 1 24  GLN 24  24  24  GLN GLN K . n 
K 1 25  TYR 25  25  25  TYR TYR K . n 
K 1 26  PHE 26  26  26  PHE PHE K . n 
K 1 27  LEU 27  27  27  LEU LEU K . n 
K 1 28  HIS 28  28  28  HIS HIS K . n 
K 1 29  SER 29  29  29  SER SER K . n 
K 1 30  ARG 30  30  30  ARG ARG K . n 
K 1 31  MET 31  31  31  MET MET K . n 
K 1 32  TRP 32  32  32  TRP TRP K . n 
K 1 33  ASN 33  33  33  ASN ASN K . n 
K 1 34  ASP 34  34  34  ASP ASP K . n 
K 1 35  TRP 35  35  35  TRP TRP K . n 
K 1 36  GLY 36  36  36  GLY GLY K . n 
K 1 37  LEU 37  37  37  LEU LEU K . n 
K 1 38  LYS 38  38  38  LYS LYS K . n 
K 1 39  ARG 39  39  39  ARG ARG K . n 
K 1 40  LEU 40  40  40  LEU LEU K . n 
K 1 41  GLY 41  41  41  GLY GLY K . n 
K 1 42  ALA 42  42  42  ALA ALA K . n 
K 1 43  HIS 43  43  43  HIS HIS K . n 
K 1 44  GLU 44  44  44  GLU GLU K . n 
K 1 45  TYR 45  45  45  TYR TYR K . n 
K 1 46  HIS 46  46  46  HIS HIS K . n 
K 1 47  GLU 47  47  47  GLU GLU K . n 
K 1 48  SER 48  48  48  SER SER K . n 
K 1 49  ILE 49  49  49  ILE ILE K . n 
K 1 50  ASP 50  50  50  ASP ASP K . n 
K 1 51  GLU 51  51  51  GLU GLU K . n 
K 1 52  MET 52  52  52  MET MET K . n 
K 1 53  LYS 53  53  53  LYS LYS K . n 
K 1 54  HIS 54  54  54  HIS HIS K . n 
K 1 55  ALA 55  55  55  ALA ALA K . n 
K 1 56  ASP 56  56  56  ASP ASP K . n 
K 1 57  LYS 57  57  57  LYS LYS K . n 
K 1 58  LEU 58  58  58  LEU LEU K . n 
K 1 59  ILE 59  59  59  ILE ILE K . n 
K 1 60  GLU 60  60  60  GLU GLU K . n 
K 1 61  ARG 61  61  61  ARG ARG K . n 
K 1 62  ILE 62  62  62  ILE ILE K . n 
K 1 63  LEU 63  63  63  LEU LEU K . n 
K 1 64  PHE 64  64  64  PHE PHE K . n 
K 1 65  LEU 65  65  65  LEU LEU K . n 
K 1 66  GLU 66  66  66  GLU GLU K . n 
K 1 67  GLY 67  67  67  GLY GLY K . n 
K 1 68  LEU 68  68  68  LEU LEU K . n 
K 1 69  PRO 69  69  69  PRO PRO K . n 
K 1 70  ASN 70  70  70  ASN ASN K . n 
K 1 71  LEU 71  71  71  LEU LEU K . n 
K 1 72  GLN 72  72  72  GLN GLN K . n 
K 1 73  ASP 73  73  73  ASP ASP K . n 
K 1 74  LEU 74  74  74  LEU LEU K . n 
K 1 75  GLY 75  75  75  GLY GLY K . n 
K 1 76  LYS 76  76  76  LYS LYS K . n 
K 1 77  LEU 77  77  77  LEU LEU K . n 
K 1 78  LEU 78  78  78  LEU LEU K . n 
K 1 79  ILE 79  79  79  ILE ILE K . n 
K 1 80  GLY 80  80  80  GLY GLY K . n 
K 1 81  GLU 81  81  81  GLU GLU K . n 
K 1 82  ASN 82  82  82  ASN ASN K . n 
K 1 83  THR 83  83  83  THR THR K . n 
K 1 84  GLN 84  84  84  GLN GLN K . n 
K 1 85  GLU 85  85  85  GLU GLU K . n 
K 1 86  MET 86  86  86  MET MET K . n 
K 1 87  LEU 87  87  87  LEU LEU K . n 
K 1 88  GLN 88  88  88  GLN GLN K . n 
K 1 89  CYS 89  89  89  CYS CYS K . n 
K 1 90  ASP 90  90  90  ASP ASP K . n 
K 1 91  LEU 91  91  91  LEU LEU K . n 
K 1 92  ASN 92  92  92  ASN ASN K . n 
K 1 93  LEU 93  93  93  LEU LEU K . n 
K 1 94  GLU 94  94  94  GLU GLU K . n 
K 1 95  LEU 95  95  95  LEU LEU K . n 
K 1 96  LYS 96  96  96  LYS LYS K . n 
K 1 97  ALA 97  97  97  ALA ALA K . n 
K 1 98  THR 98  98  98  THR THR K . n 
K 1 99  LYS 99  99  99  LYS LYS K . n 
K 1 100 ASP 100 100 100 ASP ASP K . n 
K 1 101 LEU 101 101 101 LEU LEU K . n 
K 1 102 ARG 102 102 102 ARG ARG K . n 
K 1 103 GLU 103 103 103 GLU GLU K . n 
K 1 104 ALA 104 104 104 ALA ALA K . n 
K 1 105 ILE 105 105 105 ILE ILE K . n 
K 1 106 VAL 106 106 106 VAL VAL K . n 
K 1 107 HIS 107 107 107 HIS HIS K . n 
K 1 108 CYS 108 108 108 CYS CYS K . n 
K 1 109 GLU 109 109 109 GLU GLU K . n 
K 1 110 GLN 110 110 110 GLN GLN K . n 
K 1 111 VAL 111 111 111 VAL VAL K . n 
K 1 112 HIS 112 112 112 HIS HIS K . n 
K 1 113 ASP 113 113 113 ASP ASP K . n 
K 1 114 TYR 114 114 114 TYR TYR K . n 
K 1 115 VAL 115 115 115 VAL VAL K . n 
K 1 116 SER 116 116 116 SER SER K . n 
K 1 117 ARG 117 117 117 ARG ARG K . n 
K 1 118 ASP 118 118 118 ASP ASP K . n 
K 1 119 LEU 119 119 119 LEU LEU K . n 
K 1 120 LEU 120 120 120 LEU LEU K . n 
K 1 121 LYS 121 121 121 LYS LYS K . n 
K 1 122 ASP 122 122 122 ASP ASP K . n 
K 1 123 ILE 123 123 123 ILE ILE K . n 
K 1 124 LEU 124 124 124 LEU LEU K . n 
K 1 125 GLU 125 125 125 GLU GLU K . n 
K 1 126 SER 126 126 126 SER SER K . n 
K 1 127 GLU 127 127 127 GLU GLU K . n 
K 1 128 GLU 128 128 128 GLU GLU K . n 
K 1 129 GLU 129 129 129 GLU GLU K . n 
K 1 130 HIS 130 130 130 HIS HIS K . n 
K 1 131 ILE 131 131 131 ILE ILE K . n 
K 1 132 ASP 132 132 132 ASP ASP K . n 
K 1 133 TYR 133 133 133 TYR TYR K . n 
K 1 134 LEU 134 134 134 LEU LEU K . n 
K 1 135 GLU 135 135 135 GLU GLU K . n 
K 1 136 THR 136 136 136 THR THR K . n 
K 1 137 GLN 137 137 137 GLN GLN K . n 
K 1 138 LEU 138 138 138 LEU LEU K . n 
K 1 139 GLY 139 139 139 GLY GLY K . n 
K 1 140 LEU 140 140 140 LEU LEU K . n 
K 1 141 ILE 141 141 141 ILE ILE K . n 
K 1 142 GLN 142 142 142 GLN GLN K . n 
K 1 143 LYS 143 143 143 LYS LYS K . n 
K 1 144 VAL 144 144 144 VAL VAL K . n 
K 1 145 GLY 145 145 145 GLY GLY K . n 
K 1 146 LEU 146 146 146 LEU LEU K . n 
K 1 147 GLU 147 147 147 GLU GLU K . n 
K 1 148 ASN 148 148 148 ASN ASN K . n 
K 1 149 TYR 149 149 149 TYR TYR K . n 
K 1 150 LEU 150 150 150 LEU LEU K . n 
K 1 151 GLN 151 151 151 GLN GLN K . n 
K 1 152 SER 152 152 152 SER SER K . n 
K 1 153 HIS 153 153 153 HIS HIS K . n 
K 1 154 MET 154 154 154 MET MET K . n 
K 1 155 HIS 155 155 155 HIS HIS K . n 
K 1 156 GLU 156 156 156 GLU GLU K . n 
K 1 157 ASP 157 157 ?   ?   ?   K . n 
K 1 158 ASP 158 158 ?   ?   ?   K . n 
L 1 1   MET 1   1   1   MET MET L . n 
L 1 2   LYS 2   2   2   LYS LYS L . n 
L 1 3   GLY 3   3   3   GLY GLY L . n 
L 1 4   ASP 4   4   4   ASP ASP L . n 
L 1 5   LYS 5   5   5   LYS LYS L . n 
L 1 6   LYS 6   6   6   LYS LYS L . n 
L 1 7   VAL 7   7   7   VAL VAL L . n 
L 1 8   ILE 8   8   8   ILE ILE L . n 
L 1 9   GLN 9   9   9   GLN GLN L . n 
L 1 10  HIS 10  10  10  HIS HIS L . n 
L 1 11  LEU 11  11  11  LEU LEU L . n 
L 1 12  ASN 12  12  12  ASN ASN L . n 
L 1 13  LYS 13  13  13  LYS LYS L . n 
L 1 14  ILE 14  14  14  ILE ILE L . n 
L 1 15  LEU 15  15  15  LEU LEU L . n 
L 1 16  GLY 16  16  16  GLY GLY L . n 
L 1 17  ASN 17  17  17  ASN ASN L . n 
L 1 18  GLU 18  18  18  GLU GLU L . n 
L 1 19  LEU 19  19  19  LEU LEU L . n 
L 1 20  ILE 20  20  20  ILE ILE L . n 
L 1 21  ALA 21  21  21  ALA ALA L . n 
L 1 22  ILE 22  22  22  ILE ILE L . n 
L 1 23  ASN 23  23  23  ASN ASN L . n 
L 1 24  GLN 24  24  24  GLN GLN L . n 
L 1 25  TYR 25  25  25  TYR TYR L . n 
L 1 26  PHE 26  26  26  PHE PHE L . n 
L 1 27  LEU 27  27  27  LEU LEU L . n 
L 1 28  HIS 28  28  28  HIS HIS L . n 
L 1 29  SER 29  29  29  SER SER L . n 
L 1 30  ARG 30  30  30  ARG ARG L . n 
L 1 31  MET 31  31  31  MET MET L . n 
L 1 32  TRP 32  32  32  TRP TRP L . n 
L 1 33  ASN 33  33  33  ASN ASN L . n 
L 1 34  ASP 34  34  34  ASP ASP L . n 
L 1 35  TRP 35  35  35  TRP TRP L . n 
L 1 36  GLY 36  36  36  GLY GLY L . n 
L 1 37  LEU 37  37  37  LEU LEU L . n 
L 1 38  LYS 38  38  38  LYS LYS L . n 
L 1 39  ARG 39  39  39  ARG ARG L . n 
L 1 40  LEU 40  40  40  LEU LEU L . n 
L 1 41  GLY 41  41  41  GLY GLY L . n 
L 1 42  ALA 42  42  42  ALA ALA L . n 
L 1 43  HIS 43  43  43  HIS HIS L . n 
L 1 44  GLU 44  44  44  GLU GLU L . n 
L 1 45  TYR 45  45  45  TYR TYR L . n 
L 1 46  HIS 46  46  46  HIS HIS L . n 
L 1 47  GLU 47  47  47  GLU GLU L . n 
L 1 48  SER 48  48  48  SER SER L . n 
L 1 49  ILE 49  49  49  ILE ILE L . n 
L 1 50  ASP 50  50  50  ASP ASP L . n 
L 1 51  GLU 51  51  51  GLU GLU L . n 
L 1 52  MET 52  52  52  MET MET L . n 
L 1 53  LYS 53  53  53  LYS LYS L . n 
L 1 54  HIS 54  54  54  HIS HIS L . n 
L 1 55  ALA 55  55  55  ALA ALA L . n 
L 1 56  ASP 56  56  56  ASP ASP L . n 
L 1 57  LYS 57  57  57  LYS LYS L . n 
L 1 58  LEU 58  58  58  LEU LEU L . n 
L 1 59  ILE 59  59  59  ILE ILE L . n 
L 1 60  GLU 60  60  60  GLU GLU L . n 
L 1 61  ARG 61  61  61  ARG ARG L . n 
L 1 62  ILE 62  62  62  ILE ILE L . n 
L 1 63  LEU 63  63  63  LEU LEU L . n 
L 1 64  PHE 64  64  64  PHE PHE L . n 
L 1 65  LEU 65  65  65  LEU LEU L . n 
L 1 66  GLU 66  66  66  GLU GLU L . n 
L 1 67  GLY 67  67  67  GLY GLY L . n 
L 1 68  LEU 68  68  68  LEU LEU L . n 
L 1 69  PRO 69  69  69  PRO PRO L . n 
L 1 70  ASN 70  70  70  ASN ASN L . n 
L 1 71  LEU 71  71  71  LEU LEU L . n 
L 1 72  GLN 72  72  72  GLN GLN L . n 
L 1 73  ASP 73  73  73  ASP ASP L . n 
L 1 74  LEU 74  74  74  LEU LEU L . n 
L 1 75  GLY 75  75  75  GLY GLY L . n 
L 1 76  LYS 76  76  76  LYS LYS L . n 
L 1 77  LEU 77  77  77  LEU LEU L . n 
L 1 78  LEU 78  78  78  LEU LEU L . n 
L 1 79  ILE 79  79  79  ILE ILE L . n 
L 1 80  GLY 80  80  80  GLY GLY L . n 
L 1 81  GLU 81  81  81  GLU GLU L . n 
L 1 82  ASN 82  82  82  ASN ASN L . n 
L 1 83  THR 83  83  83  THR THR L . n 
L 1 84  GLN 84  84  84  GLN GLN L . n 
L 1 85  GLU 85  85  85  GLU GLU L . n 
L 1 86  MET 86  86  86  MET MET L . n 
L 1 87  LEU 87  87  87  LEU LEU L . n 
L 1 88  GLN 88  88  88  GLN GLN L . n 
L 1 89  CYS 89  89  89  CYS CYS L . n 
L 1 90  ASP 90  90  90  ASP ASP L . n 
L 1 91  LEU 91  91  91  LEU LEU L . n 
L 1 92  ASN 92  92  92  ASN ASN L . n 
L 1 93  LEU 93  93  93  LEU LEU L . n 
L 1 94  GLU 94  94  94  GLU GLU L . n 
L 1 95  LEU 95  95  95  LEU LEU L . n 
L 1 96  LYS 96  96  96  LYS LYS L . n 
L 1 97  ALA 97  97  97  ALA ALA L . n 
L 1 98  THR 98  98  98  THR THR L . n 
L 1 99  LYS 99  99  99  LYS LYS L . n 
L 1 100 ASP 100 100 100 ASP ASP L . n 
L 1 101 LEU 101 101 101 LEU LEU L . n 
L 1 102 ARG 102 102 102 ARG ARG L . n 
L 1 103 GLU 103 103 103 GLU GLU L . n 
L 1 104 ALA 104 104 104 ALA ALA L . n 
L 1 105 ILE 105 105 105 ILE ILE L . n 
L 1 106 VAL 106 106 106 VAL VAL L . n 
L 1 107 HIS 107 107 107 HIS HIS L . n 
L 1 108 CYS 108 108 108 CYS CYS L . n 
L 1 109 GLU 109 109 109 GLU GLU L . n 
L 1 110 GLN 110 110 110 GLN GLN L . n 
L 1 111 VAL 111 111 111 VAL VAL L . n 
L 1 112 HIS 112 112 112 HIS HIS L . n 
L 1 113 ASP 113 113 113 ASP ASP L . n 
L 1 114 TYR 114 114 114 TYR TYR L . n 
L 1 115 VAL 115 115 115 VAL VAL L . n 
L 1 116 SER 116 116 116 SER SER L . n 
L 1 117 ARG 117 117 117 ARG ARG L . n 
L 1 118 ASP 118 118 118 ASP ASP L . n 
L 1 119 LEU 119 119 119 LEU LEU L . n 
L 1 120 LEU 120 120 120 LEU LEU L . n 
L 1 121 LYS 121 121 121 LYS LYS L . n 
L 1 122 ASP 122 122 122 ASP ASP L . n 
L 1 123 ILE 123 123 123 ILE ILE L . n 
L 1 124 LEU 124 124 124 LEU LEU L . n 
L 1 125 GLU 125 125 125 GLU GLU L . n 
L 1 126 SER 126 126 126 SER SER L . n 
L 1 127 GLU 127 127 127 GLU GLU L . n 
L 1 128 GLU 128 128 128 GLU GLU L . n 
L 1 129 GLU 129 129 129 GLU GLU L . n 
L 1 130 HIS 130 130 130 HIS HIS L . n 
L 1 131 ILE 131 131 131 ILE ILE L . n 
L 1 132 ASP 132 132 132 ASP ASP L . n 
L 1 133 TYR 133 133 133 TYR TYR L . n 
L 1 134 LEU 134 134 134 LEU LEU L . n 
L 1 135 GLU 135 135 135 GLU GLU L . n 
L 1 136 THR 136 136 136 THR THR L . n 
L 1 137 GLN 137 137 137 GLN GLN L . n 
L 1 138 LEU 138 138 138 LEU LEU L . n 
L 1 139 GLY 139 139 139 GLY GLY L . n 
L 1 140 LEU 140 140 140 LEU LEU L . n 
L 1 141 ILE 141 141 141 ILE ILE L . n 
L 1 142 GLN 142 142 142 GLN GLN L . n 
L 1 143 LYS 143 143 143 LYS LYS L . n 
L 1 144 VAL 144 144 144 VAL VAL L . n 
L 1 145 GLY 145 145 145 GLY GLY L . n 
L 1 146 LEU 146 146 146 LEU LEU L . n 
L 1 147 GLU 147 147 147 GLU GLU L . n 
L 1 148 ASN 148 148 148 ASN ASN L . n 
L 1 149 TYR 149 149 149 TYR TYR L . n 
L 1 150 LEU 150 150 150 LEU LEU L . n 
L 1 151 GLN 151 151 151 GLN GLN L . n 
L 1 152 SER 152 152 152 SER SER L . n 
L 1 153 HIS 153 153 153 HIS HIS L . n 
L 1 154 MET 154 154 154 MET MET L . n 
L 1 155 HIS 155 155 155 HIS HIS L . n 
L 1 156 GLU 156 156 156 GLU GLU L . n 
L 1 157 ASP 157 157 ?   ?   ?   L . n 
L 1 158 ASP 158 158 ?   ?   ?   L . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BYB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BYB 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
M  2 K     1  201 201 K     K   A . 
N  3 HEM   1  202 205 HEM   HEM A . 
O  2 K     1  201 201 K     K   B . 
P  4 PG4   1  202 204 PG4   PG4 B . 
Q  5 A1BYB 1  203 2   A1BYB K25 B . 
R  5 A1BYB 1  201 3   A1BYB K25 C . 
S  2 K     1  201 201 K     K   D . 
T  3 HEM   1  202 203 HEM   HEM D . 
U  4 PG4   1  203 204 PG4   PG4 D . 
V  3 HEM   1  201 203 HEM   HEM E . 
W  4 PG4   1  202 201 PG4   PG4 E . 
X  5 A1BYB 1  203 5   A1BYB K25 E . 
Y  3 HEM   1  201 203 HEM   HEM F . 
Z  5 A1BYB 1  202 6   A1BYB K25 F . 
AA 4 PG4   1  201 201 PG4   PG4 G . 
BA 4 PG4   1  201 201 PG4   PG4 H . 
CA 3 HEM   1  202 204 HEM   HEM H . 
DA 5 A1BYB 1  203 8   A1BYB K25 H . 
EA 3 HEM   1  201 202 HEM   HEM I . 
FA 4 PG4   1  202 203 PG4   PG4 I . 
GA 5 A1BYB 1  203 9   A1BYB K25 I . 
HA 4 PG4   1  201 205 PG4   PG4 J . 
IA 5 A1BYB 1  202 10  A1BYB K25 J . 
JA 5 A1BYB 1  201 11  A1BYB K25 K . 
KA 3 HEM   1  201 203 HEM   HEM L . 
LA 4 PG4   1  202 204 PG4   PG4 L . 
MA 5 A1BYB 1  203 12  A1BYB K25 L . 
NA 6 HOH   1  301 684 HOH   HOH A . 
NA 6 HOH   2  302 497 HOH   HOH A . 
NA 6 HOH   3  303 16  HOH   HOH A . 
NA 6 HOH   4  304 438 HOH   HOH A . 
NA 6 HOH   5  305 250 HOH   HOH A . 
NA 6 HOH   6  306 147 HOH   HOH A . 
NA 6 HOH   7  307 331 HOH   HOH A . 
NA 6 HOH   8  308 333 HOH   HOH A . 
NA 6 HOH   9  309 292 HOH   HOH A . 
NA 6 HOH   10 310 492 HOH   HOH A . 
NA 6 HOH   11 311 429 HOH   HOH A . 
NA 6 HOH   12 312 180 HOH   HOH A . 
NA 6 HOH   13 313 543 HOH   HOH A . 
NA 6 HOH   14 314 61  HOH   HOH A . 
NA 6 HOH   15 315 449 HOH   HOH A . 
NA 6 HOH   16 316 70  HOH   HOH A . 
NA 6 HOH   17 317 368 HOH   HOH A . 
NA 6 HOH   18 318 376 HOH   HOH A . 
NA 6 HOH   19 319 387 HOH   HOH A . 
NA 6 HOH   20 320 160 HOH   HOH A . 
NA 6 HOH   21 321 354 HOH   HOH A . 
NA 6 HOH   22 322 356 HOH   HOH A . 
NA 6 HOH   23 323 487 HOH   HOH A . 
NA 6 HOH   24 324 142 HOH   HOH A . 
NA 6 HOH   25 325 231 HOH   HOH A . 
NA 6 HOH   26 326 494 HOH   HOH A . 
NA 6 HOH   27 327 97  HOH   HOH A . 
NA 6 HOH   28 328 211 HOH   HOH A . 
NA 6 HOH   29 329 313 HOH   HOH A . 
NA 6 HOH   30 330 407 HOH   HOH A . 
NA 6 HOH   31 331 110 HOH   HOH A . 
NA 6 HOH   32 332 113 HOH   HOH A . 
NA 6 HOH   33 333 35  HOH   HOH A . 
NA 6 HOH   34 334 328 HOH   HOH A . 
NA 6 HOH   35 335 409 HOH   HOH A . 
NA 6 HOH   36 336 153 HOH   HOH A . 
NA 6 HOH   37 337 143 HOH   HOH A . 
NA 6 HOH   38 338 245 HOH   HOH A . 
NA 6 HOH   39 339 629 HOH   HOH A . 
NA 6 HOH   40 340 269 HOH   HOH A . 
NA 6 HOH   41 341 159 HOH   HOH A . 
NA 6 HOH   42 342 619 HOH   HOH A . 
NA 6 HOH   43 343 606 HOH   HOH A . 
NA 6 HOH   44 344 18  HOH   HOH A . 
NA 6 HOH   45 345 156 HOH   HOH A . 
NA 6 HOH   46 346 308 HOH   HOH A . 
NA 6 HOH   47 347 688 HOH   HOH A . 
NA 6 HOH   48 348 432 HOH   HOH A . 
NA 6 HOH   49 349 635 HOH   HOH A . 
NA 6 HOH   50 350 640 HOH   HOH A . 
NA 6 HOH   51 351 680 HOH   HOH A . 
NA 6 HOH   52 352 88  HOH   HOH A . 
NA 6 HOH   53 353 94  HOH   HOH A . 
NA 6 HOH   54 354 77  HOH   HOH A . 
NA 6 HOH   55 355 675 HOH   HOH A . 
NA 6 HOH   56 356 403 HOH   HOH A . 
NA 6 HOH   57 357 633 HOH   HOH A . 
NA 6 HOH   58 358 468 HOH   HOH A . 
OA 6 HOH   1  301 593 HOH   HOH B . 
OA 6 HOH   2  302 149 HOH   HOH B . 
OA 6 HOH   3  303 676 HOH   HOH B . 
OA 6 HOH   4  304 90  HOH   HOH B . 
OA 6 HOH   5  305 201 HOH   HOH B . 
OA 6 HOH   6  306 234 HOH   HOH B . 
OA 6 HOH   7  307 482 HOH   HOH B . 
OA 6 HOH   8  308 49  HOH   HOH B . 
OA 6 HOH   9  309 288 HOH   HOH B . 
OA 6 HOH   10 310 374 HOH   HOH B . 
OA 6 HOH   11 311 358 HOH   HOH B . 
OA 6 HOH   12 312 103 HOH   HOH B . 
OA 6 HOH   13 313 86  HOH   HOH B . 
OA 6 HOH   14 314 631 HOH   HOH B . 
OA 6 HOH   15 315 262 HOH   HOH B . 
OA 6 HOH   16 316 284 HOH   HOH B . 
OA 6 HOH   17 317 232 HOH   HOH B . 
OA 6 HOH   18 318 466 HOH   HOH B . 
OA 6 HOH   19 319 540 HOH   HOH B . 
OA 6 HOH   20 320 138 HOH   HOH B . 
OA 6 HOH   21 321 83  HOH   HOH B . 
OA 6 HOH   22 322 405 HOH   HOH B . 
OA 6 HOH   23 323 116 HOH   HOH B . 
OA 6 HOH   24 324 398 HOH   HOH B . 
OA 6 HOH   25 325 188 HOH   HOH B . 
OA 6 HOH   26 326 316 HOH   HOH B . 
OA 6 HOH   27 327 318 HOH   HOH B . 
OA 6 HOH   28 328 154 HOH   HOH B . 
OA 6 HOH   29 329 162 HOH   HOH B . 
OA 6 HOH   30 330 62  HOH   HOH B . 
OA 6 HOH   31 331 152 HOH   HOH B . 
OA 6 HOH   32 332 336 HOH   HOH B . 
OA 6 HOH   33 333 383 HOH   HOH B . 
OA 6 HOH   34 334 109 HOH   HOH B . 
OA 6 HOH   35 335 60  HOH   HOH B . 
OA 6 HOH   36 336 190 HOH   HOH B . 
OA 6 HOH   37 337 29  HOH   HOH B . 
OA 6 HOH   38 338 192 HOH   HOH B . 
OA 6 HOH   39 339 205 HOH   HOH B . 
OA 6 HOH   40 340 4   HOH   HOH B . 
OA 6 HOH   41 341 663 HOH   HOH B . 
OA 6 HOH   42 342 8   HOH   HOH B . 
OA 6 HOH   43 343 474 HOH   HOH B . 
OA 6 HOH   44 344 578 HOH   HOH B . 
OA 6 HOH   45 345 655 HOH   HOH B . 
OA 6 HOH   46 346 9   HOH   HOH B . 
OA 6 HOH   47 347 520 HOH   HOH B . 
OA 6 HOH   48 348 493 HOH   HOH B . 
OA 6 HOH   49 349 588 HOH   HOH B . 
OA 6 HOH   50 350 339 HOH   HOH B . 
OA 6 HOH   51 351 55  HOH   HOH B . 
OA 6 HOH   52 352 624 HOH   HOH B . 
OA 6 HOH   53 353 1   HOH   HOH B . 
OA 6 HOH   54 354 372 HOH   HOH B . 
OA 6 HOH   55 355 672 HOH   HOH B . 
OA 6 HOH   56 356 64  HOH   HOH B . 
OA 6 HOH   57 357 423 HOH   HOH B . 
OA 6 HOH   58 358 666 HOH   HOH B . 
OA 6 HOH   59 359 134 HOH   HOH B . 
OA 6 HOH   60 360 195 HOH   HOH B . 
OA 6 HOH   61 361 401 HOH   HOH B . 
OA 6 HOH   62 362 667 HOH   HOH B . 
OA 6 HOH   63 363 582 HOH   HOH B . 
OA 6 HOH   64 364 419 HOH   HOH B . 
OA 6 HOH   65 365 579 HOH   HOH B . 
PA 6 HOH   1  301 489 HOH   HOH C . 
PA 6 HOH   2  302 479 HOH   HOH C . 
PA 6 HOH   3  303 562 HOH   HOH C . 
PA 6 HOH   4  304 287 HOH   HOH C . 
PA 6 HOH   5  305 38  HOH   HOH C . 
PA 6 HOH   6  306 39  HOH   HOH C . 
PA 6 HOH   7  307 185 HOH   HOH C . 
PA 6 HOH   8  308 430 HOH   HOH C . 
PA 6 HOH   9  309 364 HOH   HOH C . 
PA 6 HOH   10 310 457 HOH   HOH C . 
PA 6 HOH   11 311 674 HOH   HOH C . 
PA 6 HOH   12 312 544 HOH   HOH C . 
PA 6 HOH   13 313 657 HOH   HOH C . 
PA 6 HOH   14 314 233 HOH   HOH C . 
PA 6 HOH   15 315 183 HOH   HOH C . 
PA 6 HOH   16 316 278 HOH   HOH C . 
PA 6 HOH   17 317 36  HOH   HOH C . 
PA 6 HOH   18 318 459 HOH   HOH C . 
PA 6 HOH   19 319 340 HOH   HOH C . 
PA 6 HOH   20 320 361 HOH   HOH C . 
PA 6 HOH   21 321 283 HOH   HOH C . 
PA 6 HOH   22 322 151 HOH   HOH C . 
PA 6 HOH   23 323 413 HOH   HOH C . 
PA 6 HOH   24 324 537 HOH   HOH C . 
PA 6 HOH   25 325 332 HOH   HOH C . 
PA 6 HOH   26 326 478 HOH   HOH C . 
PA 6 HOH   27 327 100 HOH   HOH C . 
PA 6 HOH   28 328 574 HOH   HOH C . 
PA 6 HOH   29 329 120 HOH   HOH C . 
PA 6 HOH   30 330 176 HOH   HOH C . 
PA 6 HOH   31 331 45  HOH   HOH C . 
PA 6 HOH   32 332 538 HOH   HOH C . 
PA 6 HOH   33 333 99  HOH   HOH C . 
PA 6 HOH   34 334 256 HOH   HOH C . 
PA 6 HOH   35 335 465 HOH   HOH C . 
PA 6 HOH   36 336 56  HOH   HOH C . 
PA 6 HOH   37 337 568 HOH   HOH C . 
PA 6 HOH   38 338 384 HOH   HOH C . 
PA 6 HOH   39 339 73  HOH   HOH C . 
PA 6 HOH   40 340 66  HOH   HOH C . 
PA 6 HOH   41 341 173 HOH   HOH C . 
PA 6 HOH   42 342 199 HOH   HOH C . 
PA 6 HOH   43 343 505 HOH   HOH C . 
PA 6 HOH   44 344 602 HOH   HOH C . 
PA 6 HOH   45 345 448 HOH   HOH C . 
PA 6 HOH   46 346 391 HOH   HOH C . 
PA 6 HOH   47 347 651 HOH   HOH C . 
PA 6 HOH   48 348 526 HOH   HOH C . 
PA 6 HOH   49 349 71  HOH   HOH C . 
PA 6 HOH   50 350 303 HOH   HOH C . 
PA 6 HOH   51 351 44  HOH   HOH C . 
PA 6 HOH   52 352 597 HOH   HOH C . 
PA 6 HOH   53 353 139 HOH   HOH C . 
PA 6 HOH   54 354 648 HOH   HOH C . 
PA 6 HOH   55 355 630 HOH   HOH C . 
PA 6 HOH   56 356 547 HOH   HOH C . 
QA 6 HOH   1  301 265 HOH   HOH D . 
QA 6 HOH   2  302 519 HOH   HOH D . 
QA 6 HOH   3  303 27  HOH   HOH D . 
QA 6 HOH   4  304 175 HOH   HOH D . 
QA 6 HOH   5  305 523 HOH   HOH D . 
QA 6 HOH   6  306 302 HOH   HOH D . 
QA 6 HOH   7  307 206 HOH   HOH D . 
QA 6 HOH   8  308 671 HOH   HOH D . 
QA 6 HOH   9  309 444 HOH   HOH D . 
QA 6 HOH   10 310 522 HOH   HOH D . 
QA 6 HOH   11 311 500 HOH   HOH D . 
QA 6 HOH   12 312 242 HOH   HOH D . 
QA 6 HOH   13 313 416 HOH   HOH D . 
QA 6 HOH   14 314 507 HOH   HOH D . 
QA 6 HOH   15 315 274 HOH   HOH D . 
QA 6 HOH   16 316 692 HOH   HOH D . 
QA 6 HOH   17 317 337 HOH   HOH D . 
QA 6 HOH   18 318 426 HOH   HOH D . 
QA 6 HOH   19 319 207 HOH   HOH D . 
QA 6 HOH   20 320 461 HOH   HOH D . 
QA 6 HOH   21 321 610 HOH   HOH D . 
QA 6 HOH   22 322 122 HOH   HOH D . 
QA 6 HOH   23 323 293 HOH   HOH D . 
QA 6 HOH   24 324 350 HOH   HOH D . 
QA 6 HOH   25 325 451 HOH   HOH D . 
QA 6 HOH   26 326 611 HOH   HOH D . 
QA 6 HOH   27 327 386 HOH   HOH D . 
QA 6 HOH   28 328 268 HOH   HOH D . 
QA 6 HOH   29 329 46  HOH   HOH D . 
QA 6 HOH   30 330 575 HOH   HOH D . 
QA 6 HOH   31 331 132 HOH   HOH D . 
QA 6 HOH   32 332 454 HOH   HOH D . 
QA 6 HOH   33 333 601 HOH   HOH D . 
QA 6 HOH   34 334 163 HOH   HOH D . 
QA 6 HOH   35 335 363 HOH   HOH D . 
QA 6 HOH   36 336 628 HOH   HOH D . 
QA 6 HOH   37 337 607 HOH   HOH D . 
QA 6 HOH   38 338 417 HOH   HOH D . 
QA 6 HOH   39 339 166 HOH   HOH D . 
QA 6 HOH   40 340 695 HOH   HOH D . 
QA 6 HOH   41 341 279 HOH   HOH D . 
QA 6 HOH   42 342 353 HOH   HOH D . 
RA 6 HOH   1  301 485 HOH   HOH E . 
RA 6 HOH   2  302 297 HOH   HOH E . 
RA 6 HOH   3  303 689 HOH   HOH E . 
RA 6 HOH   4  304 248 HOH   HOH E . 
RA 6 HOH   5  305 404 HOH   HOH E . 
RA 6 HOH   6  306 622 HOH   HOH E . 
RA 6 HOH   7  307 13  HOH   HOH E . 
RA 6 HOH   8  308 276 HOH   HOH E . 
RA 6 HOH   9  309 96  HOH   HOH E . 
RA 6 HOH   10 310 436 HOH   HOH E . 
RA 6 HOH   11 311 567 HOH   HOH E . 
RA 6 HOH   12 312 204 HOH   HOH E . 
RA 6 HOH   13 313 15  HOH   HOH E . 
RA 6 HOH   14 314 2   HOH   HOH E . 
RA 6 HOH   15 315 289 HOH   HOH E . 
RA 6 HOH   16 316 534 HOH   HOH E . 
RA 6 HOH   17 317 270 HOH   HOH E . 
RA 6 HOH   18 318 314 HOH   HOH E . 
RA 6 HOH   19 319 119 HOH   HOH E . 
RA 6 HOH   20 320 431 HOH   HOH E . 
RA 6 HOH   21 321 65  HOH   HOH E . 
RA 6 HOH   22 322 439 HOH   HOH E . 
RA 6 HOH   23 323 223 HOH   HOH E . 
RA 6 HOH   24 324 443 HOH   HOH E . 
RA 6 HOH   25 325 341 HOH   HOH E . 
RA 6 HOH   26 326 174 HOH   HOH E . 
RA 6 HOH   27 327 441 HOH   HOH E . 
RA 6 HOH   28 328 107 HOH   HOH E . 
RA 6 HOH   29 329 581 HOH   HOH E . 
RA 6 HOH   30 330 319 HOH   HOH E . 
RA 6 HOH   31 331 258 HOH   HOH E . 
RA 6 HOH   32 332 80  HOH   HOH E . 
RA 6 HOH   33 333 140 HOH   HOH E . 
RA 6 HOH   34 334 694 HOH   HOH E . 
RA 6 HOH   35 335 19  HOH   HOH E . 
RA 6 HOH   36 336 11  HOH   HOH E . 
RA 6 HOH   37 337 654 HOH   HOH E . 
RA 6 HOH   38 338 583 HOH   HOH E . 
RA 6 HOH   39 339 535 HOH   HOH E . 
RA 6 HOH   40 340 395 HOH   HOH E . 
RA 6 HOH   41 341 106 HOH   HOH E . 
RA 6 HOH   42 342 145 HOH   HOH E . 
RA 6 HOH   43 343 227 HOH   HOH E . 
RA 6 HOH   44 344 165 HOH   HOH E . 
RA 6 HOH   45 345 329 HOH   HOH E . 
RA 6 HOH   46 346 285 HOH   HOH E . 
RA 6 HOH   47 347 42  HOH   HOH E . 
RA 6 HOH   48 348 259 HOH   HOH E . 
RA 6 HOH   49 349 660 HOH   HOH E . 
RA 6 HOH   50 350 247 HOH   HOH E . 
RA 6 HOH   51 351 650 HOH   HOH E . 
RA 6 HOH   52 352 345 HOH   HOH E . 
RA 6 HOH   53 353 504 HOH   HOH E . 
RA 6 HOH   54 354 322 HOH   HOH E . 
RA 6 HOH   55 355 652 HOH   HOH E . 
RA 6 HOH   56 356 41  HOH   HOH E . 
RA 6 HOH   57 357 586 HOH   HOH E . 
RA 6 HOH   58 358 440 HOH   HOH E . 
RA 6 HOH   59 359 121 HOH   HOH E . 
RA 6 HOH   60 360 501 HOH   HOH E . 
RA 6 HOH   61 361 380 HOH   HOH E . 
RA 6 HOH   62 362 659 HOH   HOH E . 
RA 6 HOH   63 363 496 HOH   HOH E . 
RA 6 HOH   64 364 596 HOH   HOH E . 
RA 6 HOH   65 365 638 HOH   HOH E . 
RA 6 HOH   66 366 623 HOH   HOH E . 
SA 6 HOH   1  301 592 HOH   HOH F . 
SA 6 HOH   2  302 357 HOH   HOH F . 
SA 6 HOH   3  303 157 HOH   HOH F . 
SA 6 HOH   4  304 412 HOH   HOH F . 
SA 6 HOH   5  305 294 HOH   HOH F . 
SA 6 HOH   6  306 377 HOH   HOH F . 
SA 6 HOH   7  307 48  HOH   HOH F . 
SA 6 HOH   8  308 263 HOH   HOH F . 
SA 6 HOH   9  309 608 HOH   HOH F . 
SA 6 HOH   10 310 614 HOH   HOH F . 
SA 6 HOH   11 311 472 HOH   HOH F . 
SA 6 HOH   12 312 525 HOH   HOH F . 
SA 6 HOH   13 313 266 HOH   HOH F . 
SA 6 HOH   14 314 251 HOH   HOH F . 
SA 6 HOH   15 315 447 HOH   HOH F . 
SA 6 HOH   16 316 191 HOH   HOH F . 
SA 6 HOH   17 317 300 HOH   HOH F . 
SA 6 HOH   18 318 529 HOH   HOH F . 
SA 6 HOH   19 319 484 HOH   HOH F . 
SA 6 HOH   20 320 499 HOH   HOH F . 
SA 6 HOH   21 321 524 HOH   HOH F . 
SA 6 HOH   22 322 184 HOH   HOH F . 
SA 6 HOH   23 323 681 HOH   HOH F . 
SA 6 HOH   24 324 228 HOH   HOH F . 
SA 6 HOH   25 325 587 HOH   HOH F . 
SA 6 HOH   26 326 222 HOH   HOH F . 
SA 6 HOH   27 327 187 HOH   HOH F . 
SA 6 HOH   28 328 410 HOH   HOH F . 
SA 6 HOH   29 329 346 HOH   HOH F . 
SA 6 HOH   30 330 200 HOH   HOH F . 
SA 6 HOH   31 331 126 HOH   HOH F . 
SA 6 HOH   32 332 305 HOH   HOH F . 
SA 6 HOH   33 333 347 HOH   HOH F . 
SA 6 HOH   34 334 677 HOH   HOH F . 
SA 6 HOH   35 335 84  HOH   HOH F . 
SA 6 HOH   36 336 112 HOH   HOH F . 
SA 6 HOH   37 337 558 HOH   HOH F . 
SA 6 HOH   38 338 168 HOH   HOH F . 
SA 6 HOH   39 339 669 HOH   HOH F . 
SA 6 HOH   40 340 59  HOH   HOH F . 
SA 6 HOH   41 341 595 HOH   HOH F . 
SA 6 HOH   42 342 315 HOH   HOH F . 
SA 6 HOH   43 343 477 HOH   HOH F . 
SA 6 HOH   44 344 6   HOH   HOH F . 
SA 6 HOH   45 345 155 HOH   HOH F . 
SA 6 HOH   46 346 397 HOH   HOH F . 
SA 6 HOH   47 347 5   HOH   HOH F . 
SA 6 HOH   48 348 327 HOH   HOH F . 
SA 6 HOH   49 349 321 HOH   HOH F . 
SA 6 HOH   50 350 503 HOH   HOH F . 
SA 6 HOH   51 351 381 HOH   HOH F . 
SA 6 HOH   52 352 551 HOH   HOH F . 
SA 6 HOH   53 353 311 HOH   HOH F . 
SA 6 HOH   54 354 272 HOH   HOH F . 
SA 6 HOH   55 355 230 HOH   HOH F . 
SA 6 HOH   56 356 613 HOH   HOH F . 
SA 6 HOH   57 357 101 HOH   HOH F . 
SA 6 HOH   58 358 642 HOH   HOH F . 
SA 6 HOH   59 359 10  HOH   HOH F . 
SA 6 HOH   60 360 565 HOH   HOH F . 
SA 6 HOH   61 361 549 HOH   HOH F . 
TA 6 HOH   1  301 435 HOH   HOH G . 
TA 6 HOH   2  302 661 HOH   HOH G . 
TA 6 HOH   3  303 342 HOH   HOH G . 
TA 6 HOH   4  304 146 HOH   HOH G . 
TA 6 HOH   5  305 63  HOH   HOH G . 
TA 6 HOH   6  306 367 HOH   HOH G . 
TA 6 HOH   7  307 369 HOH   HOH G . 
TA 6 HOH   8  308 167 HOH   HOH G . 
TA 6 HOH   9  309 212 HOH   HOH G . 
TA 6 HOH   10 310 388 HOH   HOH G . 
TA 6 HOH   11 311 301 HOH   HOH G . 
TA 6 HOH   12 312 554 HOH   HOH G . 
TA 6 HOH   13 313 298 HOH   HOH G . 
TA 6 HOH   14 314 172 HOH   HOH G . 
TA 6 HOH   15 315 351 HOH   HOH G . 
TA 6 HOH   16 316 306 HOH   HOH G . 
TA 6 HOH   17 317 210 HOH   HOH G . 
TA 6 HOH   18 318 216 HOH   HOH G . 
TA 6 HOH   19 319 307 HOH   HOH G . 
TA 6 HOH   20 320 290 HOH   HOH G . 
TA 6 HOH   21 321 82  HOH   HOH G . 
TA 6 HOH   22 322 566 HOH   HOH G . 
TA 6 HOH   23 323 425 HOH   HOH G . 
TA 6 HOH   24 324 24  HOH   HOH G . 
TA 6 HOH   25 325 557 HOH   HOH G . 
TA 6 HOH   26 326 693 HOH   HOH G . 
TA 6 HOH   27 327 218 HOH   HOH G . 
TA 6 HOH   28 328 323 HOH   HOH G . 
TA 6 HOH   29 329 164 HOH   HOH G . 
TA 6 HOH   30 330 171 HOH   HOH G . 
TA 6 HOH   31 331 50  HOH   HOH G . 
TA 6 HOH   32 332 344 HOH   HOH G . 
TA 6 HOH   33 333 427 HOH   HOH G . 
TA 6 HOH   34 334 603 HOH   HOH G . 
TA 6 HOH   35 335 324 HOH   HOH G . 
TA 6 HOH   36 336 518 HOH   HOH G . 
TA 6 HOH   37 337 573 HOH   HOH G . 
TA 6 HOH   38 338 14  HOH   HOH G . 
TA 6 HOH   39 339 217 HOH   HOH G . 
TA 6 HOH   40 340 310 HOH   HOH G . 
TA 6 HOH   41 341 43  HOH   HOH G . 
TA 6 HOH   42 342 108 HOH   HOH G . 
TA 6 HOH   43 343 418 HOH   HOH G . 
TA 6 HOH   44 344 683 HOH   HOH G . 
TA 6 HOH   45 345 304 HOH   HOH G . 
TA 6 HOH   46 346 632 HOH   HOH G . 
TA 6 HOH   47 347 637 HOH   HOH G . 
UA 6 HOH   1  301 385 HOH   HOH H . 
UA 6 HOH   2  302 241 HOH   HOH H . 
UA 6 HOH   3  303 548 HOH   HOH H . 
UA 6 HOH   4  304 653 HOH   HOH H . 
UA 6 HOH   5  305 445 HOH   HOH H . 
UA 6 HOH   6  306 125 HOH   HOH H . 
UA 6 HOH   7  307 514 HOH   HOH H . 
UA 6 HOH   8  308 54  HOH   HOH H . 
UA 6 HOH   9  309 74  HOH   HOH H . 
UA 6 HOH   10 310 282 HOH   HOH H . 
UA 6 HOH   11 311 561 HOH   HOH H . 
UA 6 HOH   12 312 236 HOH   HOH H . 
UA 6 HOH   13 313 264 HOH   HOH H . 
UA 6 HOH   14 314 215 HOH   HOH H . 
UA 6 HOH   15 315 615 HOH   HOH H . 
UA 6 HOH   16 316 92  HOH   HOH H . 
UA 6 HOH   17 317 202 HOH   HOH H . 
UA 6 HOH   18 318 488 HOH   HOH H . 
UA 6 HOH   19 319 309 HOH   HOH H . 
UA 6 HOH   20 320 136 HOH   HOH H . 
UA 6 HOH   21 321 442 HOH   HOH H . 
UA 6 HOH   22 322 521 HOH   HOH H . 
UA 6 HOH   23 323 550 HOH   HOH H . 
UA 6 HOH   24 324 402 HOH   HOH H . 
UA 6 HOH   25 325 389 HOH   HOH H . 
UA 6 HOH   26 326 690 HOH   HOH H . 
UA 6 HOH   27 327 408 HOH   HOH H . 
UA 6 HOH   28 328 591 HOH   HOH H . 
UA 6 HOH   29 329 267 HOH   HOH H . 
UA 6 HOH   30 330 52  HOH   HOH H . 
UA 6 HOH   31 331 371 HOH   HOH H . 
UA 6 HOH   32 332 539 HOH   HOH H . 
UA 6 HOH   33 333 665 HOH   HOH H . 
UA 6 HOH   34 334 124 HOH   HOH H . 
UA 6 HOH   35 335 480 HOH   HOH H . 
UA 6 HOH   36 336 261 HOH   HOH H . 
UA 6 HOH   37 337 275 HOH   HOH H . 
UA 6 HOH   38 338 25  HOH   HOH H . 
UA 6 HOH   39 339 93  HOH   HOH H . 
UA 6 HOH   40 340 483 HOH   HOH H . 
UA 6 HOH   41 341 424 HOH   HOH H . 
UA 6 HOH   42 342 685 HOH   HOH H . 
UA 6 HOH   43 343 238 HOH   HOH H . 
UA 6 HOH   44 344 89  HOH   HOH H . 
UA 6 HOH   45 345 531 HOH   HOH H . 
UA 6 HOH   46 346 533 HOH   HOH H . 
UA 6 HOH   47 347 600 HOH   HOH H . 
UA 6 HOH   48 348 643 HOH   HOH H . 
UA 6 HOH   49 349 338 HOH   HOH H . 
UA 6 HOH   50 350 616 HOH   HOH H . 
UA 6 HOH   51 351 572 HOH   HOH H . 
UA 6 HOH   52 352 686 HOH   HOH H . 
UA 6 HOH   53 353 453 HOH   HOH H . 
UA 6 HOH   54 354 647 HOH   HOH H . 
VA 6 HOH   1  301 462 HOH   HOH I . 
VA 6 HOH   2  302 434 HOH   HOH I . 
VA 6 HOH   3  303 37  HOH   HOH I . 
VA 6 HOH   4  304 366 HOH   HOH I . 
VA 6 HOH   5  305 433 HOH   HOH I . 
VA 6 HOH   6  306 76  HOH   HOH I . 
VA 6 HOH   7  307 664 HOH   HOH I . 
VA 6 HOH   8  308 378 HOH   HOH I . 
VA 6 HOH   9  309 79  HOH   HOH I . 
VA 6 HOH   10 310 325 HOH   HOH I . 
VA 6 HOH   11 311 414 HOH   HOH I . 
VA 6 HOH   12 312 254 HOH   HOH I . 
VA 6 HOH   13 313 68  HOH   HOH I . 
VA 6 HOH   14 314 286 HOH   HOH I . 
VA 6 HOH   15 315 281 HOH   HOH I . 
VA 6 HOH   16 316 553 HOH   HOH I . 
VA 6 HOH   17 317 502 HOH   HOH I . 
VA 6 HOH   18 318 348 HOH   HOH I . 
VA 6 HOH   19 319 87  HOH   HOH I . 
VA 6 HOH   20 320 208 HOH   HOH I . 
VA 6 HOH   21 321 239 HOH   HOH I . 
VA 6 HOH   22 322 170 HOH   HOH I . 
VA 6 HOH   23 323 355 HOH   HOH I . 
VA 6 HOH   24 324 399 HOH   HOH I . 
VA 6 HOH   25 325 3   HOH   HOH I . 
VA 6 HOH   26 326 627 HOH   HOH I . 
VA 6 HOH   27 327 244 HOH   HOH I . 
VA 6 HOH   28 328 370 HOH   HOH I . 
VA 6 HOH   29 329 194 HOH   HOH I . 
VA 6 HOH   30 330 625 HOH   HOH I . 
VA 6 HOH   31 331 486 HOH   HOH I . 
VA 6 HOH   32 332 209 HOH   HOH I . 
VA 6 HOH   33 333 235 HOH   HOH I . 
VA 6 HOH   34 334 392 HOH   HOH I . 
VA 6 HOH   35 335 516 HOH   HOH I . 
VA 6 HOH   36 336 31  HOH   HOH I . 
VA 6 HOH   37 337 91  HOH   HOH I . 
VA 6 HOH   38 338 150 HOH   HOH I . 
VA 6 HOH   39 339 85  HOH   HOH I . 
VA 6 HOH   40 340 69  HOH   HOH I . 
VA 6 HOH   41 341 509 HOH   HOH I . 
VA 6 HOH   42 342 178 HOH   HOH I . 
VA 6 HOH   43 343 225 HOH   HOH I . 
VA 6 HOH   44 344 75  HOH   HOH I . 
VA 6 HOH   45 345 203 HOH   HOH I . 
VA 6 HOH   46 346 536 HOH   HOH I . 
VA 6 HOH   47 347 177 HOH   HOH I . 
VA 6 HOH   48 348 421 HOH   HOH I . 
VA 6 HOH   49 349 186 HOH   HOH I . 
VA 6 HOH   50 350 546 HOH   HOH I . 
VA 6 HOH   51 351 452 HOH   HOH I . 
VA 6 HOH   52 352 51  HOH   HOH I . 
VA 6 HOH   53 353 299 HOH   HOH I . 
VA 6 HOH   54 354 649 HOH   HOH I . 
VA 6 HOH   55 355 214 HOH   HOH I . 
VA 6 HOH   56 356 636 HOH   HOH I . 
VA 6 HOH   57 357 470 HOH   HOH I . 
VA 6 HOH   58 358 618 HOH   HOH I . 
WA 6 HOH   1  301 7   HOH   HOH J . 
WA 6 HOH   2  302 446 HOH   HOH J . 
WA 6 HOH   3  303 594 HOH   HOH J . 
WA 6 HOH   4  304 415 HOH   HOH J . 
WA 6 HOH   5  305 528 HOH   HOH J . 
WA 6 HOH   6  306 598 HOH   HOH J . 
WA 6 HOH   7  307 128 HOH   HOH J . 
WA 6 HOH   8  308 577 HOH   HOH J . 
WA 6 HOH   9  309 47  HOH   HOH J . 
WA 6 HOH   10 310 530 HOH   HOH J . 
WA 6 HOH   11 311 556 HOH   HOH J . 
WA 6 HOH   12 312 569 HOH   HOH J . 
WA 6 HOH   13 313 490 HOH   HOH J . 
WA 6 HOH   14 314 255 HOH   HOH J . 
WA 6 HOH   15 315 373 HOH   HOH J . 
WA 6 HOH   16 316 570 HOH   HOH J . 
WA 6 HOH   17 317 67  HOH   HOH J . 
WA 6 HOH   18 318 252 HOH   HOH J . 
WA 6 HOH   19 319 78  HOH   HOH J . 
WA 6 HOH   20 320 158 HOH   HOH J . 
WA 6 HOH   21 321 198 HOH   HOH J . 
WA 6 HOH   22 322 455 HOH   HOH J . 
WA 6 HOH   23 323 277 HOH   HOH J . 
WA 6 HOH   24 324 379 HOH   HOH J . 
WA 6 HOH   25 325 98  HOH   HOH J . 
WA 6 HOH   26 326 365 HOH   HOH J . 
WA 6 HOH   27 327 559 HOH   HOH J . 
WA 6 HOH   28 328 226 HOH   HOH J . 
WA 6 HOH   29 329 406 HOH   HOH J . 
WA 6 HOH   30 330 260 HOH   HOH J . 
WA 6 HOH   31 331 691 HOH   HOH J . 
WA 6 HOH   32 332 621 HOH   HOH J . 
WA 6 HOH   33 333 576 HOH   HOH J . 
WA 6 HOH   34 334 130 HOH   HOH J . 
WA 6 HOH   35 335 460 HOH   HOH J . 
WA 6 HOH   36 336 605 HOH   HOH J . 
WA 6 HOH   37 337 12  HOH   HOH J . 
WA 6 HOH   38 338 400 HOH   HOH J . 
WA 6 HOH   39 339 542 HOH   HOH J . 
WA 6 HOH   40 340 580 HOH   HOH J . 
WA 6 HOH   41 341 662 HOH   HOH J . 
WA 6 HOH   42 342 34  HOH   HOH J . 
WA 6 HOH   43 343 246 HOH   HOH J . 
WA 6 HOH   44 344 189 HOH   HOH J . 
WA 6 HOH   45 345 670 HOH   HOH J . 
WA 6 HOH   46 346 687 HOH   HOH J . 
WA 6 HOH   47 347 469 HOH   HOH J . 
WA 6 HOH   48 348 161 HOH   HOH J . 
WA 6 HOH   49 349 295 HOH   HOH J . 
WA 6 HOH   50 350 532 HOH   HOH J . 
WA 6 HOH   51 351 95  HOH   HOH J . 
WA 6 HOH   52 352 196 HOH   HOH J . 
WA 6 HOH   53 353 515 HOH   HOH J . 
WA 6 HOH   54 354 678 HOH   HOH J . 
WA 6 HOH   55 355 21  HOH   HOH J . 
WA 6 HOH   56 356 115 HOH   HOH J . 
WA 6 HOH   57 357 555 HOH   HOH J . 
WA 6 HOH   58 358 512 HOH   HOH J . 
WA 6 HOH   59 359 23  HOH   HOH J . 
WA 6 HOH   60 360 612 HOH   HOH J . 
WA 6 HOH   61 361 639 HOH   HOH J . 
WA 6 HOH   62 362 560 HOH   HOH J . 
XA 6 HOH   1  301 527 HOH   HOH K . 
XA 6 HOH   2  302 656 HOH   HOH K . 
XA 6 HOH   3  303 428 HOH   HOH K . 
XA 6 HOH   4  304 476 HOH   HOH K . 
XA 6 HOH   5  305 626 HOH   HOH K . 
XA 6 HOH   6  306 513 HOH   HOH K . 
XA 6 HOH   7  307 111 HOH   HOH K . 
XA 6 HOH   8  308 271 HOH   HOH K . 
XA 6 HOH   9  309 360 HOH   HOH K . 
XA 6 HOH   10 310 495 HOH   HOH K . 
XA 6 HOH   11 311 326 HOH   HOH K . 
XA 6 HOH   12 312 393 HOH   HOH K . 
XA 6 HOH   13 313 181 HOH   HOH K . 
XA 6 HOH   14 314 420 HOH   HOH K . 
XA 6 HOH   15 315 589 HOH   HOH K . 
XA 6 HOH   16 316 506 HOH   HOH K . 
XA 6 HOH   17 317 343 HOH   HOH K . 
XA 6 HOH   18 318 668 HOH   HOH K . 
XA 6 HOH   19 319 81  HOH   HOH K . 
XA 6 HOH   20 320 571 HOH   HOH K . 
XA 6 HOH   21 321 22  HOH   HOH K . 
XA 6 HOH   22 322 617 HOH   HOH K . 
XA 6 HOH   23 323 390 HOH   HOH K . 
XA 6 HOH   24 324 144 HOH   HOH K . 
XA 6 HOH   25 325 335 HOH   HOH K . 
XA 6 HOH   26 326 296 HOH   HOH K . 
XA 6 HOH   27 327 552 HOH   HOH K . 
XA 6 HOH   28 328 620 HOH   HOH K . 
XA 6 HOH   29 329 317 HOH   HOH K . 
XA 6 HOH   30 330 118 HOH   HOH K . 
XA 6 HOH   31 331 26  HOH   HOH K . 
XA 6 HOH   32 332 137 HOH   HOH K . 
XA 6 HOH   33 333 517 HOH   HOH K . 
XA 6 HOH   34 334 590 HOH   HOH K . 
XA 6 HOH   35 335 375 HOH   HOH K . 
XA 6 HOH   36 336 17  HOH   HOH K . 
XA 6 HOH   37 337 40  HOH   HOH K . 
XA 6 HOH   38 338 197 HOH   HOH K . 
XA 6 HOH   39 339 117 HOH   HOH K . 
XA 6 HOH   40 340 463 HOH   HOH K . 
XA 6 HOH   41 341 362 HOH   HOH K . 
XA 6 HOH   42 342 135 HOH   HOH K . 
XA 6 HOH   43 343 53  HOH   HOH K . 
XA 6 HOH   44 344 682 HOH   HOH K . 
XA 6 HOH   45 345 473 HOH   HOH K . 
XA 6 HOH   46 346 498 HOH   HOH K . 
XA 6 HOH   47 347 511 HOH   HOH K . 
XA 6 HOH   48 348 148 HOH   HOH K . 
XA 6 HOH   49 349 33  HOH   HOH K . 
XA 6 HOH   50 350 673 HOH   HOH K . 
XA 6 HOH   51 351 464 HOH   HOH K . 
XA 6 HOH   52 352 422 HOH   HOH K . 
XA 6 HOH   53 353 253 HOH   HOH K . 
XA 6 HOH   54 354 280 HOH   HOH K . 
XA 6 HOH   55 355 456 HOH   HOH K . 
XA 6 HOH   56 356 467 HOH   HOH K . 
XA 6 HOH   57 357 541 HOH   HOH K . 
XA 6 HOH   58 358 508 HOH   HOH K . 
XA 6 HOH   59 359 644 HOH   HOH K . 
XA 6 HOH   60 360 240 HOH   HOH K . 
XA 6 HOH   61 361 646 HOH   HOH K . 
XA 6 HOH   62 362 645 HOH   HOH K . 
XA 6 HOH   63 363 641 HOH   HOH K . 
XA 6 HOH   64 364 320 HOH   HOH K . 
YA 6 HOH   1  301 58  HOH   HOH L . 
YA 6 HOH   2  302 193 HOH   HOH L . 
YA 6 HOH   3  303 658 HOH   HOH L . 
YA 6 HOH   4  304 273 HOH   HOH L . 
YA 6 HOH   5  305 411 HOH   HOH L . 
YA 6 HOH   6  306 609 HOH   HOH L . 
YA 6 HOH   7  307 491 HOH   HOH L . 
YA 6 HOH   8  308 57  HOH   HOH L . 
YA 6 HOH   9  309 564 HOH   HOH L . 
YA 6 HOH   10 310 312 HOH   HOH L . 
YA 6 HOH   11 311 221 HOH   HOH L . 
YA 6 HOH   12 312 243 HOH   HOH L . 
YA 6 HOH   13 313 28  HOH   HOH L . 
YA 6 HOH   14 314 179 HOH   HOH L . 
YA 6 HOH   15 315 133 HOH   HOH L . 
YA 6 HOH   16 316 237 HOH   HOH L . 
YA 6 HOH   17 317 72  HOH   HOH L . 
YA 6 HOH   18 318 359 HOH   HOH L . 
YA 6 HOH   19 319 131 HOH   HOH L . 
YA 6 HOH   20 320 545 HOH   HOH L . 
YA 6 HOH   21 321 224 HOH   HOH L . 
YA 6 HOH   22 322 219 HOH   HOH L . 
YA 6 HOH   23 323 129 HOH   HOH L . 
YA 6 HOH   24 324 475 HOH   HOH L . 
YA 6 HOH   25 325 471 HOH   HOH L . 
YA 6 HOH   26 326 169 HOH   HOH L . 
YA 6 HOH   27 327 352 HOH   HOH L . 
YA 6 HOH   28 328 32  HOH   HOH L . 
YA 6 HOH   29 329 563 HOH   HOH L . 
YA 6 HOH   30 330 141 HOH   HOH L . 
YA 6 HOH   31 331 20  HOH   HOH L . 
YA 6 HOH   32 332 104 HOH   HOH L . 
YA 6 HOH   33 333 334 HOH   HOH L . 
YA 6 HOH   34 334 102 HOH   HOH L . 
YA 6 HOH   35 335 257 HOH   HOH L . 
YA 6 HOH   36 336 249 HOH   HOH L . 
YA 6 HOH   37 337 182 HOH   HOH L . 
YA 6 HOH   38 338 30  HOH   HOH L . 
YA 6 HOH   39 339 585 HOH   HOH L . 
YA 6 HOH   40 340 291 HOH   HOH L . 
YA 6 HOH   41 341 604 HOH   HOH L . 
YA 6 HOH   42 342 229 HOH   HOH L . 
YA 6 HOH   43 343 220 HOH   HOH L . 
YA 6 HOH   44 344 123 HOH   HOH L . 
YA 6 HOH   45 345 679 HOH   HOH L . 
YA 6 HOH   46 346 213 HOH   HOH L . 
YA 6 HOH   47 347 105 HOH   HOH L . 
YA 6 HOH   48 348 394 HOH   HOH L . 
YA 6 HOH   49 349 458 HOH   HOH L . 
YA 6 HOH   50 350 510 HOH   HOH L . 
YA 6 HOH   51 351 127 HOH   HOH L . 
YA 6 HOH   52 352 396 HOH   HOH L . 
YA 6 HOH   53 353 330 HOH   HOH L . 
YA 6 HOH   54 354 114 HOH   HOH L . 
YA 6 HOH   55 355 437 HOH   HOH L . 
YA 6 HOH   56 356 349 HOH   HOH L . 
YA 6 HOH   57 357 634 HOH   HOH L . 
YA 6 HOH   58 358 382 HOH   HOH L . 
YA 6 HOH   59 359 450 HOH   HOH L . 
YA 6 HOH   60 360 481 HOH   HOH L . 
YA 6 HOH   61 361 599 HOH   HOH L . 
YA 6 HOH   62 362 584 HOH   HOH L . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 2   ? CE  ? A  LYS 2   CE  
2   1 Y 1 A LYS 2   ? NZ  ? A  LYS 2   NZ  
3   1 Y 1 A LYS 5   ? CD  ? A  LYS 5   CD  
4   1 Y 1 A LYS 5   ? CE  ? A  LYS 5   CE  
5   1 Y 1 A LYS 5   ? NZ  ? A  LYS 5   NZ  
6   1 Y 1 A LYS 57  ? CE  ? A  LYS 57  CE  
7   1 Y 1 A LYS 57  ? NZ  ? A  LYS 57  NZ  
8   1 Y 1 A LYS 76  ? CD  ? A  LYS 76  CD  
9   1 Y 1 A LYS 76  ? CE  ? A  LYS 76  CE  
10  1 Y 1 A LYS 76  ? NZ  ? A  LYS 76  NZ  
11  1 Y 1 A GLU 81  ? CG  ? A  GLU 81  CG  
12  1 Y 1 A GLU 81  ? CD  ? A  GLU 81  CD  
13  1 Y 1 A GLU 81  ? OE1 ? A  GLU 81  OE1 
14  1 Y 1 A GLU 81  ? OE2 ? A  GLU 81  OE2 
15  1 Y 1 A LYS 99  ? CE  ? A  LYS 99  CE  
16  1 Y 1 A LYS 99  ? NZ  ? A  LYS 99  NZ  
17  1 Y 1 A GLN 110 ? CD  ? A  GLN 110 CD  
18  1 Y 1 A GLN 110 ? OE1 ? A  GLN 110 OE1 
19  1 Y 1 A GLN 110 ? NE2 ? A  GLN 110 NE2 
20  1 Y 1 B LYS 2   ? CG  ? B  LYS 2   CG  
21  1 Y 1 B LYS 2   ? CD  ? B  LYS 2   CD  
22  1 Y 1 B LYS 2   ? CE  ? B  LYS 2   CE  
23  1 Y 1 B LYS 2   ? NZ  ? B  LYS 2   NZ  
24  1 Y 1 B LYS 5   ? CD  ? B  LYS 5   CD  
25  1 Y 1 B LYS 5   ? CE  ? B  LYS 5   CE  
26  1 Y 1 B LYS 5   ? NZ  ? B  LYS 5   NZ  
27  1 Y 1 B LYS 6   ? CD  ? B  LYS 6   CD  
28  1 Y 1 B LYS 6   ? CE  ? B  LYS 6   CE  
29  1 Y 1 B LYS 6   ? NZ  ? B  LYS 6   NZ  
30  1 Y 1 B LYS 57  ? CE  ? B  LYS 57  CE  
31  1 Y 1 B LYS 57  ? NZ  ? B  LYS 57  NZ  
32  1 Y 1 B LYS 76  ? CD  ? B  LYS 76  CD  
33  1 Y 1 B LYS 76  ? CE  ? B  LYS 76  CE  
34  1 Y 1 B LYS 76  ? NZ  ? B  LYS 76  NZ  
35  1 Y 1 B LYS 99  ? CE  ? B  LYS 99  CE  
36  1 Y 1 B LYS 99  ? NZ  ? B  LYS 99  NZ  
37  1 Y 1 B GLN 110 ? CD  ? B  GLN 110 CD  
38  1 Y 1 B GLN 110 ? OE1 ? B  GLN 110 OE1 
39  1 Y 1 B GLN 110 ? NE2 ? B  GLN 110 NE2 
40  1 Y 1 C LYS 2   ? CG  ? C  LYS 2   CG  
41  1 Y 1 C LYS 2   ? CD  ? C  LYS 2   CD  
42  1 Y 1 C LYS 2   ? CE  ? C  LYS 2   CE  
43  1 Y 1 C LYS 2   ? NZ  ? C  LYS 2   NZ  
44  1 Y 1 C LYS 5   ? CD  ? C  LYS 5   CD  
45  1 Y 1 C LYS 5   ? CE  ? C  LYS 5   CE  
46  1 Y 1 C LYS 5   ? NZ  ? C  LYS 5   NZ  
47  1 Y 1 C LYS 6   ? CG  ? C  LYS 6   CG  
48  1 Y 1 C LYS 6   ? CD  ? C  LYS 6   CD  
49  1 Y 1 C LYS 6   ? CE  ? C  LYS 6   CE  
50  1 Y 1 C LYS 6   ? NZ  ? C  LYS 6   NZ  
51  1 Y 1 C LYS 57  ? CE  ? C  LYS 57  CE  
52  1 Y 1 C LYS 57  ? NZ  ? C  LYS 57  NZ  
53  1 Y 1 C LYS 76  ? CD  ? C  LYS 76  CD  
54  1 Y 1 C LYS 76  ? CE  ? C  LYS 76  CE  
55  1 Y 1 C LYS 76  ? NZ  ? C  LYS 76  NZ  
56  1 Y 1 C LYS 96  ? CD  ? C  LYS 96  CD  
57  1 Y 1 C LYS 96  ? CE  ? C  LYS 96  CE  
58  1 Y 1 C LYS 96  ? NZ  ? C  LYS 96  NZ  
59  1 Y 1 C LYS 99  ? CE  ? C  LYS 99  CE  
60  1 Y 1 C LYS 99  ? NZ  ? C  LYS 99  NZ  
61  1 Y 1 C GLN 110 ? CD  ? C  GLN 110 CD  
62  1 Y 1 C GLN 110 ? OE1 ? C  GLN 110 OE1 
63  1 Y 1 C GLN 110 ? NE2 ? C  GLN 110 NE2 
64  1 Y 1 D LYS 2   ? CG  ? D  LYS 2   CG  
65  1 Y 1 D LYS 2   ? CD  ? D  LYS 2   CD  
66  1 Y 1 D LYS 2   ? CE  ? D  LYS 2   CE  
67  1 Y 1 D LYS 2   ? NZ  ? D  LYS 2   NZ  
68  1 Y 1 D LYS 5   ? CD  ? D  LYS 5   CD  
69  1 Y 1 D LYS 5   ? CE  ? D  LYS 5   CE  
70  1 Y 1 D LYS 5   ? NZ  ? D  LYS 5   NZ  
71  1 Y 1 D LYS 57  ? CE  ? D  LYS 57  CE  
72  1 Y 1 D LYS 57  ? NZ  ? D  LYS 57  NZ  
73  1 Y 1 D LYS 76  ? CD  ? D  LYS 76  CD  
74  1 Y 1 D LYS 76  ? CE  ? D  LYS 76  CE  
75  1 Y 1 D LYS 76  ? NZ  ? D  LYS 76  NZ  
76  1 Y 1 D GLN 84  ? CD  ? D  GLN 84  CD  
77  1 Y 1 D GLN 84  ? OE1 ? D  GLN 84  OE1 
78  1 Y 1 D GLN 84  ? NE2 ? D  GLN 84  NE2 
79  1 Y 1 D LYS 99  ? CD  ? D  LYS 99  CD  
80  1 Y 1 D LYS 99  ? CE  ? D  LYS 99  CE  
81  1 Y 1 D LYS 99  ? NZ  ? D  LYS 99  NZ  
82  1 Y 1 E LYS 2   ? CG  ? E  LYS 2   CG  
83  1 Y 1 E LYS 2   ? CD  ? E  LYS 2   CD  
84  1 Y 1 E LYS 2   ? CE  ? E  LYS 2   CE  
85  1 Y 1 E LYS 2   ? NZ  ? E  LYS 2   NZ  
86  1 Y 1 E LYS 57  ? CE  ? E  LYS 57  CE  
87  1 Y 1 E LYS 57  ? NZ  ? E  LYS 57  NZ  
88  1 Y 1 E LYS 76  ? CD  ? E  LYS 76  CD  
89  1 Y 1 E LYS 76  ? CE  ? E  LYS 76  CE  
90  1 Y 1 E LYS 76  ? NZ  ? E  LYS 76  NZ  
91  1 Y 1 E LYS 96  ? CD  ? E  LYS 96  CD  
92  1 Y 1 E LYS 96  ? CE  ? E  LYS 96  CE  
93  1 Y 1 E LYS 96  ? NZ  ? E  LYS 96  NZ  
94  1 Y 1 E LYS 99  ? CE  ? E  LYS 99  CE  
95  1 Y 1 E LYS 99  ? NZ  ? E  LYS 99  NZ  
96  1 Y 1 E GLU 129 ? CD  ? E  GLU 129 CD  
97  1 Y 1 E GLU 129 ? OE1 ? E  GLU 129 OE1 
98  1 Y 1 E GLU 129 ? OE2 ? E  GLU 129 OE2 
99  1 Y 1 F LYS 2   ? CG  ? F  LYS 2   CG  
100 1 Y 1 F LYS 2   ? CD  ? F  LYS 2   CD  
101 1 Y 1 F LYS 2   ? CE  ? F  LYS 2   CE  
102 1 Y 1 F LYS 2   ? NZ  ? F  LYS 2   NZ  
103 1 Y 1 F LYS 5   ? CD  ? F  LYS 5   CD  
104 1 Y 1 F LYS 5   ? CE  ? F  LYS 5   CE  
105 1 Y 1 F LYS 5   ? NZ  ? F  LYS 5   NZ  
106 1 Y 1 F LYS 6   ? CE  ? F  LYS 6   CE  
107 1 Y 1 F LYS 6   ? NZ  ? F  LYS 6   NZ  
108 1 Y 1 F LYS 57  ? CE  ? F  LYS 57  CE  
109 1 Y 1 F LYS 57  ? NZ  ? F  LYS 57  NZ  
110 1 Y 1 F LYS 76  ? CD  ? F  LYS 76  CD  
111 1 Y 1 F LYS 76  ? CE  ? F  LYS 76  CE  
112 1 Y 1 F LYS 76  ? NZ  ? F  LYS 76  NZ  
113 1 Y 1 F LYS 99  ? CE  ? F  LYS 99  CE  
114 1 Y 1 F LYS 99  ? NZ  ? F  LYS 99  NZ  
115 1 Y 1 F GLU 103 ? CD  ? F  GLU 103 CD  
116 1 Y 1 F GLU 103 ? OE1 ? F  GLU 103 OE1 
117 1 Y 1 F GLU 103 ? OE2 ? F  GLU 103 OE2 
118 1 Y 1 F GLU 129 ? CD  ? F  GLU 129 CD  
119 1 Y 1 F GLU 129 ? OE1 ? F  GLU 129 OE1 
120 1 Y 1 F GLU 129 ? OE2 ? F  GLU 129 OE2 
121 1 Y 1 F GLU 147 ? CD  ? F  GLU 147 CD  
122 1 Y 1 F GLU 147 ? OE1 ? F  GLU 147 OE1 
123 1 Y 1 F GLU 147 ? OE2 ? F  GLU 147 OE2 
124 1 Y 1 G LYS 2   ? CG  ? G  LYS 2   CG  
125 1 Y 1 G LYS 2   ? CD  ? G  LYS 2   CD  
126 1 Y 1 G LYS 2   ? CE  ? G  LYS 2   CE  
127 1 Y 1 G LYS 2   ? NZ  ? G  LYS 2   NZ  
128 1 Y 1 G LYS 5   ? CD  ? G  LYS 5   CD  
129 1 Y 1 G LYS 5   ? CE  ? G  LYS 5   CE  
130 1 Y 1 G LYS 5   ? NZ  ? G  LYS 5   NZ  
131 1 Y 1 G LYS 57  ? CE  ? G  LYS 57  CE  
132 1 Y 1 G LYS 57  ? NZ  ? G  LYS 57  NZ  
133 1 Y 1 G LYS 76  ? CD  ? G  LYS 76  CD  
134 1 Y 1 G LYS 76  ? CE  ? G  LYS 76  CE  
135 1 Y 1 G LYS 76  ? NZ  ? G  LYS 76  NZ  
136 1 Y 1 G LYS 99  ? CE  ? G  LYS 99  CE  
137 1 Y 1 G LYS 99  ? NZ  ? G  LYS 99  NZ  
138 1 Y 1 G GLN 110 ? CD  ? G  GLN 110 CD  
139 1 Y 1 G GLN 110 ? OE1 ? G  GLN 110 OE1 
140 1 Y 1 G GLN 110 ? NE2 ? G  GLN 110 NE2 
141 1 Y 1 H LYS 2   ? CG  ? H  LYS 2   CG  
142 1 Y 1 H LYS 2   ? CD  ? H  LYS 2   CD  
143 1 Y 1 H LYS 2   ? CE  ? H  LYS 2   CE  
144 1 Y 1 H LYS 2   ? NZ  ? H  LYS 2   NZ  
145 1 Y 1 H LYS 5   ? CD  ? H  LYS 5   CD  
146 1 Y 1 H LYS 5   ? CE  ? H  LYS 5   CE  
147 1 Y 1 H LYS 5   ? NZ  ? H  LYS 5   NZ  
148 1 Y 1 H LYS 6   ? CD  ? H  LYS 6   CD  
149 1 Y 1 H LYS 6   ? CE  ? H  LYS 6   CE  
150 1 Y 1 H LYS 6   ? NZ  ? H  LYS 6   NZ  
151 1 Y 1 H LYS 57  ? CD  ? H  LYS 57  CD  
152 1 Y 1 H LYS 57  ? CE  ? H  LYS 57  CE  
153 1 Y 1 H LYS 57  ? NZ  ? H  LYS 57  NZ  
154 1 Y 1 H LYS 76  ? CD  ? H  LYS 76  CD  
155 1 Y 1 H LYS 76  ? CE  ? H  LYS 76  CE  
156 1 Y 1 H LYS 76  ? NZ  ? H  LYS 76  NZ  
157 1 Y 1 H LYS 96  ? CD  ? H  LYS 96  CD  
158 1 Y 1 H LYS 96  ? CE  ? H  LYS 96  CE  
159 1 Y 1 H LYS 96  ? NZ  ? H  LYS 96  NZ  
160 1 Y 1 H LYS 99  ? CD  ? H  LYS 99  CD  
161 1 Y 1 H LYS 99  ? CE  ? H  LYS 99  CE  
162 1 Y 1 H LYS 99  ? NZ  ? H  LYS 99  NZ  
163 1 Y 1 H GLU 103 ? CD  ? H  GLU 103 CD  
164 1 Y 1 H GLU 103 ? OE1 ? H  GLU 103 OE1 
165 1 Y 1 H GLU 103 ? OE2 ? H  GLU 103 OE2 
166 1 Y 1 I LYS 2   ? CG  ? I  LYS 2   CG  
167 1 Y 1 I LYS 2   ? CD  ? I  LYS 2   CD  
168 1 Y 1 I LYS 2   ? CE  ? I  LYS 2   CE  
169 1 Y 1 I LYS 2   ? NZ  ? I  LYS 2   NZ  
170 1 Y 1 I LYS 5   ? CD  ? I  LYS 5   CD  
171 1 Y 1 I LYS 5   ? CE  ? I  LYS 5   CE  
172 1 Y 1 I LYS 5   ? NZ  ? I  LYS 5   NZ  
173 1 Y 1 I LYS 76  ? CD  ? I  LYS 76  CD  
174 1 Y 1 I LYS 76  ? CE  ? I  LYS 76  CE  
175 1 Y 1 I LYS 76  ? NZ  ? I  LYS 76  NZ  
176 1 Y 1 I LYS 96  ? CD  ? I  LYS 96  CD  
177 1 Y 1 I LYS 96  ? CE  ? I  LYS 96  CE  
178 1 Y 1 I LYS 96  ? NZ  ? I  LYS 96  NZ  
179 1 Y 1 I LYS 99  ? CE  ? I  LYS 99  CE  
180 1 Y 1 I LYS 99  ? NZ  ? I  LYS 99  NZ  
181 1 Y 1 I GLN 110 ? CD  ? I  GLN 110 CD  
182 1 Y 1 I GLN 110 ? OE1 ? I  GLN 110 OE1 
183 1 Y 1 I GLN 110 ? NE2 ? I  GLN 110 NE2 
184 1 Y 1 J LYS 2   ? CG  ? J  LYS 2   CG  
185 1 Y 1 J LYS 2   ? CD  ? J  LYS 2   CD  
186 1 Y 1 J LYS 2   ? CE  ? J  LYS 2   CE  
187 1 Y 1 J LYS 2   ? NZ  ? J  LYS 2   NZ  
188 1 Y 1 J LYS 5   ? CD  ? J  LYS 5   CD  
189 1 Y 1 J LYS 5   ? CE  ? J  LYS 5   CE  
190 1 Y 1 J LYS 5   ? NZ  ? J  LYS 5   NZ  
191 1 Y 1 J LYS 57  ? CE  ? J  LYS 57  CE  
192 1 Y 1 J LYS 57  ? NZ  ? J  LYS 57  NZ  
193 1 Y 1 J LYS 76  ? CD  ? J  LYS 76  CD  
194 1 Y 1 J LYS 76  ? CE  ? J  LYS 76  CE  
195 1 Y 1 J LYS 76  ? NZ  ? J  LYS 76  NZ  
196 1 Y 1 J LYS 99  ? CE  ? J  LYS 99  CE  
197 1 Y 1 J LYS 99  ? NZ  ? J  LYS 99  NZ  
198 1 Y 1 J GLU 103 ? CD  ? J  GLU 103 CD  
199 1 Y 1 J GLU 103 ? OE1 ? J  GLU 103 OE1 
200 1 Y 1 J GLU 103 ? OE2 ? J  GLU 103 OE2 
201 1 Y 1 J GLU 129 ? CG  ? J  GLU 129 CG  
202 1 Y 1 J GLU 129 ? CD  ? J  GLU 129 CD  
203 1 Y 1 J GLU 129 ? OE1 ? J  GLU 129 OE1 
204 1 Y 1 J GLU 129 ? OE2 ? J  GLU 129 OE2 
205 1 Y 1 K LYS 2   ? CG  ? K  LYS 2   CG  
206 1 Y 1 K LYS 2   ? CD  ? K  LYS 2   CD  
207 1 Y 1 K LYS 2   ? CE  ? K  LYS 2   CE  
208 1 Y 1 K LYS 2   ? NZ  ? K  LYS 2   NZ  
209 1 Y 1 K LYS 5   ? CD  ? K  LYS 5   CD  
210 1 Y 1 K LYS 5   ? CE  ? K  LYS 5   CE  
211 1 Y 1 K LYS 5   ? NZ  ? K  LYS 5   NZ  
212 1 Y 1 K LYS 6   ? CE  ? K  LYS 6   CE  
213 1 Y 1 K LYS 6   ? NZ  ? K  LYS 6   NZ  
214 1 Y 1 K LYS 76  ? CD  ? K  LYS 76  CD  
215 1 Y 1 K LYS 76  ? CE  ? K  LYS 76  CE  
216 1 Y 1 K LYS 76  ? NZ  ? K  LYS 76  NZ  
217 1 Y 1 K LYS 96  ? CD  ? K  LYS 96  CD  
218 1 Y 1 K LYS 96  ? CE  ? K  LYS 96  CE  
219 1 Y 1 K LYS 96  ? NZ  ? K  LYS 96  NZ  
220 1 Y 1 K LYS 99  ? CE  ? K  LYS 99  CE  
221 1 Y 1 K LYS 99  ? NZ  ? K  LYS 99  NZ  
222 1 Y 1 K GLN 110 ? CD  ? K  GLN 110 CD  
223 1 Y 1 K GLN 110 ? OE1 ? K  GLN 110 OE1 
224 1 Y 1 K GLN 110 ? NE2 ? K  GLN 110 NE2 
225 1 Y 1 K GLU 129 ? CG  ? K  GLU 129 CG  
226 1 Y 1 K GLU 129 ? CD  ? K  GLU 129 CD  
227 1 Y 1 K GLU 129 ? OE1 ? K  GLU 129 OE1 
228 1 Y 1 K GLU 129 ? OE2 ? K  GLU 129 OE2 
229 1 Y 1 L LYS 2   ? CG  ? L  LYS 2   CG  
230 1 Y 1 L LYS 2   ? CD  ? L  LYS 2   CD  
231 1 Y 1 L LYS 2   ? CE  ? L  LYS 2   CE  
232 1 Y 1 L LYS 2   ? NZ  ? L  LYS 2   NZ  
233 1 Y 1 L LYS 5   ? CD  ? L  LYS 5   CD  
234 1 Y 1 L LYS 5   ? CE  ? L  LYS 5   CE  
235 1 Y 1 L LYS 5   ? NZ  ? L  LYS 5   NZ  
236 1 Y 1 L LYS 76  ? CD  ? L  LYS 76  CD  
237 1 Y 1 L LYS 76  ? CE  ? L  LYS 76  CE  
238 1 Y 1 L LYS 76  ? NZ  ? L  LYS 76  NZ  
239 1 Y 1 L LYS 99  ? CE  ? L  LYS 99  CE  
240 1 Y 1 L LYS 99  ? NZ  ? L  LYS 99  NZ  
241 1 Y 1 L GLU 103 ? CD  ? L  GLU 103 CD  
242 1 Y 1 L GLU 103 ? OE1 ? L  GLU 103 OE1 
243 1 Y 1 L GLU 103 ? OE2 ? L  GLU 103 OE2 
244 1 Y 1 L GLN 110 ? CD  ? L  GLN 110 CD  
245 1 Y 1 L GLN 110 ? OE1 ? L  GLN 110 OE1 
246 1 Y 1 L GLN 110 ? NE2 ? L  GLN 110 NE2 
247 1 Y 1 L GLU 129 ? CD  ? L  GLU 129 CD  
248 1 Y 1 L GLU 129 ? OE1 ? L  GLU 129 OE1 
249 1 Y 1 L GLU 129 ? OE2 ? L  GLU 129 OE2 
250 1 N 1 G PG4 201 ? O1  ? AA PG4 1   O1  
251 1 N 1 G PG4 201 ? C1  ? AA PG4 1   C1  
252 1 N 1 G PG4 201 ? C2  ? AA PG4 1   C2  
253 1 N 1 H PG4 201 ? O1  ? BA PG4 1   O1  
254 1 N 1 H PG4 201 ? C1  ? BA PG4 1   C1  
255 1 N 1 J PG4 201 ? O1  ? HA PG4 1   O1  
256 1 N 1 J PG4 201 ? C1  ? HA PG4 1   C1  
# 
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  ? ? ? '(dev_4210: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NHR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     129.569 
_cell.length_a_esd                 ? 
_cell.length_b                     194.357 
_cell.length_b_esd                 ? 
_cell.length_c                     203.032 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        96 
_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                         9NHR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9NHR 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.87 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.09 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.5 
_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    '30% v/v PEG200, 100 mM sodium acetate, pH 4.5, 100 mM sodium chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 XE 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-04-03 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Double Crystal Si 111' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9NHR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               48.59 
_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                                     185210 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.04 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.100 
_reflns.pdbx_Rpim_I_all                                0.038 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1284414 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.093 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.95 
_reflns_shell.d_res_low                                     1.98 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           61051 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             9123 
_reflns_shell.percent_possible_obs                          100.0 
_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                               6.7 
_reflns_shell.pdbx_chi_squared                              1.03 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.9 
_reflns_shell.pdbx_Rrim_I_all                               1.131 
_reflns_shell.pdbx_Rpim_I_all                               0.435 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.746 
_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                                  1.043 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9NHR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.95 
_refine.ls_d_res_low                             38.00 
_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                     185107 
_refine.ls_number_reflns_R_free                  9277 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1819 
_refine.ls_R_factor_R_free                       0.2213 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1798 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.02 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.99 
_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                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        38.00 
_refine_hist.number_atoms_solvent             695 
_refine_hist.number_atoms_total               16458 
_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        15173 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         590 
_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' ? 0.010  ? 16194 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.926  ? 21954 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.436 ? 5978  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.046  ? 2348  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 2780  ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.95 1.97  . . 314 5807 100.00 . . . . 0.2674 . . . . . . . . . . . . . . . 0.3039 
'X-RAY DIFFRACTION' 1.97 2.00  . . 291 5830 100.00 . . . . 0.2529 . . . . . . . . . . . . . . . 0.2955 
'X-RAY DIFFRACTION' 2.00 2.02  . . 323 5820 100.00 . . . . 0.2456 . . . . . . . . . . . . . . . 0.3047 
'X-RAY DIFFRACTION' 2.02 2.05  . . 327 5758 100.00 . . . . 0.2296 . . . . . . . . . . . . . . . 0.2658 
'X-RAY DIFFRACTION' 2.05 2.07  . . 285 5817 100.00 . . . . 0.2187 . . . . . . . . . . . . . . . 0.2515 
'X-RAY DIFFRACTION' 2.07 2.10  . . 306 5816 100.00 . . . . 0.2114 . . . . . . . . . . . . . . . 0.2484 
'X-RAY DIFFRACTION' 2.10 2.13  . . 323 5855 100.00 . . . . 0.2068 . . . . . . . . . . . . . . . 0.2792 
'X-RAY DIFFRACTION' 2.13 2.16  . . 299 5852 100.00 . . . . 0.2088 . . . . . . . . . . . . . . . 0.2553 
'X-RAY DIFFRACTION' 2.16 2.20  . . 307 5784 100.00 . . . . 0.1938 . . . . . . . . . . . . . . . 0.2604 
'X-RAY DIFFRACTION' 2.20 2.23  . . 298 5852 100.00 . . . . 0.1843 . . . . . . . . . . . . . . . 0.2265 
'X-RAY DIFFRACTION' 2.23 2.27  . . 330 5811 100.00 . . . . 0.1847 . . . . . . . . . . . . . . . 0.2318 
'X-RAY DIFFRACTION' 2.27 2.31  . . 294 5825 100.00 . . . . 0.1778 . . . . . . . . . . . . . . . 0.2287 
'X-RAY DIFFRACTION' 2.31 2.36  . . 297 5849 100.00 . . . . 0.1821 . . . . . . . . . . . . . . . 0.2430 
'X-RAY DIFFRACTION' 2.36 2.40  . . 310 5834 100.00 . . . . 0.1813 . . . . . . . . . . . . . . . 0.2475 
'X-RAY DIFFRACTION' 2.40 2.46  . . 298 5843 100.00 . . . . 0.1757 . . . . . . . . . . . . . . . 0.2203 
'X-RAY DIFFRACTION' 2.46 2.51  . . 287 5843 100.00 . . . . 0.1720 . . . . . . . . . . . . . . . 0.2129 
'X-RAY DIFFRACTION' 2.51 2.58  . . 358 5814 100.00 . . . . 0.1696 . . . . . . . . . . . . . . . 0.2171 
'X-RAY DIFFRACTION' 2.58 2.65  . . 288 5882 100.00 . . . . 0.1669 . . . . . . . . . . . . . . . 0.2108 
'X-RAY DIFFRACTION' 2.65 2.72  . . 322 5845 100.00 . . . . 0.1795 . . . . . . . . . . . . . . . 0.2319 
'X-RAY DIFFRACTION' 2.72 2.81  . . 297 5845 100.00 . . . . 0.1705 . . . . . . . . . . . . . . . 0.2343 
'X-RAY DIFFRACTION' 2.81 2.91  . . 309 5848 100.00 . . . . 0.1623 . . . . . . . . . . . . . . . 0.2045 
'X-RAY DIFFRACTION' 2.91 3.03  . . 266 5892 100.00 . . . . 0.1758 . . . . . . . . . . . . . . . 0.2166 
'X-RAY DIFFRACTION' 3.03 3.17  . . 335 5885 100.00 . . . . 0.1859 . . . . . . . . . . . . . . . 0.2356 
'X-RAY DIFFRACTION' 3.17 3.33  . . 304 5887 100.00 . . . . 0.1871 . . . . . . . . . . . . . . . 0.2340 
'X-RAY DIFFRACTION' 3.33 3.54  . . 302 5885 100.00 . . . . 0.1732 . . . . . . . . . . . . . . . 0.2093 
'X-RAY DIFFRACTION' 3.54 3.82  . . 328 5878 100.00 . . . . 0.1731 . . . . . . . . . . . . . . . 0.2007 
'X-RAY DIFFRACTION' 3.82 4.20  . . 315 5904 100.00 . . . . 0.1564 . . . . . . . . . . . . . . . 0.2016 
'X-RAY DIFFRACTION' 4.20 4.81  . . 316 5941 100.00 . . . . 0.1448 . . . . . . . . . . . . . . . 0.1662 
'X-RAY DIFFRACTION' 4.81 6.05  . . 325 5975 100.00 . . . . 0.1909 . . . . . . . . . . . . . . . 0.2350 
'X-RAY DIFFRACTION' 6.05 38.00 . . 323 6153 100.00 . . . . 0.1963 . . . . . . . . . . . . . . . 0.2189 
# 
_struct.entry_id                     9NHR 
_struct.title                        
;Crystal structure of structure of WT BfrB from Pseudomonas aeruginosa in complex with a protein-protein interaction inhibitor KM-5-25
;
_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        9NHR 
_struct_keywords.text            
'biofilms, electron transport, iron storage, iron binding, iron mobilization, protein-protein interaction inhibitor, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 1 ? 
F  N N 1 ? 
G  N N 1 ? 
H  N N 1 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 1 ? 
L  N N 1 ? 
M  N N 2 ? 
N  N N 3 ? 
O  N N 2 ? 
P  N N 4 ? 
Q  N N 5 ? 
R  N N 5 ? 
S  N N 2 ? 
T  N N 3 ? 
U  N N 4 ? 
V  N N 3 ? 
W  N N 4 ? 
X  N N 5 ? 
Y  N N 3 ? 
Z  N N 5 ? 
AA N N 4 ? 
BA N N 4 ? 
CA N N 3 ? 
DA N N 5 ? 
EA N N 3 ? 
FA N N 4 ? 
GA N N 5 ? 
HA N N 4 ? 
IA N N 5 ? 
JA N N 5 ? 
KA N N 3 ? 
LA N N 4 ? 
MA N N 5 ? 
NA N N 6 ? 
OA N N 6 ? 
PA N N 6 ? 
QA N N 6 ? 
RA N N 6 ? 
SA N N 6 ? 
TA N N 6 ? 
UA N N 6 ? 
VA N N 6 ? 
WA N N 6 ? 
XA N N 6 ? 
YA N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9HY79_PSEAE 
_struct_ref.pdbx_db_accession          Q9HY79 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKGDKKVIQHLNKILGNELIAINQYFLHSRMWNDWGLKRLGAHEYHESIDEMKHADKLIERILFLEGLPNLQDLGKLLIG
ENTQEMLQCDLNLELKATKDLREAIVHCEQVHDYVSRDLLKDILESEEEHIDYLETQLGLIQKVGLENYLQSHMHEDD
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 9NHR A 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
2  1 9NHR B 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
3  1 9NHR C 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
4  1 9NHR D 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
5  1 9NHR E 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
6  1 9NHR F 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
7  1 9NHR G 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
8  1 9NHR H 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
9  1 9NHR I 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
10 1 9NHR J 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
11 1 9NHR K 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
12 1 9NHR L 1 ? 158 ? Q9HY79 1 ? 158 ? 1 158 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   24-meric 
_pdbx_struct_assembly.oligomeric_count     24 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 98610  ? 
1 MORE         -581   ? 
1 'SSA (A^2)'  121670 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      
A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000    
2 'crystal symmetry operation' 3_554 -x,y,-z-1/2 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -101.5160000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 4   ? TRP A 35  ? ASP A 4   TRP A 35  1 ? 32 
HELX_P HELX_P2  AA2 LEU A 37  ? LEU A 65  ? LEU A 37  LEU A 65  1 ? 29 
HELX_P HELX_P3  AA3 ASN A 82  ? HIS A 112 ? ASN A 82  HIS A 112 1 ? 31 
HELX_P HELX_P4  AA4 ASP A 113 ? GLY A 145 ? ASP A 113 GLY A 145 1 ? 33 
HELX_P HELX_P5  AA5 GLY A 145 ? SER A 152 ? GLY A 145 SER A 152 1 ? 8  
HELX_P HELX_P6  AA6 ASP B 4   ? TRP B 35  ? ASP B 4   TRP B 35  1 ? 32 
HELX_P HELX_P7  AA7 LEU B 37  ? LEU B 65  ? LEU B 37  LEU B 65  1 ? 29 
HELX_P HELX_P8  AA8 ASN B 82  ? VAL B 111 ? ASN B 82  VAL B 111 1 ? 30 
HELX_P HELX_P9  AA9 ASP B 113 ? GLY B 145 ? ASP B 113 GLY B 145 1 ? 33 
HELX_P HELX_P10 AB1 GLY B 145 ? SER B 152 ? GLY B 145 SER B 152 1 ? 8  
HELX_P HELX_P11 AB2 ASP C 4   ? TRP C 35  ? ASP C 4   TRP C 35  1 ? 32 
HELX_P HELX_P12 AB3 LEU C 37  ? LEU C 65  ? LEU C 37  LEU C 65  1 ? 29 
HELX_P HELX_P13 AB4 ASN C 82  ? VAL C 111 ? ASN C 82  VAL C 111 1 ? 30 
HELX_P HELX_P14 AB5 ASP C 113 ? GLY C 145 ? ASP C 113 GLY C 145 1 ? 33 
HELX_P HELX_P15 AB6 GLY C 145 ? SER C 152 ? GLY C 145 SER C 152 1 ? 8  
HELX_P HELX_P16 AB7 ASP D 4   ? TRP D 35  ? ASP D 4   TRP D 35  1 ? 32 
HELX_P HELX_P17 AB8 LEU D 37  ? LEU D 65  ? LEU D 37  LEU D 65  1 ? 29 
HELX_P HELX_P18 AB9 ASN D 82  ? VAL D 111 ? ASN D 82  VAL D 111 1 ? 30 
HELX_P HELX_P19 AC1 ASP D 113 ? GLY D 145 ? ASP D 113 GLY D 145 1 ? 33 
HELX_P HELX_P20 AC2 GLY D 145 ? SER D 152 ? GLY D 145 SER D 152 1 ? 8  
HELX_P HELX_P21 AC3 ASP E 4   ? TRP E 35  ? ASP E 4   TRP E 35  1 ? 32 
HELX_P HELX_P22 AC4 LEU E 37  ? LEU E 65  ? LEU E 37  LEU E 65  1 ? 29 
HELX_P HELX_P23 AC5 ASN E 82  ? VAL E 111 ? ASN E 82  VAL E 111 1 ? 30 
HELX_P HELX_P24 AC6 ASP E 113 ? GLY E 145 ? ASP E 113 GLY E 145 1 ? 33 
HELX_P HELX_P25 AC7 GLY E 145 ? SER E 152 ? GLY E 145 SER E 152 1 ? 8  
HELX_P HELX_P26 AC8 ASP F 4   ? TRP F 35  ? ASP F 4   TRP F 35  1 ? 32 
HELX_P HELX_P27 AC9 LEU F 37  ? LEU F 65  ? LEU F 37  LEU F 65  1 ? 29 
HELX_P HELX_P28 AD1 ASN F 82  ? VAL F 111 ? ASN F 82  VAL F 111 1 ? 30 
HELX_P HELX_P29 AD2 ASP F 113 ? GLY F 145 ? ASP F 113 GLY F 145 1 ? 33 
HELX_P HELX_P30 AD3 GLY F 145 ? SER F 152 ? GLY F 145 SER F 152 1 ? 8  
HELX_P HELX_P31 AD4 ASP G 4   ? TRP G 35  ? ASP G 4   TRP G 35  1 ? 32 
HELX_P HELX_P32 AD5 LEU G 37  ? LEU G 65  ? LEU G 37  LEU G 65  1 ? 29 
HELX_P HELX_P33 AD6 ASN G 82  ? VAL G 111 ? ASN G 82  VAL G 111 1 ? 30 
HELX_P HELX_P34 AD7 ASP G 113 ? GLY G 145 ? ASP G 113 GLY G 145 1 ? 33 
HELX_P HELX_P35 AD8 GLY G 145 ? SER G 152 ? GLY G 145 SER G 152 1 ? 8  
HELX_P HELX_P36 AD9 ASP H 4   ? TRP H 35  ? ASP H 4   TRP H 35  1 ? 32 
HELX_P HELX_P37 AE1 LEU H 37  ? TYR H 45  ? LEU H 37  TYR H 45  1 ? 9  
HELX_P HELX_P38 AE2 SER H 48  ? LEU H 65  ? SER H 48  LEU H 65  1 ? 18 
HELX_P HELX_P39 AE3 ASN H 82  ? VAL H 111 ? ASN H 82  VAL H 111 1 ? 30 
HELX_P HELX_P40 AE4 ASP H 113 ? GLY H 145 ? ASP H 113 GLY H 145 1 ? 33 
HELX_P HELX_P41 AE5 GLY H 145 ? SER H 152 ? GLY H 145 SER H 152 1 ? 8  
HELX_P HELX_P42 AE6 ASP I 4   ? TRP I 35  ? ASP I 4   TRP I 35  1 ? 32 
HELX_P HELX_P43 AE7 LEU I 37  ? LEU I 65  ? LEU I 37  LEU I 65  1 ? 29 
HELX_P HELX_P44 AE8 ASN I 82  ? HIS I 112 ? ASN I 82  HIS I 112 1 ? 31 
HELX_P HELX_P45 AE9 ASP I 113 ? GLY I 145 ? ASP I 113 GLY I 145 1 ? 33 
HELX_P HELX_P46 AF1 GLY I 145 ? SER I 152 ? GLY I 145 SER I 152 1 ? 8  
HELX_P HELX_P47 AF2 ASP J 4   ? TRP J 35  ? ASP J 4   TRP J 35  1 ? 32 
HELX_P HELX_P48 AF3 LEU J 37  ? LEU J 65  ? LEU J 37  LEU J 65  1 ? 29 
HELX_P HELX_P49 AF4 ASN J 82  ? HIS J 112 ? ASN J 82  HIS J 112 1 ? 31 
HELX_P HELX_P50 AF5 ASP J 113 ? GLY J 145 ? ASP J 113 GLY J 145 1 ? 33 
HELX_P HELX_P51 AF6 GLY J 145 ? SER J 152 ? GLY J 145 SER J 152 1 ? 8  
HELX_P HELX_P52 AF7 ASP K 4   ? TRP K 35  ? ASP K 4   TRP K 35  1 ? 32 
HELX_P HELX_P53 AF8 LEU K 37  ? LEU K 65  ? LEU K 37  LEU K 65  1 ? 29 
HELX_P HELX_P54 AF9 ASN K 82  ? VAL K 111 ? ASN K 82  VAL K 111 1 ? 30 
HELX_P HELX_P55 AG1 ASP K 113 ? GLY K 145 ? ASP K 113 GLY K 145 1 ? 33 
HELX_P HELX_P56 AG2 GLY K 145 ? SER K 152 ? GLY K 145 SER K 152 1 ? 8  
HELX_P HELX_P57 AG3 ASP L 4   ? GLY L 36  ? ASP L 4   GLY L 36  1 ? 33 
HELX_P HELX_P58 AG4 LEU L 37  ? LEU L 65  ? LEU L 37  LEU L 65  1 ? 29 
HELX_P HELX_P59 AG5 ASN L 82  ? VAL L 111 ? ASN L 82  VAL L 111 1 ? 30 
HELX_P HELX_P60 AG6 ASP L 113 ? GLY L 145 ? ASP L 113 GLY L 145 1 ? 33 
HELX_P HELX_P61 AG7 GLY L 145 ? SER L 152 ? GLY L 145 SER L 152 1 ? 8  
# 
_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 
metalc1  metalc ? ? A  MET 52  SD  ? ? ? 1_555 N  HEM .   FE  ? ? A MET 52  A HEM 202 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
metalc2  metalc ? ? A  ASN 148 OD1 ? ? ? 1_555 M  K   .   K   ? ? A ASN 148 A K   201 1_555 ? ? ? ? ? ? ? 2.865 ? ? 
metalc3  metalc ? ? A  GLN 151 OE1 ? ? ? 1_555 M  K   .   K   ? ? A GLN 151 A K   201 1_555 ? ? ? ? ? ? ? 2.896 ? ? 
metalc4  metalc ? ? M  K   .   K   ? ? ? 1_555 E  ASN 148 OD1 ? ? A K   201 E ASN 148 1_555 ? ? ? ? ? ? ? 2.892 ? ? 
metalc5  metalc ? ? M  K   .   K   ? ? ? 1_555 E  GLN 151 OE1 ? ? A K   201 E GLN 151 1_555 ? ? ? ? ? ? ? 2.911 ? ? 
metalc6  metalc ? ? M  K   .   K   ? ? ? 1_555 J  ASN 148 OD1 ? ? A K   201 J ASN 148 1_555 ? ? ? ? ? ? ? 2.862 ? ? 
metalc7  metalc ? ? M  K   .   K   ? ? ? 1_555 J  GLN 151 OE1 ? ? A K   201 J GLN 151 1_555 ? ? ? ? ? ? ? 2.914 ? ? 
metalc8  metalc ? ? M  K   .   K   ? ? ? 1_555 K  ASN 148 OD1 ? ? A K   201 K ASN 148 1_555 ? ? ? ? ? ? ? 2.864 ? ? 
metalc9  metalc ? ? M  K   .   K   ? ? ? 1_555 K  GLN 151 OE1 ? ? A K   201 K GLN 151 1_555 ? ? ? ? ? ? ? 2.895 ? ? 
metalc10 metalc ? ? N  HEM .   FE  ? ? ? 3_554 G  MET 52  SD  ? ? A HEM 202 G MET 52  1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc11 metalc ? ? B  MET 52  SD  ? ? ? 1_555 V  HEM .   FE  ? ? B MET 52  E HEM 201 1_555 ? ? ? ? ? ? ? 2.384 ? ? 
metalc12 metalc ? ? B  ASN 148 OD1 ? ? ? 1_555 O  K   .   K   ? ? B ASN 148 B K   201 1_555 ? ? ? ? ? ? ? 2.976 ? ? 
metalc13 metalc ? ? B  GLN 151 OE1 ? ? ? 1_555 O  K   .   K   ? ? B GLN 151 B K   201 1_555 ? ? ? ? ? ? ? 2.877 ? ? 
metalc14 metalc ? ? O  K   .   K   ? ? ? 1_555 C  ASN 148 OD1 ? ? B K   201 C ASN 148 1_555 ? ? ? ? ? ? ? 2.856 ? ? 
metalc15 metalc ? ? O  K   .   K   ? ? ? 1_555 C  GLN 151 OE1 ? ? B K   201 C GLN 151 1_555 ? ? ? ? ? ? ? 2.819 ? ? 
metalc16 metalc ? ? O  K   .   K   ? ? ? 1_555 G  ASN 148 OD1 ? ? B K   201 G ASN 148 1_555 ? ? ? ? ? ? ? 2.897 ? ? 
metalc17 metalc ? ? O  K   .   K   ? ? ? 1_555 G  GLN 151 OE1 ? ? B K   201 G GLN 151 1_555 ? ? ? ? ? ? ? 2.862 ? ? 
metalc18 metalc ? ? O  K   .   K   ? ? ? 1_555 L  ASN 148 OD1 ? ? B K   201 L ASN 148 1_555 ? ? ? ? ? ? ? 2.824 ? ? 
metalc19 metalc ? ? O  K   .   K   ? ? ? 1_555 L  GLN 151 OE1 ? ? B K   201 L GLN 151 1_555 ? ? ? ? ? ? ? 2.927 ? ? 
metalc20 metalc ? ? C  MET 52  SD  ? ? ? 1_555 EA HEM .   FE  ? ? C MET 52  I HEM 201 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc21 metalc ? ? D  MET 52  SD  ? ? ? 1_555 T  HEM .   FE  ? ? D MET 52  D HEM 202 1_555 ? ? ? ? ? ? ? 2.454 ? ? 
metalc22 metalc ? ? D  MET 52  SD  ? ? ? 1_555 T  HEM .   FE  ? ? D MET 52  D HEM 202 3_554 ? ? ? ? ? ? ? 2.452 ? ? 
metalc23 metalc ? ? D  ASN 148 OD1 ? ? ? 1_555 S  K   .   K   ? ? D ASN 148 D K   201 1_555 ? ? ? ? ? ? ? 2.881 ? ? 
metalc24 metalc ? ? D  GLN 151 OE1 ? ? ? 1_555 S  K   .   K   ? ? D GLN 151 D K   201 1_555 ? ? ? ? ? ? ? 2.904 ? ? 
metalc25 metalc ? ? S  K   .   K   ? ? ? 1_555 F  ASN 148 OD1 ? ? D K   201 F ASN 148 1_555 ? ? ? ? ? ? ? 2.951 ? ? 
metalc26 metalc ? ? S  K   .   K   ? ? ? 1_555 F  GLN 151 OE1 ? ? D K   201 F GLN 151 1_555 ? ? ? ? ? ? ? 2.878 ? ? 
metalc27 metalc ? ? S  K   .   K   ? ? ? 3_554 H  ASN 148 OD1 ? ? D K   201 H ASN 148 1_555 ? ? ? ? ? ? ? 2.862 ? ? 
metalc28 metalc ? ? S  K   .   K   ? ? ? 3_554 H  GLN 151 OE1 ? ? D K   201 H GLN 151 1_555 ? ? ? ? ? ? ? 2.886 ? ? 
metalc29 metalc ? ? S  K   .   K   ? ? ? 1_555 I  ASN 148 OD1 ? ? D K   201 I ASN 148 1_555 ? ? ? ? ? ? ? 2.935 ? ? 
metalc30 metalc ? ? S  K   .   K   ? ? ? 1_555 I  GLN 151 OE1 ? ? D K   201 I GLN 151 1_555 ? ? ? ? ? ? ? 2.830 ? ? 
metalc31 metalc ? ? E  MET 52  SD  ? ? ? 1_555 V  HEM .   FE  ? ? E MET 52  E HEM 201 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc32 metalc ? ? F  MET 52  SD  ? ? ? 1_555 Y  HEM .   FE  ? ? F MET 52  F HEM 201 1_555 ? ? ? ? ? ? ? 2.347 ? ? 
metalc33 metalc ? ? Y  HEM .   FE  ? ? ? 1_555 K  MET 52  SD  ? ? F HEM 201 K MET 52  1_555 ? ? ? ? ? ? ? 2.403 ? ? 
metalc34 metalc ? ? H  MET 52  SD  ? ? ? 1_555 CA HEM .   FE  ? ? H MET 52  H HEM 202 1_555 ? ? ? ? ? ? ? 2.311 ? ? 
metalc35 metalc ? ? CA HEM .   FE  ? ? ? 1_555 J  MET 52  SD  ? ? H HEM 202 J MET 52  1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc36 metalc ? ? I  MET 52  SD  ? ? ? 1_555 EA HEM .   FE  ? ? I MET 52  I HEM 201 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc37 metalc ? ? L  MET 52  SD  ? ? ? 1_555 KA HEM .   FE  ? ? L MET 52  L HEM 201 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc38 metalc ? ? L  MET 52  SD  ? ? ? 1_555 KA HEM .   FE  ? ? L MET 52  L HEM 201 3_554 ? ? ? ? ? ? ? 2.342 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   SD  ? A  MET 52  ? A MET 52  ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 NA  ? N  HEM .   ? A HEM 202 ? 1_555 87.8  ? 
2   SD  ? A  MET 52  ? A MET 52  ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 NB  ? N  HEM .   ? A HEM 202 ? 1_555 94.8  ? 
3   NA  ? N  HEM .   ? A HEM 202 ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 NB  ? N  HEM .   ? A HEM 202 ? 1_555 86.6  ? 
4   SD  ? A  MET 52  ? A MET 52  ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 NC  ? N  HEM .   ? A HEM 202 ? 1_555 94.9  ? 
5   NA  ? N  HEM .   ? A HEM 202 ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 NC  ? N  HEM .   ? A HEM 202 ? 1_555 176.6 ? 
6   NB  ? N  HEM .   ? A HEM 202 ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 NC  ? N  HEM .   ? A HEM 202 ? 1_555 95.3  ? 
7   SD  ? A  MET 52  ? A MET 52  ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 ND  ? N  HEM .   ? A HEM 202 ? 1_555 88.4  ? 
8   NA  ? N  HEM .   ? A HEM 202 ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 ND  ? N  HEM .   ? A HEM 202 ? 1_555 93.1  ? 
9   NB  ? N  HEM .   ? A HEM 202 ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 ND  ? N  HEM .   ? A HEM 202 ? 1_555 176.8 ? 
10  NC  ? N  HEM .   ? A HEM 202 ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 ND  ? N  HEM .   ? A HEM 202 ? 1_555 84.9  ? 
11  SD  ? A  MET 52  ? A MET 52  ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 SD  ? G  MET 52  ? G MET 52  ? 1_555 80.3  ? 
12  NA  ? N  HEM .   ? A HEM 202 ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 SD  ? G  MET 52  ? G MET 52  ? 1_555 76.0  ? 
13  NB  ? N  HEM .   ? A HEM 202 ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 SD  ? G  MET 52  ? G MET 52  ? 1_555 162.1 ? 
14  NC  ? N  HEM .   ? A HEM 202 ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 SD  ? G  MET 52  ? G MET 52  ? 1_555 102.3 ? 
15  ND  ? N  HEM .   ? A HEM 202 ? 1_555 FE ? N  HEM . ? A HEM 202 ? 1_555 SD  ? G  MET 52  ? G MET 52  ? 1_555 18.7  ? 
16  OD1 ? A  ASN 148 ? A ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? A  GLN 151 ? A GLN 151 ? 1_555 73.4  ? 
17  OD1 ? A  ASN 148 ? A ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? E  ASN 148 ? E ASN 148 ? 1_555 76.4  ? 
18  OE1 ? A  GLN 151 ? A GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? E  ASN 148 ? E ASN 148 ? 1_555 142.4 ? 
19  OD1 ? A  ASN 148 ? A ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? E  GLN 151 ? E GLN 151 ? 1_555 70.7  ? 
20  OE1 ? A  GLN 151 ? A GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? E  GLN 151 ? E GLN 151 ? 1_555 74.0  ? 
21  OD1 ? E  ASN 148 ? E ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? E  GLN 151 ? E GLN 151 ? 1_555 75.3  ? 
22  OD1 ? A  ASN 148 ? A ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? J  ASN 148 ? J ASN 148 ? 1_555 75.5  ? 
23  OE1 ? A  GLN 151 ? A GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? J  ASN 148 ? J ASN 148 ? 1_555 71.3  ? 
24  OD1 ? E  ASN 148 ? E ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? J  ASN 148 ? J ASN 148 ? 1_555 121.6 ? 
25  OE1 ? E  GLN 151 ? E GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? J  ASN 148 ? J ASN 148 ? 1_555 136.9 ? 
26  OD1 ? A  ASN 148 ? A ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? J  GLN 151 ? J GLN 151 ? 1_555 143.8 ? 
27  OE1 ? A  GLN 151 ? A GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? J  GLN 151 ? J GLN 151 ? 1_555 75.7  ? 
28  OD1 ? E  ASN 148 ? E ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? J  GLN 151 ? J GLN 151 ? 1_555 139.1 ? 
29  OE1 ? E  GLN 151 ? E GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? J  GLN 151 ? J GLN 151 ? 1_555 117.7 ? 
30  OD1 ? J  ASN 148 ? J ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? J  GLN 151 ? J GLN 151 ? 1_555 77.1  ? 
31  OD1 ? A  ASN 148 ? A ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? K  ASN 148 ? K ASN 148 ? 1_555 122.1 ? 
32  OE1 ? A  GLN 151 ? A GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? K  ASN 148 ? K ASN 148 ? 1_555 138.8 ? 
33  OD1 ? E  ASN 148 ? E ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? K  ASN 148 ? K ASN 148 ? 1_555 77.1  ? 
34  OE1 ? E  GLN 151 ? E GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? K  ASN 148 ? K ASN 148 ? 1_555 145.2 ? 
35  OD1 ? J  ASN 148 ? J ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? K  ASN 148 ? K ASN 148 ? 1_555 76.4  ? 
36  OE1 ? J  GLN 151 ? J GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OD1 ? K  ASN 148 ? K ASN 148 ? 1_555 72.7  ? 
37  OD1 ? A  ASN 148 ? A ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? K  GLN 151 ? K GLN 151 ? 1_555 138.7 ? 
38  OE1 ? A  GLN 151 ? A GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? K  GLN 151 ? K GLN 151 ? 1_555 120.6 ? 
39  OD1 ? E  ASN 148 ? E ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? K  GLN 151 ? K GLN 151 ? 1_555 71.5  ? 
40  OE1 ? E  GLN 151 ? E GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? K  GLN 151 ? K GLN 151 ? 1_555 76.5  ? 
41  OD1 ? J  ASN 148 ? J ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? K  GLN 151 ? K GLN 151 ? 1_555 144.4 ? 
42  OE1 ? J  GLN 151 ? J GLN 151 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? K  GLN 151 ? K GLN 151 ? 1_555 74.5  ? 
43  OD1 ? K  ASN 148 ? K ASN 148 ? 1_555 K  ? M  K   . ? A K   201 ? 1_555 OE1 ? K  GLN 151 ? K GLN 151 ? 1_555 75.0  ? 
44  SD  ? B  MET 52  ? B MET 52  ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 NA  ? V  HEM .   ? E HEM 201 ? 1_555 84.7  ? 
45  SD  ? B  MET 52  ? B MET 52  ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 NB  ? V  HEM .   ? E HEM 201 ? 1_555 93.7  ? 
46  NA  ? V  HEM .   ? E HEM 201 ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 NB  ? V  HEM .   ? E HEM 201 ? 1_555 91.3  ? 
47  SD  ? B  MET 52  ? B MET 52  ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 NC  ? V  HEM .   ? E HEM 201 ? 1_555 94.5  ? 
48  NA  ? V  HEM .   ? E HEM 201 ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 NC  ? V  HEM .   ? E HEM 201 ? 1_555 179.2 ? 
49  NB  ? V  HEM .   ? E HEM 201 ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 NC  ? V  HEM .   ? E HEM 201 ? 1_555 89.0  ? 
50  SD  ? B  MET 52  ? B MET 52  ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 ND  ? V  HEM .   ? E HEM 201 ? 1_555 86.4  ? 
51  NA  ? V  HEM .   ? E HEM 201 ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 ND  ? V  HEM .   ? E HEM 201 ? 1_555 87.5  ? 
52  NB  ? V  HEM .   ? E HEM 201 ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 ND  ? V  HEM .   ? E HEM 201 ? 1_555 178.9 ? 
53  NC  ? V  HEM .   ? E HEM 201 ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 ND  ? V  HEM .   ? E HEM 201 ? 1_555 92.1  ? 
54  SD  ? B  MET 52  ? B MET 52  ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 SD  ? E  MET 52  ? E MET 52  ? 1_555 167.1 ? 
55  NA  ? V  HEM .   ? E HEM 201 ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 SD  ? E  MET 52  ? E MET 52  ? 1_555 86.2  ? 
56  NB  ? V  HEM .   ? E HEM 201 ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 SD  ? E  MET 52  ? E MET 52  ? 1_555 95.7  ? 
57  NC  ? V  HEM .   ? E HEM 201 ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 SD  ? E  MET 52  ? E MET 52  ? 1_555 94.5  ? 
58  ND  ? V  HEM .   ? E HEM 201 ? 1_555 FE ? V  HEM . ? E HEM 201 ? 1_555 SD  ? E  MET 52  ? E MET 52  ? 1_555 84.0  ? 
59  OD1 ? B  ASN 148 ? B ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? B  GLN 151 ? B GLN 151 ? 1_555 74.7  ? 
60  OD1 ? B  ASN 148 ? B ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? C  ASN 148 ? C ASN 148 ? 1_555 76.6  ? 
61  OE1 ? B  GLN 151 ? B GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? C  ASN 148 ? C ASN 148 ? 1_555 71.7  ? 
62  OD1 ? B  ASN 148 ? B ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? C  GLN 151 ? C GLN 151 ? 1_555 144.1 ? 
63  OE1 ? B  GLN 151 ? B GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? C  GLN 151 ? C GLN 151 ? 1_555 74.6  ? 
64  OD1 ? C  ASN 148 ? C ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? C  GLN 151 ? C GLN 151 ? 1_555 76.5  ? 
65  OD1 ? B  ASN 148 ? B ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? G  ASN 148 ? G ASN 148 ? 1_555 121.2 ? 
66  OE1 ? B  GLN 151 ? B GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? G  ASN 148 ? G ASN 148 ? 1_555 140.6 ? 
67  OD1 ? C  ASN 148 ? C ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? G  ASN 148 ? G ASN 148 ? 1_555 77.4  ? 
68  OE1 ? C  GLN 151 ? C GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? G  ASN 148 ? G ASN 148 ? 1_555 74.8  ? 
69  OD1 ? B  ASN 148 ? B ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? G  GLN 151 ? G GLN 151 ? 1_555 137.6 ? 
70  OE1 ? B  GLN 151 ? B GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? G  GLN 151 ? G GLN 151 ? 1_555 120.2 ? 
71  OD1 ? C  ASN 148 ? C ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? G  GLN 151 ? G GLN 151 ? 1_555 144.2 ? 
72  OE1 ? C  GLN 151 ? C GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? G  GLN 151 ? G GLN 151 ? 1_555 75.2  ? 
73  OD1 ? G  ASN 148 ? G ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? G  GLN 151 ? G GLN 151 ? 1_555 74.4  ? 
74  OD1 ? B  ASN 148 ? B ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? L  ASN 148 ? L ASN 148 ? 1_555 74.6  ? 
75  OE1 ? B  GLN 151 ? B GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? L  ASN 148 ? L ASN 148 ? 1_555 141.5 ? 
76  OD1 ? C  ASN 148 ? C ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? L  ASN 148 ? L ASN 148 ? 1_555 122.1 ? 
77  OE1 ? C  GLN 151 ? C GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? L  ASN 148 ? L ASN 148 ? 1_555 140.7 ? 
78  OD1 ? G  ASN 148 ? G ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? L  ASN 148 ? L ASN 148 ? 1_555 76.4  ? 
79  OE1 ? G  GLN 151 ? G GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OD1 ? L  ASN 148 ? L ASN 148 ? 1_555 71.6  ? 
80  OD1 ? B  ASN 148 ? B ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? L  GLN 151 ? L GLN 151 ? 1_555 72.2  ? 
81  OE1 ? B  GLN 151 ? B GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? L  GLN 151 ? L GLN 151 ? 1_555 74.3  ? 
82  OD1 ? C  ASN 148 ? C ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? L  GLN 151 ? L GLN 151 ? 1_555 138.7 ? 
83  OE1 ? C  GLN 151 ? C GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? L  GLN 151 ? L GLN 151 ? 1_555 116.1 ? 
84  OD1 ? G  ASN 148 ? G ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? L  GLN 151 ? L GLN 151 ? 1_555 142.7 ? 
85  OE1 ? G  GLN 151 ? G GLN 151 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? L  GLN 151 ? L GLN 151 ? 1_555 74.7  ? 
86  OD1 ? L  ASN 148 ? L ASN 148 ? 1_555 K  ? O  K   . ? B K   201 ? 1_555 OE1 ? L  GLN 151 ? L GLN 151 ? 1_555 74.5  ? 
87  SD  ? C  MET 52  ? C MET 52  ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 NA  ? EA HEM .   ? I HEM 201 ? 1_555 83.1  ? 
88  SD  ? C  MET 52  ? C MET 52  ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 NB  ? EA HEM .   ? I HEM 201 ? 1_555 91.7  ? 
89  NA  ? EA HEM .   ? I HEM 201 ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 NB  ? EA HEM .   ? I HEM 201 ? 1_555 88.0  ? 
90  SD  ? C  MET 52  ? C MET 52  ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 NC  ? EA HEM .   ? I HEM 201 ? 1_555 95.7  ? 
91  NA  ? EA HEM .   ? I HEM 201 ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 NC  ? EA HEM .   ? I HEM 201 ? 1_555 177.7 ? 
92  NB  ? EA HEM .   ? I HEM 201 ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 NC  ? EA HEM .   ? I HEM 201 ? 1_555 94.0  ? 
93  SD  ? C  MET 52  ? C MET 52  ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 ND  ? EA HEM .   ? I HEM 201 ? 1_555 88.7  ? 
94  NA  ? EA HEM .   ? I HEM 201 ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 ND  ? EA HEM .   ? I HEM 201 ? 1_555 93.1  ? 
95  NB  ? EA HEM .   ? I HEM 201 ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 ND  ? EA HEM .   ? I HEM 201 ? 1_555 178.9 ? 
96  NC  ? EA HEM .   ? I HEM 201 ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 ND  ? EA HEM .   ? I HEM 201 ? 1_555 84.9  ? 
97  SD  ? C  MET 52  ? C MET 52  ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 SD  ? I  MET 52  ? I MET 52  ? 1_555 167.4 ? 
98  NA  ? EA HEM .   ? I HEM 201 ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 SD  ? I  MET 52  ? I MET 52  ? 1_555 88.5  ? 
99  NB  ? EA HEM .   ? I HEM 201 ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 SD  ? I  MET 52  ? I MET 52  ? 1_555 97.4  ? 
100 NC  ? EA HEM .   ? I HEM 201 ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 SD  ? I  MET 52  ? I MET 52  ? 1_555 92.4  ? 
101 ND  ? EA HEM .   ? I HEM 201 ? 1_555 FE ? EA HEM . ? I HEM 201 ? 1_555 SD  ? I  MET 52  ? I MET 52  ? 1_555 82.3  ? 
102 SD  ? D  MET 52  ? D MET 52  ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 NA  ? T  HEM .   ? D HEM 202 ? 1_555 84.1  ? 
103 SD  ? D  MET 52  ? D MET 52  ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 NB  ? T  HEM .   ? D HEM 202 ? 1_555 93.5  ? 
104 NA  ? T  HEM .   ? D HEM 202 ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 NB  ? T  HEM .   ? D HEM 202 ? 1_555 86.1  ? 
105 SD  ? D  MET 52  ? D MET 52  ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 NC  ? T  HEM .   ? D HEM 202 ? 1_555 95.8  ? 
106 NA  ? T  HEM .   ? D HEM 202 ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 NC  ? T  HEM .   ? D HEM 202 ? 1_555 179.4 ? 
107 NB  ? T  HEM .   ? D HEM 202 ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 NC  ? T  HEM .   ? D HEM 202 ? 1_555 94.5  ? 
108 SD  ? D  MET 52  ? D MET 52  ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 ND  ? T  HEM .   ? D HEM 202 ? 1_555 87.1  ? 
109 NA  ? T  HEM .   ? D HEM 202 ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 ND  ? T  HEM .   ? D HEM 202 ? 1_555 92.7  ? 
110 NB  ? T  HEM .   ? D HEM 202 ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 ND  ? T  HEM .   ? D HEM 202 ? 1_555 178.6 ? 
111 NC  ? T  HEM .   ? D HEM 202 ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 ND  ? T  HEM .   ? D HEM 202 ? 1_555 86.7  ? 
112 SD  ? D  MET 52  ? D MET 52  ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 SD  ? D  MET 52  ? D MET 52  ? 1_555 0.0   ? 
113 NA  ? T  HEM .   ? D HEM 202 ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 SD  ? D  MET 52  ? D MET 52  ? 1_555 84.1  ? 
114 NB  ? T  HEM .   ? D HEM 202 ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 SD  ? D  MET 52  ? D MET 52  ? 1_555 93.5  ? 
115 NC  ? T  HEM .   ? D HEM 202 ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 SD  ? D  MET 52  ? D MET 52  ? 1_555 95.8  ? 
116 ND  ? T  HEM .   ? D HEM 202 ? 1_555 FE ? T  HEM . ? D HEM 202 ? 1_555 SD  ? D  MET 52  ? D MET 52  ? 1_555 87.1  ? 
117 OD1 ? D  ASN 148 ? D ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? D  GLN 151 ? D GLN 151 ? 1_555 77.6  ? 
118 OD1 ? D  ASN 148 ? D ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? F  ASN 148 ? F ASN 148 ? 1_555 75.8  ? 
119 OE1 ? D  GLN 151 ? D GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? F  ASN 148 ? F ASN 148 ? 1_555 146.8 ? 
120 OD1 ? D  ASN 148 ? D ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? F  GLN 151 ? F GLN 151 ? 1_555 70.9  ? 
121 OE1 ? D  GLN 151 ? D GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? F  GLN 151 ? F GLN 151 ? 1_555 77.0  ? 
122 OD1 ? F  ASN 148 ? F ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? F  GLN 151 ? F GLN 151 ? 1_555 75.8  ? 
123 OD1 ? D  ASN 148 ? D ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? H  ASN 148 ? H ASN 148 ? 1_555 74.9  ? 
124 OE1 ? D  GLN 151 ? D GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? H  ASN 148 ? H ASN 148 ? 1_555 25.8  ? 
125 OD1 ? F  ASN 148 ? F ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? H  ASN 148 ? H ASN 148 ? 1_555 125.5 ? 
126 OE1 ? F  GLN 151 ? F GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? H  ASN 148 ? H ASN 148 ? 1_555 51.5  ? 
127 OD1 ? D  ASN 148 ? D ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? H  GLN 151 ? H GLN 151 ? 1_555 77.5  ? 
128 OE1 ? D  GLN 151 ? D GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? H  GLN 151 ? H GLN 151 ? 1_555 26.8  ? 
129 OD1 ? F  ASN 148 ? F ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? H  GLN 151 ? H GLN 151 ? 1_555 125.9 ? 
130 OE1 ? F  GLN 151 ? F GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? H  GLN 151 ? H GLN 151 ? 1_555 51.1  ? 
131 OD1 ? H  ASN 148 ? H ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? H  GLN 151 ? H GLN 151 ? 1_555 2.8   ? 
132 OD1 ? D  ASN 148 ? D ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? I  ASN 148 ? I ASN 148 ? 1_555 123.2 ? 
133 OE1 ? D  GLN 151 ? D GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? I  ASN 148 ? I ASN 148 ? 1_555 137.1 ? 
134 OD1 ? F  ASN 148 ? F ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? I  ASN 148 ? I ASN 148 ? 1_555 75.2  ? 
135 OE1 ? F  GLN 151 ? F GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? I  ASN 148 ? I ASN 148 ? 1_555 142.5 ? 
136 OD1 ? H  ASN 148 ? H ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? I  ASN 148 ? I ASN 148 ? 1_555 157.5 ? 
137 OE1 ? H  GLN 151 ? H GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OD1 ? I  ASN 148 ? I ASN 148 ? 1_555 155.8 ? 
138 OD1 ? D  ASN 148 ? D ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? I  GLN 151 ? I GLN 151 ? 1_555 137.6 ? 
139 OE1 ? D  GLN 151 ? D GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? I  GLN 151 ? I GLN 151 ? 1_555 120.7 ? 
140 OD1 ? F  ASN 148 ? F ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? I  GLN 151 ? I GLN 151 ? 1_555 70.4  ? 
141 OE1 ? F  GLN 151 ? F GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? I  GLN 151 ? I GLN 151 ? 1_555 76.5  ? 
142 OD1 ? H  ASN 148 ? H ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? I  GLN 151 ? I GLN 151 ? 1_555 105.0 ? 
143 OE1 ? H  GLN 151 ? H GLN 151 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? I  GLN 151 ? I GLN 151 ? 1_555 102.4 ? 
144 OD1 ? I  ASN 148 ? I ASN 148 ? 1_555 K  ? S  K   . ? D K   201 ? 1_555 OE1 ? I  GLN 151 ? I GLN 151 ? 1_555 71.6  ? 
145 SD  ? F  MET 52  ? F MET 52  ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 NA  ? Y  HEM .   ? F HEM 201 ? 1_555 84.6  ? 
146 SD  ? F  MET 52  ? F MET 52  ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 NB  ? Y  HEM .   ? F HEM 201 ? 1_555 98.4  ? 
147 NA  ? Y  HEM .   ? F HEM 201 ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 NB  ? Y  HEM .   ? F HEM 201 ? 1_555 87.2  ? 
148 SD  ? F  MET 52  ? F MET 52  ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 NC  ? Y  HEM .   ? F HEM 201 ? 1_555 97.8  ? 
149 NA  ? Y  HEM .   ? F HEM 201 ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 NC  ? Y  HEM .   ? F HEM 201 ? 1_555 177.5 ? 
150 NB  ? Y  HEM .   ? F HEM 201 ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 NC  ? Y  HEM .   ? F HEM 201 ? 1_555 91.5  ? 
151 SD  ? F  MET 52  ? F MET 52  ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 ND  ? Y  HEM .   ? F HEM 201 ? 1_555 85.7  ? 
152 NA  ? Y  HEM .   ? F HEM 201 ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 ND  ? Y  HEM .   ? F HEM 201 ? 1_555 91.4  ? 
153 NB  ? Y  HEM .   ? F HEM 201 ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 ND  ? Y  HEM .   ? F HEM 201 ? 1_555 175.5 ? 
154 NC  ? Y  HEM .   ? F HEM 201 ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 ND  ? Y  HEM .   ? F HEM 201 ? 1_555 89.8  ? 
155 SD  ? F  MET 52  ? F MET 52  ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 SD  ? K  MET 52  ? K MET 52  ? 1_555 165.5 ? 
156 NA  ? Y  HEM .   ? F HEM 201 ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 SD  ? K  MET 52  ? K MET 52  ? 1_555 84.9  ? 
157 NB  ? Y  HEM .   ? F HEM 201 ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 SD  ? K  MET 52  ? K MET 52  ? 1_555 90.9  ? 
158 NC  ? Y  HEM .   ? F HEM 201 ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 SD  ? K  MET 52  ? K MET 52  ? 1_555 93.0  ? 
159 ND  ? Y  HEM .   ? F HEM 201 ? 1_555 FE ? Y  HEM . ? F HEM 201 ? 1_555 SD  ? K  MET 52  ? K MET 52  ? 1_555 84.6  ? 
160 SD  ? H  MET 52  ? H MET 52  ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 NA  ? CA HEM .   ? H HEM 202 ? 1_555 83.5  ? 
161 SD  ? H  MET 52  ? H MET 52  ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 NB  ? CA HEM .   ? H HEM 202 ? 1_555 95.3  ? 
162 NA  ? CA HEM .   ? H HEM 202 ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 NB  ? CA HEM .   ? H HEM 202 ? 1_555 86.8  ? 
163 SD  ? H  MET 52  ? H MET 52  ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 NC  ? CA HEM .   ? H HEM 202 ? 1_555 93.0  ? 
164 NA  ? CA HEM .   ? H HEM 202 ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 NC  ? CA HEM .   ? H HEM 202 ? 1_555 176.4 ? 
165 NB  ? CA HEM .   ? H HEM 202 ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 NC  ? CA HEM .   ? H HEM 202 ? 1_555 93.8  ? 
166 SD  ? H  MET 52  ? H MET 52  ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 ND  ? CA HEM .   ? H HEM 202 ? 1_555 82.2  ? 
167 NA  ? CA HEM .   ? H HEM 202 ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 ND  ? CA HEM .   ? H HEM 202 ? 1_555 92.8  ? 
168 NB  ? CA HEM .   ? H HEM 202 ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 ND  ? CA HEM .   ? H HEM 202 ? 1_555 177.5 ? 
169 NC  ? CA HEM .   ? H HEM 202 ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 ND  ? CA HEM .   ? H HEM 202 ? 1_555 86.5  ? 
170 SD  ? H  MET 52  ? H MET 52  ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 SD  ? J  MET 52  ? J MET 52  ? 1_555 168.1 ? 
171 NA  ? CA HEM .   ? H HEM 202 ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 SD  ? J  MET 52  ? J MET 52  ? 1_555 89.0  ? 
172 NB  ? CA HEM .   ? H HEM 202 ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 SD  ? J  MET 52  ? J MET 52  ? 1_555 93.5  ? 
173 NC  ? CA HEM .   ? H HEM 202 ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 SD  ? J  MET 52  ? J MET 52  ? 1_555 94.5  ? 
174 ND  ? CA HEM .   ? H HEM 202 ? 1_555 FE ? CA HEM . ? H HEM 202 ? 1_555 SD  ? J  MET 52  ? J MET 52  ? 1_555 89.0  ? 
175 SD  ? L  MET 52  ? L MET 52  ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 NA  ? KA HEM .   ? L HEM 201 ? 1_555 88.3  ? 
176 SD  ? L  MET 52  ? L MET 52  ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 NB  ? KA HEM .   ? L HEM 201 ? 1_555 96.5  ? 
177 NA  ? KA HEM .   ? L HEM 201 ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 NB  ? KA HEM .   ? L HEM 201 ? 1_555 90.7  ? 
178 SD  ? L  MET 52  ? L MET 52  ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 NC  ? KA HEM .   ? L HEM 201 ? 1_555 90.7  ? 
179 NA  ? KA HEM .   ? L HEM 201 ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 NC  ? KA HEM .   ? L HEM 201 ? 1_555 178.8 ? 
180 NB  ? KA HEM .   ? L HEM 201 ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 NC  ? KA HEM .   ? L HEM 201 ? 1_555 90.0  ? 
181 SD  ? L  MET 52  ? L MET 52  ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 ND  ? KA HEM .   ? L HEM 201 ? 1_555 83.2  ? 
182 NA  ? KA HEM .   ? L HEM 201 ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 ND  ? KA HEM .   ? L HEM 201 ? 1_555 91.1  ? 
183 NB  ? KA HEM .   ? L HEM 201 ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 ND  ? KA HEM .   ? L HEM 201 ? 1_555 178.2 ? 
184 NC  ? KA HEM .   ? L HEM 201 ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 ND  ? KA HEM .   ? L HEM 201 ? 1_555 88.2  ? 
185 SD  ? L  MET 52  ? L MET 52  ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 SD  ? L  MET 52  ? L MET 52  ? 1_555 0.0   ? 
186 NA  ? KA HEM .   ? L HEM 201 ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 SD  ? L  MET 52  ? L MET 52  ? 1_555 88.3  ? 
187 NB  ? KA HEM .   ? L HEM 201 ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 SD  ? L  MET 52  ? L MET 52  ? 1_555 96.5  ? 
188 NC  ? KA HEM .   ? L HEM 201 ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 SD  ? L  MET 52  ? L MET 52  ? 1_555 90.7  ? 
189 ND  ? KA HEM .   ? L HEM 201 ? 1_555 FE ? KA HEM . ? L HEM 201 ? 1_555 SD  ? L  MET 52  ? L MET 52  ? 1_555 83.2  ? 
# 
_pdbx_entry_details.entry_id                   9NHR 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE1 
_pdbx_validate_close_contact.auth_asym_id_1   I 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    18 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OE1 
_pdbx_validate_close_contact.auth_asym_id_2   I 
_pdbx_validate_close_contact.auth_comp_id_2   GLU 
_pdbx_validate_close_contact.auth_seq_id_2    51 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
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 LEU A 37 ? ? -102.03 70.68 
2 1 LEU D 37 ? ? -103.18 69.33 
3 1 GLU F 66 ? ? 75.33   31.81 
4 1 GLU L 66 ? ? 70.14   37.90 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 D HEM 202 ? T  HEM . 
2 1 D HEM 202 ? T  HEM . 
3 1 D HEM 202 ? T  HEM . 
4 1 L HEM 201 ? KA HEM . 
5 1 L HEM 201 ? KA HEM . 
6 1 L HEM 201 ? KA HEM . 
# 
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 ASP 157 ? A ASP 157 
2  1 Y 1 A ASP 158 ? A ASP 158 
3  1 Y 1 B ASP 157 ? B ASP 157 
4  1 Y 1 B ASP 158 ? B ASP 158 
5  1 Y 1 C ASP 157 ? C ASP 157 
6  1 Y 1 C ASP 158 ? C ASP 158 
7  1 Y 1 D ASP 157 ? D ASP 157 
8  1 Y 1 D ASP 158 ? D ASP 158 
9  1 Y 1 E ASP 157 ? E ASP 157 
10 1 Y 1 E ASP 158 ? E ASP 158 
11 1 Y 1 F ASP 157 ? F ASP 157 
12 1 Y 1 F ASP 158 ? F ASP 158 
13 1 Y 1 G ASP 157 ? G ASP 157 
14 1 Y 1 G ASP 158 ? G ASP 158 
15 1 Y 1 H HIS 46  ? H HIS 46  
16 1 Y 1 H ASP 157 ? H ASP 157 
17 1 Y 1 H ASP 158 ? H ASP 158 
18 1 Y 1 I ASP 157 ? I ASP 157 
19 1 Y 1 I ASP 158 ? I ASP 158 
20 1 Y 1 J ASP 157 ? J ASP 157 
21 1 Y 1 J ASP 158 ? J ASP 158 
22 1 Y 1 K ASP 157 ? K ASP 157 
23 1 Y 1 K ASP 158 ? K ASP 158 
24 1 Y 1 L ASP 157 ? L ASP 157 
25 1 Y 1 L ASP 158 ? L ASP 158 
# 
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 
A1BYB C13  C  Y N 1   
A1BYB C17  C  Y N 2   
A1BYB C02  C  N N 3   
A1BYB C04  C  N N 4   
A1BYB C05  C  Y N 5   
A1BYB C06  C  Y N 6   
A1BYB C08  C  N N 7   
A1BYB C09  C  Y N 8   
A1BYB C10  C  Y N 9   
A1BYB C11  C  Y N 10  
A1BYB C14  C  Y N 11  
A1BYB C15  C  Y N 12  
A1BYB C18  C  Y N 13  
A1BYB C19  C  Y N 14  
A1BYB C20  C  Y N 15  
A1BYB N03  N  N N 16  
A1BYB N07  N  N N 17  
A1BYB O01  O  N N 18  
A1BYB O16  O  N N 19  
A1BYB O21  O  N N 20  
A1BYB CL1  CL N N 21  
A1BYB H1   H  N N 22  
A1BYB H2   H  N N 23  
A1BYB H3   H  N N 24  
A1BYB H4   H  N N 25  
A1BYB H5   H  N N 26  
A1BYB H6   H  N N 27  
A1BYB H7   H  N N 28  
A1BYB H8   H  N N 29  
A1BYB H9   H  N N 30  
A1BYB H10  H  N N 31  
A1BYB H11  H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CYS   N    N  N N 106 
CYS   CA   C  N R 107 
CYS   C    C  N N 108 
CYS   O    O  N N 109 
CYS   CB   C  N N 110 
CYS   SG   S  N N 111 
CYS   OXT  O  N N 112 
CYS   H    H  N N 113 
CYS   H2   H  N N 114 
CYS   HA   H  N N 115 
CYS   HB2  H  N N 116 
CYS   HB3  H  N N 117 
CYS   HG   H  N N 118 
CYS   HXT  H  N N 119 
GLN   N    N  N N 120 
GLN   CA   C  N S 121 
GLN   C    C  N N 122 
GLN   O    O  N N 123 
GLN   CB   C  N N 124 
GLN   CG   C  N N 125 
GLN   CD   C  N N 126 
GLN   OE1  O  N N 127 
GLN   NE2  N  N N 128 
GLN   OXT  O  N N 129 
GLN   H    H  N N 130 
GLN   H2   H  N N 131 
GLN   HA   H  N N 132 
GLN   HB2  H  N N 133 
GLN   HB3  H  N N 134 
GLN   HG2  H  N N 135 
GLN   HG3  H  N N 136 
GLN   HE21 H  N N 137 
GLN   HE22 H  N N 138 
GLN   HXT  H  N N 139 
GLU   N    N  N N 140 
GLU   CA   C  N S 141 
GLU   C    C  N N 142 
GLU   O    O  N N 143 
GLU   CB   C  N N 144 
GLU   CG   C  N N 145 
GLU   CD   C  N N 146 
GLU   OE1  O  N N 147 
GLU   OE2  O  N N 148 
GLU   OXT  O  N N 149 
GLU   H    H  N N 150 
GLU   H2   H  N N 151 
GLU   HA   H  N N 152 
GLU   HB2  H  N N 153 
GLU   HB3  H  N N 154 
GLU   HG2  H  N N 155 
GLU   HG3  H  N N 156 
GLU   HE2  H  N N 157 
GLU   HXT  H  N N 158 
GLY   N    N  N N 159 
GLY   CA   C  N N 160 
GLY   C    C  N N 161 
GLY   O    O  N N 162 
GLY   OXT  O  N N 163 
GLY   H    H  N N 164 
GLY   H2   H  N N 165 
GLY   HA2  H  N N 166 
GLY   HA3  H  N N 167 
GLY   HXT  H  N N 168 
HEM   CHA  C  N N 169 
HEM   CHB  C  N N 170 
HEM   CHC  C  N N 171 
HEM   CHD  C  N N 172 
HEM   C1A  C  Y N 173 
HEM   C2A  C  Y N 174 
HEM   C3A  C  Y N 175 
HEM   C4A  C  Y N 176 
HEM   CMA  C  N N 177 
HEM   CAA  C  N N 178 
HEM   CBA  C  N N 179 
HEM   CGA  C  N N 180 
HEM   O1A  O  N N 181 
HEM   O2A  O  N N 182 
HEM   C1B  C  N N 183 
HEM   C2B  C  N N 184 
HEM   C3B  C  N N 185 
HEM   C4B  C  N N 186 
HEM   CMB  C  N N 187 
HEM   CAB  C  N N 188 
HEM   CBB  C  N N 189 
HEM   C1C  C  Y N 190 
HEM   C2C  C  Y N 191 
HEM   C3C  C  Y N 192 
HEM   C4C  C  Y N 193 
HEM   CMC  C  N N 194 
HEM   CAC  C  N N 195 
HEM   CBC  C  N N 196 
HEM   C1D  C  N N 197 
HEM   C2D  C  N N 198 
HEM   C3D  C  N N 199 
HEM   C4D  C  N N 200 
HEM   CMD  C  N N 201 
HEM   CAD  C  N N 202 
HEM   CBD  C  N N 203 
HEM   CGD  C  N N 204 
HEM   O1D  O  N N 205 
HEM   O2D  O  N N 206 
HEM   NA   N  Y N 207 
HEM   NB   N  N N 208 
HEM   NC   N  Y N 209 
HEM   ND   N  N N 210 
HEM   FE   FE N N 211 
HEM   HHB  H  N N 212 
HEM   HHC  H  N N 213 
HEM   HHD  H  N N 214 
HEM   HMA  H  N N 215 
HEM   HMAA H  N N 216 
HEM   HMAB H  N N 217 
HEM   HAA  H  N N 218 
HEM   HAAA H  N N 219 
HEM   HBA  H  N N 220 
HEM   HBAA H  N N 221 
HEM   HMB  H  N N 222 
HEM   HMBA H  N N 223 
HEM   HMBB H  N N 224 
HEM   HAB  H  N N 225 
HEM   HBB  H  N N 226 
HEM   HBBA H  N N 227 
HEM   HMC  H  N N 228 
HEM   HMCA H  N N 229 
HEM   HMCB H  N N 230 
HEM   HAC  H  N N 231 
HEM   HBC  H  N N 232 
HEM   HBCA H  N N 233 
HEM   HMD  H  N N 234 
HEM   HMDA H  N N 235 
HEM   HMDB H  N N 236 
HEM   HAD  H  N N 237 
HEM   HADA H  N N 238 
HEM   HBD  H  N N 239 
HEM   HBDA H  N N 240 
HEM   H2A  H  N N 241 
HEM   H2D  H  N N 242 
HEM   HHA  H  N N 243 
HIS   N    N  N N 244 
HIS   CA   C  N S 245 
HIS   C    C  N N 246 
HIS   O    O  N N 247 
HIS   CB   C  N N 248 
HIS   CG   C  Y N 249 
HIS   ND1  N  Y N 250 
HIS   CD2  C  Y N 251 
HIS   CE1  C  Y N 252 
HIS   NE2  N  Y N 253 
HIS   OXT  O  N N 254 
HIS   H    H  N N 255 
HIS   H2   H  N N 256 
HIS   HA   H  N N 257 
HIS   HB2  H  N N 258 
HIS   HB3  H  N N 259 
HIS   HD1  H  N N 260 
HIS   HD2  H  N N 261 
HIS   HE1  H  N N 262 
HIS   HE2  H  N N 263 
HIS   HXT  H  N N 264 
HOH   O    O  N N 265 
HOH   H1   H  N N 266 
HOH   H2   H  N N 267 
ILE   N    N  N N 268 
ILE   CA   C  N S 269 
ILE   C    C  N N 270 
ILE   O    O  N N 271 
ILE   CB   C  N S 272 
ILE   CG1  C  N N 273 
ILE   CG2  C  N N 274 
ILE   CD1  C  N N 275 
ILE   OXT  O  N N 276 
ILE   H    H  N N 277 
ILE   H2   H  N N 278 
ILE   HA   H  N N 279 
ILE   HB   H  N N 280 
ILE   HG12 H  N N 281 
ILE   HG13 H  N N 282 
ILE   HG21 H  N N 283 
ILE   HG22 H  N N 284 
ILE   HG23 H  N N 285 
ILE   HD11 H  N N 286 
ILE   HD12 H  N N 287 
ILE   HD13 H  N N 288 
ILE   HXT  H  N N 289 
K     K    K  N N 290 
LEU   N    N  N N 291 
LEU   CA   C  N S 292 
LEU   C    C  N N 293 
LEU   O    O  N N 294 
LEU   CB   C  N N 295 
LEU   CG   C  N N 296 
LEU   CD1  C  N N 297 
LEU   CD2  C  N N 298 
LEU   OXT  O  N N 299 
LEU   H    H  N N 300 
LEU   H2   H  N N 301 
LEU   HA   H  N N 302 
LEU   HB2  H  N N 303 
LEU   HB3  H  N N 304 
LEU   HG   H  N N 305 
LEU   HD11 H  N N 306 
LEU   HD12 H  N N 307 
LEU   HD13 H  N N 308 
LEU   HD21 H  N N 309 
LEU   HD22 H  N N 310 
LEU   HD23 H  N N 311 
LEU   HXT  H  N N 312 
LYS   N    N  N N 313 
LYS   CA   C  N S 314 
LYS   C    C  N N 315 
LYS   O    O  N N 316 
LYS   CB   C  N N 317 
LYS   CG   C  N N 318 
LYS   CD   C  N N 319 
LYS   CE   C  N N 320 
LYS   NZ   N  N N 321 
LYS   OXT  O  N N 322 
LYS   H    H  N N 323 
LYS   H2   H  N N 324 
LYS   HA   H  N N 325 
LYS   HB2  H  N N 326 
LYS   HB3  H  N N 327 
LYS   HG2  H  N N 328 
LYS   HG3  H  N N 329 
LYS   HD2  H  N N 330 
LYS   HD3  H  N N 331 
LYS   HE2  H  N N 332 
LYS   HE3  H  N N 333 
LYS   HZ1  H  N N 334 
LYS   HZ2  H  N N 335 
LYS   HZ3  H  N N 336 
LYS   HXT  H  N N 337 
MET   N    N  N N 338 
MET   CA   C  N S 339 
MET   C    C  N N 340 
MET   O    O  N N 341 
MET   CB   C  N N 342 
MET   CG   C  N N 343 
MET   SD   S  N N 344 
MET   CE   C  N N 345 
MET   OXT  O  N N 346 
MET   H    H  N N 347 
MET   H2   H  N N 348 
MET   HA   H  N N 349 
MET   HB2  H  N N 350 
MET   HB3  H  N N 351 
MET   HG2  H  N N 352 
MET   HG3  H  N N 353 
MET   HE1  H  N N 354 
MET   HE2  H  N N 355 
MET   HE3  H  N N 356 
MET   HXT  H  N N 357 
PG4   O1   O  N N 358 
PG4   C1   C  N N 359 
PG4   C2   C  N N 360 
PG4   O2   O  N N 361 
PG4   C3   C  N N 362 
PG4   C4   C  N N 363 
PG4   O3   O  N N 364 
PG4   C5   C  N N 365 
PG4   C6   C  N N 366 
PG4   O4   O  N N 367 
PG4   C7   C  N N 368 
PG4   C8   C  N N 369 
PG4   O5   O  N N 370 
PG4   HO1  H  N N 371 
PG4   H11  H  N N 372 
PG4   H12  H  N N 373 
PG4   H21  H  N N 374 
PG4   H22  H  N N 375 
PG4   H31  H  N N 376 
PG4   H32  H  N N 377 
PG4   H41  H  N N 378 
PG4   H42  H  N N 379 
PG4   H51  H  N N 380 
PG4   H52  H  N N 381 
PG4   H61  H  N N 382 
PG4   H62  H  N N 383 
PG4   H71  H  N N 384 
PG4   H72  H  N N 385 
PG4   H81  H  N N 386 
PG4   H82  H  N N 387 
PG4   HO5  H  N N 388 
PHE   N    N  N N 389 
PHE   CA   C  N S 390 
PHE   C    C  N N 391 
PHE   O    O  N N 392 
PHE   CB   C  N N 393 
PHE   CG   C  Y N 394 
PHE   CD1  C  Y N 395 
PHE   CD2  C  Y N 396 
PHE   CE1  C  Y N 397 
PHE   CE2  C  Y N 398 
PHE   CZ   C  Y N 399 
PHE   OXT  O  N N 400 
PHE   H    H  N N 401 
PHE   H2   H  N N 402 
PHE   HA   H  N N 403 
PHE   HB2  H  N N 404 
PHE   HB3  H  N N 405 
PHE   HD1  H  N N 406 
PHE   HD2  H  N N 407 
PHE   HE1  H  N N 408 
PHE   HE2  H  N N 409 
PHE   HZ   H  N N 410 
PHE   HXT  H  N N 411 
PRO   N    N  N N 412 
PRO   CA   C  N S 413 
PRO   C    C  N N 414 
PRO   O    O  N N 415 
PRO   CB   C  N N 416 
PRO   CG   C  N N 417 
PRO   CD   C  N N 418 
PRO   OXT  O  N N 419 
PRO   H    H  N N 420 
PRO   HA   H  N N 421 
PRO   HB2  H  N N 422 
PRO   HB3  H  N N 423 
PRO   HG2  H  N N 424 
PRO   HG3  H  N N 425 
PRO   HD2  H  N N 426 
PRO   HD3  H  N N 427 
PRO   HXT  H  N N 428 
SER   N    N  N N 429 
SER   CA   C  N S 430 
SER   C    C  N N 431 
SER   O    O  N N 432 
SER   CB   C  N N 433 
SER   OG   O  N N 434 
SER   OXT  O  N N 435 
SER   H    H  N N 436 
SER   H2   H  N N 437 
SER   HA   H  N N 438 
SER   HB2  H  N N 439 
SER   HB3  H  N N 440 
SER   HG   H  N N 441 
SER   HXT  H  N N 442 
THR   N    N  N N 443 
THR   CA   C  N S 444 
THR   C    C  N N 445 
THR   O    O  N N 446 
THR   CB   C  N R 447 
THR   OG1  O  N N 448 
THR   CG2  C  N N 449 
THR   OXT  O  N N 450 
THR   H    H  N N 451 
THR   H2   H  N N 452 
THR   HA   H  N N 453 
THR   HB   H  N N 454 
THR   HG1  H  N N 455 
THR   HG21 H  N N 456 
THR   HG22 H  N N 457 
THR   HG23 H  N N 458 
THR   HXT  H  N N 459 
TRP   N    N  N N 460 
TRP   CA   C  N S 461 
TRP   C    C  N N 462 
TRP   O    O  N N 463 
TRP   CB   C  N N 464 
TRP   CG   C  Y N 465 
TRP   CD1  C  Y N 466 
TRP   CD2  C  Y N 467 
TRP   NE1  N  Y N 468 
TRP   CE2  C  Y N 469 
TRP   CE3  C  Y N 470 
TRP   CZ2  C  Y N 471 
TRP   CZ3  C  Y N 472 
TRP   CH2  C  Y N 473 
TRP   OXT  O  N N 474 
TRP   H    H  N N 475 
TRP   H2   H  N N 476 
TRP   HA   H  N N 477 
TRP   HB2  H  N N 478 
TRP   HB3  H  N N 479 
TRP   HD1  H  N N 480 
TRP   HE1  H  N N 481 
TRP   HE3  H  N N 482 
TRP   HZ2  H  N N 483 
TRP   HZ3  H  N N 484 
TRP   HH2  H  N N 485 
TRP   HXT  H  N N 486 
TYR   N    N  N N 487 
TYR   CA   C  N S 488 
TYR   C    C  N N 489 
TYR   O    O  N N 490 
TYR   CB   C  N N 491 
TYR   CG   C  Y N 492 
TYR   CD1  C  Y N 493 
TYR   CD2  C  Y N 494 
TYR   CE1  C  Y N 495 
TYR   CE2  C  Y N 496 
TYR   CZ   C  Y N 497 
TYR   OH   O  N N 498 
TYR   OXT  O  N N 499 
TYR   H    H  N N 500 
TYR   H2   H  N N 501 
TYR   HA   H  N N 502 
TYR   HB2  H  N N 503 
TYR   HB3  H  N N 504 
TYR   HD1  H  N N 505 
TYR   HD2  H  N N 506 
TYR   HE1  H  N N 507 
TYR   HE2  H  N N 508 
TYR   HH   H  N N 509 
TYR   HXT  H  N N 510 
VAL   N    N  N N 511 
VAL   CA   C  N S 512 
VAL   C    C  N N 513 
VAL   O    O  N N 514 
VAL   CB   C  N N 515 
VAL   CG1  C  N N 516 
VAL   CG2  C  N N 517 
VAL   OXT  O  N N 518 
VAL   H    H  N N 519 
VAL   H2   H  N N 520 
VAL   HA   H  N N 521 
VAL   HB   H  N N 522 
VAL   HG11 H  N N 523 
VAL   HG12 H  N N 524 
VAL   HG13 H  N N 525 
VAL   HG21 H  N N 526 
VAL   HG22 H  N N 527 
VAL   HG23 H  N N 528 
VAL   HXT  H  N N 529 
# 
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 
A1BYB CL1 C11  sing N N 1   
A1BYB C13 C11  doub Y N 2   
A1BYB C13 C14  sing Y N 3   
A1BYB C11 C10  sing Y N 4   
A1BYB C14 C15  doub Y N 5   
A1BYB C10 C09  doub Y N 6   
A1BYB C15 C09  sing Y N 7   
A1BYB C15 O16  sing N N 8   
A1BYB C09 C08  sing N N 9   
A1BYB C08 N07  sing N N 10  
A1BYB N07 C06  sing N N 11  
A1BYB O21 C04  doub N N 12  
A1BYB C06 C05  doub Y N 13  
A1BYB C06 C17  sing Y N 14  
A1BYB C04 C05  sing N N 15  
A1BYB C04 N03  sing N N 16  
A1BYB C05 C20  sing Y N 17  
A1BYB C17 C18  doub Y N 18  
A1BYB N03 C02  sing N N 19  
A1BYB C20 C02  sing N N 20  
A1BYB C20 C19  doub Y N 21  
A1BYB C18 C19  sing Y N 22  
A1BYB C02 O01  doub N N 23  
A1BYB C13 H1   sing N N 24  
A1BYB C17 H2   sing N N 25  
A1BYB C08 H3   sing N N 26  
A1BYB C08 H4   sing N N 27  
A1BYB C10 H5   sing N N 28  
A1BYB C14 H6   sing N N 29  
A1BYB C18 H7   sing N N 30  
A1BYB C19 H8   sing N N 31  
A1BYB N03 H9   sing N N 32  
A1BYB N07 H10  sing N N 33  
A1BYB O16 H11  sing N N 34  
ALA   N   CA   sing N N 35  
ALA   N   H    sing N N 36  
ALA   N   H2   sing N N 37  
ALA   CA  C    sing N N 38  
ALA   CA  CB   sing N N 39  
ALA   CA  HA   sing N N 40  
ALA   C   O    doub N N 41  
ALA   C   OXT  sing N N 42  
ALA   CB  HB1  sing N N 43  
ALA   CB  HB2  sing N N 44  
ALA   CB  HB3  sing N N 45  
ALA   OXT HXT  sing N N 46  
ARG   N   CA   sing N N 47  
ARG   N   H    sing N N 48  
ARG   N   H2   sing N N 49  
ARG   CA  C    sing N N 50  
ARG   CA  CB   sing N N 51  
ARG   CA  HA   sing N N 52  
ARG   C   O    doub N N 53  
ARG   C   OXT  sing N N 54  
ARG   CB  CG   sing N N 55  
ARG   CB  HB2  sing N N 56  
ARG   CB  HB3  sing N N 57  
ARG   CG  CD   sing N N 58  
ARG   CG  HG2  sing N N 59  
ARG   CG  HG3  sing N N 60  
ARG   CD  NE   sing N N 61  
ARG   CD  HD2  sing N N 62  
ARG   CD  HD3  sing N N 63  
ARG   NE  CZ   sing N N 64  
ARG   NE  HE   sing N N 65  
ARG   CZ  NH1  sing N N 66  
ARG   CZ  NH2  doub N N 67  
ARG   NH1 HH11 sing N N 68  
ARG   NH1 HH12 sing N N 69  
ARG   NH2 HH21 sing N N 70  
ARG   NH2 HH22 sing N N 71  
ARG   OXT HXT  sing N N 72  
ASN   N   CA   sing N N 73  
ASN   N   H    sing N N 74  
ASN   N   H2   sing N N 75  
ASN   CA  C    sing N N 76  
ASN   CA  CB   sing N N 77  
ASN   CA  HA   sing N N 78  
ASN   C   O    doub N N 79  
ASN   C   OXT  sing N N 80  
ASN   CB  CG   sing N N 81  
ASN   CB  HB2  sing N N 82  
ASN   CB  HB3  sing N N 83  
ASN   CG  OD1  doub N N 84  
ASN   CG  ND2  sing N N 85  
ASN   ND2 HD21 sing N N 86  
ASN   ND2 HD22 sing N N 87  
ASN   OXT HXT  sing N N 88  
ASP   N   CA   sing N N 89  
ASP   N   H    sing N N 90  
ASP   N   H2   sing N N 91  
ASP   CA  C    sing N N 92  
ASP   CA  CB   sing N N 93  
ASP   CA  HA   sing N N 94  
ASP   C   O    doub N N 95  
ASP   C   OXT  sing N N 96  
ASP   CB  CG   sing N N 97  
ASP   CB  HB2  sing N N 98  
ASP   CB  HB3  sing N N 99  
ASP   CG  OD1  doub N N 100 
ASP   CG  OD2  sing N N 101 
ASP   OD2 HD2  sing N N 102 
ASP   OXT HXT  sing N N 103 
CYS   N   CA   sing N N 104 
CYS   N   H    sing N N 105 
CYS   N   H2   sing N N 106 
CYS   CA  C    sing N N 107 
CYS   CA  CB   sing N N 108 
CYS   CA  HA   sing N N 109 
CYS   C   O    doub N N 110 
CYS   C   OXT  sing N N 111 
CYS   CB  SG   sing N N 112 
CYS   CB  HB2  sing N N 113 
CYS   CB  HB3  sing N N 114 
CYS   SG  HG   sing N N 115 
CYS   OXT HXT  sing N N 116 
GLN   N   CA   sing N N 117 
GLN   N   H    sing N N 118 
GLN   N   H2   sing N N 119 
GLN   CA  C    sing N N 120 
GLN   CA  CB   sing N N 121 
GLN   CA  HA   sing N N 122 
GLN   C   O    doub N N 123 
GLN   C   OXT  sing N N 124 
GLN   CB  CG   sing N N 125 
GLN   CB  HB2  sing N N 126 
GLN   CB  HB3  sing N N 127 
GLN   CG  CD   sing N N 128 
GLN   CG  HG2  sing N N 129 
GLN   CG  HG3  sing N N 130 
GLN   CD  OE1  doub N N 131 
GLN   CD  NE2  sing N N 132 
GLN   NE2 HE21 sing N N 133 
GLN   NE2 HE22 sing N N 134 
GLN   OXT HXT  sing N N 135 
GLU   N   CA   sing N N 136 
GLU   N   H    sing N N 137 
GLU   N   H2   sing N N 138 
GLU   CA  C    sing N N 139 
GLU   CA  CB   sing N N 140 
GLU   CA  HA   sing N N 141 
GLU   C   O    doub N N 142 
GLU   C   OXT  sing N N 143 
GLU   CB  CG   sing N N 144 
GLU   CB  HB2  sing N N 145 
GLU   CB  HB3  sing N N 146 
GLU   CG  CD   sing N N 147 
GLU   CG  HG2  sing N N 148 
GLU   CG  HG3  sing N N 149 
GLU   CD  OE1  doub N N 150 
GLU   CD  OE2  sing N N 151 
GLU   OE2 HE2  sing N N 152 
GLU   OXT HXT  sing N N 153 
GLY   N   CA   sing N N 154 
GLY   N   H    sing N N 155 
GLY   N   H2   sing N N 156 
GLY   CA  C    sing N N 157 
GLY   CA  HA2  sing N N 158 
GLY   CA  HA3  sing N N 159 
GLY   C   O    doub N N 160 
GLY   C   OXT  sing N N 161 
GLY   OXT HXT  sing N N 162 
HEM   CHA C1A  sing N N 163 
HEM   CHA C4D  doub N N 164 
HEM   CHA HHA  sing N N 165 
HEM   CHB C4A  sing N N 166 
HEM   CHB C1B  doub N N 167 
HEM   CHB HHB  sing N N 168 
HEM   CHC C4B  sing N N 169 
HEM   CHC C1C  doub N N 170 
HEM   CHC HHC  sing N N 171 
HEM   CHD C4C  doub N N 172 
HEM   CHD C1D  sing N N 173 
HEM   CHD HHD  sing N N 174 
HEM   C1A C2A  doub Y N 175 
HEM   C1A NA   sing Y N 176 
HEM   C2A C3A  sing Y N 177 
HEM   C2A CAA  sing N N 178 
HEM   C3A C4A  doub Y N 179 
HEM   C3A CMA  sing N N 180 
HEM   C4A NA   sing Y N 181 
HEM   CMA HMA  sing N N 182 
HEM   CMA HMAA sing N N 183 
HEM   CMA HMAB sing N N 184 
HEM   CAA CBA  sing N N 185 
HEM   CAA HAA  sing N N 186 
HEM   CAA HAAA sing N N 187 
HEM   CBA CGA  sing N N 188 
HEM   CBA HBA  sing N N 189 
HEM   CBA HBAA sing N N 190 
HEM   CGA O1A  doub N N 191 
HEM   CGA O2A  sing N N 192 
HEM   C1B C2B  sing N N 193 
HEM   C1B NB   sing N N 194 
HEM   C2B C3B  doub N N 195 
HEM   C2B CMB  sing N N 196 
HEM   C3B C4B  sing N N 197 
HEM   C3B CAB  sing N N 198 
HEM   C4B NB   doub N N 199 
HEM   CMB HMB  sing N N 200 
HEM   CMB HMBA sing N N 201 
HEM   CMB HMBB sing N N 202 
HEM   CAB CBB  doub N N 203 
HEM   CAB HAB  sing N N 204 
HEM   CBB HBB  sing N N 205 
HEM   CBB HBBA sing N N 206 
HEM   C1C C2C  sing Y N 207 
HEM   C1C NC   sing Y N 208 
HEM   C2C C3C  doub Y N 209 
HEM   C2C CMC  sing N N 210 
HEM   C3C C4C  sing Y N 211 
HEM   C3C CAC  sing N N 212 
HEM   C4C NC   sing Y N 213 
HEM   CMC HMC  sing N N 214 
HEM   CMC HMCA sing N N 215 
HEM   CMC HMCB sing N N 216 
HEM   CAC CBC  doub N N 217 
HEM   CAC HAC  sing N N 218 
HEM   CBC HBC  sing N N 219 
HEM   CBC HBCA sing N N 220 
HEM   C1D C2D  sing N N 221 
HEM   C1D ND   doub N N 222 
HEM   C2D C3D  doub N N 223 
HEM   C2D CMD  sing N N 224 
HEM   C3D C4D  sing N N 225 
HEM   C3D CAD  sing N N 226 
HEM   C4D ND   sing N N 227 
HEM   CMD HMD  sing N N 228 
HEM   CMD HMDA sing N N 229 
HEM   CMD HMDB sing N N 230 
HEM   CAD CBD  sing N N 231 
HEM   CAD HAD  sing N N 232 
HEM   CAD HADA sing N N 233 
HEM   CBD CGD  sing N N 234 
HEM   CBD HBD  sing N N 235 
HEM   CBD HBDA sing N N 236 
HEM   CGD O1D  doub N N 237 
HEM   CGD O2D  sing N N 238 
HEM   O2A H2A  sing N N 239 
HEM   O2D H2D  sing N N 240 
HEM   FE  NA   sing N N 241 
HEM   FE  NB   sing N N 242 
HEM   FE  NC   sing N N 243 
HEM   FE  ND   sing N N 244 
HIS   N   CA   sing N N 245 
HIS   N   H    sing N N 246 
HIS   N   H2   sing N N 247 
HIS   CA  C    sing N N 248 
HIS   CA  CB   sing N N 249 
HIS   CA  HA   sing N N 250 
HIS   C   O    doub N N 251 
HIS   C   OXT  sing N N 252 
HIS   CB  CG   sing N N 253 
HIS   CB  HB2  sing N N 254 
HIS   CB  HB3  sing N N 255 
HIS   CG  ND1  sing Y N 256 
HIS   CG  CD2  doub Y N 257 
HIS   ND1 CE1  doub Y N 258 
HIS   ND1 HD1  sing N N 259 
HIS   CD2 NE2  sing Y N 260 
HIS   CD2 HD2  sing N N 261 
HIS   CE1 NE2  sing Y N 262 
HIS   CE1 HE1  sing N N 263 
HIS   NE2 HE2  sing N N 264 
HIS   OXT HXT  sing N N 265 
HOH   O   H1   sing N N 266 
HOH   O   H2   sing N N 267 
ILE   N   CA   sing N N 268 
ILE   N   H    sing N N 269 
ILE   N   H2   sing N N 270 
ILE   CA  C    sing N N 271 
ILE   CA  CB   sing N N 272 
ILE   CA  HA   sing N N 273 
ILE   C   O    doub N N 274 
ILE   C   OXT  sing N N 275 
ILE   CB  CG1  sing N N 276 
ILE   CB  CG2  sing N N 277 
ILE   CB  HB   sing N N 278 
ILE   CG1 CD1  sing N N 279 
ILE   CG1 HG12 sing N N 280 
ILE   CG1 HG13 sing N N 281 
ILE   CG2 HG21 sing N N 282 
ILE   CG2 HG22 sing N N 283 
ILE   CG2 HG23 sing N N 284 
ILE   CD1 HD11 sing N N 285 
ILE   CD1 HD12 sing N N 286 
ILE   CD1 HD13 sing N N 287 
ILE   OXT HXT  sing N N 288 
LEU   N   CA   sing N N 289 
LEU   N   H    sing N N 290 
LEU   N   H2   sing N N 291 
LEU   CA  C    sing N N 292 
LEU   CA  CB   sing N N 293 
LEU   CA  HA   sing N N 294 
LEU   C   O    doub N N 295 
LEU   C   OXT  sing N N 296 
LEU   CB  CG   sing N N 297 
LEU   CB  HB2  sing N N 298 
LEU   CB  HB3  sing N N 299 
LEU   CG  CD1  sing N N 300 
LEU   CG  CD2  sing N N 301 
LEU   CG  HG   sing N N 302 
LEU   CD1 HD11 sing N N 303 
LEU   CD1 HD12 sing N N 304 
LEU   CD1 HD13 sing N N 305 
LEU   CD2 HD21 sing N N 306 
LEU   CD2 HD22 sing N N 307 
LEU   CD2 HD23 sing N N 308 
LEU   OXT HXT  sing N N 309 
LYS   N   CA   sing N N 310 
LYS   N   H    sing N N 311 
LYS   N   H2   sing N N 312 
LYS   CA  C    sing N N 313 
LYS   CA  CB   sing N N 314 
LYS   CA  HA   sing N N 315 
LYS   C   O    doub N N 316 
LYS   C   OXT  sing N N 317 
LYS   CB  CG   sing N N 318 
LYS   CB  HB2  sing N N 319 
LYS   CB  HB3  sing N N 320 
LYS   CG  CD   sing N N 321 
LYS   CG  HG2  sing N N 322 
LYS   CG  HG3  sing N N 323 
LYS   CD  CE   sing N N 324 
LYS   CD  HD2  sing N N 325 
LYS   CD  HD3  sing N N 326 
LYS   CE  NZ   sing N N 327 
LYS   CE  HE2  sing N N 328 
LYS   CE  HE3  sing N N 329 
LYS   NZ  HZ1  sing N N 330 
LYS   NZ  HZ2  sing N N 331 
LYS   NZ  HZ3  sing N N 332 
LYS   OXT HXT  sing N N 333 
MET   N   CA   sing N N 334 
MET   N   H    sing N N 335 
MET   N   H2   sing N N 336 
MET   CA  C    sing N N 337 
MET   CA  CB   sing N N 338 
MET   CA  HA   sing N N 339 
MET   C   O    doub N N 340 
MET   C   OXT  sing N N 341 
MET   CB  CG   sing N N 342 
MET   CB  HB2  sing N N 343 
MET   CB  HB3  sing N N 344 
MET   CG  SD   sing N N 345 
MET   CG  HG2  sing N N 346 
MET   CG  HG3  sing N N 347 
MET   SD  CE   sing N N 348 
MET   CE  HE1  sing N N 349 
MET   CE  HE2  sing N N 350 
MET   CE  HE3  sing N N 351 
MET   OXT HXT  sing N N 352 
PG4   O1  C1   sing N N 353 
PG4   O1  HO1  sing N N 354 
PG4   C1  C2   sing N N 355 
PG4   C1  H11  sing N N 356 
PG4   C1  H12  sing N N 357 
PG4   C2  O2   sing N N 358 
PG4   C2  H21  sing N N 359 
PG4   C2  H22  sing N N 360 
PG4   O2  C3   sing N N 361 
PG4   C3  C4   sing N N 362 
PG4   C3  H31  sing N N 363 
PG4   C3  H32  sing N N 364 
PG4   C4  O3   sing N N 365 
PG4   C4  H41  sing N N 366 
PG4   C4  H42  sing N N 367 
PG4   O3  C5   sing N N 368 
PG4   C5  C6   sing N N 369 
PG4   C5  H51  sing N N 370 
PG4   C5  H52  sing N N 371 
PG4   C6  O4   sing N N 372 
PG4   C6  H61  sing N N 373 
PG4   C6  H62  sing N N 374 
PG4   O4  C7   sing N N 375 
PG4   C7  C8   sing N N 376 
PG4   C7  H71  sing N N 377 
PG4   C7  H72  sing N N 378 
PG4   C8  O5   sing N N 379 
PG4   C8  H81  sing N N 380 
PG4   C8  H82  sing N N 381 
PG4   O5  HO5  sing N N 382 
PHE   N   CA   sing N N 383 
PHE   N   H    sing N N 384 
PHE   N   H2   sing N N 385 
PHE   CA  C    sing N N 386 
PHE   CA  CB   sing N N 387 
PHE   CA  HA   sing N N 388 
PHE   C   O    doub N N 389 
PHE   C   OXT  sing N N 390 
PHE   CB  CG   sing N N 391 
PHE   CB  HB2  sing N N 392 
PHE   CB  HB3  sing N N 393 
PHE   CG  CD1  doub Y N 394 
PHE   CG  CD2  sing Y N 395 
PHE   CD1 CE1  sing Y N 396 
PHE   CD1 HD1  sing N N 397 
PHE   CD2 CE2  doub Y N 398 
PHE   CD2 HD2  sing N N 399 
PHE   CE1 CZ   doub Y N 400 
PHE   CE1 HE1  sing N N 401 
PHE   CE2 CZ   sing Y N 402 
PHE   CE2 HE2  sing N N 403 
PHE   CZ  HZ   sing N N 404 
PHE   OXT HXT  sing N N 405 
PRO   N   CA   sing N N 406 
PRO   N   CD   sing N N 407 
PRO   N   H    sing N N 408 
PRO   CA  C    sing N N 409 
PRO   CA  CB   sing N N 410 
PRO   CA  HA   sing N N 411 
PRO   C   O    doub N N 412 
PRO   C   OXT  sing N N 413 
PRO   CB  CG   sing N N 414 
PRO   CB  HB2  sing N N 415 
PRO   CB  HB3  sing N N 416 
PRO   CG  CD   sing N N 417 
PRO   CG  HG2  sing N N 418 
PRO   CG  HG3  sing N N 419 
PRO   CD  HD2  sing N N 420 
PRO   CD  HD3  sing N N 421 
PRO   OXT HXT  sing N N 422 
SER   N   CA   sing N N 423 
SER   N   H    sing N N 424 
SER   N   H2   sing N N 425 
SER   CA  C    sing N N 426 
SER   CA  CB   sing N N 427 
SER   CA  HA   sing N N 428 
SER   C   O    doub N N 429 
SER   C   OXT  sing N N 430 
SER   CB  OG   sing N N 431 
SER   CB  HB2  sing N N 432 
SER   CB  HB3  sing N N 433 
SER   OG  HG   sing N N 434 
SER   OXT HXT  sing N N 435 
THR   N   CA   sing N N 436 
THR   N   H    sing N N 437 
THR   N   H2   sing N N 438 
THR   CA  C    sing N N 439 
THR   CA  CB   sing N N 440 
THR   CA  HA   sing N N 441 
THR   C   O    doub N N 442 
THR   C   OXT  sing N N 443 
THR   CB  OG1  sing N N 444 
THR   CB  CG2  sing N N 445 
THR   CB  HB   sing N N 446 
THR   OG1 HG1  sing N N 447 
THR   CG2 HG21 sing N N 448 
THR   CG2 HG22 sing N N 449 
THR   CG2 HG23 sing N N 450 
THR   OXT HXT  sing N N 451 
TRP   N   CA   sing N N 452 
TRP   N   H    sing N N 453 
TRP   N   H2   sing N N 454 
TRP   CA  C    sing N N 455 
TRP   CA  CB   sing N N 456 
TRP   CA  HA   sing N N 457 
TRP   C   O    doub N N 458 
TRP   C   OXT  sing N N 459 
TRP   CB  CG   sing N N 460 
TRP   CB  HB2  sing N N 461 
TRP   CB  HB3  sing N N 462 
TRP   CG  CD1  doub Y N 463 
TRP   CG  CD2  sing Y N 464 
TRP   CD1 NE1  sing Y N 465 
TRP   CD1 HD1  sing N N 466 
TRP   CD2 CE2  doub Y N 467 
TRP   CD2 CE3  sing Y N 468 
TRP   NE1 CE2  sing Y N 469 
TRP   NE1 HE1  sing N N 470 
TRP   CE2 CZ2  sing Y N 471 
TRP   CE3 CZ3  doub Y N 472 
TRP   CE3 HE3  sing N N 473 
TRP   CZ2 CH2  doub Y N 474 
TRP   CZ2 HZ2  sing N N 475 
TRP   CZ3 CH2  sing Y N 476 
TRP   CZ3 HZ3  sing N N 477 
TRP   CH2 HH2  sing N N 478 
TRP   OXT HXT  sing N N 479 
TYR   N   CA   sing N N 480 
TYR   N   H    sing N N 481 
TYR   N   H2   sing N N 482 
TYR   CA  C    sing N N 483 
TYR   CA  CB   sing N N 484 
TYR   CA  HA   sing N N 485 
TYR   C   O    doub N N 486 
TYR   C   OXT  sing N N 487 
TYR   CB  CG   sing N N 488 
TYR   CB  HB2  sing N N 489 
TYR   CB  HB3  sing N N 490 
TYR   CG  CD1  doub Y N 491 
TYR   CG  CD2  sing Y N 492 
TYR   CD1 CE1  sing Y N 493 
TYR   CD1 HD1  sing N N 494 
TYR   CD2 CE2  doub Y N 495 
TYR   CD2 HD2  sing N N 496 
TYR   CE1 CZ   doub Y N 497 
TYR   CE1 HE1  sing N N 498 
TYR   CE2 CZ   sing Y N 499 
TYR   CE2 HE2  sing N N 500 
TYR   CZ  OH   sing N N 501 
TYR   OH  HH   sing N N 502 
TYR   OXT HXT  sing N N 503 
VAL   N   CA   sing N N 504 
VAL   N   H    sing N N 505 
VAL   N   H2   sing N N 506 
VAL   CA  C    sing N N 507 
VAL   CA  CB   sing N N 508 
VAL   CA  HA   sing N N 509 
VAL   C   O    doub N N 510 
VAL   C   OXT  sing N N 511 
VAL   CB  CG1  sing N N 512 
VAL   CB  CG2  sing N N 513 
VAL   CB  HB   sing N N 514 
VAL   CG1 HG11 sing N N 515 
VAL   CG1 HG12 sing N N 516 
VAL   CG1 HG13 sing N N 517 
VAL   CG2 HG21 sing N N 518 
VAL   CG2 HG22 sing N N 519 
VAL   CG2 HG23 sing N N 520 
VAL   OXT HXT  sing N N 521 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/Office of the Director'                                            'United States' 'S10 OD030394' 1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' AI169344       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   5D8O 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9NHR 
_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]   0.007718 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005145 
_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]   0.004925 
_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  
CL 
FE 
K  
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   . MET   A  1 1   ? 26.446  -3.119   -40.794 1.00 32.53 ? 1   MET   A N   1 
ATOM   2     C  CA  . MET   A  1 1   ? 25.788  -2.007   -40.046 1.00 36.16 ? 1   MET   A CA  1 
ATOM   3     C  C   . MET   A  1 1   ? 26.647  -1.765   -38.814 1.00 38.96 ? 1   MET   A C   1 
ATOM   4     O  O   . MET   A  1 1   ? 26.730  -2.632   -37.953 1.00 39.28 ? 1   MET   A O   1 
ATOM   5     C  CB  . MET   A  1 1   ? 24.353  -2.379   -39.670 1.00 34.78 ? 1   MET   A CB  1 
ATOM   6     C  CG  . MET   A  1 1   ? 23.500  -1.226   -39.139 1.00 38.91 ? 1   MET   A CG  1 
ATOM   7     S  SD  . MET   A  1 1   ? 21.879  -1.798   -38.591 1.00 41.78 ? 1   MET   A SD  1 
ATOM   8     C  CE  . MET   A  1 1   ? 22.313  -2.700   -37.119 1.00 43.66 ? 1   MET   A CE  1 
ATOM   9     N  N   . LYS   A  1 2   ? 27.302  -0.615   -38.717 1.00 39.24 ? 2   LYS   A N   1 
ATOM   10    C  CA  . LYS   A  1 2   ? 28.327  -0.447   -37.686 1.00 41.38 ? 2   LYS   A CA  1 
ATOM   11    C  C   . LYS   A  1 2   ? 27.669  -0.431   -36.320 1.00 35.52 ? 2   LYS   A C   1 
ATOM   12    O  O   . LYS   A  1 2   ? 26.784  0.387    -36.059 1.00 31.86 ? 2   LYS   A O   1 
ATOM   13    C  CB  . LYS   A  1 2   ? 29.128  0.833    -37.896 1.00 48.85 ? 2   LYS   A CB  1 
ATOM   14    C  CG  . LYS   A  1 2   ? 30.447  0.619    -38.624 1.00 50.89 ? 2   LYS   A CG  1 
ATOM   15    C  CD  . LYS   A  1 2   ? 30.952  1.911    -39.278 1.00 51.91 ? 2   LYS   A CD  1 
ATOM   16    N  N   . GLY   A  1 3   ? 28.096  -1.319   -35.449 1.00 31.49 ? 3   GLY   A N   1 
ATOM   17    C  CA  . GLY   A  1 3   ? 27.512  -1.358   -34.125 1.00 36.01 ? 3   GLY   A CA  1 
ATOM   18    C  C   . GLY   A  1 3   ? 28.229  -0.460   -33.113 1.00 40.18 ? 3   GLY   A C   1 
ATOM   19    O  O   . GLY   A  1 3   ? 29.343  0.017    -33.316 1.00 35.86 ? 3   GLY   A O   1 
ATOM   20    N  N   . ASP   A  1 4   ? 27.558  -0.264   -31.986 1.00 30.93 ? 4   ASP   A N   1 
ATOM   21    C  CA  . ASP   A  1 4   ? 28.170  0.377    -30.828 1.00 29.82 ? 4   ASP   A CA  1 
ATOM   22    C  C   . ASP   A  1 4   ? 29.431  -0.362   -30.395 1.00 35.49 ? 4   ASP   A C   1 
ATOM   23    O  O   . ASP   A  1 4   ? 29.446  -1.596   -30.283 1.00 32.80 ? 4   ASP   A O   1 
ATOM   24    C  CB  . ASP   A  1 4   ? 27.120  0.413    -29.709 1.00 34.60 ? 4   ASP   A CB  1 
ATOM   25    C  CG  . ASP   A  1 4   ? 27.656  0.971    -28.393 1.00 37.14 ? 4   ASP   A CG  1 
ATOM   26    O  OD1 . ASP   A  1 4   ? 27.593  2.194    -28.223 1.00 37.49 ? 4   ASP   A OD1 1 
ATOM   27    O  OD2 . ASP   A  1 4   ? 28.131  0.188    -27.545 1.00 34.78 ? 4   ASP   A OD2 1 
ATOM   28    N  N   . LYS   A  1 5   ? 30.509  0.394    -30.119 1.00 32.60 ? 5   LYS   A N   1 
ATOM   29    C  CA  . LYS   A  1 5   ? 31.778  -0.264   -29.818 1.00 31.53 ? 5   LYS   A CA  1 
ATOM   30    C  C   . LYS   A  1 5   ? 31.691  -1.111   -28.548 1.00 27.46 ? 5   LYS   A C   1 
ATOM   31    O  O   . LYS   A  1 5   ? 32.260  -2.208   -28.474 1.00 30.13 ? 5   LYS   A O   1 
ATOM   32    C  CB  . LYS   A  1 5   ? 32.909  0.768    -29.664 1.00 35.22 ? 5   LYS   A CB  1 
ATOM   33    C  CG  . LYS   A  1 5   ? 34.186  0.167    -29.065 1.00 41.56 ? 5   LYS   A CG  1 
ATOM   34    N  N   . LYS   A  1 6   ? 31.038  -0.603   -27.522 1.00 39.24 ? 6   LYS   A N   1 
ATOM   35    C  CA  . LYS   A  1 6   ? 31.002  -1.345   -26.270 1.00 39.82 ? 6   LYS   A CA  1 
ATOM   36    C  C   . LYS   A  1 6   ? 30.022  -2.522   -26.344 1.00 28.29 ? 6   LYS   A C   1 
ATOM   37    O  O   . LYS   A  1 6   ? 30.255  -3.551   -25.705 1.00 36.07 ? 6   LYS   A O   1 
ATOM   38    C  CB  . LYS   A  1 6   ? 30.673  -0.374   -25.134 1.00 38.42 ? 6   LYS   A CB  1 
ATOM   39    C  CG  . LYS   A  1 6   ? 30.617  -1.002   -23.745 1.00 44.81 ? 6   LYS   A CG  1 
ATOM   40    C  CD  . LYS   A  1 6   ? 32.003  -1.310   -23.197 1.00 49.52 ? 6   LYS   A CD  1 
ATOM   41    C  CE  . LYS   A  1 6   ? 31.948  -1.842   -21.764 1.00 54.17 ? 6   LYS   A CE  1 
ATOM   42    N  NZ  . LYS   A  1 6   ? 33.088  -2.768   -21.492 1.00 68.67 ? 6   LYS   A NZ  1 
ATOM   43    N  N   . VAL   A  1 7   ? 28.956  -2.418   -27.134 1.00 33.50 ? 7   VAL   A N   1 
ATOM   44    C  CA  . VAL   A  1 7   ? 28.157  -3.613   -27.431 1.00 30.17 ? 7   VAL   A CA  1 
ATOM   45    C  C   . VAL   A  1 7   ? 29.057  -4.709   -27.973 1.00 27.51 ? 7   VAL   A C   1 
ATOM   46    O  O   . VAL   A  1 7   ? 29.086  -5.840   -27.465 1.00 28.92 ? 7   VAL   A O   1 
ATOM   47    C  CB  . VAL   A  1 7   ? 27.023  -3.287   -28.419 1.00 36.65 ? 7   VAL   A CB  1 
ATOM   48    C  CG1 . VAL   A  1 7   ? 26.395  -4.585   -28.939 1.00 33.21 ? 7   VAL   A CG1 1 
ATOM   49    C  CG2 . VAL   A  1 7   ? 25.969  -2.423   -27.754 1.00 33.30 ? 7   VAL   A CG2 1 
ATOM   50    N  N   . ILE   A  1 8   ? 29.850  -4.383   -28.993 1.00 30.24 ? 8   ILE   A N   1 
ATOM   51    C  CA  . ILE   A  1 8   ? 30.706  -5.402   -29.587 1.00 30.52 ? 8   ILE   A CA  1 
ATOM   52    C  C   . ILE   A  1 8   ? 31.669  -5.978   -28.553 1.00 33.94 ? 8   ILE   A C   1 
ATOM   53    O  O   . ILE   A  1 8   ? 31.938  -7.191   -28.533 1.00 29.62 ? 8   ILE   A O   1 
ATOM   54    C  CB  . ILE   A  1 8   ? 31.434  -4.809   -30.807 1.00 30.16 ? 8   ILE   A CB  1 
ATOM   55    C  CG1 . ILE   A  1 8   ? 30.397  -4.494   -31.910 1.00 33.73 ? 8   ILE   A CG1 1 
ATOM   56    C  CG2 . ILE   A  1 8   ? 32.501  -5.721   -31.251 1.00 32.68 ? 8   ILE   A CG2 1 
ATOM   57    C  CD1 . ILE   A  1 8   ? 30.924  -3.620   -33.051 1.00 34.26 ? 8   ILE   A CD1 1 
ATOM   58    N  N   . GLN   A  1 9   ? 32.208  -5.135   -27.672 1.00 35.07 ? 9   GLN   A N   1 
ATOM   59    C  CA  . GLN   A  1 9   ? 33.131  -5.658   -26.666 1.00 34.02 ? 9   GLN   A CA  1 
ATOM   60    C  C   . GLN   A  1 9   ? 32.412  -6.607   -25.709 1.00 26.67 ? 9   GLN   A C   1 
ATOM   61    O  O   . GLN   A  1 9   ? 32.942  -7.660   -25.331 1.00 32.12 ? 9   GLN   A O   1 
ATOM   62    C  CB  . GLN   A  1 9   ? 33.788  -4.505   -25.891 1.00 37.87 ? 9   GLN   A CB  1 
ATOM   63    C  CG  . GLN   A  1 9   ? 34.958  -3.858   -26.623 1.00 39.65 ? 9   GLN   A CG  1 
ATOM   64    C  CD  . GLN   A  1 9   ? 35.312  -2.442   -26.135 1.00 53.64 ? 9   GLN   A CD  1 
ATOM   65    O  OE1 . GLN   A  1 9   ? 34.612  -1.838   -25.309 1.00 47.98 ? 9   GLN   A OE1 1 
ATOM   66    N  NE2 . GLN   A  1 9   ? 36.399  -1.904   -26.675 1.00 59.69 ? 9   GLN   A NE2 1 
ATOM   67    N  N   . HIS   A  1 10  ? 31.216  -6.242   -25.296 1.00 27.30 ? 10  HIS   A N   1 
ATOM   68    C  CA  . HIS   A  1 10  ? 30.404  -7.171   -24.513 1.00 31.96 ? 10  HIS   A CA  1 
ATOM   69    C  C   . HIS   A  1 10  ? 30.168  -8.478   -25.267 1.00 30.40 ? 10  HIS   A C   1 
ATOM   70    O  O   . HIS   A  1 10  ? 30.261  -9.567   -24.686 1.00 30.87 ? 10  HIS   A O   1 
ATOM   71    C  CB  . HIS   A  1 10  ? 29.079  -6.520   -24.185 1.00 32.11 ? 10  HIS   A CB  1 
ATOM   72    C  CG  . HIS   A  1 10  ? 29.099  -5.674   -22.952 1.00 34.71 ? 10  HIS   A CG  1 
ATOM   73    N  ND1 . HIS   A  1 10  ? 29.289  -6.204   -21.694 1.00 36.14 ? 10  HIS   A ND1 1 
ATOM   74    C  CD2 . HIS   A  1 10  ? 28.919  -4.343   -22.780 1.00 29.61 ? 10  HIS   A CD2 1 
ATOM   75    C  CE1 . HIS   A  1 10  ? 29.226  -5.234   -20.798 1.00 41.00 ? 10  HIS   A CE1 1 
ATOM   76    N  NE2 . HIS   A  1 10  ? 29.002  -4.095   -21.427 1.00 34.87 ? 10  HIS   A NE2 1 
ATOM   77    N  N   . LEU   A  1 11  ? 29.798  -8.393   -26.553 1.00 31.49 ? 11  LEU   A N   1 
ATOM   78    C  CA  . LEU   A  1 11  ? 29.556  -9.626   -27.304 1.00 28.64 ? 11  LEU   A CA  1 
ATOM   79    C  C   . LEU   A  1 11  ? 30.785  -10.508  -27.317 1.00 34.34 ? 11  LEU   A C   1 
ATOM   80    O  O   . LEU   A  1 11  ? 30.676  -11.731  -27.141 1.00 29.06 ? 11  LEU   A O   1 
ATOM   81    C  CB  . LEU   A  1 11  ? 29.091  -9.328   -28.733 1.00 26.98 ? 11  LEU   A CB  1 
ATOM   82    C  CG  . LEU   A  1 11  ? 27.792  -8.528   -28.865 1.00 34.92 ? 11  LEU   A CG  1 
ATOM   83    C  CD1 . LEU   A  1 11  ? 27.373  -8.256   -30.313 1.00 33.35 ? 11  LEU   A CD1 1 
ATOM   84    C  CD2 . LEU   A  1 11  ? 26.651  -9.214   -28.125 1.00 32.85 ? 11  LEU   A CD2 1 
ATOM   85    N  N   . ASN   A  1 12  ? 31.978  -9.900   -27.459 1.00 30.49 ? 12  ASN   A N   1 
ATOM   86    C  CA  . ASN   A  1 12  ? 33.209  -10.676  -27.427 1.00 29.38 ? 12  ASN   A CA  1 
ATOM   87    C  C   . ASN   A  1 12  ? 33.493  -11.252  -26.044 1.00 27.91 ? 12  ASN   A C   1 
ATOM   88    O  O   . ASN   A  1 12  ? 34.014  -12.366  -25.940 1.00 31.74 ? 12  ASN   A O   1 
ATOM   89    C  CB  . ASN   A  1 12  ? 34.385  -9.820   -27.935 1.00 35.90 ? 12  ASN   A CB  1 
ATOM   90    C  CG  . ASN   A  1 12  ? 34.676  -10.052  -29.428 1.00 36.04 ? 12  ASN   A CG  1 
ATOM   91    O  OD1 . ASN   A  1 12  ? 34.601  -11.186  -29.906 1.00 35.52 ? 12  ASN   A OD1 1 
ATOM   92    N  ND2 . ASN   A  1 12  ? 34.993  -8.982   -30.166 1.00 34.66 ? 12  ASN   A ND2 1 
ATOM   93    N  N   . LYS   A  1 13  ? 33.141  -10.554  -24.970 1.00 28.63 ? 13  LYS   A N   1 
ATOM   94    C  CA  . LYS   A  1 13  ? 33.287  -11.170  -23.647 1.00 28.66 ? 13  LYS   A CA  1 
ATOM   95    C  C   . LYS   A  1 13  ? 32.370  -12.389  -23.510 1.00 29.02 ? 13  LYS   A C   1 
ATOM   96    O  O   . LYS   A  1 13  ? 32.803  -13.461  -23.066 1.00 27.90 ? 13  LYS   A O   1 
ATOM   97    C  CB  . LYS   A  1 13  ? 32.985  -10.147  -22.550 1.00 31.48 ? 13  LYS   A CB  1 
ATOM   98    C  CG  . LYS   A  1 13  ? 33.302  -10.631  -21.137 1.00 30.25 ? 13  LYS   A CG  1 
ATOM   99    C  CD  . LYS   A  1 13  ? 33.061  -9.460   -20.107 1.00 33.82 ? 13  LYS   A CD  1 
ATOM   100   C  CE  . LYS   A  1 13  ? 33.414  -9.830   -18.717 1.00 35.76 ? 13  LYS   A CE  1 
ATOM   101   N  NZ  . LYS   A  1 13  ? 32.941  -8.758   -17.791 1.00 47.97 ? 13  LYS   A NZ  1 
ATOM   102   N  N   . ILE   A  1 14  ? 31.090  -12.237  -23.872 1.00 32.47 ? 14  ILE   A N   1 
ATOM   103   C  CA  . ILE   A  1 14  ? 30.176  -13.385  -23.857 1.00 29.30 ? 14  ILE   A CA  1 
ATOM   104   C  C   . ILE   A  1 14  ? 30.744  -14.509  -24.722 1.00 29.79 ? 14  ILE   A C   1 
ATOM   105   O  O   . ILE   A  1 14  ? 30.792  -15.678  -24.315 1.00 27.83 ? 14  ILE   A O   1 
ATOM   106   C  CB  . ILE   A  1 14  ? 28.772  -12.970  -24.335 1.00 32.64 ? 14  ILE   A CB  1 
ATOM   107   C  CG1 . ILE   A  1 14  ? 28.175  -11.824  -23.511 1.00 32.81 ? 14  ILE   A CG1 1 
ATOM   108   C  CG2 . ILE   A  1 14  ? 27.792  -14.163  -24.268 1.00 30.04 ? 14  ILE   A CG2 1 
ATOM   109   C  CD1 . ILE   A  1 14  ? 28.236  -12.057  -22.045 1.00 38.46 ? 14  ILE   A CD1 1 
ATOM   110   N  N   . LEU   A  1 15  ? 31.186  -14.168  -25.936 1.00 30.21 ? 15  LEU   A N   1 
ATOM   111   C  CA  . LEU   A  1 15  ? 31.778  -15.175  -26.810 1.00 33.03 ? 15  LEU   A CA  1 
ATOM   112   C  C   . LEU   A  1 15  ? 32.949  -15.868  -26.132 1.00 35.16 ? 15  LEU   A C   1 
ATOM   113   O  O   . LEU   A  1 15  ? 33.106  -17.095  -26.238 1.00 27.78 ? 15  LEU   A O   1 
ATOM   114   C  CB  . LEU   A  1 15  ? 32.227  -14.527  -28.130 1.00 34.57 ? 15  LEU   A CB  1 
ATOM   115   C  CG  . LEU   A  1 15  ? 32.991  -15.390  -29.137 1.00 36.16 ? 15  LEU   A CG  1 
ATOM   116   C  CD1 . LEU   A  1 15  ? 32.247  -16.674  -29.485 1.00 31.43 ? 15  LEU   A CD1 1 
ATOM   117   C  CD2 . LEU   A  1 15  ? 33.248  -14.579  -30.397 1.00 33.03 ? 15  LEU   A CD2 1 
ATOM   118   N  N   . GLY   A  1 16  ? 33.783  -15.103  -25.416 1.00 32.93 ? 16  GLY   A N   1 
ATOM   119   C  CA  . GLY   A  1 16  ? 34.892  -15.717  -24.705 1.00 28.85 ? 16  GLY   A CA  1 
ATOM   120   C  C   . GLY   A  1 16  ? 34.446  -16.713  -23.650 1.00 25.63 ? 16  GLY   A C   1 
ATOM   121   O  O   . GLY   A  1 16  ? 35.063  -17.773  -23.481 1.00 32.11 ? 16  GLY   A O   1 
ATOM   122   N  N   . ASN   A  1 17  ? 33.393  -16.371  -22.898 1.00 31.61 ? 17  ASN   A N   1 
ATOM   123   C  CA  . ASN   A  1 17  ? 32.802  -17.323  -21.956 1.00 38.79 ? 17  ASN   A CA  1 
ATOM   124   C  C   . ASN   A  1 17  ? 32.336  -18.601  -22.658 1.00 25.01 ? 17  ASN   A C   1 
ATOM   125   O  O   . ASN   A  1 17  ? 32.553  -19.714  -22.163 1.00 26.61 ? 17  ASN   A O   1 
ATOM   126   C  CB  . ASN   A  1 17  ? 31.619  -16.670  -21.229 1.00 34.31 ? 17  ASN   A CB  1 
ATOM   127   C  CG  . ASN   A  1 17  ? 32.030  -15.536  -20.284 1.00 35.43 ? 17  ASN   A CG  1 
ATOM   128   O  OD1 . ASN   A  1 17  ? 33.144  -15.510  -19.753 1.00 37.10 ? 17  ASN   A OD1 1 
ATOM   129   N  ND2 . ASN   A  1 17  ? 31.105  -14.593  -20.066 1.00 33.84 ? 17  ASN   A ND2 1 
ATOM   130   N  N   . GLU   A  1 18  ? 31.713  -18.458  -23.825 1.00 28.75 ? 18  GLU   A N   1 
ATOM   131   C  CA  . GLU   A  1 18  ? 31.244  -19.626  -24.582 1.00 31.32 ? 18  GLU   A CA  1 
ATOM   132   C  C   . GLU   A  1 18  ? 32.393  -20.504  -25.061 1.00 29.31 ? 18  GLU   A C   1 
ATOM   133   O  O   . GLU   A  1 18  ? 32.273  -21.732  -25.079 1.00 28.68 ? 18  GLU   A O   1 
ATOM   134   C  CB  . GLU   A  1 18  ? 30.412  -19.171  -25.792 1.00 32.53 ? 18  GLU   A CB  1 
ATOM   135   C  CG  . GLU   A  1 18  ? 29.210  -18.315  -25.428 1.00 35.30 ? 18  GLU   A CG  1 
ATOM   136   C  CD  . GLU   A  1 18  ? 28.010  -19.105  -24.983 1.00 44.56 ? 18  GLU   A CD  1 
ATOM   137   O  OE1 . GLU   A  1 18  ? 28.066  -20.355  -24.984 1.00 46.06 ? 18  GLU   A OE1 1 
ATOM   138   O  OE2 . GLU   A  1 18  ? 27.007  -18.460  -24.622 1.00 43.26 ? 18  GLU   A OE2 1 
ATOM   139   N  N   . LEU   A  1 19  ? 33.508  -19.903  -25.485 1.00 31.25 ? 19  LEU   A N   1 
ATOM   140   C  CA  . LEU   A  1 19  ? 34.632  -20.713  -25.939 1.00 28.38 ? 19  LEU   A CA  1 
ATOM   141   C  C   . LEU   A  1 19  ? 35.193  -21.549  -24.808 1.00 26.50 ? 19  LEU   A C   1 
ATOM   142   O  O   . LEU   A  1 19  ? 35.561  -22.721  -25.005 1.00 29.36 ? 19  LEU   A O   1 
ATOM   143   C  CB  . LEU   A  1 19  ? 35.718  -19.822  -26.553 1.00 30.99 ? 19  LEU   A CB  1 
ATOM   144   C  CG  . LEU   A  1 19  ? 35.332  -19.100  -27.839 1.00 34.48 ? 19  LEU   A CG  1 
ATOM   145   C  CD1 . LEU   A  1 19  ? 36.436  -18.109  -28.230 1.00 39.00 ? 19  LEU   A CD1 1 
ATOM   146   C  CD2 . LEU   A  1 19  ? 35.065  -20.104  -28.971 1.00 33.21 ? 19  LEU   A CD2 1 
ATOM   147   N  N   . ILE   A  1 20  ? 35.275  -20.966  -23.612 1.00 27.79 ? 20  ILE   A N   1 
ATOM   148   C  CA  . ILE   A  1 20  ? 35.647  -21.730  -22.427 1.00 26.21 ? 20  ILE   A CA  1 
ATOM   149   C  C   . ILE   A  1 20  ? 34.656  -22.868  -22.200 1.00 29.57 ? 20  ILE   A C   1 
ATOM   150   O  O   . ILE   A  1 20  ? 35.039  -24.035  -22.019 1.00 24.64 ? 20  ILE   A O   1 
ATOM   151   C  CB  . ILE   A  1 20  ? 35.708  -20.792  -21.203 1.00 34.08 ? 20  ILE   A CB  1 
ATOM   152   C  CG1 . ILE   A  1 20  ? 36.907  -19.837  -21.288 1.00 33.59 ? 20  ILE   A CG1 1 
ATOM   153   C  CG2 . ILE   A  1 20  ? 35.758  -21.596  -19.890 1.00 37.34 ? 20  ILE   A CG2 1 
ATOM   154   C  CD1 . ILE   A  1 20  ? 36.826  -18.672  -20.268 1.00 30.24 ? 20  ILE   A CD1 1 
ATOM   155   N  N   . ALA   A  1 21  ? 33.359  -22.529  -22.169 1.00 26.29 ? 21  ALA   A N   1 
ATOM   156   C  CA  . ALA   A  1 21  ? 32.327  -23.528  -21.899 1.00 30.24 ? 21  ALA   A CA  1 
ATOM   157   C  C   . ALA   A  1 21  ? 32.349  -24.658  -22.930 1.00 28.57 ? 21  ALA   A C   1 
ATOM   158   O  O   . ALA   A  1 21  ? 32.245  -25.835  -22.571 1.00 26.40 ? 21  ALA   A O   1 
ATOM   159   C  CB  . ALA   A  1 21  ? 30.960  -22.841  -21.854 1.00 27.77 ? 21  ALA   A CB  1 
ATOM   160   N  N   . ILE   A  1 22  ? 32.509  -24.325  -24.213 1.00 26.49 ? 22  ILE   A N   1 
ATOM   161   C  CA  . ILE   A  1 22  ? 32.597  -25.360  -25.242 1.00 23.98 ? 22  ILE   A CA  1 
ATOM   162   C  C   . ILE   A  1 22  ? 33.650  -26.388  -24.867 1.00 26.79 ? 22  ILE   A C   1 
ATOM   163   O  O   . ILE   A  1 22  ? 33.372  -27.589  -24.799 1.00 25.61 ? 22  ILE   A O   1 
ATOM   164   C  CB  . ILE   A  1 22  ? 32.877  -24.735  -26.618 1.00 25.06 ? 22  ILE   A CB  1 
ATOM   165   C  CG1 . ILE   A  1 22  ? 31.629  -24.026  -27.155 1.00 22.13 ? 22  ILE   A CG1 1 
ATOM   166   C  CG2 . ILE   A  1 22  ? 33.324  -25.796  -27.598 1.00 28.03 ? 22  ILE   A CG2 1 
ATOM   167   C  CD1 . ILE   A  1 22  ? 31.994  -22.974  -28.255 1.00 27.12 ? 22  ILE   A CD1 1 
ATOM   168   N  N   . ASN   A  1 23  ? 34.879  -25.927  -24.582 1.00 26.34 ? 23  ASN   A N   1 
ATOM   169   C  CA  . ASN   A  1 23  ? 35.964  -26.867  -24.308 1.00 27.47 ? 23  ASN   A CA  1 
ATOM   170   C  C   . ASN   A  1 23  ? 35.786  -27.573  -22.978 1.00 24.62 ? 23  ASN   A C   1 
ATOM   171   O  O   . ASN   A  1 23  ? 36.056  -28.776  -22.868 1.00 24.71 ? 23  ASN   A O   1 
ATOM   172   C  CB  . ASN   A  1 23  ? 37.319  -26.136  -24.358 1.00 29.26 ? 23  ASN   A CB  1 
ATOM   173   C  CG  . ASN   A  1 23  ? 37.710  -25.751  -25.812 1.00 36.73 ? 23  ASN   A CG  1 
ATOM   174   O  OD1 . ASN   A  1 23  ? 36.859  -25.760  -26.721 1.00 33.01 ? 23  ASN   A OD1 1 
ATOM   175   N  ND2 . ASN   A  1 23  ? 38.980  -25.412  -26.027 1.00 35.09 ? 23  ASN   A ND2 1 
ATOM   176   N  N   . GLN   A  1 24  ? 35.375  -26.846  -21.946 1.00 26.21 ? 24  GLN   A N   1 
ATOM   177   C  CA  . GLN   A  1 24  ? 35.209  -27.474  -20.637 1.00 27.54 ? 24  GLN   A CA  1 
ATOM   178   C  C   . GLN   A  1 24  ? 34.135  -28.561  -20.687 1.00 31.29 ? 24  GLN   A C   1 
ATOM   179   O  O   . GLN   A  1 24  ? 34.321  -29.668  -20.154 1.00 24.88 ? 24  GLN   A O   1 
ATOM   180   C  CB  . GLN   A  1 24  ? 34.843  -26.406  -19.605 1.00 27.67 ? 24  GLN   A CB  1 
ATOM   181   C  CG  . GLN   A  1 24  ? 34.602  -26.904  -18.162 1.00 25.45 ? 24  GLN   A CG  1 
ATOM   182   C  CD  . GLN   A  1 24  ? 34.342  -25.733  -17.221 1.00 31.57 ? 24  GLN   A CD  1 
ATOM   183   O  OE1 . GLN   A  1 24  ? 35.048  -24.738  -17.283 1.00 31.83 ? 24  GLN   A OE1 1 
ATOM   184   N  NE2 . GLN   A  1 24  ? 33.273  -25.818  -16.395 1.00 29.45 ? 24  GLN   A NE2 1 
ATOM   185   N  N   . TYR   A  1 25  ? 32.990  -28.254  -21.305 1.00 28.14 ? 25  TYR   A N   1 
ATOM   186   C  CA  . TYR   A  1 25  ? 31.933  -29.259  -21.384 1.00 26.62 ? 25  TYR   A CA  1 
ATOM   187   C  C   . TYR   A  1 25  ? 32.351  -30.401  -22.296 1.00 23.84 ? 25  TYR   A C   1 
ATOM   188   O  O   . TYR   A  1 25  ? 32.092  -31.572  -21.996 1.00 26.19 ? 25  TYR   A O   1 
ATOM   189   C  CB  . TYR   A  1 25  ? 30.605  -28.638  -21.865 1.00 28.51 ? 25  TYR   A CB  1 
ATOM   190   C  CG  . TYR   A  1 25  ? 30.113  -27.488  -21.008 1.00 29.84 ? 25  TYR   A CG  1 
ATOM   191   C  CD1 . TYR   A  1 25  ? 30.650  -27.273  -19.736 1.00 30.92 ? 25  TYR   A CD1 1 
ATOM   192   C  CD2 . TYR   A  1 25  ? 29.153  -26.587  -21.477 1.00 27.03 ? 25  TYR   A CD2 1 
ATOM   193   C  CE1 . TYR   A  1 25  ? 30.227  -26.200  -18.937 1.00 34.26 ? 25  TYR   A CE1 1 
ATOM   194   C  CE2 . TYR   A  1 25  ? 28.734  -25.510  -20.685 1.00 30.39 ? 25  TYR   A CE2 1 
ATOM   195   C  CZ  . TYR   A  1 25  ? 29.276  -25.318  -19.412 1.00 35.00 ? 25  TYR   A CZ  1 
ATOM   196   O  OH  . TYR   A  1 25  ? 28.894  -24.250  -18.595 1.00 31.08 ? 25  TYR   A OH  1 
ATOM   197   N  N   . PHE   A  1 26  ? 33.007  -30.099  -23.413 1.00 25.39 ? 26  PHE   A N   1 
ATOM   198   C  CA  . PHE   A  1 26  ? 33.427  -31.208  -24.262 1.00 26.85 ? 26  PHE   A CA  1 
ATOM   199   C  C   . PHE   A  1 26  ? 34.405  -32.125  -23.535 1.00 25.72 ? 26  PHE   A C   1 
ATOM   200   O  O   . PHE   A  1 26  ? 34.310  -33.349  -23.644 1.00 24.36 ? 26  PHE   A O   1 
ATOM   201   C  CB  . PHE   A  1 26  ? 34.021  -30.717  -25.575 1.00 27.64 ? 26  PHE   A CB  1 
ATOM   202   C  CG  . PHE   A  1 26  ? 33.920  -31.743  -26.662 1.00 30.49 ? 26  PHE   A CG  1 
ATOM   203   C  CD1 . PHE   A  1 26  ? 34.878  -32.758  -26.785 1.00 25.04 ? 26  PHE   A CD1 1 
ATOM   204   C  CD2 . PHE   A  1 26  ? 32.840  -31.741  -27.525 1.00 25.52 ? 26  PHE   A CD2 1 
ATOM   205   C  CE1 . PHE   A  1 26  ? 34.752  -33.740  -27.770 1.00 29.14 ? 26  PHE   A CE1 1 
ATOM   206   C  CE2 . PHE   A  1 26  ? 32.705  -32.732  -28.529 1.00 27.43 ? 26  PHE   A CE2 1 
ATOM   207   C  CZ  . PHE   A  1 26  ? 33.658  -33.717  -28.649 1.00 33.02 ? 26  PHE   A CZ  1 
ATOM   208   N  N   . LEU   A  1 27  ? 35.350  -31.564  -22.777 1.00 28.18 ? 27  LEU   A N   1 
ATOM   209   C  CA  . LEU   A  1 27  ? 36.274  -32.431  -22.043 1.00 29.27 ? 27  LEU   A CA  1 
ATOM   210   C  C   . LEU   A  1 27  ? 35.537  -33.235  -20.960 1.00 27.03 ? 27  LEU   A C   1 
ATOM   211   O  O   . LEU   A  1 27  ? 35.743  -34.454  -20.814 1.00 24.57 ? 27  LEU   A O   1 
ATOM   212   C  CB  . LEU   A  1 27  ? 37.407  -31.586  -21.443 1.00 27.60 ? 27  LEU   A CB  1 
ATOM   213   C  CG  . LEU   A  1 27  ? 38.474  -32.381  -20.669 1.00 30.31 ? 27  LEU   A CG  1 
ATOM   214   C  CD1 . LEU   A  1 27  ? 38.982  -33.542  -21.485 1.00 30.28 ? 27  LEU   A CD1 1 
ATOM   215   C  CD2 . LEU   A  1 27  ? 39.644  -31.503  -20.262 1.00 37.13 ? 27  LEU   A CD2 1 
ATOM   216   N  N   . HIS   A  1 28  ? 34.648  -32.580  -20.206 1.00 25.77 ? 28  HIS   A N   1 
ATOM   217   C  CA  . HIS   A  1 28  ? 33.899  -33.304  -19.179 1.00 23.38 ? 28  HIS   A CA  1 
ATOM   218   C  C   . HIS   A  1 28  ? 33.085  -34.431  -19.792 1.00 24.75 ? 28  HIS   A C   1 
ATOM   219   O  O   . HIS   A  1 28  ? 33.051  -35.555  -19.267 1.00 27.82 ? 28  HIS   A O   1 
ATOM   220   C  CB  . HIS   A  1 28  ? 32.976  -32.356  -18.426 1.00 22.54 ? 28  HIS   A CB  1 
ATOM   221   C  CG  . HIS   A  1 28  ? 33.669  -31.485  -17.438 1.00 28.36 ? 28  HIS   A CG  1 
ATOM   222   N  ND1 . HIS   A  1 28  ? 33.118  -30.307  -16.981 1.00 30.01 ? 28  HIS   A ND1 1 
ATOM   223   C  CD2 . HIS   A  1 28  ? 34.847  -31.637  -16.780 1.00 30.44 ? 28  HIS   A CD2 1 
ATOM   224   C  CE1 . HIS   A  1 28  ? 33.933  -29.763  -16.093 1.00 33.27 ? 28  HIS   A CE1 1 
ATOM   225   N  NE2 . HIS   A  1 28  ? 34.981  -30.554  -15.944 1.00 31.13 ? 28  HIS   A NE2 1 
ATOM   226   N  N   . SER   A  1 29  ? 32.439  -34.153  -20.920 1.00 25.69 ? 29  SER   A N   1 
ATOM   227   C  CA  . SER   A  1 29  ? 31.687  -35.190  -21.614 1.00 21.85 ? 29  SER   A CA  1 
ATOM   228   C  C   . SER   A  1 29  ? 32.560  -36.401  -21.906 1.00 28.18 ? 29  SER   A C   1 
ATOM   229   O  O   . SER   A  1 29  ? 32.185  -37.550  -21.633 1.00 22.40 ? 29  SER   A O   1 
ATOM   230   C  CB  . SER   A  1 29  ? 31.118  -34.623  -22.923 1.00 26.37 ? 29  SER   A CB  1 
ATOM   231   O  OG  . SER   A  1 29  ? 30.597  -35.662  -23.733 1.00 24.40 ? 29  SER   A OG  1 
ATOM   232   N  N   . ARG   A  1 30  ? 33.726  -36.163  -22.492 1.00 27.25 ? 30  ARG   A N   1 
ATOM   233   C  CA  . ARG   A  1 30  ? 34.561  -37.284  -22.912 1.00 25.66 ? 30  ARG   A CA  1 
ATOM   234   C  C   . ARG   A  1 30  ? 35.219  -37.974  -21.718 1.00 24.88 ? 30  ARG   A C   1 
ATOM   235   O  O   . ARG   A  1 30  ? 35.467  -39.178  -21.769 1.00 25.23 ? 30  ARG   A O   1 
ATOM   236   C  CB  . ARG   A  1 30  ? 35.608  -36.777  -23.920 1.00 26.55 ? 30  ARG   A CB  1 
ATOM   237   C  CG  . ARG   A  1 30  ? 35.158  -36.864  -25.371 1.00 28.08 ? 30  ARG   A CG  1 
ATOM   238   C  CD  . ARG   A  1 30  ? 33.665  -36.473  -25.548 1.00 26.92 ? 30  ARG   A CD  1 
ATOM   239   N  NE  . ARG   A  1 30  ? 33.240  -36.706  -26.920 1.00 26.86 ? 30  ARG   A NE  1 
ATOM   240   C  CZ  . ARG   A  1 30  ? 32.009  -37.062  -27.268 1.00 30.14 ? 30  ARG   A CZ  1 
ATOM   241   N  NH1 . ARG   A  1 30  ? 31.047  -37.204  -26.366 1.00 28.85 ? 30  ARG   A NH1 1 
ATOM   242   N  NH2 . ARG   A  1 30  ? 31.731  -37.267  -28.554 1.00 31.93 ? 30  ARG   A NH2 1 
ATOM   243   N  N   . MET   A  1 31  ? 35.485  -37.238  -20.640 1.00 25.46 ? 31  MET   A N   1 
ATOM   244   C  CA  . MET   A  1 31  ? 35.890  -37.872  -19.384 1.00 29.03 ? 31  MET   A CA  1 
ATOM   245   C  C   . MET   A  1 31  ? 34.804  -38.814  -18.862 1.00 31.77 ? 31  MET   A C   1 
ATOM   246   O  O   . MET   A  1 31  ? 35.054  -40.003  -18.601 1.00 23.88 ? 31  MET   A O   1 
ATOM   247   C  CB  . MET   A  1 31  ? 36.220  -36.793  -18.353 1.00 28.16 ? 31  MET   A CB  1 
ATOM   248   C  CG  . MET   A  1 31  ? 37.564  -36.095  -18.575 1.00 32.78 ? 31  MET   A CG  1 
ATOM   249   S  SD  . MET   A  1 31  ? 37.637  -34.558  -17.631 1.00 29.18 ? 31  MET   A SD  1 
ATOM   250   C  CE  . MET   A  1 31  ? 37.849  -35.262  -16.021 1.00 25.51 ? 31  MET   A CE  1 
ATOM   251   N  N   . TRP   A  1 32  ? 33.576  -38.312  -18.732 1.00 27.00 ? 32  TRP   A N   1 
ATOM   252   C  CA  . TRP   A  1 32  ? 32.488  -39.185  -18.284 1.00 27.68 ? 32  TRP   A CA  1 
ATOM   253   C  C   . TRP   A  1 32  ? 32.342  -40.408  -19.184 1.00 26.20 ? 32  TRP   A C   1 
ATOM   254   O  O   . TRP   A  1 32  ? 32.157  -41.522  -18.681 1.00 28.15 ? 32  TRP   A O   1 
ATOM   255   C  CB  . TRP   A  1 32  ? 31.159  -38.411  -18.204 1.00 25.33 ? 32  TRP   A CB  1 
ATOM   256   C  CG  . TRP   A  1 32  ? 31.015  -37.668  -16.914 1.00 24.86 ? 32  TRP   A CG  1 
ATOM   257   C  CD1 . TRP   A  1 32  ? 31.287  -38.151  -15.654 1.00 27.12 ? 32  TRP   A CD1 1 
ATOM   258   C  CD2 . TRP   A  1 32  ? 30.564  -36.328  -16.733 1.00 23.10 ? 32  TRP   A CD2 1 
ATOM   259   N  NE1 . TRP   A  1 32  ? 31.037  -37.195  -14.715 1.00 26.15 ? 32  TRP   A NE1 1 
ATOM   260   C  CE2 . TRP   A  1 32  ? 30.583  -36.067  -15.338 1.00 22.51 ? 32  TRP   A CE2 1 
ATOM   261   C  CE3 . TRP   A  1 32  ? 30.143  -35.319  -17.602 1.00 24.44 ? 32  TRP   A CE3 1 
ATOM   262   C  CZ2 . TRP   A  1 32  ? 30.188  -34.849  -14.794 1.00 23.91 ? 32  TRP   A CZ2 1 
ATOM   263   C  CZ3 . TRP   A  1 32  ? 29.754  -34.088  -17.057 1.00 25.46 ? 32  TRP   A CZ3 1 
ATOM   264   C  CH2 . TRP   A  1 32  ? 29.767  -33.876  -15.657 1.00 31.92 ? 32  TRP   A CH2 1 
ATOM   265   N  N   . ASN   A  1 33  ? 32.424  -40.236  -20.515 1.00 24.74 ? 33  ASN   A N   1 
ATOM   266   C  CA  . ASN   A  1 33  ? 32.325  -41.403  -21.396 1.00 26.37 ? 33  ASN   A CA  1 
ATOM   267   C  C   . ASN   A  1 33  ? 33.469  -42.374  -21.150 1.00 28.01 ? 33  ASN   A C   1 
ATOM   268   O  O   . ASN   A  1 33  ? 33.264  -43.597  -21.120 1.00 29.11 ? 33  ASN   A O   1 
ATOM   269   C  CB  . ASN   A  1 33  ? 32.319  -40.997  -22.869 1.00 26.74 ? 33  ASN   A CB  1 
ATOM   270   C  CG  . ASN   A  1 33  ? 30.999  -40.411  -23.319 1.00 31.51 ? 33  ASN   A CG  1 
ATOM   271   O  OD1 . ASN   A  1 33  ? 29.953  -40.536  -22.642 1.00 26.10 ? 33  ASN   A OD1 1 
ATOM   272   N  ND2 . ASN   A  1 33  ? 31.040  -39.760  -24.474 1.00 34.10 ? 33  ASN   A ND2 1 
ATOM   273   N  N   . ASP   A  1 34  ? 34.687  -41.848  -20.996 1.00 26.53 ? 34  ASP   A N   1 
ATOM   274   C  CA  . ASP   A  1 34  ? 35.833  -42.716  -20.699 1.00 31.02 ? 34  ASP   A CA  1 
ATOM   275   C  C   . ASP   A  1 34  ? 35.592  -43.507  -19.418 1.00 30.54 ? 34  ASP   A C   1 
ATOM   276   O  O   . ASP   A  1 34  ? 35.902  -44.700  -19.354 1.00 27.15 ? 34  ASP   A O   1 
ATOM   277   C  CB  . ASP   A  1 34  ? 37.111  -41.886  -20.600 1.00 30.50 ? 34  ASP   A CB  1 
ATOM   278   C  CG  . ASP   A  1 34  ? 38.341  -42.722  -20.198 1.00 34.90 ? 34  ASP   A CG  1 
ATOM   279   O  OD1 . ASP   A  1 34  ? 38.641  -43.746  -20.853 1.00 34.19 ? 34  ASP   A OD1 1 
ATOM   280   O  OD2 . ASP   A  1 34  ? 39.005  -42.330  -19.222 1.00 36.82 ? 34  ASP   A OD2 1 
ATOM   281   N  N   . TRP   A  1 35  ? 34.940  -42.896  -18.426 1.00 30.94 ? 35  TRP   A N   1 
ATOM   282   C  CA  . TRP   A  1 35  ? 34.671  -43.589  -17.169 1.00 28.39 ? 35  TRP   A CA  1 
ATOM   283   C  C   . TRP   A  1 35  ? 33.449  -44.499  -17.212 1.00 29.02 ? 35  TRP   A C   1 
ATOM   284   O  O   . TRP   A  1 35  ? 33.124  -45.109  -16.197 1.00 26.93 ? 35  TRP   A O   1 
ATOM   285   C  CB  . TRP   A  1 35  ? 34.479  -42.585  -16.039 1.00 27.67 ? 35  TRP   A CB  1 
ATOM   286   C  CG  . TRP   A  1 35  ? 35.627  -41.675  -15.829 1.00 31.30 ? 35  TRP   A CG  1 
ATOM   287   C  CD1 . TRP   A  1 35  ? 36.895  -41.861  -16.260 1.00 33.63 ? 35  TRP   A CD1 1 
ATOM   288   C  CD2 . TRP   A  1 35  ? 35.625  -40.422  -15.118 1.00 26.67 ? 35  TRP   A CD2 1 
ATOM   289   N  NE1 . TRP   A  1 35  ? 37.686  -40.814  -15.869 1.00 39.91 ? 35  TRP   A NE1 1 
ATOM   290   C  CE2 . TRP   A  1 35  ? 36.932  -39.915  -15.166 1.00 36.07 ? 35  TRP   A CE2 1 
ATOM   291   C  CE3 . TRP   A  1 35  ? 34.648  -39.691  -14.448 1.00 36.00 ? 35  TRP   A CE3 1 
ATOM   292   C  CZ2 . TRP   A  1 35  ? 37.283  -38.701  -14.584 1.00 31.44 ? 35  TRP   A CZ2 1 
ATOM   293   C  CZ3 . TRP   A  1 35  ? 34.993  -38.497  -13.867 1.00 35.75 ? 35  TRP   A CZ3 1 
ATOM   294   C  CH2 . TRP   A  1 35  ? 36.301  -38.008  -13.934 1.00 35.95 ? 35  TRP   A CH2 1 
ATOM   295   N  N   . GLY   A  1 36  ? 32.744  -44.606  -18.329 1.00 27.25 ? 36  GLY   A N   1 
ATOM   296   C  CA  . GLY   A  1 36  ? 31.598  -45.486  -18.374 1.00 27.08 ? 36  GLY   A CA  1 
ATOM   297   C  C   . GLY   A  1 36  ? 30.293  -44.838  -17.963 1.00 25.05 ? 36  GLY   A C   1 
ATOM   298   O  O   . GLY   A  1 36  ? 29.287  -45.541  -17.840 1.00 26.50 ? 36  GLY   A O   1 
ATOM   299   N  N   . LEU   A  1 37  ? 30.278  -43.522  -17.773 1.00 28.06 ? 37  LEU   A N   1 
ATOM   300   C  CA  . LEU   A  1 37  ? 29.069  -42.795  -17.364 1.00 24.80 ? 37  LEU   A CA  1 
ATOM   301   C  C   . LEU   A  1 37  ? 28.460  -42.093  -18.577 1.00 25.45 ? 37  LEU   A C   1 
ATOM   302   O  O   . LEU   A  1 37  ? 28.472  -40.873  -18.712 1.00 26.00 ? 37  LEU   A O   1 
ATOM   303   C  CB  . LEU   A  1 37  ? 29.407  -41.812  -16.257 1.00 23.75 ? 37  LEU   A CB  1 
ATOM   304   C  CG  . LEU   A  1 37  ? 30.021  -42.512  -15.048 1.00 29.04 ? 37  LEU   A CG  1 
ATOM   305   C  CD1 . LEU   A  1 37  ? 30.744  -41.509  -14.140 1.00 32.87 ? 37  LEU   A CD1 1 
ATOM   306   C  CD2 . LEU   A  1 37  ? 28.927  -43.252  -14.307 1.00 27.22 ? 37  LEU   A CD2 1 
ATOM   307   N  N   . LYS   A  1 38  ? 27.904  -42.910  -19.462 1.00 27.48 ? 38  LYS   A N   1 
ATOM   308   C  CA  . LYS   A  1 38  ? 27.589  -42.447  -20.808 1.00 24.94 ? 38  LYS   A CA  1 
ATOM   309   C  C   . LYS   A  1 38  ? 26.357  -41.557  -20.866 1.00 34.43 ? 38  LYS   A C   1 
ATOM   310   O  O   . LYS   A  1 38  ? 26.240  -40.755  -21.802 1.00 26.56 ? 38  LYS   A O   1 
ATOM   311   C  CB  . LYS   A  1 38  ? 27.428  -43.655  -21.727 1.00 33.46 ? 38  LYS   A CB  1 
ATOM   312   C  CG  . LYS   A  1 38  ? 28.595  -44.657  -21.641 1.00 33.73 ? 38  LYS   A CG  1 
ATOM   313   C  CD  . LYS   A  1 38  ? 29.612  -44.484  -22.709 1.00 43.65 ? 38  LYS   A CD  1 
ATOM   314   C  CE  . LYS   A  1 38  ? 30.763  -45.518  -22.558 1.00 49.39 ? 38  LYS   A CE  1 
ATOM   315   N  NZ  . LYS   A  1 38  ? 30.930  -46.335  -23.781 1.00 43.02 ? 38  LYS   A NZ  1 
ATOM   316   N  N   . ARG   A  1 39  ? 25.439  -41.661  -19.896 1.00 31.07 ? 39  ARG   A N   1 
ATOM   317   C  CA  . ARG   A  1 39  ? 24.322  -40.722  -19.854 1.00 28.67 ? 39  ARG   A CA  1 
ATOM   318   C  C   . ARG   A  1 39  ? 24.788  -39.319  -19.488 1.00 26.03 ? 39  ARG   A C   1 
ATOM   319   O  O   . ARG   A  1 39  ? 24.332  -38.329  -20.084 1.00 23.98 ? 39  ARG   A O   1 
ATOM   320   C  CB  . ARG   A  1 39  ? 23.274  -41.206  -18.859 1.00 32.34 ? 39  ARG   A CB  1 
ATOM   321   C  CG  . ARG   A  1 39  ? 21.884  -40.577  -19.051 1.00 37.65 ? 39  ARG   A CG  1 
ATOM   322   C  CD  . ARG   A  1 39  ? 21.000  -40.960  -17.858 1.00 46.15 ? 39  ARG   A CD  1 
ATOM   323   N  NE  . ARG   A  1 39  ? 19.576  -40.807  -18.116 1.00 53.59 ? 39  ARG   A NE  1 
ATOM   324   C  CZ  . ARG   A  1 39  ? 18.789  -41.793  -18.530 1.00 54.73 ? 39  ARG   A CZ  1 
ATOM   325   N  NH1 . ARG   A  1 39  ? 19.262  -43.010  -18.774 1.00 58.73 ? 39  ARG   A NH1 1 
ATOM   326   N  NH2 . ARG   A  1 39  ? 17.500  -41.556  -18.695 1.00 57.31 ? 39  ARG   A NH2 1 
ATOM   327   N  N   . LEU   A  1 40  ? 25.687  -39.205  -18.499 1.00 23.52 ? 40  LEU   A N   1 
ATOM   328   C  CA  . LEU   A  1 40  ? 26.336  -37.920  -18.235 1.00 23.51 ? 40  LEU   A CA  1 
ATOM   329   C  C   . LEU   A  1 40  ? 27.131  -37.448  -19.439 1.00 22.21 ? 40  LEU   A C   1 
ATOM   330   O  O   . LEU   A  1 40  ? 27.090  -36.271  -19.802 1.00 23.78 ? 40  LEU   A O   1 
ATOM   331   C  CB  . LEU   A  1 40  ? 27.261  -38.027  -17.027 1.00 27.81 ? 40  LEU   A CB  1 
ATOM   332   C  CG  . LEU   A  1 40  ? 26.589  -37.773  -15.675 1.00 31.32 ? 40  LEU   A CG  1 
ATOM   333   C  CD1 . LEU   A  1 40  ? 27.540  -38.202  -14.549 1.00 29.15 ? 40  LEU   A CD1 1 
ATOM   334   C  CD2 . LEU   A  1 40  ? 26.208  -36.301  -15.555 1.00 31.01 ? 40  LEU   A CD2 1 
ATOM   335   N  N   . GLY   A  1 41  ? 27.907  -38.345  -20.049 1.00 25.01 ? 41  GLY   A N   1 
ATOM   336   C  CA  . GLY   A  1 41  ? 28.704  -37.923  -21.192 1.00 29.36 ? 41  GLY   A CA  1 
ATOM   337   C  C   . GLY   A  1 41  ? 27.848  -37.409  -22.337 1.00 29.73 ? 41  GLY   A C   1 
ATOM   338   O  O   . GLY   A  1 41  ? 28.173  -36.402  -22.970 1.00 26.13 ? 41  GLY   A O   1 
ATOM   339   N  N   . ALA   A  1 42  ? 26.736  -38.086  -22.609 1.00 26.23 ? 42  ALA   A N   1 
ATOM   340   C  CA  . ALA   A  1 42  ? 25.832  -37.644  -23.670 1.00 29.92 ? 42  ALA   A CA  1 
ATOM   341   C  C   . ALA   A  1 42  ? 25.196  -36.292  -23.338 1.00 26.51 ? 42  ALA   A C   1 
ATOM   342   O  O   . ALA   A  1 42  ? 25.110  -35.405  -24.189 1.00 28.48 ? 42  ALA   A O   1 
ATOM   343   C  CB  . ALA   A  1 42  ? 24.738  -38.694  -23.891 1.00 31.48 ? 42  ALA   A CB  1 
ATOM   344   N  N   . HIS   A  1 43  ? 24.730  -36.120  -22.108 1.00 26.77 ? 43  HIS   A N   1 
ATOM   345   C  CA  . HIS   A  1 43  ? 24.084  -34.866  -21.753 1.00 24.96 ? 43  HIS   A CA  1 
ATOM   346   C  C   . HIS   A  1 43  ? 25.081  -33.711  -21.794 1.00 30.95 ? 43  HIS   A C   1 
ATOM   347   O  O   . HIS   A  1 43  ? 24.761  -32.617  -22.274 1.00 27.50 ? 43  HIS   A O   1 
ATOM   348   C  CB  . HIS   A  1 43  ? 23.440  -34.982  -20.359 1.00 29.58 ? 43  HIS   A CB  1 
ATOM   349   C  CG  . HIS   A  1 43  ? 22.516  -33.859  -20.056 1.00 41.45 ? 43  HIS   A CG  1 
ATOM   350   N  ND1 . HIS   A  1 43  ? 22.961  -32.625  -19.627 1.00 37.19 ? 43  HIS   A ND1 1 
ATOM   351   C  CD2 . HIS   A  1 43  ? 21.170  -33.753  -20.193 1.00 37.21 ? 43  HIS   A CD2 1 
ATOM   352   C  CE1 . HIS   A  1 43  ? 21.926  -31.810  -19.508 1.00 36.95 ? 43  HIS   A CE1 1 
ATOM   353   N  NE2 . HIS   A  1 43  ? 20.833  -32.471  -19.845 1.00 32.93 ? 43  HIS   A NE2 1 
ATOM   354   N  N   . GLU   A  1 44  ? 26.285  -33.920  -21.252 1.00 27.25 ? 44  GLU   A N   1 
ATOM   355   C  CA  . GLU   A  1 44  ? 27.312  -32.888  -21.308 1.00 24.13 ? 44  GLU   A CA  1 
ATOM   356   C  C   . GLU   A  1 44  ? 27.735  -32.605  -22.743 1.00 27.17 ? 44  GLU   A C   1 
ATOM   357   O  O   . GLU   A  1 44  ? 28.039  -31.460  -23.094 1.00 27.01 ? 44  GLU   A O   1 
ATOM   358   C  CB  . GLU   A  1 44  ? 28.520  -33.330  -20.467 1.00 28.75 ? 44  GLU   A CB  1 
ATOM   359   C  CG  . GLU   A  1 44  ? 29.569  -32.260  -20.291 1.00 28.46 ? 44  GLU   A CG  1 
ATOM   360   C  CD  . GLU   A  1 44  ? 29.219  -31.315  -19.172 1.00 36.23 ? 44  GLU   A CD  1 
ATOM   361   O  OE1 . GLU   A  1 44  ? 28.037  -31.305  -18.800 1.00 30.28 ? 44  GLU   A OE1 1 
ATOM   362   O  OE2 . GLU   A  1 44  ? 30.122  -30.615  -18.640 1.00 31.26 ? 44  GLU   A OE2 1 
ATOM   363   N  N   . TYR   A  1 45  ? 27.761  -33.632  -23.589 1.00 23.03 ? 45  TYR   A N   1 
ATOM   364   C  CA  . TYR   A  1 45  ? 28.025  -33.401  -25.002 1.00 24.18 ? 45  TYR   A CA  1 
ATOM   365   C  C   . TYR   A  1 45  ? 27.000  -32.441  -25.595 1.00 28.87 ? 45  TYR   A C   1 
ATOM   366   O  O   . TYR   A  1 45  ? 27.353  -31.505  -26.316 1.00 23.94 ? 45  TYR   A O   1 
ATOM   367   C  CB  . TYR   A  1 45  ? 28.021  -34.731  -25.750 1.00 24.92 ? 45  TYR   A CB  1 
ATOM   368   C  CG  . TYR   A  1 45  ? 27.984  -34.613  -27.276 1.00 29.84 ? 45  TYR   A CG  1 
ATOM   369   C  CD1 . TYR   A  1 45  ? 29.143  -34.359  -27.996 1.00 28.16 ? 45  TYR   A CD1 1 
ATOM   370   C  CD2 . TYR   A  1 45  ? 26.789  -34.777  -27.990 1.00 27.41 ? 45  TYR   A CD2 1 
ATOM   371   C  CE1 . TYR   A  1 45  ? 29.139  -34.270  -29.366 1.00 31.99 ? 45  TYR   A CE1 1 
ATOM   372   C  CE2 . TYR   A  1 45  ? 26.759  -34.680  -29.380 1.00 34.42 ? 45  TYR   A CE2 1 
ATOM   373   C  CZ  . TYR   A  1 45  ? 27.941  -34.422  -30.072 1.00 40.02 ? 45  TYR   A CZ  1 
ATOM   374   O  OH  . TYR   A  1 45  ? 27.960  -34.318  -31.455 1.00 40.07 ? 45  TYR   A OH  1 
ATOM   375   N  N   . HIS   A  1 46  ? 25.725  -32.642  -25.277 1.00 25.45 ? 46  HIS   A N   1 
ATOM   376   C  CA  . HIS   A  1 46  ? 24.697  -31.771  -25.829 1.00 31.69 ? 46  HIS   A CA  1 
ATOM   377   C  C   . HIS   A  1 46  ? 24.798  -30.357  -25.261 1.00 27.54 ? 46  HIS   A C   1 
ATOM   378   O  O   . HIS   A  1 46  ? 24.549  -29.390  -25.990 1.00 28.40 ? 46  HIS   A O   1 
ATOM   379   C  CB  . HIS   A  1 46  ? 23.319  -32.427  -25.609 1.00 31.42 ? 46  HIS   A CB  1 
ATOM   380   C  CG  . HIS   A  1 46  ? 23.094  -33.579  -26.537 1.00 39.55 ? 46  HIS   A CG  1 
ATOM   381   N  ND1 . HIS   A  1 46  ? 23.025  -33.420  -27.910 1.00 42.26 ? 46  HIS   A ND1 1 
ATOM   382   C  CD2 . HIS   A  1 46  ? 22.991  -34.911  -26.306 1.00 36.35 ? 46  HIS   A CD2 1 
ATOM   383   C  CE1 . HIS   A  1 46  ? 22.867  -34.603  -28.479 1.00 38.64 ? 46  HIS   A CE1 1 
ATOM   384   N  NE2 . HIS   A  1 46  ? 22.847  -35.523  -27.529 1.00 41.33 ? 46  HIS   A NE2 1 
ATOM   385   N  N   . GLU   A  1 47  ? 25.219  -30.207  -24.001 1.00 28.30 ? 47  GLU   A N   1 
ATOM   386   C  CA  . GLU   A  1 47  ? 25.507  -28.869  -23.481 1.00 26.13 ? 47  GLU   A CA  1 
ATOM   387   C  C   . GLU   A  1 47  ? 26.645  -28.209  -24.257 1.00 26.62 ? 47  GLU   A C   1 
ATOM   388   O  O   . GLU   A  1 47  ? 26.595  -27.014  -24.564 1.00 27.80 ? 47  GLU   A O   1 
ATOM   389   C  CB  . GLU   A  1 47  ? 25.873  -28.925  -21.990 1.00 27.64 ? 47  GLU   A CB  1 
ATOM   390   C  CG  . GLU   A  1 47  ? 24.822  -29.545  -21.044 1.00 41.22 ? 47  GLU   A CG  1 
ATOM   391   C  CD  . GLU   A  1 47  ? 23.620  -28.637  -20.818 1.00 37.62 ? 47  GLU   A CD  1 
ATOM   392   O  OE1 . GLU   A  1 47  ? 23.434  -27.714  -21.629 1.00 46.19 ? 47  GLU   A OE1 1 
ATOM   393   O  OE2 . GLU   A  1 47  ? 22.870  -28.833  -19.829 1.00 42.10 ? 47  GLU   A OE2 1 
ATOM   394   N  N   . SER   A  1 48  ? 27.672  -28.971  -24.591 1.00 25.26 ? 48  SER   A N   1 
ATOM   395   C  CA  . SER   A  1 48  ? 28.768  -28.395  -25.367 1.00 29.60 ? 48  SER   A CA  1 
ATOM   396   C  C   . SER   A  1 48  ? 28.272  -27.930  -26.735 1.00 31.10 ? 48  SER   A C   1 
ATOM   397   O  O   . SER   A  1 48  ? 28.584  -26.819  -27.178 1.00 24.99 ? 48  SER   A O   1 
ATOM   398   C  CB  . SER   A  1 48  ? 29.895  -29.415  -25.515 1.00 27.30 ? 48  SER   A CB  1 
ATOM   399   O  OG  . SER   A  1 48  ? 30.985  -28.846  -26.254 1.00 30.59 ? 48  SER   A OG  1 
ATOM   400   N  N   . ILE   A  1 49  ? 27.460  -28.753  -27.394 1.00 27.21 ? 49  ILE   A N   1 
ATOM   401   C  CA  . ILE   A  1 49  ? 26.887  -28.363  -28.684 1.00 27.47 ? 49  ILE   A CA  1 
ATOM   402   C  C   . ILE   A  1 49  ? 26.054  -27.092  -28.543 1.00 27.80 ? 49  ILE   A C   1 
ATOM   403   O  O   . ILE   A  1 49  ? 26.104  -26.213  -29.413 1.00 27.07 ? 49  ILE   A O   1 
ATOM   404   C  CB  . ILE   A  1 49  ? 26.049  -29.510  -29.280 1.00 31.55 ? 49  ILE   A CB  1 
ATOM   405   C  CG1 . ILE   A  1 49  ? 26.914  -30.743  -29.570 1.00 30.36 ? 49  ILE   A CG1 1 
ATOM   406   C  CG2 . ILE   A  1 49  ? 25.338  -29.028  -30.525 1.00 32.95 ? 49  ILE   A CG2 1 
ATOM   407   C  CD1 . ILE   A  1 49  ? 27.862  -30.585  -30.708 1.00 36.47 ? 49  ILE   A CD1 1 
ATOM   408   N  N   . ASP   A  1 50  ? 25.251  -26.984  -27.466 1.00 27.70 ? 50  ASP   A N   1 
ATOM   409   C  CA  . ASP   A  1 50  ? 24.449  -25.772  -27.248 1.00 27.99 ? 50  ASP   A CA  1 
ATOM   410   C  C   . ASP   A  1 50  ? 25.333  -24.533  -27.249 1.00 28.23 ? 50  ASP   A C   1 
ATOM   411   O  O   . ASP   A  1 50  ? 24.986  -23.492  -27.831 1.00 26.71 ? 50  ASP   A O   1 
ATOM   412   C  CB  . ASP   A  1 50  ? 23.698  -25.822  -25.908 1.00 34.20 ? 50  ASP   A CB  1 
ATOM   413   C  CG  . ASP   A  1 50  ? 22.461  -26.705  -25.924 1.00 49.93 ? 50  ASP   A CG  1 
ATOM   414   O  OD1 . ASP   A  1 50  ? 22.072  -27.208  -26.998 1.00 45.46 ? 50  ASP   A OD1 1 
ATOM   415   O  OD2 . ASP   A  1 50  ? 21.879  -26.888  -24.818 1.00 58.34 ? 50  ASP   A OD2 1 
ATOM   416   N  N   . GLU   A  1 51  ? 26.458  -24.610  -26.525 1.00 26.50 ? 51  GLU   A N   1 
ATOM   417   C  CA  . GLU   A  1 51  ? 27.366  -23.470  -26.462 1.00 33.79 ? 51  GLU   A CA  1 
ATOM   418   C  C   . GLU   A  1 51  ? 27.985  -23.197  -27.828 1.00 28.03 ? 51  GLU   A C   1 
ATOM   419   O  O   . GLU   A  1 51  ? 28.198  -22.039  -28.192 1.00 26.73 ? 51  GLU   A O   1 
ATOM   420   C  CB  . GLU   A  1 51  ? 28.454  -23.725  -25.407 1.00 26.23 ? 51  GLU   A CB  1 
ATOM   421   C  CG  . GLU   A  1 51  ? 27.927  -23.994  -23.982 1.00 32.89 ? 51  GLU   A CG  1 
ATOM   422   C  CD  . GLU   A  1 51  ? 27.260  -22.754  -23.360 1.00 38.97 ? 51  GLU   A CD  1 
ATOM   423   O  OE1 . GLU   A  1 51  ? 26.120  -22.444  -23.706 1.00 39.16 ? 51  GLU   A OE1 1 
ATOM   424   O  OE2 . GLU   A  1 51  ? 27.880  -22.072  -22.521 1.00 54.17 ? 51  GLU   A OE2 1 
ATOM   425   N  N   . MET   A  1 52  ? 28.292  -24.252  -28.592 1.00 26.12 ? 52  MET   A N   1 
ATOM   426   C  CA  . MET   A  1 52  ? 28.751  -24.062  -29.964 1.00 28.60 ? 52  MET   A CA  1 
ATOM   427   C  C   . MET   A  1 52  ? 27.742  -23.261  -30.781 1.00 29.51 ? 52  MET   A C   1 
ATOM   428   O  O   . MET   A  1 52  ? 28.117  -22.341  -31.530 1.00 26.18 ? 52  MET   A O   1 
ATOM   429   C  CB  . MET   A  1 52  ? 29.002  -25.418  -30.625 1.00 27.78 ? 52  MET   A CB  1 
ATOM   430   C  CG  . MET   A  1 52  ? 30.139  -26.191  -29.999 1.00 29.36 ? 52  MET   A CG  1 
ATOM   431   S  SD  . MET   A  1 52  ? 30.351  -27.800  -30.733 1.00 27.17 ? 52  MET   A SD  1 
ATOM   432   C  CE  . MET   A  1 52  ? 31.170  -28.690  -29.440 1.00 25.41 ? 52  MET   A CE  1 
ATOM   433   N  N   . LYS   A  1 53  ? 26.452  -23.606  -30.672 1.00 27.79 ? 53  LYS   A N   1 
ATOM   434   C  CA  . LYS   A  1 53  ? 25.445  -22.867  -31.426 1.00 30.64 ? 53  LYS   A CA  1 
ATOM   435   C  C   . LYS   A  1 53  ? 25.328  -21.428  -30.940 1.00 24.94 ? 53  LYS   A C   1 
ATOM   436   O  O   . LYS   A  1 53  ? 25.159  -20.526  -31.764 1.00 25.66 ? 53  LYS   A O   1 
ATOM   437   C  CB  . LYS   A  1 53  ? 24.084  -23.571  -31.352 1.00 27.34 ? 53  LYS   A CB  1 
ATOM   438   C  CG  . LYS   A  1 53  ? 24.080  -24.976  -31.992 1.00 32.86 ? 53  LYS   A CG  1 
ATOM   439   C  CD  . LYS   A  1 53  ? 22.698  -25.627  -31.848 1.00 41.65 ? 53  LYS   A CD  1 
ATOM   440   C  CE  . LYS   A  1 53  ? 22.544  -26.887  -32.694 1.00 60.05 ? 53  LYS   A CE  1 
ATOM   441   N  NZ  . LYS   A  1 53  ? 21.205  -27.550  -32.509 1.00 69.98 ? 53  LYS   A NZ  1 
ATOM   442   N  N   . HIS   A  1 54  ? 25.397  -21.191  -29.614 1.00 26.21 ? 54  HIS   A N   1 
ATOM   443   C  CA  . HIS   A  1 54  ? 25.428  -19.813  -29.102 1.00 27.67 ? 54  HIS   A CA  1 
ATOM   444   C  C   . HIS   A  1 54  ? 26.638  -19.038  -29.642 1.00 25.91 ? 54  HIS   A C   1 
ATOM   445   O  O   . HIS   A  1 54  ? 26.510  -17.874  -30.041 1.00 25.65 ? 54  HIS   A O   1 
ATOM   446   C  CB  . HIS   A  1 54  ? 25.477  -19.781  -27.565 1.00 27.71 ? 54  HIS   A CB  1 
ATOM   447   C  CG  . HIS   A  1 54  ? 24.328  -20.442  -26.876 1.00 33.25 ? 54  HIS   A CG  1 
ATOM   448   N  ND1 . HIS   A  1 54  ? 23.076  -20.559  -27.438 1.00 34.59 ? 54  HIS   A ND1 1 
ATOM   449   C  CD2 . HIS   A  1 54  ? 24.249  -21.026  -25.657 1.00 31.35 ? 54  HIS   A CD2 1 
ATOM   450   C  CE1 . HIS   A  1 54  ? 22.282  -21.208  -26.604 1.00 31.27 ? 54  HIS   A CE1 1 
ATOM   451   N  NE2 . HIS   A  1 54  ? 22.969  -21.500  -25.520 1.00 31.20 ? 54  HIS   A NE2 1 
ATOM   452   N  N   . ALA   A  1 55  ? 27.829  -19.648  -29.591 1.00 26.68 ? 55  ALA   A N   1 
ATOM   453   C  CA  . ALA   A  1 55  ? 29.021  -18.994  -30.130 1.00 27.44 ? 55  ALA   A CA  1 
ATOM   454   C  C   . ALA   A  1 55  ? 28.821  -18.619  -31.591 1.00 28.10 ? 55  ALA   A C   1 
ATOM   455   O  O   . ALA   A  1 55  ? 29.191  -17.513  -32.001 1.00 28.50 ? 55  ALA   A O   1 
ATOM   456   C  CB  . ALA   A  1 55  ? 30.244  -19.889  -29.981 1.00 29.81 ? 55  ALA   A CB  1 
ATOM   457   N  N   . ASP   A  1 56  ? 28.232  -19.530  -32.388 1.00 27.94 ? 56  ASP   A N   1 
ATOM   458   C  CA  . ASP   A  1 56  ? 27.967  -19.242  -33.798 1.00 23.34 ? 56  ASP   A CA  1 
ATOM   459   C  C   . ASP   A  1 56  ? 27.108  -17.990  -33.943 1.00 22.67 ? 56  ASP   A C   1 
ATOM   460   O  O   . ASP   A  1 56  ? 27.425  -17.087  -34.722 1.00 27.00 ? 56  ASP   A O   1 
ATOM   461   C  CB  . ASP   A  1 56  ? 27.320  -20.463  -34.456 1.00 29.68 ? 56  ASP   A CB  1 
ATOM   462   C  CG  . ASP   A  1 56  ? 27.112  -20.305  -35.948 1.00 31.71 ? 56  ASP   A CG  1 
ATOM   463   O  OD1 . ASP   A  1 56  ? 27.703  -19.403  -36.587 1.00 33.79 ? 56  ASP   A OD1 1 
ATOM   464   O  OD2 . ASP   A  1 56  ? 26.363  -21.132  -36.481 1.00 30.06 ? 56  ASP   A OD2 1 
ATOM   465   N  N   . LYS   A  1 57  ? 26.030  -17.894  -33.170 1.00 25.22 ? 57  LYS   A N   1 
ATOM   466   C  CA  . LYS   A  1 57  ? 25.152  -16.736  -33.311 1.00 26.13 ? 57  LYS   A CA  1 
ATOM   467   C  C   . LYS   A  1 57  ? 25.862  -15.447  -32.910 1.00 27.81 ? 57  LYS   A C   1 
ATOM   468   O  O   . LYS   A  1 57  ? 25.612  -14.378  -33.491 1.00 28.89 ? 57  LYS   A O   1 
ATOM   469   C  CB  . LYS   A  1 57  ? 23.896  -16.925  -32.450 1.00 26.10 ? 57  LYS   A CB  1 
ATOM   470   C  CG  . LYS   A  1 57  ? 22.966  -18.045  -32.923 1.00 37.08 ? 57  LYS   A CG  1 
ATOM   471   C  CD  . LYS   A  1 57  ? 22.468  -17.819  -34.336 1.00 36.09 ? 57  LYS   A CD  1 
ATOM   472   N  N   . LEU   A  1 58  ? 26.704  -15.519  -31.876 1.00 27.02 ? 58  LEU   A N   1 
ATOM   473   C  CA  . LEU   A  1 58  ? 27.461  -14.343  -31.449 1.00 29.49 ? 58  LEU   A CA  1 
ATOM   474   C  C   . LEU   A  1 58  ? 28.466  -13.904  -32.505 1.00 28.04 ? 58  LEU   A C   1 
ATOM   475   O  O   . LEU   A  1 58  ? 28.587  -12.711  -32.796 1.00 28.73 ? 58  LEU   A O   1 
ATOM   476   C  CB  . LEU   A  1 58  ? 28.181  -14.647  -30.142 1.00 30.33 ? 58  LEU   A CB  1 
ATOM   477   C  CG  . LEU   A  1 58  ? 27.319  -14.767  -28.863 1.00 36.89 ? 58  LEU   A CG  1 
ATOM   478   C  CD1 . LEU   A  1 58  ? 28.170  -15.432  -27.783 1.00 30.89 ? 58  LEU   A CD1 1 
ATOM   479   C  CD2 . LEU   A  1 58  ? 26.760  -13.432  -28.379 1.00 30.56 ? 58  LEU   A CD2 1 
ATOM   480   N  N   . ILE   A  1 59  ? 29.190  -14.862  -33.078 1.00 26.27 ? 59  ILE   A N   1 
ATOM   481   C  CA  . ILE   A  1 59  ? 30.132  -14.586  -34.166 1.00 30.23 ? 59  ILE   A CA  1 
ATOM   482   C  C   . ILE   A  1 59  ? 29.421  -13.910  -35.324 1.00 33.57 ? 59  ILE   A C   1 
ATOM   483   O  O   . ILE   A  1 59  ? 29.906  -12.908  -35.874 1.00 31.26 ? 59  ILE   A O   1 
ATOM   484   C  CB  . ILE   A  1 59  ? 30.825  -15.900  -34.601 1.00 27.48 ? 59  ILE   A CB  1 
ATOM   485   C  CG1 . ILE   A  1 59  ? 31.768  -16.408  -33.514 1.00 32.03 ? 59  ILE   A CG1 1 
ATOM   486   C  CG2 . ILE   A  1 59  ? 31.561  -15.733  -35.953 1.00 28.57 ? 59  ILE   A CG2 1 
ATOM   487   C  CD1 . ILE   A  1 59  ? 32.245  -17.811  -33.759 1.00 25.35 ? 59  ILE   A CD1 1 
ATOM   488   N  N   . GLU   A  1 60  ? 28.235  -14.419  -35.685 1.00 29.24 ? 60  GLU   A N   1 
ATOM   489   C  CA  . GLU   A  1 60  ? 27.459  -13.840  -36.777 1.00 28.30 ? 60  GLU   A CA  1 
ATOM   490   C  C   . GLU   A  1 60  ? 26.972  -12.425  -36.460 1.00 23.41 ? 60  GLU   A C   1 
ATOM   491   O  O   . GLU   A  1 60  ? 27.027  -11.537  -37.323 1.00 28.85 ? 60  GLU   A O   1 
ATOM   492   C  CB  . GLU   A  1 60  ? 26.270  -14.767  -37.101 1.00 30.29 ? 60  GLU   A CB  1 
ATOM   493   C  CG  . GLU   A  1 60  ? 26.702  -16.083  -37.767 1.00 24.48 ? 60  GLU   A CG  1 
ATOM   494   C  CD  . GLU   A  1 60  ? 25.571  -17.117  -37.899 1.00 37.00 ? 60  GLU   A CD  1 
ATOM   495   O  OE1 . GLU   A  1 60  ? 24.644  -17.132  -37.056 1.00 33.79 ? 60  GLU   A OE1 1 
ATOM   496   O  OE2 . GLU   A  1 60  ? 25.625  -17.920  -38.849 1.00 31.30 ? 60  GLU   A OE2 1 
ATOM   497   N  N   . ARG   A  1 61  ? 26.468  -12.197  -35.252 1.00 24.27 ? 61  ARG   A N   1 
ATOM   498   C  CA  . ARG   A  1 61  ? 26.040  -10.853  -34.867 1.00 29.63 ? 61  ARG   A CA  1 
ATOM   499   C  C   . ARG   A  1 61  ? 27.222  -9.873   -34.859 1.00 23.95 ? 61  ARG   A C   1 
ATOM   500   O  O   . ARG   A  1 61  ? 27.073  -8.729   -35.300 1.00 28.42 ? 61  ARG   A O   1 
ATOM   501   C  CB  . ARG   A  1 61  ? 25.367  -10.881  -33.490 1.00 26.32 ? 61  ARG   A CB  1 
ATOM   502   C  CG  . ARG   A  1 61  ? 24.811  -9.538   -33.000 1.00 27.12 ? 61  ARG   A CG  1 
ATOM   503   C  CD  . ARG   A  1 61  ? 23.532  -9.216   -33.719 1.00 26.56 ? 61  ARG   A CD  1 
ATOM   504   N  NE  . ARG   A  1 61  ? 23.004  -7.919   -33.323 1.00 28.02 ? 61  ARG   A NE  1 
ATOM   505   C  CZ  . ARG   A  1 61  ? 22.162  -7.186   -34.039 1.00 31.16 ? 61  ARG   A CZ  1 
ATOM   506   N  NH1 . ARG   A  1 61  ? 21.681  -7.607   -35.210 1.00 29.41 ? 61  ARG   A NH1 1 
ATOM   507   N  NH2 . ARG   A  1 61  ? 21.804  -5.989   -33.583 1.00 29.62 ? 61  ARG   A NH2 1 
ATOM   508   N  N   . ILE   A  1 62  ? 28.384  -10.301  -34.351 1.00 28.53 ? 62  ILE   A N   1 
ATOM   509   C  CA  . ILE   A  1 62  ? 29.553  -9.408   -34.294 1.00 29.97 ? 62  ILE   A CA  1 
ATOM   510   C  C   . ILE   A  1 62  ? 29.982  -9.003   -35.701 1.00 34.81 ? 62  ILE   A C   1 
ATOM   511   O  O   . ILE   A  1 62  ? 30.225  -7.822   -35.974 1.00 30.83 ? 62  ILE   A O   1 
ATOM   512   C  CB  . ILE   A  1 62  ? 30.700  -10.065  -33.508 1.00 28.44 ? 62  ILE   A CB  1 
ATOM   513   C  CG1 . ILE   A  1 62  ? 30.339  -10.164  -32.020 1.00 23.15 ? 62  ILE   A CG1 1 
ATOM   514   C  CG2 . ILE   A  1 62  ? 32.053  -9.257   -33.673 1.00 31.43 ? 62  ILE   A CG2 1 
ATOM   515   C  CD1 . ILE   A  1 62  ? 31.238  -11.085  -31.236 1.00 30.39 ? 62  ILE   A CD1 1 
ATOM   516   N  N   . LEU   A  1 63  ? 30.036  -9.964   -36.630 1.00 32.15 ? 63  LEU   A N   1 
ATOM   517   C  CA  . LEU   A  1 63  ? 30.391  -9.636   -38.009 1.00 30.19 ? 63  LEU   A CA  1 
ATOM   518   C  C   . LEU   A  1 63  ? 29.380  -8.691   -38.636 1.00 31.88 ? 63  LEU   A C   1 
ATOM   519   O  O   . LEU   A  1 63  ? 29.753  -7.755   -39.371 1.00 26.88 ? 63  LEU   A O   1 
ATOM   520   C  CB  . LEU   A  1 63  ? 30.520  -10.919  -38.841 1.00 26.36 ? 63  LEU   A CB  1 
ATOM   521   C  CG  . LEU   A  1 63  ? 31.731  -11.777  -38.460 1.00 30.63 ? 63  LEU   A CG  1 
ATOM   522   C  CD1 . LEU   A  1 63  ? 31.594  -13.175  -39.073 1.00 30.90 ? 63  LEU   A CD1 1 
ATOM   523   C  CD2 . LEU   A  1 63  ? 33.055  -11.064  -38.920 1.00 30.40 ? 63  LEU   A CD2 1 
ATOM   524   N  N   . PHE   A  1 64  ? 28.087  -8.917   -38.379 1.00 29.12 ? 64  PHE   A N   1 
ATOM   525   C  CA  . PHE   A  1 64  ? 27.081  -8.021   -38.924 1.00 27.80 ? 64  PHE   A CA  1 
ATOM   526   C  C   . PHE   A  1 64  ? 27.294  -6.605   -38.423 1.00 29.21 ? 64  PHE   A C   1 
ATOM   527   O  O   . PHE   A  1 64  ? 27.132  -5.643   -39.180 1.00 29.71 ? 64  PHE   A O   1 
ATOM   528   C  CB  . PHE   A  1 64  ? 25.673  -8.518   -38.569 1.00 29.56 ? 64  PHE   A CB  1 
ATOM   529   C  CG  . PHE   A  1 64  ? 24.604  -7.530   -38.862 1.00 30.23 ? 64  PHE   A CG  1 
ATOM   530   C  CD1 . PHE   A  1 64  ? 24.373  -7.101   -40.150 1.00 28.94 ? 64  PHE   A CD1 1 
ATOM   531   C  CD2 . PHE   A  1 64  ? 23.839  -7.014   -37.851 1.00 33.80 ? 64  PHE   A CD2 1 
ATOM   532   C  CE1 . PHE   A  1 64  ? 23.411  -6.188   -40.412 1.00 28.43 ? 64  PHE   A CE1 1 
ATOM   533   C  CE2 . PHE   A  1 64  ? 22.874  -6.115   -38.114 1.00 30.61 ? 64  PHE   A CE2 1 
ATOM   534   C  CZ  . PHE   A  1 64  ? 22.655  -5.692   -39.385 1.00 31.06 ? 64  PHE   A CZ  1 
ATOM   535   N  N   . LEU   A  1 65  ? 27.663  -6.458   -37.154 1.00 30.83 ? 65  LEU   A N   1 
ATOM   536   C  CA  . LEU   A  1 65  ? 27.925  -5.150   -36.565 1.00 28.04 ? 65  LEU   A CA  1 
ATOM   537   C  C   . LEU   A  1 65  ? 29.291  -4.591   -36.952 1.00 31.15 ? 65  LEU   A C   1 
ATOM   538   O  O   . LEU   A  1 65  ? 29.673  -3.543   -36.433 1.00 36.51 ? 65  LEU   A O   1 
ATOM   539   C  CB  . LEU   A  1 65  ? 27.821  -5.239   -35.038 1.00 30.57 ? 65  LEU   A CB  1 
ATOM   540   C  CG  . LEU   A  1 65  ? 26.444  -5.713   -34.543 1.00 29.58 ? 65  LEU   A CG  1 
ATOM   541   C  CD1 . LEU   A  1 65  ? 26.393  -5.826   -33.044 1.00 29.29 ? 65  LEU   A CD1 1 
ATOM   542   C  CD2 . LEU   A  1 65  ? 25.327  -4.787   -35.038 1.00 33.48 ? 65  LEU   A CD2 1 
ATOM   543   N  N   . GLU   A  1 66  ? 30.034  -5.284   -37.820 1.00 31.89 ? 66  GLU   A N   1 
ATOM   544   C  CA  . GLU   A  1 66  ? 31.310  -4.822   -38.372 1.00 37.11 ? 66  GLU   A CA  1 
ATOM   545   C  C   . GLU   A  1 66  ? 32.407  -4.797   -37.309 1.00 43.99 ? 66  GLU   A C   1 
ATOM   546   O  O   . GLU   A  1 66  ? 33.302  -3.949   -37.330 1.00 37.99 ? 66  GLU   A O   1 
ATOM   547   C  CB  . GLU   A  1 66  ? 31.148  -3.458   -39.056 1.00 33.53 ? 66  GLU   A CB  1 
ATOM   548   C  CG  . GLU   A  1 66  ? 29.999  -3.475   -40.029 1.00 39.09 ? 66  GLU   A CG  1 
ATOM   549   C  CD  . GLU   A  1 66  ? 29.966  -2.304   -41.000 1.00 43.40 ? 66  GLU   A CD  1 
ATOM   550   O  OE1 . GLU   A  1 66  ? 31.028  -1.730   -41.312 1.00 49.89 ? 66  GLU   A OE1 1 
ATOM   551   O  OE2 . GLU   A  1 66  ? 28.864  -1.971   -41.455 1.00 39.34 ? 66  GLU   A OE2 1 
ATOM   552   N  N   . GLY   A  1 67  ? 32.325  -5.735   -36.367 1.00 29.82 ? 67  GLY   A N   1 
ATOM   553   C  CA  . GLY   A  1 67  ? 33.385  -5.987   -35.429 1.00 32.88 ? 67  GLY   A CA  1 
ATOM   554   C  C   . GLY   A  1 67  ? 34.150  -7.250   -35.764 1.00 34.29 ? 67  GLY   A C   1 
ATOM   555   O  O   . GLY   A  1 67  ? 33.820  -7.995   -36.676 1.00 33.81 ? 67  GLY   A O   1 
ATOM   556   N  N   . LEU   A  1 68  ? 35.170  -7.503   -34.956 1.00 32.16 ? 68  LEU   A N   1 
ATOM   557   C  CA  . LEU   A  1 68  ? 36.039  -8.660   -35.126 1.00 36.44 ? 68  LEU   A CA  1 
ATOM   558   C  C   . LEU   A  1 68  ? 35.778  -9.682   -34.030 1.00 35.40 ? 68  LEU   A C   1 
ATOM   559   O  O   . LEU   A  1 68  ? 36.163  -9.445   -32.877 1.00 35.88 ? 68  LEU   A O   1 
ATOM   560   C  CB  . LEU   A  1 68  ? 37.508  -8.226   -35.111 1.00 39.30 ? 68  LEU   A CB  1 
ATOM   561   C  CG  . LEU   A  1 68  ? 37.889  -7.327   -36.285 1.00 61.01 ? 68  LEU   A CG  1 
ATOM   562   C  CD1 . LEU   A  1 68  ? 39.336  -6.889   -36.169 1.00 71.13 ? 68  LEU   A CD1 1 
ATOM   563   C  CD2 . LEU   A  1 68  ? 37.637  -8.026   -37.625 1.00 65.82 ? 68  LEU   A CD2 1 
ATOM   564   N  N   . PRO   A  1 69  ? 35.163  -10.830  -34.329 1.00 36.43 ? 69  PRO   A N   1 
ATOM   565   C  CA  . PRO   A  1 69  ? 34.987  -11.868  -33.303 1.00 32.70 ? 69  PRO   A CA  1 
ATOM   566   C  C   . PRO   A  1 69  ? 36.320  -12.363  -32.768 1.00 35.05 ? 69  PRO   A C   1 
ATOM   567   O  O   . PRO   A  1 69  ? 37.203  -12.741  -33.531 1.00 32.22 ? 69  PRO   A O   1 
ATOM   568   C  CB  . PRO   A  1 69  ? 34.250  -12.988  -34.055 1.00 33.55 ? 69  PRO   A CB  1 
ATOM   569   C  CG  . PRO   A  1 69  ? 33.696  -12.351  -35.291 1.00 32.72 ? 69  PRO   A CG  1 
ATOM   570   C  CD  . PRO   A  1 69  ? 34.639  -11.260  -35.642 1.00 35.49 ? 69  PRO   A CD  1 
ATOM   571   N  N   . ASN   A  1 70  ? 36.442  -12.432  -31.437 1.00 33.77 ? 70  ASN   A N   1 
ATOM   572   C  CA  . ASN   A  1 70  ? 37.672  -12.913  -30.811 1.00 32.90 ? 70  ASN   A CA  1 
ATOM   573   C  C   . ASN   A  1 70  ? 37.572  -14.414  -30.550 1.00 28.82 ? 70  ASN   A C   1 
ATOM   574   O  O   . ASN   A  1 70  ? 37.015  -14.842  -29.545 1.00 29.19 ? 70  ASN   A O   1 
ATOM   575   C  CB  . ASN   A  1 70  ? 37.944  -12.142  -29.518 1.00 35.32 ? 70  ASN   A CB  1 
ATOM   576   C  CG  . ASN   A  1 70  ? 39.294  -12.460  -28.916 1.00 32.87 ? 70  ASN   A CG  1 
ATOM   577   O  OD1 . ASN   A  1 70  ? 39.920  -13.448  -29.259 1.00 38.99 ? 70  ASN   A OD1 1 
ATOM   578   N  ND2 . ASN   A  1 70  ? 39.733  -11.634  -27.980 1.00 40.39 ? 70  ASN   A ND2 1 
ATOM   579   N  N   . LEU   A  1 71  ? 38.167  -15.220  -31.421 1.00 29.06 ? 71  LEU   A N   1 
ATOM   580   C  CA  . LEU   A  1 71  ? 38.318  -16.653  -31.181 1.00 31.86 ? 71  LEU   A CA  1 
ATOM   581   C  C   . LEU   A  1 71  ? 39.732  -17.022  -30.773 1.00 32.68 ? 71  LEU   A C   1 
ATOM   582   O  O   . LEU   A  1 71  ? 40.086  -18.206  -30.773 1.00 30.01 ? 71  LEU   A O   1 
ATOM   583   C  CB  . LEU   A  1 71  ? 37.931  -17.450  -32.429 1.00 32.90 ? 71  LEU   A CB  1 
ATOM   584   C  CG  . LEU   A  1 71  ? 36.421  -17.615  -32.674 1.00 35.68 ? 71  LEU   A CG  1 
ATOM   585   C  CD1 . LEU   A  1 71  ? 35.839  -16.386  -33.264 1.00 35.63 ? 71  LEU   A CD1 1 
ATOM   586   C  CD2 . LEU   A  1 71  ? 36.121  -18.832  -33.561 1.00 34.41 ? 71  LEU   A CD2 1 
ATOM   587   N  N   . GLN   A  1 72  ? 40.552  -16.036  -30.447 1.00 32.66 ? 72  GLN   A N   1 
ATOM   588   C  CA  . GLN   A  1 72  ? 41.963  -16.260  -30.141 1.00 34.27 ? 72  GLN   A CA  1 
ATOM   589   C  C   . GLN   A  1 72  ? 42.246  -16.397  -28.646 1.00 31.15 ? 72  GLN   A C   1 
ATOM   590   O  O   . GLN   A  1 72  ? 43.055  -17.245  -28.264 1.00 27.98 ? 72  GLN   A O   1 
ATOM   591   C  CB  . GLN   A  1 72  ? 42.789  -15.109  -30.715 1.00 29.30 ? 72  GLN   A CB  1 
ATOM   592   C  CG  . GLN   A  1 72  ? 44.320  -15.248  -30.523 1.00 27.88 ? 72  GLN   A CG  1 
ATOM   593   C  CD  . GLN   A  1 72  ? 44.903  -16.453  -31.226 1.00 35.36 ? 72  GLN   A CD  1 
ATOM   594   O  OE1 . GLN   A  1 72  ? 45.306  -16.387  -32.399 1.00 43.41 ? 72  GLN   A OE1 1 
ATOM   595   N  NE2 . GLN   A  1 72  ? 44.971  -17.555  -30.515 1.00 34.43 ? 72  GLN   A NE2 1 
ATOM   596   N  N   . ASP   A  1 73  ? 41.595  -15.584  -27.802 1.00 33.81 ? 73  ASP   A N   1 
ATOM   597   C  CA  . ASP   A  1 73  ? 41.828  -15.566  -26.355 1.00 32.11 ? 73  ASP   A CA  1 
ATOM   598   C  C   . ASP   A  1 73  ? 40.910  -16.579  -25.673 1.00 37.63 ? 73  ASP   A C   1 
ATOM   599   O  O   . ASP   A  1 73  ? 39.679  -16.438  -25.698 1.00 43.37 ? 73  ASP   A O   1 
ATOM   600   C  CB  . ASP   A  1 73  ? 41.577  -14.164  -25.798 1.00 33.27 ? 73  ASP   A CB  1 
ATOM   601   C  CG  . ASP   A  1 73  ? 42.462  -13.111  -26.442 1.00 36.94 ? 73  ASP   A CG  1 
ATOM   602   O  OD1 . ASP   A  1 73  ? 43.592  -13.451  -26.839 1.00 39.87 ? 73  ASP   A OD1 1 
ATOM   603   O  OD2 . ASP   A  1 73  ? 42.015  -11.959  -26.583 1.00 39.48 ? 73  ASP   A OD2 1 
ATOM   604   N  N   . LEU   A  1 74  ? 41.504  -17.608  -25.091 1.00 30.75 ? 74  LEU   A N   1 
ATOM   605   C  CA  . LEU   A  1 74  ? 40.784  -18.622  -24.336 1.00 35.47 ? 74  LEU   A CA  1 
ATOM   606   C  C   . LEU   A  1 74  ? 41.101  -18.447  -22.857 1.00 34.78 ? 74  LEU   A C   1 
ATOM   607   O  O   . LEU   A  1 74  ? 42.259  -18.584  -22.459 1.00 34.75 ? 74  LEU   A O   1 
ATOM   608   C  CB  . LEU   A  1 74  ? 41.183  -20.017  -24.796 1.00 32.81 ? 74  LEU   A CB  1 
ATOM   609   C  CG  . LEU   A  1 74  ? 40.426  -21.215  -24.220 1.00 37.75 ? 74  LEU   A CG  1 
ATOM   610   C  CD1 . LEU   A  1 74  ? 38.934  -21.121  -24.481 1.00 35.19 ? 74  LEU   A CD1 1 
ATOM   611   C  CD2 . LEU   A  1 74  ? 41.013  -22.480  -24.835 1.00 34.59 ? 74  LEU   A CD2 1 
ATOM   612   N  N   . GLY   A  1 75  ? 40.073  -18.172  -22.059 1.00 31.42 ? 75  GLY   A N   1 
ATOM   613   C  CA  . GLY   A  1 75  ? 40.201  -18.082  -20.622 1.00 34.50 ? 75  GLY   A CA  1 
ATOM   614   C  C   . GLY   A  1 75  ? 40.405  -19.444  -19.984 1.00 31.58 ? 75  GLY   A C   1 
ATOM   615   O  O   . GLY   A  1 75  ? 40.554  -20.472  -20.645 1.00 32.63 ? 75  GLY   A O   1 
ATOM   616   N  N   . LYS   A  1 76  ? 40.435  -19.434  -18.653 1.00 33.25 ? 76  LYS   A N   1 
ATOM   617   C  CA  . LYS   A  1 76  ? 40.774  -20.619  -17.878 1.00 33.12 ? 76  LYS   A CA  1 
ATOM   618   C  C   . LYS   A  1 76  ? 39.614  -21.619  -17.861 1.00 30.70 ? 76  LYS   A C   1 
ATOM   619   O  O   . LYS   A  1 76  ? 38.492  -21.280  -17.470 1.00 30.36 ? 76  LYS   A O   1 
ATOM   620   C  CB  . LYS   A  1 76  ? 41.130  -20.208  -16.456 1.00 34.53 ? 76  LYS   A CB  1 
ATOM   621   C  CG  . LYS   A  1 76  ? 41.667  -21.355  -15.601 1.00 43.31 ? 76  LYS   A CG  1 
ATOM   622   N  N   . LEU   A  1 77  ? 39.886  -22.849  -18.279 1.00 30.91 ? 77  LEU   A N   1 
ATOM   623   C  CA  . LEU   A  1 77  ? 38.928  -23.936  -18.126 1.00 35.12 ? 77  LEU   A CA  1 
ATOM   624   C  C   . LEU   A  1 77  ? 38.913  -24.400  -16.675 1.00 36.08 ? 77  LEU   A C   1 
ATOM   625   O  O   . LEU   A  1 77  ? 39.958  -24.473  -16.027 1.00 34.86 ? 77  LEU   A O   1 
ATOM   626   C  CB  . LEU   A  1 77  ? 39.308  -25.114  -19.007 1.00 28.17 ? 77  LEU   A CB  1 
ATOM   627   C  CG  . LEU   A  1 77  ? 38.961  -25.183  -20.476 1.00 37.40 ? 77  LEU   A CG  1 
ATOM   628   C  CD1 . LEU   A  1 77  ? 39.039  -23.850  -21.161 1.00 38.55 ? 77  LEU   A CD1 1 
ATOM   629   C  CD2 . LEU   A  1 77  ? 39.908  -26.164  -21.081 1.00 30.57 ? 77  LEU   A CD2 1 
ATOM   630   N  N   . LEU   A  1 78  ? 37.734  -24.743  -16.184 1.00 31.72 ? 78  LEU   A N   1 
ATOM   631   C  CA  . LEU   A  1 78  ? 37.563  -25.308  -14.845 1.00 35.99 ? 78  LEU   A CA  1 
ATOM   632   C  C   . LEU   A  1 78  ? 37.263  -26.789  -15.012 1.00 29.02 ? 78  LEU   A C   1 
ATOM   633   O  O   . LEU   A  1 78  ? 36.120  -27.168  -15.276 1.00 30.67 ? 78  LEU   A O   1 
ATOM   634   C  CB  . LEU   A  1 78  ? 36.434  -24.611  -14.088 1.00 33.11 ? 78  LEU   A CB  1 
ATOM   635   C  CG  . LEU   A  1 78  ? 36.514  -23.088  -14.101 1.00 43.37 ? 78  LEU   A CG  1 
ATOM   636   C  CD1 . LEU   A  1 78  ? 35.364  -22.471  -13.304 1.00 38.96 ? 78  LEU   A CD1 1 
ATOM   637   C  CD2 . LEU   A  1 78  ? 37.866  -22.653  -13.575 1.00 38.76 ? 78  LEU   A CD2 1 
ATOM   638   N  N   . ILE   A  1 79  ? 38.279  -27.619  -14.850 1.00 34.40 ? 79  ILE   A N   1 
ATOM   639   C  CA  . ILE   A  1 79  ? 38.157  -29.055  -15.037 1.00 34.36 ? 79  ILE   A CA  1 
ATOM   640   C  C   . ILE   A  1 79  ? 38.160  -29.747  -13.688 1.00 44.30 ? 79  ILE   A C   1 
ATOM   641   O  O   . ILE   A  1 79  ? 39.080  -29.558  -12.878 1.00 39.22 ? 79  ILE   A O   1 
ATOM   642   C  CB  . ILE   A  1 79  ? 39.290  -29.592  -15.912 1.00 34.36 ? 79  ILE   A CB  1 
ATOM   643   C  CG1 . ILE   A  1 79  ? 39.420  -28.746  -17.192 1.00 31.19 ? 79  ILE   A CG1 1 
ATOM   644   C  CG2 . ILE   A  1 79  ? 39.008  -31.019  -16.246 1.00 34.29 ? 79  ILE   A CG2 1 
ATOM   645   C  CD1 . ILE   A  1 79  ? 38.153  -28.733  -18.066 1.00 34.28 ? 79  ILE   A CD1 1 
ATOM   646   N  N   . GLY   A  1 80  ? 37.177  -30.575  -13.456 1.00 35.01 ? 80  GLY   A N   1 
ATOM   647   C  CA  . GLY   A  1 80  ? 37.121  -31.255  -12.178 1.00 30.60 ? 80  GLY   A CA  1 
ATOM   648   C  C   . GLY   A  1 80  ? 37.766  -32.598  -12.219 1.00 31.40 ? 80  GLY   A C   1 
ATOM   649   O  O   . GLY   A  1 80  ? 38.052  -33.133  -13.279 1.00 34.49 ? 80  GLY   A O   1 
ATOM   650   N  N   . GLU   A  1 81  ? 37.986  -33.158  -11.032 1.00 30.84 ? 81  GLU   A N   1 
ATOM   651   C  CA  . GLU   A  1 81  ? 38.624  -34.456  -10.913 1.00 40.48 ? 81  GLU   A CA  1 
ATOM   652   C  C   . GLU   A  1 81  ? 37.627  -35.565  -10.628 1.00 40.43 ? 81  GLU   A C   1 
ATOM   653   O  O   . GLU   A  1 81  ? 37.996  -36.744  -10.701 1.00 35.94 ? 81  GLU   A O   1 
ATOM   654   C  CB  . GLU   A  1 81  ? 39.710  -34.423  -9.815  1.00 37.20 ? 81  GLU   A CB  1 
ATOM   655   N  N   . ASN   A  1 82  ? 36.373  -35.225  -10.335 1.00 34.41 ? 82  ASN   A N   1 
ATOM   656   C  CA  . ASN   A  1 82  ? 35.350  -36.227  -10.125 1.00 28.51 ? 82  ASN   A CA  1 
ATOM   657   C  C   . ASN   A  1 82  ? 34.002  -35.618  -10.516 1.00 29.36 ? 82  ASN   A C   1 
ATOM   658   O  O   . ASN   A  1 82  ? 33.882  -34.419  -10.809 1.00 28.13 ? 82  ASN   A O   1 
ATOM   659   C  CB  . ASN   A  1 82  ? 35.368  -36.720  -8.670  1.00 27.95 ? 82  ASN   A CB  1 
ATOM   660   C  CG  . ASN   A  1 82  ? 35.168  -35.587  -7.681  1.00 33.13 ? 82  ASN   A CG  1 
ATOM   661   O  OD1 . ASN   A  1 82  ? 34.166  -34.892  -7.717  1.00 32.66 ? 82  ASN   A OD1 1 
ATOM   662   N  ND2 . ASN   A  1 82  ? 36.150  -35.368  -6.828  1.00 61.00 ? 82  ASN   A ND2 1 
ATOM   663   N  N   . THR   A  1 83  ? 32.980  -36.461  -10.530 1.00 28.60 ? 83  THR   A N   1 
ATOM   664   C  CA  . THR   A  1 83  ? 31.701  -36.023  -11.090 1.00 26.00 ? 83  THR   A CA  1 
ATOM   665   C  C   . THR   A  1 83  ? 31.174  -34.785  -10.373 1.00 28.05 ? 83  THR   A C   1 
ATOM   666   O  O   . THR   A  1 83  ? 30.786  -33.797  -11.006 1.00 28.26 ? 83  THR   A O   1 
ATOM   667   C  CB  . THR   A  1 83  ? 30.693  -37.159  -11.020 1.00 27.51 ? 83  THR   A CB  1 
ATOM   668   O  OG1 . THR   A  1 83  ? 31.058  -38.148  -11.987 1.00 30.14 ? 83  THR   A OG1 1 
ATOM   669   C  CG2 . THR   A  1 83  ? 29.255  -36.624  -11.328 1.00 26.68 ? 83  THR   A CG2 1 
ATOM   670   N  N   . GLN   A  1 84  ? 31.150  -34.815  -9.049  1.00 29.10 ? 84  GLN   A N   1 
ATOM   671   C  CA  . GLN   A  1 84  ? 30.638  -33.671  -8.303  1.00 30.61 ? 84  GLN   A CA  1 
ATOM   672   C  C   . GLN   A  1 84  ? 31.416  -32.392  -8.611  1.00 27.14 ? 84  GLN   A C   1 
ATOM   673   O  O   . GLN   A  1 84  ? 30.826  -31.317  -8.787  1.00 27.59 ? 84  GLN   A O   1 
ATOM   674   C  CB  . GLN   A  1 84  ? 30.699  -33.996  -6.810  1.00 36.62 ? 84  GLN   A CB  1 
ATOM   675   C  CG  . GLN   A  1 84  ? 29.927  -33.052  -5.933  1.00 40.87 ? 84  GLN   A CG  1 
ATOM   676   C  CD  . GLN   A  1 84  ? 29.631  -33.663  -4.551  1.00 57.81 ? 84  GLN   A CD  1 
ATOM   677   O  OE1 . GLN   A  1 84  ? 28.737  -33.204  -3.847  1.00 54.39 ? 84  GLN   A OE1 1 
ATOM   678   N  NE2 . GLN   A  1 84  ? 30.373  -34.712  -4.177  1.00 52.18 ? 84  GLN   A NE2 1 
ATOM   679   N  N   . GLU   A  1 85  ? 32.751  -32.466  -8.608  1.00 28.33 ? 85  GLU   A N   1 
ATOM   680   C  CA  . GLU   A  1 85  ? 33.557  -31.276  -8.912  1.00 30.59 ? 85  GLU   A CA  1 
ATOM   681   C  C   . GLU   A  1 85  ? 33.340  -30.805  -10.339 1.00 24.49 ? 85  GLU   A C   1 
ATOM   682   O  O   . GLU   A  1 85  ? 33.346  -29.600  -10.610 1.00 30.10 ? 85  GLU   A O   1 
ATOM   683   C  CB  . GLU   A  1 85  ? 35.053  -31.561  -8.666  1.00 37.39 ? 85  GLU   A CB  1 
ATOM   684   C  CG  . GLU   A  1 85  ? 35.926  -30.283  -8.563  1.00 46.58 ? 85  GLU   A CG  1 
ATOM   685   C  CD  . GLU   A  1 85  ? 37.432  -30.566  -8.568  1.00 56.30 ? 85  GLU   A CD  1 
ATOM   686   O  OE1 . GLU   A  1 85  ? 37.812  -31.754  -8.440  1.00 43.50 ? 85  GLU   A OE1 1 
ATOM   687   O  OE2 . GLU   A  1 85  ? 38.221  -29.593  -8.712  1.00 54.98 ? 85  GLU   A OE2 1 
ATOM   688   N  N   . MET   A  1 86  ? 33.171  -31.735  -11.270 1.00 27.07 ? 86  MET   A N   1 
ATOM   689   C  CA  . MET   A  1 86  ? 32.954  -31.337  -12.666 1.00 28.12 ? 86  MET   A CA  1 
ATOM   690   C  C   . MET   A  1 86  ? 31.656  -30.556  -12.804 1.00 32.34 ? 86  MET   A C   1 
ATOM   691   O  O   . MET   A  1 86  ? 31.604  -29.509  -13.476 1.00 28.07 ? 86  MET   A O   1 
ATOM   692   C  CB  . MET   A  1 86  ? 32.932  -32.579  -13.553 1.00 26.26 ? 86  MET   A CB  1 
ATOM   693   C  CG  . MET   A  1 86  ? 34.266  -33.281  -13.702 1.00 21.89 ? 86  MET   A CG  1 
ATOM   694   S  SD  . MET   A  1 86  ? 34.076  -35.035  -13.953 1.00 28.55 ? 86  MET   A SD  1 
ATOM   695   C  CE  . MET   A  1 86  ? 33.715  -35.063  -15.714 1.00 28.81 ? 86  MET   A CE  1 
ATOM   696   N  N   . LEU   A  1 87  ? 30.600  -31.036  -12.140 1.00 30.65 ? 87  LEU   A N   1 
ATOM   697   C  CA  . LEU   A  1 87  ? 29.327  -30.320  -12.159 1.00 29.46 ? 87  LEU   A CA  1 
ATOM   698   C  C   . LEU   A  1 87  ? 29.460  -28.957  -11.496 1.00 25.28 ? 87  LEU   A C   1 
ATOM   699   O  O   . LEU   A  1 87  ? 28.909  -27.969  -11.991 1.00 27.32 ? 87  LEU   A O   1 
ATOM   700   C  CB  . LEU   A  1 87  ? 28.243  -31.152  -11.465 1.00 29.24 ? 87  LEU   A CB  1 
ATOM   701   C  CG  . LEU   A  1 87  ? 27.847  -32.471  -12.150 1.00 28.75 ? 87  LEU   A CG  1 
ATOM   702   C  CD1 . LEU   A  1 87  ? 27.137  -33.411  -11.179 1.00 31.27 ? 87  LEU   A CD1 1 
ATOM   703   C  CD2 . LEU   A  1 87  ? 26.990  -32.224  -13.363 1.00 28.40 ? 87  LEU   A CD2 1 
ATOM   704   N  N   . GLN   A  1 88  ? 30.169  -28.880  -10.359 1.00 24.65 ? 88  GLN   A N   1 
ATOM   705   C  CA  . GLN   A  1 88  ? 30.328  -27.579  -9.711  1.00 30.22 ? 88  GLN   A CA  1 
ATOM   706   C  C   . GLN   A  1 88  ? 31.158  -26.631  -10.575 1.00 26.72 ? 88  GLN   A C   1 
ATOM   707   O  O   . GLN   A  1 88  ? 30.875  -25.425  -10.635 1.00 26.40 ? 88  GLN   A O   1 
ATOM   708   C  CB  . GLN   A  1 88  ? 30.955  -27.743  -8.318  1.00 26.98 ? 88  GLN   A CB  1 
ATOM   709   C  CG  . GLN   A  1 88  ? 31.086  -26.434  -7.558  1.00 43.80 ? 88  GLN   A CG  1 
ATOM   710   C  CD  . GLN   A  1 88  ? 29.743  -25.816  -7.181  1.00 45.91 ? 88  GLN   A CD  1 
ATOM   711   O  OE1 . GLN   A  1 88  ? 28.926  -26.457  -6.534  1.00 41.30 ? 88  GLN   A OE1 1 
ATOM   712   N  NE2 . GLN   A  1 88  ? 29.525  -24.562  -7.568  1.00 40.18 ? 88  GLN   A NE2 1 
ATOM   713   N  N   . CYS   A  1 89  ? 32.176  -27.155  -11.260 1.00 30.27 ? 89  CYS   A N   1 
ATOM   714   C  CA  . CYS   A  1 89  ? 32.936  -26.315  -12.177 1.00 30.16 ? 89  CYS   A CA  1 
ATOM   715   C  C   . CYS   A  1 89  ? 32.051  -25.781  -13.299 1.00 30.29 ? 89  CYS   A C   1 
ATOM   716   O  O   . CYS   A  1 89  ? 32.137  -24.600  -13.664 1.00 25.56 ? 89  CYS   A O   1 
ATOM   717   C  CB  . CYS   A  1 89  ? 34.118  -27.103  -12.744 1.00 38.74 ? 89  CYS   A CB  1 
ATOM   718   S  SG  . CYS   A  1 89  ? 35.516  -27.319  -11.620 1.00 34.73 ? 89  CYS   A SG  1 
ATOM   719   N  N   . ASP   A  1 90  ? 31.173  -26.622  -13.845 1.00 28.25 ? 90  ASP   A N   1 
ATOM   720   C  CA  . ASP   A  1 90  ? 30.236  -26.119  -14.843 1.00 24.92 ? 90  ASP   A CA  1 
ATOM   721   C  C   . ASP   A  1 90  ? 29.342  -25.033  -14.248 1.00 27.27 ? 90  ASP   A C   1 
ATOM   722   O  O   . ASP   A  1 90  ? 29.121  -23.983  -14.869 1.00 27.84 ? 90  ASP   A O   1 
ATOM   723   C  CB  . ASP   A  1 90  ? 29.375  -27.257  -15.397 1.00 27.46 ? 90  ASP   A CB  1 
ATOM   724   C  CG  . ASP   A  1 90  ? 30.145  -28.245  -16.248 1.00 30.24 ? 90  ASP   A CG  1 
ATOM   725   O  OD1 . ASP   A  1 90  ? 31.358  -28.065  -16.521 1.00 30.05 ? 90  ASP   A OD1 1 
ATOM   726   O  OD2 . ASP   A  1 90  ? 29.491  -29.219  -16.696 1.00 33.45 ? 90  ASP   A OD2 1 
ATOM   727   N  N   . LEU   A  1 91  ? 28.839  -25.250  -13.030 1.00 30.67 ? 91  LEU   A N   1 
ATOM   728   C  CA  . LEU   A  1 91  ? 27.935  -24.259  -12.426 1.00 30.51 ? 91  LEU   A CA  1 
ATOM   729   C  C   . LEU   A  1 91  ? 28.654  -22.924  -12.187 1.00 30.22 ? 91  LEU   A C   1 
ATOM   730   O  O   . LEU   A  1 91  ? 28.129  -21.844  -12.497 1.00 26.58 ? 91  LEU   A O   1 
ATOM   731   C  CB  . LEU   A  1 91  ? 27.357  -24.812  -11.117 1.00 27.60 ? 91  LEU   A CB  1 
ATOM   732   C  CG  . LEU   A  1 91  ? 26.383  -23.938  -10.310 1.00 28.22 ? 91  LEU   A CG  1 
ATOM   733   C  CD1 . LEU   A  1 91  ? 25.178  -23.473  -11.172 1.00 31.16 ? 91  LEU   A CD1 1 
ATOM   734   C  CD2 . LEU   A  1 91  ? 25.883  -24.712  -9.081  1.00 32.82 ? 91  LEU   A CD2 1 
ATOM   735   N  N   . ASN   A  1 92  ? 29.870  -22.974  -11.653 1.00 30.69 ? 92  ASN   A N   1 
ATOM   736   C  CA  . ASN   A  1 92  ? 30.607  -21.728  -11.436 1.00 29.01 ? 92  ASN   A CA  1 
ATOM   737   C  C   . ASN   A  1 92  ? 30.793  -20.964  -12.741 1.00 29.54 ? 92  ASN   A C   1 
ATOM   738   O  O   . ASN   A  1 92  ? 30.589  -19.743  -12.799 1.00 25.08 ? 92  ASN   A O   1 
ATOM   739   C  CB  . ASN   A  1 92  ? 31.967  -22.031  -10.787 1.00 34.21 ? 92  ASN   A CB  1 
ATOM   740   C  CG  . ASN   A  1 92  ? 31.829  -22.465  -9.347  1.00 46.14 ? 92  ASN   A CG  1 
ATOM   741   O  OD1 . ASN   A  1 92  ? 30.822  -22.177  -8.687  1.00 48.09 ? 92  ASN   A OD1 1 
ATOM   742   N  ND2 . ASN   A  1 92  ? 32.836  -23.169  -8.850  1.00 49.70 ? 92  ASN   A ND2 1 
ATOM   743   N  N   . LEU   A  1 93  ? 31.166  -21.668  -13.810 1.00 30.79 ? 93  LEU   A N   1 
ATOM   744   C  CA  . LEU   A  1 93  ? 31.262  -21.019  -15.116 1.00 28.51 ? 93  LEU   A CA  1 
ATOM   745   C  C   . LEU   A  1 93  ? 29.926  -20.409  -15.536 1.00 30.94 ? 93  LEU   A C   1 
ATOM   746   O  O   . LEU   A  1 93  ? 29.875  -19.268  -16.020 1.00 31.09 ? 93  LEU   A O   1 
ATOM   747   C  CB  . LEU   A  1 93  ? 31.753  -22.033  -16.150 1.00 29.07 ? 93  LEU   A CB  1 
ATOM   748   C  CG  . LEU   A  1 93  ? 31.949  -21.504  -17.566 1.00 30.66 ? 93  LEU   A CG  1 
ATOM   749   C  CD1 . LEU   A  1 93  ? 33.021  -20.399  -17.574 1.00 40.98 ? 93  LEU   A CD1 1 
ATOM   750   C  CD2 . LEU   A  1 93  ? 32.343  -22.625  -18.522 1.00 34.22 ? 93  LEU   A CD2 1 
ATOM   751   N  N   . GLU   A  1 94  ? 28.829  -21.169  -15.390 1.00 32.52 ? 94  GLU   A N   1 
ATOM   752   C  CA  . GLU   A  1 94  ? 27.515  -20.657  -15.789 1.00 32.62 ? 94  GLU   A CA  1 
ATOM   753   C  C   . GLU   A  1 94  ? 27.156  -19.404  -15.011 1.00 29.68 ? 94  GLU   A C   1 
ATOM   754   O  O   . GLU   A  1 94  ? 26.598  -18.451  -15.568 1.00 29.88 ? 94  GLU   A O   1 
ATOM   755   C  CB  . GLU   A  1 94  ? 26.438  -21.720  -15.575 1.00 30.02 ? 94  GLU   A CB  1 
ATOM   756   C  CG  . GLU   A  1 94  ? 26.559  -22.886  -16.512 1.00 31.01 ? 94  GLU   A CG  1 
ATOM   757   C  CD  . GLU   A  1 94  ? 26.055  -22.568  -17.892 1.00 36.06 ? 94  GLU   A CD  1 
ATOM   758   O  OE1 . GLU   A  1 94  ? 25.579  -21.445  -18.119 1.00 31.55 ? 94  GLU   A OE1 1 
ATOM   759   O  OE2 . GLU   A  1 94  ? 26.124  -23.454  -18.752 1.00 39.35 ? 94  GLU   A OE2 1 
ATOM   760   N  N   . LEU   A  1 95  ? 27.487  -19.376  -13.726 1.00 29.08 ? 95  LEU   A N   1 
ATOM   761   C  CA  . LEU   A  1 95  ? 27.115  -18.220  -12.918 1.00 30.43 ? 95  LEU   A CA  1 
ATOM   762   C  C   . LEU   A  1 95  ? 27.914  -16.990  -13.328 1.00 29.18 ? 95  LEU   A C   1 
ATOM   763   O  O   . LEU   A  1 95  ? 27.377  -15.880  -13.330 1.00 33.87 ? 95  LEU   A O   1 
ATOM   764   C  CB  . LEU   A  1 95  ? 27.281  -18.556  -11.445 1.00 33.67 ? 95  LEU   A CB  1 
ATOM   765   C  CG  . LEU   A  1 95  ? 26.257  -19.590  -10.925 1.00 35.25 ? 95  LEU   A CG  1 
ATOM   766   C  CD1 . LEU   A  1 95  ? 26.614  -20.081  -9.558  1.00 42.27 ? 95  LEU   A CD1 1 
ATOM   767   C  CD2 . LEU   A  1 95  ? 24.862  -19.002  -10.880 1.00 33.66 ? 95  LEU   A CD2 1 
ATOM   768   N  N   . LYS   A  1 96  ? 29.181  -17.161  -13.714 1.00 32.37 ? 96  LYS   A N   1 
ATOM   769   C  CA  . LYS   A  1 96  ? 29.918  -16.042  -14.297 1.00 30.51 ? 96  LYS   A CA  1 
ATOM   770   C  C   . LYS   A  1 96  ? 29.317  -15.624  -15.629 1.00 30.52 ? 96  LYS   A C   1 
ATOM   771   O  O   . LYS   A  1 96  ? 29.165  -14.423  -15.904 1.00 34.36 ? 96  LYS   A O   1 
ATOM   772   C  CB  . LYS   A  1 96  ? 31.408  -16.398  -14.456 1.00 37.51 ? 96  LYS   A CB  1 
ATOM   773   C  CG  . LYS   A  1 96  ? 32.180  -15.471  -15.433 1.00 38.41 ? 96  LYS   A CG  1 
ATOM   774   C  CD  . LYS   A  1 96  ? 33.692  -15.733  -15.453 1.00 45.94 ? 96  LYS   A CD  1 
ATOM   775   C  CE  . LYS   A  1 96  ? 34.385  -15.089  -16.676 1.00 48.18 ? 96  LYS   A CE  1 
ATOM   776   N  NZ  . LYS   A  1 96  ? 33.929  -13.676  -16.907 1.00 54.19 ? 96  LYS   A NZ  1 
ATOM   777   N  N   . ALA   A  1 97  ? 28.939  -16.594  -16.466 1.00 33.83 ? 97  ALA   A N   1 
ATOM   778   C  CA  . ALA   A  1 97  ? 28.382  -16.259  -17.778 1.00 32.50 ? 97  ALA   A CA  1 
ATOM   779   C  C   . ALA   A  1 97  ? 27.074  -15.470  -17.667 1.00 24.76 ? 97  ALA   A C   1 
ATOM   780   O  O   . ALA   A  1 97  ? 26.868  -14.480  -18.392 1.00 27.31 ? 97  ALA   A O   1 
ATOM   781   C  CB  . ALA   A  1 97  ? 28.188  -17.548  -18.599 1.00 31.73 ? 97  ALA   A CB  1 
ATOM   782   N  N   . THR   A  1 98  ? 26.184  -15.860  -16.746 1.00 30.79 ? 98  THR   A N   1 
ATOM   783   C  CA  . THR   A  1 98  ? 24.914  -15.146  -16.635 1.00 26.61 ? 98  THR   A CA  1 
ATOM   784   C  C   . THR   A  1 98  ? 25.100  -13.739  -16.068 1.00 28.73 ? 98  THR   A C   1 
ATOM   785   O  O   . THR   A  1 98  ? 24.422  -12.793  -16.503 1.00 27.17 ? 98  THR   A O   1 
ATOM   786   C  CB  . THR   A  1 98  ? 23.913  -15.961  -15.794 1.00 27.33 ? 98  THR   A CB  1 
ATOM   787   O  OG1 . THR   A  1 98  ? 24.472  -16.272  -14.509 1.00 33.59 ? 98  THR   A OG1 1 
ATOM   788   C  CG2 . THR   A  1 98  ? 23.568  -17.266  -16.555 1.00 26.62 ? 98  THR   A CG2 1 
ATOM   789   N  N   . LYS   A  1 99  ? 26.012  -13.567  -15.107 1.00 32.85 ? 99  LYS   A N   1 
ATOM   790   C  CA  . LYS   A  1 99  ? 26.397  -12.217  -14.701 1.00 35.28 ? 99  LYS   A CA  1 
ATOM   791   C  C   . LYS   A  1 99  ? 26.870  -11.392  -15.899 1.00 27.15 ? 99  LYS   A C   1 
ATOM   792   O  O   . LYS   A  1 99  ? 26.426  -10.257  -16.099 1.00 32.68 ? 99  LYS   A O   1 
ATOM   793   C  CB  . LYS   A  1 99  ? 27.500  -12.268  -13.637 1.00 39.62 ? 99  LYS   A CB  1 
ATOM   794   C  CG  . LYS   A  1 99  ? 27.886  -10.884  -13.083 1.00 41.83 ? 99  LYS   A CG  1 
ATOM   795   C  CD  . LYS   A  1 99  ? 29.096  -10.969  -12.145 1.00 49.98 ? 99  LYS   A CD  1 
ATOM   796   N  N   . ASP   A  1 100 ? 27.757  -11.949  -16.720 1.00 32.17 ? 100 ASP   A N   1 
ATOM   797   C  CA  . ASP   A  1 100 ? 28.224  -11.195  -17.883 1.00 31.95 ? 100 ASP   A CA  1 
ATOM   798   C  C   . ASP   A  1 100 ? 27.093  -10.916  -18.864 1.00 35.37 ? 100 ASP   A C   1 
ATOM   799   O  O   . ASP   A  1 100 ? 27.033  -9.827   -19.459 1.00 28.79 ? 100 ASP   A O   1 
ATOM   800   C  CB  . ASP   A  1 100 ? 29.365  -11.940  -18.550 1.00 33.61 ? 100 ASP   A CB  1 
ATOM   801   C  CG  . ASP   A  1 100 ? 30.633  -11.889  -17.723 1.00 38.10 ? 100 ASP   A CG  1 
ATOM   802   O  OD1 . ASP   A  1 100 ? 30.723  -11.010  -16.855 1.00 42.06 ? 100 ASP   A OD1 1 
ATOM   803   O  OD2 . ASP   A  1 100 ? 31.519  -12.723  -17.932 1.00 36.90 ? 100 ASP   A OD2 1 
ATOM   804   N  N   . LEU   A  1 101 ? 26.156  -11.868  -19.027 1.00 35.53 ? 101 LEU   A N   1 
ATOM   805   C  CA  . LEU   A  1 101 ? 25.046  -11.624  -19.946 1.00 31.72 ? 101 LEU   A CA  1 
ATOM   806   C  C   . LEU   A  1 101 ? 24.159  -10.485  -19.446 1.00 25.75 ? 101 LEU   A C   1 
ATOM   807   O  O   . LEU   A  1 101 ? 23.702  -9.636   -20.234 1.00 25.04 ? 101 LEU   A O   1 
ATOM   808   C  CB  . LEU   A  1 101 ? 24.240  -12.916  -20.150 1.00 33.36 ? 101 LEU   A CB  1 
ATOM   809   C  CG  . LEU   A  1 101 ? 24.874  -13.971  -21.074 1.00 32.28 ? 101 LEU   A CG  1 
ATOM   810   C  CD1 . LEU   A  1 101 ? 24.421  -15.377  -20.700 1.00 32.08 ? 101 LEU   A CD1 1 
ATOM   811   C  CD2 . LEU   A  1 101 ? 24.512  -13.676  -22.550 1.00 30.63 ? 101 LEU   A CD2 1 
ATOM   812   N  N   . ARG   A  1 102 ? 23.947  -10.415  -18.135 1.00 26.66 ? 102 ARG   A N   1 
ATOM   813   C  CA  . ARG   A  1 102 ? 23.117  -9.350   -17.577 1.00 24.89 ? 102 ARG   A CA  1 
ATOM   814   C  C   . ARG   A  1 102 ? 23.734  -7.970   -17.814 1.00 25.91 ? 102 ARG   A C   1 
ATOM   815   O  O   . ARG   A  1 102 ? 23.054  -7.033   -18.245 1.00 28.45 ? 102 ARG   A O   1 
ATOM   816   C  CB  . ARG   A  1 102 ? 22.897  -9.602   -16.087 1.00 29.52 ? 102 ARG   A CB  1 
ATOM   817   C  CG  . ARG   A  1 102 ? 21.895  -10.724  -15.802 1.00 27.10 ? 102 ARG   A CG  1 
ATOM   818   C  CD  . ARG   A  1 102 ? 21.703  -11.037  -14.324 1.00 31.19 ? 102 ARG   A CD  1 
ATOM   819   N  NE  . ARG   A  1 102 ? 21.553  -12.475  -14.115 1.00 30.57 ? 102 ARG   A NE  1 
ATOM   820   C  CZ  . ARG   A  1 102 ? 20.462  -13.163  -14.444 1.00 27.13 ? 102 ARG   A CZ  1 
ATOM   821   N  NH1 . ARG   A  1 102 ? 19.416  -12.570  -14.973 1.00 27.52 ? 102 ARG   A NH1 1 
ATOM   822   N  NH2 . ARG   A  1 102 ? 20.431  -14.483  -14.248 1.00 30.94 ? 102 ARG   A NH2 1 
ATOM   823   N  N   . GLU   A  1 103 ? 25.009  -7.813   -17.470 1.00 28.84 ? 103 GLU   A N   1 
ATOM   824   C  CA  . GLU   A  1 103 ? 25.691  -6.545   -17.720 1.00 36.22 ? 103 GLU   A CA  1 
ATOM   825   C  C   . GLU   A  1 103 ? 25.634  -6.163   -19.194 1.00 33.82 ? 103 GLU   A C   1 
ATOM   826   O  O   . GLU   A  1 103 ? 25.418  -4.996   -19.540 1.00 35.25 ? 103 GLU   A O   1 
ATOM   827   C  CB  . GLU   A  1 103 ? 27.139  -6.661   -17.254 1.00 32.61 ? 103 GLU   A CB  1 
ATOM   828   C  CG  . GLU   A  1 103 ? 27.230  -6.801   -15.731 1.00 44.56 ? 103 GLU   A CG  1 
ATOM   829   C  CD  . GLU   A  1 103 ? 28.657  -6.801   -15.215 1.00 62.56 ? 103 GLU   A CD  1 
ATOM   830   O  OE1 . GLU   A  1 103 ? 29.588  -6.583   -16.023 1.00 60.06 ? 103 GLU   A OE1 1 
ATOM   831   O  OE2 . GLU   A  1 103 ? 28.840  -7.014   -13.997 1.00 59.12 ? 103 GLU   A OE2 1 
ATOM   832   N  N   . ALA   A  1 104 ? 25.842  -7.136   -20.079 1.00 28.21 ? 104 ALA   A N   1 
ATOM   833   C  CA  . ALA   A  1 104 ? 25.785  -6.860   -21.510 1.00 27.58 ? 104 ALA   A CA  1 
ATOM   834   C  C   . ALA   A  1 104 ? 24.398  -6.399   -21.939 1.00 33.20 ? 104 ALA   A C   1 
ATOM   835   O  O   . ALA   A  1 104 ? 24.261  -5.488   -22.773 1.00 28.78 ? 104 ALA   A O   1 
ATOM   836   C  CB  . ALA   A  1 104 ? 26.224  -8.120   -22.275 1.00 28.41 ? 104 ALA   A CB  1 
ATOM   837   N  N   . ILE   A  1 105 ? 23.348  -7.013   -21.375 1.00 31.84 ? 105 ILE   A N   1 
ATOM   838   C  CA  . ILE   A  1 105 ? 21.986  -6.619   -21.713 1.00 25.67 ? 105 ILE   A CA  1 
ATOM   839   C  C   . ILE   A  1 105 ? 21.700  -5.197   -21.233 1.00 26.37 ? 105 ILE   A C   1 
ATOM   840   O  O   . ILE   A  1 105 ? 21.052  -4.412   -21.934 1.00 27.76 ? 105 ILE   A O   1 
ATOM   841   C  CB  . ILE   A  1 105 ? 20.960  -7.634   -21.146 1.00 25.64 ? 105 ILE   A CB  1 
ATOM   842   C  CG1 . ILE   A  1 105 ? 20.894  -8.877   -22.050 1.00 26.93 ? 105 ILE   A CG1 1 
ATOM   843   C  CG2 . ILE   A  1 105 ? 19.557  -7.019   -21.140 1.00 24.61 ? 105 ILE   A CG2 1 
ATOM   844   C  CD1 . ILE   A  1 105 ? 20.433  -10.210  -21.349 1.00 30.90 ? 105 ILE   A CD1 1 
ATOM   845   N  N   . VAL   A  1 106 ? 22.199  -4.820   -20.060 1.00 28.53 ? 106 VAL   A N   1 
ATOM   846   C  CA  . VAL   A  1 106 ? 21.990  -3.438   -19.621 1.00 33.02 ? 106 VAL   A CA  1 
ATOM   847   C  C   . VAL   A  1 106 ? 22.568  -2.456   -20.634 1.00 26.70 ? 106 VAL   A C   1 
ATOM   848   O  O   . VAL   A  1 106 ? 21.963  -1.419   -20.939 1.00 30.49 ? 106 VAL   A O   1 
ATOM   849   C  CB  . VAL   A  1 106 ? 22.612  -3.200   -18.237 1.00 37.00 ? 106 VAL   A CB  1 
ATOM   850   C  CG1 . VAL   A  1 106 ? 22.526  -1.706   -17.911 1.00 39.55 ? 106 VAL   A CG1 1 
ATOM   851   C  CG2 . VAL   A  1 106 ? 21.903  -4.037   -17.193 1.00 39.32 ? 106 VAL   A CG2 1 
ATOM   852   N  N   . HIS   A  1 107 ? 23.755  -2.749   -21.151 1.00 32.10 ? 107 HIS   A N   1 
ATOM   853   C  CA  . HIS   A  1 107 ? 24.363  -1.811   -22.086 1.00 37.42 ? 107 HIS   A CA  1 
ATOM   854   C  C   . HIS   A  1 107 ? 23.633  -1.820   -23.433 1.00 34.70 ? 107 HIS   A C   1 
ATOM   855   O  O   . HIS   A  1 107 ? 23.352  -0.757   -24.000 1.00 33.26 ? 107 HIS   A O   1 
ATOM   856   C  CB  . HIS   A  1 107 ? 25.857  -2.108   -22.240 1.00 34.11 ? 107 HIS   A CB  1 
ATOM   857   C  CG  . HIS   A  1 107 ? 26.535  -1.111   -23.126 1.00 41.98 ? 107 HIS   A CG  1 
ATOM   858   N  ND1 . HIS   A  1 107 ? 26.755  0.194    -22.734 1.00 38.84 ? 107 HIS   A ND1 1 
ATOM   859   C  CD2 . HIS   A  1 107 ? 26.930  -1.191   -24.418 1.00 36.05 ? 107 HIS   A CD2 1 
ATOM   860   C  CE1 . HIS   A  1 107 ? 27.302  0.862    -23.732 1.00 43.83 ? 107 HIS   A CE1 1 
ATOM   861   N  NE2 . HIS   A  1 107 ? 27.403  0.051    -24.771 1.00 41.14 ? 107 HIS   A NE2 1 
ATOM   862   N  N   . CYS   A  1 108 ? 23.267  -3.001   -23.941 1.00 34.74 ? 108 CYS   A N   1 
ATOM   863   C  CA  . CYS   A  1 108 ? 22.446  -3.039   -25.155 1.00 27.82 ? 108 CYS   A CA  1 
ATOM   864   C  C   . CYS   A  1 108 ? 21.204  -2.179   -25.013 1.00 24.66 ? 108 CYS   A C   1 
ATOM   865   O  O   . CYS   A  1 108 ? 20.826  -1.454   -25.942 1.00 33.07 ? 108 CYS   A O   1 
ATOM   866   C  CB  . CYS   A  1 108 ? 22.056  -4.481   -25.504 1.00 25.62 ? 108 CYS   A CB  1 
ATOM   867   S  SG  . CYS   A  1 108 ? 23.409  -5.454   -26.095 1.00 33.32 ? 108 CYS   A SG  1 
ATOM   868   N  N   . GLU   A  1 109 ? 20.554  -2.234   -23.851 1.00 28.17 ? 109 GLU   A N   1 
ATOM   869   C  CA  . GLU   A  1 109 ? 19.347  -1.455   -23.652 1.00 31.46 ? 109 GLU   A CA  1 
ATOM   870   C  C   . GLU   A  1 109 ? 19.654  0.024    -23.690 1.00 33.17 ? 109 GLU   A C   1 
ATOM   871   O  O   . GLU   A  1 109 ? 18.917  0.804    -24.300 1.00 32.35 ? 109 GLU   A O   1 
ATOM   872   C  CB  . GLU   A  1 109 ? 18.700  -1.809   -22.305 1.00 31.70 ? 109 GLU   A CB  1 
ATOM   873   C  CG  . GLU   A  1 109 ? 17.355  -1.091   -22.056 1.00 32.70 ? 109 GLU   A CG  1 
ATOM   874   C  CD  . GLU   A  1 109 ? 16.202  -1.591   -22.930 1.00 33.79 ? 109 GLU   A CD  1 
ATOM   875   O  OE1 . GLU   A  1 109 ? 16.333  -2.666   -23.556 1.00 30.82 ? 109 GLU   A OE1 1 
ATOM   876   O  OE2 . GLU   A  1 109 ? 15.156  -0.909   -22.971 1.00 37.47 ? 109 GLU   A OE2 1 
ATOM   877   N  N   . GLN   A  1 110 ? 20.734  0.427    -23.024 1.00 38.80 ? 110 GLN   A N   1 
ATOM   878   C  CA  . GLN   A  1 110 ? 21.081  1.842    -22.959 1.00 40.07 ? 110 GLN   A CA  1 
ATOM   879   C  C   . GLN   A  1 110 ? 21.364  2.423    -24.338 1.00 38.50 ? 110 GLN   A C   1 
ATOM   880   O  O   . GLN   A  1 110 ? 21.023  3.579    -24.599 1.00 42.74 ? 110 GLN   A O   1 
ATOM   881   C  CB  . GLN   A  1 110 ? 22.287  2.042    -22.038 1.00 46.14 ? 110 GLN   A CB  1 
ATOM   882   C  CG  . GLN   A  1 110 ? 21.946  1.951    -20.542 1.00 47.47 ? 110 GLN   A CG  1 
ATOM   883   N  N   . VAL   A  1 111 ? 21.993  1.661    -25.238 1.00 36.54 ? 111 VAL   A N   1 
ATOM   884   C  CA  . VAL   A  1 111 ? 22.287  2.207    -26.570 1.00 35.02 ? 111 VAL   A CA  1 
ATOM   885   C  C   . VAL   A  1 111 ? 21.252  1.796    -27.628 1.00 40.23 ? 111 VAL   A C   1 
ATOM   886   O  O   . VAL   A  1 111 ? 21.418  2.129    -28.805 1.00 34.09 ? 111 VAL   A O   1 
ATOM   887   C  CB  . VAL   A  1 111 ? 23.722  1.865    -27.003 1.00 35.39 ? 111 VAL   A CB  1 
ATOM   888   C  CG1 . VAL   A  1 111 ? 24.713  2.310    -25.887 1.00 37.94 ? 111 VAL   A CG1 1 
ATOM   889   C  CG2 . VAL   A  1 111 ? 23.898  0.403    -27.317 1.00 36.52 ? 111 VAL   A CG2 1 
ATOM   890   N  N   . HIS   A  1 112 ? 20.167  1.121    -27.231 1.00 32.84 ? 112 HIS   A N   1 
ATOM   891   C  CA  . HIS   A  1 112 ? 19.009  0.841    -28.102 1.00 31.85 ? 112 HIS   A CA  1 
ATOM   892   C  C   . HIS   A  1 112 ? 19.313  -0.238   -29.137 1.00 32.53 ? 112 HIS   A C   1 
ATOM   893   O  O   . HIS   A  1 112 ? 18.724  -0.264   -30.224 1.00 29.61 ? 112 HIS   A O   1 
ATOM   894   C  CB  . HIS   A  1 112 ? 18.500  2.104    -28.812 1.00 37.65 ? 112 HIS   A CB  1 
ATOM   895   C  CG  . HIS   A  1 112 ? 18.207  3.248    -27.889 1.00 41.12 ? 112 HIS   A CG  1 
ATOM   896   N  ND1 . HIS   A  1 112 ? 18.059  4.541    -28.337 1.00 53.90 ? 112 HIS   A ND1 1 
ATOM   897   C  CD2 . HIS   A  1 112 ? 18.013  3.289    -26.551 1.00 44.01 ? 112 HIS   A CD2 1 
ATOM   898   C  CE1 . HIS   A  1 112 ? 17.793  5.333    -27.314 1.00 47.50 ? 112 HIS   A CE1 1 
ATOM   899   N  NE2 . HIS   A  1 112 ? 17.759  4.598    -26.218 1.00 44.65 ? 112 HIS   A NE2 1 
ATOM   900   N  N   . ASP   A  1 113 ? 20.265  -1.106   -28.834 1.00 31.04 ? 113 ASP   A N   1 
ATOM   901   C  CA  . ASP   A  1 113 ? 20.538  -2.272   -29.667 1.00 29.96 ? 113 ASP   A CA  1 
ATOM   902   C  C   . ASP   A  1 113 ? 19.647  -3.420   -29.177 1.00 29.04 ? 113 ASP   A C   1 
ATOM   903   O  O   . ASP   A  1 113 ? 20.054  -4.355   -28.466 1.00 29.95 ? 113 ASP   A O   1 
ATOM   904   C  CB  . ASP   A  1 113 ? 22.012  -2.598   -29.627 1.00 27.79 ? 113 ASP   A CB  1 
ATOM   905   C  CG  . ASP   A  1 113 ? 22.385  -3.707   -30.578 1.00 34.59 ? 113 ASP   A CG  1 
ATOM   906   O  OD1 . ASP   A  1 113 ? 21.464  -4.314   -31.177 1.00 30.75 ? 113 ASP   A OD1 1 
ATOM   907   O  OD2 . ASP   A  1 113 ? 23.599  -3.985   -30.698 1.00 30.39 ? 113 ASP   A OD2 1 
ATOM   908   N  N   . TYR   A  1 114 ? 18.383  -3.293   -29.533 1.00 26.89 ? 114 TYR   A N   1 
ATOM   909   C  CA  . TYR   A  1 114 ? 17.358  -4.204   -29.008 1.00 31.30 ? 114 TYR   A CA  1 
ATOM   910   C  C   . TYR   A  1 114 ? 17.477  -5.606   -29.606 1.00 32.43 ? 114 TYR   A C   1 
ATOM   911   O  O   . TYR   A  1 114 ? 17.123  -6.598   -28.947 1.00 28.89 ? 114 TYR   A O   1 
ATOM   912   C  CB  . TYR   A  1 114 ? 15.982  -3.609   -29.258 1.00 33.12 ? 114 TYR   A CB  1 
ATOM   913   C  CG  . TYR   A  1 114 ? 15.792  -2.274   -28.613 1.00 27.52 ? 114 TYR   A CG  1 
ATOM   914   C  CD1 . TYR   A  1 114 ? 15.938  -2.130   -27.236 1.00 31.30 ? 114 TYR   A CD1 1 
ATOM   915   C  CD2 . TYR   A  1 114 ? 15.459  -1.159   -29.361 1.00 29.92 ? 114 TYR   A CD2 1 
ATOM   916   C  CE1 . TYR   A  1 114 ? 15.759  -0.915   -26.631 1.00 33.08 ? 114 TYR   A CE1 1 
ATOM   917   C  CE2 . TYR   A  1 114 ? 15.285  0.065    -28.769 1.00 31.23 ? 114 TYR   A CE2 1 
ATOM   918   C  CZ  . TYR   A  1 114 ? 15.435  0.179    -27.393 1.00 36.75 ? 114 TYR   A CZ  1 
ATOM   919   O  OH  . TYR   A  1 114 ? 15.231  1.382    -26.767 1.00 36.30 ? 114 TYR   A OH  1 
ATOM   920   N  N   . VAL   A  1 115 ? 18.017  -5.721   -30.818 1.00 28.15 ? 115 VAL   A N   1 
ATOM   921   C  CA  . VAL   A  1 115 ? 18.227  -7.048   -31.393 1.00 27.55 ? 115 VAL   A CA  1 
ATOM   922   C  C   . VAL   A  1 115 ? 19.346  -7.770   -30.672 1.00 28.91 ? 115 VAL   A C   1 
ATOM   923   O  O   . VAL   A  1 115 ? 19.233  -8.962   -30.369 1.00 25.51 ? 115 VAL   A O   1 
ATOM   924   C  CB  . VAL   A  1 115 ? 18.501  -6.962   -32.902 1.00 30.16 ? 115 VAL   A CB  1 
ATOM   925   C  CG1 . VAL   A  1 115 ? 18.808  -8.372   -33.460 1.00 28.01 ? 115 VAL   A CG1 1 
ATOM   926   C  CG2 . VAL   A  1 115 ? 17.312  -6.329   -33.607 1.00 28.81 ? 115 VAL   A CG2 1 
ATOM   927   N  N   . SER   A  1 116 ? 20.469  -7.082   -30.418 1.00 30.05 ? 116 SER   A N   1 
ATOM   928   C  CA  . SER   A  1 116 ? 21.519  -7.733   -29.647 1.00 30.94 ? 116 SER   A CA  1 
ATOM   929   C  C   . SER   A  1 116 ? 20.988  -8.140   -28.279 1.00 26.54 ? 116 SER   A C   1 
ATOM   930   O  O   . SER   A  1 116 ? 21.288  -9.241   -27.796 1.00 26.78 ? 116 SER   A O   1 
ATOM   931   C  CB  . SER   A  1 116 ? 22.747  -6.832   -29.494 1.00 30.75 ? 116 SER   A CB  1 
ATOM   932   O  OG  . SER   A  1 116 ? 23.444  -6.700   -30.727 1.00 33.22 ? 116 SER   A OG  1 
ATOM   933   N  N   . ARG   A  1 117 ? 20.191  -7.267   -27.648 1.00 24.55 ? 117 ARG   A N   1 
ATOM   934   C  CA  . ARG   A  1 117 ? 19.569  -7.613   -26.374 1.00 33.68 ? 117 ARG   A CA  1 
ATOM   935   C  C   . ARG   A  1 117 ? 18.771  -8.904   -26.483 1.00 30.68 ? 117 ARG   A C   1 
ATOM   936   O  O   . ARG   A  1 117 ? 18.894  -9.785   -25.630 1.00 27.68 ? 117 ARG   A O   1 
ATOM   937   C  CB  . ARG   A  1 117 ? 18.640  -6.509   -25.880 1.00 29.33 ? 117 ARG   A CB  1 
ATOM   938   C  CG  . ARG   A  1 117 ? 17.736  -7.030   -24.757 1.00 27.95 ? 117 ARG   A CG  1 
ATOM   939   C  CD  . ARG   A  1 117 ? 17.117  -5.934   -23.935 1.00 27.26 ? 117 ARG   A CD  1 
ATOM   940   N  NE  . ARG   A  1 117 ? 16.180  -6.489   -22.976 1.00 30.20 ? 117 ARG   A NE  1 
ATOM   941   C  CZ  . ARG   A  1 117 ? 15.727  -5.866   -21.897 1.00 36.51 ? 117 ARG   A CZ  1 
ATOM   942   N  NH1 . ARG   A  1 117 ? 16.077  -4.627   -21.613 1.00 35.19 ? 117 ARG   A NH1 1 
ATOM   943   N  NH2 . ARG   A  1 117 ? 14.906  -6.512   -21.073 1.00 30.26 ? 117 ARG   A NH2 1 
ATOM   944   N  N   . ASP   A  1 118 ? 17.928  -9.012   -27.520 1.00 28.66 ? 118 ASP   A N   1 
ATOM   945   C  CA  . ASP   A  1 118 ? 17.069  -10.186  -27.665 1.00 33.26 ? 118 ASP   A CA  1 
ATOM   946   C  C   . ASP   A  1 118 ? 17.885  -11.462  -27.841 1.00 24.15 ? 118 ASP   A C   1 
ATOM   947   O  O   . ASP   A  1 118 ? 17.538  -12.501  -27.266 1.00 25.95 ? 118 ASP   A O   1 
ATOM   948   C  CB  . ASP   A  1 118 ? 16.113  -9.975   -28.838 1.00 29.40 ? 118 ASP   A CB  1 
ATOM   949   C  CG  . ASP   A  1 118 ? 14.931  -10.973  -28.861 1.00 28.99 ? 118 ASP   A CG  1 
ATOM   950   O  OD1 . ASP   A  1 118 ? 14.273  -11.148  -27.832 1.00 29.93 ? 118 ASP   A OD1 1 
ATOM   951   O  OD2 . ASP   A  1 118 ? 14.625  -11.523  -29.942 1.00 31.54 ? 118 ASP   A OD2 1 
ATOM   952   N  N   . LEU   A  1 119 ? 18.984  -11.408  -28.602 1.00 31.28 ? 119 LEU   A N   1 
ATOM   953   C  CA  . LEU   A  1 119 ? 19.859  -12.582  -28.723 1.00 25.96 ? 119 LEU   A CA  1 
ATOM   954   C  C   . LEU   A  1 119 ? 20.468  -12.985  -27.386 1.00 29.08 ? 119 LEU   A C   1 
ATOM   955   O  O   . LEU   A  1 119 ? 20.524  -14.175  -27.047 1.00 26.97 ? 119 LEU   A O   1 
ATOM   956   C  CB  . LEU   A  1 119 ? 20.979  -12.319  -29.739 1.00 25.26 ? 119 LEU   A CB  1 
ATOM   957   C  CG  . LEU   A  1 119 ? 22.116  -13.354  -29.830 1.00 26.74 ? 119 LEU   A CG  1 
ATOM   958   C  CD1 . LEU   A  1 119 ? 21.642  -14.744  -30.260 1.00 30.35 ? 119 LEU   A CD1 1 
ATOM   959   C  CD2 . LEU   A  1 119 ? 23.174  -12.886  -30.795 1.00 32.50 ? 119 LEU   A CD2 1 
ATOM   960   N  N   . LEU   A  1 120 ? 21.008  -12.010  -26.633 1.00 29.97 ? 120 LEU   A N   1 
ATOM   961   C  CA  . LEU   A  1 120 ? 21.563  -12.321  -25.320 1.00 25.29 ? 120 LEU   A CA  1 
ATOM   962   C  C   . LEU   A  1 120 ? 20.492  -12.837  -24.351 1.00 23.73 ? 120 LEU   A C   1 
ATOM   963   O  O   . LEU   A  1 120 ? 20.775  -13.708  -23.513 1.00 24.16 ? 120 LEU   A O   1 
ATOM   964   C  CB  . LEU   A  1 120 ? 22.258  -11.074  -24.740 1.00 24.24 ? 120 LEU   A CB  1 
ATOM   965   C  CG  . LEU   A  1 120 ? 23.372  -10.501  -25.610 1.00 27.75 ? 120 LEU   A CG  1 
ATOM   966   C  CD1 . LEU   A  1 120 ? 23.988  -9.229   -25.039 1.00 32.34 ? 120 LEU   A CD1 1 
ATOM   967   C  CD2 . LEU   A  1 120 ? 24.467  -11.560  -25.799 1.00 25.97 ? 120 LEU   A CD2 1 
ATOM   968   N  N   . LYS   A  1 121 ? 19.271  -12.293  -24.431 1.00 25.64 ? 121 LYS   A N   1 
ATOM   969   C  CA  . LYS   A  1 121 ? 18.173  -12.802  -23.609 1.00 29.52 ? 121 LYS   A CA  1 
ATOM   970   C  C   . LYS   A  1 121 ? 17.919  -14.275  -23.915 1.00 27.45 ? 121 LYS   A C   1 
ATOM   971   O  O   . LYS   A  1 121 ? 17.763  -15.092  -22.992 1.00 28.81 ? 121 LYS   A O   1 
ATOM   972   C  CB  . LYS   A  1 121 ? 16.898  -11.982  -23.846 1.00 25.16 ? 121 LYS   A CB  1 
ATOM   973   C  CG  . LYS   A  1 121 ? 15.713  -12.391  -22.952 1.00 26.12 ? 121 LYS   A CG  1 
ATOM   974   C  CD  . LYS   A  1 121 ? 14.811  -13.482  -23.591 1.00 25.20 ? 121 LYS   A CD  1 
ATOM   975   C  CE  . LYS   A  1 121 ? 14.060  -12.979  -24.810 1.00 33.82 ? 121 LYS   A CE  1 
ATOM   976   N  NZ  . LYS   A  1 121 ? 13.287  -14.107  -25.396 1.00 31.12 ? 121 LYS   A NZ  1 
ATOM   977   N  N   . ASP   A  1 122 ? 17.887  -14.625  -25.213 1.00 24.50 ? 122 ASP   A N   1 
ATOM   978   C  CA  . ASP   A  1 122 ? 17.734  -16.021  -25.614 1.00 28.29 ? 122 ASP   A CA  1 
ATOM   979   C  C   . ASP   A  1 122 ? 18.860  -16.884  -25.065 1.00 30.20 ? 122 ASP   A C   1 
ATOM   980   O  O   . ASP   A  1 122 ? 18.616  -17.985  -24.569 1.00 25.83 ? 122 ASP   A O   1 
ATOM   981   C  CB  . ASP   A  1 122 ? 17.685  -16.143  -27.139 1.00 26.46 ? 122 ASP   A CB  1 
ATOM   982   C  CG  . ASP   A  1 122 ? 16.383  -15.618  -27.731 1.00 34.14 ? 122 ASP   A CG  1 
ATOM   983   O  OD1 . ASP   A  1 122 ? 15.393  -15.449  -26.988 1.00 33.79 ? 122 ASP   A OD1 1 
ATOM   984   O  OD2 . ASP   A  1 122 ? 16.355  -15.398  -28.955 1.00 39.89 ? 122 ASP   A OD2 1 
ATOM   985   N  N   . ILE   A  1 123 ? 20.110  -16.411  -25.155 1.00 30.82 ? 123 ILE   A N   1 
ATOM   986   C  CA  . ILE   A  1 123 ? 21.218  -17.180  -24.588 1.00 26.76 ? 123 ILE   A CA  1 
ATOM   987   C  C   . ILE   A  1 123 ? 21.075  -17.287  -23.067 1.00 26.21 ? 123 ILE   A C   1 
ATOM   988   O  O   . ILE   A  1 123 ? 21.317  -18.349  -22.477 1.00 24.04 ? 123 ILE   A O   1 
ATOM   989   C  CB  . ILE   A  1 123 ? 22.569  -16.553  -25.007 1.00 28.09 ? 123 ILE   A CB  1 
ATOM   990   C  CG1 . ILE   A  1 123 ? 22.740  -16.676  -26.531 1.00 31.85 ? 123 ILE   A CG1 1 
ATOM   991   C  CG2 . ILE   A  1 123 ? 23.719  -17.173  -24.209 1.00 25.96 ? 123 ILE   A CG2 1 
ATOM   992   C  CD1 . ILE   A  1 123 ? 23.863  -15.819  -27.149 1.00 37.36 ? 123 ILE   A CD1 1 
ATOM   993   N  N   . LEU   A  1 124 ? 20.710  -16.184  -22.405 1.00 23.35 ? 124 LEU   A N   1 
ATOM   994   C  CA  . LEU   A  1 124 ? 20.499  -16.213  -20.959 1.00 26.29 ? 124 LEU   A CA  1 
ATOM   995   C  C   . LEU   A  1 124 ? 19.457  -17.260  -20.558 1.00 26.84 ? 124 LEU   A C   1 
ATOM   996   O  O   . LEU   A  1 124 ? 19.621  -17.959  -19.545 1.00 24.10 ? 124 LEU   A O   1 
ATOM   997   C  CB  . LEU   A  1 124 ? 20.084  -14.820  -20.480 1.00 28.06 ? 124 LEU   A CB  1 
ATOM   998   C  CG  . LEU   A  1 124 ? 19.812  -14.639  -18.980 1.00 27.58 ? 124 LEU   A CG  1 
ATOM   999   C  CD1 . LEU   A  1 124 ? 21.045  -14.928  -18.194 1.00 27.44 ? 124 LEU   A CD1 1 
ATOM   1000  C  CD2 . LEU   A  1 124 ? 19.318  -13.231  -18.662 1.00 28.07 ? 124 LEU   A CD2 1 
ATOM   1001  N  N   . GLU   A  1 125 ? 18.391  -17.396  -21.348 1.00 28.60 ? 125 GLU   A N   1 
ATOM   1002  C  CA  . GLU   A  1 125 ? 17.380  -18.399  -21.039 1.00 25.90 ? 125 GLU   A CA  1 
ATOM   1003  C  C   . GLU   A  1 125 ? 17.973  -19.793  -21.086 1.00 25.89 ? 125 GLU   A C   1 
ATOM   1004  O  O   . GLU   A  1 125 ? 17.755  -20.598  -20.170 1.00 26.05 ? 125 GLU   A O   1 
ATOM   1005  C  CB  . GLU   A  1 125 ? 16.189  -18.251  -21.999 1.00 28.04 ? 125 GLU   A CB  1 
ATOM   1006  C  CG  . GLU   A  1 125 ? 15.377  -17.021  -21.665 1.00 33.68 ? 125 GLU   A CG  1 
ATOM   1007  C  CD  . GLU   A  1 125 ? 14.151  -16.747  -22.537 1.00 51.05 ? 125 GLU   A CD  1 
ATOM   1008  O  OE1 . GLU   A  1 125 ? 14.111  -17.128  -23.741 1.00 38.31 ? 125 GLU   A OE1 1 
ATOM   1009  O  OE2 . GLU   A  1 125 ? 13.216  -16.102  -21.986 1.00 44.56 ? 125 GLU   A OE2 1 
ATOM   1010  N  N   . SER   A  1 126 ? 18.780  -20.069  -22.118 1.00 26.14 ? 126 SER   A N   1 
ATOM   1011  C  CA  A SER   A  1 126 ? 19.459  -21.351  -22.227 0.50 30.52 ? 126 SER   A CA  1 
ATOM   1012  C  CA  B SER   A  1 126 ? 19.460  -21.355  -22.224 0.50 30.52 ? 126 SER   A CA  1 
ATOM   1013  C  C   . SER   A  1 126 ? 20.405  -21.582  -21.057 1.00 26.57 ? 126 SER   A C   1 
ATOM   1014  O  O   . SER   A  1 126 ? 20.446  -22.678  -20.492 1.00 27.18 ? 126 SER   A O   1 
ATOM   1015  C  CB  A SER   A  1 126 ? 20.223  -21.412  -23.552 0.50 29.28 ? 126 SER   A CB  1 
ATOM   1016  C  CB  B SER   A  1 126 ? 20.239  -21.442  -23.537 0.50 29.26 ? 126 SER   A CB  1 
ATOM   1017  O  OG  A SER   A  1 126 ? 21.064  -22.538  -23.602 0.50 23.13 ? 126 SER   A OG  1 
ATOM   1018  O  OG  B SER   A  1 126 ? 19.352  -21.455  -24.633 0.50 38.53 ? 126 SER   A OG  1 
ATOM   1019  N  N   . GLU   A  1 127 ? 21.189  -20.558  -20.683 1.00 27.21 ? 127 GLU   A N   1 
ATOM   1020  C  CA  . GLU   A  1 127 ? 22.115  -20.711  -19.569 1.00 27.17 ? 127 GLU   A CA  1 
ATOM   1021  C  C   . GLU   A  1 127 ? 21.382  -20.940  -18.238 1.00 24.44 ? 127 GLU   A C   1 
ATOM   1022  O  O   . GLU   A  1 127 ? 21.849  -21.721  -17.405 1.00 27.39 ? 127 GLU   A O   1 
ATOM   1023  C  CB  . GLU   A  1 127 ? 23.033  -19.487  -19.486 1.00 30.91 ? 127 GLU   A CB  1 
ATOM   1024  C  CG  . GLU   A  1 127 ? 23.932  -19.256  -20.738 1.00 31.14 ? 127 GLU   A CG  1 
ATOM   1025  C  CD  . GLU   A  1 127 ? 24.603  -20.503  -21.284 1.00 30.94 ? 127 GLU   A CD  1 
ATOM   1026  O  OE1 . GLU   A  1 127 ? 24.940  -21.423  -20.530 1.00 37.00 ? 127 GLU   A OE1 1 
ATOM   1027  O  OE2 . GLU   A  1 127 ? 24.800  -20.569  -22.516 1.00 41.34 ? 127 GLU   A OE2 1 
ATOM   1028  N  N   . GLU   A  1 128 ? 20.248  -20.267  -18.014 1.00 25.73 ? 128 GLU   A N   1 
ATOM   1029  C  CA  . GLU   A  1 128 ? 19.490  -20.535  -16.797 1.00 26.37 ? 128 GLU   A CA  1 
ATOM   1030  C  C   . GLU   A  1 128 ? 18.904  -21.944  -16.795 1.00 29.45 ? 128 GLU   A C   1 
ATOM   1031  O  O   . GLU   A  1 128 ? 18.814  -22.572  -15.728 1.00 25.96 ? 128 GLU   A O   1 
ATOM   1032  C  CB  . GLU   A  1 128 ? 18.401  -19.480  -16.602 1.00 28.93 ? 128 GLU   A CB  1 
ATOM   1033  C  CG  . GLU   A  1 128 ? 18.974  -18.137  -16.086 1.00 29.66 ? 128 GLU   A CG  1 
ATOM   1034  C  CD  . GLU   A  1 128 ? 17.929  -17.122  -15.618 1.00 33.13 ? 128 GLU   A CD  1 
ATOM   1035  O  OE1 . GLU   A  1 128 ? 16.715  -17.441  -15.542 1.00 28.97 ? 128 GLU   A OE1 1 
ATOM   1036  O  OE2 . GLU   A  1 128 ? 18.334  -15.977  -15.314 1.00 31.65 ? 128 GLU   A OE2 1 
ATOM   1037  N  N   . GLU   A  1 129 ? 18.528  -22.474  -17.963 1.00 26.02 ? 129 GLU   A N   1 
ATOM   1038  C  CA  . GLU   A  1 129 ? 18.144  -23.889  -18.025 1.00 29.81 ? 129 GLU   A CA  1 
ATOM   1039  C  C   . GLU   A  1 129 ? 19.313  -24.802  -17.658 1.00 23.25 ? 129 GLU   A C   1 
ATOM   1040  O  O   . GLU   A  1 129 ? 19.136  -25.769  -16.910 1.00 26.67 ? 129 GLU   A O   1 
ATOM   1041  C  CB  . GLU   A  1 129 ? 17.603  -24.246  -19.406 1.00 27.26 ? 129 GLU   A CB  1 
ATOM   1042  C  CG  . GLU   A  1 129 ? 16.216  -23.694  -19.652 1.00 44.87 ? 129 GLU   A CG  1 
ATOM   1043  C  CD  . GLU   A  1 129 ? 15.710  -24.040  -21.050 1.00 53.50 ? 129 GLU   A CD  1 
ATOM   1044  O  OE1 . GLU   A  1 129 ? 16.143  -25.074  -21.596 1.00 54.20 ? 129 GLU   A OE1 1 
ATOM   1045  O  OE2 . GLU   A  1 129 ? 14.887  -23.283  -21.597 1.00 57.77 ? 129 GLU   A OE2 1 
ATOM   1046  N  N   . HIS   A  1 130 ? 20.520  -24.509  -18.149 1.00 28.74 ? 130 HIS   A N   1 
ATOM   1047  C  CA  A HIS   A  1 130 ? 21.660  -25.327  -17.752 0.50 25.12 ? 130 HIS   A CA  1 
ATOM   1048  C  CA  B HIS   A  1 130 ? 21.700  -25.290  -17.758 0.50 25.14 ? 130 HIS   A CA  1 
ATOM   1049  C  C   . HIS   A  1 130 ? 21.939  -25.219  -16.252 1.00 28.46 ? 130 HIS   A C   1 
ATOM   1050  O  O   . HIS   A  1 130 ? 22.281  -26.220  -15.611 1.00 28.39 ? 130 HIS   A O   1 
ATOM   1051  C  CB  A HIS   A  1 130 ? 22.903  -24.944  -18.563 0.50 28.44 ? 130 HIS   A CB  1 
ATOM   1052  C  CB  B HIS   A  1 130 ? 22.972  -24.787  -18.469 0.50 28.64 ? 130 HIS   A CB  1 
ATOM   1053  C  CG  A HIS   A  1 130 ? 24.007  -25.947  -18.462 0.50 32.12 ? 130 HIS   A CG  1 
ATOM   1054  C  CG  B HIS   A  1 130 ? 22.978  -24.937  -19.960 0.50 27.23 ? 130 HIS   A CG  1 
ATOM   1055  N  ND1 A HIS   A  1 130 ? 25.281  -25.712  -18.934 0.50 34.77 ? 130 HIS   A ND1 1 
ATOM   1056  N  ND1 B HIS   A  1 130 ? 24.005  -24.442  -20.744 0.50 34.11 ? 130 HIS   A ND1 1 
ATOM   1057  C  CD2 A HIS   A  1 130 ? 24.023  -27.195  -17.942 0.50 30.28 ? 130 HIS   A CD2 1 
ATOM   1058  C  CD2 B HIS   A  1 130 ? 22.098  -25.515  -20.816 0.50 30.82 ? 130 HIS   A CD2 1 
ATOM   1059  C  CE1 A HIS   A  1 130 ? 26.033  -26.773  -18.702 0.50 34.22 ? 130 HIS   A CE1 1 
ATOM   1060  C  CE1 B HIS   A  1 130 ? 23.754  -24.708  -22.017 0.50 30.28 ? 130 HIS   A CE1 1 
ATOM   1061  N  NE2 A HIS   A  1 130 ? 25.290  -27.689  -18.111 0.50 32.81 ? 130 HIS   A NE2 1 
ATOM   1062  N  NE2 B HIS   A  1 130 ? 22.608  -25.363  -22.088 0.50 28.50 ? 130 HIS   A NE2 1 
ATOM   1063  N  N   . ILE   A  1 131 ? 21.822  -24.017  -15.677 1.00 23.09 ? 131 ILE   A N   1 
ATOM   1064  C  CA  . ILE   A  1 131 ? 21.976  -23.857  -14.239 1.00 26.23 ? 131 ILE   A CA  1 
ATOM   1065  C  C   . ILE   A  1 131 ? 20.974  -24.735  -13.496 1.00 28.89 ? 131 ILE   A C   1 
ATOM   1066  O  O   . ILE   A  1 131 ? 21.311  -25.378  -12.494 1.00 25.75 ? 131 ILE   A O   1 
ATOM   1067  C  CB  . ILE   A  1 131 ? 21.827  -22.371  -13.852 1.00 29.85 ? 131 ILE   A CB  1 
ATOM   1068  C  CG1 . ILE   A  1 131 ? 23.072  -21.594  -14.324 1.00 30.32 ? 131 ILE   A CG1 1 
ATOM   1069  C  CG2 . ILE   A  1 131 ? 21.614  -22.247  -12.336 1.00 28.85 ? 131 ILE   A CG2 1 
ATOM   1070  C  CD1 . ILE   A  1 131 ? 22.964  -20.072  -14.166 1.00 27.81 ? 131 ILE   A CD1 1 
ATOM   1071  N  N   . ASP   A  1 132 ? 19.728  -24.753  -13.964 1.00 28.73 ? 132 ASP   A N   1 
ATOM   1072  C  CA  . ASP   A  1 132 ? 18.702  -25.602  -13.349 1.00 27.82 ? 132 ASP   A CA  1 
ATOM   1073  C  C   . ASP   A  1 132 ? 19.153  -27.052  -13.379 1.00 26.18 ? 132 ASP   A C   1 
ATOM   1074  O  O   . ASP   A  1 132 ? 19.159  -27.746  -12.354 1.00 26.59 ? 132 ASP   A O   1 
ATOM   1075  C  CB  . ASP   A  1 132 ? 17.376  -25.396  -14.104 1.00 25.76 ? 132 ASP   A CB  1 
ATOM   1076  C  CG  . ASP   A  1 132 ? 16.138  -25.963  -13.360 1.00 30.49 ? 132 ASP   A CG  1 
ATOM   1077  O  OD1 . ASP   A  1 132 ? 16.235  -26.481  -12.229 1.00 33.52 ? 132 ASP   A OD1 1 
ATOM   1078  O  OD2 . ASP   A  1 132 ? 15.061  -25.839  -13.935 1.00 38.76 ? 132 ASP   A OD2 1 
ATOM   1079  N  N   . TYR   A  1 133 ? 19.599  -27.508  -14.544 1.00 23.98 ? 133 TYR   A N   1 
ATOM   1080  C  CA  . TYR   A  1 133 ? 20.061  -28.887  -14.668 1.00 27.43 ? 133 TYR   A CA  1 
ATOM   1081  C  C   . TYR   A  1 133 ? 21.181  -29.179  -13.672 1.00 28.31 ? 133 TYR   A C   1 
ATOM   1082  O  O   . TYR   A  1 133 ? 21.136  -30.180  -12.945 1.00 24.26 ? 133 TYR   A O   1 
ATOM   1083  C  CB  . TYR   A  1 133 ? 20.515  -29.167  -16.120 1.00 26.56 ? 133 TYR   A CB  1 
ATOM   1084  C  CG  . TYR   A  1 133 ? 21.321  -30.425  -16.246 1.00 28.02 ? 133 TYR   A CG  1 
ATOM   1085  C  CD1 . TYR   A  1 133 ? 20.704  -31.657  -16.303 1.00 29.76 ? 133 TYR   A CD1 1 
ATOM   1086  C  CD2 . TYR   A  1 133 ? 22.708  -30.377  -16.298 1.00 32.12 ? 133 TYR   A CD2 1 
ATOM   1087  C  CE1 . TYR   A  1 133 ? 21.446  -32.823  -16.401 1.00 31.87 ? 133 TYR   A CE1 1 
ATOM   1088  C  CE2 . TYR   A  1 133 ? 23.465  -31.536  -16.398 1.00 35.19 ? 133 TYR   A CE2 1 
ATOM   1089  C  CZ  . TYR   A  1 133 ? 22.823  -32.762  -16.439 1.00 35.67 ? 133 TYR   A CZ  1 
ATOM   1090  O  OH  . TYR   A  1 133 ? 23.547  -33.936  -16.546 1.00 35.76 ? 133 TYR   A OH  1 
ATOM   1091  N  N   . LEU   A  1 134 ? 22.184  -28.294  -13.600 1.00 28.35 ? 134 LEU   A N   1 
ATOM   1092  C  CA  . LEU   A  1 134 ? 23.343  -28.539  -12.737 1.00 29.56 ? 134 LEU   A CA  1 
ATOM   1093  C  C   . LEU   A  1 134 ? 22.967  -28.528  -11.257 1.00 28.64 ? 134 LEU   A C   1 
ATOM   1094  O  O   . LEU   A  1 134 ? 23.374  -29.409  -10.485 1.00 28.01 ? 134 LEU   A O   1 
ATOM   1095  C  CB  . LEU   A  1 134 ? 24.410  -27.481  -13.011 1.00 28.61 ? 134 LEU   A CB  1 
ATOM   1096  C  CG  . LEU   A  1 134 ? 25.065  -27.577  -14.395 1.00 30.47 ? 134 LEU   A CG  1 
ATOM   1097  C  CD1 . LEU   A  1 134 ? 25.824  -26.302  -14.774 1.00 32.12 ? 134 LEU   A CD1 1 
ATOM   1098  C  CD2 . LEU   A  1 134 ? 25.974  -28.788  -14.456 1.00 33.48 ? 134 LEU   A CD2 1 
ATOM   1099  N  N   . GLU   A  1 135 ? 22.276  -27.488  -10.822 1.00 26.55 ? 135 GLU   A N   1 
ATOM   1100  C  CA  . GLU   A  1 135 ? 21.796  -27.456  -9.445  1.00 31.34 ? 135 GLU   A CA  1 
ATOM   1101  C  C   . GLU   A  1 135 ? 21.023  -28.727  -9.119  1.00 28.51 ? 135 GLU   A C   1 
ATOM   1102  O  O   . GLU   A  1 135 ? 21.189  -29.322  -8.043  1.00 29.11 ? 135 GLU   A O   1 
ATOM   1103  C  CB  . GLU   A  1 135 ? 20.918  -26.223  -9.241  1.00 32.39 ? 135 GLU   A CB  1 
ATOM   1104  C  CG  . GLU   A  1 135 ? 21.672  -24.908  -9.306  1.00 27.39 ? 135 GLU   A CG  1 
ATOM   1105  C  CD  . GLU   A  1 135 ? 20.733  -23.708  -9.177  1.00 39.00 ? 135 GLU   A CD  1 
ATOM   1106  O  OE1 . GLU   A  1 135 ? 19.531  -23.848  -9.499  1.00 32.95 ? 135 GLU   A OE1 1 
ATOM   1107  O  OE2 . GLU   A  1 135 ? 21.185  -22.630  -8.744  1.00 36.48 ? 135 GLU   A OE2 1 
ATOM   1108  N  N   . THR   A  1 136 ? 20.185  -29.169  -10.052 1.00 29.58 ? 136 THR   A N   1 
ATOM   1109  C  CA  . THR   A  1 136 ? 19.356  -30.337  -9.789  1.00 30.98 ? 136 THR   A CA  1 
ATOM   1110  C  C   . THR   A  1 136 ? 20.212  -31.597  -9.668  1.00 26.43 ? 136 THR   A C   1 
ATOM   1111  O  O   . THR   A  1 136 ? 19.957  -32.445  -8.808  1.00 25.44 ? 136 THR   A O   1 
ATOM   1112  C  CB  . THR   A  1 136 ? 18.304  -30.481  -10.899 1.00 32.61 ? 136 THR   A CB  1 
ATOM   1113  O  OG1 . THR   A  1 136 ? 17.414  -29.355  -10.860 1.00 31.45 ? 136 THR   A OG1 1 
ATOM   1114  C  CG2 . THR   A  1 136 ? 17.515  -31.762  -10.720 1.00 30.42 ? 136 THR   A CG2 1 
ATOM   1115  N  N   . GLN   A  1 137 ? 21.234  -31.738  -10.518 1.00 24.74 ? 137 GLN   A N   1 
ATOM   1116  C  CA  . GLN   A  1 137 ? 22.089  -32.918  -10.426 1.00 23.93 ? 137 GLN   A CA  1 
ATOM   1117  C  C   . GLN   A  1 137 ? 22.820  -32.935  -9.095  1.00 27.67 ? 137 GLN   A C   1 
ATOM   1118  O  O   . GLN   A  1 137 ? 22.997  -33.995  -8.475  1.00 24.09 ? 137 GLN   A O   1 
ATOM   1119  C  CB  . GLN   A  1 137 ? 23.104  -32.947  -11.578 1.00 27.90 ? 137 GLN   A CB  1 
ATOM   1120  C  CG  . GLN   A  1 137 ? 22.519  -33.014  -13.011 1.00 27.78 ? 137 GLN   A CG  1 
ATOM   1121  C  CD  . GLN   A  1 137 ? 21.261  -33.831  -13.100 1.00 28.81 ? 137 GLN   A CD  1 
ATOM   1122  O  OE1 . GLN   A  1 137 ? 20.156  -33.297  -13.282 1.00 31.99 ? 137 GLN   A OE1 1 
ATOM   1123  N  NE2 . GLN   A  1 137 ? 21.416  -35.130  -13.005 1.00 27.86 ? 137 GLN   A NE2 1 
ATOM   1124  N  N   . LEU   A  1 138 ? 23.277  -31.762  -8.647  1.00 29.46 ? 138 LEU   A N   1 
ATOM   1125  C  CA  . LEU   A  1 138 ? 23.981  -31.706  -7.380  1.00 28.44 ? 138 LEU   A CA  1 
ATOM   1126  C  C   . LEU   A  1 138 ? 23.045  -32.062  -6.234  1.00 32.36 ? 138 LEU   A C   1 
ATOM   1127  O  O   . LEU   A  1 138 ? 23.436  -32.784  -5.305  1.00 30.76 ? 138 LEU   A O   1 
ATOM   1128  C  CB  . LEU   A  1 138 ? 24.622  -30.314  -7.213  1.00 28.10 ? 138 LEU   A CB  1 
ATOM   1129  C  CG  . LEU   A  1 138 ? 25.838  -30.135  -8.152  1.00 29.30 ? 138 LEU   A CG  1 
ATOM   1130  C  CD1 . LEU   A  1 138 ? 26.246  -28.690  -8.254  1.00 31.77 ? 138 LEU   A CD1 1 
ATOM   1131  C  CD2 . LEU   A  1 138 ? 27.045  -30.959  -7.694  1.00 33.48 ? 138 LEU   A CD2 1 
ATOM   1132  N  N   . GLY   A  1 139 ? 21.785  -31.630  -6.312  1.00 30.03 ? 139 GLY   A N   1 
ATOM   1133  C  CA  . GLY   A  1 139 ? 20.824  -32.012  -5.289  1.00 26.79 ? 139 GLY   A CA  1 
ATOM   1134  C  C   . GLY   A  1 139 ? 20.492  -33.491  -5.315  1.00 28.36 ? 139 GLY   A C   1 
ATOM   1135  O  O   . GLY   A  1 139 ? 20.349  -34.121  -4.261  1.00 31.35 ? 139 GLY   A O   1 
ATOM   1136  N  N   . LEU   A  1 140 ? 20.387  -34.070  -6.516  1.00 27.90 ? 140 LEU   A N   1 
ATOM   1137  C  CA  . LEU   A  1 140 ? 20.133  -35.504  -6.622  1.00 31.94 ? 140 LEU   A CA  1 
ATOM   1138  C  C   . LEU   A  1 140 ? 21.236  -36.304  -5.963  1.00 30.81 ? 140 LEU   A C   1 
ATOM   1139  O  O   . LEU   A  1 140 ? 20.963  -37.310  -5.301  1.00 26.77 ? 140 LEU   A O   1 
ATOM   1140  C  CB  . LEU   A  1 140 ? 20.003  -35.932  -8.082  1.00 24.78 ? 140 LEU   A CB  1 
ATOM   1141  C  CG  . LEU   A  1 140 ? 18.651  -35.588  -8.743  1.00 26.28 ? 140 LEU   A CG  1 
ATOM   1142  C  CD1 . LEU   A  1 140 ? 18.640  -35.843  -10.284 1.00 24.63 ? 140 LEU   A CD1 1 
ATOM   1143  C  CD2 . LEU   A  1 140 ? 17.519  -36.354  -8.057  1.00 28.52 ? 140 LEU   A CD2 1 
ATOM   1144  N  N   . ILE   A  1 141 ? 22.497  -35.900  -6.175  1.00 28.48 ? 141 ILE   A N   1 
ATOM   1145  C  CA  . ILE   A  1 141 ? 23.607  -36.597  -5.532  1.00 29.51 ? 141 ILE   A CA  1 
ATOM   1146  C  C   . ILE   A  1 141 ? 23.378  -36.655  -4.030  1.00 31.20 ? 141 ILE   A C   1 
ATOM   1147  O  O   . ILE   A  1 141 ? 23.553  -37.709  -3.406  1.00 30.05 ? 141 ILE   A O   1 
ATOM   1148  C  CB  . ILE   A  1 141 ? 24.946  -35.915  -5.883  1.00 35.46 ? 141 ILE   A CB  1 
ATOM   1149  C  CG1 . ILE   A  1 141 ? 25.348  -36.262  -7.329  1.00 36.43 ? 141 ILE   A CG1 1 
ATOM   1150  C  CG2 . ILE   A  1 141 ? 26.034  -36.302  -4.848  1.00 34.20 ? 141 ILE   A CG2 1 
ATOM   1151  C  CD1 . ILE   A  1 141 ? 26.565  -35.455  -7.904  1.00 37.35 ? 141 ILE   A CD1 1 
ATOM   1152  N  N   . GLN   A  1 142 ? 22.947  -35.531  -3.431  1.00 27.59 ? 142 GLN   A N   1 
ATOM   1153  C  CA  . GLN   A  1 142 ? 22.636  -35.518  -1.998  1.00 27.51 ? 142 GLN   A CA  1 
ATOM   1154  C  C   . GLN   A  1 142 ? 21.500  -36.466  -1.656  1.00 35.39 ? 142 GLN   A C   1 
ATOM   1155  O  O   . GLN   A  1 142 ? 21.559  -37.164  -0.645  1.00 33.99 ? 142 GLN   A O   1 
ATOM   1156  C  CB  . GLN   A  1 142 ? 22.260  -34.117  -1.517  1.00 31.71 ? 142 GLN   A CB  1 
ATOM   1157  C  CG  . GLN   A  1 142 ? 23.346  -33.072  -1.705  1.00 45.70 ? 142 GLN   A CG  1 
ATOM   1158  C  CD  . GLN   A  1 142 ? 24.598  -33.422  -0.935  1.00 50.19 ? 142 GLN   A CD  1 
ATOM   1159  O  OE1 . GLN   A  1 142 ? 24.530  -33.789  0.234   1.00 60.38 ? 142 GLN   A OE1 1 
ATOM   1160  N  NE2 . GLN   A  1 142 ? 25.745  -33.343  -1.597  1.00 52.45 ? 142 GLN   A NE2 1 
ATOM   1161  N  N   . LYS   A  1 143 ? 20.442  -36.484  -2.475  1.00 34.02 ? 143 LYS   A N   1 
ATOM   1162  C  CA  . LYS   A  1 143 ? 19.245  -37.229  -2.137  1.00 28.04 ? 143 LYS   A CA  1 
ATOM   1163  C  C   . LYS   A  1 143 ? 19.376  -38.722  -2.392  1.00 29.21 ? 143 LYS   A C   1 
ATOM   1164  O  O   . LYS   A  1 143 ? 18.827  -39.521  -1.623  1.00 27.03 ? 143 LYS   A O   1 
ATOM   1165  C  CB  . LYS   A  1 143 ? 18.041  -36.684  -2.932  1.00 25.72 ? 143 LYS   A CB  1 
ATOM   1166  C  CG  . LYS   A  1 143 ? 17.708  -35.224  -2.649  1.00 31.40 ? 143 LYS   A CG  1 
ATOM   1167  C  CD  . LYS   A  1 143 ? 16.528  -34.747  -3.498  1.00 41.64 ? 143 LYS   A CD  1 
ATOM   1168  C  CE  . LYS   A  1 143 ? 15.920  -33.434  -2.994  1.00 39.73 ? 143 LYS   A CE  1 
ATOM   1169  N  NZ  . LYS   A  1 143 ? 16.819  -32.284  -3.211  1.00 46.33 ? 143 LYS   A NZ  1 
ATOM   1170  N  N   . VAL   A  1 144 ? 19.958  -39.130  -3.527  1.00 22.68 ? 144 VAL   A N   1 
ATOM   1171  C  CA  . VAL   A  1 144 ? 20.057  -40.559  -3.814  1.00 28.07 ? 144 VAL   A CA  1 
ATOM   1172  C  C   . VAL   A  1 144 ? 21.423  -41.128  -3.462  1.00 31.63 ? 144 VAL   A C   1 
ATOM   1173  O  O   . VAL   A  1 144 ? 21.578  -42.361  -3.458  1.00 29.01 ? 144 VAL   A O   1 
ATOM   1174  C  CB  . VAL   A  1 144 ? 19.688  -40.880  -5.279  1.00 27.03 ? 144 VAL   A CB  1 
ATOM   1175  C  CG1 . VAL   A  1 144 ? 18.376  -40.154  -5.676  1.00 29.09 ? 144 VAL   A CG1 1 
ATOM   1176  C  CG2 . VAL   A  1 144 ? 20.806  -40.521  -6.272  1.00 23.81 ? 144 VAL   A CG2 1 
ATOM   1177  N  N   . GLY   A  1 145 ? 22.385  -40.288  -3.088  1.00 28.87 ? 145 GLY   A N   1 
ATOM   1178  C  CA  . GLY   A  1 145 ? 23.761  -40.739  -2.871  1.00 34.66 ? 145 GLY   A CA  1 
ATOM   1179  C  C   . GLY   A  1 145 ? 24.532  -40.836  -4.172  1.00 30.61 ? 145 GLY   A C   1 
ATOM   1180  O  O   . GLY   A  1 145 ? 23.975  -41.103  -5.239  1.00 25.73 ? 145 GLY   A O   1 
ATOM   1181  N  N   . LEU   A  1 146 ? 25.844  -40.606  -4.075  1.00 28.64 ? 146 LEU   A N   1 
ATOM   1182  C  CA  . LEU   A  1 146 ? 26.708  -40.554  -5.248  1.00 29.27 ? 146 LEU   A CA  1 
ATOM   1183  C  C   . LEU   A  1 146 ? 26.697  -41.867  -6.021  1.00 23.77 ? 146 LEU   A C   1 
ATOM   1184  O  O   . LEU   A  1 146 ? 26.623  -41.867  -7.257  1.00 27.82 ? 146 LEU   A O   1 
ATOM   1185  C  CB  . LEU   A  1 146 ? 28.140  -40.192  -4.812  1.00 32.35 ? 146 LEU   A CB  1 
ATOM   1186  C  CG  . LEU   A  1 146 ? 29.154  -39.985  -5.949  1.00 31.94 ? 146 LEU   A CG  1 
ATOM   1187  C  CD1 . LEU   A  1 146 ? 28.632  -38.934  -6.919  1.00 30.80 ? 146 LEU   A CD1 1 
ATOM   1188  C  CD2 . LEU   A  1 146 ? 30.605  -39.573  -5.468  1.00 31.56 ? 146 LEU   A CD2 1 
ATOM   1189  N  N   . GLU   A  1 147 ? 26.781  -43.000  -5.321  1.00 24.28 ? 147 GLU   A N   1 
ATOM   1190  C  CA  . GLU   A  1 147 ? 26.870  -44.281  -6.013  1.00 25.67 ? 147 GLU   A CA  1 
ATOM   1191  C  C   . GLU   A  1 147 ? 25.612  -44.563  -6.846  1.00 27.68 ? 147 GLU   A C   1 
ATOM   1192  O  O   . GLU   A  1 147 ? 25.708  -45.029  -7.994  1.00 25.31 ? 147 GLU   A O   1 
ATOM   1193  C  CB  . GLU   A  1 147 ? 27.135  -45.406  -5.010  1.00 34.55 ? 147 GLU   A CB  1 
ATOM   1194  C  CG  . GLU   A  1 147 ? 28.641  -45.479  -4.552  1.00 31.58 ? 147 GLU   A CG  1 
ATOM   1195  C  CD  . GLU   A  1 147 ? 28.965  -46.724  -3.677  1.00 53.34 ? 147 GLU   A CD  1 
ATOM   1196  O  OE1 . GLU   A  1 147 ? 28.048  -47.285  -3.032  1.00 47.05 ? 147 GLU   A OE1 1 
ATOM   1197  O  OE2 . GLU   A  1 147 ? 30.146  -47.151  -3.637  1.00 56.00 ? 147 GLU   A OE2 1 
ATOM   1198  N  N   . ASN   A  1 148 ? 24.428  -44.283  -6.291  1.00 26.81 ? 148 ASN   A N   1 
ATOM   1199  C  CA  . ASN   A  1 148 ? 23.194  -44.445  -7.065  1.00 24.89 ? 148 ASN   A CA  1 
ATOM   1200  C  C   . ASN   A  1 148 ? 23.116  -43.415  -8.190  1.00 23.15 ? 148 ASN   A C   1 
ATOM   1201  O  O   . ASN   A  1 148 ? 22.701  -43.738  -9.307  1.00 26.66 ? 148 ASN   A O   1 
ATOM   1202  C  CB  . ASN   A  1 148 ? 21.955  -44.335  -6.168  1.00 21.74 ? 148 ASN   A CB  1 
ATOM   1203  C  CG  . ASN   A  1 148 ? 21.603  -45.618  -5.432  1.00 29.01 ? 148 ASN   A CG  1 
ATOM   1204  O  OD1 . ASN   A  1 148 ? 22.191  -46.688  -5.625  1.00 26.40 ? 148 ASN   A OD1 1 
ATOM   1205  N  ND2 . ASN   A  1 148 ? 20.578  -45.511  -4.583  1.00 31.24 ? 148 ASN   A ND2 1 
ATOM   1206  N  N   . TYR   A  1 149 ? 23.501  -42.169  -7.923  1.00 22.62 ? 149 TYR   A N   1 
ATOM   1207  C  CA  . TYR   A  1 149 ? 23.476  -41.169  -8.983  1.00 24.95 ? 149 TYR   A CA  1 
ATOM   1208  C  C   . TYR   A  1 149 ? 24.352  -41.601  -10.160 1.00 27.35 ? 149 TYR   A C   1 
ATOM   1209  O  O   . TYR   A  1 149 ? 23.939  -41.522  -11.320 1.00 25.26 ? 149 TYR   A O   1 
ATOM   1210  C  CB  . TYR   A  1 149 ? 23.923  -39.811  -8.444  1.00 27.88 ? 149 TYR   A CB  1 
ATOM   1211  C  CG  . TYR   A  1 149 ? 23.908  -38.779  -9.514  1.00 31.72 ? 149 TYR   A CG  1 
ATOM   1212  C  CD1 . TYR   A  1 149 ? 22.734  -38.131  -9.843  1.00 28.92 ? 149 TYR   A CD1 1 
ATOM   1213  C  CD2 . TYR   A  1 149 ? 25.056  -38.477  -10.235 1.00 28.88 ? 149 TYR   A CD2 1 
ATOM   1214  C  CE1 . TYR   A  1 149 ? 22.696  -37.198  -10.847 1.00 27.73 ? 149 TYR   A CE1 1 
ATOM   1215  C  CE2 . TYR   A  1 149 ? 25.033  -37.536  -11.250 1.00 31.27 ? 149 TYR   A CE2 1 
ATOM   1216  C  CZ  . TYR   A  1 149 ? 23.848  -36.904  -11.558 1.00 28.80 ? 149 TYR   A CZ  1 
ATOM   1217  O  OH  . TYR   A  1 149 ? 23.774  -35.967  -12.560 1.00 30.00 ? 149 TYR   A OH  1 
ATOM   1218  N  N   . LEU   A  1 150 ? 25.571  -42.061  -9.878  1.00 25.59 ? 150 LEU   A N   1 
ATOM   1219  C  CA  . LEU   A  1 150 ? 26.452  -42.471  -10.968 1.00 24.01 ? 150 LEU   A CA  1 
ATOM   1220  C  C   . LEU   A  1 150 ? 25.899  -43.708  -11.659 1.00 22.83 ? 150 LEU   A C   1 
ATOM   1221  O  O   . LEU   A  1 150 ? 25.917  -43.797  -12.894 1.00 25.85 ? 150 LEU   A O   1 
ATOM   1222  C  CB  . LEU   A  1 150 ? 27.860  -42.739  -10.446 1.00 24.43 ? 150 LEU   A CB  1 
ATOM   1223  C  CG  . LEU   A  1 150 ? 28.595  -41.501  -9.925  1.00 26.27 ? 150 LEU   A CG  1 
ATOM   1224  C  CD1 . LEU   A  1 150 ? 30.013  -41.895  -9.439  1.00 36.20 ? 150 LEU   A CD1 1 
ATOM   1225  C  CD2 . LEU   A  1 150 ? 28.683  -40.406  -10.960 1.00 28.46 ? 150 LEU   A CD2 1 
ATOM   1226  N  N   . GLN   A  1 151 ? 25.386  -44.657  -10.870 1.00 24.98 ? 151 GLN   A N   1 
ATOM   1227  C  CA  . GLN   A  1 151 ? 24.752  -45.842  -11.433 1.00 19.85 ? 151 GLN   A CA  1 
ATOM   1228  C  C   . GLN   A  1 151 ? 23.668  -45.459  -12.434 1.00 23.81 ? 151 GLN   A C   1 
ATOM   1229  O  O   . GLN   A  1 151 ? 23.562  -46.059  -13.506 1.00 26.79 ? 151 GLN   A O   1 
ATOM   1230  C  CB  . GLN   A  1 151 ? 24.182  -46.710  -10.315 1.00 23.09 ? 151 GLN   A CB  1 
ATOM   1231  C  CG  . GLN   A  1 151 ? 23.377  -47.890  -10.825 1.00 23.13 ? 151 GLN   A CG  1 
ATOM   1232  C  CD  . GLN   A  1 151 ? 22.691  -48.682  -9.746  1.00 23.93 ? 151 GLN   A CD  1 
ATOM   1233  O  OE1 . GLN   A  1 151 ? 22.228  -48.138  -8.747  1.00 30.23 ? 151 GLN   A OE1 1 
ATOM   1234  N  NE2 . GLN   A  1 151 ? 22.607  -49.991  -9.953  1.00 26.38 ? 151 GLN   A NE2 1 
ATOM   1235  N  N   . SER   A  1 152 ? 22.846  -44.472  -12.086 1.00 26.65 ? 152 SER   A N   1 
ATOM   1236  C  CA  . SER   A  1 152 ? 21.750  -44.032  -12.940 1.00 25.75 ? 152 SER   A CA  1 
ATOM   1237  C  C   . SER   A  1 152 ? 22.242  -43.318  -14.190 1.00 28.31 ? 152 SER   A C   1 
ATOM   1238  O  O   . SER   A  1 152 ? 21.423  -42.971  -15.042 1.00 28.33 ? 152 SER   A O   1 
ATOM   1239  C  CB  . SER   A  1 152 ? 20.818  -43.115  -12.147 1.00 29.32 ? 152 SER   A CB  1 
ATOM   1240  O  OG  . SER   A  1 152 ? 20.152  -43.863  -11.150 1.00 26.54 ? 152 SER   A OG  1 
ATOM   1241  N  N   . HIS   A  1 153 ? 23.549  -43.076  -14.310 1.00 27.95 ? 153 HIS   A N   1 
ATOM   1242  C  CA  . HIS   A  1 153 ? 24.088  -42.383  -15.472 1.00 24.27 ? 153 HIS   A CA  1 
ATOM   1243  C  C   . HIS   A  1 153 ? 25.104  -43.232  -16.225 1.00 26.19 ? 153 HIS   A C   1 
ATOM   1244  O  O   . HIS   A  1 153 ? 25.841  -42.708  -17.060 1.00 28.69 ? 153 HIS   A O   1 
ATOM   1245  C  CB  . HIS   A  1 153 ? 24.657  -41.029  -15.045 1.00 25.14 ? 153 HIS   A CB  1 
ATOM   1246  C  CG  . HIS   A  1 153 ? 23.592  -40.038  -14.693 1.00 30.57 ? 153 HIS   A CG  1 
ATOM   1247  N  ND1 . HIS   A  1 153 ? 23.030  -39.975  -13.437 1.00 27.80 ? 153 HIS   A ND1 1 
ATOM   1248  C  CD2 . HIS   A  1 153 ? 22.938  -39.121  -15.447 1.00 31.99 ? 153 HIS   A CD2 1 
ATOM   1249  C  CE1 . HIS   A  1 153 ? 22.085  -39.044  -13.429 1.00 27.97 ? 153 HIS   A CE1 1 
ATOM   1250  N  NE2 . HIS   A  1 153 ? 22.019  -38.504  -14.630 1.00 29.95 ? 153 HIS   A NE2 1 
ATOM   1251  N  N   . MET   A  1 154 ? 25.125  -44.541  -15.975 1.00 31.51 ? 154 MET   A N   1 
ATOM   1252  C  CA  . MET   A  1 154 ? 25.994  -45.432  -16.737 1.00 36.18 ? 154 MET   A CA  1 
ATOM   1253  C  C   . MET   A  1 154 ? 25.512  -45.585  -18.180 1.00 39.23 ? 154 MET   A C   1 
ATOM   1254  O  O   . MET   A  1 154 ? 26.308  -45.492  -19.122 1.00 37.41 ? 154 MET   A O   1 
ATOM   1255  C  CB  . MET   A  1 154 ? 26.056  -46.805  -16.065 1.00 32.47 ? 154 MET   A CB  1 
ATOM   1256  C  CG  . MET   A  1 154 ? 26.921  -46.872  -14.828 1.00 40.08 ? 154 MET   A CG  1 
ATOM   1257  S  SD  . MET   A  1 154 ? 26.865  -48.506  -14.047 1.00 50.69 ? 154 MET   A SD  1 
ATOM   1258  C  CE  . MET   A  1 154 ? 27.059  -49.608  -15.456 1.00 47.50 ? 154 MET   A CE  1 
ATOM   1259  N  N   . HIS   A  1 155 ? 24.217  -45.850  -18.366 1.00 37.15 ? 155 HIS   A N   1 
ATOM   1260  C  CA  . HIS   A  1 155 ? 23.648  -46.204  -19.663 1.00 45.49 ? 155 HIS   A CA  1 
ATOM   1261  C  C   . HIS   A  1 155 ? 22.784  -45.065  -20.183 1.00 46.61 ? 155 HIS   A C   1 
ATOM   1262  O  O   . HIS   A  1 155 ? 22.091  -44.390  -19.410 1.00 47.28 ? 155 HIS   A O   1 
ATOM   1263  C  CB  . HIS   A  1 155 ? 22.775  -47.466  -19.579 1.00 48.55 ? 155 HIS   A CB  1 
ATOM   1264  C  CG  . HIS   A  1 155 ? 23.435  -48.642  -18.923 1.00 56.01 ? 155 HIS   A CG  1 
ATOM   1265  N  ND1 . HIS   A  1 155 ? 22.807  -49.396  -17.954 1.00 58.56 ? 155 HIS   A ND1 1 
ATOM   1266  C  CD2 . HIS   A  1 155 ? 24.646  -49.217  -19.121 1.00 61.33 ? 155 HIS   A CD2 1 
ATOM   1267  C  CE1 . HIS   A  1 155 ? 23.614  -50.369  -17.565 1.00 56.92 ? 155 HIS   A CE1 1 
ATOM   1268  N  NE2 . HIS   A  1 155 ? 24.736  -50.283  -18.257 1.00 50.49 ? 155 HIS   A NE2 1 
ATOM   1269  N  N   . GLU   A  1 156 ? 22.798  -44.870  -21.501 1.00 52.84 ? 156 GLU   A N   1 
ATOM   1270  C  CA  . GLU   A  1 156 ? 21.887  -43.896  -22.122 1.00 51.66 ? 156 GLU   A CA  1 
ATOM   1271  C  C   . GLU   A  1 156 ? 20.447  -44.415  -22.159 1.00 46.32 ? 156 GLU   A C   1 
ATOM   1272  O  O   . GLU   A  1 156 ? 20.209  -45.630  -22.130 1.00 54.07 ? 156 GLU   A O   1 
ATOM   1273  C  CB  . GLU   A  1 156 ? 22.339  -43.550  -23.533 1.00 51.36 ? 156 GLU   A CB  1 
ATOM   1274  C  CG  . GLU   A  1 156 ? 23.822  -43.454  -23.659 1.00 51.52 ? 156 GLU   A CG  1 
ATOM   1275  C  CD  . GLU   A  1 156 ? 24.257  -42.591  -24.819 1.00 67.50 ? 156 GLU   A CD  1 
ATOM   1276  O  OE1 . GLU   A  1 156 ? 23.380  -42.037  -25.518 1.00 65.77 ? 156 GLU   A OE1 1 
ATOM   1277  O  OE2 . GLU   A  1 156 ? 25.483  -42.469  -25.028 1.00 50.71 ? 156 GLU   A OE2 1 
ATOM   1278  N  N   . MET   B  1 1   ? 18.511  -21.558  -8.230  1.00 32.06 ? 1   MET   B N   1 
ATOM   1279  C  CA  . MET   B  1 1   ? 19.158  -20.221  -8.360  1.00 32.65 ? 1   MET   B CA  1 
ATOM   1280  C  C   . MET   B  1 1   ? 18.453  -19.216  -7.469  1.00 38.09 ? 1   MET   B C   1 
ATOM   1281  O  O   . MET   B  1 1   ? 17.273  -18.972  -7.652  1.00 40.92 ? 1   MET   B O   1 
ATOM   1282  C  CB  . MET   B  1 1   ? 19.106  -19.741  -9.813  1.00 41.51 ? 1   MET   B CB  1 
ATOM   1283  C  CG  . MET   B  1 1   ? 20.188  -18.693  -10.154 1.00 45.83 ? 1   MET   B CG  1 
ATOM   1284  S  SD  . MET   B  1 1   ? 20.146  -18.207  -11.885 1.00 41.61 ? 1   MET   B SD  1 
ATOM   1285  C  CE  . MET   B  1 1   ? 18.517  -17.478  -11.994 1.00 45.22 ? 1   MET   B CE  1 
ATOM   1286  N  N   . LYS   B  1 2   ? 19.161  -18.595  -6.535  1.00 36.83 ? 2   LYS   B N   1 
ATOM   1287  C  CA  . LYS   B  1 2   ? 18.499  -17.691  -5.600  1.00 43.22 ? 2   LYS   B CA  1 
ATOM   1288  C  C   . LYS   B  1 2   ? 17.955  -16.481  -6.345  1.00 36.52 ? 2   LYS   B C   1 
ATOM   1289  O  O   . LYS   B  1 2   ? 18.718  -15.735  -6.952  1.00 35.47 ? 2   LYS   B O   1 
ATOM   1290  C  CB  . LYS   B  1 2   ? 19.469  -17.245  -4.506  1.00 39.95 ? 2   LYS   B CB  1 
ATOM   1291  N  N   . GLY   B  1 3   ? 16.622  -16.301  -6.328  1.00 34.64 ? 3   GLY   B N   1 
ATOM   1292  C  CA  . GLY   B  1 3   ? 16.022  -15.159  -6.976  1.00 29.76 ? 3   GLY   B CA  1 
ATOM   1293  C  C   . GLY   B  1 3   ? 15.904  -13.923  -6.079  1.00 34.50 ? 3   GLY   B C   1 
ATOM   1294  O  O   . GLY   B  1 3   ? 16.038  -13.987  -4.862  1.00 35.48 ? 3   GLY   B O   1 
ATOM   1295  N  N   . ASP   B  1 4   ? 15.664  -12.780  -6.717  1.00 33.85 ? 4   ASP   B N   1 
ATOM   1296  C  CA  . ASP   B  1 4   ? 15.291  -11.565  -5.999  1.00 30.47 ? 4   ASP   B CA  1 
ATOM   1297  C  C   . ASP   B  1 4   ? 13.979  -11.765  -5.243  1.00 33.24 ? 4   ASP   B C   1 
ATOM   1298  O  O   . ASP   B  1 4   ? 12.956  -12.133  -5.827  1.00 31.17 ? 4   ASP   B O   1 
ATOM   1299  C  CB  . ASP   B  1 4   ? 15.158  -10.425  -7.005  1.00 30.47 ? 4   ASP   B CB  1 
ATOM   1300  C  CG  . ASP   B  1 4   ? 14.844  -9.098   -6.369  1.00 38.06 ? 4   ASP   B CG  1 
ATOM   1301  O  OD1 . ASP   B  1 4   ? 15.800  -8.413   -5.924  1.00 33.85 ? 4   ASP   B OD1 1 
ATOM   1302  O  OD2 . ASP   B  1 4   ? 13.648  -8.721   -6.370  1.00 35.55 ? 4   ASP   B OD2 1 
ATOM   1303  N  N   . LYS   B  1 5   ? 14.001  -11.488  -3.941  1.00 33.36 ? 5   LYS   B N   1 
ATOM   1304  C  CA  . LYS   B  1 5   ? 12.821  -11.705  -3.095  1.00 29.26 ? 5   LYS   B CA  1 
ATOM   1305  C  C   . LYS   B  1 5   ? 11.609  -10.939  -3.596  1.00 28.36 ? 5   LYS   B C   1 
ATOM   1306  O  O   . LYS   B  1 5   ? 10.483  -11.450  -3.593  1.00 32.15 ? 5   LYS   B O   1 
ATOM   1307  C  CB  . LYS   B  1 5   ? 13.116  -11.283  -1.654  1.00 39.93 ? 5   LYS   B CB  1 
ATOM   1308  C  CG  . LYS   B  1 5   ? 11.868  -11.304  -0.775  1.00 44.53 ? 5   LYS   B CG  1 
ATOM   1309  N  N   . LYS   B  1 6   ? 11.805  -9.696   -4.001  1.00 30.61 ? 6   LYS   B N   1 
ATOM   1310  C  CA  . LYS   B  1 6   ? 10.682  -8.923   -4.495  1.00 32.26 ? 6   LYS   B CA  1 
ATOM   1311  C  C   . LYS   B  1 6   ? 10.189  -9.441   -5.854  1.00 38.13 ? 6   LYS   B C   1 
ATOM   1312  O  O   . LYS   B  1 6   ? 8.982   -9.401   -6.127  1.00 33.59 ? 6   LYS   B O   1 
ATOM   1313  C  CB  . LYS   B  1 6   ? 11.074  -7.453   -4.573  1.00 35.87 ? 6   LYS   B CB  1 
ATOM   1314  C  CG  . LYS   B  1 6   ? 9.960   -6.559   -5.063  1.00 40.13 ? 6   LYS   B CG  1 
ATOM   1315  N  N   . VAL   B  1 7   ? 11.081  -9.942   -6.716  1.00 34.43 ? 7   VAL   B N   1 
ATOM   1316  C  CA  . VAL   B  1 7   ? 10.606  -10.593  -7.944  1.00 30.92 ? 7   VAL   B CA  1 
ATOM   1317  C  C   . VAL   B  1 7   ? 9.673   -11.757  -7.595  1.00 23.13 ? 7   VAL   B C   1 
ATOM   1318  O  O   . VAL   B  1 7   ? 8.571   -11.887  -8.142  1.00 30.74 ? 7   VAL   B O   1 
ATOM   1319  C  CB  . VAL   B  1 7   ? 11.786  -11.071  -8.805  1.00 31.13 ? 7   VAL   B CB  1 
ATOM   1320  C  CG1 . VAL   B  1 7   ? 11.289  -12.058  -9.855  1.00 27.10 ? 7   VAL   B CG1 1 
ATOM   1321  C  CG2 . VAL   B  1 7   ? 12.457  -9.918   -9.481  1.00 28.45 ? 7   VAL   B CG2 1 
ATOM   1322  N  N   . ILE   B  1 8   ? 10.098  -12.606  -6.660  1.00 26.26 ? 8   ILE   B N   1 
ATOM   1323  C  CA  . ILE   B  1 8   ? 9.285   -13.753  -6.252  1.00 33.03 ? 8   ILE   B CA  1 
ATOM   1324  C  C   . ILE   B  1 8   ? 7.928   -13.305  -5.722  1.00 34.06 ? 8   ILE   B C   1 
ATOM   1325  O  O   . ILE   B  1 8   ? 6.877   -13.896  -6.042  1.00 28.05 ? 8   ILE   B O   1 
ATOM   1326  C  CB  . ILE   B  1 8   ? 10.060  -14.581  -5.217  1.00 26.64 ? 8   ILE   B CB  1 
ATOM   1327  C  CG1 . ILE   B  1 8   ? 11.235  -15.241  -5.912  1.00 31.24 ? 8   ILE   B CG1 1 
ATOM   1328  C  CG2 . ILE   B  1 8   ? 9.134   -15.625  -4.518  1.00 28.22 ? 8   ILE   B CG2 1 
ATOM   1329  C  CD1 . ILE   B  1 8   ? 12.225  -15.903  -4.931  1.00 33.46 ? 8   ILE   B CD1 1 
ATOM   1330  N  N   . GLN   B  1 9   ? 7.925   -12.264  -4.901  1.00 30.74 ? 9   GLN   B N   1 
ATOM   1331  C  CA  . GLN   B  1 9   ? 6.665   -11.729  -4.415  1.00 29.18 ? 9   GLN   B CA  1 
ATOM   1332  C  C   . GLN   B  1 9   ? 5.774   -11.279  -5.568  1.00 25.58 ? 9   GLN   B C   1 
ATOM   1333  O  O   . GLN   B  1 9   ? 4.559   -11.508  -5.535  1.00 30.77 ? 9   GLN   B O   1 
ATOM   1334  C  CB  . GLN   B  1 9   ? 6.927   -10.583  -3.441  1.00 32.42 ? 9   GLN   B CB  1 
ATOM   1335  C  CG  . GLN   B  1 9   ? 7.572   -11.088  -2.139  1.00 38.75 ? 9   GLN   B CG  1 
ATOM   1336  C  CD  . GLN   B  1 9   ? 8.003   -9.968   -1.218  1.00 42.96 ? 9   GLN   B CD  1 
ATOM   1337  O  OE1 . GLN   B  1 9   ? 8.136   -8.832   -1.635  1.00 42.52 ? 9   GLN   B OE1 1 
ATOM   1338  N  NE2 . GLN   B  1 9   ? 8.204   -10.290  0.047   1.00 48.79 ? 9   GLN   B NE2 1 
ATOM   1339  N  N   . HIS   B  1 10  ? 6.355   -10.651  -6.595  1.00 28.40 ? 10  HIS   B N   1 
ATOM   1340  C  CA  . HIS   B  1 10  ? 5.575   -10.286  -7.778  1.00 31.26 ? 10  HIS   B CA  1 
ATOM   1341  C  C   . HIS   B  1 10  ? 5.019   -11.530  -8.466  1.00 24.32 ? 10  HIS   B C   1 
ATOM   1342  O  O   . HIS   B  1 10  ? 3.832   -11.590  -8.818  1.00 26.96 ? 10  HIS   B O   1 
ATOM   1343  C  CB  . HIS   B  1 10  ? 6.439   -9.493   -8.761  1.00 29.91 ? 10  HIS   B CB  1 
ATOM   1344  C  CG  . HIS   B  1 10  ? 6.464   -8.023   -8.507  1.00 30.32 ? 10  HIS   B CG  1 
ATOM   1345  N  ND1 . HIS   B  1 10  ? 5.355   -7.225   -8.677  1.00 34.22 ? 10  HIS   B ND1 1 
ATOM   1346  C  CD2 . HIS   B  1 10  ? 7.461   -7.204   -8.090  1.00 36.87 ? 10  HIS   B CD2 1 
ATOM   1347  C  CE1 . HIS   B  1 10  ? 5.667   -5.976   -8.376  1.00 40.35 ? 10  HIS   B CE1 1 
ATOM   1348  N  NE2 . HIS   B  1 10  ? 6.941   -5.935   -8.028  1.00 34.61 ? 10  HIS   B NE2 1 
ATOM   1349  N  N   . LEU   B  1 11  ? 5.894   -12.495  -8.745  1.00 31.00 ? 11  LEU   B N   1 
ATOM   1350  C  CA  . LEU   B  1 11  ? 5.458   -13.733  -9.382  1.00 26.03 ? 11  LEU   B CA  1 
ATOM   1351  C  C   . LEU   B  1 11  ? 4.311   -14.358  -8.604  1.00 31.60 ? 11  LEU   B C   1 
ATOM   1352  O  O   . LEU   B  1 11  ? 3.318   -14.807  -9.192  1.00 29.02 ? 11  LEU   B O   1 
ATOM   1353  C  CB  . LEU   B  1 11  ? 6.640   -14.705  -9.467  1.00 26.05 ? 11  LEU   B CB  1 
ATOM   1354  C  CG  . LEU   B  1 11  ? 7.736   -14.164  -10.380 1.00 28.24 ? 11  LEU   B CG  1 
ATOM   1355  C  CD1 . LEU   B  1 11  ? 8.850   -15.155  -10.475 1.00 30.11 ? 11  LEU   B CD1 1 
ATOM   1356  C  CD2 . LEU   B  1 11  ? 7.189   -13.834  -11.779 1.00 30.84 ? 11  LEU   B CD2 1 
ATOM   1357  N  N   . ASN   B  1 12  ? 4.426   -14.381  -7.273  1.00 26.91 ? 12  ASN   B N   1 
ATOM   1358  C  CA  . ASN   B  1 12  ? 3.353   -14.937  -6.459  1.00 29.96 ? 12  ASN   B CA  1 
ATOM   1359  C  C   . ASN   B  1 12  ? 2.066   -14.115  -6.569  1.00 32.31 ? 12  ASN   B C   1 
ATOM   1360  O  O   . ASN   B  1 12  ? 0.975   -14.688  -6.573  1.00 27.07 ? 12  ASN   B O   1 
ATOM   1361  C  CB  . ASN   B  1 12  ? 3.814   -15.077  -5.007  1.00 35.62 ? 12  ASN   B CB  1 
ATOM   1362  C  CG  . ASN   B  1 12  ? 4.264   -16.495  -4.693  1.00 30.47 ? 12  ASN   B CG  1 
ATOM   1363  O  OD1 . ASN   B  1 12  ? 3.752   -17.463  -5.279  1.00 31.01 ? 12  ASN   B OD1 1 
ATOM   1364  N  ND2 . ASN   B  1 12  ? 5.243   -16.628  -3.815  1.00 28.62 ? 12  ASN   B ND2 1 
ATOM   1365  N  N   . LYS   B  1 13  ? 2.161   -12.793  -6.714  1.00 31.43 ? 13  LYS   B N   1 
ATOM   1366  C  CA  . LYS   B  1 13  ? 0.957   -12.003  -6.945  1.00 32.16 ? 13  LYS   B CA  1 
ATOM   1367  C  C   . LYS   B  1 13  ? 0.305   -12.358  -8.279  1.00 33.74 ? 13  LYS   B C   1 
ATOM   1368  O  O   . LYS   B  1 13  ? -0.933  -12.459  -8.369  1.00 29.00 ? 13  LYS   B O   1 
ATOM   1369  C  CB  . LYS   B  1 13  ? 1.282   -10.509  -6.922  1.00 28.80 ? 13  LYS   B CB  1 
ATOM   1370  C  CG  . LYS   B  1 13  ? 0.034   -9.614   -6.891  1.00 34.97 ? 13  LYS   B CG  1 
ATOM   1371  C  CD  . LYS   B  1 13  ? 0.393   -8.110   -6.749  1.00 41.27 ? 13  LYS   B CD  1 
ATOM   1372  C  CE  . LYS   B  1 13  ? -0.880  -7.255   -6.633  1.00 41.08 ? 13  LYS   B CE  1 
ATOM   1373  N  NZ  . LYS   B  1 13  ? -0.609  -5.794   -6.530  1.00 49.36 ? 13  LYS   B NZ  1 
ATOM   1374  N  N   . ILE   B  1 14  ? 1.120   -12.492  -9.338  1.00 30.87 ? 14  ILE   B N   1 
ATOM   1375  C  CA  . ILE   B  1 14  ? 0.603   -12.862  -10.656 1.00 27.18 ? 14  ILE   B CA  1 
ATOM   1376  C  C   . ILE   B  1 14  ? -0.062  -14.221  -10.566 1.00 25.37 ? 14  ILE   B C   1 
ATOM   1377  O  O   . ILE   B  1 14  ? -1.181  -14.418  -11.046 1.00 28.49 ? 14  ILE   B O   1 
ATOM   1378  C  CB  . ILE   B  1 14  ? 1.740   -12.863  -11.705 1.00 29.81 ? 14  ILE   B CB  1 
ATOM   1379  C  CG1 . ILE   B  1 14  ? 2.467   -11.524  -11.732 1.00 24.68 ? 14  ILE   B CG1 1 
ATOM   1380  C  CG2 . ILE   B  1 14  ? 1.225   -13.147  -13.122 1.00 27.38 ? 14  ILE   B CG2 1 
ATOM   1381  C  CD1 . ILE   B  1 14  ? 1.553   -10.372  -11.875 1.00 32.07 ? 14  ILE   B CD1 1 
ATOM   1382  N  N   . LEU   B  1 15  ? 0.619   -15.172  -9.915  1.00 27.20 ? 15  LEU   B N   1 
ATOM   1383  C  CA  . LEU   B  1 15  ? 0.056   -16.501  -9.709  1.00 28.48 ? 15  LEU   B CA  1 
ATOM   1384  C  C   . LEU   B  1 15  ? -1.289  -16.401  -9.013  1.00 30.21 ? 15  LEU   B C   1 
ATOM   1385  O  O   . LEU   B  1 15  ? -2.259  -17.049  -9.417  1.00 27.67 ? 15  LEU   B O   1 
ATOM   1386  C  CB  . LEU   B  1 15  ? 1.022   -17.364  -8.891  1.00 25.45 ? 15  LEU   B CB  1 
ATOM   1387  C  CG  . LEU   B  1 15  ? 0.584   -18.778  -8.535  1.00 26.56 ? 15  LEU   B CG  1 
ATOM   1388  C  CD1 . LEU   B  1 15  ? 0.211   -19.599  -9.765  1.00 25.79 ? 15  LEU   B CD1 1 
ATOM   1389  C  CD2 . LEU   B  1 15  ? 1.687   -19.476  -7.768  1.00 25.35 ? 15  LEU   B CD2 1 
ATOM   1390  N  N   . GLY   B  1 16  ? -1.358  -15.603  -7.945  1.00 30.85 ? 16  GLY   B N   1 
ATOM   1391  C  CA  . GLY   B  1 16  ? -2.635  -15.379  -7.286  1.00 27.35 ? 16  GLY   B CA  1 
ATOM   1392  C  C   . GLY   B  1 16  ? -3.723  -14.962  -8.255  1.00 28.39 ? 16  GLY   B C   1 
ATOM   1393  O  O   . GLY   B  1 16  ? -4.850  -15.453  -8.173  1.00 30.74 ? 16  GLY   B O   1 
ATOM   1394  N  N   . ASN   B  1 17  ? -3.403  -14.039  -9.176  1.00 29.48 ? 17  ASN   B N   1 
ATOM   1395  C  CA  . ASN   B  1 17  ? -4.388  -13.603  -10.168 1.00 27.00 ? 17  ASN   B CA  1 
ATOM   1396  C  C   . ASN   B  1 17  ? -4.792  -14.754  -11.074 1.00 29.65 ? 17  ASN   B C   1 
ATOM   1397  O  O   . ASN   B  1 17  ? -5.967  -14.882  -11.454 1.00 29.85 ? 17  ASN   B O   1 
ATOM   1398  C  CB  . ASN   B  1 17  ? -3.828  -12.462  -11.026 1.00 30.84 ? 17  ASN   B CB  1 
ATOM   1399  C  CG  . ASN   B  1 17  ? -3.659  -11.157  -10.243 1.00 36.98 ? 17  ASN   B CG  1 
ATOM   1400  O  OD1 . ASN   B  1 17  ? -4.337  -10.928  -9.247  1.00 35.22 ? 17  ASN   B OD1 1 
ATOM   1401  N  ND2 . ASN   B  1 17  ? -2.744  -10.298  -10.700 1.00 30.11 ? 17  ASN   B ND2 1 
ATOM   1402  N  N   . GLU   B  1 18  ? -3.825  -15.604  -11.428 1.00 28.17 ? 18  GLU   B N   1 
ATOM   1403  C  CA  . GLU   B  1 18  ? -4.099  -16.735  -12.312 1.00 30.24 ? 18  GLU   B CA  1 
ATOM   1404  C  C   . GLU   B  1 18  ? -5.065  -17.696  -11.648 1.00 29.90 ? 18  GLU   B C   1 
ATOM   1405  O  O   . GLU   B  1 18  ? -5.966  -18.230  -12.295 1.00 28.67 ? 18  GLU   B O   1 
ATOM   1406  C  CB  . GLU   B  1 18  ? -2.796  -17.488  -12.655 1.00 28.86 ? 18  GLU   B CB  1 
ATOM   1407  C  CG  . GLU   B  1 18  ? -1.758  -16.715  -13.478 1.00 36.72 ? 18  GLU   B CG  1 
ATOM   1408  C  CD  . GLU   B  1 18  ? -2.232  -16.379  -14.843 1.00 45.79 ? 18  GLU   B CD  1 
ATOM   1409  O  OE1 . GLU   B  1 18  ? -3.261  -16.969  -15.257 1.00 48.88 ? 18  GLU   B OE1 1 
ATOM   1410  O  OE2 . GLU   B  1 18  ? -1.564  -15.545  -15.508 1.00 47.70 ? 18  GLU   B OE2 1 
ATOM   1411  N  N   . LEU   B  1 19  ? -4.858  -17.956  -10.351 1.00 29.31 ? 19  LEU   B N   1 
ATOM   1412  C  CA  . LEU   B  1 19  ? -5.712  -18.908  -9.644  1.00 27.86 ? 19  LEU   B CA  1 
ATOM   1413  C  C   . LEU   B  1 19  ? -7.152  -18.437  -9.620  1.00 31.12 ? 19  LEU   B C   1 
ATOM   1414  O  O   . LEU   B  1 19  ? -8.077  -19.234  -9.838  1.00 27.92 ? 19  LEU   B O   1 
ATOM   1415  C  CB  . LEU   B  1 19  ? -5.194  -19.124  -8.226  1.00 27.87 ? 19  LEU   B CB  1 
ATOM   1416  C  CG  . LEU   B  1 19  ? -3.762  -19.658  -8.215  1.00 40.46 ? 19  LEU   B CG  1 
ATOM   1417  C  CD1 . LEU   B  1 19  ? -3.123  -19.588  -6.816  1.00 34.95 ? 19  LEU   B CD1 1 
ATOM   1418  C  CD2 . LEU   B  1 19  ? -3.773  -21.074  -8.769  1.00 34.20 ? 19  LEU   B CD2 1 
ATOM   1419  N  N   . ILE   B  1 20  ? -7.364  -17.146  -9.360  1.00 27.58 ? 20  ILE   B N   1 
ATOM   1420  C  CA  . ILE   B  1 20  ? -8.709  -16.584  -9.484  1.00 24.92 ? 20  ILE   B CA  1 
ATOM   1421  C  C   . ILE   B  1 20  ? -9.258  -16.828  -10.884 1.00 22.27 ? 20  ILE   B C   1 
ATOM   1422  O  O   . ILE   B  1 20  ? -10.399 -17.269  -11.058 1.00 25.08 ? 20  ILE   B O   1 
ATOM   1423  C  CB  . ILE   B  1 20  ? -8.686  -15.086  -9.154  1.00 25.13 ? 20  ILE   B CB  1 
ATOM   1424  C  CG1 . ILE   B  1 20  ? -8.255  -14.903  -7.686  1.00 28.75 ? 20  ILE   B CG1 1 
ATOM   1425  C  CG2 . ILE   B  1 20  ? -10.013 -14.427  -9.426  1.00 27.56 ? 20  ILE   B CG2 1 
ATOM   1426  C  CD1 . ILE   B  1 20  ? -8.033  -13.463  -7.316  1.00 32.31 ? 20  ILE   B CD1 1 
ATOM   1427  N  N   . ALA   B  1 21  ? -8.475  -16.475  -11.902 1.00 22.36 ? 21  ALA   B N   1 
ATOM   1428  C  CA  . ALA   B  1 21  ? -8.961  -16.541  -13.271 1.00 23.40 ? 21  ALA   B CA  1 
ATOM   1429  C  C   . ALA   B  1 21  ? -9.277  -17.980  -13.678 1.00 28.27 ? 21  ALA   B C   1 
ATOM   1430  O  O   . ALA   B  1 21  ? -10.288 -18.233  -14.345 1.00 25.19 ? 21  ALA   B O   1 
ATOM   1431  C  CB  . ALA   B  1 21  ? -7.922  -15.918  -14.213 1.00 28.51 ? 21  ALA   B CB  1 
ATOM   1432  N  N   . ILE   B  1 22  ? -8.420  -18.936  -13.297 1.00 24.26 ? 22  ILE   B N   1 
ATOM   1433  C  CA  . ILE   B  1 22  ? -8.709  -20.344  -13.574 1.00 27.71 ? 22  ILE   B CA  1 
ATOM   1434  C  C   . ILE   B  1 22  ? -10.125 -20.692  -13.125 1.00 25.64 ? 22  ILE   B C   1 
ATOM   1435  O  O   . ILE   B  1 22  ? -10.934 -21.254  -13.887 1.00 24.05 ? 22  ILE   B O   1 
ATOM   1436  C  CB  . ILE   B  1 22  ? -7.669  -21.247  -12.890 1.00 24.70 ? 22  ILE   B CB  1 
ATOM   1437  C  CG1 . ILE   B  1 22  ? -6.311  -21.182  -13.626 1.00 24.88 ? 22  ILE   B CG1 1 
ATOM   1438  C  CG2 . ILE   B  1 22  ? -8.160  -22.702  -12.864 1.00 26.30 ? 22  ILE   B CG2 1 
ATOM   1439  C  CD1 . ILE   B  1 22  ? -5.118  -21.692  -12.771 1.00 27.81 ? 22  ILE   B CD1 1 
ATOM   1440  N  N   . ASN   B  1 23  ? -10.452 -20.346  -11.881 1.00 23.90 ? 23  ASN   B N   1 
ATOM   1441  C  CA  . ASN   B  1 23  ? -11.719 -20.784  -11.299 1.00 22.24 ? 23  ASN   B CA  1 
ATOM   1442  C  C   . ASN   B  1 23  ? -12.898 -19.973  -11.812 1.00 26.37 ? 23  ASN   B C   1 
ATOM   1443  O  O   . ASN   B  1 23  ? -13.970 -20.531  -12.063 1.00 22.82 ? 23  ASN   B O   1 
ATOM   1444  C  CB  . ASN   B  1 23  ? -11.644 -20.707  -9.785  1.00 24.05 ? 23  ASN   B CB  1 
ATOM   1445  C  CG  . ASN   B  1 23  ? -10.798 -21.829  -9.179  1.00 26.97 ? 23  ASN   B CG  1 
ATOM   1446  O  OD1 . ASN   B  1 23  ? -10.024 -22.511  -9.875  1.00 33.55 ? 23  ASN   B OD1 1 
ATOM   1447  N  ND2 . ASN   B  1 23  ? -10.910 -21.993  -7.861  1.00 29.43 ? 23  ASN   B ND2 1 
ATOM   1448  N  N   . GLN   B  1 24  ? -12.726 -18.660  -11.925 1.00 25.15 ? 24  GLN   B N   1 
ATOM   1449  C  CA  . GLN   B  1 24  ? -13.742 -17.811  -12.524 1.00 25.77 ? 24  GLN   B CA  1 
ATOM   1450  C  C   . GLN   B  1 24  ? -14.094 -18.257  -13.933 1.00 26.39 ? 24  GLN   B C   1 
ATOM   1451  O  O   . GLN   B  1 24  ? -15.283 -18.353  -14.277 1.00 25.09 ? 24  GLN   B O   1 
ATOM   1452  C  CB  . GLN   B  1 24  ? -13.254 -16.368  -12.552 1.00 24.09 ? 24  GLN   B CB  1 
ATOM   1453  C  CG  . GLN   B  1 24  ? -14.299 -15.368  -13.051 1.00 23.67 ? 24  GLN   B CG  1 
ATOM   1454  C  CD  . GLN   B  1 24  ? -13.858 -13.920  -12.820 1.00 26.87 ? 24  GLN   B CD  1 
ATOM   1455  O  OE1 . GLN   B  1 24  ? -13.404 -13.571  -11.738 1.00 28.79 ? 24  GLN   B OE1 1 
ATOM   1456  N  NE2 . GLN   B  1 24  ? -13.955 -13.096  -13.846 1.00 26.97 ? 24  GLN   B NE2 1 
ATOM   1457  N  N   . TYR   B  1 25  ? -13.074 -18.445  -14.794 1.00 28.74 ? 25  TYR   B N   1 
ATOM   1458  C  CA  . TYR   B  1 25  ? -13.334 -18.858  -16.174 1.00 27.27 ? 25  TYR   B CA  1 
ATOM   1459  C  C   . TYR   B  1 25  ? -13.911 -20.263  -16.217 1.00 24.04 ? 25  TYR   B C   1 
ATOM   1460  O  O   . TYR   B  1 25  ? -14.781 -20.548  -17.041 1.00 28.34 ? 25  TYR   B O   1 
ATOM   1461  C  CB  . TYR   B  1 25  ? -12.056 -18.765  -17.025 1.00 25.20 ? 25  TYR   B CB  1 
ATOM   1462  C  CG  . TYR   B  1 25  ? -11.470 -17.368  -17.054 1.00 30.59 ? 25  TYR   B CG  1 
ATOM   1463  C  CD1 . TYR   B  1 25  ? -12.188 -16.283  -16.548 1.00 30.33 ? 25  TYR   B CD1 1 
ATOM   1464  C  CD2 . TYR   B  1 25  ? -10.187 -17.139  -17.524 1.00 26.68 ? 25  TYR   B CD2 1 
ATOM   1465  C  CE1 . TYR   B  1 25  ? -11.644 -15.029  -16.510 1.00 27.69 ? 25  TYR   B CE1 1 
ATOM   1466  C  CE2 . TYR   B  1 25  ? -9.645  -15.904  -17.503 1.00 27.12 ? 25  TYR   B CE2 1 
ATOM   1467  C  CZ  . TYR   B  1 25  ? -10.348 -14.848  -16.990 1.00 33.61 ? 25  TYR   B CZ  1 
ATOM   1468  O  OH  . TYR   B  1 25  ? -9.749  -13.614  -16.964 1.00 32.70 ? 25  TYR   B OH  1 
ATOM   1469  N  N   . PHE   B  1 26  ? -13.459 -21.150  -15.330 1.00 25.72 ? 26  PHE   B N   1 
ATOM   1470  C  CA  . PHE   B  1 26  ? -13.973 -22.505  -15.386 1.00 22.87 ? 26  PHE   B CA  1 
ATOM   1471  C  C   . PHE   B  1 26  ? -15.451 -22.532  -14.989 1.00 21.52 ? 26  PHE   B C   1 
ATOM   1472  O  O   . PHE   B  1 26  ? -16.252 -23.210  -15.632 1.00 23.02 ? 26  PHE   B O   1 
ATOM   1473  C  CB  . PHE   B  1 26  ? -13.157 -23.469  -14.512 1.00 20.11 ? 26  PHE   B CB  1 
ATOM   1474  C  CG  . PHE   B  1 26  ? -13.271 -24.877  -14.989 1.00 24.86 ? 26  PHE   B CG  1 
ATOM   1475  C  CD1 . PHE   B  1 26  ? -14.331 -25.669  -14.587 1.00 23.78 ? 26  PHE   B CD1 1 
ATOM   1476  C  CD2 . PHE   B  1 26  ? -12.386 -25.372  -15.937 1.00 22.37 ? 26  PHE   B CD2 1 
ATOM   1477  C  CE1 . PHE   B  1 26  ? -14.496 -26.943  -15.094 1.00 26.97 ? 26  PHE   B CE1 1 
ATOM   1478  C  CE2 . PHE   B  1 26  ? -12.538 -26.656  -16.455 1.00 27.58 ? 26  PHE   B CE2 1 
ATOM   1479  C  CZ  . PHE   B  1 26  ? -13.592 -27.440  -16.045 1.00 23.33 ? 26  PHE   B CZ  1 
ATOM   1480  N  N   . LEU   B  1 27  ? -15.824 -21.779  -13.944 1.00 22.64 ? 27  LEU   B N   1 
ATOM   1481  C  CA  . LEU   B  1 27  ? -17.222 -21.716  -13.529 1.00 22.32 ? 27  LEU   B CA  1 
ATOM   1482  C  C   . LEU   B  1 27  ? -18.097 -21.072  -14.605 1.00 24.83 ? 27  LEU   B C   1 
ATOM   1483  O  O   . LEU   B  1 27  ? -19.178 -21.580  -14.916 1.00 23.24 ? 27  LEU   B O   1 
ATOM   1484  C  CB  . LEU   B  1 27  ? -17.334 -20.972  -12.195 1.00 23.23 ? 27  LEU   B CB  1 
ATOM   1485  C  CG  . LEU   B  1 27  ? -18.779 -20.817  -11.711 1.00 28.23 ? 27  LEU   B CG  1 
ATOM   1486  C  CD1 . LEU   B  1 27  ? -19.483 -22.195  -11.704 1.00 26.58 ? 27  LEU   B CD1 1 
ATOM   1487  C  CD2 . LEU   B  1 27  ? -18.849 -20.171  -10.333 1.00 36.00 ? 27  LEU   B CD2 1 
ATOM   1488  N  N   . HIS   B  1 28  ? -17.638 -19.962  -15.194 1.00 22.83 ? 28  HIS   B N   1 
ATOM   1489  C  CA  . HIS   B  1 28  ? -18.380 -19.323  -16.279 1.00 28.36 ? 28  HIS   B CA  1 
ATOM   1490  C  C   . HIS   B  1 28  ? -18.582 -20.273  -17.455 1.00 25.65 ? 28  HIS   B C   1 
ATOM   1491  O  O   . HIS   B  1 28  ? -19.674 -20.333  -18.048 1.00 23.47 ? 28  HIS   B O   1 
ATOM   1492  C  CB  . HIS   B  1 28  ? -17.642 -18.058  -16.723 1.00 25.56 ? 28  HIS   B CB  1 
ATOM   1493  C  CG  . HIS   B  1 28  ? -17.860 -16.876  -15.820 1.00 25.69 ? 28  HIS   B CG  1 
ATOM   1494  N  ND1 . HIS   B  1 28  ? -17.031 -15.769  -15.827 1.00 26.65 ? 28  HIS   B ND1 1 
ATOM   1495  C  CD2 . HIS   B  1 28  ? -18.812 -16.621  -14.888 1.00 27.58 ? 28  HIS   B CD2 1 
ATOM   1496  C  CE1 . HIS   B  1 28  ? -17.458 -14.889  -14.938 1.00 32.64 ? 28  HIS   B CE1 1 
ATOM   1497  N  NE2 . HIS   B  1 28  ? -18.543 -15.374  -14.359 1.00 24.83 ? 28  HIS   B NE2 1 
ATOM   1498  N  N   . SER   B  1 29  ? -17.535 -21.013  -17.820 1.00 23.05 ? 29  SER   B N   1 
ATOM   1499  C  CA  . SER   B  1 29  ? -17.639 -21.987  -18.902 1.00 22.10 ? 29  SER   B CA  1 
ATOM   1500  C  C   . SER   B  1 29  ? -18.741 -22.995  -18.619 1.00 27.44 ? 29  SER   B C   1 
ATOM   1501  O  O   . SER   B  1 29  ? -19.582 -23.286  -19.477 1.00 24.36 ? 29  SER   B O   1 
ATOM   1502  C  CB  . SER   B  1 29  ? -16.304 -22.715  -19.072 1.00 20.90 ? 29  SER   B CB  1 
ATOM   1503  O  OG  . SER   B  1 29  ? -16.450 -23.905  -19.842 1.00 25.90 ? 29  SER   B OG  1 
ATOM   1504  N  N   . ARG   B  1 30  ? -18.741 -23.545  -17.413 1.00 24.90 ? 30  ARG   B N   1 
ATOM   1505  C  CA  . ARG   B  1 30  ? -19.697 -24.589  -17.094 1.00 25.82 ? 30  ARG   B CA  1 
ATOM   1506  C  C   . ARG   B  1 30  ? -21.110 -24.029  -16.905 1.00 27.41 ? 30  ARG   B C   1 
ATOM   1507  O  O   . ARG   B  1 30  ? -22.079 -24.725  -17.188 1.00 23.46 ? 30  ARG   B O   1 
ATOM   1508  C  CB  . ARG   B  1 30  ? -19.216 -25.336  -15.859 1.00 24.93 ? 30  ARG   B CB  1 
ATOM   1509  C  CG  . ARG   B  1 30  ? -18.391 -26.571  -16.207 1.00 27.34 ? 30  ARG   B CG  1 
ATOM   1510  C  CD  . ARG   B  1 30  ? -17.228 -26.296  -17.218 1.00 25.18 ? 30  ARG   B CD  1 
ATOM   1511  N  NE  . ARG   B  1 30  ? -16.685 -27.556  -17.690 1.00 25.20 ? 30  ARG   B NE  1 
ATOM   1512  C  CZ  . ARG   B  1 30  ? -16.270 -27.807  -18.928 1.00 26.70 ? 30  ARG   B CZ  1 
ATOM   1513  N  NH1 . ARG   B  1 30  ? -16.323 -26.893  -19.880 1.00 26.95 ? 30  ARG   B NH1 1 
ATOM   1514  N  NH2 . ARG   B  1 30  ? -15.828 -29.025  -19.223 1.00 27.40 ? 30  ARG   B NH2 1 
ATOM   1515  N  N   . MET   B  1 31  ? -21.240 -22.770  -16.467 1.00 23.91 ? 31  MET   B N   1 
ATOM   1516  C  CA  . MET   B  1 31  ? -22.536 -22.108  -16.457 1.00 28.89 ? 31  MET   B CA  1 
ATOM   1517  C  C   . MET   B  1 31  ? -23.057 -21.951  -17.879 1.00 26.96 ? 31  MET   B C   1 
ATOM   1518  O  O   . MET   B  1 31  ? -24.209 -22.285  -18.173 1.00 24.53 ? 31  MET   B O   1 
ATOM   1519  C  CB  . MET   B  1 31  ? -22.418 -20.735  -15.781 1.00 25.75 ? 31  MET   B CB  1 
ATOM   1520  C  CG  . MET   B  1 31  ? -22.143 -20.743  -14.272 1.00 25.54 ? 31  MET   B CG  1 
ATOM   1521  S  SD  . MET   B  1 31  ? -21.661 -19.139  -13.581 1.00 27.68 ? 31  MET   B SD  1 
ATOM   1522  C  CE  . MET   B  1 31  ? -23.075 -18.092  -13.958 1.00 36.41 ? 31  MET   B CE  1 
ATOM   1523  N  N   . TRP   B  1 32  ? -22.203 -21.460  -18.791 1.00 25.31 ? 32  TRP   B N   1 
ATOM   1524  C  CA  . TRP   B  1 32  ? -22.638 -21.302  -20.175 1.00 25.46 ? 32  TRP   B CA  1 
ATOM   1525  C  C   . TRP   B  1 32  ? -23.050 -22.643  -20.760 1.00 26.92 ? 32  TRP   B C   1 
ATOM   1526  O  O   . TRP   B  1 32  ? -24.081 -22.735  -21.433 1.00 26.68 ? 32  TRP   B O   1 
ATOM   1527  C  CB  . TRP   B  1 32  ? -21.538 -20.607  -21.009 1.00 25.36 ? 32  TRP   B CB  1 
ATOM   1528  C  CG  . TRP   B  1 32  ? -21.603 -19.063  -20.921 1.00 22.69 ? 32  TRP   B CG  1 
ATOM   1529  C  CD1 . TRP   B  1 32  ? -22.749 -18.297  -20.919 1.00 28.36 ? 32  TRP   B CD1 1 
ATOM   1530  C  CD2 . TRP   B  1 32  ? -20.510 -18.129  -20.774 1.00 22.57 ? 32  TRP   B CD2 1 
ATOM   1531  N  NE1 . TRP   B  1 32  ? -22.434 -16.968  -20.810 1.00 26.44 ? 32  TRP   B NE1 1 
ATOM   1532  C  CE2 . TRP   B  1 32  ? -21.077 -16.830  -20.721 1.00 28.70 ? 32  TRP   B CE2 1 
ATOM   1533  C  CE3 . TRP   B  1 32  ? -19.118 -18.257  -20.708 1.00 24.76 ? 32  TRP   B CE3 1 
ATOM   1534  C  CZ2 . TRP   B  1 32  ? -20.306 -15.682  -20.605 1.00 26.28 ? 32  TRP   B CZ2 1 
ATOM   1535  C  CZ3 . TRP   B  1 32  ? -18.348 -17.104  -20.605 1.00 25.55 ? 32  TRP   B CZ3 1 
ATOM   1536  C  CH2 . TRP   B  1 32  ? -18.939 -15.839  -20.546 1.00 30.60 ? 32  TRP   B CH2 1 
ATOM   1537  N  N   . ASN   B  1 33  ? -22.288 -23.710  -20.491 1.00 22.95 ? 33  ASN   B N   1 
ATOM   1538  C  CA  . ASN   B  1 33  ? -22.681 -25.011  -21.030 1.00 22.60 ? 33  ASN   B CA  1 
ATOM   1539  C  C   . ASN   B  1 33  ? -24.040 -25.444  -20.471 1.00 24.13 ? 33  ASN   B C   1 
ATOM   1540  O  O   . ASN   B  1 33  ? -24.897 -25.950  -21.206 1.00 28.42 ? 33  ASN   B O   1 
ATOM   1541  C  CB  . ASN   B  1 33  ? -21.619 -26.070  -20.724 1.00 25.08 ? 33  ASN   B CB  1 
ATOM   1542  C  CG  . ASN   B  1 33  ? -20.411 -25.989  -21.657 1.00 27.62 ? 33  ASN   B CG  1 
ATOM   1543  O  OD1 . ASN   B  1 33  ? -20.450 -25.342  -22.702 1.00 28.02 ? 33  ASN   B OD1 1 
ATOM   1544  N  ND2 . ASN   B  1 33  ? -19.340 -26.655  -21.277 1.00 28.03 ? 33  ASN   B ND2 1 
ATOM   1545  N  N   . ASP   B  1 34  ? -24.244 -25.247  -19.172 1.00 25.93 ? 34  ASP   B N   1 
ATOM   1546  C  CA  . ASP   B  1 34  ? -25.507 -25.590  -18.541 1.00 26.70 ? 34  ASP   B CA  1 
ATOM   1547  C  C   . ASP   B  1 34  ? -26.665 -24.821  -19.187 1.00 28.47 ? 34  ASP   B C   1 
ATOM   1548  O  O   . ASP   B  1 34  ? -27.757 -25.367  -19.356 1.00 28.43 ? 34  ASP   B O   1 
ATOM   1549  C  CB  . ASP   B  1 34  ? -25.401 -25.292  -17.054 1.00 22.51 ? 34  ASP   B CB  1 
ATOM   1550  C  CG  . ASP   B  1 34  ? -26.733 -25.487  -16.287 1.00 31.92 ? 34  ASP   B CG  1 
ATOM   1551  O  OD1 . ASP   B  1 34  ? -27.399 -26.546  -16.354 1.00 30.91 ? 34  ASP   B OD1 1 
ATOM   1552  O  OD2 . ASP   B  1 34  ? -27.087 -24.539  -15.588 1.00 33.22 ? 34  ASP   B OD2 1 
ATOM   1553  N  N   . TRP   B  1 35  ? -26.434 -23.560  -19.581 1.00 28.37 ? 35  TRP   B N   1 
ATOM   1554  C  CA  . TRP   B  1 35  ? -27.492 -22.786  -20.229 1.00 29.52 ? 35  TRP   B CA  1 
ATOM   1555  C  C   . TRP   B  1 35  ? -27.654 -23.120  -21.712 1.00 30.96 ? 35  TRP   B C   1 
ATOM   1556  O  O   . TRP   B  1 35  ? -28.525 -22.532  -22.373 1.00 30.48 ? 35  TRP   B O   1 
ATOM   1557  C  CB  . TRP   B  1 35  ? -27.238 -21.292  -20.064 1.00 25.13 ? 35  TRP   B CB  1 
ATOM   1558  C  CG  . TRP   B  1 35  ? -27.169 -20.850  -18.634 1.00 27.33 ? 35  TRP   B CG  1 
ATOM   1559  C  CD1 . TRP   B  1 35  ? -27.623 -21.531  -17.521 1.00 35.81 ? 35  TRP   B CD1 1 
ATOM   1560  C  CD2 . TRP   B  1 35  ? -26.615 -19.625  -18.149 1.00 28.29 ? 35  TRP   B CD2 1 
ATOM   1561  N  NE1 . TRP   B  1 35  ? -27.373 -20.797  -16.388 1.00 35.72 ? 35  TRP   B NE1 1 
ATOM   1562  C  CE2 . TRP   B  1 35  ? -26.765 -19.622  -16.744 1.00 30.89 ? 35  TRP   B CE2 1 
ATOM   1563  C  CE3 . TRP   B  1 35  ? -26.018 -18.525  -18.766 1.00 33.48 ? 35  TRP   B CE3 1 
ATOM   1564  C  CZ2 . TRP   B  1 35  ? -26.319 -18.574  -15.952 1.00 34.22 ? 35  TRP   B CZ2 1 
ATOM   1565  C  CZ3 . TRP   B  1 35  ? -25.579 -17.485  -17.984 1.00 34.08 ? 35  TRP   B CZ3 1 
ATOM   1566  C  CH2 . TRP   B  1 35  ? -25.730 -17.512  -16.584 1.00 34.11 ? 35  TRP   B CH2 1 
ATOM   1567  N  N   . GLY   B  1 36  ? -26.885 -24.070  -22.243 1.00 25.03 ? 36  GLY   B N   1 
ATOM   1568  C  CA  . GLY   B  1 36  ? -26.970 -24.403  -23.647 1.00 27.00 ? 36  GLY   B CA  1 
ATOM   1569  C  C   . GLY   B  1 36  ? -26.231 -23.462  -24.569 1.00 26.99 ? 36  GLY   B C   1 
ATOM   1570  O  O   . GLY   B  1 36  ? -26.451 -23.513  -25.781 1.00 29.97 ? 36  GLY   B O   1 
ATOM   1571  N  N   . LEU   B  1 37  ? -25.370 -22.598  -24.034 1.00 23.40 ? 37  LEU   B N   1 
ATOM   1572  C  CA  . LEU   B  1 37  ? -24.557 -21.701  -24.852 1.00 27.04 ? 37  LEU   B CA  1 
ATOM   1573  C  C   . LEU   B  1 37  ? -23.153 -22.299  -25.033 1.00 25.97 ? 37  LEU   B C   1 
ATOM   1574  O  O   . LEU   B  1 37  ? -22.169 -21.829  -24.487 1.00 25.74 ? 37  LEU   B O   1 
ATOM   1575  C  CB  . LEU   B  1 37  ? -24.524 -20.327  -24.205 1.00 23.38 ? 37  LEU   B CB  1 
ATOM   1576  C  CG  . LEU   B  1 37  ? -25.924 -19.697  -24.099 1.00 26.84 ? 37  LEU   B CG  1 
ATOM   1577  C  CD1 . LEU   B  1 37  ? -26.015 -18.591  -23.039 1.00 31.12 ? 37  LEU   B CD1 1 
ATOM   1578  C  CD2 . LEU   B  1 37  ? -26.382 -19.146  -25.478 1.00 26.17 ? 37  LEU   B CD2 1 
ATOM   1579  N  N   . LYS   B  1 38  ? -23.096 -23.387  -25.808 1.00 27.46 ? 38  LYS   B N   1 
ATOM   1580  C  CA  . LYS   B  1 38  ? -21.910 -24.244  -25.827 1.00 28.36 ? 38  LYS   B CA  1 
ATOM   1581  C  C   . LYS   B  1 38  ? -20.698 -23.573  -26.473 1.00 27.37 ? 38  LYS   B C   1 
ATOM   1582  O  O   . LYS   B  1 38  ? -19.563 -23.937  -26.163 1.00 24.94 ? 38  LYS   B O   1 
ATOM   1583  C  CB  . LYS   B  1 38  ? -22.191 -25.548  -26.585 1.00 26.50 ? 38  LYS   B CB  1 
ATOM   1584  C  CG  . LYS   B  1 38  ? -23.471 -26.251  -26.205 1.00 38.95 ? 38  LYS   B CG  1 
ATOM   1585  C  CD  . LYS   B  1 38  ? -23.413 -26.807  -24.807 1.00 34.61 ? 38  LYS   B CD  1 
ATOM   1586  C  CE  . LYS   B  1 38  ? -24.519 -27.830  -24.655 1.00 47.60 ? 38  LYS   B CE  1 
ATOM   1587  N  NZ  . LYS   B  1 38  ? -24.364 -28.694  -23.507 1.00 39.77 ? 38  LYS   B NZ  1 
ATOM   1588  N  N   . ARG   B  1 39  ? -20.901 -22.666  -27.427 1.00 28.21 ? 39  ARG   B N   1 
ATOM   1589  C  CA  . ARG   B  1 39  ? -19.754 -21.994  -28.040 1.00 28.69 ? 39  ARG   B CA  1 
ATOM   1590  C  C   . ARG   B  1 39  ? -19.059 -21.090  -27.030 1.00 26.86 ? 39  ARG   B C   1 
ATOM   1591  O  O   . ARG   B  1 39  ? -17.828 -21.052  -26.960 1.00 25.36 ? 39  ARG   B O   1 
ATOM   1592  C  CB  . ARG   B  1 39  ? -20.200 -21.191  -29.262 1.00 29.37 ? 39  ARG   B CB  1 
ATOM   1593  C  CG  . ARG   B  1 39  ? -19.066 -20.847  -30.205 1.00 34.56 ? 39  ARG   B CG  1 
ATOM   1594  C  CD  . ARG   B  1 39  ? -19.468 -19.746  -31.175 1.00 45.12 ? 39  ARG   B CD  1 
ATOM   1595  N  NE  . ARG   B  1 39  ? -18.690 -19.835  -32.397 1.00 55.41 ? 39  ARG   B NE  1 
ATOM   1596  C  CZ  . ARG   B  1 39  ? -18.987 -20.650  -33.397 1.00 61.91 ? 39  ARG   B CZ  1 
ATOM   1597  N  NH1 . ARG   B  1 39  ? -20.049 -21.444  -33.352 1.00 60.54 ? 39  ARG   B NH1 1 
ATOM   1598  N  NH2 . ARG   B  1 39  ? -18.206 -20.665  -34.467 1.00 57.28 ? 39  ARG   B NH2 1 
ATOM   1599  N  N   . LEU   B  1 40  ? -19.838 -20.367  -26.223 1.00 25.64 ? 40  LEU   B N   1 
ATOM   1600  C  CA  . LEU   B  1 40  ? -19.258 -19.612  -25.116 1.00 25.68 ? 40  LEU   B CA  1 
ATOM   1601  C  C   . LEU   B  1 40  ? -18.612 -20.541  -24.092 1.00 24.25 ? 40  LEU   B C   1 
ATOM   1602  O  O   . LEU   B  1 40  ? -17.525 -20.253  -23.566 1.00 27.68 ? 40  LEU   B O   1 
ATOM   1603  C  CB  . LEU   B  1 40  ? -20.335 -18.770  -24.420 1.00 25.45 ? 40  LEU   B CB  1 
ATOM   1604  C  CG  . LEU   B  1 40  ? -20.592 -17.401  -25.033 1.00 27.81 ? 40  LEU   B CG  1 
ATOM   1605  C  CD1 . LEU   B  1 40  ? -21.917 -16.762  -24.509 1.00 30.55 ? 40  LEU   B CD1 1 
ATOM   1606  C  CD2 . LEU   B  1 40  ? -19.414 -16.471  -24.792 1.00 35.32 ? 40  LEU   B CD2 1 
ATOM   1607  N  N   . GLY   B  1 41  ? -19.294 -21.635  -23.761 1.00 25.79 ? 41  GLY   B N   1 
ATOM   1608  C  CA  . GLY   B  1 41  ? -18.737 -22.555  -22.791 1.00 25.84 ? 41  GLY   B CA  1 
ATOM   1609  C  C   . GLY   B  1 41  ? -17.393 -23.103  -23.236 1.00 22.79 ? 41  GLY   B C   1 
ATOM   1610  O  O   . GLY   B  1 41  ? -16.459 -23.192  -22.437 1.00 23.12 ? 41  GLY   B O   1 
ATOM   1611  N  N   . ALA   B  1 42  ? -17.275 -23.471  -24.518 1.00 28.39 ? 42  ALA   B N   1 
ATOM   1612  C  CA  . ALA   B  1 42  ? -16.023 -24.049  -25.020 1.00 28.59 ? 42  ALA   B CA  1 
ATOM   1613  C  C   . ALA   B  1 42  ? -14.910 -23.010  -25.069 1.00 28.17 ? 42  ALA   B C   1 
ATOM   1614  O  O   . ALA   B  1 42  ? -13.759 -23.288  -24.698 1.00 26.84 ? 42  ALA   B O   1 
ATOM   1615  C  CB  . ALA   B  1 42  ? -16.257 -24.654  -26.406 1.00 31.77 ? 42  ALA   B CB  1 
ATOM   1616  N  N   . HIS   B  1 43  ? -15.219 -21.809  -25.554 1.00 27.06 ? 43  HIS   B N   1 
ATOM   1617  C  CA  . HIS   B  1 43  ? -14.205 -20.770  -25.591 1.00 27.41 ? 43  HIS   B CA  1 
ATOM   1618  C  C   . HIS   B  1 43  ? -13.726 -20.428  -24.184 1.00 29.87 ? 43  HIS   B C   1 
ATOM   1619  O  O   . HIS   B  1 43  ? -12.518 -20.275  -23.941 1.00 25.27 ? 43  HIS   B O   1 
ATOM   1620  C  CB  . HIS   B  1 43  ? -14.744 -19.517  -26.294 1.00 24.34 ? 43  HIS   B CB  1 
ATOM   1621  C  CG  . HIS   B  1 43  ? -13.676 -18.518  -26.589 1.00 31.33 ? 43  HIS   B CG  1 
ATOM   1622  N  ND1 . HIS   B  1 43  ? -13.163 -18.326  -27.857 1.00 38.45 ? 43  HIS   B ND1 1 
ATOM   1623  C  CD2 . HIS   B  1 43  ? -12.959 -17.716  -25.768 1.00 31.41 ? 43  HIS   B CD2 1 
ATOM   1624  C  CE1 . HIS   B  1 43  ? -12.213 -17.411  -27.806 1.00 29.09 ? 43  HIS   B CE1 1 
ATOM   1625  N  NE2 . HIS   B  1 43  ? -12.058 -17.036  -26.550 1.00 32.07 ? 43  HIS   B NE2 1 
ATOM   1626  N  N   . GLU   B  1 44  ? -14.660 -20.312  -23.237 1.00 23.56 ? 44  GLU   B N   1 
ATOM   1627  C  CA  . GLU   B  1 44  ? -14.293 -19.965  -21.867 1.00 25.78 ? 44  GLU   B CA  1 
ATOM   1628  C  C   . GLU   B  1 44  ? -13.498 -21.092  -21.210 1.00 20.86 ? 44  GLU   B C   1 
ATOM   1629  O  O   . GLU   B  1 44  ? -12.580 -20.832  -20.431 1.00 24.32 ? 44  GLU   B O   1 
ATOM   1630  C  CB  . GLU   B  1 44  ? -15.554 -19.631  -21.074 1.00 22.37 ? 44  GLU   B CB  1 
ATOM   1631  C  CG  . GLU   B  1 44  ? -15.287 -19.099  -19.698 1.00 25.99 ? 44  GLU   B CG  1 
ATOM   1632  C  CD  . GLU   B  1 44  ? -14.951 -17.621  -19.704 1.00 31.49 ? 44  GLU   B CD  1 
ATOM   1633  O  OE1 . GLU   B  1 44  ? -14.658 -17.089  -20.794 1.00 31.40 ? 44  GLU   B OE1 1 
ATOM   1634  O  OE2 . GLU   B  1 44  ? -15.014 -16.993  -18.630 1.00 27.08 ? 44  GLU   B OE2 1 
ATOM   1635  N  N   . TYR   B  1 45  ? -13.829 -22.348  -21.530 1.00 24.55 ? 45  TYR   B N   1 
ATOM   1636  C  CA  . TYR   B  1 45  ? -13.011 -23.475  -21.085 1.00 25.23 ? 45  TYR   B CA  1 
ATOM   1637  C  C   . TYR   B  1 45  ? -11.560 -23.317  -21.545 1.00 23.36 ? 45  TYR   B C   1 
ATOM   1638  O  O   . TYR   B  1 45  ? -10.606 -23.482  -20.766 1.00 24.48 ? 45  TYR   B O   1 
ATOM   1639  C  CB  . TYR   B  1 45  ? -13.628 -24.763  -21.627 1.00 27.29 ? 45  TYR   B CB  1 
ATOM   1640  C  CG  . TYR   B  1 45  ? -12.778 -25.989  -21.445 1.00 24.34 ? 45  TYR   B CG  1 
ATOM   1641  C  CD1 . TYR   B  1 45  ? -12.809 -26.707  -20.253 1.00 32.98 ? 45  TYR   B CD1 1 
ATOM   1642  C  CD2 . TYR   B  1 45  ? -11.943 -26.436  -22.462 1.00 28.07 ? 45  TYR   B CD2 1 
ATOM   1643  C  CE1 . TYR   B  1 45  ? -12.011 -27.838  -20.071 1.00 31.30 ? 45  TYR   B CE1 1 
ATOM   1644  C  CE2 . TYR   B  1 45  ? -11.144 -27.559  -22.296 1.00 31.52 ? 45  TYR   B CE2 1 
ATOM   1645  C  CZ  . TYR   B  1 45  ? -11.188 -28.255  -21.097 1.00 34.57 ? 45  TYR   B CZ  1 
ATOM   1646  O  OH  . TYR   B  1 45  ? -10.404 -29.365  -20.918 1.00 37.57 ? 45  TYR   B OH  1 
ATOM   1647  N  N   . HIS   B  1 46  ? -11.368 -22.979  -22.818 1.00 25.98 ? 46  HIS   B N   1 
ATOM   1648  C  CA  . HIS   B  1 46  ? -10.012 -22.821  -23.335 1.00 29.06 ? 46  HIS   B CA  1 
ATOM   1649  C  C   . HIS   B  1 46  ? -9.280  -21.661  -22.656 1.00 26.46 ? 46  HIS   B C   1 
ATOM   1650  O  O   . HIS   B  1 46  ? -8.063  -21.738  -22.435 1.00 26.56 ? 46  HIS   B O   1 
ATOM   1651  C  CB  . HIS   B  1 46  ? -10.096 -22.684  -24.854 1.00 27.75 ? 46  HIS   B CB  1 
ATOM   1652  C  CG  . HIS   B  1 46  ? -10.497 -23.964  -25.518 1.00 33.61 ? 46  HIS   B CG  1 
ATOM   1653  N  ND1 . HIS   B  1 46  ? -9.780  -25.136  -25.362 1.00 38.41 ? 46  HIS   B ND1 1 
ATOM   1654  C  CD2 . HIS   B  1 46  ? -11.555 -24.274  -26.300 1.00 35.28 ? 46  HIS   B CD2 1 
ATOM   1655  C  CE1 . HIS   B  1 46  ? -10.380 -26.109  -26.025 1.00 37.12 ? 46  HIS   B CE1 1 
ATOM   1656  N  NE2 . HIS   B  1 46  ? -11.460 -25.614  -26.600 1.00 44.89 ? 46  HIS   B NE2 1 
ATOM   1657  N  N   . GLU   B  1 47  ? -10.000 -20.601  -22.276 1.00 27.67 ? 47  GLU   B N   1 
ATOM   1658  C  CA  . GLU   B  1 47  ? -9.385  -19.526  -21.504 1.00 26.19 ? 47  GLU   B CA  1 
ATOM   1659  C  C   . GLU   B  1 47  ? -8.915  -20.037  -20.137 1.00 25.28 ? 47  GLU   B C   1 
ATOM   1660  O  O   . GLU   B  1 47  ? -7.794  -19.730  -19.704 1.00 25.83 ? 47  GLU   B O   1 
ATOM   1661  C  CB  . GLU   B  1 47  ? -10.369 -18.360  -21.341 1.00 26.60 ? 47  GLU   B CB  1 
ATOM   1662  C  CG  . GLU   B  1 47  ? -10.877 -17.737  -22.672 1.00 35.75 ? 47  GLU   B CG  1 
ATOM   1663  C  CD  . GLU   B  1 47  ? -9.854  -16.865  -23.343 1.00 39.65 ? 47  GLU   B CD  1 
ATOM   1664  O  OE1 . GLU   B  1 47  ? -8.700  -16.919  -22.906 1.00 51.59 ? 47  GLU   B OE1 1 
ATOM   1665  O  OE2 . GLU   B  1 47  ? -10.191 -16.119  -24.294 1.00 46.06 ? 47  GLU   B OE2 1 
ATOM   1666  N  N   . SER   B  1 48  ? -9.752  -20.845  -19.460 1.00 24.67 ? 48  SER   B N   1 
ATOM   1667  C  CA  . SER   B  1 48  ? -9.368  -21.427  -18.180 1.00 25.54 ? 48  SER   B CA  1 
ATOM   1668  C  C   . SER   B  1 48  ? -8.092  -22.246  -18.330 1.00 25.48 ? 48  SER   B C   1 
ATOM   1669  O  O   . SER   B  1 48  ? -7.148  -22.114  -17.532 1.00 25.06 ? 48  SER   B O   1 
ATOM   1670  C  CB  . SER   B  1 48  ? -10.493 -22.311  -17.618 1.00 22.51 ? 48  SER   B CB  1 
ATOM   1671  O  OG  . SER   B  1 48  ? -10.168 -22.686  -16.283 1.00 27.25 ? 48  SER   B OG  1 
ATOM   1672  N  N   . ILE   B  1 49  ? -8.054  -23.091  -19.365 1.00 25.70 ? 49  ILE   B N   1 
ATOM   1673  C  CA  . ILE   B  1 49  ? -6.896  -23.935  -19.640 1.00 23.13 ? 49  ILE   B CA  1 
ATOM   1674  C  C   . ILE   B  1 49  ? -5.656  -23.066  -19.860 1.00 29.68 ? 49  ILE   B C   1 
ATOM   1675  O  O   . ILE   B  1 49  ? -4.572  -23.351  -19.328 1.00 23.33 ? 49  ILE   B O   1 
ATOM   1676  C  CB  . ILE   B  1 49  ? -7.169  -24.847  -20.858 1.00 27.00 ? 49  ILE   B CB  1 
ATOM   1677  C  CG1 . ILE   B  1 49  ? -8.278  -25.861  -20.597 1.00 30.30 ? 49  ILE   B CG1 1 
ATOM   1678  C  CG2 . ILE   B  1 49  ? -5.873  -25.577  -21.266 1.00 30.25 ? 49  ILE   B CG2 1 
ATOM   1679  C  CD1 . ILE   B  1 49  ? -8.011  -26.829  -19.540 1.00 29.55 ? 49  ILE   B CD1 1 
ATOM   1680  N  N   . ASP   B  1 50  ? -5.799  -21.981  -20.629 1.00 27.66 ? 50  ASP   B N   1 
ATOM   1681  C  CA  . ASP   B  1 50  ? -4.681  -21.073  -20.858 1.00 32.19 ? 50  ASP   B CA  1 
ATOM   1682  C  C   . ASP   B  1 50  ? -4.113  -20.555  -19.544 1.00 27.32 ? 50  ASP   B C   1 
ATOM   1683  O  O   . ASP   B  1 50  ? -2.892  -20.497  -19.361 1.00 26.41 ? 50  ASP   B O   1 
ATOM   1684  C  CB  . ASP   B  1 50  ? -5.117  -19.892  -21.736 1.00 35.57 ? 50  ASP   B CB  1 
ATOM   1685  C  CG  . ASP   B  1 50  ? -5.152  -20.225  -23.233 1.00 48.50 ? 50  ASP   B CG  1 
ATOM   1686  O  OD1 . ASP   B  1 50  ? -4.775  -21.350  -23.637 1.00 52.97 ? 50  ASP   B OD1 1 
ATOM   1687  O  OD2 . ASP   B  1 50  ? -5.560  -19.333  -24.011 1.00 56.75 ? 50  ASP   B OD2 1 
ATOM   1688  N  N   . GLU   B  1 51  ? -4.989  -20.136  -18.623 1.00 27.61 ? 51  GLU   B N   1 
ATOM   1689  C  CA  . GLU   B  1 51  ? -4.511  -19.616  -17.348 1.00 27.23 ? 51  GLU   B CA  1 
ATOM   1690  C  C   . GLU   B  1 51  ? -3.860  -20.714  -16.518 1.00 27.02 ? 51  GLU   B C   1 
ATOM   1691  O  O   . GLU   B  1 51  ? -2.896  -20.458  -15.786 1.00 23.19 ? 51  GLU   B O   1 
ATOM   1692  C  CB  . GLU   B  1 51  ? -5.658  -18.966  -16.573 1.00 32.88 ? 51  GLU   B CB  1 
ATOM   1693  C  CG  . GLU   B  1 51  ? -6.345  -17.808  -17.332 1.00 28.59 ? 51  GLU   B CG  1 
ATOM   1694  C  CD  . GLU   B  1 51  ? -5.377  -16.649  -17.628 1.00 38.81 ? 51  GLU   B CD  1 
ATOM   1695  O  OE1 . GLU   B  1 51  ? -4.767  -16.129  -16.692 1.00 48.41 ? 51  GLU   B OE1 1 
ATOM   1696  O  OE2 . GLU   B  1 51  ? -5.217  -16.256  -18.783 1.00 47.96 ? 51  GLU   B OE2 1 
ATOM   1697  N  N   . MET   B  1 52  ? -4.361  -21.935  -16.629 1.00 27.03 ? 52  MET   B N   1 
ATOM   1698  C  CA  . MET   B  1 52  ? -3.710  -23.060  -15.977 1.00 28.36 ? 52  MET   B CA  1 
ATOM   1699  C  C   . MET   B  1 52  ? -2.291  -23.245  -16.475 1.00 25.01 ? 52  MET   B C   1 
ATOM   1700  O  O   . MET   B  1 52  ? -1.383  -23.528  -15.689 1.00 25.82 ? 52  MET   B O   1 
ATOM   1701  C  CB  . MET   B  1 52  ? -4.505  -24.333  -16.222 1.00 21.88 ? 52  MET   B CB  1 
ATOM   1702  C  CG  . MET   B  1 52  ? -5.882  -24.332  -15.589 1.00 25.04 ? 52  MET   B CG  1 
ATOM   1703  S  SD  . MET   B  1 52  ? -6.751  -25.838  -16.042 1.00 25.53 ? 52  MET   B SD  1 
ATOM   1704  C  CE  . MET   B  1 52  ? -8.463  -25.322  -15.746 1.00 30.66 ? 52  MET   B CE  1 
ATOM   1705  N  N   . LYS   B  1 53  ? -2.077  -23.119  -17.789 1.00 23.11 ? 53  LYS   B N   1 
ATOM   1706  C  CA  . LYS   B  1 53  ? -0.716  -23.246  -18.305 1.00 26.72 ? 53  LYS   B CA  1 
ATOM   1707  C  C   . LYS   B  1 53  ? 0.179   -22.100  -17.817 1.00 28.03 ? 53  LYS   B C   1 
ATOM   1708  O  O   . LYS   B  1 53  ? 1.330   -22.333  -17.429 1.00 23.69 ? 53  LYS   B O   1 
ATOM   1709  C  CB  . LYS   B  1 53  ? -0.745  -23.322  -19.831 1.00 28.37 ? 53  LYS   B CB  1 
ATOM   1710  C  CG  . LYS   B  1 53  ? -1.321  -24.625  -20.393 1.00 26.59 ? 53  LYS   B CG  1 
ATOM   1711  C  CD  . LYS   B  1 53  ? -1.465  -24.516  -21.901 1.00 37.89 ? 53  LYS   B CD  1 
ATOM   1712  C  CE  . LYS   B  1 53  ? -2.128  -25.730  -22.546 1.00 56.74 ? 53  LYS   B CE  1 
ATOM   1713  N  NZ  . LYS   B  1 53  ? -2.781  -25.388  -23.877 1.00 57.81 ? 53  LYS   B NZ  1 
ATOM   1714  N  N   . HIS   B  1 54  ? -0.333  -20.863  -17.798 1.00 26.30 ? 54  HIS   B N   1 
ATOM   1715  C  CA  . HIS   B  1 54  ? 0.421   -19.762  -17.200 1.00 23.69 ? 54  HIS   B CA  1 
ATOM   1716  C  C   . HIS   B  1 54  ? 0.793   -20.059  -15.750 1.00 27.41 ? 54  HIS   B C   1 
ATOM   1717  O  O   . HIS   B  1 54  ? 1.937   -19.834  -15.333 1.00 26.07 ? 54  HIS   B O   1 
ATOM   1718  C  CB  . HIS   B  1 54  ? -0.361  -18.456  -17.228 1.00 28.78 ? 54  HIS   B CB  1 
ATOM   1719  C  CG  . HIS   B  1 54  ? -0.816  -18.038  -18.588 1.00 27.70 ? 54  HIS   B CG  1 
ATOM   1720  N  ND1 . HIS   B  1 54  ? -0.201  -18.446  -19.751 1.00 27.68 ? 54  HIS   B ND1 1 
ATOM   1721  C  CD2 . HIS   B  1 54  ? -1.849  -17.248  -18.964 1.00 22.44 ? 54  HIS   B CD2 1 
ATOM   1722  C  CE1 . HIS   B  1 54  ? -0.837  -17.924  -20.785 1.00 28.72 ? 54  HIS   B CE1 1 
ATOM   1723  N  NE2 . HIS   B  1 54  ? -1.839  -17.188  -20.332 1.00 30.16 ? 54  HIS   B NE2 1 
ATOM   1724  N  N   . ALA   B  1 55  ? -0.180  -20.495  -14.940 1.00 25.59 ? 55  ALA   B N   1 
ATOM   1725  C  CA  . ALA   B  1 55  ? 0.112   -20.791  -13.541 1.00 23.04 ? 55  ALA   B CA  1 
ATOM   1726  C  C   . ALA   B  1 55  ? 1.236   -21.821  -13.424 1.00 23.07 ? 55  ALA   B C   1 
ATOM   1727  O  O   . ALA   B  1 55  ? 2.158   -21.675  -12.604 1.00 21.40 ? 55  ALA   B O   1 
ATOM   1728  C  CB  . ALA   B  1 55  ? -1.160  -21.278  -12.839 1.00 25.77 ? 55  ALA   B CB  1 
ATOM   1729  N  N   . ASP   B  1 56  ? 1.169   -22.881  -14.234 1.00 24.31 ? 56  ASP   B N   1 
ATOM   1730  C  CA  . ASP   B  1 56  ? 2.246   -23.876  -14.258 1.00 27.26 ? 56  ASP   B CA  1 
ATOM   1731  C  C   . ASP   B  1 56  ? 3.620   -23.225  -14.476 1.00 30.53 ? 56  ASP   B C   1 
ATOM   1732  O  O   . ASP   B  1 56  ? 4.570   -23.458  -13.707 1.00 25.15 ? 56  ASP   B O   1 
ATOM   1733  C  CB  . ASP   B  1 56  ? 1.948   -24.901  -15.353 1.00 26.80 ? 56  ASP   B CB  1 
ATOM   1734  C  CG  . ASP   B  1 56  ? 2.910   -26.091  -15.344 1.00 24.93 ? 56  ASP   B CG  1 
ATOM   1735  O  OD1 . ASP   B  1 56  ? 3.619   -26.329  -14.350 1.00 26.16 ? 56  ASP   B OD1 1 
ATOM   1736  O  OD2 . ASP   B  1 56  ? 2.930   -26.821  -16.341 1.00 28.21 ? 56  ASP   B OD2 1 
ATOM   1737  N  N   . LYS   B  1 57  ? 3.736   -22.373  -15.495 1.00 23.19 ? 57  LYS   B N   1 
ATOM   1738  C  CA  . LYS   B  1 57  ? 5.028   -21.741  -15.760 1.00 28.22 ? 57  LYS   B CA  1 
ATOM   1739  C  C   . LYS   B  1 57  ? 5.466   -20.848  -14.599 1.00 25.45 ? 57  LYS   B C   1 
ATOM   1740  O  O   . LYS   B  1 57  ? 6.645   -20.836  -14.227 1.00 24.26 ? 57  LYS   B O   1 
ATOM   1741  C  CB  . LYS   B  1 57  ? 4.955   -20.957  -17.067 1.00 29.38 ? 57  LYS   B CB  1 
ATOM   1742  C  CG  . LYS   B  1 57  ? 4.796   -21.864  -18.283 1.00 30.86 ? 57  LYS   B CG  1 
ATOM   1743  C  CD  . LYS   B  1 57  ? 6.117   -22.559  -18.606 1.00 39.67 ? 57  LYS   B CD  1 
ATOM   1744  N  N   . LEU   B  1 58  ? 4.521   -20.141  -13.971 1.00 27.01 ? 58  LEU   B N   1 
ATOM   1745  C  CA  . LEU   B  1 58  ? 4.883   -19.300  -12.834 1.00 25.86 ? 58  LEU   B CA  1 
ATOM   1746  C  C   . LEU   B  1 58  ? 5.361   -20.139  -11.655 1.00 28.62 ? 58  LEU   B C   1 
ATOM   1747  O  O   . LEU   B  1 58  ? 6.356   -19.803  -11.004 1.00 25.97 ? 58  LEU   B O   1 
ATOM   1748  C  CB  . LEU   B  1 58  ? 3.707   -18.419  -12.423 1.00 23.71 ? 58  LEU   B CB  1 
ATOM   1749  C  CG  . LEU   B  1 58  ? 3.422   -17.276  -13.390 1.00 29.93 ? 58  LEU   B CG  1 
ATOM   1750  C  CD1 . LEU   B  1 58  ? 2.044   -16.708  -13.065 1.00 29.03 ? 58  LEU   B CD1 1 
ATOM   1751  C  CD2 . LEU   B  1 58  ? 4.466   -16.179  -13.364 1.00 34.12 ? 58  LEU   B CD2 1 
ATOM   1752  N  N   . ILE   B  1 59  ? 4.688   -21.255  -11.392 1.00 23.40 ? 59  ILE   B N   1 
ATOM   1753  C  CA  . ILE   B  1 59  ? 5.090   -22.127  -10.297 1.00 20.27 ? 59  ILE   B CA  1 
ATOM   1754  C  C   . ILE   B  1 59  ? 6.492   -22.656  -10.536 1.00 27.43 ? 59  ILE   B C   1 
ATOM   1755  O  O   . ILE   B  1 59  ? 7.347   -22.650  -9.637  1.00 25.76 ? 59  ILE   B O   1 
ATOM   1756  C  CB  . ILE   B  1 59  ? 4.062   -23.267  -10.143 1.00 24.85 ? 59  ILE   B CB  1 
ATOM   1757  C  CG1 . ILE   B  1 59  ? 2.748   -22.702  -9.599  1.00 27.86 ? 59  ILE   B CG1 1 
ATOM   1758  C  CG2 . ILE   B  1 59  ? 4.605   -24.369  -9.271  1.00 23.45 ? 59  ILE   B CG2 1 
ATOM   1759  C  CD1 . ILE   B  1 59  ? 1.564   -23.619  -9.838  1.00 23.14 ? 59  ILE   B CD1 1 
ATOM   1760  N  N   . GLU   B  1 60  ? 6.745   -23.105  -11.763 1.00 21.42 ? 60  GLU   B N   1 
ATOM   1761  C  CA  . GLU   B  1 60  ? 8.033   -23.661  -12.114 1.00 26.20 ? 60  GLU   B CA  1 
ATOM   1762  C  C   . GLU   B  1 60  ? 9.126   -22.617  -11.963 1.00 25.95 ? 60  GLU   B C   1 
ATOM   1763  O  O   . GLU   B  1 60  ? 10.197  -22.909  -11.435 1.00 24.58 ? 60  GLU   B O   1 
ATOM   1764  C  CB  . GLU   B  1 60  ? 7.990   -24.205  -13.549 1.00 28.89 ? 60  GLU   B CB  1 
ATOM   1765  C  CG  . GLU   B  1 60  ? 7.074   -25.462  -13.656 1.00 30.50 ? 60  GLU   B CG  1 
ATOM   1766  C  CD  . GLU   B  1 60  ? 6.862   -25.937  -15.085 1.00 34.47 ? 60  GLU   B CD  1 
ATOM   1767  O  OE1 . GLU   B  1 60  ? 6.819   -25.082  -15.988 1.00 30.71 ? 60  GLU   B OE1 1 
ATOM   1768  O  OE2 . GLU   B  1 60  ? 6.732   -27.154  -15.306 1.00 31.00 ? 60  GLU   B OE2 1 
ATOM   1769  N  N   . ARG   B  1 61  ? 8.862   -21.393  -12.416 1.00 26.39 ? 61  ARG   B N   1 
ATOM   1770  C  CA  . ARG   B  1 61  ? 9.845   -20.322  -12.283 1.00 24.75 ? 61  ARG   B CA  1 
ATOM   1771  C  C   . ARG   B  1 61  ? 10.111  -19.995  -10.812 1.00 29.61 ? 61  ARG   B C   1 
ATOM   1772  O  O   . ARG   B  1 61  ? 11.264  -19.810  -10.410 1.00 24.50 ? 61  ARG   B O   1 
ATOM   1773  C  CB  . ARG   B  1 61  ? 9.352   -19.084  -13.036 1.00 27.82 ? 61  ARG   B CB  1 
ATOM   1774  C  CG  . ARG   B  1 61  ? 10.291  -17.891  -12.996 1.00 32.68 ? 61  ARG   B CG  1 
ATOM   1775  C  CD  . ARG   B  1 61  ? 11.410  -18.095  -13.963 1.00 30.50 ? 61  ARG   B CD  1 
ATOM   1776  N  NE  . ARG   B  1 61  ? 12.428  -17.055  -13.889 1.00 27.73 ? 61  ARG   B NE  1 
ATOM   1777  C  CZ  . ARG   B  1 61  ? 13.665  -17.205  -14.329 1.00 30.23 ? 61  ARG   B CZ  1 
ATOM   1778  N  NH1 . ARG   B  1 61  ? 14.061  -18.336  -14.887 1.00 28.96 ? 61  ARG   B NH1 1 
ATOM   1779  N  NH2 . ARG   B  1 61  ? 14.536  -16.209  -14.175 1.00 29.31 ? 61  ARG   B NH2 1 
ATOM   1780  N  N   . ILE   B  1 62  ? 9.056   -19.887  -9.999  1.00 28.18 ? 62  ILE   B N   1 
ATOM   1781  C  CA  . ILE   B  1 62  ? 9.245   -19.579  -8.579  1.00 28.28 ? 62  ILE   B CA  1 
ATOM   1782  C  C   . ILE   B  1 62  ? 10.103  -20.646  -7.893  1.00 29.37 ? 62  ILE   B C   1 
ATOM   1783  O  O   . ILE   B  1 62  ? 11.018  -20.328  -7.117  1.00 26.72 ? 62  ILE   B O   1 
ATOM   1784  C  CB  . ILE   B  1 62  ? 7.877   -19.400  -7.890  1.00 28.58 ? 62  ILE   B CB  1 
ATOM   1785  C  CG1 . ILE   B  1 62  ? 7.190   -18.132  -8.377  1.00 25.78 ? 62  ILE   B CG1 1 
ATOM   1786  C  CG2 . ILE   B  1 62  ? 8.039   -19.366  -6.366  1.00 27.64 ? 62  ILE   B CG2 1 
ATOM   1787  C  CD1 . ILE   B  1 62  ? 5.668   -18.101  -8.038  1.00 27.58 ? 62  ILE   B CD1 1 
ATOM   1788  N  N   . LEU   B  1 63  ? 9.844   -21.922  -8.177  1.00 26.99 ? 63  LEU   B N   1 
ATOM   1789  C  CA  . LEU   B  1 63  ? 10.664  -22.989  -7.600  1.00 26.76 ? 63  LEU   B CA  1 
ATOM   1790  C  C   . LEU   B  1 63  ? 12.116  -22.923  -8.090  1.00 29.15 ? 63  LEU   B C   1 
ATOM   1791  O  O   . LEU   B  1 63  ? 13.047  -23.091  -7.303  1.00 27.84 ? 63  LEU   B O   1 
ATOM   1792  C  CB  . LEU   B  1 63  ? 10.053  -24.350  -7.923  1.00 22.19 ? 63  LEU   B CB  1 
ATOM   1793  C  CG  . LEU   B  1 63  ? 8.715   -24.656  -7.203  1.00 29.76 ? 63  LEU   B CG  1 
ATOM   1794  C  CD1 . LEU   B  1 63  ? 8.047   -25.900  -7.840  1.00 27.08 ? 63  LEU   B CD1 1 
ATOM   1795  C  CD2 . LEU   B  1 63  ? 8.930   -24.843  -5.689  1.00 25.48 ? 63  LEU   B CD2 1 
ATOM   1796  N  N   . PHE   B  1 64  ? 12.330  -22.689  -9.382  1.00 24.40 ? 64  PHE   B N   1 
ATOM   1797  C  CA  . PHE   B  1 64  ? 13.696  -22.505  -9.857  1.00 31.86 ? 64  PHE   B CA  1 
ATOM   1798  C  C   . PHE   B  1 64  ? 14.412  -21.413  -9.062  1.00 31.96 ? 64  PHE   B C   1 
ATOM   1799  O  O   . PHE   B  1 64  ? 15.586  -21.552  -8.720  1.00 26.47 ? 64  PHE   B O   1 
ATOM   1800  C  CB  . PHE   B  1 64  ? 13.696  -22.164  -11.351 1.00 33.17 ? 64  PHE   B CB  1 
ATOM   1801  C  CG  . PHE   B  1 64  ? 15.035  -21.733  -11.865 1.00 25.55 ? 64  PHE   B CG  1 
ATOM   1802  C  CD1 . PHE   B  1 64  ? 16.117  -22.585  -11.783 1.00 31.93 ? 64  PHE   B CD1 1 
ATOM   1803  C  CD2 . PHE   B  1 64  ? 15.217  -20.475  -12.423 1.00 31.78 ? 64  PHE   B CD2 1 
ATOM   1804  C  CE1 . PHE   B  1 64  ? 17.359  -22.196  -12.258 1.00 31.01 ? 64  PHE   B CE1 1 
ATOM   1805  C  CE2 . PHE   B  1 64  ? 16.471  -20.076  -12.891 1.00 32.59 ? 64  PHE   B CE2 1 
ATOM   1806  C  CZ  . PHE   B  1 64  ? 17.532  -20.945  -12.818 1.00 29.13 ? 64  PHE   B CZ  1 
ATOM   1807  N  N   . LEU   B  1 65  ? 13.724  -20.323  -8.766  1.00 28.07 ? 65  LEU   B N   1 
ATOM   1808  C  CA  . LEU   B  1 65  ? 14.315  -19.204  -8.049  1.00 29.71 ? 65  LEU   B CA  1 
ATOM   1809  C  C   . LEU   B  1 65  ? 14.324  -19.421  -6.541  1.00 32.21 ? 65  LEU   B C   1 
ATOM   1810  O  O   . LEU   B  1 65  ? 14.623  -18.493  -5.785  1.00 28.35 ? 65  LEU   B O   1 
ATOM   1811  C  CB  . LEU   B  1 65  ? 13.566  -17.913  -8.404  1.00 24.57 ? 65  LEU   B CB  1 
ATOM   1812  C  CG  . LEU   B  1 65  ? 13.642  -17.470  -9.869  1.00 26.52 ? 65  LEU   B CG  1 
ATOM   1813  C  CD1 . LEU   B  1 65  ? 12.844  -16.214  -10.088 1.00 30.21 ? 65  LEU   B CD1 1 
ATOM   1814  C  CD2 . LEU   B  1 65  ? 15.060  -17.224  -10.317 1.00 27.18 ? 65  LEU   B CD2 1 
ATOM   1815  N  N   . GLU   B  1 66  ? 13.975  -20.617  -6.092  1.00 31.29 ? 66  GLU   B N   1 
ATOM   1816  C  CA  . GLU   B  1 66  ? 14.088  -21.006  -4.696  1.00 33.15 ? 66  GLU   B CA  1 
ATOM   1817  C  C   . GLU   B  1 66  ? 13.064  -20.276  -3.827  1.00 32.70 ? 66  GLU   B C   1 
ATOM   1818  O  O   . GLU   B  1 66  ? 13.262  -20.125  -2.632  1.00 32.00 ? 66  GLU   B O   1 
ATOM   1819  C  CB  . GLU   B  1 66  ? 15.535  -20.810  -4.196  1.00 32.49 ? 66  GLU   B CB  1 
ATOM   1820  C  CG  . GLU   B  1 66  ? 16.500  -21.590  -5.089  1.00 28.51 ? 66  GLU   B CG  1 
ATOM   1821  C  CD  . GLU   B  1 66  ? 17.948  -21.655  -4.651  1.00 41.80 ? 66  GLU   B CD  1 
ATOM   1822  O  OE1 . GLU   B  1 66  ? 18.232  -21.357  -3.490  1.00 38.24 ? 66  GLU   B OE1 1 
ATOM   1823  O  OE2 . GLU   B  1 66  ? 18.810  -22.022  -5.493  1.00 33.36 ? 66  GLU   B OE2 1 
ATOM   1824  N  N   . GLY   B  1 67  ? 11.954  -19.841  -4.428  1.00 28.78 ? 67  GLY   B N   1 
ATOM   1825  C  CA  . GLY   B  1 67  ? 10.823  -19.317  -3.699  1.00 30.97 ? 67  GLY   B CA  1 
ATOM   1826  C  C   . GLY   B  1 67  ? 9.768   -20.384  -3.426  1.00 31.39 ? 67  GLY   B C   1 
ATOM   1827  O  O   . GLY   B  1 67  ? 9.876   -21.534  -3.845  1.00 32.63 ? 67  GLY   B O   1 
ATOM   1828  N  N   . LEU   B  1 68  ? 8.736   -19.978  -2.681  1.00 25.06 ? 68  LEU   B N   1 
ATOM   1829  C  CA  . LEU   B  1 68  ? 7.617   -20.859  -2.353  1.00 31.83 ? 68  LEU   B CA  1 
ATOM   1830  C  C   . LEU   B  1 68  ? 6.363   -20.405  -3.102  1.00 32.46 ? 68  LEU   B C   1 
ATOM   1831  O  O   . LEU   B  1 68  ? 5.799   -19.344  -2.779  1.00 27.37 ? 68  LEU   B O   1 
ATOM   1832  C  CB  . LEU   B  1 68  ? 7.365   -20.871  -0.841  1.00 32.43 ? 68  LEU   B CB  1 
ATOM   1833  C  CG  . LEU   B  1 68  ? 8.481   -21.480  0.034   1.00 49.41 ? 68  LEU   B CG  1 
ATOM   1834  C  CD1 . LEU   B  1 68  ? 8.218   -21.245  1.522   1.00 57.37 ? 68  LEU   B CD1 1 
ATOM   1835  C  CD2 . LEU   B  1 68  ? 8.658   -22.967  -0.212  1.00 48.22 ? 68  LEU   B CD2 1 
ATOM   1836  N  N   . PRO   B  1 69  ? 5.898   -21.146  -4.106  1.00 30.09 ? 69  PRO   B N   1 
ATOM   1837  C  CA  . PRO   B  1 69  ? 4.707   -20.719  -4.837  1.00 29.24 ? 69  PRO   B CA  1 
ATOM   1838  C  C   . PRO   B  1 69  ? 3.496   -20.751  -3.916  1.00 28.53 ? 69  PRO   B C   1 
ATOM   1839  O  O   . PRO   B  1 69  ? 3.322   -21.683  -3.128  1.00 31.48 ? 69  PRO   B O   1 
ATOM   1840  C  CB  . PRO   B  1 69  ? 4.579   -21.762  -5.957  1.00 27.16 ? 69  PRO   B CB  1 
ATOM   1841  C  CG  . PRO   B  1 69  ? 5.798   -22.586  -5.891  1.00 26.93 ? 69  PRO   B CG  1 
ATOM   1842  C  CD  . PRO   B  1 69  ? 6.316   -22.493  -4.513  1.00 27.27 ? 69  PRO   B CD  1 
ATOM   1843  N  N   . ASN   B  1 70  ? 2.667   -19.726  -4.011  1.00 28.09 ? 70  ASN   B N   1 
ATOM   1844  C  CA  . ASN   B  1 70  ? 1.486   -19.604  -3.163  1.00 28.83 ? 70  ASN   B CA  1 
ATOM   1845  C  C   . ASN   B  1 70  ? 0.265   -20.115  -3.915  1.00 22.09 ? 70  ASN   B C   1 
ATOM   1846  O  O   . ASN   B  1 70  ? -0.317  -19.395  -4.724  1.00 25.36 ? 70  ASN   B O   1 
ATOM   1847  C  CB  . ASN   B  1 70  ? 1.305   -18.157  -2.725  1.00 29.51 ? 70  ASN   B CB  1 
ATOM   1848  C  CG  . ASN   B  1 70  ? 0.271   -18.005  -1.639  1.00 33.85 ? 70  ASN   B CG  1 
ATOM   1849  O  OD1 . ASN   B  1 70  ? -0.600  -18.862  -1.448  1.00 29.41 ? 70  ASN   B OD1 1 
ATOM   1850  N  ND2 . ASN   B  1 70  ? 0.348   -16.896  -0.922  1.00 30.79 ? 70  ASN   B ND2 1 
ATOM   1851  N  N   . LEU   B  1 71  ? -0.131  -21.356  -3.633  1.00 27.07 ? 71  LEU   B N   1 
ATOM   1852  C  CA  . LEU   B  1 71  ? -1.372  -21.925  -4.137  1.00 31.23 ? 71  LEU   B CA  1 
ATOM   1853  C  C   . LEU   B  1 71  ? -2.450  -21.989  -3.059  1.00 28.18 ? 71  LEU   B C   1 
ATOM   1854  O  O   . LEU   B  1 71  ? -3.473  -22.643  -3.258  1.00 27.32 ? 71  LEU   B O   1 
ATOM   1855  C  CB  . LEU   B  1 71  ? -1.152  -23.331  -4.699  1.00 25.30 ? 71  LEU   B CB  1 
ATOM   1856  C  CG  . LEU   B  1 71  ? -0.469  -23.365  -6.079  1.00 32.76 ? 71  LEU   B CG  1 
ATOM   1857  C  CD1 . LEU   B  1 71  ? 0.996   -23.100  -5.933  1.00 37.98 ? 71  LEU   B CD1 1 
ATOM   1858  C  CD2 . LEU   B  1 71  ? -0.703  -24.734  -6.715  1.00 33.97 ? 71  LEU   B CD2 1 
ATOM   1859  N  N   . GLN   B  1 72  ? -2.223  -21.351  -1.921  1.00 29.90 ? 72  GLN   B N   1 
ATOM   1860  C  CA  . GLN   B  1 72  ? -3.125  -21.422  -0.773  1.00 33.89 ? 72  GLN   B CA  1 
ATOM   1861  C  C   . GLN   B  1 72  ? -4.119  -20.277  -0.730  1.00 27.77 ? 72  GLN   B C   1 
ATOM   1862  O  O   . GLN   B  1 72  ? -5.250  -20.466  -0.277  1.00 31.78 ? 72  GLN   B O   1 
ATOM   1863  C  CB  . GLN   B  1 72  ? -2.306  -21.429  0.525   1.00 31.13 ? 72  GLN   B CB  1 
ATOM   1864  C  CG  . GLN   B  1 72  ? -3.135  -21.527  1.829   1.00 31.77 ? 72  GLN   B CG  1 
ATOM   1865  C  CD  . GLN   B  1 72  ? -3.869  -22.843  1.961   1.00 27.91 ? 72  GLN   B CD  1 
ATOM   1866  O  OE1 . GLN   B  1 72  ? -3.351  -23.807  2.525   1.00 29.26 ? 72  GLN   B OE1 1 
ATOM   1867  N  NE2 . GLN   B  1 72  ? -5.092  -22.895  1.432   1.00 33.50 ? 72  GLN   B NE2 1 
ATOM   1868  N  N   . ASP   B  1 73  ? -3.705  -19.081  -1.150  1.00 31.65 ? 73  ASP   B N   1 
ATOM   1869  C  CA  . ASP   B  1 73  ? -4.499  -17.868  -0.993  1.00 36.10 ? 73  ASP   B CA  1 
ATOM   1870  C  C   . ASP   B  1 73  ? -5.263  -17.596  -2.283  1.00 33.64 ? 73  ASP   B C   1 
ATOM   1871  O  O   . ASP   B  1 73  ? -4.664  -17.365  -3.338  1.00 37.31 ? 73  ASP   B O   1 
ATOM   1872  C  CB  . ASP   B  1 73  ? -3.603  -16.677  -0.642  1.00 34.58 ? 73  ASP   B CB  1 
ATOM   1873  C  CG  . ASP   B  1 73  ? -2.995  -16.800  0.704   1.00 35.21 ? 73  ASP   B CG  1 
ATOM   1874  O  OD1 . ASP   B  1 73  ? -3.612  -17.475  1.544   1.00 37.24 ? 73  ASP   B OD1 1 
ATOM   1875  O  OD2 . ASP   B  1 73  ? -1.896  -16.246  0.928   1.00 35.44 ? 73  ASP   B OD2 1 
ATOM   1876  N  N   . LEU   B  1 74  ? -6.578  -17.629  -2.197  1.00 28.75 ? 74  LEU   B N   1 
ATOM   1877  C  CA  . LEU   B  1 74  ? -7.440  -17.434  -3.347  1.00 32.60 ? 74  LEU   B CA  1 
ATOM   1878  C  C   . LEU   B  1 74  ? -8.252  -16.166  -3.133  1.00 33.18 ? 74  LEU   B C   1 
ATOM   1879  O  O   . LEU   B  1 74  ? -9.046  -16.091  -2.192  1.00 30.47 ? 74  LEU   B O   1 
ATOM   1880  C  CB  . LEU   B  1 74  ? -8.346  -18.650  -3.516  1.00 28.46 ? 74  LEU   B CB  1 
ATOM   1881  C  CG  . LEU   B  1 74  ? -9.292  -18.661  -4.712  1.00 29.80 ? 74  LEU   B CG  1 
ATOM   1882  C  CD1 . LEU   B  1 74  ? -8.506  -18.555  -6.048  1.00 33.52 ? 74  LEU   B CD1 1 
ATOM   1883  C  CD2 . LEU   B  1 74  ? -10.098 -19.927  -4.637  1.00 30.92 ? 74  LEU   B CD2 1 
ATOM   1884  N  N   . GLY   B  1 75  ? -8.046  -15.176  -3.991  1.00 29.45 ? 75  GLY   B N   1 
ATOM   1885  C  CA  . GLY   B  1 75  ? -8.805  -13.948  -3.926  1.00 30.52 ? 75  GLY   B CA  1 
ATOM   1886  C  C   . GLY   B  1 75  ? -10.240 -14.113  -4.420  1.00 32.77 ? 75  GLY   B C   1 
ATOM   1887  O  O   . GLY   B  1 75  ? -10.730 -15.204  -4.712  1.00 29.49 ? 75  GLY   B O   1 
ATOM   1888  N  N   . LYS   B  1 76  ? -10.915 -12.977  -4.515  1.00 29.11 ? 76  LYS   B N   1 
ATOM   1889  C  CA  . LYS   B  1 76  ? -12.345 -12.954  -4.768  1.00 29.83 ? 76  LYS   B CA  1 
ATOM   1890  C  C   . LYS   B  1 76  ? -12.640 -13.247  -6.238  1.00 31.79 ? 76  LYS   B C   1 
ATOM   1891  O  O   . LYS   B  1 76  ? -12.124 -12.580  -7.135  1.00 34.47 ? 76  LYS   B O   1 
ATOM   1892  C  CB  . LYS   B  1 76  ? -12.919 -11.589  -4.371  1.00 35.03 ? 76  LYS   B CB  1 
ATOM   1893  C  CG  . LYS   B  1 76  ? -14.437 -11.502  -4.454  1.00 34.70 ? 76  LYS   B CG  1 
ATOM   1894  N  N   . LEU   B  1 77  ? -13.465 -14.255  -6.481  1.00 26.57 ? 77  LEU   B N   1 
ATOM   1895  C  CA  . LEU   B  1 77  ? -13.977 -14.520  -7.810  1.00 29.24 ? 77  LEU   B CA  1 
ATOM   1896  C  C   . LEU   B  1 77  ? -15.060 -13.502  -8.158  1.00 35.19 ? 77  LEU   B C   1 
ATOM   1897  O  O   . LEU   B  1 77  ? -15.903 -13.182  -7.323  1.00 29.41 ? 77  LEU   B O   1 
ATOM   1898  C  CB  . LEU   B  1 77  ? -14.581 -15.921  -7.871  1.00 31.54 ? 77  LEU   B CB  1 
ATOM   1899  C  CG  . LEU   B  1 77  ? -13.816 -17.150  -7.392  1.00 32.25 ? 77  LEU   B CG  1 
ATOM   1900  C  CD1 . LEU   B  1 77  ? -14.586 -18.395  -7.873  1.00 32.67 ? 77  LEU   B CD1 1 
ATOM   1901  C  CD2 . LEU   B  1 77  ? -12.361 -17.170  -7.856  1.00 32.31 ? 77  LEU   B CD2 1 
ATOM   1902  N  N   . LEU   B  1 78  ? -15.052 -13.033  -9.411  1.00 29.25 ? 78  LEU   B N   1 
ATOM   1903  C  CA  . LEU   B  1 78  ? -16.093 -12.173  -9.973  1.00 32.97 ? 78  LEU   B CA  1 
ATOM   1904  C  C   . LEU   B  1 78  ? -16.981 -13.024  -10.878 1.00 38.18 ? 78  LEU   B C   1 
ATOM   1905  O  O   . LEU   B  1 78  ? -16.639 -13.279  -12.038 1.00 30.25 ? 78  LEU   B O   1 
ATOM   1906  C  CB  . LEU   B  1 78  ? -15.481 -11.023  -10.765 1.00 32.23 ? 78  LEU   B CB  1 
ATOM   1907  C  CG  . LEU   B  1 78  ? -14.512 -10.152  -9.984  1.00 38.83 ? 78  LEU   B CG  1 
ATOM   1908  C  CD1 . LEU   B  1 78  ? -13.934 -9.075   -10.925 1.00 39.05 ? 78  LEU   B CD1 1 
ATOM   1909  C  CD2 . LEU   B  1 78  ? -15.206 -9.534   -8.774  1.00 33.89 ? 78  LEU   B CD2 1 
ATOM   1910  N  N   . ILE   B  1 79  ? -18.134 -13.440  -10.359 1.00 33.50 ? 79  ILE   B N   1 
ATOM   1911  C  CA  . ILE   B  1 79  ? -19.038 -14.330  -11.071 1.00 32.49 ? 79  ILE   B CA  1 
ATOM   1912  C  C   . ILE   B  1 79  ? -20.236 -13.519  -11.536 1.00 40.92 ? 79  ILE   B C   1 
ATOM   1913  O  O   . ILE   B  1 79  ? -20.912 -12.876  -10.727 1.00 39.75 ? 79  ILE   B O   1 
ATOM   1914  C  CB  . ILE   B  1 79  ? -19.496 -15.499  -10.191 1.00 31.34 ? 79  ILE   B CB  1 
ATOM   1915  C  CG1 . ILE   B  1 79  ? -18.293 -16.258  -9.611  1.00 39.44 ? 79  ILE   B CG1 1 
ATOM   1916  C  CG2 . ILE   B  1 79  ? -20.383 -16.407  -10.994 1.00 33.60 ? 79  ILE   B CG2 1 
ATOM   1917  C  CD1 . ILE   B  1 79  ? -17.246 -16.736  -10.658 1.00 29.14 ? 79  ILE   B CD1 1 
ATOM   1918  N  N   . GLY   B  1 80  ? -20.513 -13.550  -12.812 1.00 33.84 ? 80  GLY   B N   1 
ATOM   1919  C  CA  . GLY   B  1 80  ? -21.683 -12.832  -13.278 1.00 42.17 ? 80  GLY   B CA  1 
ATOM   1920  C  C   . GLY   B  1 80  ? -22.960 -13.627  -13.083 1.00 32.36 ? 80  GLY   B C   1 
ATOM   1921  O  O   . GLY   B  1 80  ? -22.942 -14.828  -12.799 1.00 36.47 ? 80  GLY   B O   1 
ATOM   1922  N  N   . GLU   B  1 81  ? -24.097 -12.940  -13.258 1.00 37.54 ? 81  GLU   B N   1 
ATOM   1923  C  CA  . GLU   B  1 81  ? -25.404 -13.583  -13.218 1.00 31.00 ? 81  GLU   B CA  1 
ATOM   1924  C  C   . GLU   B  1 81  ? -26.068 -13.692  -14.585 1.00 36.38 ? 81  GLU   B C   1 
ATOM   1925  O  O   . GLU   B  1 81  ? -27.124 -14.334  -14.700 1.00 31.26 ? 81  GLU   B O   1 
ATOM   1926  C  CB  . GLU   B  1 81  ? -26.333 -12.822  -12.263 1.00 44.45 ? 81  GLU   B CB  1 
ATOM   1927  C  CG  . GLU   B  1 81  ? -25.783 -12.681  -10.853 1.00 44.79 ? 81  GLU   B CG  1 
ATOM   1928  C  CD  . GLU   B  1 81  ? -26.867 -12.288  -9.854  1.00 56.79 ? 81  GLU   B CD  1 
ATOM   1929  O  OE1 . GLU   B  1 81  ? -27.989 -11.943  -10.292 1.00 61.25 ? 81  GLU   B OE1 1 
ATOM   1930  O  OE2 . GLU   B  1 81  ? -26.602 -12.335  -8.639  1.00 59.98 ? 81  GLU   B OE2 1 
ATOM   1931  N  N   . ASN   B  1 82  ? -25.493 -13.080  -15.610 1.00 33.34 ? 82  ASN   B N   1 
ATOM   1932  C  CA  . ASN   B  1 82  ? -25.941 -13.261  -16.976 1.00 37.17 ? 82  ASN   B CA  1 
ATOM   1933  C  C   . ASN   B  1 82  ? -24.723 -13.108  -17.881 1.00 33.53 ? 82  ASN   B C   1 
ATOM   1934  O  O   . ASN   B  1 82  ? -23.646 -12.722  -17.442 1.00 31.94 ? 82  ASN   B O   1 
ATOM   1935  C  CB  . ASN   B  1 82  ? -27.059 -12.268  -17.352 1.00 32.55 ? 82  ASN   B CB  1 
ATOM   1936  C  CG  . ASN   B  1 82  ? -26.664 -10.813  -17.119 1.00 37.10 ? 82  ASN   B CG  1 
ATOM   1937  O  OD1 . ASN   B  1 82  ? -25.601 -10.349  -17.547 1.00 29.93 ? 82  ASN   B OD1 1 
ATOM   1938  N  ND2 . ASN   B  1 82  ? -27.534 -10.079  -16.426 1.00 46.93 ? 82  ASN   B ND2 1 
ATOM   1939  N  N   . THR   B  1 83  ? -24.915 -13.395  -19.166 1.00 33.77 ? 83  THR   B N   1 
ATOM   1940  C  CA  . THR   B  1 83  ? -23.780 -13.451  -20.084 1.00 29.08 ? 83  THR   B CA  1 
ATOM   1941  C  C   . THR   B  1 83  ? -23.020 -12.131  -20.104 1.00 34.24 ? 83  THR   B C   1 
ATOM   1942  O  O   . THR   B  1 83  ? -21.784 -12.094  -19.965 1.00 27.28 ? 83  THR   B O   1 
ATOM   1943  C  CB  . THR   B  1 83  ? -24.269 -13.821  -21.483 1.00 26.63 ? 83  THR   B CB  1 
ATOM   1944  O  OG1 . THR   B  1 83  ? -24.618 -15.203  -21.508 1.00 29.07 ? 83  THR   B OG1 1 
ATOM   1945  C  CG2 . THR   B  1 83  ? -23.180 -13.566  -22.529 1.00 29.62 ? 83  THR   B CG2 1 
ATOM   1946  N  N   . GLN   B  1 84  ? -23.740 -11.029  -20.261 1.00 31.53 ? 84  GLN   B N   1 
ATOM   1947  C  CA  . GLN   B  1 84  ? -23.081 -9.732   -20.313 1.00 34.58 ? 84  GLN   B CA  1 
ATOM   1948  C  C   . GLN   B  1 84  ? -22.256 -9.473   -19.056 1.00 30.68 ? 84  GLN   B C   1 
ATOM   1949  O  O   . GLN   B  1 84  ? -21.105 -9.013   -19.137 1.00 31.61 ? 84  GLN   B O   1 
ATOM   1950  C  CB  . GLN   B  1 84  ? -24.124 -8.632   -20.511 1.00 39.37 ? 84  GLN   B CB  1 
ATOM   1951  C  CG  . GLN   B  1 84  ? -23.504 -7.264   -20.760 1.00 45.99 ? 84  GLN   B CG  1 
ATOM   1952  C  CD  . GLN   B  1 84  ? -24.385 -6.330   -21.590 1.00 56.17 ? 84  GLN   B CD  1 
ATOM   1953  O  OE1 . GLN   B  1 84  ? -23.900 -5.326   -22.108 1.00 66.48 ? 84  GLN   B OE1 1 
ATOM   1954  N  NE2 . GLN   B  1 84  ? -25.679 -6.660   -21.725 1.00 55.02 ? 84  GLN   B NE2 1 
ATOM   1955  N  N   . GLU   B  1 85  ? -22.843 -9.724   -17.880 1.00 29.42 ? 85  GLU   B N   1 
ATOM   1956  C  CA  . GLU   B  1 85  ? -22.113 -9.531   -16.632 1.00 33.21 ? 85  GLU   B CA  1 
ATOM   1957  C  C   . GLU   B  1 85  ? -20.917 -10.462  -16.543 1.00 26.94 ? 85  GLU   B C   1 
ATOM   1958  O  O   . GLU   B  1 85  ? -19.867 -10.083  -16.027 1.00 26.49 ? 85  GLU   B O   1 
ATOM   1959  C  CB  . GLU   B  1 85  ? -23.021 -9.775   -15.426 1.00 30.67 ? 85  GLU   B CB  1 
ATOM   1960  C  CG  . GLU   B  1 85  ? -23.920 -8.615   -15.075 1.00 45.78 ? 85  GLU   B CG  1 
ATOM   1961  C  CD  . GLU   B  1 85  ? -24.836 -8.933   -13.897 1.00 50.64 ? 85  GLU   B CD  1 
ATOM   1962  O  OE1 . GLU   B  1 85  ? -24.498 -9.843   -13.095 1.00 45.19 ? 85  GLU   B OE1 1 
ATOM   1963  O  OE2 . GLU   B  1 85  ? -25.901 -8.281   -13.795 1.00 50.54 ? 85  GLU   B OE2 1 
ATOM   1964  N  N   . MET   B  1 86  ? -21.074 -11.702  -16.997 1.00 30.25 ? 86  MET   B N   1 
ATOM   1965  C  CA  . MET   B  1 86  ? -19.958 -12.641  -16.912 1.00 28.46 ? 86  MET   B CA  1 
ATOM   1966  C  C   . MET   B  1 86  ? -18.773 -12.147  -17.734 1.00 29.09 ? 86  MET   B C   1 
ATOM   1967  O  O   . MET   B  1 86  ? -17.619 -12.239  -17.298 1.00 28.43 ? 86  MET   B O   1 
ATOM   1968  C  CB  . MET   B  1 86  ? -20.425 -14.019  -17.384 1.00 25.71 ? 86  MET   B CB  1 
ATOM   1969  C  CG  . MET   B  1 86  ? -21.443 -14.665  -16.420 1.00 26.74 ? 86  MET   B CG  1 
ATOM   1970  S  SD  . MET   B  1 86  ? -22.502 -15.851  -17.259 1.00 29.55 ? 86  MET   B SD  1 
ATOM   1971  C  CE  . MET   B  1 86  ? -21.409 -17.269  -17.402 1.00 28.77 ? 86  MET   B CE  1 
ATOM   1972  N  N   . LEU   B  1 87  ? -19.037 -11.645  -18.944 1.00 30.26 ? 87  LEU   B N   1 
ATOM   1973  C  CA  . LEU   B  1 87  ? -17.947 -11.130  -19.780 1.00 27.24 ? 87  LEU   B CA  1 
ATOM   1974  C  C   . LEU   B  1 87  ? -17.297 -9.900   -19.149 1.00 25.33 ? 87  LEU   B C   1 
ATOM   1975  O  O   . LEU   B  1 87  ? -16.068 -9.727   -19.199 1.00 29.28 ? 87  LEU   B O   1 
ATOM   1976  C  CB  . LEU   B  1 87  ? -18.483 -10.799  -21.167 1.00 29.59 ? 87  LEU   B CB  1 
ATOM   1977  C  CG  . LEU   B  1 87  ? -18.923 -11.990  -22.026 1.00 26.45 ? 87  LEU   B CG  1 
ATOM   1978  C  CD1 . LEU   B  1 87  ? -19.824 -11.529  -23.155 1.00 30.04 ? 87  LEU   B CD1 1 
ATOM   1979  C  CD2 . LEU   B  1 87  ? -17.657 -12.677  -22.549 1.00 22.66 ? 87  LEU   B CD2 1 
ATOM   1980  N  N   . GLN   B  1 88  ? -18.111 -8.998   -18.606 1.00 29.32 ? 88  GLN   B N   1 
ATOM   1981  C  CA  . GLN   B  1 88  ? -17.576 -7.816   -17.940 1.00 26.89 ? 88  GLN   B CA  1 
ATOM   1982  C  C   . GLN   B  1 88  ? -16.762 -8.197   -16.702 1.00 28.73 ? 88  GLN   B C   1 
ATOM   1983  O  O   . GLN   B  1 88  ? -15.765 -7.547   -16.396 1.00 28.04 ? 88  GLN   B O   1 
ATOM   1984  C  CB  . GLN   B  1 88  ? -18.727 -6.859   -17.563 1.00 32.07 ? 88  GLN   B CB  1 
ATOM   1985  C  CG  . GLN   B  1 88  ? -18.248 -5.496   -16.997 1.00 41.98 ? 88  GLN   B CG  1 
ATOM   1986  C  CD  . GLN   B  1 88  ? -17.445 -4.642   -17.999 1.00 45.53 ? 88  GLN   B CD  1 
ATOM   1987  O  OE1 . GLN   B  1 88  ? -17.887 -4.398   -19.120 1.00 49.66 ? 88  GLN   B OE1 1 
ATOM   1988  N  NE2 . GLN   B  1 88  ? -16.269 -4.191   -17.587 1.00 46.07 ? 88  GLN   B NE2 1 
ATOM   1989  N  N   . CYS   B  1 89  ? -17.162 -9.253   -15.982 1.00 27.74 ? 89  CYS   B N   1 
ATOM   1990  C  CA  . CYS   B  1 89  ? -16.361 -9.676   -14.835 1.00 26.44 ? 89  CYS   B CA  1 
ATOM   1991  C  C   . CYS   B  1 89  ? -15.017 -10.238  -15.282 1.00 32.16 ? 89  CYS   B C   1 
ATOM   1992  O  O   . CYS   B  1 89  ? -13.997 -10.020  -14.617 1.00 25.06 ? 89  CYS   B O   1 
ATOM   1993  C  CB  . CYS   B  1 89  ? -17.079 -10.732  -14.005 1.00 30.12 ? 89  CYS   B CB  1 
ATOM   1994  S  SG  . CYS   B  1 89  ? -18.475 -10.202  -12.942 1.00 30.90 ? 89  CYS   B SG  1 
ATOM   1995  N  N   . ASP   B  1 90  ? -15.010 -11.017  -16.367 1.00 28.82 ? 90  ASP   B N   1 
ATOM   1996  C  CA  . ASP   B  1 90  ? -13.746 -11.480  -16.933 1.00 26.81 ? 90  ASP   B CA  1 
ATOM   1997  C  C   . ASP   B  1 90  ? -12.862 -10.289  -17.303 1.00 28.97 ? 90  ASP   B C   1 
ATOM   1998  O  O   . ASP   B  1 90  ? -11.675 -10.243  -16.960 1.00 24.46 ? 90  ASP   B O   1 
ATOM   1999  C  CB  . ASP   B  1 90  ? -14.008 -12.369  -18.164 1.00 28.33 ? 90  ASP   B CB  1 
ATOM   2000  C  CG  . ASP   B  1 90  ? -14.529 -13.750  -17.817 1.00 28.85 ? 90  ASP   B CG  1 
ATOM   2001  O  OD1 . ASP   B  1 90  ? -14.751 -14.042  -16.635 1.00 29.32 ? 90  ASP   B OD1 1 
ATOM   2002  O  OD2 . ASP   B  1 90  ? -14.694 -14.575  -18.744 1.00 31.58 ? 90  ASP   B OD2 1 
ATOM   2003  N  N   . LEU   B  1 91  ? -13.444 -9.298   -17.989 1.00 30.42 ? 91  LEU   B N   1 
ATOM   2004  C  CA  . LEU   B  1 91  ? -12.685 -8.130   -18.435 1.00 25.04 ? 91  LEU   B CA  1 
ATOM   2005  C  C   . LEU   B  1 91  ? -12.128 -7.342   -17.252 1.00 28.22 ? 91  LEU   B C   1 
ATOM   2006  O  O   . LEU   B  1 91  ? -10.963 -6.930   -17.266 1.00 30.46 ? 91  LEU   B O   1 
ATOM   2007  C  CB  . LEU   B  1 91  ? -13.575 -7.240   -19.310 1.00 30.10 ? 91  LEU   B CB  1 
ATOM   2008  C  CG  . LEU   B  1 91  ? -12.905 -5.992   -19.913 1.00 28.03 ? 91  LEU   B CG  1 
ATOM   2009  C  CD1 . LEU   B  1 91  ? -11.716 -6.354   -20.731 1.00 33.07 ? 91  LEU   B CD1 1 
ATOM   2010  C  CD2 . LEU   B  1 91  ? -13.922 -5.235   -20.777 1.00 36.58 ? 91  LEU   B CD2 1 
ATOM   2011  N  N   . ASN   B  1 92  ? -12.936 -7.135   -16.211 1.00 31.11 ? 92  ASN   B N   1 
ATOM   2012  C  CA  . ASN   B  1 92  ? -12.429 -6.430   -15.034 1.00 31.79 ? 92  ASN   B CA  1 
ATOM   2013  C  C   . ASN   B  1 92  ? -11.270 -7.176   -14.392 1.00 27.44 ? 92  ASN   B C   1 
ATOM   2014  O  O   . ASN   B  1 92  ? -10.302 -6.563   -13.938 1.00 27.48 ? 92  ASN   B O   1 
ATOM   2015  C  CB  . ASN   B  1 92  ? -13.558 -6.233   -14.016 1.00 32.44 ? 92  ASN   B CB  1 
ATOM   2016  C  CG  . ASN   B  1 92  ? -14.590 -5.228   -14.486 1.00 41.07 ? 92  ASN   B CG  1 
ATOM   2017  O  OD1 . ASN   B  1 92  ? -14.352 -4.461   -15.423 1.00 41.70 ? 92  ASN   B OD1 1 
ATOM   2018  N  ND2 . ASN   B  1 92  ? -15.747 -5.224   -13.833 1.00 41.09 ? 92  ASN   B ND2 1 
ATOM   2019  N  N   . LEU   B  1 93  ? -11.364 -8.507   -14.303 1.00 27.79 ? 93  LEU   B N   1 
ATOM   2020  C  CA  . LEU   B  1 93  ? -10.244 -9.270   -13.752 1.00 27.73 ? 93  LEU   B CA  1 
ATOM   2021  C  C   . LEU   B  1 93  ? -9.000  -9.157   -14.631 1.00 28.71 ? 93  LEU   B C   1 
ATOM   2022  O  O   . LEU   B  1 93  ? -7.885  -9.013   -14.112 1.00 28.64 ? 93  LEU   B O   1 
ATOM   2023  C  CB  . LEU   B  1 93  ? -10.650 -10.734  -13.569 1.00 31.27 ? 93  LEU   B CB  1 
ATOM   2024  C  CG  . LEU   B  1 93  ? -9.622  -11.725  -13.044 1.00 30.96 ? 93  LEU   B CG  1 
ATOM   2025  C  CD1 . LEU   B  1 93  ? -9.172  -11.366  -11.629 1.00 35.84 ? 93  LEU   B CD1 1 
ATOM   2026  C  CD2 . LEU   B  1 93  ? -10.189 -13.135  -13.077 1.00 33.77 ? 93  LEU   B CD2 1 
ATOM   2027  N  N   . GLU   B  1 94  ? -9.171  -9.257   -15.958 1.00 29.43 ? 94  GLU   B N   1 
ATOM   2028  C  CA  . GLU   B  1 94  ? -8.042  -9.167   -16.886 1.00 29.35 ? 94  GLU   B CA  1 
ATOM   2029  C  C   . GLU   B  1 94  ? -7.329  -7.825   -16.761 1.00 32.80 ? 94  GLU   B C   1 
ATOM   2030  O  O   . GLU   B  1 94  ? -6.097  -7.766   -16.780 1.00 30.37 ? 94  GLU   B O   1 
ATOM   2031  C  CB  . GLU   B  1 94  ? -8.528  -9.355   -18.333 1.00 28.57 ? 94  GLU   B CB  1 
ATOM   2032  C  CG  . GLU   B  1 94  ? -8.987  -10.757  -18.680 1.00 32.54 ? 94  GLU   B CG  1 
ATOM   2033  C  CD  . GLU   B  1 94  ? -7.825  -11.692  -18.913 1.00 36.86 ? 94  GLU   B CD  1 
ATOM   2034  O  OE1 . GLU   B  1 94  ? -6.660  -11.236  -18.830 1.00 33.14 ? 94  GLU   B OE1 1 
ATOM   2035  O  OE2 . GLU   B  1 94  ? -8.078  -12.879  -19.186 1.00 42.82 ? 94  GLU   B OE2 1 
ATOM   2036  N  N   . LEU   B  1 95  ? -8.094  -6.730   -16.659 1.00 29.99 ? 95  LEU   B N   1 
ATOM   2037  C  CA  . LEU   B  1 95  ? -7.490  -5.404   -16.535 1.00 32.02 ? 95  LEU   B CA  1 
ATOM   2038  C  C   . LEU   B  1 95  ? -6.695  -5.281   -15.247 1.00 30.37 ? 95  LEU   B C   1 
ATOM   2039  O  O   . LEU   B  1 95  ? -5.606  -4.687   -15.239 1.00 34.77 ? 95  LEU   B O   1 
ATOM   2040  C  CB  . LEU   B  1 95  ? -8.557  -4.319   -16.606 1.00 34.56 ? 95  LEU   B CB  1 
ATOM   2041  C  CG  . LEU   B  1 95  ? -9.192  -4.182   -17.988 1.00 32.42 ? 95  LEU   B CG  1 
ATOM   2042  C  CD1 . LEU   B  1 95  ? -10.492 -3.362   -17.931 1.00 34.24 ? 95  LEU   B CD1 1 
ATOM   2043  C  CD2 . LEU   B  1 95  ? -8.165  -3.593   -18.951 1.00 40.78 ? 95  LEU   B CD2 1 
ATOM   2044  N  N   . LYS   B  1 96  ? -7.197  -5.866   -14.154 1.00 29.85 ? 96  LYS   B N   1 
ATOM   2045  C  CA  . LYS   B  1 96  ? -6.373  -6.002   -12.961 1.00 30.35 ? 96  LYS   B CA  1 
ATOM   2046  C  C   . LYS   B  1 96  ? -5.115  -6.810   -13.255 1.00 29.57 ? 96  LYS   B C   1 
ATOM   2047  O  O   . LYS   B  1 96  ? -4.005  -6.418   -12.873 1.00 33.68 ? 96  LYS   B O   1 
ATOM   2048  C  CB  . LYS   B  1 96  ? -7.169  -6.667   -11.829 1.00 36.25 ? 96  LYS   B CB  1 
ATOM   2049  C  CG  . LYS   B  1 96  ? -6.422  -6.682   -10.473 1.00 42.94 ? 96  LYS   B CG  1 
ATOM   2050  C  CD  . LYS   B  1 96  ? -6.533  -8.014   -9.724  1.00 51.18 ? 96  LYS   B CD  1 
ATOM   2051  C  CE  . LYS   B  1 96  ? -5.932  -7.924   -8.306  1.00 51.62 ? 96  LYS   B CE  1 
ATOM   2052  N  NZ  . LYS   B  1 96  ? -4.807  -6.919   -8.181  1.00 51.30 ? 96  LYS   B NZ  1 
ATOM   2053  N  N   . ALA   B  1 97  ? -5.275  -7.977   -13.891 1.00 31.85 ? 97  ALA   B N   1 
ATOM   2054  C  CA  . ALA   B  1 97  ? -4.127  -8.853   -14.126 1.00 31.25 ? 97  ALA   B CA  1 
ATOM   2055  C  C   . ALA   B  1 97  ? -3.052  -8.160   -14.960 1.00 26.88 ? 97  ALA   B C   1 
ATOM   2056  O  O   . ALA   B  1 97  ? -1.860  -8.301   -14.678 1.00 30.14 ? 97  ALA   B O   1 
ATOM   2057  C  CB  . ALA   B  1 97  ? -4.572  -10.150  -14.805 1.00 30.84 ? 97  ALA   B CB  1 
ATOM   2058  N  N   . THR   B  1 98  ? -3.443  -7.418   -16.003 1.00 30.39 ? 98  THR   B N   1 
ATOM   2059  C  CA  . THR   B  1 98  ? -2.413  -6.801   -16.835 1.00 30.94 ? 98  THR   B CA  1 
ATOM   2060  C  C   . THR   B  1 98  ? -1.733  -5.634   -16.122 1.00 30.98 ? 98  THR   B C   1 
ATOM   2061  O  O   . THR   B  1 98  ? -0.546  -5.384   -16.349 1.00 28.85 ? 98  THR   B O   1 
ATOM   2062  C  CB  . THR   B  1 98  ? -2.975  -6.339   -18.178 1.00 31.70 ? 98  THR   B CB  1 
ATOM   2063  O  OG1 . THR   B  1 98  ? -4.001  -5.376   -17.974 1.00 32.98 ? 98  THR   B OG1 1 
ATOM   2064  C  CG2 . THR   B  1 98  ? -3.521  -7.501   -18.998 1.00 31.58 ? 98  THR   B CG2 1 
ATOM   2065  N  N   . LYS   B  1 99  ? -2.443  -4.913   -15.251 1.00 33.21 ? 99  LYS   B N   1 
ATOM   2066  C  CA  . LYS   B  1 99  ? -1.769  -3.889   -14.461 1.00 30.63 ? 99  LYS   B CA  1 
ATOM   2067  C  C   . LYS   B  1 99  ? -0.725  -4.511   -13.538 1.00 28.85 ? 99  LYS   B C   1 
ATOM   2068  O  O   . LYS   B  1 99  ? 0.386   -3.995   -13.394 1.00 28.77 ? 99  LYS   B O   1 
ATOM   2069  C  CB  . LYS   B  1 99  ? -2.796  -3.088   -13.646 1.00 36.63 ? 99  LYS   B CB  1 
ATOM   2070  C  CG  . LYS   B  1 99  ? -2.167  -2.035   -12.721 1.00 41.27 ? 99  LYS   B CG  1 
ATOM   2071  C  CD  . LYS   B  1 99  ? -3.222  -1.269   -11.867 1.00 46.17 ? 99  LYS   B CD  1 
ATOM   2072  N  N   . ASP   B  1 100 ? -1.061  -5.616   -12.888 1.00 27.82 ? 100 ASP   B N   1 
ATOM   2073  C  CA  . ASP   B  1 100 ? -0.075  -6.265   -12.044 1.00 25.23 ? 100 ASP   B CA  1 
ATOM   2074  C  C   . ASP   B  1 100 ? 1.098   -6.796   -12.862 1.00 32.96 ? 100 ASP   B C   1 
ATOM   2075  O  O   . ASP   B  1 100 ? 2.248   -6.770   -12.400 1.00 33.38 ? 100 ASP   B O   1 
ATOM   2076  C  CB  . ASP   B  1 100 ? -0.738  -7.379   -11.243 1.00 28.32 ? 100 ASP   B CB  1 
ATOM   2077  C  CG  . ASP   B  1 100 ? -1.734  -6.846   -10.199 1.00 34.81 ? 100 ASP   B CG  1 
ATOM   2078  O  OD1 . ASP   B  1 100 ? -1.645  -5.659   -9.822  1.00 37.27 ? 100 ASP   B OD1 1 
ATOM   2079  O  OD2 . ASP   B  1 100 ? -2.598  -7.618   -9.752  1.00 33.73 ? 100 ASP   B OD2 1 
ATOM   2080  N  N   . LEU   B  1 101 ? 0.842   -7.268   -14.087 1.00 33.81 ? 101 LEU   B N   1 
ATOM   2081  C  CA  . LEU   B  1 101 ? 1.950   -7.779   -14.894 1.00 25.67 ? 101 LEU   B CA  1 
ATOM   2082  C  C   . LEU   B  1 101 ? 2.926   -6.658   -15.243 1.00 27.75 ? 101 LEU   B C   1 
ATOM   2083  O  O   . LEU   B  1 101 ? 4.140   -6.845   -15.170 1.00 28.33 ? 101 LEU   B O   1 
ATOM   2084  C  CB  . LEU   B  1 101 ? 1.436   -8.472   -16.168 1.00 30.38 ? 101 LEU   B CB  1 
ATOM   2085  C  CG  . LEU   B  1 101 ? 0.911   -9.922   -16.007 1.00 25.60 ? 101 LEU   B CG  1 
ATOM   2086  C  CD1 . LEU   B  1 101 ? -0.077  -10.321  -17.095 1.00 31.90 ? 101 LEU   B CD1 1 
ATOM   2087  C  CD2 . LEU   B  1 101 ? 2.081   -10.919  -15.999 1.00 31.05 ? 101 LEU   B CD2 1 
ATOM   2088  N  N   . ARG   B  1 102 ? 2.411   -5.486   -15.615 1.00 27.19 ? 102 ARG   B N   1 
ATOM   2089  C  CA  . ARG   B  1 102 ? 3.287   -4.372   -15.964 1.00 28.48 ? 102 ARG   B CA  1 
ATOM   2090  C  C   . ARG   B  1 102 ? 4.177   -3.974   -14.794 1.00 27.45 ? 102 ARG   B C   1 
ATOM   2091  O  O   . ARG   B  1 102 ? 5.389   -3.771   -14.955 1.00 27.94 ? 102 ARG   B O   1 
ATOM   2092  C  CB  . ARG   B  1 102 ? 2.435   -3.194   -16.447 1.00 29.88 ? 102 ARG   B CB  1 
ATOM   2093  C  CG  . ARG   B  1 102 ? 1.749   -3.471   -17.751 1.00 29.49 ? 102 ARG   B CG  1 
ATOM   2094  C  CD  . ARG   B  1 102 ? 0.800   -2.322   -18.155 1.00 30.82 ? 102 ARG   B CD  1 
ATOM   2095  N  NE  . ARG   B  1 102 ? -0.310  -2.788   -18.978 1.00 25.85 ? 102 ARG   B NE  1 
ATOM   2096  C  CZ  . ARG   B  1 102 ? -0.195  -3.249   -20.222 1.00 25.98 ? 102 ARG   B CZ  1 
ATOM   2097  N  NH1 . ARG   B  1 102 ? 0.965   -3.286   -20.842 1.00 28.49 ? 102 ARG   B NH1 1 
ATOM   2098  N  NH2 . ARG   B  1 102 ? -1.260  -3.732   -20.837 1.00 31.27 ? 102 ARG   B NH2 1 
ATOM   2099  N  N   . GLU   B  1 103 ? 3.608   -3.894   -13.594 1.00 30.96 ? 103 GLU   B N   1 
ATOM   2100  C  CA  . GLU   B  1 103 ? 4.422   -3.502   -12.444 1.00 31.64 ? 103 GLU   B CA  1 
ATOM   2101  C  C   . GLU   B  1 103 ? 5.462   -4.560   -12.110 1.00 30.15 ? 103 GLU   B C   1 
ATOM   2102  O  O   . GLU   B  1 103 ? 6.570   -4.231   -11.662 1.00 28.84 ? 103 GLU   B O   1 
ATOM   2103  C  CB  . GLU   B  1 103 ? 3.516   -3.241   -11.237 1.00 31.04 ? 103 GLU   B CB  1 
ATOM   2104  C  CG  . GLU   B  1 103 ? 2.722   -1.959   -11.359 1.00 41.03 ? 103 GLU   B CG  1 
ATOM   2105  C  CD  . GLU   B  1 103 ? 1.620   -1.829   -10.312 1.00 57.78 ? 103 GLU   B CD  1 
ATOM   2106  O  OE1 . GLU   B  1 103 ? 1.443   -2.764   -9.505  1.00 59.23 ? 103 GLU   B OE1 1 
ATOM   2107  O  OE2 . GLU   B  1 103 ? 0.923   -0.790   -10.305 1.00 67.19 ? 103 GLU   B OE2 1 
ATOM   2108  N  N   . ALA   B  1 104 ? 5.140   -5.833   -12.334 1.00 29.93 ? 104 ALA   B N   1 
ATOM   2109  C  CA  . ALA   B  1 104 ? 6.124   -6.882   -12.097 1.00 26.79 ? 104 ALA   B CA  1 
ATOM   2110  C  C   . ALA   B  1 104 ? 7.265   -6.828   -13.120 1.00 26.84 ? 104 ALA   B C   1 
ATOM   2111  O  O   . ALA   B  1 104 ? 8.437   -7.063   -12.773 1.00 27.78 ? 104 ALA   B O   1 
ATOM   2112  C  CB  . ALA   B  1 104 ? 5.417   -8.239   -12.119 1.00 27.95 ? 104 ALA   B CB  1 
ATOM   2113  N  N   . ILE   B  1 105 ? 6.943   -6.557   -14.385 1.00 29.54 ? 105 ILE   B N   1 
ATOM   2114  C  CA  . ILE   B  1 105 ? 7.991   -6.426   -15.401 1.00 30.31 ? 105 ILE   B CA  1 
ATOM   2115  C  C   . ILE   B  1 105 ? 8.914   -5.259   -15.072 1.00 29.74 ? 105 ILE   B C   1 
ATOM   2116  O  O   . ILE   B  1 105 ? 10.137  -5.368   -15.214 1.00 28.40 ? 105 ILE   B O   1 
ATOM   2117  C  CB  . ILE   B  1 105 ? 7.359   -6.272   -16.793 1.00 27.37 ? 105 ILE   B CB  1 
ATOM   2118  C  CG1 . ILE   B  1 105 ? 6.760   -7.607   -17.239 1.00 27.12 ? 105 ILE   B CG1 1 
ATOM   2119  C  CG2 . ILE   B  1 105 ? 8.359   -5.785   -17.788 1.00 29.31 ? 105 ILE   B CG2 1 
ATOM   2120  C  CD1 . ILE   B  1 105 ? 5.746   -7.439   -18.257 1.00 26.64 ? 105 ILE   B CD1 1 
ATOM   2121  N  N   . VAL   B  1 106 ? 8.343   -4.117   -14.653 1.00 30.19 ? 106 VAL   B N   1 
ATOM   2122  C  CA  . VAL   B  1 106 ? 9.181   -2.994   -14.227 1.00 27.98 ? 106 VAL   B CA  1 
ATOM   2123  C  C   . VAL   B  1 106 ? 10.196  -3.475   -13.215 1.00 28.46 ? 106 VAL   B C   1 
ATOM   2124  O  O   . VAL   B  1 106 ? 11.397  -3.174   -13.310 1.00 33.49 ? 106 VAL   B O   1 
ATOM   2125  C  CB  . VAL   B  1 106 ? 8.327   -1.853   -13.645 1.00 34.05 ? 106 VAL   B CB  1 
ATOM   2126  C  CG1 . VAL   B  1 106 ? 9.217   -0.825   -12.960 1.00 36.77 ? 106 VAL   B CG1 1 
ATOM   2127  C  CG2 . VAL   B  1 106 ? 7.540   -1.183   -14.724 1.00 37.42 ? 106 VAL   B CG2 1 
ATOM   2128  N  N   . HIS   B  1 107 ? 9.741   -4.253   -12.231 1.00 32.38 ? 107 HIS   B N   1 
ATOM   2129  C  CA  . HIS   B  1 107 ? 10.688  -4.640   -11.193 1.00 31.20 ? 107 HIS   B CA  1 
ATOM   2130  C  C   . HIS   B  1 107 ? 11.715  -5.650   -11.704 1.00 30.05 ? 107 HIS   B C   1 
ATOM   2131  O  O   . HIS   B  1 107 ? 12.900  -5.548   -11.373 1.00 30.21 ? 107 HIS   B O   1 
ATOM   2132  C  CB  . HIS   B  1 107 ? 9.977   -5.192   -9.964  1.00 39.60 ? 107 HIS   B CB  1 
ATOM   2133  C  CG  . HIS   B  1 107 ? 10.937  -5.538   -8.884  1.00 36.95 ? 107 HIS   B CG  1 
ATOM   2134  N  ND1 . HIS   B  1 107 ? 11.600  -4.572   -8.165  1.00 38.61 ? 107 HIS   B ND1 1 
ATOM   2135  C  CD2 . HIS   B  1 107 ? 11.440  -6.726   -8.479  1.00 35.78 ? 107 HIS   B CD2 1 
ATOM   2136  C  CE1 . HIS   B  1 107 ? 12.441  -5.152   -7.330  1.00 42.16 ? 107 HIS   B CE1 1 
ATOM   2137  N  NE2 . HIS   B  1 107 ? 12.361  -6.459   -7.500  1.00 40.02 ? 107 HIS   B NE2 1 
ATOM   2138  N  N   . CYS   B  1 108 ? 11.293  -6.631   -12.512 1.00 30.23 ? 108 CYS   B N   1 
ATOM   2139  C  CA  . CYS   B  1 108 ? 12.255  -7.560   -13.096 1.00 24.79 ? 108 CYS   B CA  1 
ATOM   2140  C  C   . CYS   B  1 108 ? 13.340  -6.828   -13.880 1.00 28.11 ? 108 CYS   B C   1 
ATOM   2141  O  O   . CYS   B  1 108 ? 14.518  -7.208   -13.839 1.00 32.38 ? 108 CYS   B O   1 
ATOM   2142  C  CB  . CYS   B  1 108 ? 11.543  -8.542   -14.024 1.00 27.94 ? 108 CYS   B CB  1 
ATOM   2143  S  SG  . CYS   B  1 108 ? 10.441  -9.696   -13.167 1.00 31.09 ? 108 CYS   B SG  1 
ATOM   2144  N  N   . GLU   B  1 109 ? 12.941  -5.826   -14.666 1.00 29.81 ? 109 GLU   B N   1 
ATOM   2145  C  CA  . GLU   B  1 109 ? 13.911  -5.066   -15.445 1.00 27.73 ? 109 GLU   B CA  1 
ATOM   2146  C  C   . GLU   B  1 109 ? 14.908  -4.383   -14.518 1.00 32.74 ? 109 GLU   B C   1 
ATOM   2147  O  O   . GLU   B  1 109 ? 16.115  -4.413   -14.764 1.00 33.57 ? 109 GLU   B O   1 
ATOM   2148  C  CB  . GLU   B  1 109 ? 13.183  -4.039   -16.314 1.00 29.59 ? 109 GLU   B CB  1 
ATOM   2149  C  CG  . GLU   B  1 109 ? 14.092  -3.205   -17.244 1.00 35.56 ? 109 GLU   B CG  1 
ATOM   2150  C  CD  . GLU   B  1 109 ? 14.717  -4.031   -18.375 1.00 37.98 ? 109 GLU   B CD  1 
ATOM   2151  O  OE1 . GLU   B  1 109 ? 14.214  -5.145   -18.669 1.00 31.12 ? 109 GLU   B OE1 1 
ATOM   2152  O  OE2 . GLU   B  1 109 ? 15.712  -3.563   -18.971 1.00 31.21 ? 109 GLU   B OE2 1 
ATOM   2153  N  N   . GLN   B  1 110 ? 14.414  -3.803   -13.423 1.00 37.03 ? 110 GLN   B N   1 
ATOM   2154  C  CA  . GLN   B  1 110 ? 15.271  -3.016   -12.541 1.00 32.62 ? 110 GLN   B CA  1 
ATOM   2155  C  C   . GLN   B  1 110 ? 16.321  -3.884   -11.865 1.00 34.50 ? 110 GLN   B C   1 
ATOM   2156  O  O   . GLN   B  1 110 ? 17.462  -3.444   -11.661 1.00 35.02 ? 110 GLN   B O   1 
ATOM   2157  C  CB  . GLN   B  1 110 ? 14.381  -2.272   -11.535 1.00 33.68 ? 110 GLN   B CB  1 
ATOM   2158  C  CG  . GLN   B  1 110 ? 13.525  -1.197   -12.182 1.00 42.58 ? 110 GLN   B CG  1 
ATOM   2159  N  N   . VAL   B  1 111 ? 15.992  -5.139   -11.567 1.00 31.08 ? 111 VAL   B N   1 
ATOM   2160  C  CA  . VAL   B  1 111 ? 16.964  -6.035   -10.959 1.00 27.38 ? 111 VAL   B CA  1 
ATOM   2161  C  C   . VAL   B  1 111 ? 17.581  -7.008   -11.975 1.00 27.81 ? 111 VAL   B C   1 
ATOM   2162  O  O   . VAL   B  1 111 ? 18.298  -7.927   -11.583 1.00 33.39 ? 111 VAL   B O   1 
ATOM   2163  C  CB  . VAL   B  1 111 ? 16.343  -6.781   -9.769  1.00 35.05 ? 111 VAL   B CB  1 
ATOM   2164  C  CG1 . VAL   B  1 111 ? 15.748  -5.783   -8.795  1.00 39.97 ? 111 VAL   B CG1 1 
ATOM   2165  C  CG2 . VAL   B  1 111 ? 15.294  -7.827   -10.234 1.00 32.53 ? 111 VAL   B CG2 1 
ATOM   2166  N  N   . HIS   B  1 112 ? 17.320  -6.820   -13.268 1.00 28.91 ? 112 HIS   B N   1 
ATOM   2167  C  CA  . HIS   B  1 112 ? 18.009  -7.551   -14.347 1.00 29.82 ? 112 HIS   B CA  1 
ATOM   2168  C  C   . HIS   B  1 112 ? 17.597  -9.026   -14.415 1.00 28.93 ? 112 HIS   B C   1 
ATOM   2169  O  O   . HIS   B  1 112 ? 18.385  -9.889   -14.837 1.00 27.28 ? 112 HIS   B O   1 
ATOM   2170  C  CB  . HIS   B  1 112 ? 19.535  -7.445   -14.203 1.00 35.89 ? 112 HIS   B CB  1 
ATOM   2171  C  CG  . HIS   B  1 112 ? 20.031  -6.049   -13.989 1.00 34.49 ? 112 HIS   B CG  1 
ATOM   2172  N  ND1 . HIS   B  1 112 ? 19.413  -4.947   -14.534 1.00 43.21 ? 112 HIS   B ND1 1 
ATOM   2173  C  CD2 . HIS   B  1 112 ? 21.080  -5.575   -13.282 1.00 44.91 ? 112 HIS   B CD2 1 
ATOM   2174  C  CE1 . HIS   B  1 112 ? 20.058  -3.855   -14.172 1.00 35.68 ? 112 HIS   B CE1 1 
ATOM   2175  N  NE2 . HIS   B  1 112 ? 21.077  -4.207   -13.417 1.00 39.22 ? 112 HIS   B NE2 1 
ATOM   2176  N  N   . ASP   B  1 113 ? 16.395  -9.347   -13.943 1.00 29.23 ? 113 ASP   B N   1 
ATOM   2177  C  CA  . ASP   B  1 113 ? 15.860  -10.693  -14.096 1.00 29.05 ? 113 ASP   B CA  1 
ATOM   2178  C  C   . ASP   B  1 113 ? 15.124  -10.716  -15.437 1.00 29.65 ? 113 ASP   B C   1 
ATOM   2179  O  O   . ASP   B  1 113 ? 13.897  -10.621  -15.537 1.00 28.97 ? 113 ASP   B O   1 
ATOM   2180  C  CB  . ASP   B  1 113 ? 14.966  -11.062  -12.925 1.00 27.04 ? 113 ASP   B CB  1 
ATOM   2181  C  CG  . ASP   B  1 113 ? 14.501  -12.514  -12.990 1.00 34.05 ? 113 ASP   B CG  1 
ATOM   2182  O  OD1 . ASP   B  1 113 ? 14.789  -13.197  -14.010 1.00 27.59 ? 113 ASP   B OD1 1 
ATOM   2183  O  OD2 . ASP   B  1 113 ? 13.832  -12.951  -12.035 1.00 31.03 ? 113 ASP   B OD2 1 
ATOM   2184  N  N   . TYR   B  1 114 ? 15.921  -10.836  -16.495 1.00 29.04 ? 114 TYR   B N   1 
ATOM   2185  C  CA  . TYR   B  1 114 ? 15.394  -10.669  -17.841 1.00 27.52 ? 114 TYR   B CA  1 
ATOM   2186  C  C   . TYR   B  1 114 ? 14.580  -11.882  -18.282 1.00 27.01 ? 114 TYR   B C   1 
ATOM   2187  O  O   . TYR   B  1 114 ? 13.663  -11.737  -19.092 1.00 28.00 ? 114 TYR   B O   1 
ATOM   2188  C  CB  . TYR   B  1 114 ? 16.556  -10.391  -18.789 1.00 32.69 ? 114 TYR   B CB  1 
ATOM   2189  C  CG  . TYR   B  1 114 ? 17.296  -9.121   -18.440 1.00 24.77 ? 114 TYR   B CG  1 
ATOM   2190  C  CD1 . TYR   B  1 114 ? 16.649  -7.901   -18.469 1.00 28.11 ? 114 TYR   B CD1 1 
ATOM   2191  C  CD2 . TYR   B  1 114 ? 18.645  -9.144   -18.099 1.00 32.67 ? 114 TYR   B CD2 1 
ATOM   2192  C  CE1 . TYR   B  1 114 ? 17.301  -6.732   -18.157 1.00 31.10 ? 114 TYR   B CE1 1 
ATOM   2193  C  CE2 . TYR   B  1 114 ? 19.324  -7.974   -17.783 1.00 24.97 ? 114 TYR   B CE2 1 
ATOM   2194  C  CZ  . TYR   B  1 114 ? 18.646  -6.770   -17.820 1.00 32.92 ? 114 TYR   B CZ  1 
ATOM   2195  O  OH  . TYR   B  1 114 ? 19.301  -5.598   -17.536 1.00 34.68 ? 114 TYR   B OH  1 
ATOM   2196  N  N   . VAL   B  1 115 ? 14.863  -13.062  -17.724 1.00 28.46 ? 115 VAL   B N   1 
ATOM   2197  C  CA  . VAL   B  1 115 ? 14.089  -14.252  -18.059 1.00 27.48 ? 115 VAL   B CA  1 
ATOM   2198  C  C   . VAL   B  1 115 ? 12.696  -14.176  -17.417 1.00 25.00 ? 115 VAL   B C   1 
ATOM   2199  O  O   . VAL   B  1 115 ? 11.684  -14.460  -18.069 1.00 27.35 ? 115 VAL   B O   1 
ATOM   2200  C  CB  . VAL   B  1 115 ? 14.855  -15.525  -17.648 1.00 26.85 ? 115 VAL   B CB  1 
ATOM   2201  C  CG1 . VAL   B  1 115 ? 14.001  -16.782  -17.942 1.00 27.86 ? 115 VAL   B CG1 1 
ATOM   2202  C  CG2 . VAL   B  1 115 ? 16.230  -15.603  -18.368 1.00 29.64 ? 115 VAL   B CG2 1 
ATOM   2203  N  N   . SER   B  1 116 ? 12.610  -13.716  -16.169 1.00 23.92 ? 116 SER   B N   1 
ATOM   2204  C  CA  . SER   B  1 116 ? 11.298  -13.544  -15.553 1.00 23.52 ? 116 SER   B CA  1 
ATOM   2205  C  C   . SER   B  1 116 ? 10.503  -12.493  -16.303 1.00 28.97 ? 116 SER   B C   1 
ATOM   2206  O  O   . SER   B  1 116 ? 9.297   -12.662  -16.542 1.00 24.73 ? 116 SER   B O   1 
ATOM   2207  C  CB  . SER   B  1 116 ? 11.423  -13.175  -14.069 1.00 25.83 ? 116 SER   B CB  1 
ATOM   2208  O  OG  . SER   B  1 116 ? 11.837  -14.302  -13.303 1.00 25.26 ? 116 SER   B OG  1 
ATOM   2209  N  N   . ARG   B  1 117 ? 11.177  -11.426  -16.736 1.00 23.83 ? 117 ARG   B N   1 
ATOM   2210  C  CA  . ARG   B  1 117 ? 10.512  -10.432  -17.559 1.00 27.19 ? 117 ARG   B CA  1 
ATOM   2211  C  C   . ARG   B  1 117 ? 9.928   -11.072  -18.816 1.00 26.72 ? 117 ARG   B C   1 
ATOM   2212  O  O   . ARG   B  1 117 ? 8.797   -10.759  -19.202 1.00 25.93 ? 117 ARG   B O   1 
ATOM   2213  C  CB  . ARG   B  1 117 ? 11.482  -9.311   -17.959 1.00 27.04 ? 117 ARG   B CB  1 
ATOM   2214  C  CG  . ARG   B  1 117 ? 10.923  -8.487   -19.092 1.00 28.20 ? 117 ARG   B CG  1 
ATOM   2215  C  CD  . ARG   B  1 117 ? 11.662  -7.184   -19.333 1.00 26.03 ? 117 ARG   B CD  1 
ATOM   2216  N  NE  . ARG   B  1 117 ? 11.091  -6.492   -20.491 1.00 29.16 ? 117 ARG   B NE  1 
ATOM   2217  C  CZ  . ARG   B  1 117 ? 11.098  -5.179   -20.673 1.00 33.08 ? 117 ARG   B CZ  1 
ATOM   2218  N  NH1 . ARG   B  1 117 ? 11.726  -4.362   -19.830 1.00 30.96 ? 117 ARG   B NH1 1 
ATOM   2219  N  NH2 . ARG   B  1 117 ? 10.461  -4.672   -21.727 1.00 33.24 ? 117 ARG   B NH2 1 
ATOM   2220  N  N   . ASP   B  1 118 ? 10.709  -11.942  -19.485 1.00 25.92 ? 118 ASP   B N   1 
ATOM   2221  C  CA  . ASP   B  1 118 ? 10.266  -12.520  -20.752 1.00 26.76 ? 118 ASP   B CA  1 
ATOM   2222  C  C   . ASP   B  1 118 ? 9.045   -13.426  -20.553 1.00 25.68 ? 118 ASP   B C   1 
ATOM   2223  O  O   . ASP   B  1 118 ? 8.118   -13.415  -21.362 1.00 27.36 ? 118 ASP   B O   1 
ATOM   2224  C  CB  . ASP   B  1 118 ? 11.413  -13.300  -21.389 1.00 29.40 ? 118 ASP   B CB  1 
ATOM   2225  C  CG  . ASP   B  1 118 ? 11.196  -13.537  -22.881 1.00 33.86 ? 118 ASP   B CG  1 
ATOM   2226  O  OD1 . ASP   B  1 118 ? 10.796  -12.571  -23.552 1.00 32.45 ? 118 ASP   B OD1 1 
ATOM   2227  O  OD2 . ASP   B  1 118 ? 11.412  -14.665  -23.366 1.00 28.21 ? 118 ASP   B OD2 1 
ATOM   2228  N  N   . LEU   B  1 119 ? 9.046   -14.223  -19.487 1.00 27.68 ? 119 LEU   B N   1 
ATOM   2229  C  CA  . LEU   B  1 119 ? 7.884   -15.034  -19.133 1.00 29.74 ? 119 LEU   B CA  1 
ATOM   2230  C  C   . LEU   B  1 119 ? 6.653   -14.167  -18.915 1.00 26.37 ? 119 LEU   B C   1 
ATOM   2231  O  O   . LEU   B  1 119 ? 5.563   -14.478  -19.412 1.00 24.37 ? 119 LEU   B O   1 
ATOM   2232  C  CB  . LEU   B  1 119 ? 8.182   -15.840  -17.863 1.00 26.78 ? 119 LEU   B CB  1 
ATOM   2233  C  CG  . LEU   B  1 119 ? 6.983   -16.614  -17.270 1.00 27.82 ? 119 LEU   B CG  1 
ATOM   2234  C  CD1 . LEU   B  1 119 ? 6.404   -17.663  -18.226 1.00 27.77 ? 119 LEU   B CD1 1 
ATOM   2235  C  CD2 . LEU   B  1 119 ? 7.395   -17.274  -16.005 1.00 25.47 ? 119 LEU   B CD2 1 
ATOM   2236  N  N   . LEU   B  1 120 ? 6.813   -13.065  -18.180 1.00 26.14 ? 120 LEU   B N   1 
ATOM   2237  C  CA  . LEU   B  1 120 ? 5.680   -12.199  -17.872 1.00 27.57 ? 120 LEU   B CA  1 
ATOM   2238  C  C   . LEU   B  1 120 ? 5.202   -11.456  -19.110 1.00 22.23 ? 120 LEU   B C   1 
ATOM   2239  O  O   . LEU   B  1 120 ? 3.999   -11.230  -19.271 1.00 28.24 ? 120 LEU   B O   1 
ATOM   2240  C  CB  . LEU   B  1 120 ? 6.066   -11.200  -16.769 1.00 24.86 ? 120 LEU   B CB  1 
ATOM   2241  C  CG  . LEU   B  1 120 ? 6.417   -11.833  -15.436 1.00 26.92 ? 120 LEU   B CG  1 
ATOM   2242  C  CD1 . LEU   B  1 120 ? 6.936   -10.769  -14.506 1.00 32.54 ? 120 LEU   B CD1 1 
ATOM   2243  C  CD2 . LEU   B  1 120 ? 5.228   -12.572  -14.828 1.00 27.53 ? 120 LEU   B CD2 1 
ATOM   2244  N  N   . LYS   B  1 121 ? 6.125   -11.067  -19.995 1.00 26.19 ? 121 LYS   B N   1 
ATOM   2245  C  CA  . LYS   B  1 121 ? 5.727   -10.455  -21.262 1.00 22.84 ? 121 LYS   B CA  1 
ATOM   2246  C  C   . LYS   B  1 121 ? 4.876   -11.430  -22.076 1.00 25.36 ? 121 LYS   B C   1 
ATOM   2247  O  O   . LYS   B  1 121 ? 3.836   -11.054  -22.649 1.00 25.04 ? 121 LYS   B O   1 
ATOM   2248  C  CB  . LYS   B  1 121 ? 6.985   -10.033  -22.043 1.00 26.88 ? 121 LYS   B CB  1 
ATOM   2249  C  CG  . LYS   B  1 121 ? 6.764   -9.342   -23.356 1.00 27.79 ? 121 LYS   B CG  1 
ATOM   2250  C  CD  . LYS   B  1 121 ? 6.690   -10.319  -24.526 1.00 31.53 ? 121 LYS   B CD  1 
ATOM   2251  C  CE  . LYS   B  1 121 ? 8.039   -10.962  -24.817 1.00 32.11 ? 121 LYS   B CE  1 
ATOM   2252  N  NZ  . LYS   B  1 121 ? 7.875   -11.942  -25.945 1.00 37.42 ? 121 LYS   B NZ  1 
ATOM   2253  N  N   . ASP   B  1 122 ? 5.289   -12.700  -22.117 1.00 27.06 ? 122 ASP   B N   1 
ATOM   2254  C  CA  . ASP   B  1 122 ? 4.511   -13.701  -22.852 1.00 30.28 ? 122 ASP   B CA  1 
ATOM   2255  C  C   . ASP   B  1 122 ? 3.111   -13.863  -22.252 1.00 25.66 ? 122 ASP   B C   1 
ATOM   2256  O  O   . ASP   B  1 122 ? 2.123   -13.987  -22.981 1.00 26.11 ? 122 ASP   B O   1 
ATOM   2257  C  CB  . ASP   B  1 122 ? 5.231   -15.048  -22.836 1.00 31.07 ? 122 ASP   B CB  1 
ATOM   2258  C  CG  . ASP   B  1 122 ? 6.495   -15.079  -23.695 1.00 31.65 ? 122 ASP   B CG  1 
ATOM   2259  O  OD1 . ASP   B  1 122 ? 6.680   -14.221  -24.569 1.00 29.06 ? 122 ASP   B OD1 1 
ATOM   2260  O  OD2 . ASP   B  1 122 ? 7.294   -16.014  -23.493 1.00 30.17 ? 122 ASP   B OD2 1 
ATOM   2261  N  N   . ILE   B  1 123 ? 3.012   -13.912  -20.925 1.00 26.21 ? 123 ILE   B N   1 
ATOM   2262  C  CA  . ILE   B  1 123 ? 1.696   -13.999  -20.294 1.00 24.68 ? 123 ILE   B CA  1 
ATOM   2263  C  C   . ILE   B  1 123 ? 0.884   -12.750  -20.614 1.00 25.33 ? 123 ILE   B C   1 
ATOM   2264  O  O   . ILE   B  1 123 ? -0.304  -12.829  -20.958 1.00 25.95 ? 123 ILE   B O   1 
ATOM   2265  C  CB  . ILE   B  1 123 ? 1.864   -14.232  -18.785 1.00 25.81 ? 123 ILE   B CB  1 
ATOM   2266  C  CG1 . ILE   B  1 123 ? 2.518   -15.598  -18.549 1.00 26.82 ? 123 ILE   B CG1 1 
ATOM   2267  C  CG2 . ILE   B  1 123 ? 0.496   -14.102  -18.005 1.00 26.65 ? 123 ILE   B CG2 1 
ATOM   2268  C  CD1 . ILE   B  1 123 ? 2.814   -15.890  -17.079 1.00 26.93 ? 123 ILE   B CD1 1 
ATOM   2269  N  N   . LEU   B  1 124 ? 1.521   -11.578  -20.550 1.00 27.08 ? 124 LEU   B N   1 
ATOM   2270  C  CA  . LEU   B  1 124 ? 0.816   -10.334  -20.863 1.00 25.38 ? 124 LEU   B CA  1 
ATOM   2271  C  C   . LEU   B  1 124 ? 0.271   -10.346  -22.288 1.00 23.76 ? 124 LEU   B C   1 
ATOM   2272  O  O   . LEU   B  1 124 ? -0.858  -9.889   -22.534 1.00 27.40 ? 124 LEU   B O   1 
ATOM   2273  C  CB  . LEU   B  1 124 ? 1.766   -9.150   -20.628 1.00 25.46 ? 124 LEU   B CB  1 
ATOM   2274  C  CG  . LEU   B  1 124 ? 1.280   -7.755   -20.993 1.00 27.41 ? 124 LEU   B CG  1 
ATOM   2275  C  CD1 . LEU   B  1 124 ? 0.075   -7.370   -20.131 1.00 29.77 ? 124 LEU   B CD1 1 
ATOM   2276  C  CD2 . LEU   B  1 124 ? 2.484   -6.777   -20.838 1.00 30.89 ? 124 LEU   B CD2 1 
ATOM   2277  N  N   . GLU   B  1 125 ? 1.045   -10.892  -23.247 1.00 25.48 ? 125 GLU   B N   1 
ATOM   2278  C  CA  . GLU   B  1 125 ? 0.561   -10.981  -24.625 1.00 24.10 ? 125 GLU   B CA  1 
ATOM   2279  C  C   . GLU   B  1 125 ? -0.704  -11.842  -24.707 1.00 24.09 ? 125 GLU   B C   1 
ATOM   2280  O  O   . GLU   B  1 125 ? -1.660  -11.488  -25.397 1.00 23.30 ? 125 GLU   B O   1 
ATOM   2281  C  CB  . GLU   B  1 125 ? 1.671   -11.517  -25.556 1.00 24.73 ? 125 GLU   B CB  1 
ATOM   2282  C  CG  . GLU   B  1 125 ? 2.701   -10.468  -25.846 1.00 32.75 ? 125 GLU   B CG  1 
ATOM   2283  C  CD  . GLU   B  1 125 ? 3.908   -10.942  -26.652 1.00 45.42 ? 125 GLU   B CD  1 
ATOM   2284  O  OE1 . GLU   B  1 125 ? 4.241   -12.160  -26.631 1.00 36.01 ? 125 GLU   B OE1 1 
ATOM   2285  O  OE2 . GLU   B  1 125 ? 4.533   -10.061  -27.302 1.00 40.34 ? 125 GLU   B OE2 1 
ATOM   2286  N  N   . SER   B  1 126 ? -0.740  -12.955  -23.970 1.00 25.86 ? 126 SER   B N   1 
ATOM   2287  C  CA  A SER   B  1 126 ? -1.940  -13.779  -23.902 0.50 27.74 ? 126 SER   B CA  1 
ATOM   2288  C  CA  B SER   B  1 126 ? -1.952  -13.765  -23.928 0.50 27.71 ? 126 SER   B CA  1 
ATOM   2289  C  C   . SER   B  1 126 ? -3.109  -13.008  -23.284 1.00 24.04 ? 126 SER   B C   1 
ATOM   2290  O  O   . SER   B  1 126 ? -4.238  -13.046  -23.788 1.00 26.11 ? 126 SER   B O   1 
ATOM   2291  C  CB  A SER   B  1 126 ? -1.631  -15.046  -23.095 0.50 30.90 ? 126 SER   B CB  1 
ATOM   2292  C  CB  B SER   B  1 126 ? -1.692  -15.068  -23.178 0.50 30.90 ? 126 SER   B CB  1 
ATOM   2293  O  OG  A SER   B  1 126 ? -2.806  -15.750  -22.768 0.50 23.60 ? 126 SER   B OG  1 
ATOM   2294  O  OG  B SER   B  1 126 ? -0.764  -15.846  -23.893 0.50 25.73 ? 126 SER   B OG  1 
ATOM   2295  N  N   . GLU   B  1 127 ? -2.858  -12.306  -22.184 1.00 24.60 ? 127 GLU   B N   1 
ATOM   2296  C  CA  . GLU   B  1 127 ? -3.953  -11.595  -21.519 1.00 28.52 ? 127 GLU   B CA  1 
ATOM   2297  C  C   . GLU   B  1 127 ? -4.493  -10.458  -22.392 1.00 25.62 ? 127 GLU   B C   1 
ATOM   2298  O  O   . GLU   B  1 127 ? -5.702  -10.201  -22.402 1.00 27.30 ? 127 GLU   B O   1 
ATOM   2299  C  CB  . GLU   B  1 127 ? -3.503  -11.061  -20.158 1.00 25.24 ? 127 GLU   B CB  1 
ATOM   2300  C  CG  . GLU   B  1 127 ? -2.976  -12.126  -19.140 1.00 25.38 ? 127 GLU   B CG  1 
ATOM   2301  C  CD  . GLU   B  1 127 ? -3.883  -13.345  -18.970 1.00 35.65 ? 127 GLU   B CD  1 
ATOM   2302  O  OE1 . GLU   B  1 127 ? -5.102  -13.213  -19.075 1.00 35.09 ? 127 GLU   B OE1 1 
ATOM   2303  O  OE2 . GLU   B  1 127 ? -3.370  -14.449  -18.717 1.00 46.01 ? 127 GLU   B OE2 1 
ATOM   2304  N  N   . GLU   B  1 128 ? -3.628  -9.780   -23.153 1.00 24.83 ? 128 GLU   B N   1 
ATOM   2305  C  CA  . GLU   B  1 128 ? -4.137  -8.751   -24.049 1.00 29.54 ? 128 GLU   B CA  1 
ATOM   2306  C  C   . GLU   B  1 128 ? -4.979  -9.363   -25.162 1.00 28.08 ? 128 GLU   B C   1 
ATOM   2307  O  O   . GLU   B  1 128 ? -5.977  -8.764   -25.571 1.00 25.70 ? 128 GLU   B O   1 
ATOM   2308  C  CB  . GLU   B  1 128 ? -2.988  -7.895   -24.606 1.00 26.91 ? 128 GLU   B CB  1 
ATOM   2309  C  CG  . GLU   B  1 128 ? -2.378  -6.973   -23.536 1.00 30.74 ? 128 GLU   B CG  1 
ATOM   2310  C  CD  . GLU   B  1 128 ? -1.452  -5.885   -24.075 1.00 31.06 ? 128 GLU   B CD  1 
ATOM   2311  O  OE1 . GLU   B  1 128 ? -1.328  -5.735   -25.299 1.00 28.76 ? 128 GLU   B OE1 1 
ATOM   2312  O  OE2 . GLU   B  1 128 ? -0.833  -5.168   -23.263 1.00 30.96 ? 128 GLU   B OE2 1 
ATOM   2313  N  N   . GLU   B  1 129 ? -4.632  -10.573  -25.620 1.00 28.66 ? 129 GLU   B N   1 
ATOM   2314  C  CA  . GLU   B  1 129 ? -5.503  -11.273  -26.562 1.00 31.91 ? 129 GLU   B CA  1 
ATOM   2315  C  C   . GLU   B  1 129 ? -6.854  -11.593  -25.934 1.00 25.88 ? 129 GLU   B C   1 
ATOM   2316  O  O   . GLU   B  1 129 ? -7.891  -11.483  -26.598 1.00 26.37 ? 129 GLU   B O   1 
ATOM   2317  C  CB  . GLU   B  1 129 ? -4.843  -12.559  -27.055 1.00 33.04 ? 129 GLU   B CB  1 
ATOM   2318  C  CG  . GLU   B  1 129 ? -3.666  -12.336  -28.016 1.00 41.55 ? 129 GLU   B CG  1 
ATOM   2319  C  CD  . GLU   B  1 129 ? -3.230  -13.619  -28.698 1.00 57.42 ? 129 GLU   B CD  1 
ATOM   2320  O  OE1 . GLU   B  1 129 ? -4.095  -14.505  -28.912 1.00 63.96 ? 129 GLU   B OE1 1 
ATOM   2321  O  OE2 . GLU   B  1 129 ? -2.028  -13.742  -29.017 1.00 60.00 ? 129 GLU   B OE2 1 
ATOM   2322  N  N   . HIS   B  1 130 ? -6.856  -12.024  -24.671 1.00 27.15 ? 130 HIS   B N   1 
ATOM   2323  C  CA  A HIS   B  1 130 ? -8.126  -12.274  -24.017 0.50 28.38 ? 130 HIS   B CA  1 
ATOM   2324  C  CA  B HIS   B  1 130 ? -8.105  -12.261  -23.946 0.50 28.40 ? 130 HIS   B CA  1 
ATOM   2325  C  C   . HIS   B  1 130 ? -8.916  -10.979  -23.840 1.00 30.76 ? 130 HIS   B C   1 
ATOM   2326  O  O   . HIS   B  1 130 ? -10.141 -10.979  -23.990 1.00 24.57 ? 130 HIS   B O   1 
ATOM   2327  C  CB  A HIS   B  1 130 ? -7.902  -12.988  -22.681 0.50 29.26 ? 130 HIS   B CB  1 
ATOM   2328  C  CB  B HIS   B  1 130 ? -7.846  -12.776  -22.517 0.50 29.46 ? 130 HIS   B CB  1 
ATOM   2329  C  CG  A HIS   B  1 130 ? -9.158  -13.544  -22.087 0.50 36.71 ? 130 HIS   B CG  1 
ATOM   2330  C  CG  B HIS   B  1 130 ? -7.220  -14.135  -22.420 0.50 28.56 ? 130 HIS   B CG  1 
ATOM   2331  N  ND1 A HIS   B  1 130 ? -9.234  -14.016  -20.794 0.50 34.12 ? 130 HIS   B ND1 1 
ATOM   2332  N  ND1 B HIS   B  1 130 ? -6.880  -14.898  -23.516 0.50 30.59 ? 130 HIS   B ND1 1 
ATOM   2333  C  CD2 A HIS   B  1 130 ? -10.391 -13.716  -22.622 0.50 34.92 ? 130 HIS   B CD2 1 
ATOM   2334  C  CD2 B HIS   B  1 130 ? -6.835  -14.851  -21.332 0.50 32.06 ? 130 HIS   B CD2 1 
ATOM   2335  C  CE1 A HIS   B  1 130 ? -10.463 -14.439  -20.555 0.50 31.42 ? 130 HIS   B CE1 1 
ATOM   2336  C  CE1 B HIS   B  1 130 ? -6.307  -16.018  -23.111 0.50 24.17 ? 130 HIS   B CE1 1 
ATOM   2337  N  NE2 A HIS   B  1 130 ? -11.183 -14.266  -21.646 0.50 37.70 ? 130 HIS   B NE2 1 
ATOM   2338  N  NE2 B HIS   B  1 130 ? -6.283  -16.024  -21.790 0.50 30.43 ? 130 HIS   B NE2 1 
ATOM   2339  N  N   . ILE   B  1 131 ? -8.242  -9.863   -23.547 1.00 25.08 ? 131 ILE   B N   1 
ATOM   2340  C  CA  . ILE   B  1 131 ? -8.957  -8.596   -23.427 1.00 32.26 ? 131 ILE   B CA  1 
ATOM   2341  C  C   . ILE   B  1 131 ? -9.574  -8.215   -24.769 1.00 29.60 ? 131 ILE   B C   1 
ATOM   2342  O  O   . ILE   B  1 131 ? -10.725 -7.790   -24.828 1.00 28.30 ? 131 ILE   B O   1 
ATOM   2343  C  CB  . ILE   B  1 131 ? -8.027  -7.487   -22.891 1.00 27.09 ? 131 ILE   B CB  1 
ATOM   2344  C  CG1 . ILE   B  1 131 ? -7.810  -7.647   -21.393 1.00 26.97 ? 131 ILE   B CG1 1 
ATOM   2345  C  CG2 . ILE   B  1 131 ? -8.619  -6.101   -23.175 1.00 30.43 ? 131 ILE   B CG2 1 
ATOM   2346  C  CD1 . ILE   B  1 131 ? -6.630  -6.895   -20.846 1.00 30.98 ? 131 ILE   B CD1 1 
ATOM   2347  N  N   . ASP   B  1 132 ? -8.808  -8.355   -25.858 1.00 28.79 ? 132 ASP   B N   1 
ATOM   2348  C  CA  . ASP   B  1 132 ? -9.339  -8.175   -27.210 1.00 27.15 ? 132 ASP   B CA  1 
ATOM   2349  C  C   . ASP   B  1 132 ? -10.618 -8.988   -27.416 1.00 29.02 ? 132 ASP   B C   1 
ATOM   2350  O  O   . ASP   B  1 132 ? -11.659 -8.453   -27.819 1.00 30.05 ? 132 ASP   B O   1 
ATOM   2351  C  CB  . ASP   B  1 132 ? -8.258  -8.567   -28.223 1.00 29.24 ? 132 ASP   B CB  1 
ATOM   2352  C  CG  . ASP   B  1 132 ? -8.559  -8.082   -29.656 1.00 36.45 ? 132 ASP   B CG  1 
ATOM   2353  O  OD1 . ASP   B  1 132 ? -9.534  -7.356   -29.873 1.00 31.61 ? 132 ASP   B OD1 1 
ATOM   2354  O  OD2 . ASP   B  1 132 ? -7.773  -8.415   -30.562 1.00 38.64 ? 132 ASP   B OD2 1 
ATOM   2355  N  N   . TYR   B  1 133 ? -10.561 -10.285  -27.125 1.00 27.02 ? 133 TYR   B N   1 
ATOM   2356  C  CA  . TYR   B  1 133 ? -11.751 -11.128  -27.245 1.00 26.28 ? 133 TYR   B CA  1 
ATOM   2357  C  C   . TYR   B  1 133 ? -12.922 -10.577  -26.432 1.00 29.31 ? 133 TYR   B C   1 
ATOM   2358  O  O   . TYR   B  1 133 ? -14.024 -10.423  -26.960 1.00 28.47 ? 133 TYR   B O   1 
ATOM   2359  C  CB  . TYR   B  1 133 ? -11.436 -12.573  -26.825 1.00 29.71 ? 133 TYR   B CB  1 
ATOM   2360  C  CG  . TYR   B  1 133 ? -12.672 -13.446  -26.667 1.00 28.08 ? 133 TYR   B CG  1 
ATOM   2361  C  CD1 . TYR   B  1 133 ? -13.266 -14.052  -27.751 1.00 30.41 ? 133 TYR   B CD1 1 
ATOM   2362  C  CD2 . TYR   B  1 133 ? -13.233 -13.655  -25.423 1.00 31.62 ? 133 TYR   B CD2 1 
ATOM   2363  C  CE1 . TYR   B  1 133 ? -14.415 -14.846  -27.594 1.00 29.56 ? 133 TYR   B CE1 1 
ATOM   2364  C  CE2 . TYR   B  1 133 ? -14.345 -14.437  -25.260 1.00 32.24 ? 133 TYR   B CE2 1 
ATOM   2365  C  CZ  . TYR   B  1 133 ? -14.938 -15.018  -26.350 1.00 31.48 ? 133 TYR   B CZ  1 
ATOM   2366  O  OH  . TYR   B  1 133 ? -16.049 -15.801  -26.156 1.00 36.64 ? 133 TYR   B OH  1 
ATOM   2367  N  N   . LEU   B  1 134 ? -12.698 -10.234  -25.153 1.00 31.18 ? 134 LEU   B N   1 
ATOM   2368  C  CA  . LEU   B  1 134 ? -13.808 -9.807   -24.297 1.00 27.02 ? 134 LEU   B CA  1 
ATOM   2369  C  C   . LEU   B  1 134 ? -14.398 -8.471   -24.760 1.00 34.24 ? 134 LEU   B C   1 
ATOM   2370  O  O   . LEU   B  1 134 ? -15.630 -8.321   -24.864 1.00 27.96 ? 134 LEU   B O   1 
ATOM   2371  C  CB  . LEU   B  1 134 ? -13.335 -9.714   -22.847 1.00 32.48 ? 134 LEU   B CB  1 
ATOM   2372  C  CG  . LEU   B  1 134 ? -12.960 -11.029  -22.175 1.00 27.32 ? 134 LEU   B CG  1 
ATOM   2373  C  CD1 . LEU   B  1 134 ? -12.209 -10.741  -20.925 1.00 30.05 ? 134 LEU   B CD1 1 
ATOM   2374  C  CD2 . LEU   B  1 134 ? -14.173 -11.873  -21.867 1.00 32.41 ? 134 LEU   B CD2 1 
ATOM   2375  N  N   . GLU   B  1 135 ? -13.543 -7.471   -25.014 1.00 29.30 ? 135 GLU   B N   1 
ATOM   2376  C  CA  . GLU   B  1 135 ? -14.068 -6.214   -25.540 1.00 33.48 ? 135 GLU   B CA  1 
ATOM   2377  C  C   . GLU   B  1 135 ? -14.861 -6.451   -26.817 1.00 33.90 ? 135 GLU   B C   1 
ATOM   2378  O  O   . GLU   B  1 135 ? -15.909 -5.832   -27.029 1.00 32.34 ? 135 GLU   B O   1 
ATOM   2379  C  CB  . GLU   B  1 135 ? -12.940 -5.221   -25.803 1.00 31.88 ? 135 GLU   B CB  1 
ATOM   2380  C  CG  . GLU   B  1 135 ? -12.137 -4.829   -24.592 1.00 32.72 ? 135 GLU   B CG  1 
ATOM   2381  C  CD  . GLU   B  1 135 ? -10.969 -3.922   -24.938 1.00 36.58 ? 135 GLU   B CD  1 
ATOM   2382  O  OE1 . GLU   B  1 135 ? -10.311 -4.117   -25.988 1.00 36.78 ? 135 GLU   B OE1 1 
ATOM   2383  O  OE2 . GLU   B  1 135 ? -10.674 -3.024   -24.129 1.00 37.96 ? 135 GLU   B OE2 1 
ATOM   2384  N  N   . THR   B  1 136 ? -14.373 -7.350   -27.679 1.00 29.00 ? 136 THR   B N   1 
ATOM   2385  C  CA  . THR   B  1 136 ? -15.051 -7.635   -28.939 1.00 27.23 ? 136 THR   B CA  1 
ATOM   2386  C  C   . THR   B  1 136 ? -16.405 -8.293   -28.717 1.00 28.59 ? 136 THR   B C   1 
ATOM   2387  O  O   . THR   B  1 136 ? -17.380 -7.969   -29.416 1.00 29.89 ? 136 THR   B O   1 
ATOM   2388  C  CB  . THR   B  1 136 ? -14.162 -8.521   -29.835 1.00 28.73 ? 136 THR   B CB  1 
ATOM   2389  O  OG1 . THR   B  1 136 ? -12.980 -7.797   -30.187 1.00 30.22 ? 136 THR   B OG1 1 
ATOM   2390  C  CG2 . THR   B  1 136 ? -14.896 -8.955   -31.121 1.00 32.72 ? 136 THR   B CG2 1 
ATOM   2391  N  N   . GLN   B  1 137 ? -16.499 -9.229   -27.767 1.00 28.52 ? 137 GLN   B N   1 
ATOM   2392  C  CA  . GLN   B  1 137 ? -17.802 -9.844   -27.499 1.00 32.02 ? 137 GLN   B CA  1 
ATOM   2393  C  C   . GLN   B  1 137 ? -18.798 -8.802   -26.997 1.00 30.41 ? 137 GLN   B C   1 
ATOM   2394  O  O   . GLN   B  1 137 ? -19.967 -8.783   -27.409 1.00 27.78 ? 137 GLN   B O   1 
ATOM   2395  C  CB  . GLN   B  1 137 ? -17.664 -10.976  -26.469 1.00 32.87 ? 137 GLN   B CB  1 
ATOM   2396  C  CG  . GLN   B  1 137 ? -16.732 -12.118  -26.870 1.00 30.58 ? 137 GLN   B CG  1 
ATOM   2397  C  CD  . GLN   B  1 137 ? -16.792 -12.447  -28.342 1.00 31.04 ? 137 GLN   B CD  1 
ATOM   2398  O  OE1 . GLN   B  1 137 ? -15.851 -12.164  -29.096 1.00 37.46 ? 137 GLN   B OE1 1 
ATOM   2399  N  NE2 . GLN   B  1 137 ? -17.857 -13.069  -28.751 1.00 27.35 ? 137 GLN   B NE2 1 
ATOM   2400  N  N   . LEU   B  1 138 ? -18.360 -7.943   -26.080 1.00 30.16 ? 138 LEU   B N   1 
ATOM   2401  C  CA  . LEU   B  1 138 ? -19.272 -6.948   -25.538 1.00 36.16 ? 138 LEU   B CA  1 
ATOM   2402  C  C   . LEU   B  1 138 ? -19.711 -5.965   -26.615 1.00 34.36 ? 138 LEU   B C   1 
ATOM   2403  O  O   . LEU   B  1 138 ? -20.843 -5.484   -26.578 1.00 33.14 ? 138 LEU   B O   1 
ATOM   2404  C  CB  . LEU   B  1 138 ? -18.608 -6.225   -24.363 1.00 27.98 ? 138 LEU   B CB  1 
ATOM   2405  C  CG  . LEU   B  1 138 ? -18.495 -7.050   -23.066 1.00 31.95 ? 138 LEU   B CG  1 
ATOM   2406  C  CD1 . LEU   B  1 138 ? -17.538 -6.413   -22.060 1.00 36.86 ? 138 LEU   B CD1 1 
ATOM   2407  C  CD2 . LEU   B  1 138 ? -19.892 -7.249   -22.435 1.00 37.10 ? 138 LEU   B CD2 1 
ATOM   2408  N  N   . GLY   B  1 139 ? -18.850 -5.682   -27.593 1.00 33.30 ? 139 GLY   B N   1 
ATOM   2409  C  CA  . GLY   B  1 139 ? -19.274 -4.843   -28.707 1.00 28.25 ? 139 GLY   B CA  1 
ATOM   2410  C  C   . GLY   B  1 139 ? -20.269 -5.548   -29.608 1.00 35.76 ? 139 GLY   B C   1 
ATOM   2411  O  O   . GLY   B  1 139 ? -21.235 -4.937   -30.088 1.00 34.85 ? 139 GLY   B O   1 
ATOM   2412  N  N   . LEU   B  1 140 ? -20.052 -6.848   -29.845 1.00 26.12 ? 140 LEU   B N   1 
ATOM   2413  C  CA  . LEU   B  1 140 ? -20.971 -7.617   -30.671 1.00 22.73 ? 140 LEU   B CA  1 
ATOM   2414  C  C   . LEU   B  1 140 ? -22.383 -7.613   -30.088 1.00 28.28 ? 140 LEU   B C   1 
ATOM   2415  O  O   . LEU   B  1 140 ? -23.369 -7.518   -30.838 1.00 29.42 ? 140 LEU   B O   1 
ATOM   2416  C  CB  . LEU   B  1 140 ? -20.469 -9.047   -30.846 1.00 25.91 ? 140 LEU   B CB  1 
ATOM   2417  C  CG  . LEU   B  1 140 ? -19.380 -9.163   -31.919 1.00 27.88 ? 140 LEU   B CG  1 
ATOM   2418  C  CD1 . LEU   B  1 140 ? -18.717 -10.536  -31.912 1.00 29.52 ? 140 LEU   B CD1 1 
ATOM   2419  C  CD2 . LEU   B  1 140 ? -19.956 -8.863   -33.277 1.00 26.98 ? 140 LEU   B CD2 1 
ATOM   2420  N  N   . ILE   B  1 141 ? -22.497 -7.723   -28.760 1.00 27.59 ? 141 ILE   B N   1 
ATOM   2421  C  CA  . ILE   B  1 141 ? -23.813 -7.711   -28.112 1.00 32.24 ? 141 ILE   B CA  1 
ATOM   2422  C  C   . ILE   B  1 141 ? -24.560 -6.430   -28.475 1.00 34.88 ? 141 ILE   B C   1 
ATOM   2423  O  O   . ILE   B  1 141 ? -25.749 -6.465   -28.796 1.00 34.69 ? 141 ILE   B O   1 
ATOM   2424  C  CB  . ILE   B  1 141 ? -23.662 -7.883   -26.585 1.00 31.54 ? 141 ILE   B CB  1 
ATOM   2425  C  CG1 . ILE   B  1 141 ? -23.401 -9.360   -26.219 1.00 31.19 ? 141 ILE   B CG1 1 
ATOM   2426  C  CG2 . ILE   B  1 141 ? -24.879 -7.409   -25.849 1.00 34.64 ? 141 ILE   B CG2 1 
ATOM   2427  C  CD1 . ILE   B  1 141 ? -22.963 -9.580   -24.793 1.00 31.09 ? 141 ILE   B CD1 1 
ATOM   2428  N  N   . GLN   B  1 142 ? -23.857 -5.292   -28.490 1.00 32.68 ? 142 GLN   B N   1 
ATOM   2429  C  CA  . GLN   B  1 142 ? -24.460 -4.028   -28.908 1.00 37.05 ? 142 GLN   B CA  1 
ATOM   2430  C  C   . GLN   B  1 142 ? -24.791 -4.010   -30.399 1.00 38.51 ? 142 GLN   B C   1 
ATOM   2431  O  O   . GLN   B  1 142 ? -25.817 -3.452   -30.801 1.00 43.20 ? 142 GLN   B O   1 
ATOM   2432  C  CB  . GLN   B  1 142 ? -23.523 -2.871   -28.567 1.00 32.90 ? 142 GLN   B CB  1 
ATOM   2433  C  CG  . GLN   B  1 142 ? -23.250 -2.722   -27.087 1.00 35.70 ? 142 GLN   B CG  1 
ATOM   2434  C  CD  . GLN   B  1 142 ? -24.509 -2.521   -26.253 1.00 49.39 ? 142 GLN   B CD  1 
ATOM   2435  O  OE1 . GLN   B  1 142 ? -25.388 -1.720   -26.597 1.00 51.71 ? 142 GLN   B OE1 1 
ATOM   2436  N  NE2 . GLN   B  1 142 ? -24.602 -3.260   -25.146 1.00 37.95 ? 142 GLN   B NE2 1 
ATOM   2437  N  N   . LYS   B  1 143 ? -23.935 -4.587   -31.246 1.00 36.77 ? 143 LYS   B N   1 
ATOM   2438  C  CA  . LYS   B  1 143 ? -24.157 -4.472   -32.685 1.00 36.29 ? 143 LYS   B CA  1 
ATOM   2439  C  C   . LYS   B  1 143 ? -25.254 -5.403   -33.165 1.00 39.23 ? 143 LYS   B C   1 
ATOM   2440  O  O   . LYS   B  1 143 ? -26.072 -5.014   -34.006 1.00 39.31 ? 143 LYS   B O   1 
ATOM   2441  C  CB  . LYS   B  1 143 ? -22.867 -4.754   -33.464 1.00 37.51 ? 143 LYS   B CB  1 
ATOM   2442  C  CG  . LYS   B  1 143 ? -21.806 -3.659   -33.372 1.00 44.71 ? 143 LYS   B CG  1 
ATOM   2443  C  CD  . LYS   B  1 143 ? -20.561 -4.014   -34.206 1.00 43.91 ? 143 LYS   B CD  1 
ATOM   2444  C  CE  . LYS   B  1 143 ? -19.680 -2.802   -34.448 1.00 51.40 ? 143 LYS   B CE  1 
ATOM   2445  N  NZ  . LYS   B  1 143 ? -18.998 -2.361   -33.174 1.00 58.33 ? 143 LYS   B NZ  1 
ATOM   2446  N  N   . VAL   B  1 144 ? -25.283 -6.648   -32.674 1.00 33.98 ? 144 VAL   B N   1 
ATOM   2447  C  CA  . VAL   B  1 144 ? -26.257 -7.616   -33.166 1.00 35.96 ? 144 VAL   B CA  1 
ATOM   2448  C  C   . VAL   B  1 144 ? -27.448 -7.796   -32.238 1.00 30.92 ? 144 VAL   B C   1 
ATOM   2449  O  O   . VAL   B  1 144 ? -28.442 -8.424   -32.646 1.00 32.47 ? 144 VAL   B O   1 
ATOM   2450  C  CB  . VAL   B  1 144 ? -25.589 -8.980   -33.445 1.00 31.38 ? 144 VAL   B CB  1 
ATOM   2451  C  CG1 . VAL   B  1 144 ? -24.390 -8.777   -34.316 1.00 33.03 ? 144 VAL   B CG1 1 
ATOM   2452  C  CG2 . VAL   B  1 144 ? -25.189 -9.693   -32.160 1.00 33.00 ? 144 VAL   B CG2 1 
ATOM   2453  N  N   . GLY   B  1 145 ? -27.411 -7.230   -31.036 1.00 29.62 ? 145 GLY   B N   1 
ATOM   2454  C  CA  . GLY   B  1 145 ? -28.457 -7.504   -30.047 1.00 33.64 ? 145 GLY   B CA  1 
ATOM   2455  C  C   . GLY   B  1 145 ? -28.179 -8.758   -29.237 1.00 33.98 ? 145 GLY   B C   1 
ATOM   2456  O  O   . GLY   B  1 145 ? -27.571 -9.718   -29.713 1.00 30.12 ? 145 GLY   B O   1 
ATOM   2457  N  N   . LEU   B  1 146 ? -28.665 -8.754   -27.988 1.00 30.76 ? 146 LEU   B N   1 
ATOM   2458  C  CA  . LEU   B  1 146 ? -28.366 -9.844   -27.054 1.00 30.30 ? 146 LEU   B CA  1 
ATOM   2459  C  C   . LEU   B  1 146 ? -28.944 -11.169  -27.533 1.00 28.91 ? 146 LEU   B C   1 
ATOM   2460  O  O   . LEU   B  1 146 ? -28.276 -12.211  -27.459 1.00 29.65 ? 146 LEU   B O   1 
ATOM   2461  C  CB  . LEU   B  1 146 ? -28.885 -9.497   -25.653 1.00 32.79 ? 146 LEU   B CB  1 
ATOM   2462  C  CG  . LEU   B  1 146 ? -28.592 -10.487  -24.505 1.00 31.18 ? 146 LEU   B CG  1 
ATOM   2463  C  CD1 . LEU   B  1 146 ? -27.126 -10.840  -24.416 1.00 30.56 ? 146 LEU   B CD1 1 
ATOM   2464  C  CD2 . LEU   B  1 146 ? -29.071 -9.991   -23.118 1.00 35.08 ? 146 LEU   B CD2 1 
ATOM   2465  N  N   . GLU   B  1 147 ? -30.173 -11.155  -28.053 1.00 28.86 ? 147 GLU   B N   1 
ATOM   2466  C  CA  . GLU   B  1 147 ? -30.808 -12.391  -28.506 1.00 28.16 ? 147 GLU   B CA  1 
ATOM   2467  C  C   . GLU   B  1 147 ? -30.031 -13.029  -29.660 1.00 31.07 ? 147 GLU   B C   1 
ATOM   2468  O  O   . GLU   B  1 147 ? -29.780 -14.241  -29.643 1.00 25.60 ? 147 GLU   B O   1 
ATOM   2469  C  CB  . GLU   B  1 147 ? -32.268 -12.141  -28.909 1.00 37.63 ? 147 GLU   B CB  1 
ATOM   2470  C  CG  . GLU   B  1 147 ? -33.199 -11.787  -27.747 1.00 39.50 ? 147 GLU   B CG  1 
ATOM   2471  C  CD  . GLU   B  1 147 ? -34.674 -11.854  -28.129 1.00 49.42 ? 147 GLU   B CD  1 
ATOM   2472  O  OE1 . GLU   B  1 147 ? -35.010 -11.552  -29.293 1.00 46.79 ? 147 GLU   B OE1 1 
ATOM   2473  O  OE2 . GLU   B  1 147 ? -35.494 -12.233  -27.266 1.00 49.16 ? 147 GLU   B OE2 1 
ATOM   2474  N  N   . ASN   B  1 148 ? -29.637 -12.231  -30.666 1.00 28.22 ? 148 ASN   B N   1 
ATOM   2475  C  CA  . ASN   B  1 148 ? -28.794 -12.769  -31.742 1.00 29.13 ? 148 ASN   B CA  1 
ATOM   2476  C  C   . ASN   B  1 148 ? -27.428 -13.205  -31.212 1.00 30.41 ? 148 ASN   B C   1 
ATOM   2477  O  O   . ASN   B  1 148 ? -26.923 -14.267  -31.584 1.00 28.68 ? 148 ASN   B O   1 
ATOM   2478  C  CB  . ASN   B  1 148 ? -28.599 -11.732  -32.854 1.00 29.28 ? 148 ASN   B CB  1 
ATOM   2479  C  CG  . ASN   B  1 148 ? -29.713 -11.735  -33.866 1.00 27.47 ? 148 ASN   B CG  1 
ATOM   2480  O  OD1 . ASN   B  1 148 ? -30.669 -12.499  -33.772 1.00 24.36 ? 148 ASN   B OD1 1 
ATOM   2481  N  ND2 . ASN   B  1 148 ? -29.594 -10.862  -34.855 1.00 29.45 ? 148 ASN   B ND2 1 
ATOM   2482  N  N   . TYR   B  1 149 ? -26.802 -12.388  -30.365 1.00 26.30 ? 149 TYR   B N   1 
ATOM   2483  C  CA  . TYR   B  1 149 ? -25.495 -12.746  -29.850 1.00 27.17 ? 149 TYR   B CA  1 
ATOM   2484  C  C   . TYR   B  1 149 ? -25.539 -14.095  -29.140 1.00 29.41 ? 149 TYR   B C   1 
ATOM   2485  O  O   . TYR   B  1 149 ? -24.655 -14.944  -29.340 1.00 28.61 ? 149 TYR   B O   1 
ATOM   2486  C  CB  . TYR   B  1 149 ? -24.972 -11.666  -28.914 1.00 32.24 ? 149 TYR   B CB  1 
ATOM   2487  C  CG  . TYR   B  1 149 ? -23.650 -12.079  -28.379 1.00 25.05 ? 149 TYR   B CG  1 
ATOM   2488  C  CD1 . TYR   B  1 149 ? -22.482 -11.844  -29.106 1.00 31.29 ? 149 TYR   B CD1 1 
ATOM   2489  C  CD2 . TYR   B  1 149 ? -23.545 -12.741  -27.164 1.00 30.24 ? 149 TYR   B CD2 1 
ATOM   2490  C  CE1 . TYR   B  1 149 ? -21.249 -12.251  -28.629 1.00 33.34 ? 149 TYR   B CE1 1 
ATOM   2491  C  CE2 . TYR   B  1 149 ? -22.307 -13.150  -26.689 1.00 31.14 ? 149 TYR   B CE2 1 
ATOM   2492  C  CZ  . TYR   B  1 149 ? -21.179 -12.906  -27.423 1.00 34.51 ? 149 TYR   B CZ  1 
ATOM   2493  O  OH  . TYR   B  1 149 ? -19.958 -13.321  -26.957 1.00 32.35 ? 149 TYR   B OH  1 
ATOM   2494  N  N   . LEU   B  1 150 ? -26.553 -14.310  -28.299 1.00 30.91 ? 150 LEU   B N   1 
ATOM   2495  C  CA  . LEU   B  1 150 ? -26.643 -15.568  -27.564 1.00 24.77 ? 150 LEU   B CA  1 
ATOM   2496  C  C   . LEU   B  1 150 ? -26.949 -16.706  -28.527 1.00 32.82 ? 150 LEU   B C   1 
ATOM   2497  O  O   . LEU   B  1 150 ? -26.334 -17.775  -28.446 1.00 25.81 ? 150 LEU   B O   1 
ATOM   2498  C  CB  . LEU   B  1 150 ? -27.693 -15.478  -26.449 1.00 26.79 ? 150 LEU   B CB  1 
ATOM   2499  C  CG  . LEU   B  1 150 ? -27.449 -14.451  -25.331 1.00 30.93 ? 150 LEU   B CG  1 
ATOM   2500  C  CD1 . LEU   B  1 150 ? -28.626 -14.480  -24.334 1.00 32.81 ? 150 LEU   B CD1 1 
ATOM   2501  C  CD2 . LEU   B  1 150 ? -26.130 -14.680  -24.604 1.00 32.63 ? 150 LEU   B CD2 1 
ATOM   2502  N  N   . GLN   B  1 151 ? -27.854 -16.467  -29.481 1.00 24.84 ? 151 GLN   B N   1 
ATOM   2503  C  CA  . GLN   B  1 151 ? -28.175 -17.476  -30.481 1.00 27.36 ? 151 GLN   B CA  1 
ATOM   2504  C  C   . GLN   B  1 151 ? -26.926 -17.957  -31.201 1.00 26.51 ? 151 GLN   B C   1 
ATOM   2505  O  O   . GLN   B  1 151 ? -26.805 -19.148  -31.516 1.00 25.00 ? 151 GLN   B O   1 
ATOM   2506  C  CB  . GLN   B  1 151 ? -29.178 -16.927  -31.490 1.00 27.32 ? 151 GLN   B CB  1 
ATOM   2507  C  CG  . GLN   B  1 151 ? -29.424 -17.832  -32.700 1.00 30.68 ? 151 GLN   B CG  1 
ATOM   2508  C  CD  . GLN   B  1 151 ? -30.285 -17.192  -33.770 1.00 26.92 ? 151 GLN   B CD  1 
ATOM   2509  O  OE1 . GLN   B  1 151 ? -30.157 -16.002  -34.064 1.00 28.01 ? 151 GLN   B OE1 1 
ATOM   2510  N  NE2 . GLN   B  1 151 ? -31.142 -17.997  -34.392 1.00 26.85 ? 151 GLN   B NE2 1 
ATOM   2511  N  N   . SER   B  1 152 ? -26.034 -17.029  -31.544 1.00 29.14 ? 152 SER   B N   1 
ATOM   2512  C  CA  . SER   B  1 152 ? -24.800 -17.342  -32.264 1.00 31.42 ? 152 SER   B CA  1 
ATOM   2513  C  C   . SER   B  1 152 ? -23.814 -18.120  -31.414 1.00 31.85 ? 152 SER   B C   1 
ATOM   2514  O  O   . SER   B  1 152 ? -22.801 -18.585  -31.945 1.00 27.28 ? 152 SER   B O   1 
ATOM   2515  C  CB  . SER   B  1 152 ? -24.149 -16.047  -32.751 1.00 28.34 ? 152 SER   B CB  1 
ATOM   2516  O  OG  . SER   B  1 152 ? -24.829 -15.565  -33.919 1.00 31.97 ? 152 SER   B OG  1 
ATOM   2517  N  N   . HIS   B  1 153 ? -24.099 -18.298  -30.123 1.00 27.78 ? 153 HIS   B N   1 
ATOM   2518  C  CA  . HIS   B  1 153 ? -23.188 -19.000  -29.220 1.00 27.98 ? 153 HIS   B CA  1 
ATOM   2519  C  C   . HIS   B  1 153 ? -23.831 -20.251  -28.630 1.00 27.41 ? 153 HIS   B C   1 
ATOM   2520  O  O   . HIS   B  1 153 ? -23.287 -20.862  -27.701 1.00 26.00 ? 153 HIS   B O   1 
ATOM   2521  C  CB  . HIS   B  1 153 ? -22.680 -18.051  -28.143 1.00 28.85 ? 153 HIS   B CB  1 
ATOM   2522  C  CG  . HIS   B  1 153 ? -21.675 -17.082  -28.666 1.00 24.60 ? 153 HIS   B CG  1 
ATOM   2523  N  ND1 . HIS   B  1 153 ? -22.033 -15.899  -29.278 1.00 32.97 ? 153 HIS   B ND1 1 
ATOM   2524  C  CD2 . HIS   B  1 153 ? -20.327 -17.178  -28.796 1.00 30.62 ? 153 HIS   B CD2 1 
ATOM   2525  C  CE1 . HIS   B  1 153 ? -20.945 -15.284  -29.712 1.00 39.53 ? 153 HIS   B CE1 1 
ATOM   2526  N  NE2 . HIS   B  1 153 ? -19.896 -16.034  -29.421 1.00 35.65 ? 153 HIS   B NE2 1 
ATOM   2527  N  N   . MET   B  1 154 ? -24.926 -20.705  -29.229 1.00 26.46 ? 154 MET   B N   1 
ATOM   2528  C  CA  . MET   B  1 154 ? -25.574 -21.932  -28.781 1.00 26.97 ? 154 MET   B CA  1 
ATOM   2529  C  C   . MET   B  1 154 ? -24.788 -23.160  -29.196 1.00 33.79 ? 154 MET   B C   1 
ATOM   2530  O  O   . MET   B  1 154 ? -24.587 -24.080  -28.398 1.00 32.92 ? 154 MET   B O   1 
ATOM   2531  C  CB  . MET   B  1 154 ? -26.970 -22.026  -29.376 1.00 25.68 ? 154 MET   B CB  1 
ATOM   2532  C  CG  . MET   B  1 154 ? -28.066 -21.371  -28.550 1.00 38.85 ? 154 MET   B CG  1 
ATOM   2533  S  SD  . MET   B  1 154 ? -29.661 -21.314  -29.420 1.00 43.93 ? 154 MET   B SD  1 
ATOM   2534  C  CE  . MET   B  1 154 ? -29.863 -23.034  -29.905 1.00 30.02 ? 154 MET   B CE  1 
ATOM   2535  N  N   . HIS   B  1 155 ? -24.387 -23.214  -30.463 1.00 33.96 ? 155 HIS   B N   1 
ATOM   2536  C  CA  . HIS   B  1 155 ? -23.786 -24.399  -31.048 1.00 47.71 ? 155 HIS   B CA  1 
ATOM   2537  C  C   . HIS   B  1 155 ? -22.304 -24.153  -31.272 1.00 37.19 ? 155 HIS   B C   1 
ATOM   2538  O  O   . HIS   B  1 155 ? -21.888 -23.038  -31.615 1.00 47.78 ? 155 HIS   B O   1 
ATOM   2539  C  CB  . HIS   B  1 155 ? -24.469 -24.759  -32.374 1.00 44.07 ? 155 HIS   B CB  1 
ATOM   2540  C  CG  . HIS   B  1 155 ? -25.952 -24.981  -32.257 1.00 51.61 ? 155 HIS   B CG  1 
ATOM   2541  N  ND1 . HIS   B  1 155 ? -26.853 -24.531  -33.204 1.00 47.02 ? 155 HIS   B ND1 1 
ATOM   2542  C  CD2 . HIS   B  1 155 ? -26.689 -25.620  -31.316 1.00 51.07 ? 155 HIS   B CD2 1 
ATOM   2543  C  CE1 . HIS   B  1 155 ? -28.078 -24.874  -32.844 1.00 44.32 ? 155 HIS   B CE1 1 
ATOM   2544  N  NE2 . HIS   B  1 155 ? -28.007 -25.539  -31.704 1.00 58.21 ? 155 HIS   B NE2 1 
ATOM   2545  N  N   . GLU   B  1 156 ? -21.503 -25.188  -31.064 1.00 55.09 ? 156 GLU   B N   1 
ATOM   2546  C  CA  . GLU   B  1 156 ? -20.113 -25.149  -31.509 1.00 57.70 ? 156 GLU   B CA  1 
ATOM   2547  C  C   . GLU   B  1 156 ? -20.032 -25.337  -33.027 1.00 59.31 ? 156 GLU   B C   1 
ATOM   2548  O  O   . GLU   B  1 156 ? -19.128 -24.813  -33.684 1.00 65.42 ? 156 GLU   B O   1 
ATOM   2549  C  CB  . GLU   B  1 156 ? -19.304 -26.222  -30.797 1.00 60.56 ? 156 GLU   B CB  1 
ATOM   2550  C  CG  . GLU   B  1 156 ? -19.519 -26.206  -29.295 1.00 51.44 ? 156 GLU   B CG  1 
ATOM   2551  C  CD  . GLU   B  1 156 ? -18.481 -27.013  -28.543 1.00 62.11 ? 156 GLU   B CD  1 
ATOM   2552  O  OE1 . GLU   B  1 156 ? -17.307 -27.022  -28.978 1.00 67.47 ? 156 GLU   B OE1 1 
ATOM   2553  O  OE2 . GLU   B  1 156 ? -18.846 -27.636  -27.521 1.00 59.22 ? 156 GLU   B OE2 1 
ATOM   2554  N  N   . MET   C  1 1   ? -34.716 -67.517  -14.117 1.00 37.95 ? 1   MET   C N   1 
ATOM   2555  C  CA  . MET   C  1 1   ? -34.471 -67.348  -12.643 1.00 33.79 ? 1   MET   C CA  1 
ATOM   2556  C  C   . MET   C  1 1   ? -35.696 -66.663  -12.030 1.00 36.00 ? 1   MET   C C   1 
ATOM   2557  O  O   . MET   C  1 1   ? -36.090 -65.588  -12.450 1.00 39.87 ? 1   MET   C O   1 
ATOM   2558  C  CB  . MET   C  1 1   ? -33.198 -66.528  -12.415 1.00 38.20 ? 1   MET   C CB  1 
ATOM   2559  C  CG  . MET   C  1 1   ? -32.667 -66.490  -10.970 1.00 48.53 ? 1   MET   C CG  1 
ATOM   2560  S  SD  . MET   C  1 1   ? -31.171 -65.470  -10.860 1.00 40.77 ? 1   MET   C SD  1 
ATOM   2561  C  CE  . MET   C  1 1   ? -31.896 -63.824  -10.908 1.00 35.02 ? 1   MET   C CE  1 
ATOM   2562  N  N   . LYS   C  1 2   ? -36.320 -67.274  -11.036 1.00 37.51 ? 2   LYS   C N   1 
ATOM   2563  C  CA  . LYS   C  1 2   ? -37.538 -66.685  -10.501 1.00 44.52 ? 2   LYS   C CA  1 
ATOM   2564  C  C   . LYS   C  1 2   ? -37.269 -65.317  -9.878  1.00 33.00 ? 2   LYS   C C   1 
ATOM   2565  O  O   . LYS   C  1 2   ? -36.602 -65.218  -8.849  1.00 40.78 ? 2   LYS   C O   1 
ATOM   2566  C  CB  . LYS   C  1 2   ? -38.172 -67.630  -9.475  1.00 45.62 ? 2   LYS   C CB  1 
ATOM   2567  N  N   . GLY   C  1 3   ? -37.813 -64.269  -10.465 1.00 31.30 ? 3   GLY   C N   1 
ATOM   2568  C  CA  . GLY   C  1 3   ? -37.657 -62.944  -9.907  1.00 32.32 ? 3   GLY   C CA  1 
ATOM   2569  C  C   . GLY   C  1 3   ? -38.760 -62.597  -8.926  1.00 36.43 ? 3   GLY   C C   1 
ATOM   2570  O  O   . GLY   C  1 3   ? -39.784 -63.260  -8.891  1.00 37.43 ? 3   GLY   C O   1 
ATOM   2571  N  N   . ASP   C  1 4   ? -38.505 -61.569  -8.120  1.00 32.53 ? 4   ASP   C N   1 
ATOM   2572  C  CA  . ASP   C  1 4   ? -39.498 -61.040  -7.192  1.00 36.23 ? 4   ASP   C CA  1 
ATOM   2573  C  C   . ASP   C  1 4   ? -40.699 -60.462  -7.939  1.00 38.44 ? 4   ASP   C C   1 
ATOM   2574  O  O   . ASP   C  1 4   ? -40.551 -59.700  -8.901  1.00 35.26 ? 4   ASP   C O   1 
ATOM   2575  C  CB  . ASP   C  1 4   ? -38.823 -59.981  -6.308  1.00 36.40 ? 4   ASP   C CB  1 
ATOM   2576  C  CG  . ASP   C  1 4   ? -39.777 -59.287  -5.339  1.00 35.43 ? 4   ASP   C CG  1 
ATOM   2577  O  OD1 . ASP   C  1 4   ? -40.017 -59.818  -4.227  1.00 40.03 ? 4   ASP   C OD1 1 
ATOM   2578  O  OD2 . ASP   C  1 4   ? -40.225 -58.167  -5.652  1.00 35.24 ? 4   ASP   C OD2 1 
ATOM   2579  N  N   . LYS   C  1 5   ? -41.902 -60.811  -7.476  1.00 31.34 ? 5   LYS   C N   1 
ATOM   2580  C  CA  . LYS   C  1 5   ? -43.117 -60.429  -8.198  1.00 30.45 ? 5   LYS   C CA  1 
ATOM   2581  C  C   . LYS   C  1 5   ? -43.255 -58.920  -8.276  1.00 34.50 ? 5   LYS   C C   1 
ATOM   2582  O  O   . LYS   C  1 5   ? -43.648 -58.370  -9.311  1.00 34.31 ? 5   LYS   C O   1 
ATOM   2583  C  CB  . LYS   C  1 5   ? -44.346 -61.038  -7.520  1.00 34.85 ? 5   LYS   C CB  1 
ATOM   2584  C  CG  . LYS   C  1 5   ? -45.689 -60.479  -8.030  1.00 43.62 ? 5   LYS   C CG  1 
ATOM   2585  N  N   . LYS   C  1 6   ? -42.938 -58.230  -7.199  1.00 27.77 ? 6   LYS   C N   1 
ATOM   2586  C  CA  . LYS   C  1 6   ? -43.088 -56.784  -7.211  1.00 29.70 ? 6   LYS   C CA  1 
ATOM   2587  C  C   . LYS   C  1 6   ? -41.992 -56.099  -8.015  1.00 34.09 ? 6   LYS   C C   1 
ATOM   2588  O  O   . LYS   C  1 6   ? -42.250 -55.051  -8.620  1.00 30.96 ? 6   LYS   C O   1 
ATOM   2589  C  CB  . LYS   C  1 6   ? -43.111 -56.248  -5.788  1.00 31.22 ? 6   LYS   C CB  1 
ATOM   2590  N  N   . VAL   C  1 7   ? -40.780 -56.669  -8.053  1.00 28.04 ? 7   VAL   C N   1 
ATOM   2591  C  CA  . VAL   C  1 7   ? -39.759 -56.150  -8.972  1.00 27.81 ? 7   VAL   C CA  1 
ATOM   2592  C  C   . VAL   C  1 7   ? -40.293 -56.168  -10.389 1.00 26.53 ? 7   VAL   C C   1 
ATOM   2593  O  O   . VAL   C  1 7   ? -40.238 -55.163  -11.102 1.00 27.71 ? 7   VAL   C O   1 
ATOM   2594  C  CB  . VAL   C  1 7   ? -38.452 -56.960  -8.851  1.00 30.49 ? 7   VAL   C CB  1 
ATOM   2595  C  CG1 . VAL   C  1 7   ? -37.530 -56.756  -10.091 1.00 31.67 ? 7   VAL   C CG1 1 
ATOM   2596  C  CG2 . VAL   C  1 7   ? -37.718 -56.593  -7.595  1.00 29.59 ? 7   VAL   C CG2 1 
ATOM   2597  N  N   . ILE   C  1 8   ? -40.846 -57.318  -10.803 1.00 27.95 ? 8   ILE   C N   1 
ATOM   2598  C  CA  . ILE   C  1 8   ? -41.421 -57.481  -12.142 1.00 28.05 ? 8   ILE   C CA  1 
ATOM   2599  C  C   . ILE   C  1 8   ? -42.520 -56.466  -12.404 1.00 33.17 ? 8   ILE   C C   1 
ATOM   2600  O  O   . ILE   C  1 8   ? -42.603 -55.885  -13.501 1.00 29.66 ? 8   ILE   C O   1 
ATOM   2601  C  CB  . ILE   C  1 8   ? -41.924 -58.927  -12.322 1.00 30.24 ? 8   ILE   C CB  1 
ATOM   2602  C  CG1 . ILE   C  1 8   ? -40.738 -59.894  -12.301 1.00 31.56 ? 8   ILE   C CG1 1 
ATOM   2603  C  CG2 . ILE   C  1 8   ? -42.692 -59.071  -13.633 1.00 31.05 ? 8   ILE   C CG2 1 
ATOM   2604  C  CD1 . ILE   C  1 8   ? -41.111 -61.393  -12.167 1.00 33.90 ? 8   ILE   C CD1 1 
ATOM   2605  N  N   . GLN   C  1 9   ? -43.392 -56.242  -11.419 1.00 28.82 ? 9   GLN   C N   1 
ATOM   2606  C  CA  . GLN   C  1 9   ? -44.421 -55.214  -11.564 1.00 27.96 ? 9   GLN   C CA  1 
ATOM   2607  C  C   . GLN   C  1 9   ? -43.808 -53.834  -11.736 1.00 28.26 ? 9   GLN   C C   1 
ATOM   2608  O  O   . GLN   C  1 9   ? -44.289 -53.015  -12.540 1.00 26.66 ? 9   GLN   C O   1 
ATOM   2609  C  CB  . GLN   C  1 9   ? -45.349 -55.230  -10.338 1.00 33.29 ? 9   GLN   C CB  1 
ATOM   2610  C  CG  . GLN   C  1 9   ? -46.175 -56.507  -10.251 1.00 39.05 ? 9   GLN   C CG  1 
ATOM   2611  C  CD  . GLN   C  1 9   ? -46.967 -56.626  -8.948  1.00 47.33 ? 9   GLN   C CD  1 
ATOM   2612  O  OE1 . GLN   C  1 9   ? -46.546 -56.148  -7.889  1.00 41.56 ? 9   GLN   C OE1 1 
ATOM   2613  N  NE2 . GLN   C  1 9   ? -48.116 -57.280  -9.027  1.00 54.05 ? 9   GLN   C NE2 1 
ATOM   2614  N  N   . HIS   C  1 10  ? -42.769 -53.535  -10.964 1.00 25.34 ? 10  HIS   C N   1 
ATOM   2615  C  CA  . HIS   C  1 10  ? -42.066 -52.267  -11.160 1.00 28.64 ? 10  HIS   C CA  1 
ATOM   2616  C  C   . HIS   C  1 10  ? -41.443 -52.204  -12.549 1.00 28.06 ? 10  HIS   C C   1 
ATOM   2617  O  O   . HIS   C  1 10  ? -41.554 -51.187  -13.241 1.00 30.17 ? 10  HIS   C O   1 
ATOM   2618  C  CB  . HIS   C  1 10  ? -40.990 -52.079  -10.103 1.00 29.88 ? 10  HIS   C CB  1 
ATOM   2619  C  CG  . HIS   C  1 10  ? -41.493 -51.468  -8.836  1.00 30.49 ? 10  HIS   C CG  1 
ATOM   2620  N  ND1 . HIS   C  1 10  ? -41.881 -50.147  -8.753  1.00 34.17 ? 10  HIS   C ND1 1 
ATOM   2621  C  CD2 . HIS   C  1 10  ? -41.666 -51.994  -7.598  1.00 31.31 ? 10  HIS   C CD2 1 
ATOM   2622  C  CE1 . HIS   C  1 10  ? -42.260 -49.882  -7.515  1.00 37.54 ? 10  HIS   C CE1 1 
ATOM   2623  N  NE2 . HIS   C  1 10  ? -42.141 -50.986  -6.795  1.00 40.05 ? 10  HIS   C NE2 1 
ATOM   2624  N  N   . LEU   C  1 11  ? -40.759 -53.279  -12.963 1.00 27.28 ? 11  LEU   C N   1 
ATOM   2625  C  CA  . LEU   C  1 11  ? -40.174 -53.295  -14.304 1.00 30.57 ? 11  LEU   C CA  1 
ATOM   2626  C  C   . LEU   C  1 11  ? -41.238 -53.062  -15.374 1.00 34.31 ? 11  LEU   C C   1 
ATOM   2627  O  O   . LEU   C  1 11  ? -41.006 -52.296  -16.322 1.00 28.16 ? 11  LEU   C O   1 
ATOM   2628  C  CB  . LEU   C  1 11  ? -39.428 -54.613  -14.570 1.00 26.01 ? 11  LEU   C CB  1 
ATOM   2629  C  CG  . LEU   C  1 11  ? -38.207 -54.907  -13.694 1.00 25.99 ? 11  LEU   C CG  1 
ATOM   2630  C  CD1 . LEU   C  1 11  ? -37.616 -56.264  -14.008 1.00 34.23 ? 11  LEU   C CD1 1 
ATOM   2631  C  CD2 . LEU   C  1 11  ? -37.128 -53.841  -13.834 1.00 34.51 ? 11  LEU   C CD2 1 
ATOM   2632  N  N   . ASN   C  1 12  ? -42.430 -53.689  -15.227 1.00 28.60 ? 12  ASN   C N   1 
ATOM   2633  C  CA  . ASN   C  1 12  ? -43.502 -53.468  -16.204 1.00 26.36 ? 12  ASN   C CA  1 
ATOM   2634  C  C   . ASN   C  1 12  ? -44.021 -52.050  -16.162 1.00 22.26 ? 12  ASN   C C   1 
ATOM   2635  O  O   . ASN   C  1 12  ? -44.391 -51.502  -17.209 1.00 26.29 ? 12  ASN   C O   1 
ATOM   2636  C  CB  . ASN   C  1 12  ? -44.648 -54.464  -16.011 1.00 31.52 ? 12  ASN   C CB  1 
ATOM   2637  C  CG  . ASN   C  1 12  ? -44.460 -55.681  -16.871 1.00 30.78 ? 12  ASN   C CG  1 
ATOM   2638  O  OD1 . ASN   C  1 12  ? -44.032 -55.562  -18.028 1.00 30.77 ? 12  ASN   C OD1 1 
ATOM   2639  N  ND2 . ASN   C  1 12  ? -44.689 -56.859  -16.309 1.00 32.88 ? 12  ASN   C ND2 1 
ATOM   2640  N  N   . LYS   C  1 13  ? -43.982 -51.406  -14.997 1.00 27.14 ? 13  LYS   C N   1 
ATOM   2641  C  CA  . LYS   C  1 13  ? -44.366 -50.001  -14.941 1.00 29.47 ? 13  LYS   C CA  1 
ATOM   2642  C  C   . LYS   C  1 13  ? -43.369 -49.114  -15.685 1.00 30.39 ? 13  LYS   C C   1 
ATOM   2643  O  O   . LYS   C  1 13  ? -43.765 -48.189  -16.403 1.00 29.49 ? 13  LYS   C O   1 
ATOM   2644  C  CB  . LYS   C  1 13  ? -44.501 -49.541  -13.491 1.00 29.44 ? 13  LYS   C CB  1 
ATOM   2645  C  CG  . LYS   C  1 13  ? -45.070 -48.135  -13.369 1.00 33.25 ? 13  LYS   C CG  1 
ATOM   2646  C  CD  . LYS   C  1 13  ? -45.497 -47.843  -11.956 1.00 41.32 ? 13  LYS   C CD  1 
ATOM   2647  C  CE  . LYS   C  1 13  ? -46.338 -46.566  -11.904 1.00 50.60 ? 13  LYS   C CE  1 
ATOM   2648  N  NZ  . LYS   C  1 13  ? -46.389 -46.043  -10.513 1.00 44.42 ? 13  LYS   C NZ  1 
ATOM   2649  N  N   . ILE   C  1 14  ? -42.071 -49.315  -15.448 1.00 30.73 ? 14  ILE   C N   1 
ATOM   2650  C  CA  . ILE   C  1 14  ? -41.050 -48.561  -16.174 1.00 29.53 ? 14  ILE   C CA  1 
ATOM   2651  C  C   . ILE   C  1 14  ? -41.219 -48.778  -17.682 1.00 28.08 ? 14  ILE   C C   1 
ATOM   2652  O  O   . ILE   C  1 14  ? -41.187 -47.836  -18.479 1.00 30.13 ? 14  ILE   C O   1 
ATOM   2653  C  CB  . ILE   C  1 14  ? -39.646 -48.983  -15.686 1.00 27.87 ? 14  ILE   C CB  1 
ATOM   2654  C  CG1 . ILE   C  1 14  ? -39.492 -48.774  -14.155 1.00 29.99 ? 14  ILE   C CG1 1 
ATOM   2655  C  CG2 . ILE   C  1 14  ? -38.529 -48.256  -16.460 1.00 28.99 ? 14  ILE   C CG2 1 
ATOM   2656  C  CD1 . ILE   C  1 14  ? -39.973 -47.448  -13.652 1.00 32.53 ? 14  ILE   C CD1 1 
ATOM   2657  N  N   . LEU   C  1 15  ? -41.394 -50.037  -18.089 1.00 25.10 ? 15  LEU   C N   1 
ATOM   2658  C  CA  . LEU   C  1 15  ? -41.603 -50.354  -19.500 1.00 28.94 ? 15  LEU   C CA  1 
ATOM   2659  C  C   . LEU   C  1 15  ? -42.820 -49.626  -20.054 1.00 34.15 ? 15  LEU   C C   1 
ATOM   2660  O  O   . LEU   C  1 15  ? -42.776 -49.074  -21.168 1.00 25.30 ? 15  LEU   C O   1 
ATOM   2661  C  CB  . LEU   C  1 15  ? -41.736 -51.874  -19.657 1.00 29.12 ? 15  LEU   C CB  1 
ATOM   2662  C  CG  . LEU   C  1 15  ? -42.149 -52.443  -21.020 1.00 30.17 ? 15  LEU   C CG  1 
ATOM   2663  C  CD1 . LEU   C  1 15  ? -41.121 -52.092  -22.087 1.00 29.81 ? 15  LEU   C CD1 1 
ATOM   2664  C  CD2 . LEU   C  1 15  ? -42.374 -53.969  -21.008 1.00 27.39 ? 15  LEU   C CD2 1 
ATOM   2665  N  N   . GLY   C  1 16  ? -43.912 -49.581  -19.276 1.00 32.73 ? 16  GLY   C N   1 
ATOM   2666  C  CA  . GLY   C  1 16  ? -45.080 -48.821  -19.699 1.00 29.34 ? 16  GLY   C CA  1 
ATOM   2667  C  C   . GLY   C  1 16  ? -44.772 -47.351  -19.922 1.00 32.98 ? 16  GLY   C C   1 
ATOM   2668  O  O   . GLY   C  1 16  ? -45.236 -46.740  -20.889 1.00 28.76 ? 16  GLY   C O   1 
ATOM   2669  N  N   . ASN   C  1 17  ? -43.963 -46.763  -19.053 1.00 28.60 ? 17  ASN   C N   1 
ATOM   2670  C  CA  . ASN   C  1 17  ? -43.518 -45.393  -19.310 1.00 30.41 ? 17  ASN   C CA  1 
ATOM   2671  C  C   . ASN   C  1 17  ? -42.703 -45.304  -20.604 1.00 26.51 ? 17  ASN   C C   1 
ATOM   2672  O  O   . ASN   C  1 17  ? -42.842 -44.336  -21.371 1.00 24.07 ? 17  ASN   C O   1 
ATOM   2673  C  CB  . ASN   C  1 17  ? -42.689 -44.880  -18.132 1.00 31.65 ? 17  ASN   C CB  1 
ATOM   2674  C  CG  . ASN   C  1 17  ? -43.535 -44.604  -16.898 1.00 36.16 ? 17  ASN   C CG  1 
ATOM   2675  O  OD1 . ASN   C  1 17  ? -44.759 -44.443  -16.999 1.00 35.25 ? 17  ASN   C OD1 1 
ATOM   2676  N  ND2 . ASN   C  1 17  ? -42.888 -44.513  -15.735 1.00 29.51 ? 17  ASN   C ND2 1 
ATOM   2677  N  N   . GLU   C  1 18  ? -41.815 -46.275  -20.841 1.00 27.96 ? 18  GLU   C N   1 
ATOM   2678  C  CA  . GLU   C  1 18  ? -41.004 -46.232  -22.063 1.00 29.44 ? 18  GLU   C CA  1 
ATOM   2679  C  C   . GLU   C  1 18  ? -41.880 -46.337  -23.308 1.00 30.63 ? 18  GLU   C C   1 
ATOM   2680  O  O   . GLU   C  1 18  ? -41.604 -45.691  -24.328 1.00 28.14 ? 18  GLU   C O   1 
ATOM   2681  C  CB  . GLU   C  1 18  ? -39.960 -47.362  -22.089 1.00 32.87 ? 18  GLU   C CB  1 
ATOM   2682  C  CG  . GLU   C  1 18  ? -39.019 -47.438  -20.917 1.00 35.10 ? 18  GLU   C CG  1 
ATOM   2683  C  CD  . GLU   C  1 18  ? -37.906 -46.479  -20.990 1.00 42.42 ? 18  GLU   C CD  1 
ATOM   2684  O  OE1 . GLU   C  1 18  ? -37.801 -45.736  -22.002 1.00 46.65 ? 18  GLU   C OE1 1 
ATOM   2685  O  OE2 . GLU   C  1 18  ? -37.116 -46.480  -20.025 1.00 35.83 ? 18  GLU   C OE2 1 
ATOM   2686  N  N   . LEU   C  1 19  ? -42.919 -47.178  -23.261 1.00 30.02 ? 19  LEU   C N   1 
ATOM   2687  C  CA  . LEU   C  1 19  ? -43.788 -47.322  -24.427 1.00 29.46 ? 19  LEU   C CA  1 
ATOM   2688  C  C   . LEU   C  1 19  ? -44.485 -46.009  -24.759 1.00 27.22 ? 19  LEU   C C   1 
ATOM   2689  O  O   . LEU   C  1 19  ? -44.591 -45.638  -25.939 1.00 29.61 ? 19  LEU   C O   1 
ATOM   2690  C  CB  . LEU   C  1 19  ? -44.805 -48.439  -24.198 1.00 32.49 ? 19  LEU   C CB  1 
ATOM   2691  C  CG  . LEU   C  1 19  ? -44.146 -49.791  -23.942 1.00 40.71 ? 19  LEU   C CG  1 
ATOM   2692  C  CD1 . LEU   C  1 19  ? -45.167 -50.805  -23.487 1.00 42.22 ? 19  LEU   C CD1 1 
ATOM   2693  C  CD2 . LEU   C  1 19  ? -43.412 -50.274  -25.182 1.00 42.07 ? 19  LEU   C CD2 1 
ATOM   2694  N  N   . ILE   C  1 20  ? -44.925 -45.269  -23.735 1.00 30.15 ? 20  ILE   C N   1 
ATOM   2695  C  CA  . ILE   C  1 20  ? -45.463 -43.924  -23.960 1.00 27.67 ? 20  ILE   C CA  1 
ATOM   2696  C  C   . ILE   C  1 20  ? -44.396 -43.024  -24.567 1.00 27.90 ? 20  ILE   C C   1 
ATOM   2697  O  O   . ILE   C  1 20  ? -44.629 -42.334  -25.569 1.00 28.89 ? 20  ILE   C O   1 
ATOM   2698  C  CB  . ILE   C  1 20  ? -45.995 -43.324  -22.644 1.00 29.49 ? 20  ILE   C CB  1 
ATOM   2699  C  CG1 . ILE   C  1 20  ? -47.168 -44.148  -22.089 1.00 31.21 ? 20  ILE   C CG1 1 
ATOM   2700  C  CG2 . ILE   C  1 20  ? -46.412 -41.860  -22.868 1.00 28.84 ? 20  ILE   C CG2 1 
ATOM   2701  C  CD1 . ILE   C  1 20  ? -47.659 -43.661  -20.677 1.00 37.48 ? 20  ILE   C CD1 1 
ATOM   2702  N  N   . ALA   C  1 21  ? -43.209 -43.008  -23.951 1.00 26.81 ? 21  ALA   C N   1 
ATOM   2703  C  CA  . ALA   C  1 21  ? -42.137 -42.130  -24.412 1.00 26.04 ? 21  ALA   C CA  1 
ATOM   2704  C  C   . ALA   C  1 21  ? -41.774 -42.414  -25.865 1.00 22.14 ? 21  ALA   C C   1 
ATOM   2705  O  O   . ALA   C  1 21  ? -41.605 -41.481  -26.669 1.00 26.49 ? 21  ALA   C O   1 
ATOM   2706  C  CB  . ALA   C  1 21  ? -40.918 -42.279  -23.485 1.00 26.02 ? 21  ALA   C CB  1 
ATOM   2707  N  N   . ILE   C  1 22  ? -41.709 -43.690  -26.238 1.00 25.33 ? 22  ILE   C N   1 
ATOM   2708  C  CA  . ILE   C  1 22  ? -41.291 -44.049  -27.589 1.00 33.30 ? 22  ILE   C CA  1 
ATOM   2709  C  C   . ILE   C  1 22  ? -42.211 -43.391  -28.607 1.00 29.81 ? 22  ILE   C C   1 
ATOM   2710  O  O   . ILE   C  1 22  ? -41.769 -42.711  -29.539 1.00 26.46 ? 22  ILE   C O   1 
ATOM   2711  C  CB  . ILE   C  1 22  ? -41.284 -45.577  -27.749 1.00 27.36 ? 22  ILE   C CB  1 
ATOM   2712  C  CG1 . ILE   C  1 22  ? -40.100 -46.198  -27.001 1.00 24.10 ? 22  ILE   C CG1 1 
ATOM   2713  C  CG2 . ILE   C  1 22  ? -41.325 -45.960  -29.232 1.00 33.43 ? 22  ILE   C CG2 1 
ATOM   2714  C  CD1 . ILE   C  1 22  ? -40.225 -47.703  -26.897 1.00 25.75 ? 22  ILE   C CD1 1 
ATOM   2715  N  N   . ASN   C  1 23  ? -43.524 -43.561  -28.413 1.00 25.53 ? 23  ASN   C N   1 
ATOM   2716  C  CA  . ASN   C  1 23  ? -44.499 -43.025  -29.359 1.00 25.08 ? 23  ASN   C CA  1 
ATOM   2717  C  C   . ASN   C  1 23  ? -44.607 -41.506  -29.269 1.00 23.50 ? 23  ASN   C C   1 
ATOM   2718  O  O   . ASN   C  1 23  ? -44.696 -40.817  -30.286 1.00 28.59 ? 23  ASN   C O   1 
ATOM   2719  C  CB  . ASN   C  1 23  ? -45.838 -43.671  -29.074 1.00 28.35 ? 23  ASN   C CB  1 
ATOM   2720  C  CG  . ASN   C  1 23  ? -45.902 -45.111  -29.509 1.00 29.15 ? 23  ASN   C CG  1 
ATOM   2721  O  OD1 . ASN   C  1 23  ? -44.893 -45.786  -29.768 1.00 30.41 ? 23  ASN   C OD1 1 
ATOM   2722  N  ND2 . ASN   C  1 23  ? -47.117 -45.610  -29.577 1.00 33.35 ? 23  ASN   C ND2 1 
ATOM   2723  N  N   . GLN   C  1 24  ? -44.586 -40.955  -28.065 1.00 26.75 ? 24  GLN   C N   1 
ATOM   2724  C  CA  . GLN   C  1 24  ? -44.667 -39.502  -27.932 1.00 27.27 ? 24  GLN   C CA  1 
ATOM   2725  C  C   . GLN   C  1 24  ? -43.465 -38.804  -28.573 1.00 30.55 ? 24  GLN   C C   1 
ATOM   2726  O  O   . GLN   C  1 24  ? -43.621 -37.801  -29.289 1.00 28.03 ? 24  GLN   C O   1 
ATOM   2727  C  CB  . GLN   C  1 24  ? -44.777 -39.140  -26.464 1.00 21.20 ? 24  GLN   C CB  1 
ATOM   2728  C  CG  . GLN   C  1 24  ? -44.723 -37.656  -26.190 1.00 25.14 ? 24  GLN   C CG  1 
ATOM   2729  C  CD  . GLN   C  1 24  ? -44.975 -37.341  -24.717 1.00 34.06 ? 24  GLN   C CD  1 
ATOM   2730  O  OE1 . GLN   C  1 24  ? -45.812 -37.979  -24.069 1.00 29.45 ? 24  GLN   C OE1 1 
ATOM   2731  N  NE2 . GLN   C  1 24  ? -44.243 -36.362  -24.183 1.00 28.66 ? 24  GLN   C NE2 1 
ATOM   2732  N  N   . TYR   C  1 25  ? -42.251 -39.296  -28.300 1.00 28.26 ? 25  TYR   C N   1 
ATOM   2733  C  CA  . TYR   C  1 25  ? -41.069 -38.690  -28.928 1.00 29.20 ? 25  TYR   C CA  1 
ATOM   2734  C  C   . TYR   C  1 25  ? -41.060 -38.931  -30.437 1.00 23.92 ? 25  TYR   C C   1 
ATOM   2735  O  O   . TYR   C  1 25  ? -40.705 -38.032  -31.203 1.00 25.17 ? 25  TYR   C O   1 
ATOM   2736  C  CB  . TYR   C  1 25  ? -39.784 -39.223  -28.295 1.00 28.75 ? 25  TYR   C CB  1 
ATOM   2737  C  CG  . TYR   C  1 25  ? -39.717 -39.007  -26.784 1.00 31.63 ? 25  TYR   C CG  1 
ATOM   2738  C  CD1 . TYR   C  1 25  ? -40.581 -38.117  -26.149 1.00 31.74 ? 25  TYR   C CD1 1 
ATOM   2739  C  CD2 . TYR   C  1 25  ? -38.796 -39.696  -26.003 1.00 29.23 ? 25  TYR   C CD2 1 
ATOM   2740  C  CE1 . TYR   C  1 25  ? -40.552 -37.934  -24.771 1.00 30.28 ? 25  TYR   C CE1 1 
ATOM   2741  C  CE2 . TYR   C  1 25  ? -38.734 -39.505  -24.631 1.00 33.37 ? 25  TYR   C CE2 1 
ATOM   2742  C  CZ  . TYR   C  1 25  ? -39.633 -38.636  -24.017 1.00 30.63 ? 25  TYR   C CZ  1 
ATOM   2743  O  OH  . TYR   C  1 25  ? -39.590 -38.434  -22.661 1.00 33.95 ? 25  TYR   C OH  1 
ATOM   2744  N  N   . PHE   C  1 26  ? -41.474 -40.118  -30.891 1.00 25.93 ? 26  PHE   C N   1 
ATOM   2745  C  CA  . PHE   C  1 26  ? -41.476 -40.354  -32.334 1.00 28.36 ? 26  PHE   C CA  1 
ATOM   2746  C  C   . PHE   C  1 26  ? -42.449 -39.427  -33.052 1.00 28.14 ? 26  PHE   C C   1 
ATOM   2747  O  O   . PHE   C  1 26  ? -42.132 -38.906  -34.122 1.00 26.27 ? 26  PHE   C O   1 
ATOM   2748  C  CB  . PHE   C  1 26  ? -41.794 -41.811  -32.665 1.00 24.65 ? 26  PHE   C CB  1 
ATOM   2749  C  CG  . PHE   C  1 26  ? -41.217 -42.239  -33.977 1.00 27.74 ? 26  PHE   C CG  1 
ATOM   2750  C  CD1 . PHE   C  1 26  ? -41.909 -42.052  -35.174 1.00 28.12 ? 26  PHE   C CD1 1 
ATOM   2751  C  CD2 . PHE   C  1 26  ? -39.948 -42.780  -34.016 1.00 24.97 ? 26  PHE   C CD2 1 
ATOM   2752  C  CE1 . PHE   C  1 26  ? -41.321 -42.423  -36.408 1.00 26.17 ? 26  PHE   C CE1 1 
ATOM   2753  C  CE2 . PHE   C  1 26  ? -39.338 -43.142  -35.219 1.00 26.10 ? 26  PHE   C CE2 1 
ATOM   2754  C  CZ  . PHE   C  1 26  ? -40.021 -42.986  -36.423 1.00 29.27 ? 26  PHE   C CZ  1 
ATOM   2755  N  N   . LEU   C  1 27  ? -43.641 -39.205  -32.483 1.00 28.90 ? 27  LEU   C N   1 
ATOM   2756  C  CA  . LEU   C  1 27  ? -44.598 -38.299  -33.122 1.00 27.86 ? 27  LEU   C CA  1 
ATOM   2757  C  C   . LEU   C  1 27  ? -44.076 -36.868  -33.100 1.00 23.74 ? 27  LEU   C C   1 
ATOM   2758  O  O   . LEU   C  1 27  ? -44.065 -36.177  -34.126 1.00 26.48 ? 27  LEU   C O   1 
ATOM   2759  C  CB  . LEU   C  1 27  ? -45.966 -38.405  -32.436 1.00 27.53 ? 27  LEU   C CB  1 
ATOM   2760  C  CG  . LEU   C  1 27  ? -47.049 -37.499  -33.034 1.00 28.46 ? 27  LEU   C CG  1 
ATOM   2761  C  CD1 . LEU   C  1 27  ? -47.208 -37.762  -34.527 1.00 27.76 ? 27  LEU   C CD1 1 
ATOM   2762  C  CD2 . LEU   C  1 27  ? -48.379 -37.683  -32.308 1.00 33.96 ? 27  LEU   C CD2 1 
ATOM   2763  N  N   . HIS   C  1 28  ? -43.573 -36.424  -31.947 1.00 24.32 ? 28  HIS   C N   1 
ATOM   2764  C  CA  . HIS   C  1 28  ? -42.975 -35.095  -31.886 1.00 26.14 ? 28  HIS   C CA  1 
ATOM   2765  C  C   . HIS   C  1 28  ? -41.865 -34.945  -32.923 1.00 27.00 ? 28  HIS   C C   1 
ATOM   2766  O  O   . HIS   C  1 28  ? -41.769 -33.915  -33.617 1.00 24.53 ? 28  HIS   C O   1 
ATOM   2767  C  CB  . HIS   C  1 28  ? -42.446 -34.826  -30.478 1.00 30.61 ? 28  HIS   C CB  1 
ATOM   2768  C  CG  . HIS   C  1 28  ? -43.518 -34.413  -29.515 1.00 29.64 ? 28  HIS   C CG  1 
ATOM   2769  N  ND1 . HIS   C  1 28  ? -43.353 -34.450  -28.145 1.00 31.00 ? 28  HIS   C ND1 1 
ATOM   2770  C  CD2 . HIS   C  1 28  ? -44.761 -33.930  -29.733 1.00 27.31 ? 28  HIS   C CD2 1 
ATOM   2771  C  CE1 . HIS   C  1 28  ? -44.466 -34.033  -27.563 1.00 32.30 ? 28  HIS   C CE1 1 
ATOM   2772  N  NE2 . HIS   C  1 28  ? -45.335 -33.703  -28.503 1.00 30.81 ? 28  HIS   C NE2 1 
ATOM   2773  N  N   . SER   C  1 29  ? -41.040 -35.979  -33.071 1.00 26.25 ? 29  SER   C N   1 
ATOM   2774  C  CA  . SER   C  1 29  ? -39.961 -35.907  -34.046 1.00 24.63 ? 29  SER   C CA  1 
ATOM   2775  C  C   . SER   C  1 29  ? -40.511 -35.645  -35.438 1.00 25.62 ? 29  SER   C C   1 
ATOM   2776  O  O   . SER   C  1 29  ? -40.018 -34.771  -36.169 1.00 26.81 ? 29  SER   C O   1 
ATOM   2777  C  CB  . SER   C  1 29  ? -39.161 -37.213  -34.036 1.00 24.08 ? 29  SER   C CB  1 
ATOM   2778  O  OG  . SER   C  1 29  ? -38.311 -37.318  -35.167 1.00 26.90 ? 29  SER   C OG  1 
ATOM   2779  N  N   . ARG   C  1 30  ? -41.496 -36.440  -35.841 1.00 26.39 ? 30  ARG   C N   1 
ATOM   2780  C  CA  . ARG   C  1 30  ? -42.046 -36.350  -37.196 1.00 28.23 ? 30  ARG   C CA  1 
ATOM   2781  C  C   . ARG   C  1 30  ? -42.872 -35.087  -37.399 1.00 24.81 ? 30  ARG   C C   1 
ATOM   2782  O  O   . ARG   C  1 30  ? -42.910 -34.543  -38.508 1.00 25.99 ? 30  ARG   C O   1 
ATOM   2783  C  CB  . ARG   C  1 30  ? -42.867 -37.603  -37.497 1.00 26.63 ? 30  ARG   C CB  1 
ATOM   2784  C  CG  . ARG   C  1 30  ? -42.047 -38.728  -38.113 1.00 29.10 ? 30  ARG   C CG  1 
ATOM   2785  C  CD  . ARG   C  1 30  ? -40.695 -38.938  -37.422 1.00 29.18 ? 30  ARG   C CD  1 
ATOM   2786  N  NE  . ARG   C  1 30  ? -39.854 -39.847  -38.193 1.00 28.90 ? 30  ARG   C NE  1 
ATOM   2787  C  CZ  . ARG   C  1 30  ? -38.527 -39.776  -38.288 1.00 26.12 ? 30  ARG   C CZ  1 
ATOM   2788  N  NH1 . ARG   C  1 30  ? -37.822 -38.875  -37.622 1.00 27.46 ? 30  ARG   C NH1 1 
ATOM   2789  N  NH2 . ARG   C  1 30  ? -37.901 -40.617  -39.094 1.00 28.25 ? 30  ARG   C NH2 1 
ATOM   2790  N  N   . MET   C  1 31  ? -43.495 -34.571  -36.350 1.00 27.06 ? 31  MET   C N   1 
ATOM   2791  C  CA  . MET   C  1 31  ? -44.120 -33.257  -36.456 1.00 25.29 ? 31  MET   C CA  1 
ATOM   2792  C  C   . MET   C  1 31  ? -43.074 -32.186  -36.722 1.00 31.01 ? 31  MET   C C   1 
ATOM   2793  O  O   . MET   C  1 31  ? -43.227 -31.346  -37.619 1.00 28.55 ? 31  MET   C O   1 
ATOM   2794  C  CB  . MET   C  1 31  ? -44.910 -32.935  -35.167 1.00 27.10 ? 31  MET   C CB  1 
ATOM   2795  C  CG  . MET   C  1 31  ? -46.137 -33.828  -34.934 1.00 27.33 ? 31  MET   C CG  1 
ATOM   2796  S  SD  . MET   C  1 31  ? -46.786 -33.706  -33.240 1.00 29.02 ? 31  MET   C SD  1 
ATOM   2797  C  CE  . MET   C  1 31  ? -47.117 -31.970  -33.035 1.00 28.43 ? 31  MET   C CE  1 
ATOM   2798  N  N   . TRP   C  1 32  ? -41.998 -32.182  -35.937 1.00 27.72 ? 32  TRP   C N   1 
ATOM   2799  C  CA  . TRP   C  1 32  ? -40.938 -31.198  -36.160 1.00 28.35 ? 32  TRP   C CA  1 
ATOM   2800  C  C   . TRP   C  1 32  ? -40.355 -31.317  -37.569 1.00 27.57 ? 32  TRP   C C   1 
ATOM   2801  O  O   . TRP   C  1 32  ? -40.130 -30.302  -38.242 1.00 25.59 ? 32  TRP   C O   1 
ATOM   2802  C  CB  . TRP   C  1 32  ? -39.856 -31.342  -35.081 1.00 25.03 ? 32  TRP   C CB  1 
ATOM   2803  C  CG  . TRP   C  1 32  ? -40.185 -30.545  -33.827 1.00 27.22 ? 32  TRP   C CG  1 
ATOM   2804  C  CD1 . TRP   C  1 32  ? -40.741 -29.290  -33.776 1.00 28.02 ? 32  TRP   C CD1 1 
ATOM   2805  C  CD2 . TRP   C  1 32  ? -40.030 -30.963  -32.458 1.00 25.47 ? 32  TRP   C CD2 1 
ATOM   2806  N  NE1 . TRP   C  1 32  ? -40.926 -28.904  -32.475 1.00 28.26 ? 32  TRP   C NE1 1 
ATOM   2807  C  CE2 . TRP   C  1 32  ? -40.502 -29.907  -31.643 1.00 25.20 ? 32  TRP   C CE2 1 
ATOM   2808  C  CE3 . TRP   C  1 32  ? -39.518 -32.119  -31.843 1.00 30.69 ? 32  TRP   C CE3 1 
ATOM   2809  C  CZ2 . TRP   C  1 32  ? -40.471 -29.963  -30.245 1.00 25.89 ? 32  TRP   C CZ2 1 
ATOM   2810  C  CZ3 . TRP   C  1 32  ? -39.479 -32.175  -30.444 1.00 31.50 ? 32  TRP   C CZ3 1 
ATOM   2811  C  CH2 . TRP   C  1 32  ? -39.966 -31.103  -29.661 1.00 28.41 ? 32  TRP   C CH2 1 
ATOM   2812  N  N   . ASN   C  1 33  ? -40.134 -32.540  -38.057 1.00 28.70 ? 33  ASN   C N   1 
ATOM   2813  C  CA  . ASN   C  1 33  ? -39.637 -32.672  -39.431 1.00 28.72 ? 33  ASN   C CA  1 
ATOM   2814  C  C   . ASN   C  1 33  ? -40.643 -32.106  -40.427 1.00 33.78 ? 33  ASN   C C   1 
ATOM   2815  O  O   . ASN   C  1 33  ? -40.273 -31.364  -41.346 1.00 30.20 ? 33  ASN   C O   1 
ATOM   2816  C  CB  . ASN   C  1 33  ? -39.311 -34.132  -39.761 1.00 28.87 ? 33  ASN   C CB  1 
ATOM   2817  C  CG  . ASN   C  1 33  ? -38.017 -34.598  -39.114 1.00 30.25 ? 33  ASN   C CG  1 
ATOM   2818  O  OD1 . ASN   C  1 33  ? -37.212 -33.791  -38.682 1.00 28.03 ? 33  ASN   C OD1 1 
ATOM   2819  N  ND2 . ASN   C  1 33  ? -37.828 -35.891  -39.034 1.00 30.59 ? 33  ASN   C ND2 1 
ATOM   2820  N  N   . ASP   C  1 34  ? -41.925 -32.429  -40.245 1.00 31.70 ? 34  ASP   C N   1 
ATOM   2821  C  CA  . ASP   C  1 34  ? -42.958 -31.894  -41.125 1.00 30.93 ? 34  ASP   C CA  1 
ATOM   2822  C  C   . ASP   C  1 34  ? -42.933 -30.371  -41.151 1.00 25.73 ? 34  ASP   C C   1 
ATOM   2823  O  O   . ASP   C  1 34  ? -43.139 -29.755  -42.201 1.00 31.00 ? 34  ASP   C O   1 
ATOM   2824  C  CB  . ASP   C  1 34  ? -44.321 -32.423  -40.672 1.00 29.99 ? 34  ASP   C CB  1 
ATOM   2825  C  CG  . ASP   C  1 34  ? -45.487 -31.852  -41.489 1.00 38.65 ? 34  ASP   C CG  1 
ATOM   2826  O  OD1 . ASP   C  1 34  ? -45.427 -31.829  -42.728 1.00 37.63 ? 34  ASP   C OD1 1 
ATOM   2827  O  OD2 . ASP   C  1 34  ? -46.478 -31.455  -40.856 1.00 38.62 ? 34  ASP   C OD2 1 
ATOM   2828  N  N   . TRP   C  1 35  ? -42.691 -29.742  -40.015 1.00 27.80 ? 35  TRP   C N   1 
ATOM   2829  C  CA  . TRP   C  1 35  ? -42.638 -28.291  -39.935 1.00 27.31 ? 35  TRP   C CA  1 
ATOM   2830  C  C   . TRP   C  1 35  ? -41.316 -27.698  -40.413 1.00 30.96 ? 35  TRP   C C   1 
ATOM   2831  O  O   . TRP   C  1 35  ? -41.163 -26.468  -40.396 1.00 26.78 ? 35  TRP   C O   1 
ATOM   2832  C  CB  . TRP   C  1 35  ? -42.901 -27.848  -38.491 1.00 30.52 ? 35  TRP   C CB  1 
ATOM   2833  C  CG  . TRP   C  1 35  ? -44.233 -28.274  -37.931 1.00 29.72 ? 35  TRP   C CG  1 
ATOM   2834  C  CD1 . TRP   C  1 35  ? -45.299 -28.758  -38.623 1.00 38.78 ? 35  TRP   C CD1 1 
ATOM   2835  C  CD2 . TRP   C  1 35  ? -44.630 -28.258  -36.541 1.00 33.08 ? 35  TRP   C CD2 1 
ATOM   2836  N  NE1 . TRP   C  1 35  ? -46.340 -29.038  -37.757 1.00 36.34 ? 35  TRP   C NE1 1 
ATOM   2837  C  CE2 . TRP   C  1 35  ? -45.955 -28.736  -36.478 1.00 36.79 ? 35  TRP   C CE2 1 
ATOM   2838  C  CE3 . TRP   C  1 35  ? -43.995 -27.881  -35.356 1.00 37.71 ? 35  TRP   C CE3 1 
ATOM   2839  C  CZ2 . TRP   C  1 35  ? -46.655 -28.845  -35.276 1.00 35.80 ? 35  TRP   C CZ2 1 
ATOM   2840  C  CZ3 . TRP   C  1 35  ? -44.692 -27.994  -34.156 1.00 36.44 ? 35  TRP   C CZ3 1 
ATOM   2841  C  CH2 . TRP   C  1 35  ? -46.015 -28.459  -34.134 1.00 36.74 ? 35  TRP   C CH2 1 
ATOM   2842  N  N   . GLY   C  1 36  ? -40.351 -28.523  -40.816 1.00 24.99 ? 36  GLY   C N   1 
ATOM   2843  C  CA  . GLY   C  1 36  ? -39.087 -27.985  -41.272 1.00 32.15 ? 36  GLY   C CA  1 
ATOM   2844  C  C   . GLY   C  1 36  ? -38.107 -27.691  -40.165 1.00 31.34 ? 36  GLY   C C   1 
ATOM   2845  O  O   . GLY   C  1 36  ? -37.096 -27.027  -40.413 1.00 28.59 ? 36  GLY   C O   1 
ATOM   2846  N  N   . LEU   C  1 37  ? -38.397 -28.137  -38.947 1.00 27.85 ? 37  LEU   C N   1 
ATOM   2847  C  CA  . LEU   C  1 37  ? -37.525 -27.930  -37.797 1.00 28.26 ? 37  LEU   C CA  1 
ATOM   2848  C  C   . LEU   C  1 37  ? -36.659 -29.173  -37.579 1.00 27.18 ? 37  LEU   C C   1 
ATOM   2849  O  O   . LEU   C  1 37  ? -36.759 -29.888  -36.576 1.00 24.80 ? 37  LEU   C O   1 
ATOM   2850  C  CB  . LEU   C  1 37  ? -38.370 -27.599  -36.561 1.00 29.29 ? 37  LEU   C CB  1 
ATOM   2851  C  CG  . LEU   C  1 37  ? -39.067 -26.249  -36.741 1.00 34.44 ? 37  LEU   C CG  1 
ATOM   2852  C  CD1 . LEU   C  1 37  ? -40.054 -25.980  -35.638 1.00 35.67 ? 37  LEU   C CD1 1 
ATOM   2853  C  CD2 . LEU   C  1 37  ? -38.027 -25.123  -36.806 1.00 28.35 ? 37  LEU   C CD2 1 
ATOM   2854  N  N   . LYS   C  1 38  ? -35.789 -29.420  -38.567 1.00 26.55 ? 38  LYS   C N   1 
ATOM   2855  C  CA  . LYS   C  1 38  ? -35.178 -30.738  -38.717 1.00 27.49 ? 38  LYS   C CA  1 
ATOM   2856  C  C   . LYS   C  1 38  ? -34.159 -31.046  -37.639 1.00 22.91 ? 38  LYS   C C   1 
ATOM   2857  O  O   . LYS   C  1 38  ? -33.900 -32.227  -37.378 1.00 27.12 ? 38  LYS   C O   1 
ATOM   2858  C  CB  . LYS   C  1 38  ? -34.487 -30.862  -40.075 1.00 32.57 ? 38  LYS   C CB  1 
ATOM   2859  C  CG  . LYS   C  1 38  ? -35.349 -30.499  -41.268 1.00 39.31 ? 38  LYS   C CG  1 
ATOM   2860  C  CD  . LYS   C  1 38  ? -36.289 -31.597  -41.657 1.00 45.19 ? 38  LYS   C CD  1 
ATOM   2861  C  CE  . LYS   C  1 38  ? -36.499 -31.560  -43.178 1.00 50.19 ? 38  LYS   C CE  1 
ATOM   2862  N  NZ  . LYS   C  1 38  ? -37.741 -32.196  -43.622 1.00 52.92 ? 38  LYS   C NZ  1 
ATOM   2863  N  N   . ARG   C  1 39  ? -33.550 -30.037  -37.027 1.00 25.64 ? 39  ARG   C N   1 
ATOM   2864  C  CA  . ARG   C  1 39  ? -32.600 -30.346  -35.949 1.00 35.35 ? 39  ARG   C CA  1 
ATOM   2865  C  C   . ARG   C  1 39  ? -33.321 -30.842  -34.693 1.00 30.04 ? 39  ARG   C C   1 
ATOM   2866  O  O   . ARG   C  1 39  ? -32.837 -31.760  -34.009 1.00 26.82 ? 39  ARG   C O   1 
ATOM   2867  C  CB  . ARG   C  1 39  ? -31.737 -29.130  -35.633 1.00 30.58 ? 39  ARG   C CB  1 
ATOM   2868  C  CG  . ARG   C  1 39  ? -30.536 -29.465  -34.721 1.00 37.10 ? 39  ARG   C CG  1 
ATOM   2869  C  CD  . ARG   C  1 39  ? -29.935 -28.203  -34.147 1.00 46.16 ? 39  ARG   C CD  1 
ATOM   2870  N  NE  . ARG   C  1 39  ? -28.977 -27.618  -35.065 1.00 60.36 ? 39  ARG   C NE  1 
ATOM   2871  C  CZ  . ARG   C  1 39  ? -27.662 -27.695  -34.922 1.00 62.49 ? 39  ARG   C CZ  1 
ATOM   2872  N  NH1 . ARG   C  1 39  ? -27.112 -28.315  -33.892 1.00 61.82 ? 39  ARG   C NH1 1 
ATOM   2873  N  NH2 . ARG   C  1 39  ? -26.882 -27.132  -35.834 1.00 66.35 ? 39  ARG   C NH2 1 
ATOM   2874  N  N   . LEU   C  1 40  ? -34.467 -30.234  -34.360 1.00 25.70 ? 40  LEU   C N   1 
ATOM   2875  C  CA  . LEU   C  1 40  ? -35.339 -30.807  -33.331 1.00 25.54 ? 40  LEU   C CA  1 
ATOM   2876  C  C   . LEU   C  1 40  ? -35.856 -32.179  -33.741 1.00 21.27 ? 40  LEU   C C   1 
ATOM   2877  O  O   . LEU   C  1 40  ? -35.902 -33.110  -32.920 1.00 27.02 ? 40  LEU   C O   1 
ATOM   2878  C  CB  . LEU   C  1 40  ? -36.532 -29.888  -33.052 1.00 33.50 ? 40  LEU   C CB  1 
ATOM   2879  C  CG  . LEU   C  1 40  ? -36.320 -28.667  -32.167 1.00 29.70 ? 40  LEU   C CG  1 
ATOM   2880  C  CD1 . LEU   C  1 40  ? -37.508 -27.711  -32.329 1.00 33.70 ? 40  LEU   C CD1 1 
ATOM   2881  C  CD2 . LEU   C  1 40  ? -36.168 -29.118  -30.719 1.00 36.64 ? 40  LEU   C CD2 1 
ATOM   2882  N  N   . GLY   C  1 41  ? -36.246 -32.331  -35.004 1.00 25.06 ? 41  GLY   C N   1 
ATOM   2883  C  CA  . GLY   C  1 41  ? -36.747 -33.618  -35.444 1.00 27.97 ? 41  GLY   C CA  1 
ATOM   2884  C  C   . GLY   C  1 41  ? -35.719 -34.719  -35.279 1.00 30.47 ? 41  GLY   C C   1 
ATOM   2885  O  O   . GLY   C  1 41  ? -36.041 -35.811  -34.816 1.00 27.27 ? 41  GLY   C O   1 
ATOM   2886  N  N   . ALA   C  1 42  ? -34.468 -34.448  -35.686 1.00 23.62 ? 42  ALA   C N   1 
ATOM   2887  C  CA  . ALA   C  1 42  ? -33.407 -35.442  -35.560 1.00 28.54 ? 42  ALA   C CA  1 
ATOM   2888  C  C   . ALA   C  1 42  ? -33.127 -35.758  -34.095 1.00 25.99 ? 42  ALA   C C   1 
ATOM   2889  O  O   . ALA   C  1 42  ? -32.997 -36.928  -33.710 1.00 25.00 ? 42  ALA   C O   1 
ATOM   2890  C  CB  . ALA   C  1 42  ? -32.124 -34.932  -36.245 1.00 28.92 ? 42  ALA   C CB  1 
ATOM   2891  N  N   . HIS   C  1 43  ? -33.001 -34.720  -33.266 1.00 26.50 ? 43  HIS   C N   1 
ATOM   2892  C  CA  . HIS   C  1 43  ? -32.693 -34.949  -31.859 1.00 26.61 ? 43  HIS   C CA  1 
ATOM   2893  C  C   . HIS   C  1 43  ? -33.802 -35.744  -31.178 1.00 31.38 ? 43  HIS   C C   1 
ATOM   2894  O  O   . HIS   C  1 43  ? -33.536 -36.656  -30.384 1.00 26.56 ? 43  HIS   C O   1 
ATOM   2895  C  CB  . HIS   C  1 43  ? -32.464 -33.626  -31.142 1.00 27.56 ? 43  HIS   C CB  1 
ATOM   2896  C  CG  . HIS   C  1 43  ? -31.788 -33.796  -29.827 1.00 30.86 ? 43  HIS   C CG  1 
ATOM   2897  N  ND1 . HIS   C  1 43  ? -32.472 -34.110  -28.674 1.00 32.90 ? 43  HIS   C ND1 1 
ATOM   2898  C  CD2 . HIS   C  1 43  ? -30.479 -33.744  -29.488 1.00 32.35 ? 43  HIS   C CD2 1 
ATOM   2899  C  CE1 . HIS   C  1 43  ? -31.612 -34.252  -27.681 1.00 31.14 ? 43  HIS   C CE1 1 
ATOM   2900  N  NE2 . HIS   C  1 43  ? -30.400 -34.037  -28.149 1.00 29.03 ? 43  HIS   C NE2 1 
ATOM   2901  N  N   . GLU   C  1 44  ? -35.058 -35.430  -31.491 1.00 26.77 ? 44  GLU   C N   1 
ATOM   2902  C  CA  . GLU   C  1 44  ? -36.159 -36.156  -30.865 1.00 22.39 ? 44  GLU   C CA  1 
ATOM   2903  C  C   . GLU   C  1 44  ? -36.247 -37.584  -31.383 1.00 26.64 ? 44  GLU   C C   1 
ATOM   2904  O  O   . GLU   C  1 44  ? -36.613 -38.496  -30.637 1.00 23.85 ? 44  GLU   C O   1 
ATOM   2905  C  CB  . GLU   C  1 44  ? -37.470 -35.408  -31.117 1.00 30.99 ? 44  GLU   C CB  1 
ATOM   2906  C  CG  . GLU   C  1 44  ? -38.671 -36.003  -30.373 1.00 29.56 ? 44  GLU   C CG  1 
ATOM   2907  C  CD  . GLU   C  1 44  ? -38.771 -35.450  -28.970 1.00 33.21 ? 44  GLU   C CD  1 
ATOM   2908  O  OE1 . GLU   C  1 44  ? -37.744 -34.969  -28.458 1.00 30.29 ? 44  GLU   C OE1 1 
ATOM   2909  O  OE2 . GLU   C  1 44  ? -39.881 -35.430  -28.405 1.00 29.83 ? 44  GLU   C OE2 1 
ATOM   2910  N  N   . TYR   C  1 45  ? -35.910 -37.799  -32.653 1.00 26.27 ? 45  TYR   C N   1 
ATOM   2911  C  CA  . TYR   C  1 45  ? -35.807 -39.157  -33.169 1.00 23.75 ? 45  TYR   C CA  1 
ATOM   2912  C  C   . TYR   C  1 45  ? -34.824 -39.983  -32.339 1.00 27.68 ? 45  TYR   C C   1 
ATOM   2913  O  O   . TYR   C  1 45  ? -35.092 -41.138  -31.993 1.00 26.42 ? 45  TYR   C O   1 
ATOM   2914  C  CB  . TYR   C  1 45  ? -35.370 -39.103  -34.628 1.00 27.22 ? 45  TYR   C CB  1 
ATOM   2915  C  CG  . TYR   C  1 45  ? -34.992 -40.437  -35.203 1.00 28.95 ? 45  TYR   C CG  1 
ATOM   2916  C  CD1 . TYR   C  1 45  ? -35.957 -41.267  -35.733 1.00 27.20 ? 45  TYR   C CD1 1 
ATOM   2917  C  CD2 . TYR   C  1 45  ? -33.657 -40.862  -35.238 1.00 25.25 ? 45  TYR   C CD2 1 
ATOM   2918  C  CE1 . TYR   C  1 45  ? -35.636 -42.482  -36.270 1.00 32.80 ? 45  TYR   C CE1 1 
ATOM   2919  C  CE2 . TYR   C  1 45  ? -33.323 -42.089  -35.780 1.00 33.31 ? 45  TYR   C CE2 1 
ATOM   2920  C  CZ  . TYR   C  1 45  ? -34.316 -42.890  -36.304 1.00 36.22 ? 45  TYR   C CZ  1 
ATOM   2921  O  OH  . TYR   C  1 45  ? -34.019 -44.125  -36.838 1.00 39.18 ? 45  TYR   C OH  1 
ATOM   2922  N  N   . HIS   C  1 46  ? -33.649 -39.422  -32.054 1.00 28.71 ? 46  HIS   C N   1 
ATOM   2923  C  CA  . HIS   C  1 46  ? -32.666 -40.169  -31.272 1.00 29.05 ? 46  HIS   C CA  1 
ATOM   2924  C  C   . HIS   C  1 46  ? -33.147 -40.390  -29.841 1.00 25.86 ? 46  HIS   C C   1 
ATOM   2925  O  O   . HIS   C  1 46  ? -32.836 -41.428  -29.245 1.00 30.33 ? 46  HIS   C O   1 
ATOM   2926  C  CB  . HIS   C  1 46  ? -31.316 -39.448  -31.303 1.00 27.94 ? 46  HIS   C CB  1 
ATOM   2927  C  CG  . HIS   C  1 46  ? -30.675 -39.477  -32.659 1.00 31.65 ? 46  HIS   C CG  1 
ATOM   2928  N  ND1 . HIS   C  1 46  ? -30.336 -38.335  -33.350 1.00 41.95 ? 46  HIS   C ND1 1 
ATOM   2929  C  CD2 . HIS   C  1 46  ? -30.334 -40.518  -33.460 1.00 35.25 ? 46  HIS   C CD2 1 
ATOM   2930  C  CE1 . HIS   C  1 46  ? -29.799 -38.669  -34.514 1.00 43.76 ? 46  HIS   C CE1 1 
ATOM   2931  N  NE2 . HIS   C  1 46  ? -29.788 -39.987  -34.606 1.00 45.70 ? 46  HIS   C NE2 1 
ATOM   2932  N  N   . GLU   C  1 47  ? -33.898 -39.440  -29.273 1.00 25.09 ? 47  GLU   C N   1 
ATOM   2933  C  CA  . GLU   C  1 47  ? -34.531 -39.686  -27.974 1.00 27.38 ? 47  GLU   C CA  1 
ATOM   2934  C  C   . GLU   C  1 47  ? -35.451 -40.906  -28.036 1.00 30.85 ? 47  GLU   C C   1 
ATOM   2935  O  O   . GLU   C  1 47  ? -35.435 -41.772  -27.148 1.00 24.95 ? 47  GLU   C O   1 
ATOM   2936  C  CB  . GLU   C  1 47  ? -35.331 -38.468  -27.521 1.00 28.34 ? 47  GLU   C CB  1 
ATOM   2937  C  CG  . GLU   C  1 47  ? -34.555 -37.175  -27.313 1.00 38.70 ? 47  GLU   C CG  1 
ATOM   2938  C  CD  . GLU   C  1 47  ? -33.627 -37.253  -26.131 1.00 46.55 ? 47  GLU   C CD  1 
ATOM   2939  O  OE1 . GLU   C  1 47  ? -33.622 -38.313  -25.483 1.00 51.18 ? 47  GLU   C OE1 1 
ATOM   2940  O  OE2 . GLU   C  1 47  ? -32.910 -36.264  -25.852 1.00 46.61 ? 47  GLU   C OE2 1 
ATOM   2941  N  N   . SER   C  1 48  ? -36.269 -40.985  -29.085 1.00 27.03 ? 48  SER   C N   1 
ATOM   2942  C  CA  . SER   C  1 48  ? -37.183 -42.116  -29.228 1.00 24.76 ? 48  SER   C CA  1 
ATOM   2943  C  C   . SER   C  1 48  ? -36.419 -43.425  -29.358 1.00 24.42 ? 48  SER   C C   1 
ATOM   2944  O  O   . SER   C  1 48  ? -36.796 -44.435  -28.764 1.00 25.68 ? 48  SER   C O   1 
ATOM   2945  C  CB  . SER   C  1 48  ? -38.099 -41.871  -30.455 1.00 25.99 ? 48  SER   C CB  1 
ATOM   2946  O  OG  . SER   C  1 48  ? -39.089 -42.877  -30.600 1.00 28.70 ? 48  SER   C OG  1 
ATOM   2947  N  N   . ILE   C  1 49  ? -35.334 -43.429  -30.140 1.00 26.14 ? 49  ILE   C N   1 
ATOM   2948  C  CA  . ILE   C  1 49  ? -34.509 -44.626  -30.282 1.00 27.93 ? 49  ILE   C CA  1 
ATOM   2949  C  C   . ILE   C  1 49  ? -33.931 -45.031  -28.931 1.00 23.36 ? 49  ILE   C C   1 
ATOM   2950  O  O   . ILE   C  1 49  ? -33.895 -46.223  -28.588 1.00 27.52 ? 49  ILE   C O   1 
ATOM   2951  C  CB  . ILE   C  1 49  ? -33.379 -44.395  -31.317 1.00 28.07 ? 49  ILE   C CB  1 
ATOM   2952  C  CG1 . ILE   C  1 49  ? -33.944 -44.093  -32.698 1.00 28.85 ? 49  ILE   C CG1 1 
ATOM   2953  C  CG2 . ILE   C  1 49  ? -32.418 -45.595  -31.359 1.00 29.01 ? 49  ILE   C CG2 1 
ATOM   2954  C  CD1 . ILE   C  1 49  ? -34.509 -45.276  -33.399 1.00 35.87 ? 49  ILE   C CD1 1 
ATOM   2955  N  N   . ASP   C  1 50  ? -33.461 -44.056  -28.148 1.00 25.77 ? 50  ASP   C N   1 
ATOM   2956  C  CA  . ASP   C  1 50  ? -32.922 -44.382  -26.829 1.00 28.52 ? 50  ASP   C CA  1 
ATOM   2957  C  C   . ASP   C  1 50  ? -33.964 -45.064  -25.965 1.00 26.47 ? 50  ASP   C C   1 
ATOM   2958  O  O   . ASP   C  1 50  ? -33.642 -46.001  -25.227 1.00 24.47 ? 50  ASP   C O   1 
ATOM   2959  C  CB  . ASP   C  1 50  ? -32.400 -43.135  -26.116 1.00 35.02 ? 50  ASP   C CB  1 
ATOM   2960  C  CG  . ASP   C  1 50  ? -31.066 -42.630  -26.686 1.00 50.46 ? 50  ASP   C CG  1 
ATOM   2961  O  OD1 . ASP   C  1 50  ? -30.375 -43.364  -27.440 1.00 49.61 ? 50  ASP   C OD1 1 
ATOM   2962  O  OD2 . ASP   C  1 50  ? -30.716 -41.473  -26.375 1.00 64.17 ? 50  ASP   C OD2 1 
ATOM   2963  N  N   . GLU   C  1 51  ? -35.222 -44.601  -26.029 1.00 25.55 ? 51  GLU   C N   1 
ATOM   2964  C  CA  . GLU   C  1 51  ? -36.276 -45.241  -25.235 1.00 25.92 ? 51  GLU   C CA  1 
ATOM   2965  C  C   . GLU   C  1 51  ? -36.559 -46.645  -25.738 1.00 26.61 ? 51  GLU   C C   1 
ATOM   2966  O  O   . GLU   C  1 51  ? -36.837 -47.556  -24.955 1.00 28.46 ? 51  GLU   C O   1 
ATOM   2967  C  CB  . GLU   C  1 51  ? -37.546 -44.392  -25.292 1.00 29.87 ? 51  GLU   C CB  1 
ATOM   2968  C  CG  . GLU   C  1 51  ? -37.367 -43.027  -24.638 1.00 27.78 ? 51  GLU   C CG  1 
ATOM   2969  C  CD  . GLU   C  1 51  ? -37.113 -43.149  -23.142 1.00 39.83 ? 51  GLU   C CD  1 
ATOM   2970  O  OE1 . GLU   C  1 51  ? -38.056 -43.475  -22.398 1.00 49.09 ? 51  GLU   C OE1 1 
ATOM   2971  O  OE2 . GLU   C  1 51  ? -35.985 -42.921  -22.711 1.00 33.51 ? 51  GLU   C OE2 1 
ATOM   2972  N  N   . MET   C  1 52  ? -36.523 -46.831  -27.050 1.00 24.82 ? 52  MET   C N   1 
ATOM   2973  C  CA  . MET   C  1 52  ? -36.653 -48.167  -27.608 1.00 24.77 ? 52  MET   C CA  1 
ATOM   2974  C  C   . MET   C  1 52  ? -35.596 -49.105  -27.052 1.00 29.42 ? 52  MET   C C   1 
ATOM   2975  O  O   . MET   C  1 52  ? -35.892 -50.261  -26.730 1.00 24.14 ? 52  MET   C O   1 
ATOM   2976  C  CB  . MET   C  1 52  ? -36.546 -48.106  -29.137 1.00 26.08 ? 52  MET   C CB  1 
ATOM   2977  C  CG  . MET   C  1 52  ? -37.721 -47.413  -29.826 1.00 25.32 ? 52  MET   C CG  1 
ATOM   2978  S  SD  . MET   C  1 52  ? -37.438 -47.202  -31.612 1.00 27.84 ? 52  MET   C SD  1 
ATOM   2979  C  CE  . MET   C  1 52  ? -38.308 -45.679  -31.901 1.00 25.16 ? 52  MET   C CE  1 
ATOM   2980  N  N   . LYS   C  1 53  ? -34.337 -48.644  -26.991 1.00 24.63 ? 53  LYS   C N   1 
ATOM   2981  C  CA  . LYS   C  1 53  ? -33.273 -49.485  -26.450 1.00 29.06 ? 53  LYS   C CA  1 
ATOM   2982  C  C   . LYS   C  1 53  ? -33.503 -49.792  -24.969 1.00 27.89 ? 53  LYS   C C   1 
ATOM   2983  O  O   . LYS   C  1 53  ? -33.303 -50.933  -24.539 1.00 25.31 ? 53  LYS   C O   1 
ATOM   2984  C  CB  . LYS   C  1 53  ? -31.909 -48.820  -26.639 1.00 26.80 ? 53  LYS   C CB  1 
ATOM   2985  C  CG  . LYS   C  1 53  ? -31.510 -48.642  -28.071 1.00 30.14 ? 53  LYS   C CG  1 
ATOM   2986  C  CD  . LYS   C  1 53  ? -30.139 -47.957  -28.109 1.00 42.90 ? 53  LYS   C CD  1 
ATOM   2987  C  CE  . LYS   C  1 53  ? -29.627 -47.704  -29.511 1.00 49.55 ? 53  LYS   C CE  1 
ATOM   2988  N  NZ  . LYS   C  1 53  ? -28.406 -46.829  -29.469 1.00 57.52 ? 53  LYS   C NZ  1 
ATOM   2989  N  N   . HIS   C  1 54  ? -33.934 -48.794  -24.181 1.00 24.64 ? 54  HIS   C N   1 
ATOM   2990  C  CA  . HIS   C  1 54  ? -34.290 -49.063  -22.779 1.00 31.57 ? 54  HIS   C CA  1 
ATOM   2991  C  C   . HIS   C  1 54  ? -35.408 -50.104  -22.674 1.00 26.68 ? 54  HIS   C C   1 
ATOM   2992  O  O   . HIS   C  1 54  ? -35.388 -50.970  -21.784 1.00 22.83 ? 54  HIS   C O   1 
ATOM   2993  C  CB  . HIS   C  1 54  ? -34.759 -47.794  -22.041 1.00 26.91 ? 54  HIS   C CB  1 
ATOM   2994  C  CG  . HIS   C  1 54  ? -33.786 -46.658  -22.040 1.00 30.78 ? 54  HIS   C CG  1 
ATOM   2995  N  ND1 . HIS   C  1 54  ? -32.419 -46.829  -22.140 1.00 33.90 ? 54  HIS   C ND1 1 
ATOM   2996  C  CD2 . HIS   C  1 54  ? -33.992 -45.317  -21.965 1.00 29.30 ? 54  HIS   C CD2 1 
ATOM   2997  C  CE1 . HIS   C  1 54  ? -31.825 -45.647  -22.120 1.00 29.81 ? 54  HIS   C CE1 1 
ATOM   2998  N  NE2 . HIS   C  1 54  ? -32.752 -44.712  -22.020 1.00 30.12 ? 54  HIS   C NE2 1 
ATOM   2999  N  N   . ALA   C  1 55  ? -36.439 -49.979  -23.516 1.00 28.06 ? 55  ALA   C N   1 
ATOM   3000  C  CA  . ALA   C  1 55  ? -37.552 -50.920  -23.464 1.00 24.02 ? 55  ALA   C CA  1 
ATOM   3001  C  C   . ALA   C  1 55  ? -37.074 -52.328  -23.766 1.00 29.78 ? 55  ALA   C C   1 
ATOM   3002  O  O   . ALA   C  1 55  ? -37.441 -53.278  -23.070 1.00 25.48 ? 55  ALA   C O   1 
ATOM   3003  C  CB  . ALA   C  1 55  ? -38.650 -50.485  -24.449 1.00 24.88 ? 55  ALA   C CB  1 
ATOM   3004  N  N   . ASP   C  1 56  ? -36.223 -52.481  -24.788 1.00 27.08 ? 56  ASP   C N   1 
ATOM   3005  C  CA  . ASP   C  1 56  ? -35.642 -53.784  -25.076 1.00 26.44 ? 56  ASP   C CA  1 
ATOM   3006  C  C   . ASP   C  1 56  ? -35.003 -54.373  -23.829 1.00 30.07 ? 56  ASP   C C   1 
ATOM   3007  O  O   . ASP   C  1 56  ? -35.278 -55.521  -23.454 1.00 25.80 ? 56  ASP   C O   1 
ATOM   3008  C  CB  . ASP   C  1 56  ? -34.610 -53.649  -26.208 1.00 27.35 ? 56  ASP   C CB  1 
ATOM   3009  C  CG  . ASP   C  1 56  ? -34.041 -54.986  -26.673 1.00 25.16 ? 56  ASP   C CG  1 
ATOM   3010  O  OD1 . ASP   C  1 56  ? -34.561 -56.062  -26.335 1.00 30.63 ? 56  ASP   C OD1 1 
ATOM   3011  O  OD2 . ASP   C  1 56  ? -33.053 -54.964  -27.423 1.00 31.17 ? 56  ASP   C OD2 1 
ATOM   3012  N  N   . LYS   C  1 57  ? -34.130 -53.604  -23.173 1.00 25.62 ? 57  LYS   C N   1 
ATOM   3013  C  CA  . LYS   C  1 57  ? -33.445 -54.160  -22.012 1.00 25.27 ? 57  LYS   C CA  1 
ATOM   3014  C  C   . LYS   C  1 57  ? -34.445 -54.553  -20.935 1.00 25.96 ? 57  LYS   C C   1 
ATOM   3015  O  O   . LYS   C  1 57  ? -34.286 -55.589  -20.275 1.00 25.52 ? 57  LYS   C O   1 
ATOM   3016  C  CB  . LYS   C  1 57  ? -32.430 -53.167  -21.442 1.00 27.19 ? 57  LYS   C CB  1 
ATOM   3017  C  CG  . LYS   C  1 57  ? -31.250 -52.808  -22.416 1.00 24.67 ? 57  LYS   C CG  1 
ATOM   3018  C  CD  . LYS   C  1 57  ? -30.533 -54.038  -22.890 1.00 36.97 ? 57  LYS   C CD  1 
ATOM   3019  N  N   . LEU   C  1 58  ? -35.445 -53.711  -20.696 1.00 25.76 ? 58  LEU   C N   1 
ATOM   3020  C  CA  . LEU   C  1 58  ? -36.436 -54.048  -19.671 1.00 24.58 ? 58  LEU   C CA  1 
ATOM   3021  C  C   . LEU   C  1 58  ? -37.163 -55.339  -20.020 1.00 26.99 ? 58  LEU   C C   1 
ATOM   3022  O  O   . LEU   C  1 58  ? -37.331 -56.225  -19.173 1.00 25.87 ? 58  LEU   C O   1 
ATOM   3023  C  CB  . LEU   C  1 58  ? -37.423 -52.894  -19.503 1.00 29.19 ? 58  LEU   C CB  1 
ATOM   3024  C  CG  . LEU   C  1 58  ? -36.823 -51.661  -18.830 1.00 32.92 ? 58  LEU   C CG  1 
ATOM   3025  C  CD1 . LEU   C  1 58  ? -37.717 -50.475  -19.081 1.00 29.78 ? 58  LEU   C CD1 1 
ATOM   3026  C  CD2 . LEU   C  1 58  ? -36.601 -51.906  -17.317 1.00 32.74 ? 58  LEU   C CD2 1 
ATOM   3027  N  N   . ILE   C  1 59  ? -37.574 -55.473  -21.282 1.00 28.95 ? 59  ILE   C N   1 
ATOM   3028  C  CA  . ILE   C  1 59  ? -38.245 -56.687  -21.736 1.00 29.99 ? 59  ILE   C CA  1 
ATOM   3029  C  C   . ILE   C  1 59  ? -37.351 -57.901  -21.517 1.00 29.57 ? 59  ILE   C C   1 
ATOM   3030  O  O   . ILE   C  1 59  ? -37.784 -58.947  -21.013 1.00 26.80 ? 59  ILE   C O   1 
ATOM   3031  C  CB  . ILE   C  1 59  ? -38.659 -56.529  -23.218 1.00 24.53 ? 59  ILE   C CB  1 
ATOM   3032  C  CG1 . ILE   C  1 59  ? -39.768 -55.485  -23.339 1.00 29.41 ? 59  ILE   C CG1 1 
ATOM   3033  C  CG2 . ILE   C  1 59  ? -39.060 -57.870  -23.804 1.00 25.60 ? 59  ILE   C CG2 1 
ATOM   3034  C  CD1 . ILE   C  1 59  ? -39.991 -54.962  -24.778 1.00 31.82 ? 59  ILE   C CD1 1 
ATOM   3035  N  N   . GLU   C  1 60  ? -36.080 -57.787  -21.882 1.00 27.97 ? 60  GLU   C N   1 
ATOM   3036  C  CA  . GLU   C  1 60  ? -35.169 -58.916  -21.707 1.00 28.99 ? 60  GLU   C CA  1 
ATOM   3037  C  C   . GLU   C  1 60  ? -35.020 -59.287  -20.239 1.00 28.51 ? 60  GLU   C C   1 
ATOM   3038  O  O   . GLU   C  1 60  ? -34.946 -60.472  -19.897 1.00 26.56 ? 60  GLU   C O   1 
ATOM   3039  C  CB  . GLU   C  1 60  ? -33.794 -58.591  -22.318 1.00 25.76 ? 60  GLU   C CB  1 
ATOM   3040  C  CG  . GLU   C  1 60  ? -33.893 -58.367  -23.818 1.00 29.64 ? 60  GLU   C CG  1 
ATOM   3041  C  CD  . GLU   C  1 60  ? -32.556 -57.940  -24.450 1.00 38.45 ? 60  GLU   C CD  1 
ATOM   3042  O  OE1 . GLU   C  1 60  ? -31.891 -57.093  -23.839 1.00 33.86 ? 60  GLU   C OE1 1 
ATOM   3043  O  OE2 . GLU   C  1 60  ? -32.192 -58.447  -25.545 1.00 34.80 ? 60  GLU   C OE2 1 
ATOM   3044  N  N   . ARG   C  1 61  ? -34.946 -58.284  -19.369 1.00 24.30 ? 61  ARG   C N   1 
ATOM   3045  C  CA  . ARG   C  1 61  ? -34.787 -58.542  -17.945 1.00 24.03 ? 61  ARG   C CA  1 
ATOM   3046  C  C   . ARG   C  1 61  ? -36.043 -59.185  -17.365 1.00 26.66 ? 61  ARG   C C   1 
ATOM   3047  O  O   . ARG   C  1 61  ? -35.953 -60.142  -16.586 1.00 29.51 ? 61  ARG   C O   1 
ATOM   3048  C  CB  . ARG   C  1 61  ? -34.457 -57.235  -17.230 1.00 25.10 ? 61  ARG   C CB  1 
ATOM   3049  C  CG  . ARG   C  1 61  ? -34.192 -57.368  -15.741 1.00 28.94 ? 61  ARG   C CG  1 
ATOM   3050  C  CD  . ARG   C  1 61  ? -32.928 -58.144  -15.476 1.00 29.73 ? 61  ARG   C CD  1 
ATOM   3051  N  NE  . ARG   C  1 61  ? -32.624 -58.285  -14.042 1.00 27.36 ? 61  ARG   C NE  1 
ATOM   3052  C  CZ  . ARG   C  1 61  ? -31.714 -59.112  -13.551 1.00 24.20 ? 61  ARG   C CZ  1 
ATOM   3053  N  NH1 . ARG   C  1 61  ? -30.930 -59.832  -14.346 1.00 26.18 ? 61  ARG   C NH1 1 
ATOM   3054  N  NH2 . ARG   C  1 61  ? -31.603 -59.245  -12.232 1.00 26.78 ? 61  ARG   C NH2 1 
ATOM   3055  N  N   . ILE   C  1 62  ? -37.221 -58.692  -17.758 1.00 27.23 ? 62  ILE   C N   1 
ATOM   3056  C  CA  . ILE   C  1 62  ? -38.479 -59.257  -17.252 1.00 27.60 ? 62  ILE   C CA  1 
ATOM   3057  C  C   . ILE   C  1 62  ? -38.572 -60.735  -17.607 1.00 31.96 ? 62  ILE   C C   1 
ATOM   3058  O  O   . ILE   C  1 62  ? -38.929 -61.573  -16.769 1.00 29.11 ? 62  ILE   C O   1 
ATOM   3059  C  CB  . ILE   C  1 62  ? -39.689 -58.470  -17.796 1.00 30.64 ? 62  ILE   C CB  1 
ATOM   3060  C  CG1 . ILE   C  1 62  ? -39.704 -57.068  -17.195 1.00 26.48 ? 62  ILE   C CG1 1 
ATOM   3061  C  CG2 . ILE   C  1 62  ? -41.018 -59.271  -17.546 1.00 29.15 ? 62  ILE   C CG2 1 
ATOM   3062  C  CD1 . ILE   C  1 62  ? -40.605 -56.121  -17.892 1.00 28.89 ? 62  ILE   C CD1 1 
ATOM   3063  N  N   . LEU   C  1 63  ? -38.257 -61.076  -18.859 1.00 29.77 ? 63  LEU   C N   1 
ATOM   3064  C  CA  . LEU   C  1 63  ? -38.300 -62.480  -19.277 1.00 29.48 ? 63  LEU   C CA  1 
ATOM   3065  C  C   . LEU   C  1 63  ? -37.278 -63.328  -18.555 1.00 30.67 ? 63  LEU   C C   1 
ATOM   3066  O  O   . LEU   C  1 63  ? -37.557 -64.481  -18.216 1.00 33.03 ? 63  LEU   C O   1 
ATOM   3067  C  CB  . LEU   C  1 63  ? -38.090 -62.602  -20.783 1.00 31.17 ? 63  LEU   C CB  1 
ATOM   3068  C  CG  . LEU   C  1 63  ? -39.233 -62.056  -21.630 1.00 30.75 ? 63  LEU   C CG  1 
ATOM   3069  C  CD1 . LEU   C  1 63  ? -38.717 -61.850  -23.053 1.00 26.23 ? 63  LEU   C CD1 1 
ATOM   3070  C  CD2 . LEU   C  1 63  ? -40.504 -62.957  -21.610 1.00 31.06 ? 63  LEU   C CD2 1 
ATOM   3071  N  N   . PHE   C  1 64  ? -36.066 -62.811  -18.338 1.00 30.24 ? 64  PHE   C N   1 
ATOM   3072  C  CA  . PHE   C  1 64  ? -35.121 -63.612  -17.586 1.00 27.55 ? 64  PHE   C CA  1 
ATOM   3073  C  C   . PHE   C  1 64  ? -35.640 -63.901  -16.176 1.00 26.49 ? 64  PHE   C C   1 
ATOM   3074  O  O   . PHE   C  1 64  ? -35.353 -64.959  -15.614 1.00 28.08 ? 64  PHE   C O   1 
ATOM   3075  C  CB  . PHE   C  1 64  ? -33.764 -62.904  -17.518 1.00 28.07 ? 64  PHE   C CB  1 
ATOM   3076  C  CG  . PHE   C  1 64  ? -32.842 -63.473  -16.512 1.00 31.97 ? 64  PHE   C CG  1 
ATOM   3077  C  CD1 . PHE   C  1 64  ? -32.348 -64.761  -16.649 1.00 31.42 ? 64  PHE   C CD1 1 
ATOM   3078  C  CD2 . PHE   C  1 64  ? -32.421 -62.710  -15.448 1.00 31.64 ? 64  PHE   C CD2 1 
ATOM   3079  C  CE1 . PHE   C  1 64  ? -31.470 -65.271  -15.719 1.00 30.11 ? 64  PHE   C CE1 1 
ATOM   3080  C  CE2 . PHE   C  1 64  ? -31.545 -63.214  -14.522 1.00 33.30 ? 64  PHE   C CE2 1 
ATOM   3081  C  CZ  . PHE   C  1 64  ? -31.072 -64.492  -14.653 1.00 32.26 ? 64  PHE   C CZ  1 
ATOM   3082  N  N   . LEU   C  1 65  ? -36.361 -62.964  -15.585 1.00 27.54 ? 65  LEU   C N   1 
ATOM   3083  C  CA  . LEU   C  1 65  ? -36.931 -63.125  -14.251 1.00 31.94 ? 65  LEU   C CA  1 
ATOM   3084  C  C   . LEU   C  1 65  ? -38.246 -63.911  -14.275 1.00 37.26 ? 65  LEU   C C   1 
ATOM   3085  O  O   . LEU   C  1 65  ? -38.923 -64.015  -13.241 1.00 28.75 ? 65  LEU   C O   1 
ATOM   3086  C  CB  . LEU   C  1 65  ? -37.144 -61.746  -13.607 1.00 28.35 ? 65  LEU   C CB  1 
ATOM   3087  C  CG  . LEU   C  1 65  ? -35.846 -60.967  -13.366 1.00 31.21 ? 65  LEU   C CG  1 
ATOM   3088  C  CD1 . LEU   C  1 65  ? -36.115 -59.606  -12.772 1.00 31.81 ? 65  LEU   C CD1 1 
ATOM   3089  C  CD2 . LEU   C  1 65  ? -34.912 -61.746  -12.465 1.00 26.73 ? 65  LEU   C CD2 1 
ATOM   3090  N  N   . GLU   C  1 66  ? -38.605 -64.449  -15.443 1.00 32.65 ? 66  GLU   C N   1 
ATOM   3091  C  CA  . GLU   C  1 66  ? -39.752 -65.328  -15.614 1.00 36.98 ? 66  GLU   C CA  1 
ATOM   3092  C  C   . GLU   C  1 66  ? -41.064 -64.585  -15.431 1.00 39.58 ? 66  GLU   C C   1 
ATOM   3093  O  O   . GLU   C  1 66  ? -42.075 -65.168  -15.044 1.00 37.16 ? 66  GLU   C O   1 
ATOM   3094  C  CB  . GLU   C  1 66  ? -39.636 -66.541  -14.683 1.00 34.67 ? 66  GLU   C CB  1 
ATOM   3095  C  CG  . GLU   C  1 66  ? -38.439 -67.369  -15.079 1.00 34.86 ? 66  GLU   C CG  1 
ATOM   3096  C  CD  . GLU   C  1 66  ? -38.229 -68.598  -14.239 1.00 39.54 ? 66  GLU   C CD  1 
ATOM   3097  O  OE1 . GLU   C  1 66  ? -39.228 -69.168  -13.772 1.00 47.53 ? 66  GLU   C OE1 1 
ATOM   3098  O  OE2 . GLU   C  1 66  ? -37.061 -69.001  -14.053 1.00 39.08 ? 66  GLU   C OE2 1 
ATOM   3099  N  N   . GLY   C  1 67  ? -41.049 -63.283  -15.707 1.00 32.59 ? 67  GLY   C N   1 
ATOM   3100  C  CA  . GLY   C  1 67  ? -42.254 -62.495  -15.786 1.00 28.27 ? 67  GLY   C CA  1 
ATOM   3101  C  C   . GLY   C  1 67  ? -42.730 -62.368  -17.225 1.00 34.54 ? 67  GLY   C C   1 
ATOM   3102  O  O   . GLY   C  1 67  ? -42.077 -62.803  -18.178 1.00 34.78 ? 67  GLY   C O   1 
ATOM   3103  N  N   . LEU   C  1 68  ? -43.879 -61.728  -17.359 1.00 29.73 ? 68  LEU   C N   1 
ATOM   3104  C  CA  . LEU   C  1 68  ? -44.513 -61.476  -18.645 1.00 33.27 ? 68  LEU   C CA  1 
ATOM   3105  C  C   . LEU   C  1 68  ? -44.405 -59.996  -18.945 1.00 30.70 ? 68  LEU   C C   1 
ATOM   3106  O  O   . LEU   C  1 68  ? -45.078 -59.194  -18.281 1.00 29.21 ? 68  LEU   C O   1 
ATOM   3107  C  CB  . LEU   C  1 68  ? -45.991 -61.892  -18.630 1.00 39.29 ? 68  LEU   C CB  1 
ATOM   3108  C  CG  . LEU   C  1 68  ? -46.343 -63.369  -18.456 1.00 49.25 ? 68  LEU   C CG  1 
ATOM   3109  C  CD1 . LEU   C  1 68  ? -47.860 -63.557  -18.577 1.00 63.18 ? 68  LEU   C CD1 1 
ATOM   3110  C  CD2 . LEU   C  1 68  ? -45.619 -64.249  -19.466 1.00 53.58 ? 68  LEU   C CD2 1 
ATOM   3111  N  N   . PRO   C  1 69  ? -43.598 -59.577  -19.925 1.00 24.28 ? 69  PRO   C N   1 
ATOM   3112  C  CA  . PRO   C  1 69  ? -43.509 -58.151  -20.237 1.00 27.26 ? 69  PRO   C CA  1 
ATOM   3113  C  C   . PRO   C  1 69  ? -44.829 -57.663  -20.782 1.00 27.87 ? 69  PRO   C C   1 
ATOM   3114  O  O   . PRO   C  1 69  ? -45.459 -58.329  -21.601 1.00 33.16 ? 69  PRO   C O   1 
ATOM   3115  C  CB  . PRO   C  1 69  ? -42.400 -58.071  -21.307 1.00 36.15 ? 69  PRO   C CB  1 
ATOM   3116  C  CG  . PRO   C  1 69  ? -41.695 -59.386  -21.277 1.00 42.07 ? 69  PRO   C CG  1 
ATOM   3117  C  CD  . PRO   C  1 69  ? -42.699 -60.399  -20.754 1.00 39.05 ? 69  PRO   C CD  1 
ATOM   3118  N  N   . ASN   C  1 70  ? -45.238 -56.484  -20.343 1.00 33.11 ? 70  ASN   C N   1 
ATOM   3119  C  CA  . ASN   C  1 70  ? -46.524 -55.916  -20.741 1.00 34.00 ? 70  ASN   C CA  1 
ATOM   3120  C  C   . ASN   C  1 70  ? -46.302 -54.901  -21.853 1.00 26.98 ? 70  ASN   C C   1 
ATOM   3121  O  O   . ASN   C  1 70  ? -45.959 -53.748  -21.593 1.00 29.44 ? 70  ASN   C O   1 
ATOM   3122  C  CB  . ASN   C  1 70  ? -47.223 -55.272  -19.547 1.00 29.49 ? 70  ASN   C CB  1 
ATOM   3123  C  CG  . ASN   C  1 70  ? -48.641 -54.828  -19.874 1.00 34.78 ? 70  ASN   C CG  1 
ATOM   3124  O  OD1 . ASN   C  1 70  ? -49.019 -54.707  -21.037 1.00 32.11 ? 70  ASN   C OD1 1 
ATOM   3125  N  ND2 . ASN   C  1 70  ? -49.432 -54.562  -18.833 1.00 29.15 ? 70  ASN   C ND2 1 
ATOM   3126  N  N   . LEU   C  1 71  ? -46.524 -55.329  -23.088 1.00 26.80 ? 71  LEU   C N   1 
ATOM   3127  C  CA  . LEU   C  1 71  ? -46.503 -54.446  -24.246 1.00 29.00 ? 71  LEU   C CA  1 
ATOM   3128  C  C   . LEU   C  1 71  ? -47.904 -54.139  -24.773 1.00 34.35 ? 71  LEU   C C   1 
ATOM   3129  O  O   . LEU   C  1 71  ? -48.040 -53.590  -25.880 1.00 32.42 ? 71  LEU   C O   1 
ATOM   3130  C  CB  . LEU   C  1 71  ? -45.635 -55.070  -25.352 1.00 30.23 ? 71  LEU   C CB  1 
ATOM   3131  C  CG  . LEU   C  1 71  ? -44.115 -55.050  -25.147 1.00 30.63 ? 71  LEU   C CG  1 
ATOM   3132  C  CD1 . LEU   C  1 71  ? -43.697 -56.041  -24.129 1.00 32.29 ? 71  LEU   C CD1 1 
ATOM   3133  C  CD2 . LEU   C  1 71  ? -43.372 -55.345  -26.446 1.00 31.29 ? 71  LEU   C CD2 1 
ATOM   3134  N  N   . GLN   C  1 72  ? -48.941 -54.455  -23.995 1.00 36.77 ? 72  GLN   C N   1 
ATOM   3135  C  CA  . GLN   C  1 72  ? -50.344 -54.279  -24.375 1.00 34.45 ? 72  GLN   C CA  1 
ATOM   3136  C  C   . GLN   C  1 72  ? -50.939 -52.969  -23.879 1.00 30.31 ? 72  GLN   C C   1 
ATOM   3137  O  O   . GLN   C  1 72  ? -51.726 -52.334  -24.588 1.00 31.51 ? 72  GLN   C O   1 
ATOM   3138  C  CB  . GLN   C  1 72  ? -51.194 -55.435  -23.820 1.00 33.92 ? 72  GLN   C CB  1 
ATOM   3139  C  CG  . GLN   C  1 72  ? -52.689 -55.353  -24.207 1.00 31.76 ? 72  GLN   C CG  1 
ATOM   3140  C  CD  . GLN   C  1 72  ? -52.896 -55.560  -25.679 1.00 24.28 ? 72  GLN   C CD  1 
ATOM   3141  O  OE1 . GLN   C  1 72  ? -52.873 -56.689  -26.162 1.00 36.23 ? 72  GLN   C OE1 1 
ATOM   3142  N  NE2 . GLN   C  1 72  ? -53.012 -54.475  -26.415 1.00 30.30 ? 72  GLN   C NE2 1 
ATOM   3143  N  N   . ASP   C  1 73  ? -50.572 -52.535  -22.686 1.00 30.25 ? 73  ASP   C N   1 
ATOM   3144  C  CA  . ASP   C  1 73  ? -51.179 -51.370  -22.069 1.00 29.86 ? 73  ASP   C CA  1 
ATOM   3145  C  C   . ASP   C  1 73  ? -50.351 -50.127  -22.370 1.00 41.52 ? 73  ASP   C C   1 
ATOM   3146  O  O   . ASP   C  1 73  ? -49.165 -50.050  -22.015 1.00 47.18 ? 73  ASP   C O   1 
ATOM   3147  C  CB  . ASP   C  1 73  ? -51.319 -51.581  -20.559 1.00 36.53 ? 73  ASP   C CB  1 
ATOM   3148  C  CG  . ASP   C  1 73  ? -52.216 -52.762  -20.213 1.00 38.15 ? 73  ASP   C CG  1 
ATOM   3149  O  OD1 . ASP   C  1 73  ? -53.090 -53.115  -21.030 1.00 39.52 ? 73  ASP   C OD1 1 
ATOM   3150  O  OD2 . ASP   C  1 73  ? -52.038 -53.351  -19.134 1.00 41.82 ? 73  ASP   C OD2 1 
ATOM   3151  N  N   . LEU   C  1 74  ? -50.988 -49.149  -22.996 1.00 37.13 ? 74  LEU   C N   1 
ATOM   3152  C  CA  . LEU   C  1 74  ? -50.346 -47.924  -23.441 1.00 35.14 ? 74  LEU   C CA  1 
ATOM   3153  C  C   . LEU   C  1 74  ? -51.044 -46.753  -22.762 1.00 41.26 ? 74  LEU   C C   1 
ATOM   3154  O  O   . LEU   C  1 74  ? -52.203 -46.467  -23.066 1.00 33.93 ? 74  LEU   C O   1 
ATOM   3155  C  CB  . LEU   C  1 74  ? -50.421 -47.805  -24.975 1.00 30.24 ? 74  LEU   C CB  1 
ATOM   3156  C  CG  . LEU   C  1 74  ? -49.712 -46.569  -25.536 1.00 37.08 ? 74  LEU   C CG  1 
ATOM   3157  C  CD1 . LEU   C  1 74  ? -48.227 -46.620  -25.169 1.00 33.88 ? 74  LEU   C CD1 1 
ATOM   3158  C  CD2 . LEU   C  1 74  ? -49.871 -46.479  -27.020 1.00 29.86 ? 74  LEU   C CD2 1 
ATOM   3159  N  N   . GLY   C  1 75  ? -50.332 -46.069  -21.863 1.00 31.34 ? 75  GLY   C N   1 
ATOM   3160  C  CA  . GLY   C  1 75  ? -50.838 -44.880  -21.204 1.00 31.27 ? 75  GLY   C CA  1 
ATOM   3161  C  C   . GLY   C  1 75  ? -51.046 -43.700  -22.140 1.00 32.40 ? 75  GLY   C C   1 
ATOM   3162  O  O   . GLY   C  1 75  ? -50.834 -43.763  -23.350 1.00 33.46 ? 75  GLY   C O   1 
ATOM   3163  N  N   . LYS   C  1 76  ? -51.428 -42.578  -21.534 1.00 30.18 ? 76  LYS   C N   1 
ATOM   3164  C  CA  . LYS   C  1 76  ? -51.744 -41.357  -22.264 1.00 37.52 ? 76  LYS   C CA  1 
ATOM   3165  C  C   . LYS   C  1 76  ? -50.482 -40.690  -22.816 1.00 32.69 ? 76  LYS   C C   1 
ATOM   3166  O  O   . LYS   C  1 76  ? -49.567 -40.338  -22.054 1.00 33.19 ? 76  LYS   C O   1 
ATOM   3167  C  CB  . LYS   C  1 76  ? -52.460 -40.393  -21.335 1.00 31.06 ? 76  LYS   C CB  1 
ATOM   3168  C  CG  . LYS   C  1 76  ? -52.933 -39.121  -22.019 1.00 40.11 ? 76  LYS   C CG  1 
ATOM   3169  N  N   . LEU   C  1 77  ? -50.444 -40.479  -24.131 1.00 33.40 ? 77  LEU   C N   1 
ATOM   3170  C  CA  . LEU   C  1 77  ? -49.398 -39.655  -24.732 1.00 29.68 ? 77  LEU   C CA  1 
ATOM   3171  C  C   . LEU   C  1 77  ? -49.682 -38.182  -24.473 1.00 34.44 ? 77  LEU   C C   1 
ATOM   3172  O  O   . LEU   C  1 77  ? -50.832 -37.745  -24.505 1.00 34.53 ? 77  LEU   C O   1 
ATOM   3173  C  CB  . LEU   C  1 77  ? -49.315 -39.883  -26.244 1.00 30.17 ? 77  LEU   C CB  1 
ATOM   3174  C  CG  . LEU   C  1 77  ? -49.333 -41.307  -26.751 1.00 31.82 ? 77  LEU   C CG  1 
ATOM   3175  C  CD1 . LEU   C  1 77  ? -49.032 -41.309  -28.268 1.00 33.62 ? 77  LEU   C CD1 1 
ATOM   3176  C  CD2 . LEU   C  1 77  ? -48.358 -42.118  -26.025 1.00 36.01 ? 77  LEU   C CD2 1 
ATOM   3177  N  N   . LEU   C  1 78  ? -48.635 -37.412  -24.239 1.00 31.72 ? 78  LEU   C N   1 
ATOM   3178  C  CA  . LEU   C  1 78  ? -48.747 -35.962  -24.072 1.00 34.41 ? 78  LEU   C CA  1 
ATOM   3179  C  C   . LEU   C  1 78  ? -48.183 -35.304  -25.331 1.00 40.17 ? 78  LEU   C C   1 
ATOM   3180  O  O   . LEU   C  1 78  ? -46.958 -35.212  -25.494 1.00 31.31 ? 78  LEU   C O   1 
ATOM   3181  C  CB  . LEU   C  1 78  ? -48.000 -35.509  -22.817 1.00 35.83 ? 78  LEU   C CB  1 
ATOM   3182  C  CG  . LEU   C  1 78  ? -48.312 -36.264  -21.522 1.00 42.39 ? 78  LEU   C CG  1 
ATOM   3183  C  CD1 . LEU   C  1 78  ? -47.452 -35.712  -20.351 1.00 37.31 ? 78  LEU   C CD1 1 
ATOM   3184  C  CD2 . LEU   C  1 78  ? -49.815 -36.189  -21.207 1.00 36.29 ? 78  LEU   C CD2 1 
ATOM   3185  N  N   . ILE   C  1 79  ? -49.072 -34.842  -26.222 1.00 33.87 ? 79  ILE   C N   1 
ATOM   3186  C  CA  . ILE   C  1 79  ? -48.672 -34.252  -27.501 1.00 32.21 ? 79  ILE   C CA  1 
ATOM   3187  C  C   . ILE   C  1 79  ? -48.896 -32.756  -27.436 1.00 40.67 ? 79  ILE   C C   1 
ATOM   3188  O  O   . ILE   C  1 79  ? -50.032 -32.304  -27.263 1.00 41.34 ? 79  ILE   C O   1 
ATOM   3189  C  CB  . ILE   C  1 79  ? -49.469 -34.842  -28.669 1.00 35.65 ? 79  ILE   C CB  1 
ATOM   3190  C  CG1 . ILE   C  1 79  ? -49.430 -36.362  -28.607 1.00 35.48 ? 79  ILE   C CG1 1 
ATOM   3191  C  CG2 . ILE   C  1 79  ? -48.925 -34.318  -30.011 1.00 41.42 ? 79  ILE   C CG2 1 
ATOM   3192  C  CD1 . ILE   C  1 79  ? -48.020 -36.933  -28.596 1.00 39.32 ? 79  ILE   C CD1 1 
ATOM   3193  N  N   . GLY   C  1 80  ? -47.841 -31.982  -27.601 1.00 32.10 ? 80  GLY   C N   1 
ATOM   3194  C  CA  . GLY   C  1 80  ? -48.020 -30.542  -27.693 1.00 35.76 ? 80  GLY   C CA  1 
ATOM   3195  C  C   . GLY   C  1 80  ? -48.621 -30.105  -29.031 1.00 37.27 ? 80  GLY   C C   1 
ATOM   3196  O  O   . GLY   C  1 80  ? -48.718 -30.868  -29.997 1.00 39.25 ? 80  GLY   C O   1 
ATOM   3197  N  N   . GLU   C  1 81  ? -49.029 -28.834  -29.084 1.00 34.74 ? 81  GLU   C N   1 
ATOM   3198  C  CA  . GLU   C  1 81  ? -49.499 -28.206  -30.323 1.00 46.36 ? 81  GLU   C CA  1 
ATOM   3199  C  C   . GLU   C  1 81  ? -48.531 -27.159  -30.870 1.00 40.23 ? 81  GLU   C C   1 
ATOM   3200  O  O   . GLU   C  1 81  ? -48.765 -26.608  -31.954 1.00 35.67 ? 81  GLU   C O   1 
ATOM   3201  C  CB  . GLU   C  1 81  ? -50.876 -27.568  -30.101 1.00 38.38 ? 81  GLU   C CB  1 
ATOM   3202  C  CG  . GLU   C  1 81  ? -51.948 -28.589  -29.718 1.00 56.74 ? 81  GLU   C CG  1 
ATOM   3203  C  CD  . GLU   C  1 81  ? -53.197 -27.973  -29.100 1.00 62.97 ? 81  GLU   C CD  1 
ATOM   3204  O  OE1 . GLU   C  1 81  ? -53.429 -26.752  -29.261 1.00 50.17 ? 81  GLU   C OE1 1 
ATOM   3205  O  OE2 . GLU   C  1 81  ? -53.947 -28.727  -28.449 1.00 68.70 ? 81  GLU   C OE2 1 
ATOM   3206  N  N   . ASN   C  1 82  ? -47.446 -26.878  -30.165 1.00 30.40 ? 82  ASN   C N   1 
ATOM   3207  C  CA  . ASN   C  1 82  ? -46.379 -26.033  -30.685 1.00 31.93 ? 82  ASN   C CA  1 
ATOM   3208  C  C   . ASN   C  1 82  ? -45.094 -26.444  -29.982 1.00 34.47 ? 82  ASN   C C   1 
ATOM   3209  O  O   . ASN   C  1 82  ? -45.109 -27.285  -29.075 1.00 27.98 ? 82  ASN   C O   1 
ATOM   3210  C  CB  . ASN   C  1 82  ? -46.690 -24.549  -30.493 1.00 29.71 ? 82  ASN   C CB  1 
ATOM   3211  C  CG  . ASN   C  1 82  ? -46.948 -24.191  -29.055 1.00 39.53 ? 82  ASN   C CG  1 
ATOM   3212  O  OD1 . ASN   C  1 82  ? -46.262 -24.650  -28.146 1.00 37.72 ? 82  ASN   C OD1 1 
ATOM   3213  N  ND2 . ASN   C  1 82  ? -47.953 -23.365  -28.833 1.00 48.59 ? 82  ASN   C ND2 1 
ATOM   3214  N  N   . THR   C  1 83  ? -43.979 -25.829  -30.397 1.00 29.75 ? 83  THR   C N   1 
ATOM   3215  C  CA  . THR   C  1 83  ? -42.663 -26.336  -29.981 1.00 31.63 ? 83  THR   C CA  1 
ATOM   3216  C  C   . THR   C  1 83  ? -42.492 -26.252  -28.466 1.00 26.18 ? 83  THR   C C   1 
ATOM   3217  O  O   . THR   C  1 83  ? -42.048 -27.217  -27.827 1.00 30.32 ? 83  THR   C O   1 
ATOM   3218  C  CB  . THR   C  1 83  ? -41.550 -25.579  -30.717 1.00 28.93 ? 83  THR   C CB  1 
ATOM   3219  O  OG1 . THR   C  1 83  ? -41.522 -25.996  -32.093 1.00 31.91 ? 83  THR   C OG1 1 
ATOM   3220  C  CG2 . THR   C  1 83  ? -40.166 -25.844  -30.087 1.00 27.42 ? 83  THR   C CG2 1 
ATOM   3221  N  N   . GLN   C  1 84  ? -42.852 -25.116  -27.863 1.00 30.77 ? 84  GLN   C N   1 
ATOM   3222  C  CA  . GLN   C  1 84  ? -42.784 -25.008  -26.405 1.00 27.11 ? 84  GLN   C CA  1 
ATOM   3223  C  C   . GLN   C  1 84  ? -43.591 -26.102  -25.718 1.00 34.70 ? 84  GLN   C C   1 
ATOM   3224  O  O   . GLN   C  1 84  ? -43.107 -26.751  -24.781 1.00 30.15 ? 84  GLN   C O   1 
ATOM   3225  C  CB  . GLN   C  1 84  ? -43.281 -23.651  -25.934 1.00 36.49 ? 84  GLN   C CB  1 
ATOM   3226  C  CG  . GLN   C  1 84  ? -42.308 -22.543  -26.064 1.00 50.22 ? 84  GLN   C CG  1 
ATOM   3227  C  CD  . GLN   C  1 84  ? -42.649 -21.402  -25.138 1.00 59.95 ? 84  GLN   C CD  1 
ATOM   3228  O  OE1 . GLN   C  1 84  ? -43.133 -20.359  -25.582 1.00 72.45 ? 84  GLN   C OE1 1 
ATOM   3229  N  NE2 . GLN   C  1 84  ? -42.410 -21.593  -23.841 1.00 44.58 ? 84  GLN   C NE2 1 
ATOM   3230  N  N   . GLU   C  1 85  ? -44.844 -26.297  -26.138 1.00 27.27 ? 85  GLU   C N   1 
ATOM   3231  C  CA  . GLU   C  1 85  ? -45.690 -27.258  -25.438 1.00 31.48 ? 85  GLU   C CA  1 
ATOM   3232  C  C   . GLU   C  1 85  ? -45.161 -28.669  -25.596 1.00 25.40 ? 85  GLU   C C   1 
ATOM   3233  O  O   . GLU   C  1 85  ? -45.266 -29.487  -24.676 1.00 28.14 ? 85  GLU   C O   1 
ATOM   3234  C  CB  . GLU   C  1 85  ? -47.131 -27.197  -25.960 1.00 29.90 ? 85  GLU   C CB  1 
ATOM   3235  C  CG  . GLU   C  1 85  ? -47.826 -25.917  -25.634 1.00 48.66 ? 85  GLU   C CG  1 
ATOM   3236  C  CD  . GLU   C  1 85  ? -49.248 -25.851  -26.184 1.00 50.84 ? 85  GLU   C CD  1 
ATOM   3237  O  OE1 . GLU   C  1 85  ? -49.752 -26.857  -26.770 1.00 33.63 ? 85  GLU   C OE1 1 
ATOM   3238  O  OE2 . GLU   C  1 85  ? -49.841 -24.767  -26.018 1.00 48.00 ? 85  GLU   C OE2 1 
ATOM   3239  N  N   . MET   C  1 86  ? -44.659 -28.991  -26.788 1.00 25.79 ? 86  MET   C N   1 
ATOM   3240  C  CA  . MET   C  1 86  ? -44.091 -30.311  -27.029 1.00 28.48 ? 86  MET   C CA  1 
ATOM   3241  C  C   . MET   C  1 86  ? -42.908 -30.571  -26.089 1.00 26.22 ? 86  MET   C C   1 
ATOM   3242  O  O   . MET   C  1 86  ? -42.789 -31.654  -25.495 1.00 27.50 ? 86  MET   C O   1 
ATOM   3243  C  CB  . MET   C  1 86  ? -43.657 -30.403  -28.497 1.00 24.10 ? 86  MET   C CB  1 
ATOM   3244  C  CG  . MET   C  1 86  ? -44.802 -30.305  -29.498 1.00 29.45 ? 86  MET   C CG  1 
ATOM   3245  S  SD  . MET   C  1 86  ? -44.278 -29.718  -31.137 1.00 29.28 ? 86  MET   C SD  1 
ATOM   3246  C  CE  . MET   C  1 86  ? -43.610 -31.269  -31.780 1.00 29.17 ? 86  MET   C CE  1 
ATOM   3247  N  N   . LEU   C  1 87  ? -42.023 -29.586  -25.955 1.00 25.73 ? 87  LEU   C N   1 
ATOM   3248  C  CA  . LEU   C  1 87  ? -40.904 -29.720  -25.032 1.00 31.64 ? 87  LEU   C CA  1 
ATOM   3249  C  C   . LEU   C  1 87  ? -41.402 -29.843  -23.600 1.00 35.87 ? 87  LEU   C C   1 
ATOM   3250  O  O   . LEU   C  1 87  ? -40.886 -30.654  -22.825 1.00 25.63 ? 87  LEU   C O   1 
ATOM   3251  C  CB  . LEU   C  1 87  ? -39.958 -28.524  -25.166 1.00 23.87 ? 87  LEU   C CB  1 
ATOM   3252  C  CG  . LEU   C  1 87  ? -39.146 -28.471  -26.479 1.00 21.11 ? 87  LEU   C CG  1 
ATOM   3253  C  CD1 . LEU   C  1 87  ? -38.556 -27.101  -26.645 1.00 29.83 ? 87  LEU   C CD1 1 
ATOM   3254  C  CD2 . LEU   C  1 87  ? -38.044 -29.520  -26.496 1.00 26.34 ? 87  LEU   C CD2 1 
ATOM   3255  N  N   . GLN   C  1 88  ? -42.406 -29.051  -23.221 1.00 30.18 ? 88  GLN   C N   1 
ATOM   3256  C  CA  . GLN   C  1 88  ? -42.900 -29.172  -21.847 1.00 24.02 ? 88  GLN   C CA  1 
ATOM   3257  C  C   . GLN   C  1 88  ? -43.588 -30.513  -21.633 1.00 27.89 ? 88  GLN   C C   1 
ATOM   3258  O  O   . GLN   C  1 88  ? -43.495 -31.101  -20.543 1.00 31.69 ? 88  GLN   C O   1 
ATOM   3259  C  CB  . GLN   C  1 88  ? -43.830 -28.006  -21.491 1.00 28.57 ? 88  GLN   C CB  1 
ATOM   3260  C  CG  . GLN   C  1 88  ? -44.373 -28.046  -20.024 1.00 44.28 ? 88  GLN   C CG  1 
ATOM   3261  C  CD  . GLN   C  1 88  ? -43.302 -27.848  -18.944 1.00 47.45 ? 88  GLN   C CD  1 
ATOM   3262  O  OE1 . GLN   C  1 88  ? -42.587 -26.846  -18.945 1.00 48.84 ? 88  GLN   C OE1 1 
ATOM   3263  N  NE2 . GLN   C  1 88  ? -43.202 -28.806  -18.008 1.00 43.17 ? 88  GLN   C NE2 1 
ATOM   3264  N  N   . CYS   C  1 89  ? -44.279 -31.022  -22.656 1.00 27.18 ? 89  CYS   C N   1 
ATOM   3265  C  CA  . CYS   C  1 89  ? -44.892 -32.339  -22.542 1.00 29.51 ? 89  CYS   C CA  1 
ATOM   3266  C  C   . CYS   C  1 89  ? -43.851 -33.423  -22.322 1.00 32.38 ? 89  CYS   C C   1 
ATOM   3267  O  O   . CYS   C  1 89  ? -44.060 -34.332  -21.508 1.00 26.51 ? 89  CYS   C O   1 
ATOM   3268  C  CB  . CYS   C  1 89  ? -45.698 -32.674  -23.794 1.00 29.06 ? 89  CYS   C CB  1 
ATOM   3269  S  SG  . CYS   C  1 89  ? -47.364 -31.893  -23.885 1.00 32.67 ? 89  CYS   C SG  1 
ATOM   3270  N  N   . ASP   C  1 90  ? -42.770 -33.407  -23.123 1.00 24.65 ? 90  ASP   C N   1 
ATOM   3271  C  CA  . ASP   C  1 90  ? -41.677 -34.353  -22.915 1.00 26.24 ? 90  ASP   C CA  1 
ATOM   3272  C  C   . ASP   C  1 90  ? -41.156 -34.256  -21.488 1.00 23.59 ? 90  ASP   C C   1 
ATOM   3273  O  O   . ASP   C  1 90  ? -40.919 -35.268  -20.826 1.00 26.15 ? 90  ASP   C O   1 
ATOM   3274  C  CB  . ASP   C  1 90  ? -40.513 -34.096  -23.887 1.00 27.72 ? 90  ASP   C CB  1 
ATOM   3275  C  CG  . ASP   C  1 90  ? -40.816 -34.511  -25.341 1.00 32.01 ? 90  ASP   C CG  1 
ATOM   3276  O  OD1 . ASP   C  1 90  ? -41.914 -35.036  -25.622 1.00 28.35 ? 90  ASP   C OD1 1 
ATOM   3277  O  OD2 . ASP   C  1 90  ? -39.929 -34.325  -26.222 1.00 27.21 ? 90  ASP   C OD2 1 
ATOM   3278  N  N   . LEU   C  1 91  ? -40.943 -33.036  -21.011 1.00 24.12 ? 91  LEU   C N   1 
ATOM   3279  C  CA  . LEU   C  1 91  ? -40.367 -32.863  -19.686 1.00 26.66 ? 91  LEU   C CA  1 
ATOM   3280  C  C   . LEU   C  1 91  ? -41.297 -33.414  -18.611 1.00 30.70 ? 91  LEU   C C   1 
ATOM   3281  O  O   . LEU   C  1 91  ? -40.844 -34.046  -17.649 1.00 26.96 ? 91  LEU   C O   1 
ATOM   3282  C  CB  . LEU   C  1 91  ? -40.076 -31.385  -19.445 1.00 25.13 ? 91  LEU   C CB  1 
ATOM   3283  C  CG  . LEU   C  1 91  ? -39.505 -31.039  -18.063 1.00 33.15 ? 91  LEU   C CG  1 
ATOM   3284  C  CD1 . LEU   C  1 91  ? -38.244 -31.846  -17.740 1.00 28.35 ? 91  LEU   C CD1 1 
ATOM   3285  C  CD2 . LEU   C  1 91  ? -39.216 -29.592  -18.057 1.00 29.44 ? 91  LEU   C CD2 1 
ATOM   3286  N  N   . ASN   C  1 92  ? -42.608 -33.204  -18.775 1.00 28.40 ? 92  ASN   C N   1 
ATOM   3287  C  CA  . ASN   C  1 92  ? -43.589 -33.740  -17.832 1.00 32.30 ? 92  ASN   C CA  1 
ATOM   3288  C  C   . ASN   C  1 92  ? -43.539 -35.269  -17.782 1.00 28.24 ? 92  ASN   C C   1 
ATOM   3289  O  O   . ASN   C  1 92  ? -43.512 -35.865  -16.703 1.00 26.05 ? 92  ASN   C O   1 
ATOM   3290  C  CB  . ASN   C  1 92  ? -44.997 -33.241  -18.216 1.00 30.56 ? 92  ASN   C CB  1 
ATOM   3291  C  CG  . ASN   C  1 92  ? -45.182 -31.730  -17.963 1.00 35.66 ? 92  ASN   C CG  1 
ATOM   3292  O  OD1 . ASN   C  1 92  ? -44.370 -31.097  -17.288 1.00 41.85 ? 92  ASN   C OD1 1 
ATOM   3293  N  ND2 . ASN   C  1 92  ? -46.271 -31.166  -18.471 1.00 47.26 ? 92  ASN   C ND2 1 
ATOM   3294  N  N   . LEU   C  1 93  ? -43.502 -35.920  -18.942 1.00 23.86 ? 93  LEU   C N   1 
ATOM   3295  C  CA  . LEU   C  1 93  ? -43.320 -37.368  -18.989 1.00 32.30 ? 93  LEU   C CA  1 
ATOM   3296  C  C   . LEU   C  1 93  ? -42.021 -37.790  -18.306 1.00 31.30 ? 93  LEU   C C   1 
ATOM   3297  O  O   . LEU   C  1 93  ? -42.000 -38.742  -17.511 1.00 26.17 ? 93  LEU   C O   1 
ATOM   3298  C  CB  . LEU   C  1 93  ? -43.340 -37.824  -20.445 1.00 24.30 ? 93  LEU   C CB  1 
ATOM   3299  C  CG  . LEU   C  1 93  ? -43.297 -39.326  -20.691 1.00 29.03 ? 93  LEU   C CG  1 
ATOM   3300  C  CD1 . LEU   C  1 93  ? -44.495 -40.049  -20.030 1.00 32.74 ? 93  LEU   C CD1 1 
ATOM   3301  C  CD2 . LEU   C  1 93  ? -43.255 -39.612  -22.198 1.00 27.77 ? 93  LEU   C CD2 1 
ATOM   3302  N  N   . GLU   C  1 94  ? -40.916 -37.085  -18.594 1.00 32.30 ? 94  GLU   C N   1 
ATOM   3303  C  CA  . GLU   C  1 94  ? -39.621 -37.473  -18.011 1.00 29.43 ? 94  GLU   C CA  1 
ATOM   3304  C  C   . GLU   C  1 94  ? -39.642 -37.373  -16.481 1.00 26.75 ? 94  GLU   C C   1 
ATOM   3305  O  O   . GLU   C  1 94  ? -39.128 -38.253  -15.791 1.00 30.64 ? 94  GLU   C O   1 
ATOM   3306  C  CB  . GLU   C  1 94  ? -38.501 -36.607  -18.589 1.00 29.79 ? 94  GLU   C CB  1 
ATOM   3307  C  CG  . GLU   C  1 94  ? -38.147 -36.928  -20.051 1.00 27.22 ? 94  GLU   C CG  1 
ATOM   3308  C  CD  . GLU   C  1 94  ? -37.371 -38.229  -20.179 1.00 34.34 ? 94  GLU   C CD  1 
ATOM   3309  O  OE1 . GLU   C  1 94  ? -37.023 -38.819  -19.156 1.00 32.71 ? 94  GLU   C OE1 1 
ATOM   3310  O  OE2 . GLU   C  1 94  ? -37.103 -38.676  -21.305 1.00 40.05 ? 94  GLU   C OE2 1 
ATOM   3311  N  N   . LEU   C  1 95  ? -40.255 -36.322  -15.932 1.00 29.93 ? 95  LEU   C N   1 
ATOM   3312  C  CA  . LEU   C  1 95  ? -40.355 -36.189  -14.473 1.00 28.40 ? 95  LEU   C CA  1 
ATOM   3313  C  C   . LEU   C  1 95  ? -41.192 -37.300  -13.856 1.00 29.01 ? 95  LEU   C C   1 
ATOM   3314  O  O   . LEU   C  1 95  ? -40.861 -37.802  -12.775 1.00 31.27 ? 95  LEU   C O   1 
ATOM   3315  C  CB  . LEU   C  1 95  ? -40.935 -34.831  -14.103 1.00 29.64 ? 95  LEU   C CB  1 
ATOM   3316  C  CG  . LEU   C  1 95  ? -39.972 -33.702  -14.519 1.00 25.18 ? 95  LEU   C CG  1 
ATOM   3317  C  CD1 . LEU   C  1 95  ? -40.613 -32.323  -14.344 1.00 33.51 ? 95  LEU   C CD1 1 
ATOM   3318  C  CD2 . LEU   C  1 95  ? -38.630 -33.779  -13.752 1.00 36.47 ? 95  LEU   C CD2 1 
ATOM   3319  N  N   . LYS   C  1 96  ? -42.261 -37.728  -14.541 1.00 29.52 ? 96  LYS   C N   1 
ATOM   3320  C  CA  . LYS   C  1 96  ? -42.998 -38.902  -14.084 1.00 27.56 ? 96  LYS   C CA  1 
ATOM   3321  C  C   . LYS   C  1 96  ? -42.157 -40.161  -14.191 1.00 32.81 ? 96  LYS   C C   1 
ATOM   3322  O  O   . LYS   C  1 96  ? -42.163 -41.005  -13.281 1.00 27.44 ? 96  LYS   C O   1 
ATOM   3323  C  CB  . LYS   C  1 96  ? -44.296 -39.080  -14.879 1.00 33.76 ? 96  LYS   C CB  1 
ATOM   3324  C  CG  . LYS   C  1 96  ? -45.029 -40.388  -14.536 1.00 34.73 ? 96  LYS   C CG  1 
ATOM   3325  N  N   . ALA   C  1 97  ? -41.396 -40.296  -15.279 1.00 29.73 ? 97  ALA   C N   1 
ATOM   3326  C  CA  . ALA   C  1 97  ? -40.613 -41.512  -15.450 1.00 33.03 ? 97  ALA   C CA  1 
ATOM   3327  C  C   . ALA   C  1 97  ? -39.520 -41.621  -14.392 1.00 22.30 ? 97  ALA   C C   1 
ATOM   3328  O  O   . ALA   C  1 97  ? -39.237 -42.717  -13.893 1.00 27.64 ? 97  ALA   C O   1 
ATOM   3329  C  CB  . ALA   C  1 97  ? -40.011 -41.566  -16.864 1.00 31.25 ? 97  ALA   C CB  1 
ATOM   3330  N  N   . THR   C  1 98  ? -38.888 -40.514  -14.036 1.00 22.72 ? 98  THR   C N   1 
ATOM   3331  C  CA  . THR   C  1 98  ? -37.778 -40.630  -13.094 1.00 25.57 ? 98  THR   C CA  1 
ATOM   3332  C  C   . THR   C  1 98  ? -38.272 -40.845  -11.669 1.00 26.74 ? 98  THR   C C   1 
ATOM   3333  O  O   . THR   C  1 98  ? -37.576 -41.465  -10.854 1.00 24.72 ? 98  THR   C O   1 
ATOM   3334  C  CB  . THR   C  1 98  ? -36.886 -39.395  -13.151 1.00 22.84 ? 98  THR   C CB  1 
ATOM   3335  O  OG1 . THR   C  1 98  ? -37.662 -38.222  -12.945 1.00 28.50 ? 98  THR   C OG1 1 
ATOM   3336  C  CG2 . THR   C  1 98  ? -36.154 -39.305  -14.492 1.00 31.10 ? 98  THR   C CG2 1 
ATOM   3337  N  N   . LYS   C  1 99  ? -39.456 -40.311  -11.339 1.00 29.51 ? 99  LYS   C N   1 
ATOM   3338  C  CA  . LYS   C  1 99  ? -40.093 -40.678  -10.078 1.00 29.83 ? 99  LYS   C CA  1 
ATOM   3339  C  C   . LYS   C  1 99  ? -40.302 -42.186  -10.015 1.00 27.31 ? 99  LYS   C C   1 
ATOM   3340  O  O   . LYS   C  1 99  ? -39.925 -42.842  -9.042  1.00 25.48 ? 99  LYS   C O   1 
ATOM   3341  C  CB  . LYS   C  1 99  ? -41.423 -39.931  -9.939  1.00 27.32 ? 99  LYS   C CB  1 
ATOM   3342  C  CG  . LYS   C  1 99  ? -42.120 -40.186  -8.601  1.00 36.09 ? 99  LYS   C CG  1 
ATOM   3343  C  CD  . LYS   C  1 99  ? -43.393 -39.371  -8.505  1.00 40.57 ? 99  LYS   C CD  1 
ATOM   3344  N  N   . ASP   C  1 100 ? -40.845 -42.766  -11.081 1.00 27.43 ? 100 ASP   C N   1 
ATOM   3345  C  CA  . ASP   C  1 100 ? -41.104 -44.202  -11.061 1.00 29.89 ? 100 ASP   C CA  1 
ATOM   3346  C  C   . ASP   C  1 100 ? -39.813 -45.015  -11.018 1.00 29.16 ? 100 ASP   C C   1 
ATOM   3347  O  O   . ASP   C  1 100 ? -39.775 -46.089  -10.393 1.00 26.12 ? 100 ASP   C O   1 
ATOM   3348  C  CB  . ASP   C  1 100 ? -41.957 -44.610  -12.267 1.00 28.33 ? 100 ASP   C CB  1 
ATOM   3349  C  CG  . ASP   C  1 100 ? -43.394 -44.040  -12.190 1.00 32.89 ? 100 ASP   C CG  1 
ATOM   3350  O  OD1 . ASP   C  1 100 ? -43.821 -43.598  -11.108 1.00 33.31 ? 100 ASP   C OD1 1 
ATOM   3351  O  OD2 . ASP   C  1 100 ? -44.075 -44.031  -13.217 1.00 30.90 ? 100 ASP   C OD2 1 
ATOM   3352  N  N   . LEU   C  1 101 ? -38.755 -44.548  -11.707 1.00 29.11 ? 101 LEU   C N   1 
ATOM   3353  C  CA  . LEU   C  1 101 ? -37.462 -45.232  -11.641 1.00 23.56 ? 101 LEU   C CA  1 
ATOM   3354  C  C   . LEU   C  1 101 ? -36.906 -45.262  -10.213 1.00 23.07 ? 101 LEU   C C   1 
ATOM   3355  O  O   . LEU   C  1 101 ? -36.403 -46.295  -9.759  1.00 25.03 ? 101 LEU   C O   1 
ATOM   3356  C  CB  . LEU   C  1 101 ? -36.476 -44.557  -12.598 1.00 23.60 ? 101 LEU   C CB  1 
ATOM   3357  C  CG  . LEU   C  1 101 ? -36.702 -44.928  -14.063 1.00 25.29 ? 101 LEU   C CG  1 
ATOM   3358  C  CD1 . LEU   C  1 101 ? -36.066 -43.918  -15.008 1.00 29.36 ? 101 LEU   C CD1 1 
ATOM   3359  C  CD2 . LEU   C  1 101 ? -36.149 -46.335  -14.305 1.00 29.09 ? 101 LEU   C CD2 1 
ATOM   3360  N  N   . ARG   C  1 102 ? -36.960 -44.127  -9.512  1.00 22.95 ? 102 ARG   C N   1 
ATOM   3361  C  CA  . ARG   C  1 102 ? -36.471 -44.065  -8.138  1.00 28.24 ? 102 ARG   C CA  1 
ATOM   3362  C  C   . ARG   C  1 102 ? -37.226 -45.034  -7.234  1.00 28.14 ? 102 ARG   C C   1 
ATOM   3363  O  O   . ARG   C  1 102 ? -36.615 -45.741  -6.417  1.00 27.10 ? 102 ARG   C O   1 
ATOM   3364  C  CB  . ARG   C  1 102 ? -36.579 -42.630  -7.600  1.00 30.61 ? 102 ARG   C CB  1 
ATOM   3365  C  CG  . ARG   C  1 102 ? -35.604 -41.639  -8.251  1.00 24.51 ? 102 ARG   C CG  1 
ATOM   3366  C  CD  . ARG   C  1 102 ? -35.787 -40.170  -7.746  1.00 28.58 ? 102 ARG   C CD  1 
ATOM   3367  N  NE  . ARG   C  1 102 ? -35.502 -39.218  -8.818  1.00 32.11 ? 102 ARG   C NE  1 
ATOM   3368  C  CZ  . ARG   C  1 102 ? -34.306 -39.040  -9.373  1.00 28.88 ? 102 ARG   C CZ  1 
ATOM   3369  N  NH1 . ARG   C  1 102 ? -33.224 -39.664  -8.913  1.00 29.81 ? 102 ARG   C NH1 1 
ATOM   3370  N  NH2 . ARG   C  1 102 ? -34.189 -38.214  -10.409 1.00 28.53 ? 102 ARG   C NH2 1 
ATOM   3371  N  N   . GLU   C  1 103 ? -38.559 -45.096  -7.375  1.00 28.65 ? 103 GLU   C N   1 
ATOM   3372  C  CA  . GLU   C  1 103 ? -39.352 -46.029  -6.576  1.00 28.20 ? 103 GLU   C CA  1 
ATOM   3373  C  C   . GLU   C  1 103 ? -39.028 -47.470  -6.939  1.00 24.16 ? 103 GLU   C C   1 
ATOM   3374  O  O   . GLU   C  1 103 ? -38.889 -48.328  -6.051  1.00 26.89 ? 103 GLU   C O   1 
ATOM   3375  C  CB  . GLU   C  1 103 ? -40.858 -45.736  -6.763  1.00 26.49 ? 103 GLU   C CB  1 
ATOM   3376  C  CG  . GLU   C  1 103 ? -41.249 -44.340  -6.229  1.00 47.38 ? 103 GLU   C CG  1 
ATOM   3377  C  CD  . GLU   C  1 103 ? -42.712 -43.936  -6.527  1.00 72.81 ? 103 GLU   C CD  1 
ATOM   3378  O  OE1 . GLU   C  1 103 ? -43.382 -44.608  -7.349  1.00 61.52 ? 103 GLU   C OE1 1 
ATOM   3379  O  OE2 . GLU   C  1 103 ? -43.190 -42.933  -5.940  1.00 63.38 ? 103 GLU   C OE2 1 
ATOM   3380  N  N   . ALA   C  1 104 ? -38.819 -47.746  -8.228  1.00 26.97 ? 104 ALA   C N   1 
ATOM   3381  C  CA  . ALA   C  1 104 ? -38.447 -49.100  -8.621  1.00 27.74 ? 104 ALA   C CA  1 
ATOM   3382  C  C   . ALA   C  1 104 ? -37.074 -49.469  -8.056  1.00 27.71 ? 104 ALA   C C   1 
ATOM   3383  O  O   . ALA   C  1 104 ? -36.884 -50.577  -7.548  1.00 25.42 ? 104 ALA   C O   1 
ATOM   3384  C  CB  . ALA   C  1 104 ? -38.494 -49.225  -10.148 1.00 26.64 ? 104 ALA   C CB  1 
ATOM   3385  N  N   . ILE   C  1 105 ? -36.126 -48.532  -8.081  1.00 27.41 ? 105 ILE   C N   1 
ATOM   3386  C  CA  . ILE   C  1 105 ? -34.790 -48.810  -7.549  1.00 25.03 ? 105 ILE   C CA  1 
ATOM   3387  C  C   . ILE   C  1 105 ? -34.863 -49.137  -6.061  1.00 29.88 ? 105 ILE   C C   1 
ATOM   3388  O  O   . ILE   C  1 105 ? -34.240 -50.095  -5.596  1.00 26.06 ? 105 ILE   C O   1 
ATOM   3389  C  CB  . ILE   C  1 105 ? -33.838 -47.635  -7.831  1.00 25.31 ? 105 ILE   C CB  1 
ATOM   3390  C  CG1 . ILE   C  1 105 ? -33.470 -47.612  -9.343  1.00 22.29 ? 105 ILE   C CG1 1 
ATOM   3391  C  CG2 . ILE   C  1 105 ? -32.584 -47.806  -6.966  1.00 23.43 ? 105 ILE   C CG2 1 
ATOM   3392  C  CD1 . ILE   C  1 105 ? -32.834 -46.320  -9.839  1.00 28.28 ? 105 ILE   C CD1 1 
ATOM   3393  N  N   . VAL   C  1 106 ? -35.600 -48.329  -5.286  1.00 28.73 ? 106 VAL   C N   1 
ATOM   3394  C  CA  . VAL   C  1 106 ? -35.831 -48.655  -3.873  1.00 25.92 ? 106 VAL   C CA  1 
ATOM   3395  C  C   . VAL   C  1 106 ? -36.239 -50.115  -3.713  1.00 26.01 ? 106 VAL   C C   1 
ATOM   3396  O  O   . VAL   C  1 106 ? -35.679 -50.850  -2.896  1.00 27.06 ? 106 VAL   C O   1 
ATOM   3397  C  CB  . VAL   C  1 106 ? -36.900 -47.724  -3.274  1.00 27.15 ? 106 VAL   C CB  1 
ATOM   3398  C  CG1 . VAL   C  1 106 ? -37.390 -48.283  -1.929  1.00 34.88 ? 106 VAL   C CG1 1 
ATOM   3399  C  CG2 . VAL   C  1 106 ? -36.356 -46.331  -3.091  1.00 28.00 ? 106 VAL   C CG2 1 
ATOM   3400  N  N   . HIS   C  1 107 ? -37.255 -50.560  -4.467  1.00 27.60 ? 107 HIS   C N   1 
ATOM   3401  C  CA  . HIS   C  1 107 ? -37.724 -51.927  -4.249  1.00 24.57 ? 107 HIS   C CA  1 
ATOM   3402  C  C   . HIS   C  1 107 ? -36.689 -52.972  -4.681  1.00 28.22 ? 107 HIS   C C   1 
ATOM   3403  O  O   . HIS   C  1 107 ? -36.555 -54.005  -4.022  1.00 28.14 ? 107 HIS   C O   1 
ATOM   3404  C  CB  . HIS   C  1 107 ? -39.056 -52.195  -4.956  1.00 33.22 ? 107 HIS   C CB  1 
ATOM   3405  C  CG  . HIS   C  1 107 ? -39.574 -53.557  -4.663  1.00 41.03 ? 107 HIS   C CG  1 
ATOM   3406  N  ND1 . HIS   C  1 107 ? -40.143 -53.880  -3.448  1.00 40.41 ? 107 HIS   C ND1 1 
ATOM   3407  C  CD2 . HIS   C  1 107 ? -39.511 -54.710  -5.372  1.00 38.43 ? 107 HIS   C CD2 1 
ATOM   3408  C  CE1 . HIS   C  1 107 ? -40.436 -55.168  -3.436  1.00 46.87 ? 107 HIS   C CE1 1 
ATOM   3409  N  NE2 . HIS   C  1 107 ? -40.072 -55.692  -4.595  1.00 46.03 ? 107 HIS   C NE2 1 
ATOM   3410  N  N   . CYS   C  1 108 ? -35.975 -52.763  -5.803  1.00 25.81 ? 108 CYS   C N   1 
ATOM   3411  C  CA  . CYS   C  1 108 ? -34.912 -53.707  -6.156  1.00 23.56 ? 108 CYS   C CA  1 
ATOM   3412  C  C   . CYS   C  1 108 ? -33.886 -53.802  -5.039  1.00 24.33 ? 108 CYS   C C   1 
ATOM   3413  O  O   . CYS   C  1 108 ? -33.489 -54.906  -4.654  1.00 28.72 ? 108 CYS   C O   1 
ATOM   3414  C  CB  . CYS   C  1 108 ? -34.225 -53.319  -7.465  1.00 25.92 ? 108 CYS   C CB  1 
ATOM   3415  S  SG  . CYS   C  1 108 ? -35.323 -53.348  -8.904  1.00 29.56 ? 108 CYS   C SG  1 
ATOM   3416  N  N   . GLU   C  1 109 ? -33.459 -52.653  -4.499  1.00 22.48 ? 109 GLU   C N   1 
ATOM   3417  C  CA  . GLU   C  1 109 ? -32.512 -52.653  -3.389  1.00 24.51 ? 109 GLU   C CA  1 
ATOM   3418  C  C   . GLU   C  1 109 ? -33.038 -53.479  -2.211  1.00 35.45 ? 109 GLU   C C   1 
ATOM   3419  O  O   . GLU   C  1 109 ? -32.336 -54.344  -1.674  1.00 31.36 ? 109 GLU   C O   1 
ATOM   3420  C  CB  . GLU   C  1 109 ? -32.230 -51.219  -2.940  1.00 24.76 ? 109 GLU   C CB  1 
ATOM   3421  C  CG  . GLU   C  1 109 ? -31.210 -51.101  -1.816  1.00 25.92 ? 109 GLU   C CG  1 
ATOM   3422  C  CD  . GLU   C  1 109 ? -29.764 -51.436  -2.274  1.00 29.85 ? 109 GLU   C CD  1 
ATOM   3423  O  OE1 . GLU   C  1 109 ? -29.517 -51.540  -3.488  1.00 28.09 ? 109 GLU   C OE1 1 
ATOM   3424  O  OE2 . GLU   C  1 109 ? -28.870 -51.587  -1.413  1.00 28.71 ? 109 GLU   C OE2 1 
ATOM   3425  N  N   . GLN   C  1 110 ? -34.280 -53.232  -1.804  1.00 30.86 ? 110 GLN   C N   1 
ATOM   3426  C  CA  . GLN   C  1 110 ? -34.814 -53.925  -0.627  1.00 28.12 ? 110 GLN   C CA  1 
ATOM   3427  C  C   . GLN   C  1 110 ? -34.874 -55.438  -0.811  1.00 32.33 ? 110 GLN   C C   1 
ATOM   3428  O  O   . GLN   C  1 110 ? -34.682 -56.182  0.153   1.00 34.58 ? 110 GLN   C O   1 
ATOM   3429  C  CB  . GLN   C  1 110 ? -36.178 -53.341  -0.300  1.00 27.16 ? 110 GLN   C CB  1 
ATOM   3430  C  CG  . GLN   C  1 110 ? -36.023 -51.970  0.312   1.00 34.69 ? 110 GLN   C CG  1 
ATOM   3431  N  N   . VAL   C  1 111 ? -35.083 -55.937  -2.029  1.00 28.39 ? 111 VAL   C N   1 
ATOM   3432  C  CA  . VAL   C  1 111 ? -35.123 -57.381  -2.229  1.00 30.61 ? 111 VAL   C CA  1 
ATOM   3433  C  C   . VAL   C  1 111 ? -33.806 -57.920  -2.788  1.00 28.38 ? 111 VAL   C C   1 
ATOM   3434  O  O   . VAL   C  1 111 ? -33.728 -59.095  -3.152  1.00 30.93 ? 111 VAL   C O   1 
ATOM   3435  C  CB  . VAL   C  1 111 ? -36.325 -57.792  -3.108  1.00 34.96 ? 111 VAL   C CB  1 
ATOM   3436  C  CG1 . VAL   C  1 111 ? -37.611 -57.193  -2.549  1.00 35.96 ? 111 VAL   C CG1 1 
ATOM   3437  C  CG2 . VAL   C  1 111 ? -36.140 -57.355  -4.543  1.00 33.41 ? 111 VAL   C CG2 1 
ATOM   3438  N  N   . HIS   C  1 112 ? -32.761 -57.092  -2.843  1.00 28.66 ? 112 HIS   C N   1 
ATOM   3439  C  CA  . HIS   C  1 112 ? -31.406 -57.513  -3.222  1.00 32.99 ? 112 HIS   C CA  1 
ATOM   3440  C  C   . HIS   C  1 112 ? -31.311 -57.915  -4.684  1.00 27.52 ? 112 HIS   C C   1 
ATOM   3441  O  O   . HIS   C  1 112 ? -30.493 -58.762  -5.037  1.00 26.26 ? 112 HIS   C O   1 
ATOM   3442  C  CB  . HIS   C  1 112 ? -30.899 -58.662  -2.358  1.00 31.16 ? 112 HIS   C CB  1 
ATOM   3443  C  CG  . HIS   C  1 112 ? -31.051 -58.415  -0.891  1.00 32.34 ? 112 HIS   C CG  1 
ATOM   3444  N  ND1 . HIS   C  1 112 ? -30.976 -59.423  0.041   1.00 43.39 ? 112 HIS   C ND1 1 
ATOM   3445  C  CD2 . HIS   C  1 112 ? -31.297 -57.279  -0.199  1.00 34.31 ? 112 HIS   C CD2 1 
ATOM   3446  C  CE1 . HIS   C  1 112 ? -31.175 -58.920  1.246   1.00 45.11 ? 112 HIS   C CE1 1 
ATOM   3447  N  NE2 . HIS   C  1 112 ? -31.373 -57.622  1.131   1.00 41.06 ? 112 HIS   C NE2 1 
ATOM   3448  N  N   . ASP   C  1 113 ? -32.154 -57.341  -5.534  1.00 27.96 ? 113 ASP   C N   1 
ATOM   3449  C  CA  . ASP   C  1 113 ? -32.030 -57.544  -6.981  1.00 28.90 ? 113 ASP   C CA  1 
ATOM   3450  C  C   . ASP   C  1 113 ? -31.147 -56.421  -7.521  1.00 29.92 ? 113 ASP   C C   1 
ATOM   3451  O  O   . ASP   C  1 113 ? -31.600 -55.436  -8.106  1.00 27.95 ? 113 ASP   C O   1 
ATOM   3452  C  CB  . ASP   C  1 113 ? -33.394 -57.568  -7.649  1.00 28.30 ? 113 ASP   C CB  1 
ATOM   3453  C  CG  . ASP   C  1 113 ? -33.312 -57.944  -9.119  1.00 32.20 ? 113 ASP   C CG  1 
ATOM   3454  O  OD1 . ASP   C  1 113 ? -32.176 -58.091  -9.640  1.00 29.68 ? 113 ASP   C OD1 1 
ATOM   3455  O  OD2 . ASP   C  1 113 ? -34.379 -58.072  -9.762  1.00 29.11 ? 113 ASP   C OD2 1 
ATOM   3456  N  N   . TYR   C  1 114 ? -29.859 -56.568  -7.227  1.00 26.64 ? 114 TYR   C N   1 
ATOM   3457  C  CA  . TYR   C  1 114 ? -28.909 -55.502  -7.493  1.00 24.23 ? 114 TYR   C CA  1 
ATOM   3458  C  C   . TYR   C  1 114 ? -28.672 -55.343  -8.990  1.00 23.95 ? 114 TYR   C C   1 
ATOM   3459  O  O   . TYR   C  1 114 ? -28.342 -54.249  -9.438  1.00 26.40 ? 114 TYR   C O   1 
ATOM   3460  C  CB  . TYR   C  1 114 ? -27.594 -55.784  -6.738  1.00 23.53 ? 114 TYR   C CB  1 
ATOM   3461  C  CG  . TYR   C  1 114 ? -27.771 -55.901  -5.235  1.00 25.98 ? 114 TYR   C CG  1 
ATOM   3462  C  CD1 . TYR   C  1 114 ? -28.225 -54.830  -4.483  1.00 28.99 ? 114 TYR   C CD1 1 
ATOM   3463  C  CD2 . TYR   C  1 114 ? -27.497 -57.083  -4.576  1.00 24.85 ? 114 TYR   C CD2 1 
ATOM   3464  C  CE1 . TYR   C  1 114 ? -28.378 -54.922  -3.122  1.00 29.33 ? 114 TYR   C CE1 1 
ATOM   3465  C  CE2 . TYR   C  1 114 ? -27.648 -57.186  -3.224  1.00 23.23 ? 114 TYR   C CE2 1 
ATOM   3466  C  CZ  . TYR   C  1 114 ? -28.106 -56.095  -2.504  1.00 29.17 ? 114 TYR   C CZ  1 
ATOM   3467  O  OH  . TYR   C  1 114 ? -28.263 -56.160  -1.155  1.00 30.81 ? 114 TYR   C OH  1 
ATOM   3468  N  N   . VAL   C  1 115 ? -28.873 -56.398  -9.782  1.00 25.74 ? 115 VAL   C N   1 
ATOM   3469  C  CA  . VAL   C  1 115 ? -28.682 -56.279  -11.231 1.00 25.38 ? 115 VAL   C CA  1 
ATOM   3470  C  C   . VAL   C  1 115 ? -29.817 -55.474  -11.852 1.00 29.27 ? 115 VAL   C C   1 
ATOM   3471  O  O   . VAL   C  1 115 ? -29.586 -54.573  -12.668 1.00 24.02 ? 115 VAL   C O   1 
ATOM   3472  C  CB  . VAL   C  1 115 ? -28.547 -57.666  -11.882 1.00 26.05 ? 115 VAL   C CB  1 
ATOM   3473  C  CG1 . VAL   C  1 115 ? -28.482 -57.510  -13.404 1.00 30.78 ? 115 VAL   C CG1 1 
ATOM   3474  C  CG2 . VAL   C  1 115 ? -27.287 -58.369  -11.365 1.00 26.41 ? 115 VAL   C CG2 1 
ATOM   3475  N  N   . SER   C  1 116 ? -31.067 -55.764  -11.465 1.00 24.65 ? 116 SER   C N   1 
ATOM   3476  C  CA  . SER   C  1 116 ? -32.173 -54.927  -11.930 1.00 25.91 ? 116 SER   C CA  1 
ATOM   3477  C  C   . SER   C  1 116 ? -31.955 -53.482  -11.508 1.00 23.97 ? 116 SER   C C   1 
ATOM   3478  O  O   . SER   C  1 116 ? -32.216 -52.551  -12.284 1.00 26.44 ? 116 SER   C O   1 
ATOM   3479  C  CB  . SER   C  1 116 ? -33.524 -55.450  -11.401 1.00 20.73 ? 116 SER   C CB  1 
ATOM   3480  O  OG  . SER   C  1 116 ? -33.854 -56.715  -11.951 1.00 27.10 ? 116 SER   C OG  1 
ATOM   3481  N  N   . ARG   C  1 117 ? -31.444 -53.272  -10.292 1.00 26.41 ? 117 ARG   C N   1 
ATOM   3482  C  CA  . ARG   C  1 117 ? -31.159 -51.911  -9.852  1.00 23.85 ? 117 ARG   C CA  1 
ATOM   3483  C  C   . ARG   C  1 117 ? -30.153 -51.233  -10.772 1.00 24.60 ? 117 ARG   C C   1 
ATOM   3484  O  O   . ARG   C  1 117 ? -30.307 -50.058  -11.114 1.00 24.11 ? 117 ARG   C O   1 
ATOM   3485  C  CB  . ARG   C  1 117 ? -30.621 -51.896  -8.429  1.00 25.98 ? 117 ARG   C CB  1 
ATOM   3486  C  CG  . ARG   C  1 117 ? -30.035 -50.525  -8.075  1.00 25.49 ? 117 ARG   C CG  1 
ATOM   3487  C  CD  . ARG   C  1 117 ? -29.627 -50.390  -6.624  1.00 24.07 ? 117 ARG   C CD  1 
ATOM   3488  N  NE  . ARG   C  1 117 ? -28.861 -49.165  -6.451  1.00 26.67 ? 117 ARG   C NE  1 
ATOM   3489  C  CZ  . ARG   C  1 117 ? -28.898 -48.416  -5.359  1.00 30.02 ? 117 ARG   C CZ  1 
ATOM   3490  N  NH1 . ARG   C  1 117 ? -29.605 -48.777  -4.301  1.00 27.87 ? 117 ARG   C NH1 1 
ATOM   3491  N  NH2 . ARG   C  1 117 ? -28.243 -47.252  -5.344  1.00 30.80 ? 117 ARG   C NH2 1 
ATOM   3492  N  N   . ASP   C  1 118 ? -29.103 -51.952  -11.164 1.00 24.67 ? 118 ASP   C N   1 
ATOM   3493  C  CA  . ASP   C  1 118 ? -28.063 -51.352  -12.000 1.00 27.18 ? 118 ASP   C CA  1 
ATOM   3494  C  C   . ASP   C  1 118 ? -28.626 -50.954  -13.363 1.00 25.28 ? 118 ASP   C C   1 
ATOM   3495  O  O   . ASP   C  1 118 ? -28.332 -49.866  -13.883 1.00 24.40 ? 118 ASP   C O   1 
ATOM   3496  C  CB  . ASP   C  1 118 ? -26.916 -52.355  -12.143 1.00 27.08 ? 118 ASP   C CB  1 
ATOM   3497  C  CG  . ASP   C  1 118 ? -25.605 -51.707  -12.547 1.00 29.12 ? 118 ASP   C CG  1 
ATOM   3498  O  OD1 . ASP   C  1 118 ? -25.242 -50.652  -11.992 1.00 27.41 ? 118 ASP   C OD1 1 
ATOM   3499  O  OD2 . ASP   C  1 118 ? -24.944 -52.314  -13.389 1.00 24.77 ? 118 ASP   C OD2 1 
ATOM   3500  N  N   . LEU   C  1 119 ? -29.429 -51.830  -13.961 1.00 23.85 ? 119 LEU   C N   1 
ATOM   3501  C  CA  . LEU   C  1 119 ? -30.090 -51.498  -15.210 1.00 22.99 ? 119 LEU   C CA  1 
ATOM   3502  C  C   . LEU   C  1 119 ? -30.921 -50.248  -15.045 1.00 27.79 ? 119 LEU   C C   1 
ATOM   3503  O  O   . LEU   C  1 119 ? -30.876 -49.354  -15.887 1.00 23.09 ? 119 LEU   C O   1 
ATOM   3504  C  CB  . LEU   C  1 119 ? -30.974 -52.664  -15.670 1.00 30.34 ? 119 LEU   C CB  1 
ATOM   3505  C  CG  . LEU   C  1 119 ? -31.888 -52.377  -16.860 1.00 30.87 ? 119 LEU   C CG  1 
ATOM   3506  C  CD1 . LEU   C  1 119 ? -31.084 -52.011  -18.096 1.00 29.83 ? 119 LEU   C CD1 1 
ATOM   3507  C  CD2 . LEU   C  1 119 ? -32.747 -53.598  -17.153 1.00 30.04 ? 119 LEU   C CD2 1 
ATOM   3508  N  N   . LEU   C  1 120 ? -31.698 -50.168  -13.951 1.00 26.29 ? 120 LEU   C N   1 
ATOM   3509  C  CA  . LEU   C  1 120 ? -32.584 -49.023  -13.769 1.00 24.78 ? 120 LEU   C CA  1 
ATOM   3510  C  C   . LEU   C  1 120 ? -31.784 -47.756  -13.517 1.00 22.93 ? 120 LEU   C C   1 
ATOM   3511  O  O   . LEU   C  1 120 ? -32.169 -46.665  -13.949 1.00 24.12 ? 120 LEU   C O   1 
ATOM   3512  C  CB  . LEU   C  1 120 ? -33.557 -49.283  -12.614 1.00 24.00 ? 120 LEU   C CB  1 
ATOM   3513  C  CG  . LEU   C  1 120 ? -34.578 -50.402  -12.886 1.00 26.19 ? 120 LEU   C CG  1 
ATOM   3514  C  CD1 . LEU   C  1 120 ? -35.469 -50.683  -11.674 1.00 26.96 ? 120 LEU   C CD1 1 
ATOM   3515  C  CD2 . LEU   C  1 120 ? -35.431 -50.074  -14.098 1.00 24.93 ? 120 LEU   C CD2 1 
ATOM   3516  N  N   . LYS   C  1 121 ? -30.683 -47.876  -12.794 1.00 25.18 ? 121 LYS   C N   1 
ATOM   3517  C  CA  . LYS   C  1 121 ? -29.825 -46.717  -12.574 1.00 26.66 ? 121 LYS   C CA  1 
ATOM   3518  C  C   . LYS   C  1 121 ? -29.263 -46.208  -13.898 1.00 24.86 ? 121 LYS   C C   1 
ATOM   3519  O  O   . LYS   C  1 121 ? -29.205 -44.993  -14.126 1.00 21.93 ? 121 LYS   C O   1 
ATOM   3520  C  CB  . LYS   C  1 121 ? -28.706 -47.095  -11.590 1.00 19.18 ? 121 LYS   C CB  1 
ATOM   3521  C  CG  . LYS   C  1 121 ? -27.715 -45.995  -11.292 1.00 21.94 ? 121 LYS   C CG  1 
ATOM   3522  C  CD  . LYS   C  1 121 ? -26.555 -45.949  -12.334 1.00 26.51 ? 121 LYS   C CD  1 
ATOM   3523  C  CE  . LYS   C  1 121 ? -25.583 -47.112  -12.176 1.00 31.20 ? 121 LYS   C CE  1 
ATOM   3524  N  NZ  . LYS   C  1 121 ? -24.518 -46.986  -13.205 1.00 34.77 ? 121 LYS   C NZ  1 
ATOM   3525  N  N   . ASP   C  1 122 ? -28.895 -47.120  -14.806 1.00 23.94 ? 122 ASP   C N   1 
ATOM   3526  C  CA  . ASP   C  1 122 ? -28.395 -46.689  -16.113 1.00 26.11 ? 122 ASP   C CA  1 
ATOM   3527  C  C   . ASP   C  1 122 ? -29.496 -45.982  -16.911 1.00 30.02 ? 122 ASP   C C   1 
ATOM   3528  O  O   . ASP   C  1 122 ? -29.257 -44.956  -17.561 1.00 23.79 ? 122 ASP   C O   1 
ATOM   3529  C  CB  . ASP   C  1 122 ? -27.877 -47.884  -16.917 1.00 24.31 ? 122 ASP   C CB  1 
ATOM   3530  C  CG  . ASP   C  1 122 ? -26.551 -48.445  -16.409 1.00 29.65 ? 122 ASP   C CG  1 
ATOM   3531  O  OD1 . ASP   C  1 122 ? -25.797 -47.781  -15.663 1.00 28.14 ? 122 ASP   C OD1 1 
ATOM   3532  O  OD2 . ASP   C  1 122 ? -26.245 -49.594  -16.800 1.00 29.10 ? 122 ASP   C OD2 1 
ATOM   3533  N  N   . ILE   C  1 123 ? -30.713 -46.524  -16.895 1.00 28.19 ? 123 ILE   C N   1 
ATOM   3534  C  CA  . ILE   C  1 123 ? -31.806 -45.836  -17.572 1.00 21.67 ? 123 ILE   C CA  1 
ATOM   3535  C  C   . ILE   C  1 123 ? -32.032 -44.465  -16.947 1.00 21.11 ? 123 ILE   C C   1 
ATOM   3536  O  O   . ILE   C  1 123 ? -32.203 -43.464  -17.657 1.00 24.71 ? 123 ILE   C O   1 
ATOM   3537  C  CB  . ILE   C  1 123 ? -33.069 -46.716  -17.535 1.00 23.71 ? 123 ILE   C CB  1 
ATOM   3538  C  CG1 . ILE   C  1 123 ? -32.823 -48.005  -18.326 1.00 32.91 ? 123 ILE   C CG1 1 
ATOM   3539  C  CG2 . ILE   C  1 123 ? -34.319 -45.941  -18.050 1.00 29.80 ? 123 ILE   C CG2 1 
ATOM   3540  C  CD1 . ILE   C  1 123 ? -33.922 -49.030  -18.172 1.00 33.25 ? 123 ILE   C CD1 1 
ATOM   3541  N  N   . LEU   C  1 124 ? -32.026 -44.394  -15.611 1.00 25.38 ? 124 LEU   C N   1 
ATOM   3542  C  CA  . LEU   C  1 124 ? -32.215 -43.122  -14.914 1.00 22.02 ? 124 LEU   C CA  1 
ATOM   3543  C  C   . LEU   C  1 124 ? -31.178 -42.086  -15.329 1.00 28.66 ? 124 LEU   C C   1 
ATOM   3544  O  O   . LEU   C  1 124 ? -31.495 -40.891  -15.486 1.00 22.10 ? 124 LEU   C O   1 
ATOM   3545  C  CB  . LEU   C  1 124 ? -32.136 -43.363  -13.399 1.00 21.81 ? 124 LEU   C CB  1 
ATOM   3546  C  CG  . LEU   C  1 124 ? -32.232 -42.162  -12.473 1.00 23.36 ? 124 LEU   C CG  1 
ATOM   3547  C  CD1 . LEU   C  1 124 ? -33.577 -41.489  -12.649 1.00 26.18 ? 124 LEU   C CD1 1 
ATOM   3548  C  CD2 . LEU   C  1 124 ? -32.038 -42.570  -11.003 1.00 23.40 ? 124 LEU   C CD2 1 
ATOM   3549  N  N   . GLU   C  1 125 ? -29.913 -42.508  -15.449 1.00 22.61 ? 125 GLU   C N   1 
ATOM   3550  C  CA  . GLU   C  1 125 ? -28.890 -41.595  -15.960 1.00 20.77 ? 125 GLU   C CA  1 
ATOM   3551  C  C   . GLU   C  1 125 ? -29.271 -41.043  -17.333 1.00 21.97 ? 125 GLU   C C   1 
ATOM   3552  O  O   . GLU   C  1 125 ? -29.111 -39.843  -17.596 1.00 21.87 ? 125 GLU   C O   1 
ATOM   3553  C  CB  . GLU   C  1 125 ? -27.518 -42.295  -16.010 1.00 24.27 ? 125 GLU   C CB  1 
ATOM   3554  C  CG  . GLU   C  1 125 ? -26.883 -42.296  -14.661 1.00 29.32 ? 125 GLU   C CG  1 
ATOM   3555  C  CD  . GLU   C  1 125 ? -25.607 -43.129  -14.504 1.00 42.74 ? 125 GLU   C CD  1 
ATOM   3556  O  OE1 . GLU   C  1 125 ? -25.248 -43.943  -15.388 1.00 37.78 ? 125 GLU   C OE1 1 
ATOM   3557  O  OE2 . GLU   C  1 125 ? -24.963 -42.952  -13.449 1.00 41.26 ? 125 GLU   C OE2 1 
ATOM   3558  N  N   . SER   C  1 126 ? -29.769 -41.899  -18.225 1.00 24.73 ? 126 SER   C N   1 
ATOM   3559  C  CA  A SER   C  1 126 ? -30.170 -41.425  -19.543 0.50 28.99 ? 126 SER   C CA  1 
ATOM   3560  C  CA  B SER   C  1 126 ? -30.177 -41.429  -19.547 0.50 29.00 ? 126 SER   C CA  1 
ATOM   3561  C  C   . SER   C  1 126 ? -31.330 -40.442  -19.449 1.00 29.79 ? 126 SER   C C   1 
ATOM   3562  O  O   . SER   C  1 126 ? -31.334 -39.414  -20.132 1.00 26.10 ? 126 SER   C O   1 
ATOM   3563  C  CB  A SER   C  1 126 ? -30.543 -42.609  -20.433 0.50 28.67 ? 126 SER   C CB  1 
ATOM   3564  C  CB  B SER   C  1 126 ? -30.570 -42.608  -20.440 0.50 28.67 ? 126 SER   C CB  1 
ATOM   3565  O  OG  A SER   C  1 126 ? -31.031 -42.149  -21.674 0.50 26.23 ? 126 SER   C OG  1 
ATOM   3566  O  OG  B SER   C  1 126 ? -29.447 -43.392  -20.782 0.50 29.62 ? 126 SER   C OG  1 
ATOM   3567  N  N   . GLU   C  1 127 ? -32.323 -40.733  -18.592 1.00 27.17 ? 127 GLU   C N   1 
ATOM   3568  C  CA  . GLU   C  1 127 ? -33.459 -39.829  -18.477 1.00 21.99 ? 127 GLU   C CA  1 
ATOM   3569  C  C   . GLU   C  1 127 ? -33.046 -38.482  -17.883 1.00 21.43 ? 127 GLU   C C   1 
ATOM   3570  O  O   . GLU   C  1 127 ? -33.549 -37.432  -18.306 1.00 22.97 ? 127 GLU   C O   1 
ATOM   3571  C  CB  . GLU   C  1 127 ? -34.588 -40.474  -17.663 1.00 23.79 ? 127 GLU   C CB  1 
ATOM   3572  C  CG  . GLU   C  1 127 ? -35.049 -41.846  -18.156 1.00 23.29 ? 127 GLU   C CG  1 
ATOM   3573  C  CD  . GLU   C  1 127 ? -35.439 -41.852  -19.609 1.00 36.00 ? 127 GLU   C CD  1 
ATOM   3574  O  OE1 . GLU   C  1 127 ? -35.834 -40.779  -20.117 1.00 34.74 ? 127 GLU   C OE1 1 
ATOM   3575  O  OE2 . GLU   C  1 127 ? -35.324 -42.920  -20.245 1.00 40.25 ? 127 GLU   C OE2 1 
ATOM   3576  N  N   . GLU   C  1 128 ? -32.104 -38.464  -16.934 1.00 23.46 ? 128 GLU   C N   1 
ATOM   3577  C  CA  . GLU   C  1 128 ? -31.705 -37.162  -16.413 1.00 22.28 ? 128 GLU   C CA  1 
ATOM   3578  C  C   . GLU   C  1 128 ? -30.922 -36.363  -17.446 1.00 24.41 ? 128 GLU   C C   1 
ATOM   3579  O  O   . GLU   C  1 128 ? -30.980 -35.126  -17.427 1.00 26.03 ? 128 GLU   C O   1 
ATOM   3580  C  CB  . GLU   C  1 128 ? -30.891 -37.311  -15.118 1.00 25.63 ? 128 GLU   C CB  1 
ATOM   3581  C  CG  . GLU   C  1 128 ? -31.753 -37.714  -13.913 1.00 31.28 ? 128 GLU   C CG  1 
ATOM   3582  C  CD  . GLU   C  1 128 ? -30.981 -37.751  -12.564 1.00 35.48 ? 128 GLU   C CD  1 
ATOM   3583  O  OE1 . GLU   C  1 128 ? -29.812 -37.266  -12.505 1.00 29.01 ? 128 GLU   C OE1 1 
ATOM   3584  O  OE2 . GLU   C  1 128 ? -31.550 -38.280  -11.558 1.00 26.07 ? 128 GLU   C OE2 1 
ATOM   3585  N  N   . GLU   C  1 129 ? -30.210 -37.034  -18.357 1.00 24.07 ? 129 GLU   C N   1 
ATOM   3586  C  CA  . GLU   C  1 129 ? -29.607 -36.320  -19.485 1.00 25.73 ? 129 GLU   C CA  1 
ATOM   3587  C  C   . GLU   C  1 129 ? -30.685 -35.709  -20.379 1.00 22.88 ? 129 GLU   C C   1 
ATOM   3588  O  O   . GLU   C  1 129 ? -30.529 -34.592  -20.875 1.00 24.42 ? 129 GLU   C O   1 
ATOM   3589  C  CB  . GLU   C  1 129 ? -28.731 -37.262  -20.328 1.00 29.50 ? 129 GLU   C CB  1 
ATOM   3590  C  CG  . GLU   C  1 129 ? -27.328 -37.500  -19.755 1.00 40.43 ? 129 GLU   C CG  1 
ATOM   3591  C  CD  . GLU   C  1 129 ? -26.519 -38.522  -20.569 1.00 45.53 ? 129 GLU   C CD  1 
ATOM   3592  O  OE1 . GLU   C  1 129 ? -26.920 -38.859  -21.700 1.00 47.36 ? 129 GLU   C OE1 1 
ATOM   3593  O  OE2 . GLU   C  1 129 ? -25.479 -38.994  -20.067 1.00 55.59 ? 129 GLU   C OE2 1 
ATOM   3594  N  N   . HIS   C  1 130 ? -31.770 -36.440  -20.617 1.00 24.75 ? 130 HIS   C N   1 
ATOM   3595  C  CA  . HIS   C  1 130 ? -32.856 -35.891  -21.435 1.00 29.32 ? 130 HIS   C CA  1 
ATOM   3596  C  C   . HIS   C  1 130 ? -33.527 -34.722  -20.722 1.00 26.76 ? 130 HIS   C C   1 
ATOM   3597  O  O   . HIS   C  1 130 ? -33.848 -33.706  -21.352 1.00 24.82 ? 130 HIS   C O   1 
ATOM   3598  C  CB  . HIS   C  1 130 ? -33.865 -37.000  -21.791 1.00 29.21 ? 130 HIS   C CB  1 
ATOM   3599  C  CG  . HIS   C  1 130 ? -34.848 -36.620  -22.860 1.00 55.18 ? 130 HIS   C CG  1 
ATOM   3600  N  ND1 . HIS   C  1 130 ? -35.997 -37.343  -23.110 1.00 61.50 ? 130 HIS   C ND1 1 
ATOM   3601  C  CD2 . HIS   C  1 130 ? -34.843 -35.607  -23.763 1.00 57.62 ? 130 HIS   C CD2 1 
ATOM   3602  C  CE1 . HIS   C  1 130 ? -36.661 -36.788  -24.110 1.00 53.44 ? 130 HIS   C CE1 1 
ATOM   3603  N  NE2 . HIS   C  1 130 ? -35.976 -35.739  -24.531 1.00 57.32 ? 130 HIS   C NE2 1 
ATOM   3604  N  N   . ILE   C  1 131 ? -33.715 -34.828  -19.401 1.00 25.41 ? 131 ILE   C N   1 
ATOM   3605  C  CA  . ILE   C  1 131 ? -34.260 -33.707  -18.636 1.00 22.24 ? 131 ILE   C CA  1 
ATOM   3606  C  C   . ILE   C  1 131 ? -33.365 -32.476  -18.752 1.00 27.84 ? 131 ILE   C C   1 
ATOM   3607  O  O   . ILE   C  1 131 ? -33.841 -31.347  -18.948 1.00 25.35 ? 131 ILE   C O   1 
ATOM   3608  C  CB  . ILE   C  1 131 ? -34.468 -34.124  -17.163 1.00 26.42 ? 131 ILE   C CB  1 
ATOM   3609  C  CG1 . ILE   C  1 131 ? -35.653 -35.084  -17.072 1.00 30.38 ? 131 ILE   C CG1 1 
ATOM   3610  C  CG2 . ILE   C  1 131 ? -34.650 -32.904  -16.290 1.00 32.68 ? 131 ILE   C CG2 1 
ATOM   3611  C  CD1 . ILE   C  1 131 ? -35.759 -35.823  -15.712 1.00 36.17 ? 131 ILE   C CD1 1 
ATOM   3612  N  N   . ASP   C  1 132 ? -32.055 -32.660  -18.593 1.00 26.65 ? 132 ASP   C N   1 
ATOM   3613  C  CA  . ASP   C  1 132 ? -31.143 -31.532  -18.776 1.00 27.14 ? 132 ASP   C CA  1 
ATOM   3614  C  C   . ASP   C  1 132 ? -31.340 -30.890  -20.148 1.00 22.57 ? 132 ASP   C C   1 
ATOM   3615  O  O   . ASP   C  1 132 ? -31.404 -29.664  -20.273 1.00 24.10 ? 132 ASP   C O   1 
ATOM   3616  C  CB  . ASP   C  1 132 ? -29.696 -32.003  -18.626 1.00 30.33 ? 132 ASP   C CB  1 
ATOM   3617  C  CG  . ASP   C  1 132 ? -28.684 -30.852  -18.522 1.00 34.49 ? 132 ASP   C CG  1 
ATOM   3618  O  OD1 . ASP   C  1 132 ? -29.054 -29.664  -18.446 1.00 39.10 ? 132 ASP   C OD1 1 
ATOM   3619  O  OD2 . ASP   C  1 132 ? -27.476 -31.167  -18.499 1.00 45.21 ? 132 ASP   C OD2 1 
ATOM   3620  N  N   . TYR   C  1 133 ? -31.392 -31.711  -21.190 1.00 23.60 ? 133 TYR   C N   1 
ATOM   3621  C  CA  . TYR   C  1 133 ? -31.600 -31.190  -22.534 1.00 25.87 ? 133 TYR   C CA  1 
ATOM   3622  C  C   . TYR   C  1 133 ? -32.910 -30.407  -22.626 1.00 28.74 ? 133 TYR   C C   1 
ATOM   3623  O  O   . TYR   C  1 133 ? -32.930 -29.284  -23.137 1.00 26.93 ? 133 TYR   C O   1 
ATOM   3624  C  CB  . TYR   C  1 133 ? -31.579 -32.339  -23.538 1.00 24.29 ? 133 TYR   C CB  1 
ATOM   3625  C  CG  . TYR   C  1 133 ? -32.149 -31.962  -24.885 1.00 29.69 ? 133 TYR   C CG  1 
ATOM   3626  C  CD1 . TYR   C  1 133 ? -31.351 -31.333  -25.835 1.00 32.92 ? 133 TYR   C CD1 1 
ATOM   3627  C  CD2 . TYR   C  1 133 ? -33.490 -32.209  -25.193 1.00 32.78 ? 133 TYR   C CD2 1 
ATOM   3628  C  CE1 . TYR   C  1 133 ? -31.856 -30.969  -27.067 1.00 35.06 ? 133 TYR   C CE1 1 
ATOM   3629  C  CE2 . TYR   C  1 133 ? -34.009 -31.853  -26.441 1.00 34.61 ? 133 TYR   C CE2 1 
ATOM   3630  C  CZ  . TYR   C  1 133 ? -33.183 -31.234  -27.368 1.00 32.66 ? 133 TYR   C CZ  1 
ATOM   3631  O  OH  . TYR   C  1 133 ? -33.651 -30.860  -28.616 1.00 36.90 ? 133 TYR   C OH  1 
ATOM   3632  N  N   . LEU   C  1 134 ? -34.014 -30.982  -22.119 1.00 28.96 ? 134 LEU   C N   1 
ATOM   3633  C  CA  . LEU   C  1 134 ? -35.322 -30.322  -22.211 1.00 26.86 ? 134 LEU   C CA  1 
ATOM   3634  C  C   . LEU   C  1 134 ? -35.341 -28.995  -21.458 1.00 28.02 ? 134 LEU   C C   1 
ATOM   3635  O  O   . LEU   C  1 134 ? -35.802 -27.971  -21.986 1.00 28.14 ? 134 LEU   C O   1 
ATOM   3636  C  CB  . LEU   C  1 134 ? -36.408 -31.261  -21.679 1.00 26.51 ? 134 LEU   C CB  1 
ATOM   3637  C  CG  . LEU   C  1 134 ? -36.633 -32.469  -22.568 1.00 22.87 ? 134 LEU   C CG  1 
ATOM   3638  C  CD1 . LEU   C  1 134 ? -37.411 -33.556  -21.839 1.00 31.50 ? 134 LEU   C CD1 1 
ATOM   3639  C  CD2 . LEU   C  1 134 ? -37.347 -32.058  -23.821 1.00 29.99 ? 134 LEU   C CD2 1 
ATOM   3640  N  N   . GLU   C  1 135 ? -34.878 -29.004  -20.199 1.00 31.12 ? 135 GLU   C N   1 
ATOM   3641  C  CA  . GLU   C  1 135 ? -34.829 -27.782  -19.400 1.00 24.73 ? 135 GLU   C CA  1 
ATOM   3642  C  C   . GLU   C  1 135 ? -33.979 -26.721  -20.079 1.00 31.14 ? 135 GLU   C C   1 
ATOM   3643  O  O   . GLU   C  1 135 ? -34.301 -25.523  -20.044 1.00 30.41 ? 135 GLU   C O   1 
ATOM   3644  C  CB  . GLU   C  1 135 ? -34.261 -28.095  -18.016 1.00 30.54 ? 135 GLU   C CB  1 
ATOM   3645  C  CG  . GLU   C  1 135 ? -35.171 -28.993  -17.187 1.00 34.52 ? 135 GLU   C CG  1 
ATOM   3646  C  CD  . GLU   C  1 135 ? -34.547 -29.347  -15.826 1.00 32.42 ? 135 GLU   C CD  1 
ATOM   3647  O  OE1 . GLU   C  1 135 ? -33.325 -29.493  -15.720 1.00 30.05 ? 135 GLU   C OE1 1 
ATOM   3648  O  OE2 . GLU   C  1 135 ? -35.289 -29.444  -14.848 1.00 31.60 ? 135 GLU   C OE2 1 
ATOM   3649  N  N   . THR   C  1 136 ? -32.882 -27.146  -20.689 1.00 27.19 ? 136 THR   C N   1 
ATOM   3650  C  CA  . THR   C  1 136 ? -32.018 -26.210  -21.391 1.00 27.10 ? 136 THR   C CA  1 
ATOM   3651  C  C   . THR   C  1 136 ? -32.720 -25.629  -22.612 1.00 27.58 ? 136 THR   C C   1 
ATOM   3652  O  O   . THR   C  1 136 ? -32.614 -24.427  -22.874 1.00 27.64 ? 136 THR   C O   1 
ATOM   3653  C  CB  . THR   C  1 136 ? -30.710 -26.907  -21.771 1.00 30.10 ? 136 THR   C CB  1 
ATOM   3654  O  OG1 . THR   C  1 136 ? -30.047 -27.338  -20.575 1.00 33.34 ? 136 THR   C OG1 1 
ATOM   3655  C  CG2 . THR   C  1 136 ? -29.800 -25.975  -22.546 1.00 26.19 ? 136 THR   C CG2 1 
ATOM   3656  N  N   . GLN   C  1 137 ? -33.420 -26.458  -23.389 1.00 24.51 ? 137 GLN   C N   1 
ATOM   3657  C  CA  . GLN   C  1 137 ? -34.121 -25.906  -24.551 1.00 32.62 ? 137 GLN   C CA  1 
ATOM   3658  C  C   . GLN   C  1 137 ? -35.157 -24.873  -24.114 1.00 25.94 ? 137 GLN   C C   1 
ATOM   3659  O  O   . GLN   C  1 137 ? -35.244 -23.783  -24.690 1.00 29.39 ? 137 GLN   C O   1 
ATOM   3660  C  CB  . GLN   C  1 137 ? -34.794 -27.013  -25.354 1.00 28.90 ? 137 GLN   C CB  1 
ATOM   3661  C  CG  . GLN   C  1 137 ? -33.866 -28.114  -25.844 1.00 27.04 ? 137 GLN   C CG  1 
ATOM   3662  C  CD  . GLN   C  1 137 ? -32.514 -27.597  -26.263 1.00 33.23 ? 137 GLN   C CD  1 
ATOM   3663  O  OE1 . GLN   C  1 137 ? -31.517 -27.805  -25.571 1.00 35.59 ? 137 GLN   C OE1 1 
ATOM   3664  N  NE2 . GLN   C  1 137 ? -32.470 -26.912  -27.381 1.00 27.86 ? 137 GLN   C NE2 1 
ATOM   3665  N  N   . LEU   C  1 138 ? -35.949 -25.193  -23.085 1.00 27.77 ? 138 LEU   C N   1 
ATOM   3666  C  CA  . LEU   C  1 138 ? -36.968 -24.241  -22.641 1.00 24.97 ? 138 LEU   C CA  1 
ATOM   3667  C  C   . LEU   C  1 138 ? -36.327 -22.961  -22.143 1.00 31.62 ? 138 LEU   C C   1 
ATOM   3668  O  O   . LEU   C  1 138 ? -36.857 -21.874  -22.375 1.00 26.02 ? 138 LEU   C O   1 
ATOM   3669  C  CB  . LEU   C  1 138 ? -37.840 -24.874  -21.547 1.00 27.10 ? 138 LEU   C CB  1 
ATOM   3670  C  CG  . LEU   C  1 138 ? -38.731 -26.023  -22.030 1.00 27.42 ? 138 LEU   C CG  1 
ATOM   3671  C  CD1 . LEU   C  1 138 ? -39.240 -26.856  -20.862 1.00 32.55 ? 138 LEU   C CD1 1 
ATOM   3672  C  CD2 . LEU   C  1 138 ? -39.906 -25.495  -22.876 1.00 31.22 ? 138 LEU   C CD2 1 
ATOM   3673  N  N   . GLY   C  1 139 ? -35.156 -23.063  -21.515 1.00 28.79 ? 139 GLY   C N   1 
ATOM   3674  C  CA  . GLY   C  1 139 ? -34.444 -21.867  -21.104 1.00 31.96 ? 139 GLY   C CA  1 
ATOM   3675  C  C   . GLY   C  1 139 ? -33.934 -21.068  -22.289 1.00 34.38 ? 139 GLY   C C   1 
ATOM   3676  O  O   . GLY   C  1 139 ? -33.949 -19.838  -22.274 1.00 32.47 ? 139 GLY   C O   1 
ATOM   3677  N  N   . LEU   C  1 140 ? -33.486 -21.750  -23.336 1.00 28.89 ? 140 LEU   C N   1 
ATOM   3678  C  CA  . LEU   C  1 140 ? -32.951 -21.013  -24.474 1.00 31.96 ? 140 LEU   C CA  1 
ATOM   3679  C  C   . LEU   C  1 140 ? -34.061 -20.215  -25.160 1.00 26.85 ? 140 LEU   C C   1 
ATOM   3680  O  O   . LEU   C  1 140 ? -33.835 -19.094  -25.623 1.00 29.78 ? 140 LEU   C O   1 
ATOM   3681  C  CB  . LEU   C  1 140 ? -32.281 -21.980  -25.452 1.00 31.67 ? 140 LEU   C CB  1 
ATOM   3682  C  CG  . LEU   C  1 140 ? -30.864 -22.445  -25.048 1.00 31.06 ? 140 LEU   C CG  1 
ATOM   3683  C  CD1 . LEU   C  1 140 ? -30.398 -23.601  -25.938 1.00 32.78 ? 140 LEU   C CD1 1 
ATOM   3684  C  CD2 . LEU   C  1 140 ? -29.877 -21.283  -25.122 1.00 31.24 ? 140 LEU   C CD2 1 
ATOM   3685  N  N   . ILE   C  1 141 ? -35.257 -20.786  -25.238 1.00 28.29 ? 141 ILE   C N   1 
ATOM   3686  C  CA  . ILE   C  1 141 ? -36.376 -20.059  -25.841 1.00 34.75 ? 141 ILE   C CA  1 
ATOM   3687  C  C   . ILE   C  1 141 ? -36.546 -18.713  -25.154 1.00 34.85 ? 141 ILE   C C   1 
ATOM   3688  O  O   . ILE   C  1 141 ? -36.803 -17.690  -25.801 1.00 33.36 ? 141 ILE   C O   1 
ATOM   3689  C  CB  . ILE   C  1 141 ? -37.657 -20.910  -25.775 1.00 30.36 ? 141 ILE   C CB  1 
ATOM   3690  C  CG1 . ILE   C  1 141 ? -37.574 -22.037  -26.806 1.00 28.21 ? 141 ILE   C CG1 1 
ATOM   3691  C  CG2 . ILE   C  1 141 ? -38.902 -20.028  -25.994 1.00 33.43 ? 141 ILE   C CG2 1 
ATOM   3692  C  CD1 . ILE   C  1 141 ? -38.607 -23.102  -26.615 1.00 36.46 ? 141 ILE   C CD1 1 
ATOM   3693  N  N   . GLN   C  1 142 ? -36.342 -18.688  -23.834 1.00 32.12 ? 142 GLN   C N   1 
ATOM   3694  C  CA  . GLN   C  1 142 ? -36.464 -17.459  -23.067 1.00 33.56 ? 142 GLN   C CA  1 
ATOM   3695  C  C   . GLN   C  1 142 ? -35.280 -16.548  -23.301 1.00 37.19 ? 142 GLN   C C   1 
ATOM   3696  O  O   . GLN   C  1 142 ? -35.438 -15.324  -23.313 1.00 38.26 ? 142 GLN   C O   1 
ATOM   3697  C  CB  . GLN   C  1 142 ? -36.602 -17.787  -21.570 1.00 38.39 ? 142 GLN   C CB  1 
ATOM   3698  C  CG  . GLN   C  1 142 ? -37.833 -18.633  -21.226 1.00 37.92 ? 142 GLN   C CG  1 
ATOM   3699  C  CD  . GLN   C  1 142 ? -39.134 -17.966  -21.679 1.00 39.29 ? 142 GLN   C CD  1 
ATOM   3700  O  OE1 . GLN   C  1 142 ? -39.332 -16.769  -21.475 1.00 40.19 ? 142 GLN   C OE1 1 
ATOM   3701  N  NE2 . GLN   C  1 142 ? -40.000 -18.731  -22.327 1.00 43.37 ? 142 GLN   C NE2 1 
ATOM   3702  N  N   . LYS   C  1 143 ? -34.089 -17.112  -23.502 1.00 30.26 ? 143 LYS   C N   1 
ATOM   3703  C  CA  . LYS   C  1 143 ? -32.917 -16.262  -23.632 1.00 32.23 ? 143 LYS   C CA  1 
ATOM   3704  C  C   . LYS   C  1 143 ? -32.782 -15.694  -25.040 1.00 34.41 ? 143 LYS   C C   1 
ATOM   3705  O  O   . LYS   C  1 143 ? -32.372 -14.538  -25.204 1.00 31.21 ? 143 LYS   C O   1 
ATOM   3706  C  CB  . LYS   C  1 143 ? -31.646 -17.030  -23.263 1.00 29.56 ? 143 LYS   C CB  1 
ATOM   3707  C  CG  . LYS   C  1 143 ? -31.527 -17.445  -21.812 1.00 38.04 ? 143 LYS   C CG  1 
ATOM   3708  C  CD  . LYS   C  1 143 ? -30.204 -18.236  -21.619 1.00 39.70 ? 143 LYS   C CD  1 
ATOM   3709  C  CE  . LYS   C  1 143 ? -29.761 -18.263  -20.157 1.00 53.82 ? 143 LYS   C CE  1 
ATOM   3710  N  NZ  . LYS   C  1 143 ? -30.698 -19.052  -19.303 1.00 52.56 ? 143 LYS   C NZ  1 
ATOM   3711  N  N   . VAL   C  1 144 ? -33.058 -16.491  -26.072 1.00 29.95 ? 144 VAL   C N   1 
ATOM   3712  C  CA  . VAL   C  1 144 ? -32.810 -16.004  -27.434 1.00 32.05 ? 144 VAL   C CA  1 
ATOM   3713  C  C   . VAL   C  1 144 ? -34.083 -15.573  -28.138 1.00 38.41 ? 144 VAL   C C   1 
ATOM   3714  O  O   . VAL   C  1 144 ? -34.000 -14.957  -29.216 1.00 30.03 ? 144 VAL   C O   1 
ATOM   3715  C  CB  . VAL   C  1 144 ? -32.052 -17.047  -28.285 1.00 34.80 ? 144 VAL   C CB  1 
ATOM   3716  C  CG1 . VAL   C  1 144 ? -30.780 -17.493  -27.566 1.00 31.81 ? 144 VAL   C CG1 1 
ATOM   3717  C  CG2 . VAL   C  1 144 ? -32.924 -18.213  -28.610 1.00 25.76 ? 144 VAL   C CG2 1 
ATOM   3718  N  N   . GLY   C  1 145 ? -35.248 -15.835  -27.552 1.00 33.18 ? 145 GLY   C N   1 
ATOM   3719  C  CA  . GLY   C  1 145 ? -36.521 -15.576  -28.222 1.00 33.36 ? 145 GLY   C CA  1 
ATOM   3720  C  C   . GLY   C  1 145 ? -37.002 -16.784  -28.998 1.00 33.08 ? 145 GLY   C C   1 
ATOM   3721  O  O   . GLY   C  1 145 ? -36.223 -17.593  -29.503 1.00 28.56 ? 145 GLY   C O   1 
ATOM   3722  N  N   . LEU   C  1 146 ? -38.329 -16.916  -29.098 1.00 29.85 ? 146 LEU   C N   1 
ATOM   3723  C  CA  . LEU   C  1 146 ? -38.883 -18.093  -29.757 1.00 30.43 ? 146 LEU   C CA  1 
ATOM   3724  C  C   . LEU   C  1 146 ? -38.459 -18.168  -31.222 1.00 32.90 ? 146 LEU   C C   1 
ATOM   3725  O  O   . LEU   C  1 146 ? -38.164 -19.261  -31.733 1.00 26.38 ? 146 LEU   C O   1 
ATOM   3726  C  CB  . LEU   C  1 146 ? -40.406 -18.108  -29.664 1.00 35.47 ? 146 LEU   C CB  1 
ATOM   3727  C  CG  . LEU   C  1 146 ? -40.994 -19.364  -30.300 1.00 29.14 ? 146 LEU   C CG  1 
ATOM   3728  C  CD1 . LEU   C  1 146 ? -40.424 -20.635  -29.640 1.00 33.51 ? 146 LEU   C CD1 1 
ATOM   3729  C  CD2 . LEU   C  1 146 ? -42.526 -19.393  -30.244 1.00 39.82 ? 146 LEU   C CD2 1 
ATOM   3730  N  N   . GLU   C  1 147 ? -38.457 -17.025  -31.921 1.00 26.43 ? 147 GLU   C N   1 
ATOM   3731  C  CA  . GLU   C  1 147 ? -38.187 -17.026  -33.359 1.00 27.09 ? 147 GLU   C CA  1 
ATOM   3732  C  C   . GLU   C  1 147 ? -36.740 -17.459  -33.658 1.00 26.23 ? 147 GLU   C C   1 
ATOM   3733  O  O   . GLU   C  1 147 ? -36.513 -18.296  -34.535 1.00 27.99 ? 147 GLU   C O   1 
ATOM   3734  C  CB  . GLU   C  1 147 ? -38.462 -15.650  -33.944 1.00 30.30 ? 147 GLU   C CB  1 
ATOM   3735  C  CG  . GLU   C  1 147 ? -39.937 -15.380  -34.220 1.00 32.89 ? 147 GLU   C CG  1 
ATOM   3736  C  CD  . GLU   C  1 147 ? -40.146 -14.046  -34.926 1.00 49.13 ? 147 GLU   C CD  1 
ATOM   3737  O  OE1 . GLU   C  1 147 ? -39.376 -13.096  -34.655 1.00 54.70 ? 147 GLU   C OE1 1 
ATOM   3738  O  OE2 . GLU   C  1 147 ? -41.066 -13.945  -35.763 1.00 55.94 ? 147 GLU   C OE2 1 
ATOM   3739  N  N   . ASN   C  1 148 ? -35.757 -16.909  -32.928 1.00 25.36 ? 148 ASN   C N   1 
ATOM   3740  C  CA  . ASN   C  1 148 ? -34.372 -17.367  -33.074 1.00 30.39 ? 148 ASN   C CA  1 
ATOM   3741  C  C   . ASN   C  1 148 ? -34.228 -18.829  -32.670 1.00 33.04 ? 148 ASN   C C   1 
ATOM   3742  O  O   . ASN   C  1 148 ? -33.513 -19.603  -33.329 1.00 30.06 ? 148 ASN   C O   1 
ATOM   3743  C  CB  . ASN   C  1 148 ? -33.405 -16.538  -32.224 1.00 23.09 ? 148 ASN   C CB  1 
ATOM   3744  C  CG  . ASN   C  1 148 ? -33.047 -15.225  -32.823 1.00 29.23 ? 148 ASN   C CG  1 
ATOM   3745  O  OD1 . ASN   C  1 148 ? -33.339 -14.929  -33.986 1.00 28.95 ? 148 ASN   C OD1 1 
ATOM   3746  N  ND2 . ASN   C  1 148 ? -32.351 -14.419  -32.031 1.00 27.86 ? 148 ASN   C ND2 1 
ATOM   3747  N  N   . TYR   C  1 149 ? -34.863 -19.224  -31.564 1.00 27.60 ? 149 TYR   C N   1 
ATOM   3748  C  CA  . TYR   C  1 149 ? -34.754 -20.617  -31.127 1.00 27.91 ? 149 TYR   C CA  1 
ATOM   3749  C  C   . TYR   C  1 149 ? -35.175 -21.559  -32.248 1.00 29.96 ? 149 TYR   C C   1 
ATOM   3750  O  O   . TYR   C  1 149 ? -34.485 -22.535  -32.550 1.00 26.38 ? 149 TYR   C O   1 
ATOM   3751  C  CB  . TYR   C  1 149 ? -35.586 -20.906  -29.862 1.00 29.60 ? 149 TYR   C CB  1 
ATOM   3752  C  CG  . TYR   C  1 149 ? -35.458 -22.371  -29.484 1.00 29.29 ? 149 TYR   C CG  1 
ATOM   3753  C  CD1 . TYR   C  1 149 ? -34.323 -22.828  -28.812 1.00 27.27 ? 149 TYR   C CD1 1 
ATOM   3754  C  CD2 . TYR   C  1 149 ? -36.424 -23.307  -29.853 1.00 28.10 ? 149 TYR   C CD2 1 
ATOM   3755  C  CE1 . TYR   C  1 149 ? -34.164 -24.155  -28.508 1.00 27.60 ? 149 TYR   C CE1 1 
ATOM   3756  C  CE2 . TYR   C  1 149 ? -36.254 -24.660  -29.559 1.00 32.50 ? 149 TYR   C CE2 1 
ATOM   3757  C  CZ  . TYR   C  1 149 ? -35.109 -25.067  -28.897 1.00 31.06 ? 149 TYR   C CZ  1 
ATOM   3758  O  OH  . TYR   C  1 149 ? -34.905 -26.387  -28.580 1.00 30.93 ? 149 TYR   C OH  1 
ATOM   3759  N  N   . LEU   C  1 150 ? -36.303 -21.273  -32.890 1.00 24.75 ? 150 LEU   C N   1 
ATOM   3760  C  CA  . LEU   C  1 150 ? -36.773 -22.161  -33.941 1.00 24.47 ? 150 LEU   C CA  1 
ATOM   3761  C  C   . LEU   C  1 150 ? -35.855 -22.073  -35.147 1.00 25.66 ? 150 LEU   C C   1 
ATOM   3762  O  O   . LEU   C  1 150 ? -35.531 -23.092  -35.758 1.00 26.52 ? 150 LEU   C O   1 
ATOM   3763  C  CB  . LEU   C  1 150 ? -38.211 -21.821  -34.314 1.00 25.96 ? 150 LEU   C CB  1 
ATOM   3764  C  CG  . LEU   C  1 150 ? -39.238 -21.980  -33.175 1.00 27.88 ? 150 LEU   C CG  1 
ATOM   3765  C  CD1 . LEU   C  1 150 ? -40.577 -21.398  -33.614 1.00 30.54 ? 150 LEU   C CD1 1 
ATOM   3766  C  CD2 . LEU   C  1 150 ? -39.413 -23.427  -32.742 1.00 34.13 ? 150 LEU   C CD2 1 
ATOM   3767  N  N   . GLN   C  1 151 ? -35.415 -20.859  -35.482 1.00 26.24 ? 151 GLN   C N   1 
ATOM   3768  C  CA  . GLN   C  1 151 ? -34.469 -20.670  -36.580 1.00 32.50 ? 151 GLN   C CA  1 
ATOM   3769  C  C   . GLN   C  1 151 ? -33.249 -21.564  -36.402 1.00 28.44 ? 151 GLN   C C   1 
ATOM   3770  O  O   . GLN   C  1 151 ? -32.787 -22.206  -37.353 1.00 28.26 ? 151 GLN   C O   1 
ATOM   3771  C  CB  . GLN   C  1 151 ? -34.028 -19.203  -36.661 1.00 32.24 ? 151 GLN   C CB  1 
ATOM   3772  C  CG  . GLN   C  1 151 ? -32.945 -18.949  -37.733 1.00 25.90 ? 151 GLN   C CG  1 
ATOM   3773  C  CD  . GLN   C  1 151 ? -32.401 -17.541  -37.714 1.00 26.06 ? 151 GLN   C CD  1 
ATOM   3774  O  OE1 . GLN   C  1 151 ? -32.238 -16.927  -36.659 1.00 27.98 ? 151 GLN   C OE1 1 
ATOM   3775  N  NE2 . GLN   C  1 151 ? -32.104 -17.015  -38.895 1.00 33.55 ? 151 GLN   C NE2 1 
ATOM   3776  N  N   . SER   C  1 152 ? -32.721 -21.622  -35.182 1.00 26.68 ? 152 SER   C N   1 
ATOM   3777  C  CA  . SER   C  1 152 ? -31.529 -22.403  -34.909 1.00 30.02 ? 152 SER   C CA  1 
ATOM   3778  C  C   . SER   C  1 152 ? -31.768 -23.900  -34.974 1.00 32.59 ? 152 SER   C C   1 
ATOM   3779  O  O   . SER   C  1 152 ? -30.791 -24.647  -34.874 1.00 33.43 ? 152 SER   C O   1 
ATOM   3780  C  CB  . SER   C  1 152 ? -30.969 -22.038  -33.555 1.00 27.61 ? 152 SER   C CB  1 
ATOM   3781  O  OG  . SER   C  1 152 ? -30.452 -20.740  -33.596 1.00 28.40 ? 152 SER   C OG  1 
ATOM   3782  N  N   . HIS   C  1 153 ? -33.018 -24.348  -35.158 1.00 25.97 ? 153 HIS   C N   1 
ATOM   3783  C  CA  . HIS   C  1 153 ? -33.343 -25.767  -35.235 1.00 25.41 ? 153 HIS   C CA  1 
ATOM   3784  C  C   . HIS   C  1 153 ? -33.948 -26.145  -36.581 1.00 23.42 ? 153 HIS   C C   1 
ATOM   3785  O  O   . HIS   C  1 153 ? -34.438 -27.258  -36.741 1.00 28.00 ? 153 HIS   C O   1 
ATOM   3786  C  CB  . HIS   C  1 153 ? -34.243 -26.167  -34.057 1.00 24.55 ? 153 HIS   C CB  1 
ATOM   3787  C  CG  . HIS   C  1 153 ? -33.514 -26.151  -32.757 1.00 30.61 ? 153 HIS   C CG  1 
ATOM   3788  N  ND1 . HIS   C  1 153 ? -33.250 -24.984  -32.075 1.00 31.54 ? 153 HIS   C ND1 1 
ATOM   3789  C  CD2 . HIS   C  1 153 ? -32.849 -27.133  -32.096 1.00 30.44 ? 153 HIS   C CD2 1 
ATOM   3790  C  CE1 . HIS   C  1 153 ? -32.505 -25.258  -31.017 1.00 34.18 ? 153 HIS   C CE1 1 
ATOM   3791  N  NE2 . HIS   C  1 153 ? -32.253 -26.554  -31.008 1.00 27.00 ? 153 HIS   C NE2 1 
ATOM   3792  N  N   . MET   C  1 154 ? -33.820 -25.275  -37.587 1.00 25.90 ? 154 MET   C N   1 
ATOM   3793  C  CA  . MET   C  1 154 ? -34.285 -25.618  -38.927 1.00 28.39 ? 154 MET   C CA  1 
ATOM   3794  C  C   . MET   C  1 154 ? -33.374 -26.643  -39.589 1.00 34.23 ? 154 MET   C C   1 
ATOM   3795  O  O   . MET   C  1 154 ? -33.852 -27.613  -40.187 1.00 31.06 ? 154 MET   C O   1 
ATOM   3796  C  CB  . MET   C  1 154 ? -34.365 -24.365  -39.808 1.00 31.49 ? 154 MET   C CB  1 
ATOM   3797  C  CG  . MET   C  1 154 ? -35.582 -23.444  -39.587 1.00 41.02 ? 154 MET   C CG  1 
ATOM   3798  S  SD  . MET   C  1 154 ? -35.468 -21.949  -40.625 1.00 47.00 ? 154 MET   C SD  1 
ATOM   3799  C  CE  . MET   C  1 154 ? -34.852 -22.694  -42.120 1.00 41.49 ? 154 MET   C CE  1 
ATOM   3800  N  N   . HIS   C  1 155 ? -32.063 -26.460  -39.478 1.00 39.70 ? 155 HIS   C N   1 
ATOM   3801  C  CA  . HIS   C  1 155 ? -31.098 -27.270  -40.208 1.00 42.18 ? 155 HIS   C CA  1 
ATOM   3802  C  C   . HIS   C  1 155 ? -30.249 -28.094  -39.245 1.00 47.03 ? 155 HIS   C C   1 
ATOM   3803  O  O   . HIS   C  1 155 ? -29.874 -27.625  -38.161 1.00 49.77 ? 155 HIS   C O   1 
ATOM   3804  C  CB  . HIS   C  1 155 ? -30.196 -26.376  -41.064 1.00 39.32 ? 155 HIS   C CB  1 
ATOM   3805  C  CG  . HIS   C  1 155 ? -30.940 -25.587  -42.090 1.00 43.98 ? 155 HIS   C CG  1 
ATOM   3806  N  ND1 . HIS   C  1 155 ? -30.657 -24.265  -42.364 1.00 49.13 ? 155 HIS   C ND1 1 
ATOM   3807  C  CD2 . HIS   C  1 155 ? -31.960 -25.935  -42.913 1.00 53.88 ? 155 HIS   C CD2 1 
ATOM   3808  C  CE1 . HIS   C  1 155 ? -31.474 -23.832  -43.312 1.00 50.89 ? 155 HIS   C CE1 1 
ATOM   3809  N  NE2 . HIS   C  1 155 ? -32.276 -24.825  -43.660 1.00 58.58 ? 155 HIS   C NE2 1 
ATOM   3810  N  N   . GLU   C  1 156 ? -29.943 -29.321  -39.645 1.00 47.60 ? 156 GLU   C N   1 
ATOM   3811  C  CA  . GLU   C  1 156 ? -28.927 -30.117  -38.947 1.00 71.05 ? 156 GLU   C CA  1 
ATOM   3812  C  C   . GLU   C  1 156 ? -27.516 -29.638  -39.304 1.00 62.96 ? 156 GLU   C C   1 
ATOM   3813  O  O   . GLU   C  1 156 ? -26.563 -29.835  -38.543 1.00 68.64 ? 156 GLU   C O   1 
ATOM   3814  C  CB  . GLU   C  1 156 ? -29.080 -31.596  -39.294 1.00 70.17 ? 156 GLU   C CB  1 
ATOM   3815  C  CG  . GLU   C  1 156 ? -30.525 -32.018  -39.392 1.00 48.51 ? 156 GLU   C CG  1 
ATOM   3816  C  CD  . GLU   C  1 156 ? -30.708 -33.513  -39.577 1.00 66.22 ? 156 GLU   C CD  1 
ATOM   3817  O  OE1 . GLU   C  1 156 ? -29.843 -34.294  -39.108 1.00 66.58 ? 156 GLU   C OE1 1 
ATOM   3818  O  OE2 . GLU   C  1 156 ? -31.729 -33.900  -40.191 1.00 51.19 ? 156 GLU   C OE2 1 
ATOM   3819  N  N   . MET   D  1 1   ? 24.476  -96.013  -41.863 1.00 45.91 ? 1   MET   D N   1 
ATOM   3820  C  CA  . MET   D  1 1   ? 24.936  -96.465  -40.511 1.00 45.95 ? 1   MET   D CA  1 
ATOM   3821  C  C   . MET   D  1 1   ? 24.323  -97.819  -40.193 1.00 43.96 ? 1   MET   D C   1 
ATOM   3822  O  O   . MET   D  1 1   ? 23.111  -97.924  -40.089 1.00 45.32 ? 1   MET   D O   1 
ATOM   3823  C  CB  . MET   D  1 1   ? 24.537  -95.450  -39.436 1.00 46.35 ? 1   MET   D CB  1 
ATOM   3824  C  CG  . MET   D  1 1   ? 25.421  -95.446  -38.200 1.00 48.95 ? 1   MET   D CG  1 
ATOM   3825  S  SD  . MET   D  1 1   ? 24.868  -94.223  -37.000 1.00 51.27 ? 1   MET   D SD  1 
ATOM   3826  C  CE  . MET   D  1 1   ? 23.239  -94.807  -36.629 1.00 47.03 ? 1   MET   D CE  1 
ATOM   3827  N  N   . LYS   D  1 2   ? 25.141  -98.859  -40.031 1.00 40.61 ? 2   LYS   D N   1 
ATOM   3828  C  CA  . LYS   D  1 2   ? 24.591  -100.197 -39.827 1.00 36.71 ? 2   LYS   D CA  1 
ATOM   3829  C  C   . LYS   D  1 2   ? 23.780  -100.239 -38.531 1.00 36.04 ? 2   LYS   D C   1 
ATOM   3830  O  O   . LYS   D  1 2   ? 24.320  -100.043 -37.444 1.00 48.72 ? 2   LYS   D O   1 
ATOM   3831  C  CB  . LYS   D  1 2   ? 25.715  -101.231 -39.801 1.00 43.57 ? 2   LYS   D CB  1 
ATOM   3832  N  N   . GLY   D  1 3   ? 22.485  -100.482 -38.657 1.00 36.83 ? 3   GLY   D N   1 
ATOM   3833  C  CA  . GLY   D  1 3   ? 21.611  -100.579 -37.514 1.00 46.67 ? 3   GLY   D CA  1 
ATOM   3834  C  C   . GLY   D  1 3   ? 21.437  -102.005 -37.016 1.00 53.00 ? 3   GLY   D C   1 
ATOM   3835  O  O   . GLY   D  1 3   ? 21.751  -102.975 -37.710 1.00 47.48 ? 3   GLY   D O   1 
ATOM   3836  N  N   . ASP   D  1 4   ? 20.934  -102.103 -35.783 1.00 43.58 ? 4   ASP   D N   1 
ATOM   3837  C  CA  . ASP   D  1 4   ? 20.571  -103.387 -35.184 1.00 41.67 ? 4   ASP   D CA  1 
ATOM   3838  C  C   . ASP   D  1 4   ? 19.538  -104.101 -36.049 1.00 46.11 ? 4   ASP   D C   1 
ATOM   3839  O  O   . ASP   D  1 4   ? 18.483  -103.542 -36.365 1.00 43.22 ? 4   ASP   D O   1 
ATOM   3840  C  CB  . ASP   D  1 4   ? 20.036  -103.148 -33.767 1.00 48.70 ? 4   ASP   D CB  1 
ATOM   3841  C  CG  . ASP   D  1 4   ? 19.663  -104.430 -33.037 1.00 46.33 ? 4   ASP   D CG  1 
ATOM   3842  O  OD1 . ASP   D  1 4   ? 20.562  -105.042 -32.415 1.00 47.48 ? 4   ASP   D OD1 1 
ATOM   3843  O  OD2 . ASP   D  1 4   ? 18.466  -104.800 -33.067 1.00 44.42 ? 4   ASP   D OD2 1 
ATOM   3844  N  N   . LYS   D  1 5   ? 19.852  -105.341 -36.445 1.00 44.01 ? 5   LYS   D N   1 
ATOM   3845  C  CA  . LYS   D  1 5   ? 18.963  -106.102 -37.322 1.00 36.65 ? 5   LYS   D CA  1 
ATOM   3846  C  C   . LYS   D  1 5   ? 17.552  -106.206 -36.762 1.00 41.46 ? 5   LYS   D C   1 
ATOM   3847  O  O   . LYS   D  1 5   ? 16.563  -106.081 -37.498 1.00 42.94 ? 5   LYS   D O   1 
ATOM   3848  C  CB  . LYS   D  1 5   ? 19.542  -107.503 -37.553 1.00 42.22 ? 5   LYS   D CB  1 
ATOM   3849  C  CG  . LYS   D  1 5   ? 18.547  -108.505 -38.161 1.00 44.73 ? 5   LYS   D CG  1 
ATOM   3850  N  N   . LYS   D  1 6   ? 17.428  -106.452 -35.462 1.00 48.38 ? 6   LYS   D N   1 
ATOM   3851  C  CA  . LYS   D  1 6   ? 16.098  -106.653 -34.897 1.00 46.10 ? 6   LYS   D CA  1 
ATOM   3852  C  C   . LYS   D  1 6   ? 15.338  -105.332 -34.780 1.00 45.50 ? 6   LYS   D C   1 
ATOM   3853  O  O   . LYS   D  1 6   ? 14.105  -105.322 -34.847 1.00 42.27 ? 6   LYS   D O   1 
ATOM   3854  C  CB  . LYS   D  1 6   ? 16.210  -107.351 -33.538 1.00 47.89 ? 6   LYS   D CB  1 
ATOM   3855  C  CG  . LYS   D  1 6   ? 14.873  -107.607 -32.860 1.00 54.08 ? 6   LYS   D CG  1 
ATOM   3856  C  CD  . LYS   D  1 6   ? 14.001  -108.589 -33.633 1.00 56.86 ? 6   LYS   D CD  1 
ATOM   3857  C  CE  . LYS   D  1 6   ? 12.771  -108.970 -32.819 1.00 58.98 ? 6   LYS   D CE  1 
ATOM   3858  N  NZ  . LYS   D  1 6   ? 11.912  -109.954 -33.531 1.00 64.59 ? 6   LYS   D NZ  1 
ATOM   3859  N  N   . VAL   D  1 7   ? 16.049  -104.217 -34.607 1.00 41.37 ? 7   VAL   D N   1 
ATOM   3860  C  CA  . VAL   D  1 7   ? 15.417  -102.904 -34.737 1.00 47.49 ? 7   VAL   D CA  1 
ATOM   3861  C  C   . VAL   D  1 7   ? 14.806  -102.755 -36.128 1.00 43.81 ? 7   VAL   D C   1 
ATOM   3862  O  O   . VAL   D  1 7   ? 13.616  -102.459 -36.280 1.00 43.92 ? 7   VAL   D O   1 
ATOM   3863  C  CB  . VAL   D  1 7   ? 16.438  -101.789 -34.455 1.00 44.47 ? 7   VAL   D CB  1 
ATOM   3864  C  CG1 . VAL   D  1 7   ? 15.978  -100.460 -35.080 1.00 47.29 ? 7   VAL   D CG1 1 
ATOM   3865  C  CG2 . VAL   D  1 7   ? 16.641  -101.637 -32.965 1.00 42.48 ? 7   VAL   D CG2 1 
ATOM   3866  N  N   . ILE   D  1 8   ? 15.624  -102.969 -37.166 1.00 44.53 ? 8   ILE   D N   1 
ATOM   3867  C  CA  . ILE   D  1 8   ? 15.135  -102.897 -38.539 1.00 43.64 ? 8   ILE   D CA  1 
ATOM   3868  C  C   . ILE   D  1 8   ? 13.911  -103.789 -38.722 1.00 38.61 ? 8   ILE   D C   1 
ATOM   3869  O  O   . ILE   D  1 8   ? 12.950  -103.417 -39.403 1.00 39.86 ? 8   ILE   D O   1 
ATOM   3870  C  CB  . ILE   D  1 8   ? 16.270  -103.249 -39.519 1.00 42.89 ? 8   ILE   D CB  1 
ATOM   3871  C  CG1 . ILE   D  1 8   ? 17.287  -102.117 -39.541 1.00 39.76 ? 8   ILE   D CG1 1 
ATOM   3872  C  CG2 . ILE   D  1 8   ? 15.710  -103.498 -40.908 1.00 46.60 ? 8   ILE   D CG2 1 
ATOM   3873  C  CD1 . ILE   D  1 8   ? 18.556  -102.469 -40.175 1.00 46.54 ? 8   ILE   D CD1 1 
ATOM   3874  N  N   . GLN   D  1 9   ? 13.906  -104.968 -38.097 1.00 44.43 ? 9   GLN   D N   1 
ATOM   3875  C  CA  . GLN   D  1 9   ? 12.744  -105.845 -38.220 1.00 37.57 ? 9   GLN   D CA  1 
ATOM   3876  C  C   . GLN   D  1 9   ? 11.506  -105.215 -37.593 1.00 48.03 ? 9   GLN   D C   1 
ATOM   3877  O  O   . GLN   D  1 9   ? 10.405  -105.281 -38.162 1.00 38.32 ? 9   GLN   D O   1 
ATOM   3878  C  CB  . GLN   D  1 9   ? 13.029  -107.199 -37.566 1.00 48.49 ? 9   GLN   D CB  1 
ATOM   3879  C  CG  . GLN   D  1 9   ? 14.096  -108.044 -38.229 1.00 53.04 ? 9   GLN   D CG  1 
ATOM   3880  C  CD  . GLN   D  1 9   ? 14.373  -109.328 -37.444 1.00 57.01 ? 9   GLN   D CD  1 
ATOM   3881  O  OE1 . GLN   D  1 9   ? 13.752  -109.584 -36.417 1.00 65.94 ? 9   GLN   D OE1 1 
ATOM   3882  N  NE2 . GLN   D  1 9   ? 15.301  -110.129 -37.927 1.00 56.79 ? 9   GLN   D NE2 1 
ATOM   3883  N  N   . HIS   D  1 10  ? 11.661  -104.608 -36.413 1.00 44.62 ? 10  HIS   D N   1 
ATOM   3884  C  CA  . HIS   D  1 10  ? 10.534  -103.920 -35.790 1.00 44.25 ? 10  HIS   D CA  1 
ATOM   3885  C  C   . HIS   D  1 10  ? 10.025  -102.797 -36.687 1.00 36.44 ? 10  HIS   D C   1 
ATOM   3886  O  O   . HIS   D  1 10  ? 8.820   -102.677 -36.943 1.00 36.59 ? 10  HIS   D O   1 
ATOM   3887  C  CB  . HIS   D  1 10  ? 10.954  -103.358 -34.435 1.00 42.78 ? 10  HIS   D CB  1 
ATOM   3888  C  CG  . HIS   D  1 10  ? 10.992  -104.371 -33.343 1.00 45.23 ? 10  HIS   D CG  1 
ATOM   3889  N  ND1 . HIS   D  1 10  ? 9.849   -104.935 -32.822 1.00 42.90 ? 10  HIS   D ND1 1 
ATOM   3890  C  CD2 . HIS   D  1 10  ? 12.029  -104.919 -32.669 1.00 39.96 ? 10  HIS   D CD2 1 
ATOM   3891  C  CE1 . HIS   D  1 10  ? 10.182  -105.785 -31.867 1.00 42.43 ? 10  HIS   D CE1 1 
ATOM   3892  N  NE2 . HIS   D  1 10  ? 11.497  -105.794 -31.755 1.00 48.73 ? 10  HIS   D NE2 1 
ATOM   3893  N  N   . LEU   D  1 11  ? 10.941  -101.950 -37.156 1.00 40.43 ? 11  LEU   D N   1 
ATOM   3894  C  CA  . LEU   D  1 11  ? 10.557  -100.856 -38.043 1.00 39.31 ? 11  LEU   D CA  1 
ATOM   3895  C  C   . LEU   D  1 11  ? 9.757   -101.382 -39.228 1.00 41.36 ? 11  LEU   D C   1 
ATOM   3896  O  O   . LEU   D  1 11  ? 8.686   -100.856 -39.564 1.00 37.34 ? 11  LEU   D O   1 
ATOM   3897  C  CB  . LEU   D  1 11  ? 11.811  -100.101 -38.505 1.00 34.06 ? 11  LEU   D CB  1 
ATOM   3898  C  CG  . LEU   D  1 11  ? 12.667  -99.455  -37.421 1.00 32.90 ? 11  LEU   D CG  1 
ATOM   3899  C  CD1 . LEU   D  1 11  ? 13.868  -98.667  -37.980 1.00 38.19 ? 11  LEU   D CD1 1 
ATOM   3900  C  CD2 . LEU   D  1 11  ? 11.791  -98.557  -36.526 1.00 40.21 ? 11  LEU   D CD2 1 
ATOM   3901  N  N   . ASN   D  1 12  ? 10.241  -102.454 -39.854 1.00 40.20 ? 12  ASN   D N   1 
ATOM   3902  C  CA  . ASN   D  1 12  ? 9.502   -103.034 -40.969 1.00 42.26 ? 12  ASN   D CA  1 
ATOM   3903  C  C   . ASN   D  1 12  ? 8.146   -103.548 -40.526 1.00 40.16 ? 12  ASN   D C   1 
ATOM   3904  O  O   . ASN   D  1 12  ? 7.166   -103.453 -41.266 1.00 39.76 ? 12  ASN   D O   1 
ATOM   3905  C  CB  . ASN   D  1 12  ? 10.314  -104.156 -41.624 1.00 44.11 ? 12  ASN   D CB  1 
ATOM   3906  C  CG  . ASN   D  1 12  ? 10.960  -103.708 -42.904 1.00 43.98 ? 12  ASN   D CG  1 
ATOM   3907  O  OD1 . ASN   D  1 12  ? 10.354  -102.963 -43.680 1.00 45.18 ? 12  ASN   D OD1 1 
ATOM   3908  N  ND2 . ASN   D  1 12  ? 12.180  -104.143 -43.137 1.00 43.20 ? 12  ASN   D ND2 1 
ATOM   3909  N  N   . LYS   D  1 13  ? 8.057   -104.109 -39.325 1.00 44.31 ? 13  LYS   D N   1 
ATOM   3910  C  CA  . LYS   D  1 13  ? 6.739   -104.521 -38.874 1.00 41.60 ? 13  LYS   D CA  1 
ATOM   3911  C  C   . LYS   D  1 13  ? 5.849   -103.300 -38.672 1.00 40.37 ? 13  LYS   D C   1 
ATOM   3912  O  O   . LYS   D  1 13  ? 4.673   -103.314 -39.052 1.00 38.17 ? 13  LYS   D O   1 
ATOM   3913  C  CB  . LYS   D  1 13  ? 6.840   -105.355 -37.594 1.00 43.27 ? 13  LYS   D CB  1 
ATOM   3914  C  CG  . LYS   D  1 13  ? 5.482   -105.893 -37.130 1.00 42.22 ? 13  LYS   D CG  1 
ATOM   3915  C  CD  . LYS   D  1 13  ? 5.576   -106.767 -35.861 1.00 55.54 ? 13  LYS   D CD  1 
ATOM   3916  C  CE  . LYS   D  1 13  ? 4.220   -107.417 -35.560 1.00 54.71 ? 13  LYS   D CE  1 
ATOM   3917  N  NZ  . LYS   D  1 13  ? 4.185   -108.168 -34.278 1.00 62.57 ? 13  LYS   D NZ  1 
ATOM   3918  N  N   . ILE   D  1 14  ? 6.401   -102.222 -38.106 1.00 38.71 ? 14  ILE   D N   1 
ATOM   3919  C  CA  . ILE   D  1 14  ? 5.606   -101.010 -37.951 1.00 39.09 ? 14  ILE   D CA  1 
ATOM   3920  C  C   . ILE   D  1 14  ? 5.189   -100.492 -39.330 1.00 39.23 ? 14  ILE   D C   1 
ATOM   3921  O  O   . ILE   D  1 14  ? 4.029   -100.117 -39.549 1.00 37.92 ? 14  ILE   D O   1 
ATOM   3922  C  CB  . ILE   D  1 14  ? 6.390   -99.961  -37.134 1.00 40.31 ? 14  ILE   D CB  1 
ATOM   3923  C  CG1 . ILE   D  1 14  ? 6.760   -100.500 -35.739 1.00 39.06 ? 14  ILE   D CG1 1 
ATOM   3924  C  CG2 . ILE   D  1 14  ? 5.566   -98.701  -36.948 1.00 40.19 ? 14  ILE   D CG2 1 
ATOM   3925  C  CD1 . ILE   D  1 14  ? 5.540   -100.935 -34.902 1.00 43.33 ? 14  ILE   D CD1 1 
ATOM   3926  N  N   . LEU   D  1 15  ? 6.107   -100.536 -40.296 1.00 42.89 ? 15  LEU   D N   1 
ATOM   3927  C  CA  . LEU   D  1 15  ? 5.788   -100.069 -41.643 1.00 41.87 ? 15  LEU   D CA  1 
ATOM   3928  C  C   . LEU   D  1 15  ? 4.678   -100.900 -42.267 1.00 42.92 ? 15  LEU   D C   1 
ATOM   3929  O  O   . LEU   D  1 15  ? 3.783   -100.355 -42.919 1.00 39.77 ? 15  LEU   D O   1 
ATOM   3930  C  CB  . LEU   D  1 15  ? 7.045   -100.089 -42.508 1.00 39.65 ? 15  LEU   D CB  1 
ATOM   3931  C  CG  . LEU   D  1 15  ? 6.955   -99.812  -44.015 1.00 36.32 ? 15  LEU   D CG  1 
ATOM   3932  C  CD1 . LEU   D  1 15  ? 6.311   -98.458  -44.332 1.00 38.53 ? 15  LEU   D CD1 1 
ATOM   3933  C  CD2 . LEU   D  1 15  ? 8.365   -99.867  -44.549 1.00 35.79 ? 15  LEU   D CD2 1 
ATOM   3934  N  N   . GLY   D  1 16  ? 4.700   -102.218 -42.057 1.00 42.21 ? 16  GLY   D N   1 
ATOM   3935  C  CA  . GLY   D  1 16  ? 3.600   -103.043 -42.535 1.00 38.14 ? 16  GLY   D CA  1 
ATOM   3936  C  C   . GLY   D  1 16  ? 2.251   -102.596 -42.008 1.00 40.28 ? 16  GLY   D C   1 
ATOM   3937  O  O   . GLY   D  1 16  ? 1.253   -102.607 -42.733 1.00 40.42 ? 16  GLY   D O   1 
ATOM   3938  N  N   . ASN   D  1 17  ? 2.194   -102.196 -40.741 1.00 45.50 ? 17  ASN   D N   1 
ATOM   3939  C  CA  . ASN   D  1 17  ? 0.932   -101.702 -40.204 1.00 42.72 ? 17  ASN   D CA  1 
ATOM   3940  C  C   . ASN   D  1 17  ? 0.495   -100.417 -40.895 1.00 36.01 ? 17  ASN   D C   1 
ATOM   3941  O  O   . ASN   D  1 17  ? -0.691  -100.243 -41.205 1.00 41.06 ? 17  ASN   D O   1 
ATOM   3942  C  CB  . ASN   D  1 17  ? 1.065   -101.466 -38.709 1.00 40.97 ? 17  ASN   D CB  1 
ATOM   3943  C  CG  . ASN   D  1 17  ? 1.216   -102.747 -37.928 1.00 46.92 ? 17  ASN   D CG  1 
ATOM   3944  O  OD1 . ASN   D  1 17  ? 0.705   -103.790 -38.322 1.00 50.72 ? 17  ASN   D OD1 1 
ATOM   3945  N  ND2 . ASN   D  1 17  ? 1.899   -102.668 -36.797 1.00 45.65 ? 17  ASN   D ND2 1 
ATOM   3946  N  N   . GLU   D  1 18  ? 1.427   -99.474  -41.072 1.00 40.69 ? 18  GLU   D N   1 
ATOM   3947  C  CA  . GLU   D  1 18  ? 1.106   -98.215  -41.743 1.00 49.02 ? 18  GLU   D CA  1 
ATOM   3948  C  C   . GLU   D  1 18  ? 0.551   -98.456  -43.149 1.00 38.22 ? 18  GLU   D C   1 
ATOM   3949  O  O   . GLU   D  1 18  ? -0.445  -97.837  -43.546 1.00 41.72 ? 18  GLU   D O   1 
ATOM   3950  C  CB  . GLU   D  1 18  ? 2.354   -97.325  -41.796 1.00 49.50 ? 18  GLU   D CB  1 
ATOM   3951  C  CG  . GLU   D  1 18  ? 2.976   -96.962  -40.434 1.00 44.22 ? 18  GLU   D CG  1 
ATOM   3952  C  CD  . GLU   D  1 18  ? 2.214   -95.903  -39.708 1.00 47.61 ? 18  GLU   D CD  1 
ATOM   3953  O  OE1 . GLU   D  1 18  ? 1.277   -95.335  -40.308 1.00 51.01 ? 18  GLU   D OE1 1 
ATOM   3954  O  OE2 . GLU   D  1 18  ? 2.557   -95.629  -38.540 1.00 50.16 ? 18  GLU   D OE2 1 
ATOM   3955  N  N   . LEU   D  1 19  ? 1.154   -99.388  -43.903 1.00 42.54 ? 19  LEU   D N   1 
ATOM   3956  C  CA  . LEU   D  1 19  ? 0.651   -99.692  -45.246 1.00 39.90 ? 19  LEU   D CA  1 
ATOM   3957  C  C   . LEU   D  1 19  ? -0.768  -100.235 -45.206 1.00 41.56 ? 19  LEU   D C   1 
ATOM   3958  O  O   . LEU   D  1 19  ? -1.605  -99.885  -46.056 1.00 45.81 ? 19  LEU   D O   1 
ATOM   3959  C  CB  . LEU   D  1 19  ? 1.591   -100.672 -45.941 1.00 42.92 ? 19  LEU   D CB  1 
ATOM   3960  C  CG  . LEU   D  1 19  ? 3.002   -100.091 -46.060 1.00 42.86 ? 19  LEU   D CG  1 
ATOM   3961  C  CD1 . LEU   D  1 19  ? 4.011   -101.159 -46.432 1.00 54.02 ? 19  LEU   D CD1 1 
ATOM   3962  C  CD2 . LEU   D  1 19  ? 3.061   -98.939  -47.065 1.00 45.48 ? 19  LEU   D CD2 1 
ATOM   3963  N  N   . ILE   D  1 20  ? -1.078  -101.080 -44.223 1.00 39.51 ? 20  ILE   D N   1 
ATOM   3964  C  CA  . ILE   D  1 20  ? -2.473  -101.470 -44.028 1.00 34.57 ? 20  ILE   D CA  1 
ATOM   3965  C  C   . ILE   D  1 20  ? -3.327  -100.242 -43.736 1.00 37.14 ? 20  ILE   D C   1 
ATOM   3966  O  O   . ILE   D  1 20  ? -4.413  -100.064 -44.304 1.00 36.57 ? 20  ILE   D O   1 
ATOM   3967  C  CB  . ILE   D  1 20  ? -2.596  -102.520 -42.904 1.00 38.67 ? 20  ILE   D CB  1 
ATOM   3968  C  CG1 . ILE   D  1 20  ? -1.780  -103.773 -43.240 1.00 45.94 ? 20  ILE   D CG1 1 
ATOM   3969  C  CG2 . ILE   D  1 20  ? -4.043  -102.914 -42.710 1.00 40.10 ? 20  ILE   D CG2 1 
ATOM   3970  C  CD1 . ILE   D  1 20  ? -1.676  -104.790 -42.085 1.00 51.46 ? 20  ILE   D CD1 1 
ATOM   3971  N  N   . ALA   D  1 21  ? -2.858  -99.379  -42.831 1.00 40.02 ? 21  ALA   D N   1 
ATOM   3972  C  CA  . ALA   D  1 21  ? -3.674  -98.235  -42.427 1.00 39.57 ? 21  ALA   D CA  1 
ATOM   3973  C  C   . ALA   D  1 21  ? -3.892  -97.285  -43.607 1.00 31.36 ? 21  ALA   D C   1 
ATOM   3974  O  O   . ALA   D  1 21  ? -5.022  -96.858  -43.884 1.00 35.47 ? 21  ALA   D O   1 
ATOM   3975  C  CB  . ALA   D  1 21  ? -3.017  -97.511  -41.244 1.00 33.60 ? 21  ALA   D CB  1 
ATOM   3976  N  N   . ILE   D  1 22  ? -2.818  -96.962  -44.323 1.00 39.98 ? 22  ILE   D N   1 
ATOM   3977  C  CA  . ILE   D  1 22  ? -2.942  -96.119  -45.513 1.00 38.53 ? 22  ILE   D CA  1 
ATOM   3978  C  C   . ILE   D  1 22  ? -4.113  -96.582  -46.366 1.00 39.44 ? 22  ILE   D C   1 
ATOM   3979  O  O   . ILE   D  1 22  ? -5.038  -95.815  -46.652 1.00 36.07 ? 22  ILE   D O   1 
ATOM   3980  C  CB  . ILE   D  1 22  ? -1.632  -96.124  -46.315 1.00 34.93 ? 22  ILE   D CB  1 
ATOM   3981  C  CG1 . ILE   D  1 22  ? -0.533  -95.415  -45.532 1.00 33.72 ? 22  ILE   D CG1 1 
ATOM   3982  C  CG2 . ILE   D  1 22  ? -1.828  -95.469  -47.669 1.00 41.67 ? 22  ILE   D CG2 1 
ATOM   3983  C  CD1 . ILE   D  1 22  ? 0.820   -95.602  -46.140 1.00 40.63 ? 22  ILE   D CD1 1 
ATOM   3984  N  N   . ASN   D  1 23  ? -4.103  -97.860  -46.767 1.00 38.11 ? 23  ASN   D N   1 
ATOM   3985  C  CA  . ASN   D  1 23  ? -5.120  -98.340  -47.704 1.00 35.94 ? 23  ASN   D CA  1 
ATOM   3986  C  C   . ASN   D  1 23  ? -6.488  -98.448  -47.052 1.00 38.42 ? 23  ASN   D C   1 
ATOM   3987  O  O   . ASN   D  1 23  ? -7.514  -98.123  -47.672 1.00 40.92 ? 23  ASN   D O   1 
ATOM   3988  C  CB  . ASN   D  1 23  ? -4.706  -99.689  -48.285 1.00 41.80 ? 23  ASN   D CB  1 
ATOM   3989  C  CG  . ASN   D  1 23  ? -3.591  -99.560  -49.307 1.00 43.27 ? 23  ASN   D CG  1 
ATOM   3990  O  OD1 . ASN   D  1 23  ? -2.883  -98.552  -49.348 1.00 46.03 ? 23  ASN   D OD1 1 
ATOM   3991  N  ND2 . ASN   D  1 23  ? -3.420  -100.588 -50.130 1.00 49.18 ? 23  ASN   D ND2 1 
ATOM   3992  N  N   . GLN   D  1 24  ? -6.535  -98.913  -45.806 1.00 39.53 ? 24  GLN   D N   1 
ATOM   3993  C  CA  . GLN   D  1 24  ? -7.817  -99.026  -45.116 1.00 35.64 ? 24  GLN   D CA  1 
ATOM   3994  C  C   . GLN   D  1 24  ? -8.466  -97.657  -44.952 1.00 37.54 ? 24  GLN   D C   1 
ATOM   3995  O  O   . GLN   D  1 24  ? -9.672  -97.483  -45.203 1.00 34.69 ? 24  GLN   D O   1 
ATOM   3996  C  CB  . GLN   D  1 24  ? -7.604  -99.684  -43.746 1.00 39.47 ? 24  GLN   D CB  1 
ATOM   3997  C  CG  . GLN   D  1 24  ? -8.886  -99.944  -42.936 1.00 36.46 ? 24  GLN   D CG  1 
ATOM   3998  C  CD  . GLN   D  1 24  ? -8.566  -100.684 -41.650 1.00 44.50 ? 24  GLN   D CD  1 
ATOM   3999  O  OE1 . GLN   D  1 24  ? -7.827  -101.661 -41.669 1.00 42.79 ? 24  GLN   D OE1 1 
ATOM   4000  N  NE2 . GLN   D  1 24  ? -9.073  -100.189 -40.521 1.00 40.26 ? 24  GLN   D NE2 1 
ATOM   4001  N  N   . TYR   D  1 25  ? -7.691  -96.673  -44.486 1.00 38.23 ? 25  TYR   D N   1 
ATOM   4002  C  CA  . TYR   D  1 25  ? -8.293  -95.361  -44.257 1.00 37.11 ? 25  TYR   D CA  1 
ATOM   4003  C  C   . TYR   D  1 25  ? -8.650  -94.705  -45.591 1.00 36.07 ? 25  TYR   D C   1 
ATOM   4004  O  O   . TYR   D  1 25  ? -9.689  -94.043  -45.706 1.00 32.11 ? 25  TYR   D O   1 
ATOM   4005  C  CB  . TYR   D  1 25  ? -7.357  -94.459  -43.434 1.00 31.53 ? 25  TYR   D CB  1 
ATOM   4006  C  CG  . TYR   D  1 25  ? -6.936  -95.021  -42.080 1.00 35.16 ? 25  TYR   D CG  1 
ATOM   4007  C  CD1 . TYR   D  1 25  ? -7.616  -96.082  -41.488 1.00 41.54 ? 25  TYR   D CD1 1 
ATOM   4008  C  CD2 . TYR   D  1 25  ? -5.843  -94.502  -41.410 1.00 36.05 ? 25  TYR   D CD2 1 
ATOM   4009  C  CE1 . TYR   D  1 25  ? -7.211  -96.595  -40.265 1.00 35.20 ? 25  TYR   D CE1 1 
ATOM   4010  C  CE2 . TYR   D  1 25  ? -5.430  -95.014  -40.185 1.00 39.66 ? 25  TYR   D CE2 1 
ATOM   4011  C  CZ  . TYR   D  1 25  ? -6.122  -96.057  -39.618 1.00 48.99 ? 25  TYR   D CZ  1 
ATOM   4012  O  OH  . TYR   D  1 25  ? -5.715  -96.571  -38.398 1.00 50.27 ? 25  TYR   D OH  1 
ATOM   4013  N  N   . PHE   D  1 26  ? -7.814  -94.902  -46.619 1.00 33.61 ? 26  PHE   D N   1 
ATOM   4014  C  CA  . PHE   D  1 26  ? -8.117  -94.284  -47.908 1.00 39.70 ? 26  PHE   D CA  1 
ATOM   4015  C  C   . PHE   D  1 26  ? -9.425  -94.809  -48.471 1.00 34.88 ? 26  PHE   D C   1 
ATOM   4016  O  O   . PHE   D  1 26  ? -10.255 -94.030  -48.963 1.00 35.31 ? 26  PHE   D O   1 
ATOM   4017  C  CB  . PHE   D  1 26  ? -6.993  -94.491  -48.930 1.00 38.34 ? 26  PHE   D CB  1 
ATOM   4018  C  CG  . PHE   D  1 26  ? -7.019  -93.457  -50.021 1.00 36.91 ? 26  PHE   D CG  1 
ATOM   4019  C  CD1 . PHE   D  1 26  ? -7.803  -93.628  -51.160 1.00 35.72 ? 26  PHE   D CD1 1 
ATOM   4020  C  CD2 . PHE   D  1 26  ? -6.321  -92.275  -49.867 1.00 38.47 ? 26  PHE   D CD2 1 
ATOM   4021  C  CE1 . PHE   D  1 26  ? -7.862  -92.645  -52.130 1.00 39.49 ? 26  PHE   D CE1 1 
ATOM   4022  C  CE2 . PHE   D  1 26  ? -6.375  -91.292  -50.841 1.00 38.11 ? 26  PHE   D CE2 1 
ATOM   4023  C  CZ  . PHE   D  1 26  ? -7.131  -91.478  -51.969 1.00 35.02 ? 26  PHE   D CZ  1 
ATOM   4024  N  N   . LEU   D  1 27  ? -9.638  -96.131  -48.401 1.00 44.69 ? 27  LEU   D N   1 
ATOM   4025  C  CA  . LEU   D  1 27  ? -10.881 -96.706  -48.926 1.00 42.88 ? 27  LEU   D CA  1 
ATOM   4026  C  C   . LEU   D  1 27  ? -12.082 -96.284  -48.094 1.00 33.04 ? 27  LEU   D C   1 
ATOM   4027  O  O   . LEU   D  1 27  ? -13.135 -95.952  -48.643 1.00 36.11 ? 27  LEU   D O   1 
ATOM   4028  C  CB  . LEU   D  1 27  ? -10.790 -98.240  -48.999 1.00 40.91 ? 27  LEU   D CB  1 
ATOM   4029  C  CG  . LEU   D  1 27  ? -12.065 -98.961  -49.477 1.00 37.29 ? 27  LEU   D CG  1 
ATOM   4030  C  CD1 . LEU   D  1 27  ? -12.537 -98.384  -50.773 1.00 39.29 ? 27  LEU   D CD1 1 
ATOM   4031  C  CD2 . LEU   D  1 27  ? -11.874 -100.483 -49.629 1.00 41.88 ? 27  LEU   D CD2 1 
ATOM   4032  N  N   . HIS   D  1 28  ? -11.952 -96.280  -46.766 1.00 37.68 ? 28  HIS   D N   1 
ATOM   4033  C  CA  . HIS   D  1 28  ? -13.054 -95.788  -45.941 1.00 44.46 ? 28  HIS   D CA  1 
ATOM   4034  C  C   . HIS   D  1 28  ? -13.396 -94.344  -46.297 1.00 33.42 ? 28  HIS   D C   1 
ATOM   4035  O  O   . HIS   D  1 28  ? -14.574 -93.970  -46.360 1.00 34.48 ? 28  HIS   D O   1 
ATOM   4036  C  CB  . HIS   D  1 28  ? -12.698 -95.902  -44.450 1.00 41.40 ? 28  HIS   D CB  1 
ATOM   4037  C  CG  . HIS   D  1 28  ? -12.812 -97.294  -43.908 1.00 42.13 ? 28  HIS   D CG  1 
ATOM   4038  N  ND1 . HIS   D  1 28  ? -12.062 -97.740  -42.841 1.00 43.88 ? 28  HIS   D ND1 1 
ATOM   4039  C  CD2 . HIS   D  1 28  ? -13.575 -98.344  -44.298 1.00 41.78 ? 28  HIS   D CD2 1 
ATOM   4040  C  CE1 . HIS   D  1 28  ? -12.349 -99.007  -42.600 1.00 38.40 ? 28  HIS   D CE1 1 
ATOM   4041  N  NE2 . HIS   D  1 28  ? -13.263 -99.398  -43.471 1.00 43.41 ? 28  HIS   D NE2 1 
ATOM   4042  N  N   . SER   D  1 29  ? -12.372 -93.515  -46.504 1.00 40.07 ? 29  SER   D N   1 
ATOM   4043  C  CA  . SER   D  1 29  ? -12.595 -92.127  -46.902 1.00 33.32 ? 29  SER   D CA  1 
ATOM   4044  C  C   . SER   D  1 29  ? -13.418 -92.054  -48.175 1.00 35.94 ? 29  SER   D C   1 
ATOM   4045  O  O   . SER   D  1 29  ? -14.420 -91.329  -48.253 1.00 33.25 ? 29  SER   D O   1 
ATOM   4046  C  CB  . SER   D  1 29  ? -11.235 -91.440  -47.084 1.00 38.71 ? 29  SER   D CB  1 
ATOM   4047  O  OG  . SER   D  1 29  ? -11.363 -90.208  -47.771 1.00 36.43 ? 29  SER   D OG  1 
ATOM   4048  N  N   . ARG   D  1 30  ? -13.009 -92.807  -49.196 1.00 36.68 ? 30  ARG   D N   1 
ATOM   4049  C  CA  . ARG   D  1 30  ? -13.717 -92.736  -50.464 1.00 33.99 ? 30  ARG   D CA  1 
ATOM   4050  C  C   . ARG   D  1 30  ? -15.064 -93.425  -50.385 1.00 34.52 ? 30  ARG   D C   1 
ATOM   4051  O  O   . ARG   D  1 30  ? -16.013 -93.000  -51.049 1.00 36.93 ? 30  ARG   D O   1 
ATOM   4052  C  CB  . ARG   D  1 30  ? -12.838 -93.318  -51.573 1.00 33.52 ? 30  ARG   D CB  1 
ATOM   4053  C  CG  . ARG   D  1 30  ? -12.029 -92.238  -52.274 1.00 38.07 ? 30  ARG   D CG  1 
ATOM   4054  C  CD  . ARG   D  1 30  ? -11.205 -91.409  -51.288 1.00 35.33 ? 30  ARG   D CD  1 
ATOM   4055  N  NE  . ARG   D  1 30  ? -10.505 -90.350  -51.997 1.00 40.21 ? 30  ARG   D NE  1 
ATOM   4056  C  CZ  . ARG   D  1 30  ? -10.290 -89.130  -51.526 1.00 38.60 ? 30  ARG   D CZ  1 
ATOM   4057  N  NH1 . ARG   D  1 30  ? -10.691 -88.768  -50.311 1.00 35.26 ? 30  ARG   D NH1 1 
ATOM   4058  N  NH2 . ARG   D  1 30  ? -9.646  -88.253  -52.289 1.00 43.88 ? 30  ARG   D NH2 1 
ATOM   4059  N  N   . MET   D  1 31  ? -15.201 -94.432  -49.529 1.00 34.90 ? 31  MET   D N   1 
ATOM   4060  C  CA  . MET   D  1 31  ? -16.536 -94.949  -49.265 1.00 37.61 ? 31  MET   D CA  1 
ATOM   4061  C  C   . MET   D  1 31  ? -17.416 -93.881  -48.626 1.00 38.55 ? 31  MET   D C   1 
ATOM   4062  O  O   . MET   D  1 31  ? -18.546 -93.638  -49.075 1.00 31.67 ? 31  MET   D O   1 
ATOM   4063  C  CB  . MET   D  1 31  ? -16.447 -96.186  -48.381 1.00 43.30 ? 31  MET   D CB  1 
ATOM   4064  C  CG  . MET   D  1 31  ? -15.846 -97.372  -49.089 1.00 46.15 ? 31  MET   D CG  1 
ATOM   4065  S  SD  . MET   D  1 31  ? -15.394 -98.686  -47.947 1.00 45.31 ? 31  MET   D SD  1 
ATOM   4066  C  CE  . MET   D  1 31  ? -17.015 -99.041  -47.302 1.00 39.92 ? 31  MET   D CE  1 
ATOM   4067  N  N   . TRP   D  1 32  ? -16.915 -93.214  -47.578 1.00 39.85 ? 32  TRP   D N   1 
ATOM   4068  C  CA  . TRP   D  1 32  ? -17.738 -92.200  -46.919 1.00 37.87 ? 32  TRP   D CA  1 
ATOM   4069  C  C   . TRP   D  1 32  ? -18.115 -91.077  -47.883 1.00 37.09 ? 32  TRP   D C   1 
ATOM   4070  O  O   . TRP   D  1 32  ? -19.258 -90.593  -47.880 1.00 34.79 ? 32  TRP   D O   1 
ATOM   4071  C  CB  . TRP   D  1 32  ? -17.010 -91.644  -45.688 1.00 36.15 ? 32  TRP   D CB  1 
ATOM   4072  C  CG  . TRP   D  1 32  ? -17.321 -92.433  -44.443 1.00 34.35 ? 32  TRP   D CG  1 
ATOM   4073  C  CD1 . TRP   D  1 32  ? -18.560 -92.861  -44.034 1.00 37.53 ? 32  TRP   D CD1 1 
ATOM   4074  C  CD2 . TRP   D  1 32  ? -16.398 -92.882  -43.445 1.00 31.37 ? 32  TRP   D CD2 1 
ATOM   4075  N  NE1 . TRP   D  1 32  ? -18.458 -93.543  -42.848 1.00 36.62 ? 32  TRP   D NE1 1 
ATOM   4076  C  CE2 . TRP   D  1 32  ? -17.142 -93.579  -42.470 1.00 32.34 ? 32  TRP   D CE2 1 
ATOM   4077  C  CE3 . TRP   D  1 32  ? -15.007 -92.764  -43.280 1.00 36.77 ? 32  TRP   D CE3 1 
ATOM   4078  C  CZ2 . TRP   D  1 32  ? -16.555 -94.147  -41.358 1.00 34.94 ? 32  TRP   D CZ2 1 
ATOM   4079  C  CZ3 . TRP   D  1 32  ? -14.429 -93.317  -42.179 1.00 36.33 ? 32  TRP   D CZ3 1 
ATOM   4080  C  CH2 . TRP   D  1 32  ? -15.200 -94.012  -41.219 1.00 40.26 ? 32  TRP   D CH2 1 
ATOM   4081  N  N   . ASN   D  1 33  ? -17.174 -90.643  -48.720 1.00 33.98 ? 33  ASN   D N   1 
ATOM   4082  C  CA  . ASN   D  1 33  ? -17.509 -89.605  -49.693 1.00 33.51 ? 33  ASN   D CA  1 
ATOM   4083  C  C   . ASN   D  1 33  ? -18.576 -90.076  -50.668 1.00 39.00 ? 33  ASN   D C   1 
ATOM   4084  O  O   . ASN   D  1 33  ? -19.533 -89.342  -50.965 1.00 36.44 ? 33  ASN   D O   1 
ATOM   4085  C  CB  . ASN   D  1 33  ? -16.267 -89.178  -50.454 1.00 34.63 ? 33  ASN   D CB  1 
ATOM   4086  C  CG  . ASN   D  1 33  ? -15.385 -88.271  -49.659 1.00 39.51 ? 33  ASN   D CG  1 
ATOM   4087  O  OD1 . ASN   D  1 33  ? -15.830 -87.588  -48.739 1.00 37.25 ? 33  ASN   D OD1 1 
ATOM   4088  N  ND2 . ASN   D  1 33  ? -14.126 -88.250  -50.013 1.00 40.09 ? 33  ASN   D ND2 1 
ATOM   4089  N  N   . ASP   D  1 34  ? -18.427 -91.297  -51.195 1.00 37.50 ? 34  ASP   D N   1 
ATOM   4090  C  CA  . ASP   D  1 34  ? -19.451 -91.826  -52.101 1.00 35.15 ? 34  ASP   D CA  1 
ATOM   4091  C  C   . ASP   D  1 34  ? -20.823 -91.853  -51.442 1.00 39.60 ? 34  ASP   D C   1 
ATOM   4092  O  O   . ASP   D  1 34  ? -21.822 -91.579  -52.111 1.00 38.01 ? 34  ASP   D O   1 
ATOM   4093  C  CB  . ASP   D  1 34  ? -19.055 -93.216  -52.605 1.00 43.84 ? 34  ASP   D CB  1 
ATOM   4094  C  CG  . ASP   D  1 34  ? -20.130 -93.862  -53.497 1.00 46.91 ? 34  ASP   D CG  1 
ATOM   4095  O  OD1 . ASP   D  1 34  ? -20.700 -93.195  -54.390 1.00 48.70 ? 34  ASP   D OD1 1 
ATOM   4096  O  OD2 . ASP   D  1 34  ? -20.388 -95.063  -53.297 1.00 47.97 ? 34  ASP   D OD2 1 
ATOM   4097  N  N   . TRP   D  1 35  ? -20.896 -92.111  -50.130 1.00 38.80 ? 35  TRP   D N   1 
ATOM   4098  C  CA  . TRP   D  1 35  ? -22.186 -92.096  -49.436 1.00 39.38 ? 35  TRP   D CA  1 
ATOM   4099  C  C   . TRP   D  1 35  ? -22.670 -90.698  -49.091 1.00 37.72 ? 35  TRP   D C   1 
ATOM   4100  O  O   . TRP   D  1 35  ? -23.755 -90.564  -48.526 1.00 34.80 ? 35  TRP   D O   1 
ATOM   4101  C  CB  . TRP   D  1 35  ? -22.129 -92.914  -48.136 1.00 40.64 ? 35  TRP   D CB  1 
ATOM   4102  C  CG  . TRP   D  1 35  ? -21.758 -94.347  -48.345 1.00 42.24 ? 35  TRP   D CG  1 
ATOM   4103  C  CD1 . TRP   D  1 35  ? -21.818 -95.029  -49.513 1.00 46.64 ? 35  TRP   D CD1 1 
ATOM   4104  C  CD2 . TRP   D  1 35  ? -21.227 -95.258  -47.372 1.00 42.26 ? 35  TRP   D CD2 1 
ATOM   4105  N  NE1 . TRP   D  1 35  ? -21.377 -96.315  -49.333 1.00 47.92 ? 35  TRP   D NE1 1 
ATOM   4106  C  CE2 . TRP   D  1 35  ? -21.014 -96.483  -48.024 1.00 37.01 ? 35  TRP   D CE2 1 
ATOM   4107  C  CE3 . TRP   D  1 35  ? -20.922 -95.158  -46.011 1.00 50.27 ? 35  TRP   D CE3 1 
ATOM   4108  C  CZ2 . TRP   D  1 35  ? -20.501 -97.601  -47.369 1.00 44.04 ? 35  TRP   D CZ2 1 
ATOM   4109  C  CZ3 . TRP   D  1 35  ? -20.418 -96.270  -45.360 1.00 48.46 ? 35  TRP   D CZ3 1 
ATOM   4110  C  CH2 . TRP   D  1 35  ? -20.207 -97.472  -46.039 1.00 44.06 ? 35  TRP   D CH2 1 
ATOM   4111  N  N   . GLY   D  1 36  ? -21.910 -89.658  -49.405 1.00 39.17 ? 36  GLY   D N   1 
ATOM   4112  C  CA  . GLY   D  1 36  ? -22.347 -88.320  -49.050 1.00 36.60 ? 36  GLY   D CA  1 
ATOM   4113  C  C   . GLY   D  1 36  ? -22.073 -87.924  -47.617 1.00 33.03 ? 36  GLY   D C   1 
ATOM   4114  O  O   . GLY   D  1 36  ? -22.676 -86.965  -47.123 1.00 39.14 ? 36  GLY   D O   1 
ATOM   4115  N  N   . LEU   D  1 37  ? -21.189 -88.637  -46.934 1.00 32.10 ? 37  LEU   D N   1 
ATOM   4116  C  CA  . LEU   D  1 37  ? -20.778 -88.297  -45.576 1.00 39.92 ? 37  LEU   D CA  1 
ATOM   4117  C  C   . LEU   D  1 37  ? -19.395 -87.646  -45.639 1.00 29.43 ? 37  LEU   D C   1 
ATOM   4118  O  O   . LEU   D  1 37  ? -18.376 -88.221  -45.246 1.00 31.24 ? 37  LEU   D O   1 
ATOM   4119  C  CB  . LEU   D  1 37  ? -20.775 -89.546  -44.698 1.00 36.06 ? 37  LEU   D CB  1 
ATOM   4120  C  CG  . LEU   D  1 37  ? -22.143 -90.231  -44.618 1.00 42.94 ? 37  LEU   D CG  1 
ATOM   4121  C  CD1 . LEU   D  1 37  ? -22.013 -91.611  -43.999 1.00 44.35 ? 37  LEU   D CD1 1 
ATOM   4122  C  CD2 . LEU   D  1 37  ? -23.081 -89.367  -43.840 1.00 36.80 ? 37  LEU   D CD2 1 
ATOM   4123  N  N   . LYS   D  1 38  ? -19.381 -86.430  -46.199 1.00 30.55 ? 38  LYS   D N   1 
ATOM   4124  C  CA  . LYS   D  1 38  ? -18.117 -85.826  -46.631 1.00 35.59 ? 38  LYS   D CA  1 
ATOM   4125  C  C   . LYS   D  1 38  ? -17.238 -85.404  -45.458 1.00 33.70 ? 38  LYS   D C   1 
ATOM   4126  O  O   . LYS   D  1 38  ? -16.008 -85.384  -45.582 1.00 35.84 ? 38  LYS   D O   1 
ATOM   4127  C  CB  . LYS   D  1 38  ? -18.386 -84.616  -47.525 1.00 40.22 ? 38  LYS   D CB  1 
ATOM   4128  C  CG  . LYS   D  1 38  ? -19.334 -84.879  -48.671 1.00 45.27 ? 38  LYS   D CG  1 
ATOM   4129  C  CD  . LYS   D  1 38  ? -18.701 -85.574  -49.837 1.00 47.13 ? 38  LYS   D CD  1 
ATOM   4130  C  CE  . LYS   D  1 38  ? -19.734 -85.707  -50.948 1.00 56.20 ? 38  LYS   D CE  1 
ATOM   4131  N  NZ  . LYS   D  1 38  ? -19.150 -85.736  -52.296 1.00 50.87 ? 38  LYS   D NZ  1 
ATOM   4132  N  N   . ARG   D  1 39  ? -17.824 -85.057  -44.321 1.00 34.33 ? 39  ARG   D N   1 
ATOM   4133  C  CA  . ARG   D  1 39  ? -16.970 -84.686  -43.200 1.00 37.62 ? 39  ARG   D CA  1 
ATOM   4134  C  C   . ARG   D  1 39  ? -16.180 -85.893  -42.714 1.00 34.78 ? 39  ARG   D C   1 
ATOM   4135  O  O   . ARG   D  1 39  ? -14.988 -85.786  -42.406 1.00 32.79 ? 39  ARG   D O   1 
ATOM   4136  C  CB  . ARG   D  1 39  ? -17.812 -84.090  -42.076 1.00 38.88 ? 39  ARG   D CB  1 
ATOM   4137  C  CG  . ARG   D  1 39  ? -16.999 -83.375  -41.022 1.00 41.28 ? 39  ARG   D CG  1 
ATOM   4138  C  CD  . ARG   D  1 39  ? -17.828 -83.154  -39.781 1.00 49.28 ? 39  ARG   D CD  1 
ATOM   4139  N  NE  . ARG   D  1 39  ? -17.276 -82.116  -38.924 1.00 61.41 ? 39  ARG   D NE  1 
ATOM   4140  C  CZ  . ARG   D  1 39  ? -17.644 -80.844  -38.962 1.00 66.72 ? 39  ARG   D CZ  1 
ATOM   4141  N  NH1 . ARG   D  1 39  ? -18.565 -80.410  -39.814 1.00 67.04 ? 39  ARG   D NH1 1 
ATOM   4142  N  NH2 . ARG   D  1 39  ? -17.078 -79.985  -38.120 1.00 61.93 ? 39  ARG   D NH2 1 
ATOM   4143  N  N   . LEU   D  1 40  ? -16.820 -87.060  -42.660 1.00 38.77 ? 40  LEU   D N   1 
ATOM   4144  C  CA  . LEU   D  1 40  ? -16.088 -88.288  -42.365 1.00 36.95 ? 40  LEU   D CA  1 
ATOM   4145  C  C   . LEU   D  1 40  ? -15.078 -88.584  -43.463 1.00 27.78 ? 40  LEU   D C   1 
ATOM   4146  O  O   . LEU   D  1 40  ? -13.916 -88.919  -43.187 1.00 36.81 ? 40  LEU   D O   1 
ATOM   4147  C  CB  . LEU   D  1 40  ? -17.084 -89.447  -42.215 1.00 35.92 ? 40  LEU   D CB  1 
ATOM   4148  C  CG  . LEU   D  1 40  ? -17.771 -89.532  -40.858 1.00 32.08 ? 40  LEU   D CG  1 
ATOM   4149  C  CD1 . LEU   D  1 40  ? -18.972 -90.449  -40.876 1.00 34.84 ? 40  LEU   D CD1 1 
ATOM   4150  C  CD2 . LEU   D  1 40  ? -16.747 -90.011  -39.834 1.00 38.32 ? 40  LEU   D CD2 1 
ATOM   4151  N  N   . GLY   D  1 41  ? -15.506 -88.442  -44.721 1.00 32.21 ? 41  GLY   D N   1 
ATOM   4152  C  CA  . GLY   D  1 41  ? -14.600 -88.673  -45.834 1.00 35.37 ? 41  GLY   D CA  1 
ATOM   4153  C  C   . GLY   D  1 41  ? -13.350 -87.824  -45.730 1.00 37.26 ? 41  GLY   D C   1 
ATOM   4154  O  O   . GLY   D  1 41  ? -12.232 -88.307  -45.923 1.00 33.71 ? 41  GLY   D O   1 
ATOM   4155  N  N   . ALA   D  1 42  ? -13.516 -86.548  -45.389 1.00 35.09 ? 42  ALA   D N   1 
ATOM   4156  C  CA  . ALA   D  1 42  ? -12.358 -85.659  -45.355 1.00 32.37 ? 42  ALA   D CA  1 
ATOM   4157  C  C   . ALA   D  1 42  ? -11.442 -86.000  -44.190 1.00 28.71 ? 42  ALA   D C   1 
ATOM   4158  O  O   . ALA   D  1 42  ? -10.215 -86.070  -44.345 1.00 35.13 ? 42  ALA   D O   1 
ATOM   4159  C  CB  . ALA   D  1 42  ? -12.836 -84.208  -45.282 1.00 36.75 ? 42  ALA   D CB  1 
ATOM   4160  N  N   . HIS   D  1 43  ? -12.019 -86.248  -43.016 1.00 29.05 ? 43  HIS   D N   1 
ATOM   4161  C  CA  . HIS   D  1 43  ? -11.193 -86.563  -41.862 1.00 33.66 ? 43  HIS   D CA  1 
ATOM   4162  C  C   . HIS   D  1 43  ? -10.424 -87.861  -42.084 1.00 30.15 ? 43  HIS   D C   1 
ATOM   4163  O  O   . HIS   D  1 43  ? -9.246  -87.969  -41.719 1.00 29.09 ? 43  HIS   D O   1 
ATOM   4164  C  CB  . HIS   D  1 43  ? -12.072 -86.644  -40.616 1.00 34.46 ? 43  HIS   D CB  1 
ATOM   4165  C  CG  . HIS   D  1 43  ? -11.287 -86.661  -39.346 1.00 43.47 ? 43  HIS   D CG  1 
ATOM   4166  N  ND1 . HIS   D  1 43  ? -10.681 -87.800  -38.860 1.00 40.74 ? 43  HIS   D ND1 1 
ATOM   4167  C  CD2 . HIS   D  1 43  ? -10.981 -85.671  -38.476 1.00 43.81 ? 43  HIS   D CD2 1 
ATOM   4168  C  CE1 . HIS   D  1 43  ? -10.037 -87.512  -37.742 1.00 40.95 ? 43  HIS   D CE1 1 
ATOM   4169  N  NE2 . HIS   D  1 43  ? -10.206 -86.227  -37.485 1.00 46.65 ? 43  HIS   D NE2 1 
ATOM   4170  N  N   . GLU   D  1 44  ? -11.086 -88.860  -42.666 1.00 31.12 ? 44  GLU   D N   1 
ATOM   4171  C  CA  . GLU   D  1 44  ? -10.465 -90.164  -42.898 1.00 32.17 ? 44  GLU   D CA  1 
ATOM   4172  C  C   . GLU   D  1 44  ? -9.362  -90.080  -43.951 1.00 30.92 ? 44  GLU   D C   1 
ATOM   4173  O  O   . GLU   D  1 44  ? -8.335  -90.764  -43.841 1.00 38.18 ? 44  GLU   D O   1 
ATOM   4174  C  CB  . GLU   D  1 44  ? -11.553 -91.163  -43.313 1.00 31.72 ? 44  GLU   D CB  1 
ATOM   4175  C  CG  . GLU   D  1 44  ? -11.074 -92.604  -43.412 1.00 36.08 ? 44  GLU   D CG  1 
ATOM   4176  C  CD  . GLU   D  1 44  ? -10.898 -93.265  -42.041 1.00 45.01 ? 44  GLU   D CD  1 
ATOM   4177  O  OE1 . GLU   D  1 44  ? -10.968 -92.566  -41.015 1.00 42.26 ? 44  GLU   D OE1 1 
ATOM   4178  O  OE2 . GLU   D  1 44  ? -10.683 -94.484  -41.985 1.00 40.44 ? 44  GLU   D OE2 1 
ATOM   4179  N  N   . TYR   D  1 45  ? -9.556  -89.228  -44.957 1.00 34.17 ? 45  TYR   D N   1 
ATOM   4180  C  CA  . TYR   D  1 45  ? -8.490  -88.892  -45.901 1.00 29.69 ? 45  TYR   D CA  1 
ATOM   4181  C  C   . TYR   D  1 45  ? -7.263  -88.349  -45.182 1.00 31.58 ? 45  TYR   D C   1 
ATOM   4182  O  O   . TYR   D  1 45  ? -6.135  -88.789  -45.437 1.00 33.75 ? 45  TYR   D O   1 
ATOM   4183  C  CB  . TYR   D  1 45  ? -9.032  -87.883  -46.917 1.00 36.69 ? 45  TYR   D CB  1 
ATOM   4184  C  CG  . TYR   D  1 45  ? -7.991  -87.278  -47.809 1.00 36.16 ? 45  TYR   D CG  1 
ATOM   4185  C  CD1 . TYR   D  1 45  ? -7.617  -87.904  -48.996 1.00 36.76 ? 45  TYR   D CD1 1 
ATOM   4186  C  CD2 . TYR   D  1 45  ? -7.397  -86.066  -47.486 1.00 37.75 ? 45  TYR   D CD2 1 
ATOM   4187  C  CE1 . TYR   D  1 45  ? -6.668  -87.355  -49.818 1.00 40.25 ? 45  TYR   D CE1 1 
ATOM   4188  C  CE2 . TYR   D  1 45  ? -6.445  -85.501  -48.317 1.00 42.05 ? 45  TYR   D CE2 1 
ATOM   4189  C  CZ  . TYR   D  1 45  ? -6.085  -86.152  -49.482 1.00 39.21 ? 45  TYR   D CZ  1 
ATOM   4190  O  OH  . TYR   D  1 45  ? -5.117  -85.602  -50.308 1.00 41.47 ? 45  TYR   D OH  1 
ATOM   4191  N  N   . HIS   D  1 46  ? -7.459  -87.411  -44.248 1.00 32.22 ? 46  HIS   D N   1 
ATOM   4192  C  CA  . HIS   D  1 46  ? -6.304  -86.827  -43.567 1.00 35.44 ? 46  HIS   D CA  1 
ATOM   4193  C  C   . HIS   D  1 46  ? -5.619  -87.844  -42.658 1.00 35.71 ? 46  HIS   D C   1 
ATOM   4194  O  O   . HIS   D  1 46  ? -4.394  -87.781  -42.462 1.00 32.30 ? 46  HIS   D O   1 
ATOM   4195  C  CB  . HIS   D  1 46  ? -6.742  -85.565  -42.812 1.00 37.10 ? 46  HIS   D CB  1 
ATOM   4196  C  CG  . HIS   D  1 46  ? -7.039  -84.411  -43.727 1.00 44.96 ? 46  HIS   D CG  1 
ATOM   4197  N  ND1 . HIS   D  1 46  ? -8.316  -83.927  -43.935 1.00 51.95 ? 46  HIS   D ND1 1 
ATOM   4198  C  CD2 . HIS   D  1 46  ? -6.227  -83.684  -44.534 1.00 46.01 ? 46  HIS   D CD2 1 
ATOM   4199  C  CE1 . HIS   D  1 46  ? -8.276  -82.939  -44.812 1.00 41.30 ? 46  HIS   D CE1 1 
ATOM   4200  N  NE2 . HIS   D  1 46  ? -7.021  -82.774  -45.196 1.00 53.18 ? 46  HIS   D NE2 1 
ATOM   4201  N  N   . GLU   D  1 47  ? -6.376  -88.807  -42.128 1.00 34.34 ? 47  GLU   D N   1 
ATOM   4202  C  CA  . GLU   D  1 47  ? -5.758  -89.912  -41.403 1.00 35.83 ? 47  GLU   D CA  1 
ATOM   4203  C  C   . GLU   D  1 47  ? -4.908  -90.764  -42.334 1.00 31.71 ? 47  GLU   D C   1 
ATOM   4204  O  O   . GLU   D  1 47  ? -3.788  -91.154  -41.982 1.00 35.80 ? 47  GLU   D O   1 
ATOM   4205  C  CB  . GLU   D  1 47  ? -6.828  -90.766  -40.736 1.00 35.09 ? 47  GLU   D CB  1 
ATOM   4206  C  CG  . GLU   D  1 47  ? -7.696  -90.019  -39.729 1.00 40.10 ? 47  GLU   D CG  1 
ATOM   4207  C  CD  . GLU   D  1 47  ? -6.988  -89.769  -38.427 1.00 44.41 ? 47  GLU   D CD  1 
ATOM   4208  O  OE1 . GLU   D  1 47  ? -5.809  -90.129  -38.311 1.00 50.45 ? 47  GLU   D OE1 1 
ATOM   4209  O  OE2 . GLU   D  1 47  ? -7.625  -89.237  -37.495 1.00 57.34 ? 47  GLU   D OE2 1 
ATOM   4210  N  N   . SER   D  1 48  ? -5.419  -91.048  -43.535 1.00 35.43 ? 48  SER   D N   1 
ATOM   4211  C  CA  . SER   D  1 48  ? -4.609  -91.750  -44.528 1.00 32.71 ? 48  SER   D CA  1 
ATOM   4212  C  C   . SER   D  1 48  ? -3.337  -90.972  -44.835 1.00 35.19 ? 48  SER   D C   1 
ATOM   4213  O  O   . SER   D  1 48  ? -2.238  -91.532  -44.843 1.00 35.18 ? 48  SER   D O   1 
ATOM   4214  C  CB  . SER   D  1 48  ? -5.425  -92.005  -45.809 1.00 33.92 ? 48  SER   D CB  1 
ATOM   4215  O  OG  . SER   D  1 48  ? -4.740  -92.921  -46.665 1.00 37.29 ? 48  SER   D OG  1 
ATOM   4216  N  N   . ILE   D  1 49  ? -3.461  -89.673  -45.100 1.00 40.94 ? 49  ILE   D N   1 
ATOM   4217  C  CA  . ILE   D  1 49  ? -2.266  -88.872  -45.370 1.00 39.47 ? 49  ILE   D CA  1 
ATOM   4218  C  C   . ILE   D  1 49  ? -1.284  -88.978  -44.210 1.00 33.76 ? 49  ILE   D C   1 
ATOM   4219  O  O   . ILE   D  1 49  ? -0.068  -89.111  -44.407 1.00 33.67 ? 49  ILE   D O   1 
ATOM   4220  C  CB  . ILE   D  1 49  ? -2.662  -87.408  -45.644 1.00 39.42 ? 49  ILE   D CB  1 
ATOM   4221  C  CG1 . ILE   D  1 49  ? -3.526  -87.326  -46.898 1.00 30.77 ? 49  ILE   D CG1 1 
ATOM   4222  C  CG2 . ILE   D  1 49  ? -1.411  -86.538  -45.754 1.00 37.89 ? 49  ILE   D CG2 1 
ATOM   4223  C  CD1 . ILE   D  1 49  ? -2.774  -87.682  -48.183 1.00 38.95 ? 49  ILE   D CD1 1 
ATOM   4224  N  N   . ASP   D  1 50  ? -1.807  -88.947  -42.981 1.00 32.64 ? 50  ASP   D N   1 
ATOM   4225  C  CA  . ASP   D  1 50  ? -0.970  -89.040  -41.786 1.00 42.97 ? 50  ASP   D CA  1 
ATOM   4226  C  C   . ASP   D  1 50  ? -0.131  -90.310  -41.782 1.00 35.14 ? 50  ASP   D C   1 
ATOM   4227  O  O   . ASP   D  1 50  ? 1.064   -90.287  -41.451 1.00 32.35 ? 50  ASP   D O   1 
ATOM   4228  C  CB  . ASP   D  1 50  ? -1.864  -89.017  -40.550 1.00 46.43 ? 50  ASP   D CB  1 
ATOM   4229  C  CG  . ASP   D  1 50  ? -1.591  -87.852  -39.669 1.00 57.52 ? 50  ASP   D CG  1 
ATOM   4230  O  OD1 . ASP   D  1 50  ? -0.474  -87.803  -39.108 1.00 57.54 ? 50  ASP   D OD1 1 
ATOM   4231  O  OD2 . ASP   D  1 50  ? -2.495  -86.993  -39.540 1.00 60.82 ? 50  ASP   D OD2 1 
ATOM   4232  N  N   . GLU   D  1 51  ? -0.771  -91.442  -42.077 1.00 33.82 ? 51  GLU   D N   1 
ATOM   4233  C  CA  . GLU   D  1 51  ? -0.069  -92.719  -42.109 1.00 35.94 ? 51  GLU   D CA  1 
ATOM   4234  C  C   . GLU   D  1 51  ? 0.938   -92.763  -43.254 1.00 31.92 ? 51  GLU   D C   1 
ATOM   4235  O  O   . GLU   D  1 51  ? 2.026   -93.315  -43.096 1.00 39.46 ? 51  GLU   D O   1 
ATOM   4236  C  CB  . GLU   D  1 51  ? -1.081  -93.859  -42.225 1.00 30.11 ? 51  GLU   D CB  1 
ATOM   4237  C  CG  . GLU   D  1 51  ? -2.034  -93.908  -41.073 1.00 40.91 ? 51  GLU   D CG  1 
ATOM   4238  C  CD  . GLU   D  1 51  ? -1.308  -94.039  -39.735 1.00 45.65 ? 51  GLU   D CD  1 
ATOM   4239  O  OE1 . GLU   D  1 51  ? -0.868  -95.150  -39.405 1.00 59.30 ? 51  GLU   D OE1 1 
ATOM   4240  O  OE2 . GLU   D  1 51  ? -1.155  -93.030  -39.024 1.00 47.36 ? 51  GLU   D OE2 1 
ATOM   4241  N  N   . MET   D  1 52  ? 0.603   -92.159  -44.400 1.00 35.18 ? 52  MET   D N   1 
ATOM   4242  C  CA  . MET   D  1 52  ? 1.588   -92.006  -45.468 1.00 34.69 ? 52  MET   D CA  1 
ATOM   4243  C  C   . MET   D  1 52  ? 2.823   -91.254  -44.998 1.00 35.53 ? 52  MET   D C   1 
ATOM   4244  O  O   . MET   D  1 52  ? 3.949   -91.638  -45.326 1.00 34.11 ? 52  MET   D O   1 
ATOM   4245  C  CB  . MET   D  1 52  ? 0.967   -91.293  -46.655 1.00 36.40 ? 52  MET   D CB  1 
ATOM   4246  C  CG  . MET   D  1 52  ? -0.126  -92.075  -47.343 1.00 29.77 ? 52  MET   D CG  1 
ATOM   4247  S  SD  . MET   D  1 52  ? -0.963  -90.985  -48.518 1.00 37.44 ? 52  MET   D SD  1 
ATOM   4248  C  CE  . MET   D  1 52  ? -2.600  -91.680  -48.647 1.00 35.64 ? 52  MET   D CE  1 
ATOM   4249  N  N   . LYS   D  1 53  ? 2.648   -90.180  -44.221 1.00 38.62 ? 53  LYS   D N   1 
ATOM   4250  C  CA  . LYS   D  1 53  ? 3.830   -89.461  -43.761 1.00 30.83 ? 53  LYS   D CA  1 
ATOM   4251  C  C   . LYS   D  1 53  ? 4.641   -90.314  -42.781 1.00 30.64 ? 53  LYS   D C   1 
ATOM   4252  O  O   . LYS   D  1 53  ? 5.878   -90.295  -42.820 1.00 34.90 ? 53  LYS   D O   1 
ATOM   4253  C  CB  . LYS   D  1 53  ? 3.456   -88.129  -43.121 1.00 37.46 ? 53  LYS   D CB  1 
ATOM   4254  C  CG  . LYS   D  1 53  ? 2.933   -87.061  -44.110 1.00 42.01 ? 53  LYS   D CG  1 
ATOM   4255  C  CD  . LYS   D  1 53  ? 2.736   -85.708  -43.394 1.00 45.69 ? 53  LYS   D CD  1 
ATOM   4256  C  CE  . LYS   D  1 53  ? 1.689   -84.815  -44.070 1.00 53.42 ? 53  LYS   D CE  1 
ATOM   4257  N  NZ  . LYS   D  1 53  ? 1.477   -83.516  -43.328 1.00 54.55 ? 53  LYS   D NZ  1 
ATOM   4258  N  N   . HIS   D  1 54  ? 3.964   -91.068  -41.903 1.00 32.79 ? 54  HIS   D N   1 
ATOM   4259  C  CA  . HIS   D  1 54  ? 4.671   -91.975  -40.988 1.00 36.69 ? 54  HIS   D CA  1 
ATOM   4260  C  C   . HIS   D  1 54  ? 5.433   -93.034  -41.766 1.00 38.50 ? 54  HIS   D C   1 
ATOM   4261  O  O   . HIS   D  1 54  ? 6.603   -93.314  -41.483 1.00 33.91 ? 54  HIS   D O   1 
ATOM   4262  C  CB  . HIS   D  1 54  ? 3.693   -92.658  -40.022 1.00 39.02 ? 54  HIS   D CB  1 
ATOM   4263  C  CG  . HIS   D  1 54  ? 2.930   -91.709  -39.153 1.00 35.47 ? 54  HIS   D CG  1 
ATOM   4264  N  ND1 . HIS   D  1 54  ? 1.609   -91.907  -38.804 1.00 46.55 ? 54  HIS   D ND1 1 
ATOM   4265  C  CD2 . HIS   D  1 54  ? 3.314   -90.563  -38.541 1.00 35.67 ? 54  HIS   D CD2 1 
ATOM   4266  C  CE1 . HIS   D  1 54  ? 1.205   -90.907  -38.039 1.00 37.69 ? 54  HIS   D CE1 1 
ATOM   4267  N  NE2 . HIS   D  1 54  ? 2.218   -90.075  -37.871 1.00 41.14 ? 54  HIS   D NE2 1 
ATOM   4268  N  N   . ALA   D  1 55  ? 4.776   -93.638  -42.757 1.00 34.63 ? 55  ALA   D N   1 
ATOM   4269  C  CA  . ALA   D  1 55  ? 5.454   -94.606  -43.617 1.00 40.20 ? 55  ALA   D CA  1 
ATOM   4270  C  C   . ALA   D  1 55  ? 6.708   -94.003  -44.230 1.00 34.39 ? 55  ALA   D C   1 
ATOM   4271  O  O   . ALA   D  1 55  ? 7.786   -94.610  -44.227 1.00 41.19 ? 55  ALA   D O   1 
ATOM   4272  C  CB  . ALA   D  1 55  ? 4.496   -95.068  -44.715 1.00 33.17 ? 55  ALA   D CB  1 
ATOM   4273  N  N   . ASP   D  1 56  ? 6.577   -92.797  -44.773 1.00 35.51 ? 56  ASP   D N   1 
ATOM   4274  C  CA  . ASP   D  1 56  ? 7.719   -92.132  -45.370 1.00 31.24 ? 56  ASP   D CA  1 
ATOM   4275  C  C   . ASP   D  1 56  ? 8.865   -92.049  -44.365 1.00 37.27 ? 56  ASP   D C   1 
ATOM   4276  O  O   . ASP   D  1 56  ? 9.995   -92.434  -44.665 1.00 31.86 ? 56  ASP   D O   1 
ATOM   4277  C  CB  . ASP   D  1 56  ? 7.286   -90.752  -45.877 1.00 36.69 ? 56  ASP   D CB  1 
ATOM   4278  C  CG  . ASP   D  1 56  ? 8.388   -90.005  -46.584 1.00 37.45 ? 56  ASP   D CG  1 
ATOM   4279  O  OD1 . ASP   D  1 56  ? 9.393   -90.633  -46.986 1.00 34.02 ? 56  ASP   D OD1 1 
ATOM   4280  O  OD2 . ASP   D  1 56  ? 8.235   -88.769  -46.749 1.00 40.86 ? 56  ASP   D OD2 1 
ATOM   4281  N  N   . LYS   D  1 57  ? 8.582   -91.611  -43.138 1.00 33.23 ? 57  LYS   D N   1 
ATOM   4282  C  CA  . LYS   D  1 57  ? 9.674   -91.499  -42.174 1.00 33.43 ? 57  LYS   D CA  1 
ATOM   4283  C  C   . LYS   D  1 57  ? 10.245  -92.871  -41.803 1.00 35.42 ? 57  LYS   D C   1 
ATOM   4284  O  O   . LYS   D  1 57  ? 11.447  -92.991  -41.570 1.00 31.81 ? 57  LYS   D O   1 
ATOM   4285  C  CB  . LYS   D  1 57  ? 9.214   -90.763  -40.917 1.00 36.90 ? 57  LYS   D CB  1 
ATOM   4286  C  CG  . LYS   D  1 57  ? 8.749   -89.335  -41.135 1.00 38.31 ? 57  LYS   D CG  1 
ATOM   4287  C  CD  . LYS   D  1 57  ? 9.892   -88.383  -41.333 1.00 44.74 ? 57  LYS   D CD  1 
ATOM   4288  N  N   . LEU   D  1 58  ? 9.416   -93.916  -41.740 1.00 31.71 ? 58  LEU   D N   1 
ATOM   4289  C  CA  . LEU   D  1 58  ? 9.961   -95.242  -41.440 1.00 35.62 ? 58  LEU   D CA  1 
ATOM   4290  C  C   . LEU   D  1 58  ? 10.847  -95.739  -42.581 1.00 32.01 ? 58  LEU   D C   1 
ATOM   4291  O  O   . LEU   D  1 58  ? 11.966  -96.224  -42.351 1.00 32.91 ? 58  LEU   D O   1 
ATOM   4292  C  CB  . LEU   D  1 58  ? 8.820   -96.221  -41.170 1.00 37.39 ? 58  LEU   D CB  1 
ATOM   4293  C  CG  . LEU   D  1 58  ? 8.078   -96.020  -39.841 1.00 36.42 ? 58  LEU   D CG  1 
ATOM   4294  C  CD1 . LEU   D  1 58  ? 6.752   -96.718  -39.899 1.00 36.68 ? 58  LEU   D CD1 1 
ATOM   4295  C  CD2 . LEU   D  1 58  ? 8.882   -96.512  -38.634 1.00 36.94 ? 58  LEU   D CD2 1 
ATOM   4296  N  N   . ILE   D  1 59  ? 10.365  -95.604  -43.823 1.00 40.90 ? 59  ILE   D N   1 
ATOM   4297  C  CA  . ILE   D  1 59  ? 11.178  -95.939  -44.998 1.00 33.27 ? 59  ILE   D CA  1 
ATOM   4298  C  C   . ILE   D  1 59  ? 12.524  -95.245  -44.929 1.00 38.48 ? 59  ILE   D C   1 
ATOM   4299  O  O   . ILE   D  1 59  ? 13.576  -95.873  -45.110 1.00 38.49 ? 59  ILE   D O   1 
ATOM   4300  C  CB  . ILE   D  1 59  ? 10.433  -95.588  -46.298 1.00 34.77 ? 59  ILE   D CB  1 
ATOM   4301  C  CG1 . ILE   D  1 59  ? 9.310   -96.581  -46.502 1.00 33.68 ? 59  ILE   D CG1 1 
ATOM   4302  C  CG2 . ILE   D  1 59  ? 11.395  -95.635  -47.488 1.00 40.26 ? 59  ILE   D CG2 1 
ATOM   4303  C  CD1 . ILE   D  1 59  ? 8.154   -96.096  -47.344 1.00 38.70 ? 59  ILE   D CD1 1 
ATOM   4304  N  N   . GLU   D  1 60  ? 12.514  -93.941  -44.640 1.00 40.93 ? 60  GLU   D N   1 
ATOM   4305  C  CA  . GLU   D  1 60  ? 13.765  -93.183  -44.590 1.00 34.45 ? 60  GLU   D CA  1 
ATOM   4306  C  C   . GLU   D  1 60  ? 14.681  -93.669  -43.466 1.00 34.82 ? 60  GLU   D C   1 
ATOM   4307  O  O   . GLU   D  1 60  ? 15.898  -93.769  -43.647 1.00 31.27 ? 60  GLU   D O   1 
ATOM   4308  C  CB  . GLU   D  1 60  ? 13.465  -91.688  -44.426 1.00 39.07 ? 60  GLU   D CB  1 
ATOM   4309  C  CG  . GLU   D  1 60  ? 12.660  -91.082  -45.598 1.00 45.23 ? 60  GLU   D CG  1 
ATOM   4310  C  CD  . GLU   D  1 60  ? 12.246  -89.618  -45.379 1.00 46.81 ? 60  GLU   D CD  1 
ATOM   4311  O  OE1 . GLU   D  1 60  ? 11.776  -89.280  -44.270 1.00 41.01 ? 60  GLU   D OE1 1 
ATOM   4312  O  OE2 . GLU   D  1 60  ? 12.381  -88.813  -46.331 1.00 36.09 ? 60  GLU   D OE2 1 
ATOM   4313  N  N   . ARG   D  1 61  ? 14.130  -93.951  -42.290 1.00 35.83 ? 61  ARG   D N   1 
ATOM   4314  C  CA  . ARG   D  1 61  ? 14.977  -94.427  -41.195 1.00 37.79 ? 61  ARG   D CA  1 
ATOM   4315  C  C   . ARG   D  1 61  ? 15.608  -95.787  -41.541 1.00 31.74 ? 61  ARG   D C   1 
ATOM   4316  O  O   . ARG   D  1 61  ? 16.793  -96.027  -41.279 1.00 37.32 ? 61  ARG   D O   1 
ATOM   4317  C  CB  . ARG   D  1 61  ? 14.126  -94.508  -39.922 1.00 31.33 ? 61  ARG   D CB  1 
ATOM   4318  C  CG  . ARG   D  1 61  ? 14.850  -94.896  -38.633 1.00 35.07 ? 61  ARG   D CG  1 
ATOM   4319  C  CD  . ARG   D  1 61  ? 15.835  -93.833  -38.215 1.00 37.57 ? 61  ARG   D CD  1 
ATOM   4320  N  NE  . ARG   D  1 61  ? 16.588  -94.203  -37.025 1.00 35.02 ? 61  ARG   D NE  1 
ATOM   4321  C  CZ  . ARG   D  1 61  ? 17.710  -93.609  -36.640 1.00 39.67 ? 61  ARG   D CZ  1 
ATOM   4322  N  NH1 . ARG   D  1 61  ? 18.164  -92.522  -37.237 1.00 39.78 ? 61  ARG   D NH1 1 
ATOM   4323  N  NH2 . ARG   D  1 61  ? 18.418  -94.139  -35.651 1.00 44.03 ? 61  ARG   D NH2 1 
ATOM   4324  N  N   . ILE   D  1 62  ? 14.821  -96.678  -42.139 1.00 37.21 ? 62  ILE   D N   1 
ATOM   4325  C  CA  . ILE   D  1 62  ? 15.299  -98.023  -42.448 1.00 41.46 ? 62  ILE   D CA  1 
ATOM   4326  C  C   . ILE   D  1 62  ? 16.435  -97.959  -43.455 1.00 46.69 ? 62  ILE   D C   1 
ATOM   4327  O  O   . ILE   D  1 62  ? 17.466  -98.625  -43.299 1.00 40.64 ? 62  ILE   D O   1 
ATOM   4328  C  CB  . ILE   D  1 62  ? 14.140  -98.900  -42.960 1.00 36.42 ? 62  ILE   D CB  1 
ATOM   4329  C  CG1 . ILE   D  1 62  ? 13.154  -99.159  -41.836 1.00 34.26 ? 62  ILE   D CG1 1 
ATOM   4330  C  CG2 . ILE   D  1 62  ? 14.689  -100.232 -43.537 1.00 43.53 ? 62  ILE   D CG2 1 
ATOM   4331  C  CD1 . ILE   D  1 62  ? 11.870  -99.812  -42.237 1.00 34.53 ? 62  ILE   D CD1 1 
ATOM   4332  N  N   . LEU   D  1 63  ? 16.260  -97.162  -44.514 1.00 41.08 ? 63  LEU   D N   1 
ATOM   4333  C  CA  . LEU   D  1 63  ? 17.337  -97.005  -45.482 1.00 40.46 ? 63  LEU   D CA  1 
ATOM   4334  C  C   . LEU   D  1 63  ? 18.576  -96.446  -44.816 1.00 37.76 ? 63  LEU   D C   1 
ATOM   4335  O  O   . LEU   D  1 63  ? 19.699  -96.884  -45.104 1.00 41.61 ? 63  LEU   D O   1 
ATOM   4336  C  CB  . LEU   D  1 63  ? 16.891  -96.101  -46.638 1.00 38.11 ? 63  LEU   D CB  1 
ATOM   4337  C  CG  . LEU   D  1 63  ? 15.771  -96.640  -47.505 1.00 39.94 ? 63  LEU   D CG  1 
ATOM   4338  C  CD1 . LEU   D  1 63  ? 15.275  -95.542  -48.429 1.00 41.61 ? 63  LEU   D CD1 1 
ATOM   4339  C  CD2 . LEU   D  1 63  ? 16.273  -97.818  -48.308 1.00 43.80 ? 63  LEU   D CD2 1 
ATOM   4340  N  N   . PHE   D  1 64  ? 18.399  -95.480  -43.911 1.00 36.63 ? 64  PHE   D N   1 
ATOM   4341  C  CA  . PHE   D  1 64  ? 19.549  -94.936  -43.189 1.00 39.14 ? 64  PHE   D CA  1 
ATOM   4342  C  C   . PHE   D  1 64  ? 20.265  -96.011  -42.376 1.00 37.11 ? 64  PHE   D C   1 
ATOM   4343  O  O   . PHE   D  1 64  ? 21.499  -96.026  -42.306 1.00 35.94 ? 64  PHE   D O   1 
ATOM   4344  C  CB  . PHE   D  1 64  ? 19.118  -93.803  -42.258 1.00 37.52 ? 64  PHE   D CB  1 
ATOM   4345  C  CG  . PHE   D  1 64  ? 20.207  -93.341  -41.346 1.00 31.70 ? 64  PHE   D CG  1 
ATOM   4346  C  CD1 . PHE   D  1 64  ? 21.325  -92.717  -41.848 1.00 32.79 ? 64  PHE   D CD1 1 
ATOM   4347  C  CD2 . PHE   D  1 64  ? 20.110  -93.543  -39.985 1.00 36.74 ? 64  PHE   D CD2 1 
ATOM   4348  C  CE1 . PHE   D  1 64  ? 22.334  -92.318  -41.008 1.00 38.67 ? 64  PHE   D CE1 1 
ATOM   4349  C  CE2 . PHE   D  1 64  ? 21.111  -93.134  -39.132 1.00 39.26 ? 64  PHE   D CE2 1 
ATOM   4350  C  CZ  . PHE   D  1 64  ? 22.211  -92.519  -39.630 1.00 39.81 ? 64  PHE   D CZ  1 
ATOM   4351  N  N   . LEU   D  1 65  ? 19.511  -96.894  -41.727 1.00 36.71 ? 65  LEU   D N   1 
ATOM   4352  C  CA  . LEU   D  1 65  ? 20.129  -97.991  -40.992 1.00 42.61 ? 65  LEU   D CA  1 
ATOM   4353  C  C   . LEU   D  1 65  ? 20.614  -99.117  -41.920 1.00 48.44 ? 65  LEU   D C   1 
ATOM   4354  O  O   . LEU   D  1 65  ? 20.975  -100.194 -41.430 1.00 43.79 ? 65  LEU   D O   1 
ATOM   4355  C  CB  . LEU   D  1 65  ? 19.152  -98.543  -39.957 1.00 34.64 ? 65  LEU   D CB  1 
ATOM   4356  C  CG  . LEU   D  1 65  ? 18.648  -97.502  -38.942 1.00 39.56 ? 65  LEU   D CG  1 
ATOM   4357  C  CD1 . LEU   D  1 65  ? 17.578  -98.063  -38.021 1.00 40.66 ? 65  LEU   D CD1 1 
ATOM   4358  C  CD2 . LEU   D  1 65  ? 19.769  -96.949  -38.144 1.00 34.46 ? 65  LEU   D CD2 1 
ATOM   4359  N  N   . GLU   D  1 66  ? 20.602  -98.884  -43.237 1.00 47.27 ? 66  GLU   D N   1 
ATOM   4360  C  CA  . GLU   D  1 66  ? 21.091  -99.834  -44.242 1.00 39.52 ? 66  GLU   D CA  1 
ATOM   4361  C  C   . GLU   D  1 66  ? 20.292  -101.126 -44.205 1.00 44.82 ? 66  GLU   D C   1 
ATOM   4362  O  O   . GLU   D  1 66  ? 20.817  -102.212 -44.440 1.00 48.99 ? 66  GLU   D O   1 
ATOM   4363  C  CB  . GLU   D  1 66  ? 22.590  -100.103 -44.086 1.00 38.99 ? 66  GLU   D CB  1 
ATOM   4364  C  CG  . GLU   D  1 66  ? 23.398  -98.819  -43.860 1.00 43.01 ? 66  GLU   D CG  1 
ATOM   4365  C  CD  . GLU   D  1 66  ? 24.882  -99.008  -43.983 1.00 41.78 ? 66  GLU   D CD  1 
ATOM   4366  O  OE1 . GLU   D  1 66  ? 25.307  -99.999  -44.608 1.00 50.79 ? 66  GLU   D OE1 1 
ATOM   4367  O  OE2 . GLU   D  1 66  ? 25.640  -98.157  -43.451 1.00 44.23 ? 66  GLU   D OE2 1 
ATOM   4368  N  N   . GLY   D  1 67  ? 19.004  -101.006 -43.895 1.00 34.26 ? 67  GLY   D N   1 
ATOM   4369  C  CA  . GLY   D  1 67  ? 18.071  -102.090 -44.056 1.00 40.53 ? 67  GLY   D CA  1 
ATOM   4370  C  C   . GLY   D  1 67  ? 17.290  -101.930 -45.349 1.00 41.59 ? 67  GLY   D C   1 
ATOM   4371  O  O   . GLY   D  1 67  ? 17.432  -100.953 -46.073 1.00 42.33 ? 67  GLY   D O   1 
ATOM   4372  N  N   . LEU   D  1 68  ? 16.442  -102.921 -45.614 1.00 46.33 ? 68  LEU   D N   1 
ATOM   4373  C  CA  . LEU   D  1 68  ? 15.588  -102.947 -46.795 1.00 48.18 ? 68  LEU   D CA  1 
ATOM   4374  C  C   . LEU   D  1 68  ? 14.130  -102.754 -46.401 1.00 40.19 ? 68  LEU   D C   1 
ATOM   4375  O  O   . LEU   D  1 68  ? 13.552  -103.641 -45.754 1.00 39.45 ? 68  LEU   D O   1 
ATOM   4376  C  CB  . LEU   D  1 68  ? 15.766  -104.269 -47.547 1.00 50.62 ? 68  LEU   D CB  1 
ATOM   4377  C  CG  . LEU   D  1 68  ? 16.974  -104.257 -48.490 1.00 63.09 ? 68  LEU   D CG  1 
ATOM   4378  C  CD1 . LEU   D  1 68  ? 17.892  -105.466 -48.271 1.00 62.77 ? 68  LEU   D CD1 1 
ATOM   4379  C  CD2 . LEU   D  1 68  ? 16.500  -104.162 -49.947 1.00 62.65 ? 68  LEU   D CD2 1 
ATOM   4380  N  N   . PRO   D  1 69  ? 13.489  -101.636 -46.767 1.00 42.26 ? 69  PRO   D N   1 
ATOM   4381  C  CA  . PRO   D  1 69  ? 12.082  -101.432 -46.386 1.00 37.24 ? 69  PRO   D CA  1 
ATOM   4382  C  C   . PRO   D  1 69  ? 11.171  -102.374 -47.149 1.00 41.18 ? 69  PRO   D C   1 
ATOM   4383  O  O   . PRO   D  1 69  ? 11.266  -102.498 -48.370 1.00 48.10 ? 69  PRO   D O   1 
ATOM   4384  C  CB  . PRO   D  1 69  ? 11.806  -99.967  -46.763 1.00 44.21 ? 69  PRO   D CB  1 
ATOM   4385  C  CG  . PRO   D  1 69  ? 13.099  -99.368  -47.127 1.00 45.21 ? 69  PRO   D CG  1 
ATOM   4386  C  CD  . PRO   D  1 69  ? 14.054  -100.464 -47.452 1.00 42.52 ? 69  PRO   D CD  1 
ATOM   4387  N  N   . ASN   D  1 70  ? 10.261  -103.009 -46.424 1.00 43.96 ? 70  ASN   D N   1 
ATOM   4388  C  CA  . ASN   D  1 70  ? 9.304   -103.930 -47.022 1.00 44.39 ? 70  ASN   D CA  1 
ATOM   4389  C  C   . ASN   D  1 70  ? 8.055   -103.157 -47.418 1.00 43.60 ? 70  ASN   D C   1 
ATOM   4390  O  O   . ASN   D  1 70  ? 7.210   -102.857 -46.573 1.00 40.15 ? 70  ASN   D O   1 
ATOM   4391  C  CB  . ASN   D  1 70  ? 8.965   -105.048 -46.042 1.00 49.63 ? 70  ASN   D CB  1 
ATOM   4392  C  CG  . ASN   D  1 70  ? 8.079   -106.119 -46.652 1.00 49.02 ? 70  ASN   D CG  1 
ATOM   4393  O  OD1 . ASN   D  1 70  ? 7.462   -105.921 -47.701 1.00 48.47 ? 70  ASN   D OD1 1 
ATOM   4394  N  ND2 . ASN   D  1 70  ? 7.990   -107.261 -45.975 1.00 57.62 ? 70  ASN   D ND2 1 
ATOM   4395  N  N   . LEU   D  1 71  ? 7.906   -102.862 -48.712 1.00 38.67 ? 71  LEU   D N   1 
ATOM   4396  C  CA  . LEU   D  1 71  ? 6.623   -102.385 -49.225 1.00 44.06 ? 71  LEU   D CA  1 
ATOM   4397  C  C   . LEU   D  1 71  ? 5.905   -103.447 -50.038 1.00 42.70 ? 71  LEU   D C   1 
ATOM   4398  O  O   . LEU   D  1 71  ? 4.864   -103.156 -50.639 1.00 46.10 ? 71  LEU   D O   1 
ATOM   4399  C  CB  . LEU   D  1 71  ? 6.802   -101.123 -50.070 1.00 40.15 ? 71  LEU   D CB  1 
ATOM   4400  C  CG  . LEU   D  1 71  ? 7.073   -99.832  -49.291 1.00 47.58 ? 71  LEU   D CG  1 
ATOM   4401  C  CD1 . LEU   D  1 71  ? 8.544   -99.801  -48.852 1.00 46.80 ? 71  LEU   D CD1 1 
ATOM   4402  C  CD2 . LEU   D  1 71  ? 6.750   -98.593  -50.111 1.00 52.59 ? 71  LEU   D CD2 1 
ATOM   4403  N  N   . GLN   D  1 72  ? 6.435   -104.673 -50.066 1.00 44.55 ? 72  GLN   D N   1 
ATOM   4404  C  CA  . GLN   D  1 72  ? 5.843   -105.752 -50.855 1.00 46.22 ? 72  GLN   D CA  1 
ATOM   4405  C  C   . GLN   D  1 72  ? 4.727   -106.468 -50.103 1.00 42.94 ? 72  GLN   D C   1 
ATOM   4406  O  O   . GLN   D  1 72  ? 3.733   -106.882 -50.713 1.00 46.38 ? 72  GLN   D O   1 
ATOM   4407  C  CB  . GLN   D  1 72  ? 6.934   -106.760 -51.242 1.00 45.86 ? 72  GLN   D CB  1 
ATOM   4408  C  CG  . GLN   D  1 72  ? 6.427   -107.909 -52.059 1.00 41.29 ? 72  GLN   D CG  1 
ATOM   4409  C  CD  . GLN   D  1 72  ? 5.951   -107.446 -53.407 1.00 38.09 ? 72  GLN   D CD  1 
ATOM   4410  O  OE1 . GLN   D  1 72  ? 6.761   -107.237 -54.309 1.00 46.51 ? 72  GLN   D OE1 1 
ATOM   4411  N  NE2 . GLN   D  1 72  ? 4.648   -107.250 -53.547 1.00 41.32 ? 72  GLN   D NE2 1 
ATOM   4412  N  N   . ASP   D  1 73  ? 4.860   -106.603 -48.787 1.00 52.25 ? 73  ASP   D N   1 
ATOM   4413  C  CA  . ASP   D  1 73  ? 3.995   -107.468 -47.996 1.00 54.83 ? 73  ASP   D CA  1 
ATOM   4414  C  C   . ASP   D  1 73  ? 2.912   -106.639 -47.326 1.00 44.53 ? 73  ASP   D C   1 
ATOM   4415  O  O   . ASP   D  1 73  ? 3.188   -105.824 -46.441 1.00 53.97 ? 73  ASP   D O   1 
ATOM   4416  C  CB  . ASP   D  1 73  ? 4.818   -108.263 -46.984 1.00 50.21 ? 73  ASP   D CB  1 
ATOM   4417  C  CG  . ASP   D  1 73  ? 5.547   -109.414 -47.640 1.00 51.51 ? 73  ASP   D CG  1 
ATOM   4418  O  OD1 . ASP   D  1 73  ? 4.997   -109.961 -48.623 1.00 57.06 ? 73  ASP   D OD1 1 
ATOM   4419  O  OD2 . ASP   D  1 73  ? 6.659   -109.761 -47.206 1.00 48.47 ? 73  ASP   D OD2 1 
ATOM   4420  N  N   . LEU   D  1 74  ? 1.682   -106.876 -47.749 1.00 44.32 ? 74  LEU   D N   1 
ATOM   4421  C  CA  . LEU   D  1 74  ? 0.517   -106.127 -47.325 1.00 42.05 ? 74  LEU   D CA  1 
ATOM   4422  C  C   . LEU   D  1 74  ? -0.385  -107.076 -46.556 1.00 50.87 ? 74  LEU   D C   1 
ATOM   4423  O  O   . LEU   D  1 74  ? -0.796  -108.108 -47.094 1.00 46.93 ? 74  LEU   D O   1 
ATOM   4424  C  CB  . LEU   D  1 74  ? -0.223  -105.545 -48.530 1.00 44.13 ? 74  LEU   D CB  1 
ATOM   4425  C  CG  . LEU   D  1 74  ? -1.483  -104.735 -48.213 1.00 45.36 ? 74  LEU   D CG  1 
ATOM   4426  C  CD1 . LEU   D  1 74  ? -1.117  -103.504 -47.396 1.00 45.01 ? 74  LEU   D CD1 1 
ATOM   4427  C  CD2 . LEU   D  1 74  ? -2.187  -104.350 -49.494 1.00 46.13 ? 74  LEU   D CD2 1 
ATOM   4428  N  N   . GLY   D  1 75  ? -0.694  -106.718 -45.310 1.00 51.60 ? 75  GLY   D N   1 
ATOM   4429  C  CA  . GLY   D  1 75  ? -1.552  -107.521 -44.467 1.00 40.32 ? 75  GLY   D CA  1 
ATOM   4430  C  C   . GLY   D  1 75  ? -3.015  -107.310 -44.752 1.00 43.30 ? 75  GLY   D C   1 
ATOM   4431  O  O   . GLY   D  1 75  ? -3.418  -106.568 -45.645 1.00 47.60 ? 75  GLY   D O   1 
ATOM   4432  N  N   . LYS   D  1 76  ? -3.830  -107.973 -43.945 1.00 39.07 ? 76  LYS   D N   1 
ATOM   4433  C  CA  . LYS   D  1 76  ? -5.270  -107.968 -44.150 1.00 40.09 ? 76  LYS   D CA  1 
ATOM   4434  C  C   . LYS   D  1 76  ? -5.846  -106.612 -43.759 1.00 50.15 ? 76  LYS   D C   1 
ATOM   4435  O  O   . LYS   D  1 76  ? -5.610  -106.123 -42.649 1.00 55.94 ? 76  LYS   D O   1 
ATOM   4436  C  CB  . LYS   D  1 76  ? -5.918  -109.089 -43.336 1.00 49.58 ? 76  LYS   D CB  1 
ATOM   4437  C  CG  . LYS   D  1 76  ? -7.441  -109.184 -43.500 1.00 46.50 ? 76  LYS   D CG  1 
ATOM   4438  N  N   . LEU   D  1 77  ? -6.585  -106.002 -44.679 1.00 46.72 ? 77  LEU   D N   1 
ATOM   4439  C  CA  . LEU   D  1 77  ? -7.290  -104.765 -44.388 1.00 43.52 ? 77  LEU   D CA  1 
ATOM   4440  C  C   . LEU   D  1 77  ? -8.602  -105.065 -43.693 1.00 48.21 ? 77  LEU   D C   1 
ATOM   4441  O  O   . LEU   D  1 77  ? -9.326  -105.993 -44.069 1.00 44.87 ? 77  LEU   D O   1 
ATOM   4442  C  CB  . LEU   D  1 77  ? -7.590  -103.985 -45.665 1.00 51.37 ? 77  LEU   D CB  1 
ATOM   4443  C  CG  . LEU   D  1 77  ? -6.548  -103.931 -46.769 1.00 42.06 ? 77  LEU   D CG  1 
ATOM   4444  C  CD1 . LEU   D  1 77  ? -7.140  -103.218 -47.992 1.00 45.77 ? 77  LEU   D CD1 1 
ATOM   4445  C  CD2 . LEU   D  1 77  ? -5.273  -103.261 -46.293 1.00 43.29 ? 77  LEU   D CD2 1 
ATOM   4446  N  N   . LEU   D  1 78  ? -8.933  -104.244 -42.711 1.00 47.00 ? 78  LEU   D N   1 
ATOM   4447  C  CA  . LEU   D  1 78  ? -10.176 -104.393 -41.961 1.00 46.74 ? 78  LEU   D CA  1 
ATOM   4448  C  C   . LEU   D  1 78  ? -11.162 -103.378 -42.523 1.00 47.33 ? 78  LEU   D C   1 
ATOM   4449  O  O   . LEU   D  1 78  ? -11.287 -102.264 -42.020 1.00 46.81 ? 78  LEU   D O   1 
ATOM   4450  C  CB  . LEU   D  1 78  ? -9.932  -104.191 -40.476 1.00 41.71 ? 78  LEU   D CB  1 
ATOM   4451  C  CG  . LEU   D  1 78  ? -8.923  -105.164 -39.872 1.00 49.73 ? 78  LEU   D CG  1 
ATOM   4452  C  CD1 . LEU   D  1 78  ? -8.859  -104.958 -38.377 1.00 44.57 ? 78  LEU   D CD1 1 
ATOM   4453  C  CD2 . LEU   D  1 78  ? -9.287  -106.598 -40.211 1.00 48.54 ? 78  LEU   D CD2 1 
ATOM   4454  N  N   . ILE   D  1 79  ? -11.860 -103.766 -43.584 1.00 43.53 ? 79  ILE   D N   1 
ATOM   4455  C  CA  . ILE   D  1 79  ? -12.793 -102.879 -44.257 1.00 48.84 ? 79  ILE   D CA  1 
ATOM   4456  C  C   . ILE   D  1 79  ? -14.170 -103.139 -43.694 1.00 43.71 ? 79  ILE   D C   1 
ATOM   4457  O  O   . ILE   D  1 79  ? -14.688 -104.259 -43.784 1.00 54.18 ? 79  ILE   D O   1 
ATOM   4458  C  CB  . ILE   D  1 79  ? -12.785 -103.073 -45.783 1.00 43.27 ? 79  ILE   D CB  1 
ATOM   4459  C  CG1 . ILE   D  1 79  ? -11.364 -103.029 -46.332 1.00 45.30 ? 79  ILE   D CG1 1 
ATOM   4460  C  CG2 . ILE   D  1 79  ? -13.595 -101.980 -46.419 1.00 47.45 ? 79  ILE   D CG2 1 
ATOM   4461  C  CD1 . ILE   D  1 79  ? -10.592 -101.772 -45.949 1.00 47.82 ? 79  ILE   D CD1 1 
ATOM   4462  N  N   . GLY   D  1 80  ? -14.769 -102.112 -43.136 1.00 41.31 ? 80  GLY   D N   1 
ATOM   4463  C  CA  . GLY   D  1 80  ? -16.134 -102.220 -42.677 1.00 46.11 ? 80  GLY   D CA  1 
ATOM   4464  C  C   . GLY   D  1 80  ? -17.096 -101.912 -43.777 1.00 41.25 ? 80  GLY   D C   1 
ATOM   4465  O  O   . GLY   D  1 80  ? -16.720 -101.507 -44.869 1.00 50.04 ? 80  GLY   D O   1 
ATOM   4466  N  N   . GLU   D  1 81  ? -18.369 -102.126 -43.488 1.00 48.03 ? 81  GLU   D N   1 
ATOM   4467  C  CA  . GLU   D  1 81  ? -19.413 -101.936 -44.480 1.00 47.39 ? 81  GLU   D CA  1 
ATOM   4468  C  C   . GLU   D  1 81  ? -20.502 -100.999 -43.979 1.00 47.83 ? 81  GLU   D C   1 
ATOM   4469  O  O   . GLU   D  1 81  ? -21.491 -100.787 -44.685 1.00 42.84 ? 81  GLU   D O   1 
ATOM   4470  C  CB  . GLU   D  1 81  ? -20.008 -103.296 -44.887 1.00 60.03 ? 81  GLU   D CB  1 
ATOM   4471  C  CG  . GLU   D  1 81  ? -19.076 -104.487 -44.577 1.00 68.19 ? 81  GLU   D CG  1 
ATOM   4472  C  CD  . GLU   D  1 81  ? -19.173 -105.634 -45.575 1.00 78.72 ? 81  GLU   D CD  1 
ATOM   4473  O  OE1 . GLU   D  1 81  ? -20.277 -105.906 -46.098 1.00 70.95 ? 81  GLU   D OE1 1 
ATOM   4474  O  OE2 . GLU   D  1 81  ? -18.124 -106.265 -45.836 1.00 81.71 ? 81  GLU   D OE2 1 
ATOM   4475  N  N   . ASN   D  1 82  ? -20.339 -100.427 -42.790 1.00 45.70 ? 82  ASN   D N   1 
ATOM   4476  C  CA  . ASN   D  1 82  ? -21.170 -99.325  -42.335 1.00 46.72 ? 82  ASN   D CA  1 
ATOM   4477  C  C   . ASN   D  1 82  ? -20.329 -98.450  -41.407 1.00 42.64 ? 82  ASN   D C   1 
ATOM   4478  O  O   . ASN   D  1 82  ? -19.240 -98.838  -40.957 1.00 41.94 ? 82  ASN   D O   1 
ATOM   4479  C  CB  . ASN   D  1 82  ? -22.427 -99.831  -41.645 1.00 49.02 ? 82  ASN   D CB  1 
ATOM   4480  C  CG  . ASN   D  1 82  ? -22.111 -100.710 -40.474 1.00 53.82 ? 82  ASN   D CG  1 
ATOM   4481  O  OD1 . ASN   D  1 82  ? -21.599 -100.243 -39.457 1.00 46.85 ? 82  ASN   D OD1 1 
ATOM   4482  N  ND2 . ASN   D  1 82  ? -22.391 -102.001 -40.612 1.00 63.54 ? 82  ASN   D ND2 1 
ATOM   4483  N  N   . THR   D  1 83  ? -20.831 -97.241  -41.150 1.00 43.45 ? 83  THR   D N   1 
ATOM   4484  C  CA  . THR   D  1 83  ? -20.010 -96.240  -40.476 1.00 38.73 ? 83  THR   D CA  1 
ATOM   4485  C  C   . THR   D  1 83  ? -19.503 -96.756  -39.129 1.00 40.77 ? 83  THR   D C   1 
ATOM   4486  O  O   . THR   D  1 83  ? -18.291 -96.742  -38.857 1.00 34.02 ? 83  THR   D O   1 
ATOM   4487  C  CB  . THR   D  1 83  ? -20.805 -94.944  -40.322 1.00 38.84 ? 83  THR   D CB  1 
ATOM   4488  O  OG1 . THR   D  1 83  ? -21.016 -94.363  -41.615 1.00 38.48 ? 83  THR   D OG1 1 
ATOM   4489  C  CG2 . THR   D  1 83  ? -20.054 -93.947  -39.448 1.00 38.26 ? 83  THR   D CG2 1 
ATOM   4490  N  N   . GLN   D  1 84  ? -20.414 -97.245  -38.283 1.00 39.93 ? 84  GLN   D N   1 
ATOM   4491  C  CA  . GLN   D  1 84  ? -20.007 -97.771  -36.982 1.00 44.13 ? 84  GLN   D CA  1 
ATOM   4492  C  C   . GLN   D  1 84  ? -18.956 -98.874  -37.132 1.00 41.96 ? 84  GLN   D C   1 
ATOM   4493  O  O   . GLN   D  1 84  ? -17.954 -98.889  -36.406 1.00 42.91 ? 84  GLN   D O   1 
ATOM   4494  C  CB  . GLN   D  1 84  ? -21.246 -98.271  -36.214 1.00 43.06 ? 84  GLN   D CB  1 
ATOM   4495  C  CG  . GLN   D  1 84  ? -20.961 -98.706  -34.787 1.00 48.06 ? 84  GLN   D CG  1 
ATOM   4496  N  N   . GLU   D  1 85  ? -19.139 -99.785  -38.093 1.00 39.74 ? 85  GLU   D N   1 
ATOM   4497  C  CA  . GLU   D  1 85  ? -18.166 -100.861 -38.260 1.00 40.72 ? 85  GLU   D CA  1 
ATOM   4498  C  C   . GLU   D  1 85  ? -16.852 -100.362 -38.854 1.00 42.05 ? 85  GLU   D C   1 
ATOM   4499  O  O   . GLU   D  1 85  ? -15.786 -100.873 -38.500 1.00 38.21 ? 85  GLU   D O   1 
ATOM   4500  C  CB  . GLU   D  1 85  ? -18.746 -101.980 -39.133 1.00 46.72 ? 85  GLU   D CB  1 
ATOM   4501  C  CG  . GLU   D  1 85  ? -17.921 -103.258 -39.071 1.00 54.51 ? 85  GLU   D CG  1 
ATOM   4502  C  CD  . GLU   D  1 85  ? -18.375 -104.331 -40.048 1.00 58.61 ? 85  GLU   D CD  1 
ATOM   4503  O  OE1 . GLU   D  1 85  ? -18.943 -103.984 -41.101 1.00 59.04 ? 85  GLU   D OE1 1 
ATOM   4504  O  OE2 . GLU   D  1 85  ? -18.147 -105.525 -39.762 1.00 70.44 ? 85  GLU   D OE2 1 
ATOM   4505  N  N   . MET   D  1 86  ? -16.897 -99.363  -39.742 1.00 43.13 ? 86  MET   D N   1 
ATOM   4506  C  CA  . MET   D  1 86  ? -15.656 -98.812  -40.280 1.00 34.00 ? 86  MET   D CA  1 
ATOM   4507  C  C   . MET   D  1 86  ? -14.828 -98.157  -39.186 1.00 39.60 ? 86  MET   D C   1 
ATOM   4508  O  O   . MET   D  1 86  ? -13.602 -98.317  -39.142 1.00 36.05 ? 86  MET   D O   1 
ATOM   4509  C  CB  . MET   D  1 86  ? -15.972 -97.816  -41.387 1.00 38.61 ? 86  MET   D CB  1 
ATOM   4510  C  CG  . MET   D  1 86  ? -16.663 -98.495  -42.586 1.00 38.91 ? 86  MET   D CG  1 
ATOM   4511  S  SD  . MET   D  1 86  ? -17.673 -97.379  -43.521 1.00 41.20 ? 86  MET   D SD  1 
ATOM   4512  C  CE  . MET   D  1 86  ? -16.370 -96.462  -44.371 1.00 42.76 ? 86  MET   D CE  1 
ATOM   4513  N  N   . LEU   D  1 87  ? -15.481 -97.416  -38.290 1.00 40.47 ? 87  LEU   D N   1 
ATOM   4514  C  CA  . LEU   D  1 87  ? -14.757 -96.828  -37.170 1.00 41.35 ? 87  LEU   D CA  1 
ATOM   4515  C  C   . LEU   D  1 87  ? -14.168 -97.914  -36.285 1.00 37.63 ? 87  LEU   D C   1 
ATOM   4516  O  O   . LEU   D  1 87  ? -13.012 -97.822  -35.855 1.00 34.03 ? 87  LEU   D O   1 
ATOM   4517  C  CB  . LEU   D  1 87  ? -15.687 -95.931  -36.359 1.00 38.79 ? 87  LEU   D CB  1 
ATOM   4518  C  CG  . LEU   D  1 87  ? -16.211 -94.712  -37.110 1.00 39.89 ? 87  LEU   D CG  1 
ATOM   4519  C  CD1 . LEU   D  1 87  ? -17.406 -94.179  -36.375 1.00 40.74 ? 87  LEU   D CD1 1 
ATOM   4520  C  CD2 . LEU   D  1 87  ? -15.134 -93.653  -37.260 1.00 34.28 ? 87  LEU   D CD2 1 
ATOM   4521  N  N   . GLN   D  1 88  ? -14.946 -98.964  -36.015 1.00 39.70 ? 88  GLN   D N   1 
ATOM   4522  C  CA  . GLN   D  1 88  ? -14.435 -100.027 -35.160 1.00 43.90 ? 88  GLN   D CA  1 
ATOM   4523  C  C   . GLN   D  1 88  ? -13.251 -100.738 -35.821 1.00 42.16 ? 88  GLN   D C   1 
ATOM   4524  O  O   . GLN   D  1 88  ? -12.259 -101.057 -35.146 1.00 37.60 ? 88  GLN   D O   1 
ATOM   4525  C  CB  . GLN   D  1 88  ? -15.573 -100.994 -34.810 1.00 46.78 ? 88  GLN   D CB  1 
ATOM   4526  C  CG  . GLN   D  1 88  ? -15.228 -102.059 -33.751 1.00 64.17 ? 88  GLN   D CG  1 
ATOM   4527  C  CD  . GLN   D  1 88  ? -14.831 -101.481 -32.397 1.00 57.58 ? 88  GLN   D CD  1 
ATOM   4528  O  OE1 . GLN   D  1 88  ? -15.612 -100.786 -31.754 1.00 57.19 ? 88  GLN   D OE1 1 
ATOM   4529  N  NE2 . GLN   D  1 88  ? -13.610 -101.769 -31.966 1.00 47.18 ? 88  GLN   D NE2 1 
ATOM   4530  N  N   . CYS   D  1 89  ? -13.309 -100.957 -37.148 1.00 42.37 ? 89  CYS   D N   1 
ATOM   4531  C  CA  . CYS   D  1 89  ? -12.165 -101.566 -37.831 1.00 40.89 ? 89  CYS   D CA  1 
ATOM   4532  C  C   . CYS   D  1 89  ? -10.930 -100.693 -37.708 1.00 38.33 ? 89  CYS   D C   1 
ATOM   4533  O  O   . CYS   D  1 89  ? -9.820  -101.199 -37.507 1.00 39.37 ? 89  CYS   D O   1 
ATOM   4534  C  CB  . CYS   D  1 89  ? -12.462 -101.819 -39.318 1.00 39.79 ? 89  CYS   D CB  1 
ATOM   4535  S  SG  . CYS   D  1 89  ? -13.666 -103.121 -39.700 1.00 48.13 ? 89  CYS   D SG  1 
ATOM   4536  N  N   . ASP   D  1 90  ? -11.095 -99.374  -37.845 1.00 41.75 ? 90  ASP   D N   1 
ATOM   4537  C  CA  . ASP   D  1 90  ? -9.952  -98.484  -37.680 1.00 38.19 ? 90  ASP   D CA  1 
ATOM   4538  C  C   . ASP   D  1 90  ? -9.384  -98.607  -36.272 1.00 36.27 ? 90  ASP   D C   1 
ATOM   4539  O  O   . ASP   D  1 90  ? -8.165  -98.632  -36.081 1.00 39.67 ? 90  ASP   D O   1 
ATOM   4540  C  CB  . ASP   D  1 90  ? -10.352 -97.029  -37.946 1.00 41.94 ? 90  ASP   D CB  1 
ATOM   4541  C  CG  . ASP   D  1 90  ? -10.559 -96.720  -39.419 1.00 46.59 ? 90  ASP   D CG  1 
ATOM   4542  O  OD1 . ASP   D  1 90  ? -10.320 -97.591  -40.284 1.00 42.61 ? 90  ASP   D OD1 1 
ATOM   4543  O  OD2 . ASP   D  1 90  ? -10.978 -95.581  -39.701 1.00 43.98 ? 90  ASP   D OD2 1 
ATOM   4544  N  N   . LEU   D  1 91  ? -10.266 -98.669  -35.275 1.00 37.38 ? 91  LEU   D N   1 
ATOM   4545  C  CA  . LEU   D  1 91  ? -9.829  -98.768  -33.885 1.00 43.34 ? 91  LEU   D CA  1 
ATOM   4546  C  C   . LEU   D  1 91  ? -9.077  -100.071 -33.624 1.00 36.26 ? 91  LEU   D C   1 
ATOM   4547  O  O   . LEU   D  1 91  ? -8.019  -100.076 -32.980 1.00 41.10 ? 91  LEU   D O   1 
ATOM   4548  C  CB  . LEU   D  1 91  ? -11.045 -98.646  -32.971 1.00 37.90 ? 91  LEU   D CB  1 
ATOM   4549  C  CG  . LEU   D  1 91  ? -10.811 -98.704  -31.472 1.00 37.90 ? 91  LEU   D CG  1 
ATOM   4550  C  CD1 . LEU   D  1 91  ? -9.808  -97.656  -31.056 1.00 42.24 ? 91  LEU   D CD1 1 
ATOM   4551  C  CD2 . LEU   D  1 91  ? -12.129 -98.497  -30.802 1.00 36.20 ? 91  LEU   D CD2 1 
ATOM   4552  N  N   . ASN   D  1 92  ? -9.618  -101.193 -34.095 1.00 44.10 ? 92  ASN   D N   1 
ATOM   4553  C  CA  . ASN   D  1 92  ? -8.924  -102.460 -33.899 1.00 39.98 ? 92  ASN   D CA  1 
ATOM   4554  C  C   . ASN   D  1 92  ? -7.516  -102.405 -34.474 1.00 42.26 ? 92  ASN   D C   1 
ATOM   4555  O  O   . ASN   D  1 92  ? -6.545  -102.813 -33.821 1.00 38.05 ? 92  ASN   D O   1 
ATOM   4556  C  CB  . ASN   D  1 92  ? -9.737  -103.589 -34.520 1.00 44.33 ? 92  ASN   D CB  1 
ATOM   4557  C  CG  . ASN   D  1 92  ? -11.037 -103.851 -33.772 1.00 51.24 ? 92  ASN   D CG  1 
ATOM   4558  O  OD1 . ASN   D  1 92  ? -11.248 -103.336 -32.676 1.00 50.90 ? 92  ASN   D OD1 1 
ATOM   4559  N  ND2 . ASN   D  1 92  ? -11.920 -104.645 -34.371 1.00 58.12 ? 92  ASN   D ND2 1 
ATOM   4560  N  N   . LEU   D  1 93  ? -7.377  -101.842 -35.674 1.00 42.07 ? 93  LEU   D N   1 
ATOM   4561  C  CA  . LEU   D  1 93  ? -6.064  -101.711 -36.289 1.00 43.30 ? 93  LEU   D CA  1 
ATOM   4562  C  C   . LEU   D  1 93  ? -5.161  -100.810 -35.458 1.00 36.73 ? 93  LEU   D C   1 
ATOM   4563  O  O   . LEU   D  1 93  ? -3.968  -101.103 -35.283 1.00 41.83 ? 93  LEU   D O   1 
ATOM   4564  C  CB  . LEU   D  1 93  ? -6.217  -101.169 -37.721 1.00 46.54 ? 93  LEU   D CB  1 
ATOM   4565  C  CG  . LEU   D  1 93  ? -4.950  -100.955 -38.546 1.00 41.68 ? 93  LEU   D CG  1 
ATOM   4566  C  CD1 . LEU   D  1 93  ? -4.169  -102.249 -38.707 1.00 44.92 ? 93  LEU   D CD1 1 
ATOM   4567  C  CD2 . LEU   D  1 93  ? -5.274  -100.385 -39.924 1.00 38.70 ? 93  LEU   D CD2 1 
ATOM   4568  N  N   . GLU   D  1 94  ? -5.699  -99.703  -34.938 1.00 39.48 ? 94  GLU   D N   1 
ATOM   4569  C  CA  . GLU   D  1 94  ? -4.857  -98.828  -34.120 1.00 38.00 ? 94  GLU   D CA  1 
ATOM   4570  C  C   . GLU   D  1 94  ? -4.370  -99.554  -32.873 1.00 33.44 ? 94  GLU   D C   1 
ATOM   4571  O  O   . GLU   D  1 94  ? -3.211  -99.398  -32.466 1.00 45.01 ? 94  GLU   D O   1 
ATOM   4572  C  CB  . GLU   D  1 94  ? -5.616  -97.562  -33.730 1.00 37.02 ? 94  GLU   D CB  1 
ATOM   4573  C  CG  . GLU   D  1 94  ? -5.813  -96.535  -34.867 1.00 44.84 ? 94  GLU   D CG  1 
ATOM   4574  C  CD  . GLU   D  1 94  ? -4.542  -95.870  -35.320 1.00 45.11 ? 94  GLU   D CD  1 
ATOM   4575  O  OE1 . GLU   D  1 94  ? -3.518  -95.998  -34.625 1.00 45.43 ? 94  GLU   D OE1 1 
ATOM   4576  O  OE2 . GLU   D  1 94  ? -4.555  -95.232  -36.393 1.00 57.47 ? 94  GLU   D OE2 1 
ATOM   4577  N  N   . LEU   D  1 95  ? -5.247  -100.348 -32.248 1.00 46.26 ? 95  LEU   D N   1 
ATOM   4578  C  CA  . LEU   D  1 95  ? -4.857  -101.059 -31.033 1.00 39.87 ? 95  LEU   D CA  1 
ATOM   4579  C  C   . LEU   D  1 95  ? -3.755  -102.063 -31.323 1.00 35.37 ? 95  LEU   D C   1 
ATOM   4580  O  O   . LEU   D  1 95  ? -2.804  -102.193 -30.546 1.00 40.66 ? 95  LEU   D O   1 
ATOM   4581  C  CB  . LEU   D  1 95  ? -6.074  -101.741 -30.420 1.00 43.77 ? 95  LEU   D CB  1 
ATOM   4582  C  CG  . LEU   D  1 95  ? -7.147  -100.729 -30.008 1.00 40.23 ? 95  LEU   D CG  1 
ATOM   4583  C  CD1 . LEU   D  1 95  ? -8.467  -101.393 -29.673 1.00 48.28 ? 95  LEU   D CD1 1 
ATOM   4584  C  CD2 . LEU   D  1 95  ? -6.652  -99.896  -28.866 1.00 40.85 ? 95  LEU   D CD2 1 
ATOM   4585  N  N   . LYS   D  1 96  ? -3.850  -102.770 -32.450 1.00 35.64 ? 96  LYS   D N   1 
ATOM   4586  C  CA  . LYS   D  1 96  ? -2.732  -103.608 -32.870 1.00 37.76 ? 96  LYS   D CA  1 
ATOM   4587  C  C   . LYS   D  1 96  ? -1.484  -102.770 -33.108 1.00 36.59 ? 96  LYS   D C   1 
ATOM   4588  O  O   . LYS   D  1 96  ? -0.383  -103.130 -32.667 1.00 41.75 ? 96  LYS   D O   1 
ATOM   4589  C  CB  . LYS   D  1 96  ? -3.107  -104.390 -34.131 1.00 43.34 ? 96  LYS   D CB  1 
ATOM   4590  C  CG  . LYS   D  1 96  ? -1.920  -105.158 -34.731 1.00 46.63 ? 96  LYS   D CG  1 
ATOM   4591  C  CD  . LYS   D  1 96  ? -2.335  -106.210 -35.743 1.00 65.03 ? 96  LYS   D CD  1 
ATOM   4592  C  CE  . LYS   D  1 96  ? -1.129  -106.666 -36.548 1.00 64.18 ? 96  LYS   D CE  1 
ATOM   4593  N  NZ  . LYS   D  1 96  ? 0.064   -106.830 -35.668 1.00 59.47 ? 96  LYS   D NZ  1 
ATOM   4594  N  N   . ALA   D  1 97  ? -1.644  -101.634 -33.793 1.00 41.52 ? 97  ALA   D N   1 
ATOM   4595  C  CA  . ALA   D  1 97  ? -0.496  -100.815 -34.169 1.00 38.30 ? 97  ALA   D CA  1 
ATOM   4596  C  C   . ALA   D  1 97  ? 0.251   -100.294 -32.948 1.00 33.02 ? 97  ALA   D C   1 
ATOM   4597  O  O   . ALA   D  1 97  ? 1.487   -100.244 -32.941 1.00 37.92 ? 97  ALA   D O   1 
ATOM   4598  C  CB  . ALA   D  1 97  ? -0.969  -99.645  -35.035 1.00 41.29 ? 97  ALA   D CB  1 
ATOM   4599  N  N   . THR   D  1 98  ? -0.478  -99.868  -31.912 1.00 42.96 ? 98  THR   D N   1 
ATOM   4600  C  CA  . THR   D  1 98  ? 0.195   -99.296  -30.746 1.00 41.27 ? 98  THR   D CA  1 
ATOM   4601  C  C   . THR   D  1 98  ? 0.879   -100.365 -29.897 1.00 39.58 ? 98  THR   D C   1 
ATOM   4602  O  O   . THR   D  1 98  ? 1.934   -100.097 -29.317 1.00 38.74 ? 98  THR   D O   1 
ATOM   4603  C  CB  . THR   D  1 98  ? -0.791  -98.480  -29.892 1.00 38.93 ? 98  THR   D CB  1 
ATOM   4604  O  OG1 . THR   D  1 98  ? -1.884  -99.300  -29.483 1.00 43.66 ? 98  THR   D OG1 1 
ATOM   4605  C  CG2 . THR   D  1 98  ? -1.338  -97.287  -30.684 1.00 40.94 ? 98  THR   D CG2 1 
ATOM   4606  N  N   . LYS   D  1 99  ? 0.313   -101.570 -29.807 1.00 39.97 ? 99  LYS   D N   1 
ATOM   4607  C  CA  . LYS   D  1 99  ? 1.039   -102.657 -29.142 1.00 39.02 ? 99  LYS   D CA  1 
ATOM   4608  C  C   . LYS   D  1 99  ? 2.372   -102.935 -29.832 1.00 39.42 ? 99  LYS   D C   1 
ATOM   4609  O  O   . LYS   D  1 99  ? 3.401   -103.131 -29.171 1.00 41.16 ? 99  LYS   D O   1 
ATOM   4610  C  CB  . LYS   D  1 99  ? 0.181   -103.921 -29.119 1.00 45.65 ? 99  LYS   D CB  1 
ATOM   4611  C  CG  . LYS   D  1 99  ? 0.878   -105.114 -28.472 1.00 44.13 ? 99  LYS   D CG  1 
ATOM   4612  N  N   . ASP   D  1 100 ? 2.382   -102.945 -31.167 1.00 44.56 ? 100 ASP   D N   1 
ATOM   4613  C  CA  . ASP   D  1 100 ? 3.625   -103.230 -31.877 1.00 39.56 ? 100 ASP   D CA  1 
ATOM   4614  C  C   . ASP   D  1 100 ? 4.623   -102.107 -31.689 1.00 36.56 ? 100 ASP   D C   1 
ATOM   4615  O  O   . ASP   D  1 100 ? 5.814   -102.358 -31.477 1.00 42.61 ? 100 ASP   D O   1 
ATOM   4616  C  CB  . ASP   D  1 100 ? 3.339   -103.471 -33.353 1.00 43.84 ? 100 ASP   D CB  1 
ATOM   4617  C  CG  . ASP   D  1 100 ? 2.531   -104.732 -33.579 1.00 53.23 ? 100 ASP   D CG  1 
ATOM   4618  O  OD1 . ASP   D  1 100 ? 2.614   -105.636 -32.716 1.00 57.49 ? 100 ASP   D OD1 1 
ATOM   4619  O  OD2 . ASP   D  1 100 ? 1.810   -104.821 -34.600 1.00 48.77 ? 100 ASP   D OD2 1 
ATOM   4620  N  N   . LEU   D  1 101 ? 4.144   -100.860 -31.705 1.00 42.97 ? 101 LEU   D N   1 
ATOM   4621  C  CA  . LEU   D  1 101 ? 5.016   -99.727  -31.421 1.00 36.94 ? 101 LEU   D CA  1 
ATOM   4622  C  C   . LEU   D  1 101 ? 5.663   -99.870  -30.055 1.00 30.37 ? 101 LEU   D C   1 
ATOM   4623  O  O   . LEU   D  1 101 ? 6.870   -99.675  -29.903 1.00 37.29 ? 101 LEU   D O   1 
ATOM   4624  C  CB  . LEU   D  1 101 ? 4.218   -98.424  -31.512 1.00 40.09 ? 101 LEU   D CB  1 
ATOM   4625  C  CG  . LEU   D  1 101 ? 3.991   -97.982  -32.968 1.00 43.95 ? 101 LEU   D CG  1 
ATOM   4626  C  CD1 . LEU   D  1 101 ? 2.794   -97.072  -33.118 1.00 39.65 ? 101 LEU   D CD1 1 
ATOM   4627  C  CD2 . LEU   D  1 101 ? 5.267   -97.324  -33.502 1.00 36.49 ? 101 LEU   D CD2 1 
ATOM   4628  N  N   . ARG   D  1 102 ? 4.876   -100.228 -29.046 1.00 36.23 ? 102 ARG   D N   1 
ATOM   4629  C  CA  . ARG   D  1 102 ? 5.438   -100.360 -27.705 1.00 37.14 ? 102 ARG   D CA  1 
ATOM   4630  C  C   . ARG   D  1 102 ? 6.511   -101.432 -27.666 1.00 31.50 ? 102 ARG   D C   1 
ATOM   4631  O  O   . ARG   D  1 102 ? 7.577   -101.240 -27.069 1.00 38.36 ? 102 ARG   D O   1 
ATOM   4632  C  CB  . ARG   D  1 102 ? 4.337   -100.676 -26.693 1.00 42.78 ? 102 ARG   D CB  1 
ATOM   4633  C  CG  . ARG   D  1 102 ? 3.354   -99.555  -26.475 1.00 36.61 ? 102 ARG   D CG  1 
ATOM   4634  C  CD  . ARG   D  1 102 ? 2.315   -99.944  -25.458 1.00 34.43 ? 102 ARG   D CD  1 
ATOM   4635  N  NE  . ARG   D  1 102 ? 1.084   -99.227  -25.708 1.00 37.06 ? 102 ARG   D NE  1 
ATOM   4636  C  CZ  . ARG   D  1 102 ? 0.946   -97.923  -25.533 1.00 34.41 ? 102 ARG   D CZ  1 
ATOM   4637  N  NH1 . ARG   D  1 102 ? 1.905   -97.197  -24.984 1.00 35.60 ? 102 ARG   D NH1 1 
ATOM   4638  N  NH2 . ARG   D  1 102 ? -0.161  -97.332  -25.950 1.00 36.93 ? 102 ARG   D NH2 1 
ATOM   4639  N  N   . GLU   D  1 103 ? 6.238   -102.590 -28.271 1.00 40.58 ? 103 GLU   D N   1 
ATOM   4640  C  CA  . GLU   D  1 103 ? 7.255   -103.639 -28.312 1.00 40.73 ? 103 GLU   D CA  1 
ATOM   4641  C  C   . GLU   D  1 103 ? 8.481   -103.205 -29.109 1.00 44.32 ? 103 GLU   D C   1 
ATOM   4642  O  O   . GLU   D  1 103 ? 9.611   -103.544 -28.744 1.00 38.43 ? 103 GLU   D O   1 
ATOM   4643  C  CB  . GLU   D  1 103 ? 6.643   -104.926 -28.876 1.00 48.87 ? 103 GLU   D CB  1 
ATOM   4644  C  CG  . GLU   D  1 103 ? 5.436   -105.426 -28.053 1.00 53.76 ? 103 GLU   D CG  1 
ATOM   4645  C  CD  . GLU   D  1 103 ? 4.729   -106.657 -28.652 1.00 70.00 ? 103 GLU   D CD  1 
ATOM   4646  O  OE1 . GLU   D  1 103 ? 5.265   -107.261 -29.605 1.00 75.58 ? 103 GLU   D OE1 1 
ATOM   4647  O  OE2 . GLU   D  1 103 ? 3.632   -107.027 -28.162 1.00 65.07 ? 103 GLU   D OE2 1 
ATOM   4648  N  N   . ALA   D  1 104 ? 8.294   -102.431 -30.179 1.00 42.17 ? 104 ALA   D N   1 
ATOM   4649  C  CA  . ALA   D  1 104 ? 9.451   -101.911 -30.900 1.00 40.52 ? 104 ALA   D CA  1 
ATOM   4650  C  C   . ALA   D  1 104 ? 10.258  -100.950 -30.037 1.00 38.06 ? 104 ALA   D C   1 
ATOM   4651  O  O   . ALA   D  1 104 ? 11.494  -100.981 -30.052 1.00 39.30 ? 104 ALA   D O   1 
ATOM   4652  C  CB  . ALA   D  1 104 ? 8.989   -101.230 -32.187 1.00 38.33 ? 104 ALA   D CB  1 
ATOM   4653  N  N   . ILE   D  1 105 ? 9.580   -100.109 -29.249 1.00 37.70 ? 105 ILE   D N   1 
ATOM   4654  C  CA  . ILE   D  1 105 ? 10.298  -99.133  -28.433 1.00 37.14 ? 105 ILE   D CA  1 
ATOM   4655  C  C   . ILE   D  1 105 ? 11.119  -99.835  -27.345 1.00 35.79 ? 105 ILE   D C   1 
ATOM   4656  O  O   . ILE   D  1 105 ? 12.219  -99.396  -27.011 1.00 33.18 ? 105 ILE   D O   1 
ATOM   4657  C  CB  . ILE   D  1 105 ? 9.309   -98.111  -27.826 1.00 35.47 ? 105 ILE   D CB  1 
ATOM   4658  C  CG1 . ILE   D  1 105 ? 8.861   -97.081  -28.874 1.00 28.39 ? 105 ILE   D CG1 1 
ATOM   4659  C  CG2 . ILE   D  1 105 ? 9.981   -97.371  -26.702 1.00 37.69 ? 105 ILE   D CG2 1 
ATOM   4660  C  CD1 . ILE   D  1 105 ? 7.501   -96.429  -28.606 1.00 37.18 ? 105 ILE   D CD1 1 
ATOM   4661  N  N   . VAL   D  1 106 ? 10.578  -100.897 -26.737 1.00 38.34 ? 106 VAL   D N   1 
ATOM   4662  C  CA  . VAL   D  1 106 ? 11.340  -101.649 -25.739 1.00 41.41 ? 106 VAL   D CA  1 
ATOM   4663  C  C   . VAL   D  1 106 ? 12.667  -102.117 -26.326 1.00 39.72 ? 106 VAL   D C   1 
ATOM   4664  O  O   . VAL   D  1 106 ? 13.731  -101.975 -25.707 1.00 37.34 ? 106 VAL   D O   1 
ATOM   4665  C  CB  . VAL   D  1 106 ? 10.527  -102.847 -25.216 1.00 40.64 ? 106 VAL   D CB  1 
ATOM   4666  C  CG1 . VAL   D  1 106 ? 11.416  -103.701 -24.339 1.00 48.40 ? 106 VAL   D CG1 1 
ATOM   4667  C  CG2 . VAL   D  1 106 ? 9.328   -102.393 -24.434 1.00 48.22 ? 106 VAL   D CG2 1 
ATOM   4668  N  N   . HIS   D  1 107 ? 12.623  -102.711 -27.516 1.00 37.51 ? 107 HIS   D N   1 
ATOM   4669  C  CA  . HIS   D  1 107 ? 13.862  -103.219 -28.082 1.00 43.37 ? 107 HIS   D CA  1 
ATOM   4670  C  C   . HIS   D  1 107 ? 14.813  -102.086 -28.461 1.00 38.94 ? 107 HIS   D C   1 
ATOM   4671  O  O   . HIS   D  1 107 ? 16.011  -102.172 -28.186 1.00 38.49 ? 107 HIS   D O   1 
ATOM   4672  C  CB  . HIS   D  1 107 ? 13.590  -104.119 -29.283 1.00 37.45 ? 107 HIS   D CB  1 
ATOM   4673  C  CG  . HIS   D  1 107 ? 14.844  -104.695 -29.839 1.00 45.31 ? 107 HIS   D CG  1 
ATOM   4674  N  ND1 . HIS   D  1 107 ? 15.621  -105.585 -29.130 1.00 43.38 ? 107 HIS   D ND1 1 
ATOM   4675  C  CD2 . HIS   D  1 107 ? 15.505  -104.448 -30.993 1.00 50.84 ? 107 HIS   D CD2 1 
ATOM   4676  C  CE1 . HIS   D  1 107 ? 16.693  -105.887 -29.839 1.00 52.71 ? 107 HIS   D CE1 1 
ATOM   4677  N  NE2 . HIS   D  1 107 ? 16.650  -105.207 -30.971 1.00 54.08 ? 107 HIS   D NE2 1 
ATOM   4678  N  N   . CYS   D  1 108 ? 14.315  -101.018 -29.101 1.00 48.01 ? 108 CYS   D N   1 
ATOM   4679  C  CA  . CYS   D  1 108 ? 15.181  -99.862  -29.351 1.00 35.65 ? 108 CYS   D CA  1 
ATOM   4680  C  C   . CYS   D  1 108 ? 15.854  -99.392  -28.073 1.00 34.86 ? 108 CYS   D C   1 
ATOM   4681  O  O   . CYS   D  1 108 ? 17.029  -99.019  -28.080 1.00 39.11 ? 108 CYS   D O   1 
ATOM   4682  C  CB  . CYS   D  1 108 ? 14.387  -98.692  -29.946 1.00 40.18 ? 108 CYS   D CB  1 
ATOM   4683  S  SG  . CYS   D  1 108 ? 13.753  -98.944  -31.567 1.00 38.73 ? 108 CYS   D SG  1 
ATOM   4684  N  N   . GLU   D  1 109 ? 15.112  -99.372  -26.958 1.00 42.16 ? 109 GLU   D N   1 
ATOM   4685  C  CA  . GLU   D  1 109 ? 15.709  -98.904  -25.708 1.00 35.43 ? 109 GLU   D CA  1 
ATOM   4686  C  C   . GLU   D  1 109 ? 16.834  -99.832  -25.266 1.00 37.75 ? 109 GLU   D C   1 
ATOM   4687  O  O   . GLU   D  1 109 ? 17.899  -99.373  -24.848 1.00 40.92 ? 109 GLU   D O   1 
ATOM   4688  C  CB  . GLU   D  1 109 ? 14.648  -98.814  -24.606 1.00 38.11 ? 109 GLU   D CB  1 
ATOM   4689  C  CG  . GLU   D  1 109 ? 15.181  -98.277  -23.248 1.00 38.58 ? 109 GLU   D CG  1 
ATOM   4690  C  CD  . GLU   D  1 109 ? 15.671  -96.827  -23.303 1.00 41.06 ? 109 GLU   D CD  1 
ATOM   4691  O  OE1 . GLU   D  1 109 ? 15.260  -96.087  -24.220 1.00 41.57 ? 109 GLU   D OE1 1 
ATOM   4692  O  OE2 . GLU   D  1 109 ? 16.465  -96.425  -22.432 1.00 38.61 ? 109 GLU   D OE2 1 
ATOM   4693  N  N   . GLN   D  1 110 ? 16.611  -101.144 -25.374 1.00 47.45 ? 110 GLN   D N   1 
ATOM   4694  C  CA  . GLN   D  1 110 ? 17.614  -102.121 -24.953 1.00 43.31 ? 110 GLN   D CA  1 
ATOM   4695  C  C   . GLN   D  1 110 ? 18.896  -102.011 -25.769 1.00 40.16 ? 110 GLN   D C   1 
ATOM   4696  O  O   . GLN   D  1 110 ? 19.998  -102.080 -25.207 1.00 45.18 ? 110 GLN   D O   1 
ATOM   4697  C  CB  . GLN   D  1 110 ? 17.031  -103.532 -25.058 1.00 45.06 ? 110 GLN   D CB  1 
ATOM   4698  C  CG  . GLN   D  1 110 ? 15.984  -103.838 -23.999 1.00 52.79 ? 110 GLN   D CG  1 
ATOM   4699  C  CD  . GLN   D  1 110 ? 15.183  -105.097 -24.304 1.00 67.99 ? 110 GLN   D CD  1 
ATOM   4700  O  OE1 . GLN   D  1 110 ? 15.300  -105.682 -25.389 1.00 68.82 ? 110 GLN   D OE1 1 
ATOM   4701  N  NE2 . GLN   D  1 110 ? 14.353  -105.515 -23.347 1.00 61.39 ? 110 GLN   D NE2 1 
ATOM   4702  N  N   . VAL   D  1 111 ? 18.789  -101.831 -27.094 1.00 43.59 ? 111 VAL   D N   1 
ATOM   4703  C  CA  . VAL   D  1 111 ? 19.996  -101.794 -27.918 1.00 36.27 ? 111 VAL   D CA  1 
ATOM   4704  C  C   . VAL   D  1 111 ? 20.482  -100.361 -28.105 1.00 43.73 ? 111 VAL   D C   1 
ATOM   4705  O  O   . VAL   D  1 111 ? 21.414  -100.121 -28.878 1.00 40.32 ? 111 VAL   D O   1 
ATOM   4706  C  CB  . VAL   D  1 111 ? 19.795  -102.479 -29.288 1.00 49.82 ? 111 VAL   D CB  1 
ATOM   4707  C  CG1 . VAL   D  1 111 ? 19.134  -103.846 -29.120 1.00 52.54 ? 111 VAL   D CG1 1 
ATOM   4708  C  CG2 . VAL   D  1 111 ? 18.977  -101.621 -30.244 1.00 44.15 ? 111 VAL   D CG2 1 
ATOM   4709  N  N   . HIS   D  1 112 ? 19.881  -99.400  -27.396 1.00 41.40 ? 112 HIS   D N   1 
ATOM   4710  C  CA  . HIS   D  1 112 ? 20.397  -98.024  -27.328 1.00 32.16 ? 112 HIS   D CA  1 
ATOM   4711  C  C   . HIS   D  1 112 ? 20.148  -97.243  -28.616 1.00 32.64 ? 112 HIS   D C   1 
ATOM   4712  O  O   . HIS   D  1 112 ? 20.901  -96.324  -28.942 1.00 37.59 ? 112 HIS   D O   1 
ATOM   4713  C  CB  . HIS   D  1 112 ? 21.889  -97.982  -27.027 1.00 37.84 ? 112 HIS   D CB  1 
ATOM   4714  C  CG  . HIS   D  1 112 ? 22.260  -98.618  -25.727 1.00 46.09 ? 112 HIS   D CG  1 
ATOM   4715  N  ND1 . HIS   D  1 112 ? 21.322  -99.011  -24.798 1.00 46.75 ? 112 HIS   D ND1 1 
ATOM   4716  C  CD2 . HIS   D  1 112 ? 23.467  -98.923  -25.198 1.00 43.76 ? 112 HIS   D CD2 1 
ATOM   4717  C  CE1 . HIS   D  1 112 ? 21.937  -99.525  -23.747 1.00 43.23 ? 112 HIS   D CE1 1 
ATOM   4718  N  NE2 . HIS   D  1 112 ? 23.238  -99.494  -23.971 1.00 49.65 ? 112 HIS   D NE2 1 
ATOM   4719  N  N   . ASP   D  1 113 ? 19.144  -97.617  -29.387 1.00 31.35 ? 113 ASP   D N   1 
ATOM   4720  C  CA  . ASP   D  1 113 ? 18.848  -96.874  -30.613 1.00 35.69 ? 113 ASP   D CA  1 
ATOM   4721  C  C   . ASP   D  1 113 ? 17.844  -95.790  -30.239 1.00 32.59 ? 113 ASP   D C   1 
ATOM   4722  O  O   . ASP   D  1 113 ? 16.639  -95.909  -30.446 1.00 33.46 ? 113 ASP   D O   1 
ATOM   4723  C  CB  . ASP   D  1 113 ? 18.322  -97.788  -31.711 1.00 35.57 ? 113 ASP   D CB  1 
ATOM   4724  C  CG  . ASP   D  1 113 ? 18.149  -97.044  -33.036 1.00 41.29 ? 113 ASP   D CG  1 
ATOM   4725  O  OD1 . ASP   D  1 113 ? 18.383  -95.800  -33.052 1.00 36.11 ? 113 ASP   D OD1 1 
ATOM   4726  O  OD2 . ASP   D  1 113 ? 17.812  -97.692  -34.043 1.00 36.35 ? 113 ASP   D OD2 1 
ATOM   4727  N  N   . TYR   D  1 114 ? 18.363  -94.742  -29.604 1.00 33.46 ? 114 TYR   D N   1 
ATOM   4728  C  CA  . TYR   D  1 114 ? 17.484  -93.757  -28.996 1.00 39.04 ? 114 TYR   D CA  1 
ATOM   4729  C  C   . TYR   D  1 114 ? 16.770  -92.917  -30.053 1.00 41.85 ? 114 TYR   D C   1 
ATOM   4730  O  O   . TYR   D  1 114 ? 15.653  -92.447  -29.809 1.00 31.71 ? 114 TYR   D O   1 
ATOM   4731  C  CB  . TYR   D  1 114 ? 18.291  -92.889  -28.035 1.00 42.23 ? 114 TYR   D CB  1 
ATOM   4732  C  CG  . TYR   D  1 114 ? 18.886  -93.695  -26.893 1.00 35.63 ? 114 TYR   D CG  1 
ATOM   4733  C  CD1 . TYR   D  1 114 ? 18.062  -94.437  -26.053 1.00 41.37 ? 114 TYR   D CD1 1 
ATOM   4734  C  CD2 . TYR   D  1 114 ? 20.261  -93.727  -26.671 1.00 36.84 ? 114 TYR   D CD2 1 
ATOM   4735  C  CE1 . TYR   D  1 114 ? 18.592  -95.197  -25.013 1.00 45.11 ? 114 TYR   D CE1 1 
ATOM   4736  C  CE2 . TYR   D  1 114 ? 20.804  -94.473  -25.623 1.00 39.50 ? 114 TYR   D CE2 1 
ATOM   4737  C  CZ  . TYR   D  1 114 ? 19.954  -95.205  -24.801 1.00 42.28 ? 114 TYR   D CZ  1 
ATOM   4738  O  OH  . TYR   D  1 114 ? 20.445  -95.953  -23.762 1.00 47.05 ? 114 TYR   D OH  1 
ATOM   4739  N  N   . VAL   D  1 115 ? 17.378  -92.747  -31.232 1.00 37.21 ? 115 VAL   D N   1 
ATOM   4740  C  CA  . VAL   D  1 115 ? 16.729  -91.980  -32.300 1.00 36.63 ? 115 VAL   D CA  1 
ATOM   4741  C  C   . VAL   D  1 115 ? 15.555  -92.750  -32.883 1.00 38.31 ? 115 VAL   D C   1 
ATOM   4742  O  O   . VAL   D  1 115 ? 14.460  -92.199  -33.065 1.00 35.32 ? 115 VAL   D O   1 
ATOM   4743  C  CB  . VAL   D  1 115 ? 17.760  -91.580  -33.376 1.00 38.83 ? 115 VAL   D CB  1 
ATOM   4744  C  CG1 . VAL   D  1 115 ? 17.075  -90.920  -34.596 1.00 38.18 ? 115 VAL   D CG1 1 
ATOM   4745  C  CG2 . VAL   D  1 115 ? 18.759  -90.620  -32.769 1.00 33.90 ? 115 VAL   D CG2 1 
ATOM   4746  N  N   . SER   D  1 116 ? 15.733  -94.043  -33.163 1.00 34.70 ? 116 SER   D N   1 
ATOM   4747  C  CA  . SER   D  1 116 ? 14.573  -94.805  -33.611 1.00 33.91 ? 116 SER   D CA  1 
ATOM   4748  C  C   . SER   D  1 116 ? 13.482  -94.792  -32.550 1.00 32.88 ? 116 SER   D C   1 
ATOM   4749  O  O   . SER   D  1 116 ? 12.293  -94.732  -32.878 1.00 33.71 ? 116 SER   D O   1 
ATOM   4750  C  CB  . SER   D  1 116 ? 14.963  -96.244  -33.967 1.00 38.00 ? 116 SER   D CB  1 
ATOM   4751  O  OG  . SER   D  1 116 ? 15.920  -96.250  -35.020 1.00 41.22 ? 116 SER   D OG  1 
ATOM   4752  N  N   . ARG   D  1 117 ? 13.861  -94.863  -31.268 1.00 37.09 ? 117 ARG   D N   1 
ATOM   4753  C  CA  . ARG   D  1 117 ? 12.843  -94.793  -30.224 1.00 37.59 ? 117 ARG   D CA  1 
ATOM   4754  C  C   . ARG   D  1 117 ? 12.021  -93.512  -30.361 1.00 30.22 ? 117 ARG   D C   1 
ATOM   4755  O  O   . ARG   D  1 117 ? 10.784  -93.531  -30.295 1.00 35.48 ? 117 ARG   D O   1 
ATOM   4756  C  CB  . ARG   D  1 117 ? 13.489  -94.861  -28.835 1.00 35.21 ? 117 ARG   D CB  1 
ATOM   4757  C  CG  . ARG   D  1 117 ? 12.482  -94.580  -27.718 1.00 40.50 ? 117 ARG   D CG  1 
ATOM   4758  C  CD  . ARG   D  1 117 ? 13.011  -94.801  -26.291 1.00 36.19 ? 117 ARG   D CD  1 
ATOM   4759  N  NE  . ARG   D  1 117 ? 12.032  -94.286  -25.339 1.00 30.72 ? 117 ARG   D NE  1 
ATOM   4760  C  CZ  . ARG   D  1 117 ? 11.790  -94.791  -24.135 1.00 39.54 ? 117 ARG   D CZ  1 
ATOM   4761  N  NH1 . ARG   D  1 117 ? 12.469  -95.826  -23.667 1.00 39.02 ? 117 ARG   D NH1 1 
ATOM   4762  N  NH2 . ARG   D  1 117 ? 10.845  -94.236  -23.378 1.00 39.34 ? 117 ARG   D NH2 1 
ATOM   4763  N  N   . ASP   D  1 118 ? 12.712  -92.389  -30.551 1.00 34.69 ? 118 ASP   D N   1 
ATOM   4764  C  CA  . ASP   D  1 118 ? 12.050  -91.094  -30.577 1.00 33.06 ? 118 ASP   D CA  1 
ATOM   4765  C  C   . ASP   D  1 118 ? 11.087  -91.014  -31.745 1.00 35.48 ? 118 ASP   D C   1 
ATOM   4766  O  O   . ASP   D  1 118 ? 9.939   -90.576  -31.587 1.00 35.34 ? 118 ASP   D O   1 
ATOM   4767  C  CB  . ASP   D  1 118 ? 13.119  -89.999  -30.624 1.00 27.53 ? 118 ASP   D CB  1 
ATOM   4768  C  CG  . ASP   D  1 118 ? 12.571  -88.618  -30.264 1.00 40.16 ? 118 ASP   D CG  1 
ATOM   4769  O  OD1 . ASP   D  1 118 ? 11.904  -88.493  -29.227 1.00 39.58 ? 118 ASP   D OD1 1 
ATOM   4770  O  OD2 . ASP   D  1 118 ? 12.834  -87.654  -31.007 1.00 37.11 ? 118 ASP   D OD2 1 
ATOM   4771  N  N   . LEU   D  1 119 ? 11.508  -91.498  -32.916 1.00 34.94 ? 119 LEU   D N   1 
ATOM   4772  C  CA  . LEU   D  1 119 ? 10.587  -91.564  -34.043 1.00 33.19 ? 119 LEU   D CA  1 
ATOM   4773  C  C   . LEU   D  1 119 ? 9.359   -92.397  -33.705 1.00 35.09 ? 119 LEU   D C   1 
ATOM   4774  O  O   . LEU   D  1 119 ? 8.225   -91.992  -33.987 1.00 33.48 ? 119 LEU   D O   1 
ATOM   4775  C  CB  . LEU   D  1 119 ? 11.298  -92.121  -35.273 1.00 35.75 ? 119 LEU   D CB  1 
ATOM   4776  C  CG  . LEU   D  1 119 ? 10.391  -92.424  -36.462 1.00 35.89 ? 119 LEU   D CG  1 
ATOM   4777  C  CD1 . LEU   D  1 119 ? 9.673   -91.142  -36.993 1.00 35.87 ? 119 LEU   D CD1 1 
ATOM   4778  C  CD2 . LEU   D  1 119 ? 11.212  -93.081  -37.569 1.00 39.96 ? 119 LEU   D CD2 1 
ATOM   4779  N  N   . LEU   D  1 120 ? 9.551   -93.574  -33.102 1.00 36.74 ? 120 LEU   D N   1 
ATOM   4780  C  CA  . LEU   D  1 120 ? 8.390   -94.413  -32.809 1.00 30.84 ? 120 LEU   D CA  1 
ATOM   4781  C  C   . LEU   D  1 120 ? 7.505   -93.799  -31.720 1.00 29.08 ? 120 LEU   D C   1 
ATOM   4782  O  O   . LEU   D  1 120 ? 6.283   -93.966  -31.744 1.00 36.81 ? 120 LEU   D O   1 
ATOM   4783  C  CB  . LEU   D  1 120 ? 8.837   -95.826  -32.418 1.00 42.02 ? 120 LEU   D CB  1 
ATOM   4784  C  CG  . LEU   D  1 120 ? 9.577   -96.617  -33.515 1.00 40.96 ? 120 LEU   D CG  1 
ATOM   4785  C  CD1 . LEU   D  1 120 ? 10.118  -97.931  -32.970 1.00 45.14 ? 120 LEU   D CD1 1 
ATOM   4786  C  CD2 . LEU   D  1 120 ? 8.680   -96.885  -34.730 1.00 37.63 ? 120 LEU   D CD2 1 
ATOM   4787  N  N   . LYS   D  1 121 ? 8.102   -93.103  -30.762 1.00 37.06 ? 121 LYS   D N   1 
ATOM   4788  C  CA  . LYS   D  1 121 ? 7.305   -92.390  -29.774 1.00 32.64 ? 121 LYS   D CA  1 
ATOM   4789  C  C   . LYS   D  1 121 ? 6.424   -91.333  -30.445 1.00 34.95 ? 121 LYS   D C   1 
ATOM   4790  O  O   . LYS   D  1 121 ? 5.246   -91.179  -30.096 1.00 31.26 ? 121 LYS   D O   1 
ATOM   4791  C  CB  . LYS   D  1 121 ? 8.238   -91.771  -28.736 1.00 29.39 ? 121 LYS   D CB  1 
ATOM   4792  C  CG  . LYS   D  1 121 ? 7.549   -91.007  -27.638 1.00 38.91 ? 121 LYS   D CG  1 
ATOM   4793  C  CD  . LYS   D  1 121 ? 7.355   -89.526  -27.974 1.00 43.31 ? 121 LYS   D CD  1 
ATOM   4794  C  CE  . LYS   D  1 121 ? 8.674   -88.803  -27.959 1.00 42.83 ? 121 LYS   D CE  1 
ATOM   4795  N  NZ  . LYS   D  1 121 ? 8.519   -87.389  -28.347 1.00 42.81 ? 121 LYS   D NZ  1 
ATOM   4796  N  N   . ASP   D  1 122 ? 6.976   -90.597  -31.417 1.00 34.91 ? 122 ASP   D N   1 
ATOM   4797  C  CA  . ASP   D  1 122 ? 6.172   -89.583  -32.095 1.00 34.92 ? 122 ASP   D CA  1 
ATOM   4798  C  C   . ASP   D  1 122 ? 5.049   -90.234  -32.876 1.00 35.96 ? 122 ASP   D C   1 
ATOM   4799  O  O   . ASP   D  1 122 ? 3.920   -89.735  -32.886 1.00 30.92 ? 122 ASP   D O   1 
ATOM   4800  C  CB  . ASP   D  1 122 ? 7.039   -88.723  -33.019 1.00 30.21 ? 122 ASP   D CB  1 
ATOM   4801  C  CG  . ASP   D  1 122 ? 8.016   -87.819  -32.253 1.00 37.32 ? 122 ASP   D CG  1 
ATOM   4802  O  OD1 . ASP   D  1 122 ? 7.788   -87.503  -31.076 1.00 41.28 ? 122 ASP   D OD1 1 
ATOM   4803  O  OD2 . ASP   D  1 122 ? 9.021   -87.400  -32.836 1.00 39.13 ? 122 ASP   D OD2 1 
ATOM   4804  N  N   . ILE   D  1 123 ? 5.334   -91.356  -33.537 1.00 34.19 ? 123 ILE   D N   1 
ATOM   4805  C  CA  . ILE   D  1 123 ? 4.272   -92.068  -34.232 1.00 27.59 ? 123 ILE   D CA  1 
ATOM   4806  C  C   . ILE   D  1 123 ? 3.218   -92.529  -33.229 1.00 29.10 ? 123 ILE   D C   1 
ATOM   4807  O  O   . ILE   D  1 123 ? 2.011   -92.434  -33.482 1.00 33.80 ? 123 ILE   D O   1 
ATOM   4808  C  CB  . ILE   D  1 123 ? 4.845   -93.244  -35.053 1.00 33.84 ? 123 ILE   D CB  1 
ATOM   4809  C  CG1 . ILE   D  1 123 ? 5.674   -92.735  -36.229 1.00 33.94 ? 123 ILE   D CG1 1 
ATOM   4810  C  CG2 . ILE   D  1 123 ? 3.720   -94.102  -35.636 1.00 37.09 ? 123 ILE   D CG2 1 
ATOM   4811  C  CD1 . ILE   D  1 123 ? 6.388   -93.831  -36.993 1.00 36.09 ? 123 ILE   D CD1 1 
ATOM   4812  N  N   . LEU   D  1 124 ? 3.664   -93.031  -32.071 1.00 34.15 ? 124 LEU   D N   1 
ATOM   4813  C  CA  . LEU   D  1 124 ? 2.728   -93.516  -31.053 1.00 31.05 ? 124 LEU   D CA  1 
ATOM   4814  C  C   . LEU   D  1 124 ? 1.805   -92.402  -30.575 1.00 29.82 ? 124 LEU   D C   1 
ATOM   4815  O  O   . LEU   D  1 124 ? 0.602   -92.619  -30.379 1.00 34.24 ? 124 LEU   D O   1 
ATOM   4816  C  CB  . LEU   D  1 124 ? 3.511   -94.102  -29.884 1.00 33.13 ? 124 LEU   D CB  1 
ATOM   4817  C  CG  . LEU   D  1 124 ? 2.716   -94.609  -28.674 1.00 32.73 ? 124 LEU   D CG  1 
ATOM   4818  C  CD1 . LEU   D  1 124 ? 1.685   -95.673  -29.020 1.00 35.32 ? 124 LEU   D CD1 1 
ATOM   4819  C  CD2 . LEU   D  1 124 ? 3.650   -95.169  -27.644 1.00 35.02 ? 124 LEU   D CD2 1 
ATOM   4820  N  N   . GLU   D  1 125 ? 2.349   -91.196  -30.397 1.00 32.54 ? 125 GLU   D N   1 
ATOM   4821  C  CA  . GLU   D  1 125 ? 1.518   -90.053  -30.012 1.00 35.40 ? 125 GLU   D CA  1 
ATOM   4822  C  C   . GLU   D  1 125 ? 0.454   -89.776  -31.057 1.00 34.31 ? 125 GLU   D C   1 
ATOM   4823  O  O   . GLU   D  1 125 ? -0.710  -89.515  -30.722 1.00 33.20 ? 125 GLU   D O   1 
ATOM   4824  C  CB  . GLU   D  1 125 ? 2.395   -88.810  -29.790 1.00 37.74 ? 125 GLU   D CB  1 
ATOM   4825  C  CG  . GLU   D  1 125 ? 3.209   -88.910  -28.517 1.00 35.91 ? 125 GLU   D CG  1 
ATOM   4826  C  CD  . GLU   D  1 125 ? 4.158   -87.749  -28.239 1.00 44.22 ? 125 GLU   D CD  1 
ATOM   4827  O  OE1 . GLU   D  1 125 ? 4.750   -87.150  -29.175 1.00 42.67 ? 125 GLU   D OE1 1 
ATOM   4828  O  OE2 . GLU   D  1 125 ? 4.355   -87.475  -27.034 1.00 45.85 ? 125 GLU   D OE2 1 
ATOM   4829  N  N   . SER   D  1 126 ? 0.820   -89.843  -32.340 1.00 35.73 ? 126 SER   D N   1 
ATOM   4830  C  CA  A SER   D  1 126 ? -0.180  -89.652  -33.378 0.50 34.60 ? 126 SER   D CA  1 
ATOM   4831  C  CA  B SER   D  1 126 ? -0.178  -89.656  -33.388 0.50 34.60 ? 126 SER   D CA  1 
ATOM   4832  C  C   . SER   D  1 126 ? -1.248  -90.737  -33.317 1.00 31.37 ? 126 SER   D C   1 
ATOM   4833  O  O   . SER   D  1 126 ? -2.446  -90.451  -33.454 1.00 34.64 ? 126 SER   D O   1 
ATOM   4834  C  CB  A SER   D  1 126 ? 0.486   -89.641  -34.751 0.50 31.77 ? 126 SER   D CB  1 
ATOM   4835  C  CB  B SER   D  1 126 ? 0.483   -89.663  -34.770 0.50 31.76 ? 126 SER   D CB  1 
ATOM   4836  O  OG  A SER   D  1 126 ? -0.492  -89.484  -35.744 0.50 28.64 ? 126 SER   D OG  1 
ATOM   4837  O  OG  B SER   D  1 126 ? 1.458   -88.646  -34.879 0.50 37.64 ? 126 SER   D OG  1 
ATOM   4838  N  N   . GLU   D  1 127 ? -0.835  -91.993  -33.114 1.00 31.54 ? 127 GLU   D N   1 
ATOM   4839  C  CA  . GLU   D  1 127 ? -1.814  -93.078  -33.127 1.00 41.13 ? 127 GLU   D CA  1 
ATOM   4840  C  C   . GLU   D  1 127 ? -2.735  -93.012  -31.909 1.00 30.24 ? 127 GLU   D C   1 
ATOM   4841  O  O   . GLU   D  1 127 ? -3.929  -93.306  -32.016 1.00 37.12 ? 127 GLU   D O   1 
ATOM   4842  C  CB  . GLU   D  1 127 ? -1.107  -94.433  -33.200 1.00 35.59 ? 127 GLU   D CB  1 
ATOM   4843  C  CG  . GLU   D  1 127 ? -0.210  -94.637  -34.421 1.00 37.17 ? 127 GLU   D CG  1 
ATOM   4844  C  CD  . GLU   D  1 127 ? -0.877  -94.230  -35.727 1.00 40.42 ? 127 GLU   D CD  1 
ATOM   4845  O  OE1 . GLU   D  1 127 ? -2.101  -94.399  -35.868 1.00 42.06 ? 127 GLU   D OE1 1 
ATOM   4846  O  OE2 . GLU   D  1 127 ? -0.163  -93.719  -36.609 1.00 55.25 ? 127 GLU   D OE2 1 
ATOM   4847  N  N   . GLU   D  1 128 ? -2.205  -92.637  -30.742 1.00 32.50 ? 128 GLU   D N   1 
ATOM   4848  C  CA  . GLU   D  1 128 ? -3.103  -92.478  -29.606 1.00 30.06 ? 128 GLU   D CA  1 
ATOM   4849  C  C   . GLU   D  1 128 ? -4.082  -91.326  -29.830 1.00 34.58 ? 128 GLU   D C   1 
ATOM   4850  O  O   . GLU   D  1 128 ? -5.245  -91.426  -29.425 1.00 32.99 ? 128 GLU   D O   1 
ATOM   4851  C  CB  . GLU   D  1 128 ? -2.306  -92.311  -28.313 1.00 33.04 ? 128 GLU   D CB  1 
ATOM   4852  C  CG  . GLU   D  1 128 ? -1.796  -93.638  -27.742 1.00 41.03 ? 128 GLU   D CG  1 
ATOM   4853  C  CD  . GLU   D  1 128 ? -1.129  -93.488  -26.381 1.00 37.29 ? 128 GLU   D CD  1 
ATOM   4854  O  OE1 . GLU   D  1 128 ? -1.418  -92.495  -25.691 1.00 39.36 ? 128 GLU   D OE1 1 
ATOM   4855  O  OE2 . GLU   D  1 128 ? -0.300  -94.343  -26.000 1.00 41.78 ? 128 GLU   D OE2 1 
ATOM   4856  N  N   . GLU   D  1 129 ? -3.666  -90.254  -30.521 1.00 39.77 ? 129 GLU   D N   1 
ATOM   4857  C  CA  . GLU   D  1 129 ? -4.633  -89.215  -30.886 1.00 36.10 ? 129 GLU   D CA  1 
ATOM   4858  C  C   . GLU   D  1 129 ? -5.732  -89.778  -31.782 1.00 30.27 ? 129 GLU   D C   1 
ATOM   4859  O  O   . GLU   D  1 129 ? -6.908  -89.440  -31.635 1.00 38.38 ? 129 GLU   D O   1 
ATOM   4860  C  CB  . GLU   D  1 129 ? -3.925  -88.051  -31.585 1.00 34.89 ? 129 GLU   D CB  1 
ATOM   4861  C  CG  . GLU   D  1 129 ? -3.116  -87.164  -30.648 1.00 45.55 ? 129 GLU   D CG  1 
ATOM   4862  C  CD  . GLU   D  1 129 ? -2.561  -85.909  -31.322 1.00 62.79 ? 129 GLU   D CD  1 
ATOM   4863  O  OE1 . GLU   D  1 129 ? -3.136  -85.452  -32.335 1.00 66.05 ? 129 GLU   D OE1 1 
ATOM   4864  O  OE2 . GLU   D  1 129 ? -1.545  -85.371  -30.827 1.00 66.24 ? 129 GLU   D OE2 1 
ATOM   4865  N  N   . HIS   D  1 130 ? -5.356  -90.623  -32.739 1.00 32.66 ? 130 HIS   D N   1 
ATOM   4866  C  CA  . HIS   D  1 130 ? -6.340  -91.284  -33.577 1.00 33.15 ? 130 HIS   D CA  1 
ATOM   4867  C  C   . HIS   D  1 130 ? -7.262  -92.176  -32.752 1.00 36.27 ? 130 HIS   D C   1 
ATOM   4868  O  O   . HIS   D  1 130 ? -8.475  -92.191  -32.970 1.00 32.03 ? 130 HIS   D O   1 
ATOM   4869  C  CB  . HIS   D  1 130 ? -5.608  -92.092  -34.665 1.00 39.32 ? 130 HIS   D CB  1 
ATOM   4870  C  CG  . HIS   D  1 130 ? -6.483  -92.503  -35.807 1.00 60.07 ? 130 HIS   D CG  1 
ATOM   4871  N  ND1 . HIS   D  1 130 ? -6.025  -93.265  -36.861 1.00 68.51 ? 130 HIS   D ND1 1 
ATOM   4872  C  CD2 . HIS   D  1 130 ? -7.786  -92.242  -36.071 1.00 60.93 ? 130 HIS   D CD2 1 
ATOM   4873  C  CE1 . HIS   D  1 130 ? -7.013  -93.469  -37.715 1.00 61.91 ? 130 HIS   D CE1 1 
ATOM   4874  N  NE2 . HIS   D  1 130 ? -8.092  -92.860  -37.260 1.00 56.85 ? 130 HIS   D NE2 1 
ATOM   4875  N  N   . ILE   D  1 131 ? -6.704  -92.941  -31.810 1.00 36.98 ? 131 ILE   D N   1 
ATOM   4876  C  CA  . ILE   D  1 131 ? -7.547  -93.764  -30.942 1.00 36.31 ? 131 ILE   D CA  1 
ATOM   4877  C  C   . ILE   D  1 131 ? -8.557  -92.894  -30.196 1.00 36.04 ? 131 ILE   D C   1 
ATOM   4878  O  O   . ILE   D  1 131 ? -9.758  -93.196  -30.150 1.00 37.32 ? 131 ILE   D O   1 
ATOM   4879  C  CB  . ILE   D  1 131 ? -6.667  -94.585  -29.978 1.00 35.10 ? 131 ILE   D CB  1 
ATOM   4880  C  CG1 . ILE   D  1 131 ? -5.935  -95.663  -30.776 1.00 35.51 ? 131 ILE   D CG1 1 
ATOM   4881  C  CG2 . ILE   D  1 131 ? -7.520  -95.204  -28.856 1.00 37.55 ? 131 ILE   D CG2 1 
ATOM   4882  C  CD1 . ILE   D  1 131 ? -4.886  -96.406  -29.996 1.00 33.40 ? 131 ILE   D CD1 1 
ATOM   4883  N  N   . ASP   D  1 132 ? -8.083  -91.801  -29.594 1.00 34.64 ? 132 ASP   D N   1 
ATOM   4884  C  CA  . ASP   D  1 132 ? -8.981  -90.851  -28.939 1.00 34.68 ? 132 ASP   D CA  1 
ATOM   4885  C  C   . ASP   D  1 132 ? -10.110 -90.433  -29.875 1.00 36.05 ? 132 ASP   D C   1 
ATOM   4886  O  O   . ASP   D  1 132 ? -11.294 -90.437  -29.506 1.00 37.54 ? 132 ASP   D O   1 
ATOM   4887  C  CB  . ASP   D  1 132 ? -8.165  -89.631  -28.500 1.00 36.65 ? 132 ASP   D CB  1 
ATOM   4888  C  CG  . ASP   D  1 132 ? -8.936  -88.697  -27.568 1.00 43.36 ? 132 ASP   D CG  1 
ATOM   4889  O  OD1 . ASP   D  1 132 ? -10.065 -89.037  -27.181 1.00 41.43 ? 132 ASP   D OD1 1 
ATOM   4890  O  OD2 . ASP   D  1 132 ? -8.390  -87.629  -27.214 1.00 43.50 ? 132 ASP   D OD2 1 
ATOM   4891  N  N   . TYR   D  1 133 ? -9.746  -90.053  -31.100 1.00 32.67 ? 133 TYR   D N   1 
ATOM   4892  C  CA  . TYR   D  1 133 ? -10.742 -89.655  -32.079 1.00 30.98 ? 133 TYR   D CA  1 
ATOM   4893  C  C   . TYR   D  1 133 ? -11.759 -90.774  -32.293 1.00 33.60 ? 133 TYR   D C   1 
ATOM   4894  O  O   . TYR   D  1 133 ? -12.970 -90.552  -32.226 1.00 31.61 ? 133 TYR   D O   1 
ATOM   4895  C  CB  . TYR   D  1 133 ? -10.049 -89.274  -33.396 1.00 36.07 ? 133 TYR   D CB  1 
ATOM   4896  C  CG  . TYR   D  1 133 ? -11.017 -89.194  -34.550 1.00 38.49 ? 133 TYR   D CG  1 
ATOM   4897  C  CD1 . TYR   D  1 133 ? -11.846 -88.093  -34.710 1.00 36.50 ? 133 TYR   D CD1 1 
ATOM   4898  C  CD2 . TYR   D  1 133 ? -11.123 -90.235  -35.461 1.00 42.09 ? 133 TYR   D CD2 1 
ATOM   4899  C  CE1 . TYR   D  1 133 ? -12.755 -88.026  -35.751 1.00 39.26 ? 133 TYR   D CE1 1 
ATOM   4900  C  CE2 . TYR   D  1 133 ? -12.038 -90.178  -36.507 1.00 38.65 ? 133 TYR   D CE2 1 
ATOM   4901  C  CZ  . TYR   D  1 133 ? -12.843 -89.070  -36.638 1.00 38.53 ? 133 TYR   D CZ  1 
ATOM   4902  O  OH  . TYR   D  1 133 ? -13.732 -89.003  -37.662 1.00 37.87 ? 133 TYR   D OH  1 
ATOM   4903  N  N   . LEU   D  1 134 ? -11.272 -91.993  -32.543 1.00 39.24 ? 134 LEU   D N   1 
ATOM   4904  C  CA  . LEU   D  1 134 ? -12.162 -93.104  -32.860 1.00 34.53 ? 134 LEU   D CA  1 
ATOM   4905  C  C   . LEU   D  1 134 ? -13.056 -93.454  -31.673 1.00 30.30 ? 134 LEU   D C   1 
ATOM   4906  O  O   . LEU   D  1 134 ? -14.277 -93.586  -31.818 1.00 34.15 ? 134 LEU   D O   1 
ATOM   4907  C  CB  . LEU   D  1 134 ? -11.322 -94.307  -33.293 1.00 34.46 ? 134 LEU   D CB  1 
ATOM   4908  C  CG  . LEU   D  1 134 ? -10.590 -94.106  -34.617 1.00 40.14 ? 134 LEU   D CG  1 
ATOM   4909  C  CD1 . LEU   D  1 134 ? -9.611  -95.201  -34.851 1.00 39.09 ? 134 LEU   D CD1 1 
ATOM   4910  C  CD2 . LEU   D  1 134 ? -11.584 -94.050  -35.780 1.00 39.00 ? 134 LEU   D CD2 1 
ATOM   4911  N  N   . GLU   D  1 135 ? -12.466 -93.610  -30.488 1.00 34.51 ? 135 GLU   D N   1 
ATOM   4912  C  CA  . GLU   D  1 135 ? -13.273 -93.862  -29.294 1.00 40.21 ? 135 GLU   D CA  1 
ATOM   4913  C  C   . GLU   D  1 135 ? -14.329 -92.779  -29.117 1.00 39.98 ? 135 GLU   D C   1 
ATOM   4914  O  O   . GLU   D  1 135 ? -15.487 -93.063  -28.791 1.00 41.44 ? 135 GLU   D O   1 
ATOM   4915  C  CB  . GLU   D  1 135 ? -12.357 -93.945  -28.068 1.00 43.29 ? 135 GLU   D CB  1 
ATOM   4916  C  CG  . GLU   D  1 135 ? -11.501 -95.191  -28.063 1.00 38.75 ? 135 GLU   D CG  1 
ATOM   4917  C  CD  . GLU   D  1 135 ? -10.514 -95.241  -26.915 1.00 42.22 ? 135 GLU   D CD  1 
ATOM   4918  O  OE1 . GLU   D  1 135 ? -10.167 -94.177  -26.347 1.00 42.26 ? 135 GLU   D OE1 1 
ATOM   4919  O  OE2 . GLU   D  1 135 ? -10.073 -96.358  -26.589 1.00 47.82 ? 135 GLU   D OE2 1 
ATOM   4920  N  N   . THR   D  1 136 ? -13.951 -91.525  -29.354 1.00 37.85 ? 136 THR   D N   1 
ATOM   4921  C  CA  . THR   D  1 136 ? -14.910 -90.441  -29.216 1.00 39.31 ? 136 THR   D CA  1 
ATOM   4922  C  C   . THR   D  1 136 ? -16.039 -90.545  -30.242 1.00 34.90 ? 136 THR   D C   1 
ATOM   4923  O  O   . THR   D  1 136 ? -17.210 -90.359  -29.893 1.00 35.57 ? 136 THR   D O   1 
ATOM   4924  C  CB  . THR   D  1 136 ? -14.180 -89.107  -29.328 1.00 40.56 ? 136 THR   D CB  1 
ATOM   4925  O  OG1 . THR   D  1 136 ? -13.204 -89.019  -28.283 1.00 39.72 ? 136 THR   D OG1 1 
ATOM   4926  C  CG2 . THR   D  1 136 ? -15.163 -87.952  -29.219 1.00 40.37 ? 136 THR   D CG2 1 
ATOM   4927  N  N   . GLN   D  1 137 ? -15.720 -90.850  -31.509 1.00 31.10 ? 137 GLN   D N   1 
ATOM   4928  C  CA  . GLN   D  1 137 ? -16.784 -91.019  -32.505 1.00 31.83 ? 137 GLN   D CA  1 
ATOM   4929  C  C   . GLN   D  1 137 ? -17.744 -92.143  -32.112 1.00 32.70 ? 137 GLN   D C   1 
ATOM   4930  O  O   . GLN   D  1 137 ? -18.959 -92.012  -32.247 1.00 32.51 ? 137 GLN   D O   1 
ATOM   4931  C  CB  . GLN   D  1 137 ? -16.202 -91.318  -33.883 1.00 35.52 ? 137 GLN   D CB  1 
ATOM   4932  C  CG  . GLN   D  1 137 ? -15.336 -90.247  -34.473 1.00 36.32 ? 137 GLN   D CG  1 
ATOM   4933  C  CD  . GLN   D  1 137 ? -15.809 -88.861  -34.119 1.00 29.22 ? 137 GLN   D CD  1 
ATOM   4934  O  OE1 . GLN   D  1 137 ? -16.807 -88.367  -34.656 1.00 38.86 ? 137 GLN   D OE1 1 
ATOM   4935  N  NE2 . GLN   D  1 137 ? -15.092 -88.224  -33.215 1.00 37.95 ? 137 GLN   D NE2 1 
ATOM   4936  N  N   . LEU   D  1 138 ? -17.207 -93.273  -31.664 1.00 40.44 ? 138 LEU   D N   1 
ATOM   4937  C  CA  . LEU   D  1 138 ? -18.070 -94.381  -31.285 1.00 39.98 ? 138 LEU   D CA  1 
ATOM   4938  C  C   . LEU   D  1 138 ? -18.952 -93.997  -30.104 1.00 35.99 ? 138 LEU   D C   1 
ATOM   4939  O  O   . LEU   D  1 138 ? -20.153 -94.287  -30.098 1.00 35.25 ? 138 LEU   D O   1 
ATOM   4940  C  CB  . LEU   D  1 138 ? -17.205 -95.605  -30.984 1.00 39.39 ? 138 LEU   D CB  1 
ATOM   4941  C  CG  . LEU   D  1 138 ? -16.695 -96.201  -32.304 1.00 34.30 ? 138 LEU   D CG  1 
ATOM   4942  C  CD1 . LEU   D  1 138 ? -15.487 -97.073  -32.078 1.00 49.80 ? 138 LEU   D CD1 1 
ATOM   4943  C  CD2 . LEU   D  1 138 ? -17.795 -96.983  -32.995 1.00 42.17 ? 138 LEU   D CD2 1 
ATOM   4944  N  N   . GLY   D  1 139 ? -18.387 -93.297  -29.119 1.00 42.29 ? 139 GLY   D N   1 
ATOM   4945  C  CA  . GLY   D  1 139 ? -19.209 -92.777  -28.041 1.00 37.37 ? 139 GLY   D CA  1 
ATOM   4946  C  C   . GLY   D  1 139 ? -20.297 -91.845  -28.532 1.00 40.48 ? 139 GLY   D C   1 
ATOM   4947  O  O   . GLY   D  1 139 ? -21.444 -91.937  -28.088 1.00 42.98 ? 139 GLY   D O   1 
ATOM   4948  N  N   . LEU   D  1 140 ? -19.965 -90.945  -29.471 1.00 38.31 ? 140 LEU   D N   1 
ATOM   4949  C  CA  . LEU   D  1 140 ? -20.958 -89.972  -29.927 1.00 40.86 ? 140 LEU   D CA  1 
ATOM   4950  C  C   . LEU   D  1 140 ? -22.132 -90.659  -30.605 1.00 35.90 ? 140 LEU   D C   1 
ATOM   4951  O  O   . LEU   D  1 140 ? -23.266 -90.186  -30.506 1.00 35.34 ? 140 LEU   D O   1 
ATOM   4952  C  CB  . LEU   D  1 140 ? -20.334 -88.949  -30.888 1.00 44.08 ? 140 LEU   D CB  1 
ATOM   4953  C  CG  . LEU   D  1 140 ? -19.460 -87.854  -30.264 1.00 44.87 ? 140 LEU   D CG  1 
ATOM   4954  C  CD1 . LEU   D  1 140 ? -18.695 -87.015  -31.330 1.00 36.12 ? 140 LEU   D CD1 1 
ATOM   4955  C  CD2 . LEU   D  1 140 ? -20.319 -86.978  -29.378 1.00 37.69 ? 140 LEU   D CD2 1 
ATOM   4956  N  N   . ILE   D  1 141 ? -21.874 -91.738  -31.354 1.00 39.01 ? 141 ILE   D N   1 
ATOM   4957  C  CA  . ILE   D  1 141 ? -22.971 -92.470  -31.984 1.00 35.14 ? 141 ILE   D CA  1 
ATOM   4958  C  C   . ILE   D  1 141 ? -23.974 -92.925  -30.926 1.00 40.34 ? 141 ILE   D C   1 
ATOM   4959  O  O   . ILE   D  1 141 ? -25.192 -92.826  -31.114 1.00 37.18 ? 141 ILE   D O   1 
ATOM   4960  C  CB  . ILE   D  1 141 ? -22.423 -93.664  -32.788 1.00 35.90 ? 141 ILE   D CB  1 
ATOM   4961  C  CG1 . ILE   D  1 141 ? -21.706 -93.183  -34.047 1.00 39.28 ? 141 ILE   D CG1 1 
ATOM   4962  C  CG2 . ILE   D  1 141 ? -23.554 -94.613  -33.160 1.00 38.29 ? 141 ILE   D CG2 1 
ATOM   4963  C  CD1 . ILE   D  1 141 ? -20.804 -94.235  -34.662 1.00 42.76 ? 141 ILE   D CD1 1 
ATOM   4964  N  N   . GLN   D  1 142 ? -23.477 -93.414  -29.789 1.00 35.77 ? 142 GLN   D N   1 
ATOM   4965  C  CA  . GLN   D  1 142 ? -24.372 -93.795  -28.690 1.00 41.36 ? 142 GLN   D CA  1 
ATOM   4966  C  C   . GLN   D  1 142 ? -25.106 -92.590  -28.097 1.00 39.92 ? 142 GLN   D C   1 
ATOM   4967  O  O   . GLN   D  1 142 ? -26.293 -92.678  -27.772 1.00 40.26 ? 142 GLN   D O   1 
ATOM   4968  C  CB  . GLN   D  1 142 ? -23.571 -94.515  -27.605 1.00 36.40 ? 142 GLN   D CB  1 
ATOM   4969  C  CG  . GLN   D  1 142 ? -22.848 -95.740  -28.099 1.00 42.34 ? 142 GLN   D CG  1 
ATOM   4970  C  CD  . GLN   D  1 142 ? -23.795 -96.763  -28.708 1.00 51.52 ? 142 GLN   D CD  1 
ATOM   4971  O  OE1 . GLN   D  1 142 ? -24.903 -96.977  -28.209 1.00 61.66 ? 142 GLN   D OE1 1 
ATOM   4972  N  NE2 . GLN   D  1 142 ? -23.363 -97.397  -29.790 1.00 50.38 ? 142 GLN   D NE2 1 
ATOM   4973  N  N   . LYS   D  1 143 ? -24.429 -91.450  -27.943 1.00 45.23 ? 143 LYS   D N   1 
ATOM   4974  C  CA  . LYS   D  1 143 ? -25.044 -90.328  -27.233 1.00 37.81 ? 143 LYS   D CA  1 
ATOM   4975  C  C   . LYS   D  1 143 ? -26.052 -89.561  -28.083 1.00 36.33 ? 143 LYS   D C   1 
ATOM   4976  O  O   . LYS   D  1 143 ? -27.111 -89.169  -27.580 1.00 37.80 ? 143 LYS   D O   1 
ATOM   4977  C  CB  . LYS   D  1 143 ? -23.958 -89.369  -26.726 1.00 42.35 ? 143 LYS   D CB  1 
ATOM   4978  C  CG  . LYS   D  1 143 ? -23.052 -89.961  -25.643 1.00 50.50 ? 143 LYS   D CG  1 
ATOM   4979  C  CD  . LYS   D  1 143 ? -22.046 -88.928  -25.090 1.00 47.40 ? 143 LYS   D CD  1 
ATOM   4980  C  CE  . LYS   D  1 143 ? -21.302 -89.449  -23.851 1.00 53.31 ? 143 LYS   D CE  1 
ATOM   4981  N  NZ  . LYS   D  1 143 ? -20.165 -90.384  -24.145 1.00 59.08 ? 143 LYS   D NZ  1 
ATOM   4982  N  N   . VAL   D  1 144 ? -25.745 -89.296  -29.360 1.00 36.18 ? 144 VAL   D N   1 
ATOM   4983  C  CA  . VAL   D  1 144 ? -26.647 -88.509  -30.199 1.00 33.98 ? 144 VAL   D CA  1 
ATOM   4984  C  C   . VAL   D  1 144 ? -27.537 -89.377  -31.089 1.00 33.14 ? 144 VAL   D C   1 
ATOM   4985  O  O   . VAL   D  1 144 ? -28.550 -88.876  -31.602 1.00 35.71 ? 144 VAL   D O   1 
ATOM   4986  C  CB  . VAL   D  1 144 ? -25.875 -87.494  -31.078 1.00 36.91 ? 144 VAL   D CB  1 
ATOM   4987  C  CG1 . VAL   D  1 144 ? -24.897 -86.708  -30.254 1.00 33.88 ? 144 VAL   D CG1 1 
ATOM   4988  C  CG2 . VAL   D  1 144 ? -25.166 -88.183  -32.232 1.00 33.94 ? 144 VAL   D CG2 1 
ATOM   4989  N  N   . GLY   D  1 145 ? -27.222 -90.651  -31.250 1.00 34.98 ? 145 GLY   D N   1 
ATOM   4990  C  CA  . GLY   D  1 145 ? -27.962 -91.533  -32.135 1.00 44.01 ? 145 GLY   D CA  1 
ATOM   4991  C  C   . GLY   D  1 145 ? -27.292 -91.637  -33.493 1.00 39.28 ? 145 GLY   D C   1 
ATOM   4992  O  O   . GLY   D  1 145 ? -26.650 -90.699  -33.972 1.00 37.95 ? 145 GLY   D O   1 
ATOM   4993  N  N   . LEU   D  1 146 ? -27.439 -92.795  -34.131 1.00 35.08 ? 146 LEU   D N   1 
ATOM   4994  C  CA  . LEU   D  1 146 ? -26.741 -93.024  -35.395 1.00 44.10 ? 146 LEU   D CA  1 
ATOM   4995  C  C   . LEU   D  1 146 ? -27.175 -92.027  -36.468 1.00 36.05 ? 146 LEU   D C   1 
ATOM   4996  O  O   . LEU   D  1 146 ? -26.338 -91.473  -37.191 1.00 36.86 ? 146 LEU   D O   1 
ATOM   4997  C  CB  . LEU   D  1 146 ? -26.981 -94.453  -35.879 1.00 39.20 ? 146 LEU   D CB  1 
ATOM   4998  C  CG  . LEU   D  1 146 ? -26.294 -94.786  -37.205 1.00 35.89 ? 146 LEU   D CG  1 
ATOM   4999  C  CD1 . LEU   D  1 146 ? -24.848 -94.452  -37.144 1.00 37.86 ? 146 LEU   D CD1 1 
ATOM   5000  C  CD2 . LEU   D  1 146 ? -26.507 -96.259  -37.573 1.00 42.14 ? 146 LEU   D CD2 1 
ATOM   5001  N  N   . GLU   D  1 147 ? -28.482 -91.813  -36.607 1.00 33.86 ? 147 GLU   D N   1 
ATOM   5002  C  CA  . GLU   D  1 147 ? -28.979 -90.918  -37.646 1.00 37.80 ? 147 GLU   D CA  1 
ATOM   5003  C  C   . GLU   D  1 147 ? -28.424 -89.501  -37.470 1.00 43.49 ? 147 GLU   D C   1 
ATOM   5004  O  O   . GLU   D  1 147 ? -27.975 -88.873  -38.442 1.00 33.31 ? 147 GLU   D O   1 
ATOM   5005  C  CB  . GLU   D  1 147 ? -30.513 -90.913  -37.647 1.00 41.16 ? 147 GLU   D CB  1 
ATOM   5006  C  CG  . GLU   D  1 147 ? -31.160 -92.188  -38.228 1.00 43.40 ? 147 GLU   D CG  1 
ATOM   5007  C  CD  . GLU   D  1 147 ? -32.641 -92.003  -38.584 1.00 54.64 ? 147 GLU   D CD  1 
ATOM   5008  O  OE1 . GLU   D  1 147 ? -33.356 -91.256  -37.878 1.00 66.65 ? 147 GLU   D OE1 1 
ATOM   5009  O  OE2 . GLU   D  1 147 ? -33.090 -92.593  -39.586 1.00 57.43 ? 147 GLU   D OE2 1 
ATOM   5010  N  N   . ASN   D  1 148 ? -28.459 -88.976  -36.235 1.00 36.42 ? 148 ASN   D N   1 
ATOM   5011  C  CA  . ASN   D  1 148 ? -27.914 -87.643  -35.968 1.00 34.40 ? 148 ASN   D CA  1 
ATOM   5012  C  C   . ASN   D  1 148 ? -26.409 -87.601  -36.210 1.00 34.28 ? 148 ASN   D C   1 
ATOM   5013  O  O   . ASN   D  1 148 ? -25.896 -86.625  -36.770 1.00 39.74 ? 148 ASN   D O   1 
ATOM   5014  C  CB  . ASN   D  1 148 ? -28.218 -87.211  -34.531 1.00 35.28 ? 148 ASN   D CB  1 
ATOM   5015  C  CG  . ASN   D  1 148 ? -29.595 -86.568  -34.366 1.00 35.44 ? 148 ASN   D CG  1 
ATOM   5016  O  OD1 . ASN   D  1 148 ? -30.335 -86.327  -35.321 1.00 31.32 ? 148 ASN   D OD1 1 
ATOM   5017  N  ND2 . ASN   D  1 148 ? -29.930 -86.263  -33.117 1.00 38.79 ? 148 ASN   D ND2 1 
ATOM   5018  N  N   . TYR   D  1 149 ? -25.678 -88.640  -35.779 1.00 30.62 ? 149 TYR   D N   1 
ATOM   5019  C  CA  . TYR   D  1 149 ? -24.244 -88.666  -36.001 1.00 40.47 ? 149 TYR   D CA  1 
ATOM   5020  C  C   . TYR   D  1 149 ? -23.950 -88.605  -37.485 1.00 41.49 ? 149 TYR   D C   1 
ATOM   5021  O  O   . TYR   D  1 149 ? -23.069 -87.857  -37.924 1.00 31.86 ? 149 TYR   D O   1 
ATOM   5022  C  CB  . TYR   D  1 149 ? -23.602 -89.915  -35.397 1.00 30.91 ? 149 TYR   D CB  1 
ATOM   5023  C  CG  . TYR   D  1 149 ? -22.110 -89.951  -35.624 1.00 40.43 ? 149 TYR   D CG  1 
ATOM   5024  C  CD1 . TYR   D  1 149 ? -21.252 -89.226  -34.808 1.00 38.05 ? 149 TYR   D CD1 1 
ATOM   5025  C  CD2 . TYR   D  1 149 ? -21.556 -90.693  -36.664 1.00 39.87 ? 149 TYR   D CD2 1 
ATOM   5026  C  CE1 . TYR   D  1 149 ? -19.904 -89.233  -35.012 1.00 33.62 ? 149 TYR   D CE1 1 
ATOM   5027  C  CE2 . TYR   D  1 149 ? -20.187 -90.713  -36.870 1.00 34.78 ? 149 TYR   D CE2 1 
ATOM   5028  C  CZ  . TYR   D  1 149 ? -19.373 -89.968  -36.047 1.00 34.14 ? 149 TYR   D CZ  1 
ATOM   5029  O  OH  . TYR   D  1 149 ? -18.021 -89.970  -36.235 1.00 38.28 ? 149 TYR   D OH  1 
ATOM   5030  N  N   . LEU   D  1 150 ? -24.689 -89.377  -38.274 1.00 34.30 ? 150 LEU   D N   1 
ATOM   5031  C  CA  . LEU   D  1 150 ? -24.467 -89.339  -39.709 1.00 37.31 ? 150 LEU   D CA  1 
ATOM   5032  C  C   . LEU   D  1 150 ? -24.830 -87.972  -40.269 1.00 29.72 ? 150 LEU   D C   1 
ATOM   5033  O  O   . LEU   D  1 150 ? -24.054 -87.388  -41.037 1.00 32.84 ? 150 LEU   D O   1 
ATOM   5034  C  CB  . LEU   D  1 150 ? -25.261 -90.449  -40.387 1.00 35.61 ? 150 LEU   D CB  1 
ATOM   5035  C  CG  . LEU   D  1 150 ? -24.805 -91.847  -39.995 1.00 34.30 ? 150 LEU   D CG  1 
ATOM   5036  C  CD1 . LEU   D  1 150 ? -25.651 -92.915  -40.689 1.00 40.63 ? 150 LEU   D CD1 1 
ATOM   5037  C  CD2 . LEU   D  1 150 ? -23.335 -92.053  -40.310 1.00 36.09 ? 150 LEU   D CD2 1 
ATOM   5038  N  N   . GLN   D  1 151 ? -25.973 -87.423  -39.853 1.00 31.44 ? 151 GLN   D N   1 
ATOM   5039  C  CA  . GLN   D  1 151 ? -26.380 -86.111  -40.337 1.00 37.18 ? 151 GLN   D CA  1 
ATOM   5040  C  C   . GLN   D  1 151 ? -25.291 -85.067  -40.095 1.00 40.55 ? 151 GLN   D C   1 
ATOM   5041  O  O   . GLN   D  1 151 ? -25.022 -84.221  -40.963 1.00 32.60 ? 151 GLN   D O   1 
ATOM   5042  C  CB  . GLN   D  1 151 ? -27.683 -85.692  -39.673 1.00 33.34 ? 151 GLN   D CB  1 
ATOM   5043  C  CG  . GLN   D  1 151 ? -28.218 -84.381  -40.153 1.00 36.03 ? 151 GLN   D CG  1 
ATOM   5044  C  CD  . GLN   D  1 151 ? -29.355 -83.884  -39.308 1.00 32.35 ? 151 GLN   D CD  1 
ATOM   5045  O  OE1 . GLN   D  1 151 ? -29.452 -84.182  -38.104 1.00 32.58 ? 151 GLN   D OE1 1 
ATOM   5046  N  NE2 . GLN   D  1 151 ? -30.224 -83.120  -39.918 1.00 32.39 ? 151 GLN   D NE2 1 
ATOM   5047  N  N   . SER   D  1 152 ? -24.651 -85.122  -38.928 1.00 33.19 ? 152 SER   D N   1 
ATOM   5048  C  CA  . SER   D  1 152 ? -23.627 -84.151  -38.566 1.00 36.26 ? 152 SER   D CA  1 
ATOM   5049  C  C   . SER   D  1 152 ? -22.332 -84.346  -39.333 1.00 39.82 ? 152 SER   D C   1 
ATOM   5050  O  O   . SER   D  1 152 ? -21.455 -83.484  -39.236 1.00 39.52 ? 152 SER   D O   1 
ATOM   5051  C  CB  . SER   D  1 152 ? -23.359 -84.210  -37.055 1.00 30.88 ? 152 SER   D CB  1 
ATOM   5052  O  OG  . SER   D  1 152 ? -24.541 -83.829  -36.339 1.00 34.74 ? 152 SER   D OG  1 
ATOM   5053  N  N   . HIS   D  1 153 ? -22.183 -85.438  -40.093 1.00 35.21 ? 153 HIS   D N   1 
ATOM   5054  C  CA  . HIS   D  1 153 ? -20.992 -85.644  -40.898 1.00 37.45 ? 153 HIS   D CA  1 
ATOM   5055  C  C   . HIS   D  1 153 ? -21.277 -85.617  -42.392 1.00 34.25 ? 153 HIS   D C   1 
ATOM   5056  O  O   . HIS   D  1 153 ? -20.433 -86.046  -43.185 1.00 35.16 ? 153 HIS   D O   1 
ATOM   5057  C  CB  . HIS   D  1 153 ? -20.308 -86.936  -40.480 1.00 34.20 ? 153 HIS   D CB  1 
ATOM   5058  C  CG  . HIS   D  1 153 ? -19.660 -86.824  -39.141 1.00 38.73 ? 153 HIS   D CG  1 
ATOM   5059  N  ND1 . HIS   D  1 153 ? -20.389 -86.797  -37.974 1.00 37.65 ? 153 HIS   D ND1 1 
ATOM   5060  C  CD2 . HIS   D  1 153 ? -18.366 -86.644  -38.783 1.00 37.50 ? 153 HIS   D CD2 1 
ATOM   5061  C  CE1 . HIS   D  1 153 ? -19.568 -86.657  -36.948 1.00 39.86 ? 153 HIS   D CE1 1 
ATOM   5062  N  NE2 . HIS   D  1 153 ? -18.334 -86.553  -37.412 1.00 38.66 ? 153 HIS   D NE2 1 
ATOM   5063  N  N   . MET   D  1 154 ? -22.424 -85.074  -42.790 1.00 36.23 ? 154 MET   D N   1 
ATOM   5064  C  CA  . MET   D  1 154 ? -22.758 -84.967  -44.206 1.00 36.97 ? 154 MET   D CA  1 
ATOM   5065  C  C   . MET   D  1 154 ? -21.924 -83.893  -44.898 1.00 42.27 ? 154 MET   D C   1 
ATOM   5066  O  O   . MET   D  1 154 ? -21.336 -84.129  -45.962 1.00 38.61 ? 154 MET   D O   1 
ATOM   5067  C  CB  . MET   D  1 154 ? -24.237 -84.641  -44.365 1.00 39.12 ? 154 MET   D CB  1 
ATOM   5068  C  CG  . MET   D  1 154 ? -25.147 -85.845  -44.343 1.00 50.97 ? 154 MET   D CG  1 
ATOM   5069  S  SD  . MET   D  1 154 ? -26.890 -85.357  -44.339 1.00 52.80 ? 154 MET   D SD  1 
ATOM   5070  C  CE  . MET   D  1 154 ? -26.889 -84.234  -45.752 1.00 44.65 ? 154 MET   D CE  1 
ATOM   5071  N  N   . HIS   D  1 155 ? -21.872 -82.706  -44.312 1.00 42.67 ? 155 HIS   D N   1 
ATOM   5072  C  CA  . HIS   D  1 155 ? -21.256 -81.544  -44.927 1.00 51.98 ? 155 HIS   D CA  1 
ATOM   5073  C  C   . HIS   D  1 155 ? -19.957 -81.202  -44.214 1.00 47.95 ? 155 HIS   D C   1 
ATOM   5074  O  O   . HIS   D  1 155 ? -19.761 -81.510  -43.032 1.00 57.03 ? 155 HIS   D O   1 
ATOM   5075  C  CB  . HIS   D  1 155 ? -22.206 -80.338  -44.889 1.00 47.93 ? 155 HIS   D CB  1 
ATOM   5076  C  CG  . HIS   D  1 155 ? -23.536 -80.592  -45.525 1.00 47.21 ? 155 HIS   D CG  1 
ATOM   5077  N  ND1 . HIS   D  1 155 ? -24.730 -80.352  -44.877 1.00 51.95 ? 155 HIS   D ND1 1 
ATOM   5078  C  CD2 . HIS   D  1 155 ? -23.864 -81.055  -46.757 1.00 58.21 ? 155 HIS   D CD2 1 
ATOM   5079  C  CE1 . HIS   D  1 155 ? -25.735 -80.652  -45.685 1.00 47.29 ? 155 HIS   D CE1 1 
ATOM   5080  N  NE2 . HIS   D  1 155 ? -25.236 -81.083  -46.830 1.00 57.69 ? 155 HIS   D NE2 1 
ATOM   5081  N  N   . GLU   D  1 156 ? -19.065 -80.556  -44.950 1.00 64.47 ? 156 GLU   D N   1 
ATOM   5082  C  CA  . GLU   D  1 156 ? -17.818 -80.074  -44.377 1.00 61.70 ? 156 GLU   D CA  1 
ATOM   5083  C  C   . GLU   D  1 156 ? -17.991 -78.641  -43.875 1.00 59.77 ? 156 GLU   D C   1 
ATOM   5084  O  O   . GLU   D  1 156 ? -17.672 -78.334  -42.728 1.00 71.84 ? 156 GLU   D O   1 
ATOM   5085  C  CB  . GLU   D  1 156 ? -16.704 -80.152  -45.411 1.00 65.13 ? 156 GLU   D CB  1 
ATOM   5086  C  CG  . GLU   D  1 156 ? -16.785 -81.388  -46.300 1.00 67.48 ? 156 GLU   D CG  1 
ATOM   5087  C  CD  . GLU   D  1 156 ? -15.497 -81.657  -47.060 1.00 62.57 ? 156 GLU   D CD  1 
ATOM   5088  O  OE1 . GLU   D  1 156 ? -14.423 -81.314  -46.529 1.00 63.83 ? 156 GLU   D OE1 1 
ATOM   5089  O  OE2 . GLU   D  1 156 ? -15.557 -82.212  -48.183 1.00 54.89 ? 156 GLU   D OE2 1 
ATOM   5090  N  N   . MET   E  1 1   ? -32.796 -29.235  -13.014 1.00 31.89 ? 1   MET   E N   1 
ATOM   5091  C  CA  . MET   E  1 1   ? -33.673 -30.128  -12.195 1.00 33.80 ? 1   MET   E CA  1 
ATOM   5092  C  C   . MET   E  1 1   ? -33.418 -29.803  -10.733 1.00 31.04 ? 1   MET   E C   1 
ATOM   5093  O  O   . MET   E  1 1   ? -32.280 -29.758  -10.323 1.00 31.59 ? 1   MET   E O   1 
ATOM   5094  C  CB  . MET   E  1 1   ? -33.360 -31.594  -12.507 1.00 39.63 ? 1   MET   E CB  1 
ATOM   5095  C  CG  . MET   E  1 1   ? -34.303 -32.611  -11.907 1.00 39.30 ? 1   MET   E CG  1 
ATOM   5096  S  SD  . MET   E  1 1   ? -33.807 -34.283  -12.384 1.00 41.44 ? 1   MET   E SD  1 
ATOM   5097  C  CE  . MET   E  1 1   ? -32.492 -34.557  -11.214 1.00 44.25 ? 1   MET   E CE  1 
ATOM   5098  N  N   . LYS   E  1 2   ? -34.458 -29.588  -9.930  1.00 31.12 ? 2   LYS   E N   1 
ATOM   5099  C  CA  . LYS   E  1 2   ? -34.264 -29.063  -8.585  1.00 30.41 ? 2   LYS   E CA  1 
ATOM   5100  C  C   . LYS   E  1 2   ? -33.666 -30.166  -7.721  1.00 31.15 ? 2   LYS   E C   1 
ATOM   5101  O  O   . LYS   E  1 2   ? -34.309 -31.188  -7.477  1.00 29.37 ? 2   LYS   E O   1 
ATOM   5102  C  CB  . LYS   E  1 2   ? -35.589 -28.547  -8.019  1.00 43.20 ? 2   LYS   E CB  1 
ATOM   5103  N  N   . GLY   E  1 3   ? -32.403 -29.997  -7.304  1.00 29.72 ? 3   GLY   E N   1 
ATOM   5104  C  CA  . GLY   E  1 3   ? -31.758 -31.015  -6.506  1.00 30.53 ? 3   GLY   E CA  1 
ATOM   5105  C  C   . GLY   E  1 3   ? -32.107 -30.882  -5.035  1.00 29.28 ? 3   GLY   E C   1 
ATOM   5106  O  O   . GLY   E  1 3   ? -32.583 -29.846  -4.599  1.00 30.01 ? 3   GLY   E O   1 
ATOM   5107  N  N   . ASP   E  1 4   ? -31.868 -31.956  -4.292  1.00 29.08 ? 4   ASP   E N   1 
ATOM   5108  C  CA  . ASP   E  1 4   ? -31.898 -31.898  -2.835  1.00 26.19 ? 4   ASP   E CA  1 
ATOM   5109  C  C   . ASP   E  1 4   ? -30.841 -30.921  -2.329  1.00 34.10 ? 4   ASP   E C   1 
ATOM   5110  O  O   . ASP   E  1 4   ? -29.674 -30.964  -2.746  1.00 29.77 ? 4   ASP   E O   1 
ATOM   5111  C  CB  . ASP   E  1 4   ? -31.665 -33.295  -2.297  1.00 29.78 ? 4   ASP   E CB  1 
ATOM   5112  C  CG  . ASP   E  1 4   ? -31.682 -33.359  -0.785  1.00 42.56 ? 4   ASP   E CG  1 
ATOM   5113  O  OD1 . ASP   E  1 4   ? -32.789 -33.327  -0.202  1.00 28.49 ? 4   ASP   E OD1 1 
ATOM   5114  O  OD2 . ASP   E  1 4   ? -30.588 -33.471  -0.187  1.00 26.06 ? 4   ASP   E OD2 1 
ATOM   5115  N  N   . LYS   E  1 5   ? -31.250 -30.020  -1.434  1.00 27.06 ? 5   LYS   E N   1 
ATOM   5116  C  CA  . LYS   E  1 5   ? -30.331 -28.978  -0.980  1.00 29.11 ? 5   LYS   E CA  1 
ATOM   5117  C  C   . LYS   E  1 5   ? -29.114 -29.579  -0.286  1.00 28.42 ? 5   LYS   E C   1 
ATOM   5118  O  O   . LYS   E  1 5   ? -27.981 -29.095  -0.451  1.00 29.00 ? 5   LYS   E O   1 
ATOM   5119  C  CB  . LYS   E  1 5   ? -31.043 -28.020  -0.038  1.00 34.70 ? 5   LYS   E CB  1 
ATOM   5120  C  CG  . LYS   E  1 5   ? -30.140 -26.929  0.535   1.00 44.17 ? 5   LYS   E CG  1 
ATOM   5121  C  CD  . LYS   E  1 5   ? -30.939 -25.941  1.403   1.00 60.48 ? 5   LYS   E CD  1 
ATOM   5122  C  CE  . LYS   E  1 5   ? -30.171 -24.650  1.702   1.00 64.68 ? 5   LYS   E CE  1 
ATOM   5123  N  NZ  . LYS   E  1 5   ? -29.029 -24.856  2.646   1.00 69.77 ? 5   LYS   E NZ  1 
ATOM   5124  N  N   . LYS   E  1 6   ? -29.326 -30.635  0.493   1.00 27.71 ? 6   LYS   E N   1 
ATOM   5125  C  CA  . LYS   E  1 6   ? -28.208 -31.255  1.206   1.00 29.02 ? 6   LYS   E CA  1 
ATOM   5126  C  C   . LYS   E  1 6   ? -27.328 -32.105  0.287   1.00 25.63 ? 6   LYS   E C   1 
ATOM   5127  O  O   . LYS   E  1 6   ? -26.110 -32.218  0.529   1.00 27.39 ? 6   LYS   E O   1 
ATOM   5128  C  CB  . LYS   E  1 6   ? -28.757 -32.076  2.388   1.00 33.26 ? 6   LYS   E CB  1 
ATOM   5129  C  CG  . LYS   E  1 6   ? -27.709 -32.914  3.151   1.00 31.83 ? 6   LYS   E CG  1 
ATOM   5130  C  CD  . LYS   E  1 6   ? -26.613 -32.080  3.809   1.00 33.51 ? 6   LYS   E CD  1 
ATOM   5131  C  CE  . LYS   E  1 6   ? -27.145 -31.229  4.971   1.00 35.74 ? 6   LYS   E CE  1 
ATOM   5132  N  NZ  . LYS   E  1 6   ? -26.001 -30.660  5.792   1.00 33.22 ? 6   LYS   E NZ  1 
ATOM   5133  N  N   . VAL   E  1 7   ? -27.880 -32.698  -0.782  1.00 27.18 ? 7   VAL   E N   1 
ATOM   5134  C  CA  . VAL   E  1 7   ? -26.998 -33.308  -1.775  1.00 27.01 ? 7   VAL   E CA  1 
ATOM   5135  C  C   . VAL   E  1 7   ? -26.036 -32.262  -2.314  1.00 27.15 ? 7   VAL   E C   1 
ATOM   5136  O  O   . VAL   E  1 7   ? -24.836 -32.505  -2.447  1.00 27.88 ? 7   VAL   E O   1 
ATOM   5137  C  CB  . VAL   E  1 7   ? -27.793 -33.940  -2.931  1.00 32.67 ? 7   VAL   E CB  1 
ATOM   5138  C  CG1 . VAL   E  1 7   ? -26.834 -34.173  -4.183  1.00 26.13 ? 7   VAL   E CG1 1 
ATOM   5139  C  CG2 . VAL   E  1 7   ? -28.442 -35.212  -2.496  1.00 27.38 ? 7   VAL   E CG2 1 
ATOM   5140  N  N   . ILE   E  1 8   ? -26.562 -31.084  -2.659  1.00 29.02 ? 8   ILE   E N   1 
ATOM   5141  C  CA  . ILE   E  1 8   ? -25.712 -30.046  -3.227  1.00 27.35 ? 8   ILE   E CA  1 
ATOM   5142  C  C   . ILE   E  1 8   ? -24.636 -29.618  -2.234  1.00 27.51 ? 8   ILE   E C   1 
ATOM   5143  O  O   . ILE   E  1 8   ? -23.469 -29.399  -2.607  1.00 23.08 ? 8   ILE   E O   1 
ATOM   5144  C  CB  . ILE   E  1 8   ? -26.575 -28.866  -3.699  1.00 24.47 ? 8   ILE   E CB  1 
ATOM   5145  C  CG1 . ILE   E  1 8   ? -27.405 -29.280  -4.933  1.00 26.65 ? 8   ILE   E CG1 1 
ATOM   5146  C  CG2 . ILE   E  1 8   ? -25.666 -27.649  -4.023  1.00 23.99 ? 8   ILE   E CG2 1 
ATOM   5147  C  CD1 . ILE   E  1 8   ? -28.668 -28.424  -5.134  1.00 30.47 ? 8   ILE   E CD1 1 
ATOM   5148  N  N   . GLN   E  1 9   ? -24.985 -29.515  -0.952  1.00 25.51 ? 9   GLN   E N   1 
ATOM   5149  C  CA  . GLN   E  1 9   ? -23.968 -29.192  0.053   1.00 24.57 ? 9   GLN   E CA  1 
ATOM   5150  C  C   . GLN   E  1 9   ? -22.871 -30.242  0.100   1.00 23.85 ? 9   GLN   E C   1 
ATOM   5151  O  O   . GLN   E  1 9   ? -21.676 -29.911  0.211   1.00 25.73 ? 9   GLN   E O   1 
ATOM   5152  C  CB  . GLN   E  1 9   ? -24.590 -29.069  1.441   1.00 27.04 ? 9   GLN   E CB  1 
ATOM   5153  C  CG  . GLN   E  1 9   ? -25.520 -27.908  1.597   1.00 33.43 ? 9   GLN   E CG  1 
ATOM   5154  C  CD  . GLN   E  1 9   ? -26.231 -27.971  2.931   1.00 40.55 ? 9   GLN   E CD  1 
ATOM   5155  O  OE1 . GLN   E  1 9   ? -27.272 -28.599  3.043   1.00 33.76 ? 9   GLN   E OE1 1 
ATOM   5156  N  NE2 . GLN   E  1 9   ? -25.650 -27.367  3.951   1.00 36.29 ? 9   GLN   E NE2 1 
ATOM   5157  N  N   . HIS   E  1 10  ? -23.259 -31.512  0.045   1.00 24.47 ? 10  HIS   E N   1 
ATOM   5158  C  CA  . HIS   E  1 10  ? -22.288 -32.601  0.007   1.00 26.15 ? 10  HIS   E CA  1 
ATOM   5159  C  C   . HIS   E  1 10  ? -21.406 -32.509  -1.235  1.00 29.60 ? 10  HIS   E C   1 
ATOM   5160  O  O   . HIS   E  1 10  ? -20.175 -32.632  -1.138  1.00 27.46 ? 10  HIS   E O   1 
ATOM   5161  C  CB  . HIS   E  1 10  ? -23.014 -33.943  0.050   1.00 26.66 ? 10  HIS   E CB  1 
ATOM   5162  C  CG  . HIS   E  1 10  ? -23.255 -34.447  1.432   1.00 30.32 ? 10  HIS   E CG  1 
ATOM   5163  N  ND1 . HIS   E  1 10  ? -22.231 -34.894  2.251   1.00 26.18 ? 10  HIS   E ND1 1 
ATOM   5164  C  CD2 . HIS   E  1 10  ? -24.398 -34.546  2.157   1.00 32.69 ? 10  HIS   E CD2 1 
ATOM   5165  C  CE1 . HIS   E  1 10  ? -22.739 -35.252  3.418   1.00 34.48 ? 10  HIS   E CE1 1 
ATOM   5166  N  NE2 . HIS   E  1 10  ? -24.049 -35.049  3.386   1.00 34.39 ? 10  HIS   E NE2 1 
ATOM   5167  N  N   . LEU   E  1 11  ? -22.024 -32.305  -2.418  1.00 25.35 ? 11  LEU   E N   1 
ATOM   5168  C  CA  . LEU   E  1 11  ? -21.246 -32.192  -3.659  1.00 25.35 ? 11  LEU   E CA  1 
ATOM   5169  C  C   . LEU   E  1 11  ? -20.257 -31.021  -3.583  1.00 25.77 ? 11  LEU   E C   1 
ATOM   5170  O  O   . LEU   E  1 11  ? -19.110 -31.143  -4.032  1.00 24.45 ? 11  LEU   E O   1 
ATOM   5171  C  CB  . LEU   E  1 11  ? -22.166 -32.064  -4.885  1.00 23.35 ? 11  LEU   E CB  1 
ATOM   5172  C  CG  . LEU   E  1 11  ? -23.115 -33.242  -5.156  1.00 28.82 ? 11  LEU   E CG  1 
ATOM   5173  C  CD1 . LEU   E  1 11  ? -24.047 -32.998  -6.331  1.00 28.52 ? 11  LEU   E CD1 1 
ATOM   5174  C  CD2 . LEU   E  1 11  ? -22.345 -34.525  -5.400  1.00 27.13 ? 11  LEU   E CD2 1 
ATOM   5175  N  N   . ASN   E  1 12  ? -20.653 -29.908  -2.951  1.00 25.22 ? 12  ASN   E N   1 
ATOM   5176  C  CA  . ASN   E  1 12  ? -19.736 -28.787  -2.753  1.00 23.69 ? 12  ASN   E CA  1 
ATOM   5177  C  C   . ASN   E  1 12  ? -18.650 -29.118  -1.738  1.00 25.73 ? 12  ASN   E C   1 
ATOM   5178  O  O   . ASN   E  1 12  ? -17.533 -28.613  -1.851  1.00 25.37 ? 12  ASN   E O   1 
ATOM   5179  C  CB  . ASN   E  1 12  ? -20.499 -27.539  -2.324  1.00 26.90 ? 12  ASN   E CB  1 
ATOM   5180  C  CG  . ASN   E  1 12  ? -20.860 -26.628  -3.510  1.00 31.41 ? 12  ASN   E CG  1 
ATOM   5181  O  OD1 . ASN   E  1 12  ? -20.118 -26.525  -4.491  1.00 24.12 ? 12  ASN   E OD1 1 
ATOM   5182  N  ND2 . ASN   E  1 12  ? -21.998 -25.951  -3.408  1.00 29.47 ? 12  ASN   E ND2 1 
ATOM   5183  N  N   . LYS   E  1 13  ? -18.938 -29.959  -0.749  1.00 22.29 ? 13  LYS   E N   1 
ATOM   5184  C  CA  . LYS   E  1 13  ? -17.883 -30.389  0.160   1.00 24.11 ? 13  LYS   E CA  1 
ATOM   5185  C  C   . LYS   E  1 13  ? -16.863 -31.284  -0.565  1.00 25.14 ? 13  LYS   E C   1 
ATOM   5186  O  O   . LYS   E  1 13  ? -15.651 -31.143  -0.373  1.00 24.26 ? 13  LYS   E O   1 
ATOM   5187  C  CB  . LYS   E  1 13  ? -18.481 -31.115  1.366   1.00 22.74 ? 13  LYS   E CB  1 
ATOM   5188  C  CG  . LYS   E  1 13  ? -17.452 -31.315  2.454   1.00 24.94 ? 13  LYS   E CG  1 
ATOM   5189  C  CD  . LYS   E  1 13  ? -18.024 -32.046  3.650   1.00 37.62 ? 13  LYS   E CD  1 
ATOM   5190  C  CE  . LYS   E  1 13  ? -17.043 -32.135  4.783   1.00 36.42 ? 13  LYS   E CE  1 
ATOM   5191  N  NZ  . LYS   E  1 13  ? -17.762 -32.499  6.019   1.00 46.77 ? 13  LYS   E NZ  1 
ATOM   5192  N  N   . ILE   E  1 14  ? -17.338 -32.230  -1.373  1.00 24.06 ? 14  ILE   E N   1 
ATOM   5193  C  CA  . ILE   E  1 14  ? -16.429 -33.056  -2.160  1.00 23.21 ? 14  ILE   E CA  1 
ATOM   5194  C  C   . ILE   E  1 14  ? -15.620 -32.175  -3.117  1.00 25.24 ? 14  ILE   E C   1 
ATOM   5195  O  O   . ILE   E  1 14  ? -14.401 -32.351  -3.270  1.00 26.53 ? 14  ILE   E O   1 
ATOM   5196  C  CB  . ILE   E  1 14  ? -17.202 -34.151  -2.918  1.00 25.17 ? 14  ILE   E CB  1 
ATOM   5197  C  CG1 . ILE   E  1 14  ? -18.063 -35.024  -1.980  1.00 24.97 ? 14  ILE   E CG1 1 
ATOM   5198  C  CG2 . ILE   E  1 14  ? -16.245 -35.024  -3.724  1.00 27.71 ? 14  ILE   E CG2 1 
ATOM   5199  C  CD1 . ILE   E  1 14  ? -17.383 -35.551  -0.795  1.00 29.17 ? 14  ILE   E CD1 1 
ATOM   5200  N  N   . LEU   E  1 15  ? -16.288 -31.220  -3.780  1.00 26.24 ? 15  LEU   E N   1 
ATOM   5201  C  CA  . LEU   E  1 15  ? -15.595 -30.288  -4.667  1.00 25.03 ? 15  LEU   E CA  1 
ATOM   5202  C  C   . LEU   E  1 15  ? -14.519 -29.513  -3.915  1.00 28.22 ? 15  LEU   E C   1 
ATOM   5203  O  O   . LEU   E  1 15  ? -13.393 -29.330  -4.417  1.00 27.20 ? 15  LEU   E O   1 
ATOM   5204  C  CB  . LEU   E  1 15  ? -16.607 -29.337  -5.304  1.00 23.23 ? 15  LEU   E CB  1 
ATOM   5205  C  CG  . LEU   E  1 15  ? -16.052 -28.204  -6.155  1.00 26.23 ? 15  LEU   E CG  1 
ATOM   5206  C  CD1 . LEU   E  1 15  ? -15.210 -28.728  -7.356  1.00 21.84 ? 15  LEU   E CD1 1 
ATOM   5207  C  CD2 . LEU   E  1 15  ? -17.224 -27.397  -6.641  1.00 24.60 ? 15  LEU   E CD2 1 
ATOM   5208  N  N   . GLY   E  1 16  ? -14.828 -29.086  -2.688  1.00 26.60 ? 16  GLY   E N   1 
ATOM   5209  C  CA  . GLY   E  1 16  ? -13.835 -28.398  -1.874  1.00 23.56 ? 16  GLY   E CA  1 
ATOM   5210  C  C   . GLY   E  1 16  ? -12.605 -29.247  -1.621  1.00 29.62 ? 16  GLY   E C   1 
ATOM   5211  O  O   . GLY   E  1 16  ? -11.470 -28.763  -1.719  1.00 27.51 ? 16  GLY   E O   1 
ATOM   5212  N  N   . ASN   E  1 17  ? -12.810 -30.529  -1.300  1.00 23.34 ? 17  ASN   E N   1 
ATOM   5213  C  CA  . ASN   E  1 17  ? -11.684 -31.453  -1.172  1.00 25.68 ? 17  ASN   E CA  1 
ATOM   5214  C  C   . ASN   E  1 17  ? -10.896 -31.540  -2.475  1.00 27.32 ? 17  ASN   E C   1 
ATOM   5215  O  O   . ASN   E  1 17  ? -9.658  -31.605  -2.462  1.00 23.95 ? 17  ASN   E O   1 
ATOM   5216  C  CB  . ASN   E  1 17  ? -12.189 -32.843  -0.771  1.00 25.48 ? 17  ASN   E CB  1 
ATOM   5217  C  CG  . ASN   E  1 17  ? -12.777 -32.878  0.633   1.00 29.09 ? 17  ASN   E CG  1 
ATOM   5218  O  OD1 . ASN   E  1 17  ? -12.452 -32.049  1.467   1.00 27.59 ? 17  ASN   E OD1 1 
ATOM   5219  N  ND2 . ASN   E  1 17  ? -13.608 -33.881  0.907   1.00 28.94 ? 17  ASN   E ND2 1 
ATOM   5220  N  N   . GLU   E  1 18  ? -11.595 -31.524  -3.613  1.00 23.90 ? 18  GLU   E N   1 
ATOM   5221  C  CA  . GLU   E  1 18  ? -10.904 -31.639  -4.895  1.00 22.07 ? 18  GLU   E CA  1 
ATOM   5222  C  C   . GLU   E  1 18  ? -10.033 -30.425  -5.171  1.00 27.92 ? 18  GLU   E C   1 
ATOM   5223  O  O   . GLU   E  1 18  ? -8.908  -30.556  -5.677  1.00 26.69 ? 18  GLU   E O   1 
ATOM   5224  C  CB  . GLU   E  1 18  ? -11.903 -31.817  -6.040  1.00 29.07 ? 18  GLU   E CB  1 
ATOM   5225  C  CG  . GLU   E  1 18  ? -12.747 -33.056  -5.956  1.00 35.53 ? 18  GLU   E CG  1 
ATOM   5226  C  CD  . GLU   E  1 18  ? -12.011 -34.300  -6.299  1.00 40.52 ? 18  GLU   E CD  1 
ATOM   5227  O  OE1 . GLU   E  1 18  ? -10.820 -34.212  -6.709  1.00 35.72 ? 18  GLU   E OE1 1 
ATOM   5228  O  OE2 . GLU   E  1 18  ? -12.654 -35.372  -6.188  1.00 39.22 ? 18  GLU   E OE2 1 
ATOM   5229  N  N   . LEU   E  1 19  ? -10.533 -29.238  -4.850  1.00 25.98 ? 19  LEU   E N   1 
ATOM   5230  C  CA  . LEU   E  1 19  ? -9.766  -28.020  -5.073  1.00 26.83 ? 19  LEU   E CA  1 
ATOM   5231  C  C   . LEU   E  1 19  ? -8.470  -28.032  -4.285  1.00 25.95 ? 19  LEU   E C   1 
ATOM   5232  O  O   . LEU   E  1 19  ? -7.429  -27.598  -4.789  1.00 25.55 ? 19  LEU   E O   1 
ATOM   5233  C  CB  . LEU   E  1 19  ? -10.614 -26.805  -4.705  1.00 25.31 ? 19  LEU   E CB  1 
ATOM   5234  C  CG  . LEU   E  1 19  ? -11.864 -26.623  -5.579  1.00 29.96 ? 19  LEU   E CG  1 
ATOM   5235  C  CD1 . LEU   E  1 19  ? -12.613 -25.392  -5.102  1.00 37.60 ? 19  LEU   E CD1 1 
ATOM   5236  C  CD2 . LEU   E  1 19  ? -11.508 -26.522  -7.054  1.00 33.28 ? 19  LEU   E CD2 1 
ATOM   5237  N  N   . ILE   E  1 20  ? -8.519  -28.528  -3.045  1.00 22.21 ? 20  ILE   E N   1 
ATOM   5238  C  CA  . ILE   E  1 20  ? -7.314  -28.714  -2.248  1.00 28.67 ? 20  ILE   E CA  1 
ATOM   5239  C  C   . ILE   E  1 20  ? -6.384  -29.707  -2.923  1.00 27.06 ? 20  ILE   E C   1 
ATOM   5240  O  O   . ILE   E  1 20  ? -5.199  -29.433  -3.122  1.00 25.12 ? 20  ILE   E O   1 
ATOM   5241  C  CB  . ILE   E  1 20  ? -7.672  -29.183  -0.823  1.00 26.78 ? 20  ILE   E CB  1 
ATOM   5242  C  CG1 . ILE   E  1 20  ? -8.487  -28.127  -0.086  1.00 23.30 ? 20  ILE   E CG1 1 
ATOM   5243  C  CG2 . ILE   E  1 20  ? -6.396  -29.495  -0.045  1.00 22.06 ? 20  ILE   E CG2 1 
ATOM   5244  C  CD1 . ILE   E  1 20  ? -8.999  -28.613  1.256   1.00 28.34 ? 20  ILE   E CD1 1 
ATOM   5245  N  N   . ALA   E  1 21  ? -6.915  -30.873  -3.290  1.00 21.37 ? 21  ALA   E N   1 
ATOM   5246  C  CA  . ALA   E  1 21  ? -6.099  -31.914  -3.909  1.00 21.71 ? 21  ALA   E CA  1 
ATOM   5247  C  C   . ALA   E  1 21  ? -5.438  -31.430  -5.202  1.00 26.05 ? 21  ALA   E C   1 
ATOM   5248  O  O   . ALA   E  1 21  ? -4.263  -31.708  -5.439  1.00 25.31 ? 21  ALA   E O   1 
ATOM   5249  C  CB  . ALA   E  1 21  ? -6.946  -33.150  -4.208  1.00 27.77 ? 21  ALA   E CB  1 
ATOM   5250  N  N   . ILE   E  1 22  ? -6.191  -30.728  -6.056  1.00 23.56 ? 22  ILE   E N   1 
ATOM   5251  C  CA  . ILE   E  1 22  ? -5.642  -30.190  -7.293  1.00 23.03 ? 22  ILE   E CA  1 
ATOM   5252  C  C   . ILE   E  1 22  ? -4.356  -29.416  -7.012  1.00 24.75 ? 22  ILE   E C   1 
ATOM   5253  O  O   . ILE   E  1 22  ? -3.311  -29.672  -7.618  1.00 26.05 ? 22  ILE   E O   1 
ATOM   5254  C  CB  . ILE   E  1 22  ? -6.685  -29.302  -7.994  1.00 21.50 ? 22  ILE   E CB  1 
ATOM   5255  C  CG1 . ILE   E  1 22  ? -7.815  -30.145  -8.582  1.00 23.27 ? 22  ILE   E CG1 1 
ATOM   5256  C  CG2 . ILE   E  1 22  ? -6.053  -28.469  -9.067  1.00 22.69 ? 22  ILE   E CG2 1 
ATOM   5257  C  CD1 . ILE   E  1 22  ? -8.963  -29.323  -9.008  1.00 24.17 ? 22  ILE   E CD1 1 
ATOM   5258  N  N   . ASN   E  1 23  ? -4.427  -28.443  -6.097  1.00 21.93 ? 23  ASN   E N   1 
ATOM   5259  C  CA  . ASN   E  1 23  ? -3.298  -27.548  -5.845  1.00 26.44 ? 23  ASN   E CA  1 
ATOM   5260  C  C   . ASN   E  1 23  ? -2.179  -28.258  -5.101  1.00 25.40 ? 23  ASN   E C   1 
ATOM   5261  O  O   . ASN   E  1 23  ? -1.000  -28.051  -5.400  1.00 25.08 ? 23  ASN   E O   1 
ATOM   5262  C  CB  . ASN   E  1 23  ? -3.768  -26.324  -5.048  1.00 27.59 ? 23  ASN   E CB  1 
ATOM   5263  C  CG  . ASN   E  1 23  ? -4.575  -25.360  -5.893  1.00 28.04 ? 23  ASN   E CG  1 
ATOM   5264  O  OD1 . ASN   E  1 23  ? -5.018  -25.705  -6.983  1.00 33.16 ? 23  ASN   E OD1 1 
ATOM   5265  N  ND2 . ASN   E  1 23  ? -4.751  -24.136  -5.402  1.00 31.89 ? 23  ASN   E ND2 1 
ATOM   5266  N  N   . GLN   E  1 24  ? -2.529  -29.102  -4.133  1.00 25.69 ? 24  GLN   E N   1 
ATOM   5267  C  CA  . GLN   E  1 24  ? -1.505  -29.815  -3.376  1.00 25.86 ? 24  GLN   E CA  1 
ATOM   5268  C  C   . GLN   E  1 24  ? -0.736  -30.766  -4.277  1.00 24.18 ? 24  GLN   E C   1 
ATOM   5269  O  O   . GLN   E  1 24  ? 0.496   -30.835  -4.212  1.00 24.20 ? 24  GLN   E O   1 
ATOM   5270  C  CB  . GLN   E  1 24  ? -2.144  -30.572  -2.215  1.00 24.23 ? 24  GLN   E CB  1 
ATOM   5271  C  CG  . GLN   E  1 24  ? -1.236  -31.509  -1.419  1.00 25.78 ? 24  GLN   E CG  1 
ATOM   5272  C  CD  . GLN   E  1 24  ? -1.947  -32.055  -0.157  1.00 27.15 ? 24  GLN   E CD  1 
ATOM   5273  O  OE1 . GLN   E  1 24  ? -2.632  -31.311  0.550   1.00 25.76 ? 24  GLN   E OE1 1 
ATOM   5274  N  NE2 . GLN   E  1 24  ? -1.811  -33.354  0.095   1.00 28.03 ? 24  GLN   E NE2 1 
ATOM   5275  N  N   . TYR   E  1 25  ? -1.452  -31.526  -5.116  1.00 25.44 ? 25  TYR   E N   1 
ATOM   5276  C  CA  . TYR   E  1 25  ? -0.773  -32.460  -6.003  1.00 24.00 ? 25  TYR   E CA  1 
ATOM   5277  C  C   . TYR   E  1 25  ? -0.020  -31.705  -7.085  1.00 26.76 ? 25  TYR   E C   1 
ATOM   5278  O  O   . TYR   E  1 25  ? 1.057   -32.140  -7.506  1.00 25.47 ? 25  TYR   E O   1 
ATOM   5279  C  CB  . TYR   E  1 25  ? -1.758  -33.452  -6.635  1.00 24.65 ? 25  TYR   E CB  1 
ATOM   5280  C  CG  . TYR   E  1 25  ? -2.566  -34.271  -5.653  1.00 27.35 ? 25  TYR   E CG  1 
ATOM   5281  C  CD1 . TYR   E  1 25  ? -2.211  -34.329  -4.310  1.00 29.54 ? 25  TYR   E CD1 1 
ATOM   5282  C  CD2 . TYR   E  1 25  ? -3.681  -34.997  -6.072  1.00 26.88 ? 25  TYR   E CD2 1 
ATOM   5283  C  CE1 . TYR   E  1 25  ? -2.937  -35.065  -3.404  1.00 23.31 ? 25  TYR   E CE1 1 
ATOM   5284  C  CE2 . TYR   E  1 25  ? -4.419  -35.760  -5.166  1.00 28.73 ? 25  TYR   E CE2 1 
ATOM   5285  C  CZ  . TYR   E  1 25  ? -4.048  -35.778  -3.824  1.00 33.78 ? 25  TYR   E CZ  1 
ATOM   5286  O  OH  . TYR   E  1 25  ? -4.766  -36.491  -2.861  1.00 27.75 ? 25  TYR   E OH  1 
ATOM   5287  N  N   . PHE   E  1 26  ? -0.569  -30.576  -7.562  1.00 24.80 ? 26  PHE   E N   1 
ATOM   5288  C  CA  . PHE   E  1 26  ? 0.155   -29.852  -8.603  1.00 24.87 ? 26  PHE   E CA  1 
ATOM   5289  C  C   . PHE   E  1 26  ? 1.458   -29.290  -8.057  1.00 24.07 ? 26  PHE   E C   1 
ATOM   5290  O  O   . PHE   E  1 26  ? 2.508   -29.384  -8.713  1.00 24.15 ? 26  PHE   E O   1 
ATOM   5291  C  CB  . PHE   E  1 26  ? -0.688  -28.736  -9.223  1.00 27.27 ? 26  PHE   E CB  1 
ATOM   5292  C  CG  . PHE   E  1 26  ? -0.226  -28.379  -10.606 1.00 26.59 ? 26  PHE   E CG  1 
ATOM   5293  C  CD1 . PHE   E  1 26  ? -0.726  -29.052  -11.704 1.00 27.34 ? 26  PHE   E CD1 1 
ATOM   5294  C  CD2 . PHE   E  1 26  ? 0.752   -27.427  -10.800 1.00 24.62 ? 26  PHE   E CD2 1 
ATOM   5295  C  CE1 . PHE   E  1 26  ? -0.272  -28.770  -12.975 1.00 27.00 ? 26  PHE   E CE1 1 
ATOM   5296  C  CE2 . PHE   E  1 26  ? 1.238   -27.147  -12.075 1.00 26.51 ? 26  PHE   E CE2 1 
ATOM   5297  C  CZ  . PHE   E  1 26  ? 0.716   -27.811  -13.169 1.00 24.02 ? 26  PHE   E CZ  1 
ATOM   5298  N  N   . LEU   E  1 27  ? 1.409   -28.700  -6.873  1.00 20.42 ? 27  LEU   E N   1 
ATOM   5299  C  CA  . LEU   E  1 27  ? 2.623   -28.169  -6.254  1.00 24.57 ? 27  LEU   E CA  1 
ATOM   5300  C  C   . LEU   E  1 27  ? 3.596   -29.289  -5.899  1.00 26.82 ? 27  LEU   E C   1 
ATOM   5301  O  O   . LEU   E  1 27  ? 4.807   -29.152  -6.095  1.00 25.13 ? 27  LEU   E O   1 
ATOM   5302  C  CB  . LEU   E  1 27  ? 2.275   -27.342  -5.023  1.00 28.62 ? 27  LEU   E CB  1 
ATOM   5303  C  CG  . LEU   E  1 27  ? 3.501   -26.829  -4.233  1.00 28.65 ? 27  LEU   E CG  1 
ATOM   5304  C  CD1 . LEU   E  1 27  ? 4.415   -25.931  -5.124  1.00 28.43 ? 27  LEU   E CD1 1 
ATOM   5305  C  CD2 . LEU   E  1 27  ? 3.034   -26.085  -3.008  1.00 29.84 ? 27  LEU   E CD2 1 
ATOM   5306  N  N   . HIS   E  1 28  ? 3.097   -30.426  -5.409  1.00 27.48 ? 28  HIS   E N   1 
ATOM   5307  C  CA  . HIS   E  1 28  ? 4.027   -31.516  -5.133  1.00 23.39 ? 28  HIS   E CA  1 
ATOM   5308  C  C   . HIS   E  1 28  ? 4.706   -31.987  -6.416  1.00 22.06 ? 28  HIS   E C   1 
ATOM   5309  O  O   . HIS   E  1 28  ? 5.913   -32.264  -6.426  1.00 23.95 ? 28  HIS   E O   1 
ATOM   5310  C  CB  . HIS   E  1 28  ? 3.302   -32.666  -4.434  1.00 23.55 ? 28  HIS   E CB  1 
ATOM   5311  C  CG  . HIS   E  1 28  ? 3.104   -32.456  -2.966  1.00 25.46 ? 28  HIS   E CG  1 
ATOM   5312  N  ND1 . HIS   E  1 28  ? 2.206   -33.198  -2.225  1.00 25.77 ? 28  HIS   E ND1 1 
ATOM   5313  C  CD2 . HIS   E  1 28  ? 3.701   -31.610  -2.092  1.00 26.86 ? 28  HIS   E CD2 1 
ATOM   5314  C  CE1 . HIS   E  1 28  ? 2.267   -32.821  -0.960  1.00 28.32 ? 28  HIS   E CE1 1 
ATOM   5315  N  NE2 . HIS   E  1 28  ? 3.149   -31.847  -0.855  1.00 29.09 ? 28  HIS   E NE2 1 
ATOM   5316  N  N   . SER   E  1 29  ? 3.939   -32.085  -7.505  1.00 21.48 ? 29  SER   E N   1 
ATOM   5317  C  CA  . SER   E  1 29  ? 4.490   -32.488  -8.797  1.00 27.08 ? 29  SER   E CA  1 
ATOM   5318  C  C   . SER   E  1 29  ? 5.629   -31.578  -9.218  1.00 27.05 ? 29  SER   E C   1 
ATOM   5319  O  O   . SER   E  1 29  ? 6.693   -32.047  -9.642  1.00 24.10 ? 29  SER   E O   1 
ATOM   5320  C  CB  . SER   E  1 29  ? 3.404   -32.458  -9.863  1.00 21.79 ? 29  SER   E CB  1 
ATOM   5321  O  OG  . SER   E  1 29  ? 3.949   -32.667  -11.160 1.00 21.82 ? 29  SER   E OG  1 
ATOM   5322  N  N   . ARG   E  1 30  ? 5.398   -30.273  -9.151  1.00 23.16 ? 30  ARG   E N   1 
ATOM   5323  C  CA  . ARG   E  1 30  ? 6.408   -29.322  -9.589  1.00 25.40 ? 30  ARG   E CA  1 
ATOM   5324  C  C   . ARG   E  1 30  ? 7.600   -29.272  -8.629  1.00 27.13 ? 30  ARG   E C   1 
ATOM   5325  O  O   . ARG   E  1 30  ? 8.742   -29.042  -9.065  1.00 26.54 ? 30  ARG   E O   1 
ATOM   5326  C  CB  . ARG   E  1 30  ? 5.742   -27.960  -9.800  1.00 24.26 ? 30  ARG   E CB  1 
ATOM   5327  C  CG  . ARG   E  1 30  ? 5.225   -27.767  -11.240 1.00 28.84 ? 30  ARG   E CG  1 
ATOM   5328  C  CD  . ARG   E  1 30  ? 4.412   -28.957  -11.714 1.00 22.06 ? 30  ARG   E CD  1 
ATOM   5329  N  NE  . ARG   E  1 30  ? 4.055   -28.798  -13.119 1.00 21.86 ? 30  ARG   E NE  1 
ATOM   5330  C  CZ  . ARG   E  1 30  ? 4.010   -29.796  -13.994 1.00 26.60 ? 30  ARG   E CZ  1 
ATOM   5331  N  NH1 . ARG   E  1 30  ? 4.189   -31.048  -13.622 1.00 26.47 ? 30  ARG   E NH1 1 
ATOM   5332  N  NH2 . ARG   E  1 30  ? 3.802   -29.527  -15.281 1.00 32.41 ? 30  ARG   E NH2 1 
ATOM   5333  N  N   . MET   E  1 31  ? 7.391   -29.550  -7.343  1.00 25.54 ? 31  MET   E N   1 
ATOM   5334  C  CA  . MET   E  1 31  ? 8.536   -29.694  -6.435  1.00 23.42 ? 31  MET   E CA  1 
ATOM   5335  C  C   . MET   E  1 31  ? 9.381   -30.901  -6.822  1.00 29.00 ? 31  MET   E C   1 
ATOM   5336  O  O   . MET   E  1 31  ? 10.622  -30.817  -6.898  1.00 26.47 ? 31  MET   E O   1 
ATOM   5337  C  CB  . MET   E  1 31  ? 8.050   -29.831  -4.990  1.00 25.32 ? 31  MET   E CB  1 
ATOM   5338  C  CG  . MET   E  1 31  ? 7.411   -28.574  -4.424  1.00 29.59 ? 31  MET   E CG  1 
ATOM   5339  S  SD  . MET   E  1 31  ? 6.489   -28.857  -2.869  1.00 27.01 ? 31  MET   E SD  1 
ATOM   5340  C  CE  . MET   E  1 31  ? 7.811   -29.381  -1.802  1.00 28.08 ? 31  MET   E CE  1 
ATOM   5341  N  N   . TRP   E  1 32  ? 8.724   -32.043  -7.073  1.00 21.78 ? 32  TRP   E N   1 
ATOM   5342  C  CA  . TRP   E  1 32  ? 9.460   -33.242  -7.478  1.00 23.30 ? 32  TRP   E CA  1 
ATOM   5343  C  C   . TRP   E  1 32  ? 10.204  -33.012  -8.790  1.00 27.60 ? 32  TRP   E C   1 
ATOM   5344  O  O   . TRP   E  1 32  ? 11.364  -33.430  -8.930  1.00 24.21 ? 32  TRP   E O   1 
ATOM   5345  C  CB  . TRP   E  1 32  ? 8.532   -34.464  -7.562  1.00 23.29 ? 32  TRP   E CB  1 
ATOM   5346  C  CG  . TRP   E  1 32  ? 8.372   -35.170  -6.243  1.00 23.39 ? 32  TRP   E CG  1 
ATOM   5347  C  CD1 . TRP   E  1 32  ? 9.362   -35.415  -5.329  1.00 27.22 ? 32  TRP   E CD1 1 
ATOM   5348  C  CD2 . TRP   E  1 32  ? 7.162   -35.696  -5.667  1.00 24.32 ? 32  TRP   E CD2 1 
ATOM   5349  N  NE1 . TRP   E  1 32  ? 8.845   -36.057  -4.241  1.00 24.78 ? 32  TRP   E NE1 1 
ATOM   5350  C  CE2 . TRP   E  1 32  ? 7.500   -36.239  -4.414  1.00 22.96 ? 32  TRP   E CE2 1 
ATOM   5351  C  CE3 . TRP   E  1 32  ? 5.825   -35.772  -6.094  1.00 25.73 ? 32  TRP   E CE3 1 
ATOM   5352  C  CZ2 . TRP   E  1 32  ? 6.553   -36.837  -3.571  1.00 23.79 ? 32  TRP   E CZ2 1 
ATOM   5353  C  CZ3 . TRP   E  1 32  ? 4.884   -36.366  -5.245  1.00 23.06 ? 32  TRP   E CZ3 1 
ATOM   5354  C  CH2 . TRP   E  1 32  ? 5.253   -36.888  -4.014  1.00 28.63 ? 32  TRP   E CH2 1 
ATOM   5355  N  N   . ASN   E  1 33  ? 9.584   -32.318  -9.740  1.00 24.46 ? 33  ASN   E N   1 
ATOM   5356  C  CA  . ASN   E  1 33  ? 10.269  -32.042  -11.000 1.00 24.98 ? 33  ASN   E CA  1 
ATOM   5357  C  C   . ASN   E  1 33  ? 11.472  -31.141  -10.783 1.00 31.47 ? 33  ASN   E C   1 
ATOM   5358  O  O   . ASN   E  1 33  ? 12.543  -31.378  -11.354 1.00 28.55 ? 33  ASN   E O   1 
ATOM   5359  C  CB  . ASN   E  1 33  ? 9.328   -31.396  -12.021 1.00 29.16 ? 33  ASN   E CB  1 
ATOM   5360  C  CG  . ASN   E  1 33  ? 8.409   -32.403  -12.695 1.00 31.57 ? 33  ASN   E CG  1 
ATOM   5361  O  OD1 . ASN   E  1 33  ? 8.658   -33.614  -12.668 1.00 26.64 ? 33  ASN   E OD1 1 
ATOM   5362  N  ND2 . ASN   E  1 33  ? 7.340   -31.909  -13.301 1.00 28.71 ? 33  ASN   E ND2 1 
ATOM   5363  N  N   . ASP   E  1 34  ? 11.312  -30.100  -9.967  1.00 27.78 ? 34  ASP   E N   1 
ATOM   5364  C  CA  . ASP   E  1 34  ? 12.431  -29.221  -9.652  1.00 29.82 ? 34  ASP   E CA  1 
ATOM   5365  C  C   . ASP   E  1 34  ? 13.593  -30.007  -9.032  1.00 29.77 ? 34  ASP   E C   1 
ATOM   5366  O  O   . ASP   E  1 34  ? 14.760  -29.729  -9.319  1.00 29.29 ? 34  ASP   E O   1 
ATOM   5367  C  CB  . ASP   E  1 34  ? 11.950  -28.095  -8.731  1.00 29.60 ? 34  ASP   E CB  1 
ATOM   5368  C  CG  . ASP   E  1 34  ? 13.100  -27.161  -8.272  1.00 32.37 ? 34  ASP   E CG  1 
ATOM   5369  O  OD1 . ASP   E  1 34  ? 13.758  -26.537  -9.119  1.00 38.69 ? 34  ASP   E OD1 1 
ATOM   5370  O  OD2 . ASP   E  1 34  ? 13.302  -27.036  -7.055  1.00 37.37 ? 34  ASP   E OD2 1 
ATOM   5371  N  N   . TRP   E  1 35  ? 13.291  -31.021  -8.218  1.00 29.78 ? 35  TRP   E N   1 
ATOM   5372  C  CA  . TRP   E  1 35  ? 14.322  -31.810  -7.546  1.00 32.13 ? 35  TRP   E CA  1 
ATOM   5373  C  C   . TRP   E  1 35  ? 14.910  -32.900  -8.428  1.00 29.72 ? 35  TRP   E C   1 
ATOM   5374  O  O   . TRP   E  1 35  ? 15.817  -33.625  -7.985  1.00 24.09 ? 35  TRP   E O   1 
ATOM   5375  C  CB  . TRP   E  1 35  ? 13.770  -32.447  -6.274  1.00 27.48 ? 35  TRP   E CB  1 
ATOM   5376  C  CG  . TRP   E  1 35  ? 13.279  -31.462  -5.247  1.00 28.50 ? 35  TRP   E CG  1 
ATOM   5377  C  CD1 . TRP   E  1 35  ? 13.536  -30.127  -5.196  1.00 35.21 ? 35  TRP   E CD1 1 
ATOM   5378  C  CD2 . TRP   E  1 35  ? 12.424  -31.748  -4.133  1.00 33.92 ? 35  TRP   E CD2 1 
ATOM   5379  N  NE1 . TRP   E  1 35  ? 12.893  -29.559  -4.116  1.00 43.03 ? 35  TRP   E NE1 1 
ATOM   5380  C  CE2 . TRP   E  1 35  ? 12.195  -30.532  -3.456  1.00 35.38 ? 35  TRP   E CE2 1 
ATOM   5381  C  CE3 . TRP   E  1 35  ? 11.811  -32.907  -3.661  1.00 37.19 ? 35  TRP   E CE3 1 
ATOM   5382  C  CZ2 . TRP   E  1 35  ? 11.393  -30.444  -2.325  1.00 34.63 ? 35  TRP   E CZ2 1 
ATOM   5383  C  CZ3 . TRP   E  1 35  ? 11.008  -32.823  -2.524  1.00 30.46 ? 35  TRP   E CZ3 1 
ATOM   5384  C  CH2 . TRP   E  1 35  ? 10.817  -31.600  -1.864  1.00 31.72 ? 35  TRP   E CH2 1 
ATOM   5385  N  N   . GLY   E  1 36  ? 14.444  -33.023  -9.659  1.00 27.72 ? 36  GLY   E N   1 
ATOM   5386  C  CA  . GLY   E  1 36  ? 14.945  -34.052  -10.542 1.00 31.87 ? 36  GLY   E CA  1 
ATOM   5387  C  C   . GLY   E  1 36  ? 14.303  -35.403  -10.369 1.00 31.82 ? 36  GLY   E C   1 
ATOM   5388  O  O   . GLY   E  1 36  ? 14.762  -36.374  -10.985 1.00 27.89 ? 36  GLY   E O   1 
ATOM   5389  N  N   . LEU   E  1 37  ? 13.239  -35.508  -9.565  1.00 24.80 ? 37  LEU   E N   1 
ATOM   5390  C  CA  . LEU   E  1 37  ? 12.516  -36.773  -9.433  1.00 28.29 ? 37  LEU   E CA  1 
ATOM   5391  C  C   . LEU   E  1 37  ? 11.326  -36.795  -10.403 1.00 25.08 ? 37  LEU   E C   1 
ATOM   5392  O  O   . LEU   E  1 37  ? 10.157  -36.769  -10.004 1.00 23.82 ? 37  LEU   E O   1 
ATOM   5393  C  CB  . LEU   E  1 37  ? 12.092  -36.959  -7.983  1.00 25.51 ? 37  LEU   E CB  1 
ATOM   5394  C  CG  . LEU   E  1 37  ? 13.314  -36.918  -7.050  1.00 25.38 ? 37  LEU   E CG  1 
ATOM   5395  C  CD1 . LEU   E  1 37  ? 12.869  -36.638  -5.673  1.00 30.70 ? 37  LEU   E CD1 1 
ATOM   5396  C  CD2 . LEU   E  1 37  ? 14.115  -38.244  -7.157  1.00 28.97 ? 37  LEU   E CD2 1 
ATOM   5397  N  N   . LYS   E  1 38  ? 11.646  -36.843  -11.709 1.00 24.74 ? 38  LYS   E N   1 
ATOM   5398  C  CA  . LYS   E  1 38  ? 10.634  -36.577  -12.739 1.00 29.87 ? 38  LYS   E CA  1 
ATOM   5399  C  C   . LYS   E  1 38  ? 9.592   -37.684  -12.853 1.00 26.87 ? 38  LYS   E C   1 
ATOM   5400  O  O   . LYS   E  1 38  ? 8.508   -37.455  -13.401 1.00 25.21 ? 38  LYS   E O   1 
ATOM   5401  C  CB  . LYS   E  1 38  ? 11.277  -36.404  -14.109 1.00 31.68 ? 38  LYS   E CB  1 
ATOM   5402  C  CG  . LYS   E  1 38  ? 12.455  -35.478  -14.145 1.00 38.20 ? 38  LYS   E CG  1 
ATOM   5403  C  CD  . LYS   E  1 38  ? 12.058  -34.039  -13.970 1.00 41.67 ? 38  LYS   E CD  1 
ATOM   5404  C  CE  . LYS   E  1 38  ? 13.193  -33.126  -14.385 1.00 43.33 ? 38  LYS   E CE  1 
ATOM   5405  N  NZ  . LYS   E  1 38  ? 12.740  -31.740  -14.582 1.00 58.13 ? 38  LYS   E NZ  1 
ATOM   5406  N  N   . ARG   E  1 39  ? 9.904   -38.886  -12.407 1.00 29.76 ? 39  ARG   E N   1 
ATOM   5407  C  CA  . ARG   E  1 39  ? 8.905   -39.946  -12.465 1.00 31.63 ? 39  ARG   E CA  1 
ATOM   5408  C  C   . ARG   E  1 39  ? 7.821   -39.714  -11.424 1.00 30.81 ? 39  ARG   E C   1 
ATOM   5409  O  O   . ARG   E  1 39  ? 6.640   -39.986  -11.673 1.00 24.51 ? 39  ARG   E O   1 
ATOM   5410  C  CB  . ARG   E  1 39  ? 9.573   -41.286  -12.239 1.00 30.41 ? 39  ARG   E CB  1 
ATOM   5411  C  CG  . ARG   E  1 39  ? 8.692   -42.481  -12.604 1.00 42.85 ? 39  ARG   E CG  1 
ATOM   5412  C  CD  . ARG   E  1 39  ? 9.369   -43.754  -12.111 1.00 43.43 ? 39  ARG   E CD  1 
ATOM   5413  N  NE  . ARG   E  1 39  ? 8.720   -44.947  -12.623 1.00 44.64 ? 39  ARG   E NE  1 
ATOM   5414  C  CZ  . ARG   E  1 39  ? 9.011   -45.509  -13.784 1.00 47.39 ? 39  ARG   E CZ  1 
ATOM   5415  N  NH1 . ARG   E  1 39  ? 9.966   -45.025  -14.566 1.00 56.16 ? 39  ARG   E NH1 1 
ATOM   5416  N  NH2 . ARG   E  1 39  ? 8.323   -46.577  -14.171 1.00 51.50 ? 39  ARG   E NH2 1 
ATOM   5417  N  N   . LEU   E  1 40  ? 8.221   -39.235  -10.237 1.00 28.49 ? 40  LEU   E N   1 
ATOM   5418  C  CA  . LEU   E  1 40  ? 7.261   -38.807  -9.233  1.00 26.62 ? 40  LEU   E CA  1 
ATOM   5419  C  C   . LEU   E  1 40  ? 6.511   -37.570  -9.709  1.00 25.88 ? 40  LEU   E C   1 
ATOM   5420  O  O   . LEU   E  1 40  ? 5.290   -37.482  -9.570  1.00 24.03 ? 40  LEU   E O   1 
ATOM   5421  C  CB  . LEU   E  1 40  ? 7.968   -38.522  -7.902  1.00 26.25 ? 40  LEU   E CB  1 
ATOM   5422  C  CG  . LEU   E  1 40  ? 8.186   -39.747  -6.987  1.00 27.25 ? 40  LEU   E CG  1 
ATOM   5423  C  CD1 . LEU   E  1 40  ? 9.217   -39.429  -5.900  1.00 26.87 ? 40  LEU   E CD1 1 
ATOM   5424  C  CD2 . LEU   E  1 40  ? 6.836   -40.158  -6.376  1.00 29.98 ? 40  LEU   E CD2 1 
ATOM   5425  N  N   . GLY   E  1 41  ? 7.230   -36.611  -10.287 1.00 24.43 ? 41  GLY   E N   1 
ATOM   5426  C  CA  . GLY   E  1 41  ? 6.579   -35.414  -10.790 1.00 23.70 ? 41  GLY   E CA  1 
ATOM   5427  C  C   . GLY   E  1 41  ? 5.522   -35.708  -11.842 1.00 27.50 ? 41  GLY   E C   1 
ATOM   5428  O  O   . GLY   E  1 41  ? 4.424   -35.140  -11.808 1.00 22.63 ? 41  GLY   E O   1 
ATOM   5429  N  N   . ALA   E  1 42  ? 5.846   -36.584  -12.802 1.00 24.38 ? 42  ALA   E N   1 
ATOM   5430  C  CA  . ALA   E  1 42  ? 4.863   -36.956  -13.820 1.00 25.58 ? 42  ALA   E CA  1 
ATOM   5431  C  C   . ALA   E  1 42  ? 3.662   -37.672  -13.197 1.00 21.72 ? 42  ALA   E C   1 
ATOM   5432  O  O   . ALA   E  1 42  ? 2.510   -37.379  -13.522 1.00 23.75 ? 42  ALA   E O   1 
ATOM   5433  C  CB  . ALA   E  1 42  ? 5.518   -37.839  -14.901 1.00 28.17 ? 42  ALA   E CB  1 
ATOM   5434  N  N   . HIS   E  1 43  ? 3.908   -38.622  -12.304 1.00 21.24 ? 43  HIS   E N   1 
ATOM   5435  C  CA  . HIS   E  1 43  ? 2.800   -39.367  -11.723 1.00 25.13 ? 43  HIS   E CA  1 
ATOM   5436  C  C   . HIS   E  1 43  ? 1.885   -38.447  -10.910 1.00 25.76 ? 43  HIS   E C   1 
ATOM   5437  O  O   . HIS   E  1 43  ? 0.648   -38.517  -11.030 1.00 24.17 ? 43  HIS   E O   1 
ATOM   5438  C  CB  . HIS   E  1 43  ? 3.330   -40.503  -10.860 1.00 27.98 ? 43  HIS   E CB  1 
ATOM   5439  C  CG  . HIS   E  1 43  ? 2.272   -41.466  -10.450 1.00 25.97 ? 43  HIS   E CG  1 
ATOM   5440  N  ND1 . HIS   E  1 43  ? 1.345   -41.180  -9.468  1.00 37.39 ? 43  HIS   E ND1 1 
ATOM   5441  C  CD2 . HIS   E  1 43  ? 1.953   -42.690  -10.927 1.00 34.02 ? 43  HIS   E CD2 1 
ATOM   5442  C  CE1 . HIS   E  1 43  ? 0.513   -42.198  -9.345  1.00 30.49 ? 43  HIS   E CE1 1 
ATOM   5443  N  NE2 . HIS   E  1 43  ? 0.853   -43.122  -10.226 1.00 35.82 ? 43  HIS   E NE2 1 
ATOM   5444  N  N   . GLU   E  1 44  ? 2.479   -37.574  -10.081 1.00 25.02 ? 44  GLU   E N   1 
ATOM   5445  C  CA  . GLU   E  1 44  ? 1.705   -36.626  -9.274  1.00 23.15 ? 44  GLU   E CA  1 
ATOM   5446  C  C   . GLU   E  1 44  ? 0.954   -35.626  -10.156 1.00 24.64 ? 44  GLU   E C   1 
ATOM   5447  O  O   . GLU   E  1 44  ? -0.167  -35.215  -9.817  1.00 25.05 ? 44  GLU   E O   1 
ATOM   5448  C  CB  . GLU   E  1 44  ? 2.636   -35.893  -8.293  1.00 25.52 ? 44  GLU   E CB  1 
ATOM   5449  C  CG  . GLU   E  1 44  ? 1.929   -34.989  -7.254  1.00 26.51 ? 44  GLU   E CG  1 
ATOM   5450  C  CD  . GLU   E  1 44  ? 1.367   -35.773  -6.085  1.00 29.82 ? 44  GLU   E CD  1 
ATOM   5451  O  OE1 . GLU   E  1 44  ? 1.271   -37.004  -6.226  1.00 27.75 ? 44  GLU   E OE1 1 
ATOM   5452  O  OE2 . GLU   E  1 44  ? 1.042   -35.162  -5.027  1.00 27.16 ? 44  GLU   E OE2 1 
ATOM   5453  N  N   . TYR   E  1 45  ? 1.570   -35.208  -11.270 1.00 26.34 ? 45  TYR   E N   1 
ATOM   5454  C  CA  . TYR   E  1 45  ? 0.894   -34.361  -12.262 1.00 22.00 ? 45  TYR   E CA  1 
ATOM   5455  C  C   . TYR   E  1 45  ? -0.386  -35.018  -12.742 1.00 26.69 ? 45  TYR   E C   1 
ATOM   5456  O  O   . TYR   E  1 45  ? -1.447  -34.391  -12.760 1.00 23.82 ? 45  TYR   E O   1 
ATOM   5457  C  CB  . TYR   E  1 45  ? 1.806   -34.082  -13.462 1.00 27.29 ? 45  TYR   E CB  1 
ATOM   5458  C  CG  . TYR   E  1 45  ? 1.109   -33.395  -14.642 1.00 25.50 ? 45  TYR   E CG  1 
ATOM   5459  C  CD1 . TYR   E  1 45  ? 0.913   -32.024  -14.653 1.00 31.49 ? 45  TYR   E CD1 1 
ATOM   5460  C  CD2 . TYR   E  1 45  ? 0.670   -34.119  -15.750 1.00 24.47 ? 45  TYR   E CD2 1 
ATOM   5461  C  CE1 . TYR   E  1 45  ? 0.299   -31.396  -15.717 1.00 34.27 ? 45  TYR   E CE1 1 
ATOM   5462  C  CE2 . TYR   E  1 45  ? 0.049   -33.485  -16.833 1.00 32.14 ? 45  TYR   E CE2 1 
ATOM   5463  C  CZ  . TYR   E  1 45  ? -0.128  -32.126  -16.800 1.00 34.54 ? 45  TYR   E CZ  1 
ATOM   5464  O  OH  . TYR   E  1 45  ? -0.753  -31.466  -17.842 1.00 34.72 ? 45  TYR   E OH  1 
ATOM   5465  N  N   . HIS   E  1 46  ? -0.311  -36.304  -13.086 1.00 23.09 ? 46  HIS   E N   1 
ATOM   5466  C  CA  . HIS   E  1 46  ? -1.505  -37.000  -13.543 1.00 24.32 ? 46  HIS   E CA  1 
ATOM   5467  C  C   . HIS   E  1 46  ? -2.552  -37.141  -12.436 1.00 28.15 ? 46  HIS   E C   1 
ATOM   5468  O  O   . HIS   E  1 46  ? -3.757  -37.071  -12.725 1.00 25.72 ? 46  HIS   E O   1 
ATOM   5469  C  CB  . HIS   E  1 46  ? -1.102  -38.340  -14.144 1.00 27.03 ? 46  HIS   E CB  1 
ATOM   5470  C  CG  . HIS   E  1 46  ? -0.403  -38.187  -15.458 1.00 30.54 ? 46  HIS   E CG  1 
ATOM   5471  N  ND1 . HIS   E  1 46  ? 0.898   -38.588  -15.670 1.00 39.70 ? 46  HIS   E ND1 1 
ATOM   5472  C  CD2 . HIS   E  1 46  ? -0.819  -37.634  -16.625 1.00 34.36 ? 46  HIS   E CD2 1 
ATOM   5473  C  CE1 . HIS   E  1 46  ? 1.249   -38.299  -16.913 1.00 35.02 ? 46  HIS   E CE1 1 
ATOM   5474  N  NE2 . HIS   E  1 46  ? 0.223   -37.721  -17.513 1.00 41.76 ? 46  HIS   E NE2 1 
ATOM   5475  N  N   . GLU   E  1 47  ? -2.133  -37.306  -11.183 1.00 26.78 ? 47  GLU   E N   1 
ATOM   5476  C  CA  . GLU   E  1 47  ? -3.103  -37.318  -10.077 1.00 26.49 ? 47  GLU   E CA  1 
ATOM   5477  C  C   . GLU   E  1 47  ? -3.839  -35.985  -9.987  1.00 26.53 ? 47  GLU   E C   1 
ATOM   5478  O  O   . GLU   E  1 47  ? -5.057  -35.943  -9.784  1.00 28.21 ? 47  GLU   E O   1 
ATOM   5479  C  CB  . GLU   E  1 47  ? -2.401  -37.605  -8.745  1.00 29.91 ? 47  GLU   E CB  1 
ATOM   5480  C  CG  . GLU   E  1 47  ? -1.646  -38.919  -8.675  1.00 37.66 ? 47  GLU   E CG  1 
ATOM   5481  C  CD  . GLU   E  1 47  ? -2.558  -40.096  -8.506  1.00 49.57 ? 47  GLU   E CD  1 
ATOM   5482  O  OE1 . GLU   E  1 47  ? -3.778  -39.898  -8.633  1.00 54.76 ? 47  GLU   E OE1 1 
ATOM   5483  O  OE2 . GLU   E  1 47  ? -2.071  -41.208  -8.217  1.00 46.09 ? 47  GLU   E OE2 1 
ATOM   5484  N  N   . SER   E  1 48  ? -3.100  -34.882  -10.111 1.00 24.67 ? 48  SER   E N   1 
ATOM   5485  C  CA  . SER   E  1 48  ? -3.706  -33.550  -10.157 1.00 21.99 ? 48  SER   E CA  1 
ATOM   5486  C  C   . SER   E  1 48  ? -4.749  -33.435  -11.274 1.00 25.41 ? 48  SER   E C   1 
ATOM   5487  O  O   . SER   E  1 48  ? -5.868  -32.950  -11.053 1.00 26.57 ? 48  SER   E O   1 
ATOM   5488  C  CB  . SER   E  1 48  ? -2.605  -32.508  -10.358 1.00 28.40 ? 48  SER   E CB  1 
ATOM   5489  O  OG  . SER   E  1 48  ? -3.081  -31.206  -10.101 1.00 26.76 ? 48  SER   E OG  1 
ATOM   5490  N  N   . ILE   E  1 49  ? -4.386  -33.860  -12.490 1.00 24.01 ? 49  ILE   E N   1 
ATOM   5491  C  CA  . ILE   E  1 49  ? -5.317  -33.811  -13.614 1.00 23.92 ? 49  ILE   E CA  1 
ATOM   5492  C  C   . ILE   E  1 49  ? -6.548  -34.657  -13.326 1.00 25.40 ? 49  ILE   E C   1 
ATOM   5493  O  O   . ILE   E  1 49  ? -7.680  -34.281  -13.681 1.00 23.35 ? 49  ILE   E O   1 
ATOM   5494  C  CB  . ILE   E  1 49  ? -4.611  -34.270  -14.909 1.00 22.60 ? 49  ILE   E CB  1 
ATOM   5495  C  CG1 . ILE   E  1 49  ? -3.448  -33.325  -15.240 1.00 25.97 ? 49  ILE   E CG1 1 
ATOM   5496  C  CG2 . ILE   E  1 49  ? -5.599  -34.411  -16.024 1.00 29.86 ? 49  ILE   E CG2 1 
ATOM   5497  C  CD1 . ILE   E  1 49  ? -3.825  -32.097  -15.946 1.00 30.72 ? 49  ILE   E CD1 1 
ATOM   5498  N  N   . ASP   E  1 50  ? -6.359  -35.829  -12.721 1.00 24.59 ? 50  ASP   E N   1 
ATOM   5499  C  CA  . ASP   E  1 50  ? -7.529  -36.647  -12.436 1.00 30.65 ? 50  ASP   E CA  1 
ATOM   5500  C  C   . ASP   E  1 50  ? -8.459  -35.925  -11.476 1.00 25.86 ? 50  ASP   E C   1 
ATOM   5501  O  O   . ASP   E  1 50  ? -9.686  -36.012  -11.617 1.00 27.38 ? 50  ASP   E O   1 
ATOM   5502  C  CB  . ASP   E  1 50  ? -7.153  -38.011  -11.857 1.00 32.15 ? 50  ASP   E CB  1 
ATOM   5503  C  CG  . ASP   E  1 50  ? -6.499  -38.939  -12.885 1.00 44.82 ? 50  ASP   E CG  1 
ATOM   5504  O  OD1 . ASP   E  1 50  ? -6.673  -38.734  -14.115 1.00 48.61 ? 50  ASP   E OD1 1 
ATOM   5505  O  OD2 . ASP   E  1 50  ? -5.816  -39.889  -12.441 1.00 52.74 ? 50  ASP   E OD2 1 
ATOM   5506  N  N   . GLU   E  1 51  ? -7.901  -35.214  -10.482 1.00 22.96 ? 51  GLU   E N   1 
ATOM   5507  C  CA  . GLU   E  1 51  ? -8.762  -34.449  -9.576  1.00 26.18 ? 51  GLU   E CA  1 
ATOM   5508  C  C   . GLU   E  1 51  ? -9.462  -33.308  -10.310 1.00 25.31 ? 51  GLU   E C   1 
ATOM   5509  O  O   . GLU   E  1 51  ? -10.629 -33.001  -10.034 1.00 24.96 ? 51  GLU   E O   1 
ATOM   5510  C  CB  . GLU   E  1 51  ? -7.942  -33.920  -8.387  1.00 26.95 ? 51  GLU   E CB  1 
ATOM   5511  C  CG  . GLU   E  1 51  ? -7.279  -35.033  -7.573  1.00 28.65 ? 51  GLU   E CG  1 
ATOM   5512  C  CD  . GLU   E  1 51  ? -8.315  -36.004  -6.969  1.00 39.04 ? 51  GLU   E CD  1 
ATOM   5513  O  OE1 . GLU   E  1 51  ? -9.018  -35.592  -6.031  1.00 47.56 ? 51  GLU   E OE1 1 
ATOM   5514  O  OE2 . GLU   E  1 51  ? -8.437  -37.157  -7.429  1.00 36.25 ? 51  GLU   E OE2 1 
ATOM   5515  N  N   . MET   E  1 52  ? -8.781  -32.681  -11.263 1.00 21.86 ? 52  MET   E N   1 
ATOM   5516  C  CA  . MET   E  1 52  ? -9.413  -31.632  -12.053 1.00 23.86 ? 52  MET   E CA  1 
ATOM   5517  C  C   . MET   E  1 52  ? -10.602 -32.180  -12.832 1.00 22.94 ? 52  MET   E C   1 
ATOM   5518  O  O   . MET   E  1 52  ? -11.627 -31.509  -12.968 1.00 25.00 ? 52  MET   E O   1 
ATOM   5519  C  CB  . MET   E  1 52  ? -8.401  -31.039  -13.036 1.00 26.38 ? 52  MET   E CB  1 
ATOM   5520  C  CG  . MET   E  1 52  ? -7.277  -30.213  -12.413 1.00 24.88 ? 52  MET   E CG  1 
ATOM   5521  S  SD  . MET   E  1 52  ? -6.003  -29.819  -13.693 1.00 23.63 ? 52  MET   E SD  1 
ATOM   5522  C  CE  . MET   E  1 52  ? -4.454  -29.758  -12.711 1.00 23.50 ? 52  MET   E CE  1 
ATOM   5523  N  N   . LYS   E  1 53  ? -10.472 -33.388  -13.376 1.00 24.32 ? 53  LYS   E N   1 
ATOM   5524  C  CA  . LYS   E  1 53  ? -11.587 -33.987  -14.104 1.00 24.79 ? 53  LYS   E CA  1 
ATOM   5525  C  C   . LYS   E  1 53  ? -12.746 -34.281  -13.152 1.00 24.05 ? 53  LYS   E C   1 
ATOM   5526  O  O   . LYS   E  1 53  ? -13.916 -34.028  -13.486 1.00 24.46 ? 53  LYS   E O   1 
ATOM   5527  C  CB  . LYS   E  1 53  ? -11.114 -35.263  -14.811 1.00 26.25 ? 53  LYS   E CB  1 
ATOM   5528  C  CG  . LYS   E  1 53  ? -10.128 -35.001  -15.956 1.00 29.94 ? 53  LYS   E CG  1 
ATOM   5529  C  CD  . LYS   E  1 53  ? -9.665  -36.290  -16.609 1.00 38.53 ? 53  LYS   E CD  1 
ATOM   5530  C  CE  . LYS   E  1 53  ? -8.734  -36.014  -17.775 1.00 48.79 ? 53  LYS   E CE  1 
ATOM   5531  N  NZ  . LYS   E  1 53  ? -8.266  -37.308  -18.375 1.00 56.48 ? 53  LYS   E NZ  1 
ATOM   5532  N  N   . HIS   E  1 54  ? -12.432 -34.783  -11.948 1.00 24.06 ? 54  HIS   E N   1 
ATOM   5533  C  CA  . HIS   E  1 54  ? -13.468 -34.987  -10.925 1.00 25.98 ? 54  HIS   E CA  1 
ATOM   5534  C  C   . HIS   E  1 54  ? -14.163 -33.675  -10.590 1.00 28.75 ? 54  HIS   E C   1 
ATOM   5535  O  O   . HIS   E  1 54  ? -15.390 -33.627  -10.463 1.00 23.27 ? 54  HIS   E O   1 
ATOM   5536  C  CB  . HIS   E  1 54  ? -12.889 -35.585  -9.630  1.00 25.19 ? 54  HIS   E CB  1 
ATOM   5537  C  CG  . HIS   E  1 54  ? -12.198 -36.898  -9.811  1.00 24.81 ? 54  HIS   E CG  1 
ATOM   5538  N  ND1 . HIS   E  1 54  ? -12.475 -37.750  -10.851 1.00 30.89 ? 54  HIS   E ND1 1 
ATOM   5539  C  CD2 . HIS   E  1 54  ? -11.224 -37.499  -9.082  1.00 25.17 ? 54  HIS   E CD2 1 
ATOM   5540  C  CE1 . HIS   E  1 54  ? -11.694 -38.814  -10.770 1.00 30.36 ? 54  HIS   E CE1 1 
ATOM   5541  N  NE2 . HIS   E  1 54  ? -10.923 -38.683  -9.708  1.00 24.83 ? 54  HIS   E NE2 1 
ATOM   5542  N  N   . ALA   E  1 55  ? -13.388 -32.611  -10.383 1.00 21.25 ? 55  ALA   E N   1 
ATOM   5543  C  CA  . ALA   E  1 55  ? -13.981 -31.327  -10.034 1.00 26.17 ? 55  ALA   E CA  1 
ATOM   5544  C  C   . ALA   E  1 55  ? -14.916 -30.833  -11.135 1.00 29.15 ? 55  ALA   E C   1 
ATOM   5545  O  O   . ALA   E  1 55  ? -15.986 -30.262  -10.845 1.00 23.40 ? 55  ALA   E O   1 
ATOM   5546  C  CB  . ALA   E  1 55  ? -12.880 -30.312  -9.769  1.00 24.66 ? 55  ALA   E CB  1 
ATOM   5547  N  N   . ASP   E  1 56  ? -14.541 -31.089  -12.400 1.00 26.01 ? 56  ASP   E N   1 
ATOM   5548  C  CA  . ASP   E  1 56  ? -15.385 -30.736  -13.540 1.00 21.09 ? 56  ASP   E CA  1 
ATOM   5549  C  C   . ASP   E  1 56  ? -16.732 -31.431  -13.434 1.00 22.35 ? 56  ASP   E C   1 
ATOM   5550  O  O   . ASP   E  1 56  ? -17.784 -30.794  -13.541 1.00 21.05 ? 56  ASP   E O   1 
ATOM   5551  C  CB  . ASP   E  1 56  ? -14.675 -31.115  -14.851 1.00 23.09 ? 56  ASP   E CB  1 
ATOM   5552  C  CG  . ASP   E  1 56  ? -15.376 -30.606  -16.097 1.00 27.53 ? 56  ASP   E CG  1 
ATOM   5553  O  OD1 . ASP   E  1 56  ? -16.295 -29.775  -16.001 1.00 25.58 ? 56  ASP   E OD1 1 
ATOM   5554  O  OD2 . ASP   E  1 56  ? -14.980 -31.038  -17.202 1.00 28.97 ? 56  ASP   E OD2 1 
ATOM   5555  N  N   . LYS   E  1 57  ? -16.717 -32.746  -13.221 1.00 22.76 ? 57  LYS   E N   1 
ATOM   5556  C  CA  . LYS   E  1 57  ? -17.974 -33.481  -13.148 1.00 23.14 ? 57  LYS   E CA  1 
ATOM   5557  C  C   . LYS   E  1 57  ? -18.845 -33.003  -11.977 1.00 22.62 ? 57  LYS   E C   1 
ATOM   5558  O  O   . LYS   E  1 57  ? -20.074 -32.921  -12.108 1.00 23.98 ? 57  LYS   E O   1 
ATOM   5559  C  CB  . LYS   E  1 57  ? -17.701 -34.984  -13.044 1.00 24.77 ? 57  LYS   E CB  1 
ATOM   5560  C  CG  . LYS   E  1 57  ? -16.957 -35.591  -14.259 1.00 27.57 ? 57  LYS   E CG  1 
ATOM   5561  C  CD  . LYS   E  1 57  ? -17.689 -35.311  -15.564 1.00 34.96 ? 57  LYS   E CD  1 
ATOM   5562  N  N   . LEU   E  1 58  ? -18.236 -32.672  -10.842 1.00 22.25 ? 58  LEU   E N   1 
ATOM   5563  C  CA  . LEU   E  1 58  ? -19.022 -32.180  -9.701  1.00 22.84 ? 58  LEU   E CA  1 
ATOM   5564  C  C   . LEU   E  1 58  ? -19.668 -30.827  -10.007 1.00 22.35 ? 58  LEU   E C   1 
ATOM   5565  O  O   . LEU   E  1 58  ? -20.846 -30.598  -9.698  1.00 25.34 ? 58  LEU   E O   1 
ATOM   5566  C  CB  . LEU   E  1 58  ? -18.141 -32.065  -8.473  1.00 21.48 ? 58  LEU   E CB  1 
ATOM   5567  C  CG  . LEU   E  1 58  ? -17.676 -33.409  -7.918  1.00 27.11 ? 58  LEU   E CG  1 
ATOM   5568  C  CD1 . LEU   E  1 58  ? -16.460 -33.215  -6.995  1.00 26.70 ? 58  LEU   E CD1 1 
ATOM   5569  C  CD2 . LEU   E  1 58  ? -18.829 -34.107  -7.200  1.00 30.03 ? 58  LEU   E CD2 1 
ATOM   5570  N  N   . ILE   E  1 59  ? -18.892 -29.909  -10.581 1.00 25.72 ? 59  ILE   E N   1 
ATOM   5571  C  CA  . ILE   E  1 59  ? -19.416 -28.606  -10.972 1.00 25.30 ? 59  ILE   E CA  1 
ATOM   5572  C  C   . ILE   E  1 59  ? -20.592 -28.778  -11.919 1.00 22.85 ? 59  ILE   E C   1 
ATOM   5573  O  O   . ILE   E  1 59  ? -21.659 -28.172  -11.736 1.00 23.38 ? 59  ILE   E O   1 
ATOM   5574  C  CB  . ILE   E  1 59  ? -18.289 -27.760  -11.603 1.00 29.39 ? 59  ILE   E CB  1 
ATOM   5575  C  CG1 . ILE   E  1 59  ? -17.241 -27.427  -10.531 1.00 25.61 ? 59  ILE   E CG1 1 
ATOM   5576  C  CG2 . ILE   E  1 59  ? -18.817 -26.479  -12.216 1.00 22.89 ? 59  ILE   E CG2 1 
ATOM   5577  C  CD1 . ILE   E  1 59  ? -15.875 -27.063  -11.090 1.00 27.28 ? 59  ILE   E CD1 1 
ATOM   5578  N  N   . GLU   E  1 60  ? -20.433 -29.643  -12.916 1.00 23.49 ? 60  GLU   E N   1 
ATOM   5579  C  CA  . GLU   E  1 60  ? -21.505 -29.853  -13.882 1.00 29.41 ? 60  GLU   E CA  1 
ATOM   5580  C  C   . GLU   E  1 60  ? -22.754 -30.418  -13.208 1.00 26.30 ? 60  GLU   E C   1 
ATOM   5581  O  O   . GLU   E  1 60  ? -23.878 -29.959  -13.466 1.00 25.35 ? 60  GLU   E O   1 
ATOM   5582  C  CB  . GLU   E  1 60  ? -20.998 -30.779  -14.988 1.00 29.30 ? 60  GLU   E CB  1 
ATOM   5583  C  CG  . GLU   E  1 60  ? -19.900 -30.122  -15.875 1.00 24.64 ? 60  GLU   E CG  1 
ATOM   5584  C  CD  . GLU   E  1 60  ? -19.260 -31.109  -16.837 1.00 32.56 ? 60  GLU   E CD  1 
ATOM   5585  O  OE1 . GLU   E  1 60  ? -19.179 -32.313  -16.503 1.00 31.29 ? 60  GLU   E OE1 1 
ATOM   5586  O  OE2 . GLU   E  1 60  ? -18.871 -30.685  -17.938 1.00 31.18 ? 60  GLU   E OE2 1 
ATOM   5587  N  N   . ARG   E  1 61  ? -22.572 -31.420  -12.346 1.00 24.08 ? 61  ARG   E N   1 
ATOM   5588  C  CA  . ARG   E  1 61  ? -23.693 -32.013  -11.600 1.00 22.48 ? 61  ARG   E CA  1 
ATOM   5589  C  C   . ARG   E  1 61  ? -24.409 -30.988  -10.720 1.00 23.20 ? 61  ARG   E C   1 
ATOM   5590  O  O   . ARG   E  1 61  ? -25.662 -30.962  -10.652 1.00 24.88 ? 61  ARG   E O   1 
ATOM   5591  C  CB  . ARG   E  1 61  ? -23.192 -33.182  -10.731 1.00 27.23 ? 61  ARG   E CB  1 
ATOM   5592  C  CG  . ARG   E  1 61  ? -24.324 -33.957  -9.990  1.00 28.03 ? 61  ARG   E CG  1 
ATOM   5593  C  CD  . ARG   E  1 61  ? -25.144 -34.790  -10.918 1.00 27.17 ? 61  ARG   E CD  1 
ATOM   5594  N  NE  . ARG   E  1 61  ? -26.279 -35.447  -10.259 1.00 28.35 ? 61  ARG   E NE  1 
ATOM   5595  C  CZ  . ARG   E  1 61  ? -27.349 -35.883  -10.906 1.00 31.61 ? 61  ARG   E CZ  1 
ATOM   5596  N  NH1 . ARG   E  1 61  ? -27.422 -35.816  -12.225 1.00 29.16 ? 61  ARG   E NH1 1 
ATOM   5597  N  NH2 . ARG   E  1 61  ? -28.385 -36.385  -10.211 1.00 24.16 ? 61  ARG   E NH2 1 
ATOM   5598  N  N   . ILE   E  1 62  ? -23.640 -30.157  -10.014 1.00 23.19 ? 62  ILE   E N   1 
ATOM   5599  C  CA  . ILE   E  1 62  ? -24.224 -29.151  -9.131  1.00 24.99 ? 62  ILE   E CA  1 
ATOM   5600  C  C   . ILE   E  1 62  ? -25.085 -28.179  -9.936  1.00 26.20 ? 62  ILE   E C   1 
ATOM   5601  O  O   . ILE   E  1 62  ? -26.241 -27.897  -9.577  1.00 24.55 ? 62  ILE   E O   1 
ATOM   5602  C  CB  . ILE   E  1 62  ? -23.118 -28.422  -8.342  1.00 25.36 ? 62  ILE   E CB  1 
ATOM   5603  C  CG1 . ILE   E  1 62  ? -22.490 -29.346  -7.299  1.00 20.46 ? 62  ILE   E CG1 1 
ATOM   5604  C  CG2 . ILE   E  1 62  ? -23.679 -27.207  -7.635  1.00 20.31 ? 62  ILE   E CG2 1 
ATOM   5605  C  CD1 . ILE   E  1 62  ? -21.137 -28.851  -6.746  1.00 23.99 ? 62  ILE   E CD1 1 
ATOM   5606  N  N   . LEU   E  1 63  ? -24.550 -27.683  -11.059 1.00 24.03 ? 63  LEU   E N   1 
ATOM   5607  C  CA  . LEU   E  1 63  ? -25.298 -26.775  -11.933 1.00 25.37 ? 63  LEU   E CA  1 
ATOM   5608  C  C   . LEU   E  1 63  ? -26.555 -27.429  -12.480 1.00 22.17 ? 63  LEU   E C   1 
ATOM   5609  O  O   . LEU   E  1 63  ? -27.635 -26.815  -12.473 1.00 26.00 ? 63  LEU   E O   1 
ATOM   5610  C  CB  . LEU   E  1 63  ? -24.400 -26.280  -13.083 1.00 25.53 ? 63  LEU   E CB  1 
ATOM   5611  C  CG  . LEU   E  1 63  ? -23.293 -25.304  -12.665 1.00 24.30 ? 63  LEU   E CG  1 
ATOM   5612  C  CD1 . LEU   E  1 63  ? -22.290 -25.077  -13.835 1.00 24.21 ? 63  LEU   E CD1 1 
ATOM   5613  C  CD2 . LEU   E  1 63  ? -23.911 -23.977  -12.206 1.00 29.17 ? 63  LEU   E CD2 1 
ATOM   5614  N  N   . PHE   E  1 64  ? -26.467 -28.689  -12.915 1.00 20.35 ? 64  PHE   E N   1 
ATOM   5615  C  CA  . PHE   E  1 64  ? -27.681 -29.367  -13.366 1.00 25.40 ? 64  PHE   E CA  1 
ATOM   5616  C  C   . PHE   E  1 64  ? -28.721 -29.404  -12.254 1.00 28.41 ? 64  PHE   E C   1 
ATOM   5617  O  O   . PHE   E  1 64  ? -29.916 -29.182  -12.498 1.00 25.85 ? 64  PHE   E O   1 
ATOM   5618  C  CB  . PHE   E  1 64  ? -27.352 -30.778  -13.860 1.00 23.87 ? 64  PHE   E CB  1 
ATOM   5619  C  CG  . PHE   E  1 64  ? -28.545 -31.649  -14.068 1.00 26.72 ? 64  PHE   E CG  1 
ATOM   5620  C  CD1 . PHE   E  1 64  ? -29.487 -31.355  -15.046 1.00 25.90 ? 64  PHE   E CD1 1 
ATOM   5621  C  CD2 . PHE   E  1 64  ? -28.736 -32.763  -13.280 1.00 28.07 ? 64  PHE   E CD2 1 
ATOM   5622  C  CE1 . PHE   E  1 64  ? -30.597 -32.150  -15.236 1.00 32.24 ? 64  PHE   E CE1 1 
ATOM   5623  C  CE2 . PHE   E  1 64  ? -29.855 -33.575  -13.448 1.00 30.99 ? 64  PHE   E CE2 1 
ATOM   5624  C  CZ  . PHE   E  1 64  ? -30.788 -33.268  -14.439 1.00 27.26 ? 64  PHE   E CZ  1 
ATOM   5625  N  N   . LEU   E  1 65  ? -28.278 -29.627  -11.017 1.00 23.62 ? 65  LEU   E N   1 
ATOM   5626  C  CA  . LEU   E  1 65  ? -29.174 -29.676  -9.863  1.00 24.23 ? 65  LEU   E CA  1 
ATOM   5627  C  C   . LEU   E  1 65  ? -29.599 -28.289  -9.383  1.00 29.01 ? 65  LEU   E C   1 
ATOM   5628  O  O   . LEU   E  1 65  ? -30.300 -28.171  -8.359  1.00 25.79 ? 65  LEU   E O   1 
ATOM   5629  C  CB  . LEU   E  1 65  ? -28.499 -30.459  -8.736  1.00 21.13 ? 65  LEU   E CB  1 
ATOM   5630  C  CG  . LEU   E  1 65  ? -28.323 -31.939  -9.038  1.00 28.98 ? 65  LEU   E CG  1 
ATOM   5631  C  CD1 . LEU   E  1 65  ? -27.652 -32.668  -7.855  1.00 25.77 ? 65  LEU   E CD1 1 
ATOM   5632  C  CD2 . LEU   E  1 65  ? -29.662 -32.592  -9.404  1.00 27.60 ? 65  LEU   E CD2 1 
ATOM   5633  N  N   . GLU   E  1 66  ? -29.201 -27.250  -10.103 1.00 24.24 ? 66  GLU   E N   1 
ATOM   5634  C  CA  . GLU   E  1 66  ? -29.618 -25.875  -9.862  1.00 26.69 ? 66  GLU   E CA  1 
ATOM   5635  C  C   . GLU   E  1 66  ? -29.007 -25.333  -8.582  1.00 33.38 ? 66  GLU   E C   1 
ATOM   5636  O  O   . GLU   E  1 66  ? -29.572 -24.467  -7.926  1.00 30.66 ? 66  GLU   E O   1 
ATOM   5637  C  CB  . GLU   E  1 66  ? -31.165 -25.756  -9.875  1.00 28.01 ? 66  GLU   E CB  1 
ATOM   5638  C  CG  . GLU   E  1 66  ? -31.714 -26.254  -11.232 1.00 30.45 ? 66  GLU   E CG  1 
ATOM   5639  C  CD  . GLU   E  1 66  ? -33.221 -26.125  -11.407 1.00 34.89 ? 66  GLU   E CD  1 
ATOM   5640  O  OE1 . GLU   E  1 66  ? -33.855 -25.315  -10.701 1.00 37.41 ? 66  GLU   E OE1 1 
ATOM   5641  O  OE2 . GLU   E  1 66  ? -33.759 -26.862  -12.257 1.00 34.55 ? 66  GLU   E OE2 1 
ATOM   5642  N  N   . GLY   E  1 67  ? -27.829 -25.839  -8.218  1.00 25.44 ? 67  GLY   E N   1 
ATOM   5643  C  CA  . GLY   E  1 67  ? -27.037 -25.259  -7.164  1.00 23.73 ? 67  GLY   E CA  1 
ATOM   5644  C  C   . GLY   E  1 67  ? -25.940 -24.342  -7.701  1.00 31.14 ? 67  GLY   E C   1 
ATOM   5645  O  O   . GLY   E  1 67  ? -25.755 -24.182  -8.903  1.00 30.66 ? 67  GLY   E O   1 
ATOM   5646  N  N   . LEU   E  1 68  ? -25.213 -23.739  -6.750  1.00 25.96 ? 68  LEU   E N   1 
ATOM   5647  C  CA  . LEU   E  1 68  ? -24.074 -22.872  -6.982  1.00 32.11 ? 68  LEU   E CA  1 
ATOM   5648  C  C   . LEU   E  1 68  ? -22.807 -23.625  -6.611  1.00 33.72 ? 68  LEU   E C   1 
ATOM   5649  O  O   . LEU   E  1 68  ? -22.578 -23.883  -5.421  1.00 27.75 ? 68  LEU   E O   1 
ATOM   5650  C  CB  . LEU   E  1 68  ? -24.178 -21.601  -6.150  1.00 33.77 ? 68  LEU   E CB  1 
ATOM   5651  C  CG  . LEU   E  1 68  ? -25.394 -20.728  -6.489  1.00 53.26 ? 68  LEU   E CG  1 
ATOM   5652  C  CD1 . LEU   E  1 68  ? -25.298 -19.365  -5.791  1.00 58.73 ? 68  LEU   E CD1 1 
ATOM   5653  C  CD2 . LEU   E  1 68  ? -25.546 -20.561  -8.015  1.00 52.85 ? 68  LEU   E CD2 1 
ATOM   5654  N  N   . PRO   E  1 69  ? -21.945 -23.962  -7.567  1.00 25.45 ? 69  PRO   E N   1 
ATOM   5655  C  CA  . PRO   E  1 69  ? -20.688 -24.642  -7.218  1.00 22.57 ? 69  PRO   E CA  1 
ATOM   5656  C  C   . PRO   E  1 69  ? -19.779 -23.689  -6.476  1.00 26.93 ? 69  PRO   E C   1 
ATOM   5657  O  O   . PRO   E  1 69  ? -19.621 -22.528  -6.866  1.00 30.83 ? 69  PRO   E O   1 
ATOM   5658  C  CB  . PRO   E  1 69  ? -20.105 -25.033  -8.586  1.00 29.04 ? 69  PRO   E CB  1 
ATOM   5659  C  CG  . PRO   E  1 69  ? -21.260 -24.802  -9.612  1.00 28.52 ? 69  PRO   E CG  1 
ATOM   5660  C  CD  . PRO   E  1 69  ? -22.075 -23.718  -9.012  1.00 29.75 ? 69  PRO   E CD  1 
ATOM   5661  N  N   . ASN   E  1 70  ? -19.171 -24.175  -5.401  1.00 28.99 ? 70  ASN   E N   1 
ATOM   5662  C  CA  . ASN   E  1 70  ? -18.316 -23.319  -4.579  1.00 30.80 ? 70  ASN   E CA  1 
ATOM   5663  C  C   . ASN   E  1 70  ? -16.859 -23.473  -5.040  1.00 25.43 ? 70  ASN   E C   1 
ATOM   5664  O  O   . ASN   E  1 70  ? -16.180 -24.440  -4.684  1.00 25.43 ? 70  ASN   E O   1 
ATOM   5665  C  CB  . ASN   E  1 70  ? -18.471 -23.644  -3.092  1.00 31.01 ? 70  ASN   E CB  1 
ATOM   5666  C  CG  . ASN   E  1 70  ? -17.691 -22.673  -2.206  1.00 32.71 ? 70  ASN   E CG  1 
ATOM   5667  O  OD1 . ASN   E  1 70  ? -16.767 -22.004  -2.668  1.00 31.62 ? 70  ASN   E OD1 1 
ATOM   5668  N  ND2 . ASN   E  1 70  ? -18.047 -22.604  -0.924  1.00 32.12 ? 70  ASN   E ND2 1 
ATOM   5669  N  N   . LEU   E  1 71  ? -16.367 -22.519  -5.838  1.00 23.37 ? 71  LEU   E N   1 
ATOM   5670  C  CA  . LEU   E  1 71  ? -14.950 -22.499  -6.228  1.00 28.79 ? 71  LEU   E CA  1 
ATOM   5671  C  C   . LEU   E  1 71  ? -14.178 -21.383  -5.536  1.00 32.32 ? 71  LEU   E C   1 
ATOM   5672  O  O   . LEU   E  1 71  ? -13.047 -21.068  -5.938  1.00 31.75 ? 71  LEU   E O   1 
ATOM   5673  C  CB  . LEU   E  1 71  ? -14.775 -22.340  -7.734  1.00 27.66 ? 71  LEU   E CB  1 
ATOM   5674  C  CG  . LEU   E  1 71  ? -15.042 -23.536  -8.661  1.00 31.81 ? 71  LEU   E CG  1 
ATOM   5675  C  CD1 . LEU   E  1 71  ? -16.495 -23.736  -8.810  1.00 32.27 ? 71  LEU   E CD1 1 
ATOM   5676  C  CD2 . LEU   E  1 71  ? -14.442 -23.313  -10.040 1.00 33.03 ? 71  LEU   E CD2 1 
ATOM   5677  N  N   . GLN   E  1 72  ? -14.771 -20.775  -4.511  1.00 29.16 ? 72  GLN   E N   1 
ATOM   5678  C  CA  . GLN   E  1 72  ? -14.204 -19.637  -3.788  1.00 29.38 ? 72  GLN   E CA  1 
ATOM   5679  C  C   . GLN   E  1 72  ? -13.447 -20.055  -2.539  1.00 30.44 ? 72  GLN   E C   1 
ATOM   5680  O  O   . GLN   E  1 72  ? -12.448 -19.413  -2.168  1.00 30.97 ? 72  GLN   E O   1 
ATOM   5681  C  CB  . GLN   E  1 72  ? -15.328 -18.671  -3.389  1.00 29.63 ? 72  GLN   E CB  1 
ATOM   5682  C  CG  . GLN   E  1 72  ? -14.870 -17.433  -2.671  1.00 29.00 ? 72  GLN   E CG  1 
ATOM   5683  C  CD  . GLN   E  1 72  ? -13.995 -16.554  -3.552  1.00 26.74 ? 72  GLN   E CD  1 
ATOM   5684  O  OE1 . GLN   E  1 72  ? -14.476 -15.704  -4.283  1.00 30.28 ? 72  GLN   E OE1 1 
ATOM   5685  N  NE2 . GLN   E  1 72  ? -12.707 -16.797  -3.508  1.00 27.20 ? 72  GLN   E NE2 1 
ATOM   5686  N  N   . ASP   E  1 73  ? -13.916 -21.097  -1.857  1.00 28.82 ? 73  ASP   E N   1 
ATOM   5687  C  CA  . ASP   E  1 73  ? -13.381 -21.476  -0.555  1.00 30.57 ? 73  ASP   E CA  1 
ATOM   5688  C  C   . ASP   E  1 73  ? -12.350 -22.586  -0.737  1.00 31.12 ? 73  ASP   E C   1 
ATOM   5689  O  O   . ASP   E  1 73  ? -12.660 -23.661  -1.258  1.00 41.54 ? 73  ASP   E O   1 
ATOM   5690  C  CB  . ASP   E  1 73  ? -14.507 -21.899  0.384   1.00 29.11 ? 73  ASP   E CB  1 
ATOM   5691  C  CG  . ASP   E  1 73  ? -15.437 -20.741  0.739   1.00 36.25 ? 73  ASP   E CG  1 
ATOM   5692  O  OD1 . ASP   E  1 73  ? -14.978 -19.604  0.881   1.00 39.08 ? 73  ASP   E OD1 1 
ATOM   5693  O  OD2 . ASP   E  1 73  ? -16.647 -20.960  0.851   1.00 35.35 ? 73  ASP   E OD2 1 
ATOM   5694  N  N   . LEU   E  1 74  ? -11.117 -22.298  -0.358  1.00 30.20 ? 74  LEU   E N   1 
ATOM   5695  C  CA  . LEU   E  1 74  ? -9.988  -23.220  -0.500  1.00 27.28 ? 74  LEU   E CA  1 
ATOM   5696  C  C   . LEU   E  1 74  ? -9.451  -23.550  0.883   1.00 34.75 ? 74  LEU   E C   1 
ATOM   5697  O  O   . LEU   E  1 74  ? -8.935  -22.666  1.578   1.00 30.69 ? 74  LEU   E O   1 
ATOM   5698  C  CB  . LEU   E  1 74  ? -8.884  -22.592  -1.354  1.00 29.30 ? 74  LEU   E CB  1 
ATOM   5699  C  CG  . LEU   E  1 74  ? -7.633  -23.434  -1.560  1.00 31.82 ? 74  LEU   E CG  1 
ATOM   5700  C  CD1 . LEU   E  1 74  ? -8.023  -24.776  -2.170  1.00 29.07 ? 74  LEU   E CD1 1 
ATOM   5701  C  CD2 . LEU   E  1 74  ? -6.614  -22.717  -2.451  1.00 35.91 ? 74  LEU   E CD2 1 
ATOM   5702  N  N   . GLY   E  1 75  ? -9.560  -24.812  1.272   1.00 29.64 ? 75  GLY   E N   1 
ATOM   5703  C  CA  . GLY   E  1 75  ? -9.071  -25.274  2.553   1.00 30.05 ? 75  GLY   E CA  1 
ATOM   5704  C  C   . GLY   E  1 75  ? -7.560  -25.406  2.582   1.00 31.98 ? 75  GLY   E C   1 
ATOM   5705  O  O   . GLY   E  1 75  ? -6.845  -25.027  1.652   1.00 27.31 ? 75  GLY   E O   1 
ATOM   5706  N  N   . LYS   E  1 76  ? -7.070  -25.978  3.680   1.00 30.13 ? 76  LYS   E N   1 
ATOM   5707  C  CA  . LYS   E  1 76  ? -5.637  -25.983  3.986   1.00 34.13 ? 76  LYS   E CA  1 
ATOM   5708  C  C   . LYS   E  1 76  ? -4.909  -27.026  3.142   1.00 30.28 ? 76  LYS   E C   1 
ATOM   5709  O  O   . LYS   E  1 76  ? -5.230  -28.216  3.212   1.00 29.16 ? 76  LYS   E O   1 
ATOM   5710  C  CB  . LYS   E  1 76  ? -5.439  -26.263  5.477   1.00 32.55 ? 76  LYS   E CB  1 
ATOM   5711  C  CG  . LYS   E  1 76  ? -3.990  -26.232  5.981   1.00 33.22 ? 76  LYS   E CG  1 
ATOM   5712  N  N   . LEU   E  1 77  ? -3.935  -26.587  2.346   1.00 24.81 ? 77  LEU   E N   1 
ATOM   5713  C  CA  . LEU   E  1 77  ? -3.075  -27.537  1.645   1.00 31.09 ? 77  LEU   E CA  1 
ATOM   5714  C  C   . LEU   E  1 77  ? -2.118  -28.208  2.624   1.00 31.99 ? 77  LEU   E C   1 
ATOM   5715  O  O   . LEU   E  1 77  ? -1.616  -27.564  3.538   1.00 28.34 ? 77  LEU   E O   1 
ATOM   5716  C  CB  . LEU   E  1 77  ? -2.250  -26.823  0.580   1.00 32.62 ? 77  LEU   E CB  1 
ATOM   5717  C  CG  . LEU   E  1 77  ? -2.811  -26.429  -0.783  1.00 38.60 ? 77  LEU   E CG  1 
ATOM   5718  C  CD1 . LEU   E  1 77  ? -4.246  -26.033  -0.727  1.00 37.52 ? 77  LEU   E CD1 1 
ATOM   5719  C  CD2 . LEU   E  1 77  ? -1.929  -25.295  -1.428  1.00 30.78 ? 77  LEU   E CD2 1 
ATOM   5720  N  N   . LEU   E  1 78  ? -1.851  -29.501  2.427   1.00 31.52 ? 78  LEU   E N   1 
ATOM   5721  C  CA  . LEU   E  1 78  ? -0.830  -30.223  3.200   1.00 32.27 ? 78  LEU   E CA  1 
ATOM   5722  C  C   . LEU   E  1 78  ? 0.381   -30.456  2.303   1.00 31.50 ? 78  LEU   E C   1 
ATOM   5723  O  O   . LEU   E  1 78  ? 0.391   -31.399  1.496   1.00 31.32 ? 78  LEU   E O   1 
ATOM   5724  C  CB  . LEU   E  1 78  ? -1.349  -31.563  3.730   1.00 30.28 ? 78  LEU   E CB  1 
ATOM   5725  C  CG  . LEU   E  1 78  ? -2.702  -31.516  4.432   1.00 33.38 ? 78  LEU   E CG  1 
ATOM   5726  C  CD1 . LEU   E  1 78  ? -3.129  -32.920  4.794   1.00 36.61 ? 78  LEU   E CD1 1 
ATOM   5727  C  CD2 . LEU   E  1 78  ? -2.625  -30.622  5.668   1.00 39.70 ? 78  LEU   E CD2 1 
ATOM   5728  N  N   . ILE   E  1 79  ? 1.406   -29.620  2.471   1.00 30.23 ? 79  ILE   E N   1 
ATOM   5729  C  CA  . ILE   E  1 79  ? 2.615   -29.634  1.641   1.00 27.59 ? 79  ILE   E CA  1 
ATOM   5730  C  C   . ILE   E  1 79  ? 3.748   -30.241  2.440   1.00 33.22 ? 79  ILE   E C   1 
ATOM   5731  O  O   . ILE   E  1 79  ? 4.154   -29.688  3.466   1.00 36.14 ? 79  ILE   E O   1 
ATOM   5732  C  CB  . ILE   E  1 79  ? 3.012   -28.223  1.186   1.00 34.23 ? 79  ILE   E CB  1 
ATOM   5733  C  CG1 . ILE   E  1 79  ? 1.826   -27.516  0.528   1.00 31.35 ? 79  ILE   E CG1 1 
ATOM   5734  C  CG2 . ILE   E  1 79  ? 4.238   -28.295  0.251   1.00 34.68 ? 79  ILE   E CG2 1 
ATOM   5735  C  CD1 . ILE   E  1 79  ? 1.191   -28.299  -0.594  1.00 30.64 ? 79  ILE   E CD1 1 
ATOM   5736  N  N   . GLY   E  1 80  ? 4.287   -31.340  1.985   1.00 29.79 ? 80  GLY   E N   1 
ATOM   5737  C  CA  . GLY   E  1 80  ? 5.442   -31.863  2.706   1.00 34.50 ? 80  GLY   E CA  1 
ATOM   5738  C  C   . GLY   E  1 80  ? 6.740   -31.112  2.390   1.00 30.85 ? 80  GLY   E C   1 
ATOM   5739  O  O   . GLY   E  1 80  ? 6.811   -30.289  1.483   1.00 29.23 ? 80  GLY   E O   1 
ATOM   5740  N  N   . GLU   E  1 81  ? 7.795   -31.453  3.139   1.00 31.99 ? 81  GLU   E N   1 
ATOM   5741  C  CA  . GLU   E  1 81  ? 9.116   -30.867  2.964   1.00 38.14 ? 81  GLU   E CA  1 
ATOM   5742  C  C   . GLU   E  1 81  ? 10.142  -31.842  2.399   1.00 35.26 ? 81  GLU   E C   1 
ATOM   5743  O  O   . GLU   E  1 81  ? 11.249  -31.417  2.044   1.00 34.84 ? 81  GLU   E O   1 
ATOM   5744  C  CB  . GLU   E  1 81  ? 9.609   -30.309  4.304   1.00 41.36 ? 81  GLU   E CB  1 
ATOM   5745  C  CG  . GLU   E  1 81  ? 8.816   -29.077  4.748   1.00 54.95 ? 81  GLU   E CG  1 
ATOM   5746  C  CD  . GLU   E  1 81  ? 9.283   -28.519  6.083   1.00 60.79 ? 81  GLU   E CD  1 
ATOM   5747  O  OE1 . GLU   E  1 81  ? 10.145  -29.156  6.733   1.00 50.15 ? 81  GLU   E OE1 1 
ATOM   5748  O  OE2 . GLU   E  1 81  ? 8.786   -27.445  6.475   1.00 60.63 ? 81  GLU   E OE2 1 
ATOM   5749  N  N   . ASN   E  1 82  ? 9.786   -33.116  2.264   1.00 29.34 ? 82  ASN   E N   1 
ATOM   5750  C  CA  . ASN   E  1 82  ? 10.584  -34.121  1.583   1.00 32.98 ? 82  ASN   E CA  1 
ATOM   5751  C  C   . ASN   E  1 82  ? 9.616   -35.165  1.035   1.00 28.55 ? 82  ASN   E C   1 
ATOM   5752  O  O   . ASN   E  1 82  ? 8.425   -35.140  1.329   1.00 24.02 ? 82  ASN   E O   1 
ATOM   5753  C  CB  . ASN   E  1 82  ? 11.607  -34.749  2.527   1.00 30.16 ? 82  ASN   E CB  1 
ATOM   5754  C  CG  . ASN   E  1 82  ? 10.968  -35.322  3.782   1.00 37.06 ? 82  ASN   E CG  1 
ATOM   5755  O  OD1 . ASN   E  1 82  ? 9.954   -36.002  3.718   1.00 30.10 ? 82  ASN   E OD1 1 
ATOM   5756  N  ND2 . ASN   E  1 82  ? 11.572  -35.050  4.940   1.00 40.43 ? 82  ASN   E ND2 1 
ATOM   5757  N  N   . THR   E  1 83  ? 10.153  -36.117  0.271   1.00 25.92 ? 83  THR   E N   1 
ATOM   5758  C  CA  . THR   E  1 83  ? 9.302   -37.022  -0.497  1.00 28.44 ? 83  THR   E CA  1 
ATOM   5759  C  C   . THR   E  1 83  ? 8.370   -37.812  0.411   1.00 31.95 ? 83  THR   E C   1 
ATOM   5760  O  O   . THR   E  1 83  ? 7.165   -37.937  0.139   1.00 26.12 ? 83  THR   E O   1 
ATOM   5761  C  CB  . THR   E  1 83  ? 10.181  -37.949  -1.342  1.00 26.67 ? 83  THR   E CB  1 
ATOM   5762  O  OG1 . THR   E  1 83  ? 10.794  -37.165  -2.381  1.00 26.45 ? 83  THR   E OG1 1 
ATOM   5763  C  CG2 . THR   E  1 83  ? 9.332   -39.061  -1.992  1.00 25.38 ? 83  THR   E CG2 1 
ATOM   5764  N  N   . GLN   E  1 84  ? 8.910   -38.360  1.491   1.00 25.77 ? 84  GLN   E N   1 
ATOM   5765  C  CA  . GLN   E  1 84  ? 8.094   -39.153  2.406   1.00 28.24 ? 84  GLN   E CA  1 
ATOM   5766  C  C   . GLN   E  1 84  ? 6.974   -38.325  3.034   1.00 28.04 ? 84  GLN   E C   1 
ATOM   5767  O  O   . GLN   E  1 84  ? 5.834   -38.799  3.175   1.00 26.22 ? 84  GLN   E O   1 
ATOM   5768  C  CB  . GLN   E  1 84  ? 8.966   -39.751  3.505   1.00 32.19 ? 84  GLN   E CB  1 
ATOM   5769  C  CG  . GLN   E  1 84  ? 8.195   -40.740  4.369   1.00 39.62 ? 84  GLN   E CG  1 
ATOM   5770  C  CD  . GLN   E  1 84  ? 9.096   -41.785  5.014   1.00 50.13 ? 84  GLN   E CD  1 
ATOM   5771  O  OE1 . GLN   E  1 84  ? 8.684   -42.931  5.223   1.00 56.26 ? 84  GLN   E OE1 1 
ATOM   5772  N  NE2 . GLN   E  1 84  ? 10.335  -41.401  5.312   1.00 52.64 ? 84  GLN   E NE2 1 
ATOM   5773  N  N   . GLU   E  1 85  ? 7.279   -37.100  3.446   1.00 24.29 ? 85  GLU   E N   1 
ATOM   5774  C  CA  . GLU   E  1 85  ? 6.238   -36.255  4.003   1.00 23.51 ? 85  GLU   E CA  1 
ATOM   5775  C  C   . GLU   E  1 85  ? 5.197   -35.910  2.946   1.00 29.06 ? 85  GLU   E C   1 
ATOM   5776  O  O   . GLU   E  1 85  ? 4.001   -35.887  3.240   1.00 22.58 ? 85  GLU   E O   1 
ATOM   5777  C  CB  . GLU   E  1 85  ? 6.834   -34.980  4.590   1.00 31.87 ? 85  GLU   E CB  1 
ATOM   5778  C  CG  . GLU   E  1 85  ? 7.704   -35.212  5.793   1.00 45.73 ? 85  GLU   E CG  1 
ATOM   5779  C  CD  . GLU   E  1 85  ? 8.096   -33.920  6.504   1.00 53.67 ? 85  GLU   E CD  1 
ATOM   5780  O  OE1 . GLU   E  1 85  ? 7.750   -32.819  6.001   1.00 36.26 ? 85  GLU   E OE1 1 
ATOM   5781  O  OE2 . GLU   E  1 85  ? 8.746   -34.022  7.575   1.00 54.82 ? 85  GLU   E OE2 1 
ATOM   5782  N  N   . MET   E  1 86  ? 5.633   -35.659  1.704   1.00 24.10 ? 86  MET   E N   1 
ATOM   5783  C  CA  . MET   E  1 86  ? 4.682   -35.262  0.672   1.00 23.03 ? 86  MET   E CA  1 
ATOM   5784  C  C   . MET   E  1 86  ? 3.718   -36.401  0.386   1.00 27.34 ? 86  MET   E C   1 
ATOM   5785  O  O   . MET   E  1 86  ? 2.504   -36.182  0.212   1.00 25.02 ? 86  MET   E O   1 
ATOM   5786  C  CB  . MET   E  1 86  ? 5.405   -34.851  -0.612  1.00 23.87 ? 86  MET   E CB  1 
ATOM   5787  C  CG  . MET   E  1 86  ? 6.266   -33.593  -0.469  1.00 28.92 ? 86  MET   E CG  1 
ATOM   5788  S  SD  . MET   E  1 86  ? 7.729   -33.592  -1.572  1.00 27.88 ? 86  MET   E SD  1 
ATOM   5789  C  CE  . MET   E  1 86  ? 6.983   -33.264  -3.191  1.00 26.31 ? 86  MET   E CE  1 
ATOM   5790  N  N   . LEU   E  1 87  ? 4.242   -37.627  0.340   1.00 23.40 ? 87  LEU   E N   1 
ATOM   5791  C  CA  . LEU   E  1 87  ? 3.393   -38.785  0.126   1.00 25.82 ? 87  LEU   E CA  1 
ATOM   5792  C  C   . LEU   E  1 87  ? 2.420   -38.971  1.291   1.00 30.95 ? 87  LEU   E C   1 
ATOM   5793  O  O   . LEU   E  1 87  ? 1.238   -39.262  1.085   1.00 24.10 ? 87  LEU   E O   1 
ATOM   5794  C  CB  . LEU   E  1 87  ? 4.256   -40.022  -0.065  1.00 24.21 ? 87  LEU   E CB  1 
ATOM   5795  C  CG  . LEU   E  1 87  ? 5.047   -40.152  -1.384  1.00 26.78 ? 87  LEU   E CG  1 
ATOM   5796  C  CD1 . LEU   E  1 87  ? 6.074   -41.298  -1.271  1.00 24.84 ? 87  LEU   E CD1 1 
ATOM   5797  C  CD2 . LEU   E  1 87  ? 4.154   -40.391  -2.599  1.00 27.76 ? 87  LEU   E CD2 1 
ATOM   5798  N  N   . GLN   E  1 88  ? 2.896   -38.805  2.520   1.00 24.31 ? 88  GLN   E N   1 
ATOM   5799  C  CA  . GLN   E  1 88  ? 2.020   -38.976  3.664   1.00 24.92 ? 88  GLN   E CA  1 
ATOM   5800  C  C   . GLN   E  1 88  ? 0.955   -37.873  3.720   1.00 24.64 ? 88  GLN   E C   1 
ATOM   5801  O  O   . GLN   E  1 88  ? -0.208  -38.145  4.078   1.00 24.86 ? 88  GLN   E O   1 
ATOM   5802  C  CB  . GLN   E  1 88  ? 2.877   -39.030  4.944   1.00 28.04 ? 88  GLN   E CB  1 
ATOM   5803  C  CG  . GLN   E  1 88  ? 2.050   -39.230  6.222   1.00 39.89 ? 88  GLN   E CG  1 
ATOM   5804  C  CD  . GLN   E  1 88  ? 1.348   -40.594  6.313   1.00 49.52 ? 88  GLN   E CD  1 
ATOM   5805  O  OE1 . GLN   E  1 88  ? 2.002   -41.630  6.334   1.00 42.24 ? 88  GLN   E OE1 1 
ATOM   5806  N  NE2 . GLN   E  1 88  ? 0.008   -40.586  6.394   1.00 35.06 ? 88  GLN   E NE2 1 
ATOM   5807  N  N   . CYS   E  1 89  ? 1.311   -36.643  3.313   1.00 26.89 ? 89  CYS   E N   1 
ATOM   5808  C  CA  . CYS   E  1 89  ? 0.336   -35.551  3.205   1.00 26.80 ? 89  CYS   E CA  1 
ATOM   5809  C  C   . CYS   E  1 89  ? -0.751  -35.859  2.182   1.00 31.28 ? 89  CYS   E C   1 
ATOM   5810  O  O   . CYS   E  1 89  ? -1.936  -35.578  2.409   1.00 25.75 ? 89  CYS   E O   1 
ATOM   5811  C  CB  . CYS   E  1 89  ? 1.023   -34.243  2.804   1.00 30.26 ? 89  CYS   E CB  1 
ATOM   5812  S  SG  . CYS   E  1 89  ? 1.933   -33.389  4.144   1.00 31.70 ? 89  CYS   E SG  1 
ATOM   5813  N  N   . ASP   E  1 90  ? -0.359  -36.382  1.027   1.00 22.51 ? 90  ASP   E N   1 
ATOM   5814  C  CA  . ASP   E  1 90  ? -1.338  -36.763  0.020   1.00 26.00 ? 90  ASP   E CA  1 
ATOM   5815  C  C   . ASP   E  1 90  ? -2.269  -37.827  0.585   1.00 25.38 ? 90  ASP   E C   1 
ATOM   5816  O  O   . ASP   E  1 90  ? -3.496  -37.758  0.416   1.00 25.75 ? 90  ASP   E O   1 
ATOM   5817  C  CB  . ASP   E  1 90  ? -0.647  -37.302  -1.238  1.00 24.65 ? 90  ASP   E CB  1 
ATOM   5818  C  CG  . ASP   E  1 90  ? -0.042  -36.217  -2.133  1.00 23.08 ? 90  ASP   E CG  1 
ATOM   5819  O  OD1 . ASP   E  1 90  ? -0.073  -35.018  -1.804  1.00 27.07 ? 90  ASP   E OD1 1 
ATOM   5820  O  OD2 . ASP   E  1 90  ? 0.485   -36.584  -3.206  1.00 27.83 ? 90  ASP   E OD2 1 
ATOM   5821  N  N   . LEU   E  1 91  ? -1.694  -38.796  1.299   1.00 23.54 ? 91  LEU   E N   1 
ATOM   5822  C  CA  . LEU   E  1 91  ? -2.475  -39.902  1.844   1.00 28.46 ? 91  LEU   E CA  1 
ATOM   5823  C  C   . LEU   E  1 91  ? -3.446  -39.409  2.914   1.00 26.53 ? 91  LEU   E C   1 
ATOM   5824  O  O   . LEU   E  1 91  ? -4.624  -39.804  2.926   1.00 25.43 ? 91  LEU   E O   1 
ATOM   5825  C  CB  . LEU   E  1 91  ? -1.520  -40.969  2.391   1.00 28.76 ? 91  LEU   E CB  1 
ATOM   5826  C  CG  . LEU   E  1 91  ? -2.109  -42.217  3.082   1.00 26.07 ? 91  LEU   E CG  1 
ATOM   5827  C  CD1 . LEU   E  1 91  ? -3.070  -42.930  2.134   1.00 30.97 ? 91  LEU   E CD1 1 
ATOM   5828  C  CD2 . LEU   E  1 91  ? -1.000  -43.167  3.561   1.00 29.66 ? 91  LEU   E CD2 1 
ATOM   5829  N  N   . ASN   E  1 92  ? -2.995  -38.497  3.778   1.00 25.00 ? 92  ASN   E N   1 
ATOM   5830  C  CA  . ASN   E  1 92  ? -3.901  -37.922  4.773   1.00 25.77 ? 92  ASN   E CA  1 
ATOM   5831  C  C   . ASN   E  1 92  ? -5.089  -37.208  4.118   1.00 27.28 ? 92  ASN   E C   1 
ATOM   5832  O  O   . ASN   E  1 92  ? -6.240  -37.377  4.549   1.00 24.35 ? 92  ASN   E O   1 
ATOM   5833  C  CB  . ASN   E  1 92  ? -3.140  -36.975  5.694   1.00 23.80 ? 92  ASN   E CB  1 
ATOM   5834  C  CG  . ASN   E  1 92  ? -2.132  -37.709  6.601   1.00 36.19 ? 92  ASN   E CG  1 
ATOM   5835  O  OD1 . ASN   E  1 92  ? -2.212  -38.928  6.820   1.00 35.47 ? 92  ASN   E OD1 1 
ATOM   5836  N  ND2 . ASN   E  1 92  ? -1.176  -36.954  7.127   1.00 30.96 ? 92  ASN   E ND2 1 
ATOM   5837  N  N   . LEU   E  1 93  ? -4.838  -36.449  3.045   1.00 24.61 ? 93  LEU   E N   1 
ATOM   5838  C  CA  . LEU   E  1 93  ? -5.920  -35.794  2.312   1.00 29.65 ? 93  LEU   E CA  1 
ATOM   5839  C  C   . LEU   E  1 93  ? -6.868  -36.818  1.693   1.00 29.08 ? 93  LEU   E C   1 
ATOM   5840  O  O   . LEU   E  1 93  ? -8.092  -36.691  1.797   1.00 27.78 ? 93  LEU   E O   1 
ATOM   5841  C  CB  . LEU   E  1 93  ? -5.323  -34.868  1.243   1.00 26.70 ? 93  LEU   E CB  1 
ATOM   5842  C  CG  . LEU   E  1 93  ? -6.298  -34.046  0.387   1.00 29.42 ? 93  LEU   E CG  1 
ATOM   5843  C  CD1 . LEU   E  1 93  ? -7.045  -33.070  1.253   1.00 33.73 ? 93  LEU   E CD1 1 
ATOM   5844  C  CD2 . LEU   E  1 93  ? -5.570  -33.254  -0.684  1.00 30.06 ? 93  LEU   E CD2 1 
ATOM   5845  N  N   . GLU   E  1 94  ? -6.316  -37.854  1.055   1.00 23.27 ? 94  GLU   E N   1 
ATOM   5846  C  CA  . GLU   E  1 94  ? -7.142  -38.879  0.435   1.00 25.19 ? 94  GLU   E CA  1 
ATOM   5847  C  C   . GLU   E  1 94  ? -8.036  -39.565  1.461   1.00 25.44 ? 94  GLU   E C   1 
ATOM   5848  O  O   . GLU   E  1 94  ? -9.215  -39.836  1.189   1.00 25.77 ? 94  GLU   E O   1 
ATOM   5849  C  CB  . GLU   E  1 94  ? -6.256  -39.894  -0.268  1.00 26.00 ? 94  GLU   E CB  1 
ATOM   5850  C  CG  . GLU   E  1 94  ? -5.580  -39.350  -1.514  1.00 26.77 ? 94  GLU   E CG  1 
ATOM   5851  C  CD  . GLU   E  1 94  ? -6.533  -39.299  -2.692  1.00 31.91 ? 94  GLU   E CD  1 
ATOM   5852  O  OE1 . GLU   E  1 94  ? -7.685  -39.672  -2.505  1.00 32.34 ? 94  GLU   E OE1 1 
ATOM   5853  O  OE2 . GLU   E  1 94  ? -6.120  -38.944  -3.815  1.00 38.99 ? 94  GLU   E OE2 1 
ATOM   5854  N  N   . LEU   E  1 95  ? -7.504  -39.848  2.649   1.00 22.79 ? 95  LEU   E N   1 
ATOM   5855  C  CA  . LEU   E  1 95  ? -8.314  -40.499  3.676   1.00 25.18 ? 95  LEU   E CA  1 
ATOM   5856  C  C   . LEU   E  1 95  ? -9.457  -39.601  4.143   1.00 26.35 ? 95  LEU   E C   1 
ATOM   5857  O  O   . LEU   E  1 95  ? -10.583 -40.075  4.385   1.00 28.60 ? 95  LEU   E O   1 
ATOM   5858  C  CB  . LEU   E  1 95  ? -7.434  -40.904  4.852   1.00 30.42 ? 95  LEU   E CB  1 
ATOM   5859  C  CG  . LEU   E  1 95  ? -6.494  -42.046  4.490   1.00 27.36 ? 95  LEU   E CG  1 
ATOM   5860  C  CD1 . LEU   E  1 95  ? -5.432  -42.192  5.575   1.00 30.63 ? 95  LEU   E CD1 1 
ATOM   5861  C  CD2 . LEU   E  1 95  ? -7.214  -43.361  4.285   1.00 33.24 ? 95  LEU   E CD2 1 
ATOM   5862  N  N   . LYS   E  1 96  ? -9.195  -38.308  4.295   1.00 28.67 ? 96  LYS   E N   1 
ATOM   5863  C  CA  . LYS   E  1 96  ? -10.286 -37.387  4.577   1.00 30.14 ? 96  LYS   E CA  1 
ATOM   5864  C  C   . LYS   E  1 96  ? -11.286 -37.346  3.412   1.00 35.97 ? 96  LYS   E C   1 
ATOM   5865  O  O   . LYS   E  1 96  ? -12.511 -37.323  3.623   1.00 27.73 ? 96  LYS   E O   1 
ATOM   5866  C  CB  . LYS   E  1 96  ? -9.727  -36.001  4.868   1.00 31.37 ? 96  LYS   E CB  1 
ATOM   5867  C  CG  . LYS   E  1 96  ? -10.803 -34.929  5.139   1.00 36.46 ? 96  LYS   E CG  1 
ATOM   5868  N  N   . ALA   E  1 97  ? -10.780 -37.340  2.174   1.00 29.39 ? 97  ALA   E N   1 
ATOM   5869  C  CA  . ALA   E  1 97  ? -11.663 -37.226  1.019   1.00 25.23 ? 97  ALA   E CA  1 
ATOM   5870  C  C   . ALA   E  1 97  ? -12.567 -38.447  0.884   1.00 24.28 ? 97  ALA   E C   1 
ATOM   5871  O  O   . ALA   E  1 97  ? -13.751 -38.315  0.548   1.00 24.46 ? 97  ALA   E O   1 
ATOM   5872  C  CB  . ALA   E  1 97  ? -10.844 -37.011  -0.254  1.00 24.26 ? 97  ALA   E CB  1 
ATOM   5873  N  N   . THR   E  1 98  ? -12.047 -39.642  1.158   1.00 23.38 ? 98  THR   E N   1 
ATOM   5874  C  CA  . THR   E  1 98  ? -12.880 -40.823  1.006   1.00 23.34 ? 98  THR   E CA  1 
ATOM   5875  C  C   . THR   E  1 98  ? -13.884 -40.945  2.139   1.00 27.37 ? 98  THR   E C   1 
ATOM   5876  O  O   . THR   E  1 98  ? -14.973 -41.479  1.921   1.00 24.46 ? 98  THR   E O   1 
ATOM   5877  C  CB  . THR   E  1 98  ? -12.040 -42.098  0.920   1.00 26.42 ? 98  THR   E CB  1 
ATOM   5878  O  OG1 . THR   E  1 98  ? -11.188 -42.200  2.061   1.00 28.87 ? 98  THR   E OG1 1 
ATOM   5879  C  CG2 . THR   E  1 98  ? -11.202 -42.086  -0.366  1.00 27.98 ? 98  THR   E CG2 1 
ATOM   5880  N  N   . LYS   E  1 99  ? -13.533 -40.480  3.343   1.00 25.51 ? 99  LYS   E N   1 
ATOM   5881  C  CA  . LYS   E  1 99  ? -14.518 -40.376  4.425   1.00 29.36 ? 99  LYS   E CA  1 
ATOM   5882  C  C   . LYS   E  1 99  ? -15.695 -39.495  4.004   1.00 27.97 ? 99  LYS   E C   1 
ATOM   5883  O  O   . LYS   E  1 99  ? -16.866 -39.847  4.194   1.00 25.59 ? 99  LYS   E O   1 
ATOM   5884  C  CB  . LYS   E  1 99  ? -13.846 -39.800  5.676   1.00 31.04 ? 99  LYS   E CB  1 
ATOM   5885  C  CG  . LYS   E  1 99  ? -14.777 -39.586  6.867   1.00 40.63 ? 99  LYS   E CG  1 
ATOM   5886  C  CD  . LYS   E  1 99  ? -14.007 -39.083  8.068   1.00 45.09 ? 99  LYS   E CD  1 
ATOM   5887  N  N   . ASP   E  1 100 ? -15.395 -38.316  3.470   1.00 26.01 ? 100 ASP   E N   1 
ATOM   5888  C  CA  . ASP   E  1 100 ? -16.451 -37.418  3.028   1.00 25.31 ? 100 ASP   E CA  1 
ATOM   5889  C  C   . ASP   E  1 100 ? -17.254 -38.010  1.874   1.00 30.59 ? 100 ASP   E C   1 
ATOM   5890  O  O   . ASP   E  1 100 ? -18.485 -37.818  1.803   1.00 25.86 ? 100 ASP   E O   1 
ATOM   5891  C  CB  . ASP   E  1 100 ? -15.846 -36.084  2.631   1.00 25.68 ? 100 ASP   E CB  1 
ATOM   5892  C  CG  . ASP   E  1 100 ? -15.280 -35.336  3.825   1.00 35.25 ? 100 ASP   E CG  1 
ATOM   5893  O  OD1 . ASP   E  1 100 ? -15.569 -35.753  4.956   1.00 36.66 ? 100 ASP   E OD1 1 
ATOM   5894  O  OD2 . ASP   E  1 100 ? -14.542 -34.354  3.634   1.00 32.40 ? 100 ASP   E OD2 1 
ATOM   5895  N  N   . LEU   E  1 101 ? -16.578 -38.708  0.941   1.00 23.53 ? 101 LEU   E N   1 
ATOM   5896  C  CA  . LEU   E  1 101 ? -17.300 -39.338  -0.166  1.00 25.11 ? 101 LEU   E CA  1 
ATOM   5897  C  C   . LEU   E  1 101 ? -18.323 -40.350  0.358   1.00 30.03 ? 101 LEU   E C   1 
ATOM   5898  O  O   . LEU   E  1 101 ? -19.465 -40.408  -0.125  1.00 25.52 ? 101 LEU   E O   1 
ATOM   5899  C  CB  . LEU   E  1 101 ? -16.321 -40.028  -1.129  1.00 21.55 ? 101 LEU   E CB  1 
ATOM   5900  C  CG  . LEU   E  1 101 ? -15.603 -39.074  -2.078  1.00 26.29 ? 101 LEU   E CG  1 
ATOM   5901  C  CD1 . LEU   E  1 101 ? -14.400 -39.714  -2.720  1.00 20.72 ? 101 LEU   E CD1 1 
ATOM   5902  C  CD2 . LEU   E  1 101 ? -16.536 -38.679  -3.184  1.00 30.03 ? 101 LEU   E CD2 1 
ATOM   5903  N  N   . ARG   E  1 102 ? -17.939 -41.129  1.376   1.00 24.59 ? 102 ARG   E N   1 
ATOM   5904  C  CA  . ARG   E  1 102 ? -18.834 -42.160  1.888   1.00 25.30 ? 102 ARG   E CA  1 
ATOM   5905  C  C   . ARG   E  1 102 ? -20.069 -41.532  2.534   1.00 22.20 ? 102 ARG   E C   1 
ATOM   5906  O  O   . ARG   E  1 102 ? -21.195 -42.002  2.341   1.00 25.30 ? 102 ARG   E O   1 
ATOM   5907  C  CB  . ARG   E  1 102 ? -18.094 -43.040  2.899   1.00 27.42 ? 102 ARG   E CB  1 
ATOM   5908  C  CG  . ARG   E  1 102 ? -17.021 -43.928  2.306   1.00 25.97 ? 102 ARG   E CG  1 
ATOM   5909  C  CD  . ARG   E  1 102 ? -16.214 -44.673  3.405   1.00 24.63 ? 102 ARG   E CD  1 
ATOM   5910  N  NE  . ARG   E  1 102 ? -14.850 -44.975  2.925   1.00 23.42 ? 102 ARG   E NE  1 
ATOM   5911  C  CZ  . ARG   E  1 102 ? -14.567 -45.800  1.925   1.00 28.58 ? 102 ARG   E CZ  1 
ATOM   5912  N  NH1 . ARG   E  1 102 ? -15.512 -46.494  1.312   1.00 28.27 ? 102 ARG   E NH1 1 
ATOM   5913  N  NH2 . ARG   E  1 102 ? -13.305 -45.903  1.498   1.00 26.74 ? 102 ARG   E NH2 1 
ATOM   5914  N  N   . GLU   E  1 103 ? -19.867 -40.456  3.292   1.00 23.61 ? 103 GLU   E N   1 
ATOM   5915  C  CA  . GLU   E  1 103 ? -20.980 -39.767  3.927   1.00 27.30 ? 103 GLU   E CA  1 
ATOM   5916  C  C   . GLU   E  1 103 ? -21.888 -39.146  2.882   1.00 32.95 ? 103 GLU   E C   1 
ATOM   5917  O  O   . GLU   E  1 103 ? -23.122 -39.110  3.056   1.00 24.86 ? 103 GLU   E O   1 
ATOM   5918  C  CB  . GLU   E  1 103 ? -20.432 -38.697  4.874   1.00 24.32 ? 103 GLU   E CB  1 
ATOM   5919  C  CG  . GLU   E  1 103 ? -19.681 -39.269  6.044   1.00 30.81 ? 103 GLU   E CG  1 
ATOM   5920  C  CD  . GLU   E  1 103 ? -18.884 -38.228  6.810   1.00 59.77 ? 103 GLU   E CD  1 
ATOM   5921  O  OE1 . GLU   E  1 103 ? -19.017 -37.023  6.492   1.00 56.50 ? 103 GLU   E OE1 1 
ATOM   5922  O  OE2 . GLU   E  1 103 ? -18.113 -38.621  7.721   1.00 62.75 ? 103 GLU   E OE2 1 
ATOM   5923  N  N   . ALA   E  1 104 ? -21.289 -38.663  1.775   1.00 27.57 ? 104 ALA   E N   1 
ATOM   5924  C  CA  . ALA   E  1 104 ? -22.081 -38.083  0.707   1.00 22.76 ? 104 ALA   E CA  1 
ATOM   5925  C  C   . ALA   E  1 104 ? -22.920 -39.152  0.027   1.00 26.96 ? 104 ALA   E C   1 
ATOM   5926  O  O   . ALA   E  1 104 ? -24.097 -38.924  -0.251  1.00 23.42 ? 104 ALA   E O   1 
ATOM   5927  C  CB  . ALA   E  1 104 ? -21.191 -37.362  -0.302  1.00 21.06 ? 104 ALA   E CB  1 
ATOM   5928  N  N   . ILE   E  1 105 ? -22.339 -40.335  -0.211  1.00 24.64 ? 105 ILE   E N   1 
ATOM   5929  C  CA  . ILE   E  1 105 ? -23.083 -41.434  -0.826  1.00 23.85 ? 105 ILE   E CA  1 
ATOM   5930  C  C   . ILE   E  1 105 ? -24.252 -41.851  0.069   1.00 25.86 ? 105 ILE   E C   1 
ATOM   5931  O  O   . ILE   E  1 105 ? -25.355 -42.149  -0.417  1.00 23.98 ? 105 ILE   E O   1 
ATOM   5932  C  CB  . ILE   E  1 105 ? -22.134 -42.611  -1.127  1.00 24.09 ? 105 ILE   E CB  1 
ATOM   5933  C  CG1 . ILE   E  1 105 ? -21.202 -42.210  -2.309  1.00 22.67 ? 105 ILE   E CG1 1 
ATOM   5934  C  CG2 . ILE   E  1 105 ? -22.925 -43.896  -1.396  1.00 21.44 ? 105 ILE   E CG2 1 
ATOM   5935  C  CD1 . ILE   E  1 105 ? -20.010 -43.107  -2.508  1.00 24.94 ? 105 ILE   E CD1 1 
ATOM   5936  N  N   . VAL   E  1 106 ? -24.027 -41.886  1.386   1.00 21.91 ? 106 VAL   E N   1 
ATOM   5937  C  CA  . VAL   E  1 106 ? -25.099 -42.247  2.315   1.00 26.32 ? 106 VAL   E CA  1 
ATOM   5938  C  C   . VAL   E  1 106 ? -26.301 -41.329  2.117   1.00 23.80 ? 106 VAL   E C   1 
ATOM   5939  O  O   . VAL   E  1 106 ? -27.446 -41.785  2.027   1.00 24.18 ? 106 VAL   E O   1 
ATOM   5940  C  CB  . VAL   E  1 106 ? -24.587 -42.198  3.763   1.00 22.40 ? 106 VAL   E CB  1 
ATOM   5941  C  CG1 . VAL   E  1 106 ? -25.786 -42.250  4.757   1.00 27.91 ? 106 VAL   E CG1 1 
ATOM   5942  C  CG2 . VAL   E  1 106 ? -23.564 -43.351  4.043   1.00 27.53 ? 106 VAL   E CG2 1 
ATOM   5943  N  N   . HIS   E  1 107 ? -26.063 -40.012  2.064   1.00 25.71 ? 107 HIS   E N   1 
ATOM   5944  C  CA  . HIS   E  1 107 ? -27.184 -39.088  1.924   1.00 26.24 ? 107 HIS   E CA  1 
ATOM   5945  C  C   . HIS   E  1 107 ? -27.835 -39.183  0.548   1.00 25.03 ? 107 HIS   E C   1 
ATOM   5946  O  O   . HIS   E  1 107 ? -29.075 -39.125  0.447   1.00 27.19 ? 107 HIS   E O   1 
ATOM   5947  C  CB  . HIS   E  1 107 ? -26.743 -37.643  2.207   1.00 24.75 ? 107 HIS   E CB  1 
ATOM   5948  C  CG  . HIS   E  1 107 ? -27.868 -36.668  2.093   1.00 31.97 ? 107 HIS   E CG  1 
ATOM   5949  N  ND1 . HIS   E  1 107 ? -28.784 -36.469  3.109   1.00 28.61 ? 107 HIS   E ND1 1 
ATOM   5950  C  CD2 . HIS   E  1 107 ? -28.294 -35.917  1.044   1.00 33.86 ? 107 HIS   E CD2 1 
ATOM   5951  C  CE1 . HIS   E  1 107 ? -29.699 -35.602  2.703   1.00 35.27 ? 107 HIS   E CE1 1 
ATOM   5952  N  NE2 . HIS   E  1 107 ? -29.424 -35.252  1.456   1.00 35.75 ? 107 HIS   E NE2 1 
ATOM   5953  N  N   . CYS   E  1 108 ? -27.028 -39.277  -0.537  1.00 23.01 ? 108 CYS   E N   1 
ATOM   5954  C  CA  . CYS   E  1 108 ? -27.603 -39.458  -1.869  1.00 21.54 ? 108 CYS   E CA  1 
ATOM   5955  C  C   . CYS   E  1 108 ? -28.519 -40.673  -1.898  1.00 23.40 ? 108 CYS   E C   1 
ATOM   5956  O  O   . CYS   E  1 108 ? -29.602 -40.623  -2.487  1.00 23.16 ? 108 CYS   E O   1 
ATOM   5957  C  CB  . CYS   E  1 108 ? -26.508 -39.607  -2.944  1.00 25.46 ? 108 CYS   E CB  1 
ATOM   5958  S  SG  . CYS   E  1 108 ? -25.586 -38.084  -3.223  1.00 25.79 ? 108 CYS   E SG  1 
ATOM   5959  N  N   . GLU   E  1 109 ? -28.102 -41.774  -1.259  1.00 22.49 ? 109 GLU   E N   1 
ATOM   5960  C  CA  . GLU   E  1 109 ? -28.936 -42.969  -1.250  1.00 30.85 ? 109 GLU   E CA  1 
ATOM   5961  C  C   . GLU   E  1 109 ? -30.261 -42.712  -0.519  1.00 30.17 ? 109 GLU   E C   1 
ATOM   5962  O  O   . GLU   E  1 109 ? -31.336 -43.144  -0.974  1.00 28.84 ? 109 GLU   E O   1 
ATOM   5963  C  CB  . GLU   E  1 109 ? -28.164 -44.118  -0.604  1.00 28.04 ? 109 GLU   E CB  1 
ATOM   5964  C  CG  . GLU   E  1 109 ? -28.942 -45.428  -0.534  1.00 26.88 ? 109 GLU   E CG  1 
ATOM   5965  C  CD  . GLU   E  1 109 ? -29.102 -46.125  -1.868  1.00 31.96 ? 109 GLU   E CD  1 
ATOM   5966  O  OE1 . GLU   E  1 109 ? -28.343 -45.774  -2.819  1.00 26.36 ? 109 GLU   E OE1 1 
ATOM   5967  O  OE2 . GLU   E  1 109 ? -29.966 -47.051  -1.965  1.00 25.56 ? 109 GLU   E OE2 1 
ATOM   5968  N  N   . GLN   E  1 110 ? -30.205 -41.954  0.581   1.00 27.64 ? 110 GLN   E N   1 
ATOM   5969  C  CA  . GLN   E  1 110 ? -31.388 -41.759  1.412   1.00 26.07 ? 110 GLN   E CA  1 
ATOM   5970  C  C   . GLN   E  1 110 ? -32.423 -40.865  0.743   1.00 27.86 ? 110 GLN   E C   1 
ATOM   5971  O  O   . GLN   E  1 110 ? -33.621 -41.021  1.000   1.00 28.05 ? 110 GLN   E O   1 
ATOM   5972  C  CB  . GLN   E  1 110 ? -30.978 -41.175  2.771   1.00 26.31 ? 110 GLN   E CB  1 
ATOM   5973  C  CG  . GLN   E  1 110 ? -30.300 -42.162  3.668   1.00 25.73 ? 110 GLN   E CG  1 
ATOM   5974  C  CD  . GLN   E  1 110 ? -29.746 -41.521  4.925   1.00 34.53 ? 110 GLN   E CD  1 
ATOM   5975  O  OE1 . GLN   E  1 110 ? -29.564 -40.305  5.005   1.00 31.48 ? 110 GLN   E OE1 1 
ATOM   5976  N  NE2 . GLN   E  1 110 ? -29.498 -42.339  5.920   1.00 32.68 ? 110 GLN   E NE2 1 
ATOM   5977  N  N   . VAL   E  1 111 ? -32.003 -39.918  -0.099  1.00 24.69 ? 111 VAL   E N   1 
ATOM   5978  C  CA  . VAL   E  1 111 ? -32.938 -39.071  -0.830  1.00 27.34 ? 111 VAL   E CA  1 
ATOM   5979  C  C   . VAL   E  1 111 ? -33.113 -39.533  -2.283  1.00 24.27 ? 111 VAL   E C   1 
ATOM   5980  O  O   . VAL   E  1 111 ? -33.695 -38.818  -3.086  1.00 23.90 ? 111 VAL   E O   1 
ATOM   5981  C  CB  . VAL   E  1 111 ? -32.526 -37.587  -0.757  1.00 32.11 ? 111 VAL   E CB  1 
ATOM   5982  C  CG1 . VAL   E  1 111 ? -32.428 -37.118  0.704   1.00 35.06 ? 111 VAL   E CG1 1 
ATOM   5983  C  CG2 . VAL   E  1 111 ? -31.201 -37.313  -1.472  1.00 29.76 ? 111 VAL   E CG2 1 
ATOM   5984  N  N   . HIS   E  1 112 ? -32.637 -40.725  -2.623  1.00 24.04 ? 112 HIS   E N   1 
ATOM   5985  C  CA  . HIS   E  1 112 ? -32.877 -41.365  -3.917  1.00 26.37 ? 112 HIS   E CA  1 
ATOM   5986  C  C   . HIS   E  1 112 ? -32.237 -40.632  -5.095  1.00 25.66 ? 112 HIS   E C   1 
ATOM   5987  O  O   . HIS   E  1 112 ? -32.695 -40.781  -6.235  1.00 23.43 ? 112 HIS   E O   1 
ATOM   5988  C  CB  . HIS   E  1 112 ? -34.379 -41.539  -4.144  1.00 29.56 ? 112 HIS   E CB  1 
ATOM   5989  C  CG  . HIS   E  1 112 ? -35.087 -42.037  -2.929  1.00 28.09 ? 112 HIS   E CG  1 
ATOM   5990  N  ND1 . HIS   E  1 112 ? -34.871 -43.297  -2.426  1.00 30.84 ? 112 HIS   E ND1 1 
ATOM   5991  C  CD2 . HIS   E  1 112 ? -35.931 -41.422  -2.065  1.00 37.14 ? 112 HIS   E CD2 1 
ATOM   5992  C  CE1 . HIS   E  1 112 ? -35.592 -43.460  -1.328  1.00 32.30 ? 112 HIS   E CE1 1 
ATOM   5993  N  NE2 . HIS   E  1 112 ? -36.241 -42.336  -1.084  1.00 32.89 ? 112 HIS   E NE2 1 
ATOM   5994  N  N   . ASP   E  1 113 ? -31.164 -39.877  -4.853  1.00 27.85 ? 113 ASP   E N   1 
ATOM   5995  C  CA  . ASP   E  1 113 ? -30.401 -39.260  -5.946  1.00 23.85 ? 113 ASP   E CA  1 
ATOM   5996  C  C   . ASP   E  1 113 ? -29.353 -40.287  -6.378  1.00 26.94 ? 113 ASP   E C   1 
ATOM   5997  O  O   . ASP   E  1 113 ? -28.174 -40.245  -6.010  1.00 24.78 ? 113 ASP   E O   1 
ATOM   5998  C  CB  . ASP   E  1 113 ? -29.809 -37.929  -5.505  1.00 25.07 ? 113 ASP   E CB  1 
ATOM   5999  C  CG  . ASP   E  1 113 ? -29.112 -37.183  -6.637  1.00 24.59 ? 113 ASP   E CG  1 
ATOM   6000  O  OD1 . ASP   E  1 113 ? -28.975 -37.746  -7.741  1.00 22.71 ? 113 ASP   E OD1 1 
ATOM   6001  O  OD2 . ASP   E  1 113 ? -28.663 -36.045  -6.395  1.00 26.50 ? 113 ASP   E OD2 1 
ATOM   6002  N  N   . TYR   E  1 114 ? -29.820 -41.265  -7.151  1.00 25.59 ? 114 TYR   E N   1 
ATOM   6003  C  CA  . TYR   E  1 114 ? -28.982 -42.410  -7.479  1.00 21.56 ? 114 TYR   E CA  1 
ATOM   6004  C  C   . TYR   E  1 114 ? -27.902 -42.060  -8.508  1.00 25.02 ? 114 TYR   E C   1 
ATOM   6005  O  O   . TYR   E  1 114 ? -26.843 -42.719  -8.543  1.00 25.03 ? 114 TYR   E O   1 
ATOM   6006  C  CB  . TYR   E  1 114 ? -29.872 -43.555  -7.972  1.00 26.08 ? 114 TYR   E CB  1 
ATOM   6007  C  CG  . TYR   E  1 114 ? -30.846 -44.033  -6.909  1.00 22.88 ? 114 TYR   E CG  1 
ATOM   6008  C  CD1 . TYR   E  1 114 ? -30.385 -44.582  -5.722  1.00 20.01 ? 114 TYR   E CD1 1 
ATOM   6009  C  CD2 . TYR   E  1 114 ? -32.217 -43.925  -7.088  1.00 26.40 ? 114 TYR   E CD2 1 
ATOM   6010  C  CE1 . TYR   E  1 114 ? -31.251 -45.031  -4.731  1.00 23.22 ? 114 TYR   E CE1 1 
ATOM   6011  C  CE2 . TYR   E  1 114 ? -33.109 -44.369  -6.087  1.00 33.40 ? 114 TYR   E CE2 1 
ATOM   6012  C  CZ  . TYR   E  1 114 ? -32.602 -44.919  -4.917  1.00 30.55 ? 114 TYR   E CZ  1 
ATOM   6013  O  OH  . TYR   E  1 114 ? -33.448 -45.370  -3.934  1.00 28.27 ? 114 TYR   E OH  1 
ATOM   6014  N  N   . VAL   E  1 115 ? -28.124 -41.016  -9.300  1.00 24.55 ? 115 VAL   E N   1 
ATOM   6015  C  CA  . VAL   E  1 115 ? -27.125 -40.612  -10.289 1.00 24.16 ? 115 VAL   E CA  1 
ATOM   6016  C  C   . VAL   E  1 115 ? -25.977 -39.895  -9.600  1.00 26.52 ? 115 VAL   E C   1 
ATOM   6017  O  O   . VAL   E  1 115 ? -24.807 -40.142  -9.906  1.00 24.18 ? 115 VAL   E O   1 
ATOM   6018  C  CB  . VAL   E  1 115 ? -27.758 -39.735  -11.390 1.00 23.92 ? 115 VAL   E CB  1 
ATOM   6019  C  CG1 . VAL   E  1 115 ? -26.673 -39.295  -12.416 1.00 23.04 ? 115 VAL   E CG1 1 
ATOM   6020  C  CG2 . VAL   E  1 115 ? -28.881 -40.490  -12.083 1.00 25.34 ? 115 VAL   E CG2 1 
ATOM   6021  N  N   . SER   E  1 116 ? -26.292 -39.030  -8.628  1.00 24.03 ? 116 SER   E N   1 
ATOM   6022  C  CA  . SER   E  1 116 ? -25.247 -38.419  -7.825  1.00 23.70 ? 116 SER   E CA  1 
ATOM   6023  C  C   . SER   E  1 116 ? -24.453 -39.461  -7.064  1.00 24.33 ? 116 SER   E C   1 
ATOM   6024  O  O   . SER   E  1 116 ? -23.217 -39.381  -7.009  1.00 23.48 ? 116 SER   E O   1 
ATOM   6025  C  CB  . SER   E  1 116 ? -25.811 -37.389  -6.864  1.00 24.65 ? 116 SER   E CB  1 
ATOM   6026  O  OG  . SER   E  1 116 ? -26.239 -36.259  -7.582  1.00 24.17 ? 116 SER   E OG  1 
ATOM   6027  N  N   . ARG   E  1 117 ? -25.130 -40.475  -6.518  1.00 24.07 ? 117 ARG   E N   1 
ATOM   6028  C  CA  . ARG   E  1 117 ? -24.399 -41.578  -5.893  1.00 24.73 ? 117 ARG   E CA  1 
ATOM   6029  C  C   . ARG   E  1 117 ? -23.450 -42.255  -6.875  1.00 24.48 ? 117 ARG   E C   1 
ATOM   6030  O  O   . ARG   E  1 117 ? -22.301 -42.566  -6.526  1.00 24.37 ? 117 ARG   E O   1 
ATOM   6031  C  CB  . ARG   E  1 117 ? -25.357 -42.615  -5.304  1.00 27.95 ? 117 ARG   E CB  1 
ATOM   6032  C  CG  . ARG   E  1 117 ? -24.631 -43.887  -4.943  1.00 22.62 ? 117 ARG   E CG  1 
ATOM   6033  C  CD  . ARG   E  1 117 ? -25.494 -44.849  -4.138  1.00 26.35 ? 117 ARG   E CD  1 
ATOM   6034  N  NE  . ARG   E  1 117 ? -24.799 -46.123  -4.006  1.00 25.94 ? 117 ARG   E NE  1 
ATOM   6035  C  CZ  . ARG   E  1 117 ? -24.952 -46.949  -2.987  1.00 32.52 ? 117 ARG   E CZ  1 
ATOM   6036  N  NH1 . ARG   E  1 117 ? -25.839 -46.707  -2.034  1.00 25.04 ? 117 ARG   E NH1 1 
ATOM   6037  N  NH2 . ARG   E  1 117 ? -24.165 -48.018  -2.895  1.00 26.16 ? 117 ARG   E NH2 1 
ATOM   6038  N  N   . ASP   E  1 118 ? -23.902 -42.506  -8.102  1.00 22.48 ? 118 ASP   E N   1 
ATOM   6039  C  CA  . ASP   E  1 118 ? -23.043 -43.207  -9.052  1.00 23.51 ? 118 ASP   E CA  1 
ATOM   6040  C  C   . ASP   E  1 118 ? -21.797 -42.380  -9.378  1.00 25.80 ? 118 ASP   E C   1 
ATOM   6041  O  O   . ASP   E  1 118 ? -20.683 -42.913  -9.468  1.00 22.69 ? 118 ASP   E O   1 
ATOM   6042  C  CB  . ASP   E  1 118 ? -23.832 -43.514  -10.318 1.00 21.25 ? 118 ASP   E CB  1 
ATOM   6043  C  CG  . ASP   E  1 118 ? -23.240 -44.640  -11.121 1.00 24.43 ? 118 ASP   E CG  1 
ATOM   6044  O  OD1 . ASP   E  1 118 ? -22.928 -45.693  -10.546 1.00 25.55 ? 118 ASP   E OD1 1 
ATOM   6045  O  OD2 . ASP   E  1 118 ? -23.114 -44.474  -12.335 1.00 27.34 ? 118 ASP   E OD2 1 
ATOM   6046  N  N   . LEU   E  1 119 ? -21.965 -41.076  -9.559  1.00 23.18 ? 119 LEU   E N   1 
ATOM   6047  C  CA  . LEU   E  1 119 ? -20.813 -40.205  -9.769  1.00 25.02 ? 119 LEU   E CA  1 
ATOM   6048  C  C   . LEU   E  1 119 ? -19.836 -40.265  -8.592  1.00 27.60 ? 119 LEU   E C   1 
ATOM   6049  O  O   . LEU   E  1 119 ? -18.618 -40.376  -8.777  1.00 21.49 ? 119 LEU   E O   1 
ATOM   6050  C  CB  . LEU   E  1 119 ? -21.301 -38.781  -9.990  1.00 22.21 ? 119 LEU   E CB  1 
ATOM   6051  C  CG  . LEU   E  1 119 ? -20.228 -37.688  -9.970  1.00 23.07 ? 119 LEU   E CG  1 
ATOM   6052  C  CD1 . LEU   E  1 119 ? -19.209 -37.913  -11.059 1.00 28.81 ? 119 LEU   E CD1 1 
ATOM   6053  C  CD2 . LEU   E  1 119 ? -20.866 -36.323  -10.127 1.00 33.01 ? 119 LEU   E CD2 1 
ATOM   6054  N  N   . LEU   E  1 120 ? -20.348 -40.160  -7.363  1.00 22.80 ? 120 LEU   E N   1 
ATOM   6055  C  CA  . LEU   E  1 120 ? -19.483 -40.197  -6.194  1.00 25.01 ? 120 LEU   E CA  1 
ATOM   6056  C  C   . LEU   E  1 120 ? -18.798 -41.555  -6.031  1.00 21.63 ? 120 LEU   E C   1 
ATOM   6057  O  O   . LEU   E  1 120 ? -17.640 -41.626  -5.588  1.00 23.93 ? 120 LEU   E O   1 
ATOM   6058  C  CB  . LEU   E  1 120 ? -20.309 -39.841  -4.960  1.00 22.14 ? 120 LEU   E CB  1 
ATOM   6059  C  CG  . LEU   E  1 120 ? -20.851 -38.409  -5.001  1.00 27.13 ? 120 LEU   E CG  1 
ATOM   6060  C  CD1 . LEU   E  1 120 ? -21.755 -38.170  -3.816  1.00 28.59 ? 120 LEU   E CD1 1 
ATOM   6061  C  CD2 . LEU   E  1 120 ? -19.768 -37.318  -5.060  1.00 31.76 ? 120 LEU   E CD2 1 
ATOM   6062  N  N   . LYS   E  1 121 ? -19.493 -42.645  -6.358  1.00 22.02 ? 121 LYS   E N   1 
ATOM   6063  C  CA  . LYS   E  1 121 ? -18.859 -43.973  -6.296  1.00 27.32 ? 121 LYS   E CA  1 
ATOM   6064  C  C   . LYS   E  1 121 ? -17.680 -44.087  -7.273  1.00 25.55 ? 121 LYS   E C   1 
ATOM   6065  O  O   . LYS   E  1 121 ? -16.611 -44.630  -6.927  1.00 24.05 ? 121 LYS   E O   1 
ATOM   6066  C  CB  . LYS   E  1 121 ? -19.908 -45.044  -6.602  1.00 25.22 ? 121 LYS   E CB  1 
ATOM   6067  C  CG  . LYS   E  1 121 ? -19.440 -46.496  -6.566  1.00 24.98 ? 121 LYS   E CG  1 
ATOM   6068  C  CD  . LYS   E  1 121 ? -18.926 -47.043  -7.896  1.00 30.47 ? 121 LYS   E CD  1 
ATOM   6069  C  CE  . LYS   E  1 121 ? -19.992 -47.095  -8.987  1.00 30.17 ? 121 LYS   E CE  1 
ATOM   6070  N  NZ  . LYS   E  1 121 ? -19.396 -47.568  -10.272 1.00 30.56 ? 121 LYS   E NZ  1 
ATOM   6071  N  N   . ASP   E  1 122 ? -17.862 -43.604  -8.503  1.00 24.47 ? 122 ASP   E N   1 
ATOM   6072  C  CA  . ASP   E  1 122 ? -16.753 -43.610  -9.473  1.00 27.46 ? 122 ASP   E CA  1 
ATOM   6073  C  C   . ASP   E  1 122 ? -15.559 -42.789  -8.975  1.00 29.56 ? 122 ASP   E C   1 
ATOM   6074  O  O   . ASP   E  1 122 ? -14.393 -43.212  -9.095  1.00 23.63 ? 122 ASP   E O   1 
ATOM   6075  C  CB  . ASP   E  1 122 ? -17.223 -43.065  -10.821 1.00 25.18 ? 122 ASP   E CB  1 
ATOM   6076  C  CG  . ASP   E  1 122 ? -18.194 -43.991  -11.537 1.00 32.59 ? 122 ASP   E CG  1 
ATOM   6077  O  OD1 . ASP   E  1 122 ? -18.280 -45.197  -11.219 1.00 34.51 ? 122 ASP   E OD1 1 
ATOM   6078  O  OD2 . ASP   E  1 122 ? -18.878 -43.504  -12.447 1.00 30.76 ? 122 ASP   E OD2 1 
ATOM   6079  N  N   . ILE   E  1 123 ? -15.819 -41.606  -8.413  1.00 25.10 ? 123 ILE   E N   1 
ATOM   6080  C  CA  . ILE   E  1 123 ? -14.732 -40.820  -7.843  1.00 23.52 ? 123 ILE   E CA  1 
ATOM   6081  C  C   . ILE   E  1 123 ? -14.056 -41.594  -6.712  1.00 25.86 ? 123 ILE   E C   1 
ATOM   6082  O  O   . ILE   E  1 123 ? -12.821 -41.585  -6.586  1.00 25.32 ? 123 ILE   E O   1 
ATOM   6083  C  CB  . ILE   E  1 123 ? -15.253 -39.445  -7.378  1.00 21.16 ? 123 ILE   E CB  1 
ATOM   6084  C  CG1 . ILE   E  1 123 ? -15.631 -38.560  -8.572  1.00 27.58 ? 123 ILE   E CG1 1 
ATOM   6085  C  CG2 . ILE   E  1 123 ? -14.236 -38.676  -6.494  1.00 22.84 ? 123 ILE   E CG2 1 
ATOM   6086  C  CD1 . ILE   E  1 123 ? -16.374 -37.310  -8.109  1.00 26.34 ? 123 ILE   E CD1 1 
ATOM   6087  N  N   . LEU   E  1 124 ? -14.848 -42.276  -5.874  1.00 26.00 ? 124 LEU   E N   1 
ATOM   6088  C  CA  . LEU   E  1 124 ? -14.287 -43.016  -4.746  1.00 24.48 ? 124 LEU   E CA  1 
ATOM   6089  C  C   . LEU   E  1 124 ? -13.397 -44.157  -5.230  1.00 23.98 ? 124 LEU   E C   1 
ATOM   6090  O  O   . LEU   E  1 124 ? -12.374 -44.461  -4.605  1.00 24.79 ? 124 LEU   E O   1 
ATOM   6091  C  CB  . LEU   E  1 124 ? -15.412 -43.559  -3.860  1.00 24.18 ? 124 LEU   E CB  1 
ATOM   6092  C  CG  . LEU   E  1 124 ? -15.104 -44.476  -2.681  1.00 29.42 ? 124 LEU   E CG  1 
ATOM   6093  C  CD1 . LEU   E  1 124 ? -14.246 -43.782  -1.644  1.00 28.36 ? 124 LEU   E CD1 1 
ATOM   6094  C  CD2 . LEU   E  1 124 ? -16.418 -44.999  -2.002  1.00 28.32 ? 124 LEU   E CD2 1 
ATOM   6095  N  N   . GLU   E  1 125 ? -13.795 -44.814  -6.318  1.00 22.90 ? 125 GLU   E N   1 
ATOM   6096  C  CA  . GLU   E  1 125 ? -12.969 -45.843  -6.933  1.00 24.95 ? 125 GLU   E CA  1 
ATOM   6097  C  C   . GLU   E  1 125 ? -11.624 -45.263  -7.354  1.00 23.70 ? 125 GLU   E C   1 
ATOM   6098  O  O   . GLU   E  1 125 ? -10.575 -45.865  -7.094  1.00 26.97 ? 125 GLU   E O   1 
ATOM   6099  C  CB  . GLU   E  1 125 ? -13.721 -46.464  -8.114  1.00 31.06 ? 125 GLU   E CB  1 
ATOM   6100  C  CG  . GLU   E  1 125 ? -14.893 -47.295  -7.614  1.00 29.20 ? 125 GLU   E CG  1 
ATOM   6101  C  CD  . GLU   E  1 125 ? -15.653 -48.046  -8.676  1.00 41.40 ? 125 GLU   E CD  1 
ATOM   6102  O  OE1 . GLU   E  1 125 ? -15.817 -47.509  -9.816  1.00 35.30 ? 125 GLU   E OE1 1 
ATOM   6103  O  OE2 . GLU   E  1 125 ? -16.121 -49.170  -8.323  1.00 34.63 ? 125 GLU   E OE2 1 
ATOM   6104  N  N   . SER   E  1 126 ? -11.631 -44.066  -7.937  1.00 26.13 ? 126 SER   E N   1 
ATOM   6105  C  CA  A SER   E  1 126 ? -10.380 -43.402  -8.295  0.50 26.08 ? 126 SER   E CA  1 
ATOM   6106  C  CA  B SER   E  1 126 ? -10.376 -43.404  -8.290  0.50 26.09 ? 126 SER   E CA  1 
ATOM   6107  C  C   . SER   E  1 126 ? -9.569  -43.054  -7.049  1.00 29.63 ? 126 SER   E C   1 
ATOM   6108  O  O   . SER   E  1 126 ? -8.337  -43.247  -7.022  1.00 25.03 ? 126 SER   E O   1 
ATOM   6109  C  CB  A SER   E  1 126 ? -10.679 -42.150  -9.128  0.50 26.14 ? 126 SER   E CB  1 
ATOM   6110  C  CB  B SER   E  1 126 ? -10.655 -42.144  -9.105  0.50 26.14 ? 126 SER   E CB  1 
ATOM   6111  O  OG  A SER   E  1 126 ? -9.534  -41.332  -9.275  0.50 26.97 ? 126 SER   E OG  1 
ATOM   6112  O  OG  B SER   E  1 126 ? -11.357 -42.475  -10.275 0.50 29.92 ? 126 SER   E OG  1 
ATOM   6113  N  N   . GLU   E  1 127 ? -10.237 -42.540  -6.004  1.00 24.93 ? 127 GLU   E N   1 
ATOM   6114  C  CA  . GLU   E  1 127 ? -9.495  -42.175  -4.809  1.00 24.72 ? 127 GLU   E CA  1 
ATOM   6115  C  C   . GLU   E  1 127 ? -8.921  -43.408  -4.120  1.00 24.48 ? 127 GLU   E C   1 
ATOM   6116  O  O   . GLU   E  1 127 ? -7.820  -43.348  -3.570  1.00 23.04 ? 127 GLU   E O   1 
ATOM   6117  C  CB  . GLU   E  1 127 ? -10.370 -41.368  -3.852  1.00 23.63 ? 127 GLU   E CB  1 
ATOM   6118  C  CG  . GLU   E  1 127 ? -10.934 -40.041  -4.409  1.00 27.53 ? 127 GLU   E CG  1 
ATOM   6119  C  CD  . GLU   E  1 127 ? -9.896  -39.209  -5.123  1.00 39.81 ? 127 GLU   E CD  1 
ATOM   6120  O  OE1 . GLU   E  1 127 ? -8.742  -39.140  -4.658  1.00 35.92 ? 127 GLU   E OE1 1 
ATOM   6121  O  OE2 . GLU   E  1 127 ? -10.242 -38.643  -6.176  1.00 38.72 ? 127 GLU   E OE2 1 
ATOM   6122  N  N   . GLU   E  1 128 ? -9.654  -44.526  -4.097  1.00 23.33 ? 128 GLU   E N   1 
ATOM   6123  C  CA  . GLU   E  1 128 ? -9.078  -45.724  -3.481  1.00 24.92 ? 128 GLU   E CA  1 
ATOM   6124  C  C   . GLU   E  1 128 ? -7.888  -46.249  -4.288  1.00 27.72 ? 128 GLU   E C   1 
ATOM   6125  O  O   . GLU   E  1 128 ? -6.947  -46.798  -3.701  1.00 22.22 ? 128 GLU   E O   1 
ATOM   6126  C  CB  . GLU   E  1 128 ? -10.125 -46.828  -3.307  1.00 26.53 ? 128 GLU   E CB  1 
ATOM   6127  C  CG  . GLU   E  1 128 ? -11.038 -46.564  -2.105  1.00 27.84 ? 128 GLU   E CG  1 
ATOM   6128  C  CD  . GLU   E  1 128 ? -11.921 -47.736  -1.715  1.00 25.76 ? 128 GLU   E CD  1 
ATOM   6129  O  OE1 . GLU   E  1 128 ? -11.754 -48.873  -2.247  1.00 24.19 ? 128 GLU   E OE1 1 
ATOM   6130  O  OE2 . GLU   E  1 128 ? -12.795 -47.499  -0.854  1.00 28.70 ? 128 GLU   E OE2 1 
ATOM   6131  N  N   . GLU   E  1 129 ? -7.901  -46.067  -5.610  1.00 22.18 ? 129 GLU   E N   1 
ATOM   6132  C  CA  . GLU   E  1 129 ? -6.715  -46.381  -6.415  1.00 27.40 ? 129 GLU   E CA  1 
ATOM   6133  C  C   . GLU   E  1 129 ? -5.530  -45.499  -6.030  1.00 25.54 ? 129 GLU   E C   1 
ATOM   6134  O  O   . GLU   E  1 129 ? -4.383  -45.985  -5.944  1.00 23.94 ? 129 GLU   E O   1 
ATOM   6135  C  CB  . GLU   E  1 129 ? -7.039  -46.242  -7.915  1.00 23.51 ? 129 GLU   E CB  1 
ATOM   6136  C  CG  . GLU   E  1 129 ? -5.895  -46.578  -8.815  1.00 36.11 ? 129 GLU   E CG  1 
ATOM   6137  N  N   . HIS   E  1 130 ? -5.777  -44.202  -5.793  1.00 24.53 ? 130 HIS   E N   1 
ATOM   6138  C  CA  A HIS   E  1 130 ? -4.699  -43.326  -5.353  0.50 28.79 ? 130 HIS   E CA  1 
ATOM   6139  C  CA  B HIS   E  1 130 ? -4.705  -43.316  -5.346  0.50 28.80 ? 130 HIS   E CA  1 
ATOM   6140  C  C   . HIS   E  1 130 ? -4.191  -43.731  -3.973  1.00 31.18 ? 130 HIS   E C   1 
ATOM   6141  O  O   . HIS   E  1 130 ? -2.977  -43.714  -3.718  1.00 25.38 ? 130 HIS   E O   1 
ATOM   6142  C  CB  A HIS   E  1 130 ? -5.177  -41.873  -5.364  0.50 30.19 ? 130 HIS   E CB  1 
ATOM   6143  C  CB  B HIS   E  1 130 ? -5.179  -41.856  -5.301  0.50 30.20 ? 130 HIS   E CB  1 
ATOM   6144  C  CG  A HIS   E  1 130 ? -4.072  -40.868  -5.265  0.50 33.60 ? 130 HIS   E CG  1 
ATOM   6145  C  CG  B HIS   E  1 130 ? -5.623  -41.297  -6.620  0.50 32.05 ? 130 HIS   E CG  1 
ATOM   6146  N  ND1 A HIS   E  1 130 ? -4.306  -39.526  -5.063  0.50 35.22 ? 130 HIS   E ND1 1 
ATOM   6147  N  ND1 B HIS   E  1 130 ? -5.453  -41.957  -7.819  0.50 30.23 ? 130 HIS   E ND1 1 
ATOM   6148  C  CD2 A HIS   E  1 130 ? -2.725  -41.006  -5.342  0.50 31.81 ? 130 HIS   E CD2 1 
ATOM   6149  C  CD2 B HIS   E  1 130 ? -6.248  -40.131  -6.920  0.50 32.80 ? 130 HIS   E CD2 1 
ATOM   6150  C  CE1 A HIS   E  1 130 ? -3.154  -38.883  -5.008  0.50 29.33 ? 130 HIS   E CE1 1 
ATOM   6151  C  CE1 B HIS   E  1 130 ? -5.968  -41.233  -8.798  0.50 27.96 ? 130 HIS   E CE1 1 
ATOM   6152  N  NE2 A HIS   E  1 130 ? -2.181  -39.757  -5.180  0.50 32.38 ? 130 HIS   E NE2 1 
ATOM   6153  N  NE2 B HIS   E  1 130 ? -6.434  -40.109  -8.284  0.50 33.28 ? 130 HIS   E NE2 1 
ATOM   6154  N  N   . ILE   E  1 131 ? -5.100  -44.106  -3.062  1.00 22.51 ? 131 ILE   E N   1 
ATOM   6155  C  CA  . ILE   E  1 131 ? -4.677  -44.570  -1.748  1.00 27.95 ? 131 ILE   E CA  1 
ATOM   6156  C  C   . ILE   E  1 131 ? -3.772  -45.790  -1.870  1.00 25.49 ? 131 ILE   E C   1 
ATOM   6157  O  O   . ILE   E  1 131 ? -2.752  -45.898  -1.174  1.00 24.26 ? 131 ILE   E O   1 
ATOM   6158  C  CB  . ILE   E  1 131 ? -5.905  -44.858  -0.858  1.00 24.67 ? 131 ILE   E CB  1 
ATOM   6159  C  CG1 . ILE   E  1 131 ? -6.492  -43.542  -0.349  1.00 26.33 ? 131 ILE   E CG1 1 
ATOM   6160  C  CG2 . ILE   E  1 131 ? -5.493  -45.730  0.331   1.00 27.87 ? 131 ILE   E CG2 1 
ATOM   6161  C  CD1 . ILE   E  1 131 ? -7.899  -43.682  0.299   1.00 29.15 ? 131 ILE   E CD1 1 
ATOM   6162  N  N   . ASP   E  1 132 ? -4.147  -46.735  -2.733  1.00 24.36 ? 132 ASP   E N   1 
ATOM   6163  C  CA  . ASP   E  1 132 ? -3.326  -47.916  -2.983  1.00 31.22 ? 132 ASP   E CA  1 
ATOM   6164  C  C   . ASP   E  1 132 ? -1.927  -47.519  -3.450  1.00 31.12 ? 132 ASP   E C   1 
ATOM   6165  O  O   . ASP   E  1 132 ? -0.919  -48.020  -2.934  1.00 25.31 ? 132 ASP   E O   1 
ATOM   6166  C  CB  . ASP   E  1 132 ? -4.013  -48.796  -4.031  1.00 25.12 ? 132 ASP   E CB  1 
ATOM   6167  C  CG  . ASP   E  1 132 ? -3.415  -50.211  -4.110  1.00 34.95 ? 132 ASP   E CG  1 
ATOM   6168  O  OD1 . ASP   E  1 132 ? -2.598  -50.577  -3.253  1.00 41.44 ? 132 ASP   E OD1 1 
ATOM   6169  O  OD2 . ASP   E  1 132 ? -3.778  -50.954  -5.033  1.00 37.69 ? 132 ASP   E OD2 1 
ATOM   6170  N  N   . TYR   E  1 133 ? -1.861  -46.587  -4.400  1.00 26.28 ? 133 TYR   E N   1 
ATOM   6171  C  CA  . TYR   E  1 133 ? -0.584  -46.117  -4.911  1.00 26.51 ? 133 TYR   E CA  1 
ATOM   6172  C  C   . TYR   E  1 133 ? 0.267   -45.519  -3.789  1.00 26.32 ? 133 TYR   E C   1 
ATOM   6173  O  O   . TYR   E  1 133 ? 1.443   -45.876  -3.636  1.00 25.96 ? 133 TYR   E O   1 
ATOM   6174  C  CB  . TYR   E  1 133 ? -0.804  -45.097  -6.036  1.00 25.97 ? 133 TYR   E CB  1 
ATOM   6175  C  CG  . TYR   E  1 133 ? 0.454   -44.282  -6.363  1.00 27.78 ? 133 TYR   E CG  1 
ATOM   6176  C  CD1 . TYR   E  1 133 ? 1.398   -44.759  -7.250  1.00 31.12 ? 133 TYR   E CD1 1 
ATOM   6177  C  CD2 . TYR   E  1 133 ? 0.666   -43.028  -5.788  1.00 33.45 ? 133 TYR   E CD2 1 
ATOM   6178  C  CE1 . TYR   E  1 133 ? 2.561   -44.023  -7.538  1.00 31.52 ? 133 TYR   E CE1 1 
ATOM   6179  C  CE2 . TYR   E  1 133 ? 1.800   -42.286  -6.079  1.00 27.42 ? 133 TYR   E CE2 1 
ATOM   6180  C  CZ  . TYR   E  1 133 ? 2.745   -42.796  -6.954  1.00 25.88 ? 133 TYR   E CZ  1 
ATOM   6181  O  OH  . TYR   E  1 133 ? 3.866   -42.058  -7.269  1.00 36.70 ? 133 TYR   E OH  1 
ATOM   6182  N  N   . LEU   E  1 134 ? -0.307  -44.605  -3.000  1.00 22.36 ? 134 LEU   E N   1 
ATOM   6183  C  CA  . LEU   E  1 134 ? 0.454   -43.932  -1.948  1.00 26.43 ? 134 LEU   E CA  1 
ATOM   6184  C  C   . LEU   E  1 134 ? 0.917   -44.914  -0.879  1.00 25.09 ? 134 LEU   E C   1 
ATOM   6185  O  O   . LEU   E  1 134 ? 2.072   -44.857  -0.426  1.00 26.50 ? 134 LEU   E O   1 
ATOM   6186  C  CB  . LEU   E  1 134 ? -0.378  -42.816  -1.296  1.00 23.80 ? 134 LEU   E CB  1 
ATOM   6187  C  CG  . LEU   E  1 134 ? -0.731  -41.635  -2.197  1.00 27.22 ? 134 LEU   E CG  1 
ATOM   6188  C  CD1 . LEU   E  1 134 ? -1.950  -40.843  -1.637  1.00 25.13 ? 134 LEU   E CD1 1 
ATOM   6189  C  CD2 . LEU   E  1 134 ? 0.438   -40.715  -2.389  1.00 28.12 ? 134 LEU   E CD2 1 
ATOM   6190  N  N   . GLU   E  1 135 ? 0.006   -45.771  -0.401  1.00 23.03 ? 135 GLU   E N   1 
ATOM   6191  C  CA  . GLU   E  1 135 ? 0.398   -46.733  0.626   1.00 28.18 ? 135 GLU   E CA  1 
ATOM   6192  C  C   . GLU   E  1 135 ? 1.544   -47.596  0.119   1.00 26.78 ? 135 GLU   E C   1 
ATOM   6193  O  O   . GLU   E  1 135 ? 2.471   -47.937  0.879   1.00 25.94 ? 135 GLU   E O   1 
ATOM   6194  C  CB  . GLU   E  1 135 ? -0.771  -47.624  1.019   1.00 28.88 ? 135 GLU   E CB  1 
ATOM   6195  C  CG  . GLU   E  1 135 ? -1.897  -46.910  1.801   1.00 27.32 ? 135 GLU   E CG  1 
ATOM   6196  C  CD  . GLU   E  1 135 ? -3.085  -47.826  2.076   1.00 30.28 ? 135 GLU   E CD  1 
ATOM   6197  O  OE1 . GLU   E  1 135 ? -3.354  -48.752  1.265   1.00 31.18 ? 135 GLU   E OE1 1 
ATOM   6198  O  OE2 . GLU   E  1 135 ? -3.755  -47.598  3.102   1.00 30.15 ? 135 GLU   E OE2 1 
ATOM   6199  N  N   . THR   E  1 136 ? 1.462   -47.989  -1.155  1.00 25.83 ? 136 THR   E N   1 
ATOM   6200  C  CA  . THR   E  1 136 ? 2.482   -48.830  -1.779  1.00 30.14 ? 136 THR   E CA  1 
ATOM   6201  C  C   . THR   E  1 136 ? 3.818   -48.101  -1.856  1.00 33.55 ? 136 THR   E C   1 
ATOM   6202  O  O   . THR   E  1 136 ? 4.866   -48.696  -1.553  1.00 27.45 ? 136 THR   E O   1 
ATOM   6203  C  CB  . THR   E  1 136 ? 1.986   -49.276  -3.162  1.00 34.86 ? 136 THR   E CB  1 
ATOM   6204  O  OG1 . THR   E  1 136 ? 0.781   -50.040  -3.019  1.00 30.99 ? 136 THR   E OG1 1 
ATOM   6205  C  CG2 . THR   E  1 136 ? 2.996   -50.147  -3.872  1.00 30.67 ? 136 THR   E CG2 1 
ATOM   6206  N  N   . GLN   E  1 137 ? 3.796   -46.796  -2.193  1.00 23.75 ? 137 GLN   E N   1 
ATOM   6207  C  CA  . GLN   E  1 137 ? 5.037   -46.026  -2.271  1.00 28.16 ? 137 GLN   E CA  1 
ATOM   6208  C  C   . GLN   E  1 137 ? 5.691   -45.939  -0.898  1.00 27.64 ? 137 GLN   E C   1 
ATOM   6209  O  O   . GLN   E  1 137 ? 6.901   -46.143  -0.761  1.00 24.19 ? 137 GLN   E O   1 
ATOM   6210  C  CB  . GLN   E  1 137 ? 4.779   -44.616  -2.813  1.00 25.72 ? 137 GLN   E CB  1 
ATOM   6211  C  CG  . GLN   E  1 137 ? 4.198   -44.525  -4.220  1.00 24.98 ? 137 GLN   E CG  1 
ATOM   6212  C  CD  . GLN   E  1 137 ? 4.713   -45.620  -5.138  1.00 33.80 ? 137 GLN   E CD  1 
ATOM   6213  O  OE1 . GLN   E  1 137 ? 4.012   -46.599  -5.421  1.00 38.69 ? 137 GLN   E OE1 1 
ATOM   6214  N  NE2 . GLN   E  1 137 ? 5.952   -45.478  -5.574  1.00 24.29 ? 137 GLN   E NE2 1 
ATOM   6215  N  N   . LEU   E  1 138 ? 4.889   -45.677  0.140   1.00 26.84 ? 138 LEU   E N   1 
ATOM   6216  C  CA  . LEU   E  1 138 ? 5.436   -45.554  1.479   1.00 27.34 ? 138 LEU   E CA  1 
ATOM   6217  C  C   . LEU   E  1 138 ? 6.004   -46.878  1.950   1.00 32.74 ? 138 LEU   E C   1 
ATOM   6218  O  O   . LEU   E  1 138 ? 7.045   -46.915  2.619   1.00 29.22 ? 138 LEU   E O   1 
ATOM   6219  C  CB  . LEU   E  1 138 ? 4.368   -45.032  2.444   1.00 27.01 ? 138 LEU   E CB  1 
ATOM   6220  C  CG  . LEU   E  1 138 ? 3.995   -43.570  2.218   1.00 29.88 ? 138 LEU   E CG  1 
ATOM   6221  C  CD1 . LEU   E  1 138 ? 2.662   -43.206  2.929   1.00 26.78 ? 138 LEU   E CD1 1 
ATOM   6222  C  CD2 . LEU   E  1 138 ? 5.160   -42.653  2.683   1.00 28.57 ? 138 LEU   E CD2 1 
ATOM   6223  N  N   . GLY   E  1 139 ? 5.343   -47.975  1.608   1.00 24.25 ? 139 GLY   E N   1 
ATOM   6224  C  CA  . GLY   E  1 139 ? 5.910   -49.281  1.901   1.00 29.38 ? 139 GLY   E CA  1 
ATOM   6225  C  C   . GLY   E  1 139 ? 7.181   -49.560  1.107   1.00 30.27 ? 139 GLY   E C   1 
ATOM   6226  O  O   . GLY   E  1 139 ? 8.126   -50.152  1.623   1.00 28.24 ? 139 GLY   E O   1 
ATOM   6227  N  N   . LEU   E  1 140 ? 7.222   -49.135  -0.154  1.00 27.14 ? 140 LEU   E N   1 
ATOM   6228  C  CA  . LEU   E  1 140 ? 8.411   -49.385  -0.960  1.00 30.64 ? 140 LEU   E CA  1 
ATOM   6229  C  C   . LEU   E  1 140 ? 9.619   -48.672  -0.372  1.00 29.31 ? 140 LEU   E C   1 
ATOM   6230  O  O   . LEU   E  1 140 ? 10.726  -49.225  -0.357  1.00 29.13 ? 140 LEU   E O   1 
ATOM   6231  C  CB  . LEU   E  1 140 ? 8.181   -48.957  -2.413  1.00 29.48 ? 140 LEU   E CB  1 
ATOM   6232  C  CG  . LEU   E  1 140 ? 7.435   -49.956  -3.310  1.00 26.82 ? 140 LEU   E CG  1 
ATOM   6233  C  CD1 . LEU   E  1 140 ? 7.191   -49.308  -4.667  1.00 28.11 ? 140 LEU   E CD1 1 
ATOM   6234  C  CD2 . LEU   E  1 140 ? 8.192   -51.278  -3.520  1.00 26.15 ? 140 LEU   E CD2 1 
ATOM   6235  N  N   . ILE   E  1 141 ? 9.425   -47.452  0.136   1.00 26.40 ? 141 ILE   E N   1 
ATOM   6236  C  CA  . ILE   E  1 141 ? 10.519  -46.746  0.798   1.00 26.68 ? 141 ILE   E CA  1 
ATOM   6237  C  C   . ILE   E  1 141 ? 11.120  -47.615  1.899   1.00 33.34 ? 141 ILE   E C   1 
ATOM   6238  O  O   . ILE   E  1 141 ? 12.348  -47.663  2.084   1.00 29.08 ? 141 ILE   E O   1 
ATOM   6239  C  CB  . ILE   E  1 141 ? 10.033  -45.394  1.335   1.00 26.81 ? 141 ILE   E CB  1 
ATOM   6240  C  CG1 . ILE   E  1 141 ? 9.822   -44.443  0.169   1.00 25.79 ? 141 ILE   E CG1 1 
ATOM   6241  C  CG2 . ILE   E  1 141 ? 11.048  -44.799  2.366   1.00 28.64 ? 141 ILE   E CG2 1 
ATOM   6242  C  CD1 . ILE   E  1 141 ? 9.066   -43.217  0.555   1.00 35.85 ? 141 ILE   E CD1 1 
ATOM   6243  N  N   . GLN   E  1 142 ? 10.270  -48.342  2.624   1.00 29.58 ? 142 GLN   E N   1 
ATOM   6244  C  CA  . GLN   E  1 142 ? 10.778  -49.187  3.700   1.00 30.82 ? 142 GLN   E CA  1 
ATOM   6245  C  C   . GLN   E  1 142 ? 11.482  -50.413  3.143   1.00 32.96 ? 142 GLN   E C   1 
ATOM   6246  O  O   . GLN   E  1 142 ? 12.438  -50.907  3.744   1.00 36.39 ? 142 GLN   E O   1 
ATOM   6247  C  CB  . GLN   E  1 142 ? 9.652   -49.622  4.628   1.00 30.12 ? 142 GLN   E CB  1 
ATOM   6248  C  CG  . GLN   E  1 142 ? 8.960   -48.489  5.363   1.00 40.67 ? 142 GLN   E CG  1 
ATOM   6249  C  CD  . GLN   E  1 142 ? 9.927   -47.654  6.193   1.00 44.16 ? 142 GLN   E CD  1 
ATOM   6250  O  OE1 . GLN   E  1 142 ? 10.691  -48.185  6.998   1.00 51.86 ? 142 GLN   E OE1 1 
ATOM   6251  N  NE2 . GLN   E  1 142 ? 9.902   -46.338  5.990   1.00 44.52 ? 142 GLN   E NE2 1 
ATOM   6252  N  N   . LYS   E  1 143 ? 11.018  -50.934  2.017   1.00 30.55 ? 143 LYS   E N   1 
ATOM   6253  C  CA  . LYS   E  1 143 ? 11.554  -52.204  1.551   1.00 34.10 ? 143 LYS   E CA  1 
ATOM   6254  C  C   . LYS   E  1 143 ? 12.857  -52.029  0.779   1.00 36.17 ? 143 LYS   E C   1 
ATOM   6255  O  O   . LYS   E  1 143 ? 13.757  -52.859  0.904   1.00 31.55 ? 143 LYS   E O   1 
ATOM   6256  C  CB  . LYS   E  1 143 ? 10.507  -52.920  0.691   1.00 33.25 ? 143 LYS   E CB  1 
ATOM   6257  C  CG  . LYS   E  1 143 ? 9.332   -53.457  1.500   1.00 31.00 ? 143 LYS   E CG  1 
ATOM   6258  C  CD  . LYS   E  1 143 ? 8.313   -54.181  0.584   1.00 38.25 ? 143 LYS   E CD  1 
ATOM   6259  C  CE  . LYS   E  1 143 ? 7.150   -54.776  1.402   1.00 50.34 ? 143 LYS   E CE  1 
ATOM   6260  N  NZ  . LYS   E  1 143 ? 6.273   -53.743  2.050   1.00 55.86 ? 143 LYS   E NZ  1 
ATOM   6261  N  N   . VAL   E  1 144 ? 12.981  -50.983  -0.041  1.00 31.75 ? 144 VAL   E N   1 
ATOM   6262  C  CA  . VAL   E  1 144 ? 14.173  -50.802  -0.865  1.00 27.55 ? 144 VAL   E CA  1 
ATOM   6263  C  C   . VAL   E  1 144 ? 15.071  -49.702  -0.327  1.00 31.68 ? 144 VAL   E C   1 
ATOM   6264  O  O   . VAL   E  1 144 ? 16.204  -49.528  -0.827  1.00 28.14 ? 144 VAL   E O   1 
ATOM   6265  C  CB  . VAL   E  1 144 ? 13.805  -50.551  -2.350  1.00 31.25 ? 144 VAL   E CB  1 
ATOM   6266  C  CG1 . VAL   E  1 144 ? 12.750  -51.545  -2.824  1.00 33.33 ? 144 VAL   E CG1 1 
ATOM   6267  C  CG2 . VAL   E  1 144 ? 13.347  -49.136  -2.604  1.00 28.18 ? 144 VAL   E CG2 1 
ATOM   6268  N  N   . GLY   E  1 145 ? 14.636  -48.989  0.710   1.00 28.57 ? 145 GLY   E N   1 
ATOM   6269  C  CA  . GLY   E  1 145 ? 15.419  -47.884  1.249   1.00 29.76 ? 145 GLY   E CA  1 
ATOM   6270  C  C   . GLY   E  1 145 ? 15.193  -46.575  0.513   1.00 28.73 ? 145 GLY   E C   1 
ATOM   6271  O  O   . GLY   E  1 145 ? 14.857  -46.554  -0.675  1.00 30.70 ? 145 GLY   E O   1 
ATOM   6272  N  N   . LEU   E  1 146 ? 15.336  -45.460  1.217   1.00 24.74 ? 146 LEU   E N   1 
ATOM   6273  C  CA  . LEU   E  1 146 ? 14.918  -44.185  0.637   1.00 31.52 ? 146 LEU   E CA  1 
ATOM   6274  C  C   . LEU   E  1 146 ? 15.754  -43.821  -0.586  1.00 31.06 ? 146 LEU   E C   1 
ATOM   6275  O  O   . LEU   E  1 146 ? 15.225  -43.360  -1.606  1.00 25.65 ? 146 LEU   E O   1 
ATOM   6276  C  CB  . LEU   E  1 146 ? 15.021  -43.087  1.691   1.00 29.26 ? 146 LEU   E CB  1 
ATOM   6277  C  CG  . LEU   E  1 146 ? 14.565  -41.711  1.220   1.00 30.21 ? 146 LEU   E CG  1 
ATOM   6278  C  CD1 . LEU   E  1 146 ? 13.107  -41.785  0.738   1.00 31.80 ? 146 LEU   E CD1 1 
ATOM   6279  C  CD2 . LEU   E  1 146 ? 14.688  -40.699  2.335   1.00 33.36 ? 146 LEU   E CD2 1 
ATOM   6280  N  N   . GLU   E  1 147 ? 17.070  -44.005  -0.500  1.00 25.20 ? 147 GLU   E N   1 
ATOM   6281  C  CA  . GLU   E  1 147 ? 17.949  -43.613  -1.601  1.00 23.15 ? 147 GLU   E CA  1 
ATOM   6282  C  C   . GLU   E  1 147 ? 17.629  -44.374  -2.883  1.00 23.47 ? 147 GLU   E C   1 
ATOM   6283  O  O   . GLU   E  1 147 ? 17.613  -43.782  -3.970  1.00 23.74 ? 147 GLU   E O   1 
ATOM   6284  C  CB  . GLU   E  1 147 ? 19.413  -43.812  -1.191  1.00 26.90 ? 147 GLU   E CB  1 
ATOM   6285  C  CG  . GLU   E  1 147 ? 19.872  -42.767  -0.199  1.00 34.02 ? 147 GLU   E CG  1 
ATOM   6286  C  CD  . GLU   E  1 147 ? 21.380  -42.830  0.078   1.00 54.27 ? 147 GLU   E CD  1 
ATOM   6287  O  OE1 . GLU   E  1 147 ? 21.946  -43.940  0.051   1.00 50.33 ? 147 GLU   E OE1 1 
ATOM   6288  O  OE2 . GLU   E  1 147 ? 21.997  -41.767  0.310   1.00 52.46 ? 147 GLU   E OE2 1 
ATOM   6289  N  N   . ASN   E  1 148 ? 17.376  -45.685  -2.784  1.00 24.06 ? 148 ASN   E N   1 
ATOM   6290  C  CA  . ASN   E  1 148 ? 16.963  -46.442  -3.966  1.00 22.73 ? 148 ASN   E CA  1 
ATOM   6291  C  C   . ASN   E  1 148 ? 15.574  -45.986  -4.435  1.00 29.87 ? 148 ASN   E C   1 
ATOM   6292  O  O   . ASN   E  1 148 ? 15.346  -45.789  -5.631  1.00 22.94 ? 148 ASN   E O   1 
ATOM   6293  C  CB  . ASN   E  1 148 ? 16.904  -47.944  -3.673  1.00 25.87 ? 148 ASN   E CB  1 
ATOM   6294  C  CG  . ASN   E  1 148 ? 18.269  -48.627  -3.712  1.00 27.78 ? 148 ASN   E CG  1 
ATOM   6295  O  OD1 . ASN   E  1 148 ? 19.255  -48.055  -4.145  1.00 24.71 ? 148 ASN   E OD1 1 
ATOM   6296  N  ND2 . ASN   E  1 148 ? 18.298  -49.883  -3.315  1.00 25.39 ? 148 ASN   E ND2 1 
ATOM   6297  N  N   . TYR   E  1 149 ? 14.655  -45.774  -3.497  1.00 26.89 ? 149 TYR   E N   1 
ATOM   6298  C  CA  . TYR   E  1 149 ? 13.309  -45.377  -3.893  1.00 26.34 ? 149 TYR   E CA  1 
ATOM   6299  C  C   . TYR   E  1 149 ? 13.367  -44.107  -4.720  1.00 23.30 ? 149 TYR   E C   1 
ATOM   6300  O  O   . TYR   E  1 149 ? 12.757  -44.015  -5.787  1.00 26.64 ? 149 TYR   E O   1 
ATOM   6301  C  CB  . TYR   E  1 149 ? 12.396  -45.177  -2.677  1.00 29.88 ? 149 TYR   E CB  1 
ATOM   6302  C  CG  . TYR   E  1 149 ? 11.029  -44.720  -3.140  1.00 25.29 ? 149 TYR   E CG  1 
ATOM   6303  C  CD1 . TYR   E  1 149 ? 10.104  -45.627  -3.610  1.00 26.87 ? 149 TYR   E CD1 1 
ATOM   6304  C  CD2 . TYR   E  1 149 ? 10.697  -43.374  -3.172  1.00 29.40 ? 149 TYR   E CD2 1 
ATOM   6305  C  CE1 . TYR   E  1 149 ? 8.842   -45.206  -4.058  1.00 28.16 ? 149 TYR   E CE1 1 
ATOM   6306  C  CE2 . TYR   E  1 149 ? 9.436   -42.949  -3.624  1.00 26.09 ? 149 TYR   E CE2 1 
ATOM   6307  C  CZ  . TYR   E  1 149 ? 8.531   -43.867  -4.067  1.00 26.29 ? 149 TYR   E CZ  1 
ATOM   6308  O  OH  . TYR   E  1 149 ? 7.295   -43.440  -4.549  1.00 29.29 ? 149 TYR   E OH  1 
ATOM   6309  N  N   . LEU   E  1 150 ? 14.110  -43.118  -4.248  1.00 23.71 ? 150 LEU   E N   1 
ATOM   6310  C  CA  . LEU   E  1 150 ? 14.221  -41.880  -4.995  1.00 24.49 ? 150 LEU   E CA  1 
ATOM   6311  C  C   . LEU   E  1 150 ? 14.937  -42.092  -6.329  1.00 28.49 ? 150 LEU   E C   1 
ATOM   6312  O  O   . LEU   E  1 150 ? 14.519  -41.547  -7.363  1.00 27.58 ? 150 LEU   E O   1 
ATOM   6313  C  CB  . LEU   E  1 150 ? 14.926  -40.851  -4.132  1.00 20.87 ? 150 LEU   E CB  1 
ATOM   6314  C  CG  . LEU   E  1 150 ? 14.200  -40.509  -2.822  1.00 30.37 ? 150 LEU   E CG  1 
ATOM   6315  C  CD1 . LEU   E  1 150 ? 15.016  -39.533  -1.986  1.00 33.77 ? 150 LEU   E CD1 1 
ATOM   6316  C  CD2 . LEU   E  1 150 ? 12.801  -39.899  -3.080  1.00 27.39 ? 150 LEU   E CD2 1 
ATOM   6317  N  N   . GLN   E  1 151 ? 15.972  -42.931  -6.337  1.00 24.27 ? 151 GLN   E N   1 
ATOM   6318  C  CA  . GLN   E  1 151 ? 16.696  -43.209  -7.575  1.00 26.07 ? 151 GLN   E CA  1 
ATOM   6319  C  C   . GLN   E  1 151 ? 15.764  -43.783  -8.627  1.00 24.90 ? 151 GLN   E C   1 
ATOM   6320  O  O   . GLN   E  1 151 ? 15.860  -43.450  -9.816  1.00 26.10 ? 151 GLN   E O   1 
ATOM   6321  C  CB  . GLN   E  1 151 ? 17.822  -44.201  -7.302  1.00 25.80 ? 151 GLN   E CB  1 
ATOM   6322  C  CG  . GLN   E  1 151 ? 18.576  -44.685  -8.563  1.00 23.10 ? 151 GLN   E CG  1 
ATOM   6323  C  CD  . GLN   E  1 151 ? 19.560  -45.826  -8.292  1.00 28.04 ? 151 GLN   E CD  1 
ATOM   6324  O  OE1 . GLN   E  1 151 ? 19.360  -46.664  -7.404  1.00 25.67 ? 151 GLN   E OE1 1 
ATOM   6325  N  NE2 . GLN   E  1 151 ? 20.623  -45.866  -9.082  1.00 27.17 ? 151 GLN   E NE2 1 
ATOM   6326  N  N   . SER   E  1 152 ? 14.892  -44.689  -8.205  1.00 22.30 ? 152 SER   E N   1 
ATOM   6327  C  CA  . SER   E  1 152 ? 13.948  -45.312  -9.117  1.00 24.07 ? 152 SER   E CA  1 
ATOM   6328  C  C   . SER   E  1 152 ? 12.915  -44.330  -9.644  1.00 31.39 ? 152 SER   E C   1 
ATOM   6329  O  O   . SER   E  1 152 ? 12.159  -44.696  -10.550 1.00 27.89 ? 152 SER   E O   1 
ATOM   6330  C  CB  . SER   E  1 152 ? 13.238  -46.465  -8.428  1.00 26.45 ? 152 SER   E CB  1 
ATOM   6331  O  OG  . SER   E  1 152 ? 14.119  -47.559  -8.268  1.00 27.87 ? 152 SER   E OG  1 
ATOM   6332  N  N   . HIS   E  1 153 ? 12.844  -43.117  -9.087  1.00 25.04 ? 153 HIS   E N   1 
ATOM   6333  C  CA  . HIS   E  1 153 ? 11.884  -42.108  -9.534  1.00 29.83 ? 153 HIS   E CA  1 
ATOM   6334  C  C   . HIS   E  1 153 ? 12.552  -40.891  -10.166 1.00 26.66 ? 153 HIS   E C   1 
ATOM   6335  O  O   . HIS   E  1 153 ? 11.921  -39.837  -10.319 1.00 25.88 ? 153 HIS   E O   1 
ATOM   6336  C  CB  . HIS   E  1 153 ? 10.983  -41.744  -8.355  1.00 27.11 ? 153 HIS   E CB  1 
ATOM   6337  C  CG  . HIS   E  1 153 ? 9.985   -42.812  -8.074  1.00 26.89 ? 153 HIS   E CG  1 
ATOM   6338  N  ND1 . HIS   E  1 153 ? 10.255  -43.895  -7.267  1.00 25.35 ? 153 HIS   E ND1 1 
ATOM   6339  C  CD2 . HIS   E  1 153 ? 8.744   -43.023  -8.583  1.00 28.08 ? 153 HIS   E CD2 1 
ATOM   6340  C  CE1 . HIS   E  1 153 ? 9.207   -44.697  -7.243  1.00 38.13 ? 153 HIS   E CE1 1 
ATOM   6341  N  NE2 . HIS   E  1 153 ? 8.276   -44.192  -8.038  1.00 29.05 ? 153 HIS   E NE2 1 
ATOM   6342  N  N   . MET   E  1 154 ? 13.815  -41.028  -10.588 1.00 27.78 ? 154 MET   E N   1 
ATOM   6343  C  CA  . MET   E  1 154 ? 14.514  -39.910  -11.213 1.00 28.50 ? 154 MET   E CA  1 
ATOM   6344  C  C   . MET   E  1 154 ? 14.101  -39.738  -12.668 1.00 28.34 ? 154 MET   E C   1 
ATOM   6345  O  O   . MET   E  1 154 ? 13.876  -38.618  -13.127 1.00 30.78 ? 154 MET   E O   1 
ATOM   6346  C  CB  . MET   E  1 154 ? 16.039  -40.114  -11.160 1.00 28.05 ? 154 MET   E CB  1 
ATOM   6347  C  CG  . MET   E  1 154 ? 16.724  -39.770  -9.865  1.00 34.56 ? 154 MET   E CG  1 
ATOM   6348  S  SD  . MET   E  1 154 ? 18.538  -40.127  -9.927  1.00 41.50 ? 154 MET   E SD  1 
ATOM   6349  C  CE  . MET   E  1 154 ? 18.944  -39.714  -11.632 1.00 32.26 ? 154 MET   E CE  1 
ATOM   6350  N  N   . HIS   E  1 155 ? 14.004  -40.831  -13.402 1.00 30.42 ? 155 HIS   E N   1 
ATOM   6351  C  CA  . HIS   E  1 155 ? 13.756  -40.793  -14.834 1.00 41.97 ? 155 HIS   E CA  1 
ATOM   6352  C  C   . HIS   E  1 155 ? 12.353  -41.322  -15.129 1.00 35.84 ? 155 HIS   E C   1 
ATOM   6353  O  O   . HIS   E  1 155 ? 11.887  -42.267  -14.488 1.00 43.96 ? 155 HIS   E O   1 
ATOM   6354  C  CB  . HIS   E  1 155 ? 14.796  -41.638  -15.583 1.00 38.73 ? 155 HIS   E CB  1 
ATOM   6355  C  CG  . HIS   E  1 155 ? 16.225  -41.224  -15.364 1.00 41.43 ? 155 HIS   E CG  1 
ATOM   6356  N  ND1 . HIS   E  1 155 ? 17.257  -42.140  -15.303 1.00 50.67 ? 155 HIS   E ND1 1 
ATOM   6357  C  CD2 . HIS   E  1 155 ? 16.803  -40.001  -15.222 1.00 41.57 ? 155 HIS   E CD2 1 
ATOM   6358  C  CE1 . HIS   E  1 155 ? 18.402  -41.504  -15.111 1.00 44.70 ? 155 HIS   E CE1 1 
ATOM   6359  N  NE2 . HIS   E  1 155 ? 18.157  -40.207  -15.060 1.00 46.43 ? 155 HIS   E NE2 1 
ATOM   6360  N  N   . GLU   E  1 156 ? 11.673  -40.710  -16.091 1.00 50.42 ? 156 GLU   E N   1 
ATOM   6361  C  CA  . GLU   E  1 156 ? 10.532  -41.366  -16.729 1.00 61.28 ? 156 GLU   E CA  1 
ATOM   6362  C  C   . GLU   E  1 156 ? 11.051  -42.343  -17.797 1.00 56.45 ? 156 GLU   E C   1 
ATOM   6363  O  O   . GLU   E  1 156 ? 10.872  -43.558  -17.689 1.00 57.11 ? 156 GLU   E O   1 
ATOM   6364  C  CB  . GLU   E  1 156 ? 9.596   -40.348  -17.366 1.00 56.25 ? 156 GLU   E CB  1 
ATOM   6365  C  CG  . GLU   E  1 156 ? 9.472   -39.064  -16.580 1.00 49.39 ? 156 GLU   E CG  1 
ATOM   6366  C  CD  . GLU   E  1 156 ? 8.463   -38.111  -17.183 1.00 61.51 ? 156 GLU   E CD  1 
ATOM   6367  O  OE1 . GLU   E  1 156 ? 7.458   -38.601  -17.753 1.00 66.58 ? 156 GLU   E OE1 1 
ATOM   6368  O  OE2 . GLU   E  1 156 ? 8.678   -36.876  -17.085 1.00 53.43 ? 156 GLU   E OE2 1 
ATOM   6369  N  N   . MET   F  1 1   ? -5.093  -50.378  2.760   1.00 26.10 ? 1   MET   F N   1 
ATOM   6370  C  CA  . MET   F  1 1   ? -6.125  -49.589  3.504   1.00 32.48 ? 1   MET   F CA  1 
ATOM   6371  C  C   . MET   F  1 1   ? -6.865  -50.602  4.390   1.00 29.52 ? 1   MET   F C   1 
ATOM   6372  O  O   . MET   F  1 1   ? -7.324  -51.633  3.904   1.00 37.73 ? 1   MET   F O   1 
ATOM   6373  C  CB  . MET   F  1 1   ? -7.060  -48.882  2.514   1.00 36.30 ? 1   MET   F CB  1 
ATOM   6374  C  CG  . MET   F  1 1   ? -8.036  -47.853  3.117   1.00 40.83 ? 1   MET   F CG  1 
ATOM   6375  S  SD  . MET   F  1 1   ? -9.169  -47.209  1.850   1.00 42.47 ? 1   MET   F SD  1 
ATOM   6376  C  CE  . MET   F  1 1   ? -10.073 -48.681  1.435   1.00 40.83 ? 1   MET   F CE  1 
ATOM   6377  N  N   . LYS   F  1 2   ? -6.988  -50.330  5.682   1.00 28.83 ? 2   LYS   F N   1 
ATOM   6378  C  CA  . LYS   F  1 2   ? -7.530  -51.333  6.607   1.00 27.97 ? 2   LYS   F CA  1 
ATOM   6379  C  C   . LYS   F  1 2   ? -9.021  -51.532  6.334   1.00 30.64 ? 2   LYS   F C   1 
ATOM   6380  O  O   . LYS   F  1 2   ? -9.833  -50.635  6.571   1.00 34.37 ? 2   LYS   F O   1 
ATOM   6381  C  CB  . LYS   F  1 2   ? -7.275  -50.899  8.046   1.00 38.13 ? 2   LYS   F CB  1 
ATOM   6382  N  N   . GLY   F  1 3   ? -9.384  -52.712  5.823   1.00 25.92 ? 3   GLY   F N   1 
ATOM   6383  C  CA  . GLY   F  1 3   ? -10.773 -53.002  5.516   1.00 30.28 ? 3   GLY   F CA  1 
ATOM   6384  C  C   . GLY   F  1 3   ? -11.551 -53.504  6.721   1.00 35.08 ? 3   GLY   F C   1 
ATOM   6385  O  O   . GLY   F  1 3   ? -10.993 -53.853  7.748   1.00 32.36 ? 3   GLY   F O   1 
ATOM   6386  N  N   . ASP   F  1 4   ? -12.873 -53.521  6.568   1.00 27.79 ? 4   ASP   F N   1 
ATOM   6387  C  CA  . ASP   F  1 4   ? -13.760 -54.116  7.557   1.00 27.48 ? 4   ASP   F CA  1 
ATOM   6388  C  C   . ASP   F  1 4   ? -13.541 -55.629  7.603   1.00 32.07 ? 4   ASP   F C   1 
ATOM   6389  O  O   . ASP   F  1 4   ? -13.466 -56.292  6.574   1.00 29.36 ? 4   ASP   F O   1 
ATOM   6390  C  CB  . ASP   F  1 4   ? -15.209 -53.725  7.202   1.00 27.72 ? 4   ASP   F CB  1 
ATOM   6391  C  CG  . ASP   F  1 4   ? -16.260 -54.351  8.113   1.00 33.36 ? 4   ASP   F CG  1 
ATOM   6392  O  OD1 . ASP   F  1 4   ? -16.598 -53.737  9.128   1.00 32.35 ? 4   ASP   F OD1 1 
ATOM   6393  O  OD2 . ASP   F  1 4   ? -16.787 -55.429  7.775   1.00 28.80 ? 4   ASP   F OD2 1 
ATOM   6394  N  N   . LYS   F  1 5   ? -13.414 -56.180  8.812   1.00 30.30 ? 5   LYS   F N   1 
ATOM   6395  C  CA  . LYS   F  1 5   ? -13.077 -57.594  8.948   1.00 27.85 ? 5   LYS   F CA  1 
ATOM   6396  C  C   . LYS   F  1 5   ? -14.152 -58.506  8.358   1.00 28.39 ? 5   LYS   F C   1 
ATOM   6397  O  O   . LYS   F  1 5   ? -13.839 -59.525  7.732   1.00 29.87 ? 5   LYS   F O   1 
ATOM   6398  C  CB  . LYS   F  1 5   ? -12.867 -57.932  10.432  1.00 39.44 ? 5   LYS   F CB  1 
ATOM   6399  C  CG  . LYS   F  1 5   ? -12.545 -59.388  10.699  1.00 44.99 ? 5   LYS   F CG  1 
ATOM   6400  N  N   . LYS   F  1 6   ? -15.420 -58.216  8.627   1.00 25.45 ? 6   LYS   F N   1 
ATOM   6401  C  CA  . LYS   F  1 6   ? -16.496 -59.031  8.060   1.00 30.43 ? 6   LYS   F CA  1 
ATOM   6402  C  C   . LYS   F  1 6   ? -16.629 -58.852  6.543   1.00 28.80 ? 6   LYS   F C   1 
ATOM   6403  O  O   . LYS   F  1 6   ? -17.031 -59.795  5.843   1.00 29.44 ? 6   LYS   F O   1 
ATOM   6404  C  CB  . LYS   F  1 6   ? -17.818 -58.698  8.780   1.00 32.56 ? 6   LYS   F CB  1 
ATOM   6405  C  CG  . LYS   F  1 6   ? -19.079 -59.460  8.263   1.00 44.42 ? 6   LYS   F CG  1 
ATOM   6406  C  CD  . LYS   F  1 6   ? -19.112 -60.922  8.738   1.00 45.61 ? 6   LYS   F CD  1 
ATOM   6407  N  N   . VAL   F  1 7   ? -16.319 -57.673  5.997   1.00 30.06 ? 7   VAL   F N   1 
ATOM   6408  C  CA  . VAL   F  1 7   ? -16.227 -57.573  4.531   1.00 26.21 ? 7   VAL   F CA  1 
ATOM   6409  C  C   . VAL   F  1 7   ? -15.196 -58.550  4.012   1.00 26.72 ? 7   VAL   F C   1 
ATOM   6410  O  O   . VAL   F  1 7   ? -15.424 -59.257  3.019   1.00 29.67 ? 7   VAL   F O   1 
ATOM   6411  C  CB  . VAL   F  1 7   ? -15.904 -56.141  4.075   1.00 27.44 ? 7   VAL   F CB  1 
ATOM   6412  C  CG1 . VAL   F  1 7   ? -15.472 -56.144  2.620   1.00 32.17 ? 7   VAL   F CG1 1 
ATOM   6413  C  CG2 . VAL   F  1 7   ? -17.141 -55.264  4.203   1.00 27.61 ? 7   VAL   F CG2 1 
ATOM   6414  N  N   . ILE   F  1 8   ? -14.025 -58.585  4.661   1.00 29.59 ? 8   ILE   F N   1 
ATOM   6415  C  CA  . ILE   F  1 8   ? -12.964 -59.480  4.211   1.00 26.88 ? 8   ILE   F CA  1 
ATOM   6416  C  C   . ILE   F  1 8   ? -13.437 -60.935  4.298   1.00 28.26 ? 8   ILE   F C   1 
ATOM   6417  O  O   . ILE   F  1 8   ? -13.205 -61.745  3.385   1.00 26.16 ? 8   ILE   F O   1 
ATOM   6418  C  CB  . ILE   F  1 8   ? -11.675 -59.230  5.023   1.00 28.02 ? 8   ILE   F CB  1 
ATOM   6419  C  CG1 . ILE   F  1 8   ? -11.086 -57.850  4.673   1.00 32.31 ? 8   ILE   F CG1 1 
ATOM   6420  C  CG2 . ILE   F  1 8   ? -10.651 -60.330  4.776   1.00 29.87 ? 8   ILE   F CG2 1 
ATOM   6421  C  CD1 . ILE   F  1 8   ? -9.990  -57.343  5.637   1.00 33.83 ? 8   ILE   F CD1 1 
ATOM   6422  N  N   . GLN   F  1 9   ? -14.131 -61.285  5.382   1.00 27.66 ? 9   GLN   F N   1 
ATOM   6423  C  CA  . GLN   F  1 9   ? -14.695 -62.624  5.488   1.00 31.03 ? 9   GLN   F CA  1 
ATOM   6424  C  C   . GLN   F  1 9   ? -15.678 -62.893  4.352   1.00 22.82 ? 9   GLN   F C   1 
ATOM   6425  O  O   . GLN   F  1 9   ? -15.654 -63.966  3.737   1.00 31.38 ? 9   GLN   F O   1 
ATOM   6426  C  CB  . GLN   F  1 9   ? -15.370 -62.808  6.857   1.00 25.78 ? 9   GLN   F CB  1 
ATOM   6427  C  CG  . GLN   F  1 9   ? -14.375 -62.932  7.989   1.00 38.74 ? 9   GLN   F CG  1 
ATOM   6428  C  CD  . GLN   F  1 9   ? -15.030 -62.752  9.364   1.00 50.60 ? 9   GLN   F CD  1 
ATOM   6429  O  OE1 . GLN   F  1 9   ? -16.182 -62.355  9.458   1.00 40.74 ? 9   GLN   F OE1 1 
ATOM   6430  N  NE2 . GLN   F  1 9   ? -14.283 -63.029  10.422  1.00 46.23 ? 9   GLN   F NE2 1 
ATOM   6431  N  N   . HIS   F  1 10  ? -16.554 -61.944  4.050   1.00 29.12 ? 10  HIS   F N   1 
ATOM   6432  C  CA  . HIS   F  1 10  ? -17.477 -62.183  2.945   1.00 27.40 ? 10  HIS   F CA  1 
ATOM   6433  C  C   . HIS   F  1 10  ? -16.710 -62.384  1.633   1.00 24.59 ? 10  HIS   F C   1 
ATOM   6434  O  O   . HIS   F  1 10  ? -17.001 -63.314  0.874   1.00 27.67 ? 10  HIS   F O   1 
ATOM   6435  C  CB  . HIS   F  1 10  ? -18.463 -61.040  2.816   1.00 30.30 ? 10  HIS   F CB  1 
ATOM   6436  C  CG  . HIS   F  1 10  ? -19.668 -61.177  3.686   1.00 30.48 ? 10  HIS   F CG  1 
ATOM   6437  N  ND1 . HIS   F  1 10  ? -20.702 -62.038  3.391   1.00 31.31 ? 10  HIS   F ND1 1 
ATOM   6438  C  CD2 . HIS   F  1 10  ? -20.018 -60.542  4.827   1.00 30.71 ? 10  HIS   F CD2 1 
ATOM   6439  C  CE1 . HIS   F  1 10  ? -21.631 -61.941  4.327   1.00 41.20 ? 10  HIS   F CE1 1 
ATOM   6440  N  NE2 . HIS   F  1 10  ? -21.244 -61.034  5.208   1.00 36.49 ? 10  HIS   F NE2 1 
ATOM   6441  N  N   . LEU   F  1 11  ? -15.717 -61.527  1.363   1.00 27.92 ? 11  LEU   F N   1 
ATOM   6442  C  CA  . LEU   F  1 11  ? -14.932 -61.655  0.129   1.00 26.55 ? 11  LEU   F CA  1 
ATOM   6443  C  C   . LEU   F  1 11  ? -14.224 -62.999  0.054   1.00 25.93 ? 11  LEU   F C   1 
ATOM   6444  O  O   . LEU   F  1 11  ? -14.157 -63.616  -1.016  1.00 24.47 ? 11  LEU   F O   1 
ATOM   6445  C  CB  . LEU   F  1 11  ? -13.919 -60.525  0.033   1.00 24.53 ? 11  LEU   F CB  1 
ATOM   6446  C  CG  . LEU   F  1 11  ? -14.490 -59.109  -0.089  1.00 27.59 ? 11  LEU   F CG  1 
ATOM   6447  C  CD1 . LEU   F  1 11  ? -13.382 -58.013  -0.133  1.00 32.55 ? 11  LEU   F CD1 1 
ATOM   6448  C  CD2 . LEU   F  1 11  ? -15.382 -59.003  -1.306  1.00 31.46 ? 11  LEU   F CD2 1 
ATOM   6449  N  N   . ASN   F  1 12  ? -13.676 -63.471  1.181   1.00 27.33 ? 12  ASN   F N   1 
ATOM   6450  C  CA  . ASN   F  1 12  ? -13.087 -64.800  1.184   1.00 26.27 ? 12  ASN   F CA  1 
ATOM   6451  C  C   . ASN   F  1 12  ? -14.138 -65.869  0.946   1.00 31.40 ? 12  ASN   F C   1 
ATOM   6452  O  O   . ASN   F  1 12  ? -13.836 -66.895  0.333   1.00 30.81 ? 12  ASN   F O   1 
ATOM   6453  C  CB  . ASN   F  1 12  ? -12.328 -65.065  2.482   1.00 28.34 ? 12  ASN   F CB  1 
ATOM   6454  C  CG  . ASN   F  1 12  ? -10.882 -64.709  2.356   1.00 32.07 ? 12  ASN   F CG  1 
ATOM   6455  O  OD1 . ASN   F  1 12  ? -10.300 -64.884  1.287   1.00 32.97 ? 12  ASN   F OD1 1 
ATOM   6456  N  ND2 . ASN   F  1 12  ? -10.282 -64.189  3.426   1.00 31.48 ? 12  ASN   F ND2 1 
ATOM   6457  N  N   . LYS   F  1 13  ? -15.373 -65.653  1.406   1.00 28.06 ? 13  LYS   F N   1 
ATOM   6458  C  CA  . LYS   F  1 13  ? -16.427 -66.621  1.120   1.00 33.03 ? 13  LYS   F CA  1 
ATOM   6459  C  C   . LYS   F  1 13  ? -16.782 -66.640  -0.367  1.00 31.21 ? 13  LYS   F C   1 
ATOM   6460  O  O   . LYS   F  1 13  ? -17.017 -67.711  -0.944  1.00 28.60 ? 13  LYS   F O   1 
ATOM   6461  C  CB  . LYS   F  1 13  ? -17.676 -66.315  1.953   1.00 32.29 ? 13  LYS   F CB  1 
ATOM   6462  C  CG  . LYS   F  1 13  ? -18.738 -67.415  1.858   1.00 36.43 ? 13  LYS   F CG  1 
ATOM   6463  C  CD  . LYS   F  1 13  ? -19.948 -67.108  2.693   1.00 39.61 ? 13  LYS   F CD  1 
ATOM   6464  C  CE  . LYS   F  1 13  ? -20.951 -68.246  2.648   1.00 41.17 ? 13  LYS   F CE  1 
ATOM   6465  N  NZ  . LYS   F  1 13  ? -22.239 -67.827  3.257   1.00 54.43 ? 13  LYS   F NZ  1 
ATOM   6466  N  N   . ILE   F  1 14  ? -16.871 -65.465  -0.990  1.00 28.93 ? 14  ILE   F N   1 
ATOM   6467  C  CA  . ILE   F  1 14  ? -17.080 -65.398  -2.431  1.00 27.17 ? 14  ILE   F CA  1 
ATOM   6468  C  C   . ILE   F  1 14  ? -15.906 -66.064  -3.175  1.00 29.97 ? 14  ILE   F C   1 
ATOM   6469  O  O   . ILE   F  1 14  ? -16.101 -66.846  -4.121  1.00 28.99 ? 14  ILE   F O   1 
ATOM   6470  C  CB  . ILE   F  1 14  ? -17.275 -63.926  -2.864  1.00 26.05 ? 14  ILE   F CB  1 
ATOM   6471  C  CG1 . ILE   F  1 14  ? -18.376 -63.203  -2.024  1.00 26.97 ? 14  ILE   F CG1 1 
ATOM   6472  C  CG2 . ILE   F  1 14  ? -17.616 -63.881  -4.327  1.00 32.16 ? 14  ILE   F CG2 1 
ATOM   6473  C  CD1 . ILE   F  1 14  ? -19.685 -63.885  -2.014  1.00 31.95 ? 14  ILE   F CD1 1 
ATOM   6474  N  N   . LEU   F  1 15  ? -14.671 -65.768  -2.752  1.00 27.05 ? 15  LEU   F N   1 
ATOM   6475  C  CA  . LEU   F  1 15  ? -13.493 -66.387  -3.353  1.00 27.88 ? 15  LEU   F CA  1 
ATOM   6476  C  C   . LEU   F  1 15  ? -13.562 -67.909  -3.261  1.00 30.18 ? 15  LEU   F C   1 
ATOM   6477  O  O   . LEU   F  1 15  ? -13.248 -68.618  -4.231  1.00 27.64 ? 15  LEU   F O   1 
ATOM   6478  C  CB  . LEU   F  1 15  ? -12.225 -65.869  -2.668  1.00 27.18 ? 15  LEU   F CB  1 
ATOM   6479  C  CG  . LEU   F  1 15  ? -10.907 -66.463  -3.142  1.00 28.42 ? 15  LEU   F CG  1 
ATOM   6480  C  CD1 . LEU   F  1 15  ? -10.705 -66.208  -4.634  1.00 27.96 ? 15  LEU   F CD1 1 
ATOM   6481  C  CD2 . LEU   F  1 15  ? -9.767  -65.864  -2.353  1.00 26.44 ? 15  LEU   F CD2 1 
ATOM   6482  N  N   . GLY   F  1 16  ? -13.996 -68.428  -2.110  1.00 33.20 ? 16  GLY   F N   1 
ATOM   6483  C  CA  . GLY   F  1 16  ? -14.141 -69.875  -1.959  1.00 27.68 ? 16  GLY   F CA  1 
ATOM   6484  C  C   . GLY   F  1 16  ? -15.099 -70.486  -2.970  1.00 27.43 ? 16  GLY   F C   1 
ATOM   6485  O  O   . GLY   F  1 16  ? -14.851 -71.585  -3.479  1.00 30.30 ? 16  GLY   F O   1 
ATOM   6486  N  N   . ASN   F  1 17  ? -16.212 -69.795  -3.261  1.00 26.73 ? 17  ASN   F N   1 
ATOM   6487  C  CA  . ASN   F  1 17  ? -17.151 -70.300  -4.254  1.00 30.92 ? 17  ASN   F CA  1 
ATOM   6488  C  C   . ASN   F  1 17  ? -16.519 -70.284  -5.639  1.00 33.11 ? 17  ASN   F C   1 
ATOM   6489  O  O   . ASN   F  1 17  ? -16.750 -71.200  -6.440  1.00 30.60 ? 17  ASN   F O   1 
ATOM   6490  C  CB  . ASN   F  1 17  ? -18.440 -69.473  -4.267  1.00 32.98 ? 17  ASN   F CB  1 
ATOM   6491  C  CG  . ASN   F  1 17  ? -19.250 -69.616  -2.991  1.00 37.74 ? 17  ASN   F CG  1 
ATOM   6492  O  OD1 . ASN   F  1 17  ? -19.092 -70.580  -2.259  1.00 36.41 ? 17  ASN   F OD1 1 
ATOM   6493  N  ND2 . ASN   F  1 17  ? -20.139 -68.660  -2.737  1.00 35.43 ? 17  ASN   F ND2 1 
ATOM   6494  N  N   . GLU   F  1 18  ? -15.716 -69.259  -5.902  1.00 28.08 ? 18  GLU   F N   1 
ATOM   6495  C  CA  . GLU   F  1 18  ? -15.063 -69.123  -7.223  1.00 32.86 ? 18  GLU   F CA  1 
ATOM   6496  C  C   . GLU   F  1 18  ? -14.057 -70.261  -7.415  1.00 27.14 ? 18  GLU   F C   1 
ATOM   6497  O  O   . GLU   F  1 18  ? -13.972 -70.777  -8.527  1.00 30.38 ? 18  GLU   F O   1 
ATOM   6498  C  CB  . GLU   F  1 18  ? -14.375 -67.767  -7.330  1.00 32.12 ? 18  GLU   F CB  1 
ATOM   6499  C  CG  . GLU   F  1 18  ? -15.318 -66.588  -7.126  1.00 38.72 ? 18  GLU   F CG  1 
ATOM   6500  C  CD  . GLU   F  1 18  ? -15.938 -66.130  -8.424  1.00 44.55 ? 18  GLU   F CD  1 
ATOM   6501  O  OE1 . GLU   F  1 18  ? -15.433 -66.588  -9.460  1.00 46.07 ? 18  GLU   F OE1 1 
ATOM   6502  O  OE2 . GLU   F  1 18  ? -16.891 -65.332  -8.413  1.00 42.94 ? 18  GLU   F OE2 1 
ATOM   6503  N  N   . LEU   F  1 19  ? -13.344 -70.628  -6.353  1.00 28.55 ? 19  LEU   F N   1 
ATOM   6504  C  CA  . LEU   F  1 19  ? -12.345 -71.686  -6.467  1.00 31.22 ? 19  LEU   F CA  1 
ATOM   6505  C  C   . LEU   F  1 19  ? -13.012 -73.027  -6.758  1.00 38.67 ? 19  LEU   F C   1 
ATOM   6506  O  O   . LEU   F  1 19  ? -12.512 -73.805  -7.579  1.00 29.57 ? 19  LEU   F O   1 
ATOM   6507  C  CB  . LEU   F  1 19  ? -11.496 -71.767  -5.193  1.00 29.66 ? 19  LEU   F CB  1 
ATOM   6508  C  CG  . LEU   F  1 19  ? -10.586 -70.552  -4.935  1.00 43.25 ? 19  LEU   F CG  1 
ATOM   6509  C  CD1 . LEU   F  1 19  ? -9.956  -70.618  -3.549  1.00 39.51 ? 19  LEU   F CD1 1 
ATOM   6510  C  CD2 . LEU   F  1 19  ? -9.477  -70.432  -5.990  1.00 38.57 ? 19  LEU   F CD2 1 
ATOM   6511  N  N   . ILE   F  1 20  ? -14.162 -73.295  -6.126  1.00 31.64 ? 20  ILE   F N   1 
ATOM   6512  C  CA  . ILE   F  1 20  ? -14.952 -74.471  -6.490  1.00 31.84 ? 20  ILE   F CA  1 
ATOM   6513  C  C   . ILE   F  1 20  ? -15.373 -74.374  -7.949  1.00 30.29 ? 20  ILE   F C   1 
ATOM   6514  O  O   . ILE   F  1 20  ? -15.200 -75.312  -8.733  1.00 30.49 ? 20  ILE   F O   1 
ATOM   6515  C  CB  . ILE   F  1 20  ? -16.177 -74.605  -5.562  1.00 34.09 ? 20  ILE   F CB  1 
ATOM   6516  C  CG1 . ILE   F  1 20  ? -15.742 -74.924  -4.125  1.00 33.14 ? 20  ILE   F CG1 1 
ATOM   6517  C  CG2 . ILE   F  1 20  ? -17.188 -75.678  -6.083  1.00 30.50 ? 20  ILE   F CG2 1 
ATOM   6518  C  CD1 . ILE   F  1 20  ? -16.944 -74.967  -3.115  1.00 37.17 ? 20  ILE   F CD1 1 
ATOM   6519  N  N   . ALA   F  1 21  ? -15.908 -73.217  -8.337  1.00 30.40 ? 21  ALA   F N   1 
ATOM   6520  C  CA  . ALA   F  1 21  ? -16.435 -73.063  -9.688  1.00 30.16 ? 21  ALA   F CA  1 
ATOM   6521  C  C   . ALA   F  1 21  ? -15.335 -73.207  -10.736 1.00 31.87 ? 21  ALA   F C   1 
ATOM   6522  O  O   . ALA   F  1 21  ? -15.539 -73.852  -11.769 1.00 28.54 ? 21  ALA   F O   1 
ATOM   6523  C  CB  . ALA   F  1 21  ? -17.154 -71.715  -9.804  1.00 29.67 ? 21  ALA   F CB  1 
ATOM   6524  N  N   . ILE   F  1 22  ? -14.147 -72.651  -10.478 1.00 30.27 ? 22  ILE   F N   1 
ATOM   6525  C  CA  . ILE   F  1 22  ? -13.058 -72.779  -11.440 1.00 28.02 ? 22  ILE   F CA  1 
ATOM   6526  C  C   . ILE   F  1 22  ? -12.832 -74.252  -11.765 1.00 32.58 ? 22  ILE   F C   1 
ATOM   6527  O  O   . ILE   F  1 22  ? -12.861 -74.662  -12.931 1.00 31.17 ? 22  ILE   F O   1 
ATOM   6528  C  CB  . ILE   F  1 22  ? -11.775 -72.120  -10.901 1.00 27.06 ? 22  ILE   F CB  1 
ATOM   6529  C  CG1 . ILE   F  1 22  ? -11.841 -70.588  -10.930 1.00 27.65 ? 22  ILE   F CG1 1 
ATOM   6530  C  CG2 . ILE   F  1 22  ? -10.572 -72.589  -11.703 1.00 25.84 ? 22  ILE   F CG2 1 
ATOM   6531  C  CD1 . ILE   F  1 22  ? -10.863 -69.944  -9.989  1.00 25.68 ? 22  ILE   F CD1 1 
ATOM   6532  N  N   . ASN   F  1 23  ? -12.622 -75.073  -10.721 1.00 30.47 ? 23  ASN   F N   1 
ATOM   6533  C  CA  . ASN   F  1 23  ? -12.285 -76.481  -10.918 1.00 33.97 ? 23  ASN   F CA  1 
ATOM   6534  C  C   . ASN   F  1 23  ? -13.464 -77.271  -11.473 1.00 30.21 ? 23  ASN   F C   1 
ATOM   6535  O  O   . ASN   F  1 23  ? -13.276 -78.171  -12.300 1.00 29.19 ? 23  ASN   F O   1 
ATOM   6536  C  CB  . ASN   F  1 23  ? -11.819 -77.101  -9.599  1.00 30.39 ? 23  ASN   F CB  1 
ATOM   6537  C  CG  . ASN   F  1 23  ? -10.455 -76.605  -9.169  1.00 35.28 ? 23  ASN   F CG  1 
ATOM   6538  O  OD1 . ASN   F  1 23  ? -9.952  -75.614  -9.699  1.00 34.85 ? 23  ASN   F OD1 1 
ATOM   6539  N  ND2 . ASN   F  1 23  ? -9.850  -77.283  -8.193  1.00 33.88 ? 23  ASN   F ND2 1 
ATOM   6540  N  N   . GLN   F  1 24  ? -14.669 -77.005  -10.972 1.00 33.37 ? 24  GLN   F N   1 
ATOM   6541  C  CA  . GLN   F  1 24  ? -15.845 -77.731  -11.446 1.00 32.20 ? 24  GLN   F CA  1 
ATOM   6542  C  C   . GLN   F  1 24  ? -16.109 -77.449  -12.915 1.00 32.39 ? 24  GLN   F C   1 
ATOM   6543  O  O   . GLN   F  1 24  ? -16.388 -78.370  -13.696 1.00 29.44 ? 24  GLN   F O   1 
ATOM   6544  C  CB  . GLN   F  1 24  ? -17.063 -77.359  -10.605 1.00 27.03 ? 24  GLN   F CB  1 
ATOM   6545  C  CG  . GLN   F  1 24  ? -18.411 -77.881  -11.153 1.00 28.36 ? 24  GLN   F CG  1 
ATOM   6546  C  CD  . GLN   F  1 24  ? -19.538 -77.722  -10.163 1.00 35.18 ? 24  GLN   F CD  1 
ATOM   6547  O  OE1 . GLN   F  1 24  ? -19.351 -77.881  -8.952  1.00 33.23 ? 24  GLN   F OE1 1 
ATOM   6548  N  NE2 . GLN   F  1 24  ? -20.698 -77.345  -10.661 1.00 33.47 ? 24  GLN   F NE2 1 
ATOM   6549  N  N   . TYR   F  1 25  ? -16.023 -76.180  -13.320 1.00 32.16 ? 25  TYR   F N   1 
ATOM   6550  C  CA  . TYR   F  1 25  ? -16.272 -75.876  -14.716 1.00 28.08 ? 25  TYR   F CA  1 
ATOM   6551  C  C   . TYR   F  1 25  ? -15.126 -76.379  -15.595 1.00 29.80 ? 25  TYR   F C   1 
ATOM   6552  O  O   . TYR   F  1 25  ? -15.361 -76.842  -16.719 1.00 31.46 ? 25  TYR   F O   1 
ATOM   6553  C  CB  . TYR   F  1 25  ? -16.509 -74.374  -14.930 1.00 29.26 ? 25  TYR   F CB  1 
ATOM   6554  C  CG  . TYR   F  1 25  ? -17.659 -73.779  -14.126 1.00 34.94 ? 25  TYR   F CG  1 
ATOM   6555  C  CD1 . TYR   F  1 25  ? -18.633 -74.591  -13.543 1.00 37.98 ? 25  TYR   F CD1 1 
ATOM   6556  C  CD2 . TYR   F  1 25  ? -17.769 -72.396  -13.945 1.00 25.84 ? 25  TYR   F CD2 1 
ATOM   6557  C  CE1 . TYR   F  1 25  ? -19.664 -74.037  -12.784 1.00 32.67 ? 25  TYR   F CE1 1 
ATOM   6558  C  CE2 . TYR   F  1 25  ? -18.798 -71.840  -13.199 1.00 36.19 ? 25  TYR   F CE2 1 
ATOM   6559  C  CZ  . TYR   F  1 25  ? -19.733 -72.664  -12.618 1.00 35.41 ? 25  TYR   F CZ  1 
ATOM   6560  O  OH  . TYR   F  1 25  ? -20.740 -72.120  -11.867 1.00 37.03 ? 25  TYR   F OH  1 
ATOM   6561  N  N   . PHE   F  1 26  ? -13.886 -76.316  -15.106 1.00 27.99 ? 26  PHE   F N   1 
ATOM   6562  C  CA  . PHE   F  1 26  ? -12.784 -76.821  -15.912 1.00 28.74 ? 26  PHE   F CA  1 
ATOM   6563  C  C   . PHE   F  1 26  ? -12.913 -78.325  -16.126 1.00 34.79 ? 26  PHE   F C   1 
ATOM   6564  O  O   . PHE   F  1 26  ? -12.770 -78.828  -17.255 1.00 28.57 ? 26  PHE   F O   1 
ATOM   6565  C  CB  . PHE   F  1 26  ? -11.444 -76.471  -15.269 1.00 26.50 ? 26  PHE   F CB  1 
ATOM   6566  C  CG  . PHE   F  1 26  ? -10.329 -76.405  -16.261 1.00 27.46 ? 26  PHE   F CG  1 
ATOM   6567  C  CD1 . PHE   F  1 26  ? -9.661  -77.546  -16.648 1.00 31.78 ? 26  PHE   F CD1 1 
ATOM   6568  C  CD2 . PHE   F  1 26  ? -10.016 -75.212  -16.874 1.00 32.85 ? 26  PHE   F CD2 1 
ATOM   6569  C  CE1 . PHE   F  1 26  ? -8.662  -77.497  -17.618 1.00 33.24 ? 26  PHE   F CE1 1 
ATOM   6570  C  CE2 . PHE   F  1 26  ? -9.012  -75.144  -17.847 1.00 33.50 ? 26  PHE   F CE2 1 
ATOM   6571  C  CZ  . PHE   F  1 26  ? -8.344  -76.295  -18.224 1.00 35.52 ? 26  PHE   F CZ  1 
ATOM   6572  N  N   . LEU   F  1 27  ? -13.225 -79.061  -15.062 1.00 28.10 ? 27  LEU   F N   1 
ATOM   6573  C  CA  . LEU   F  1 27  ? -13.386 -80.503  -15.217 1.00 34.98 ? 27  LEU   F CA  1 
ATOM   6574  C  C   . LEU   F  1 27  ? -14.548 -80.821  -16.147 1.00 27.24 ? 27  LEU   F C   1 
ATOM   6575  O  O   . LEU   F  1 27  ? -14.430 -81.688  -17.020 1.00 32.41 ? 27  LEU   F O   1 
ATOM   6576  C  CB  . LEU   F  1 27  ? -13.586 -81.169  -13.857 1.00 33.01 ? 27  LEU   F CB  1 
ATOM   6577  C  CG  . LEU   F  1 27  ? -13.838 -82.672  -13.904 1.00 28.34 ? 27  LEU   F CG  1 
ATOM   6578  C  CD1 . LEU   F  1 27  ? -12.779 -83.378  -14.733 1.00 34.34 ? 27  LEU   F CD1 1 
ATOM   6579  C  CD2 . LEU   F  1 27  ? -13.869 -83.250  -12.489 1.00 38.70 ? 27  LEU   F CD2 1 
ATOM   6580  N  N   . HIS   F  1 28  ? -15.679 -80.132  -15.986 1.00 31.79 ? 28  HIS   F N   1 
ATOM   6581  C  CA  . HIS   F  1 28  ? -16.796 -80.363  -16.894 1.00 31.52 ? 28  HIS   F CA  1 
ATOM   6582  C  C   . HIS   F  1 28  ? -16.409 -80.069  -18.345 1.00 34.70 ? 28  HIS   F C   1 
ATOM   6583  O  O   . HIS   F  1 28  ? -16.766 -80.825  -19.260 1.00 29.13 ? 28  HIS   F O   1 
ATOM   6584  C  CB  . HIS   F  1 28  ? -17.988 -79.516  -16.488 1.00 30.07 ? 28  HIS   F CB  1 
ATOM   6585  C  CG  . HIS   F  1 28  ? -18.793 -80.095  -15.354 1.00 36.87 ? 28  HIS   F CG  1 
ATOM   6586  N  ND1 . HIS   F  1 28  ? -19.726 -79.359  -14.656 1.00 29.27 ? 28  HIS   F ND1 1 
ATOM   6587  C  CD2 . HIS   F  1 28  ? -18.791 -81.327  -14.788 1.00 35.49 ? 28  HIS   F CD2 1 
ATOM   6588  C  CE1 . HIS   F  1 28  ? -20.282 -80.118  -13.724 1.00 34.05 ? 28  HIS   F CE1 1 
ATOM   6589  N  NE2 . HIS   F  1 28  ? -19.725 -81.314  -13.776 1.00 36.93 ? 28  HIS   F NE2 1 
ATOM   6590  N  N   . SER   F  1 29  ? -15.677 -78.976  -18.572 1.00 28.16 ? 29  SER   F N   1 
ATOM   6591  C  CA  . SER   F  1 29  ? -15.225 -78.649  -19.919 1.00 29.53 ? 29  SER   F CA  1 
ATOM   6592  C  C   . SER   F  1 29  ? -14.425 -79.798  -20.516 1.00 31.85 ? 29  SER   F C   1 
ATOM   6593  O  O   . SER   F  1 29  ? -14.661 -80.220  -21.657 1.00 31.79 ? 29  SER   F O   1 
ATOM   6594  C  CB  . SER   F  1 29  ? -14.367 -77.374  -19.888 1.00 30.79 ? 29  SER   F CB  1 
ATOM   6595  O  OG  . SER   F  1 29  ? -13.711 -77.159  -21.129 1.00 30.28 ? 29  SER   F OG  1 
ATOM   6596  N  N   . ARG   F  1 30  ? -13.445 -80.292  -19.768 1.00 28.53 ? 30  ARG   F N   1 
ATOM   6597  C  CA  . ARG   F  1 30  ? -12.570 -81.325  -20.298 1.00 29.24 ? 30  ARG   F CA  1 
ATOM   6598  C  C   . ARG   F  1 30  ? -13.302 -82.648  -20.464 1.00 35.67 ? 30  ARG   F C   1 
ATOM   6599  O  O   . ARG   F  1 30  ? -12.940 -83.438  -21.347 1.00 33.48 ? 30  ARG   F O   1 
ATOM   6600  C  CB  . ARG   F  1 30  ? -11.356 -81.469  -19.400 1.00 28.15 ? 30  ARG   F CB  1 
ATOM   6601  C  CG  . ARG   F  1 30  ? -10.223 -80.503  -19.771 1.00 35.35 ? 30  ARG   F CG  1 
ATOM   6602  C  CD  . ARG   F  1 30  ? -10.689 -79.071  -20.135 1.00 27.31 ? 30  ARG   F CD  1 
ATOM   6603  N  NE  . ARG   F  1 30  ? -9.626  -78.363  -20.855 1.00 29.82 ? 30  ARG   F NE  1 
ATOM   6604  C  CZ  . ARG   F  1 30  ? -9.790  -77.485  -21.838 1.00 29.33 ? 30  ARG   F CZ  1 
ATOM   6605  N  NH1 . ARG   F  1 30  ? -10.992 -77.098  -22.244 1.00 31.50 ? 30  ARG   F NH1 1 
ATOM   6606  N  NH2 . ARG   F  1 30  ? -8.713  -76.996  -22.446 1.00 30.23 ? 30  ARG   F NH2 1 
ATOM   6607  N  N   . MET   F  1 31  ? -14.325 -82.906  -19.634 1.00 30.75 ? 31  MET   F N   1 
ATOM   6608  C  CA  . MET   F  1 31  ? -15.178 -84.076  -19.862 1.00 35.31 ? 31  MET   F CA  1 
ATOM   6609  C  C   . MET   F  1 31  ? -15.963 -83.932  -21.156 1.00 36.51 ? 31  MET   F C   1 
ATOM   6610  O  O   . MET   F  1 31  ? -16.013 -84.859  -21.976 1.00 34.41 ? 31  MET   F O   1 
ATOM   6611  C  CB  . MET   F  1 31  ? -16.140 -84.277  -18.689 1.00 30.42 ? 31  MET   F CB  1 
ATOM   6612  C  CG  . MET   F  1 31  ? -15.441 -84.719  -17.340 1.00 30.77 ? 31  MET   F CG  1 
ATOM   6613  S  SD  . MET   F  1 31  ? -16.526 -84.439  -15.886 1.00 33.65 ? 31  MET   F SD  1 
ATOM   6614  C  CE  . MET   F  1 31  ? -17.933 -85.473  -16.261 1.00 38.47 ? 31  MET   F CE  1 
ATOM   6615  N  N   . TRP   F  1 32  ? -16.614 -82.786  -21.345 1.00 31.24 ? 32  TRP   F N   1 
ATOM   6616  C  CA  . TRP   F  1 32  ? -17.356 -82.569  -22.574 1.00 31.95 ? 32  TRP   F CA  1 
ATOM   6617  C  C   . TRP   F  1 32  ? -16.456 -82.677  -23.795 1.00 32.22 ? 32  TRP   F C   1 
ATOM   6618  O  O   . TRP   F  1 32  ? -16.856 -83.268  -24.795 1.00 31.05 ? 32  TRP   F O   1 
ATOM   6619  C  CB  . TRP   F  1 32  ? -18.070 -81.222  -22.530 1.00 32.86 ? 32  TRP   F CB  1 
ATOM   6620  C  CG  . TRP   F  1 32  ? -19.396 -81.305  -21.868 1.00 34.85 ? 32  TRP   F CG  1 
ATOM   6621  C  CD1 . TRP   F  1 32  ? -20.305 -82.302  -22.014 1.00 30.80 ? 32  TRP   F CD1 1 
ATOM   6622  C  CD2 . TRP   F  1 32  ? -19.976 -80.368  -20.930 1.00 32.92 ? 32  TRP   F CD2 1 
ATOM   6623  N  NE1 . TRP   F  1 32  ? -21.414 -82.053  -21.246 1.00 30.43 ? 32  TRP   F NE1 1 
ATOM   6624  C  CE2 . TRP   F  1 32  ? -21.243 -80.875  -20.573 1.00 29.72 ? 32  TRP   F CE2 1 
ATOM   6625  C  CE3 . TRP   F  1 32  ? -19.546 -79.161  -20.367 1.00 28.57 ? 32  TRP   F CE3 1 
ATOM   6626  C  CZ2 . TRP   F  1 32  ? -22.096 -80.216  -19.689 1.00 33.47 ? 32  TRP   F CZ2 1 
ATOM   6627  C  CZ3 . TRP   F  1 32  ? -20.391 -78.501  -19.496 1.00 31.45 ? 32  TRP   F CZ3 1 
ATOM   6628  C  CH2 . TRP   F  1 32  ? -21.653 -79.036  -19.155 1.00 35.04 ? 32  TRP   F CH2 1 
ATOM   6629  N  N   . ASN   F  1 33  ? -15.222 -82.146  -23.724 1.00 33.81 ? 33  ASN   F N   1 
ATOM   6630  C  CA  . ASN   F  1 33  ? -14.302 -82.288  -24.846 1.00 35.18 ? 33  ASN   F CA  1 
ATOM   6631  C  C   . ASN   F  1 33  ? -13.924 -83.747  -25.069 1.00 37.21 ? 33  ASN   F C   1 
ATOM   6632  O  O   . ASN   F  1 33  ? -13.847 -84.212  -26.212 1.00 34.70 ? 33  ASN   F O   1 
ATOM   6633  C  CB  . ASN   F  1 33  ? -13.037 -81.451  -24.623 1.00 37.98 ? 33  ASN   F CB  1 
ATOM   6634  C  CG  . ASN   F  1 33  ? -13.254 -79.966  -24.906 1.00 32.15 ? 33  ASN   F CG  1 
ATOM   6635  O  OD1 . ASN   F  1 33  ? -14.238 -79.579  -25.549 1.00 31.12 ? 33  ASN   F OD1 1 
ATOM   6636  N  ND2 . ASN   F  1 33  ? -12.329 -79.131  -24.429 1.00 39.01 ? 33  ASN   F ND2 1 
ATOM   6637  N  N   . ASP   F  1 34  ? -13.703 -84.491  -23.991 1.00 31.87 ? 34  ASP   F N   1 
ATOM   6638  C  CA  . ASP   F  1 34  ? -13.320 -85.886  -24.156 1.00 37.06 ? 34  ASP   F CA  1 
ATOM   6639  C  C   . ASP   F  1 34  ? -14.433 -86.691  -24.819 1.00 37.76 ? 34  ASP   F C   1 
ATOM   6640  O  O   . ASP   F  1 34  ? -14.151 -87.631  -25.562 1.00 38.52 ? 34  ASP   F O   1 
ATOM   6641  C  CB  . ASP   F  1 34  ? -12.954 -86.497  -22.804 1.00 34.24 ? 34  ASP   F CB  1 
ATOM   6642  C  CG  . ASP   F  1 34  ? -12.509 -87.963  -22.923 1.00 39.67 ? 34  ASP   F CG  1 
ATOM   6643  O  OD1 . ASP   F  1 34  ? -11.546 -88.255  -23.659 1.00 47.48 ? 34  ASP   F OD1 1 
ATOM   6644  O  OD2 . ASP   F  1 34  ? -13.124 -88.821  -22.272 1.00 47.62 ? 34  ASP   F OD2 1 
ATOM   6645  N  N   . TRP   F  1 35  ? -15.695 -86.343  -24.566 1.00 33.00 ? 35  TRP   F N   1 
ATOM   6646  C  CA  . TRP   F  1 35  ? -16.815 -87.061  -25.165 1.00 38.12 ? 35  TRP   F CA  1 
ATOM   6647  C  C   . TRP   F  1 35  ? -17.148 -86.553  -26.565 1.00 38.73 ? 35  TRP   F C   1 
ATOM   6648  O  O   . TRP   F  1 35  ? -18.096 -87.042  -27.194 1.00 37.42 ? 35  TRP   F O   1 
ATOM   6649  C  CB  . TRP   F  1 35  ? -18.059 -86.948  -24.275 1.00 40.56 ? 35  TRP   F CB  1 
ATOM   6650  C  CG  . TRP   F  1 35  ? -17.904 -87.391  -22.798 1.00 41.73 ? 35  TRP   F CG  1 
ATOM   6651  C  CD1 . TRP   F  1 35  ? -16.950 -88.203  -22.267 1.00 43.89 ? 35  TRP   F CD1 1 
ATOM   6652  C  CD2 . TRP   F  1 35  ? -18.765 -87.026  -21.703 1.00 36.41 ? 35  TRP   F CD2 1 
ATOM   6653  N  NE1 . TRP   F  1 35  ? -17.163 -88.370  -20.912 1.00 46.16 ? 35  TRP   F NE1 1 
ATOM   6654  C  CE2 . TRP   F  1 35  ? -18.274 -87.659  -20.549 1.00 41.71 ? 35  TRP   F CE2 1 
ATOM   6655  C  CE3 . TRP   F  1 35  ? -19.905 -86.232  -21.598 1.00 37.08 ? 35  TRP   F CE3 1 
ATOM   6656  C  CZ2 . TRP   F  1 35  ? -18.874 -87.504  -19.304 1.00 42.60 ? 35  TRP   F CZ2 1 
ATOM   6657  C  CZ3 . TRP   F  1 35  ? -20.503 -86.085  -20.361 1.00 47.59 ? 35  TRP   F CZ3 1 
ATOM   6658  C  CH2 . TRP   F  1 35  ? -19.985 -86.716  -19.233 1.00 40.81 ? 35  TRP   F CH2 1 
ATOM   6659  N  N   . GLY   F  1 36  ? -16.406 -85.579  -27.067 1.00 31.49 ? 36  GLY   F N   1 
ATOM   6660  C  CA  . GLY   F  1 36  ? -16.646 -85.053  -28.396 1.00 39.26 ? 36  GLY   F CA  1 
ATOM   6661  C  C   . GLY   F  1 36  ? -17.677 -83.952  -28.461 1.00 36.69 ? 36  GLY   F C   1 
ATOM   6662  O  O   . GLY   F  1 36  ? -18.107 -83.586  -29.566 1.00 29.67 ? 36  GLY   F O   1 
ATOM   6663  N  N   . LEU   F  1 37  ? -18.115 -83.431  -27.321 1.00 32.81 ? 37  LEU   F N   1 
ATOM   6664  C  CA  . LEU   F  1 37  ? -19.095 -82.351  -27.310 1.00 29.88 ? 37  LEU   F CA  1 
ATOM   6665  C  C   . LEU   F  1 37  ? -18.362 -81.017  -27.147 1.00 35.75 ? 37  LEU   F C   1 
ATOM   6666  O  O   . LEU   F  1 37  ? -18.379 -80.373  -26.100 1.00 32.00 ? 37  LEU   F O   1 
ATOM   6667  C  CB  . LEU   F  1 37  ? -20.112 -82.598  -26.214 1.00 31.00 ? 37  LEU   F CB  1 
ATOM   6668  C  CG  . LEU   F  1 37  ? -20.825 -83.941  -26.359 1.00 35.85 ? 37  LEU   F CG  1 
ATOM   6669  C  CD1 . LEU   F  1 37  ? -21.542 -84.313  -25.093 1.00 36.84 ? 37  LEU   F CD1 1 
ATOM   6670  C  CD2 . LEU   F  1 37  ? -21.838 -83.839  -27.461 1.00 32.01 ? 37  LEU   F CD2 1 
ATOM   6671  N  N   . LYS   F  1 38  ? -17.691 -80.616  -28.232 1.00 35.83 ? 38  LYS   F N   1 
ATOM   6672  C  CA  . LYS   F  1 38  ? -16.684 -79.565  -28.141 1.00 34.74 ? 38  LYS   F CA  1 
ATOM   6673  C  C   . LYS   F  1 38  ? -17.295 -78.181  -28.004 1.00 28.46 ? 38  LYS   F C   1 
ATOM   6674  O  O   . LYS   F  1 38  ? -16.620 -77.265  -27.522 1.00 34.88 ? 38  LYS   F O   1 
ATOM   6675  C  CB  . LYS   F  1 38  ? -15.777 -79.580  -29.371 1.00 36.49 ? 38  LYS   F CB  1 
ATOM   6676  C  CG  . LYS   F  1 38  ? -15.243 -80.929  -29.755 1.00 44.16 ? 38  LYS   F CG  1 
ATOM   6677  C  CD  . LYS   F  1 38  ? -14.101 -81.330  -28.873 1.00 43.32 ? 38  LYS   F CD  1 
ATOM   6678  C  CE  . LYS   F  1 38  ? -13.459 -82.616  -29.367 1.00 48.91 ? 38  LYS   F CE  1 
ATOM   6679  N  NZ  . LYS   F  1 38  ? -11.978 -82.527  -29.440 1.00 47.79 ? 38  LYS   F NZ  1 
ATOM   6680  N  N   . ARG   F  1 39  ? -18.534 -77.994  -28.444 1.00 30.00 ? 39  ARG   F N   1 
ATOM   6681  C  CA  . ARG   F  1 39  ? -19.190 -76.710  -28.244 1.00 28.18 ? 39  ARG   F CA  1 
ATOM   6682  C  C   . ARG   F  1 39  ? -19.485 -76.485  -26.765 1.00 33.48 ? 39  ARG   F C   1 
ATOM   6683  O  O   . ARG   F  1 39  ? -19.242 -75.394  -26.235 1.00 33.83 ? 39  ARG   F O   1 
ATOM   6684  C  CB  . ARG   F  1 39  ? -20.473 -76.635  -29.061 1.00 33.18 ? 39  ARG   F CB  1 
ATOM   6685  C  CG  . ARG   F  1 39  ? -20.937 -75.219  -29.313 1.00 34.19 ? 39  ARG   F CG  1 
ATOM   6686  C  CD  . ARG   F  1 39  ? -22.208 -75.204  -30.136 1.00 42.13 ? 39  ARG   F CD  1 
ATOM   6687  N  NE  . ARG   F  1 39  ? -22.698 -73.854  -30.388 1.00 54.45 ? 39  ARG   F NE  1 
ATOM   6688  C  CZ  . ARG   F  1 39  ? -22.548 -73.199  -31.535 1.00 59.79 ? 39  ARG   F CZ  1 
ATOM   6689  N  NH1 . ARG   F  1 39  ? -21.890 -73.728  -32.556 1.00 60.78 ? 39  ARG   F NH1 1 
ATOM   6690  N  NH2 . ARG   F  1 39  ? -23.078 -71.984  -31.661 1.00 54.89 ? 39  ARG   F NH2 1 
ATOM   6691  N  N   . LEU   F  1 40  ? -20.020 -77.505  -26.082 1.00 35.59 ? 40  LEU   F N   1 
ATOM   6692  C  CA  . LEU   F  1 40  ? -20.135 -77.431  -24.626 1.00 34.37 ? 40  LEU   F CA  1 
ATOM   6693  C  C   . LEU   F  1 40  ? -18.771 -77.282  -23.981 1.00 29.87 ? 40  LEU   F C   1 
ATOM   6694  O  O   . LEU   F  1 40  ? -18.590 -76.465  -23.075 1.00 28.22 ? 40  LEU   F O   1 
ATOM   6695  C  CB  . LEU   F  1 40  ? -20.840 -78.671  -24.069 1.00 34.27 ? 40  LEU   F CB  1 
ATOM   6696  C  CG  . LEU   F  1 40  ? -22.359 -78.605  -24.142 1.00 36.57 ? 40  LEU   F CG  1 
ATOM   6697  C  CD1 . LEU   F  1 40  ? -22.989 -79.986  -23.965 1.00 41.88 ? 40  LEU   F CD1 1 
ATOM   6698  C  CD2 . LEU   F  1 40  ? -22.889 -77.646  -23.094 1.00 37.26 ? 40  LEU   F CD2 1 
ATOM   6699  N  N   . GLY   F  1 41  ? -17.789 -78.062  -24.434 1.00 32.41 ? 41  GLY   F N   1 
ATOM   6700  C  CA  . GLY   F  1 41  ? -16.486 -77.999  -23.798 1.00 32.47 ? 41  GLY   F CA  1 
ATOM   6701  C  C   . GLY   F  1 41  ? -15.874 -76.607  -23.865 1.00 36.77 ? 41  GLY   F C   1 
ATOM   6702  O  O   . GLY   F  1 41  ? -15.315 -76.112  -22.883 1.00 32.05 ? 41  GLY   F O   1 
ATOM   6703  N  N   . ALA   F  1 42  ? -15.969 -75.964  -25.029 1.00 29.93 ? 42  ALA   F N   1 
ATOM   6704  C  CA  . ALA   F  1 42  ? -15.442 -74.614  -25.207 1.00 27.19 ? 42  ALA   F CA  1 
ATOM   6705  C  C   . ALA   F  1 42  ? -16.181 -73.597  -24.358 1.00 28.37 ? 42  ALA   F C   1 
ATOM   6706  O  O   . ALA   F  1 42  ? -15.563 -72.707  -23.766 1.00 28.68 ? 42  ALA   F O   1 
ATOM   6707  C  CB  . ALA   F  1 42  ? -15.531 -74.199  -26.677 1.00 35.98 ? 42  ALA   F CB  1 
ATOM   6708  N  N   . HIS   F  1 43  ? -17.509 -73.653  -24.354 1.00 27.32 ? 43  HIS   F N   1 
ATOM   6709  C  CA  . HIS   F  1 43  ? -18.266 -72.673  -23.591 1.00 30.75 ? 43  HIS   F CA  1 
ATOM   6710  C  C   . HIS   F  1 43  ? -17.976 -72.824  -22.105 1.00 34.40 ? 43  HIS   F C   1 
ATOM   6711  O  O   . HIS   F  1 43  ? -17.797 -71.830  -21.381 1.00 28.76 ? 43  HIS   F O   1 
ATOM   6712  C  CB  . HIS   F  1 43  ? -19.769 -72.836  -23.877 1.00 29.89 ? 43  HIS   F CB  1 
ATOM   6713  C  CG  . HIS   F  1 43  ? -20.596 -71.705  -23.358 1.00 40.09 ? 43  HIS   F CG  1 
ATOM   6714  N  ND1 . HIS   F  1 43  ? -20.900 -71.553  -22.024 1.00 39.94 ? 43  HIS   F ND1 1 
ATOM   6715  C  CD2 . HIS   F  1 43  ? -21.142 -70.641  -23.990 1.00 42.96 ? 43  HIS   F CD2 1 
ATOM   6716  C  CE1 . HIS   F  1 43  ? -21.610 -70.450  -21.856 1.00 35.91 ? 43  HIS   F CE1 1 
ATOM   6717  N  NE2 . HIS   F  1 43  ? -21.767 -69.877  -23.032 1.00 40.26 ? 43  HIS   F NE2 1 
ATOM   6718  N  N   . GLU   F  1 44  ? -17.914 -74.069  -21.636 1.00 31.21 ? 44  GLU   F N   1 
ATOM   6719  C  CA  . GLU   F  1 44  ? -17.606 -74.313  -20.235 1.00 32.14 ? 44  GLU   F CA  1 
ATOM   6720  C  C   . GLU   F  1 44  ? -16.187 -73.869  -19.886 1.00 32.23 ? 44  GLU   F C   1 
ATOM   6721  O  O   . GLU   F  1 44  ? -15.936 -73.396  -18.769 1.00 29.12 ? 44  GLU   F O   1 
ATOM   6722  C  CB  . GLU   F  1 44  ? -17.793 -75.792  -19.913 1.00 33.66 ? 44  GLU   F CB  1 
ATOM   6723  C  CG  . GLU   F  1 44  ? -17.748 -76.107  -18.423 1.00 32.14 ? 44  GLU   F CG  1 
ATOM   6724  C  CD  . GLU   F  1 44  ? -19.024 -75.775  -17.683 1.00 36.51 ? 44  GLU   F CD  1 
ATOM   6725  O  OE1 . GLU   F  1 44  ? -19.852 -74.981  -18.186 1.00 36.44 ? 44  GLU   F OE1 1 
ATOM   6726  O  OE2 . GLU   F  1 44  ? -19.200 -76.345  -16.582 1.00 34.95 ? 44  GLU   F OE2 1 
ATOM   6727  N  N   . TYR   F  1 45  ? -15.233 -74.055  -20.805 1.00 33.09 ? 45  TYR   F N   1 
ATOM   6728  C  CA  . TYR   F  1 45  ? -13.886 -73.513  -20.598 1.00 28.49 ? 45  TYR   F CA  1 
ATOM   6729  C  C   . TYR   F  1 45  ? -13.943 -72.015  -20.346 1.00 26.47 ? 45  TYR   F C   1 
ATOM   6730  O  O   . TYR   F  1 45  ? -13.386 -71.513  -19.365 1.00 27.19 ? 45  TYR   F O   1 
ATOM   6731  C  CB  . TYR   F  1 45  ? -13.015 -73.805  -21.815 1.00 30.51 ? 45  TYR   F CB  1 
ATOM   6732  C  CG  . TYR   F  1 45  ? -11.671 -73.120  -21.833 1.00 25.69 ? 45  TYR   F CG  1 
ATOM   6733  C  CD1 . TYR   F  1 45  ? -10.598 -73.636  -21.125 1.00 29.15 ? 45  TYR   F CD1 1 
ATOM   6734  C  CD2 . TYR   F  1 45  ? -11.459 -71.977  -22.590 1.00 32.25 ? 45  TYR   F CD2 1 
ATOM   6735  C  CE1 . TYR   F  1 45  ? -9.362  -73.036  -21.156 1.00 36.44 ? 45  TYR   F CE1 1 
ATOM   6736  C  CE2 . TYR   F  1 45  ? -10.211 -71.362  -22.627 1.00 32.84 ? 45  TYR   F CE2 1 
ATOM   6737  C  CZ  . TYR   F  1 45  ? -9.171  -71.903  -21.910 1.00 38.11 ? 45  TYR   F CZ  1 
ATOM   6738  O  OH  . TYR   F  1 45  ? -7.921  -71.316  -21.933 1.00 35.73 ? 45  TYR   F OH  1 
ATOM   6739  N  N   . HIS   F  1 46  ? -14.682 -71.291  -21.186 1.00 32.26 ? 46  HIS   F N   1 
ATOM   6740  C  CA  . HIS   F  1 46  ? -14.763 -69.844  -21.020 1.00 29.79 ? 46  HIS   F CA  1 
ATOM   6741  C  C   . HIS   F  1 46  ? -15.450 -69.468  -19.722 1.00 29.42 ? 46  HIS   F C   1 
ATOM   6742  O  O   . HIS   F  1 46  ? -15.092 -68.455  -19.113 1.00 29.68 ? 46  HIS   F O   1 
ATOM   6743  C  CB  . HIS   F  1 46  ? -15.447 -69.224  -22.233 1.00 31.02 ? 46  HIS   F CB  1 
ATOM   6744  C  CG  . HIS   F  1 46  ? -14.576 -69.276  -23.448 1.00 46.18 ? 46  HIS   F CG  1 
ATOM   6745  N  ND1 . HIS   F  1 46  ? -14.845 -70.089  -24.529 1.00 43.77 ? 46  HIS   F ND1 1 
ATOM   6746  C  CD2 . HIS   F  1 46  ? -13.385 -68.688  -23.707 1.00 44.46 ? 46  HIS   F CD2 1 
ATOM   6747  C  CE1 . HIS   F  1 46  ? -13.878 -69.966  -25.420 1.00 44.54 ? 46  HIS   F CE1 1 
ATOM   6748  N  NE2 . HIS   F  1 46  ? -12.977 -69.123  -24.944 1.00 47.67 ? 46  HIS   F NE2 1 
ATOM   6749  N  N   . GLU   F  1 47  ? -16.384 -70.298  -19.253 1.00 26.38 ? 47  GLU   F N   1 
ATOM   6750  C  CA  . GLU   F  1 47  ? -16.994 -70.049  -17.954 1.00 29.77 ? 47  GLU   F CA  1 
ATOM   6751  C  C   . GLU   F  1 47  ? -15.956 -70.190  -16.837 1.00 29.63 ? 47  GLU   F C   1 
ATOM   6752  O  O   . GLU   F  1 47  ? -15.899 -69.363  -15.919 1.00 29.13 ? 47  GLU   F O   1 
ATOM   6753  C  CB  . GLU   F  1 47  ? -18.176 -71.006  -17.737 1.00 25.76 ? 47  GLU   F CB  1 
ATOM   6754  C  CG  . GLU   F  1 47  ? -19.373 -70.851  -18.689 1.00 35.84 ? 47  GLU   F CG  1 
ATOM   6755  C  CD  . GLU   F  1 47  ? -20.151 -69.593  -18.461 1.00 40.77 ? 47  GLU   F CD  1 
ATOM   6756  O  OE1 . GLU   F  1 47  ? -19.669 -68.757  -17.689 1.00 49.27 ? 47  GLU   F OE1 1 
ATOM   6757  O  OE2 . GLU   F  1 47  ? -21.260 -69.447  -19.017 1.00 49.46 ? 47  GLU   F OE2 1 
ATOM   6758  N  N   . SER   F  1 48  ? -15.095 -71.209  -16.928 1.00 26.37 ? 48  SER   F N   1 
ATOM   6759  C  CA  . SER   F  1 48  ? -14.027 -71.381  -15.944 1.00 22.41 ? 48  SER   F CA  1 
ATOM   6760  C  C   . SER   F  1 48  ? -13.070 -70.184  -15.929 1.00 27.51 ? 48  SER   F C   1 
ATOM   6761  O  O   . SER   F  1 48  ? -12.711 -69.679  -14.859 1.00 26.11 ? 48  SER   F O   1 
ATOM   6762  C  CB  . SER   F  1 48  ? -13.272 -72.692  -16.250 1.00 25.56 ? 48  SER   F CB  1 
ATOM   6763  O  OG  . SER   F  1 48  ? -12.357 -73.056  -15.227 1.00 29.81 ? 48  SER   F OG  1 
ATOM   6764  N  N   . ILE   F  1 49  ? -12.615 -69.742  -17.117 1.00 25.44 ? 49  ILE   F N   1 
ATOM   6765  C  CA  . ILE   F  1 49  ? -11.766 -68.561  -17.229 1.00 31.25 ? 49  ILE   F CA  1 
ATOM   6766  C  C   . ILE   F  1 49  ? -12.437 -67.344  -16.605 1.00 25.90 ? 49  ILE   F C   1 
ATOM   6767  O  O   . ILE   F  1 49  ? -11.789 -66.547  -15.917 1.00 28.36 ? 49  ILE   F O   1 
ATOM   6768  C  CB  . ILE   F  1 49  ? -11.403 -68.304  -18.708 1.00 31.41 ? 49  ILE   F CB  1 
ATOM   6769  C  CG1 . ILE   F  1 49  ? -10.673 -69.499  -19.297 1.00 30.51 ? 49  ILE   F CG1 1 
ATOM   6770  C  CG2 . ILE   F  1 49  ? -10.543 -67.073  -18.818 1.00 33.90 ? 49  ILE   F CG2 1 
ATOM   6771  C  CD1 . ILE   F  1 49  ? -9.284  -69.643  -18.790 1.00 33.46 ? 49  ILE   F CD1 1 
ATOM   6772  N  N   . ASP   F  1 50  ? -13.733 -67.164  -16.831 1.00 26.28 ? 50  ASP   F N   1 
ATOM   6773  C  CA  . ASP   F  1 50  ? -14.410 -66.039  -16.196 1.00 26.22 ? 50  ASP   F CA  1 
ATOM   6774  C  C   . ASP   F  1 50  ? -14.293 -66.077  -14.681 1.00 31.02 ? 50  ASP   F C   1 
ATOM   6775  O  O   . ASP   F  1 50  ? -14.051 -65.037  -14.043 1.00 29.50 ? 50  ASP   F O   1 
ATOM   6776  C  CB  . ASP   F  1 50  ? -15.883 -66.000  -16.577 1.00 28.75 ? 50  ASP   F CB  1 
ATOM   6777  C  CG  . ASP   F  1 50  ? -16.180 -64.849  -17.458 1.00 57.72 ? 50  ASP   F CG  1 
ATOM   6778  O  OD1 . ASP   F  1 50  ? -16.036 -65.033  -18.684 1.00 51.29 ? 50  ASP   F OD1 1 
ATOM   6779  O  OD2 . ASP   F  1 50  ? -16.494 -63.760  -16.913 1.00 57.62 ? 50  ASP   F OD2 1 
ATOM   6780  N  N   . GLU   F  1 51  ? -14.496 -67.254  -14.080 1.00 30.12 ? 51  GLU   F N   1 
ATOM   6781  C  CA  . GLU   F  1 51  ? -14.387 -67.354  -12.628 1.00 28.50 ? 51  GLU   F CA  1 
ATOM   6782  C  C   . GLU   F  1 51  ? -12.962 -67.136  -12.165 1.00 29.04 ? 51  GLU   F C   1 
ATOM   6783  O  O   . GLU   F  1 51  ? -12.739 -66.627  -11.061 1.00 29.17 ? 51  GLU   F O   1 
ATOM   6784  C  CB  . GLU   F  1 51  ? -14.898 -68.716  -12.142 1.00 28.28 ? 51  GLU   F CB  1 
ATOM   6785  C  CG  . GLU   F  1 51  ? -16.360 -69.012  -12.573 1.00 32.43 ? 51  GLU   F CG  1 
ATOM   6786  C  CD  . GLU   F  1 51  ? -17.351 -67.911  -12.146 1.00 34.33 ? 51  GLU   F CD  1 
ATOM   6787  O  OE1 . GLU   F  1 51  ? -17.385 -67.584  -10.959 1.00 45.29 ? 51  GLU   F OE1 1 
ATOM   6788  O  OE2 . GLU   F  1 51  ? -18.070 -67.352  -12.989 1.00 48.16 ? 51  GLU   F OE2 1 
ATOM   6789  N  N   . MET   F  1 52  ? -11.987 -67.535  -12.981 1.00 25.69 ? 52  MET   F N   1 
ATOM   6790  C  CA  . MET   F  1 52  ? -10.598 -67.212  -12.686 1.00 25.45 ? 52  MET   F CA  1 
ATOM   6791  C  C   . MET   F  1 52  ? -10.405 -65.705  -12.600 1.00 26.44 ? 52  MET   F C   1 
ATOM   6792  O  O   . MET   F  1 52  ? -9.750  -65.198  -11.681 1.00 23.82 ? 52  MET   F O   1 
ATOM   6793  C  CB  . MET   F  1 52  ? -9.688  -67.808  -13.762 1.00 30.76 ? 52  MET   F CB  1 
ATOM   6794  C  CG  . MET   F  1 52  ? -9.602  -69.327  -13.748 1.00 27.93 ? 52  MET   F CG  1 
ATOM   6795  S  SD  . MET   F  1 52  ? -8.662  -69.969  -15.168 1.00 28.11 ? 52  MET   F SD  1 
ATOM   6796  C  CE  . MET   F  1 52  ? -9.274  -71.646  -15.314 1.00 27.93 ? 52  MET   F CE  1 
ATOM   6797  N  N   . LYS   F  1 53  ? -10.971 -64.971  -13.547 1.00 22.95 ? 53  LYS   F N   1 
ATOM   6798  C  CA  . LYS   F  1 53  ? -10.803 -63.528  -13.528 1.00 27.88 ? 53  LYS   F CA  1 
ATOM   6799  C  C   . LYS   F  1 53  ? -11.487 -62.914  -12.311 1.00 25.48 ? 53  LYS   F C   1 
ATOM   6800  O  O   . LYS   F  1 53  ? -10.933 -62.007  -11.670 1.00 26.69 ? 53  LYS   F O   1 
ATOM   6801  C  CB  . LYS   F  1 53  ? -11.350 -62.948  -14.827 1.00 24.87 ? 53  LYS   F CB  1 
ATOM   6802  C  CG  . LYS   F  1 53  ? -10.534 -63.325  -16.060 1.00 30.48 ? 53  LYS   F CG  1 
ATOM   6803  C  CD  . LYS   F  1 53  ? -11.212 -62.741  -17.307 1.00 38.38 ? 53  LYS   F CD  1 
ATOM   6804  C  CE  . LYS   F  1 53  ? -10.270 -62.634  -18.480 1.00 49.80 ? 53  LYS   F CE  1 
ATOM   6805  N  NZ  . LYS   F  1 53  ? -11.017 -62.505  -19.795 1.00 67.87 ? 53  LYS   F NZ  1 
ATOM   6806  N  N   . HIS   F  1 54  ? -12.666 -63.428  -11.942 1.00 24.74 ? 54  HIS   F N   1 
ATOM   6807  C  CA  . HIS   F  1 54  ? -13.337 -62.925  -10.739 1.00 27.36 ? 54  HIS   F CA  1 
ATOM   6808  C  C   . HIS   F  1 54  ? -12.484 -63.177  -9.505  1.00 26.63 ? 54  HIS   F C   1 
ATOM   6809  O  O   . HIS   F  1 54  ? -12.365 -62.318  -8.618  1.00 26.07 ? 54  HIS   F O   1 
ATOM   6810  C  CB  . HIS   F  1 54  ? -14.703 -63.599  -10.543 1.00 27.05 ? 54  HIS   F CB  1 
ATOM   6811  C  CG  . HIS   F  1 54  ? -15.659 -63.423  -11.680 1.00 30.80 ? 54  HIS   F CG  1 
ATOM   6812  N  ND1 . HIS   F  1 54  ? -15.636 -62.332  -12.522 1.00 31.41 ? 54  HIS   F ND1 1 
ATOM   6813  C  CD2 . HIS   F  1 54  ? -16.700 -64.192  -12.090 1.00 30.47 ? 54  HIS   F CD2 1 
ATOM   6814  C  CE1 . HIS   F  1 54  ? -16.598 -62.455  -13.422 1.00 30.51 ? 54  HIS   F CE1 1 
ATOM   6815  N  NE2 . HIS   F  1 54  ? -17.253 -63.577  -13.185 1.00 29.72 ? 54  HIS   F NE2 1 
ATOM   6816  N  N   . ALA   F  1 55  ? -11.901 -64.371  -9.417  1.00 25.61 ? 55  ALA   F N   1 
ATOM   6817  C  CA  . ALA   F  1 55  ? -11.083 -64.699  -8.264  1.00 22.62 ? 55  ALA   F CA  1 
ATOM   6818  C  C   . ALA   F  1 55  ? -9.871  -63.780  -8.184  1.00 26.06 ? 55  ALA   F C   1 
ATOM   6819  O  O   . ALA   F  1 55  ? -9.518  -63.312  -7.098  1.00 25.42 ? 55  ALA   F O   1 
ATOM   6820  C  CB  . ALA   F  1 55  ? -10.663 -66.174  -8.325  1.00 30.72 ? 55  ALA   F CB  1 
ATOM   6821  N  N   . ASP   F  1 56  ? -9.213  -63.520  -9.329  1.00 28.11 ? 56  ASP   F N   1 
ATOM   6822  C  CA  . ASP   F  1 56  ? -8.114  -62.558  -9.363  1.00 26.09 ? 56  ASP   F CA  1 
ATOM   6823  C  C   . ASP   F  1 56  ? -8.550  -61.229  -8.753  1.00 22.84 ? 56  ASP   F C   1 
ATOM   6824  O  O   . ASP   F  1 56  ? -7.914  -60.722  -7.823  1.00 23.12 ? 56  ASP   F O   1 
ATOM   6825  C  CB  . ASP   F  1 56  ? -7.604  -62.382  -10.808 1.00 24.82 ? 56  ASP   F CB  1 
ATOM   6826  C  CG  . ASP   F  1 56  ? -6.354  -61.477  -10.907 1.00 26.10 ? 56  ASP   F CG  1 
ATOM   6827  O  OD1 . ASP   F  1 56  ? -5.620  -61.308  -9.919  1.00 28.95 ? 56  ASP   F OD1 1 
ATOM   6828  O  OD2 . ASP   F  1 56  ? -6.114  -60.927  -11.984 1.00 29.97 ? 56  ASP   F OD2 1 
ATOM   6829  N  N   . LYS   F  1 57  ? -9.698  -60.692  -9.199  1.00 27.71 ? 57  LYS   F N   1 
ATOM   6830  C  CA  . LYS   F  1 57  ? -10.145 -59.406  -8.660  1.00 24.12 ? 57  LYS   F CA  1 
ATOM   6831  C  C   . LYS   F  1 57  ? -10.436 -59.495  -7.167  1.00 25.73 ? 57  LYS   F C   1 
ATOM   6832  O  O   . LYS   F  1 57  ? -10.159 -58.552  -6.413  1.00 24.85 ? 57  LYS   F O   1 
ATOM   6833  C  CB  . LYS   F  1 57  ? -11.373 -58.894  -9.398  1.00 25.72 ? 57  LYS   F CB  1 
ATOM   6834  C  CG  . LYS   F  1 57  ? -11.167 -58.611  -10.891 1.00 26.51 ? 57  LYS   F CG  1 
ATOM   6835  C  CD  . LYS   F  1 57  ? -10.229 -57.447  -11.053 1.00 32.28 ? 57  LYS   F CD  1 
ATOM   6836  N  N   . LEU   F  1 58  ? -10.981 -60.614  -6.714  1.00 23.28 ? 58  LEU   F N   1 
ATOM   6837  C  CA  . LEU   F  1 58  ? -11.267 -60.726  -5.287  1.00 22.31 ? 58  LEU   F CA  1 
ATOM   6838  C  C   . LEU   F  1 58  ? -9.982  -60.782  -4.482  1.00 23.91 ? 58  LEU   F C   1 
ATOM   6839  O  O   . LEU   F  1 58  ? -9.886  -60.172  -3.416  1.00 25.82 ? 58  LEU   F O   1 
ATOM   6840  C  CB  . LEU   F  1 58  ? -12.105 -61.961  -4.994  1.00 26.94 ? 58  LEU   F CB  1 
ATOM   6841  C  CG  . LEU   F  1 58  ? -13.544 -61.921  -5.517  1.00 29.03 ? 58  LEU   F CG  1 
ATOM   6842  C  CD1 . LEU   F  1 58  ? -14.128 -63.321  -5.622  1.00 33.32 ? 58  LEU   F CD1 1 
ATOM   6843  C  CD2 . LEU   F  1 58  ? -14.421 -61.048  -4.612  1.00 31.65 ? 58  LEU   F CD2 1 
ATOM   6844  N  N   . ILE   F  1 59  ? -9.005  -61.554  -4.956  1.00 25.46 ? 59  ILE   F N   1 
ATOM   6845  C  CA  . ILE   F  1 59  ? -7.719  -61.634  -4.275  1.00 24.91 ? 59  ILE   F CA  1 
ATOM   6846  C  C   . ILE   F  1 59  ? -7.087  -60.249  -4.187  1.00 22.21 ? 59  ILE   F C   1 
ATOM   6847  O  O   . ILE   F  1 59  ? -6.606  -59.824  -3.129  1.00 25.31 ? 59  ILE   F O   1 
ATOM   6848  C  CB  . ILE   F  1 59  ? -6.813  -62.639  -5.001  1.00 28.63 ? 59  ILE   F CB  1 
ATOM   6849  C  CG1 . ILE   F  1 59  ? -7.376  -64.044  -4.848  1.00 26.89 ? 59  ILE   F CG1 1 
ATOM   6850  C  CG2 . ILE   F  1 59  ? -5.354  -62.566  -4.501  1.00 26.06 ? 59  ILE   F CG2 1 
ATOM   6851  C  CD1 . ILE   F  1 59  ? -6.839  -65.009  -5.854  1.00 29.92 ? 59  ILE   F CD1 1 
ATOM   6852  N  N   . GLU   F  1 60  ? -7.117  -59.515  -5.288  1.00 24.68 ? 60  GLU   F N   1 
ATOM   6853  C  CA  . GLU   F  1 60  ? -6.519  -58.181  -5.310  1.00 26.48 ? 60  GLU   F CA  1 
ATOM   6854  C  C   . GLU   F  1 60  ? -7.208  -57.259  -4.315  1.00 24.22 ? 60  GLU   F C   1 
ATOM   6855  O  O   . GLU   F  1 60  ? -6.548  -56.525  -3.577  1.00 25.25 ? 60  GLU   F O   1 
ATOM   6856  C  CB  . GLU   F  1 60  ? -6.599  -57.612  -6.729  1.00 22.68 ? 60  GLU   F CB  1 
ATOM   6857  C  CG  . GLU   F  1 60  ? -5.718  -58.393  -7.707  1.00 27.37 ? 60  GLU   F CG  1 
ATOM   6858  C  CD  . GLU   F  1 60  ? -5.828  -57.914  -9.156  1.00 37.71 ? 60  GLU   F CD  1 
ATOM   6859  O  OE1 . GLU   F  1 60  ? -6.946  -57.550  -9.557  1.00 32.36 ? 60  GLU   F OE1 1 
ATOM   6860  O  OE2 . GLU   F  1 60  ? -4.802  -57.900  -9.883  1.00 28.86 ? 60  GLU   F OE2 1 
ATOM   6861  N  N   . ARG   F  1 61  ? -8.540  -57.297  -4.272  1.00 23.46 ? 61  ARG   F N   1 
ATOM   6862  C  CA  . ARG   F  1 61  ? -9.282  -56.442  -3.342  1.00 24.48 ? 61  ARG   F CA  1 
ATOM   6863  C  C   . ARG   F  1 61  ? -8.981  -56.800  -1.891  1.00 25.55 ? 61  ARG   F C   1 
ATOM   6864  O  O   . ARG   F  1 61  ? -8.813  -55.907  -1.051  1.00 24.47 ? 61  ARG   F O   1 
ATOM   6865  C  CB  . ARG   F  1 61  ? -10.779 -56.560  -3.608  1.00 23.79 ? 61  ARG   F CB  1 
ATOM   6866  C  CG  . ARG   F  1 61  ? -11.637 -55.635  -2.783  1.00 21.82 ? 61  ARG   F CG  1 
ATOM   6867  C  CD  . ARG   F  1 61  ? -11.595 -54.247  -3.336  1.00 26.45 ? 61  ARG   F CD  1 
ATOM   6868  N  NE  . ARG   F  1 61  ? -12.333 -53.360  -2.442  1.00 27.21 ? 61  ARG   F NE  1 
ATOM   6869  C  CZ  . ARG   F  1 61  ? -12.099 -52.065  -2.326  1.00 27.70 ? 61  ARG   F CZ  1 
ATOM   6870  N  NH1 . ARG   F  1 61  ? -11.169 -51.452  -3.062  1.00 25.50 ? 61  ARG   F NH1 1 
ATOM   6871  N  NH2 . ARG   F  1 61  ? -12.796 -51.367  -1.443  1.00 23.12 ? 61  ARG   F NH2 1 
ATOM   6872  N  N   . ILE   F  1 62  ? -8.954  -58.096  -1.574  1.00 23.20 ? 62  ILE   F N   1 
ATOM   6873  C  CA  . ILE   F  1 62  ? -8.677  -58.518  -0.201  1.00 27.39 ? 62  ILE   F CA  1 
ATOM   6874  C  C   . ILE   F  1 62  ? -7.297  -58.040  0.228   1.00 27.87 ? 62  ILE   F C   1 
ATOM   6875  O  O   . ILE   F  1 62  ? -7.108  -57.560  1.358   1.00 25.78 ? 62  ILE   F O   1 
ATOM   6876  C  CB  . ILE   F  1 62  ? -8.815  -60.048  -0.062  1.00 25.21 ? 62  ILE   F CB  1 
ATOM   6877  C  CG1 . ILE   F  1 62  ? -10.271 -60.467  -0.180  1.00 26.65 ? 62  ILE   F CG1 1 
ATOM   6878  C  CG2 . ILE   F  1 62  ? -8.235  -60.533  1.300   1.00 25.02 ? 62  ILE   F CG2 1 
ATOM   6879  C  CD1 . ILE   F  1 62  ? -10.445 -61.970  -0.570  1.00 27.98 ? 62  ILE   F CD1 1 
ATOM   6880  N  N   . LEU   F  1 63  ? -6.311  -58.143  -0.663  1.00 22.78 ? 63  LEU   F N   1 
ATOM   6881  C  CA  . LEU   F  1 63  ? -4.964  -57.698  -0.292  1.00 24.51 ? 63  LEU   F CA  1 
ATOM   6882  C  C   . LEU   F  1 63  ? -4.915  -56.195  -0.102  1.00 25.87 ? 63  LEU   F C   1 
ATOM   6883  O  O   . LEU   F  1 63  ? -4.299  -55.707  0.859   1.00 24.79 ? 63  LEU   F O   1 
ATOM   6884  C  CB  . LEU   F  1 63  ? -3.936  -58.130  -1.342  1.00 29.68 ? 63  LEU   F CB  1 
ATOM   6885  C  CG  . LEU   F  1 63  ? -3.643  -59.628  -1.364  1.00 22.91 ? 63  LEU   F CG  1 
ATOM   6886  C  CD1 . LEU   F  1 63  ? -2.908  -59.995  -2.660  1.00 24.53 ? 63  LEU   F CD1 1 
ATOM   6887  C  CD2 . LEU   F  1 63  ? -2.804  -60.010  -0.145  1.00 24.27 ? 63  LEU   F CD2 1 
ATOM   6888  N  N   . PHE   F  1 64  ? -5.616  -55.446  -0.961  1.00 25.76 ? 64  PHE   F N   1 
ATOM   6889  C  CA  . PHE   F  1 64  ? -5.704  -54.003  -0.782  1.00 24.83 ? 64  PHE   F CA  1 
ATOM   6890  C  C   . PHE   F  1 64  ? -6.271  -53.655  0.590   1.00 28.61 ? 64  PHE   F C   1 
ATOM   6891  O  O   . PHE   F  1 64  ? -5.815  -52.703  1.240   1.00 28.64 ? 64  PHE   F O   1 
ATOM   6892  C  CB  . PHE   F  1 64  ? -6.578  -53.363  -1.882  1.00 25.55 ? 64  PHE   F CB  1 
ATOM   6893  C  CG  . PHE   F  1 64  ? -6.810  -51.895  -1.653  1.00 27.08 ? 64  PHE   F CG  1 
ATOM   6894  C  CD1 . PHE   F  1 64  ? -5.728  -51.028  -1.500  1.00 30.06 ? 64  PHE   F CD1 1 
ATOM   6895  C  CD2 . PHE   F  1 64  ? -8.078  -51.387  -1.527  1.00 30.20 ? 64  PHE   F CD2 1 
ATOM   6896  C  CE1 . PHE   F  1 64  ? -5.931  -49.677  -1.252  1.00 29.80 ? 64  PHE   F CE1 1 
ATOM   6897  C  CE2 . PHE   F  1 64  ? -8.285  -50.039  -1.269  1.00 30.89 ? 64  PHE   F CE2 1 
ATOM   6898  C  CZ  . PHE   F  1 64  ? -7.221  -49.184  -1.138  1.00 31.77 ? 64  PHE   F CZ  1 
ATOM   6899  N  N   . LEU   F  1 65  ? -7.291  -54.400  1.028   1.00 24.13 ? 65  LEU   F N   1 
ATOM   6900  C  CA  . LEU   F  1 65  ? -7.954  -54.165  2.308   1.00 28.45 ? 65  LEU   F CA  1 
ATOM   6901  C  C   . LEU   F  1 65  ? -7.199  -54.780  3.472   1.00 28.06 ? 65  LEU   F C   1 
ATOM   6902  O  O   . LEU   F  1 65  ? -7.709  -54.788  4.612   1.00 27.87 ? 65  LEU   F O   1 
ATOM   6903  C  CB  . LEU   F  1 65  ? -9.389  -54.719  2.258   1.00 21.10 ? 65  LEU   F CB  1 
ATOM   6904  C  CG  . LEU   F  1 65  ? -10.329 -54.087  1.223   1.00 26.51 ? 65  LEU   F CG  1 
ATOM   6905  C  CD1 . LEU   F  1 65  ? -11.626 -54.827  1.151   1.00 30.20 ? 65  LEU   F CD1 1 
ATOM   6906  C  CD2 . LEU   F  1 65  ? -10.587 -52.622  1.556   1.00 30.92 ? 65  LEU   F CD2 1 
ATOM   6907  N  N   . GLU   F  1 66  ? -6.034  -55.361  3.188   1.00 26.77 ? 66  GLU   F N   1 
ATOM   6908  C  CA  . GLU   F  1 66  ? -5.083  -55.797  4.189   1.00 26.87 ? 66  GLU   F CA  1 
ATOM   6909  C  C   . GLU   F  1 66  ? -5.548  -57.072  4.861   1.00 32.82 ? 66  GLU   F C   1 
ATOM   6910  O  O   . GLU   F  1 66  ? -5.245  -57.322  6.018   1.00 31.75 ? 66  GLU   F O   1 
ATOM   6911  C  CB  . GLU   F  1 66  ? -4.796  -54.677  5.203   1.00 25.40 ? 66  GLU   F CB  1 
ATOM   6912  C  CG  . GLU   F  1 66  ? -4.213  -53.489  4.463   1.00 27.56 ? 66  GLU   F CG  1 
ATOM   6913  C  CD  . GLU   F  1 66  ? -3.698  -52.357  5.338   1.00 36.89 ? 66  GLU   F CD  1 
ATOM   6914  O  OE1 . GLU   F  1 66  ? -3.414  -52.560  6.521   1.00 35.24 ? 66  GLU   F OE1 1 
ATOM   6915  O  OE2 . GLU   F  1 66  ? -3.578  -51.242  4.823   1.00 31.65 ? 66  GLU   F OE2 1 
ATOM   6916  N  N   . GLY   F  1 67  ? -6.257  -57.911  4.122   1.00 28.26 ? 67  GLY   F N   1 
ATOM   6917  C  CA  . GLY   F  1 67  ? -6.630  -59.224  4.588   1.00 26.68 ? 67  GLY   F CA  1 
ATOM   6918  C  C   . GLY   F  1 67  ? -5.793  -60.286  3.894   1.00 31.24 ? 67  GLY   F C   1 
ATOM   6919  O  O   . GLY   F  1 67  ? -4.991  -60.004  3.015   1.00 27.42 ? 67  GLY   F O   1 
ATOM   6920  N  N   . LEU   F  1 68  ? -6.056  -61.532  4.276   1.00 30.21 ? 68  LEU   F N   1 
ATOM   6921  C  CA  . LEU   F  1 68  ? -5.364  -62.693  3.738   1.00 31.01 ? 68  LEU   F CA  1 
ATOM   6922  C  C   . LEU   F  1 68  ? -6.323  -63.460  2.851   1.00 33.38 ? 68  LEU   F C   1 
ATOM   6923  O  O   . LEU   F  1 68  ? -7.287  -64.032  3.370   1.00 28.37 ? 68  LEU   F O   1 
ATOM   6924  C  CB  . LEU   F  1 68  ? -4.879  -63.589  4.876   1.00 33.19 ? 68  LEU   F CB  1 
ATOM   6925  C  CG  . LEU   F  1 68  ? -3.751  -63.004  5.733   1.00 45.81 ? 68  LEU   F CG  1 
ATOM   6926  C  CD1 . LEU   F  1 68  ? -3.318  -64.028  6.776   1.00 54.38 ? 68  LEU   F CD1 1 
ATOM   6927  C  CD2 . LEU   F  1 68  ? -2.573  -62.556  4.879   1.00 53.00 ? 68  LEU   F CD2 1 
ATOM   6928  N  N   . PRO   F  1 69  ? -6.125  -63.514  1.532   1.00 28.65 ? 69  PRO   F N   1 
ATOM   6929  C  CA  . PRO   F  1 69  ? -7.049  -64.276  0.693   1.00 29.76 ? 69  PRO   F CA  1 
ATOM   6930  C  C   . PRO   F  1 69  ? -6.855  -65.751  0.955   1.00 34.68 ? 69  PRO   F C   1 
ATOM   6931  O  O   . PRO   F  1 69  ? -5.723  -66.214  1.117   1.00 31.57 ? 69  PRO   F O   1 
ATOM   6932  C  CB  . PRO   F  1 69  ? -6.647  -63.899  -0.740  1.00 34.03 ? 69  PRO   F CB  1 
ATOM   6933  C  CG  . PRO   F  1 69  ? -5.615  -62.812  -0.594  1.00 24.19 ? 69  PRO   F CG  1 
ATOM   6934  C  CD  . PRO   F  1 69  ? -5.012  -62.964  0.753   1.00 27.94 ? 69  PRO   F CD  1 
ATOM   6935  N  N   . ASN   F  1 70  ? -7.966  -66.484  1.012   1.00 31.67 ? 70  ASN   F N   1 
ATOM   6936  C  CA  . ASN   F  1 70  ? -7.949  -67.903  1.357   1.00 32.59 ? 70  ASN   F CA  1 
ATOM   6937  C  C   . ASN   F  1 70  ? -7.956  -68.710  0.067   1.00 25.86 ? 70  ASN   F C   1 
ATOM   6938  O  O   . ASN   F  1 70  ? -8.988  -68.847  -0.584  1.00 29.33 ? 70  ASN   F O   1 
ATOM   6939  C  CB  . ASN   F  1 70  ? -9.137  -68.244  2.252   1.00 34.82 ? 70  ASN   F CB  1 
ATOM   6940  C  CG  . ASN   F  1 70  ? -9.137  -69.697  2.717   1.00 35.31 ? 70  ASN   F CG  1 
ATOM   6941  O  OD1 . ASN   F  1 70  ? -8.444  -70.547  2.164   1.00 33.22 ? 70  ASN   F OD1 1 
ATOM   6942  N  ND2 . ASN   F  1 70  ? -9.937  -69.988  3.739   1.00 34.06 ? 70  ASN   F ND2 1 
ATOM   6943  N  N   . LEU   F  1 71  ? -6.789  -69.202  -0.345  1.00 30.07 ? 71  LEU   F N   1 
ATOM   6944  C  CA  . LEU   F  1 71  ? -6.704  -70.105  -1.490  1.00 28.85 ? 71  LEU   F CA  1 
ATOM   6945  C  C   . LEU   F  1 71  ? -6.448  -71.534  -1.053  1.00 33.13 ? 71  LEU   F C   1 
ATOM   6946  O  O   . LEU   F  1 71  ? -6.127  -72.395  -1.885  1.00 34.40 ? 71  LEU   F O   1 
ATOM   6947  C  CB  . LEU   F  1 71  ? -5.620  -69.647  -2.460  1.00 31.85 ? 71  LEU   F CB  1 
ATOM   6948  C  CG  . LEU   F  1 71  ? -5.990  -68.521  -3.433  1.00 36.92 ? 71  LEU   F CG  1 
ATOM   6949  C  CD1 . LEU   F  1 71  ? -5.915  -67.191  -2.744  1.00 35.45 ? 71  LEU   F CD1 1 
ATOM   6950  C  CD2 . LEU   F  1 71  ? -5.073  -68.524  -4.670  1.00 37.41 ? 71  LEU   F CD2 1 
ATOM   6951  N  N   . GLN   F  1 72  ? -6.586  -71.803  0.244   1.00 33.77 ? 72  GLN   F N   1 
ATOM   6952  C  CA  . GLN   F  1 72  ? -6.260  -73.101  0.819   1.00 32.54 ? 72  GLN   F CA  1 
ATOM   6953  C  C   . GLN   F  1 72  ? -7.469  -74.020  0.938   1.00 36.13 ? 72  GLN   F C   1 
ATOM   6954  O  O   . GLN   F  1 72  ? -7.338  -75.234  0.747   1.00 36.31 ? 72  GLN   F O   1 
ATOM   6955  C  CB  . GLN   F  1 72  ? -5.632  -72.899  2.207   1.00 31.07 ? 72  GLN   F CB  1 
ATOM   6956  C  CG  . GLN   F  1 72  ? -5.187  -74.204  2.897   1.00 34.30 ? 72  GLN   F CG  1 
ATOM   6957  C  CD  . GLN   F  1 72  ? -4.099  -74.915  2.119   1.00 27.06 ? 72  GLN   F CD  1 
ATOM   6958  O  OE1 . GLN   F  1 72  ? -2.917  -74.630  2.301   1.00 36.80 ? 72  GLN   F OE1 1 
ATOM   6959  N  NE2 . GLN   F  1 72  ? -4.495  -75.827  1.224   1.00 31.45 ? 72  GLN   F NE2 1 
ATOM   6960  N  N   . ASP   F  1 73  ? -8.638  -73.470  1.244   1.00 32.80 ? 73  ASP   F N   1 
ATOM   6961  C  CA  . ASP   F  1 73  ? -9.826  -74.252  1.569   1.00 36.81 ? 73  ASP   F CA  1 
ATOM   6962  C  C   . ASP   F  1 73  ? -10.702 -74.416  0.328   1.00 36.17 ? 73  ASP   F C   1 
ATOM   6963  O  O   . ASP   F  1 73  ? -11.278 -73.448  -0.170  1.00 38.89 ? 73  ASP   F O   1 
ATOM   6964  C  CB  . ASP   F  1 73  ? -10.593 -73.567  2.704   1.00 35.66 ? 73  ASP   F CB  1 
ATOM   6965  C  CG  . ASP   F  1 73  ? -9.796  -73.513  3.988   1.00 40.11 ? 73  ASP   F CG  1 
ATOM   6966  O  OD1 . ASP   F  1 73  ? -8.918  -74.381  4.178   1.00 37.56 ? 73  ASP   F OD1 1 
ATOM   6967  O  OD2 . ASP   F  1 73  ? -10.024 -72.603  4.799   1.00 41.91 ? 73  ASP   F OD2 1 
ATOM   6968  N  N   . LEU   F  1 74  ? -10.799 -75.635  -0.180  1.00 34.41 ? 74  LEU   F N   1 
ATOM   6969  C  CA  . LEU   F  1 74  ? -11.625 -75.923  -1.347  1.00 35.29 ? 74  LEU   F CA  1 
ATOM   6970  C  C   . LEU   F  1 74  ? -12.862 -76.703  -0.911  1.00 36.06 ? 74  LEU   F C   1 
ATOM   6971  O  O   . LEU   F  1 74  ? -12.740 -77.810  -0.388  1.00 38.64 ? 74  LEU   F O   1 
ATOM   6972  C  CB  . LEU   F  1 74  ? -10.821 -76.706  -2.382  1.00 31.76 ? 74  LEU   F CB  1 
ATOM   6973  C  CG  . LEU   F  1 74  ? -11.535 -77.070  -3.670  1.00 35.01 ? 74  LEU   F CG  1 
ATOM   6974  C  CD1 . LEU   F  1 74  ? -12.067 -75.826  -4.376  1.00 39.66 ? 74  LEU   F CD1 1 
ATOM   6975  C  CD2 . LEU   F  1 74  ? -10.571 -77.831  -4.542  1.00 41.07 ? 74  LEU   F CD2 1 
ATOM   6976  N  N   . GLY   F  1 75  ? -14.042 -76.122  -1.123  1.00 33.49 ? 75  GLY   F N   1 
ATOM   6977  C  CA  . GLY   F  1 75  ? -15.309 -76.783  -0.848  1.00 36.80 ? 75  GLY   F CA  1 
ATOM   6978  C  C   . GLY   F  1 75  ? -15.589 -77.887  -1.849  1.00 35.27 ? 75  GLY   F C   1 
ATOM   6979  O  O   . GLY   F  1 75  ? -14.765 -78.236  -2.693  1.00 33.26 ? 75  GLY   F O   1 
ATOM   6980  N  N   . LYS   F  1 76  ? -16.799 -78.423  -1.768  1.00 32.57 ? 76  LYS   F N   1 
ATOM   6981  C  CA  . LYS   F  1 76  ? -17.145 -79.646  -2.487  1.00 32.62 ? 76  LYS   F CA  1 
ATOM   6982  C  C   . LYS   F  1 76  ? -17.509 -79.359  -3.942  1.00 31.75 ? 76  LYS   F C   1 
ATOM   6983  O  O   . LYS   F  1 76  ? -18.428 -78.589  -4.226  1.00 35.17 ? 76  LYS   F O   1 
ATOM   6984  C  CB  . LYS   F  1 76  ? -18.311 -80.363  -1.809  1.00 39.88 ? 76  LYS   F CB  1 
ATOM   6985  C  CG  . LYS   F  1 76  ? -18.617 -81.734  -2.436  1.00 35.67 ? 76  LYS   F CG  1 
ATOM   6986  N  N   . LEU   F  1 77  ? -16.798 -80.001  -4.853  1.00 30.16 ? 77  LEU   F N   1 
ATOM   6987  C  CA  . LEU   F  1 77  ? -17.142 -79.942  -6.267  1.00 37.01 ? 77  LEU   F CA  1 
ATOM   6988  C  C   . LEU   F  1 77  ? -18.416 -80.730  -6.536  1.00 33.76 ? 77  LEU   F C   1 
ATOM   6989  O  O   . LEU   F  1 77  ? -18.609 -81.816  -5.988  1.00 42.15 ? 77  LEU   F O   1 
ATOM   6990  C  CB  . LEU   F  1 77  ? -15.991 -80.528  -7.097  1.00 39.42 ? 77  LEU   F CB  1 
ATOM   6991  C  CG  . LEU   F  1 77  ? -14.826 -79.627  -7.536  1.00 41.00 ? 77  LEU   F CG  1 
ATOM   6992  C  CD1 . LEU   F  1 77  ? -14.372 -78.723  -6.467  1.00 37.71 ? 77  LEU   F CD1 1 
ATOM   6993  C  CD2 . LEU   F  1 77  ? -13.659 -80.487  -8.053  1.00 40.08 ? 77  LEU   F CD2 1 
ATOM   6994  N  N   . LEU   F  1 78  ? -19.272 -80.197  -7.409  1.00 33.00 ? 78  LEU   F N   1 
ATOM   6995  C  CA  . LEU   F  1 78  ? -20.477 -80.891  -7.879  1.00 34.19 ? 78  LEU   F CA  1 
ATOM   6996  C  C   . LEU   F  1 78  ? -20.229 -81.312  -9.324  1.00 35.32 ? 78  LEU   F C   1 
ATOM   6997  O  O   . LEU   F  1 78  ? -20.368 -80.496  -10.241 1.00 34.65 ? 78  LEU   F O   1 
ATOM   6998  C  CB  . LEU   F  1 78  ? -21.711 -79.995  -7.791  1.00 36.93 ? 78  LEU   F CB  1 
ATOM   6999  C  CG  . LEU   F  1 78  ? -21.961 -79.182  -6.524  1.00 43.65 ? 78  LEU   F CG  1 
ATOM   7000  C  CD1 . LEU   F  1 78  ? -23.262 -78.368  -6.674  1.00 43.99 ? 78  LEU   F CD1 1 
ATOM   7001  C  CD2 . LEU   F  1 78  ? -22.040 -80.083  -5.315  1.00 41.78 ? 78  LEU   F CD2 1 
ATOM   7002  N  N   . ILE   F  1 79  ? -19.845 -82.574  -9.533  1.00 35.26 ? 79  ILE   F N   1 
ATOM   7003  C  CA  . ILE   F  1 79  ? -19.502 -83.090  -10.855 1.00 38.40 ? 79  ILE   F CA  1 
ATOM   7004  C  C   . ILE   F  1 79  ? -20.632 -83.979  -11.338 1.00 44.92 ? 79  ILE   F C   1 
ATOM   7005  O  O   . ILE   F  1 79  ? -20.971 -84.966  -10.679 1.00 48.73 ? 79  ILE   F O   1 
ATOM   7006  C  CB  . ILE   F  1 79  ? -18.180 -83.874  -10.840 1.00 45.22 ? 79  ILE   F CB  1 
ATOM   7007  C  CG1 . ILE   F  1 79  ? -17.076 -83.021  -10.234 1.00 42.85 ? 79  ILE   F CG1 1 
ATOM   7008  C  CG2 . ILE   F  1 79  ? -17.797 -84.297  -12.268 1.00 39.63 ? 79  ILE   F CG2 1 
ATOM   7009  C  CD1 . ILE   F  1 79  ? -16.926 -81.659  -10.931 1.00 45.17 ? 79  ILE   F CD1 1 
ATOM   7010  N  N   . GLY   F  1 80  ? -21.200 -83.650  -12.493 1.00 34.99 ? 80  GLY   F N   1 
ATOM   7011  C  CA  . GLY   F  1 80  ? -22.232 -84.496  -13.062 1.00 44.00 ? 80  GLY   F CA  1 
ATOM   7012  C  C   . GLY   F  1 80  ? -21.664 -85.761  -13.698 1.00 45.54 ? 80  GLY   F C   1 
ATOM   7013  O  O   . GLY   F  1 80  ? -20.458 -85.921  -13.917 1.00 45.01 ? 80  GLY   F O   1 
ATOM   7014  N  N   . GLU   F  1 81  ? -22.572 -86.691  -13.987 1.00 40.14 ? 81  GLU   F N   1 
ATOM   7015  C  CA  . GLU   F  1 81  ? -22.227 -87.943  -14.646 1.00 44.25 ? 81  GLU   F CA  1 
ATOM   7016  C  C   . GLU   F  1 81  ? -22.757 -88.010  -16.066 1.00 45.12 ? 81  GLU   F C   1 
ATOM   7017  O  O   . GLU   F  1 81  ? -22.390 -88.926  -16.804 1.00 47.48 ? 81  GLU   F O   1 
ATOM   7018  C  CB  . GLU   F  1 81  ? -22.769 -89.140  -13.847 1.00 54.33 ? 81  GLU   F CB  1 
ATOM   7019  C  CG  . GLU   F  1 81  ? -22.307 -89.207  -12.381 1.00 61.64 ? 81  GLU   F CG  1 
ATOM   7020  C  CD  . GLU   F  1 81  ? -22.515 -90.585  -11.766 1.00 62.31 ? 81  GLU   F CD  1 
ATOM   7021  O  OE1 . GLU   F  1 81  ? -22.335 -91.591  -12.480 1.00 78.01 ? 81  GLU   F OE1 1 
ATOM   7022  O  OE2 . GLU   F  1 81  ? -22.861 -90.667  -10.572 1.00 63.04 ? 81  GLU   F OE2 1 
ATOM   7023  N  N   . ASN   F  1 82  ? -23.628 -87.083  -16.448 1.00 38.34 ? 82  ASN   F N   1 
ATOM   7024  C  CA  . ASN   F  1 82  ? -24.016 -86.891  -17.833 1.00 44.42 ? 82  ASN   F CA  1 
ATOM   7025  C  C   . ASN   F  1 82  ? -24.279 -85.405  -18.048 1.00 43.98 ? 82  ASN   F C   1 
ATOM   7026  O  O   . ASN   F  1 82  ? -24.222 -84.598  -17.110 1.00 34.07 ? 82  ASN   F O   1 
ATOM   7027  C  CB  . ASN   F  1 82  ? -25.237 -87.746  -18.201 1.00 38.64 ? 82  ASN   F CB  1 
ATOM   7028  C  CG  . ASN   F  1 82  ? -26.421 -87.492  -17.301 1.00 42.50 ? 82  ASN   F CG  1 
ATOM   7029  O  OD1 . ASN   F  1 82  ? -26.756 -86.351  -16.999 1.00 44.02 ? 82  ASN   F OD1 1 
ATOM   7030  N  ND2 . ASN   F  1 82  ? -27.064 -88.569  -16.856 1.00 51.27 ? 82  ASN   F ND2 1 
ATOM   7031  N  N   . THR   F  1 83  ? -24.583 -85.049  -19.299 1.00 38.63 ? 83  THR   F N   1 
ATOM   7032  C  CA  . THR   F  1 83  ? -24.659 -83.640  -19.672 1.00 40.71 ? 83  THR   F CA  1 
ATOM   7033  C  C   . THR   F  1 83  ? -25.740 -82.920  -18.880 1.00 35.70 ? 83  THR   F C   1 
ATOM   7034  O  O   . THR   F  1 83  ? -25.527 -81.824  -18.351 1.00 35.56 ? 83  THR   F O   1 
ATOM   7035  C  CB  . THR   F  1 83  ? -24.901 -83.518  -21.182 1.00 35.29 ? 83  THR   F CB  1 
ATOM   7036  O  OG1 . THR   F  1 83  ? -23.695 -83.856  -21.885 1.00 31.89 ? 83  THR   F OG1 1 
ATOM   7037  C  CG2 . THR   F  1 83  ? -25.334 -82.101  -21.567 1.00 29.72 ? 83  THR   F CG2 1 
ATOM   7038  N  N   . GLN   F  1 84  ? -26.909 -83.525  -18.771 1.00 36.82 ? 84  GLN   F N   1 
ATOM   7039  C  CA  . GLN   F  1 84  ? -27.972 -82.888  -18.018 1.00 30.99 ? 84  GLN   F CA  1 
ATOM   7040  C  C   . GLN   F  1 84  ? -27.563 -82.642  -16.564 1.00 38.06 ? 84  GLN   F C   1 
ATOM   7041  O  O   . GLN   F  1 84  ? -27.834 -81.572  -16.009 1.00 35.03 ? 84  GLN   F O   1 
ATOM   7042  C  CB  . GLN   F  1 84  ? -29.220 -83.756  -18.094 1.00 39.23 ? 84  GLN   F CB  1 
ATOM   7043  C  CG  . GLN   F  1 84  ? -30.490 -83.064  -17.681 1.00 45.13 ? 84  GLN   F CG  1 
ATOM   7044  C  CD  . GLN   F  1 84  ? -31.695 -83.673  -18.391 1.00 62.20 ? 84  GLN   F CD  1 
ATOM   7045  O  OE1 . GLN   F  1 84  ? -31.602 -84.744  -19.007 1.00 71.59 ? 84  GLN   F OE1 1 
ATOM   7046  N  NE2 . GLN   F  1 84  ? -32.809 -82.984  -18.338 1.00 50.23 ? 84  GLN   F NE2 1 
ATOM   7047  N  N   . GLU   F  1 85  ? -26.917 -83.625  -15.926 1.00 36.16 ? 85  GLU   F N   1 
ATOM   7048  C  CA  . GLU   F  1 85  ? -26.548 -83.470  -14.524 1.00 38.84 ? 85  GLU   F CA  1 
ATOM   7049  C  C   . GLU   F  1 85  ? -25.465 -82.422  -14.358 1.00 34.95 ? 85  GLU   F C   1 
ATOM   7050  O  O   . GLU   F  1 85  ? -25.497 -81.634  -13.408 1.00 31.82 ? 85  GLU   F O   1 
ATOM   7051  C  CB  . GLU   F  1 85  ? -26.056 -84.792  -13.947 1.00 37.74 ? 85  GLU   F CB  1 
ATOM   7052  C  CG  . GLU   F  1 85  ? -27.147 -85.765  -13.630 1.00 54.91 ? 85  GLU   F CG  1 
ATOM   7053  C  CD  . GLU   F  1 85  ? -26.620 -87.064  -13.075 1.00 58.43 ? 85  GLU   F CD  1 
ATOM   7054  O  OE1 . GLU   F  1 85  ? -25.386 -87.163  -12.839 1.00 49.69 ? 85  GLU   F OE1 1 
ATOM   7055  O  OE2 . GLU   F  1 85  ? -27.451 -87.981  -12.888 1.00 62.43 ? 85  GLU   F OE2 1 
ATOM   7056  N  N   . MET   F  1 86  ? -24.472 -82.445  -15.247 1.00 32.82 ? 86  MET   F N   1 
ATOM   7057  C  CA  . MET   F  1 86  ? -23.397 -81.462  -15.202 1.00 32.65 ? 86  MET   F CA  1 
ATOM   7058  C  C   . MET   F  1 86  ? -23.974 -80.059  -15.235 1.00 33.55 ? 86  MET   F C   1 
ATOM   7059  O  O   . MET   F  1 86  ? -23.621 -79.205  -14.420 1.00 34.94 ? 86  MET   F O   1 
ATOM   7060  C  CB  . MET   F  1 86  ? -22.443 -81.688  -16.383 1.00 32.73 ? 86  MET   F CB  1 
ATOM   7061  C  CG  . MET   F  1 86  ? -21.739 -83.022  -16.326 1.00 34.44 ? 86  MET   F CG  1 
ATOM   7062  S  SD  . MET   F  1 86  ? -21.175 -83.670  -17.904 1.00 35.14 ? 86  MET   F SD  1 
ATOM   7063  C  CE  . MET   F  1 86  ? -19.583 -82.816  -18.124 1.00 34.24 ? 86  MET   F CE  1 
ATOM   7064  N  N   . LEU   F  1 87  ? -24.900 -79.817  -16.161 1.00 30.79 ? 87  LEU   F N   1 
ATOM   7065  C  CA  . LEU   F  1 87  ? -25.534 -78.509  -16.243 1.00 28.93 ? 87  LEU   F CA  1 
ATOM   7066  C  C   . LEU   F  1 87  ? -26.293 -78.180  -14.969 1.00 38.95 ? 87  LEU   F C   1 
ATOM   7067  O  O   . LEU   F  1 87  ? -26.294 -77.026  -14.534 1.00 31.15 ? 87  LEU   F O   1 
ATOM   7068  C  CB  . LEU   F  1 87  ? -26.474 -78.433  -17.446 1.00 34.29 ? 87  LEU   F CB  1 
ATOM   7069  C  CG  . LEU   F  1 87  ? -25.864 -78.410  -18.858 1.00 38.02 ? 87  LEU   F CG  1 
ATOM   7070  C  CD1 . LEU   F  1 87  ? -26.971 -78.716  -19.929 1.00 31.00 ? 87  LEU   F CD1 1 
ATOM   7071  C  CD2 . LEU   F  1 87  ? -25.167 -77.069  -19.153 1.00 36.32 ? 87  LEU   F CD2 1 
ATOM   7072  N  N   . GLN   F  1 88  ? -26.967 -79.174  -14.368 1.00 33.26 ? 88  GLN   F N   1 
ATOM   7073  C  CA  . GLN   F  1 88  ? -27.694 -78.912  -13.125 1.00 32.40 ? 88  GLN   F CA  1 
ATOM   7074  C  C   . GLN   F  1 88  ? -26.730 -78.662  -11.966 1.00 27.61 ? 88  GLN   F C   1 
ATOM   7075  O  O   . GLN   F  1 88  ? -26.986 -77.804  -11.122 1.00 35.06 ? 88  GLN   F O   1 
ATOM   7076  C  CB  . GLN   F  1 88  ? -28.658 -80.077  -12.821 1.00 33.55 ? 88  GLN   F CB  1 
ATOM   7077  C  CG  . GLN   F  1 88  ? -29.639 -79.843  -11.658 1.00 49.22 ? 88  GLN   F CG  1 
ATOM   7078  C  CD  . GLN   F  1 88  ? -30.628 -78.711  -11.910 1.00 46.15 ? 88  GLN   F CD  1 
ATOM   7079  O  OE1 . GLN   F  1 88  ? -31.316 -78.687  -12.932 1.00 50.01 ? 88  GLN   F OE1 1 
ATOM   7080  N  NE2 . GLN   F  1 88  ? -30.694 -77.761  -10.978 1.00 44.15 ? 88  GLN   F NE2 1 
ATOM   7081  N  N   . CYS   F  1 89  ? -25.606 -79.382  -11.918 1.00 30.15 ? 89  CYS   F N   1 
ATOM   7082  C  CA  . CYS   F  1 89  ? -24.608 -79.120  -10.886 1.00 31.52 ? 89  CYS   F CA  1 
ATOM   7083  C  C   . CYS   F  1 89  ? -24.057 -77.698  -10.998 1.00 35.74 ? 89  CYS   F C   1 
ATOM   7084  O  O   . CYS   F  1 89  ? -23.921 -76.990  -9.989  1.00 32.72 ? 89  CYS   F O   1 
ATOM   7085  C  CB  . CYS   F  1 89  ? -23.476 -80.135  -10.971 1.00 39.70 ? 89  CYS   F CB  1 
ATOM   7086  S  SG  . CYS   F  1 89  ? -23.933 -81.790  -10.436 1.00 38.21 ? 89  CYS   F SG  1 
ATOM   7087  N  N   . ASP   F  1 90  ? -23.729 -77.264  -12.224 1.00 30.83 ? 90  ASP   F N   1 
ATOM   7088  C  CA  . ASP   F  1 90  ? -23.314 -75.877  -12.436 1.00 34.29 ? 90  ASP   F CA  1 
ATOM   7089  C  C   . ASP   F  1 90  ? -24.387 -74.912  -11.944 1.00 28.81 ? 90  ASP   F C   1 
ATOM   7090  O  O   . ASP   F  1 90  ? -24.092 -73.931  -11.250 1.00 29.55 ? 90  ASP   F O   1 
ATOM   7091  C  CB  . ASP   F  1 90  ? -23.019 -75.619  -13.921 1.00 33.20 ? 90  ASP   F CB  1 
ATOM   7092  C  CG  . ASP   F  1 90  ? -21.718 -76.267  -14.405 1.00 34.05 ? 90  ASP   F CG  1 
ATOM   7093  O  OD1 . ASP   F  1 90  ? -20.975 -76.887  -13.612 1.00 32.24 ? 90  ASP   F OD1 1 
ATOM   7094  O  OD2 . ASP   F  1 90  ? -21.421 -76.139  -15.615 1.00 37.41 ? 90  ASP   F OD2 1 
ATOM   7095  N  N   . LEU   F  1 91  ? -25.649 -75.188  -12.272 1.00 29.78 ? 91  LEU   F N   1 
ATOM   7096  C  CA  . LEU   F  1 91  ? -26.713 -74.278  -11.871 1.00 30.19 ? 91  LEU   F CA  1 
ATOM   7097  C  C   . LEU   F  1 91  ? -26.866 -74.237  -10.348 1.00 32.08 ? 91  LEU   F C   1 
ATOM   7098  O  O   . LEU   F  1 91  ? -27.064 -73.168  -9.765  1.00 28.39 ? 91  LEU   F O   1 
ATOM   7099  C  CB  . LEU   F  1 91  ? -28.016 -74.692  -12.552 1.00 30.71 ? 91  LEU   F CB  1 
ATOM   7100  C  CG  . LEU   F  1 91  ? -29.302 -73.909  -12.225 1.00 35.71 ? 91  LEU   F CG  1 
ATOM   7101  C  CD1 . LEU   F  1 91  ? -29.055 -72.452  -12.468 1.00 32.87 ? 91  LEU   F CD1 1 
ATOM   7102  C  CD2 . LEU   F  1 91  ? -30.526 -74.387  -13.058 1.00 35.61 ? 91  LEU   F CD2 1 
ATOM   7103  N  N   . ASN   F  1 92  ? -26.768 -75.387  -9.685  1.00 32.65 ? 92  ASN   F N   1 
ATOM   7104  C  CA  . ASN   F  1 92  ? -26.869 -75.391  -8.226  1.00 33.77 ? 92  ASN   F CA  1 
ATOM   7105  C  C   . ASN   F  1 92  ? -25.740 -74.579  -7.588  1.00 30.41 ? 92  ASN   F C   1 
ATOM   7106  O  O   . ASN   F  1 92  ? -25.968 -73.792  -6.659  1.00 31.03 ? 92  ASN   F O   1 
ATOM   7107  C  CB  . ASN   F  1 92  ? -26.866 -76.829  -7.721  1.00 38.30 ? 92  ASN   F CB  1 
ATOM   7108  C  CG  . ASN   F  1 92  ? -28.157 -77.582  -8.076  1.00 48.50 ? 92  ASN   F CG  1 
ATOM   7109  O  OD1 . ASN   F  1 92  ? -29.198 -76.971  -8.338  1.00 42.51 ? 92  ASN   F OD1 1 
ATOM   7110  N  ND2 . ASN   F  1 92  ? -28.088 -78.913  -8.078  1.00 50.63 ? 92  ASN   F ND2 1 
ATOM   7111  N  N   . LEU   F  1 93  ? -24.519 -74.742  -8.078  1.00 33.41 ? 93  LEU   F N   1 
ATOM   7112  C  CA  . LEU   F  1 93  ? -23.408 -73.928  -7.582  1.00 32.06 ? 93  LEU   F CA  1 
ATOM   7113  C  C   . LEU   F  1 93  ? -23.671 -72.440  -7.800  1.00 33.88 ? 93  LEU   F C   1 
ATOM   7114  O  O   . LEU   F  1 93  ? -23.456 -71.623  -6.897  1.00 28.01 ? 93  LEU   F O   1 
ATOM   7115  C  CB  . LEU   F  1 93  ? -22.118 -74.353  -8.272  1.00 33.27 ? 93  LEU   F CB  1 
ATOM   7116  C  CG  . LEU   F  1 93  ? -20.821 -73.706  -7.781  1.00 28.41 ? 93  LEU   F CG  1 
ATOM   7117  C  CD1 . LEU   F  1 93  ? -20.676 -73.984  -6.303  1.00 33.90 ? 93  LEU   F CD1 1 
ATOM   7118  C  CD2 . LEU   F  1 93  ? -19.636 -74.246  -8.512  1.00 29.58 ? 93  LEU   F CD2 1 
ATOM   7119  N  N   . GLU   F  1 94  ? -24.121 -72.070  -9.010  1.00 34.45 ? 94  GLU   F N   1 
ATOM   7120  C  CA  . GLU   F  1 94  ? -24.369 -70.661  -9.327  1.00 29.09 ? 94  GLU   F CA  1 
ATOM   7121  C  C   . GLU   F  1 94  ? -25.399 -70.052  -8.401  1.00 28.72 ? 94  GLU   F C   1 
ATOM   7122  O  O   . GLU   F  1 94  ? -25.292 -68.880  -8.032  1.00 32.11 ? 94  GLU   F O   1 
ATOM   7123  C  CB  . GLU   F  1 94  ? -24.835 -70.510  -10.780 1.00 29.64 ? 94  GLU   F CB  1 
ATOM   7124  C  CG  . GLU   F  1 94  ? -23.755 -70.729  -11.803 1.00 38.32 ? 94  GLU   F CG  1 
ATOM   7125  C  CD  . GLU   F  1 94  ? -22.821 -69.543  -11.933 1.00 33.67 ? 94  GLU   F CD  1 
ATOM   7126  O  OE1 . GLU   F  1 94  ? -22.942 -68.571  -11.178 1.00 33.56 ? 94  GLU   F OE1 1 
ATOM   7127  O  OE2 . GLU   F  1 94  ? -21.962 -69.589  -12.817 1.00 43.32 ? 94  GLU   F OE2 1 
ATOM   7128  N  N   . LEU   F  1 95  ? -26.437 -70.815  -8.053  1.00 31.95 ? 95  LEU   F N   1 
ATOM   7129  C  CA  . LEU   F  1 95  ? -27.492 -70.266  -7.213  1.00 29.37 ? 95  LEU   F CA  1 
ATOM   7130  C  C   . LEU   F  1 95  ? -26.991 -70.032  -5.788  1.00 25.05 ? 95  LEU   F C   1 
ATOM   7131  O  O   . LEU   F  1 95  ? -27.332 -69.021  -5.162  1.00 30.91 ? 95  LEU   F O   1 
ATOM   7132  C  CB  . LEU   F  1 95  ? -28.713 -71.191  -7.232  1.00 32.70 ? 95  LEU   F CB  1 
ATOM   7133  C  CG  . LEU   F  1 95  ? -29.498 -71.254  -8.552  1.00 41.82 ? 95  LEU   F CG  1 
ATOM   7134  C  CD1 . LEU   F  1 95  ? -30.637 -72.246  -8.488  1.00 41.34 ? 95  LEU   F CD1 1 
ATOM   7135  C  CD2 . LEU   F  1 95  ? -30.058 -69.899  -8.924  1.00 36.53 ? 95  LEU   F CD2 1 
ATOM   7136  N  N   . LYS   F  1 96  ? -26.195 -70.956  -5.259  1.00 35.12 ? 96  LYS   F N   1 
ATOM   7137  C  CA  . LYS   F  1 96  ? -25.550 -70.717  -3.973  1.00 33.67 ? 96  LYS   F CA  1 
ATOM   7138  C  C   . LYS   F  1 96  ? -24.618 -69.509  -4.063  1.00 36.98 ? 96  LYS   F C   1 
ATOM   7139  O  O   . LYS   F  1 96  ? -24.634 -68.630  -3.186  1.00 31.59 ? 96  LYS   F O   1 
ATOM   7140  C  CB  . LYS   F  1 96  ? -24.812 -71.988  -3.554  1.00 36.03 ? 96  LYS   F CB  1 
ATOM   7141  C  CG  . LYS   F  1 96  ? -23.676 -71.844  -2.542  1.00 43.45 ? 96  LYS   F CG  1 
ATOM   7142  C  CD  . LYS   F  1 96  ? -24.162 -71.654  -1.145  1.00 49.06 ? 96  LYS   F CD  1 
ATOM   7143  C  CE  . LYS   F  1 96  ? -23.040 -72.013  -0.170  1.00 52.29 ? 96  LYS   F CE  1 
ATOM   7144  N  NZ  . LYS   F  1 96  ? -21.715 -71.470  -0.586  1.00 49.74 ? 96  LYS   F NZ  1 
ATOM   7145  N  N   . ALA   F  1 97  ? -23.842 -69.421  -5.149  1.00 32.31 ? 97  ALA   F N   1 
ATOM   7146  C  CA  . ALA   F  1 97  ? -22.905 -68.308  -5.326  1.00 28.86 ? 97  ALA   F CA  1 
ATOM   7147  C  C   . ALA   F  1 97  ? -23.618 -66.957  -5.330  1.00 25.86 ? 97  ALA   F C   1 
ATOM   7148  O  O   . ALA   F  1 97  ? -23.152 -65.995  -4.708  1.00 29.40 ? 97  ALA   F O   1 
ATOM   7149  C  CB  . ALA   F  1 97  ? -22.118 -68.494  -6.627  1.00 29.00 ? 97  ALA   F CB  1 
ATOM   7150  N  N   . THR   F  1 98  ? -24.733 -66.847  -6.056  1.00 24.96 ? 98  THR   F N   1 
ATOM   7151  C  CA  . THR   F  1 98  ? -25.421 -65.556  -6.100  1.00 32.79 ? 98  THR   F CA  1 
ATOM   7152  C  C   . THR   F  1 98  ? -26.101 -65.230  -4.773  1.00 33.46 ? 98  THR   F C   1 
ATOM   7153  O  O   . THR   F  1 98  ? -26.234 -64.047  -4.421  1.00 27.35 ? 98  THR   F O   1 
ATOM   7154  C  CB  . THR   F  1 98  ? -26.450 -65.518  -7.239  1.00 31.49 ? 98  THR   F CB  1 
ATOM   7155  O  OG1 . THR   F  1 98  ? -27.388 -66.601  -7.097  1.00 31.50 ? 98  THR   F OG1 1 
ATOM   7156  C  CG2 . THR   F  1 98  ? -25.738 -65.630  -8.596  1.00 34.27 ? 98  THR   F CG2 1 
ATOM   7157  N  N   . LYS   F  1 99  ? -26.544 -66.247  -4.027  1.00 28.91 ? 99  LYS   F N   1 
ATOM   7158  C  CA  . LYS   F  1 99  ? -27.003 -66.000  -2.661  1.00 32.79 ? 99  LYS   F CA  1 
ATOM   7159  C  C   . LYS   F  1 99  ? -25.901 -65.363  -1.828  1.00 28.13 ? 99  LYS   F C   1 
ATOM   7160  O  O   . LYS   F  1 99  ? -26.111 -64.342  -1.160  1.00 27.46 ? 99  LYS   F O   1 
ATOM   7161  C  CB  . LYS   F  1 99  ? -27.458 -67.315  -2.015  1.00 29.89 ? 99  LYS   F CB  1 
ATOM   7162  C  CG  . LYS   F  1 99  ? -28.129 -67.147  -0.672  1.00 38.96 ? 99  LYS   F CG  1 
ATOM   7163  C  CD  . LYS   F  1 99  ? -28.833 -68.446  -0.241  1.00 45.90 ? 99  LYS   F CD  1 
ATOM   7164  N  N   . ASP   F  1 100 ? -24.719 -65.969  -1.842  1.00 27.98 ? 100 ASP   F N   1 
ATOM   7165  C  CA  . ASP   F  1 100 ? -23.612 -65.442  -1.054  1.00 29.92 ? 100 ASP   F CA  1 
ATOM   7166  C  C   . ASP   F  1 100 ? -23.219 -64.039  -1.505  1.00 32.18 ? 100 ASP   F C   1 
ATOM   7167  O  O   . ASP   F  1 100 ? -22.849 -63.196  -0.670  1.00 27.99 ? 100 ASP   F O   1 
ATOM   7168  C  CB  . ASP   F  1 100 ? -22.420 -66.389  -1.130  1.00 31.80 ? 100 ASP   F CB  1 
ATOM   7169  C  CG  . ASP   F  1 100 ? -22.702 -67.729  -0.461  1.00 40.62 ? 100 ASP   F CG  1 
ATOM   7170  O  OD1 . ASP   F  1 100 ? -23.666 -67.837  0.327   1.00 36.22 ? 100 ASP   F OD1 1 
ATOM   7171  O  OD2 . ASP   F  1 100 ? -21.956 -68.681  -0.717  1.00 34.69 ? 100 ASP   F OD2 1 
ATOM   7172  N  N   . LEU   F  1 101 ? -23.304 -63.765  -2.813  1.00 30.43 ? 101 LEU   F N   1 
ATOM   7173  C  CA  . LEU   F  1 101 ? -22.958 -62.445  -3.319  1.00 22.98 ? 101 LEU   F CA  1 
ATOM   7174  C  C   . LEU   F  1 101 ? -23.908 -61.396  -2.782  1.00 22.54 ? 101 LEU   F C   1 
ATOM   7175  O  O   . LEU   F  1 101 ? -23.486 -60.304  -2.377  1.00 26.41 ? 101 LEU   F O   1 
ATOM   7176  C  CB  . LEU   F  1 101 ? -22.971 -62.444  -4.856  1.00 28.52 ? 101 LEU   F CB  1 
ATOM   7177  C  CG  . LEU   F  1 101 ? -21.755 -63.045  -5.570  1.00 27.94 ? 101 LEU   F CG  1 
ATOM   7178  C  CD1 . LEU   F  1 101 ? -22.047 -63.491  -6.995  1.00 26.62 ? 101 LEU   F CD1 1 
ATOM   7179  C  CD2 . LEU   F  1 101 ? -20.600 -62.043  -5.556  1.00 35.45 ? 101 LEU   F CD2 1 
ATOM   7180  N  N   . ARG   F  1 102 ? -25.205 -61.691  -2.780  1.00 26.55 ? 102 ARG   F N   1 
ATOM   7181  C  CA  . ARG   F  1 102 ? -26.146 -60.695  -2.294  1.00 26.60 ? 102 ARG   F CA  1 
ATOM   7182  C  C   . ARG   F  1 102 ? -25.924 -60.417  -0.819  1.00 23.26 ? 102 ARG   F C   1 
ATOM   7183  O  O   . ARG   F  1 102 ? -25.999 -59.266  -0.381  1.00 26.90 ? 102 ARG   F O   1 
ATOM   7184  C  CB  . ARG   F  1 102 ? -27.594 -61.146  -2.541  1.00 26.55 ? 102 ARG   F CB  1 
ATOM   7185  C  CG  . ARG   F  1 102 ? -27.936 -61.346  -4.002  1.00 26.90 ? 102 ARG   F CG  1 
ATOM   7186  C  CD  . ARG   F  1 102 ? -29.363 -61.955  -4.190  1.00 30.04 ? 102 ARG   F CD  1 
ATOM   7187  N  NE  . ARG   F  1 102 ? -29.485 -62.644  -5.471  1.00 31.24 ? 102 ARG   F NE  1 
ATOM   7188  C  CZ  . ARG   F  1 102 ? -29.479 -62.029  -6.648  1.00 29.73 ? 102 ARG   F CZ  1 
ATOM   7189  N  NH1 . ARG   F  1 102 ? -29.485 -60.714  -6.739  1.00 36.39 ? 102 ARG   F NH1 1 
ATOM   7190  N  NH2 . ARG   F  1 102 ? -29.427 -62.754  -7.760  1.00 29.59 ? 102 ARG   F NH2 1 
ATOM   7191  N  N   . GLU   F  1 103 ? -25.701 -61.462  -0.023  1.00 26.77 ? 103 GLU   F N   1 
ATOM   7192  C  CA  . GLU   F  1 103 ? -25.466 -61.241  1.406   1.00 29.99 ? 103 GLU   F CA  1 
ATOM   7193  C  C   . GLU   F  1 103 ? -24.208 -60.401  1.621   1.00 29.71 ? 103 GLU   F C   1 
ATOM   7194  O  O   . GLU   F  1 103 ? -24.173 -59.511  2.481   1.00 26.50 ? 103 GLU   F O   1 
ATOM   7195  C  CB  . GLU   F  1 103 ? -25.347 -62.588  2.133   1.00 29.67 ? 103 GLU   F CB  1 
ATOM   7196  C  CG  . GLU   F  1 103 ? -26.630 -63.445  2.074   1.00 38.01 ? 103 GLU   F CG  1 
ATOM   7197  N  N   . ALA   F  1 104 ? -23.179 -60.657  0.819   1.00 29.16 ? 104 ALA   F N   1 
ATOM   7198  C  CA  . ALA   F  1 104 ? -21.946 -59.875  0.887   1.00 29.19 ? 104 ALA   F CA  1 
ATOM   7199  C  C   . ALA   F  1 104 ? -22.200 -58.417  0.506   1.00 24.22 ? 104 ALA   F C   1 
ATOM   7200  O  O   . ALA   F  1 104 ? -21.675 -57.502  1.144   1.00 28.31 ? 104 ALA   F O   1 
ATOM   7201  C  CB  . ALA   F  1 104 ? -20.902 -60.522  -0.033  1.00 26.37 ? 104 ALA   F CB  1 
ATOM   7202  N  N   . ILE   F  1 105 ? -23.031 -58.176  -0.516  1.00 27.27 ? 105 ILE   F N   1 
ATOM   7203  C  CA  . ILE   F  1 105 ? -23.335 -56.795  -0.891  1.00 27.79 ? 105 ILE   F CA  1 
ATOM   7204  C  C   . ILE   F  1 105 ? -24.051 -56.061  0.237   1.00 26.65 ? 105 ILE   F C   1 
ATOM   7205  O  O   . ILE   F  1 105 ? -23.748 -54.896  0.527   1.00 25.55 ? 105 ILE   F O   1 
ATOM   7206  C  CB  . ILE   F  1 105 ? -24.128 -56.771  -2.210  1.00 25.92 ? 105 ILE   F CB  1 
ATOM   7207  C  CG1 . ILE   F  1 105 ? -23.154 -57.077  -3.362  1.00 25.73 ? 105 ILE   F CG1 1 
ATOM   7208  C  CG2 . ILE   F  1 105 ? -24.814 -55.421  -2.418  1.00 23.89 ? 105 ILE   F CG2 1 
ATOM   7209  C  CD1 . ILE   F  1 105 ? -23.867 -57.534  -4.691  1.00 24.89 ? 105 ILE   F CD1 1 
ATOM   7210  N  N   . VAL   F  1 106 ? -25.009 -56.724  0.903   1.00 25.19 ? 106 VAL   F N   1 
ATOM   7211  C  CA  . VAL   F  1 106 ? -25.692 -56.075  2.016   1.00 24.61 ? 106 VAL   F CA  1 
ATOM   7212  C  C   . VAL   F  1 106 ? -24.681 -55.598  3.034   1.00 24.27 ? 106 VAL   F C   1 
ATOM   7213  O  O   . VAL   F  1 106 ? -24.756 -54.467  3.541   1.00 24.09 ? 106 VAL   F O   1 
ATOM   7214  C  CB  . VAL   F  1 106 ? -26.710 -57.032  2.665   1.00 27.76 ? 106 VAL   F CB  1 
ATOM   7215  C  CG1 . VAL   F  1 106 ? -27.234 -56.437  3.999   1.00 33.21 ? 106 VAL   F CG1 1 
ATOM   7216  C  CG2 . VAL   F  1 106 ? -27.853 -57.287  1.727   1.00 35.21 ? 106 VAL   F CG2 1 
ATOM   7217  N  N   . HIS   F  1 107 ? -23.716 -56.455  3.361   1.00 25.26 ? 107 HIS   F N   1 
ATOM   7218  C  CA  . HIS   F  1 107 ? -22.796 -56.071  4.416   1.00 28.78 ? 107 HIS   F CA  1 
ATOM   7219  C  C   . HIS   F  1 107 ? -21.879 -54.943  3.964   1.00 28.67 ? 107 HIS   F C   1 
ATOM   7220  O  O   . HIS   F  1 107 ? -21.614 -54.019  4.744   1.00 25.26 ? 107 HIS   F O   1 
ATOM   7221  C  CB  . HIS   F  1 107 ? -21.956 -57.241  4.909   1.00 31.85 ? 107 HIS   F CB  1 
ATOM   7222  C  CG  . HIS   F  1 107 ? -21.113 -56.857  6.076   1.00 33.16 ? 107 HIS   F CG  1 
ATOM   7223  N  ND1 . HIS   F  1 107 ? -21.649 -56.608  7.320   1.00 33.25 ? 107 HIS   F ND1 1 
ATOM   7224  C  CD2 . HIS   F  1 107 ? -19.798 -56.561  6.167   1.00 36.36 ? 107 HIS   F CD2 1 
ATOM   7225  C  CE1 . HIS   F  1 107 ? -20.694 -56.214  8.140   1.00 39.53 ? 107 HIS   F CE1 1 
ATOM   7226  N  NE2 . HIS   F  1 107 ? -19.558 -56.185  7.466   1.00 37.95 ? 107 HIS   F NE2 1 
ATOM   7227  N  N   . CYS   F  1 108 ? -21.382 -55.010  2.714   1.00 25.39 ? 108 CYS   F N   1 
ATOM   7228  C  CA  . CYS   F  1 108 ? -20.612 -53.898  2.157   1.00 24.12 ? 108 CYS   F CA  1 
ATOM   7229  C  C   . CYS   F  1 108 ? -21.374 -52.587  2.267   1.00 26.08 ? 108 CYS   F C   1 
ATOM   7230  O  O   . CYS   F  1 108 ? -20.820 -51.561  2.670   1.00 27.53 ? 108 CYS   F O   1 
ATOM   7231  C  CB  . CYS   F  1 108 ? -20.255 -54.174  0.689   1.00 28.67 ? 108 CYS   F CB  1 
ATOM   7232  S  SG  . CYS   F  1 108 ? -19.016 -55.486  0.454   1.00 28.32 ? 108 CYS   F SG  1 
ATOM   7233  N  N   . GLU   F  1 109 ? -22.639 -52.590  1.851   1.00 25.53 ? 109 GLU   F N   1 
ATOM   7234  C  CA  . GLU   F  1 109 ? -23.458 -51.389  1.947   1.00 26.29 ? 109 GLU   F CA  1 
ATOM   7235  C  C   . GLU   F  1 109 ? -23.542 -50.890  3.385   1.00 29.92 ? 109 GLU   F C   1 
ATOM   7236  O  O   . GLU   F  1 109 ? -23.362 -49.698  3.660   1.00 24.76 ? 109 GLU   F O   1 
ATOM   7237  C  CB  . GLU   F  1 109 ? -24.851 -51.699  1.393   1.00 26.33 ? 109 GLU   F CB  1 
ATOM   7238  C  CG  . GLU   F  1 109 ? -25.820 -50.518  1.339   1.00 27.40 ? 109 GLU   F CG  1 
ATOM   7239  C  CD  . GLU   F  1 109 ? -25.414 -49.490  0.302   1.00 30.31 ? 109 GLU   F CD  1 
ATOM   7240  O  OE1 . GLU   F  1 109 ? -24.621 -49.829  -0.610  1.00 24.50 ? 109 GLU   F OE1 1 
ATOM   7241  O  OE2 . GLU   F  1 109 ? -25.899 -48.350  0.389   1.00 27.50 ? 109 GLU   F OE2 1 
ATOM   7242  N  N   . GLN   F  1 110 ? -23.796 -51.803  4.328   1.00 28.21 ? 110 GLN   F N   1 
ATOM   7243  C  CA  . GLN   F  1 110 ? -23.955 -51.406  5.724   1.00 28.88 ? 110 GLN   F CA  1 
ATOM   7244  C  C   . GLN   F  1 110 ? -22.713 -50.702  6.263   1.00 31.39 ? 110 GLN   F C   1 
ATOM   7245  O  O   . GLN   F  1 110 ? -22.826 -49.748  7.032   1.00 26.90 ? 110 GLN   F O   1 
ATOM   7246  C  CB  . GLN   F  1 110 ? -24.285 -52.644  6.583   1.00 33.91 ? 110 GLN   F CB  1 
ATOM   7247  C  CG  . GLN   F  1 110 ? -24.487 -52.387  8.082   1.00 47.88 ? 110 GLN   F CG  1 
ATOM   7248  C  CD  . GLN   F  1 110 ? -24.624 -53.699  8.884   1.00 63.76 ? 110 GLN   F CD  1 
ATOM   7249  O  OE1 . GLN   F  1 110 ? -23.807 -54.616  8.738   1.00 62.79 ? 110 GLN   F OE1 1 
ATOM   7250  N  NE2 . GLN   F  1 110 ? -25.660 -53.791  9.717   1.00 71.34 ? 110 GLN   F NE2 1 
ATOM   7251  N  N   . VAL   F  1 111 ? -21.513 -51.155  5.894   1.00 27.63 ? 111 VAL   F N   1 
ATOM   7252  C  CA  . VAL   F  1 111 ? -20.312 -50.517  6.417   1.00 25.81 ? 111 VAL   F CA  1 
ATOM   7253  C  C   . VAL   F  1 111 ? -19.704 -49.531  5.426   1.00 28.42 ? 111 VAL   F C   1 
ATOM   7254  O  O   . VAL   F  1 111 ? -18.548 -49.135  5.585   1.00 25.67 ? 111 VAL   F O   1 
ATOM   7255  C  CB  . VAL   F  1 111 ? -19.284 -51.564  6.870   1.00 27.61 ? 111 VAL   F CB  1 
ATOM   7256  C  CG1 . VAL   F  1 111 ? -19.933 -52.515  7.895   1.00 29.01 ? 111 VAL   F CG1 1 
ATOM   7257  C  CG2 . VAL   F  1 111 ? -18.725 -52.356  5.697   1.00 27.86 ? 111 VAL   F CG2 1 
ATOM   7258  N  N   . HIS   F  1 112 ? -20.446 -49.151  4.390   1.00 26.03 ? 112 HIS   F N   1 
ATOM   7259  C  CA  . HIS   F  1 112 ? -20.041 -48.101  3.461   1.00 26.01 ? 112 HIS   F CA  1 
ATOM   7260  C  C   . HIS   F  1 112 ? -18.798 -48.482  2.642   1.00 25.76 ? 112 HIS   F C   1 
ATOM   7261  O  O   . HIS   F  1 112 ? -18.050 -47.608  2.207   1.00 26.13 ? 112 HIS   F O   1 
ATOM   7262  C  CB  . HIS   F  1 112 ? -19.795 -46.768  4.184   1.00 27.56 ? 112 HIS   F CB  1 
ATOM   7263  C  CG  . HIS   F  1 112 ? -20.871 -46.393  5.167   1.00 30.28 ? 112 HIS   F CG  1 
ATOM   7264  N  ND1 . HIS   F  1 112 ? -22.213 -46.474  4.883   1.00 33.27 ? 112 HIS   F ND1 1 
ATOM   7265  C  CD2 . HIS   F  1 112 ? -20.786 -45.983  6.454   1.00 39.07 ? 112 HIS   F CD2 1 
ATOM   7266  C  CE1 . HIS   F  1 112 ? -22.913 -46.099  5.941   1.00 29.49 ? 112 HIS   F CE1 1 
ATOM   7267  N  NE2 . HIS   F  1 112 ? -22.069 -45.803  6.910   1.00 45.21 ? 112 HIS   F NE2 1 
ATOM   7268  N  N   . ASP   F  1 113 ? -18.571 -49.770  2.382   1.00 26.97 ? 113 ASP   F N   1 
ATOM   7269  C  CA  . ASP   F  1 113 ? -17.500 -50.181  1.464   1.00 25.21 ? 113 ASP   F CA  1 
ATOM   7270  C  C   . ASP   F  1 113 ? -18.107 -50.277  0.057   1.00 23.89 ? 113 ASP   F C   1 
ATOM   7271  O  O   . ASP   F  1 113 ? -18.439 -51.344  -0.466  1.00 22.90 ? 113 ASP   F O   1 
ATOM   7272  C  CB  . ASP   F  1 113 ? -16.872 -51.479  1.936   1.00 24.72 ? 113 ASP   F CB  1 
ATOM   7273  C  CG  . ASP   F  1 113 ? -15.701 -51.917  1.075   1.00 30.43 ? 113 ASP   F CG  1 
ATOM   7274  O  OD1 . ASP   F  1 113 ? -15.412 -51.254  0.051   1.00 25.01 ? 113 ASP   F OD1 1 
ATOM   7275  O  OD2 . ASP   F  1 113 ? -15.096 -52.946  1.426   1.00 27.86 ? 113 ASP   F OD2 1 
ATOM   7276  N  N   . TYR   F  1 114 ? -18.275 -49.110  -0.554  1.00 22.28 ? 114 TYR   F N   1 
ATOM   7277  C  CA  . TYR   F  1 114 ? -19.023 -49.036  -1.806  1.00 25.16 ? 114 TYR   F CA  1 
ATOM   7278  C  C   . TYR   F  1 114 ? -18.225 -49.583  -2.979  1.00 26.77 ? 114 TYR   F C   1 
ATOM   7279  O  O   . TYR   F  1 114 ? -18.818 -50.056  -3.955  1.00 22.65 ? 114 TYR   F O   1 
ATOM   7280  C  CB  . TYR   F  1 114 ? -19.436 -47.594  -2.045  1.00 22.00 ? 114 TYR   F CB  1 
ATOM   7281  C  CG  . TYR   F  1 114 ? -20.362 -47.066  -0.965  1.00 23.18 ? 114 TYR   F CG  1 
ATOM   7282  C  CD1 . TYR   F  1 114 ? -21.619 -47.658  -0.729  1.00 26.08 ? 114 TYR   F CD1 1 
ATOM   7283  C  CD2 . TYR   F  1 114 ? -19.984 -46.008  -0.174  1.00 23.40 ? 114 TYR   F CD2 1 
ATOM   7284  C  CE1 . TYR   F  1 114 ? -22.463 -47.178  0.263   1.00 27.66 ? 114 TYR   F CE1 1 
ATOM   7285  C  CE2 . TYR   F  1 114 ? -20.799 -45.532  0.829   1.00 26.48 ? 114 TYR   F CE2 1 
ATOM   7286  C  CZ  . TYR   F  1 114 ? -22.044 -46.109  1.037   1.00 29.46 ? 114 TYR   F CZ  1 
ATOM   7287  O  OH  . TYR   F  1 114 ? -22.850 -45.608  2.027   1.00 27.78 ? 114 TYR   F OH  1 
ATOM   7288  N  N   . VAL   F  1 115 ? -16.885 -49.549  -2.895  1.00 22.13 ? 115 VAL   F N   1 
ATOM   7289  C  CA  . VAL   F  1 115 ? -16.072 -50.085  -3.982  1.00 22.58 ? 115 VAL   F CA  1 
ATOM   7290  C  C   . VAL   F  1 115 ? -16.157 -51.605  -3.995  1.00 21.45 ? 115 VAL   F C   1 
ATOM   7291  O  O   . VAL   F  1 115 ? -16.350 -52.218  -5.060  1.00 23.90 ? 115 VAL   F O   1 
ATOM   7292  C  CB  . VAL   F  1 115 ? -14.614 -49.581  -3.877  1.00 28.16 ? 115 VAL   F CB  1 
ATOM   7293  C  CG1 . VAL   F  1 115 ? -13.761 -50.169  -5.008  1.00 27.50 ? 115 VAL   F CG1 1 
ATOM   7294  C  CG2 . VAL   F  1 115 ? -14.575 -48.074  -3.932  1.00 27.95 ? 115 VAL   F CG2 1 
ATOM   7295  N  N   . SER   F  1 116 ? -16.068 -52.238  -2.818  1.00 23.39 ? 116 SER   F N   1 
ATOM   7296  C  CA  . SER   F  1 116 ? -16.276 -53.687  -2.744  1.00 29.14 ? 116 SER   F CA  1 
ATOM   7297  C  C   . SER   F  1 116 ? -17.658 -54.081  -3.248  1.00 21.13 ? 116 SER   F C   1 
ATOM   7298  O  O   . SER   F  1 116 ? -17.798 -55.053  -4.002  1.00 23.47 ? 116 SER   F O   1 
ATOM   7299  C  CB  . SER   F  1 116 ? -16.085 -54.191  -1.317  1.00 28.76 ? 116 SER   F CB  1 
ATOM   7300  O  OG  . SER   F  1 116 ? -14.705 -54.181  -0.952  1.00 24.39 ? 116 SER   F OG  1 
ATOM   7301  N  N   . ARG   F  1 117 ? -18.689 -53.336  -2.855  1.00 25.18 ? 117 ARG   F N   1 
ATOM   7302  C  CA  . ARG   F  1 117 ? -20.023 -53.602  -3.389  1.00 23.90 ? 117 ARG   F CA  1 
ATOM   7303  C  C   . ARG   F  1 117 ? -20.022 -53.570  -4.920  1.00 28.79 ? 117 ARG   F C   1 
ATOM   7304  O  O   . ARG   F  1 117 ? -20.577 -54.468  -5.569  1.00 23.48 ? 117 ARG   F O   1 
ATOM   7305  C  CB  . ARG   F  1 117 ? -21.048 -52.608  -2.821  1.00 26.12 ? 117 ARG   F CB  1 
ATOM   7306  C  CG  . ARG   F  1 117 ? -22.369 -52.604  -3.639  1.00 23.24 ? 117 ARG   F CG  1 
ATOM   7307  C  CD  . ARG   F  1 117 ? -23.461 -51.780  -3.040  1.00 27.84 ? 117 ARG   F CD  1 
ATOM   7308  N  NE  . ARG   F  1 117 ? -24.620 -51.754  -3.928  1.00 27.46 ? 117 ARG   F NE  1 
ATOM   7309  C  CZ  . ARG   F  1 117 ? -25.882 -51.652  -3.526  1.00 27.70 ? 117 ARG   F CZ  1 
ATOM   7310  N  NH1 . ARG   F  1 117 ? -26.190 -51.470  -2.253  1.00 23.17 ? 117 ARG   F NH1 1 
ATOM   7311  N  NH2 . ARG   F  1 117 ? -26.856 -51.726  -4.424  1.00 28.87 ? 117 ARG   F NH2 1 
ATOM   7312  N  N   . ASP   F  1 118 ? -19.398 -52.542  -5.514  1.00 24.59 ? 118 ASP   F N   1 
ATOM   7313  C  CA  . ASP   F  1 118 ? -19.434 -52.392  -6.971  1.00 23.65 ? 118 ASP   F CA  1 
ATOM   7314  C  C   . ASP   F  1 118 ? -18.770 -53.589  -7.652  1.00 28.60 ? 118 ASP   F C   1 
ATOM   7315  O  O   . ASP   F  1 118 ? -19.286 -54.124  -8.647  1.00 24.79 ? 118 ASP   F O   1 
ATOM   7316  C  CB  . ASP   F  1 118 ? -18.762 -51.061  -7.343  1.00 22.67 ? 118 ASP   F CB  1 
ATOM   7317  C  CG  . ASP   F  1 118 ? -19.101 -50.592  -8.738  1.00 29.18 ? 118 ASP   F CG  1 
ATOM   7318  O  OD1 . ASP   F  1 118 ? -20.283 -50.694  -9.103  1.00 27.58 ? 118 ASP   F OD1 1 
ATOM   7319  O  OD2 . ASP   F  1 118 ? -18.190 -50.100  -9.464  1.00 28.20 ? 118 ASP   F OD2 1 
ATOM   7320  N  N   . LEU   F  1 119 ? -17.660 -54.068  -7.081  1.00 26.23 ? 119 LEU   F N   1 
ATOM   7321  C  CA  . LEU   F  1 119 ? -16.997 -55.261  -7.602  1.00 27.52 ? 119 LEU   F CA  1 
ATOM   7322  C  C   . LEU   F  1 119 ? -17.905 -56.489  -7.512  1.00 24.77 ? 119 LEU   F C   1 
ATOM   7323  O  O   . LEU   F  1 119 ? -18.000 -57.279  -8.463  1.00 22.71 ? 119 LEU   F O   1 
ATOM   7324  C  CB  . LEU   F  1 119 ? -15.692 -55.487  -6.834  1.00 24.35 ? 119 LEU   F CB  1 
ATOM   7325  C  CG  . LEU   F  1 119 ? -14.983 -56.833  -7.019  1.00 25.64 ? 119 LEU   F CG  1 
ATOM   7326  C  CD1 . LEU   F  1 119 ? -14.535 -56.953  -8.456  1.00 28.87 ? 119 LEU   F CD1 1 
ATOM   7327  C  CD2 . LEU   F  1 119 ? -13.789 -56.948  -6.038  1.00 32.00 ? 119 LEU   F CD2 1 
ATOM   7328  N  N   . LEU   F  1 120 ? -18.559 -56.682  -6.361  1.00 22.92 ? 120 LEU   F N   1 
ATOM   7329  C  CA  . LEU   F  1 120 ? -19.477 -57.803  -6.207  1.00 26.56 ? 120 LEU   F CA  1 
ATOM   7330  C  C   . LEU   F  1 120 ? -20.666 -57.679  -7.145  1.00 24.97 ? 120 LEU   F C   1 
ATOM   7331  O  O   . LEU   F  1 120 ? -21.140 -58.682  -7.673  1.00 23.52 ? 120 LEU   F O   1 
ATOM   7332  C  CB  . LEU   F  1 120 ? -19.972 -57.901  -4.761  1.00 21.55 ? 120 LEU   F CB  1 
ATOM   7333  C  CG  . LEU   F  1 120 ? -18.830 -58.207  -3.763  1.00 25.59 ? 120 LEU   F CG  1 
ATOM   7334  C  CD1 . LEU   F  1 120 ? -19.306 -58.322  -2.321  1.00 31.25 ? 120 LEU   F CD1 1 
ATOM   7335  C  CD2 . LEU   F  1 120 ? -18.093 -59.478  -4.141  1.00 31.11 ? 120 LEU   F CD2 1 
ATOM   7336  N  N   . LYS   F  1 121 ? -21.193 -56.468  -7.332  1.00 27.23 ? 121 LYS   F N   1 
ATOM   7337  C  CA  . LYS   F  1 121 ? -22.290 -56.305  -8.277  1.00 32.54 ? 121 LYS   F CA  1 
ATOM   7338  C  C   . LYS   F  1 121 ? -21.855 -56.763  -9.677  1.00 33.26 ? 121 LYS   F C   1 
ATOM   7339  O  O   . LYS   F  1 121 ? -22.585 -57.497  -10.364 1.00 24.83 ? 121 LYS   F O   1 
ATOM   7340  C  CB  . LYS   F  1 121 ? -22.777 -54.840  -8.262  1.00 25.36 ? 121 LYS   F CB  1 
ATOM   7341  C  CG  . LYS   F  1 121 ? -23.932 -54.533  -9.229  1.00 31.12 ? 121 LYS   F CG  1 
ATOM   7342  C  CD  . LYS   F  1 121 ? -23.423 -54.143  -10.625 1.00 32.78 ? 121 LYS   F CD  1 
ATOM   7343  C  CE  . LYS   F  1 121 ? -22.842 -52.740  -10.681 1.00 37.52 ? 121 LYS   F CE  1 
ATOM   7344  N  NZ  . LYS   F  1 121 ? -22.361 -52.417  -12.072 1.00 35.64 ? 121 LYS   F NZ  1 
ATOM   7345  N  N   . ASP   F  1 122 ? -20.651 -56.367  -10.104 1.00 26.88 ? 122 ASP   F N   1 
ATOM   7346  C  CA  . ASP   F  1 122 ? -20.185 -56.753  -11.435 1.00 26.23 ? 122 ASP   F CA  1 
ATOM   7347  C  C   . ASP   F  1 122 ? -20.077 -58.263  -11.556 1.00 29.73 ? 122 ASP   F C   1 
ATOM   7348  O  O   . ASP   F  1 122 ? -20.472 -58.834  -12.573 1.00 23.18 ? 122 ASP   F O   1 
ATOM   7349  C  CB  . ASP   F  1 122 ? -18.828 -56.131  -11.740 1.00 26.35 ? 122 ASP   F CB  1 
ATOM   7350  C  CG  . ASP   F  1 122 ? -18.910 -54.637  -11.986 1.00 33.53 ? 122 ASP   F CG  1 
ATOM   7351  O  OD1 . ASP   F  1 122 ? -20.009 -54.134  -12.268 1.00 31.83 ? 122 ASP   F OD1 1 
ATOM   7352  O  OD2 . ASP   F  1 122 ? -17.865 -53.960  -11.889 1.00 34.08 ? 122 ASP   F OD2 1 
ATOM   7353  N  N   . ILE   F  1 123 ? -19.511 -58.914  -10.532 1.00 23.85 ? 123 ILE   F N   1 
ATOM   7354  C  CA  . ILE   F  1 123 ? -19.433 -60.370  -10.515 1.00 26.84 ? 123 ILE   F CA  1 
ATOM   7355  C  C   . ILE   F  1 123 ? -20.822 -60.952  -10.583 1.00 27.30 ? 123 ILE   F C   1 
ATOM   7356  O  O   . ILE   F  1 123 ? -21.066 -61.924  -11.309 1.00 23.40 ? 123 ILE   F O   1 
ATOM   7357  C  CB  . ILE   F  1 123 ? -18.686 -60.869  -9.260  1.00 25.03 ? 123 ILE   F CB  1 
ATOM   7358  C  CG1 . ILE   F  1 123 ? -17.231 -60.384  -9.303  1.00 30.13 ? 123 ILE   F CG1 1 
ATOM   7359  C  CG2 . ILE   F  1 123 ? -18.783 -62.410  -9.139  1.00 27.97 ? 123 ILE   F CG2 1 
ATOM   7360  C  CD1 . ILE   F  1 123 ? -16.376 -60.899  -8.136  1.00 29.55 ? 123 ILE   F CD1 1 
ATOM   7361  N  N   . LEU   F  1 124 ? -21.754 -60.358  -9.828  1.00 26.23 ? 124 LEU   F N   1 
ATOM   7362  C  CA  . LEU   F  1 124 ? -23.130 -60.851  -9.786  1.00 26.49 ? 124 LEU   F CA  1 
ATOM   7363  C  C   . LEU   F  1 124 ? -23.787 -60.769  -11.161 1.00 28.71 ? 124 LEU   F C   1 
ATOM   7364  O  O   . LEU   F  1 124 ? -24.520 -61.680  -11.569 1.00 25.19 ? 124 LEU   F O   1 
ATOM   7365  C  CB  . LEU   F  1 124 ? -23.930 -60.058  -8.746  1.00 25.56 ? 124 LEU   F CB  1 
ATOM   7366  C  CG  . LEU   F  1 124 ? -25.433 -60.376  -8.610  1.00 25.25 ? 124 LEU   F CG  1 
ATOM   7367  C  CD1 . LEU   F  1 124 ? -25.674 -61.801  -8.106  1.00 30.02 ? 124 LEU   F CD1 1 
ATOM   7368  C  CD2 . LEU   F  1 124 ? -26.106 -59.391  -7.686  1.00 25.19 ? 124 LEU   F CD2 1 
ATOM   7369  N  N   . GLU   F  1 125 ? -23.518 -59.695  -11.900 1.00 33.26 ? 125 GLU   F N   1 
ATOM   7370  C  CA  . GLU   F  1 125 ? -24.020 -59.599  -13.265 1.00 28.82 ? 125 GLU   F CA  1 
ATOM   7371  C  C   . GLU   F  1 125 ? -23.498 -60.752  -14.115 1.00 26.79 ? 125 GLU   F C   1 
ATOM   7372  O  O   . GLU   F  1 125 ? -24.256 -61.387  -14.854 1.00 28.86 ? 125 GLU   F O   1 
ATOM   7373  C  CB  . GLU   F  1 125 ? -23.651 -58.234  -13.858 1.00 28.89 ? 125 GLU   F CB  1 
ATOM   7374  C  CG  . GLU   F  1 125 ? -24.547 -57.143  -13.308 1.00 30.88 ? 125 GLU   F CG  1 
ATOM   7375  C  CD  . GLU   F  1 125 ? -24.177 -55.710  -13.690 1.00 45.23 ? 125 GLU   F CD  1 
ATOM   7376  O  OE1 . GLU   F  1 125 ? -23.046 -55.457  -14.170 1.00 38.20 ? 125 GLU   F OE1 1 
ATOM   7377  O  OE2 . GLU   F  1 125 ? -25.044 -54.825  -13.466 1.00 37.21 ? 125 GLU   F OE2 1 
ATOM   7378  N  N   . SER   F  1 126 ? -22.211 -61.062  -13.992 1.00 27.77 ? 126 SER   F N   1 
ATOM   7379  C  CA  A SER   F  1 126 ? -21.647 -62.182  -14.737 0.50 28.98 ? 126 SER   F CA  1 
ATOM   7380  C  CA  B SER   F  1 126 ? -21.652 -62.183  -14.739 0.50 28.98 ? 126 SER   F CA  1 
ATOM   7381  C  C   . SER   F  1 126 ? -22.291 -63.498  -14.325 1.00 28.86 ? 126 SER   F C   1 
ATOM   7382  O  O   . SER   F  1 126 ? -22.578 -64.349  -15.177 1.00 30.23 ? 126 SER   F O   1 
ATOM   7383  C  CB  A SER   F  1 126 ? -20.137 -62.244  -14.525 0.50 29.30 ? 126 SER   F CB  1 
ATOM   7384  C  CB  B SER   F  1 126 ? -20.143 -62.246  -14.537 0.50 29.29 ? 126 SER   F CB  1 
ATOM   7385  O  OG  A SER   F  1 126 ? -19.617 -63.470  -14.996 0.50 30.55 ? 126 SER   F OG  1 
ATOM   7386  O  OG  B SER   F  1 126 ? -19.525 -61.172  -15.206 0.50 36.38 ? 126 SER   F OG  1 
ATOM   7387  N  N   . GLU   F  1 127 ? -22.520 -63.690  -13.017 1.00 27.20 ? 127 GLU   F N   1 
ATOM   7388  C  CA  . GLU   F  1 127 ? -23.093 -64.958  -12.566 1.00 25.95 ? 127 GLU   F CA  1 
ATOM   7389  C  C   . GLU   F  1 127 ? -24.552 -65.093  -13.022 1.00 27.69 ? 127 GLU   F C   1 
ATOM   7390  O  O   . GLU   F  1 127 ? -24.995 -66.192  -13.374 1.00 27.76 ? 127 GLU   F O   1 
ATOM   7391  C  CB  . GLU   F  1 127 ? -22.974 -65.094  -11.047 1.00 26.55 ? 127 GLU   F CB  1 
ATOM   7392  C  CG  . GLU   F  1 127 ? -21.532 -65.110  -10.468 1.00 31.25 ? 127 GLU   F CG  1 
ATOM   7393  C  CD  . GLU   F  1 127 ? -20.556 -66.005  -11.258 1.00 39.23 ? 127 GLU   F CD  1 
ATOM   7394  O  OE1 . GLU   F  1 127 ? -20.956 -67.074  -11.759 1.00 35.86 ? 127 GLU   F OE1 1 
ATOM   7395  O  OE2 . GLU   F  1 127 ? -19.374 -65.630  -11.386 1.00 46.46 ? 127 GLU   F OE2 1 
ATOM   7396  N  N   . GLU   F  1 128 ? -25.304 -63.988  -13.066 1.00 29.94 ? 128 GLU   F N   1 
ATOM   7397  C  CA  . GLU   F  1 128 ? -26.673 -64.073  -13.559 1.00 31.38 ? 128 GLU   F CA  1 
ATOM   7398  C  C   . GLU   F  1 128 ? -26.716 -64.374  -15.051 1.00 32.28 ? 128 GLU   F C   1 
ATOM   7399  O  O   . GLU   F  1 128 ? -27.643 -65.056  -15.518 1.00 29.21 ? 128 GLU   F O   1 
ATOM   7400  C  CB  . GLU   F  1 128 ? -27.445 -62.787  -13.237 1.00 28.29 ? 128 GLU   F CB  1 
ATOM   7401  C  CG  . GLU   F  1 128 ? -27.762 -62.642  -11.736 1.00 31.27 ? 128 GLU   F CG  1 
ATOM   7402  C  CD  . GLU   F  1 128 ? -28.838 -61.604  -11.425 1.00 31.27 ? 128 GLU   F CD  1 
ATOM   7403  O  OE1 . GLU   F  1 128 ? -29.380 -60.985  -12.366 1.00 32.61 ? 128 GLU   F OE1 1 
ATOM   7404  O  OE2 . GLU   F  1 128 ? -29.122 -61.374  -10.221 1.00 30.30 ? 128 GLU   F OE2 1 
ATOM   7405  N  N   . GLU   F  1 129 ? -25.729 -63.897  -15.820 1.00 33.02 ? 129 GLU   F N   1 
ATOM   7406  C  CA  . GLU   F  1 129 ? -25.656 -64.292  -17.225 1.00 30.18 ? 129 GLU   F CA  1 
ATOM   7407  C  C   . GLU   F  1 129 ? -25.369 -65.792  -17.355 1.00 30.07 ? 129 GLU   F C   1 
ATOM   7408  O  O   . GLU   F  1 129 ? -25.940 -66.463  -18.225 1.00 28.42 ? 129 GLU   F O   1 
ATOM   7409  C  CB  . GLU   F  1 129 ? -24.609 -63.442  -17.976 1.00 29.21 ? 129 GLU   F CB  1 
ATOM   7410  C  CG  . GLU   F  1 129 ? -24.554 -63.691  -19.467 1.00 45.26 ? 129 GLU   F CG  1 
ATOM   7411  N  N   . HIS   F  1 130 ? -24.534 -66.353  -16.469 1.00 27.06 ? 130 HIS   F N   1 
ATOM   7412  C  CA  A HIS   F  1 130 ? -24.290 -67.792  -16.533 0.50 31.50 ? 130 HIS   F CA  1 
ATOM   7413  C  CA  B HIS   F  1 130 ? -24.275 -67.796  -16.492 0.50 31.51 ? 130 HIS   F CA  1 
ATOM   7414  C  C   . HIS   F  1 130 ? -25.552 -68.577  -16.173 1.00 32.53 ? 130 HIS   F C   1 
ATOM   7415  O  O   . HIS   F  1 130 ? -25.853 -69.598  -16.803 1.00 29.81 ? 130 HIS   F O   1 
ATOM   7416  C  CB  A HIS   F  1 130 ? -23.126 -68.176  -15.614 0.50 30.59 ? 130 HIS   F CB  1 
ATOM   7417  C  CB  B HIS   F  1 130 ? -23.190 -68.190  -15.473 0.50 30.72 ? 130 HIS   F CB  1 
ATOM   7418  C  CG  A HIS   F  1 130 ? -22.571 -69.542  -15.876 0.50 34.75 ? 130 HIS   F CG  1 
ATOM   7419  C  CG  B HIS   F  1 130 ? -21.835 -67.583  -15.697 0.50 30.83 ? 130 HIS   F CG  1 
ATOM   7420  N  ND1 A HIS   F  1 130 ? -21.654 -70.146  -15.041 0.50 34.91 ? 130 HIS   F ND1 1 
ATOM   7421  N  ND1 B HIS   F  1 130 ? -21.508 -66.819  -16.799 0.50 34.29 ? 130 HIS   F ND1 1 
ATOM   7422  C  CD2 A HIS   F  1 130 ? -22.780 -70.413  -16.893 0.50 37.87 ? 130 HIS   F CD2 1 
ATOM   7423  C  CD2 B HIS   F  1 130 ? -20.712 -67.645  -14.939 0.50 36.07 ? 130 HIS   F CD2 1 
ATOM   7424  C  CE1 A HIS   F  1 130 ? -21.333 -71.333  -15.526 0.50 31.18 ? 130 HIS   F CE1 1 
ATOM   7425  C  CE1 B HIS   F  1 130 ? -20.248 -66.426  -16.702 0.50 26.27 ? 130 HIS   F CE1 1 
ATOM   7426  N  NE2 A HIS   F  1 130 ? -21.996 -71.515  -16.653 0.50 38.26 ? 130 HIS   F NE2 1 
ATOM   7427  N  NE2 B HIS   F  1 130 ? -19.738 -66.924  -15.590 0.50 30.51 ? 130 HIS   F NE2 1 
ATOM   7428  N  N   . ILE   F  1 131 ? -26.296 -68.127  -15.165 1.00 27.72 ? 131 ILE   F N   1 
ATOM   7429  C  CA  . ILE   F  1 131 ? -27.548 -68.788  -14.801 1.00 28.01 ? 131 ILE   F CA  1 
ATOM   7430  C  C   . ILE   F  1 131 ? -28.515 -68.768  -15.971 1.00 33.26 ? 131 ILE   F C   1 
ATOM   7431  O  O   . ILE   F  1 131 ? -29.151 -69.778  -16.288 1.00 34.88 ? 131 ILE   F O   1 
ATOM   7432  C  CB  . ILE   F  1 131 ? -28.163 -68.117  -13.563 1.00 28.81 ? 131 ILE   F CB  1 
ATOM   7433  C  CG1 . ILE   F  1 131 ? -27.327 -68.457  -12.332 1.00 28.31 ? 131 ILE   F CG1 1 
ATOM   7434  C  CG2 . ILE   F  1 131 ? -29.673 -68.503  -13.426 1.00 29.95 ? 131 ILE   F CG2 1 
ATOM   7435  C  CD1 . ILE   F  1 131 ? -27.587 -67.510  -11.164 1.00 34.27 ? 131 ILE   F CD1 1 
ATOM   7436  N  N   . ASP   F  1 132 ? -28.666 -67.606  -16.610 1.00 27.84 ? 132 ASP   F N   1 
ATOM   7437  C  CA  . ASP   F  1 132 ? -29.499 -67.510  -17.811 1.00 30.79 ? 132 ASP   F CA  1 
ATOM   7438  C  C   . ASP   F  1 132 ? -29.107 -68.571  -18.828 1.00 31.14 ? 132 ASP   F C   1 
ATOM   7439  O  O   . ASP   F  1 132 ? -29.952 -69.326  -19.323 1.00 34.24 ? 132 ASP   F O   1 
ATOM   7440  C  CB  . ASP   F  1 132 ? -29.364 -66.112  -18.410 1.00 30.60 ? 132 ASP   F CB  1 
ATOM   7441  C  CG  . ASP   F  1 132 ? -30.400 -65.804  -19.478 1.00 37.88 ? 132 ASP   F CG  1 
ATOM   7442  O  OD1 . ASP   F  1 132 ? -31.393 -66.537  -19.639 1.00 42.08 ? 132 ASP   F OD1 1 
ATOM   7443  O  OD2 . ASP   F  1 132 ? -30.212 -64.789  -20.165 1.00 41.06 ? 132 ASP   F OD2 1 
ATOM   7444  N  N   . TYR   F  1 133 ? -27.814 -68.670  -19.113 1.00 30.16 ? 133 TYR   F N   1 
ATOM   7445  C  CA  . TYR   F  1 133 ? -27.324 -69.666  -20.055 1.00 36.63 ? 133 TYR   F CA  1 
ATOM   7446  C  C   . TYR   F  1 133 ? -27.674 -71.081  -19.606 1.00 37.89 ? 133 TYR   F C   1 
ATOM   7447  O  O   . TYR   F  1 133 ? -28.171 -71.885  -20.396 1.00 31.56 ? 133 TYR   F O   1 
ATOM   7448  C  CB  . TYR   F  1 133 ? -25.807 -69.511  -20.220 1.00 29.59 ? 133 TYR   F CB  1 
ATOM   7449  C  CG  . TYR   F  1 133 ? -25.146 -70.683  -20.895 1.00 33.22 ? 133 TYR   F CG  1 
ATOM   7450  C  CD1 . TYR   F  1 133 ? -25.131 -70.793  -22.270 1.00 32.30 ? 133 TYR   F CD1 1 
ATOM   7451  C  CD2 . TYR   F  1 133 ? -24.539 -71.689  -20.147 1.00 32.52 ? 133 TYR   F CD2 1 
ATOM   7452  C  CE1 . TYR   F  1 133 ? -24.537 -71.872  -22.886 1.00 33.69 ? 133 TYR   F CE1 1 
ATOM   7453  C  CE2 . TYR   F  1 133 ? -23.956 -72.759  -20.751 1.00 35.68 ? 133 TYR   F CE2 1 
ATOM   7454  C  CZ  . TYR   F  1 133 ? -23.951 -72.844  -22.124 1.00 33.31 ? 133 TYR   F CZ  1 
ATOM   7455  O  OH  . TYR   F  1 133 ? -23.332 -73.910  -22.743 1.00 43.88 ? 133 TYR   F OH  1 
ATOM   7456  N  N   . LEU   F  1 134 ? -27.385 -71.418  -18.343 1.00 30.58 ? 134 LEU   F N   1 
ATOM   7457  C  CA  . LEU   F  1 134 ? -27.641 -72.776  -17.862 1.00 30.68 ? 134 LEU   F CA  1 
ATOM   7458  C  C   . LEU   F  1 134 ? -29.122 -73.112  -17.915 1.00 27.14 ? 134 LEU   F C   1 
ATOM   7459  O  O   . LEU   F  1 134 ? -29.516 -74.178  -18.397 1.00 37.10 ? 134 LEU   F O   1 
ATOM   7460  C  CB  . LEU   F  1 134 ? -27.123 -72.930  -16.427 1.00 29.99 ? 134 LEU   F CB  1 
ATOM   7461  C  CG  . LEU   F  1 134 ? -25.622 -72.899  -16.311 1.00 32.78 ? 134 LEU   F CG  1 
ATOM   7462  C  CD1 . LEU   F  1 134 ? -25.252 -72.622  -14.866 1.00 31.17 ? 134 LEU   F CD1 1 
ATOM   7463  C  CD2 . LEU   F  1 134 ? -25.078 -74.224  -16.794 1.00 33.97 ? 134 LEU   F CD2 1 
ATOM   7464  N  N   . GLU   F  1 135 ? -29.964 -72.205  -17.422 1.00 31.42 ? 135 GLU   F N   1 
ATOM   7465  C  CA  . GLU   F  1 135 ? -31.400 -72.444  -17.454 1.00 33.54 ? 135 GLU   F CA  1 
ATOM   7466  C  C   . GLU   F  1 135 ? -31.859 -72.638  -18.887 1.00 34.30 ? 135 GLU   F C   1 
ATOM   7467  O  O   . GLU   F  1 135 ? -32.721 -73.474  -19.176 1.00 32.20 ? 135 GLU   F O   1 
ATOM   7468  C  CB  . GLU   F  1 135 ? -32.139 -71.273  -16.807 1.00 33.49 ? 135 GLU   F CB  1 
ATOM   7469  C  CG  . GLU   F  1 135 ? -32.020 -71.190  -15.307 1.00 29.78 ? 135 GLU   F CG  1 
ATOM   7470  C  CD  . GLU   F  1 135 ? -32.707 -69.957  -14.748 1.00 36.09 ? 135 GLU   F CD  1 
ATOM   7471  O  OE1 . GLU   F  1 135 ? -32.874 -68.967  -15.495 1.00 32.59 ? 135 GLU   F OE1 1 
ATOM   7472  O  OE2 . GLU   F  1 135 ? -33.115 -69.978  -13.568 1.00 37.26 ? 135 GLU   F OE2 1 
ATOM   7473  N  N   . THR   F  1 136 ? -31.281 -71.872  -19.796 1.00 28.12 ? 136 THR   F N   1 
ATOM   7474  C  CA  . THR   F  1 136 ? -31.646 -71.970  -21.195 1.00 29.70 ? 136 THR   F CA  1 
ATOM   7475  C  C   . THR   F  1 136 ? -31.239 -73.314  -21.782 1.00 34.34 ? 136 THR   F C   1 
ATOM   7476  O  O   . THR   F  1 136 ? -32.003 -73.911  -22.556 1.00 34.02 ? 136 THR   F O   1 
ATOM   7477  C  CB  . THR   F  1 136 ? -31.020 -70.812  -21.961 1.00 37.09 ? 136 THR   F CB  1 
ATOM   7478  O  OG1 . THR   F  1 136 ? -31.554 -69.582  -21.458 1.00 34.41 ? 136 THR   F OG1 1 
ATOM   7479  C  CG2 . THR   F  1 136 ? -31.330 -70.919  -23.461 1.00 36.31 ? 136 THR   F CG2 1 
ATOM   7480  N  N   . GLN   F  1 137 ? -30.033 -73.790  -21.454 1.00 31.51 ? 137 GLN   F N   1 
ATOM   7481  C  CA  . GLN   F  1 137 ? -29.597 -75.093  -21.951 1.00 35.34 ? 137 GLN   F CA  1 
ATOM   7482  C  C   . GLN   F  1 137 ? -30.520 -76.201  -21.459 1.00 37.65 ? 137 GLN   F C   1 
ATOM   7483  O  O   . GLN   F  1 137 ? -30.852 -77.124  -22.209 1.00 31.88 ? 137 GLN   F O   1 
ATOM   7484  C  CB  . GLN   F  1 137 ? -28.164 -75.396  -21.507 1.00 27.77 ? 137 GLN   F CB  1 
ATOM   7485  C  CG  . GLN   F  1 137 ? -27.055 -74.461  -22.039 1.00 31.29 ? 137 GLN   F CG  1 
ATOM   7486  C  CD  . GLN   F  1 137 ? -27.357 -73.930  -23.427 1.00 32.25 ? 137 GLN   F CD  1 
ATOM   7487  O  OE1 . GLN   F  1 137 ? -27.808 -72.803  -23.580 1.00 40.54 ? 137 GLN   F OE1 1 
ATOM   7488  N  NE2 . GLN   F  1 137 ? -27.141 -74.753  -24.431 1.00 26.74 ? 137 GLN   F NE2 1 
ATOM   7489  N  N   . LEU   F  1 138 ? -30.896 -76.159  -20.181 1.00 32.59 ? 138 LEU   F N   1 
ATOM   7490  C  CA  . LEU   F  1 138 ? -31.775 -77.193  -19.635 1.00 36.59 ? 138 LEU   F CA  1 
ATOM   7491  C  C   . LEU   F  1 138 ? -33.154 -77.153  -20.288 1.00 35.62 ? 138 LEU   F C   1 
ATOM   7492  O  O   . LEU   F  1 138 ? -33.753 -78.200  -20.555 1.00 36.23 ? 138 LEU   F O   1 
ATOM   7493  C  CB  . LEU   F  1 138 ? -31.885 -77.032  -18.113 1.00 34.58 ? 138 LEU   F CB  1 
ATOM   7494  C  CG  . LEU   F  1 138 ? -30.580 -77.415  -17.412 1.00 38.51 ? 138 LEU   F CG  1 
ATOM   7495  C  CD1 . LEU   F  1 138 ? -30.486 -76.843  -16.034 1.00 35.08 ? 138 LEU   F CD1 1 
ATOM   7496  C  CD2 . LEU   F  1 138 ? -30.426 -78.933  -17.368 1.00 36.60 ? 138 LEU   F CD2 1 
ATOM   7497  N  N   . GLY   F  1 139 ? -33.668 -75.955  -20.562 1.00 31.02 ? 139 GLY   F N   1 
ATOM   7498  C  CA  . GLY   F  1 139 ? -34.901 -75.850  -21.314 1.00 35.38 ? 139 GLY   F CA  1 
ATOM   7499  C  C   . GLY   F  1 139 ? -34.765 -76.388  -22.722 1.00 37.53 ? 139 GLY   F C   1 
ATOM   7500  O  O   . GLY   F  1 139 ? -35.670 -77.057  -23.230 1.00 34.41 ? 139 GLY   F O   1 
ATOM   7501  N  N   . LEU   F  1 140 ? -33.630 -76.117  -23.372 1.00 35.29 ? 140 LEU   F N   1 
ATOM   7502  C  CA  . LEU   F  1 140 ? -33.473 -76.571  -24.748 1.00 35.20 ? 140 LEU   F CA  1 
ATOM   7503  C  C   . LEU   F  1 140 ? -33.485 -78.092  -24.822 1.00 34.62 ? 140 LEU   F C   1 
ATOM   7504  O  O   . LEU   F  1 140 ? -34.042 -78.667  -25.765 1.00 36.62 ? 140 LEU   F O   1 
ATOM   7505  C  CB  . LEU   F  1 140 ? -32.187 -76.006  -25.352 1.00 31.99 ? 140 LEU   F CB  1 
ATOM   7506  C  CG  . LEU   F  1 140 ? -32.277 -74.547  -25.833 1.00 33.53 ? 140 LEU   F CG  1 
ATOM   7507  C  CD1 . LEU   F  1 140 ? -30.890 -73.993  -26.219 1.00 35.82 ? 140 LEU   F CD1 1 
ATOM   7508  C  CD2 . LEU   F  1 140 ? -33.201 -74.461  -27.022 1.00 31.36 ? 140 LEU   F CD2 1 
ATOM   7509  N  N   . ILE   F  1 141 ? -32.885 -78.764  -23.834 1.00 33.61 ? 141 ILE   F N   1 
ATOM   7510  C  CA  . ILE   F  1 141 ? -32.928 -80.227  -23.818 1.00 36.71 ? 141 ILE   F CA  1 
ATOM   7511  C  C   . ILE   F  1 141 ? -34.373 -80.713  -23.887 1.00 38.71 ? 141 ILE   F C   1 
ATOM   7512  O  O   . ILE   F  1 141 ? -34.690 -81.675  -24.608 1.00 33.31 ? 141 ILE   F O   1 
ATOM   7513  C  CB  . ILE   F  1 141 ? -32.203 -80.776  -22.580 1.00 30.91 ? 141 ILE   F CB  1 
ATOM   7514  C  CG1 . ILE   F  1 141 ? -30.697 -80.703  -22.761 1.00 32.32 ? 141 ILE   F CG1 1 
ATOM   7515  C  CG2 . ILE   F  1 141 ? -32.610 -82.235  -22.324 1.00 35.68 ? 141 ILE   F CG2 1 
ATOM   7516  C  CD1 . ILE   F  1 141 ? -29.922 -80.865  -21.469 1.00 32.01 ? 141 ILE   F CD1 1 
ATOM   7517  N  N   . GLN   F  1 142 ? -35.280 -80.031  -23.180 1.00 37.54 ? 142 GLN   F N   1 
ATOM   7518  C  CA  . GLN   F  1 142 ? -36.677 -80.460  -23.185 1.00 41.84 ? 142 GLN   F CA  1 
ATOM   7519  C  C   . GLN   F  1 142 ? -37.373 -80.130  -24.506 1.00 50.24 ? 142 GLN   F C   1 
ATOM   7520  O  O   . GLN   F  1 142 ? -38.235 -80.897  -24.959 1.00 41.06 ? 142 GLN   F O   1 
ATOM   7521  C  CB  . GLN   F  1 142 ? -37.439 -79.816  -22.023 1.00 40.25 ? 142 GLN   F CB  1 
ATOM   7522  C  CG  . GLN   F  1 142 ? -36.935 -80.206  -20.640 1.00 42.29 ? 142 GLN   F CG  1 
ATOM   7523  C  CD  . GLN   F  1 142 ? -36.961 -81.713  -20.408 1.00 51.49 ? 142 GLN   F CD  1 
ATOM   7524  O  OE1 . GLN   F  1 142 ? -37.910 -82.393  -20.800 1.00 52.86 ? 142 GLN   F OE1 1 
ATOM   7525  N  NE2 . GLN   F  1 142 ? -35.903 -82.242  -19.788 1.00 43.56 ? 142 GLN   F NE2 1 
ATOM   7526  N  N   . LYS   F  1 143 ? -37.024 -79.000  -25.131 1.00 36.13 ? 143 LYS   F N   1 
ATOM   7527  C  CA  . LYS   F  1 143 ? -37.714 -78.566  -26.341 1.00 45.09 ? 143 LYS   F CA  1 
ATOM   7528  C  C   . LYS   F  1 143 ? -37.234 -79.317  -27.587 1.00 41.64 ? 143 LYS   F C   1 
ATOM   7529  O  O   . LYS   F  1 143 ? -38.051 -79.669  -28.442 1.00 41.40 ? 143 LYS   F O   1 
ATOM   7530  C  CB  . LYS   F  1 143 ? -37.545 -77.051  -26.530 1.00 49.64 ? 143 LYS   F CB  1 
ATOM   7531  C  CG  . LYS   F  1 143 ? -38.461 -76.161  -25.647 1.00 50.69 ? 143 LYS   F CG  1 
ATOM   7532  C  CD  . LYS   F  1 143 ? -38.010 -74.690  -25.693 1.00 53.37 ? 143 LYS   F CD  1 
ATOM   7533  C  CE  . LYS   F  1 143 ? -39.011 -73.715  -25.040 1.00 57.74 ? 143 LYS   F CE  1 
ATOM   7534  N  NZ  . LYS   F  1 143 ? -38.818 -73.447  -23.571 1.00 58.09 ? 143 LYS   F NZ  1 
ATOM   7535  N  N   . VAL   F  1 144 ? -35.928 -79.573  -27.729 1.00 34.59 ? 144 VAL   F N   1 
ATOM   7536  C  CA  . VAL   F  1 144 ? -35.430 -80.223  -28.938 1.00 37.06 ? 144 VAL   F CA  1 
ATOM   7537  C  C   . VAL   F  1 144 ? -35.096 -81.692  -28.716 1.00 39.41 ? 144 VAL   F C   1 
ATOM   7538  O  O   . VAL   F  1 144 ? -34.823 -82.407  -29.697 1.00 36.91 ? 144 VAL   F O   1 
ATOM   7539  C  CB  . VAL   F  1 144 ? -34.209 -79.466  -29.510 1.00 35.20 ? 144 VAL   F CB  1 
ATOM   7540  C  CG1 . VAL   F  1 144 ? -34.521 -77.993  -29.574 1.00 35.86 ? 144 VAL   F CG1 1 
ATOM   7541  C  CG2 . VAL   F  1 144 ? -32.955 -79.738  -28.693 1.00 27.44 ? 144 VAL   F CG2 1 
ATOM   7542  N  N   . GLY   F  1 145 ? -35.152 -82.177  -27.479 1.00 32.23 ? 145 GLY   F N   1 
ATOM   7543  C  CA  . GLY   F  1 145 ? -34.697 -83.537  -27.217 1.00 38.56 ? 145 GLY   F CA  1 
ATOM   7544  C  C   . GLY   F  1 145 ? -33.207 -83.615  -26.945 1.00 43.17 ? 145 GLY   F C   1 
ATOM   7545  O  O   . GLY   F  1 145 ? -32.396 -82.876  -27.515 1.00 39.31 ? 145 GLY   F O   1 
ATOM   7546  N  N   . LEU   F  1 146 ? -32.830 -84.549  -26.055 1.00 35.25 ? 146 LEU   F N   1 
ATOM   7547  C  CA  . LEU   F  1 146 ? -31.433 -84.642  -25.637 1.00 36.77 ? 146 LEU   F CA  1 
ATOM   7548  C  C   . LEU   F  1 146 ? -30.510 -84.982  -26.802 1.00 37.63 ? 146 LEU   F C   1 
ATOM   7549  O  O   . LEU   F  1 146 ? -29.406 -84.434  -26.902 1.00 31.17 ? 146 LEU   F O   1 
ATOM   7550  C  CB  . LEU   F  1 146 ? -31.263 -85.681  -24.528 1.00 33.37 ? 146 LEU   F CB  1 
ATOM   7551  C  CG  . LEU   F  1 146 ? -29.820 -85.848  -24.004 1.00 44.49 ? 146 LEU   F CG  1 
ATOM   7552  C  CD1 . LEU   F  1 146 ? -29.295 -84.590  -23.297 1.00 43.89 ? 146 LEU   F CD1 1 
ATOM   7553  C  CD2 . LEU   F  1 146 ? -29.738 -87.030  -23.065 1.00 48.07 ? 146 LEU   F CD2 1 
ATOM   7554  N  N   . GLU   F  1 147 ? -30.909 -85.924  -27.661 1.00 31.38 ? 147 GLU   F N   1 
ATOM   7555  C  CA  . GLU   F  1 147 ? -30.041 -86.313  -28.768 1.00 29.25 ? 147 GLU   F CA  1 
ATOM   7556  C  C   . GLU   F  1 147 ? -29.791 -85.139  -29.725 1.00 29.80 ? 147 GLU   F C   1 
ATOM   7557  O  O   . GLU   F  1 147 ? -28.651 -84.913  -30.151 1.00 35.06 ? 147 GLU   F O   1 
ATOM   7558  C  CB  . GLU   F  1 147 ? -30.631 -87.515  -29.505 1.00 37.50 ? 147 GLU   F CB  1 
ATOM   7559  C  CG  . GLU   F  1 147 ? -30.413 -88.856  -28.752 1.00 32.65 ? 147 GLU   F CG  1 
ATOM   7560  N  N   . ASN   F  1 148 ? -30.842 -84.394  -30.092 1.00 32.15 ? 148 ASN   F N   1 
ATOM   7561  C  CA  . ASN   F  1 148 ? -30.629 -83.175  -30.880 1.00 35.00 ? 148 ASN   F CA  1 
ATOM   7562  C  C   . ASN   F  1 148 ? -29.761 -82.182  -30.112 1.00 38.42 ? 148 ASN   F C   1 
ATOM   7563  O  O   . ASN   F  1 148 ? -28.835 -81.586  -30.687 1.00 33.36 ? 148 ASN   F O   1 
ATOM   7564  C  CB  . ASN   F  1 148 ? -31.960 -82.524  -31.264 1.00 32.41 ? 148 ASN   F CB  1 
ATOM   7565  C  CG  . ASN   F  1 148 ? -32.571 -83.136  -32.518 1.00 34.27 ? 148 ASN   F CG  1 
ATOM   7566  O  OD1 . ASN   F  1 148 ? -32.012 -84.056  -33.113 1.00 30.76 ? 148 ASN   F OD1 1 
ATOM   7567  N  ND2 . ASN   F  1 148 ? -33.690 -82.601  -32.931 1.00 29.59 ? 148 ASN   F ND2 1 
ATOM   7568  N  N   . TYR   F  1 149 ? -30.041 -82.002  -28.807 1.00 35.43 ? 149 TYR   F N   1 
ATOM   7569  C  CA  . TYR   F  1 149 ? -29.258 -81.071  -27.989 1.00 31.79 ? 149 TYR   F CA  1 
ATOM   7570  C  C   . TYR   F  1 149 ? -27.771 -81.423  -28.011 1.00 33.31 ? 149 TYR   F C   1 
ATOM   7571  O  O   . TYR   F  1 149 ? -26.921 -80.561  -28.271 1.00 35.26 ? 149 TYR   F O   1 
ATOM   7572  C  CB  . TYR   F  1 149 ? -29.791 -81.008  -26.546 1.00 36.56 ? 149 TYR   F CB  1 
ATOM   7573  C  CG  . TYR   F  1 149 ? -28.978 -80.017  -25.740 1.00 36.60 ? 149 TYR   F CG  1 
ATOM   7574  C  CD1 . TYR   F  1 149 ? -29.274 -78.665  -25.769 1.00 32.78 ? 149 TYR   F CD1 1 
ATOM   7575  C  CD2 . TYR   F  1 149 ? -27.863 -80.424  -25.024 1.00 33.56 ? 149 TYR   F CD2 1 
ATOM   7576  C  CE1 . TYR   F  1 149 ? -28.482 -77.743  -25.087 1.00 29.80 ? 149 TYR   F CE1 1 
ATOM   7577  C  CE2 . TYR   F  1 149 ? -27.079 -79.503  -24.319 1.00 38.02 ? 149 TYR   F CE2 1 
ATOM   7578  C  CZ  . TYR   F  1 149 ? -27.400 -78.170  -24.356 1.00 36.44 ? 149 TYR   F CZ  1 
ATOM   7579  O  OH  . TYR   F  1 149 ? -26.614 -77.241  -23.689 1.00 40.94 ? 149 TYR   F OH  1 
ATOM   7580  N  N   . LEU   F  1 150 ? -27.430 -82.688  -27.755 1.00 28.00 ? 150 LEU   F N   1 
ATOM   7581  C  CA  . LEU   F  1 150 ? -26.039 -83.083  -27.802 1.00 30.50 ? 150 LEU   F CA  1 
ATOM   7582  C  C   . LEU   F  1 150 ? -25.465 -82.952  -29.214 1.00 35.18 ? 150 LEU   F C   1 
ATOM   7583  O  O   . LEU   F  1 150 ? -24.324 -82.509  -29.383 1.00 32.97 ? 150 LEU   F O   1 
ATOM   7584  C  CB  . LEU   F  1 150 ? -25.894 -84.505  -27.276 1.00 33.00 ? 150 LEU   F CB  1 
ATOM   7585  C  CG  . LEU   F  1 150 ? -26.405 -84.626  -25.825 1.00 44.33 ? 150 LEU   F CG  1 
ATOM   7586  C  CD1 . LEU   F  1 150 ? -26.440 -86.079  -25.359 1.00 42.04 ? 150 LEU   F CD1 1 
ATOM   7587  C  CD2 . LEU   F  1 150 ? -25.590 -83.777  -24.831 1.00 40.97 ? 150 LEU   F CD2 1 
ATOM   7588  N  N   . GLN   F  1 151 ? -26.232 -83.343  -30.235 1.00 27.35 ? 151 GLN   F N   1 
ATOM   7589  C  CA  . GLN   F  1 151 ? -25.772 -83.199  -31.613 1.00 28.82 ? 151 GLN   F CA  1 
ATOM   7590  C  C   . GLN   F  1 151 ? -25.347 -81.756  -31.889 1.00 31.76 ? 151 GLN   F C   1 
ATOM   7591  O  O   . GLN   F  1 151 ? -24.291 -81.504  -32.475 1.00 33.40 ? 151 GLN   F O   1 
ATOM   7592  C  CB  . GLN   F  1 151 ? -26.877 -83.627  -32.578 1.00 34.42 ? 151 GLN   F CB  1 
ATOM   7593  C  CG  . GLN   F  1 151 ? -26.496 -83.513  -34.049 1.00 35.31 ? 151 GLN   F CG  1 
ATOM   7594  C  CD  . GLN   F  1 151 ? -27.683 -83.689  -34.988 1.00 28.00 ? 151 GLN   F CD  1 
ATOM   7595  O  OE1 . GLN   F  1 151 ? -28.835 -83.422  -34.642 1.00 32.78 ? 151 GLN   F OE1 1 
ATOM   7596  N  NE2 . GLN   F  1 151 ? -27.394 -84.130  -36.197 1.00 28.35 ? 151 GLN   F NE2 1 
ATOM   7597  N  N   . SER   F  1 152 ? -26.168 -80.798  -31.458 1.00 28.58 ? 152 SER   F N   1 
ATOM   7598  C  CA  . SER   F  1 152 ? -25.921 -79.380  -31.662 1.00 35.42 ? 152 SER   F CA  1 
ATOM   7599  C  C   . SER   F  1 152 ? -24.731 -78.847  -30.874 1.00 36.93 ? 152 SER   F C   1 
ATOM   7600  O  O   . SER   F  1 152 ? -24.368 -77.680  -31.072 1.00 38.41 ? 152 SER   F O   1 
ATOM   7601  C  CB  . SER   F  1 152 ? -27.167 -78.590  -31.283 1.00 32.23 ? 152 SER   F CB  1 
ATOM   7602  O  OG  . SER   F  1 152 ? -28.193 -78.784  -32.236 1.00 33.70 ? 152 SER   F OG  1 
ATOM   7603  N  N   . HIS   F  1 153 ? -24.116 -79.650  -30.001 1.00 32.01 ? 153 HIS   F N   1 
ATOM   7604  C  CA  . HIS   F  1 153 ? -22.954 -79.200  -29.236 1.00 31.41 ? 153 HIS   F CA  1 
ATOM   7605  C  C   . HIS   F  1 153 ? -21.729 -80.049  -29.506 1.00 32.18 ? 153 HIS   F C   1 
ATOM   7606  O  O   . HIS   F  1 153 ? -20.746 -79.973  -28.760 1.00 34.10 ? 153 HIS   F O   1 
ATOM   7607  C  CB  . HIS   F  1 153 ? -23.301 -79.140  -27.744 1.00 33.85 ? 153 HIS   F CB  1 
ATOM   7608  C  CG  . HIS   F  1 153 ? -24.223 -78.011  -27.435 1.00 35.49 ? 153 HIS   F CG  1 
ATOM   7609  N  ND1 . HIS   F  1 153 ? -25.576 -78.073  -27.683 1.00 32.73 ? 153 HIS   F ND1 1 
ATOM   7610  C  CD2 . HIS   F  1 153 ? -23.973 -76.751  -27.013 1.00 32.76 ? 153 HIS   F CD2 1 
ATOM   7611  C  CE1 . HIS   F  1 153 ? -26.128 -76.910  -27.381 1.00 36.37 ? 153 HIS   F CE1 1 
ATOM   7612  N  NE2 . HIS   F  1 153 ? -25.173 -76.086  -26.990 1.00 32.33 ? 153 HIS   F NE2 1 
ATOM   7613  N  N   . MET   F  1 154 ? -21.744 -80.809  -30.607 1.00 32.73 ? 154 MET   F N   1 
ATOM   7614  C  CA  . MET   F  1 154 ? -20.571 -81.585  -31.003 1.00 37.72 ? 154 MET   F CA  1 
ATOM   7615  C  C   . MET   F  1 154 ? -19.468 -80.687  -31.564 1.00 39.88 ? 154 MET   F C   1 
ATOM   7616  O  O   . MET   F  1 154 ? -18.294 -80.837  -31.213 1.00 41.84 ? 154 MET   F O   1 
ATOM   7617  C  CB  . MET   F  1 154 ? -20.956 -82.632  -32.055 1.00 38.14 ? 154 MET   F CB  1 
ATOM   7618  C  CG  . MET   F  1 154 ? -21.526 -83.958  -31.527 1.00 53.97 ? 154 MET   F CG  1 
ATOM   7619  S  SD  . MET   F  1 154 ? -22.250 -84.982  -32.846 1.00 51.99 ? 154 MET   F SD  1 
ATOM   7620  C  CE  . MET   F  1 154 ? -20.976 -84.806  -34.099 1.00 45.49 ? 154 MET   F CE  1 
ATOM   7621  N  N   . HIS   F  1 155 ? -19.823 -79.772  -32.458 1.00 48.20 ? 155 HIS   F N   1 
ATOM   7622  C  CA  . HIS   F  1 155 ? -18.862 -78.993  -33.231 1.00 50.82 ? 155 HIS   F CA  1 
ATOM   7623  C  C   . HIS   F  1 155 ? -18.869 -77.538  -32.767 1.00 48.25 ? 155 HIS   F C   1 
ATOM   7624  O  O   . HIS   F  1 155 ? -19.934 -76.970  -32.503 1.00 43.52 ? 155 HIS   F O   1 
ATOM   7625  C  CB  . HIS   F  1 155 ? -19.200 -79.064  -34.730 1.00 46.77 ? 155 HIS   F CB  1 
ATOM   7626  C  CG  . HIS   F  1 155 ? -19.126 -80.445  -35.313 1.00 51.57 ? 155 HIS   F CG  1 
ATOM   7627  N  ND1 . HIS   F  1 155 ? -19.967 -80.872  -36.317 1.00 52.71 ? 155 HIS   F ND1 1 
ATOM   7628  C  CD2 . HIS   F  1 155 ? -18.309 -81.491  -35.039 1.00 64.77 ? 155 HIS   F CD2 1 
ATOM   7629  C  CE1 . HIS   F  1 155 ? -19.672 -82.120  -36.639 1.00 53.23 ? 155 HIS   F CE1 1 
ATOM   7630  N  NE2 . HIS   F  1 155 ? -18.672 -82.521  -35.876 1.00 52.08 ? 155 HIS   F NE2 1 
ATOM   7631  N  N   . GLU   F  1 156 ? -17.686 -76.931  -32.667 1.00 54.16 ? 156 GLU   F N   1 
ATOM   7632  C  CA  . GLU   F  1 156 ? -17.606 -75.483  -32.422 1.00 60.32 ? 156 GLU   F CA  1 
ATOM   7633  C  C   . GLU   F  1 156 ? -18.008 -74.723  -33.690 1.00 60.25 ? 156 GLU   F C   1 
ATOM   7634  O  O   . GLU   F  1 156 ? -18.573 -73.630  -33.619 1.00 65.35 ? 156 GLU   F O   1 
ATOM   7635  C  CB  . GLU   F  1 156 ? -16.195 -75.061  -31.985 1.00 56.08 ? 156 GLU   F CB  1 
ATOM   7636  C  CG  . GLU   F  1 156 ? -15.633 -75.909  -30.887 1.00 47.50 ? 156 GLU   F CG  1 
ATOM   7637  C  CD  . GLU   F  1 156 ? -14.369 -75.343  -30.281 1.00 64.88 ? 156 GLU   F CD  1 
ATOM   7638  O  OE1 . GLU   F  1 156 ? -14.239 -74.101  -30.201 1.00 61.59 ? 156 GLU   F OE1 1 
ATOM   7639  O  OE2 . GLU   F  1 156 ? -13.512 -76.152  -29.869 1.00 65.15 ? 156 GLU   F OE2 1 
ATOM   7640  N  N   . MET   G  1 1   ? -44.398 -47.768  -81.036 1.00 38.21 ? 1   MET   G N   1 
ATOM   7641  C  CA  . MET   G  1 1   ? -45.691 -48.408  -80.626 1.00 37.64 ? 1   MET   G CA  1 
ATOM   7642  C  C   . MET   G  1 1   ? -46.798 -47.378  -80.696 1.00 33.46 ? 1   MET   G C   1 
ATOM   7643  O  O   . MET   G  1 1   ? -46.687 -46.306  -80.103 1.00 36.95 ? 1   MET   G O   1 
ATOM   7644  C  CB  . MET   G  1 1   ? -45.595 -48.969  -79.207 1.00 38.34 ? 1   MET   G CB  1 
ATOM   7645  C  CG  . MET   G  1 1   ? -46.591 -50.061  -78.895 1.00 39.41 ? 1   MET   G CG  1 
ATOM   7646  S  SD  . MET   G  1 1   ? -46.202 -50.807  -77.316 1.00 43.16 ? 1   MET   G SD  1 
ATOM   7647  C  CE  . MET   G  1 1   ? -46.716 -49.437  -76.315 1.00 40.27 ? 1   MET   G CE  1 
ATOM   7648  N  N   . LYS   G  1 2   ? -47.893 -47.700  -81.383 1.00 33.41 ? 2   LYS   G N   1 
ATOM   7649  C  CA  . LYS   G  1 2   ? -48.991 -46.744  -81.500 1.00 36.57 ? 2   LYS   G CA  1 
ATOM   7650  C  C   . LYS   G  1 2   ? -49.681 -46.581  -80.151 1.00 38.55 ? 2   LYS   G C   1 
ATOM   7651  O  O   . LYS   G  1 2   ? -50.233 -47.538  -79.601 1.00 38.30 ? 2   LYS   G O   1 
ATOM   7652  C  CB  . LYS   G  1 2   ? -49.997 -47.193  -82.562 1.00 38.70 ? 2   LYS   G CB  1 
ATOM   7653  N  N   . GLY   G  1 3   ? -49.659 -45.365  -79.632 1.00 36.49 ? 3   GLY   G N   1 
ATOM   7654  C  CA  . GLY   G  1 3   ? -50.332 -45.067  -78.391 1.00 37.87 ? 3   GLY   G CA  1 
ATOM   7655  C  C   . GLY   G  1 3   ? -51.770 -44.557  -78.579 1.00 37.92 ? 3   GLY   G C   1 
ATOM   7656  O  O   . GLY   G  1 3   ? -52.214 -44.181  -79.673 1.00 34.33 ? 3   GLY   G O   1 
ATOM   7657  N  N   . ASP   G  1 4   ? -52.495 -44.570  -77.473 1.00 36.37 ? 4   ASP   G N   1 
ATOM   7658  C  CA  . ASP   G  1 4   ? -53.802 -43.933  -77.390 1.00 34.12 ? 4   ASP   G CA  1 
ATOM   7659  C  C   . ASP   G  1 4   ? -53.654 -42.437  -77.599 1.00 39.10 ? 4   ASP   G C   1 
ATOM   7660  O  O   . ASP   G  1 4   ? -52.812 -41.793  -76.972 1.00 31.14 ? 4   ASP   G O   1 
ATOM   7661  C  CB  . ASP   G  1 4   ? -54.415 -44.232  -76.023 1.00 38.16 ? 4   ASP   G CB  1 
ATOM   7662  C  CG  . ASP   G  1 4   ? -55.786 -43.601  -75.837 1.00 36.66 ? 4   ASP   G CG  1 
ATOM   7663  O  OD1 . ASP   G  1 4   ? -56.777 -44.274  -76.189 1.00 39.10 ? 4   ASP   G OD1 1 
ATOM   7664  O  OD2 . ASP   G  1 4   ? -55.875 -42.450  -75.348 1.00 38.34 ? 4   ASP   G OD2 1 
ATOM   7665  N  N   . LYS   G  1 5   ? -54.473 -41.882  -78.493 1.00 31.56 ? 5   LYS   G N   1 
ATOM   7666  C  CA  . LYS   G  1 5   ? -54.340 -40.471  -78.856 1.00 31.35 ? 5   LYS   G CA  1 
ATOM   7667  C  C   . LYS   G  1 5   ? -54.550 -39.538  -77.673 1.00 40.94 ? 5   LYS   G C   1 
ATOM   7668  O  O   . LYS   G  1 5   ? -53.893 -38.490  -77.570 1.00 40.11 ? 5   LYS   G O   1 
ATOM   7669  C  CB  . LYS   G  1 5   ? -55.342 -40.122  -79.954 1.00 37.94 ? 5   LYS   G CB  1 
ATOM   7670  C  CG  . LYS   G  1 5   ? -55.466 -38.631  -80.165 1.00 45.18 ? 5   LYS   G CG  1 
ATOM   7671  N  N   . LYS   G  1 6   ? -55.505 -39.856  -76.802 1.00 35.84 ? 6   LYS   G N   1 
ATOM   7672  C  CA  . LYS   G  1 6   ? -55.761 -38.981  -75.671 1.00 33.79 ? 6   LYS   G CA  1 
ATOM   7673  C  C   . LYS   G  1 6   ? -54.685 -39.120  -74.593 1.00 24.93 ? 6   LYS   G C   1 
ATOM   7674  O  O   . LYS   G  1 6   ? -54.431 -38.166  -73.858 1.00 29.92 ? 6   LYS   G O   1 
ATOM   7675  C  CB  . LYS   G  1 6   ? -57.149 -39.289  -75.094 1.00 37.14 ? 6   LYS   G CB  1 
ATOM   7676  C  CG  . LYS   G  1 6   ? -57.538 -38.445  -73.893 1.00 43.72 ? 6   LYS   G CG  1 
ATOM   7677  C  CD  . LYS   G  1 6   ? -57.787 -36.976  -74.277 1.00 48.57 ? 6   LYS   G CD  1 
ATOM   7678  C  CE  . LYS   G  1 6   ? -58.469 -36.212  -73.145 1.00 55.09 ? 6   LYS   G CE  1 
ATOM   7679  N  NZ  . LYS   G  1 6   ? -58.394 -34.730  -73.341 1.00 69.91 ? 6   LYS   G NZ  1 
ATOM   7680  N  N   . VAL   G  1 7   ? -54.099 -40.302  -74.435 1.00 28.55 ? 7   VAL   G N   1 
ATOM   7681  C  CA  . VAL   G  1 7   ? -52.919 -40.405  -73.559 1.00 35.19 ? 7   VAL   G CA  1 
ATOM   7682  C  C   . VAL   G  1 7   ? -51.857 -39.401  -74.001 1.00 30.79 ? 7   VAL   G C   1 
ATOM   7683  O  O   . VAL   G  1 7   ? -51.328 -38.622  -73.197 1.00 31.38 ? 7   VAL   G O   1 
ATOM   7684  C  CB  . VAL   G  1 7   ? -52.350 -41.834  -73.552 1.00 33.01 ? 7   VAL   G CB  1 
ATOM   7685  C  CG1 . VAL   G  1 7   ? -50.896 -41.843  -72.927 1.00 32.39 ? 7   VAL   G CG1 1 
ATOM   7686  C  CG2 . VAL   G  1 7   ? -53.237 -42.764  -72.801 1.00 36.76 ? 7   VAL   G CG2 1 
ATOM   7687  N  N   . ILE   G  1 8   ? -51.569 -39.378  -75.308 1.00 31.21 ? 8   ILE   G N   1 
ATOM   7688  C  CA  . ILE   G  1 8   ? -50.523 -38.511  -75.840 1.00 28.29 ? 8   ILE   G CA  1 
ATOM   7689  C  C   . ILE   G  1 8   ? -50.868 -37.047  -75.607 1.00 36.51 ? 8   ILE   G C   1 
ATOM   7690  O  O   . ILE   G  1 8   ? -50.002 -36.245  -75.244 1.00 29.78 ? 8   ILE   G O   1 
ATOM   7691  C  CB  . ILE   G  1 8   ? -50.292 -38.837  -77.328 1.00 32.64 ? 8   ILE   G CB  1 
ATOM   7692  C  CG1 . ILE   G  1 8   ? -49.625 -40.211  -77.438 1.00 33.73 ? 8   ILE   G CG1 1 
ATOM   7693  C  CG2 . ILE   G  1 8   ? -49.492 -37.748  -77.987 1.00 32.38 ? 8   ILE   G CG2 1 
ATOM   7694  C  CD1 . ILE   G  1 8   ? -49.701 -40.856  -78.789 1.00 39.91 ? 8   ILE   G CD1 1 
ATOM   7695  N  N   . GLN   G  1 9   ? -52.138 -36.678  -75.789 1.00 30.90 ? 9   GLN   G N   1 
ATOM   7696  C  CA  . GLN   G  1 9   ? -52.588 -35.332  -75.428 1.00 36.03 ? 9   GLN   G CA  1 
ATOM   7697  C  C   . GLN   G  1 9   ? -52.403 -35.041  -73.942 1.00 29.01 ? 9   GLN   G C   1 
ATOM   7698  O  O   . GLN   G  1 9   ? -52.055 -33.915  -73.561 1.00 30.48 ? 9   GLN   G O   1 
ATOM   7699  C  CB  . GLN   G  1 9   ? -54.067 -35.155  -75.790 1.00 32.70 ? 9   GLN   G CB  1 
ATOM   7700  C  CG  . GLN   G  1 9   ? -54.353 -35.334  -77.282 1.00 41.42 ? 9   GLN   G CG  1 
ATOM   7701  C  CD  . GLN   G  1 9   ? -55.860 -35.288  -77.592 1.00 47.59 ? 9   GLN   G CD  1 
ATOM   7702  O  OE1 . GLN   G  1 9   ? -56.659 -35.898  -76.903 1.00 53.37 ? 9   GLN   G OE1 1 
ATOM   7703  N  NE2 . GLN   G  1 9   ? -56.230 -34.551  -78.623 1.00 49.11 ? 9   GLN   G NE2 1 
ATOM   7704  N  N   . HIS   G  1 10  ? -52.682 -36.018  -73.085 1.00 25.65 ? 10  HIS   G N   1 
ATOM   7705  C  CA  . HIS   G  1 10  ? -52.429 -35.824  -71.660 1.00 34.25 ? 10  HIS   G CA  1 
ATOM   7706  C  C   . HIS   G  1 10  ? -50.927 -35.655  -71.391 1.00 32.06 ? 10  HIS   G C   1 
ATOM   7707  O  O   . HIS   G  1 10  ? -50.522 -34.771  -70.625 1.00 29.01 ? 10  HIS   G O   1 
ATOM   7708  C  CB  . HIS   G  1 10  ? -52.968 -37.002  -70.861 1.00 31.29 ? 10  HIS   G CB  1 
ATOM   7709  C  CG  . HIS   G  1 10  ? -54.387 -36.844  -70.424 1.00 32.83 ? 10  HIS   G CG  1 
ATOM   7710  N  ND1 . HIS   G  1 10  ? -54.787 -35.878  -69.523 1.00 35.23 ? 10  HIS   G ND1 1 
ATOM   7711  C  CD2 . HIS   G  1 10  ? -55.496 -37.538  -70.758 1.00 31.04 ? 10  HIS   G CD2 1 
ATOM   7712  C  CE1 . HIS   G  1 10  ? -56.091 -35.982  -69.329 1.00 38.83 ? 10  HIS   G CE1 1 
ATOM   7713  N  NE2 . HIS   G  1 10  ? -56.543 -36.983  -70.062 1.00 41.71 ? 10  HIS   G NE2 1 
ATOM   7714  N  N   . LEU   G  1 11  ? -50.097 -36.485  -72.022 1.00 31.80 ? 11  LEU   G N   1 
ATOM   7715  C  CA  . LEU   G  1 11  ? -48.648 -36.377  -71.811 1.00 31.62 ? 11  LEU   G CA  1 
ATOM   7716  C  C   . LEU   G  1 11  ? -48.131 -35.030  -72.281 1.00 32.60 ? 11  LEU   G C   1 
ATOM   7717  O  O   . LEU   G  1 11  ? -47.266 -34.424  -71.641 1.00 30.50 ? 11  LEU   G O   1 
ATOM   7718  C  CB  . LEU   G  1 11  ? -47.926 -37.506  -72.531 1.00 26.69 ? 11  LEU   G CB  1 
ATOM   7719  C  CG  . LEU   G  1 11  ? -48.282 -38.917  -72.059 1.00 28.77 ? 11  LEU   G CG  1 
ATOM   7720  C  CD1 . LEU   G  1 11  ? -47.540 -39.931  -72.883 1.00 31.68 ? 11  LEU   G CD1 1 
ATOM   7721  C  CD2 . LEU   G  1 11  ? -47.961 -39.138  -70.561 1.00 34.03 ? 11  LEU   G CD2 1 
ATOM   7722  N  N   . ASN   G  1 12  ? -48.651 -34.537  -73.399 1.00 30.09 ? 12  ASN   G N   1 
ATOM   7723  C  CA  . ASN   G  1 12  ? -48.236 -33.218  -73.850 1.00 26.13 ? 12  ASN   G CA  1 
ATOM   7724  C  C   . ASN   G  1 12  ? -48.721 -32.127  -72.916 1.00 30.60 ? 12  ASN   G C   1 
ATOM   7725  O  O   . ASN   G  1 12  ? -48.065 -31.090  -72.790 1.00 33.24 ? 12  ASN   G O   1 
ATOM   7726  C  CB  . ASN   G  1 12  ? -48.738 -32.977  -75.288 1.00 30.56 ? 12  ASN   G CB  1 
ATOM   7727  C  CG  . ASN   G  1 12  ? -47.681 -33.303  -76.329 1.00 39.71 ? 12  ASN   G CG  1 
ATOM   7728  O  OD1 . ASN   G  1 12  ? -46.492 -33.066  -76.106 1.00 32.21 ? 12  ASN   G OD1 1 
ATOM   7729  N  ND2 . ASN   G  1 12  ? -48.108 -33.829  -77.481 1.00 30.27 ? 12  ASN   G ND2 1 
ATOM   7730  N  N   . LYS   G  1 13  ? -49.879 -32.316  -72.273 1.00 29.36 ? 13  LYS   G N   1 
ATOM   7731  C  CA  . LYS   G  1 13  ? -50.326 -31.328  -71.300 1.00 30.07 ? 13  LYS   G CA  1 
ATOM   7732  C  C   . LYS   G  1 13  ? -49.409 -31.311  -70.076 1.00 24.80 ? 13  LYS   G C   1 
ATOM   7733  O  O   . LYS   G  1 13  ? -49.046 -30.240  -69.579 1.00 27.32 ? 13  LYS   G O   1 
ATOM   7734  C  CB  . LYS   G  1 13  ? -51.777 -31.612  -70.884 1.00 33.02 ? 13  LYS   G CB  1 
ATOM   7735  C  CG  . LYS   G  1 13  ? -52.365 -30.536  -69.970 1.00 38.15 ? 13  LYS   G CG  1 
ATOM   7736  C  CD  . LYS   G  1 13  ? -53.879 -30.790  -69.736 1.00 44.00 ? 13  LYS   G CD  1 
ATOM   7737  C  CE  . LYS   G  1 13  ? -54.517 -29.649  -68.956 1.00 46.33 ? 13  LYS   G CE  1 
ATOM   7738  N  NZ  . LYS   G  1 13  ? -55.909 -29.978  -68.528 1.00 54.15 ? 13  LYS   G NZ  1 
ATOM   7739  N  N   . ILE   G  1 14  ? -49.018 -32.487  -69.592 1.00 26.78 ? 14  ILE   G N   1 
ATOM   7740  C  CA  . ILE   G  1 14  ? -48.068 -32.559  -68.480 1.00 32.71 ? 14  ILE   G CA  1 
ATOM   7741  C  C   . ILE   G  1 14  ? -46.723 -31.962  -68.895 1.00 33.64 ? 14  ILE   G C   1 
ATOM   7742  O  O   . ILE   G  1 14  ? -46.087 -31.217  -68.134 1.00 30.07 ? 14  ILE   G O   1 
ATOM   7743  C  CB  . ILE   G  1 14  ? -47.904 -34.015  -68.014 1.00 28.84 ? 14  ILE   G CB  1 
ATOM   7744  C  CG1 . ILE   G  1 14  ? -49.243 -34.671  -67.649 1.00 30.77 ? 14  ILE   G CG1 1 
ATOM   7745  C  CG2 . ILE   G  1 14  ? -46.917 -34.065  -66.834 1.00 27.60 ? 14  ILE   G CG2 1 
ATOM   7746  C  CD1 . ILE   G  1 14  ? -50.066 -33.883  -66.767 1.00 36.37 ? 14  ILE   G CD1 1 
ATOM   7747  N  N   . LEU   G  1 15  ? -46.263 -32.291  -70.112 1.00 31.43 ? 15  LEU   G N   1 
ATOM   7748  C  CA  . LEU   G  1 15  ? -45.034 -31.690  -70.640 1.00 23.89 ? 15  LEU   G CA  1 
ATOM   7749  C  C   . LEU   G  1 15  ? -45.137 -30.181  -70.666 1.00 30.74 ? 15  LEU   G C   1 
ATOM   7750  O  O   . LEU   G  1 15  ? -44.196 -29.476  -70.260 1.00 27.62 ? 15  LEU   G O   1 
ATOM   7751  C  CB  . LEU   G  1 15  ? -44.745 -32.243  -72.040 1.00 28.59 ? 15  LEU   G CB  1 
ATOM   7752  C  CG  . LEU   G  1 15  ? -43.500 -31.722  -72.763 1.00 29.81 ? 15  LEU   G CG  1 
ATOM   7753  C  CD1 . LEU   G  1 15  ? -42.239 -31.887  -71.899 1.00 29.60 ? 15  LEU   G CD1 1 
ATOM   7754  C  CD2 . LEU   G  1 15  ? -43.334 -32.415  -74.113 1.00 31.69 ? 15  LEU   G CD2 1 
ATOM   7755  N  N   . GLY   G  1 16  ? -46.290 -29.656  -71.081 1.00 32.62 ? 16  GLY   G N   1 
ATOM   7756  C  CA  . GLY   G  1 16  ? -46.466 -28.215  -71.071 1.00 32.95 ? 16  GLY   G CA  1 
ATOM   7757  C  C   . GLY   G  1 16  ? -46.301 -27.616  -69.687 1.00 31.59 ? 16  GLY   G C   1 
ATOM   7758  O  O   . GLY   G  1 16  ? -45.761 -26.516  -69.540 1.00 32.03 ? 16  GLY   G O   1 
ATOM   7759  N  N   . ASN   G  1 17  ? -46.790 -28.318  -68.653 1.00 33.17 ? 17  ASN   G N   1 
ATOM   7760  C  CA  . ASN   G  1 17  ? -46.641 -27.827  -67.292 1.00 31.57 ? 17  ASN   G CA  1 
ATOM   7761  C  C   . ASN   G  1 17  ? -45.157 -27.820  -66.876 1.00 29.67 ? 17  ASN   G C   1 
ATOM   7762  O  O   . ASN   G  1 17  ? -44.675 -26.863  -66.259 1.00 31.14 ? 17  ASN   G O   1 
ATOM   7763  C  CB  . ASN   G  1 17  ? -47.457 -28.704  -66.320 1.00 33.40 ? 17  ASN   G CB  1 
ATOM   7764  C  CG  . ASN   G  1 17  ? -48.972 -28.507  -66.441 1.00 39.96 ? 17  ASN   G CG  1 
ATOM   7765  O  OD1 . ASN   G  1 17  ? -49.443 -27.441  -66.788 1.00 33.88 ? 17  ASN   G OD1 1 
ATOM   7766  N  ND2 . ASN   G  1 17  ? -49.728 -29.544  -66.120 1.00 33.45 ? 17  ASN   G ND2 1 
ATOM   7767  N  N   . GLU   G  1 18  ? -44.451 -28.910  -67.168 1.00 28.69 ? 18  GLU   G N   1 
ATOM   7768  C  CA  . GLU   G  1 18  ? -43.012 -29.009  -66.877 1.00 31.78 ? 18  GLU   G CA  1 
ATOM   7769  C  C   . GLU   G  1 18  ? -42.224 -27.887  -67.545 1.00 25.33 ? 18  GLU   G C   1 
ATOM   7770  O  O   . GLU   G  1 18  ? -41.325 -27.289  -66.931 1.00 32.13 ? 18  GLU   G O   1 
ATOM   7771  C  CB  . GLU   G  1 18  ? -42.466 -30.352  -67.355 1.00 32.76 ? 18  GLU   G CB  1 
ATOM   7772  C  CG  . GLU   G  1 18  ? -43.104 -31.617  -66.762 1.00 33.91 ? 18  GLU   G CG  1 
ATOM   7773  C  CD  . GLU   G  1 18  ? -42.731 -31.893  -65.329 1.00 50.07 ? 18  GLU   G CD  1 
ATOM   7774  O  OE1 . GLU   G  1 18  ? -41.903 -31.138  -64.775 1.00 48.84 ? 18  GLU   G OE1 1 
ATOM   7775  O  OE2 . GLU   G  1 18  ? -43.269 -32.876  -64.759 1.00 51.30 ? 18  GLU   G OE2 1 
ATOM   7776  N  N   . LEU   G  1 19  ? -42.521 -27.608  -68.820 1.00 28.20 ? 19  LEU   G N   1 
ATOM   7777  C  CA  . LEU   G  1 19  ? -41.847 -26.519  -69.530 1.00 29.65 ? 19  LEU   G CA  1 
ATOM   7778  C  C   . LEU   G  1 19  ? -42.061 -25.183  -68.840 1.00 32.75 ? 19  LEU   G C   1 
ATOM   7779  O  O   . LEU   G  1 19  ? -41.125 -24.365  -68.750 1.00 27.24 ? 19  LEU   G O   1 
ATOM   7780  C  CB  . LEU   G  1 19  ? -42.315 -26.425  -70.984 1.00 31.66 ? 19  LEU   G CB  1 
ATOM   7781  C  CG  . LEU   G  1 19  ? -41.994 -27.612  -71.891 1.00 33.76 ? 19  LEU   G CG  1 
ATOM   7782  C  CD1 . LEU   G  1 19  ? -42.625 -27.382  -73.275 1.00 35.79 ? 19  LEU   G CD1 1 
ATOM   7783  C  CD2 . LEU   G  1 19  ? -40.496 -27.835  -72.009 1.00 36.20 ? 19  LEU   G CD2 1 
ATOM   7784  N  N   . ILE   G  1 20  ? -43.285 -24.929  -68.357 1.00 30.64 ? 20  ILE   G N   1 
ATOM   7785  C  CA  . ILE   G  1 20  ? -43.510 -23.769  -67.503 1.00 27.90 ? 20  ILE   G CA  1 
ATOM   7786  C  C   . ILE   G  1 20  ? -42.632 -23.863  -66.251 1.00 27.80 ? 20  ILE   G C   1 
ATOM   7787  O  O   . ILE   G  1 20  ? -41.946 -22.907  -65.878 1.00 29.40 ? 20  ILE   G O   1 
ATOM   7788  C  CB  . ILE   G  1 20  ? -45.004 -23.645  -67.122 1.00 29.55 ? 20  ILE   G CB  1 
ATOM   7789  C  CG1 . ILE   G  1 20  ? -45.858 -23.390  -68.368 1.00 29.67 ? 20  ILE   G CG1 1 
ATOM   7790  C  CG2 . ILE   G  1 20  ? -45.207 -22.559  -66.030 1.00 33.66 ? 20  ILE   G CG2 1 
ATOM   7791  C  CD1 . ILE   G  1 20  ? -47.400 -23.450  -68.129 1.00 32.66 ? 20  ILE   G CD1 1 
ATOM   7792  N  N   . ALA   G  1 21  ? -42.681 -25.003  -65.567 1.00 26.25 ? 21  ALA   G N   1 
ATOM   7793  C  CA  . ALA   G  1 21  ? -41.972 -25.137  -64.294 1.00 29.60 ? 21  ALA   G CA  1 
ATOM   7794  C  C   . ALA   G  1 21  ? -40.459 -24.946  -64.472 1.00 30.81 ? 21  ALA   G C   1 
ATOM   7795  O  O   . ALA   G  1 21  ? -39.812 -24.257  -63.672 1.00 27.02 ? 21  ALA   G O   1 
ATOM   7796  C  CB  . ALA   G  1 21  ? -42.287 -26.503  -63.670 1.00 27.71 ? 21  ALA   G CB  1 
ATOM   7797  N  N   . ILE   G  1 22  ? -39.885 -25.515  -65.532 1.00 28.30 ? 22  ILE   G N   1 
ATOM   7798  C  CA  . ILE   G  1 22  ? -38.448 -25.348  -65.772 1.00 28.82 ? 22  ILE   G CA  1 
ATOM   7799  C  C   . ILE   G  1 22  ? -38.063 -23.876  -65.731 1.00 30.63 ? 22  ILE   G C   1 
ATOM   7800  O  O   . ILE   G  1 22  ? -37.158 -23.466  -64.990 1.00 27.99 ? 22  ILE   G O   1 
ATOM   7801  C  CB  . ILE   G  1 22  ? -38.045 -25.987  -67.112 1.00 30.44 ? 22  ILE   G CB  1 
ATOM   7802  C  CG1 . ILE   G  1 22  ? -38.118 -27.503  -67.013 1.00 24.32 ? 22  ILE   G CG1 1 
ATOM   7803  C  CG2 . ILE   G  1 22  ? -36.615 -25.539  -67.500 1.00 29.95 ? 22  ILE   G CG2 1 
ATOM   7804  C  CD1 . ILE   G  1 22  ? -38.151 -28.198  -68.414 1.00 28.24 ? 22  ILE   G CD1 1 
ATOM   7805  N  N   . ASN   G  1 23  ? -38.755 -23.051  -66.521 1.00 28.71 ? 23  ASN   G N   1 
ATOM   7806  C  CA  . ASN   G  1 23  ? -38.373 -21.642  -66.657 1.00 30.06 ? 23  ASN   G CA  1 
ATOM   7807  C  C   . ASN   G  1 23  ? -38.691 -20.843  -65.400 1.00 26.98 ? 23  ASN   G C   1 
ATOM   7808  O  O   . ASN   G  1 23  ? -37.925 -19.951  -65.004 1.00 26.20 ? 23  ASN   G O   1 
ATOM   7809  C  CB  . ASN   G  1 23  ? -39.075 -21.027  -67.888 1.00 30.04 ? 23  ASN   G CB  1 
ATOM   7810  C  CG  . ASN   G  1 23  ? -38.523 -21.581  -69.229 1.00 33.91 ? 23  ASN   G CG  1 
ATOM   7811  O  OD1 . ASN   G  1 23  ? -37.881 -22.627  -69.266 1.00 33.90 ? 23  ASN   G OD1 1 
ATOM   7812  N  ND2 . ASN   G  1 23  ? -38.799 -20.890  -70.314 1.00 36.53 ? 23  ASN   G ND2 1 
ATOM   7813  N  N   . GLN   G  1 24  ? -39.834 -21.117  -64.774 1.00 28.25 ? 24  GLN   G N   1 
ATOM   7814  C  CA  . GLN   G  1 24  ? -40.189 -20.384  -63.566 1.00 31.31 ? 24  GLN   G CA  1 
ATOM   7815  C  C   . GLN   G  1 24  ? -39.213 -20.688  -62.426 1.00 25.72 ? 24  GLN   G C   1 
ATOM   7816  O  O   . GLN   G  1 24  ? -38.765 -19.781  -61.716 1.00 27.22 ? 24  GLN   G O   1 
ATOM   7817  C  CB  . GLN   G  1 24  ? -41.627 -20.739  -63.162 1.00 29.21 ? 24  GLN   G CB  1 
ATOM   7818  C  CG  . GLN   G  1 24  ? -42.074 -20.134  -61.844 1.00 31.66 ? 24  GLN   G CG  1 
ATOM   7819  C  CD  . GLN   G  1 24  ? -43.550 -20.408  -61.575 1.00 37.62 ? 24  GLN   G CD  1 
ATOM   7820  O  OE1 . GLN   G  1 24  ? -44.395 -20.306  -62.483 1.00 34.60 ? 24  GLN   G OE1 1 
ATOM   7821  N  NE2 . GLN   G  1 24  ? -43.864 -20.792  -60.340 1.00 35.13 ? 24  GLN   G NE2 1 
ATOM   7822  N  N   . TYR   G  1 25  ? -38.897 -21.959  -62.219 1.00 30.22 ? 25  TYR   G N   1 
ATOM   7823  C  CA  . TYR   G  1 25  ? -37.933 -22.307  -61.169 1.00 27.28 ? 25  TYR   G CA  1 
ATOM   7824  C  C   . TYR   G  1 25  ? -36.540 -21.800  -61.536 1.00 27.44 ? 25  TYR   G C   1 
ATOM   7825  O  O   . TYR   G  1 25  ? -35.821 -21.270  -60.676 1.00 29.32 ? 25  TYR   G O   1 
ATOM   7826  C  CB  . TYR   G  1 25  ? -37.913 -23.823  -60.938 1.00 29.09 ? 25  TYR   G CB  1 
ATOM   7827  C  CG  . TYR   G  1 25  ? -39.259 -24.413  -60.588 1.00 26.83 ? 25  TYR   G CG  1 
ATOM   7828  C  CD1 . TYR   G  1 25  ? -40.324 -23.589  -60.223 1.00 34.76 ? 25  TYR   G CD1 1 
ATOM   7829  C  CD2 . TYR   G  1 25  ? -39.486 -25.776  -60.648 1.00 27.06 ? 25  TYR   G CD2 1 
ATOM   7830  C  CE1 . TYR   G  1 25  ? -41.554 -24.112  -59.912 1.00 33.63 ? 25  TYR   G CE1 1 
ATOM   7831  C  CE2 . TYR   G  1 25  ? -40.723 -26.306  -60.322 1.00 30.96 ? 25  TYR   G CE2 1 
ATOM   7832  C  CZ  . TYR   G  1 25  ? -41.755 -25.458  -59.958 1.00 36.61 ? 25  TYR   G CZ  1 
ATOM   7833  O  OH  . TYR   G  1 25  ? -43.014 -25.932  -59.651 1.00 36.57 ? 25  TYR   G OH  1 
ATOM   7834  N  N   . PHE   G  1 26  ? -36.152 -21.902  -62.817 1.00 29.39 ? 26  PHE   G N   1 
ATOM   7835  C  CA  . PHE   G  1 26  ? -34.821 -21.420  -63.170 1.00 28.31 ? 26  PHE   G CA  1 
ATOM   7836  C  C   . PHE   G  1 26  ? -34.694 -19.922  -62.929 1.00 30.16 ? 26  PHE   G C   1 
ATOM   7837  O  O   . PHE   G  1 26  ? -33.670 -19.454  -62.420 1.00 28.10 ? 26  PHE   G O   1 
ATOM   7838  C  CB  . PHE   G  1 26  ? -34.446 -21.758  -64.617 1.00 32.71 ? 26  PHE   G CB  1 
ATOM   7839  C  CG  . PHE   G  1 26  ? -32.958 -21.857  -64.795 1.00 26.63 ? 26  PHE   G CG  1 
ATOM   7840  C  CD1 . PHE   G  1 26  ? -32.199 -20.720  -65.020 1.00 28.53 ? 26  PHE   G CD1 1 
ATOM   7841  C  CD2 . PHE   G  1 26  ? -32.310 -23.067  -64.623 1.00 30.29 ? 26  PHE   G CD2 1 
ATOM   7842  C  CE1 . PHE   G  1 26  ? -30.819 -20.796  -65.125 1.00 33.93 ? 26  PHE   G CE1 1 
ATOM   7843  C  CE2 . PHE   G  1 26  ? -30.917 -23.153  -64.731 1.00 34.12 ? 26  PHE   G CE2 1 
ATOM   7844  C  CZ  . PHE   G  1 26  ? -30.181 -22.015  -64.970 1.00 29.74 ? 26  PHE   G CZ  1 
ATOM   7845  N  N   . LEU   G  1 27  ? -35.720 -19.150  -63.284 1.00 27.03 ? 27  LEU   G N   1 
ATOM   7846  C  CA  . LEU   G  1 27  ? -35.651 -17.710  -63.050 1.00 25.73 ? 27  LEU   G CA  1 
ATOM   7847  C  C   . LEU   G  1 27  ? -35.720 -17.374  -61.551 1.00 25.23 ? 27  LEU   G C   1 
ATOM   7848  O  O   . LEU   G  1 27  ? -34.985 -16.498  -61.070 1.00 29.83 ? 27  LEU   G O   1 
ATOM   7849  C  CB  . LEU   G  1 27  ? -36.769 -16.998  -63.830 1.00 26.86 ? 27  LEU   G CB  1 
ATOM   7850  C  CG  . LEU   G  1 27  ? -36.768 -15.472  -63.664 1.00 28.10 ? 27  LEU   G CG  1 
ATOM   7851  C  CD1 . LEU   G  1 27  ? -35.453 -14.886  -63.970 1.00 32.99 ? 27  LEU   G CD1 1 
ATOM   7852  C  CD2 . LEU   G  1 27  ? -37.848 -14.761  -64.535 1.00 37.47 ? 27  LEU   G CD2 1 
ATOM   7853  N  N   . HIS   G  1 28  ? -36.593 -18.044  -60.798 1.00 27.75 ? 28  HIS   G N   1 
ATOM   7854  C  CA  . HIS   G  1 28  ? -36.616 -17.825  -59.349 1.00 32.27 ? 28  HIS   G CA  1 
ATOM   7855  C  C   . HIS   G  1 28  ? -35.254 -18.170  -58.727 1.00 25.96 ? 28  HIS   G C   1 
ATOM   7856  O  O   . HIS   G  1 28  ? -34.760 -17.445  -57.861 1.00 27.93 ? 28  HIS   G O   1 
ATOM   7857  C  CB  . HIS   G  1 28  ? -37.730 -18.645  -58.688 1.00 28.40 ? 28  HIS   G CB  1 
ATOM   7858  C  CG  . HIS   G  1 28  ? -39.122 -18.090  -58.875 1.00 31.32 ? 28  HIS   G CG  1 
ATOM   7859  N  ND1 . HIS   G  1 28  ? -40.250 -18.866  -58.726 1.00 35.62 ? 28  HIS   G ND1 1 
ATOM   7860  C  CD2 . HIS   G  1 28  ? -39.566 -16.844  -59.176 1.00 31.79 ? 28  HIS   G CD2 1 
ATOM   7861  C  CE1 . HIS   G  1 28  ? -41.328 -18.129  -58.929 1.00 33.84 ? 28  HIS   G CE1 1 
ATOM   7862  N  NE2 . HIS   G  1 28  ? -40.940 -16.898  -59.212 1.00 31.90 ? 28  HIS   G NE2 1 
ATOM   7863  N  N   . SER   G  1 29  ? -34.620 -19.253  -59.193 1.00 26.56 ? 29  SER   G N   1 
ATOM   7864  C  CA  . SER   G  1 29  ? -33.284 -19.602  -58.693 1.00 28.85 ? 29  SER   G CA  1 
ATOM   7865  C  C   . SER   G  1 29  ? -32.298 -18.470  -58.916 1.00 25.48 ? 29  SER   G C   1 
ATOM   7866  O  O   . SER   G  1 29  ? -31.536 -18.084  -58.013 1.00 25.76 ? 29  SER   G O   1 
ATOM   7867  C  CB  . SER   G  1 29  ? -32.758 -20.865  -59.374 1.00 27.82 ? 29  SER   G CB  1 
ATOM   7868  O  OG  . SER   G  1 29  ? -31.350 -20.976  -59.145 1.00 27.25 ? 29  SER   G OG  1 
ATOM   7869  N  N   . ARG   G  1 30  ? -32.284 -17.930  -60.124 1.00 25.16 ? 30  ARG   G N   1 
ATOM   7870  C  CA  . ARG   G  1 30  ? -31.297 -16.916  -60.434 1.00 23.80 ? 30  ARG   G CA  1 
ATOM   7871  C  C   . ARG   G  1 30  ? -31.636 -15.580  -59.806 1.00 29.44 ? 30  ARG   G C   1 
ATOM   7872  O  O   . ARG   G  1 30  ? -30.721 -14.799  -59.527 1.00 27.20 ? 30  ARG   G O   1 
ATOM   7873  C  CB  . ARG   G  1 30  ? -31.132 -16.792  -61.947 1.00 24.74 ? 30  ARG   G CB  1 
ATOM   7874  C  CG  . ARG   G  1 30  ? -29.986 -17.663  -62.472 1.00 24.64 ? 30  ARG   G CG  1 
ATOM   7875  C  CD  . ARG   G  1 30  ? -30.167 -19.152  -62.078 1.00 31.08 ? 30  ARG   G CD  1 
ATOM   7876  N  NE  . ARG   G  1 30  ? -29.029 -19.978  -62.474 1.00 30.98 ? 30  ARG   G NE  1 
ATOM   7877  C  CZ  . ARG   G  1 30  ? -28.371 -20.813  -61.680 1.00 26.09 ? 30  ARG   G CZ  1 
ATOM   7878  N  NH1 . ARG   G  1 30  ? -28.796 -21.098  -60.460 1.00 29.02 ? 30  ARG   G NH1 1 
ATOM   7879  N  NH2 . ARG   G  1 30  ? -27.241 -21.372  -62.119 1.00 31.18 ? 30  ARG   G NH2 1 
ATOM   7880  N  N   . MET   G  1 31  ? -32.923 -15.290  -59.581 1.00 29.53 ? 31  MET   G N   1 
ATOM   7881  C  CA  . MET   G  1 31  ? -33.265 -14.119  -58.776 1.00 29.64 ? 31  MET   G CA  1 
ATOM   7882  C  C   . MET   G  1 31  ? -32.721 -14.257  -57.354 1.00 29.61 ? 31  MET   G C   1 
ATOM   7883  O  O   . MET   G  1 31  ? -32.061 -13.353  -56.835 1.00 30.75 ? 31  MET   G O   1 
ATOM   7884  C  CB  . MET   G  1 31  ? -34.779 -13.926  -58.746 1.00 28.30 ? 31  MET   G CB  1 
ATOM   7885  C  CG  . MET   G  1 31  ? -35.379 -13.484  -60.106 1.00 31.20 ? 31  MET   G CG  1 
ATOM   7886  S  SD  . MET   G  1 31  ? -37.155 -13.678  -60.242 1.00 32.96 ? 31  MET   G SD  1 
ATOM   7887  C  CE  . MET   G  1 31  ? -37.668 -12.585  -58.911 1.00 35.18 ? 31  MET   G CE  1 
ATOM   7888  N  N   . TRP   G  1 32  ? -32.989 -15.392  -56.715 1.00 25.51 ? 32  TRP   G N   1 
ATOM   7889  C  CA  . TRP   G  1 32  ? -32.490 -15.610  -55.364 1.00 31.40 ? 32  TRP   G CA  1 
ATOM   7890  C  C   . TRP   G  1 32  ? -30.967 -15.523  -55.296 1.00 31.55 ? 32  TRP   G C   1 
ATOM   7891  O  O   . TRP   G  1 32  ? -30.417 -14.905  -54.368 1.00 27.22 ? 32  TRP   G O   1 
ATOM   7892  C  CB  . TRP   G  1 32  ? -33.017 -16.949  -54.844 1.00 29.81 ? 32  TRP   G CB  1 
ATOM   7893  C  CG  . TRP   G  1 32  ? -34.398 -16.838  -54.237 1.00 25.27 ? 32  TRP   G CG  1 
ATOM   7894  C  CD1 . TRP   G  1 32  ? -34.861 -15.822  -53.461 1.00 29.81 ? 32  TRP   G CD1 1 
ATOM   7895  C  CD2 . TRP   G  1 32  ? -35.478 -17.783  -54.348 1.00 26.70 ? 32  TRP   G CD2 1 
ATOM   7896  N  NE1 . TRP   G  1 32  ? -36.159 -16.069  -53.074 1.00 28.66 ? 32  TRP   G NE1 1 
ATOM   7897  C  CE2 . TRP   G  1 32  ? -36.564 -17.263  -53.609 1.00 25.29 ? 32  TRP   G CE2 1 
ATOM   7898  C  CE3 . TRP   G  1 32  ? -35.631 -19.013  -54.997 1.00 28.92 ? 32  TRP   G CE3 1 
ATOM   7899  C  CZ2 . TRP   G  1 32  ? -37.775 -17.921  -53.504 1.00 29.33 ? 32  TRP   G CZ2 1 
ATOM   7900  C  CZ3 . TRP   G  1 32  ? -36.846 -19.663  -54.906 1.00 27.56 ? 32  TRP   G CZ3 1 
ATOM   7901  C  CH2 . TRP   G  1 32  ? -37.906 -19.115  -54.153 1.00 31.38 ? 32  TRP   G CH2 1 
ATOM   7902  N  N   . ASN   G  1 33  ? -30.252 -16.117  -56.268 1.00 27.03 ? 33  ASN   G N   1 
ATOM   7903  C  CA  . ASN   G  1 33  ? -28.800 -15.951  -56.268 1.00 29.49 ? 33  ASN   G CA  1 
ATOM   7904  C  C   . ASN   G  1 33  ? -28.415 -14.490  -56.383 1.00 32.20 ? 33  ASN   G C   1 
ATOM   7905  O  O   . ASN   G  1 33  ? -27.524 -14.018  -55.669 1.00 28.56 ? 33  ASN   G O   1 
ATOM   7906  C  CB  . ASN   G  1 33  ? -28.154 -16.742  -57.395 1.00 29.79 ? 33  ASN   G CB  1 
ATOM   7907  C  CG  . ASN   G  1 33  ? -28.130 -18.223  -57.114 1.00 32.05 ? 33  ASN   G CG  1 
ATOM   7908  O  OD1 . ASN   G  1 33  ? -28.325 -18.643  -55.970 1.00 29.94 ? 33  ASN   G OD1 1 
ATOM   7909  N  ND2 . ASN   G  1 33  ? -27.882 -19.025  -58.146 1.00 34.89 ? 33  ASN   G ND2 1 
ATOM   7910  N  N   . ASP   G  1 34  ? -29.076 -13.760  -57.279 1.00 29.70 ? 34  ASP   G N   1 
ATOM   7911  C  CA  . ASP   G  1 34  ? -28.806 -12.336  -57.442 1.00 39.01 ? 34  ASP   G CA  1 
ATOM   7912  C  C   . ASP   G  1 34  ? -29.040 -11.564  -56.148 1.00 34.68 ? 34  ASP   G C   1 
ATOM   7913  O  O   . ASP   G  1 34  ? -28.354 -10.571  -55.890 1.00 30.95 ? 34  ASP   G O   1 
ATOM   7914  C  CB  . ASP   G  1 34  ? -29.695 -11.753  -58.560 1.00 28.03 ? 34  ASP   G CB  1 
ATOM   7915  C  CG  . ASP   G  1 34  ? -29.441 -10.263  -58.783 1.00 37.66 ? 34  ASP   G CG  1 
ATOM   7916  O  OD1 . ASP   G  1 34  ? -28.262 -9.863   -58.935 1.00 44.64 ? 34  ASP   G OD1 1 
ATOM   7917  O  OD2 . ASP   G  1 34  ? -30.422 -9.498   -58.818 1.00 50.99 ? 34  ASP   G OD2 1 
ATOM   7918  N  N   . TRP   G  1 35  ? -30.018 -11.983  -55.344 1.00 29.82 ? 35  TRP   G N   1 
ATOM   7919  C  CA  . TRP   G  1 35  ? -30.316 -11.318  -54.078 1.00 32.21 ? 35  TRP   G CA  1 
ATOM   7920  C  C   . TRP   G  1 35  ? -29.416 -11.787  -52.940 1.00 35.58 ? 35  TRP   G C   1 
ATOM   7921  O  O   . TRP   G  1 35  ? -29.532 -11.276  -51.819 1.00 30.06 ? 35  TRP   G O   1 
ATOM   7922  C  CB  . TRP   G  1 35  ? -31.781 -11.557  -53.683 1.00 34.89 ? 35  TRP   G CB  1 
ATOM   7923  C  CG  . TRP   G  1 35  ? -32.795 -11.005  -54.680 1.00 36.23 ? 35  TRP   G CG  1 
ATOM   7924  C  CD1 . TRP   G  1 35  ? -32.547 -10.121  -55.691 1.00 43.19 ? 35  TRP   G CD1 1 
ATOM   7925  C  CD2 . TRP   G  1 35  ? -34.202 -11.304  -54.748 1.00 39.02 ? 35  TRP   G CD2 1 
ATOM   7926  N  NE1 . TRP   G  1 35  ? -33.708 -9.859   -56.389 1.00 48.11 ? 35  TRP   G NE1 1 
ATOM   7927  C  CE2 . TRP   G  1 35  ? -34.738 -10.564  -55.828 1.00 46.37 ? 35  TRP   G CE2 1 
ATOM   7928  C  CE3 . TRP   G  1 35  ? -35.059 -12.123  -54.005 1.00 42.73 ? 35  TRP   G CE3 1 
ATOM   7929  C  CZ2 . TRP   G  1 35  ? -36.092 -10.625  -56.190 1.00 42.22 ? 35  TRP   G CZ2 1 
ATOM   7930  C  CZ3 . TRP   G  1 35  ? -36.409 -12.187  -54.365 1.00 45.05 ? 35  TRP   G CZ3 1 
ATOM   7931  C  CH2 . TRP   G  1 35  ? -36.908 -11.439  -55.450 1.00 45.56 ? 35  TRP   G CH2 1 
ATOM   7932  N  N   . GLY   G  1 36  ? -28.532 -12.746  -53.178 1.00 31.46 ? 36  GLY   G N   1 
ATOM   7933  C  CA  . GLY   G  1 36  ? -27.685 -13.196  -52.090 1.00 27.75 ? 36  GLY   G CA  1 
ATOM   7934  C  C   . GLY   G  1 36  ? -28.315 -14.265  -51.233 1.00 24.41 ? 36  GLY   G C   1 
ATOM   7935  O  O   . GLY   G  1 36  ? -27.769 -14.606  -50.187 1.00 29.63 ? 36  GLY   G O   1 
ATOM   7936  N  N   . LEU   G  1 37  ? -29.449 -14.810  -51.650 1.00 26.94 ? 37  LEU   G N   1 
ATOM   7937  C  CA  . LEU   G  1 37  ? -30.102 -15.892  -50.934 1.00 28.56 ? 37  LEU   G CA  1 
ATOM   7938  C  C   . LEU   G  1 37  ? -29.737 -17.209  -51.618 1.00 31.71 ? 37  LEU   G C   1 
ATOM   7939  O  O   . LEU   G  1 37  ? -30.551 -17.871  -52.259 1.00 27.51 ? 37  LEU   G O   1 
ATOM   7940  C  CB  . LEU   G  1 37  ? -31.607 -15.657  -50.901 1.00 27.88 ? 37  LEU   G CB  1 
ATOM   7941  C  CG  . LEU   G  1 37  ? -31.956 -14.341  -50.209 1.00 31.42 ? 37  LEU   G CG  1 
ATOM   7942  C  CD1 . LEU   G  1 37  ? -33.397 -13.908  -50.470 1.00 30.77 ? 37  LEU   G CD1 1 
ATOM   7943  C  CD2 . LEU   G  1 37  ? -31.730 -14.550  -48.723 1.00 31.57 ? 37  LEU   G CD2 1 
ATOM   7944  N  N   . LYS   G  1 38  ? -28.467 -17.591  -51.451 1.00 27.98 ? 38  LYS   G N   1 
ATOM   7945  C  CA  . LYS   G  1 38  ? -27.915 -18.637  -52.309 1.00 31.32 ? 38  LYS   G CA  1 
ATOM   7946  C  C   . LYS   G  1 38  ? -28.420 -20.014  -51.936 1.00 27.77 ? 38  LYS   G C   1 
ATOM   7947  O  O   . LYS   G  1 38  ? -28.413 -20.900  -52.784 1.00 26.82 ? 38  LYS   G O   1 
ATOM   7948  C  CB  . LYS   G  1 38  ? -26.379 -18.642  -52.262 1.00 38.46 ? 38  LYS   G CB  1 
ATOM   7949  C  CG  . LYS   G  1 38  ? -25.713 -17.308  -52.524 1.00 44.47 ? 38  LYS   G CG  1 
ATOM   7950  C  CD  . LYS   G  1 38  ? -25.498 -17.039  -53.989 1.00 45.16 ? 38  LYS   G CD  1 
ATOM   7951  C  CE  . LYS   G  1 38  ? -24.649 -15.775  -54.167 1.00 45.43 ? 38  LYS   G CE  1 
ATOM   7952  N  NZ  . LYS   G  1 38  ? -23.805 -15.774  -55.406 1.00 57.03 ? 38  LYS   G NZ  1 
ATOM   7953  N  N   . ARG   G  1 39  ? -28.889 -20.219  -50.698 1.00 28.76 ? 39  ARG   G N   1 
ATOM   7954  C  CA  . ARG   G  1 39  ? -29.429 -21.525  -50.355 1.00 29.38 ? 39  ARG   G CA  1 
ATOM   7955  C  C   . ARG   G  1 39  ? -30.782 -21.763  -51.025 1.00 24.79 ? 39  ARG   G C   1 
ATOM   7956  O  O   . ARG   G  1 39  ? -31.079 -22.885  -51.461 1.00 29.17 ? 39  ARG   G O   1 
ATOM   7957  C  CB  . ARG   G  1 39  ? -29.549 -21.664  -48.838 1.00 30.38 ? 39  ARG   G CB  1 
ATOM   7958  C  CG  . ARG   G  1 39  ? -29.916 -23.090  -48.393 1.00 30.82 ? 39  ARG   G CG  1 
ATOM   7959  C  CD  . ARG   G  1 39  ? -30.266 -23.126  -46.895 1.00 48.41 ? 39  ARG   G CD  1 
ATOM   7960  N  NE  . ARG   G  1 39  ? -30.014 -24.429  -46.297 1.00 45.71 ? 39  ARG   G NE  1 
ATOM   7961  C  CZ  . ARG   G  1 39  ? -28.983 -24.712  -45.510 1.00 52.26 ? 39  ARG   G CZ  1 
ATOM   7962  N  NH1 . ARG   G  1 39  ? -28.077 -23.798  -45.186 1.00 60.17 ? 39  ARG   G NH1 1 
ATOM   7963  N  NH2 . ARG   G  1 39  ? -28.863 -25.939  -45.026 1.00 50.42 ? 39  ARG   G NH2 1 
ATOM   7964  N  N   . LEU   G  1 40  ? -31.638 -20.742  -51.073 1.00 28.57 ? 40  LEU   G N   1 
ATOM   7965  C  CA  . LEU   G  1 40  ? -32.833 -20.829  -51.907 1.00 27.87 ? 40  LEU   G CA  1 
ATOM   7966  C  C   . LEU   G  1 40  ? -32.466 -20.970  -53.375 1.00 25.44 ? 40  LEU   G C   1 
ATOM   7967  O  O   . LEU   G  1 40  ? -33.082 -21.741  -54.114 1.00 29.15 ? 40  LEU   G O   1 
ATOM   7968  C  CB  . LEU   G  1 40  ? -33.698 -19.591  -51.712 1.00 26.56 ? 40  LEU   G CB  1 
ATOM   7969  C  CG  . LEU   G  1 40  ? -34.553 -19.597  -50.445 1.00 33.35 ? 40  LEU   G CG  1 
ATOM   7970  C  CD1 . LEU   G  1 40  ? -34.957 -18.170  -50.103 1.00 32.21 ? 40  LEU   G CD1 1 
ATOM   7971  C  CD2 . LEU   G  1 40  ? -35.755 -20.521  -50.644 1.00 35.95 ? 40  LEU   G CD2 1 
ATOM   7972  N  N   . GLY   G  1 41  ? -31.472 -20.219  -53.820 1.00 26.57 ? 41  GLY   G N   1 
ATOM   7973  C  CA  . GLY   G  1 41  ? -31.128 -20.268  -55.232 1.00 34.97 ? 41  GLY   G CA  1 
ATOM   7974  C  C   . GLY   G  1 41  ? -30.689 -21.655  -55.648 1.00 32.47 ? 41  GLY   G C   1 
ATOM   7975  O  O   . GLY   G  1 41  ? -31.169 -22.195  -56.652 1.00 30.66 ? 41  GLY   G O   1 
ATOM   7976  N  N   . ALA   G  1 42  ? -29.814 -22.278  -54.834 1.00 28.30 ? 42  ALA   G N   1 
ATOM   7977  C  CA  . ALA   G  1 42  ? -29.330 -23.629  -55.127 1.00 31.58 ? 42  ALA   G CA  1 
ATOM   7978  C  C   . ALA   G  1 42  ? -30.464 -24.642  -55.078 1.00 28.81 ? 42  ALA   G C   1 
ATOM   7979  O  O   . ALA   G  1 42  ? -30.554 -25.530  -55.927 1.00 25.36 ? 42  ALA   G O   1 
ATOM   7980  C  CB  . ALA   G  1 42  ? -28.202 -24.027  -54.138 1.00 29.57 ? 42  ALA   G CB  1 
ATOM   7981  N  N   . HIS   G  1 43  ? -31.356 -24.527  -54.097 1.00 26.76 ? 43  HIS   G N   1 
ATOM   7982  C  CA  . HIS   G  1 43  ? -32.427 -25.504  -54.015 1.00 29.78 ? 43  HIS   G CA  1 
ATOM   7983  C  C   . HIS   G  1 43  ? -33.391 -25.350  -55.189 1.00 28.19 ? 43  HIS   G C   1 
ATOM   7984  O  O   . HIS   G  1 43  ? -33.895 -26.341  -55.730 1.00 26.12 ? 43  HIS   G O   1 
ATOM   7985  C  CB  . HIS   G  1 43  ? -33.161 -25.359  -52.675 1.00 34.59 ? 43  HIS   G CB  1 
ATOM   7986  C  CG  . HIS   G  1 43  ? -34.119 -26.470  -52.412 1.00 31.70 ? 43  HIS   G CG  1 
ATOM   7987  N  ND1 . HIS   G  1 43  ? -35.362 -26.532  -53.002 1.00 36.04 ? 43  HIS   G ND1 1 
ATOM   7988  C  CD2 . HIS   G  1 43  ? -33.994 -27.599  -51.677 1.00 36.10 ? 43  HIS   G CD2 1 
ATOM   7989  C  CE1 . HIS   G  1 43  ? -35.970 -27.642  -52.630 1.00 30.38 ? 43  HIS   G CE1 1 
ATOM   7990  N  NE2 . HIS   G  1 43  ? -35.160 -28.312  -51.832 1.00 33.67 ? 43  HIS   G NE2 1 
ATOM   7991  N  N   . GLU   G  1 44  ? -33.654 -24.114  -55.594 1.00 29.36 ? 44  GLU   G N   1 
ATOM   7992  C  CA  . GLU   G  1 44  ? -34.579 -23.889  -56.690 1.00 29.33 ? 44  GLU   G CA  1 
ATOM   7993  C  C   . GLU   G  1 44  ? -33.944 -24.320  -58.001 1.00 26.95 ? 44  GLU   G C   1 
ATOM   7994  O  O   . GLU   G  1 44  ? -34.638 -24.813  -58.895 1.00 31.04 ? 44  GLU   G O   1 
ATOM   7995  C  CB  . GLU   G  1 44  ? -34.996 -22.411  -56.708 1.00 28.08 ? 44  GLU   G CB  1 
ATOM   7996  C  CG  . GLU   G  1 44  ? -36.116 -22.019  -57.712 1.00 29.16 ? 44  GLU   G CG  1 
ATOM   7997  C  CD  . GLU   G  1 44  ? -37.508 -22.335  -57.167 1.00 32.44 ? 44  GLU   G CD  1 
ATOM   7998  O  OE1 . GLU   G  1 44  ? -37.586 -23.054  -56.146 1.00 34.27 ? 44  GLU   G OE1 1 
ATOM   7999  O  OE2 . GLU   G  1 44  ? -38.499 -21.835  -57.752 1.00 31.37 ? 44  GLU   G OE2 1 
ATOM   8000  N  N   . TYR   G  1 45  ? -32.618 -24.179  -58.114 1.00 28.91 ? 45  TYR   G N   1 
ATOM   8001  C  CA  . TYR   G  1 45  ? -31.924 -24.696  -59.288 1.00 26.51 ? 45  TYR   G CA  1 
ATOM   8002  C  C   . TYR   G  1 45  ? -32.155 -26.190  -59.423 1.00 24.92 ? 45  TYR   G C   1 
ATOM   8003  O  O   . TYR   G  1 45  ? -32.512 -26.690  -60.504 1.00 26.01 ? 45  TYR   G O   1 
ATOM   8004  C  CB  . TYR   G  1 45  ? -30.432 -24.354  -59.185 1.00 28.72 ? 45  TYR   G CB  1 
ATOM   8005  C  CG  . TYR   G  1 45  ? -29.561 -25.082  -60.166 1.00 25.33 ? 45  TYR   G CG  1 
ATOM   8006  C  CD1 . TYR   G  1 45  ? -29.407 -24.599  -61.452 1.00 26.55 ? 45  TYR   G CD1 1 
ATOM   8007  C  CD2 . TYR   G  1 45  ? -28.894 -26.255  -59.813 1.00 29.87 ? 45  TYR   G CD2 1 
ATOM   8008  C  CE1 . TYR   G  1 45  ? -28.613 -25.238  -62.359 1.00 31.97 ? 45  TYR   G CE1 1 
ATOM   8009  C  CE2 . TYR   G  1 45  ? -28.081 -26.919  -60.747 1.00 30.16 ? 45  TYR   G CE2 1 
ATOM   8010  C  CZ  . TYR   G  1 45  ? -27.951 -26.393  -62.010 1.00 35.07 ? 45  TYR   G CZ  1 
ATOM   8011  O  OH  . TYR   G  1 45  ? -27.181 -27.016  -62.985 1.00 38.51 ? 45  TYR   G OH  1 
ATOM   8012  N  N   . HIS   G  1 46  ? -32.035 -26.915  -58.319 1.00 25.67 ? 46  HIS   G N   1 
ATOM   8013  C  CA  . HIS   G  1 46  ? -32.222 -28.356  -58.386 1.00 27.09 ? 46  HIS   G CA  1 
ATOM   8014  C  C   . HIS   G  1 46  ? -33.664 -28.728  -58.671 1.00 28.71 ? 46  HIS   G C   1 
ATOM   8015  O  O   . HIS   G  1 46  ? -33.912 -29.729  -59.343 1.00 28.78 ? 46  HIS   G O   1 
ATOM   8016  C  CB  . HIS   G  1 46  ? -31.709 -29.000  -57.107 1.00 32.06 ? 46  HIS   G CB  1 
ATOM   8017  C  CG  . HIS   G  1 46  ? -30.214 -28.986  -57.027 1.00 40.22 ? 46  HIS   G CG  1 
ATOM   8018  N  ND1 . HIS   G  1 46  ? -29.518 -28.210  -56.123 1.00 44.21 ? 46  HIS   G ND1 1 
ATOM   8019  C  CD2 . HIS   G  1 46  ? -29.277 -29.604  -57.790 1.00 36.92 ? 46  HIS   G CD2 1 
ATOM   8020  C  CE1 . HIS   G  1 46  ? -28.221 -28.357  -56.323 1.00 40.63 ? 46  HIS   G CE1 1 
ATOM   8021  N  NE2 . HIS   G  1 46  ? -28.047 -29.201  -57.328 1.00 46.93 ? 46  HIS   G NE2 1 
ATOM   8022  N  N   . GLU   G  1 47  ? -34.630 -27.940  -58.189 1.00 29.61 ? 47  GLU   G N   1 
ATOM   8023  C  CA  . GLU   G  1 47  ? -36.016 -28.192  -58.574 1.00 33.48 ? 47  GLU   G CA  1 
ATOM   8024  C  C   . GLU   G  1 47  ? -36.194 -28.031  -60.086 1.00 29.79 ? 47  GLU   G C   1 
ATOM   8025  O  O   . GLU   G  1 47  ? -36.870 -28.841  -60.729 1.00 28.09 ? 47  GLU   G O   1 
ATOM   8026  C  CB  . GLU   G  1 47  ? -36.956 -27.246  -57.821 1.00 36.56 ? 47  GLU   G CB  1 
ATOM   8027  C  CG  . GLU   G  1 47  ? -36.992 -27.414  -56.292 1.00 39.37 ? 47  GLU   G CG  1 
ATOM   8028  C  CD  . GLU   G  1 47  ? -37.747 -28.646  -55.824 1.00 49.44 ? 47  GLU   G CD  1 
ATOM   8029  O  OE1 . GLU   G  1 47  ? -38.226 -29.435  -56.671 1.00 59.55 ? 47  GLU   G OE1 1 
ATOM   8030  O  OE2 . GLU   G  1 47  ? -37.882 -28.813  -54.590 1.00 50.39 ? 47  GLU   G OE2 1 
ATOM   8031  N  N   . SER   G  1 48  ? -35.557 -27.013  -60.670 1.00 25.07 ? 48  SER   G N   1 
ATOM   8032  C  CA  . SER   G  1 48  ? -35.620 -26.811  -62.114 1.00 28.53 ? 48  SER   G CA  1 
ATOM   8033  C  C   . SER   G  1 48  ? -35.028 -28.009  -62.864 1.00 29.39 ? 48  SER   G C   1 
ATOM   8034  O  O   . SER   G  1 48  ? -35.610 -28.502  -63.839 1.00 28.92 ? 48  SER   G O   1 
ATOM   8035  C  CB  . SER   G  1 48  ? -34.896 -25.506  -62.473 1.00 26.95 ? 48  SER   G CB  1 
ATOM   8036  O  OG  . SER   G  1 48  ? -35.073 -25.153  -63.850 1.00 28.58 ? 48  SER   G OG  1 
ATOM   8037  N  N   . ILE   G  1 49  ? -33.869 -28.496  -62.414 1.00 29.74 ? 49  ILE   G N   1 
ATOM   8038  C  CA  . ILE   G  1 49  ? -33.239 -29.646  -63.049 1.00 22.27 ? 49  ILE   G CA  1 
ATOM   8039  C  C   . ILE   G  1 49  ? -34.132 -30.864  -62.953 1.00 24.14 ? 49  ILE   G C   1 
ATOM   8040  O  O   . ILE   G  1 49  ? -34.220 -31.660  -63.894 1.00 26.97 ? 49  ILE   G O   1 
ATOM   8041  C  CB  . ILE   G  1 49  ? -31.865 -29.949  -62.389 1.00 25.35 ? 49  ILE   G CB  1 
ATOM   8042  C  CG1 . ILE   G  1 49  ? -30.917 -28.764  -62.505 1.00 30.00 ? 49  ILE   G CG1 1 
ATOM   8043  C  CG2 . ILE   G  1 49  ? -31.290 -31.259  -62.934 1.00 29.00 ? 49  ILE   G CG2 1 
ATOM   8044  C  CD1 . ILE   G  1 49  ? -30.430 -28.508  -63.878 1.00 35.75 ? 49  ILE   G CD1 1 
ATOM   8045  N  N   . ASP   G  1 50  ? -34.774 -31.062  -61.794 1.00 27.65 ? 50  ASP   G N   1 
ATOM   8046  C  CA  . ASP   G  1 50  ? -35.697 -32.186  -61.658 1.00 26.53 ? 50  ASP   G CA  1 
ATOM   8047  C  C   . ASP   G  1 50  ? -36.760 -32.133  -62.739 1.00 26.11 ? 50  ASP   G C   1 
ATOM   8048  O  O   . ASP   G  1 50  ? -37.113 -33.167  -63.321 1.00 28.61 ? 50  ASP   G O   1 
ATOM   8049  C  CB  . ASP   G  1 50  ? -36.381 -32.186  -60.278 1.00 32.79 ? 50  ASP   G CB  1 
ATOM   8050  C  CG  . ASP   G  1 50  ? -35.449 -32.587  -59.142 1.00 55.22 ? 50  ASP   G CG  1 
ATOM   8051  O  OD1 . ASP   G  1 50  ? -34.338 -33.092  -59.416 1.00 50.90 ? 50  ASP   G OD1 1 
ATOM   8052  O  OD2 . ASP   G  1 50  ? -35.840 -32.390  -57.963 1.00 57.66 ? 50  ASP   G OD2 1 
ATOM   8053  N  N   . GLU   G  1 51  ? -37.299 -30.931  -62.997 1.00 28.24 ? 51  GLU   G N   1 
ATOM   8054  C  CA  . GLU   G  1 51  ? -38.379 -30.777  -63.965 1.00 30.63 ? 51  GLU   G CA  1 
ATOM   8055  C  C   . GLU   G  1 51  ? -37.857 -31.005  -65.363 1.00 30.42 ? 51  GLU   G C   1 
ATOM   8056  O  O   . GLU   G  1 51  ? -38.571 -31.517  -66.233 1.00 28.27 ? 51  GLU   G O   1 
ATOM   8057  C  CB  . GLU   G  1 51  ? -38.987 -29.371  -63.893 1.00 28.93 ? 51  GLU   G CB  1 
ATOM   8058  C  CG  . GLU   G  1 51  ? -39.706 -29.033  -62.590 1.00 31.40 ? 51  GLU   G CG  1 
ATOM   8059  C  CD  . GLU   G  1 51  ? -40.930 -29.915  -62.358 1.00 43.03 ? 51  GLU   G CD  1 
ATOM   8060  O  OE1 . GLU   G  1 51  ? -42.017 -29.581  -62.868 1.00 58.60 ? 51  GLU   G OE1 1 
ATOM   8061  O  OE2 . GLU   G  1 51  ? -40.801 -30.947  -61.679 1.00 44.91 ? 51  GLU   G OE2 1 
ATOM   8062  N  N   . MET   G  1 52  ? -36.626 -30.564  -65.602 1.00 24.87 ? 52  MET   G N   1 
ATOM   8063  C  CA  . MET   G  1 52  ? -35.975 -30.850  -66.869 1.00 23.54 ? 52  MET   G CA  1 
ATOM   8064  C  C   . MET   G  1 52  ? -35.918 -32.341  -67.104 1.00 27.35 ? 52  MET   G C   1 
ATOM   8065  O  O   . MET   G  1 52  ? -36.171 -32.819  -68.216 1.00 27.54 ? 52  MET   G O   1 
ATOM   8066  C  CB  . MET   G  1 52  ? -34.566 -30.260  -66.869 1.00 26.72 ? 52  MET   G CB  1 
ATOM   8067  C  CG  . MET   G  1 52  ? -34.528 -28.757  -66.966 1.00 26.86 ? 52  MET   G CG  1 
ATOM   8068  S  SD  . MET   G  1 52  ? -32.831 -28.150  -66.798 1.00 29.20 ? 52  MET   G SD  1 
ATOM   8069  C  CE  . MET   G  1 52  ? -33.070 -26.513  -66.154 1.00 33.35 ? 52  MET   G CE  1 
ATOM   8070  N  N   . LYS   G  1 53  ? -35.572 -33.092  -66.063 1.00 25.43 ? 53  LYS   G N   1 
ATOM   8071  C  CA  . LYS   G  1 53  ? -35.480 -34.539  -66.190 1.00 26.74 ? 53  LYS   G CA  1 
ATOM   8072  C  C   . LYS   G  1 53  ? -36.849 -35.161  -66.432 1.00 26.98 ? 53  LYS   G C   1 
ATOM   8073  O  O   . LYS   G  1 53  ? -36.978 -36.098  -67.233 1.00 26.83 ? 53  LYS   G O   1 
ATOM   8074  C  CB  . LYS   G  1 53  ? -34.839 -35.130  -64.930 1.00 26.57 ? 53  LYS   G CB  1 
ATOM   8075  C  CG  . LYS   G  1 53  ? -33.350 -34.817  -64.742 1.00 31.18 ? 53  LYS   G CG  1 
ATOM   8076  C  CD  . LYS   G  1 53  ? -32.804 -35.500  -63.455 1.00 42.62 ? 53  LYS   G CD  1 
ATOM   8077  C  CE  . LYS   G  1 53  ? -31.383 -35.077  -63.104 1.00 51.86 ? 53  LYS   G CE  1 
ATOM   8078  N  NZ  . LYS   G  1 53  ? -30.833 -35.816  -61.914 1.00 70.60 ? 53  LYS   G NZ  1 
ATOM   8079  N  N   . HIS   G  1 54  ? -37.889 -34.653  -65.759 1.00 26.46 ? 54  HIS   G N   1 
ATOM   8080  C  CA  . HIS   G  1 54  ? -39.235 -35.162  -66.022 1.00 25.52 ? 54  HIS   G CA  1 
ATOM   8081  C  C   . HIS   G  1 54  ? -39.636 -34.886  -67.468 1.00 26.57 ? 54  HIS   G C   1 
ATOM   8082  O  O   . HIS   G  1 54  ? -40.230 -35.739  -68.128 1.00 23.24 ? 54  HIS   G O   1 
ATOM   8083  C  CB  . HIS   G  1 54  ? -40.268 -34.522  -65.075 1.00 27.82 ? 54  HIS   G CB  1 
ATOM   8084  C  CG  . HIS   G  1 54  ? -39.974 -34.691  -63.608 1.00 30.26 ? 54  HIS   G CG  1 
ATOM   8085  N  ND1 . HIS   G  1 54  ? -39.369 -35.812  -63.080 1.00 30.06 ? 54  HIS   G ND1 1 
ATOM   8086  C  CD2 . HIS   G  1 54  ? -40.274 -33.892  -62.550 1.00 30.25 ? 54  HIS   G CD2 1 
ATOM   8087  C  CE1 . HIS   G  1 54  ? -39.254 -35.672  -61.764 1.00 27.02 ? 54  HIS   G CE1 1 
ATOM   8088  N  NE2 . HIS   G  1 54  ? -39.803 -34.517  -61.419 1.00 32.54 ? 54  HIS   G NE2 1 
ATOM   8089  N  N   . ALA   G  1 55  ? -39.365 -33.681  -67.957 1.00 23.49 ? 55  ALA   G N   1 
ATOM   8090  C  CA  . ALA   G  1 55  ? -39.741 -33.354  -69.327 1.00 26.13 ? 55  ALA   G CA  1 
ATOM   8091  C  C   . ALA   G  1 55  ? -39.036 -34.273  -70.313 1.00 32.05 ? 55  ALA   G C   1 
ATOM   8092  O  O   . ALA   G  1 55  ? -39.603 -34.650  -71.345 1.00 25.89 ? 55  ALA   G O   1 
ATOM   8093  C  CB  . ALA   G  1 55  ? -39.414 -31.886  -69.628 1.00 24.34 ? 55  ALA   G CB  1 
ATOM   8094  N  N   . ASP   G  1 56  ? -37.780 -34.621  -70.021 1.00 27.44 ? 56  ASP   G N   1 
ATOM   8095  C  CA  . ASP   G  1 56  ? -37.042 -35.544  -70.875 1.00 27.96 ? 56  ASP   G CA  1 
ATOM   8096  C  C   . ASP   G  1 56  ? -37.783 -36.864  -70.973 1.00 28.06 ? 56  ASP   G C   1 
ATOM   8097  O  O   . ASP   G  1 56  ? -37.988 -37.398  -72.067 1.00 24.71 ? 56  ASP   G O   1 
ATOM   8098  C  CB  . ASP   G  1 56  ? -35.625 -35.748  -70.306 1.00 26.68 ? 56  ASP   G CB  1 
ATOM   8099  C  CG  . ASP   G  1 56  ? -34.727 -36.620  -71.175 1.00 35.63 ? 56  ASP   G CG  1 
ATOM   8100  O  OD1 . ASP   G  1 56  ? -35.017 -36.857  -72.371 1.00 29.07 ? 56  ASP   G OD1 1 
ATOM   8101  O  OD2 . ASP   G  1 56  ? -33.686 -37.074  -70.633 1.00 33.24 ? 56  ASP   G OD2 1 
ATOM   8102  N  N   . LYS   G  1 57  ? -38.157 -37.431  -69.821 1.00 23.60 ? 57  LYS   G N   1 
ATOM   8103  C  CA  . LYS   G  1 57  ? -38.817 -38.730  -69.850 1.00 29.46 ? 57  LYS   G CA  1 
ATOM   8104  C  C   . LYS   G  1 57  ? -40.151 -38.644  -70.591 1.00 27.61 ? 57  LYS   G C   1 
ATOM   8105  O  O   . LYS   G  1 57  ? -40.539 -39.590  -71.278 1.00 25.50 ? 57  LYS   G O   1 
ATOM   8106  C  CB  . LYS   G  1 57  ? -39.049 -39.249  -68.428 1.00 28.71 ? 57  LYS   G CB  1 
ATOM   8107  C  CG  . LYS   G  1 57  ? -37.775 -39.607  -67.614 1.00 28.25 ? 57  LYS   G CG  1 
ATOM   8108  C  CD  . LYS   G  1 57  ? -36.858 -40.533  -68.384 1.00 41.08 ? 57  LYS   G CD  1 
ATOM   8109  N  N   . LEU   G  1 58  ? -40.861 -37.531  -70.451 1.00 25.89 ? 58  LEU   G N   1 
ATOM   8110  C  CA  . LEU   G  1 58  ? -42.153 -37.400  -71.139 1.00 29.50 ? 58  LEU   G CA  1 
ATOM   8111  C  C   . LEU   G  1 58  ? -41.946 -37.301  -72.642 1.00 31.57 ? 58  LEU   G C   1 
ATOM   8112  O  O   . LEU   G  1 58  ? -42.650 -37.958  -73.422 1.00 27.57 ? 58  LEU   G O   1 
ATOM   8113  C  CB  . LEU   G  1 58  ? -42.889 -36.175  -70.632 1.00 26.85 ? 58  LEU   G CB  1 
ATOM   8114  C  CG  . LEU   G  1 58  ? -43.545 -36.297  -69.241 1.00 23.96 ? 58  LEU   G CG  1 
ATOM   8115  C  CD1 . LEU   G  1 58  ? -43.844 -34.916  -68.774 1.00 25.06 ? 58  LEU   G CD1 1 
ATOM   8116  C  CD2 . LEU   G  1 58  ? -44.813 -37.151  -69.285 1.00 32.35 ? 58  LEU   G CD2 1 
ATOM   8117  N  N   . ILE   G  1 59  ? -40.981 -36.468  -73.058 1.00 30.92 ? 59  ILE   G N   1 
ATOM   8118  C  CA  . ILE   G  1 59  ? -40.602 -36.388  -74.469 1.00 24.60 ? 59  ILE   G CA  1 
ATOM   8119  C  C   . ILE   G  1 59  ? -40.270 -37.772  -75.001 1.00 26.22 ? 59  ILE   G C   1 
ATOM   8120  O  O   . ILE   G  1 59  ? -40.774 -38.196  -76.056 1.00 27.78 ? 59  ILE   G O   1 
ATOM   8121  C  CB  . ILE   G  1 59  ? -39.432 -35.404  -74.663 1.00 27.53 ? 59  ILE   G CB  1 
ATOM   8122  C  CG1 . ILE   G  1 59  ? -39.885 -33.998  -74.309 1.00 27.56 ? 59  ILE   G CG1 1 
ATOM   8123  C  CG2 . ILE   G  1 59  ? -38.925 -35.461  -76.101 1.00 31.56 ? 59  ILE   G CG2 1 
ATOM   8124  C  CD1 . ILE   G  1 59  ? -38.770 -32.992  -74.255 1.00 29.98 ? 59  ILE   G CD1 1 
ATOM   8125  N  N   . GLU   G  1 60  ? -39.457 -38.524  -74.253 1.00 25.24 ? 60  GLU   G N   1 
ATOM   8126  C  CA  . GLU   G  1 60  ? -39.071 -39.855  -74.709 1.00 23.14 ? 60  GLU   G CA  1 
ATOM   8127  C  C   . GLU   G  1 60  ? -40.280 -40.783  -74.812 1.00 31.95 ? 60  GLU   G C   1 
ATOM   8128  O  O   . GLU   G  1 60  ? -40.380 -41.597  -75.747 1.00 27.44 ? 60  GLU   G O   1 
ATOM   8129  C  CB  . GLU   G  1 60  ? -38.009 -40.441  -73.774 1.00 27.65 ? 60  GLU   G CB  1 
ATOM   8130  C  CG  . GLU   G  1 60  ? -36.666 -39.645  -73.854 1.00 26.67 ? 60  GLU   G CG  1 
ATOM   8131  C  CD  . GLU   G  1 60  ? -35.688 -40.053  -72.755 1.00 39.28 ? 60  GLU   G CD  1 
ATOM   8132  O  OE1 . GLU   G  1 60  ? -36.147 -40.482  -71.666 1.00 34.75 ? 60  GLU   G OE1 1 
ATOM   8133  O  OE2 . GLU   G  1 60  ? -34.466 -39.959  -73.000 1.00 35.25 ? 60  GLU   G OE2 1 
ATOM   8134  N  N   . ARG   G  1 61  ? -41.223 -40.658  -73.880 1.00 28.10 ? 61  ARG   G N   1 
ATOM   8135  C  CA  . ARG   G  1 61  ? -42.390 -41.539  -73.905 1.00 26.76 ? 61  ARG   G CA  1 
ATOM   8136  C  C   . ARG   G  1 61  ? -43.313 -41.206  -75.073 1.00 23.90 ? 61  ARG   G C   1 
ATOM   8137  O  O   . ARG   G  1 61  ? -43.858 -42.111  -75.718 1.00 26.61 ? 61  ARG   G O   1 
ATOM   8138  C  CB  . ARG   G  1 61  ? -43.144 -41.424  -72.573 1.00 26.88 ? 61  ARG   G CB  1 
ATOM   8139  C  CG  . ARG   G  1 61  ? -44.365 -42.332  -72.428 1.00 27.62 ? 61  ARG   G CG  1 
ATOM   8140  C  CD  . ARG   G  1 61  ? -43.984 -43.762  -72.238 1.00 30.77 ? 61  ARG   G CD  1 
ATOM   8141  N  NE  . ARG   G  1 61  ? -45.126 -44.663  -72.169 1.00 30.17 ? 61  ARG   G NE  1 
ATOM   8142  C  CZ  . ARG   G  1 61  ? -45.046 -45.970  -72.369 1.00 32.59 ? 61  ARG   G CZ  1 
ATOM   8143  N  NH1 . ARG   G  1 61  ? -43.893 -46.558  -72.624 1.00 29.70 ? 61  ARG   G NH1 1 
ATOM   8144  N  NH2 . ARG   G  1 61  ? -46.151 -46.707  -72.333 1.00 31.56 ? 61  ARG   G NH2 1 
ATOM   8145  N  N   . ILE   G  1 62  ? -43.519 -39.916  -75.332 1.00 24.90 ? 62  ILE   G N   1 
ATOM   8146  C  CA  . ILE   G  1 62  ? -44.397 -39.488  -76.414 1.00 32.40 ? 62  ILE   G CA  1 
ATOM   8147  C  C   . ILE   G  1 62  ? -43.873 -39.971  -77.748 1.00 35.90 ? 62  ILE   G C   1 
ATOM   8148  O  O   . ILE   G  1 62  ? -44.642 -40.417  -78.605 1.00 28.55 ? 62  ILE   G O   1 
ATOM   8149  C  CB  . ILE   G  1 62  ? -44.539 -37.956  -76.393 1.00 29.97 ? 62  ILE   G CB  1 
ATOM   8150  C  CG1 . ILE   G  1 62  ? -45.322 -37.517  -75.158 1.00 27.89 ? 62  ILE   G CG1 1 
ATOM   8151  C  CG2 . ILE   G  1 62  ? -45.160 -37.434  -77.708 1.00 27.75 ? 62  ILE   G CG2 1 
ATOM   8152  C  CD1 . ILE   G  1 62  ? -45.209 -36.030  -74.901 1.00 31.04 ? 62  ILE   G CD1 1 
ATOM   8153  N  N   . LEU   G  1 63  ? -42.553 -39.895  -77.947 1.00 29.49 ? 63  LEU   G N   1 
ATOM   8154  C  CA  . LEU   G  1 63  ? -41.971 -40.322  -79.211 1.00 28.57 ? 63  LEU   G CA  1 
ATOM   8155  C  C   . LEU   G  1 63  ? -42.091 -41.822  -79.392 1.00 27.69 ? 63  LEU   G C   1 
ATOM   8156  O  O   . LEU   G  1 63  ? -42.381 -42.294  -80.492 1.00 26.97 ? 63  LEU   G O   1 
ATOM   8157  C  CB  . LEU   G  1 63  ? -40.503 -39.883  -79.283 1.00 29.81 ? 63  LEU   G CB  1 
ATOM   8158  C  CG  . LEU   G  1 63  ? -40.245 -38.388  -79.495 1.00 29.04 ? 63  LEU   G CG  1 
ATOM   8159  C  CD1 . LEU   G  1 63  ? -38.791 -38.021  -79.216 1.00 34.45 ? 63  LEU   G CD1 1 
ATOM   8160  C  CD2 . LEU   G  1 63  ? -40.651 -37.964  -80.911 1.00 29.08 ? 63  LEU   G CD2 1 
ATOM   8161  N  N   . PHE   G  1 64  ? -41.868 -42.585  -78.324 1.00 24.96 ? 64  PHE   G N   1 
ATOM   8162  C  CA  . PHE   G  1 64  ? -42.074 -44.030  -78.376 1.00 31.31 ? 64  PHE   G CA  1 
ATOM   8163  C  C   . PHE   G  1 64  ? -43.510 -44.385  -78.762 1.00 29.67 ? 64  PHE   G C   1 
ATOM   8164  O  O   . PHE   G  1 64  ? -43.746 -45.369  -79.479 1.00 27.62 ? 64  PHE   G O   1 
ATOM   8165  C  CB  . PHE   G  1 64  ? -41.755 -44.655  -77.017 1.00 31.69 ? 64  PHE   G CB  1 
ATOM   8166  C  CG  . PHE   G  1 64  ? -42.175 -46.113  -76.902 1.00 30.54 ? 64  PHE   G CG  1 
ATOM   8167  C  CD1 . PHE   G  1 64  ? -41.565 -47.076  -77.669 1.00 31.05 ? 64  PHE   G CD1 1 
ATOM   8168  C  CD2 . PHE   G  1 64  ? -43.181 -46.502  -76.031 1.00 30.39 ? 64  PHE   G CD2 1 
ATOM   8169  C  CE1 . PHE   G  1 64  ? -41.918 -48.394  -77.571 1.00 27.57 ? 64  PHE   G CE1 1 
ATOM   8170  C  CE2 . PHE   G  1 64  ? -43.546 -47.837  -75.922 1.00 31.55 ? 64  PHE   G CE2 1 
ATOM   8171  C  CZ  . PHE   G  1 64  ? -42.916 -48.783  -76.692 1.00 32.69 ? 64  PHE   G CZ  1 
ATOM   8172  N  N   . LEU   G  1 65  ? -44.481 -43.628  -78.245 1.00 30.08 ? 65  LEU   G N   1 
ATOM   8173  C  CA  . LEU   G  1 65  ? -45.888 -43.816  -78.557 1.00 34.72 ? 65  LEU   G CA  1 
ATOM   8174  C  C   . LEU   G  1 65  ? -46.253 -43.173  -79.892 1.00 35.97 ? 65  LEU   G C   1 
ATOM   8175  O  O   . LEU   G  1 65  ? -47.432 -43.120  -80.249 1.00 34.78 ? 65  LEU   G O   1 
ATOM   8176  C  CB  . LEU   G  1 65  ? -46.751 -43.239  -77.421 1.00 30.80 ? 65  LEU   G CB  1 
ATOM   8177  C  CG  . LEU   G  1 65  ? -46.650 -43.956  -76.066 1.00 32.51 ? 65  LEU   G CG  1 
ATOM   8178  C  CD1 . LEU   G  1 65  ? -47.554 -43.312  -75.042 1.00 33.29 ? 65  LEU   G CD1 1 
ATOM   8179  C  CD2 . LEU   G  1 65  ? -46.968 -45.447  -76.170 1.00 32.21 ? 65  LEU   G CD2 1 
ATOM   8180  N  N   . GLU   G  1 66  ? -45.253 -42.665  -80.616 1.00 37.95 ? 66  GLU   G N   1 
ATOM   8181  C  CA  . GLU   G  1 66  ? -45.414 -42.156  -81.967 1.00 34.40 ? 66  GLU   G CA  1 
ATOM   8182  C  C   . GLU   G  1 66  ? -46.263 -40.891  -82.005 1.00 34.01 ? 66  GLU   G C   1 
ATOM   8183  O  O   . GLU   G  1 66  ? -46.964 -40.635  -82.977 1.00 35.61 ? 66  GLU   G O   1 
ATOM   8184  C  CB  . GLU   G  1 66  ? -45.982 -43.236  -82.891 1.00 33.01 ? 66  GLU   G CB  1 
ATOM   8185  C  CG  . GLU   G  1 66  ? -45.132 -44.506  -82.833 1.00 33.43 ? 66  GLU   G CG  1 
ATOM   8186  C  CD  . GLU   G  1 66  ? -45.615 -45.593  -83.740 1.00 37.83 ? 66  GLU   G CD  1 
ATOM   8187  O  OE1 . GLU   G  1 66  ? -46.451 -45.283  -84.611 1.00 47.94 ? 66  GLU   G OE1 1 
ATOM   8188  O  OE2 . GLU   G  1 66  ? -45.170 -46.756  -83.584 1.00 36.77 ? 66  GLU   G OE2 1 
ATOM   8189  N  N   . GLY   G  1 67  ? -46.196 -40.083  -80.952 1.00 29.24 ? 67  GLY   G N   1 
ATOM   8190  C  CA  . GLY   G  1 67  ? -46.746 -38.746  -80.962 1.00 28.05 ? 67  GLY   G CA  1 
ATOM   8191  C  C   . GLY   G  1 67  ? -45.678 -37.682  -81.173 1.00 36.17 ? 67  GLY   G C   1 
ATOM   8192  O  O   . GLY   G  1 67  ? -44.491 -37.966  -81.305 1.00 32.65 ? 67  GLY   G O   1 
ATOM   8193  N  N   . LEU   G  1 68  ? -46.128 -36.424  -81.189 1.00 33.43 ? 68  LEU   G N   1 
ATOM   8194  C  CA  . LEU   G  1 68  ? -45.233 -35.298  -81.436 1.00 32.00 ? 68  LEU   G CA  1 
ATOM   8195  C  C   . LEU   G  1 68  ? -45.113 -34.469  -80.170 1.00 34.65 ? 68  LEU   G C   1 
ATOM   8196  O  O   . LEU   G  1 68  ? -46.098 -33.833  -79.760 1.00 33.24 ? 68  LEU   G O   1 
ATOM   8197  C  CB  . LEU   G  1 68  ? -45.729 -34.422  -82.593 1.00 43.24 ? 68  LEU   G CB  1 
ATOM   8198  C  CG  . LEU   G  1 68  ? -45.796 -35.061  -83.991 1.00 53.98 ? 68  LEU   G CG  1 
ATOM   8199  C  CD1 . LEU   G  1 68  ? -46.538 -34.139  -84.947 1.00 51.44 ? 68  LEU   G CD1 1 
ATOM   8200  C  CD2 . LEU   G  1 68  ? -44.405 -35.394  -84.544 1.00 54.72 ? 68  LEU   G CD2 1 
ATOM   8201  N  N   . PRO   G  1 69  ? -43.967 -34.473  -79.489 1.00 32.18 ? 69  PRO   G N   1 
ATOM   8202  C  CA  . PRO   G  1 69  ? -43.849 -33.669  -78.275 1.00 26.59 ? 69  PRO   G CA  1 
ATOM   8203  C  C   . PRO   G  1 69  ? -44.009 -32.210  -78.627 1.00 30.23 ? 69  PRO   G C   1 
ATOM   8204  O  O   . PRO   G  1 69  ? -43.478 -31.738  -79.631 1.00 33.59 ? 69  PRO   G O   1 
ATOM   8205  C  CB  . PRO   G  1 69  ? -42.429 -33.985  -77.756 1.00 27.32 ? 69  PRO   G CB  1 
ATOM   8206  C  CG  . PRO   G  1 69  ? -42.059 -35.287  -78.386 1.00 36.58 ? 69  PRO   G CG  1 
ATOM   8207  C  CD  . PRO   G  1 69  ? -42.776 -35.307  -79.728 1.00 36.36 ? 69  PRO   G CD  1 
ATOM   8208  N  N   . ASN   G  1 70  ? -44.765 -31.496  -77.805 1.00 28.38 ? 70  ASN   G N   1 
ATOM   8209  C  CA  . ASN   G  1 70  ? -45.003 -30.070  -78.017 1.00 35.09 ? 70  ASN   G CA  1 
ATOM   8210  C  C   . ASN   G  1 70  ? -44.035 -29.285  -77.127 1.00 31.48 ? 70  ASN   G C   1 
ATOM   8211  O  O   . ASN   G  1 70  ? -44.247 -29.134  -75.925 1.00 30.56 ? 70  ASN   G O   1 
ATOM   8212  C  CB  . ASN   G  1 70  ? -46.474 -29.749  -77.742 1.00 33.35 ? 70  ASN   G CB  1 
ATOM   8213  C  CG  . ASN   G  1 70  ? -46.815 -28.301  -77.980 1.00 36.69 ? 70  ASN   G CG  1 
ATOM   8214  O  OD1 . ASN   G  1 70  ? -45.942 -27.444  -78.067 1.00 32.51 ? 70  ASN   G OD1 1 
ATOM   8215  N  ND2 . ASN   G  1 70  ? -48.118 -28.012  -78.080 1.00 44.79 ? 70  ASN   G ND2 1 
ATOM   8216  N  N   . LEU   G  1 71  ? -42.946 -28.803  -77.711 1.00 27.80 ? 71  LEU   G N   1 
ATOM   8217  C  CA  . LEU   G  1 71  ? -42.031 -27.912  -77.007 1.00 36.30 ? 71  LEU   G CA  1 
ATOM   8218  C  C   . LEU   G  1 71  ? -42.210 -26.470  -77.436 1.00 28.38 ? 71  LEU   G C   1 
ATOM   8219  O  O   . LEU   G  1 71  ? -41.372 -25.629  -77.122 1.00 33.47 ? 71  LEU   G O   1 
ATOM   8220  C  CB  . LEU   G  1 71  ? -40.575 -28.335  -77.219 1.00 35.08 ? 71  LEU   G CB  1 
ATOM   8221  C  CG  . LEU   G  1 71  ? -40.113 -29.556  -76.417 1.00 35.25 ? 71  LEU   G CG  1 
ATOM   8222  C  CD1 . LEU   G  1 71  ? -40.576 -30.817  -77.056 1.00 31.48 ? 71  LEU   G CD1 1 
ATOM   8223  C  CD2 . LEU   G  1 71  ? -38.610 -29.563  -76.284 1.00 36.27 ? 71  LEU   G CD2 1 
ATOM   8224  N  N   . GLN   G  1 72  ? -43.288 -26.178  -78.161 1.00 33.04 ? 72  GLN   G N   1 
ATOM   8225  C  CA  . GLN   G  1 72  ? -43.543 -24.879  -78.759 1.00 26.54 ? 72  GLN   G CA  1 
ATOM   8226  C  C   . GLN   G  1 72  ? -44.471 -24.010  -77.920 1.00 28.36 ? 72  GLN   G C   1 
ATOM   8227  O  O   . GLN   G  1 72  ? -44.263 -22.799  -77.816 1.00 27.82 ? 72  GLN   G O   1 
ATOM   8228  C  CB  . GLN   G  1 72  ? -44.160 -25.076  -80.153 1.00 33.50 ? 72  GLN   G CB  1 
ATOM   8229  C  CG  . GLN   G  1 72  ? -44.428 -23.767  -80.940 1.00 32.76 ? 72  GLN   G CG  1 
ATOM   8230  C  CD  . GLN   G  1 72  ? -43.141 -23.019  -81.358 1.00 27.09 ? 72  GLN   G CD  1 
ATOM   8231  O  OE1 . GLN   G  1 72  ? -42.580 -23.261  -82.434 1.00 31.35 ? 72  GLN   G OE1 1 
ATOM   8232  N  NE2 . GLN   G  1 72  ? -42.704 -22.092  -80.526 1.00 30.60 ? 72  GLN   G NE2 1 
ATOM   8233  N  N   . ASP   G  1 73  ? -45.497 -24.600  -77.334 1.00 33.28 ? 73  ASP   G N   1 
ATOM   8234  C  CA  . ASP   G  1 73  ? -46.492 -23.845  -76.589 1.00 34.19 ? 73  ASP   G CA  1 
ATOM   8235  C  C   . ASP   G  1 73  ? -46.039 -23.717  -75.131 1.00 42.10 ? 73  ASP   G C   1 
ATOM   8236  O  O   . ASP   G  1 73  ? -45.876 -24.715  -74.416 1.00 41.32 ? 73  ASP   G O   1 
ATOM   8237  C  CB  . ASP   G  1 73  ? -47.855 -24.534  -76.725 1.00 34.57 ? 73  ASP   G CB  1 
ATOM   8238  C  CG  . ASP   G  1 73  ? -48.337 -24.593  -78.191 1.00 34.83 ? 73  ASP   G CG  1 
ATOM   8239  O  OD1 . ASP   G  1 73  ? -47.994 -23.687  -78.984 1.00 38.04 ? 73  ASP   G OD1 1 
ATOM   8240  O  OD2 . ASP   G  1 73  ? -49.003 -25.575  -78.570 1.00 44.05 ? 73  ASP   G OD2 1 
ATOM   8241  N  N   . LEU   G  1 74  ? -45.805 -22.490  -74.703 1.00 37.79 ? 74  LEU   G N   1 
ATOM   8242  C  CA  . LEU   G  1 74  ? -45.390 -22.206  -73.342 1.00 43.50 ? 74  LEU   G CA  1 
ATOM   8243  C  C   . LEU   G  1 74  ? -46.481 -21.385  -72.671 1.00 40.46 ? 74  LEU   G C   1 
ATOM   8244  O  O   . LEU   G  1 74  ? -46.775 -20.280  -73.126 1.00 38.78 ? 74  LEU   G O   1 
ATOM   8245  C  CB  . LEU   G  1 74  ? -44.071 -21.441  -73.339 1.00 34.59 ? 74  LEU   G CB  1 
ATOM   8246  C  CG  . LEU   G  1 74  ? -43.489 -21.113  -71.972 1.00 38.14 ? 74  LEU   G CG  1 
ATOM   8247  C  CD1 . LEU   G  1 74  ? -43.183 -22.402  -71.218 1.00 37.95 ? 74  LEU   G CD1 1 
ATOM   8248  C  CD2 . LEU   G  1 74  ? -42.248 -20.262  -72.120 1.00 36.07 ? 74  LEU   G CD2 1 
ATOM   8249  N  N   . GLY   G  1 75  ? -47.055 -21.917  -71.590 1.00 39.00 ? 75  GLY   G N   1 
ATOM   8250  C  CA  . GLY   G  1 75  ? -48.077 -21.226  -70.824 1.00 39.60 ? 75  GLY   G CA  1 
ATOM   8251  C  C   . GLY   G  1 75  ? -47.506 -20.102  -69.981 1.00 44.26 ? 75  GLY   G C   1 
ATOM   8252  O  O   . GLY   G  1 75  ? -46.324 -19.770  -70.040 1.00 32.73 ? 75  GLY   G O   1 
ATOM   8253  N  N   . LYS   G  1 76  ? -48.382 -19.499  -69.169 1.00 34.01 ? 76  LYS   G N   1 
ATOM   8254  C  CA  . LYS   G  1 76  ? -47.979 -18.332  -68.391 1.00 42.39 ? 76  LYS   G CA  1 
ATOM   8255  C  C   . LYS   G  1 76  ? -47.083 -18.754  -67.236 1.00 36.47 ? 76  LYS   G C   1 
ATOM   8256  O  O   . LYS   G  1 76  ? -47.422 -19.666  -66.476 1.00 36.06 ? 76  LYS   G O   1 
ATOM   8257  C  CB  . LYS   G  1 76  ? -49.194 -17.579  -67.835 1.00 38.03 ? 76  LYS   G CB  1 
ATOM   8258  C  CG  . LYS   G  1 76  ? -48.814 -16.172  -67.271 1.00 32.34 ? 76  LYS   G CG  1 
ATOM   8259  N  N   . LEU   G  1 77  ? -45.945 -18.076  -67.101 1.00 39.61 ? 77  LEU   G N   1 
ATOM   8260  C  CA  . LEU   G  1 77  ? -45.074 -18.263  -65.951 1.00 42.87 ? 77  LEU   G CA  1 
ATOM   8261  C  C   . LEU   G  1 77  ? -45.622 -17.461  -64.781 1.00 39.30 ? 77  LEU   G C   1 
ATOM   8262  O  O   . LEU   G  1 77  ? -46.015 -16.307  -64.942 1.00 32.34 ? 77  LEU   G O   1 
ATOM   8263  C  CB  . LEU   G  1 77  ? -43.645 -17.788  -66.250 1.00 33.88 ? 77  LEU   G CB  1 
ATOM   8264  C  CG  . LEU   G  1 77  ? -42.928 -18.270  -67.531 1.00 31.91 ? 77  LEU   G CG  1 
ATOM   8265  C  CD1 . LEU   G  1 77  ? -41.498 -17.766  -67.507 1.00 37.12 ? 77  LEU   G CD1 1 
ATOM   8266  C  CD2 . LEU   G  1 77  ? -42.976 -19.783  -67.738 1.00 32.84 ? 77  LEU   G CD2 1 
ATOM   8267  N  N   . LEU   G  1 78  ? -45.583 -18.050  -63.593 1.00 40.04 ? 78  LEU   G N   1 
ATOM   8268  C  CA  . LEU   G  1 78  ? -45.944 -17.350  -62.366 1.00 36.78 ? 78  LEU   G CA  1 
ATOM   8269  C  C   . LEU   G  1 78  ? -44.650 -16.894  -61.695 1.00 37.61 ? 78  LEU   G C   1 
ATOM   8270  O  O   . LEU   G  1 78  ? -44.005 -17.674  -60.993 1.00 34.53 ? 78  LEU   G O   1 
ATOM   8271  C  CB  . LEU   G  1 78  ? -46.755 -18.270  -61.457 1.00 37.81 ? 78  LEU   G CB  1 
ATOM   8272  C  CG  . LEU   G  1 78  ? -47.855 -19.078  -62.147 1.00 45.00 ? 78  LEU   G CG  1 
ATOM   8273  C  CD1 . LEU   G  1 78  ? -48.614 -19.928  -61.145 1.00 41.44 ? 78  LEU   G CD1 1 
ATOM   8274  C  CD2 . LEU   G  1 78  ? -48.820 -18.161  -62.909 1.00 50.22 ? 78  LEU   G CD2 1 
ATOM   8275  N  N   . ILE   G  1 79  ? -44.271 -15.629  -61.893 1.00 37.38 ? 79  ILE   G N   1 
ATOM   8276  C  CA  . ILE   G  1 79  ? -43.017 -15.092  -61.361 1.00 42.82 ? 79  ILE   G CA  1 
ATOM   8277  C  C   . ILE   G  1 79  ? -43.340 -14.137  -60.224 1.00 45.90 ? 79  ILE   G C   1 
ATOM   8278  O  O   . ILE   G  1 79  ? -44.060 -13.151  -60.420 1.00 46.75 ? 79  ILE   G O   1 
ATOM   8279  C  CB  . ILE   G  1 79  ? -42.195 -14.366  -62.438 1.00 37.72 ? 79  ILE   G CB  1 
ATOM   8280  C  CG1 . ILE   G  1 79  ? -41.930 -15.287  -63.633 1.00 41.49 ? 79  ILE   G CG1 1 
ATOM   8281  C  CG2 . ILE   G  1 79  ? -40.894 -13.855  -61.840 1.00 39.86 ? 79  ILE   G CG2 1 
ATOM   8282  C  CD1 . ILE   G  1 79  ? -41.404 -16.623  -63.252 1.00 41.33 ? 79  ILE   G CD1 1 
ATOM   8283  N  N   . GLY   G  1 80  ? -42.784 -14.403  -59.043 1.00 37.83 ? 80  GLY   G N   1 
ATOM   8284  C  CA  . GLY   G  1 80  ? -42.992 -13.519  -57.919 1.00 39.47 ? 80  GLY   G CA  1 
ATOM   8285  C  C   . GLY   G  1 80  ? -41.934 -12.460  -57.884 1.00 38.61 ? 80  GLY   G C   1 
ATOM   8286  O  O   . GLY   G  1 80  ? -40.953 -12.522  -58.609 1.00 41.33 ? 80  GLY   G O   1 
ATOM   8287  N  N   . GLU   G  1 81  ? -42.145 -11.461  -57.033 1.00 38.35 ? 81  GLU   G N   1 
ATOM   8288  C  CA  . GLU   G  1 81  ? -41.152 -10.411  -56.846 1.00 44.08 ? 81  GLU   G CA  1 
ATOM   8289  C  C   . GLU   G  1 81  ? -40.629 -10.364  -55.421 1.00 36.30 ? 81  GLU   G C   1 
ATOM   8290  O  O   . GLU   G  1 81  ? -39.851 -9.461   -55.086 1.00 45.45 ? 81  GLU   G O   1 
ATOM   8291  C  CB  . GLU   G  1 81  ? -41.727 -9.051   -57.249 1.00 60.41 ? 81  GLU   G CB  1 
ATOM   8292  C  CG  . GLU   G  1 81  ? -41.795 -8.866   -58.761 1.00 66.53 ? 81  GLU   G CG  1 
ATOM   8293  C  CD  . GLU   G  1 81  ? -43.116 -8.289   -59.195 1.00 64.91 ? 81  GLU   G CD  1 
ATOM   8294  O  OE1 . GLU   G  1 81  ? -43.256 -7.047   -59.171 1.00 66.26 ? 81  GLU   G OE1 1 
ATOM   8295  O  OE2 . GLU   G  1 81  ? -44.026 -9.077   -59.526 1.00 65.06 ? 81  GLU   G OE2 1 
ATOM   8296  N  N   . ASN   G  1 82  ? -40.999 -11.331  -54.589 1.00 37.32 ? 82  ASN   G N   1 
ATOM   8297  C  CA  . ASN   G  1 82  ? -40.414 -11.468  -53.264 1.00 31.92 ? 82  ASN   G CA  1 
ATOM   8298  C  C   . ASN   G  1 82  ? -40.448 -12.941  -52.902 1.00 33.58 ? 82  ASN   G C   1 
ATOM   8299  O  O   . ASN   G  1 82  ? -41.177 -13.744  -53.509 1.00 31.52 ? 82  ASN   G O   1 
ATOM   8300  C  CB  . ASN   G  1 82  ? -41.154 -10.647  -52.200 1.00 36.87 ? 82  ASN   G CB  1 
ATOM   8301  C  CG  . ASN   G  1 82  ? -42.563 -11.112  -52.019 1.00 36.79 ? 82  ASN   G CG  1 
ATOM   8302  O  OD1 . ASN   G  1 82  ? -42.825 -12.118  -51.356 1.00 39.74 ? 82  ASN   G OD1 1 
ATOM   8303  N  ND2 . ASN   G  1 82  ? -43.487 -10.420  -52.657 1.00 50.74 ? 82  ASN   G ND2 1 
ATOM   8304  N  N   . THR   G  1 83  ? -39.678 -13.282  -51.868 1.00 32.71 ? 83  THR   G N   1 
ATOM   8305  C  CA  . THR   G  1 83  ? -39.467 -14.692  -51.555 1.00 31.03 ? 83  THR   G CA  1 
ATOM   8306  C  C   . THR   G  1 83  ? -40.789 -15.392  -51.268 1.00 29.40 ? 83  THR   G C   1 
ATOM   8307  O  O   . THR   G  1 83  ? -41.083 -16.451  -51.830 1.00 27.87 ? 83  THR   G O   1 
ATOM   8308  C  CB  . THR   G  1 83  ? -38.492 -14.821  -50.376 1.00 28.89 ? 83  THR   G CB  1 
ATOM   8309  O  OG1 . THR   G  1 83  ? -37.212 -14.343  -50.783 1.00 29.19 ? 83  THR   G OG1 1 
ATOM   8310  C  CG2 . THR   G  1 83  ? -38.322 -16.256  -49.956 1.00 29.58 ? 83  THR   G CG2 1 
ATOM   8311  N  N   . GLN   G  1 84  ? -41.618 -14.812  -50.401 1.00 30.11 ? 84  GLN   G N   1 
ATOM   8312  C  CA  . GLN   G  1 84  ? -42.877 -15.469  -50.086 1.00 34.03 ? 84  GLN   G CA  1 
ATOM   8313  C  C   . GLN   G  1 84  ? -43.732 -15.627  -51.332 1.00 31.17 ? 84  GLN   G C   1 
ATOM   8314  O  O   . GLN   G  1 84  ? -44.349 -16.674  -51.552 1.00 29.24 ? 84  GLN   G O   1 
ATOM   8315  C  CB  . GLN   G  1 84  ? -43.600 -14.664  -49.011 1.00 39.40 ? 84  GLN   G CB  1 
ATOM   8316  C  CG  . GLN   G  1 84  ? -44.827 -15.292  -48.482 1.00 45.59 ? 84  GLN   G CG  1 
ATOM   8317  C  CD  . GLN   G  1 84  ? -45.286 -14.557  -47.256 1.00 51.33 ? 84  GLN   G CD  1 
ATOM   8318  O  OE1 . GLN   G  1 84  ? -44.756 -13.489  -46.916 1.00 52.90 ? 84  GLN   G OE1 1 
ATOM   8319  N  NE2 . GLN   G  1 84  ? -46.228 -15.132  -46.561 1.00 50.12 ? 84  GLN   G NE2 1 
ATOM   8320  N  N   . GLU   G  1 85  ? -43.762 -14.612  -52.173 1.00 30.98 ? 85  GLU   G N   1 
ATOM   8321  C  CA  . GLU   G  1 85  ? -44.594 -14.712  -53.360 1.00 35.87 ? 85  GLU   G CA  1 
ATOM   8322  C  C   . GLU   G  1 85  ? -44.039 -15.736  -54.347 1.00 31.59 ? 85  GLU   G C   1 
ATOM   8323  O  O   . GLU   G  1 85  ? -44.801 -16.477  -54.968 1.00 28.70 ? 85  GLU   G O   1 
ATOM   8324  C  CB  . GLU   G  1 85  ? -44.703 -13.346  -54.016 1.00 38.09 ? 85  GLU   G CB  1 
ATOM   8325  C  CG  . GLU   G  1 85  ? -45.684 -13.328  -55.164 1.00 49.34 ? 85  GLU   G CG  1 
ATOM   8326  C  CD  . GLU   G  1 85  ? -45.836 -11.954  -55.760 1.00 54.85 ? 85  GLU   G CD  1 
ATOM   8327  O  OE1 . GLU   G  1 85  ? -44.803 -11.294  -55.995 1.00 54.24 ? 85  GLU   G OE1 1 
ATOM   8328  O  OE2 . GLU   G  1 85  ? -46.989 -11.532  -55.974 1.00 73.69 ? 85  GLU   G OE2 1 
ATOM   8329  N  N   . MET   G  1 86  ? -42.706 -15.801  -54.496 1.00 33.73 ? 86  MET   G N   1 
ATOM   8330  C  CA  . MET   G  1 86  ? -42.122 -16.783  -55.409 1.00 25.54 ? 86  MET   G CA  1 
ATOM   8331  C  C   . MET   G  1 86  ? -42.473 -18.189  -54.980 1.00 25.72 ? 86  MET   G C   1 
ATOM   8332  O  O   . MET   G  1 86  ? -42.897 -19.015  -55.797 1.00 31.24 ? 86  MET   G O   1 
ATOM   8333  C  CB  . MET   G  1 86  ? -40.598 -16.595  -55.485 1.00 30.28 ? 86  MET   G CB  1 
ATOM   8334  C  CG  . MET   G  1 86  ? -40.205 -15.223  -55.987 1.00 30.45 ? 86  MET   G CG  1 
ATOM   8335  S  SD  . MET   G  1 86  ? -38.621 -14.577  -55.383 1.00 30.79 ? 86  MET   G SD  1 
ATOM   8336  C  CE  . MET   G  1 86  ? -37.436 -15.504  -56.386 1.00 32.25 ? 86  MET   G CE  1 
ATOM   8337  N  N   . LEU   G  1 87  ? -42.346 -18.473  -53.683 1.00 28.83 ? 87  LEU   G N   1 
ATOM   8338  C  CA  . LEU   G  1 87  ? -42.713 -19.785  -53.178 1.00 28.53 ? 87  LEU   G CA  1 
ATOM   8339  C  C   . LEU   G  1 87  ? -44.197 -20.075  -53.394 1.00 28.51 ? 87  LEU   G C   1 
ATOM   8340  O  O   . LEU   G  1 87  ? -44.578 -21.203  -53.728 1.00 30.65 ? 87  LEU   G O   1 
ATOM   8341  C  CB  . LEU   G  1 87  ? -42.354 -19.873  -51.689 1.00 33.90 ? 87  LEU   G CB  1 
ATOM   8342  C  CG  . LEU   G  1 87  ? -40.864 -19.855  -51.306 1.00 33.70 ? 87  LEU   G CG  1 
ATOM   8343  C  CD1 . LEU   G  1 87  ? -40.689 -19.459  -49.824 1.00 29.43 ? 87  LEU   G CD1 1 
ATOM   8344  C  CD2 . LEU   G  1 87  ? -40.170 -21.203  -51.612 1.00 26.88 ? 87  LEU   G CD2 1 
ATOM   8345  N  N   . GLN   G  1 88  ? -45.054 -19.078  -53.175 1.00 31.13 ? 88  GLN   G N   1 
ATOM   8346  C  CA  . GLN   G  1 88  ? -46.486 -19.286  -53.381 1.00 31.20 ? 88  GLN   G CA  1 
ATOM   8347  C  C   . GLN   G  1 88  ? -46.818 -19.506  -54.862 1.00 31.72 ? 88  GLN   G C   1 
ATOM   8348  O  O   . GLN   G  1 88  ? -47.709 -20.309  -55.198 1.00 30.62 ? 88  GLN   G O   1 
ATOM   8349  C  CB  . GLN   G  1 88  ? -47.252 -18.088  -52.807 1.00 38.64 ? 88  GLN   G CB  1 
ATOM   8350  C  CG  . GLN   G  1 88  ? -48.789 -18.246  -52.799 1.00 65.23 ? 88  GLN   G CG  1 
ATOM   8351  C  CD  . GLN   G  1 88  ? -49.294 -19.324  -51.845 1.00 71.89 ? 88  GLN   G CD  1 
ATOM   8352  O  OE1 . GLN   G  1 88  ? -49.010 -19.282  -50.645 1.00 68.60 ? 88  GLN   G OE1 1 
ATOM   8353  N  NE2 . GLN   G  1 88  ? -50.059 -20.293  -52.377 1.00 52.48 ? 88  GLN   G NE2 1 
ATOM   8354  N  N   . CYS   G  1 89  ? -46.118 -18.797  -55.759 1.00 32.60 ? 89  CYS   G N   1 
ATOM   8355  C  CA  . CYS   G  1 89  ? -46.236 -19.069  -57.192 1.00 34.14 ? 89  CYS   G CA  1 
ATOM   8356  C  C   . CYS   G  1 89  ? -45.817 -20.487  -57.530 1.00 33.08 ? 89  CYS   G C   1 
ATOM   8357  O  O   . CYS   G  1 89  ? -46.477 -21.158  -58.330 1.00 27.75 ? 89  CYS   G O   1 
ATOM   8358  C  CB  . CYS   G  1 89  ? -45.399 -18.082  -57.990 1.00 36.64 ? 89  CYS   G CB  1 
ATOM   8359  S  SG  . CYS   G  1 89  ? -46.100 -16.417  -58.044 1.00 38.29 ? 89  CYS   G SG  1 
ATOM   8360  N  N   . ASP   G  1 90  ? -44.694 -20.956  -56.966 1.00 31.20 ? 90  ASP   G N   1 
ATOM   8361  C  CA  . ASP   G  1 90  ? -44.295 -22.335  -57.205 1.00 28.41 ? 90  ASP   G CA  1 
ATOM   8362  C  C   . ASP   G  1 90  ? -45.374 -23.292  -56.721 1.00 27.16 ? 90  ASP   G C   1 
ATOM   8363  O  O   . ASP   G  1 90  ? -45.729 -24.255  -57.412 1.00 31.24 ? 90  ASP   G O   1 
ATOM   8364  C  CB  . ASP   G  1 90  ? -42.944 -22.650  -56.515 1.00 31.11 ? 90  ASP   G CB  1 
ATOM   8365  C  CG  . ASP   G  1 90  ? -41.720 -22.028  -57.221 1.00 34.60 ? 90  ASP   G CG  1 
ATOM   8366  O  OD1 . ASP   G  1 90  ? -41.830 -21.323  -58.261 1.00 30.15 ? 90  ASP   G OD1 1 
ATOM   8367  O  OD2 . ASP   G  1 90  ? -40.598 -22.249  -56.715 1.00 34.71 ? 90  ASP   G OD2 1 
ATOM   8368  N  N   . LEU   G  1 91  ? -45.887 -23.059  -55.505 1.00 31.64 ? 91  LEU   G N   1 
ATOM   8369  C  CA  . LEU   G  1 91  ? -46.926 -23.919  -54.954 1.00 31.50 ? 91  LEU   G CA  1 
ATOM   8370  C  C   . LEU   G  1 91  ? -48.166 -23.920  -55.848 1.00 29.49 ? 91  LEU   G C   1 
ATOM   8371  O  O   . LEU   G  1 91  ? -48.748 -24.975  -56.128 1.00 27.14 ? 91  LEU   G O   1 
ATOM   8372  C  CB  . LEU   G  1 91  ? -47.273 -23.461  -53.534 1.00 30.11 ? 91  LEU   G CB  1 
ATOM   8373  C  CG  . LEU   G  1 91  ? -48.313 -24.310  -52.797 1.00 32.57 ? 91  LEU   G CG  1 
ATOM   8374  C  CD1 . LEU   G  1 91  ? -47.978 -25.816  -52.838 1.00 32.95 ? 91  LEU   G CD1 1 
ATOM   8375  C  CD2 . LEU   G  1 91  ? -48.439 -23.815  -51.367 1.00 34.70 ? 91  LEU   G CD2 1 
ATOM   8376  N  N   . ASN   G  1 92  ? -48.563 -22.758  -56.339 1.00 28.89 ? 92  ASN   G N   1 
ATOM   8377  C  CA  . ASN   G  1 92  ? -49.756 -22.731  -57.183 1.00 34.88 ? 92  ASN   G CA  1 
ATOM   8378  C  C   . ASN   G  1 92  ? -49.535 -23.516  -58.465 1.00 38.42 ? 92  ASN   G C   1 
ATOM   8379  O  O   . ASN   G  1 92  ? -50.417 -24.249  -58.917 1.00 28.25 ? 92  ASN   G O   1 
ATOM   8380  C  CB  . ASN   G  1 92  ? -50.136 -21.289  -57.483 1.00 39.48 ? 92  ASN   G CB  1 
ATOM   8381  C  CG  . ASN   G  1 92  ? -50.649 -20.574  -56.253 1.00 43.60 ? 92  ASN   G CG  1 
ATOM   8382  O  OD1 . ASN   G  1 92  ? -50.948 -21.217  -55.248 1.00 45.16 ? 92  ASN   G OD1 1 
ATOM   8383  N  ND2 . ASN   G  1 92  ? -50.760 -19.247  -56.322 1.00 43.39 ? 92  ASN   G ND2 1 
ATOM   8384  N  N   . LEU   G  1 93  ? -48.351 -23.387  -59.067 1.00 31.74 ? 93  LEU   G N   1 
ATOM   8385  C  CA  . LEU   G  1 93  ? -48.068 -24.171  -60.262 1.00 28.21 ? 93  LEU   G CA  1 
ATOM   8386  C  C   . LEU   G  1 93  ? -48.080 -25.660  -59.961 1.00 29.67 ? 93  LEU   G C   1 
ATOM   8387  O  O   . LEU   G  1 93  ? -48.587 -26.458  -60.759 1.00 29.30 ? 93  LEU   G O   1 
ATOM   8388  C  CB  . LEU   G  1 93  ? -46.726 -23.735  -60.855 1.00 34.43 ? 93  LEU   G CB  1 
ATOM   8389  C  CG  . LEU   G  1 93  ? -46.278 -24.488  -62.098 1.00 36.41 ? 93  LEU   G CG  1 
ATOM   8390  C  CD1 . LEU   G  1 93  ? -47.235 -24.262  -63.258 1.00 35.43 ? 93  LEU   G CD1 1 
ATOM   8391  C  CD2 . LEU   G  1 93  ? -44.871 -24.063  -62.479 1.00 37.17 ? 93  LEU   G CD2 1 
ATOM   8392  N  N   . GLU   G  1 94  ? -47.505 -26.063  -58.824 1.00 29.35 ? 94  GLU   G N   1 
ATOM   8393  C  CA  . GLU   G  1 94  ? -47.460 -27.484  -58.485 1.00 31.09 ? 94  GLU   G CA  1 
ATOM   8394  C  C   . GLU   G  1 94  ? -48.858 -28.051  -58.275 1.00 27.93 ? 94  GLU   G C   1 
ATOM   8395  O  O   . GLU   G  1 94  ? -49.132 -29.194  -58.633 1.00 31.95 ? 94  GLU   G O   1 
ATOM   8396  C  CB  . GLU   G  1 94  ? -46.626 -27.700  -57.213 1.00 29.91 ? 94  GLU   G CB  1 
ATOM   8397  C  CG  . GLU   G  1 94  ? -45.104 -27.506  -57.414 1.00 38.25 ? 94  GLU   G CG  1 
ATOM   8398  C  CD  . GLU   G  1 94  ? -44.471 -28.700  -58.123 1.00 35.69 ? 94  GLU   G CD  1 
ATOM   8399  O  OE1 . GLU   G  1 94  ? -45.204 -29.623  -58.494 1.00 37.38 ? 94  GLU   G OE1 1 
ATOM   8400  O  OE2 . GLU   G  1 94  ? -43.239 -28.723  -58.305 1.00 43.99 ? 94  GLU   G OE2 1 
ATOM   8401  N  N   . LEU   G  1 95  ? -49.727 -27.303  -57.619 1.00 29.49 ? 95  LEU   G N   1 
ATOM   8402  C  CA  . LEU   G  1 95  ? -51.063 -27.833  -57.365 1.00 35.15 ? 95  LEU   G CA  1 
ATOM   8403  C  C   . LEU   G  1 95  ? -51.824 -27.979  -58.677 1.00 35.28 ? 95  LEU   G C   1 
ATOM   8404  O  O   . LEU   G  1 95  ? -52.490 -28.996  -58.921 1.00 28.25 ? 95  LEU   G O   1 
ATOM   8405  C  CB  . LEU   G  1 95  ? -51.796 -26.920  -56.391 1.00 36.60 ? 95  LEU   G CB  1 
ATOM   8406  C  CG  . LEU   G  1 95  ? -51.211 -26.867  -54.981 1.00 32.26 ? 95  LEU   G CG  1 
ATOM   8407  C  CD1 . LEU   G  1 95  ? -51.854 -25.735  -54.175 1.00 39.06 ? 95  LEU   G CD1 1 
ATOM   8408  C  CD2 . LEU   G  1 95  ? -51.420 -28.177  -54.259 1.00 35.13 ? 95  LEU   G CD2 1 
ATOM   8409  N  N   . LYS   G  1 96  ? -51.667 -27.007  -59.566 1.00 31.38 ? 96  LYS   G N   1 
ATOM   8410  C  CA  . LYS   G  1 96  ? -52.220 -27.173  -60.905 1.00 28.72 ? 96  LYS   G CA  1 
ATOM   8411  C  C   . LYS   G  1 96  ? -51.559 -28.349  -61.609 1.00 36.30 ? 96  LYS   G C   1 
ATOM   8412  O  O   . LYS   G  1 96  ? -52.245 -29.174  -62.222 1.00 33.66 ? 96  LYS   G O   1 
ATOM   8413  C  CB  . LYS   G  1 96  ? -52.091 -25.851  -61.651 1.00 33.04 ? 96  LYS   G CB  1 
ATOM   8414  C  CG  . LYS   G  1 96  ? -51.622 -25.899  -63.097 1.00 45.62 ? 96  LYS   G CG  1 
ATOM   8415  C  CD  . LYS   G  1 96  ? -52.634 -26.454  -64.021 1.00 51.72 ? 96  LYS   G CD  1 
ATOM   8416  C  CE  . LYS   G  1 96  ? -52.388 -25.899  -65.442 1.00 57.74 ? 96  LYS   G CE  1 
ATOM   8417  N  NZ  . LYS   G  1 96  ? -53.002 -26.748  -66.486 1.00 52.84 ? 96  LYS   G NZ  1 
ATOM   8418  N  N   . ALA   G  1 97  ? -50.238 -28.522  -61.439 1.00 33.21 ? 97  ALA   G N   1 
ATOM   8419  C  CA  . ALA   G  1 97  ? -49.568 -29.627  -62.120 1.00 27.90 ? 97  ALA   G CA  1 
ATOM   8420  C  C   . ALA   G  1 97  ? -50.033 -30.983  -61.605 1.00 27.51 ? 97  ALA   G C   1 
ATOM   8421  O  O   . ALA   G  1 97  ? -50.174 -31.934  -62.388 1.00 29.69 ? 97  ALA   G O   1 
ATOM   8422  C  CB  . ALA   G  1 97  ? -48.037 -29.500  -61.981 1.00 36.83 ? 97  ALA   G CB  1 
ATOM   8423  N  N   . THR   G  1 98  ? -50.222 -31.119  -60.289 1.00 26.22 ? 98  THR   G N   1 
ATOM   8424  C  CA  . THR   G  1 98  ? -50.612 -32.423  -59.752 1.00 25.14 ? 98  THR   G CA  1 
ATOM   8425  C  C   . THR   G  1 98  ? -52.077 -32.759  -60.079 1.00 30.46 ? 98  THR   G C   1 
ATOM   8426  O  O   . THR   G  1 98  ? -52.421 -33.931  -60.252 1.00 28.11 ? 98  THR   G O   1 
ATOM   8427  C  CB  . THR   G  1 98  ? -50.392 -32.468  -58.243 1.00 28.78 ? 98  THR   G CB  1 
ATOM   8428  O  OG1 . THR   G  1 98  ? -51.131 -31.408  -57.610 1.00 31.28 ? 98  THR   G OG1 1 
ATOM   8429  C  CG2 . THR   G  1 98  ? -48.848 -32.353  -57.914 1.00 33.32 ? 98  THR   G CG2 1 
ATOM   8430  N  N   . LYS   G  1 99  ? -52.956 -31.759  -60.103 1.00 30.15 ? 99  LYS   G N   1 
ATOM   8431  C  CA  . LYS   G  1 99  ? -54.301 -31.975  -60.660 1.00 38.69 ? 99  LYS   G CA  1 
ATOM   8432  C  C   . LYS   G  1 99  ? -54.235 -32.617  -62.052 1.00 33.63 ? 99  LYS   G C   1 
ATOM   8433  O  O   . LYS   G  1 99  ? -54.924 -33.610  -62.337 1.00 30.17 ? 99  LYS   G O   1 
ATOM   8434  C  CB  . LYS   G  1 99  ? -55.047 -30.631  -60.699 1.00 37.20 ? 99  LYS   G CB  1 
ATOM   8435  C  CG  . LYS   G  1 99  ? -56.370 -30.611  -61.475 1.00 48.95 ? 99  LYS   G CG  1 
ATOM   8436  C  CD  . LYS   G  1 99  ? -56.792 -29.172  -61.788 1.00 49.54 ? 99  LYS   G CD  1 
ATOM   8437  N  N   . ASP   G  1 100 ? -53.405 -32.064  -62.944 1.00 34.18 ? 100 ASP   G N   1 
ATOM   8438  C  CA  . ASP   G  1 100 ? -53.342 -32.598  -64.303 1.00 32.96 ? 100 ASP   G CA  1 
ATOM   8439  C  C   . ASP   G  1 100 ? -52.761 -34.003  -64.331 1.00 34.91 ? 100 ASP   G C   1 
ATOM   8440  O  O   . ASP   G  1 100 ? -53.160 -34.828  -65.166 1.00 30.50 ? 100 ASP   G O   1 
ATOM   8441  C  CB  . ASP   G  1 100 ? -52.529 -31.675  -65.212 1.00 32.91 ? 100 ASP   G CB  1 
ATOM   8442  C  CG  . ASP   G  1 100 ? -53.180 -30.317  -65.398 1.00 43.11 ? 100 ASP   G CG  1 
ATOM   8443  O  OD1 . ASP   G  1 100 ? -54.378 -30.198  -65.086 1.00 41.29 ? 100 ASP   G OD1 1 
ATOM   8444  O  OD2 . ASP   G  1 100 ? -52.500 -29.365  -65.845 1.00 38.04 ? 100 ASP   G OD2 1 
ATOM   8445  N  N   . LEU   G  1 101 ? -51.774 -34.281  -63.476 1.00 34.79 ? 101 LEU   G N   1 
ATOM   8446  C  CA  . LEU   G  1 101 ? -51.206 -35.626  -63.430 1.00 28.97 ? 101 LEU   G CA  1 
ATOM   8447  C  C   . LEU   G  1 101 ? -52.254 -36.640  -63.008 1.00 27.18 ? 101 LEU   G C   1 
ATOM   8448  O  O   . LEU   G  1 101 ? -52.308 -37.754  -63.540 1.00 27.20 ? 101 LEU   G O   1 
ATOM   8449  C  CB  . LEU   G  1 101 ? -50.011 -35.656  -62.457 1.00 33.97 ? 101 LEU   G CB  1 
ATOM   8450  C  CG  . LEU   G  1 101 ? -48.693 -35.062  -62.983 1.00 31.60 ? 101 LEU   G CG  1 
ATOM   8451  C  CD1 . LEU   G  1 101 ? -47.759 -34.636  -61.840 1.00 34.33 ? 101 LEU   G CD1 1 
ATOM   8452  C  CD2 . LEU   G  1 101 ? -48.006 -36.061  -63.906 1.00 28.47 ? 101 LEU   G CD2 1 
ATOM   8453  N  N   . ARG   G  1 102 ? -53.087 -36.276  -62.030 1.00 25.64 ? 102 ARG   G N   1 
ATOM   8454  C  CA  . ARG   G  1 102 ? -54.139 -37.186  -61.574 1.00 34.18 ? 102 ARG   G CA  1 
ATOM   8455  C  C   . ARG   G  1 102 ? -55.134 -37.490  -62.695 1.00 27.82 ? 102 ARG   G C   1 
ATOM   8456  O  O   . ARG   G  1 102 ? -55.494 -38.653  -62.928 1.00 27.94 ? 102 ARG   G O   1 
ATOM   8457  C  CB  . ARG   G  1 102 ? -54.860 -36.584  -60.359 1.00 37.72 ? 102 ARG   G CB  1 
ATOM   8458  C  CG  . ARG   G  1 102 ? -54.027 -36.591  -59.066 1.00 31.79 ? 102 ARG   G CG  1 
ATOM   8459  C  CD  . ARG   G  1 102 ? -54.776 -35.975  -57.877 1.00 32.16 ? 102 ARG   G CD  1 
ATOM   8460  N  NE  . ARG   G  1 102 ? -53.817 -35.294  -57.013 1.00 34.94 ? 102 ARG   G NE  1 
ATOM   8461  C  CZ  . ARG   G  1 102 ? -52.925 -35.926  -56.262 1.00 37.09 ? 102 ARG   G CZ  1 
ATOM   8462  N  NH1 . ARG   G  1 102 ? -52.887 -37.243  -56.197 1.00 32.36 ? 102 ARG   G NH1 1 
ATOM   8463  N  NH2 . ARG   G  1 102 ? -52.065 -35.220  -55.543 1.00 30.27 ? 102 ARG   G NH2 1 
ATOM   8464  N  N   . GLU   G  1 103 ? -55.562 -36.463  -63.427 1.00 31.63 ? 103 GLU   G N   1 
ATOM   8465  C  CA  . GLU   G  1 103 ? -56.491 -36.721  -64.533 1.00 31.68 ? 103 GLU   G CA  1 
ATOM   8466  C  C   . GLU   G  1 103 ? -55.826 -37.560  -65.617 1.00 36.04 ? 103 GLU   G C   1 
ATOM   8467  O  O   . GLU   G  1 103 ? -56.457 -38.454  -66.195 1.00 33.24 ? 103 GLU   G O   1 
ATOM   8468  C  CB  . GLU   G  1 103 ? -57.010 -35.405  -65.120 1.00 35.76 ? 103 GLU   G CB  1 
ATOM   8469  C  CG  . GLU   G  1 103 ? -57.914 -34.582  -64.177 1.00 46.40 ? 103 GLU   G CG  1 
ATOM   8470  C  CD  . GLU   G  1 103 ? -58.071 -33.114  -64.609 1.00 68.41 ? 103 GLU   G CD  1 
ATOM   8471  O  OE1 . GLU   G  1 103 ? -57.420 -32.697  -65.594 1.00 70.50 ? 103 GLU   G OE1 1 
ATOM   8472  O  OE2 . GLU   G  1 103 ? -58.847 -32.374  -63.955 1.00 65.93 ? 103 GLU   G OE2 1 
ATOM   8473  N  N   . ALA   G  1 104 ? -54.534 -37.313  -65.888 1.00 31.37 ? 104 ALA   G N   1 
ATOM   8474  C  CA  . ALA   G  1 104 ? -53.832 -38.102  -66.898 1.00 25.02 ? 104 ALA   G CA  1 
ATOM   8475  C  C   . ALA   G  1 104 ? -53.741 -39.562  -66.488 1.00 27.61 ? 104 ALA   G C   1 
ATOM   8476  O  O   . ALA   G  1 104 ? -53.942 -40.458  -67.308 1.00 30.81 ? 104 ALA   G O   1 
ATOM   8477  C  CB  . ALA   G  1 104 ? -52.442 -37.518  -67.125 1.00 27.65 ? 104 ALA   G CB  1 
ATOM   8478  N  N   . ILE   G  1 105 ? -53.443 -39.822  -65.209 1.00 28.05 ? 105 ILE   G N   1 
ATOM   8479  C  CA  . ILE   G  1 105 ? -53.360 -41.196  -64.731 1.00 25.49 ? 105 ILE   G CA  1 
ATOM   8480  C  C   . ILE   G  1 105 ? -54.707 -41.897  -64.867 1.00 30.97 ? 105 ILE   G C   1 
ATOM   8481  O  O   . ILE   G  1 105 ? -54.783 -43.068  -65.275 1.00 31.51 ? 105 ILE   G O   1 
ATOM   8482  C  CB  . ILE   G  1 105 ? -52.848 -41.209  -63.280 1.00 30.34 ? 105 ILE   G CB  1 
ATOM   8483  C  CG1 . ILE   G  1 105 ? -51.328 -40.913  -63.282 1.00 29.33 ? 105 ILE   G CG1 1 
ATOM   8484  C  CG2 . ILE   G  1 105 ? -53.139 -42.546  -62.633 1.00 27.11 ? 105 ILE   G CG2 1 
ATOM   8485  C  CD1 . ILE   G  1 105 ? -50.761 -40.567  -61.873 1.00 34.30 ? 105 ILE   G CD1 1 
ATOM   8486  N  N   . VAL   G  1 106 ? -55.786 -41.218  -64.472 1.00 30.89 ? 106 VAL   G N   1 
ATOM   8487  C  CA  . VAL   G  1 106 ? -57.115 -41.802  -64.661 1.00 34.01 ? 106 VAL   G CA  1 
ATOM   8488  C  C   . VAL   G  1 106 ? -57.262 -42.309  -66.088 1.00 34.35 ? 106 VAL   G C   1 
ATOM   8489  O  O   . VAL   G  1 106 ? -57.651 -43.461  -66.322 1.00 32.26 ? 106 VAL   G O   1 
ATOM   8490  C  CB  . VAL   G  1 106 ? -58.221 -40.790  -64.310 1.00 31.21 ? 106 VAL   G CB  1 
ATOM   8491  C  CG1 . VAL   G  1 106 ? -59.585 -41.332  -64.777 1.00 38.21 ? 106 VAL   G CG1 1 
ATOM   8492  C  CG2 . VAL   G  1 106 ? -58.264 -40.560  -62.812 1.00 31.36 ? 106 VAL   G CG2 1 
ATOM   8493  N  N   . HIS   G  1 107 ? -56.913 -41.473  -67.067 1.00 34.62 ? 107 HIS   G N   1 
ATOM   8494  C  CA  . HIS   G  1 107 ? -57.122 -41.901  -68.447 1.00 35.45 ? 107 HIS   G CA  1 
ATOM   8495  C  C   . HIS   G  1 107 ? -56.204 -43.049  -68.851 1.00 38.37 ? 107 HIS   G C   1 
ATOM   8496  O  O   . HIS   G  1 107 ? -56.649 -43.981  -69.542 1.00 28.29 ? 107 HIS   G O   1 
ATOM   8497  C  CB  . HIS   G  1 107 ? -56.970 -40.757  -69.430 1.00 39.39 ? 107 HIS   G CB  1 
ATOM   8498  C  CG  . HIS   G  1 107 ? -57.277 -41.190  -70.827 1.00 44.75 ? 107 HIS   G CG  1 
ATOM   8499  N  ND1 . HIS   G  1 107 ? -58.534 -41.617  -71.203 1.00 41.59 ? 107 HIS   G ND1 1 
ATOM   8500  C  CD2 . HIS   G  1 107 ? -56.476 -41.377  -71.901 1.00 40.69 ? 107 HIS   G CD2 1 
ATOM   8501  C  CE1 . HIS   G  1 107 ? -58.504 -41.996  -72.469 1.00 45.85 ? 107 HIS   G CE1 1 
ATOM   8502  N  NE2 . HIS   G  1 107 ? -57.266 -41.861  -72.916 1.00 43.89 ? 107 HIS   G NE2 1 
ATOM   8503  N  N   . CYS   G  1 108 ? -54.919 -43.016  -68.444 1.00 31.58 ? 108 CYS   G N   1 
ATOM   8504  C  CA  . CYS   G  1 108 ? -54.041 -44.145  -68.750 1.00 26.67 ? 108 CYS   G CA  1 
ATOM   8505  C  C   . CYS   G  1 108 ? -54.599 -45.445  -68.186 1.00 27.85 ? 108 CYS   G C   1 
ATOM   8506  O  O   . CYS   G  1 108 ? -54.539 -46.498  -68.836 1.00 32.88 ? 108 CYS   G O   1 
ATOM   8507  C  CB  . CYS   G  1 108 ? -52.618 -43.898  -68.184 1.00 31.07 ? 108 CYS   G CB  1 
ATOM   8508  S  SG  . CYS   G  1 108 ? -51.751 -42.488  -68.910 1.00 31.09 ? 108 CYS   G SG  1 
ATOM   8509  N  N   . GLU   G  1 109 ? -55.108 -45.406  -66.950 1.00 27.85 ? 109 GLU   G N   1 
ATOM   8510  C  CA  . GLU   G  1 109 ? -55.701 -46.604  -66.379 1.00 29.47 ? 109 GLU   G CA  1 
ATOM   8511  C  C   . GLU   G  1 109 ? -56.860 -47.085  -67.249 1.00 32.26 ? 109 GLU   G C   1 
ATOM   8512  O  O   . GLU   G  1 109 ? -56.958 -48.270  -67.585 1.00 32.47 ? 109 GLU   G O   1 
ATOM   8513  C  CB  . GLU   G  1 109 ? -56.179 -46.316  -64.959 1.00 29.69 ? 109 GLU   G CB  1 
ATOM   8514  C  CG  . GLU   G  1 109 ? -56.704 -47.521  -64.255 1.00 28.45 ? 109 GLU   G CG  1 
ATOM   8515  C  CD  . GLU   G  1 109 ? -55.645 -48.527  -63.873 1.00 40.12 ? 109 GLU   G CD  1 
ATOM   8516  O  OE1 . GLU   G  1 109 ? -54.442 -48.170  -63.906 1.00 31.19 ? 109 GLU   G OE1 1 
ATOM   8517  O  OE2 . GLU   G  1 109 ? -56.020 -49.680  -63.534 1.00 31.99 ? 109 GLU   G OE2 1 
ATOM   8518  N  N   . GLN   G  1 110 ? -57.732 -46.164  -67.638 1.00 32.72 ? 110 GLN   G N   1 
ATOM   8519  C  CA  . GLN   G  1 110 ? -58.920 -46.551  -68.401 1.00 36.25 ? 110 GLN   G CA  1 
ATOM   8520  C  C   . GLN   G  1 110 ? -58.531 -47.279  -69.683 1.00 42.46 ? 110 GLN   G C   1 
ATOM   8521  O  O   . GLN   G  1 110 ? -59.094 -48.328  -69.999 1.00 36.95 ? 110 GLN   G O   1 
ATOM   8522  C  CB  . GLN   G  1 110 ? -59.772 -45.318  -68.705 1.00 40.17 ? 110 GLN   G CB  1 
ATOM   8523  C  CG  . GLN   G  1 110 ? -60.445 -44.702  -67.480 1.00 44.93 ? 110 GLN   G CG  1 
ATOM   8524  N  N   . VAL   G  1 111 ? -57.522 -46.776  -70.404 1.00 36.87 ? 111 VAL   G N   1 
ATOM   8525  C  CA  . VAL   G  1 111 ? -57.136 -47.375  -71.683 1.00 35.62 ? 111 VAL   G CA  1 
ATOM   8526  C  C   . VAL   G  1 111 ? -55.991 -48.373  -71.515 1.00 39.20 ? 111 VAL   G C   1 
ATOM   8527  O  O   . VAL   G  1 111 ? -55.437 -48.868  -72.502 1.00 30.95 ? 111 VAL   G O   1 
ATOM   8528  C  CB  . VAL   G  1 111 ? -56.769 -46.292  -72.715 1.00 37.41 ? 111 VAL   G CB  1 
ATOM   8529  C  CG1 . VAL   G  1 111 ? -57.900 -45.285  -72.869 1.00 37.02 ? 111 VAL   G CG1 1 
ATOM   8530  C  CG2 . VAL   G  1 111 ? -55.486 -45.580  -72.312 1.00 32.96 ? 111 VAL   G CG2 1 
ATOM   8531  N  N   . HIS   G  1 112 ? -55.635 -48.698  -70.278 1.00 32.14 ? 112 HIS   G N   1 
ATOM   8532  C  CA  . HIS   G  1 112 ? -54.695 -49.774  -69.987 1.00 32.31 ? 112 HIS   G CA  1 
ATOM   8533  C  C   . HIS   G  1 112 ? -53.248 -49.403  -70.333 1.00 27.00 ? 112 HIS   G C   1 
ATOM   8534  O  O   . HIS   G  1 112 ? -52.433 -50.280  -70.598 1.00 24.69 ? 112 HIS   G O   1 
ATOM   8535  C  CB  . HIS   G  1 112 ? -55.063 -51.069  -70.714 1.00 39.17 ? 112 HIS   G CB  1 
ATOM   8536  C  CG  . HIS   G  1 112 ? -56.451 -51.555  -70.433 1.00 37.70 ? 112 HIS   G CG  1 
ATOM   8537  N  ND1 . HIS   G  1 112 ? -57.179 -51.142  -69.338 1.00 48.74 ? 112 HIS   G ND1 1 
ATOM   8538  C  CD2 . HIS   G  1 112 ? -57.242 -52.422  -71.106 1.00 42.16 ? 112 HIS   G CD2 1 
ATOM   8539  C  CE1 . HIS   G  1 112 ? -58.367 -51.722  -69.357 1.00 41.61 ? 112 HIS   G CE1 1 
ATOM   8540  N  NE2 . HIS   G  1 112 ? -58.429 -52.509  -70.416 1.00 42.98 ? 112 HIS   G NE2 1 
ATOM   8541  N  N   . ASP   G  1 113 ? -52.910 -48.123  -70.364 1.00 28.56 ? 113 ASP   G N   1 
ATOM   8542  C  CA  . ASP   G  1 113 ? -51.521 -47.733  -70.633 1.00 26.44 ? 113 ASP   G CA  1 
ATOM   8543  C  C   . ASP   G  1 113 ? -50.800 -47.656  -69.289 1.00 26.29 ? 113 ASP   G C   1 
ATOM   8544  O  O   . ASP   G  1 113 ? -50.566 -46.584  -68.728 1.00 25.12 ? 113 ASP   G O   1 
ATOM   8545  C  CB  . ASP   G  1 113 ? -51.445 -46.417  -71.387 1.00 28.60 ? 113 ASP   G CB  1 
ATOM   8546  C  CG  . ASP   G  1 113 ? -50.009 -46.080  -71.794 1.00 31.92 ? 113 ASP   G CG  1 
ATOM   8547  O  OD1 . ASP   G  1 113 ? -49.084 -46.854  -71.406 1.00 29.26 ? 113 ASP   G OD1 1 
ATOM   8548  O  OD2 . ASP   G  1 113 ? -49.816 -45.050  -72.473 1.00 30.97 ? 113 ASP   G OD2 1 
ATOM   8549  N  N   . TYR   G  1 114 ? -50.449 -48.830  -68.781 1.00 24.49 ? 114 TYR   G N   1 
ATOM   8550  C  CA  . TYR   G  1 114 ? -49.980 -48.945  -67.404 1.00 24.77 ? 114 TYR   G CA  1 
ATOM   8551  C  C   . TYR   G  1 114 ? -48.532 -48.472  -67.245 1.00 28.66 ? 114 TYR   G C   1 
ATOM   8552  O  O   . TYR   G  1 114 ? -48.140 -48.023  -66.165 1.00 28.53 ? 114 TYR   G O   1 
ATOM   8553  C  CB  . TYR   G  1 114 ? -50.099 -50.386  -66.935 1.00 27.16 ? 114 TYR   G CB  1 
ATOM   8554  C  CG  . TYR   G  1 114 ? -51.517 -50.925  -66.925 1.00 31.17 ? 114 TYR   G CG  1 
ATOM   8555  C  CD1 . TYR   G  1 114 ? -52.500 -50.351  -66.131 1.00 35.05 ? 114 TYR   G CD1 1 
ATOM   8556  C  CD2 . TYR   G  1 114 ? -51.865 -52.026  -67.710 1.00 30.18 ? 114 TYR   G CD2 1 
ATOM   8557  C  CE1 . TYR   G  1 114 ? -53.825 -50.866  -66.119 1.00 34.29 ? 114 TYR   G CE1 1 
ATOM   8558  C  CE2 . TYR   G  1 114 ? -53.167 -52.535  -67.703 1.00 34.54 ? 114 TYR   G CE2 1 
ATOM   8559  C  CZ  . TYR   G  1 114 ? -54.137 -51.952  -66.912 1.00 36.57 ? 114 TYR   G CZ  1 
ATOM   8560  O  OH  . TYR   G  1 114 ? -55.422 -52.483  -66.940 1.00 33.78 ? 114 TYR   G OH  1 
ATOM   8561  N  N   . VAL   G  1 115 ? -47.738 -48.540  -68.304 1.00 25.51 ? 115 VAL   G N   1 
ATOM   8562  C  CA  . VAL   G  1 115 ? -46.386 -47.968  -68.241 1.00 24.56 ? 115 VAL   G CA  1 
ATOM   8563  C  C   . VAL   G  1 115 ? -46.439 -46.447  -68.196 1.00 25.51 ? 115 VAL   G C   1 
ATOM   8564  O  O   . VAL   G  1 115 ? -45.764 -45.807  -67.375 1.00 28.15 ? 115 VAL   G O   1 
ATOM   8565  C  CB  . VAL   G  1 115 ? -45.541 -48.473  -69.411 1.00 25.79 ? 115 VAL   G CB  1 
ATOM   8566  C  CG1 . VAL   G  1 115 ? -44.118 -47.853  -69.350 1.00 29.17 ? 115 VAL   G CG1 1 
ATOM   8567  C  CG2 . VAL   G  1 115 ? -45.481 -49.979  -69.357 1.00 26.97 ? 115 VAL   G CG2 1 
ATOM   8568  N  N   . SER   G  1 116 ? -47.246 -45.829  -69.057 1.00 26.64 ? 116 SER   G N   1 
ATOM   8569  C  CA  . SER   G  1 116 ? -47.430 -44.382  -68.940 1.00 24.14 ? 116 SER   G CA  1 
ATOM   8570  C  C   . SER   G  1 116 ? -47.927 -43.980  -67.558 1.00 29.98 ? 116 SER   G C   1 
ATOM   8571  O  O   . SER   G  1 116 ? -47.492 -42.954  -67.005 1.00 28.14 ? 116 SER   G O   1 
ATOM   8572  C  CB  . SER   G  1 116 ? -48.386 -43.867  -69.997 1.00 29.63 ? 116 SER   G CB  1 
ATOM   8573  O  OG  . SER   G  1 116 ? -47.790 -43.959  -71.266 1.00 27.82 ? 116 SER   G OG  1 
ATOM   8574  N  N   . ARG   G  1 117 ? -48.847 -44.759  -66.981 1.00 25.46 ? 117 ARG   G N   1 
ATOM   8575  C  CA  . ARG   G  1 117 ? -49.325 -44.423  -65.646 1.00 27.60 ? 117 ARG   G CA  1 
ATOM   8576  C  C   . ARG   G  1 117 ? -48.171 -44.449  -64.652 1.00 26.74 ? 117 ARG   G C   1 
ATOM   8577  O  O   . ARG   G  1 117 ? -48.072 -43.588  -63.781 1.00 27.09 ? 117 ARG   G O   1 
ATOM   8578  C  CB  . ARG   G  1 117 ? -50.402 -45.407  -65.195 1.00 29.83 ? 117 ARG   G CB  1 
ATOM   8579  C  CG  . ARG   G  1 117 ? -50.667 -45.363  -63.663 1.00 29.53 ? 117 ARG   G CG  1 
ATOM   8580  C  CD  . ARG   G  1 117 ? -51.897 -46.199  -63.247 1.00 31.44 ? 117 ARG   G CD  1 
ATOM   8581  N  NE  . ARG   G  1 117 ? -51.974 -46.272  -61.786 1.00 35.22 ? 117 ARG   G NE  1 
ATOM   8582  C  CZ  . ARG   G  1 117 ? -53.098 -46.296  -61.082 1.00 35.20 ? 117 ARG   G CZ  1 
ATOM   8583  N  NH1 . ARG   G  1 117 ? -54.286 -46.378  -61.663 1.00 32.00 ? 117 ARG   G NH1 1 
ATOM   8584  N  NH2 . ARG   G  1 117 ? -53.030 -46.231  -59.758 1.00 33.86 ? 117 ARG   G NH2 1 
ATOM   8585  N  N   . ASP   G  1 118 ? -47.318 -45.466  -64.751 1.00 26.79 ? 118 ASP   G N   1 
ATOM   8586  C  CA  . ASP   G  1 118 ? -46.220 -45.609  -63.802 1.00 28.67 ? 118 ASP   G CA  1 
ATOM   8587  C  C   . ASP   G  1 118 ? -45.263 -44.431  -63.915 1.00 25.71 ? 118 ASP   G C   1 
ATOM   8588  O  O   . ASP   G  1 118 ? -44.853 -43.854  -62.901 1.00 32.77 ? 118 ASP   G O   1 
ATOM   8589  C  CB  . ASP   G  1 118 ? -45.520 -46.939  -64.048 1.00 30.00 ? 118 ASP   G CB  1 
ATOM   8590  C  CG  . ASP   G  1 118 ? -44.665 -47.389  -62.866 1.00 36.32 ? 118 ASP   G CG  1 
ATOM   8591  O  OD1 . ASP   G  1 118 ? -45.162 -47.284  -61.727 1.00 28.35 ? 118 ASP   G OD1 1 
ATOM   8592  O  OD2 . ASP   G  1 118 ? -43.531 -47.895  -63.093 1.00 32.20 ? 118 ASP   G OD2 1 
ATOM   8593  N  N   . LEU   G  1 119 ? -44.923 -44.025  -65.147 1.00 27.69 ? 119 LEU   G N   1 
ATOM   8594  C  CA  . LEU   G  1 119 ? -44.137 -42.805  -65.320 1.00 25.61 ? 119 LEU   G CA  1 
ATOM   8595  C  C   . LEU   G  1 119 ? -44.796 -41.620  -64.633 1.00 30.47 ? 119 LEU   G C   1 
ATOM   8596  O  O   . LEU   G  1 119 ? -44.143 -40.876  -63.892 1.00 28.02 ? 119 LEU   G O   1 
ATOM   8597  C  CB  . LEU   G  1 119 ? -43.926 -42.510  -66.798 1.00 25.55 ? 119 LEU   G CB  1 
ATOM   8598  C  CG  . LEU   G  1 119 ? -43.260 -41.167  -67.126 1.00 30.02 ? 119 LEU   G CG  1 
ATOM   8599  C  CD1 . LEU   G  1 119 ? -41.862 -41.135  -66.555 1.00 32.53 ? 119 LEU   G CD1 1 
ATOM   8600  C  CD2 . LEU   G  1 119 ? -43.195 -40.938  -68.616 1.00 32.30 ? 119 LEU   G CD2 1 
ATOM   8601  N  N   . LEU   G  1 120 ? -46.105 -41.433  -64.852 1.00 22.55 ? 120 LEU   G N   1 
ATOM   8602  C  CA  . LEU   G  1 120 ? -46.766 -40.269  -64.276 1.00 21.69 ? 120 LEU   G CA  1 
ATOM   8603  C  C   . LEU   G  1 120 ? -46.813 -40.358  -62.759 1.00 20.46 ? 120 LEU   G C   1 
ATOM   8604  O  O   . LEU   G  1 120 ? -46.703 -39.343  -62.077 1.00 24.37 ? 120 LEU   G O   1 
ATOM   8605  C  CB  . LEU   G  1 120 ? -48.184 -40.124  -64.839 1.00 30.36 ? 120 LEU   G CB  1 
ATOM   8606  C  CG  . LEU   G  1 120 ? -48.200 -39.860  -66.359 1.00 39.81 ? 120 LEU   G CG  1 
ATOM   8607  C  CD1 . LEU   G  1 120 ? -49.651 -39.836  -66.952 1.00 31.85 ? 120 LEU   G CD1 1 
ATOM   8608  C  CD2 . LEU   G  1 120 ? -47.432 -38.565  -66.679 1.00 27.82 ? 120 LEU   G CD2 1 
ATOM   8609  N  N   . LYS   G  1 121 ? -47.012 -41.560  -62.222 1.00 23.56 ? 121 LYS   G N   1 
ATOM   8610  C  CA  . LYS   G  1 121 ? -47.011 -41.738  -60.780 1.00 29.13 ? 121 LYS   G CA  1 
ATOM   8611  C  C   . LYS   G  1 121 ? -45.656 -41.329  -60.201 1.00 30.71 ? 121 LYS   G C   1 
ATOM   8612  O  O   . LYS   G  1 121 ? -45.591 -40.645  -59.168 1.00 27.71 ? 121 LYS   G O   1 
ATOM   8613  C  CB  . LYS   G  1 121 ? -47.347 -43.196  -60.448 1.00 28.08 ? 121 LYS   G CB  1 
ATOM   8614  C  CG  . LYS   G  1 121 ? -47.396 -43.549  -58.980 1.00 37.96 ? 121 LYS   G CG  1 
ATOM   8615  C  CD  . LYS   G  1 121 ? -46.047 -43.954  -58.388 1.00 29.13 ? 121 LYS   G CD  1 
ATOM   8616  C  CE  . LYS   G  1 121 ? -45.558 -45.286  -58.892 1.00 39.78 ? 121 LYS   G CE  1 
ATOM   8617  N  NZ  . LYS   G  1 121 ? -44.250 -45.587  -58.223 1.00 35.33 ? 121 LYS   G NZ  1 
ATOM   8618  N  N   . ASP   G  1 122 ? -44.559 -41.719  -60.869 1.00 29.42 ? 122 ASP   G N   1 
ATOM   8619  C  CA  . ASP   G  1 122 ? -43.232 -41.316  -60.381 1.00 29.20 ? 122 ASP   G CA  1 
ATOM   8620  C  C   . ASP   G  1 122 ? -43.094 -39.803  -60.403 1.00 26.88 ? 122 ASP   G C   1 
ATOM   8621  O  O   . ASP   G  1 122 ? -42.611 -39.200  -59.438 1.00 27.68 ? 122 ASP   G O   1 
ATOM   8622  C  CB  . ASP   G  1 122 ? -42.119 -41.959  -61.213 1.00 26.87 ? 122 ASP   G CB  1 
ATOM   8623  C  CG  . ASP   G  1 122 ? -42.061 -43.462  -61.046 1.00 32.26 ? 122 ASP   G CG  1 
ATOM   8624  O  OD1 . ASP   G  1 122 ? -42.591 -43.971  -60.058 1.00 32.26 ? 122 ASP   G OD1 1 
ATOM   8625  O  OD2 . ASP   G  1 122 ? -41.466 -44.147  -61.896 1.00 35.64 ? 122 ASP   G OD2 1 
ATOM   8626  N  N   . ILE   G  1 123 ? -43.547 -39.166  -61.480 1.00 24.59 ? 123 ILE   G N   1 
ATOM   8627  C  CA  . ILE   G  1 123 ? -43.508 -37.712  -61.543 1.00 30.47 ? 123 ILE   G CA  1 
ATOM   8628  C  C   . ILE   G  1 123 ? -44.348 -37.115  -60.418 1.00 27.17 ? 123 ILE   G C   1 
ATOM   8629  O  O   . ILE   G  1 123 ? -43.938 -36.143  -59.762 1.00 25.50 ? 123 ILE   G O   1 
ATOM   8630  C  CB  . ILE   G  1 123 ? -43.968 -37.236  -62.934 1.00 26.62 ? 123 ILE   G CB  1 
ATOM   8631  C  CG1 . ILE   G  1 123 ? -42.956 -37.703  -63.993 1.00 30.75 ? 123 ILE   G CG1 1 
ATOM   8632  C  CG2 . ILE   G  1 123 ? -44.151 -35.697  -62.974 1.00 26.02 ? 123 ILE   G CG2 1 
ATOM   8633  C  CD1 . ILE   G  1 123 ? -43.308 -37.292  -65.411 1.00 28.91 ? 123 ILE   G CD1 1 
ATOM   8634  N  N   . LEU   G  1 124 ? -45.522 -37.699  -60.165 1.00 27.11 ? 124 LEU   G N   1 
ATOM   8635  C  CA  . LEU   G  1 124 ? -46.421 -37.176  -59.123 1.00 23.05 ? 124 LEU   G CA  1 
ATOM   8636  C  C   . LEU   G  1 124 ? -45.779 -37.282  -57.737 1.00 24.44 ? 124 LEU   G C   1 
ATOM   8637  O  O   . LEU   G  1 124 ? -45.964 -36.405  -56.895 1.00 28.41 ? 124 LEU   G O   1 
ATOM   8638  C  CB  . LEU   G  1 124 ? -47.735 -37.944  -59.160 1.00 28.26 ? 124 LEU   G CB  1 
ATOM   8639  C  CG  . LEU   G  1 124 ? -48.794 -37.648  -58.088 1.00 33.23 ? 124 LEU   G CG  1 
ATOM   8640  C  CD1 . LEU   G  1 124 ? -49.211 -36.169  -58.139 1.00 29.99 ? 124 LEU   G CD1 1 
ATOM   8641  C  CD2 . LEU   G  1 124 ? -50.008 -38.592  -58.269 1.00 31.33 ? 124 LEU   G CD2 1 
ATOM   8642  N  N   . GLU   G  1 125 ? -45.028 -38.351  -57.486 1.00 26.77 ? 125 GLU   G N   1 
ATOM   8643  C  CA  . GLU   G  1 125 ? -44.301 -38.472  -56.217 1.00 28.52 ? 125 GLU   G CA  1 
ATOM   8644  C  C   . GLU   G  1 125 ? -43.285 -37.347  -56.048 1.00 25.49 ? 125 GLU   G C   1 
ATOM   8645  O  O   . GLU   G  1 125 ? -43.170 -36.757  -54.964 1.00 27.79 ? 125 GLU   G O   1 
ATOM   8646  C  CB  . GLU   G  1 125 ? -43.625 -39.839  -56.139 1.00 32.61 ? 125 GLU   G CB  1 
ATOM   8647  C  CG  . GLU   G  1 125 ? -44.597 -40.946  -55.880 1.00 36.76 ? 125 GLU   G CG  1 
ATOM   8648  C  CD  . GLU   G  1 125 ? -44.002 -42.344  -55.831 1.00 46.43 ? 125 GLU   G CD  1 
ATOM   8649  O  OE1 . GLU   G  1 125 ? -43.012 -42.637  -56.554 1.00 38.27 ? 125 GLU   G OE1 1 
ATOM   8650  O  OE2 . GLU   G  1 125 ? -44.582 -43.169  -55.082 1.00 36.62 ? 125 GLU   G OE2 1 
ATOM   8651  N  N   . SER   G  1 126 ? -42.549 -37.010  -57.118 1.00 26.59 ? 126 SER   G N   1 
ATOM   8652  C  CA  A SER   G  1 126 ? -41.607 -35.899  -57.048 0.50 27.82 ? 126 SER   G CA  1 
ATOM   8653  C  CA  B SER   G  1 126 ? -41.610 -35.894  -57.049 0.50 27.82 ? 126 SER   G CA  1 
ATOM   8654  C  C   . SER   G  1 126 ? -42.328 -34.574  -56.820 1.00 29.80 ? 126 SER   G C   1 
ATOM   8655  O  O   . SER   G  1 126 ? -41.863 -33.738  -56.042 1.00 26.89 ? 126 SER   G O   1 
ATOM   8656  C  CB  A SER   G  1 126 ? -40.763 -35.845  -58.329 0.50 26.37 ? 126 SER   G CB  1 
ATOM   8657  C  CB  B SER   G  1 126 ? -40.783 -35.801  -58.332 0.50 26.37 ? 126 SER   G CB  1 
ATOM   8658  O  OG  A SER   G  1 126 ? -40.078 -34.614  -58.457 0.50 21.86 ? 126 SER   G OG  1 
ATOM   8659  O  OG  B SER   G  1 126 ? -39.910 -36.894  -58.442 0.50 27.38 ? 126 SER   G OG  1 
ATOM   8660  N  N   . GLU   G  1 127 ? -43.456 -34.343  -57.517 1.00 25.60 ? 127 GLU   G N   1 
ATOM   8661  C  CA  . GLU   G  1 127 ? -44.148 -33.067  -57.315 1.00 28.11 ? 127 GLU   G CA  1 
ATOM   8662  C  C   . GLU   G  1 127 ? -44.752 -32.972  -55.913 1.00 24.48 ? 127 GLU   G C   1 
ATOM   8663  O  O   . GLU   G  1 127 ? -44.794 -31.883  -55.332 1.00 28.93 ? 127 GLU   G O   1 
ATOM   8664  C  CB  . GLU   G  1 127 ? -45.233 -32.842  -58.372 1.00 29.27 ? 127 GLU   G CB  1 
ATOM   8665  C  CG  . GLU   G  1 127 ? -44.758 -32.983  -59.825 1.00 33.07 ? 127 GLU   G CG  1 
ATOM   8666  C  CD  . GLU   G  1 127 ? -43.528 -32.137  -60.156 1.00 42.59 ? 127 GLU   G CD  1 
ATOM   8667  O  OE1 . GLU   G  1 127 ? -43.418 -30.981  -59.688 1.00 34.14 ? 127 GLU   G OE1 1 
ATOM   8668  O  OE2 . GLU   G  1 127 ? -42.665 -32.639  -60.912 1.00 47.57 ? 127 GLU   G OE2 1 
ATOM   8669  N  N   . GLU   G  1 128 ? -45.232 -34.078  -55.355 1.00 23.66 ? 128 GLU   G N   1 
ATOM   8670  C  CA  . GLU   G  1 128 ? -45.706 -34.017  -53.976 1.00 24.76 ? 128 GLU   G CA  1 
ATOM   8671  C  C   . GLU   G  1 128 ? -44.567 -33.773  -52.991 1.00 31.47 ? 128 GLU   G C   1 
ATOM   8672  O  O   . GLU   G  1 128 ? -44.778 -33.126  -51.959 1.00 27.09 ? 128 GLU   G O   1 
ATOM   8673  C  CB  . GLU   G  1 128 ? -46.453 -35.297  -53.626 1.00 31.50 ? 128 GLU   G CB  1 
ATOM   8674  C  CG  . GLU   G  1 128 ? -47.914 -35.254  -54.139 1.00 36.61 ? 128 GLU   G CG  1 
ATOM   8675  C  CD  . GLU   G  1 128 ? -48.777 -36.387  -53.625 1.00 34.84 ? 128 GLU   G CD  1 
ATOM   8676  O  OE1 . GLU   G  1 128 ? -48.390 -37.042  -52.648 1.00 30.74 ? 128 GLU   G OE1 1 
ATOM   8677  O  OE2 . GLU   G  1 128 ? -49.849 -36.644  -54.214 1.00 32.22 ? 128 GLU   G OE2 1 
ATOM   8678  N  N   . GLU   G  1 129 ? -43.353 -34.254  -53.290 1.00 29.23 ? 129 GLU   G N   1 
ATOM   8679  C  CA  . GLU   G  1 129 ? -42.198 -33.855  -52.480 1.00 25.83 ? 129 GLU   G CA  1 
ATOM   8680  C  C   . GLU   G  1 129 ? -41.930 -32.355  -52.599 1.00 25.26 ? 129 GLU   G C   1 
ATOM   8681  O  O   . GLU   G  1 129 ? -41.581 -31.699  -51.613 1.00 26.05 ? 129 GLU   G O   1 
ATOM   8682  C  CB  . GLU   G  1 129 ? -40.944 -34.638  -52.887 1.00 34.16 ? 129 GLU   G CB  1 
ATOM   8683  C  CG  . GLU   G  1 129 ? -40.966 -36.118  -52.569 1.00 37.19 ? 129 GLU   G CG  1 
ATOM   8684  C  CD  . GLU   G  1 129 ? -39.650 -36.817  -52.956 1.00 57.31 ? 129 GLU   G CD  1 
ATOM   8685  O  OE1 . GLU   G  1 129 ? -38.618 -36.121  -53.089 1.00 63.02 ? 129 GLU   G OE1 1 
ATOM   8686  O  OE2 . GLU   G  1 129 ? -39.645 -38.058  -53.134 1.00 57.87 ? 129 GLU   G OE2 1 
ATOM   8687  N  N   . HIS   G  1 130 ? -42.055 -31.792  -53.802 1.00 25.60 ? 130 HIS   G N   1 
ATOM   8688  C  CA  . HIS   G  1 130 ? -41.838 -30.354  -53.932 1.00 29.57 ? 130 HIS   G CA  1 
ATOM   8689  C  C   . HIS   G  1 130 ? -42.931 -29.574  -53.201 1.00 28.78 ? 130 HIS   G C   1 
ATOM   8690  O  O   . HIS   G  1 130 ? -42.659 -28.530  -52.594 1.00 28.17 ? 130 HIS   G O   1 
ATOM   8691  C  CB  . HIS   G  1 130 ? -41.764 -29.964  -55.419 1.00 31.49 ? 130 HIS   G CB  1 
ATOM   8692  C  CG  . HIS   G  1 130 ? -41.257 -28.571  -55.665 1.00 47.12 ? 130 HIS   G CG  1 
ATOM   8693  N  ND1 . HIS   G  1 130 ? -41.507 -27.878  -56.832 1.00 58.10 ? 130 HIS   G ND1 1 
ATOM   8694  C  CD2 . HIS   G  1 130 ? -40.500 -27.746  -54.900 1.00 51.84 ? 130 HIS   G CD2 1 
ATOM   8695  C  CE1 . HIS   G  1 130 ? -40.940 -26.685  -56.769 1.00 50.69 ? 130 HIS   G CE1 1 
ATOM   8696  N  NE2 . HIS   G  1 130 ? -40.321 -26.580  -55.607 1.00 51.62 ? 130 HIS   G NE2 1 
ATOM   8697  N  N   . ILE   G  1 131 ? -44.173 -30.056  -53.261 1.00 28.90 ? 131 ILE   G N   1 
ATOM   8698  C  CA  . ILE   G  1 131 ? -45.258 -29.395  -52.542 1.00 30.43 ? 131 ILE   G CA  1 
ATOM   8699  C  C   . ILE   G  1 131 ? -44.965 -29.401  -51.044 1.00 28.35 ? 131 ILE   G C   1 
ATOM   8700  O  O   . ILE   G  1 131 ? -45.099 -28.383  -50.351 1.00 27.08 ? 131 ILE   G O   1 
ATOM   8701  C  CB  . ILE   G  1 131 ? -46.603 -30.076  -52.861 1.00 28.52 ? 131 ILE   G CB  1 
ATOM   8702  C  CG1 . ILE   G  1 131 ? -47.086 -29.701  -54.277 1.00 24.88 ? 131 ILE   G CG1 1 
ATOM   8703  C  CG2 . ILE   G  1 131 ? -47.661 -29.676  -51.825 1.00 29.25 ? 131 ILE   G CG2 1 
ATOM   8704  C  CD1 . ILE   G  1 131 ? -48.216 -30.614  -54.831 1.00 26.79 ? 131 ILE   G CD1 1 
ATOM   8705  N  N   . ASP   G  1 132 ? -44.544 -30.543  -50.525 1.00 28.78 ? 132 ASP   G N   1 
ATOM   8706  C  CA  . ASP   G  1 132 ? -44.147 -30.594  -49.118 1.00 32.70 ? 132 ASP   G CA  1 
ATOM   8707  C  C   . ASP   G  1 132 ? -43.074 -29.546  -48.805 1.00 32.98 ? 132 ASP   G C   1 
ATOM   8708  O  O   . ASP   G  1 132 ? -43.208 -28.756  -47.857 1.00 28.34 ? 132 ASP   G O   1 
ATOM   8709  C  CB  . ASP   G  1 132 ? -43.663 -31.994  -48.777 1.00 33.49 ? 132 ASP   G CB  1 
ATOM   8710  C  CG  . ASP   G  1 132 ? -43.515 -32.214  -47.271 1.00 33.46 ? 132 ASP   G CG  1 
ATOM   8711  O  OD1 . ASP   G  1 132 ? -43.828 -31.302  -46.469 1.00 40.53 ? 132 ASP   G OD1 1 
ATOM   8712  O  OD2 . ASP   G  1 132 ? -43.111 -33.313  -46.909 1.00 38.18 ? 132 ASP   G OD2 1 
ATOM   8713  N  N   . TYR   G  1 133 ? -42.010 -29.502  -49.607 1.00 28.99 ? 133 TYR   G N   1 
ATOM   8714  C  CA  . TYR   G  1 133 ? -40.964 -28.503  -49.380 1.00 27.16 ? 133 TYR   G CA  1 
ATOM   8715  C  C   . TYR   G  1 133 ? -41.535 -27.091  -49.358 1.00 29.35 ? 133 TYR   G C   1 
ATOM   8716  O  O   . TYR   G  1 133 ? -41.231 -26.292  -48.465 1.00 31.98 ? 133 TYR   G O   1 
ATOM   8717  C  CB  . TYR   G  1 133 ? -39.875 -28.627  -50.458 1.00 25.46 ? 133 TYR   G CB  1 
ATOM   8718  C  CG  . TYR   G  1 133 ? -38.964 -27.438  -50.508 1.00 28.64 ? 133 TYR   G CG  1 
ATOM   8719  C  CD1 . TYR   G  1 133 ? -37.883 -27.335  -49.641 1.00 25.33 ? 133 TYR   G CD1 1 
ATOM   8720  C  CD2 . TYR   G  1 133 ? -39.187 -26.415  -51.408 1.00 36.78 ? 133 TYR   G CD2 1 
ATOM   8721  C  CE1 . TYR   G  1 133 ? -37.048 -26.231  -49.672 1.00 31.93 ? 133 TYR   G CE1 1 
ATOM   8722  C  CE2 . TYR   G  1 133 ? -38.352 -25.311  -51.456 1.00 39.06 ? 133 TYR   G CE2 1 
ATOM   8723  C  CZ  . TYR   G  1 133 ? -37.302 -25.227  -50.581 1.00 32.43 ? 133 TYR   G CZ  1 
ATOM   8724  O  OH  . TYR   G  1 133 ? -36.490 -24.134  -50.635 1.00 35.50 ? 133 TYR   G OH  1 
ATOM   8725  N  N   . LEU   G  1 134 ? -42.361 -26.759  -50.350 1.00 26.51 ? 134 LEU   G N   1 
ATOM   8726  C  CA  . LEU   G  1 134 ? -42.894 -25.407  -50.470 1.00 27.43 ? 134 LEU   G CA  1 
ATOM   8727  C  C   . LEU   G  1 134 ? -43.790 -25.060  -49.284 1.00 26.64 ? 134 LEU   G C   1 
ATOM   8728  O  O   . LEU   G  1 134 ? -43.671 -23.987  -48.680 1.00 31.86 ? 134 LEU   G O   1 
ATOM   8729  C  CB  . LEU   G  1 134 ? -43.689 -25.303  -51.784 1.00 27.30 ? 134 LEU   G CB  1 
ATOM   8730  C  CG  . LEU   G  1 134 ? -42.821 -25.353  -53.057 1.00 37.37 ? 134 LEU   G CG  1 
ATOM   8731  C  CD1 . LEU   G  1 134 ? -43.660 -25.522  -54.307 1.00 36.75 ? 134 LEU   G CD1 1 
ATOM   8732  C  CD2 . LEU   G  1 134 ? -42.018 -24.104  -53.161 1.00 33.28 ? 134 LEU   G CD2 1 
ATOM   8733  N  N   . GLU   G  1 135 ? -44.718 -25.944  -48.968 1.00 30.12 ? 135 GLU   G N   1 
ATOM   8734  C  CA  . GLU   G  1 135 ? -45.602 -25.710  -47.833 1.00 33.69 ? 135 GLU   G CA  1 
ATOM   8735  C  C   . GLU   G  1 135 ? -44.797 -25.523  -46.558 1.00 39.18 ? 135 GLU   G C   1 
ATOM   8736  O  O   . GLU   G  1 135 ? -45.093 -24.642  -45.737 1.00 32.95 ? 135 GLU   G O   1 
ATOM   8737  C  CB  . GLU   G  1 135 ? -46.562 -26.886  -47.698 1.00 32.87 ? 135 GLU   G CB  1 
ATOM   8738  C  CG  . GLU   G  1 135 ? -47.615 -26.968  -48.821 1.00 34.51 ? 135 GLU   G CG  1 
ATOM   8739  C  CD  . GLU   G  1 135 ? -48.509 -28.184  -48.666 1.00 34.60 ? 135 GLU   G CD  1 
ATOM   8740  O  OE1 . GLU   G  1 135 ? -48.085 -29.173  -48.024 1.00 34.48 ? 135 GLU   G OE1 1 
ATOM   8741  O  OE2 . GLU   G  1 135 ? -49.643 -28.168  -49.183 1.00 42.55 ? 135 GLU   G OE2 1 
ATOM   8742  N  N   . THR   G  1 136 ? -43.778 -26.362  -46.372 1.00 31.52 ? 136 THR   G N   1 
ATOM   8743  C  CA  . THR   G  1 136 ? -42.907 -26.235  -45.216 1.00 31.36 ? 136 THR   G CA  1 
ATOM   8744  C  C   . THR   G  1 136 ? -42.207 -24.876  -45.203 1.00 30.32 ? 136 THR   G C   1 
ATOM   8745  O  O   . THR   G  1 136 ? -42.178 -24.199  -44.166 1.00 30.92 ? 136 THR   G O   1 
ATOM   8746  C  CB  . THR   G  1 136 ? -41.924 -27.410  -45.222 1.00 32.95 ? 136 THR   G CB  1 
ATOM   8747  O  OG1 . THR   G  1 136 ? -42.682 -28.629  -45.133 1.00 36.51 ? 136 THR   G OG1 1 
ATOM   8748  C  CG2 . THR   G  1 136 ? -40.930 -27.338  -44.070 1.00 26.59 ? 136 THR   G CG2 1 
ATOM   8749  N  N   . GLN   G  1 137 ? -41.687 -24.418  -46.352 1.00 27.06 ? 137 GLN   G N   1 
ATOM   8750  C  CA  . GLN   G  1 137 ? -41.011 -23.120  -46.351 1.00 26.44 ? 137 GLN   G CA  1 
ATOM   8751  C  C   . GLN   G  1 137 ? -41.969 -22.007  -45.926 1.00 27.23 ? 137 GLN   G C   1 
ATOM   8752  O  O   . GLN   G  1 137 ? -41.615 -21.120  -45.140 1.00 29.49 ? 137 GLN   G O   1 
ATOM   8753  C  CB  . GLN   G  1 137 ? -40.423 -22.794  -47.731 1.00 30.64 ? 137 GLN   G CB  1 
ATOM   8754  C  CG  . GLN   G  1 137 ? -39.331 -23.754  -48.230 1.00 29.11 ? 137 GLN   G CG  1 
ATOM   8755  C  CD  . GLN   G  1 137 ? -38.557 -24.351  -47.114 1.00 31.43 ? 137 GLN   G CD  1 
ATOM   8756  O  OE1 . GLN   G  1 137 ? -38.810 -25.486  -46.686 1.00 38.04 ? 137 GLN   G OE1 1 
ATOM   8757  N  NE2 . GLN   G  1 137 ? -37.620 -23.602  -46.614 1.00 25.01 ? 137 GLN   G NE2 1 
ATOM   8758  N  N   . LEU   G  1 138 ? -43.152 -21.982  -46.527 1.00 27.95 ? 138 LEU   G N   1 
ATOM   8759  C  CA  . LEU   G  1 138 ? -44.138 -20.966  -46.180 1.00 26.58 ? 138 LEU   G CA  1 
ATOM   8760  C  C   . LEU   G  1 138 ? -44.487 -21.026  -44.694 1.00 32.33 ? 138 LEU   G C   1 
ATOM   8761  O  O   . LEU   G  1 138 ? -44.603 -19.989  -44.029 1.00 33.16 ? 138 LEU   G O   1 
ATOM   8762  C  CB  . LEU   G  1 138 ? -45.389 -21.171  -47.044 1.00 32.44 ? 138 LEU   G CB  1 
ATOM   8763  C  CG  . LEU   G  1 138 ? -45.143 -20.819  -48.519 1.00 34.79 ? 138 LEU   G CG  1 
ATOM   8764  C  CD1 . LEU   G  1 138 ? -46.233 -21.373  -49.427 1.00 36.17 ? 138 LEU   G CD1 1 
ATOM   8765  C  CD2 . LEU   G  1 138 ? -44.997 -19.309  -48.691 1.00 39.76 ? 138 LEU   G CD2 1 
ATOM   8766  N  N   . GLY   G  1 139 ? -44.672 -22.232  -44.160 1.00 35.49 ? 139 GLY   G N   1 
ATOM   8767  C  CA  . GLY   G  1 139 ? -44.862 -22.362  -42.720 1.00 35.21 ? 139 GLY   G CA  1 
ATOM   8768  C  C   . GLY   G  1 139 ? -43.693 -21.833  -41.912 1.00 36.06 ? 139 GLY   G C   1 
ATOM   8769  O  O   . GLY   G  1 139 ? -43.885 -21.149  -40.896 1.00 29.46 ? 139 GLY   G O   1 
ATOM   8770  N  N   . LEU   G  1 140 ? -42.455 -22.132  -42.347 1.00 31.25 ? 140 LEU   G N   1 
ATOM   8771  C  CA  . LEU   G  1 140 ? -41.309 -21.630  -41.601 1.00 26.96 ? 140 LEU   G CA  1 
ATOM   8772  C  C   . LEU   G  1 140 ? -41.306 -20.119  -41.560 1.00 30.50 ? 140 LEU   G C   1 
ATOM   8773  O  O   . LEU   G  1 140 ? -40.949 -19.522  -40.533 1.00 27.73 ? 140 LEU   G O   1 
ATOM   8774  C  CB  . LEU   G  1 140 ? -39.987 -22.129  -42.195 1.00 25.68 ? 140 LEU   G CB  1 
ATOM   8775  C  CG  . LEU   G  1 140 ? -39.649 -23.560  -41.819 1.00 33.06 ? 140 LEU   G CG  1 
ATOM   8776  C  CD1 . LEU   G  1 140 ? -38.537 -24.024  -42.722 1.00 30.02 ? 140 LEU   G CD1 1 
ATOM   8777  C  CD2 . LEU   G  1 140 ? -39.276 -23.646  -40.306 1.00 28.20 ? 140 LEU   G CD2 1 
ATOM   8778  N  N   . ILE   G  1 141 ? -41.690 -19.475  -42.662 1.00 28.33 ? 141 ILE   G N   1 
ATOM   8779  C  CA  . ILE   G  1 141 ? -41.705 -18.017  -42.670 1.00 26.19 ? 141 ILE   G CA  1 
ATOM   8780  C  C   . ILE   G  1 141 ? -42.594 -17.496  -41.548 1.00 32.90 ? 141 ILE   G C   1 
ATOM   8781  O  O   . ILE   G  1 141 ? -42.274 -16.491  -40.900 1.00 33.04 ? 141 ILE   G O   1 
ATOM   8782  C  CB  . ILE   G  1 141 ? -42.165 -17.503  -44.047 1.00 30.50 ? 141 ILE   G CB  1 
ATOM   8783  C  CG1 . ILE   G  1 141 ? -41.021 -17.646  -45.044 1.00 26.47 ? 141 ILE   G CG1 1 
ATOM   8784  C  CG2 . ILE   G  1 141 ? -42.606 -16.067  -43.949 1.00 29.80 ? 141 ILE   G CG2 1 
ATOM   8785  C  CD1 . ILE   G  1 141 ? -41.421 -17.559  -46.528 1.00 29.66 ? 141 ILE   G CD1 1 
ATOM   8786  N  N   . GLN   G  1 142 ? -43.708 -18.189  -41.282 1.00 36.35 ? 142 GLN   G N   1 
ATOM   8787  C  CA  . GLN   G  1 142 ? -44.600 -17.765  -40.201 1.00 38.65 ? 142 GLN   G CA  1 
ATOM   8788  C  C   . GLN   G  1 142 ? -44.016 -18.071  -38.825 1.00 36.82 ? 142 GLN   G C   1 
ATOM   8789  O  O   . GLN   G  1 142 ? -44.235 -17.314  -37.876 1.00 37.09 ? 142 GLN   G O   1 
ATOM   8790  C  CB  . GLN   G  1 142 ? -45.961 -18.452  -40.339 1.00 38.67 ? 142 GLN   G CB  1 
ATOM   8791  C  CG  . GLN   G  1 142 ? -46.715 -18.143  -41.613 1.00 46.82 ? 142 GLN   G CG  1 
ATOM   8792  C  CD  . GLN   G  1 142 ? -46.836 -16.650  -41.888 1.00 48.54 ? 142 GLN   G CD  1 
ATOM   8793  O  OE1 . GLN   G  1 142 ? -47.197 -15.870  -40.995 1.00 44.88 ? 142 GLN   G OE1 1 
ATOM   8794  N  NE2 . GLN   G  1 142 ? -46.523 -16.240  -43.128 1.00 48.09 ? 142 GLN   G NE2 1 
ATOM   8795  N  N   . LYS   G  1 143 ? -43.296 -19.186  -38.683 1.00 35.33 ? 143 LYS   G N   1 
ATOM   8796  C  CA  . LYS   G  1 143 ? -42.785 -19.566  -37.369 1.00 34.82 ? 143 LYS   G CA  1 
ATOM   8797  C  C   . LYS   G  1 143 ? -41.559 -18.758  -36.967 1.00 34.86 ? 143 LYS   G C   1 
ATOM   8798  O  O   . LYS   G  1 143 ? -41.483 -18.254  -35.839 1.00 33.50 ? 143 LYS   G O   1 
ATOM   8799  C  CB  . LYS   G  1 143 ? -42.468 -21.057  -37.347 1.00 32.10 ? 143 LYS   G CB  1 
ATOM   8800  C  CG  . LYS   G  1 143 ? -43.687 -21.934  -37.496 1.00 39.03 ? 143 LYS   G CG  1 
ATOM   8801  C  CD  . LYS   G  1 143 ? -43.299 -23.382  -37.319 1.00 48.13 ? 143 LYS   G CD  1 
ATOM   8802  C  CE  . LYS   G  1 143 ? -44.502 -24.255  -37.048 1.00 56.06 ? 143 LYS   G CE  1 
ATOM   8803  N  NZ  . LYS   G  1 143 ? -45.418 -24.345  -38.217 1.00 62.44 ? 143 LYS   G NZ  1 
ATOM   8804  N  N   . VAL   G  1 144 ? -40.565 -18.645  -37.854 1.00 33.97 ? 144 VAL   G N   1 
ATOM   8805  C  CA  . VAL   G  1 144 ? -39.322 -17.969  -37.481 1.00 27.52 ? 144 VAL   G CA  1 
ATOM   8806  C  C   . VAL   G  1 144 ? -39.331 -16.500  -37.861 1.00 29.18 ? 144 VAL   G C   1 
ATOM   8807  O  O   . VAL   G  1 144 ? -38.460 -15.748  -37.404 1.00 29.72 ? 144 VAL   G O   1 
ATOM   8808  C  CB  . VAL   G  1 144 ? -38.068 -18.643  -38.094 1.00 29.95 ? 144 VAL   G CB  1 
ATOM   8809  C  CG1 . VAL   G  1 144 ? -38.048 -20.152  -37.786 1.00 30.72 ? 144 VAL   G CG1 1 
ATOM   8810  C  CG2 . VAL   G  1 144 ? -37.933 -18.363  -39.624 1.00 27.79 ? 144 VAL   G CG2 1 
ATOM   8811  N  N   . GLY   G  1 145 ? -40.291 -16.060  -38.662 1.00 32.83 ? 145 GLY   G N   1 
ATOM   8812  C  CA  . GLY   G  1 145 ? -40.295 -14.675  -39.119 1.00 31.42 ? 145 GLY   G CA  1 
ATOM   8813  C  C   . GLY   G  1 145 ? -39.509 -14.505  -40.405 1.00 31.48 ? 145 GLY   G C   1 
ATOM   8814  O  O   . GLY   G  1 145 ? -38.547 -15.217  -40.675 1.00 30.88 ? 145 GLY   G O   1 
ATOM   8815  N  N   . LEU   G  1 146 ? -39.927 -13.526  -41.220 1.00 33.23 ? 146 LEU   G N   1 
ATOM   8816  C  CA  . LEU   G  1 146 ? -39.379 -13.425  -42.571 1.00 36.17 ? 146 LEU   G CA  1 
ATOM   8817  C  C   . LEU   G  1 146 ? -37.881 -13.143  -42.550 1.00 28.58 ? 146 LEU   G C   1 
ATOM   8818  O  O   . LEU   G  1 146 ? -37.121 -13.725  -43.333 1.00 32.16 ? 146 LEU   G O   1 
ATOM   8819  C  CB  . LEU   G  1 146 ? -40.106 -12.334  -43.372 1.00 30.13 ? 146 LEU   G CB  1 
ATOM   8820  C  CG  . LEU   G  1 146 ? -39.590 -12.126  -44.794 1.00 31.16 ? 146 LEU   G CG  1 
ATOM   8821  C  CD1 . LEU   G  1 146 ? -39.636 -13.431  -45.590 1.00 29.02 ? 146 LEU   G CD1 1 
ATOM   8822  C  CD2 . LEU   G  1 146 ? -40.396 -11.058  -45.489 1.00 38.25 ? 146 LEU   G CD2 1 
ATOM   8823  N  N   . GLU   G  1 147 ? -37.443 -12.230  -41.686 1.00 25.89 ? 147 GLU   G N   1 
ATOM   8824  C  CA  . GLU   G  1 147 ? -36.050 -11.818  -41.689 1.00 31.02 ? 147 GLU   G CA  1 
ATOM   8825  C  C   . GLU   G  1 147 ? -35.125 -12.963  -41.290 1.00 31.65 ? 147 GLU   G C   1 
ATOM   8826  O  O   . GLU   G  1 147 ? -34.086 -13.175  -41.941 1.00 27.76 ? 147 GLU   G O   1 
ATOM   8827  C  CB  . GLU   G  1 147 ? -35.861 -10.622  -40.777 1.00 35.68 ? 147 GLU   G CB  1 
ATOM   8828  C  CG  . GLU   G  1 147 ? -36.395 -9.331   -41.358 1.00 39.07 ? 147 GLU   G CG  1 
ATOM   8829  C  CD  . GLU   G  1 147 ? -35.965 -8.129   -40.529 1.00 54.05 ? 147 GLU   G CD  1 
ATOM   8830  O  OE1 . GLU   G  1 147 ? -35.784 -8.302   -39.300 1.00 58.15 ? 147 GLU   G OE1 1 
ATOM   8831  O  OE2 . GLU   G  1 147 ? -35.803 -7.024   -41.093 1.00 60.59 ? 147 GLU   G OE2 1 
ATOM   8832  N  N   . ASN   G  1 148 ? -35.505 -13.732  -40.258 1.00 26.27 ? 148 ASN   G N   1 
ATOM   8833  C  CA  . ASN   G  1 148 ? -34.760 -14.936  -39.905 1.00 33.40 ? 148 ASN   G CA  1 
ATOM   8834  C  C   . ASN   G  1 148 ? -34.832 -15.967  -41.003 1.00 29.78 ? 148 ASN   G C   1 
ATOM   8835  O  O   . ASN   G  1 148 ? -33.830 -16.636  -41.296 1.00 30.21 ? 148 ASN   G O   1 
ATOM   8836  C  CB  . ASN   G  1 148 ? -35.283 -15.576  -38.625 1.00 27.10 ? 148 ASN   G CB  1 
ATOM   8837  C  CG  . ASN   G  1 148 ? -34.789 -14.874  -37.360 1.00 23.26 ? 148 ASN   G CG  1 
ATOM   8838  O  OD1 . ASN   G  1 148 ? -33.946 -13.995  -37.406 1.00 25.15 ? 148 ASN   G OD1 1 
ATOM   8839  N  ND2 . ASN   G  1 148 ? -35.324 -15.281  -36.223 1.00 30.55 ? 148 ASN   G ND2 1 
ATOM   8840  N  N   . TYR   G  1 149 ? -36.010 -16.132  -41.622 1.00 25.59 ? 149 TYR   G N   1 
ATOM   8841  C  CA  . TYR   G  1 149 ? -36.109 -17.147  -42.656 1.00 23.16 ? 149 TYR   G CA  1 
ATOM   8842  C  C   . TYR   G  1 149 ? -35.130 -16.854  -43.790 1.00 30.60 ? 149 TYR   G C   1 
ATOM   8843  O  O   . TYR   G  1 149 ? -34.475 -17.763  -44.314 1.00 28.42 ? 149 TYR   G O   1 
ATOM   8844  C  CB  . TYR   G  1 149 ? -37.529 -17.238  -43.202 1.00 28.44 ? 149 TYR   G CB  1 
ATOM   8845  C  CG  . TYR   G  1 149 ? -37.605 -18.232  -44.322 1.00 25.78 ? 149 TYR   G CG  1 
ATOM   8846  C  CD1 . TYR   G  1 149 ? -37.758 -19.586  -44.051 1.00 29.74 ? 149 TYR   G CD1 1 
ATOM   8847  C  CD2 . TYR   G  1 149 ? -37.440 -17.831  -45.654 1.00 30.57 ? 149 TYR   G CD2 1 
ATOM   8848  C  CE1 . TYR   G  1 149 ? -37.797 -20.516  -45.077 1.00 27.58 ? 149 TYR   G CE1 1 
ATOM   8849  C  CE2 . TYR   G  1 149 ? -37.472 -18.748  -46.679 1.00 28.69 ? 149 TYR   G CE2 1 
ATOM   8850  C  CZ  . TYR   G  1 149 ? -37.639 -20.082  -46.390 1.00 30.54 ? 149 TYR   G CZ  1 
ATOM   8851  O  OH  . TYR   G  1 149 ? -37.637 -20.970  -47.428 1.00 33.00 ? 149 TYR   G OH  1 
ATOM   8852  N  N   . LEU   G  1 150 ? -35.048 -15.589  -44.203 1.00 27.02 ? 150 LEU   G N   1 
ATOM   8853  C  CA  . LEU   G  1 150 ? -34.175 -15.205  -45.298 1.00 29.91 ? 150 LEU   G CA  1 
ATOM   8854  C  C   . LEU   G  1 150 ? -32.725 -15.299  -44.864 1.00 29.22 ? 150 LEU   G C   1 
ATOM   8855  O  O   . LEU   G  1 150 ? -31.861 -15.764  -45.624 1.00 27.48 ? 150 LEU   G O   1 
ATOM   8856  C  CB  . LEU   G  1 150 ? -34.515 -13.784  -45.752 1.00 24.85 ? 150 LEU   G CB  1 
ATOM   8857  C  CG  . LEU   G  1 150 ? -35.919 -13.595  -46.344 1.00 34.77 ? 150 LEU   G CG  1 
ATOM   8858  C  CD1 . LEU   G  1 150 ? -36.193 -12.139  -46.630 1.00 33.63 ? 150 LEU   G CD1 1 
ATOM   8859  C  CD2 . LEU   G  1 150 ? -36.097 -14.410  -47.618 1.00 31.87 ? 150 LEU   G CD2 1 
ATOM   8860  N  N   . GLN   G  1 151 ? -32.453 -14.878  -43.631 1.00 28.88 ? 151 GLN   G N   1 
ATOM   8861  C  CA  . GLN   G  1 151 ? -31.122 -15.023  -43.062 1.00 31.36 ? 151 GLN   G CA  1 
ATOM   8862  C  C   . GLN   G  1 151 ? -30.623 -16.456  -43.196 1.00 30.66 ? 151 GLN   G C   1 
ATOM   8863  O  O   . GLN   G  1 151 ? -29.472 -16.706  -43.583 1.00 27.86 ? 151 GLN   G O   1 
ATOM   8864  C  CB  . GLN   G  1 151 ? -31.149 -14.608  -41.598 1.00 29.99 ? 151 GLN   G CB  1 
ATOM   8865  C  CG  . GLN   G  1 151 ? -29.773 -14.809  -40.919 1.00 29.58 ? 151 GLN   G CG  1 
ATOM   8866  C  CD  . GLN   G  1 151 ? -29.795 -14.417  -39.465 1.00 30.11 ? 151 GLN   G CD  1 
ATOM   8867  O  OE1 . GLN   G  1 151 ? -30.810 -14.598  -38.792 1.00 28.62 ? 151 GLN   G OE1 1 
ATOM   8868  N  NE2 . GLN   G  1 151 ? -28.688 -13.839  -38.974 1.00 25.93 ? 151 GLN   G NE2 1 
ATOM   8869  N  N   . SER   G  1 152 ? -31.489 -17.406  -42.888 1.00 25.40 ? 152 SER   G N   1 
ATOM   8870  C  CA  . SER   G  1 152 ? -31.126 -18.810  -42.901 1.00 35.33 ? 152 SER   G CA  1 
ATOM   8871  C  C   . SER   G  1 152 ? -30.937 -19.347  -44.303 1.00 34.81 ? 152 SER   G C   1 
ATOM   8872  O  O   . SER   G  1 152 ? -30.448 -20.473  -44.452 1.00 30.07 ? 152 SER   G O   1 
ATOM   8873  C  CB  . SER   G  1 152 ? -32.190 -19.617  -42.162 1.00 30.93 ? 152 SER   G CB  1 
ATOM   8874  O  OG  . SER   G  1 152 ? -32.115 -19.323  -40.773 1.00 31.79 ? 152 SER   G OG  1 
ATOM   8875  N  N   . HIS   G  1 153 ? -31.268 -18.562  -45.326 1.00 31.11 ? 153 HIS   G N   1 
ATOM   8876  C  CA  . HIS   G  1 153 ? -31.090 -18.986  -46.699 1.00 27.99 ? 153 HIS   G CA  1 
ATOM   8877  C  C   . HIS   G  1 153 ? -30.058 -18.148  -47.448 1.00 31.30 ? 153 HIS   G C   1 
ATOM   8878  O  O   . HIS   G  1 153 ? -29.920 -18.298  -48.671 1.00 30.05 ? 153 HIS   G O   1 
ATOM   8879  C  CB  . HIS   G  1 153 ? -32.449 -19.001  -47.387 1.00 26.97 ? 153 HIS   G CB  1 
ATOM   8880  C  CG  . HIS   G  1 153 ? -33.296 -20.132  -46.915 1.00 30.88 ? 153 HIS   G CG  1 
ATOM   8881  N  ND1 . HIS   G  1 153 ? -33.973 -20.102  -45.712 1.00 29.92 ? 153 HIS   G ND1 1 
ATOM   8882  C  CD2 . HIS   G  1 153 ? -33.435 -21.388  -47.392 1.00 29.19 ? 153 HIS   G CD2 1 
ATOM   8883  C  CE1 . HIS   G  1 153 ? -34.571 -21.263  -45.522 1.00 30.54 ? 153 HIS   G CE1 1 
ATOM   8884  N  NE2 . HIS   G  1 153 ? -34.253 -22.064  -46.522 1.00 28.67 ? 153 HIS   G NE2 1 
ATOM   8885  N  N   . MET   G  1 154 ? -29.278 -17.330  -46.735 1.00 25.90 ? 154 MET   G N   1 
ATOM   8886  C  CA  . MET   G  1 154 ? -28.195 -16.594  -47.384 1.00 35.28 ? 154 MET   G CA  1 
ATOM   8887  C  C   . MET   G  1 154 ? -27.095 -17.526  -47.878 1.00 34.53 ? 154 MET   G C   1 
ATOM   8888  O  O   . MET   G  1 154 ? -26.647 -17.422  -49.028 1.00 33.99 ? 154 MET   G O   1 
ATOM   8889  C  CB  . MET   G  1 154 ? -27.603 -15.569  -46.420 1.00 36.40 ? 154 MET   G CB  1 
ATOM   8890  C  CG  . MET   G  1 154 ? -28.474 -14.339  -46.222 1.00 40.25 ? 154 MET   G CG  1 
ATOM   8891  S  SD  . MET   G  1 154 ? -27.817 -13.208  -44.975 1.00 46.29 ? 154 MET   G SD  1 
ATOM   8892  C  CE  . MET   G  1 154 ? -26.052 -13.357  -45.266 1.00 39.03 ? 154 MET   G CE  1 
ATOM   8893  N  N   . HIS   G  1 155 ? -26.620 -18.411  -47.013 1.00 37.32 ? 155 HIS   G N   1 
ATOM   8894  C  CA  . HIS   G  1 155 ? -25.453 -19.246  -47.282 1.00 45.03 ? 155 HIS   G CA  1 
ATOM   8895  C  C   . HIS   G  1 155 ? -25.855 -20.696  -47.564 1.00 41.63 ? 155 HIS   G C   1 
ATOM   8896  O  O   . HIS   G  1 155 ? -26.765 -21.236  -46.927 1.00 45.31 ? 155 HIS   G O   1 
ATOM   8897  C  CB  . HIS   G  1 155 ? -24.499 -19.214  -46.080 1.00 46.23 ? 155 HIS   G CB  1 
ATOM   8898  C  CG  . HIS   G  1 155 ? -24.015 -17.841  -45.710 1.00 43.34 ? 155 HIS   G CG  1 
ATOM   8899  N  ND1 . HIS   G  1 155 ? -23.857 -17.433  -44.402 1.00 45.05 ? 155 HIS   G ND1 1 
ATOM   8900  C  CD2 . HIS   G  1 155 ? -23.631 -16.790  -46.477 1.00 58.20 ? 155 HIS   G CD2 1 
ATOM   8901  C  CE1 . HIS   G  1 155 ? -23.411 -16.188  -44.378 1.00 50.61 ? 155 HIS   G CE1 1 
ATOM   8902  N  NE2 . HIS   G  1 155 ? -23.261 -15.775  -45.625 1.00 49.72 ? 155 HIS   G NE2 1 
ATOM   8903  N  N   . GLU   G  1 156 ? -25.164 -21.333  -48.506 1.00 48.98 ? 156 GLU   G N   1 
ATOM   8904  C  CA  . GLU   G  1 156 ? -25.176 -22.799  -48.597 1.00 54.58 ? 156 GLU   G CA  1 
ATOM   8905  C  C   . GLU   G  1 156 ? -24.275 -23.409  -47.508 1.00 49.68 ? 156 GLU   G C   1 
ATOM   8906  O  O   . GLU   G  1 156 ? -24.644 -24.389  -46.852 1.00 58.86 ? 156 GLU   G O   1 
ATOM   8907  C  CB  . GLU   G  1 156 ? -24.700 -23.272  -49.969 1.00 57.07 ? 156 GLU   G CB  1 
ATOM   8908  C  CG  . GLU   G  1 156 ? -25.215 -22.449  -51.118 1.00 45.95 ? 156 GLU   G CG  1 
ATOM   8909  C  CD  . GLU   G  1 156 ? -24.864 -23.046  -52.465 1.00 64.37 ? 156 GLU   G CD  1 
ATOM   8910  O  OE1 . GLU   G  1 156 ? -24.735 -24.289  -52.542 1.00 70.57 ? 156 GLU   G OE1 1 
ATOM   8911  O  OE2 . GLU   G  1 156 ? -24.722 -22.274  -53.445 1.00 54.21 ? 156 GLU   G OE2 1 
ATOM   8912  N  N   . MET   H  1 1   ? 20.988  -76.385  -9.122  1.00 37.55 ? 1   MET   H N   1 
ATOM   8913  C  CA  . MET   H  1 1   ? 20.404  -77.702  -8.723  1.00 45.28 ? 1   MET   H CA  1 
ATOM   8914  C  C   . MET   H  1 1   ? 21.523  -78.740  -8.752  1.00 46.63 ? 1   MET   H C   1 
ATOM   8915  O  O   . MET   H  1 1   ? 22.176  -78.892  -9.768  1.00 39.28 ? 1   MET   H O   1 
ATOM   8916  C  CB  . MET   H  1 1   ? 19.269  -78.093  -9.662  1.00 42.21 ? 1   MET   H CB  1 
ATOM   8917  C  CG  . MET   H  1 1   ? 18.347  -79.166  -9.112  1.00 43.78 ? 1   MET   H CG  1 
ATOM   8918  S  SD  . MET   H  1 1   ? 17.126  -79.665  -10.300 1.00 50.37 ? 1   MET   H SD  1 
ATOM   8919  C  CE  . MET   H  1 1   ? 18.096  -80.673  -11.428 1.00 57.22 ? 1   MET   H CE  1 
ATOM   8920  N  N   . LYS   H  1 2   ? 21.761  -79.441  -7.646  1.00 47.13 ? 2   LYS   H N   1 
ATOM   8921  C  CA  . LYS   H  1 2   ? 22.894  -80.359  -7.574  1.00 39.63 ? 2   LYS   H CA  1 
ATOM   8922  C  C   . LYS   H  1 2   ? 22.655  -81.567  -8.480  1.00 39.27 ? 2   LYS   H C   1 
ATOM   8923  O  O   . LYS   H  1 2   ? 21.719  -82.340  -8.266  1.00 37.64 ? 2   LYS   H O   1 
ATOM   8924  C  CB  . LYS   H  1 2   ? 23.130  -80.812  -6.132  1.00 41.55 ? 2   LYS   H CB  1 
ATOM   8925  N  N   . GLY   H  1 3   ? 23.493  -81.725  -9.498  1.00 35.05 ? 3   GLY   H N   1 
ATOM   8926  C  CA  . GLY   H  1 3   ? 23.387  -82.868  -10.372 1.00 38.49 ? 3   GLY   H CA  1 
ATOM   8927  C  C   . GLY   H  1 3   ? 24.272  -84.039  -9.955  1.00 36.71 ? 3   GLY   H C   1 
ATOM   8928  O  O   . GLY   H  1 3   ? 25.218  -83.897  -9.186  1.00 41.42 ? 3   GLY   H O   1 
ATOM   8929  N  N   . ASP   H  1 4   ? 23.912  -85.203  -10.480 1.00 35.37 ? 4   ASP   H N   1 
ATOM   8930  C  CA  . ASP   H  1 4   ? 24.741  -86.401  -10.422 1.00 39.90 ? 4   ASP   H CA  1 
ATOM   8931  C  C   . ASP   H  1 4   ? 26.161  -86.135  -10.923 1.00 43.74 ? 4   ASP   H C   1 
ATOM   8932  O  O   . ASP   H  1 4   ? 26.376  -85.580  -12.003 1.00 35.91 ? 4   ASP   H O   1 
ATOM   8933  C  CB  . ASP   H  1 4   ? 24.051  -87.492  -11.247 1.00 44.24 ? 4   ASP   H CB  1 
ATOM   8934  C  CG  . ASP   H  1 4   ? 24.660  -88.878  -11.053 1.00 49.69 ? 4   ASP   H CG  1 
ATOM   8935  O  OD1 . ASP   H  1 4   ? 24.364  -89.516  -10.024 1.00 42.19 ? 4   ASP   H OD1 1 
ATOM   8936  O  OD2 . ASP   H  1 4   ? 25.391  -89.345  -11.956 1.00 47.23 ? 4   ASP   H OD2 1 
ATOM   8937  N  N   . LYS   H  1 5   ? 27.143  -86.530  -10.114 1.00 39.60 ? 5   LYS   H N   1 
ATOM   8938  C  CA  . LYS   H  1 5   ? 28.536  -86.280  -10.470 1.00 46.41 ? 5   LYS   H CA  1 
ATOM   8939  C  C   . LYS   H  1 5   ? 28.919  -87.009  -11.759 1.00 34.83 ? 5   LYS   H C   1 
ATOM   8940  O  O   . LYS   H  1 5   ? 29.645  -86.466  -12.595 1.00 37.34 ? 5   LYS   H O   1 
ATOM   8941  C  CB  . LYS   H  1 5   ? 29.443  -86.703  -9.308  1.00 42.70 ? 5   LYS   H CB  1 
ATOM   8942  C  CG  . LYS   H  1 5   ? 30.834  -86.099  -9.333  1.00 43.72 ? 5   LYS   H CG  1 
ATOM   8943  N  N   . LYS   H  1 6   ? 28.437  -88.232  -11.941 1.00 35.04 ? 6   LYS   H N   1 
ATOM   8944  C  CA  . LYS   H  1 6   ? 28.763  -88.980  -13.151 1.00 41.49 ? 6   LYS   H CA  1 
ATOM   8945  C  C   . LYS   H  1 6   ? 28.001  -88.470  -14.384 1.00 46.24 ? 6   LYS   H C   1 
ATOM   8946  O  O   . LYS   H  1 6   ? 28.527  -88.533  -15.503 1.00 37.00 ? 6   LYS   H O   1 
ATOM   8947  C  CB  . LYS   H  1 6   ? 28.477  -90.468  -12.920 1.00 44.93 ? 6   LYS   H CB  1 
ATOM   8948  C  CG  . LYS   H  1 6   ? 28.739  -91.365  -14.112 1.00 52.86 ? 6   LYS   H CG  1 
ATOM   8949  N  N   . VAL   H  1 7   ? 26.769  -87.981  -14.221 1.00 33.01 ? 7   VAL   H N   1 
ATOM   8950  C  CA  . VAL   H  1 7   ? 26.128  -87.275  -15.329 1.00 34.94 ? 7   VAL   H CA  1 
ATOM   8951  C  C   . VAL   H  1 7   ? 27.006  -86.124  -15.785 1.00 29.09 ? 7   VAL   H C   1 
ATOM   8952  O  O   . VAL   H  1 7   ? 27.331  -86.002  -16.967 1.00 30.19 ? 7   VAL   H O   1 
ATOM   8953  C  CB  . VAL   H  1 7   ? 24.720  -86.784  -14.950 1.00 37.08 ? 7   VAL   H CB  1 
ATOM   8954  C  CG1 . VAL   H  1 7   ? 24.163  -85.887  -16.086 1.00 37.21 ? 7   VAL   H CG1 1 
ATOM   8955  C  CG2 . VAL   H  1 7   ? 23.806  -87.946  -14.725 1.00 38.38 ? 7   VAL   H CG2 1 
ATOM   8956  N  N   . ILE   H  1 8   ? 27.439  -85.280  -14.853 1.00 35.55 ? 8   ILE   H N   1 
ATOM   8957  C  CA  . ILE   H  1 8   ? 28.281  -84.151  -15.229 1.00 33.03 ? 8   ILE   H CA  1 
ATOM   8958  C  C   . ILE   H  1 8   ? 29.550  -84.625  -15.930 1.00 45.08 ? 8   ILE   H C   1 
ATOM   8959  O  O   . ILE   H  1 8   ? 30.042  -83.977  -16.871 1.00 33.36 ? 8   ILE   H O   1 
ATOM   8960  C  CB  . ILE   H  1 8   ? 28.609  -83.302  -13.990 1.00 31.00 ? 8   ILE   H CB  1 
ATOM   8961  C  CG1 . ILE   H  1 8   ? 27.344  -82.634  -13.453 1.00 41.65 ? 8   ILE   H CG1 1 
ATOM   8962  C  CG2 . ILE   H  1 8   ? 29.689  -82.254  -14.330 1.00 35.98 ? 8   ILE   H CG2 1 
ATOM   8963  C  CD1 . ILE   H  1 8   ? 27.528  -81.946  -12.075 1.00 49.73 ? 8   ILE   H CD1 1 
ATOM   8964  N  N   . GLN   H  1 9   ? 30.115  -85.750  -15.482 1.00 36.80 ? 9   GLN   H N   1 
ATOM   8965  C  CA  . GLN   H  1 9   ? 31.321  -86.248  -16.137 1.00 40.27 ? 9   GLN   H CA  1 
ATOM   8966  C  C   . GLN   H  1 9   ? 31.016  -86.661  -17.564 1.00 32.58 ? 9   GLN   H C   1 
ATOM   8967  O  O   . GLN   H  1 9   ? 31.783  -86.350  -18.487 1.00 36.96 ? 9   GLN   H O   1 
ATOM   8968  C  CB  . GLN   H  1 9   ? 31.923  -87.421  -15.348 1.00 37.45 ? 9   GLN   H CB  1 
ATOM   8969  C  CG  . GLN   H  1 9   ? 32.561  -86.983  -14.042 1.00 46.81 ? 9   GLN   H CG  1 
ATOM   8970  C  CD  . GLN   H  1 9   ? 33.091  -88.145  -13.209 1.00 50.98 ? 9   GLN   H CD  1 
ATOM   8971  O  OE1 . GLN   H  1 9   ? 32.548  -89.248  -13.238 1.00 50.13 ? 9   GLN   H OE1 1 
ATOM   8972  N  NE2 . GLN   H  1 9   ? 34.167  -87.895  -12.477 1.00 44.05 ? 9   GLN   H NE2 1 
ATOM   8973  N  N   . HIS   H  1 10  ? 29.900  -87.358  -17.754 1.00 33.64 ? 10  HIS   H N   1 
ATOM   8974  C  CA  . HIS   H  1 10  ? 29.473  -87.728  -19.095 1.00 38.89 ? 10  HIS   H CA  1 
ATOM   8975  C  C   . HIS   H  1 10  ? 29.229  -86.493  -19.948 1.00 36.92 ? 10  HIS   H C   1 
ATOM   8976  O  O   . HIS   H  1 10  ? 29.613  -86.463  -21.117 1.00 36.08 ? 10  HIS   H O   1 
ATOM   8977  C  CB  . HIS   H  1 10  ? 28.214  -88.574  -19.040 1.00 37.86 ? 10  HIS   H CB  1 
ATOM   8978  C  CG  . HIS   H  1 10  ? 28.470  -90.029  -18.833 1.00 45.56 ? 10  HIS   H CG  1 
ATOM   8979  N  ND1 . HIS   H  1 10  ? 29.043  -90.828  -19.799 1.00 42.03 ? 10  HIS   H ND1 1 
ATOM   8980  C  CD2 . HIS   H  1 10  ? 28.205  -90.836  -17.780 1.00 41.24 ? 10  HIS   H CD2 1 
ATOM   8981  C  CE1 . HIS   H  1 10  ? 29.108  -92.068  -19.352 1.00 46.29 ? 10  HIS   H CE1 1 
ATOM   8982  N  NE2 . HIS   H  1 10  ? 28.612  -92.098  -18.127 1.00 45.97 ? 10  HIS   H NE2 1 
ATOM   8983  N  N   . LEU   H  1 11  ? 28.599  -85.461  -19.373 1.00 35.63 ? 11  LEU   H N   1 
ATOM   8984  C  CA  . LEU   H  1 11  ? 28.317  -84.252  -20.140 1.00 40.37 ? 11  LEU   H CA  1 
ATOM   8985  C  C   . LEU   H  1 11  ? 29.609  -83.557  -20.530 1.00 35.79 ? 11  LEU   H C   1 
ATOM   8986  O  O   . LEU   H  1 11  ? 29.726  -83.026  -21.638 1.00 39.00 ? 11  LEU   H O   1 
ATOM   8987  C  CB  . LEU   H  1 11  ? 27.410  -83.307  -19.345 1.00 34.51 ? 11  LEU   H CB  1 
ATOM   8988  C  CG  . LEU   H  1 11  ? 25.976  -83.797  -19.082 1.00 29.91 ? 11  LEU   H CG  1 
ATOM   8989  C  CD1 . LEU   H  1 11  ? 25.192  -82.819  -18.207 1.00 33.41 ? 11  LEU   H CD1 1 
ATOM   8990  C  CD2 . LEU   H  1 11  ? 25.225  -84.044  -20.351 1.00 35.61 ? 11  LEU   H CD2 1 
ATOM   8991  N  N   . ASN   H  1 12  ? 30.592  -83.542  -19.630 1.00 33.00 ? 12  ASN   H N   1 
ATOM   8992  C  CA  . ASN   H  1 12  ? 31.876  -82.941  -19.963 1.00 37.38 ? 12  ASN   H CA  1 
ATOM   8993  C  C   . ASN   H  1 12  ? 32.616  -83.754  -21.019 1.00 38.00 ? 12  ASN   H C   1 
ATOM   8994  O  O   . ASN   H  1 12  ? 33.400  -83.196  -21.793 1.00 34.24 ? 12  ASN   H O   1 
ATOM   8995  C  CB  . ASN   H  1 12  ? 32.726  -82.792  -18.711 1.00 39.30 ? 12  ASN   H CB  1 
ATOM   8996  C  CG  . ASN   H  1 12  ? 32.711  -81.375  -18.164 1.00 42.33 ? 12  ASN   H CG  1 
ATOM   8997  O  OD1 . ASN   H  1 12  ? 32.588  -80.403  -18.920 1.00 32.66 ? 12  ASN   H OD1 1 
ATOM   8998  N  ND2 . ASN   H  1 12  ? 32.847  -81.245  -16.844 1.00 36.05 ? 12  ASN   H ND2 1 
ATOM   8999  N  N   . LYS   H  1 13  ? 32.364  -85.058  -21.090 1.00 35.92 ? 13  LYS   H N   1 
ATOM   9000  C  CA  . LYS   H  1 13  ? 32.960  -85.851  -22.159 1.00 41.51 ? 13  LYS   H CA  1 
ATOM   9001  C  C   . LYS   H  1 13  ? 32.325  -85.510  -23.505 1.00 38.89 ? 13  LYS   H C   1 
ATOM   9002  O  O   . LYS   H  1 13  ? 33.031  -85.342  -24.501 1.00 35.45 ? 13  LYS   H O   1 
ATOM   9003  C  CB  . LYS   H  1 13  ? 32.795  -87.341  -21.856 1.00 40.02 ? 13  LYS   H CB  1 
ATOM   9004  C  CG  . LYS   H  1 13  ? 33.627  -88.285  -22.747 1.00 40.91 ? 13  LYS   H CG  1 
ATOM   9005  C  CD  . LYS   H  1 13  ? 33.488  -89.754  -22.281 1.00 49.27 ? 13  LYS   H CD  1 
ATOM   9006  C  CE  . LYS   H  1 13  ? 34.341  -90.720  -23.093 1.00 50.31 ? 13  LYS   H CE  1 
ATOM   9007  N  NZ  . LYS   H  1 13  ? 33.970  -92.132  -22.794 1.00 60.17 ? 13  LYS   H NZ  1 
ATOM   9008  N  N   . ILE   H  1 14  ? 30.989  -85.420  -23.557 1.00 38.67 ? 14  ILE   H N   1 
ATOM   9009  C  CA  . ILE   H  1 14  ? 30.326  -84.968  -24.777 1.00 35.38 ? 14  ILE   H CA  1 
ATOM   9010  C  C   . ILE   H  1 14  ? 30.846  -83.599  -25.158 1.00 39.24 ? 14  ILE   H C   1 
ATOM   9011  O  O   . ILE   H  1 14  ? 31.207  -83.343  -26.316 1.00 37.08 ? 14  ILE   H O   1 
ATOM   9012  C  CB  . ILE   H  1 14  ? 28.796  -84.932  -24.604 1.00 33.35 ? 14  ILE   H CB  1 
ATOM   9013  C  CG1 . ILE   H  1 14  ? 28.249  -86.254  -24.079 1.00 33.13 ? 14  ILE   H CG1 1 
ATOM   9014  C  CG2 . ILE   H  1 14  ? 28.124  -84.511  -25.937 1.00 32.40 ? 14  ILE   H CG2 1 
ATOM   9015  C  CD1 . ILE   H  1 14  ? 28.937  -87.445  -24.658 1.00 43.29 ? 14  ILE   H CD1 1 
ATOM   9016  N  N   . LEU   H  1 15  ? 30.885  -82.694  -24.180 1.00 34.81 ? 15  LEU   H N   1 
ATOM   9017  C  CA  . LEU   H  1 15  ? 31.411  -81.364  -24.431 1.00 30.27 ? 15  LEU   H CA  1 
ATOM   9018  C  C   . LEU   H  1 15  ? 32.781  -81.448  -25.072 1.00 37.87 ? 15  LEU   H C   1 
ATOM   9019  O  O   . LEU   H  1 15  ? 33.064  -80.751  -26.056 1.00 31.76 ? 15  LEU   H O   1 
ATOM   9020  C  CB  . LEU   H  1 15  ? 31.460  -80.563  -23.127 1.00 34.12 ? 15  LEU   H CB  1 
ATOM   9021  C  CG  . LEU   H  1 15  ? 32.009  -79.139  -23.245 1.00 31.81 ? 15  LEU   H CG  1 
ATOM   9022  C  CD1 . LEU   H  1 15  ? 31.260  -78.380  -24.372 1.00 36.73 ? 15  LEU   H CD1 1 
ATOM   9023  C  CD2 . LEU   H  1 15  ? 31.876  -78.390  -21.929 1.00 29.70 ? 15  LEU   H CD2 1 
ATOM   9024  N  N   . GLY   H  1 16  ? 33.640  -82.324  -24.547 1.00 35.32 ? 16  GLY   H N   1 
ATOM   9025  C  CA  . GLY   H  1 16  ? 34.974  -82.418  -25.086 1.00 28.34 ? 16  GLY   H CA  1 
ATOM   9026  C  C   . GLY   H  1 16  ? 34.972  -82.858  -26.533 1.00 30.76 ? 16  GLY   H C   1 
ATOM   9027  O  O   . GLY   H  1 16  ? 35.779  -82.381  -27.335 1.00 35.32 ? 16  GLY   H O   1 
ATOM   9028  N  N   . ASN   H  1 17  ? 34.060  -83.773  -26.886 1.00 34.20 ? 17  ASN   H N   1 
ATOM   9029  C  CA  . ASN   H  1 17  ? 33.934  -84.185  -28.281 1.00 36.92 ? 17  ASN   H CA  1 
ATOM   9030  C  C   . ASN   H  1 17  ? 33.475  -83.022  -29.153 1.00 41.29 ? 17  ASN   H C   1 
ATOM   9031  O  O   . ASN   H  1 17  ? 33.919  -82.889  -30.295 1.00 33.56 ? 17  ASN   H O   1 
ATOM   9032  C  CB  . ASN   H  1 17  ? 32.949  -85.351  -28.427 1.00 38.80 ? 17  ASN   H CB  1 
ATOM   9033  C  CG  . ASN   H  1 17  ? 33.463  -86.667  -27.828 1.00 39.00 ? 17  ASN   H CG  1 
ATOM   9034  O  OD1 . ASN   H  1 17  ? 34.662  -86.859  -27.642 1.00 47.59 ? 17  ASN   H OD1 1 
ATOM   9035  N  ND2 . ASN   H  1 17  ? 32.545  -87.578  -27.543 1.00 38.87 ? 17  ASN   H ND2 1 
ATOM   9036  N  N   . GLU   H  1 18  ? 32.561  -82.185  -28.634 1.00 40.70 ? 18  GLU   H N   1 
ATOM   9037  C  CA  . GLU   H  1 18  ? 32.055  -81.043  -29.391 1.00 40.13 ? 18  GLU   H CA  1 
ATOM   9038  C  C   . GLU   H  1 18  ? 33.150  -80.025  -29.670 1.00 31.95 ? 18  GLU   H C   1 
ATOM   9039  O  O   . GLU   H  1 18  ? 33.168  -79.410  -30.741 1.00 33.10 ? 18  GLU   H O   1 
ATOM   9040  C  CB  . GLU   H  1 18  ? 30.909  -80.369  -28.631 1.00 39.79 ? 18  GLU   H CB  1 
ATOM   9041  C  CG  . GLU   H  1 18  ? 29.645  -81.217  -28.403 1.00 40.92 ? 18  GLU   H CG  1 
ATOM   9042  C  CD  . GLU   H  1 18  ? 28.830  -81.424  -29.636 1.00 48.11 ? 18  GLU   H CD  1 
ATOM   9043  O  OE1 . GLU   H  1 18  ? 29.138  -80.754  -30.644 1.00 46.29 ? 18  GLU   H OE1 1 
ATOM   9044  O  OE2 . GLU   H  1 18  ? 27.873  -82.242  -29.600 1.00 45.47 ? 18  GLU   H OE2 1 
ATOM   9045  N  N   . LEU   H  1 19  ? 34.054  -79.800  -28.705 1.00 29.19 ? 19  LEU   H N   1 
ATOM   9046  C  CA  . LEU   H  1 19  ? 35.138  -78.838  -28.916 1.00 33.50 ? 19  LEU   H CA  1 
ATOM   9047  C  C   . LEU   H  1 19  ? 36.077  -79.299  -30.012 1.00 38.14 ? 19  LEU   H C   1 
ATOM   9048  O  O   . LEU   H  1 19  ? 36.596  -78.483  -30.796 1.00 30.32 ? 19  LEU   H O   1 
ATOM   9049  C  CB  . LEU   H  1 19  ? 35.936  -78.622  -27.630 1.00 37.74 ? 19  LEU   H CB  1 
ATOM   9050  C  CG  . LEU   H  1 19  ? 35.109  -78.162  -26.436 1.00 47.61 ? 19  LEU   H CG  1 
ATOM   9051  C  CD1 . LEU   H  1 19  ? 35.981  -78.122  -25.180 1.00 42.50 ? 19  LEU   H CD1 1 
ATOM   9052  C  CD2 . LEU   H  1 19  ? 34.476  -76.808  -26.736 1.00 38.99 ? 19  LEU   H CD2 1 
ATOM   9053  N  N   . ILE   H  1 20  ? 36.331  -80.601  -30.071 1.00 34.75 ? 20  ILE   H N   1 
ATOM   9054  C  CA  . ILE   H  1 20  ? 37.129  -81.121  -31.172 1.00 35.54 ? 20  ILE   H CA  1 
ATOM   9055  C  C   . ILE   H  1 20  ? 36.372  -80.940  -32.483 1.00 29.17 ? 20  ILE   H C   1 
ATOM   9056  O  O   . ILE   H  1 20  ? 36.927  -80.496  -33.488 1.00 32.16 ? 20  ILE   H O   1 
ATOM   9057  C  CB  . ILE   H  1 20  ? 37.484  -82.599  -30.932 1.00 29.97 ? 20  ILE   H CB  1 
ATOM   9058  C  CG1 . ILE   H  1 20  ? 38.359  -82.781  -29.688 1.00 34.25 ? 20  ILE   H CG1 1 
ATOM   9059  C  CG2 . ILE   H  1 20  ? 38.217  -83.166  -32.148 1.00 36.63 ? 20  ILE   H CG2 1 
ATOM   9060  C  CD1 . ILE   H  1 20  ? 38.262  -84.194  -29.156 1.00 37.30 ? 20  ILE   H CD1 1 
ATOM   9061  N  N   . ALA   H  1 21  ? 35.101  -81.324  -32.499 1.00 27.97 ? 21  ALA   H N   1 
ATOM   9062  C  CA  . ALA   H  1 21  ? 34.338  -81.225  -33.734 1.00 33.57 ? 21  ALA   H CA  1 
ATOM   9063  C  C   . ALA   H  1 21  ? 34.334  -79.793  -34.260 1.00 33.44 ? 21  ALA   H C   1 
ATOM   9064  O  O   . ALA   H  1 21  ? 34.477  -79.563  -35.467 1.00 31.20 ? 21  ALA   H O   1 
ATOM   9065  C  CB  . ALA   H  1 21  ? 32.922  -81.728  -33.499 1.00 29.49 ? 21  ALA   H CB  1 
ATOM   9066  N  N   . ILE   H  1 22  ? 34.204  -78.817  -33.363 1.00 35.37 ? 22  ILE   H N   1 
ATOM   9067  C  CA  . ILE   H  1 22  ? 34.112  -77.421  -33.774 1.00 32.56 ? 22  ILE   H CA  1 
ATOM   9068  C  C   . ILE   H  1 22  ? 35.358  -77.015  -34.539 1.00 37.18 ? 22  ILE   H C   1 
ATOM   9069  O  O   . ILE   H  1 22  ? 35.276  -76.427  -35.625 1.00 31.53 ? 22  ILE   H O   1 
ATOM   9070  C  CB  . ILE   H  1 22  ? 33.901  -76.520  -32.547 1.00 28.64 ? 22  ILE   H CB  1 
ATOM   9071  C  CG1 . ILE   H  1 22  ? 32.460  -76.648  -32.026 1.00 28.52 ? 22  ILE   H CG1 1 
ATOM   9072  C  CG2 . ILE   H  1 22  ? 34.223  -75.098  -32.885 1.00 25.15 ? 22  ILE   H CG2 1 
ATOM   9073  C  CD1 . ILE   H  1 22  ? 32.311  -76.162  -30.590 1.00 34.59 ? 22  ILE   H CD1 1 
ATOM   9074  N  N   . ASN   H  1 23  ? 36.530  -77.270  -33.945 1.00 30.64 ? 23  ASN   H N   1 
ATOM   9075  C  CA  . ASN   H  1 23  ? 37.792  -76.886  -34.560 1.00 29.43 ? 23  ASN   H CA  1 
ATOM   9076  C  C   . ASN   H  1 23  ? 38.062  -77.723  -35.800 1.00 30.53 ? 23  ASN   H C   1 
ATOM   9077  O  O   . ASN   H  1 23  ? 38.546  -77.209  -36.808 1.00 30.66 ? 23  ASN   H O   1 
ATOM   9078  C  CB  . ASN   H  1 23  ? 38.939  -77.020  -33.557 1.00 27.58 ? 23  ASN   H CB  1 
ATOM   9079  C  CG  . ASN   H  1 23  ? 38.892  -75.973  -32.458 1.00 36.55 ? 23  ASN   H CG  1 
ATOM   9080  O  OD1 . ASN   H  1 23  ? 37.906  -75.254  -32.299 1.00 38.70 ? 23  ASN   H OD1 1 
ATOM   9081  N  ND2 . ASN   H  1 23  ? 39.971  -75.882  -31.689 1.00 37.49 ? 23  ASN   H ND2 1 
ATOM   9082  N  N   . GLN   H  1 24  ? 37.733  -79.007  -35.751 1.00 29.84 ? 24  GLN   H N   1 
ATOM   9083  C  CA  . GLN   H  1 24  ? 37.996  -79.871  -36.893 1.00 36.64 ? 24  GLN   H CA  1 
ATOM   9084  C  C   . GLN   H  1 24  ? 37.130  -79.480  -38.084 1.00 36.87 ? 24  GLN   H C   1 
ATOM   9085  O  O   . GLN   H  1 24  ? 37.629  -79.324  -39.204 1.00 33.61 ? 24  GLN   H O   1 
ATOM   9086  C  CB  . GLN   H  1 24  ? 37.745  -81.318  -36.502 1.00 31.62 ? 24  GLN   H CB  1 
ATOM   9087  C  CG  . GLN   H  1 24  ? 37.839  -82.305  -37.660 1.00 36.41 ? 24  GLN   H CG  1 
ATOM   9088  C  CD  . GLN   H  1 24  ? 37.747  -83.730  -37.169 1.00 36.23 ? 24  GLN   H CD  1 
ATOM   9089  O  OE1 . GLN   H  1 24  ? 38.349  -84.083  -36.140 1.00 37.82 ? 24  GLN   H OE1 1 
ATOM   9090  N  NE2 . GLN   H  1 24  ? 36.954  -84.541  -37.854 1.00 40.69 ? 24  GLN   H NE2 1 
ATOM   9091  N  N   . TYR   H  1 25  ? 35.829  -79.318  -37.858 1.00 32.51 ? 25  TYR   H N   1 
ATOM   9092  C  CA  . TYR   H  1 25  ? 34.959  -78.905  -38.950 1.00 33.29 ? 25  TYR   H CA  1 
ATOM   9093  C  C   . TYR   H  1 25  ? 35.301  -77.499  -39.410 1.00 29.64 ? 25  TYR   H C   1 
ATOM   9094  O  O   . TYR   H  1 25  ? 35.223  -77.198  -40.607 1.00 32.64 ? 25  TYR   H O   1 
ATOM   9095  C  CB  . TYR   H  1 25  ? 33.496  -78.980  -38.540 1.00 29.47 ? 25  TYR   H CB  1 
ATOM   9096  C  CG  . TYR   H  1 25  ? 33.052  -80.339  -38.097 1.00 33.88 ? 25  TYR   H CG  1 
ATOM   9097  C  CD1 . TYR   H  1 25  ? 33.859  -81.468  -38.291 1.00 43.29 ? 25  TYR   H CD1 1 
ATOM   9098  C  CD2 . TYR   H  1 25  ? 31.839  -80.507  -37.462 1.00 26.98 ? 25  TYR   H CD2 1 
ATOM   9099  C  CE1 . TYR   H  1 25  ? 33.448  -82.717  -37.859 1.00 40.31 ? 25  TYR   H CE1 1 
ATOM   9100  C  CE2 . TYR   H  1 25  ? 31.420  -81.732  -37.023 1.00 36.84 ? 25  TYR   H CE2 1 
ATOM   9101  C  CZ  . TYR   H  1 25  ? 32.230  -82.841  -37.216 1.00 43.02 ? 25  TYR   H CZ  1 
ATOM   9102  O  OH  . TYR   H  1 25  ? 31.802  -84.071  -36.777 1.00 46.90 ? 25  TYR   H OH  1 
ATOM   9103  N  N   . PHE   H  1 26  ? 35.647  -76.607  -38.480 1.00 30.93 ? 26  PHE   H N   1 
ATOM   9104  C  CA  . PHE   H  1 26  ? 35.939  -75.252  -38.912 1.00 28.75 ? 26  PHE   H CA  1 
ATOM   9105  C  C   . PHE   H  1 26  ? 37.186  -75.233  -39.791 1.00 36.12 ? 26  PHE   H C   1 
ATOM   9106  O  O   . PHE   H  1 26  ? 37.216  -74.567  -40.841 1.00 29.24 ? 26  PHE   H O   1 
ATOM   9107  C  CB  . PHE   H  1 26  ? 36.084  -74.293  -37.728 1.00 24.82 ? 26  PHE   H CB  1 
ATOM   9108  C  CG  . PHE   H  1 26  ? 35.858  -72.853  -38.126 1.00 33.07 ? 26  PHE   H CG  1 
ATOM   9109  C  CD1 . PHE   H  1 26  ? 36.886  -72.078  -38.641 1.00 30.62 ? 26  PHE   H CD1 1 
ATOM   9110  C  CD2 . PHE   H  1 26  ? 34.581  -72.307  -38.061 1.00 31.00 ? 26  PHE   H CD2 1 
ATOM   9111  C  CE1 . PHE   H  1 26  ? 36.652  -70.761  -39.071 1.00 34.07 ? 26  PHE   H CE1 1 
ATOM   9112  C  CE2 . PHE   H  1 26  ? 34.320  -71.007  -38.489 1.00 32.99 ? 26  PHE   H CE2 1 
ATOM   9113  C  CZ  . PHE   H  1 26  ? 35.354  -70.223  -38.990 1.00 32.80 ? 26  PHE   H CZ  1 
ATOM   9114  N  N   . LEU   H  1 27  ? 38.215  -75.993  -39.417 1.00 30.87 ? 27  LEU   H N   1 
ATOM   9115  C  CA  . LEU   H  1 27  ? 39.427  -75.949  -40.232 1.00 31.13 ? 27  LEU   H CA  1 
ATOM   9116  C  C   . LEU   H  1 27  ? 39.188  -76.617  -41.580 1.00 28.02 ? 27  LEU   H C   1 
ATOM   9117  O  O   . LEU   H  1 27  ? 39.691  -76.147  -42.611 1.00 31.86 ? 27  LEU   H O   1 
ATOM   9118  C  CB  . LEU   H  1 27  ? 40.616  -76.575  -39.480 1.00 30.04 ? 27  LEU   H CB  1 
ATOM   9119  C  CG  . LEU   H  1 27  ? 41.938  -76.669  -40.247 1.00 30.20 ? 27  LEU   H CG  1 
ATOM   9120  C  CD1 . LEU   H  1 27  ? 42.470  -75.310  -40.611 1.00 29.55 ? 27  LEU   H CD1 1 
ATOM   9121  C  CD2 . LEU   H  1 27  ? 42.988  -77.415  -39.400 1.00 36.19 ? 27  LEU   H CD2 1 
ATOM   9122  N  N   . HIS   H  1 28  ? 38.405  -77.692  -41.605 1.00 26.20 ? 28  HIS   H N   1 
ATOM   9123  C  CA  . HIS   H  1 28  ? 38.087  -78.319  -42.881 1.00 32.73 ? 28  HIS   H CA  1 
ATOM   9124  C  C   . HIS   H  1 28  ? 37.312  -77.352  -43.776 1.00 38.71 ? 28  HIS   H C   1 
ATOM   9125  O  O   . HIS   H  1 28  ? 37.612  -77.228  -44.968 1.00 29.70 ? 28  HIS   H O   1 
ATOM   9126  C  CB  . HIS   H  1 28  ? 37.284  -79.594  -42.663 1.00 35.59 ? 28  HIS   H CB  1 
ATOM   9127  C  CG  . HIS   H  1 28  ? 38.100  -80.770  -42.205 1.00 37.04 ? 28  HIS   H CG  1 
ATOM   9128  N  ND1 . HIS   H  1 28  ? 37.517  -81.924  -41.729 1.00 32.63 ? 28  HIS   H ND1 1 
ATOM   9129  C  CD2 . HIS   H  1 28  ? 39.436  -80.990  -42.189 1.00 36.34 ? 28  HIS   H CD2 1 
ATOM   9130  C  CE1 . HIS   H  1 28  ? 38.458  -82.799  -41.422 1.00 34.39 ? 28  HIS   H CE1 1 
ATOM   9131  N  NE2 . HIS   H  1 28  ? 39.633  -82.257  -41.688 1.00 38.52 ? 28  HIS   H NE2 1 
ATOM   9132  N  N   . SER   H  1 29  ? 36.317  -76.653  -43.215 1.00 28.89 ? 29  SER   H N   1 
ATOM   9133  C  CA  . SER   H  1 29  ? 35.595  -75.637  -43.981 1.00 26.13 ? 29  SER   H CA  1 
ATOM   9134  C  C   . SER   H  1 29  ? 36.558  -74.671  -44.644 1.00 22.77 ? 29  SER   H C   1 
ATOM   9135  O  O   . SER   H  1 29  ? 36.479  -74.418  -45.855 1.00 32.19 ? 29  SER   H O   1 
ATOM   9136  C  CB  . SER   H  1 29  ? 34.627  -74.865  -43.077 1.00 31.97 ? 29  SER   H CB  1 
ATOM   9137  O  OG  . SER   H  1 29  ? 34.184  -73.675  -43.717 1.00 30.23 ? 29  SER   H OG  1 
ATOM   9138  N  N   . ARG   H  1 30  ? 37.503  -74.146  -43.875 1.00 23.68 ? 30  ARG   H N   1 
ATOM   9139  C  CA  . ARG   H  1 30  ? 38.383  -73.129  -44.414 1.00 25.49 ? 30  ARG   H CA  1 
ATOM   9140  C  C   . ARG   H  1 30  ? 39.402  -73.704  -45.392 1.00 33.97 ? 30  ARG   H C   1 
ATOM   9141  O  O   . ARG   H  1 30  ? 39.850  -72.989  -46.291 1.00 28.76 ? 30  ARG   H O   1 
ATOM   9142  C  CB  . ARG   H  1 30  ? 39.067  -72.390  -43.289 1.00 29.25 ? 30  ARG   H CB  1 
ATOM   9143  C  CG  . ARG   H  1 30  ? 38.262  -71.157  -42.799 1.00 36.94 ? 30  ARG   H CG  1 
ATOM   9144  C  CD  . ARG   H  1 30  ? 36.738  -71.404  -42.793 1.00 33.02 ? 30  ARG   H CD  1 
ATOM   9145  N  NE  . ARG   H  1 30  ? 36.019  -70.159  -42.575 1.00 35.58 ? 30  ARG   H NE  1 
ATOM   9146  C  CZ  . ARG   H  1 30  ? 34.772  -69.946  -42.961 1.00 31.11 ? 30  ARG   H CZ  1 
ATOM   9147  N  NH1 . ARG   H  1 30  ? 34.075  -70.880  -43.587 1.00 31.87 ? 30  ARG   H NH1 1 
ATOM   9148  N  NH2 . ARG   H  1 30  ? 34.215  -68.764  -42.713 1.00 33.47 ? 30  ARG   H NH2 1 
ATOM   9149  N  N   . MET   H  1 31  ? 39.739  -74.989  -45.268 1.00 27.31 ? 31  MET   H N   1 
ATOM   9150  C  CA  . MET   H  1 31  ? 40.624  -75.614  -46.247 1.00 31.85 ? 31  MET   H CA  1 
ATOM   9151  C  C   . MET   H  1 31  ? 39.894  -75.790  -47.575 1.00 29.58 ? 31  MET   H C   1 
ATOM   9152  O  O   . MET   H  1 31  ? 40.427  -75.489  -48.650 1.00 36.02 ? 31  MET   H O   1 
ATOM   9153  C  CB  . MET   H  1 31  ? 41.110  -76.970  -45.715 1.00 28.49 ? 31  MET   H CB  1 
ATOM   9154  C  CG  . MET   H  1 31  ? 42.135  -76.923  -44.544 1.00 30.91 ? 31  MET   H CG  1 
ATOM   9155  S  SD  . MET   H  1 31  ? 42.211  -78.530  -43.676 1.00 34.28 ? 31  MET   H SD  1 
ATOM   9156  C  CE  . MET   H  1 31  ? 42.808  -79.548  -45.029 1.00 39.31 ? 31  MET   H CE  1 
ATOM   9157  N  N   . TRP   H  1 32  ? 38.662  -76.275  -47.513 1.00 27.84 ? 32  TRP   H N   1 
ATOM   9158  C  CA  . TRP   H  1 32  ? 37.868  -76.410  -48.722 1.00 30.99 ? 32  TRP   H CA  1 
ATOM   9159  C  C   . TRP   H  1 32  ? 37.685  -75.065  -49.419 1.00 33.46 ? 32  TRP   H C   1 
ATOM   9160  O  O   . TRP   H  1 32  ? 37.826  -74.966  -50.648 1.00 28.14 ? 32  TRP   H O   1 
ATOM   9161  C  CB  . TRP   H  1 32  ? 36.545  -77.057  -48.367 1.00 31.91 ? 32  TRP   H CB  1 
ATOM   9162  C  CG  . TRP   H  1 32  ? 36.602  -78.567  -48.405 1.00 37.93 ? 32  TRP   H CG  1 
ATOM   9163  C  CD1 . TRP   H  1 32  ? 37.254  -79.335  -49.321 1.00 41.37 ? 32  TRP   H CD1 1 
ATOM   9164  C  CD2 . TRP   H  1 32  ? 35.988  -79.482  -47.485 1.00 36.57 ? 32  TRP   H CD2 1 
ATOM   9165  N  NE1 . TRP   H  1 32  ? 37.076  -80.667  -49.040 1.00 33.75 ? 32  TRP   H NE1 1 
ATOM   9166  C  CE2 . TRP   H  1 32  ? 36.307  -80.787  -47.917 1.00 36.74 ? 32  TRP   H CE2 1 
ATOM   9167  C  CE3 . TRP   H  1 32  ? 35.204  -79.325  -46.335 1.00 37.28 ? 32  TRP   H CE3 1 
ATOM   9168  C  CZ2 . TRP   H  1 32  ? 35.863  -81.931  -47.245 1.00 34.62 ? 32  TRP   H CZ2 1 
ATOM   9169  C  CZ3 . TRP   H  1 32  ? 34.762  -80.448  -45.672 1.00 36.30 ? 32  TRP   H CZ3 1 
ATOM   9170  C  CH2 . TRP   H  1 32  ? 35.098  -81.740  -46.122 1.00 46.78 ? 32  TRP   H CH2 1 
ATOM   9171  N  N   . ASN   H  1 33  ? 37.368  -74.010  -48.660 1.00 34.43 ? 33  ASN   H N   1 
ATOM   9172  C  CA  . ASN   H  1 33  ? 37.226  -72.701  -49.289 1.00 35.65 ? 33  ASN   H CA  1 
ATOM   9173  C  C   . ASN   H  1 33  ? 38.517  -72.280  -49.969 1.00 37.35 ? 33  ASN   H C   1 
ATOM   9174  O  O   . ASN   H  1 33  ? 38.502  -71.762  -51.093 1.00 31.12 ? 33  ASN   H O   1 
ATOM   9175  C  CB  . ASN   H  1 33  ? 36.817  -71.652  -48.265 1.00 32.67 ? 33  ASN   H CB  1 
ATOM   9176  C  CG  . ASN   H  1 33  ? 35.339  -71.727  -47.897 1.00 33.32 ? 33  ASN   H CG  1 
ATOM   9177  O  OD1 . ASN   H  1 33  ? 34.512  -72.329  -48.591 1.00 30.64 ? 33  ASN   H OD1 1 
ATOM   9178  N  ND2 . ASN   H  1 33  ? 35.008  -71.099  -46.791 1.00 31.36 ? 33  ASN   H ND2 1 
ATOM   9179  N  N   . ASP   H  1 34  ? 39.649  -72.474  -49.287 1.00 33.39 ? 34  ASP   H N   1 
ATOM   9180  C  CA  . ASP   H  1 34  ? 40.939  -72.142  -49.875 1.00 35.60 ? 34  ASP   H CA  1 
ATOM   9181  C  C   . ASP   H  1 34  ? 41.207  -72.939  -51.150 1.00 31.08 ? 34  ASP   H C   1 
ATOM   9182  O  O   . ASP   H  1 34  ? 41.854  -72.430  -52.069 1.00 33.37 ? 34  ASP   H O   1 
ATOM   9183  C  CB  . ASP   H  1 34  ? 42.031  -72.380  -48.834 1.00 34.37 ? 34  ASP   H CB  1 
ATOM   9184  C  CG  . ASP   H  1 34  ? 43.421  -72.149  -49.372 1.00 37.81 ? 34  ASP   H CG  1 
ATOM   9185  O  OD1 . ASP   H  1 34  ? 43.717  -71.052  -49.903 1.00 42.85 ? 34  ASP   H OD1 1 
ATOM   9186  O  OD2 . ASP   H  1 34  ? 44.230  -73.074  -49.217 1.00 40.35 ? 34  ASP   H OD2 1 
ATOM   9187  N  N   . TRP   H  1 35  ? 40.723  -74.173  -51.229 1.00 31.41 ? 35  TRP   H N   1 
ATOM   9188  C  CA  . TRP   H  1 35  ? 40.918  -74.984  -52.426 1.00 35.57 ? 35  TRP   H CA  1 
ATOM   9189  C  C   . TRP   H  1 35  ? 39.896  -74.690  -53.518 1.00 37.35 ? 35  TRP   H C   1 
ATOM   9190  O  O   . TRP   H  1 35  ? 39.955  -75.331  -54.567 1.00 34.23 ? 35  TRP   H O   1 
ATOM   9191  C  CB  . TRP   H  1 35  ? 40.854  -76.480  -52.083 1.00 30.74 ? 35  TRP   H CB  1 
ATOM   9192  C  CG  . TRP   H  1 35  ? 41.898  -76.945  -51.076 1.00 36.73 ? 35  TRP   H CG  1 
ATOM   9193  C  CD1 . TRP   H  1 35  ? 43.030  -76.279  -50.684 1.00 37.58 ? 35  TRP   H CD1 1 
ATOM   9194  C  CD2 . TRP   H  1 35  ? 41.873  -78.170  -50.329 1.00 40.39 ? 35  TRP   H CD2 1 
ATOM   9195  N  NE1 . TRP   H  1 35  ? 43.720  -77.030  -49.737 1.00 39.37 ? 35  TRP   H NE1 1 
ATOM   9196  C  CE2 . TRP   H  1 35  ? 43.028  -78.194  -49.514 1.00 39.80 ? 35  TRP   H CE2 1 
ATOM   9197  C  CE3 . TRP   H  1 35  ? 40.996  -79.258  -50.286 1.00 39.14 ? 35  TRP   H CE3 1 
ATOM   9198  C  CZ2 . TRP   H  1 35  ? 43.310  -79.255  -48.658 1.00 43.38 ? 35  TRP   H CZ2 1 
ATOM   9199  C  CZ3 . TRP   H  1 35  ? 41.287  -80.315  -49.426 1.00 39.32 ? 35  TRP   H CZ3 1 
ATOM   9200  C  CH2 . TRP   H  1 35  ? 42.430  -80.302  -48.633 1.00 35.48 ? 35  TRP   H CH2 1 
ATOM   9201  N  N   . GLY   H  1 36  ? 38.952  -73.773  -53.286 1.00 33.77 ? 36  GLY   H N   1 
ATOM   9202  C  CA  . GLY   H  1 36  ? 37.921  -73.475  -54.251 1.00 34.04 ? 36  GLY   H CA  1 
ATOM   9203  C  C   . GLY   H  1 36  ? 36.779  -74.449  -54.253 1.00 36.82 ? 36  GLY   H C   1 
ATOM   9204  O  O   . GLY   H  1 36  ? 35.978  -74.446  -55.191 1.00 34.44 ? 36  GLY   H O   1 
ATOM   9205  N  N   . LEU   H  1 37  ? 36.668  -75.291  -53.233 1.00 34.13 ? 37  LEU   H N   1 
ATOM   9206  C  CA  . LEU   H  1 37  ? 35.509  -76.155  -53.092 1.00 29.11 ? 37  LEU   H CA  1 
ATOM   9207  C  C   . LEU   H  1 37  ? 34.492  -75.491  -52.152 1.00 40.32 ? 37  LEU   H C   1 
ATOM   9208  O  O   . LEU   H  1 37  ? 34.225  -75.941  -51.030 1.00 30.81 ? 37  LEU   H O   1 
ATOM   9209  C  CB  . LEU   H  1 37  ? 35.945  -77.540  -52.621 1.00 35.14 ? 37  LEU   H CB  1 
ATOM   9210  C  CG  . LEU   H  1 37  ? 36.971  -78.113  -53.629 1.00 38.19 ? 37  LEU   H CG  1 
ATOM   9211  C  CD1 . LEU   H  1 37  ? 37.729  -79.287  -53.038 1.00 39.54 ? 37  LEU   H CD1 1 
ATOM   9212  C  CD2 . LEU   H  1 37  ? 36.263  -78.498  -54.913 1.00 34.01 ? 37  LEU   H CD2 1 
ATOM   9213  N  N   . LYS   H  1 38  ? 33.886  -74.406  -52.666 1.00 35.62 ? 38  LYS   H N   1 
ATOM   9214  C  CA  . LYS   H  1 38  ? 33.118  -73.496  -51.810 1.00 37.04 ? 38  LYS   H CA  1 
ATOM   9215  C  C   . LYS   H  1 38  ? 31.840  -74.131  -51.285 1.00 32.51 ? 38  LYS   H C   1 
ATOM   9216  O  O   . LYS   H  1 38  ? 31.353  -73.732  -50.222 1.00 36.02 ? 38  LYS   H O   1 
ATOM   9217  C  CB  . LYS   H  1 38  ? 32.792  -72.206  -52.566 1.00 37.71 ? 38  LYS   H CB  1 
ATOM   9218  C  CG  . LYS   H  1 38  ? 34.036  -71.425  -53.025 1.00 41.79 ? 38  LYS   H CG  1 
ATOM   9219  C  CD  . LYS   H  1 38  ? 34.728  -70.719  -51.895 1.00 46.99 ? 38  LYS   H CD  1 
ATOM   9220  C  CE  . LYS   H  1 38  ? 36.090  -70.144  -52.316 1.00 46.82 ? 38  LYS   H CE  1 
ATOM   9221  N  NZ  . LYS   H  1 38  ? 36.075  -68.667  -52.491 1.00 52.07 ? 38  LYS   H NZ  1 
ATOM   9222  N  N   . ARG   H  1 39  ? 31.252  -75.090  -52.007 1.00 31.38 ? 39  ARG   H N   1 
ATOM   9223  C  CA  . ARG   H  1 39  ? 30.033  -75.706  -51.509 1.00 33.67 ? 39  ARG   H CA  1 
ATOM   9224  C  C   . ARG   H  1 39  ? 30.318  -76.622  -50.321 1.00 33.11 ? 39  ARG   H C   1 
ATOM   9225  O  O   . ARG   H  1 39  ? 29.544  -76.656  -49.358 1.00 31.17 ? 39  ARG   H O   1 
ATOM   9226  C  CB  . ARG   H  1 39  ? 29.353  -76.477  -52.631 1.00 34.46 ? 39  ARG   H CB  1 
ATOM   9227  C  CG  . ARG   H  1 39  ? 27.897  -76.724  -52.412 1.00 47.79 ? 39  ARG   H CG  1 
ATOM   9228  C  CD  . ARG   H  1 39  ? 27.423  -77.892  -53.286 1.00 57.48 ? 39  ARG   H CD  1 
ATOM   9229  N  NE  . ARG   H  1 39  ? 25.982  -78.105  -53.208 1.00 58.55 ? 39  ARG   H NE  1 
ATOM   9230  C  CZ  . ARG   H  1 39  ? 25.098  -77.538  -54.019 1.00 58.33 ? 39  ARG   H CZ  1 
ATOM   9231  N  NH1 . ARG   H  1 39  ? 25.470  -76.706  -54.980 1.00 59.16 ? 39  ARG   H NH1 1 
ATOM   9232  N  NH2 . ARG   H  1 39  ? 23.812  -77.814  -53.862 1.00 58.11 ? 39  ARG   H NH2 1 
ATOM   9233  N  N   . LEU   H  1 40  ? 31.413  -77.382  -50.378 1.00 31.02 ? 40  LEU   H N   1 
ATOM   9234  C  CA  . LEU   H  1 40  ? 31.846  -78.125  -49.193 1.00 31.50 ? 40  LEU   H CA  1 
ATOM   9235  C  C   . LEU   H  1 40  ? 32.220  -77.173  -48.076 1.00 25.90 ? 40  LEU   H C   1 
ATOM   9236  O  O   . LEU   H  1 40  ? 31.868  -77.400  -46.919 1.00 33.24 ? 40  LEU   H O   1 
ATOM   9237  C  CB  . LEU   H  1 40  ? 33.038  -79.036  -49.504 1.00 30.59 ? 40  LEU   H CB  1 
ATOM   9238  C  CG  . LEU   H  1 40  ? 32.676  -80.306  -50.250 1.00 35.16 ? 40  LEU   H CG  1 
ATOM   9239  C  CD1 . LEU   H  1 40  ? 33.935  -80.811  -50.957 1.00 34.51 ? 40  LEU   H CD1 1 
ATOM   9240  C  CD2 . LEU   H  1 40  ? 32.083  -81.335  -49.302 1.00 39.15 ? 40  LEU   H CD2 1 
ATOM   9241  N  N   . GLY   H  1 41  ? 32.888  -76.077  -48.406 1.00 25.28 ? 41  GLY   H N   1 
ATOM   9242  C  CA  . GLY   H  1 41  ? 33.325  -75.165  -47.362 1.00 31.09 ? 41  GLY   H CA  1 
ATOM   9243  C  C   . GLY   H  1 41  ? 32.156  -74.582  -46.592 1.00 35.14 ? 41  GLY   H C   1 
ATOM   9244  O  O   . GLY   H  1 41  ? 32.220  -74.444  -45.366 1.00 32.94 ? 41  GLY   H O   1 
ATOM   9245  N  N   . ALA   H  1 42  ? 31.065  -74.247  -47.307 1.00 31.41 ? 42  ALA   H N   1 
ATOM   9246  C  CA  . ALA   H  1 42  ? 29.879  -73.668  -46.684 1.00 31.61 ? 42  ALA   H CA  1 
ATOM   9247  C  C   . ALA   H  1 42  ? 29.147  -74.707  -45.853 1.00 31.28 ? 42  ALA   H C   1 
ATOM   9248  O  O   . ALA   H  1 42  ? 28.719  -74.436  -44.724 1.00 29.60 ? 42  ALA   H O   1 
ATOM   9249  C  CB  . ALA   H  1 42  ? 28.934  -73.101  -47.764 1.00 31.35 ? 42  ALA   H CB  1 
ATOM   9250  N  N   . HIS   H  1 43  ? 28.962  -75.900  -46.411 1.00 28.85 ? 43  HIS   H N   1 
ATOM   9251  C  CA  . HIS   H  1 43  ? 28.266  -76.931  -45.666 1.00 26.83 ? 43  HIS   H CA  1 
ATOM   9252  C  C   . HIS   H  1 43  ? 29.022  -77.260  -44.385 1.00 32.69 ? 43  HIS   H C   1 
ATOM   9253  O  O   . HIS   H  1 43  ? 28.407  -77.424  -43.316 1.00 31.08 ? 43  HIS   H O   1 
ATOM   9254  C  CB  . HIS   H  1 43  ? 28.075  -78.172  -46.519 1.00 29.24 ? 43  HIS   H CB  1 
ATOM   9255  C  CG  . HIS   H  1 43  ? 27.170  -79.172  -45.905 1.00 34.49 ? 43  HIS   H CG  1 
ATOM   9256  N  ND1 . HIS   H  1 43  ? 25.851  -79.299  -46.274 1.00 39.82 ? 43  HIS   H ND1 1 
ATOM   9257  C  CD2 . HIS   H  1 43  ? 27.375  -80.070  -44.915 1.00 43.11 ? 43  HIS   H CD2 1 
ATOM   9258  C  CE1 . HIS   H  1 43  ? 25.284  -80.243  -45.549 1.00 38.32 ? 43  HIS   H CE1 1 
ATOM   9259  N  NE2 . HIS   H  1 43  ? 26.188  -80.728  -44.718 1.00 37.53 ? 43  HIS   H NE2 1 
ATOM   9260  N  N   . GLU   H  1 44  ? 30.359  -77.332  -44.470 1.00 28.61 ? 44  GLU   H N   1 
ATOM   9261  C  CA  . GLU   H  1 44  ? 31.164  -77.699  -43.300 1.00 31.22 ? 44  GLU   H CA  1 
ATOM   9262  C  C   . GLU   H  1 44  ? 31.131  -76.594  -42.246 1.00 34.54 ? 44  GLU   H C   1 
ATOM   9263  O  O   . GLU   H  1 44  ? 31.089  -76.868  -41.035 1.00 30.19 ? 44  GLU   H O   1 
ATOM   9264  C  CB  . GLU   H  1 44  ? 32.606  -77.993  -43.735 1.00 33.66 ? 44  GLU   H CB  1 
ATOM   9265  C  CG  . GLU   H  1 44  ? 33.504  -78.632  -42.675 1.00 35.50 ? 44  GLU   H CG  1 
ATOM   9266  C  CD  . GLU   H  1 44  ? 33.236  -80.104  -42.431 1.00 38.42 ? 44  GLU   H CD  1 
ATOM   9267  O  OE1 . GLU   H  1 44  ? 32.186  -80.624  -42.861 1.00 38.33 ? 44  GLU   H OE1 1 
ATOM   9268  O  OE2 . GLU   H  1 44  ? 34.112  -80.759  -41.819 1.00 35.34 ? 44  GLU   H OE2 1 
ATOM   9269  N  N   . TYR   H  1 45  ? 31.128  -75.343  -42.686 1.00 30.29 ? 45  TYR   H N   1 
ATOM   9270  C  CA  . TYR   H  1 45  ? 30.955  -74.208  -41.787 1.00 35.76 ? 45  TYR   H CA  1 
ATOM   9271  C  C   . TYR   H  1 45  ? 29.629  -74.328  -41.007 1.00 40.31 ? 45  TYR   H C   1 
ATOM   9272  O  O   . TYR   H  1 45  ? 29.629  -74.225  -39.768 1.00 35.34 ? 45  TYR   H O   1 
ATOM   9273  C  CB  . TYR   H  1 45  ? 30.993  -72.912  -42.577 1.00 26.62 ? 45  TYR   H CB  1 
ATOM   9274  C  CG  . TYR   H  1 45  ? 30.578  -71.705  -41.806 1.00 29.93 ? 45  TYR   H CG  1 
ATOM   9275  C  CD1 . TYR   H  1 45  ? 31.501  -70.964  -41.078 1.00 34.31 ? 45  TYR   H CD1 1 
ATOM   9276  C  CD2 . TYR   H  1 45  ? 29.247  -71.288  -41.805 1.00 37.55 ? 45  TYR   H CD2 1 
ATOM   9277  C  CE1 . TYR   H  1 45  ? 31.106  -69.829  -40.358 1.00 34.16 ? 45  TYR   H CE1 1 
ATOM   9278  C  CE2 . TYR   H  1 45  ? 28.844  -70.155  -41.085 1.00 36.77 ? 45  TYR   H CE2 1 
ATOM   9279  C  CZ  . TYR   H  1 45  ? 29.774  -69.427  -40.387 1.00 39.27 ? 45  TYR   H CZ  1 
ATOM   9280  O  OH  . TYR   H  1 45  ? 29.362  -68.316  -39.683 1.00 39.30 ? 45  TYR   H OH  1 
ATOM   9281  N  N   . GLU   H  1 47  ? 27.853  -77.046  -40.260 1.00 29.43 ? 47  GLU   H N   1 
ATOM   9282  C  CA  . GLU   H  1 47  ? 28.223  -78.155  -39.345 1.00 37.99 ? 47  GLU   H CA  1 
ATOM   9283  C  C   . GLU   H  1 47  ? 29.030  -77.669  -38.123 1.00 27.32 ? 47  GLU   H C   1 
ATOM   9284  O  O   . GLU   H  1 47  ? 28.730  -78.020  -36.978 1.00 34.56 ? 47  GLU   H O   1 
ATOM   9285  C  CB  . GLU   H  1 47  ? 29.035  -79.246  -40.074 1.00 37.64 ? 47  GLU   H CB  1 
ATOM   9286  C  CG  . GLU   H  1 47  ? 28.354  -79.894  -41.296 1.00 41.85 ? 47  GLU   H CG  1 
ATOM   9287  C  CD  . GLU   H  1 47  ? 27.246  -80.869  -40.926 1.00 42.84 ? 47  GLU   H CD  1 
ATOM   9288  O  OE1 . GLU   H  1 47  ? 26.847  -80.883  -39.751 1.00 52.36 ? 47  GLU   H OE1 1 
ATOM   9289  O  OE2 . GLU   H  1 47  ? 26.765  -81.618  -41.812 1.00 50.48 ? 47  GLU   H OE2 1 
ATOM   9290  N  N   . SER   H  1 48  ? 30.054  -76.861  -38.350 1.00 27.14 ? 48  SER   H N   1 
ATOM   9291  C  CA  . SER   H  1 48  ? 30.816  -76.322  -37.228 1.00 28.15 ? 48  SER   H CA  1 
ATOM   9292  C  C   . SER   H  1 48  ? 29.922  -75.453  -36.341 1.00 35.02 ? 48  SER   H C   1 
ATOM   9293  O  O   . SER   H  1 48  ? 29.980  -75.532  -35.106 1.00 30.89 ? 48  SER   H O   1 
ATOM   9294  C  CB  . SER   H  1 48  ? 32.008  -75.516  -37.731 1.00 24.37 ? 48  SER   H CB  1 
ATOM   9295  O  OG  . SER   H  1 48  ? 32.863  -75.151  -36.639 1.00 30.25 ? 48  SER   H OG  1 
ATOM   9296  N  N   . ILE   H  1 49  ? 29.061  -74.646  -36.966 1.00 32.41 ? 49  ILE   H N   1 
ATOM   9297  C  CA  . ILE   H  1 49  ? 28.114  -73.827  -36.219 1.00 34.50 ? 49  ILE   H CA  1 
ATOM   9298  C  C   . ILE   H  1 49  ? 27.185  -74.716  -35.413 1.00 29.14 ? 49  ILE   H C   1 
ATOM   9299  O  O   . ILE   H  1 49  ? 26.909  -74.444  -34.237 1.00 32.27 ? 49  ILE   H O   1 
ATOM   9300  C  CB  . ILE   H  1 49  ? 27.321  -72.910  -37.182 1.00 32.50 ? 49  ILE   H CB  1 
ATOM   9301  C  CG1 . ILE   H  1 49  ? 28.233  -71.840  -37.785 1.00 31.15 ? 49  ILE   H CG1 1 
ATOM   9302  C  CG2 . ILE   H  1 49  ? 26.146  -72.252  -36.464 1.00 34.96 ? 49  ILE   H CG2 1 
ATOM   9303  C  CD1 . ILE   H  1 49  ? 28.701  -70.799  -36.819 1.00 38.47 ? 49  ILE   H CD1 1 
ATOM   9304  N  N   . ASP   H  1 50  ? 26.688  -75.796  -36.023 1.00 25.92 ? 50  ASP   H N   1 
ATOM   9305  C  CA  . ASP   H  1 50  ? 25.778  -76.674  -35.299 1.00 31.48 ? 50  ASP   H CA  1 
ATOM   9306  C  C   . ASP   H  1 50  ? 26.435  -77.239  -34.045 1.00 35.33 ? 50  ASP   H C   1 
ATOM   9307  O  O   . ASP   H  1 50  ? 25.770  -77.399  -33.016 1.00 30.02 ? 50  ASP   H O   1 
ATOM   9308  C  CB  . ASP   H  1 50  ? 25.290  -77.822  -36.178 1.00 33.20 ? 50  ASP   H CB  1 
ATOM   9309  C  CG  . ASP   H  1 50  ? 24.278  -77.373  -37.227 1.00 51.68 ? 50  ASP   H CG  1 
ATOM   9310  O  OD1 . ASP   H  1 50  ? 23.709  -76.268  -37.088 1.00 62.80 ? 50  ASP   H OD1 1 
ATOM   9311  O  OD2 . ASP   H  1 50  ? 24.057  -78.135  -38.191 1.00 55.27 ? 50  ASP   H OD2 1 
ATOM   9312  N  N   . GLU   H  1 51  ? 27.730  -77.589  -34.124 1.00 29.64 ? 51  GLU   H N   1 
ATOM   9313  C  CA  . GLU   H  1 51  ? 28.407  -78.131  -32.953 1.00 28.69 ? 51  GLU   H CA  1 
ATOM   9314  C  C   . GLU   H  1 51  ? 28.660  -77.041  -31.920 1.00 27.48 ? 51  GLU   H C   1 
ATOM   9315  O  O   . GLU   H  1 51  ? 28.654  -77.305  -30.712 1.00 29.38 ? 51  GLU   H O   1 
ATOM   9316  C  CB  . GLU   H  1 51  ? 29.736  -78.808  -33.363 1.00 35.34 ? 51  GLU   H CB  1 
ATOM   9317  C  CG  . GLU   H  1 51  ? 29.545  -79.981  -34.347 1.00 36.96 ? 51  GLU   H CG  1 
ATOM   9318  C  CD  . GLU   H  1 51  ? 28.650  -81.076  -33.782 1.00 42.49 ? 51  GLU   H CD  1 
ATOM   9319  O  OE1 . GLU   H  1 51  ? 28.981  -81.610  -32.720 1.00 50.43 ? 51  GLU   H OE1 1 
ATOM   9320  O  OE2 . GLU   H  1 51  ? 27.608  -81.402  -34.375 1.00 45.80 ? 51  GLU   H OE2 1 
ATOM   9321  N  N   . MET   H  1 52  ? 28.910  -75.819  -32.371 1.00 28.45 ? 52  MET   H N   1 
ATOM   9322  C  CA  . MET   H  1 52  ? 29.024  -74.705  -31.441 1.00 31.56 ? 52  MET   H CA  1 
ATOM   9323  C  C   . MET   H  1 52  ? 27.748  -74.544  -30.620 1.00 33.03 ? 52  MET   H C   1 
ATOM   9324  O  O   . MET   H  1 52  ? 27.801  -74.292  -29.409 1.00 31.24 ? 52  MET   H O   1 
ATOM   9325  C  CB  . MET   H  1 52  ? 29.318  -73.427  -32.210 1.00 32.41 ? 52  MET   H CB  1 
ATOM   9326  C  CG  . MET   H  1 52  ? 30.639  -73.380  -32.862 1.00 30.99 ? 52  MET   H CG  1 
ATOM   9327  S  SD  . MET   H  1 52  ? 30.855  -71.849  -33.779 1.00 29.82 ? 52  MET   H SD  1 
ATOM   9328  C  CE  . MET   H  1 52  ? 32.116  -72.305  -34.984 1.00 28.79 ? 52  MET   H CE  1 
ATOM   9329  N  N   . LYS   H  1 53  ? 26.589  -74.722  -31.262 1.00 28.44 ? 53  LYS   H N   1 
ATOM   9330  C  CA  . LYS   H  1 53  ? 25.307  -74.609  -30.556 1.00 31.58 ? 53  LYS   H CA  1 
ATOM   9331  C  C   . LYS   H  1 53  ? 25.096  -75.753  -29.570 1.00 37.86 ? 53  LYS   H C   1 
ATOM   9332  O  O   . LYS   H  1 53  ? 24.596  -75.535  -28.453 1.00 33.14 ? 53  LYS   H O   1 
ATOM   9333  C  CB  . LYS   H  1 53  ? 24.153  -74.580  -31.564 1.00 31.38 ? 53  LYS   H CB  1 
ATOM   9334  C  CG  . LYS   H  1 53  ? 24.177  -73.400  -32.538 1.00 35.02 ? 53  LYS   H CG  1 
ATOM   9335  C  CD  . LYS   H  1 53  ? 22.958  -73.494  -33.473 1.00 34.31 ? 53  LYS   H CD  1 
ATOM   9336  C  CE  . LYS   H  1 53  ? 22.677  -72.199  -34.190 1.00 52.05 ? 53  LYS   H CE  1 
ATOM   9337  N  NZ  . LYS   H  1 53  ? 21.413  -72.285  -34.997 1.00 59.45 ? 53  LYS   H NZ  1 
ATOM   9338  N  N   . HIS   H  1 54  ? 25.435  -76.985  -29.974 1.00 32.88 ? 54  HIS   H N   1 
ATOM   9339  C  CA  . HIS   H  1 54  ? 25.428  -78.107  -29.035 1.00 36.04 ? 54  HIS   H CA  1 
ATOM   9340  C  C   . HIS   H  1 54  ? 26.317  -77.830  -27.821 1.00 35.32 ? 54  HIS   H C   1 
ATOM   9341  O  O   . HIS   H  1 54  ? 25.931  -78.095  -26.674 1.00 33.65 ? 54  HIS   H O   1 
ATOM   9342  C  CB  . HIS   H  1 54  ? 25.898  -79.392  -29.722 1.00 31.80 ? 54  HIS   H CB  1 
ATOM   9343  C  CG  . HIS   H  1 54  ? 25.099  -79.784  -30.921 1.00 38.39 ? 54  HIS   H CG  1 
ATOM   9344  N  ND1 . HIS   H  1 54  ? 23.778  -79.427  -31.099 1.00 37.45 ? 54  HIS   H ND1 1 
ATOM   9345  C  CD2 . HIS   H  1 54  ? 25.440  -80.525  -32.004 1.00 38.59 ? 54  HIS   H CD2 1 
ATOM   9346  C  CE1 . HIS   H  1 54  ? 23.344  -79.923  -32.246 1.00 35.12 ? 54  HIS   H CE1 1 
ATOM   9347  N  NE2 . HIS   H  1 54  ? 24.331  -80.596  -32.811 1.00 32.30 ? 54  HIS   H NE2 1 
ATOM   9348  N  N   . ALA   H  1 55  ? 27.529  -77.332  -28.054 1.00 31.39 ? 55  ALA   H N   1 
ATOM   9349  C  CA  . ALA   H  1 55  ? 28.428  -77.059  -26.942 1.00 33.41 ? 55  ALA   H CA  1 
ATOM   9350  C  C   . ALA   H  1 55  ? 27.800  -76.063  -25.984 1.00 36.67 ? 55  ALA   H C   1 
ATOM   9351  O  O   . ALA   H  1 55  ? 27.805  -76.270  -24.768 1.00 30.95 ? 55  ALA   H O   1 
ATOM   9352  C  CB  . ALA   H  1 55  ? 29.765  -76.527  -27.440 1.00 33.83 ? 55  ALA   H CB  1 
ATOM   9353  N  N   . ASP   H  1 56  ? 27.263  -74.970  -26.525 1.00 31.32 ? 56  ASP   H N   1 
ATOM   9354  C  CA  . ASP   H  1 56  ? 26.594  -73.960  -25.706 1.00 30.49 ? 56  ASP   H CA  1 
ATOM   9355  C  C   . ASP   H  1 56  ? 25.544  -74.600  -24.785 1.00 27.73 ? 56  ASP   H C   1 
ATOM   9356  O  O   . ASP   H  1 56  ? 25.577  -74.411  -23.564 1.00 29.89 ? 56  ASP   H O   1 
ATOM   9357  C  CB  . ASP   H  1 56  ? 25.978  -72.906  -26.636 1.00 36.03 ? 56  ASP   H CB  1 
ATOM   9358  C  CG  . ASP   H  1 56  ? 25.325  -71.752  -25.894 1.00 35.41 ? 56  ASP   H CG  1 
ATOM   9359  O  OD1 . ASP   H  1 56  ? 25.652  -71.509  -24.710 1.00 29.94 ? 56  ASP   H OD1 1 
ATOM   9360  O  OD2 . ASP   H  1 56  ? 24.456  -71.098  -26.510 1.00 32.90 ? 56  ASP   H OD2 1 
ATOM   9361  N  N   . LYS   H  1 57  ? 24.667  -75.437  -25.329 1.00 27.73 ? 57  LYS   H N   1 
ATOM   9362  C  CA  . LYS   H  1 57  ? 23.644  -76.048  -24.486 1.00 28.92 ? 57  LYS   H CA  1 
ATOM   9363  C  C   . LYS   H  1 57  ? 24.262  -76.960  -23.417 1.00 35.66 ? 57  LYS   H C   1 
ATOM   9364  O  O   . LYS   H  1 57  ? 23.774  -77.011  -22.272 1.00 26.66 ? 57  LYS   H O   1 
ATOM   9365  C  CB  . LYS   H  1 57  ? 22.647  -76.825  -25.343 1.00 30.72 ? 57  LYS   H CB  1 
ATOM   9366  C  CG  . LYS   H  1 57  ? 21.716  -75.948  -26.266 1.00 34.31 ? 57  LYS   H CG  1 
ATOM   9367  N  N   . LEU   H  1 58  ? 25.318  -77.704  -23.771 1.00 35.50 ? 58  LEU   H N   1 
ATOM   9368  C  CA  . LEU   H  1 58  ? 25.998  -78.554  -22.788 1.00 31.66 ? 58  LEU   H CA  1 
ATOM   9369  C  C   . LEU   H  1 58  ? 26.590  -77.725  -21.657 1.00 28.11 ? 58  LEU   H C   1 
ATOM   9370  O  O   . LEU   H  1 58  ? 26.485  -78.081  -20.475 1.00 33.13 ? 58  LEU   H O   1 
ATOM   9371  C  CB  . LEU   H  1 58  ? 27.092  -79.368  -23.464 1.00 32.19 ? 58  LEU   H CB  1 
ATOM   9372  C  CG  . LEU   H  1 58  ? 26.628  -80.469  -24.413 1.00 34.87 ? 58  LEU   H CG  1 
ATOM   9373  C  CD1 . LEU   H  1 58  ? 27.822  -80.966  -25.252 1.00 34.52 ? 58  LEU   H CD1 1 
ATOM   9374  C  CD2 . LEU   H  1 58  ? 25.979  -81.610  -23.631 1.00 35.27 ? 58  LEU   H CD2 1 
ATOM   9375  N  N   . ILE   H  1 59  ? 27.258  -76.637  -22.012 1.00 24.32 ? 59  ILE   H N   1 
ATOM   9376  C  CA  . ILE   H  1 59  ? 27.812  -75.731  -21.022 1.00 30.27 ? 59  ILE   H CA  1 
ATOM   9377  C  C   . ILE   H  1 59  ? 26.718  -75.207  -20.115 1.00 34.72 ? 59  ILE   H C   1 
ATOM   9378  O  O   . ILE   H  1 59  ? 26.876  -75.155  -18.883 1.00 31.88 ? 59  ILE   H O   1 
ATOM   9379  C  CB  . ILE   H  1 59  ? 28.563  -74.588  -21.725 1.00 31.98 ? 59  ILE   H CB  1 
ATOM   9380  C  CG1 . ILE   H  1 59  ? 29.813  -75.140  -22.427 1.00 32.61 ? 59  ILE   H CG1 1 
ATOM   9381  C  CG2 . ILE   H  1 59  ? 28.916  -73.519  -20.722 1.00 30.46 ? 59  ILE   H CG2 1 
ATOM   9382  C  CD1 . ILE   H  1 59  ? 30.385  -74.217  -23.493 1.00 30.00 ? 59  ILE   H CD1 1 
ATOM   9383  N  N   . GLU   H  1 60  ? 25.570  -74.853  -20.700 1.00 28.31 ? 60  GLU   H N   1 
ATOM   9384  C  CA  . GLU   H  1 60  ? 24.479  -74.297  -19.903 1.00 28.18 ? 60  GLU   H CA  1 
ATOM   9385  C  C   . GLU   H  1 60  ? 23.906  -75.339  -18.945 1.00 31.70 ? 60  GLU   H C   1 
ATOM   9386  O  O   . GLU   H  1 60  ? 23.610  -75.034  -17.784 1.00 29.53 ? 60  GLU   H O   1 
ATOM   9387  C  CB  . GLU   H  1 60  ? 23.395  -73.751  -20.846 1.00 30.61 ? 60  GLU   H CB  1 
ATOM   9388  C  CG  . GLU   H  1 60  ? 23.898  -72.539  -21.632 1.00 30.04 ? 60  GLU   H CG  1 
ATOM   9389  C  CD  . GLU   H  1 60  ? 22.912  -72.067  -22.709 1.00 39.21 ? 60  GLU   H CD  1 
ATOM   9390  O  OE1 . GLU   H  1 60  ? 22.203  -72.912  -23.283 1.00 29.26 ? 60  GLU   H OE1 1 
ATOM   9391  O  OE2 . GLU   H  1 60  ? 22.850  -70.855  -22.970 1.00 31.24 ? 60  GLU   H OE2 1 
ATOM   9392  N  N   . ARG   H  1 61  ? 23.752  -76.577  -19.410 1.00 26.36 ? 61  ARG   H N   1 
ATOM   9393  C  CA  . ARG   H  1 61  ? 23.228  -77.639  -18.562 1.00 28.47 ? 61  ARG   H CA  1 
ATOM   9394  C  C   . ARG   H  1 61  ? 24.196  -77.977  -17.421 1.00 31.50 ? 61  ARG   H C   1 
ATOM   9395  O  O   . ARG   H  1 61  ? 23.772  -78.153  -16.269 1.00 30.34 ? 61  ARG   H O   1 
ATOM   9396  C  CB  . ARG   H  1 61  ? 22.935  -78.858  -19.431 1.00 29.67 ? 61  ARG   H CB  1 
ATOM   9397  C  CG  . ARG   H  1 61  ? 22.312  -80.056  -18.718 1.00 31.08 ? 61  ARG   H CG  1 
ATOM   9398  C  CD  . ARG   H  1 61  ? 20.916  -79.790  -18.339 1.00 29.95 ? 61  ARG   H CD  1 
ATOM   9399  N  NE  . ARG   H  1 61  ? 20.343  -80.874  -17.556 1.00 29.36 ? 61  ARG   H NE  1 
ATOM   9400  C  CZ  . ARG   H  1 61  ? 19.226  -80.765  -16.848 1.00 38.93 ? 61  ARG   H CZ  1 
ATOM   9401  N  NH1 . ARG   H  1 61  ? 18.514  -79.649  -16.845 1.00 40.38 ? 61  ARG   H NH1 1 
ATOM   9402  N  NH2 . ARG   H  1 61  ? 18.808  -81.800  -16.125 1.00 38.48 ? 61  ARG   H NH2 1 
ATOM   9403  N  N   . ILE   H  1 62  ? 25.497  -78.044  -17.717 1.00 29.93 ? 62  ILE   H N   1 
ATOM   9404  C  CA  . ILE   H  1 62  ? 26.483  -78.362  -16.693 1.00 33.68 ? 62  ILE   H CA  1 
ATOM   9405  C  C   . ILE   H  1 62  ? 26.485  -77.298  -15.593 1.00 38.07 ? 62  ILE   H C   1 
ATOM   9406  O  O   . ILE   H  1 62  ? 26.503  -77.623  -14.394 1.00 32.60 ? 62  ILE   H O   1 
ATOM   9407  C  CB  . ILE   H  1 62  ? 27.869  -78.543  -17.338 1.00 33.78 ? 62  ILE   H CB  1 
ATOM   9408  C  CG1 . ILE   H  1 62  ? 27.863  -79.804  -18.199 1.00 28.76 ? 62  ILE   H CG1 1 
ATOM   9409  C  CG2 . ILE   H  1 62  ? 28.943  -78.636  -16.271 1.00 33.90 ? 62  ILE   H CG2 1 
ATOM   9410  C  CD1 . ILE   H  1 62  ? 28.980  -79.852  -19.224 1.00 35.89 ? 62  ILE   H CD1 1 
ATOM   9411  N  N   . LEU   H  1 63  ? 26.461  -76.015  -15.976 1.00 28.24 ? 63  LEU   H N   1 
ATOM   9412  C  CA  . LEU   H  1 63  ? 26.369  -74.944  -14.988 1.00 32.39 ? 63  LEU   H CA  1 
ATOM   9413  C  C   . LEU   H  1 63  ? 25.068  -75.026  -14.178 1.00 31.51 ? 63  LEU   H C   1 
ATOM   9414  O  O   . LEU   H  1 63  ? 25.086  -74.840  -12.956 1.00 33.57 ? 63  LEU   H O   1 
ATOM   9415  C  CB  . LEU   H  1 63  ? 26.507  -73.578  -15.670 1.00 26.52 ? 63  LEU   H CB  1 
ATOM   9416  C  CG  . LEU   H  1 63  ? 27.875  -73.283  -16.318 1.00 39.37 ? 63  LEU   H CG  1 
ATOM   9417  C  CD1 . LEU   H  1 63  ? 27.807  -72.011  -17.152 1.00 37.39 ? 63  LEU   H CD1 1 
ATOM   9418  C  CD2 . LEU   H  1 63  ? 29.004  -73.148  -15.287 1.00 32.71 ? 63  LEU   H CD2 1 
ATOM   9419  N  N   . PHE   H  1 64  ? 23.942  -75.339  -14.813 1.00 32.39 ? 64  PHE   H N   1 
ATOM   9420  C  CA  . PHE   H  1 64  ? 22.699  -75.470  -14.040 1.00 36.20 ? 64  PHE   H CA  1 
ATOM   9421  C  C   . PHE   H  1 64  ? 22.817  -76.561  -12.986 1.00 36.37 ? 64  PHE   H C   1 
ATOM   9422  O  O   . PHE   H  1 64  ? 22.271  -76.429  -11.880 1.00 33.33 ? 64  PHE   H O   1 
ATOM   9423  C  CB  . PHE   H  1 64  ? 21.507  -75.778  -14.949 1.00 31.13 ? 64  PHE   H CB  1 
ATOM   9424  C  CG  . PHE   H  1 64  ? 20.253  -76.186  -14.212 1.00 34.19 ? 64  PHE   H CG  1 
ATOM   9425  C  CD1 . PHE   H  1 64  ? 19.609  -75.299  -13.374 1.00 35.44 ? 64  PHE   H CD1 1 
ATOM   9426  C  CD2 . PHE   H  1 64  ? 19.703  -77.454  -14.385 1.00 29.41 ? 64  PHE   H CD2 1 
ATOM   9427  C  CE1 . PHE   H  1 64  ? 18.464  -75.677  -12.710 1.00 34.73 ? 64  PHE   H CE1 1 
ATOM   9428  C  CE2 . PHE   H  1 64  ? 18.572  -77.833  -13.737 1.00 40.37 ? 64  PHE   H CE2 1 
ATOM   9429  C  CZ  . PHE   H  1 64  ? 17.932  -76.944  -12.898 1.00 33.48 ? 64  PHE   H CZ  1 
ATOM   9430  N  N   . LEU   H  1 65  ? 23.503  -77.657  -13.324 1.00 34.60 ? 65  LEU   H N   1 
ATOM   9431  C  CA  . LEU   H  1 65  ? 23.668  -78.789  -12.424 1.00 37.24 ? 65  LEU   H CA  1 
ATOM   9432  C  C   . LEU   H  1 65  ? 24.852  -78.582  -11.475 1.00 34.93 ? 65  LEU   H C   1 
ATOM   9433  O  O   . LEU   H  1 65  ? 25.255  -79.519  -10.777 1.00 38.62 ? 65  LEU   H O   1 
ATOM   9434  C  CB  . LEU   H  1 65  ? 23.815  -80.095  -13.231 1.00 37.84 ? 65  LEU   H CB  1 
ATOM   9435  C  CG  . LEU   H  1 65  ? 22.598  -80.570  -14.047 1.00 33.04 ? 65  LEU   H CG  1 
ATOM   9436  C  CD1 . LEU   H  1 65  ? 22.865  -81.801  -14.882 1.00 36.65 ? 65  LEU   H CD1 1 
ATOM   9437  C  CD2 . LEU   H  1 65  ? 21.415  -80.872  -13.166 1.00 35.99 ? 65  LEU   H CD2 1 
ATOM   9438  N  N   . GLU   H  1 66  ? 25.417  -77.376  -11.450 1.00 31.31 ? 66  GLU   H N   1 
ATOM   9439  C  CA  . GLU   H  1 66  ? 26.471  -76.982  -10.525 1.00 30.09 ? 66  GLU   H CA  1 
ATOM   9440  C  C   . GLU   H  1 66  ? 27.783  -77.731  -10.764 1.00 43.72 ? 66  GLU   H C   1 
ATOM   9441  O  O   . GLU   H  1 66  ? 28.577  -77.915  -9.838  1.00 36.43 ? 66  GLU   H O   1 
ATOM   9442  C  CB  . GLU   H  1 66  ? 25.984  -77.128  -9.068  1.00 36.74 ? 66  GLU   H CB  1 
ATOM   9443  C  CG  . GLU   H  1 66  ? 24.602  -76.412  -8.909  1.00 30.97 ? 66  GLU   H CG  1 
ATOM   9444  C  CD  . GLU   H  1 66  ? 24.054  -76.313  -7.494  1.00 38.66 ? 66  GLU   H CD  1 
ATOM   9445  O  OE1 . GLU   H  1 66  ? 24.810  -76.471  -6.515  1.00 38.61 ? 66  GLU   H OE1 1 
ATOM   9446  O  OE2 . GLU   H  1 66  ? 22.840  -76.054  -7.376  1.00 38.95 ? 66  GLU   H OE2 1 
ATOM   9447  N  N   . GLY   H  1 67  ? 28.059  -78.106  -12.016 1.00 32.73 ? 67  GLY   H N   1 
ATOM   9448  C  CA  . GLY   H  1 67  ? 29.355  -78.608  -12.408 1.00 35.66 ? 67  GLY   H CA  1 
ATOM   9449  C  C   . GLY   H  1 67  ? 30.237  -77.538  -13.046 1.00 38.06 ? 67  GLY   H C   1 
ATOM   9450  O  O   . GLY   H  1 67  ? 29.836  -76.403  -13.274 1.00 35.59 ? 67  GLY   H O   1 
ATOM   9451  N  N   . LEU   H  1 68  ? 31.477  -77.929  -13.341 1.00 33.30 ? 68  LEU   H N   1 
ATOM   9452  C  CA  . LEU   H  1 68  ? 32.420  -77.033  -14.010 1.00 38.40 ? 68  LEU   H CA  1 
ATOM   9453  C  C   . LEU   H  1 68  ? 32.560  -77.474  -15.455 1.00 41.31 ? 68  LEU   H C   1 
ATOM   9454  O  O   . LEU   H  1 68  ? 33.080  -78.573  -15.707 1.00 37.65 ? 68  LEU   H O   1 
ATOM   9455  C  CB  . LEU   H  1 68  ? 33.779  -77.045  -13.320 1.00 42.43 ? 68  LEU   H CB  1 
ATOM   9456  C  CG  . LEU   H  1 68  ? 33.786  -76.309  -11.985 1.00 43.27 ? 68  LEU   H CG  1 
ATOM   9457  C  CD1 . LEU   H  1 68  ? 34.922  -76.832  -11.122 1.00 65.79 ? 68  LEU   H CD1 1 
ATOM   9458  C  CD2 . LEU   H  1 68  ? 33.953  -74.811  -12.217 1.00 66.26 ? 68  LEU   H CD2 1 
ATOM   9459  N  N   . PRO   H  1 69  ? 32.095  -76.696  -16.434 1.00 35.76 ? 69  PRO   H N   1 
ATOM   9460  C  CA  . PRO   H  1 69  ? 32.250  -77.124  -17.830 1.00 41.37 ? 69  PRO   H CA  1 
ATOM   9461  C  C   . PRO   H  1 69  ? 33.720  -77.111  -18.220 1.00 33.15 ? 69  PRO   H C   1 
ATOM   9462  O  O   . PRO   H  1 69  ? 34.426  -76.127  -17.999 1.00 35.80 ? 69  PRO   H O   1 
ATOM   9463  C  CB  . PRO   H  1 69  ? 31.431  -76.093  -18.624 1.00 38.24 ? 69  PRO   H CB  1 
ATOM   9464  C  CG  . PRO   H  1 69  ? 30.497  -75.468  -17.617 1.00 41.28 ? 69  PRO   H CG  1 
ATOM   9465  C  CD  . PRO   H  1 69  ? 31.253  -75.492  -16.308 1.00 37.25 ? 69  PRO   H CD  1 
ATOM   9466  N  N   . ASN   H  1 70  ? 34.180  -78.207  -18.813 1.00 33.70 ? 70  ASN   H N   1 
ATOM   9467  C  CA  . ASN   H  1 70  ? 35.583  -78.315  -19.211 1.00 41.94 ? 70  ASN   H CA  1 
ATOM   9468  C  C   . ASN   H  1 70  ? 35.785  -77.765  -20.622 1.00 29.88 ? 70  ASN   H C   1 
ATOM   9469  O  O   . ASN   H  1 70  ? 35.609  -78.476  -21.607 1.00 31.32 ? 70  ASN   H O   1 
ATOM   9470  C  CB  . ASN   H  1 70  ? 36.055  -79.762  -19.147 1.00 40.42 ? 70  ASN   H CB  1 
ATOM   9471  C  CG  . ASN   H  1 70  ? 37.571  -79.877  -19.270 1.00 36.87 ? 70  ASN   H CG  1 
ATOM   9472  O  OD1 . ASN   H  1 70  ? 38.239  -78.995  -19.820 1.00 38.61 ? 70  ASN   H OD1 1 
ATOM   9473  N  ND2 . ASN   H  1 70  ? 38.123  -80.945  -18.706 1.00 44.36 ? 70  ASN   H ND2 1 
ATOM   9474  N  N   . LEU   H  1 71  ? 36.239  -76.528  -20.729 1.00 32.79 ? 71  LEU   H N   1 
ATOM   9475  C  CA  . LEU   H  1 71  ? 36.654  -76.017  -22.029 1.00 36.93 ? 71  LEU   H CA  1 
ATOM   9476  C  C   . LEU   H  1 71  ? 38.165  -75.990  -22.183 1.00 40.27 ? 71  LEU   H C   1 
ATOM   9477  O  O   . LEU   H  1 71  ? 38.671  -75.389  -23.138 1.00 34.41 ? 71  LEU   H O   1 
ATOM   9478  C  CB  . LEU   H  1 71  ? 36.101  -74.617  -22.261 1.00 40.67 ? 71  LEU   H CB  1 
ATOM   9479  C  CG  . LEU   H  1 71  ? 34.607  -74.553  -22.591 1.00 34.82 ? 71  LEU   H CG  1 
ATOM   9480  C  CD1 . LEU   H  1 71  ? 33.775  -74.701  -21.361 1.00 43.06 ? 71  LEU   H CD1 1 
ATOM   9481  C  CD2 . LEU   H  1 71  ? 34.308  -73.236  -23.284 1.00 35.51 ? 71  LEU   H CD2 1 
ATOM   9482  N  N   . GLN   H  1 72  ? 38.896  -76.597  -21.248 1.00 34.66 ? 72  GLN   H N   1 
ATOM   9483  C  CA  . GLN   H  1 72  ? 40.350  -76.499  -21.224 1.00 35.22 ? 72  GLN   H CA  1 
ATOM   9484  C  C   . GLN   H  1 72  ? 41.023  -77.651  -21.957 1.00 32.28 ? 72  GLN   H C   1 
ATOM   9485  O  O   . GLN   H  1 72  ? 42.098  -77.456  -22.530 1.00 34.53 ? 72  GLN   H O   1 
ATOM   9486  C  CB  . GLN   H  1 72  ? 40.853  -76.466  -19.771 1.00 38.12 ? 72  GLN   H CB  1 
ATOM   9487  C  CG  . GLN   H  1 72  ? 42.385  -76.435  -19.627 1.00 32.92 ? 72  GLN   H CG  1 
ATOM   9488  C  CD  . GLN   H  1 72  ? 42.983  -75.120  -20.092 1.00 31.69 ? 72  GLN   H CD  1 
ATOM   9489  O  OE1 . GLN   H  1 72  ? 43.175  -74.190  -19.297 1.00 30.21 ? 72  GLN   H OE1 1 
ATOM   9490  N  NE2 . GLN   H  1 72  ? 43.301  -75.036  -21.378 1.00 39.15 ? 72  GLN   H NE2 1 
ATOM   9491  N  N   . ASP   H  1 73  ? 40.427  -78.841  -21.924 1.00 38.19 ? 73  ASP   H N   1 
ATOM   9492  C  CA  . ASP   H  1 73  ? 41.035  -80.063  -22.445 1.00 38.63 ? 73  ASP   H CA  1 
ATOM   9493  C  C   . ASP   H  1 73  ? 40.524  -80.343  -23.859 1.00 37.85 ? 73  ASP   H C   1 
ATOM   9494  O  O   . ASP   H  1 73  ? 39.348  -80.667  -24.059 1.00 47.71 ? 73  ASP   H O   1 
ATOM   9495  C  CB  . ASP   H  1 73  ? 40.734  -81.248  -21.526 1.00 40.14 ? 73  ASP   H CB  1 
ATOM   9496  C  CG  . ASP   H  1 73  ? 41.298  -81.063  -20.120 1.00 40.89 ? 73  ASP   H CG  1 
ATOM   9497  O  OD1 . ASP   H  1 73  ? 42.250  -80.267  -19.962 1.00 41.71 ? 73  ASP   H OD1 1 
ATOM   9498  O  OD2 . ASP   H  1 73  ? 40.775  -81.700  -19.178 1.00 34.57 ? 73  ASP   H OD2 1 
ATOM   9499  N  N   . LEU   H  1 74  ? 41.408  -80.232  -24.826 1.00 42.15 ? 74  LEU   H N   1 
ATOM   9500  C  CA  . LEU   H  1 74  ? 41.087  -80.438  -26.233 1.00 33.89 ? 74  LEU   H CA  1 
ATOM   9501  C  C   . LEU   H  1 74  ? 41.792  -81.699  -26.716 1.00 36.35 ? 74  LEU   H C   1 
ATOM   9502  O  O   . LEU   H  1 74  ? 43.020  -81.703  -26.861 1.00 41.15 ? 74  LEU   H O   1 
ATOM   9503  C  CB  . LEU   H  1 74  ? 41.531  -79.228  -27.045 1.00 34.29 ? 74  LEU   H CB  1 
ATOM   9504  C  CG  . LEU   H  1 74  ? 41.171  -79.238  -28.527 1.00 37.67 ? 74  LEU   H CG  1 
ATOM   9505  C  CD1 . LEU   H  1 74  ? 39.649  -79.389  -28.681 1.00 40.09 ? 74  LEU   H CD1 1 
ATOM   9506  C  CD2 . LEU   H  1 74  ? 41.685  -77.977  -29.181 1.00 36.79 ? 74  LEU   H CD2 1 
ATOM   9507  N  N   . GLY   H  1 75  ? 41.013  -82.754  -26.954 1.00 34.03 ? 75  GLY   H N   1 
ATOM   9508  C  CA  . GLY   H  1 75  ? 41.495  -83.970  -27.583 1.00 42.98 ? 75  GLY   H CA  1 
ATOM   9509  C  C   . GLY   H  1 75  ? 41.970  -83.790  -29.013 1.00 40.50 ? 75  GLY   H C   1 
ATOM   9510  O  O   . GLY   H  1 75  ? 41.990  -82.679  -29.554 1.00 36.52 ? 75  GLY   H O   1 
ATOM   9511  N  N   . LYS   H  1 76  ? 42.362  -84.886  -29.645 1.00 39.26 ? 76  LYS   H N   1 
ATOM   9512  C  CA  . LYS   H  1 76  ? 43.093  -84.802  -30.899 1.00 41.65 ? 76  LYS   H CA  1 
ATOM   9513  C  C   . LYS   H  1 76  ? 42.124  -84.544  -32.048 1.00 31.48 ? 76  LYS   H C   1 
ATOM   9514  O  O   . LYS   H  1 76  ? 41.107  -85.233  -32.183 1.00 36.54 ? 76  LYS   H O   1 
ATOM   9515  C  CB  . LYS   H  1 76  ? 43.889  -86.091  -31.132 1.00 42.61 ? 76  LYS   H CB  1 
ATOM   9516  C  CG  . LYS   H  1 76  ? 44.551  -86.222  -32.517 1.00 38.62 ? 76  LYS   H CG  1 
ATOM   9517  N  N   . LEU   H  1 77  ? 42.451  -83.550  -32.875 1.00 35.16 ? 77  LEU   H N   1 
ATOM   9518  C  CA  . LEU   H  1 77  ? 41.703  -83.304  -34.105 1.00 39.41 ? 77  LEU   H CA  1 
ATOM   9519  C  C   . LEU   H  1 77  ? 42.107  -84.290  -35.194 1.00 38.43 ? 77  LEU   H C   1 
ATOM   9520  O  O   . LEU   H  1 77  ? 43.292  -84.586  -35.365 1.00 38.86 ? 77  LEU   H O   1 
ATOM   9521  C  CB  . LEU   H  1 77  ? 41.979  -81.894  -34.618 1.00 39.35 ? 77  LEU   H CB  1 
ATOM   9522  C  CG  . LEU   H  1 77  ? 41.977  -80.779  -33.585 1.00 45.50 ? 77  LEU   H CG  1 
ATOM   9523  C  CD1 . LEU   H  1 77  ? 42.273  -79.416  -34.234 1.00 41.91 ? 77  LEU   H CD1 1 
ATOM   9524  C  CD2 . LEU   H  1 77  ? 40.632  -80.792  -32.908 1.00 38.70 ? 77  LEU   H CD2 1 
ATOM   9525  N  N   . LEU   H  1 78  ? 41.127  -84.752  -35.954 1.00 35.52 ? 78  LEU   H N   1 
ATOM   9526  C  CA  . LEU   H  1 78  ? 41.348  -85.594  -37.134 1.00 36.48 ? 78  LEU   H CA  1 
ATOM   9527  C  C   . LEU   H  1 78  ? 41.215  -84.719  -38.383 1.00 41.51 ? 78  LEU   H C   1 
ATOM   9528  O  O   . LEU   H  1 78  ? 40.107  -84.458  -38.857 1.00 36.86 ? 78  LEU   H O   1 
ATOM   9529  C  CB  . LEU   H  1 78  ? 40.358  -86.751  -37.166 1.00 32.27 ? 78  LEU   H CB  1 
ATOM   9530  C  CG  . LEU   H  1 78  ? 40.262  -87.549  -35.865 1.00 38.70 ? 78  LEU   H CG  1 
ATOM   9531  C  CD1 . LEU   H  1 78  ? 39.180  -88.570  -36.015 1.00 41.26 ? 78  LEU   H CD1 1 
ATOM   9532  C  CD2 . LEU   H  1 78  ? 41.607  -88.181  -35.474 1.00 39.99 ? 78  LEU   H CD2 1 
ATOM   9533  N  N   . ILE   H  1 79  ? 42.350  -84.270  -38.908 1.00 38.13 ? 79  ILE   H N   1 
ATOM   9534  C  CA  . ILE   H  1 79  ? 42.413  -83.383  -40.061 1.00 40.09 ? 79  ILE   H CA  1 
ATOM   9535  C  C   . ILE   H  1 79  ? 42.881  -84.195  -41.255 1.00 45.88 ? 79  ILE   H C   1 
ATOM   9536  O  O   . ILE   H  1 79  ? 43.987  -84.742  -41.240 1.00 41.56 ? 79  ILE   H O   1 
ATOM   9537  C  CB  . ILE   H  1 79  ? 43.373  -82.213  -39.820 1.00 38.75 ? 79  ILE   H CB  1 
ATOM   9538  C  CG1 . ILE   H  1 79  ? 43.104  -81.554  -38.467 1.00 41.41 ? 79  ILE   H CG1 1 
ATOM   9539  C  CG2 . ILE   H  1 79  ? 43.291  -81.226  -40.968 1.00 44.67 ? 79  ILE   H CG2 1 
ATOM   9540  C  CD1 . ILE   H  1 79  ? 41.618  -81.159  -38.240 1.00 39.49 ? 79  ILE   H CD1 1 
ATOM   9541  N  N   . GLY   H  1 80  ? 42.072  -84.249  -42.293 1.00 40.32 ? 80  GLY   H N   1 
ATOM   9542  C  CA  . GLY   H  1 80  ? 42.486  -84.962  -43.483 1.00 43.27 ? 80  GLY   H CA  1 
ATOM   9543  C  C   . GLY   H  1 80  ? 43.401  -84.143  -44.375 1.00 40.94 ? 80  GLY   H C   1 
ATOM   9544  O  O   . GLY   H  1 80  ? 43.619  -82.952  -44.189 1.00 42.70 ? 80  GLY   H O   1 
ATOM   9545  N  N   . GLU   H  1 81  ? 43.964  -84.805  -45.381 1.00 45.33 ? 81  GLU   H N   1 
ATOM   9546  C  CA  . GLU   H  1 81  ? 44.832  -84.125  -46.330 1.00 42.81 ? 81  GLU   H CA  1 
ATOM   9547  C  C   . GLU   H  1 81  ? 44.222  -84.003  -47.722 1.00 38.38 ? 81  GLU   H C   1 
ATOM   9548  O  O   . GLU   H  1 81  ? 44.796  -83.318  -48.580 1.00 40.95 ? 81  GLU   H O   1 
ATOM   9549  C  CB  . GLU   H  1 81  ? 46.181  -84.844  -46.403 1.00 48.29 ? 81  GLU   H CB  1 
ATOM   9550  C  CG  . GLU   H  1 81  ? 47.016  -84.629  -45.153 1.00 48.85 ? 81  GLU   H CG  1 
ATOM   9551  C  CD  . GLU   H  1 81  ? 48.322  -85.381  -45.197 1.00 53.65 ? 81  GLU   H CD  1 
ATOM   9552  O  OE1 . GLU   H  1 81  ? 49.099  -85.154  -46.147 1.00 65.07 ? 81  GLU   H OE1 1 
ATOM   9553  O  OE2 . GLU   H  1 81  ? 48.559  -86.202  -44.287 1.00 57.85 ? 81  GLU   H OE2 1 
ATOM   9554  N  N   . ASN   H  1 82  ? 43.091  -84.645  -47.965 1.00 38.98 ? 82  ASN   H N   1 
ATOM   9555  C  CA  . ASN   H  1 82  ? 42.294  -84.408  -49.156 1.00 43.27 ? 82  ASN   H CA  1 
ATOM   9556  C  C   . ASN   H  1 82  ? 40.829  -84.552  -48.761 1.00 34.52 ? 82  ASN   H C   1 
ATOM   9557  O  O   . ASN   H  1 82  ? 40.499  -84.873  -47.615 1.00 34.90 ? 82  ASN   H O   1 
ATOM   9558  C  CB  . ASN   H  1 82  ? 42.684  -85.360  -50.301 1.00 39.47 ? 82  ASN   H CB  1 
ATOM   9559  C  CG  . ASN   H  1 82  ? 42.594  -86.809  -49.900 1.00 36.21 ? 82  ASN   H CG  1 
ATOM   9560  O  OD1 . ASN   H  1 82  ? 41.686  -87.200  -49.191 1.00 34.22 ? 82  ASN   H OD1 1 
ATOM   9561  N  ND2 . ASN   H  1 82  ? 43.551  -87.612  -50.334 1.00 42.31 ? 82  ASN   H ND2 1 
ATOM   9562  N  N   . THR   H  1 83  ? 39.950  -84.344  -49.737 1.00 33.70 ? 83  THR   H N   1 
ATOM   9563  C  CA  . THR   H  1 83  ? 38.524  -84.242  -49.453 1.00 34.00 ? 83  THR   H CA  1 
ATOM   9564  C  C   . THR   H  1 83  ? 37.970  -85.544  -48.899 1.00 39.54 ? 83  THR   H C   1 
ATOM   9565  O  O   . THR   H  1 83  ? 37.186  -85.545  -47.941 1.00 31.16 ? 83  THR   H O   1 
ATOM   9566  C  CB  . THR   H  1 83  ? 37.792  -83.840  -50.736 1.00 33.78 ? 83  THR   H CB  1 
ATOM   9567  O  OG1 . THR   H  1 83  ? 38.144  -82.485  -51.050 1.00 33.86 ? 83  THR   H OG1 1 
ATOM   9568  C  CG2 . THR   H  1 83  ? 36.265  -84.011  -50.611 1.00 36.54 ? 83  THR   H CG2 1 
ATOM   9569  N  N   . GLN   H  1 84  ? 38.313  -86.663  -49.530 1.00 35.05 ? 84  GLN   H N   1 
ATOM   9570  C  CA  . GLN   H  1 84  ? 37.861  -87.961  -49.041 1.00 36.20 ? 84  GLN   H CA  1 
ATOM   9571  C  C   . GLN   H  1 84  ? 38.303  -88.189  -47.594 1.00 28.93 ? 84  GLN   H C   1 
ATOM   9572  O  O   . GLN   H  1 84  ? 37.508  -88.599  -46.737 1.00 36.83 ? 84  GLN   H O   1 
ATOM   9573  C  CB  . GLN   H  1 84  ? 38.403  -89.073  -49.941 1.00 38.79 ? 84  GLN   H CB  1 
ATOM   9574  C  CG  . GLN   H  1 84  ? 37.859  -90.442  -49.580 1.00 36.06 ? 84  GLN   H CG  1 
ATOM   9575  C  CD  . GLN   H  1 84  ? 38.466  -91.579  -50.403 1.00 50.35 ? 84  GLN   H CD  1 
ATOM   9576  O  OE1 . GLN   H  1 84  ? 39.684  -91.635  -50.609 1.00 46.78 ? 84  GLN   H OE1 1 
ATOM   9577  N  NE2 . GLN   H  1 84  ? 37.617  -92.495  -50.861 1.00 48.41 ? 84  GLN   H NE2 1 
ATOM   9578  N  N   . GLU   H  1 85  ? 39.571  -87.933  -47.313 1.00 33.92 ? 85  GLU   H N   1 
ATOM   9579  C  CA  . GLU   H  1 85  ? 40.073  -88.094  -45.952 1.00 40.58 ? 85  GLU   H CA  1 
ATOM   9580  C  C   . GLU   H  1 85  ? 39.326  -87.201  -44.962 1.00 38.93 ? 85  GLU   H C   1 
ATOM   9581  O  O   . GLU   H  1 85  ? 38.991  -87.631  -43.850 1.00 31.71 ? 85  GLU   H O   1 
ATOM   9582  C  CB  . GLU   H  1 85  ? 41.567  -87.786  -45.923 1.00 37.74 ? 85  GLU   H CB  1 
ATOM   9583  C  CG  . GLU   H  1 85  ? 42.403  -88.930  -45.493 1.00 46.09 ? 85  GLU   H CG  1 
ATOM   9584  C  CD  . GLU   H  1 85  ? 43.856  -88.707  -45.775 1.00 43.41 ? 85  GLU   H CD  1 
ATOM   9585  O  OE1 . GLU   H  1 85  ? 44.372  -87.609  -45.447 1.00 47.87 ? 85  GLU   H OE1 1 
ATOM   9586  O  OE2 . GLU   H  1 85  ? 44.488  -89.638  -46.324 1.00 60.07 ? 85  GLU   H OE2 1 
ATOM   9587  N  N   . MET   H  1 86  ? 39.072  -85.951  -45.339 1.00 38.54 ? 86  MET   H N   1 
ATOM   9588  C  CA  . MET   H  1 86  ? 38.408  -85.027  -44.420 1.00 37.44 ? 86  MET   H CA  1 
ATOM   9589  C  C   . MET   H  1 86  ? 37.030  -85.532  -44.046 1.00 32.56 ? 86  MET   H C   1 
ATOM   9590  O  O   . MET   H  1 86  ? 36.660  -85.554  -42.867 1.00 36.19 ? 86  MET   H O   1 
ATOM   9591  C  CB  . MET   H  1 86  ? 38.343  -83.651  -45.061 1.00 36.26 ? 86  MET   H CB  1 
ATOM   9592  C  CG  . MET   H  1 86  ? 39.725  -83.089  -45.272 1.00 29.78 ? 86  MET   H CG  1 
ATOM   9593  S  SD  . MET   H  1 86  ? 39.901  -81.919  -46.675 1.00 34.36 ? 86  MET   H SD  1 
ATOM   9594  C  CE  . MET   H  1 86  ? 39.213  -80.426  -45.904 1.00 41.55 ? 86  MET   H CE  1 
ATOM   9595  N  N   . LEU   H  1 87  ? 36.253  -85.945  -45.045 1.00 33.46 ? 87  LEU   H N   1 
ATOM   9596  C  CA  . LEU   H  1 87  ? 34.930  -86.496  -44.793 1.00 29.62 ? 87  LEU   H CA  1 
ATOM   9597  C  C   . LEU   H  1 87  ? 35.019  -87.719  -43.888 1.00 41.89 ? 87  LEU   H C   1 
ATOM   9598  O  O   . LEU   H  1 87  ? 34.216  -87.882  -42.954 1.00 34.97 ? 87  LEU   H O   1 
ATOM   9599  C  CB  . LEU   H  1 87  ? 34.268  -86.848  -46.127 1.00 30.22 ? 87  LEU   H CB  1 
ATOM   9600  C  CG  . LEU   H  1 87  ? 33.937  -85.676  -47.065 1.00 36.64 ? 87  LEU   H CG  1 
ATOM   9601  C  CD1 . LEU   H  1 87  ? 33.646  -86.159  -48.494 1.00 33.59 ? 87  LEU   H CD1 1 
ATOM   9602  C  CD2 . LEU   H  1 87  ? 32.747  -84.891  -46.518 1.00 31.40 ? 87  LEU   H CD2 1 
ATOM   9603  N  N   . GLN   H  1 88  ? 35.998  -88.591  -44.157 1.00 34.81 ? 88  GLN   H N   1 
ATOM   9604  C  CA  A GLN   H  1 88  ? 36.196  -89.762  -43.309 0.50 36.81 ? 88  GLN   H CA  1 
ATOM   9605  C  CA  B GLN   H  1 88  ? 36.227  -89.761  -43.315 0.50 36.84 ? 88  GLN   H CA  1 
ATOM   9606  C  C   . GLN   H  1 88  ? 36.634  -89.360  -41.904 1.00 30.84 ? 88  GLN   H C   1 
ATOM   9607  O  O   . GLN   H  1 88  ? 36.198  -89.970  -40.918 1.00 37.19 ? 88  GLN   H O   1 
ATOM   9608  C  CB  A GLN   H  1 88  ? 37.223  -90.714  -43.942 0.50 33.61 ? 88  GLN   H CB  1 
ATOM   9609  C  CB  B GLN   H  1 88  ? 37.307  -90.644  -43.954 0.50 33.54 ? 88  GLN   H CB  1 
ATOM   9610  C  CG  A GLN   H  1 88  ? 37.300  -92.070  -43.233 0.50 39.25 ? 88  GLN   H CG  1 
ATOM   9611  C  CG  B GLN   H  1 88  ? 36.759  -91.489  -45.064 0.50 25.73 ? 88  GLN   H CG  1 
ATOM   9612  C  CD  A GLN   H  1 88  ? 35.976  -92.831  -43.265 0.50 37.80 ? 88  GLN   H CD  1 
ATOM   9613  C  CD  B GLN   H  1 88  ? 37.813  -92.068  -45.964 0.50 24.31 ? 88  GLN   H CD  1 
ATOM   9614  O  OE1 A GLN   H  1 88  ? 35.281  -92.855  -44.289 0.50 46.79 ? 88  GLN   H OE1 1 
ATOM   9615  O  OE1 B GLN   H  1 88  ? 39.014  -91.922  -45.750 0.50 24.82 ? 88  GLN   H OE1 1 
ATOM   9616  N  NE2 A GLN   H  1 88  ? 35.626  -93.455  -42.153 0.50 29.11 ? 88  GLN   H NE2 1 
ATOM   9617  N  NE2 B GLN   H  1 88  ? 37.357  -92.715  -46.993 0.50 23.96 ? 88  GLN   H NE2 1 
ATOM   9618  N  N   . CYS   H  1 89  ? 37.502  -88.355  -41.784 1.00 30.90 ? 89  CYS   H N   1 
ATOM   9619  C  CA  . CYS   H  1 89  ? 37.853  -87.885  -40.455 1.00 31.06 ? 89  CYS   H CA  1 
ATOM   9620  C  C   . CYS   H  1 89  ? 36.613  -87.418  -39.690 1.00 42.52 ? 89  CYS   H C   1 
ATOM   9621  O  O   . CYS   H  1 89  ? 36.474  -87.695  -38.486 1.00 32.88 ? 89  CYS   H O   1 
ATOM   9622  C  CB  . CYS   H  1 89  ? 38.882  -86.767  -40.550 1.00 37.70 ? 89  CYS   H CB  1 
ATOM   9623  S  SG  . CYS   H  1 89  ? 40.600  -87.333  -40.872 1.00 36.78 ? 89  CYS   H SG  1 
ATOM   9624  N  N   . ASP   H  1 90  ? 35.715  -86.712  -40.374 1.00 34.64 ? 90  ASP   H N   1 
ATOM   9625  C  CA  . ASP   H  1 90  ? 34.468  -86.250  -39.716 1.00 35.43 ? 90  ASP   H CA  1 
ATOM   9626  C  C   . ASP   H  1 90  ? 33.631  -87.474  -39.327 1.00 37.64 ? 90  ASP   H C   1 
ATOM   9627  O  O   . ASP   H  1 90  ? 33.144  -87.509  -38.190 1.00 36.78 ? 90  ASP   H O   1 
ATOM   9628  C  CB  . ASP   H  1 90  ? 33.709  -85.259  -40.581 1.00 37.27 ? 90  ASP   H CB  1 
ATOM   9629  C  CG  . ASP   H  1 90  ? 34.442  -83.983  -40.955 1.00 29.82 ? 90  ASP   H CG  1 
ATOM   9630  O  OD1 . ASP   H  1 90  ? 35.407  -83.625  -40.262 1.00 31.85 ? 90  ASP   H OD1 1 
ATOM   9631  O  OD2 . ASP   H  1 90  ? 34.027  -83.372  -41.946 1.00 39.17 ? 90  ASP   H OD2 1 
ATOM   9632  N  N   . LEU   H  1 91  ? 33.501  -88.439  -40.240 1.00 31.95 ? 91  LEU   H N   1 
ATOM   9633  C  CA  . LEU   H  1 91  ? 32.702  -89.619  -39.940 1.00 29.50 ? 91  LEU   H CA  1 
ATOM   9634  C  C   . LEU   H  1 91  ? 33.252  -90.341  -38.709 1.00 36.20 ? 91  LEU   H C   1 
ATOM   9635  O  O   . LEU   H  1 91  ? 32.494  -90.715  -37.804 1.00 34.69 ? 91  LEU   H O   1 
ATOM   9636  C  CB  . LEU   H  1 91  ? 32.655  -90.539  -41.165 1.00 31.28 ? 91  LEU   H CB  1 
ATOM   9637  C  CG  . LEU   H  1 91  ? 31.799  -91.804  -41.064 1.00 31.95 ? 91  LEU   H CG  1 
ATOM   9638  C  CD1 . LEU   H  1 91  ? 30.400  -91.517  -40.496 1.00 36.38 ? 91  LEU   H CD1 1 
ATOM   9639  C  CD2 . LEU   H  1 91  ? 31.695  -92.522  -42.411 1.00 35.95 ? 91  LEU   H CD2 1 
ATOM   9640  N  N   . ASN   H  1 92  ? 34.575  -90.495  -38.632 1.00 38.88 ? 92  ASN   H N   1 
ATOM   9641  C  CA  . ASN   H  1 92  ? 35.153  -91.227  -37.507 1.00 37.44 ? 92  ASN   H CA  1 
ATOM   9642  C  C   . ASN   H  1 92  ? 34.924  -90.485  -36.193 1.00 37.99 ? 92  ASN   H C   1 
ATOM   9643  O  O   . ASN   H  1 92  ? 34.603  -91.098  -35.170 1.00 34.58 ? 92  ASN   H O   1 
ATOM   9644  C  CB  . ASN   H  1 92  ? 36.640  -91.452  -37.734 1.00 37.20 ? 92  ASN   H CB  1 
ATOM   9645  C  CG  . ASN   H  1 92  ? 36.927  -92.309  -38.952 1.00 35.84 ? 92  ASN   H CG  1 
ATOM   9646  O  OD1 . ASN   H  1 92  ? 36.073  -93.050  -39.428 1.00 38.07 ? 92  ASN   H OD1 1 
ATOM   9647  N  ND2 . ASN   H  1 92  ? 38.141  -92.216  -39.448 1.00 46.39 ? 92  ASN   H ND2 1 
ATOM   9648  N  N   . LEU   H  1 93  ? 35.106  -89.167  -36.195 1.00 37.60 ? 93  LEU   H N   1 
ATOM   9649  C  CA  . LEU   H  1 93  ? 34.796  -88.386  -35.002 1.00 36.25 ? 93  LEU   H CA  1 
ATOM   9650  C  C   . LEU   H  1 93  ? 33.330  -88.544  -34.615 1.00 37.81 ? 93  LEU   H C   1 
ATOM   9651  O  O   . LEU   H  1 93  ? 33.018  -88.768  -33.439 1.00 39.11 ? 93  LEU   H O   1 
ATOM   9652  C  CB  . LEU   H  1 93  ? 35.159  -86.924  -35.236 1.00 38.87 ? 93  LEU   H CB  1 
ATOM   9653  C  CG  . LEU   H  1 93  ? 34.750  -85.972  -34.129 1.00 36.43 ? 93  LEU   H CG  1 
ATOM   9654  C  CD1 . LEU   H  1 93  ? 35.237  -86.512  -32.811 1.00 45.38 ? 93  LEU   H CD1 1 
ATOM   9655  C  CD2 . LEU   H  1 93  ? 35.308  -84.587  -34.385 1.00 33.03 ? 93  LEU   H CD2 1 
ATOM   9656  N  N   . GLU   H  1 94  ? 32.413  -88.490  -35.603 1.00 36.40 ? 94  GLU   H N   1 
ATOM   9657  C  CA  . GLU   H  1 94  ? 30.980  -88.614  -35.311 1.00 35.69 ? 94  GLU   H CA  1 
ATOM   9658  C  C   . GLU   H  1 94  ? 30.630  -89.976  -34.726 1.00 42.02 ? 94  GLU   H C   1 
ATOM   9659  O  O   . GLU   H  1 94  ? 29.703  -90.087  -33.912 1.00 34.59 ? 94  GLU   H O   1 
ATOM   9660  C  CB  . GLU   H  1 94  ? 30.112  -88.407  -36.567 1.00 36.02 ? 94  GLU   H CB  1 
ATOM   9661  C  CG  . GLU   H  1 94  ? 30.071  -86.992  -37.114 1.00 41.87 ? 94  GLU   H CG  1 
ATOM   9662  C  CD  . GLU   H  1 94  ? 29.235  -86.053  -36.251 1.00 47.65 ? 94  GLU   H CD  1 
ATOM   9663  O  OE1 . GLU   H  1 94  ? 28.495  -86.552  -35.396 1.00 43.17 ? 94  GLU   H OE1 1 
ATOM   9664  O  OE2 . GLU   H  1 94  ? 29.327  -84.818  -36.423 1.00 54.55 ? 94  GLU   H OE2 1 
ATOM   9665  N  N   . LEU   H  1 95  ? 31.315  -91.031  -35.158 1.00 38.43 ? 95  LEU   H N   1 
ATOM   9666  C  CA  . LEU   H  1 95  ? 30.949  -92.356  -34.675 1.00 45.10 ? 95  LEU   H CA  1 
ATOM   9667  C  C   . LEU   H  1 95  ? 31.404  -92.539  -33.232 1.00 36.27 ? 95  LEU   H C   1 
ATOM   9668  O  O   . LEU   H  1 95  ? 30.700  -93.160  -32.426 1.00 42.04 ? 95  LEU   H O   1 
ATOM   9669  C  CB  . LEU   H  1 95  ? 31.548  -93.422  -35.587 1.00 41.25 ? 95  LEU   H CB  1 
ATOM   9670  C  CG  . LEU   H  1 95  ? 30.998  -93.394  -37.007 1.00 41.73 ? 95  LEU   H CG  1 
ATOM   9671  C  CD1 . LEU   H  1 95  ? 31.937  -94.073  -37.977 1.00 49.37 ? 95  LEU   H CD1 1 
ATOM   9672  C  CD2 . LEU   H  1 95  ? 29.659  -94.055  -37.024 1.00 36.57 ? 95  LEU   H CD2 1 
ATOM   9673  N  N   . LYS   H  1 96  ? 32.557  -91.971  -32.886 1.00 33.59 ? 96  LYS   H N   1 
ATOM   9674  C  CA  . LYS   H  1 96  ? 32.960  -91.922  -31.488 1.00 36.17 ? 96  LYS   H CA  1 
ATOM   9675  C  C   . LYS   H  1 96  ? 31.957  -91.103  -30.680 1.00 44.22 ? 96  LYS   H C   1 
ATOM   9676  O  O   . LYS   H  1 96  ? 31.503  -91.530  -29.609 1.00 36.31 ? 96  LYS   H O   1 
ATOM   9677  C  CB  . LYS   H  1 96  ? 34.376  -91.337  -31.353 1.00 37.52 ? 96  LYS   H CB  1 
ATOM   9678  C  CG  . LYS   H  1 96  ? 34.817  -91.069  -29.911 1.00 37.95 ? 96  LYS   H CG  1 
ATOM   9679  N  N   . ALA   H  1 97  ? 31.579  -89.928  -31.201 1.00 44.02 ? 97  ALA   H N   1 
ATOM   9680  C  CA  . ALA   H  1 97  ? 30.700  -89.037  -30.448 1.00 41.58 ? 97  ALA   H CA  1 
ATOM   9681  C  C   . ALA   H  1 97  ? 29.353  -89.694  -30.173 1.00 32.01 ? 97  ALA   H C   1 
ATOM   9682  O  O   . ALA   H  1 97  ? 28.843  -89.613  -29.056 1.00 38.59 ? 97  ALA   H O   1 
ATOM   9683  C  CB  . ALA   H  1 97  ? 30.523  -87.700  -31.181 1.00 36.46 ? 97  ALA   H CB  1 
ATOM   9684  N  N   . THR   H  1 98  ? 28.775  -90.381  -31.164 1.00 32.86 ? 98  THR   H N   1 
ATOM   9685  C  CA  . THR   H  1 98  ? 27.472  -91.003  -30.959 1.00 36.51 ? 98  THR   H CA  1 
ATOM   9686  C  C   . THR   H  1 98  ? 27.558  -92.176  -29.987 1.00 43.43 ? 98  THR   H C   1 
ATOM   9687  O  O   . THR   H  1 98  ? 26.596  -92.437  -29.260 1.00 35.58 ? 98  THR   H O   1 
ATOM   9688  C  CB  . THR   H  1 98  ? 26.858  -91.484  -32.279 1.00 40.54 ? 98  THR   H CB  1 
ATOM   9689  O  OG1 . THR   H  1 98  ? 27.794  -92.305  -32.980 1.00 39.73 ? 98  THR   H OG1 1 
ATOM   9690  C  CG2 . THR   H  1 98  ? 26.443  -90.314  -33.182 1.00 31.89 ? 98  THR   H CG2 1 
ATOM   9691  N  N   . LYS   H  1 99  ? 28.680  -92.904  -29.974 1.00 43.85 ? 99  LYS   H N   1 
ATOM   9692  C  CA  . LYS   H  1 99  ? 28.875  -93.936  -28.956 1.00 42.88 ? 99  LYS   H CA  1 
ATOM   9693  C  C   . LYS   H  1 99  ? 28.913  -93.324  -27.560 1.00 33.48 ? 99  LYS   H C   1 
ATOM   9694  O  O   . LYS   H  1 99  ? 28.304  -93.851  -26.620 1.00 40.04 ? 99  LYS   H O   1 
ATOM   9695  C  CB  . LYS   H  1 99  ? 30.167  -94.707  -29.229 1.00 37.37 ? 99  LYS   H CB  1 
ATOM   9696  C  CG  . LYS   H  1 99  ? 30.542  -95.697  -28.118 1.00 43.42 ? 99  LYS   H CG  1 
ATOM   9697  N  N   . ASP   H  1 100 ? 29.638  -92.217  -27.397 1.00 34.01 ? 100 ASP   H N   1 
ATOM   9698  C  CA  . ASP   H  1 100 ? 29.703  -91.590  -26.089 1.00 33.37 ? 100 ASP   H CA  1 
ATOM   9699  C  C   . ASP   H  1 100 ? 28.356  -91.024  -25.668 1.00 38.07 ? 100 ASP   H C   1 
ATOM   9700  O  O   . ASP   H  1 100 ? 28.027  -91.046  -24.473 1.00 37.21 ? 100 ASP   H O   1 
ATOM   9701  C  CB  . ASP   H  1 100 ? 30.764  -90.509  -26.094 1.00 36.96 ? 100 ASP   H CB  1 
ATOM   9702  C  CG  . ASP   H  1 100 ? 32.147  -91.080  -26.192 1.00 41.47 ? 100 ASP   H CG  1 
ATOM   9703  O  OD1 . ASP   H  1 100 ? 32.260  -92.321  -26.105 1.00 42.39 ? 100 ASP   H OD1 1 
ATOM   9704  O  OD2 . ASP   H  1 100 ? 33.103  -90.297  -26.345 1.00 34.21 ? 100 ASP   H OD2 1 
ATOM   9705  N  N   . LEU   H  1 101 ? 27.562  -90.535  -26.626 1.00 39.88 ? 101 LEU   H N   1 
ATOM   9706  C  CA  . LEU   H  1 101 ? 26.222  -90.049  -26.301 1.00 34.82 ? 101 LEU   H CA  1 
ATOM   9707  C  C   . LEU   H  1 101 ? 25.337  -91.170  -25.781 1.00 37.88 ? 101 LEU   H C   1 
ATOM   9708  O  O   . LEU   H  1 101 ? 24.598  -90.983  -24.802 1.00 33.06 ? 101 LEU   H O   1 
ATOM   9709  C  CB  . LEU   H  1 101 ? 25.568  -89.397  -27.528 1.00 35.33 ? 101 LEU   H CB  1 
ATOM   9710  C  CG  . LEU   H  1 101 ? 26.109  -88.002  -27.830 1.00 39.43 ? 101 LEU   H CG  1 
ATOM   9711  C  CD1 . LEU   H  1 101 ? 25.838  -87.659  -29.284 1.00 32.40 ? 101 LEU   H CD1 1 
ATOM   9712  C  CD2 . LEU   H  1 101 ? 25.472  -86.963  -26.895 1.00 44.90 ? 101 LEU   H CD2 1 
ATOM   9713  N  N   . ARG   H  1 102 ? 25.361  -92.335  -26.447 1.00 31.88 ? 102 ARG   H N   1 
ATOM   9714  C  CA  . ARG   H  1 102 ? 24.514  -93.443  -25.995 1.00 37.35 ? 102 ARG   H CA  1 
ATOM   9715  C  C   . ARG   H  1 102 ? 24.882  -93.875  -24.582 1.00 35.45 ? 102 ARG   H C   1 
ATOM   9716  O  O   . ARG   H  1 102 ? 23.996  -94.162  -23.767 1.00 41.86 ? 102 ARG   H O   1 
ATOM   9717  C  CB  . ARG   H  1 102 ? 24.613  -94.647  -26.936 1.00 46.90 ? 102 ARG   H CB  1 
ATOM   9718  C  CG  . ARG   H  1 102 ? 24.100  -94.404  -28.337 1.00 41.03 ? 102 ARG   H CG  1 
ATOM   9719  C  CD  . ARG   H  1 102 ? 24.330  -95.599  -29.261 1.00 38.57 ? 102 ARG   H CD  1 
ATOM   9720  N  NE  . ARG   H  1 102 ? 24.464  -95.137  -30.643 1.00 40.06 ? 102 ARG   H NE  1 
ATOM   9721  C  CZ  . ARG   H  1 102 ? 23.458  -94.665  -31.371 1.00 38.76 ? 102 ARG   H CZ  1 
ATOM   9722  N  NH1 . ARG   H  1 102 ? 22.216  -94.646  -30.907 1.00 38.22 ? 102 ARG   H NH1 1 
ATOM   9723  N  NH2 . ARG   H  1 102 ? 23.704  -94.190  -32.591 1.00 41.08 ? 102 ARG   H NH2 1 
ATOM   9724  N  N   . GLU   H  1 103 ? 26.184  -93.944  -24.279 1.00 35.07 ? 103 GLU   H N   1 
ATOM   9725  C  CA  . GLU   H  1 103 ? 26.600  -94.335  -22.934 1.00 43.88 ? 103 GLU   H CA  1 
ATOM   9726  C  C   . GLU   H  1 103 ? 26.146  -93.304  -21.904 1.00 41.60 ? 103 GLU   H C   1 
ATOM   9727  O  O   . GLU   H  1 103 ? 25.772  -93.658  -20.778 1.00 39.31 ? 103 GLU   H O   1 
ATOM   9728  C  CB  . GLU   H  1 103 ? 28.124  -94.512  -22.867 1.00 38.55 ? 103 GLU   H CB  1 
ATOM   9729  C  CG  . GLU   H  1 103 ? 28.675  -95.684  -23.692 1.00 37.27 ? 103 GLU   H CG  1 
ATOM   9730  N  N   . ALA   H  1 104 ? 26.194  -92.019  -22.265 1.00 40.87 ? 104 ALA   H N   1 
ATOM   9731  C  CA  . ALA   H  1 104 ? 25.743  -90.982  -21.347 1.00 33.22 ? 104 ALA   H CA  1 
ATOM   9732  C  C   . ALA   H  1 104 ? 24.232  -91.051  -21.151 1.00 39.01 ? 104 ALA   H C   1 
ATOM   9733  O  O   . ALA   H  1 104 ? 23.739  -90.902  -20.022 1.00 39.04 ? 104 ALA   H O   1 
ATOM   9734  C  CB  . ALA   H  1 104 ? 26.199  -89.606  -21.851 1.00 35.70 ? 104 ALA   H CB  1 
ATOM   9735  N  N   . ILE   H  1 105 ? 23.478  -91.327  -22.217 1.00 34.96 ? 105 ILE   H N   1 
ATOM   9736  C  CA  . ILE   H  1 105 ? 22.039  -91.491  -22.053 1.00 36.41 ? 105 ILE   H CA  1 
ATOM   9737  C  C   . ILE   H  1 105 ? 21.735  -92.664  -21.123 1.00 46.25 ? 105 ILE   H C   1 
ATOM   9738  O  O   . ILE   H  1 105 ? 20.846  -92.570  -20.270 1.00 34.50 ? 105 ILE   H O   1 
ATOM   9739  C  CB  . ILE   H  1 105 ? 21.347  -91.657  -23.412 1.00 36.78 ? 105 ILE   H CB  1 
ATOM   9740  C  CG1 . ILE   H  1 105 ? 21.263  -90.314  -24.148 1.00 36.11 ? 105 ILE   H CG1 1 
ATOM   9741  C  CG2 . ILE   H  1 105 ? 19.986  -92.245  -23.237 1.00 34.99 ? 105 ILE   H CG2 1 
ATOM   9742  C  CD1 . ILE   H  1 105 ? 21.170  -90.471  -25.679 1.00 41.93 ? 105 ILE   H CD1 1 
ATOM   9743  N  N   . VAL   H  1 106 ? 22.444  -93.793  -21.281 1.00 44.53 ? 106 VAL   H N   1 
ATOM   9744  C  CA  . VAL   H  1 106 ? 22.184  -94.945  -20.410 1.00 46.44 ? 106 VAL   H CA  1 
ATOM   9745  C  C   . VAL   H  1 106 ? 22.253  -94.503  -18.953 1.00 33.09 ? 106 VAL   H C   1 
ATOM   9746  O  O   . VAL   H  1 106 ? 21.354  -94.785  -18.146 1.00 41.22 ? 106 VAL   H O   1 
ATOM   9747  C  CB  . VAL   H  1 106 ? 23.178  -96.094  -20.682 1.00 42.59 ? 106 VAL   H CB  1 
ATOM   9748  C  CG1 . VAL   H  1 106 ? 23.035  -97.173  -19.613 1.00 42.05 ? 106 VAL   H CG1 1 
ATOM   9749  C  CG2 . VAL   H  1 106 ? 22.941  -96.731  -22.032 1.00 42.16 ? 106 VAL   H CG2 1 
ATOM   9750  N  N   . HIS   H  1 107 ? 23.301  -93.760  -18.619 1.00 34.94 ? 107 HIS   H N   1 
ATOM   9751  C  CA  . HIS   H  1 107 ? 23.524  -93.353  -17.243 1.00 39.38 ? 107 HIS   H CA  1 
ATOM   9752  C  C   . HIS   H  1 107 ? 22.504  -92.312  -16.789 1.00 45.17 ? 107 HIS   H C   1 
ATOM   9753  O  O   . HIS   H  1 107 ? 21.965  -92.412  -15.680 1.00 38.99 ? 107 HIS   H O   1 
ATOM   9754  C  CB  . HIS   H  1 107 ? 24.930  -92.816  -17.076 1.00 35.02 ? 107 HIS   H CB  1 
ATOM   9755  C  CG  . HIS   H  1 107 ? 25.255  -92.483  -15.656 1.00 48.65 ? 107 HIS   H CG  1 
ATOM   9756  N  ND1 . HIS   H  1 107 ? 25.233  -93.429  -14.653 1.00 47.44 ? 107 HIS   H ND1 1 
ATOM   9757  C  CD2 . HIS   H  1 107 ? 25.519  -91.299  -15.053 1.00 45.81 ? 107 HIS   H CD2 1 
ATOM   9758  C  CE1 . HIS   H  1 107 ? 25.511  -92.848  -13.500 1.00 45.28 ? 107 HIS   H CE1 1 
ATOM   9759  N  NE2 . HIS   H  1 107 ? 25.681  -91.555  -13.714 1.00 48.55 ? 107 HIS   H NE2 1 
ATOM   9760  N  N   . CYS   H  1 108 ? 22.240  -91.290  -17.618 1.00 38.01 ? 108 CYS   H N   1 
ATOM   9761  C  CA  . CYS   H  1 108 ? 21.168  -90.346  -17.292 1.00 33.40 ? 108 CYS   H CA  1 
ATOM   9762  C  C   . CYS   H  1 108 ? 19.876  -91.087  -16.940 1.00 33.96 ? 108 CYS   H C   1 
ATOM   9763  O  O   . CYS   H  1 108 ? 19.163  -90.715  -16.000 1.00 38.29 ? 108 CYS   H O   1 
ATOM   9764  C  CB  . CYS   H  1 108 ? 20.937  -89.379  -18.468 1.00 36.44 ? 108 CYS   H CB  1 
ATOM   9765  S  SG  . CYS   H  1 108 ? 22.235  -88.188  -18.709 1.00 36.58 ? 108 CYS   H SG  1 
ATOM   9766  N  N   . GLU   H  1 109 ? 19.552  -92.141  -17.690 1.00 36.14 ? 109 GLU   H N   1 
ATOM   9767  C  CA  . GLU   H  1 109 ? 18.313  -92.860  -17.422 1.00 33.47 ? 109 GLU   H CA  1 
ATOM   9768  C  C   . GLU   H  1 109 ? 18.378  -93.579  -16.080 1.00 36.15 ? 109 GLU   H C   1 
ATOM   9769  O  O   . GLU   H  1 109 ? 17.421  -93.539  -15.298 1.00 38.27 ? 109 GLU   H O   1 
ATOM   9770  C  CB  . GLU   H  1 109 ? 18.034  -93.856  -18.543 1.00 28.38 ? 109 GLU   H CB  1 
ATOM   9771  C  CG  . GLU   H  1 109 ? 16.780  -94.666  -18.346 1.00 33.25 ? 109 GLU   H CG  1 
ATOM   9772  C  CD  . GLU   H  1 109 ? 15.510  -93.880  -18.655 1.00 37.51 ? 109 GLU   H CD  1 
ATOM   9773  O  OE1 . GLU   H  1 109 ? 15.631  -92.776  -19.223 1.00 34.76 ? 109 GLU   H OE1 1 
ATOM   9774  O  OE2 . GLU   H  1 109 ? 14.393  -94.371  -18.358 1.00 39.25 ? 109 GLU   H OE2 1 
ATOM   9775  N  N   . GLN   H  1 110 ? 19.508  -94.224  -15.797 1.00 44.27 ? 110 GLN   H N   1 
ATOM   9776  C  CA  . GLN   H  1 110 ? 19.682  -94.917  -14.523 1.00 42.30 ? 110 GLN   H CA  1 
ATOM   9777  C  C   . GLN   H  1 110 ? 19.469  -93.978  -13.341 1.00 39.06 ? 110 GLN   H C   1 
ATOM   9778  O  O   . GLN   H  1 110 ? 18.778  -94.328  -12.374 1.00 43.17 ? 110 GLN   H O   1 
ATOM   9779  C  CB  . GLN   H  1 110 ? 21.077  -95.554  -14.477 1.00 36.97 ? 110 GLN   H CB  1 
ATOM   9780  C  CG  . GLN   H  1 110 ? 21.150  -96.803  -15.345 1.00 47.10 ? 110 GLN   H CG  1 
ATOM   9781  C  CD  . GLN   H  1 110 ? 22.554  -97.348  -15.541 1.00 47.01 ? 110 GLN   H CD  1 
ATOM   9782  O  OE1 . GLN   H  1 110 ? 23.556  -96.707  -15.209 1.00 55.21 ? 110 GLN   H OE1 1 
ATOM   9783  N  NE2 . GLN   H  1 110 ? 22.627  -98.549  -16.099 1.00 52.20 ? 110 GLN   H NE2 1 
ATOM   9784  N  N   . VAL   H  1 111 ? 20.052  -92.779  -13.392 1.00 37.28 ? 111 VAL   H N   1 
ATOM   9785  C  CA  . VAL   H  1 111 ? 19.962  -91.864  -12.253 1.00 34.21 ? 111 VAL   H CA  1 
ATOM   9786  C  C   . VAL   H  1 111 ? 18.773  -90.921  -12.383 1.00 30.76 ? 111 VAL   H C   1 
ATOM   9787  O  O   . VAL   H  1 111 ? 18.665  -89.955  -11.621 1.00 36.50 ? 111 VAL   H O   1 
ATOM   9788  C  CB  . VAL   H  1 111 ? 21.248  -91.041  -12.091 1.00 39.90 ? 111 VAL   H CB  1 
ATOM   9789  C  CG1 . VAL   H  1 111 ? 22.459  -91.932  -11.743 1.00 43.35 ? 111 VAL   H CG1 1 
ATOM   9790  C  CG2 . VAL   H  1 111 ? 21.505  -90.204  -13.347 1.00 40.88 ? 111 VAL   H CG2 1 
ATOM   9791  N  N   . HIS   H  1 112 ? 17.918  -91.142  -13.380 1.00 33.26 ? 112 HIS   H N   1 
ATOM   9792  C  CA  . HIS   H  1 112 ? 16.633  -90.453  -13.509 1.00 42.51 ? 112 HIS   H CA  1 
ATOM   9793  C  C   . HIS   H  1 112 ? 16.780  -88.998  -13.925 1.00 36.69 ? 112 HIS   H C   1 
ATOM   9794  O  O   . HIS   H  1 112 ? 15.886  -88.172  -13.656 1.00 30.86 ? 112 HIS   H O   1 
ATOM   9795  C  CB  . HIS   H  1 112 ? 15.833  -90.543  -12.199 1.00 43.66 ? 112 HIS   H CB  1 
ATOM   9796  C  CG  . HIS   H  1 112 ? 15.535  -91.948  -11.792 1.00 45.84 ? 112 HIS   H CG  1 
ATOM   9797  N  ND1 . HIS   H  1 112 ? 15.139  -92.291  -10.519 1.00 55.04 ? 112 HIS   H ND1 1 
ATOM   9798  C  CD2 . HIS   H  1 112 ? 15.573  -93.101  -12.501 1.00 49.29 ? 112 HIS   H CD2 1 
ATOM   9799  C  CE1 . HIS   H  1 112 ? 14.944  -93.597  -10.461 1.00 54.04 ? 112 HIS   H CE1 1 
ATOM   9800  N  NE2 . HIS   H  1 112 ? 15.200  -94.112  -11.650 1.00 51.34 ? 112 HIS   H NE2 1 
ATOM   9801  N  N   . ASP   H  1 113 ? 17.892  -88.658  -14.571 1.00 35.09 ? 113 ASP   H N   1 
ATOM   9802  C  CA  . ASP   H  1 113 ? 18.094  -87.314  -15.089 1.00 35.49 ? 113 ASP   H CA  1 
ATOM   9803  C  C   . ASP   H  1 113 ? 17.523  -87.257  -16.506 1.00 30.67 ? 113 ASP   H C   1 
ATOM   9804  O  O   . ASP   H  1 113 ? 18.237  -87.288  -17.508 1.00 33.67 ? 113 ASP   H O   1 
ATOM   9805  C  CB  . ASP   H  1 113 ? 19.558  -86.934  -15.059 1.00 30.48 ? 113 ASP   H CB  1 
ATOM   9806  C  CG  . ASP   H  1 113 ? 19.761  -85.488  -15.412 1.00 33.39 ? 113 ASP   H CG  1 
ATOM   9807  O  OD1 . ASP   H  1 113 ? 18.762  -84.877  -15.856 1.00 34.68 ? 113 ASP   H OD1 1 
ATOM   9808  O  OD2 . ASP   H  1 113 ? 20.871  -84.959  -15.242 1.00 31.07 ? 113 ASP   H OD2 1 
ATOM   9809  N  N   . TYR   H  1 114 ? 16.196  -87.214  -16.564 1.00 32.23 ? 114 TYR   H N   1 
ATOM   9810  C  CA  . TYR   H  1 114 ? 15.506  -87.306  -17.845 1.00 38.94 ? 114 TYR   H CA  1 
ATOM   9811  C  C   . TYR   H  1 114 ? 15.663  -86.050  -18.704 1.00 33.39 ? 114 TYR   H C   1 
ATOM   9812  O  O   . TYR   H  1 114 ? 15.532  -86.140  -19.937 1.00 33.20 ? 114 TYR   H O   1 
ATOM   9813  C  CB  . TYR   H  1 114 ? 14.034  -87.598  -17.609 1.00 30.68 ? 114 TYR   H CB  1 
ATOM   9814  C  CG  . TYR   H  1 114 ? 13.788  -88.848  -16.806 1.00 39.97 ? 114 TYR   H CG  1 
ATOM   9815  C  CD1 . TYR   H  1 114 ? 14.124  -90.095  -17.308 1.00 37.02 ? 114 TYR   H CD1 1 
ATOM   9816  C  CD2 . TYR   H  1 114 ? 13.202  -88.780  -15.551 1.00 38.82 ? 114 TYR   H CD2 1 
ATOM   9817  C  CE1 . TYR   H  1 114 ? 13.900  -91.243  -16.586 1.00 37.77 ? 114 TYR   H CE1 1 
ATOM   9818  C  CE2 . TYR   H  1 114 ? 12.964  -89.923  -14.815 1.00 36.53 ? 114 TYR   H CE2 1 
ATOM   9819  C  CZ  . TYR   H  1 114 ? 13.321  -91.156  -15.338 1.00 40.96 ? 114 TYR   H CZ  1 
ATOM   9820  O  OH  . TYR   H  1 114 ? 13.096  -92.304  -14.619 1.00 36.90 ? 114 TYR   H OH  1 
ATOM   9821  N  N   . VAL   H  1 115 ? 15.936  -84.892  -18.093 1.00 30.36 ? 115 VAL   H N   1 
ATOM   9822  C  CA  . VAL   H  1 115 ? 16.134  -83.668  -18.873 1.00 34.54 ? 115 VAL   H CA  1 
ATOM   9823  C  C   . VAL   H  1 115 ? 17.479  -83.713  -19.589 1.00 34.82 ? 115 VAL   H C   1 
ATOM   9824  O  O   . VAL   H  1 115 ? 17.578  -83.427  -20.790 1.00 32.61 ? 115 VAL   H O   1 
ATOM   9825  C  CB  . VAL   H  1 115 ? 16.004  -82.423  -17.969 1.00 29.18 ? 115 VAL   H CB  1 
ATOM   9826  C  CG1 . VAL   H  1 115 ? 16.468  -81.158  -18.729 1.00 30.36 ? 115 VAL   H CG1 1 
ATOM   9827  C  CG2 . VAL   H  1 115 ? 14.550  -82.280  -17.470 1.00 32.85 ? 115 VAL   H CG2 1 
ATOM   9828  N  N   . SER   H  1 116 ? 18.539  -84.080  -18.868 1.00 30.99 ? 116 SER   H N   1 
ATOM   9829  C  CA  . SER   H  1 116 ? 19.816  -84.314  -19.527 1.00 33.56 ? 116 SER   H CA  1 
ATOM   9830  C  C   . SER   H  1 116 ? 19.678  -85.369  -20.618 1.00 30.17 ? 116 SER   H C   1 
ATOM   9831  O  O   . SER   H  1 116 ? 20.262  -85.237  -21.699 1.00 34.31 ? 116 SER   H O   1 
ATOM   9832  C  CB  . SER   H  1 116 ? 20.856  -84.737  -18.489 1.00 28.96 ? 116 SER   H CB  1 
ATOM   9833  O  OG  . SER   H  1 116 ? 21.198  -83.645  -17.668 1.00 31.14 ? 116 SER   H OG  1 
ATOM   9834  N  N   . ARG   H  1 117 ? 18.901  -86.418  -20.363 1.00 30.89 ? 117 ARG   H N   1 
ATOM   9835  C  CA  . ARG   H  1 117 ? 18.734  -87.440  -21.388 1.00 31.12 ? 117 ARG   H CA  1 
ATOM   9836  C  C   . ARG   H  1 117 ? 18.116  -86.839  -22.646 1.00 38.47 ? 117 ARG   H C   1 
ATOM   9837  O  O   . ARG   H  1 117 ? 18.596  -87.068  -23.763 1.00 30.84 ? 117 ARG   H O   1 
ATOM   9838  C  CB  . ARG   H  1 117 ? 17.873  -88.584  -20.866 1.00 27.25 ? 117 ARG   H CB  1 
ATOM   9839  C  CG  . ARG   H  1 117 ? 17.338  -89.409  -22.005 1.00 29.33 ? 117 ARG   H CG  1 
ATOM   9840  C  CD  . ARG   H  1 117 ? 16.843  -90.748  -21.616 1.00 33.04 ? 117 ARG   H CD  1 
ATOM   9841  N  NE  . ARG   H  1 117 ? 16.216  -91.397  -22.761 1.00 33.78 ? 117 ARG   H NE  1 
ATOM   9842  C  CZ  . ARG   H  1 117 ? 16.024  -92.706  -22.840 1.00 39.08 ? 117 ARG   H CZ  1 
ATOM   9843  N  NH1 . ARG   H  1 117 ? 16.332  -93.504  -21.829 1.00 31.55 ? 117 ARG   H NH1 1 
ATOM   9844  N  NH2 . ARG   H  1 117 ? 15.533  -93.226  -23.960 1.00 36.53 ? 117 ARG   H NH2 1 
ATOM   9845  N  N   . ASP   H  1 118 ? 17.061  -86.038  -22.470 1.00 29.57 ? 118 ASP   H N   1 
ATOM   9846  C  CA  . ASP   H  1 118 ? 16.379  -85.428  -23.601 1.00 28.55 ? 118 ASP   H CA  1 
ATOM   9847  C  C   . ASP   H  1 118 ? 17.327  -84.541  -24.397 1.00 29.45 ? 118 ASP   H C   1 
ATOM   9848  O  O   . ASP   H  1 118 ? 17.310  -84.556  -25.640 1.00 33.64 ? 118 ASP   H O   1 
ATOM   9849  C  CB  . ASP   H  1 118 ? 15.174  -84.631  -23.104 1.00 29.60 ? 118 ASP   H CB  1 
ATOM   9850  C  CG  . ASP   H  1 118 ? 14.164  -84.383  -24.190 1.00 32.95 ? 118 ASP   H CG  1 
ATOM   9851  O  OD1 . ASP   H  1 118 ? 13.855  -85.340  -24.921 1.00 34.62 ? 118 ASP   H OD1 1 
ATOM   9852  O  OD2 . ASP   H  1 118 ? 13.660  -83.247  -24.292 1.00 40.59 ? 118 ASP   H OD2 1 
ATOM   9853  N  N   . LEU   H  1 119 ? 18.185  -83.786  -23.710 1.00 33.22 ? 119 LEU   H N   1 
ATOM   9854  C  CA  . LEU   H  1 119 ? 19.141  -82.943  -24.416 1.00 36.00 ? 119 LEU   H CA  1 
ATOM   9855  C  C   . LEU   H  1 119 ? 20.134  -83.791  -25.209 1.00 38.29 ? 119 LEU   H C   1 
ATOM   9856  O  O   . LEU   H  1 119 ? 20.425  -83.505  -26.379 1.00 32.82 ? 119 LEU   H O   1 
ATOM   9857  C  CB  . LEU   H  1 119 ? 19.877  -82.032  -23.427 1.00 29.64 ? 119 LEU   H CB  1 
ATOM   9858  C  CG  . LEU   H  1 119 ? 21.090  -81.299  -24.000 1.00 34.90 ? 119 LEU   H CG  1 
ATOM   9859  C  CD1 . LEU   H  1 119 ? 20.644  -80.265  -25.025 1.00 40.39 ? 119 LEU   H CD1 1 
ATOM   9860  C  CD2 . LEU   H  1 119 ? 21.930  -80.648  -22.880 1.00 38.60 ? 119 LEU   H CD2 1 
ATOM   9861  N  N   . LEU   H  1 120 ? 20.681  -84.834  -24.583 1.00 34.05 ? 120 LEU   H N   1 
ATOM   9862  C  CA  . LEU   H  1 120 ? 21.628  -85.690  -25.306 1.00 36.34 ? 120 LEU   H CA  1 
ATOM   9863  C  C   . LEU   H  1 120 ? 20.980  -86.350  -26.513 1.00 32.31 ? 120 LEU   H C   1 
ATOM   9864  O  O   . LEU   H  1 120 ? 21.622  -86.524  -27.563 1.00 33.44 ? 120 LEU   H O   1 
ATOM   9865  C  CB  . LEU   H  1 120 ? 22.188  -86.746  -24.364 1.00 30.68 ? 120 LEU   H CB  1 
ATOM   9866  C  CG  . LEU   H  1 120 ? 22.959  -86.151  -23.222 1.00 31.92 ? 120 LEU   H CG  1 
ATOM   9867  C  CD1 . LEU   H  1 120 ? 23.507  -87.257  -22.306 1.00 40.40 ? 120 LEU   H CD1 1 
ATOM   9868  C  CD2 . LEU   H  1 120 ? 24.085  -85.244  -23.739 1.00 33.33 ? 120 LEU   H CD2 1 
ATOM   9869  N  N   . LYS   H  1 121 ? 19.708  -86.733  -26.379 1.00 29.08 ? 121 LYS   H N   1 
ATOM   9870  C  CA  . LYS   H  1 121 ? 18.990  -87.357  -27.474 1.00 36.35 ? 121 LYS   H CA  1 
ATOM   9871  C  C   . LYS   H  1 121 ? 18.841  -86.407  -28.658 1.00 36.16 ? 121 LYS   H C   1 
ATOM   9872  O  O   . LYS   H  1 121 ? 18.971  -86.825  -29.815 1.00 32.64 ? 121 LYS   H O   1 
ATOM   9873  C  CB  . LYS   H  1 121 ? 17.625  -87.807  -26.981 1.00 35.82 ? 121 LYS   H CB  1 
ATOM   9874  C  CG  . LYS   H  1 121 ? 16.780  -88.514  -28.000 1.00 33.98 ? 121 LYS   H CG  1 
ATOM   9875  C  CD  . LYS   H  1 121 ? 15.887  -87.566  -28.836 1.00 34.10 ? 121 LYS   H CD  1 
ATOM   9876  C  CE  . LYS   H  1 121 ? 14.842  -86.805  -28.013 1.00 40.38 ? 121 LYS   H CE  1 
ATOM   9877  N  NZ  . LYS   H  1 121 ? 14.150  -85.812  -28.913 1.00 44.04 ? 121 LYS   H NZ  1 
ATOM   9878  N  N   . ASP   H  1 122 ? 18.528  -85.137  -28.387 1.00 31.75 ? 122 ASP   H N   1 
ATOM   9879  C  CA  . ASP   H  1 122 ? 18.405  -84.154  -29.461 1.00 34.93 ? 122 ASP   H CA  1 
ATOM   9880  C  C   . ASP   H  1 122 ? 19.734  -83.976  -30.179 1.00 31.94 ? 122 ASP   H C   1 
ATOM   9881  O  O   . ASP   H  1 122 ? 19.780  -83.890  -31.416 1.00 31.03 ? 122 ASP   H O   1 
ATOM   9882  C  CB  . ASP   H  1 122 ? 17.920  -82.808  -28.913 1.00 30.85 ? 122 ASP   H CB  1 
ATOM   9883  C  CG  . ASP   H  1 122 ? 16.455  -82.836  -28.475 1.00 32.84 ? 122 ASP   H CG  1 
ATOM   9884  O  OD1 . ASP   H  1 122 ? 15.686  -83.730  -28.882 1.00 35.82 ? 122 ASP   H OD1 1 
ATOM   9885  O  OD2 . ASP   H  1 122 ? 16.083  -81.939  -27.701 1.00 39.32 ? 122 ASP   H OD2 1 
ATOM   9886  N  N   . ILE   H  1 123 ? 20.822  -83.906  -29.415 1.00 30.01 ? 123 ILE   H N   1 
ATOM   9887  C  CA  . ILE   H  1 123 ? 22.159  -83.821  -29.993 1.00 33.38 ? 123 ILE   H CA  1 
ATOM   9888  C  C   . ILE   H  1 123 ? 22.455  -85.075  -30.806 1.00 33.21 ? 123 ILE   H C   1 
ATOM   9889  O  O   . ILE   H  1 123 ? 22.921  -85.001  -31.949 1.00 37.34 ? 123 ILE   H O   1 
ATOM   9890  C  CB  . ILE   H  1 123 ? 23.187  -83.587  -28.876 1.00 34.60 ? 123 ILE   H CB  1 
ATOM   9891  C  CG1 . ILE   H  1 123 ? 22.929  -82.224  -28.246 1.00 33.28 ? 123 ILE   H CG1 1 
ATOM   9892  C  CG2 . ILE   H  1 123 ? 24.635  -83.660  -29.391 1.00 33.57 ? 123 ILE   H CG2 1 
ATOM   9893  C  CD1 . ILE   H  1 123 ? 23.837  -81.895  -27.096 1.00 31.65 ? 123 ILE   H CD1 1 
ATOM   9894  N  N   . LEU   H  1 124 ? 22.163  -86.243  -30.235 1.00 35.12 ? 124 LEU   H N   1 
ATOM   9895  C  CA  . LEU   H  1 124 ? 22.340  -87.493  -30.970 1.00 36.94 ? 124 LEU   H CA  1 
ATOM   9896  C  C   . LEU   H  1 124 ? 21.599  -87.457  -32.299 1.00 35.40 ? 124 LEU   H C   1 
ATOM   9897  O  O   . LEU   H  1 124 ? 22.123  -87.920  -33.316 1.00 33.80 ? 124 LEU   H O   1 
ATOM   9898  C  CB  . LEU   H  1 124 ? 21.856  -88.674  -30.126 1.00 36.75 ? 124 LEU   H CB  1 
ATOM   9899  C  CG  . LEU   H  1 124 ? 21.891  -90.053  -30.773 1.00 37.04 ? 124 LEU   H CG  1 
ATOM   9900  C  CD1 . LEU   H  1 124 ? 23.336  -90.468  -31.070 1.00 36.13 ? 124 LEU   H CD1 1 
ATOM   9901  C  CD2 . LEU   H  1 124 ? 21.195  -91.077  -29.897 1.00 34.46 ? 124 LEU   H CD2 1 
ATOM   9902  N  N   . GLU   H  1 125 ? 20.382  -86.903  -32.310 1.00 34.36 ? 125 GLU   H N   1 
ATOM   9903  C  CA  . GLU   H  1 125 ? 19.625  -86.785  -33.554 1.00 37.34 ? 125 GLU   H CA  1 
ATOM   9904  C  C   . GLU   H  1 125 ? 20.388  -85.960  -34.581 1.00 29.27 ? 125 GLU   H C   1 
ATOM   9905  O  O   . GLU   H  1 125 ? 20.535  -86.375  -35.739 1.00 32.20 ? 125 GLU   H O   1 
ATOM   9906  C  CB  . GLU   H  1 125 ? 18.232  -86.193  -33.296 1.00 33.54 ? 125 GLU   H CB  1 
ATOM   9907  C  CG  . GLU   H  1 125 ? 17.134  -87.224  -33.332 1.00 43.18 ? 125 GLU   H CG  1 
ATOM   9908  C  CD  . GLU   H  1 125 ? 15.878  -86.851  -32.514 1.00 51.96 ? 125 GLU   H CD  1 
ATOM   9909  O  OE1 . GLU   H  1 125 ? 15.775  -85.701  -32.024 1.00 45.93 ? 125 GLU   H OE1 1 
ATOM   9910  O  OE2 . GLU   H  1 125 ? 14.983  -87.723  -32.371 1.00 46.39 ? 125 GLU   H OE2 1 
ATOM   9911  N  N   . SER   H  1 126 ? 20.927  -84.810  -34.171 1.00 31.56 ? 126 SER   H N   1 
ATOM   9912  C  CA  A SER   H  1 126 ? 21.721  -83.993  -35.085 0.50 35.06 ? 126 SER   H CA  1 
ATOM   9913  C  CA  B SER   H  1 126 ? 21.704  -84.009  -35.108 0.50 35.06 ? 126 SER   H CA  1 
ATOM   9914  C  C   . SER   H  1 126 ? 22.952  -84.753  -35.579 1.00 37.93 ? 126 SER   H C   1 
ATOM   9915  O  O   . SER   H  1 126 ? 23.302  -84.694  -36.767 1.00 30.40 ? 126 SER   H O   1 
ATOM   9916  C  CB  A SER   H  1 126 ? 22.128  -82.691  -34.386 0.50 33.28 ? 126 SER   H CB  1 
ATOM   9917  C  CB  B SER   H  1 126 ? 22.074  -82.678  -34.465 0.50 33.25 ? 126 SER   H CB  1 
ATOM   9918  O  OG  A SER   H  1 126 ? 23.135  -81.993  -35.095 0.50 32.50 ? 126 SER   H OG  1 
ATOM   9919  O  OG  B SER   H  1 126 ? 20.900  -82.032  -34.026 0.50 36.78 ? 126 SER   H OG  1 
ATOM   9920  N  N   . GLU   H  1 127 ? 23.640  -85.466  -34.676 1.00 32.39 ? 127 GLU   H N   1 
ATOM   9921  C  CA  . GLU   H  1 127 ? 24.848  -86.171  -35.111 1.00 33.79 ? 127 GLU   H CA  1 
ATOM   9922  C  C   . GLU   H  1 127 ? 24.515  -87.306  -36.076 1.00 29.19 ? 127 GLU   H C   1 
ATOM   9923  O  O   . GLU   H  1 127 ? 25.291  -87.560  -37.011 1.00 34.32 ? 127 GLU   H O   1 
ATOM   9924  C  CB  . GLU   H  1 127 ? 25.637  -86.707  -33.910 1.00 28.71 ? 127 GLU   H CB  1 
ATOM   9925  C  CG  . GLU   H  1 127 ? 26.052  -85.682  -32.861 1.00 36.56 ? 127 GLU   H CG  1 
ATOM   9926  C  CD  . GLU   H  1 127 ? 26.749  -84.443  -33.431 1.00 47.54 ? 127 GLU   H CD  1 
ATOM   9927  O  OE1 . GLU   H  1 127 ? 27.410  -84.520  -34.486 1.00 49.04 ? 127 GLU   H OE1 1 
ATOM   9928  O  OE2 . GLU   H  1 127 ? 26.664  -83.375  -32.791 1.00 52.39 ? 127 GLU   H OE2 1 
ATOM   9929  N  N   . GLU   H  1 128 ? 23.367  -87.985  -35.907 1.00 31.50 ? 128 GLU   H N   1 
ATOM   9930  C  CA  . GLU   H  1 128 ? 23.030  -89.054  -36.848 1.00 34.20 ? 128 GLU   H CA  1 
ATOM   9931  C  C   . GLU   H  1 128 ? 22.685  -88.490  -38.219 1.00 41.72 ? 128 GLU   H C   1 
ATOM   9932  O  O   . GLU   H  1 128 ? 22.971  -89.124  -39.242 1.00 33.01 ? 128 GLU   H O   1 
ATOM   9933  C  CB  . GLU   H  1 128 ? 21.883  -89.922  -36.334 1.00 32.97 ? 128 GLU   H CB  1 
ATOM   9934  C  CG  . GLU   H  1 128 ? 22.345  -90.893  -35.218 1.00 40.19 ? 128 GLU   H CG  1 
ATOM   9935  C  CD  . GLU   H  1 128 ? 21.342  -91.990  -34.886 1.00 39.57 ? 128 GLU   H CD  1 
ATOM   9936  O  OE1 . GLU   H  1 128 ? 20.331  -92.149  -35.599 1.00 37.77 ? 128 GLU   H OE1 1 
ATOM   9937  O  OE2 . GLU   H  1 128 ? 21.585  -92.721  -33.898 1.00 40.86 ? 128 GLU   H OE2 1 
ATOM   9938  N  N   . GLU   H  1 129 ? 22.045  -87.317  -38.261 1.00 41.29 ? 129 GLU   H N   1 
ATOM   9939  C  CA  . GLU   H  1 129 ? 21.838  -86.644  -39.540 1.00 35.97 ? 129 GLU   H CA  1 
ATOM   9940  C  C   . GLU   H  1 129 ? 23.169  -86.295  -40.186 1.00 32.64 ? 129 GLU   H C   1 
ATOM   9941  O  O   . GLU   H  1 129 ? 23.315  -86.386  -41.409 1.00 33.51 ? 129 GLU   H O   1 
ATOM   9942  C  CB  . GLU   H  1 129 ? 20.998  -85.387  -39.349 1.00 34.81 ? 129 GLU   H CB  1 
ATOM   9943  C  CG  . GLU   H  1 129 ? 19.569  -85.703  -39.167 1.00 44.39 ? 129 GLU   H CG  1 
ATOM   9944  C  CD  . GLU   H  1 129 ? 18.690  -84.469  -39.285 1.00 67.28 ? 129 GLU   H CD  1 
ATOM   9945  O  OE1 . GLU   H  1 129 ? 18.864  -83.691  -40.249 1.00 67.69 ? 129 GLU   H OE1 1 
ATOM   9946  O  OE2 . GLU   H  1 129 ? 17.832  -84.279  -38.407 1.00 51.58 ? 129 GLU   H OE2 1 
ATOM   9947  N  N   . HIS   H  1 130 ? 24.147  -85.888  -39.383 1.00 33.50 ? 130 HIS   H N   1 
ATOM   9948  C  CA  . HIS   H  1 130 ? 25.454  -85.544  -39.934 1.00 37.95 ? 130 HIS   H CA  1 
ATOM   9949  C  C   . HIS   H  1 130 ? 26.158  -86.784  -40.488 1.00 39.06 ? 130 HIS   H C   1 
ATOM   9950  O  O   . HIS   H  1 130 ? 26.843  -86.710  -41.520 1.00 32.64 ? 130 HIS   H O   1 
ATOM   9951  C  CB  . HIS   H  1 130 ? 26.320  -84.859  -38.868 1.00 32.46 ? 130 HIS   H CB  1 
ATOM   9952  C  CG  . HIS   H  1 130 ? 27.586  -84.261  -39.411 1.00 51.01 ? 130 HIS   H CG  1 
ATOM   9953  N  ND1 . HIS   H  1 130 ? 28.653  -83.906  -38.613 1.00 59.61 ? 130 HIS   H ND1 1 
ATOM   9954  C  CD2 . HIS   H  1 130 ? 27.955  -83.959  -40.681 1.00 51.29 ? 130 HIS   H CD2 1 
ATOM   9955  C  CE1 . HIS   H  1 130 ? 29.624  -83.411  -39.364 1.00 51.34 ? 130 HIS   H CE1 1 
ATOM   9956  N  NE2 . HIS   H  1 130 ? 29.223  -83.428  -40.623 1.00 55.10 ? 130 HIS   H NE2 1 
ATOM   9957  N  N   . ILE   H  1 131 ? 26.003  -87.924  -39.806 1.00 35.53 ? 131 ILE   H N   1 
ATOM   9958  C  CA  . ILE   H  1 131 ? 26.533  -89.194  -40.298 1.00 40.54 ? 131 ILE   H CA  1 
ATOM   9959  C  C   . ILE   H  1 131 ? 25.869  -89.574  -41.613 1.00 36.60 ? 131 ILE   H C   1 
ATOM   9960  O  O   . ILE   H  1 131 ? 26.519  -90.083  -42.531 1.00 34.48 ? 131 ILE   H O   1 
ATOM   9961  C  CB  . ILE   H  1 131 ? 26.346  -90.298  -39.237 1.00 38.82 ? 131 ILE   H CB  1 
ATOM   9962  C  CG1 . ILE   H  1 131 ? 27.312  -90.065  -38.061 1.00 31.78 ? 131 ILE   H CG1 1 
ATOM   9963  C  CG2 . ILE   H  1 131 ? 26.511  -91.698  -39.870 1.00 34.60 ? 131 ILE   H CG2 1 
ATOM   9964  C  CD1 . ILE   H  1 131 ? 27.022  -90.932  -36.817 1.00 38.99 ? 131 ILE   H CD1 1 
ATOM   9965  N  N   . ASP   H  1 132 ? 24.563  -89.366  -41.709 1.00 31.93 ? 132 ASP   H N   1 
ATOM   9966  C  CA  . ASP   H  1 132 ? 23.857  -89.632  -42.957 1.00 34.39 ? 132 ASP   H CA  1 
ATOM   9967  C  C   . ASP   H  1 132 ? 24.456  -88.823  -44.097 1.00 37.44 ? 132 ASP   H C   1 
ATOM   9968  O  O   . ASP   H  1 132 ? 24.740  -89.356  -45.176 1.00 36.26 ? 132 ASP   H O   1 
ATOM   9969  C  CB  . ASP   H  1 132 ? 22.371  -89.310  -42.779 1.00 36.90 ? 132 ASP   H CB  1 
ATOM   9970  C  CG  . ASP   H  1 132 ? 21.535  -89.765  -43.942 1.00 38.75 ? 132 ASP   H CG  1 
ATOM   9971  O  OD1 . ASP   H  1 132 ? 22.086  -90.377  -44.891 1.00 45.70 ? 132 ASP   H OD1 1 
ATOM   9972  O  OD2 . ASP   H  1 132 ? 20.322  -89.514  -43.891 1.00 44.37 ? 132 ASP   H OD2 1 
ATOM   9973  N  N   . TYR   H  1 133 ? 24.706  -87.539  -43.854 1.00 33.74 ? 133 TYR   H N   1 
ATOM   9974  C  CA  . TYR   H  1 133 ? 25.292  -86.689  -44.883 1.00 35.18 ? 133 TYR   H CA  1 
ATOM   9975  C  C   . TYR   H  1 133 ? 26.686  -87.178  -45.284 1.00 37.76 ? 133 TYR   H C   1 
ATOM   9976  O  O   . TYR   H  1 133 ? 27.010  -87.251  -46.474 1.00 34.90 ? 133 TYR   H O   1 
ATOM   9977  C  CB  . TYR   H  1 133 ? 25.340  -85.240  -44.384 1.00 32.59 ? 133 TYR   H CB  1 
ATOM   9978  C  CG  . TYR   H  1 133 ? 26.286  -84.368  -45.177 1.00 31.27 ? 133 TYR   H CG  1 
ATOM   9979  C  CD1 . TYR   H  1 133 ? 25.881  -83.732  -46.346 1.00 36.13 ? 133 TYR   H CD1 1 
ATOM   9980  C  CD2 . TYR   H  1 133 ? 27.599  -84.183  -44.751 1.00 37.51 ? 133 TYR   H CD2 1 
ATOM   9981  C  CE1 . TYR   H  1 133 ? 26.785  -82.932  -47.072 1.00 33.43 ? 133 TYR   H CE1 1 
ATOM   9982  C  CE2 . TYR   H  1 133 ? 28.481  -83.414  -45.461 1.00 38.91 ? 133 TYR   H CE2 1 
ATOM   9983  C  CZ  . TYR   H  1 133 ? 28.072  -82.796  -46.620 1.00 31.52 ? 133 TYR   H CZ  1 
ATOM   9984  O  OH  . TYR   H  1 133 ? 28.997  -82.019  -47.285 1.00 39.96 ? 133 TYR   H OH  1 
ATOM   9985  N  N   . LEU   H  1 134 ? 27.532  -87.492  -44.298 1.00 34.44 ? 134 LEU   H N   1 
ATOM   9986  C  CA  . LEU   H  1 134 ? 28.907  -87.919  -44.574 1.00 34.95 ? 134 LEU   H CA  1 
ATOM   9987  C  C   . LEU   H  1 134 ? 28.948  -89.249  -45.316 1.00 31.34 ? 134 LEU   H C   1 
ATOM   9988  O  O   . LEU   H  1 134 ? 29.731  -89.420  -46.257 1.00 36.09 ? 134 LEU   H O   1 
ATOM   9989  C  CB  . LEU   H  1 134 ? 29.679  -88.043  -43.264 1.00 34.49 ? 134 LEU   H CB  1 
ATOM   9990  C  CG  . LEU   H  1 134 ? 29.864  -86.768  -42.463 1.00 36.15 ? 134 LEU   H CG  1 
ATOM   9991  C  CD1 . LEU   H  1 134 ? 30.278  -87.097  -41.056 1.00 37.22 ? 134 LEU   H CD1 1 
ATOM   9992  C  CD2 . LEU   H  1 134 ? 30.891  -85.864  -43.104 1.00 26.72 ? 134 LEU   H CD2 1 
ATOM   9993  N  N   . GLU   H  1 135 ? 28.144  -90.216  -44.889 1.00 33.08 ? 135 GLU   H N   1 
ATOM   9994  C  CA  . GLU   H  1 135 ? 28.120  -91.493  -45.591 1.00 35.11 ? 135 GLU   H CA  1 
ATOM   9995  C  C   . GLU   H  1 135 ? 27.652  -91.293  -47.024 1.00 45.13 ? 135 GLU   H C   1 
ATOM   9996  O  O   . GLU   H  1 135 ? 28.196  -91.891  -47.960 1.00 35.90 ? 135 GLU   H O   1 
ATOM   9997  C  CB  . GLU   H  1 135 ? 27.204  -92.486  -44.876 1.00 34.56 ? 135 GLU   H CB  1 
ATOM   9998  C  CG  . GLU   H  1 135 ? 27.708  -92.987  -43.492 1.00 36.57 ? 135 GLU   H CG  1 
ATOM   9999  C  CD  . GLU   H  1 135 ? 26.661  -93.813  -42.718 1.00 37.75 ? 135 GLU   H CD  1 
ATOM   10000 O  OE1 . GLU   H  1 135 ? 25.434  -93.732  -42.990 1.00 39.83 ? 135 GLU   H OE1 1 
ATOM   10001 O  OE2 . GLU   H  1 135 ? 27.074  -94.549  -41.796 1.00 52.05 ? 135 GLU   H OE2 1 
ATOM   10002 N  N   . THR   H  1 136 ? 26.636  -90.451  -47.209 1.00 42.46 ? 136 THR   H N   1 
ATOM   10003 C  CA  . THR   H  1 136 ? 26.120  -90.192  -48.545 1.00 38.79 ? 136 THR   H CA  1 
ATOM   10004 C  C   . THR   H  1 136 ? 27.190  -89.558  -49.428 1.00 33.87 ? 136 THR   H C   1 
ATOM   10005 O  O   . THR   H  1 136 ? 27.346  -89.940  -50.594 1.00 34.83 ? 136 THR   H O   1 
ATOM   10006 C  CB  . THR   H  1 136 ? 24.866  -89.308  -48.453 1.00 43.28 ? 136 THR   H CB  1 
ATOM   10007 O  OG1 . THR   H  1 136 ? 23.884  -89.941  -47.618 1.00 40.97 ? 136 THR   H OG1 1 
ATOM   10008 C  CG2 . THR   H  1 136 ? 24.247  -89.081  -49.840 1.00 38.04 ? 136 THR   H CG2 1 
ATOM   10009 N  N   . GLN   H  1 137 ? 27.942  -88.598  -48.888 1.00 30.48 ? 137 GLN   H N   1 
ATOM   10010 C  CA  . GLN   H  1 137 ? 29.009  -87.968  -49.653 1.00 35.13 ? 137 GLN   H CA  1 
ATOM   10011 C  C   . GLN   H  1 137 ? 30.097  -88.974  -50.043 1.00 42.40 ? 137 GLN   H C   1 
ATOM   10012 O  O   . GLN   H  1 137 ? 30.632  -88.917  -51.154 1.00 31.61 ? 137 GLN   H O   1 
ATOM   10013 C  CB  . GLN   H  1 137 ? 29.652  -86.819  -48.861 1.00 31.83 ? 137 GLN   H CB  1 
ATOM   10014 C  CG  . GLN   H  1 137 ? 28.726  -85.652  -48.505 1.00 39.29 ? 137 GLN   H CG  1 
ATOM   10015 C  CD  . GLN   H  1 137 ? 27.855  -85.219  -49.660 1.00 31.43 ? 137 GLN   H CD  1 
ATOM   10016 O  OE1 . GLN   H  1 137 ? 28.338  -84.661  -50.656 1.00 36.36 ? 137 GLN   H OE1 1 
ATOM   10017 N  NE2 . GLN   H  1 137 ? 26.569  -85.488  -49.544 1.00 42.21 ? 137 GLN   H NE2 1 
ATOM   10018 N  N   . LEU   H  1 138 ? 30.480  -89.867  -49.125 1.00 36.73 ? 138 LEU   H N   1 
ATOM   10019 C  CA  . LEU   H  1 138 ? 31.561  -90.793  -49.440 1.00 39.21 ? 138 LEU   H CA  1 
ATOM   10020 C  C   . LEU   H  1 138 ? 31.115  -91.795  -50.490 1.00 36.75 ? 138 LEU   H C   1 
ATOM   10021 O  O   . LEU   H  1 138 ? 31.909  -92.186  -51.352 1.00 39.45 ? 138 LEU   H O   1 
ATOM   10022 C  CB  . LEU   H  1 138 ? 32.047  -91.495  -48.171 1.00 37.36 ? 138 LEU   H CB  1 
ATOM   10023 C  CG  . LEU   H  1 138 ? 32.806  -90.559  -47.245 1.00 30.50 ? 138 LEU   H CG  1 
ATOM   10024 C  CD1 . LEU   H  1 138 ? 32.859  -91.035  -45.775 1.00 32.94 ? 138 LEU   H CD1 1 
ATOM   10025 C  CD2 . LEU   H  1 138 ? 34.235  -90.305  -47.773 1.00 38.53 ? 138 LEU   H CD2 1 
ATOM   10026 N  N   . GLY   H  1 139 ? 29.845  -92.180  -50.453 1.00 31.04 ? 139 GLY   H N   1 
ATOM   10027 C  CA  . GLY   H  1 139 ? 29.278  -93.012  -51.499 1.00 39.02 ? 139 GLY   H CA  1 
ATOM   10028 C  C   . GLY   H  1 139 ? 29.149  -92.309  -52.834 1.00 43.53 ? 139 GLY   H C   1 
ATOM   10029 O  O   . GLY   H  1 139 ? 29.271  -92.947  -53.884 1.00 36.76 ? 139 GLY   H O   1 
ATOM   10030 N  N   . LEU   H  1 140 ? 28.901  -90.996  -52.826 1.00 40.94 ? 140 LEU   H N   1 
ATOM   10031 C  CA  . LEU   H  1 140 ? 28.765  -90.287  -54.094 1.00 39.02 ? 140 LEU   H CA  1 
ATOM   10032 C  C   . LEU   H  1 140 ? 30.106  -90.226  -54.803 1.00 38.10 ? 140 LEU   H C   1 
ATOM   10033 O  O   . LEU   H  1 140 ? 30.164  -90.305  -56.036 1.00 36.72 ? 140 LEU   H O   1 
ATOM   10034 C  CB  . LEU   H  1 140 ? 28.206  -88.873  -53.880 1.00 31.86 ? 140 LEU   H CB  1 
ATOM   10035 C  CG  . LEU   H  1 140 ? 26.694  -88.736  -53.745 1.00 31.70 ? 140 LEU   H CG  1 
ATOM   10036 C  CD1 . LEU   H  1 140 ? 26.292  -87.320  -53.307 1.00 38.01 ? 140 LEU   H CD1 1 
ATOM   10037 C  CD2 . LEU   H  1 140 ? 26.004  -89.099  -55.042 1.00 36.76 ? 140 LEU   H CD2 1 
ATOM   10038 N  N   . ILE   H  1 141 ? 31.189  -90.100  -54.028 1.00 36.01 ? 141 ILE   H N   1 
ATOM   10039 C  CA  . ILE   H  1 141 ? 32.541  -90.138  -54.580 1.00 42.70 ? 141 ILE   H CA  1 
ATOM   10040 C  C   . ILE   H  1 141 ? 32.761  -91.407  -55.407 1.00 38.17 ? 141 ILE   H C   1 
ATOM   10041 O  O   . ILE   H  1 141 ? 33.360  -91.358  -56.485 1.00 37.30 ? 141 ILE   H O   1 
ATOM   10042 C  CB  . ILE   H  1 141 ? 33.565  -90.012  -53.442 1.00 37.17 ? 141 ILE   H CB  1 
ATOM   10043 C  CG1 . ILE   H  1 141 ? 33.583  -88.577  -52.923 1.00 38.88 ? 141 ILE   H CG1 1 
ATOM   10044 C  CG2 . ILE   H  1 141 ? 34.962  -90.438  -53.898 1.00 36.64 ? 141 ILE   H CG2 1 
ATOM   10045 C  CD1 . ILE   H  1 141 ? 34.538  -88.324  -51.795 1.00 39.09 ? 141 ILE   H CD1 1 
ATOM   10046 N  N   . GLN   H  1 142 ? 32.290  -92.557  -54.906 1.00 40.94 ? 142 GLN   H N   1 
ATOM   10047 C  CA  . GLN   H  1 142 ? 32.367  -93.806  -55.659 1.00 43.34 ? 142 GLN   H CA  1 
ATOM   10048 C  C   . GLN   H  1 142 ? 31.485  -93.747  -56.894 1.00 43.46 ? 142 GLN   H C   1 
ATOM   10049 O  O   . GLN   H  1 142 ? 31.904  -94.134  -57.986 1.00 44.76 ? 142 GLN   H O   1 
ATOM   10050 C  CB  . GLN   H  1 142 ? 31.934  -94.999  -54.788 1.00 40.66 ? 142 GLN   H CB  1 
ATOM   10051 C  CG  . GLN   H  1 142 ? 32.738  -95.189  -53.507 1.00 43.44 ? 142 GLN   H CG  1 
ATOM   10052 C  CD  . GLN   H  1 142 ? 34.224  -95.286  -53.778 1.00 45.45 ? 142 GLN   H CD  1 
ATOM   10053 O  OE1 . GLN   H  1 142 ? 34.650  -96.062  -54.637 1.00 55.35 ? 142 GLN   H OE1 1 
ATOM   10054 N  NE2 . GLN   H  1 142 ? 35.027  -94.481  -53.066 1.00 48.11 ? 142 GLN   H NE2 1 
ATOM   10055 N  N   . LYS   H  1 143 ? 30.252  -93.279  -56.727 1.00 35.67 ? 143 LYS   H N   1 
ATOM   10056 C  CA  . LYS   H  1 143 ? 29.233  -93.440  -57.752 1.00 36.79 ? 143 LYS   H CA  1 
ATOM   10057 C  C   . LYS   H  1 143 ? 29.476  -92.519  -58.945 1.00 41.54 ? 143 LYS   H C   1 
ATOM   10058 O  O   . LYS   H  1 143 ? 29.271  -92.932  -60.094 1.00 38.94 ? 143 LYS   H O   1 
ATOM   10059 C  CB  . LYS   H  1 143 ? 27.851  -93.185  -57.150 1.00 44.09 ? 143 LYS   H CB  1 
ATOM   10060 C  CG  . LYS   H  1 143 ? 27.313  -94.310  -56.257 1.00 48.05 ? 143 LYS   H CG  1 
ATOM   10061 C  CD  . LYS   H  1 143 ? 25.813  -94.190  -56.015 1.00 48.05 ? 143 LYS   H CD  1 
ATOM   10062 C  CE  . LYS   H  1 143 ? 25.282  -95.274  -55.053 1.00 65.25 ? 143 LYS   H CE  1 
ATOM   10063 N  NZ  . LYS   H  1 143 ? 25.754  -95.151  -53.618 1.00 59.61 ? 143 LYS   H NZ  1 
ATOM   10064 N  N   . VAL   H  1 144 ? 29.889  -91.269  -58.703 1.00 34.31 ? 144 VAL   H N   1 
ATOM   10065 C  CA  . VAL   H  1 144 ? 30.110  -90.309  -59.791 1.00 37.79 ? 144 VAL   H CA  1 
ATOM   10066 C  C   . VAL   H  1 144 ? 31.588  -90.093  -60.109 1.00 39.08 ? 144 VAL   H C   1 
ATOM   10067 O  O   . VAL   H  1 144 ? 31.898  -89.474  -61.140 1.00 39.70 ? 144 VAL   H O   1 
ATOM   10068 C  CB  . VAL   H  1 144 ? 29.427  -88.951  -59.486 1.00 33.84 ? 144 VAL   H CB  1 
ATOM   10069 C  CG1 . VAL   H  1 144 ? 28.004  -89.184  -59.039 1.00 36.46 ? 144 VAL   H CG1 1 
ATOM   10070 C  CG2 . VAL   H  1 144 ? 30.172  -88.158  -58.442 1.00 36.85 ? 144 VAL   H CG2 1 
ATOM   10071 N  N   . GLY   H  1 145 ? 32.500  -90.596  -59.282 1.00 35.10 ? 145 GLY   H N   1 
ATOM   10072 C  CA  . GLY   H  1 145 ? 33.939  -90.391  -59.439 1.00 32.00 ? 145 GLY   H CA  1 
ATOM   10073 C  C   . GLY   H  1 145 ? 34.392  -89.132  -58.736 1.00 42.45 ? 145 GLY   H C   1 
ATOM   10074 O  O   . GLY   H  1 145 ? 33.624  -88.192  -58.525 1.00 40.19 ? 145 GLY   H O   1 
ATOM   10075 N  N   . LEU   H  1 146 ? 35.664  -89.136  -58.323 1.00 34.88 ? 146 LEU   H N   1 
ATOM   10076 C  CA  . LEU   H  1 146 ? 36.175  -88.050  -57.495 1.00 41.46 ? 146 LEU   H CA  1 
ATOM   10077 C  C   . LEU   H  1 146 ? 36.178  -86.729  -58.244 1.00 46.40 ? 146 LEU   H C   1 
ATOM   10078 O  O   . LEU   H  1 146 ? 35.869  -85.679  -57.665 1.00 38.91 ? 146 LEU   H O   1 
ATOM   10079 C  CB  . LEU   H  1 146 ? 37.591  -88.359  -57.035 1.00 34.13 ? 146 LEU   H CB  1 
ATOM   10080 C  CG  . LEU   H  1 146 ? 38.267  -87.361  -56.089 1.00 32.06 ? 146 LEU   H CG  1 
ATOM   10081 C  CD1 . LEU   H  1 146 ? 37.483  -87.151  -54.820 1.00 34.47 ? 146 LEU   H CD1 1 
ATOM   10082 C  CD2 . LEU   H  1 146 ? 39.665  -87.819  -55.722 1.00 42.55 ? 146 LEU   H CD2 1 
ATOM   10083 N  N   . GLU   H  1 147 ? 36.580  -86.751  -59.515 1.00 35.47 ? 147 GLU   H N   1 
ATOM   10084 C  CA  . GLU   H  1 147 ? 36.699  -85.503  -60.267 1.00 38.62 ? 147 GLU   H CA  1 
ATOM   10085 C  C   . GLU   H  1 147 ? 35.332  -84.850  -60.454 1.00 32.40 ? 147 GLU   H C   1 
ATOM   10086 O  O   . GLU   H  1 147 ? 35.200  -83.634  -60.287 1.00 32.42 ? 147 GLU   H O   1 
ATOM   10087 C  CB  . GLU   H  1 147 ? 37.378  -85.749  -61.617 1.00 40.12 ? 147 GLU   H CB  1 
ATOM   10088 C  CG  . GLU   H  1 147 ? 38.897  -85.950  -61.535 1.00 48.13 ? 147 GLU   H CG  1 
ATOM   10089 C  CD  . GLU   H  1 147 ? 39.560  -85.961  -62.920 1.00 62.32 ? 147 GLU   H CD  1 
ATOM   10090 O  OE1 . GLU   H  1 147 ? 38.901  -86.387  -63.895 1.00 52.95 ? 147 GLU   H OE1 1 
ATOM   10091 O  OE2 . GLU   H  1 147 ? 40.731  -85.530  -63.040 1.00 46.97 ? 147 GLU   H OE2 1 
ATOM   10092 N  N   . ASN   H  1 148 ? 34.304  -85.647  -60.760 1.00 38.46 ? 148 ASN   H N   1 
ATOM   10093 C  CA  . ASN   H  1 148 ? 32.941  -85.123  -60.811 1.00 30.91 ? 148 ASN   H CA  1 
ATOM   10094 C  C   . ASN   H  1 148 ? 32.439  -84.691  -59.439 1.00 37.90 ? 148 ASN   H C   1 
ATOM   10095 O  O   . ASN   H  1 148 ? 31.652  -83.739  -59.329 1.00 32.92 ? 148 ASN   H O   1 
ATOM   10096 C  CB  . ASN   H  1 148 ? 31.976  -86.163  -61.368 1.00 32.15 ? 148 ASN   H CB  1 
ATOM   10097 C  CG  . ASN   H  1 148 ? 31.893  -86.135  -62.876 1.00 33.35 ? 148 ASN   H CG  1 
ATOM   10098 O  OD1 . ASN   H  1 148 ? 32.586  -85.367  -63.546 1.00 30.18 ? 148 ASN   H OD1 1 
ATOM   10099 N  ND2 . ASN   H  1 148 ? 31.064  -86.992  -63.418 1.00 30.69 ? 148 ASN   H ND2 1 
ATOM   10100 N  N   . TYR   H  1 149 ? 32.793  -85.435  -58.394 1.00 33.60 ? 149 TYR   H N   1 
ATOM   10101 C  CA  . TYR   H  1 149 ? 32.308  -85.079  -57.068 1.00 32.92 ? 149 TYR   H CA  1 
ATOM   10102 C  C   . TYR   H  1 149 ? 32.882  -83.739  -56.633 1.00 28.98 ? 149 TYR   H C   1 
ATOM   10103 O  O   . TYR   H  1 149 ? 32.140  -82.870  -56.164 1.00 33.47 ? 149 TYR   H O   1 
ATOM   10104 C  CB  . TYR   H  1 149 ? 32.636  -86.160  -56.029 1.00 35.38 ? 149 TYR   H CB  1 
ATOM   10105 C  CG  . TYR   H  1 149 ? 32.171  -85.748  -54.634 1.00 33.62 ? 149 TYR   H CG  1 
ATOM   10106 C  CD1 . TYR   H  1 149 ? 30.876  -85.996  -54.225 1.00 35.49 ? 149 TYR   H CD1 1 
ATOM   10107 C  CD2 . TYR   H  1 149 ? 33.021  -85.084  -53.753 1.00 36.05 ? 149 TYR   H CD2 1 
ATOM   10108 C  CE1 . TYR   H  1 149 ? 30.433  -85.610  -52.981 1.00 33.15 ? 149 TYR   H CE1 1 
ATOM   10109 C  CE2 . TYR   H  1 149 ? 32.582  -84.696  -52.499 1.00 35.99 ? 149 TYR   H CE2 1 
ATOM   10110 C  CZ  . TYR   H  1 149 ? 31.285  -84.960  -52.125 1.00 36.22 ? 149 TYR   H CZ  1 
ATOM   10111 O  OH  . TYR   H  1 149 ? 30.812  -84.585  -50.891 1.00 39.88 ? 149 TYR   H OH  1 
ATOM   10112 N  N   . LEU   H  1 150 ? 34.186  -83.531  -56.821 1.00 27.71 ? 150 LEU   H N   1 
ATOM   10113 C  CA  . LEU   H  1 150 ? 34.773  -82.240  -56.477 1.00 36.87 ? 150 LEU   H CA  1 
ATOM   10114 C  C   . LEU   H  1 150 ? 34.208  -81.127  -57.351 1.00 35.48 ? 150 LEU   H C   1 
ATOM   10115 O  O   . LEU   H  1 150 ? 33.914  -80.030  -56.861 1.00 33.79 ? 150 LEU   H O   1 
ATOM   10116 C  CB  . LEU   H  1 150 ? 36.291  -82.283  -56.591 1.00 29.81 ? 150 LEU   H CB  1 
ATOM   10117 C  CG  . LEU   H  1 150 ? 36.991  -83.320  -55.696 1.00 40.23 ? 150 LEU   H CG  1 
ATOM   10118 C  CD1 . LEU   H  1 150 ? 38.474  -83.377  -55.998 1.00 38.34 ? 150 LEU   H CD1 1 
ATOM   10119 C  CD2 . LEU   H  1 150 ? 36.750  -83.026  -54.178 1.00 42.57 ? 150 LEU   H CD2 1 
ATOM   10120 N  N   . GLN   H  1 151 ? 34.042  -81.393  -58.645 1.00 34.29 ? 151 GLN   H N   1 
ATOM   10121 C  CA  . GLN   H  1 151 ? 33.484  -80.388  -59.548 1.00 33.66 ? 151 GLN   H CA  1 
ATOM   10122 C  C   . GLN   H  1 151 ? 32.127  -79.900  -59.048 1.00 31.15 ? 151 GLN   H C   1 
ATOM   10123 O  O   . GLN   H  1 151 ? 31.831  -78.702  -59.075 1.00 32.26 ? 151 GLN   H O   1 
ATOM   10124 C  CB  . GLN   H  1 151 ? 33.354  -80.971  -60.949 1.00 35.88 ? 151 GLN   H CB  1 
ATOM   10125 C  CG  . GLN   H  1 151 ? 32.563  -80.106  -61.919 1.00 33.45 ? 151 GLN   H CG  1 
ATOM   10126 C  CD  . GLN   H  1 151 ? 32.384  -80.781  -63.269 1.00 34.38 ? 151 GLN   H CD  1 
ATOM   10127 O  OE1 . GLN   H  1 151 ? 32.096  -81.979  -63.357 1.00 32.35 ? 151 GLN   H OE1 1 
ATOM   10128 N  NE2 . GLN   H  1 151 ? 32.537  -80.003  -64.330 1.00 34.36 ? 151 GLN   H NE2 1 
ATOM   10129 N  N   . SER   H  1 152 ? 31.280  -80.829  -58.623 1.00 30.70 ? 152 SER   H N   1 
ATOM   10130 C  CA  . SER   H  1 152 ? 29.962  -80.509  -58.104 1.00 36.76 ? 152 SER   H CA  1 
ATOM   10131 C  C   . SER   H  1 152 ? 29.994  -79.698  -56.817 1.00 39.22 ? 152 SER   H C   1 
ATOM   10132 O  O   . SER   H  1 152 ? 28.945  -79.177  -56.424 1.00 36.22 ? 152 SER   H O   1 
ATOM   10133 C  CB  . SER   H  1 152 ? 29.182  -81.796  -57.868 1.00 30.87 ? 152 SER   H CB  1 
ATOM   10134 O  OG  . SER   H  1 152 ? 28.760  -82.336  -59.099 1.00 36.44 ? 152 SER   H OG  1 
ATOM   10135 N  N   . HIS   H  1 153 ? 31.148  -79.568  -56.154 1.00 34.94 ? 153 HIS   H N   1 
ATOM   10136 C  CA  . HIS   H  1 153 ? 31.231  -78.810  -54.908 1.00 35.09 ? 153 HIS   H CA  1 
ATOM   10137 C  C   . HIS   H  1 153 ? 32.117  -77.578  -55.020 1.00 28.58 ? 153 HIS   H C   1 
ATOM   10138 O  O   . HIS   H  1 153 ? 32.483  -76.990  -53.999 1.00 33.08 ? 153 HIS   H O   1 
ATOM   10139 C  CB  . HIS   H  1 153 ? 31.693  -79.725  -53.765 1.00 32.70 ? 153 HIS   H CB  1 
ATOM   10140 C  CG  . HIS   H  1 153 ? 30.655  -80.730  -53.386 1.00 28.62 ? 153 HIS   H CG  1 
ATOM   10141 N  ND1 . HIS   H  1 153 ? 30.457  -81.896  -54.098 1.00 40.61 ? 153 HIS   H ND1 1 
ATOM   10142 C  CD2 . HIS   H  1 153 ? 29.684  -80.703  -52.439 1.00 30.04 ? 153 HIS   H CD2 1 
ATOM   10143 C  CE1 . HIS   H  1 153 ? 29.432  -82.556  -53.591 1.00 36.80 ? 153 HIS   H CE1 1 
ATOM   10144 N  NE2 . HIS   H  1 153 ? 28.947  -81.854  -52.579 1.00 35.45 ? 153 HIS   H NE2 1 
ATOM   10145 N  N   . MET   H  1 154 ? 32.435  -77.138  -56.236 1.00 28.81 ? 154 MET   H N   1 
ATOM   10146 C  CA  . MET   H  1 154 ? 33.196  -75.898  -56.421 1.00 35.00 ? 154 MET   H CA  1 
ATOM   10147 C  C   . MET   H  1 154 ? 32.371  -74.662  -56.066 1.00 40.02 ? 154 MET   H C   1 
ATOM   10148 O  O   . MET   H  1 154 ? 32.838  -73.771  -55.348 1.00 36.28 ? 154 MET   H O   1 
ATOM   10149 C  CB  . MET   H  1 154 ? 33.683  -75.779  -57.874 1.00 31.09 ? 154 MET   H CB  1 
ATOM   10150 C  CG  . MET   H  1 154 ? 34.901  -76.628  -58.220 1.00 43.48 ? 154 MET   H CG  1 
ATOM   10151 S  SD  . MET   H  1 154 ? 35.328  -76.689  -59.986 1.00 49.72 ? 154 MET   H SD  1 
ATOM   10152 C  CE  . MET   H  1 154 ? 35.221  -74.941  -60.428 1.00 42.85 ? 154 MET   H CE  1 
ATOM   10153 N  N   . HIS   H  1 155 ? 31.170  -74.560  -56.618 1.00 42.54 ? 155 HIS   H N   1 
ATOM   10154 C  CA  . HIS   H  1 155 ? 30.334  -73.375  -56.489 1.00 52.57 ? 155 HIS   H CA  1 
ATOM   10155 C  C   . HIS   H  1 155 ? 29.130  -73.672  -55.601 1.00 49.48 ? 155 HIS   H C   1 
ATOM   10156 O  O   . HIS   H  1 155 ? 28.543  -74.757  -55.676 1.00 58.21 ? 155 HIS   H O   1 
ATOM   10157 C  CB  . HIS   H  1 155 ? 29.844  -72.909  -57.869 1.00 50.17 ? 155 HIS   H CB  1 
ATOM   10158 C  CG  . HIS   H  1 155 ? 30.940  -72.691  -58.870 1.00 49.30 ? 155 HIS   H CG  1 
ATOM   10159 N  ND1 . HIS   H  1 155 ? 30.846  -73.111  -60.182 1.00 49.63 ? 155 HIS   H ND1 1 
ATOM   10160 C  CD2 . HIS   H  1 155 ? 32.146  -72.081  -58.757 1.00 58.55 ? 155 HIS   H CD2 1 
ATOM   10161 C  CE1 . HIS   H  1 155 ? 31.947  -72.772  -60.830 1.00 45.16 ? 155 HIS   H CE1 1 
ATOM   10162 N  NE2 . HIS   H  1 155 ? 32.753  -72.148  -59.989 1.00 55.46 ? 155 HIS   H NE2 1 
ATOM   10163 N  N   . GLU   H  1 156 ? 28.752  -72.708  -54.766 1.00 54.06 ? 156 GLU   H N   1 
ATOM   10164 C  CA  . GLU   H  1 156 ? 27.425  -72.767  -54.136 1.00 64.91 ? 156 GLU   H CA  1 
ATOM   10165 C  C   . GLU   H  1 156 ? 26.377  -72.209  -55.104 1.00 55.31 ? 156 GLU   H C   1 
ATOM   10166 O  O   . GLU   H  1 156 ? 25.494  -72.926  -55.565 1.00 64.94 ? 156 GLU   H O   1 
ATOM   10167 C  CB  . GLU   H  1 156 ? 27.377  -71.980  -52.828 1.00 68.13 ? 156 GLU   H CB  1 
ATOM   10168 C  CG  . GLU   H  1 156 ? 28.728  -71.627  -52.217 1.00 53.89 ? 156 GLU   H CG  1 
ATOM   10169 C  CD  . GLU   H  1 156 ? 28.555  -70.899  -50.905 1.00 63.61 ? 156 GLU   H CD  1 
ATOM   10170 O  OE1 . GLU   H  1 156 ? 27.536  -71.162  -50.223 1.00 68.43 ? 156 GLU   H OE1 1 
ATOM   10171 O  OE2 . GLU   H  1 156 ? 29.414  -70.054  -50.566 1.00 60.38 ? 156 GLU   H OE2 1 
ATOM   10172 N  N   . MET   I  1 1   ? -50.356 -30.693  -47.453 1.00 42.40 ? 1   MET   I N   1 
ATOM   10173 C  CA  . MET   I  1 1   ? -51.351 -30.751  -48.571 1.00 43.40 ? 1   MET   I CA  1 
ATOM   10174 C  C   . MET   I  1 1   ? -52.630 -31.444  -48.070 1.00 38.88 ? 1   MET   I C   1 
ATOM   10175 O  O   . MET   I  1 1   ? -52.578 -32.583  -47.618 1.00 38.18 ? 1   MET   I O   1 
ATOM   10176 C  CB  . MET   I  1 1   ? -50.731 -31.490  -49.755 1.00 36.37 ? 1   MET   I CB  1 
ATOM   10177 C  CG  . MET   I  1 1   ? -51.527 -31.460  -51.036 1.00 42.73 ? 1   MET   I CG  1 
ATOM   10178 S  SD  . MET   I  1 1   ? -50.679 -32.411  -52.315 1.00 43.03 ? 1   MET   I SD  1 
ATOM   10179 C  CE  . MET   I  1 1   ? -51.064 -34.090  -51.923 1.00 36.53 ? 1   MET   I CE  1 
ATOM   10180 N  N   . LYS   I  1 2   ? -53.774 -30.766  -48.113 1.00 45.62 ? 2   LYS   I N   1 
ATOM   10181 C  CA  . LYS   I  1 2   ? -54.967 -31.328  -47.479 1.00 36.09 ? 2   LYS   I CA  1 
ATOM   10182 C  C   . LYS   I  1 2   ? -55.347 -32.642  -48.136 1.00 33.59 ? 2   LYS   I C   1 
ATOM   10183 O  O   . LYS   I  1 2   ? -55.715 -32.683  -49.314 1.00 38.58 ? 2   LYS   I O   1 
ATOM   10184 C  CB  . LYS   I  1 2   ? -56.134 -30.337  -47.531 1.00 44.16 ? 2   LYS   I CB  1 
ATOM   10185 N  N   . GLY   I  1 3   ? -55.273 -33.728  -47.366 1.00 33.40 ? 3   GLY   I N   1 
ATOM   10186 C  CA  . GLY   I  1 3   ? -55.620 -35.026  -47.891 1.00 37.99 ? 3   GLY   I CA  1 
ATOM   10187 C  C   . GLY   I  1 3   ? -57.095 -35.362  -47.720 1.00 35.79 ? 3   GLY   I C   1 
ATOM   10188 O  O   . GLY   I  1 3   ? -57.842 -34.669  -47.033 1.00 34.57 ? 3   GLY   I O   1 
ATOM   10189 N  N   . ASP   I  1 4   ? -57.483 -36.469  -48.338 1.00 39.80 ? 4   ASP   I N   1 
ATOM   10190 C  CA  . ASP   I  1 4   ? -58.835 -36.995  -48.186 1.00 39.45 ? 4   ASP   I CA  1 
ATOM   10191 C  C   . ASP   I  1 4   ? -59.010 -37.597  -46.800 1.00 41.01 ? 4   ASP   I C   1 
ATOM   10192 O  O   . ASP   I  1 4   ? -58.224 -38.449  -46.369 1.00 31.79 ? 4   ASP   I O   1 
ATOM   10193 C  CB  . ASP   I  1 4   ? -59.101 -38.050  -49.253 1.00 35.41 ? 4   ASP   I CB  1 
ATOM   10194 C  CG  . ASP   I  1 4   ? -60.480 -38.698  -49.120 1.00 43.43 ? 4   ASP   I CG  1 
ATOM   10195 O  OD1 . ASP   I  1 4   ? -61.462 -38.063  -49.552 1.00 49.50 ? 4   ASP   I OD1 1 
ATOM   10196 O  OD2 . ASP   I  1 4   ? -60.576 -39.840  -48.608 1.00 40.44 ? 4   ASP   I OD2 1 
ATOM   10197 N  N   . LYS   I  1 5   ? -60.066 -37.181  -46.102 1.00 40.10 ? 5   LYS   I N   1 
ATOM   10198 C  CA  . LYS   I  1 5   ? -60.211 -37.593  -44.711 1.00 34.51 ? 5   LYS   I CA  1 
ATOM   10199 C  C   . LYS   I  1 5   ? -60.255 -39.106  -44.581 1.00 33.44 ? 5   LYS   I C   1 
ATOM   10200 O  O   . LYS   I  1 5   ? -59.727 -39.668  -43.615 1.00 34.56 ? 5   LYS   I O   1 
ATOM   10201 C  CB  . LYS   I  1 5   ? -61.465 -36.969  -44.097 1.00 39.44 ? 5   LYS   I CB  1 
ATOM   10202 C  CG  . LYS   I  1 5   ? -61.270 -35.513  -43.700 1.00 55.38 ? 5   LYS   I CG  1 
ATOM   10203 N  N   . LYS   I  1 6   ? -60.882 -39.787  -45.531 1.00 27.71 ? 6   LYS   I N   1 
ATOM   10204 C  CA  . LYS   I  1 6   ? -61.030 -41.231  -45.413 1.00 34.90 ? 6   LYS   I CA  1 
ATOM   10205 C  C   . LYS   I  1 6   ? -59.732 -41.964  -45.761 1.00 33.79 ? 6   LYS   I C   1 
ATOM   10206 O  O   . LYS   I  1 6   ? -59.468 -43.053  -45.226 1.00 33.98 ? 6   LYS   I O   1 
ATOM   10207 C  CB  . LYS   I  1 6   ? -62.184 -41.691  -46.312 1.00 43.34 ? 6   LYS   I CB  1 
ATOM   10208 C  CG  . LYS   I  1 6   ? -62.440 -43.176  -46.284 1.00 46.42 ? 6   LYS   I CG  1 
ATOM   10209 C  CD  . LYS   I  1 6   ? -62.933 -43.634  -44.923 1.00 48.65 ? 6   LYS   I CD  1 
ATOM   10210 C  CE  . LYS   I  1 6   ? -63.113 -45.142  -44.891 1.00 52.50 ? 6   LYS   I CE  1 
ATOM   10211 N  NZ  . LYS   I  1 6   ? -63.653 -45.609  -43.575 1.00 65.73 ? 6   LYS   I NZ  1 
ATOM   10212 N  N   . VAL   I  1 7   ? -58.925 -41.382  -46.647 1.00 32.69 ? 7   VAL   I N   1 
ATOM   10213 C  CA  . VAL   I  1 7   ? -57.548 -41.841  -46.834 1.00 29.15 ? 7   VAL   I CA  1 
ATOM   10214 C  C   . VAL   I  1 7   ? -56.797 -41.806  -45.509 1.00 23.50 ? 7   VAL   I C   1 
ATOM   10215 O  O   . VAL   I  1 7   ? -56.195 -42.800  -45.092 1.00 31.21 ? 7   VAL   I O   1 
ATOM   10216 C  CB  . VAL   I  1 7   ? -56.851 -40.978  -47.893 1.00 33.62 ? 7   VAL   I CB  1 
ATOM   10217 C  CG1 . VAL   I  1 7   ? -55.323 -41.200  -47.851 1.00 36.08 ? 7   VAL   I CG1 1 
ATOM   10218 C  CG2 . VAL   I  1 7   ? -57.436 -41.278  -49.263 1.00 36.67 ? 7   VAL   I CG2 1 
ATOM   10219 N  N   . ILE   I  1 8   ? -56.839 -40.662  -44.822 1.00 28.56 ? 8   ILE   I N   1 
ATOM   10220 C  CA  . ILE   I  1 8   ? -56.142 -40.531  -43.543 1.00 30.75 ? 8   ILE   I CA  1 
ATOM   10221 C  C   . ILE   I  1 8   ? -56.641 -41.556  -42.528 1.00 37.62 ? 8   ILE   I C   1 
ATOM   10222 O  O   . ILE   I  1 8   ? -55.842 -42.139  -41.779 1.00 30.91 ? 8   ILE   I O   1 
ATOM   10223 C  CB  . ILE   I  1 8   ? -56.271 -39.093  -43.009 1.00 29.27 ? 8   ILE   I CB  1 
ATOM   10224 C  CG1 . ILE   I  1 8   ? -55.440 -38.156  -43.879 1.00 30.37 ? 8   ILE   I CG1 1 
ATOM   10225 C  CG2 . ILE   I  1 8   ? -55.809 -39.017  -41.558 1.00 28.98 ? 8   ILE   I CG2 1 
ATOM   10226 C  CD1 . ILE   I  1 8   ? -55.875 -36.705  -43.781 1.00 33.40 ? 8   ILE   I CD1 1 
ATOM   10227 N  N   . GLN   I  1 9   ? -57.964 -41.785  -42.466 1.00 30.73 ? 9   GLN   I N   1 
ATOM   10228 C  CA  . GLN   I  1 9   ? -58.490 -42.780  -41.539 1.00 29.36 ? 9   GLN   I CA  1 
ATOM   10229 C  C   . GLN   I  1 9   ? -57.971 -44.148  -41.884 1.00 27.77 ? 9   GLN   I C   1 
ATOM   10230 O  O   . GLN   I  1 9   ? -57.598 -44.926  -40.991 1.00 29.79 ? 9   GLN   I O   1 
ATOM   10231 C  CB  . GLN   I  1 9   ? -60.033 -42.808  -41.545 1.00 34.34 ? 9   GLN   I CB  1 
ATOM   10232 C  CG  . GLN   I  1 9   ? -60.628 -41.597  -40.946 1.00 32.58 ? 9   GLN   I CG  1 
ATOM   10233 C  CD  . GLN   I  1 9   ? -62.136 -41.551  -41.123 1.00 45.84 ? 9   GLN   I CD  1 
ATOM   10234 O  OE1 . GLN   I  1 9   ? -62.685 -42.184  -42.019 1.00 44.93 ? 9   GLN   I OE1 1 
ATOM   10235 N  NE2 . GLN   I  1 9   ? -62.806 -40.811  -40.256 1.00 44.54 ? 9   GLN   I NE2 1 
ATOM   10236 N  N   . HIS   I  1 10  ? -57.917 -44.447  -43.184 1.00 28.89 ? 10  HIS   I N   1 
ATOM   10237 C  CA  . HIS   I  1 10  ? -57.354 -45.709  -43.637 1.00 31.04 ? 10  HIS   I CA  1 
ATOM   10238 C  C   . HIS   I  1 10  ? -55.882 -45.816  -43.267 1.00 24.96 ? 10  HIS   I C   1 
ATOM   10239 O  O   . HIS   I  1 10  ? -55.426 -46.874  -42.811 1.00 27.23 ? 10  HIS   I O   1 
ATOM   10240 C  CB  . HIS   I  1 10  ? -57.484 -45.837  -45.149 1.00 33.99 ? 10  HIS   I CB  1 
ATOM   10241 C  CG  . HIS   I  1 10  ? -58.709 -46.540  -45.606 1.00 31.26 ? 10  HIS   I CG  1 
ATOM   10242 N  ND1 . HIS   I  1 10  ? -58.909 -47.891  -45.418 1.00 36.49 ? 10  HIS   I ND1 1 
ATOM   10243 C  CD2 . HIS   I  1 10  ? -59.794 -46.082  -46.273 1.00 33.93 ? 10  HIS   I CD2 1 
ATOM   10244 C  CE1 . HIS   I  1 10  ? -60.070 -48.233  -45.955 1.00 41.88 ? 10  HIS   I CE1 1 
ATOM   10245 N  NE2 . HIS   I  1 10  ? -60.628 -47.151  -46.467 1.00 35.88 ? 10  HIS   I NE2 1 
ATOM   10246 N  N   . LEU   I  1 11  ? -55.124 -44.744  -43.480 1.00 30.03 ? 11  LEU   I N   1 
ATOM   10247 C  CA  . LEU   I  1 11  ? -53.703 -44.775  -43.095 1.00 32.48 ? 11  LEU   I CA  1 
ATOM   10248 C  C   . LEU   I  1 11  ? -53.554 -45.002  -41.586 1.00 33.71 ? 11  LEU   I C   1 
ATOM   10249 O  O   . LEU   I  1 11  ? -52.711 -45.794  -41.144 1.00 33.68 ? 11  LEU   I O   1 
ATOM   10250 C  CB  . LEU   I  1 11  ? -53.020 -43.477  -43.529 1.00 29.91 ? 11  LEU   I CB  1 
ATOM   10251 C  CG  . LEU   I  1 11  ? -52.943 -43.180  -45.042 1.00 28.36 ? 11  LEU   I CG  1 
ATOM   10252 C  CD1 . LEU   I  1 11  ? -52.328 -41.816  -45.351 1.00 26.73 ? 11  LEU   I CD1 1 
ATOM   10253 C  CD2 . LEU   I  1 11  ? -52.201 -44.273  -45.751 1.00 35.35 ? 11  LEU   I CD2 1 
ATOM   10254 N  N   . ASN   I  1 12  ? -54.392 -44.340  -40.773 1.00 33.01 ? 12  ASN   I N   1 
ATOM   10255 C  CA  . ASN   I  1 12  ? -54.349 -44.585  -39.329 1.00 30.71 ? 12  ASN   I CA  1 
ATOM   10256 C  C   . ASN   I  1 12  ? -54.749 -46.017  -38.976 1.00 35.65 ? 12  ASN   I C   1 
ATOM   10257 O  O   . ASN   I  1 12  ? -54.188 -46.610  -38.041 1.00 28.82 ? 12  ASN   I O   1 
ATOM   10258 C  CB  . ASN   I  1 12  ? -55.222 -43.560  -38.607 1.00 32.47 ? 12  ASN   I CB  1 
ATOM   10259 C  CG  . ASN   I  1 12  ? -54.438 -42.349  -38.187 1.00 30.58 ? 12  ASN   I CG  1 
ATOM   10260 O  OD1 . ASN   I  1 12  ? -53.262 -42.464  -37.814 1.00 32.84 ? 12  ASN   I OD1 1 
ATOM   10261 N  ND2 . ASN   I  1 12  ? -55.062 -41.184  -38.230 1.00 28.67 ? 12  ASN   I ND2 1 
ATOM   10262 N  N   . LYS   I  1 13  ? -55.660 -46.621  -39.732 1.00 35.24 ? 13  LYS   I N   1 
ATOM   10263 C  CA  . LYS   I  1 13  ? -55.957 -48.023  -39.467 1.00 31.54 ? 13  LYS   I CA  1 
ATOM   10264 C  C   . LYS   I  1 13  ? -54.758 -48.898  -39.796 1.00 29.39 ? 13  LYS   I C   1 
ATOM   10265 O  O   . LYS   I  1 13  ? -54.448 -49.851  -39.065 1.00 28.32 ? 13  LYS   I O   1 
ATOM   10266 C  CB  . LYS   I  1 13  ? -57.196 -48.471  -40.263 1.00 27.14 ? 13  LYS   I CB  1 
ATOM   10267 C  CG  . LYS   I  1 13  ? -57.610 -49.909  -39.930 1.00 36.13 ? 13  LYS   I CG  1 
ATOM   10268 C  CD  . LYS   I  1 13  ? -58.983 -50.311  -40.474 1.00 38.19 ? 13  LYS   I CD  1 
ATOM   10269 C  CE  . LYS   I  1 13  ? -59.420 -51.620  -39.815 1.00 41.49 ? 13  LYS   I CE  1 
ATOM   10270 N  NZ  . LYS   I  1 13  ? -60.647 -52.207  -40.436 1.00 50.30 ? 13  LYS   I NZ  1 
ATOM   10271 N  N   . ILE   I  1 14  ? -54.066 -48.602  -40.895 1.00 32.10 ? 14  ILE   I N   1 
ATOM   10272 C  CA  . ILE   I  1 14  ? -52.865 -49.372  -41.210 1.00 29.38 ? 14  ILE   I CA  1 
ATOM   10273 C  C   . ILE   I  1 14  ? -51.810 -49.146  -40.132 1.00 26.89 ? 14  ILE   I C   1 
ATOM   10274 O  O   . ILE   I  1 14  ? -51.202 -50.087  -39.631 1.00 30.99 ? 14  ILE   I O   1 
ATOM   10275 C  CB  . ILE   I  1 14  ? -52.341 -49.011  -42.612 1.00 32.82 ? 14  ILE   I CB  1 
ATOM   10276 C  CG1 . ILE   I  1 14  ? -53.454 -49.134  -43.667 1.00 35.79 ? 14  ILE   I CG1 1 
ATOM   10277 C  CG2 . ILE   I  1 14  ? -51.186 -49.922  -42.994 1.00 30.59 ? 14  ILE   I CG2 1 
ATOM   10278 C  CD1 . ILE   I  1 14  ? -54.150 -50.469  -43.673 1.00 36.52 ? 14  ILE   I CD1 1 
ATOM   10279 N  N   . LEU   I  1 15  ? -51.610 -47.894  -39.743 1.00 27.59 ? 15  LEU   I N   1 
ATOM   10280 C  CA  . LEU   I  1 15  ? -50.652 -47.590  -38.690 1.00 28.94 ? 15  LEU   I CA  1 
ATOM   10281 C  C   . LEU   I  1 15  ? -50.998 -48.343  -37.419 1.00 35.97 ? 15  LEU   I C   1 
ATOM   10282 O  O   . LEU   I  1 15  ? -50.110 -48.857  -36.727 1.00 33.72 ? 15  LEU   I O   1 
ATOM   10283 C  CB  . LEU   I  1 15  ? -50.637 -46.084  -38.455 1.00 28.28 ? 15  LEU   I CB  1 
ATOM   10284 C  CG  . LEU   I  1 15  ? -49.834 -45.572  -37.264 1.00 34.81 ? 15  LEU   I CG  1 
ATOM   10285 C  CD1 . LEU   I  1 15  ? -48.363 -45.984  -37.381 1.00 29.90 ? 15  LEU   I CD1 1 
ATOM   10286 C  CD2 . LEU   I  1 15  ? -49.952 -44.061  -37.220 1.00 30.31 ? 15  LEU   I CD2 1 
ATOM   10287 N  N   . GLY   I  1 16  ? -52.293 -48.447  -37.117 1.00 31.90 ? 16  GLY   I N   1 
ATOM   10288 C  CA  . GLY   I  1 16  ? -52.711 -49.134  -35.915 1.00 30.01 ? 16  GLY   I CA  1 
ATOM   10289 C  C   . GLY   I  1 16  ? -52.338 -50.594  -35.941 1.00 26.51 ? 16  GLY   I C   1 
ATOM   10290 O  O   . GLY   I  1 16  ? -51.859 -51.135  -34.936 1.00 28.57 ? 16  GLY   I O   1 
ATOM   10291 N  N   . ASN   I  1 17  ? -52.489 -51.234  -37.112 1.00 28.14 ? 17  ASN   I N   1 
ATOM   10292 C  CA  . ASN   I  1 17  ? -52.022 -52.606  -37.293 1.00 31.34 ? 17  ASN   I CA  1 
ATOM   10293 C  C   . ASN   I  1 17  ? -50.510 -52.701  -37.130 1.00 29.03 ? 17  ASN   I C   1 
ATOM   10294 O  O   . ASN   I  1 17  ? -49.989 -53.725  -36.668 1.00 27.28 ? 17  ASN   I O   1 
ATOM   10295 C  CB  . ASN   I  1 17  ? -52.377 -53.130  -38.696 1.00 36.45 ? 17  ASN   I CB  1 
ATOM   10296 C  CG  . ASN   I  1 17  ? -53.856 -53.469  -38.865 1.00 42.95 ? 17  ASN   I CG  1 
ATOM   10297 O  OD1 . ASN   I  1 17  ? -54.531 -53.819  -37.906 1.00 37.35 ? 17  ASN   I OD1 1 
ATOM   10298 N  ND2 . ASN   I  1 17  ? -54.355 -53.384  -40.105 1.00 29.87 ? 17  ASN   I ND2 1 
ATOM   10299 N  N   . GLU   I  1 18  ? -49.781 -51.691  -37.609 1.00 32.90 ? 18  GLU   I N   1 
ATOM   10300 C  CA  . GLU   I  1 18  ? -48.320 -51.746  -37.495 1.00 33.16 ? 18  GLU   I CA  1 
ATOM   10301 C  C   . GLU   I  1 18  ? -47.890 -51.643  -36.028 1.00 27.66 ? 18  GLU   I C   1 
ATOM   10302 O  O   . GLU   I  1 18  ? -46.937 -52.312  -35.598 1.00 32.50 ? 18  GLU   I O   1 
ATOM   10303 C  CB  . GLU   I  1 18  ? -47.677 -50.623  -38.331 1.00 31.87 ? 18  GLU   I CB  1 
ATOM   10304 C  CG  . GLU   I  1 18  ? -47.922 -50.655  -39.835 1.00 33.96 ? 18  GLU   I CG  1 
ATOM   10305 C  CD  . GLU   I  1 18  ? -47.163 -51.730  -40.532 1.00 44.61 ? 18  GLU   I CD  1 
ATOM   10306 O  OE1 . GLU   I  1 18  ? -46.329 -52.374  -39.841 1.00 41.33 ? 18  GLU   I OE1 1 
ATOM   10307 O  OE2 . GLU   I  1 18  ? -47.364 -51.905  -41.769 1.00 42.25 ? 18  GLU   I OE2 1 
ATOM   10308 N  N   . LEU   I  1 19  ? -48.579 -50.812  -35.240 1.00 33.90 ? 19  LEU   I N   1 
ATOM   10309 C  CA  . LEU   I  1 19  ? -48.214 -50.683  -33.829 1.00 32.65 ? 19  LEU   I CA  1 
ATOM   10310 C  C   . LEU   I  1 19  ? -48.389 -52.005  -33.101 1.00 40.34 ? 19  LEU   I C   1 
ATOM   10311 O  O   . LEU   I  1 19  ? -47.538 -52.390  -32.276 1.00 32.12 ? 19  LEU   I O   1 
ATOM   10312 C  CB  . LEU   I  1 19  ? -49.038 -49.587  -33.156 1.00 37.54 ? 19  LEU   I CB  1 
ATOM   10313 C  CG  . LEU   I  1 19  ? -48.857 -48.200  -33.779 1.00 38.06 ? 19  LEU   I CG  1 
ATOM   10314 C  CD1 . LEU   I  1 19  ? -49.732 -47.186  -33.087 1.00 39.20 ? 19  LEU   I CD1 1 
ATOM   10315 C  CD2 . LEU   I  1 19  ? -47.394 -47.738  -33.770 1.00 36.78 ? 19  LEU   I CD2 1 
ATOM   10316 N  N   . ILE   I  1 20  ? -49.474 -52.730  -33.413 1.00 29.43 ? 20  ILE   I N   1 
ATOM   10317 C  CA  . ILE   I  1 20  ? -49.658 -54.065  -32.857 1.00 30.17 ? 20  ILE   I CA  1 
ATOM   10318 C  C   . ILE   I  1 20  ? -48.517 -54.989  -33.283 1.00 34.13 ? 20  ILE   I C   1 
ATOM   10319 O  O   . ILE   I  1 20  ? -47.965 -55.748  -32.471 1.00 28.51 ? 20  ILE   I O   1 
ATOM   10320 C  CB  . ILE   I  1 20  ? -51.016 -54.657  -33.287 1.00 29.26 ? 20  ILE   I CB  1 
ATOM   10321 C  CG1 . ILE   I  1 20  ? -52.210 -53.845  -32.767 1.00 32.05 ? 20  ILE   I CG1 1 
ATOM   10322 C  CG2 . ILE   I  1 20  ? -51.096 -56.076  -32.807 1.00 31.42 ? 20  ILE   I CG2 1 
ATOM   10323 C  CD1 . ILE   I  1 20  ? -53.601 -54.285  -33.422 1.00 32.81 ? 20  ILE   I CD1 1 
ATOM   10324 N  N   . ALA   I  1 21  ? -48.165 -54.966  -34.579 1.00 26.18 ? 21  ALA   I N   1 
ATOM   10325 C  CA  . ALA   I  1 21  ? -47.183 -55.923  -35.077 1.00 32.50 ? 21  ALA   I CA  1 
ATOM   10326 C  C   . ALA   I  1 21  ? -45.795 -55.631  -34.496 1.00 28.24 ? 21  ALA   I C   1 
ATOM   10327 O  O   . ALA   I  1 21  ? -45.072 -56.553  -34.112 1.00 28.05 ? 21  ALA   I O   1 
ATOM   10328 C  CB  . ALA   I  1 21  ? -47.142 -55.890  -36.614 1.00 33.84 ? 21  ALA   I CB  1 
ATOM   10329 N  N   . ILE   I  1 22  ? -45.444 -54.350  -34.380 1.00 25.78 ? 22  ILE   I N   1 
ATOM   10330 C  CA  . ILE   I  1 22  ? -44.165 -53.963  -33.771 1.00 31.28 ? 22  ILE   I CA  1 
ATOM   10331 C  C   . ILE   I  1 22  ? -44.000 -54.638  -32.418 1.00 33.13 ? 22  ILE   I C   1 
ATOM   10332 O  O   . ILE   I  1 22  ? -43.014 -55.339  -32.171 1.00 30.15 ? 22  ILE   I O   1 
ATOM   10333 C  CB  . ILE   I  1 22  ? -44.082 -52.432  -33.655 1.00 28.19 ? 22  ILE   I CB  1 
ATOM   10334 C  CG1 . ILE   I  1 22  ? -43.856 -51.794  -35.045 1.00 29.20 ? 22  ILE   I CG1 1 
ATOM   10335 C  CG2 . ILE   I  1 22  ? -42.988 -52.001  -32.668 1.00 31.68 ? 22  ILE   I CG2 1 
ATOM   10336 C  CD1 . ILE   I  1 22  ? -44.140 -50.296  -35.071 1.00 29.60 ? 22  ILE   I CD1 1 
ATOM   10337 N  N   . ASN   I  1 23  ? -45.008 -54.492  -31.547 1.00 29.35 ? 23  ASN   I N   1 
ATOM   10338 C  CA  . ASN   I  1 23  ? -44.908 -55.026  -30.184 1.00 27.40 ? 23  ASN   I CA  1 
ATOM   10339 C  C   . ASN   I  1 23  ? -45.004 -56.548  -30.160 1.00 29.96 ? 23  ASN   I C   1 
ATOM   10340 O  O   . ASN   I  1 23  ? -44.241 -57.213  -29.448 1.00 28.25 ? 23  ASN   I O   1 
ATOM   10341 C  CB  . ASN   I  1 23  ? -45.979 -54.375  -29.318 1.00 33.67 ? 23  ASN   I CB  1 
ATOM   10342 C  CG  . ASN   I  1 23  ? -45.699 -52.919  -29.077 1.00 37.46 ? 23  ASN   I CG  1 
ATOM   10343 O  OD1 . ASN   I  1 23  ? -44.836 -52.324  -29.736 1.00 34.63 ? 23  ASN   I OD1 1 
ATOM   10344 N  ND2 . ASN   I  1 23  ? -46.400 -52.329  -28.113 1.00 33.38 ? 23  ASN   I ND2 1 
ATOM   10345 N  N   . GLN   I  1 24  ? -45.912 -57.124  -30.954 1.00 28.95 ? 24  GLN   I N   1 
ATOM   10346 C  CA  . GLN   I  1 24  ? -46.067 -58.575  -30.985 1.00 28.22 ? 24  GLN   I CA  1 
ATOM   10347 C  C   . GLN   I  1 24  ? -44.804 -59.253  -31.485 1.00 32.70 ? 24  GLN   I C   1 
ATOM   10348 O  O   . GLN   I  1 24  ? -44.366 -60.262  -30.925 1.00 29.97 ? 24  GLN   I O   1 
ATOM   10349 C  CB  . GLN   I  1 24  ? -47.276 -58.950  -31.863 1.00 26.56 ? 24  GLN   I CB  1 
ATOM   10350 C  CG  . GLN   I  1 24  ? -47.537 -60.446  -32.043 1.00 28.33 ? 24  GLN   I CG  1 
ATOM   10351 C  CD  . GLN   I  1 24  ? -48.870 -60.718  -32.826 1.00 31.68 ? 24  GLN   I CD  1 
ATOM   10352 O  OE1 . GLN   I  1 24  ? -49.882 -60.032  -32.624 1.00 29.91 ? 24  GLN   I OE1 1 
ATOM   10353 N  NE2 . GLN   I  1 24  ? -48.847 -61.698  -33.710 1.00 30.28 ? 24  GLN   I NE2 1 
ATOM   10354 N  N   . TYR   I  1 25  ? -44.222 -58.740  -32.569 1.00 26.90 ? 25  TYR   I N   1 
ATOM   10355 C  CA  . TYR   I  1 25  ? -43.006 -59.354  -33.090 1.00 30.56 ? 25  TYR   I CA  1 
ATOM   10356 C  C   . TYR   I  1 25  ? -41.850 -59.133  -32.131 1.00 27.27 ? 25  TYR   I C   1 
ATOM   10357 O  O   . TYR   I  1 25  ? -41.071 -60.055  -31.869 1.00 28.20 ? 25  TYR   I O   1 
ATOM   10358 C  CB  . TYR   I  1 25  ? -42.662 -58.792  -34.477 1.00 25.58 ? 25  TYR   I CB  1 
ATOM   10359 C  CG  . TYR   I  1 25  ? -43.765 -59.013  -35.493 1.00 34.44 ? 25  TYR   I CG  1 
ATOM   10360 C  CD1 . TYR   I  1 25  ? -44.761 -59.982  -35.289 1.00 40.64 ? 25  TYR   I CD1 1 
ATOM   10361 C  CD2 . TYR   I  1 25  ? -43.839 -58.235  -36.636 1.00 37.89 ? 25  TYR   I CD2 1 
ATOM   10362 C  CE1 . TYR   I  1 25  ? -45.794 -60.162  -36.220 1.00 44.45 ? 25  TYR   I CE1 1 
ATOM   10363 C  CE2 . TYR   I  1 25  ? -44.856 -58.409  -37.565 1.00 38.25 ? 25  TYR   I CE2 1 
ATOM   10364 C  CZ  . TYR   I  1 25  ? -45.831 -59.370  -37.355 1.00 42.82 ? 25  TYR   I CZ  1 
ATOM   10365 O  OH  . TYR   I  1 25  ? -46.850 -59.534  -38.277 1.00 34.76 ? 25  TYR   I OH  1 
ATOM   10366 N  N   . PHE   I  1 26  ? -41.752 -57.933  -31.560 1.00 25.66 ? 26  PHE   I N   1 
ATOM   10367 C  CA  . PHE   I  1 26  ? -40.639 -57.673  -30.654 1.00 30.06 ? 26  PHE   I CA  1 
ATOM   10368 C  C   . PHE   I  1 26  ? -40.702 -58.604  -29.451 1.00 30.71 ? 26  PHE   I C   1 
ATOM   10369 O  O   . PHE   I  1 26  ? -39.682 -59.192  -29.045 1.00 27.67 ? 26  PHE   I O   1 
ATOM   10370 C  CB  . PHE   I  1 26  ? -40.613 -56.207  -30.215 1.00 27.69 ? 26  PHE   I CB  1 
ATOM   10371 C  CG  . PHE   I  1 26  ? -39.224 -55.759  -29.817 1.00 35.05 ? 26  PHE   I CG  1 
ATOM   10372 C  CD1 . PHE   I  1 26  ? -38.742 -55.997  -28.541 1.00 29.44 ? 26  PHE   I CD1 1 
ATOM   10373 C  CD2 . PHE   I  1 26  ? -38.384 -55.176  -30.744 1.00 30.53 ? 26  PHE   I CD2 1 
ATOM   10374 C  CE1 . PHE   I  1 26  ? -37.432 -55.632  -28.185 1.00 31.65 ? 26  PHE   I CE1 1 
ATOM   10375 C  CE2 . PHE   I  1 26  ? -37.076 -54.812  -30.409 1.00 33.81 ? 26  PHE   I CE2 1 
ATOM   10376 C  CZ  . PHE   I  1 26  ? -36.602 -55.043  -29.131 1.00 34.34 ? 26  PHE   I CZ  1 
ATOM   10377 N  N   . LEU   I  1 27  ? -41.898 -58.774  -28.874 1.00 29.06 ? 27  LEU   I N   1 
ATOM   10378 C  CA  . LEU   I  1 27  ? -42.015 -59.678  -27.733 1.00 28.43 ? 27  LEU   I CA  1 
ATOM   10379 C  C   . LEU   I  1 27  ? -41.752 -61.117  -28.148 1.00 25.43 ? 27  LEU   I C   1 
ATOM   10380 O  O   . LEU   I  1 27  ? -41.017 -61.845  -27.469 1.00 31.41 ? 27  LEU   I O   1 
ATOM   10381 C  CB  . LEU   I  1 27  ? -43.395 -59.519  -27.085 1.00 33.15 ? 27  LEU   I CB  1 
ATOM   10382 C  CG  . LEU   I  1 27  ? -43.691 -60.396  -25.855 1.00 31.30 ? 27  LEU   I CG  1 
ATOM   10383 C  CD1 . LEU   I  1 27  ? -42.687 -60.143  -24.713 1.00 30.20 ? 27  LEU   I CD1 1 
ATOM   10384 C  CD2 . LEU   I  1 27  ? -45.112 -60.176  -25.349 1.00 34.91 ? 27  LEU   I CD2 1 
ATOM   10385 N  N   . HIS   I  1 28  ? -42.297 -61.543  -29.287 1.00 25.14 ? 28  HIS   I N   1 
ATOM   10386 C  CA  . HIS   I  1 28  ? -41.991 -62.889  -29.754 1.00 25.87 ? 28  HIS   I CA  1 
ATOM   10387 C  C   . HIS   I  1 28  ? -40.487 -63.064  -29.936 1.00 27.87 ? 28  HIS   I C   1 
ATOM   10388 O  O   . HIS   I  1 28  ? -39.928 -64.110  -29.591 1.00 26.47 ? 28  HIS   I O   1 
ATOM   10389 C  CB  . HIS   I  1 28  ? -42.740 -63.175  -31.060 1.00 30.20 ? 28  HIS   I CB  1 
ATOM   10390 C  CG  . HIS   I  1 28  ? -44.175 -63.587  -30.855 1.00 35.74 ? 28  HIS   I CG  1 
ATOM   10391 N  ND1 . HIS   I  1 28  ? -45.118 -63.550  -31.863 1.00 33.60 ? 28  HIS   I ND1 1 
ATOM   10392 C  CD2 . HIS   I  1 28  ? -44.818 -64.053  -29.756 1.00 33.27 ? 28  HIS   I CD2 1 
ATOM   10393 C  CE1 . HIS   I  1 28  ? -46.284 -63.962  -31.389 1.00 33.25 ? 28  HIS   I CE1 1 
ATOM   10394 N  NE2 . HIS   I  1 28  ? -46.126 -64.298  -30.121 1.00 30.43 ? 28  HIS   I NE2 1 
ATOM   10395 N  N   . SER   I  1 29  ? -39.822 -62.040  -30.463 1.00 28.22 ? 29  SER   I N   1 
ATOM   10396 C  CA  . SER   I  1 29  ? -38.380 -62.117  -30.674 1.00 28.28 ? 29  SER   I CA  1 
ATOM   10397 C  C   . SER   I  1 29  ? -37.649 -62.339  -29.364 1.00 23.92 ? 29  SER   I C   1 
ATOM   10398 O  O   . SER   I  1 29  ? -36.767 -63.197  -29.271 1.00 25.07 ? 29  SER   I O   1 
ATOM   10399 C  CB  . SER   I  1 29  ? -37.883 -60.832  -31.340 1.00 30.54 ? 29  SER   I CB  1 
ATOM   10400 O  OG  . SER   I  1 29  ? -36.492 -60.667  -31.182 1.00 30.21 ? 29  SER   I OG  1 
ATOM   10401 N  N   . ARG   I  1 30  ? -38.005 -61.574  -28.338 1.00 24.53 ? 30  ARG   I N   1 
ATOM   10402 C  CA  . ARG   I  1 30  ? -37.267 -61.669  -27.087 1.00 25.54 ? 30  ARG   I CA  1 
ATOM   10403 C  C   . ARG   I  1 30  ? -37.608 -62.941  -26.333 1.00 27.31 ? 30  ARG   I C   1 
ATOM   10404 O  O   . ARG   I  1 30  ? -36.765 -63.484  -25.617 1.00 25.45 ? 30  ARG   I O   1 
ATOM   10405 C  CB  . ARG   I  1 30  ? -37.535 -60.427  -26.248 1.00 27.56 ? 30  ARG   I CB  1 
ATOM   10406 C  CG  . ARG   I  1 30  ? -36.525 -59.300  -26.534 1.00 29.64 ? 30  ARG   I CG  1 
ATOM   10407 C  CD  . ARG   I  1 30  ? -36.278 -59.058  -28.059 1.00 27.28 ? 30  ARG   I CD  1 
ATOM   10408 N  NE  . ARG   I  1 30  ? -35.129 -58.177  -28.215 1.00 27.08 ? 30  ARG   I NE  1 
ATOM   10409 C  CZ  . ARG   I  1 30  ? -34.174 -58.311  -29.128 1.00 34.26 ? 30  ARG   I CZ  1 
ATOM   10410 N  NH1 . ARG   I  1 30  ? -34.231 -59.244  -30.076 1.00 27.68 ? 30  ARG   I NH1 1 
ATOM   10411 N  NH2 . ARG   I  1 30  ? -33.138 -57.482  -29.093 1.00 28.67 ? 30  ARG   I NH2 1 
ATOM   10412 N  N   . MET   I  1 31  ? -38.828 -63.439  -26.486 1.00 25.75 ? 31  MET   I N   1 
ATOM   10413 C  CA  . MET   I  1 31  ? -39.152 -64.757  -25.947 1.00 28.06 ? 31  MET   I CA  1 
ATOM   10414 C  C   . MET   I  1 31  ? -38.260 -65.818  -26.569 1.00 29.03 ? 31  MET   I C   1 
ATOM   10415 O  O   . MET   I  1 31  ? -37.661 -66.637  -25.869 1.00 30.15 ? 31  MET   I O   1 
ATOM   10416 C  CB  . MET   I  1 31  ? -40.629 -65.083  -26.202 1.00 26.78 ? 31  MET   I CB  1 
ATOM   10417 C  CG  . MET   I  1 31  ? -41.623 -64.199  -25.411 1.00 28.68 ? 31  MET   I CG  1 
ATOM   10418 S  SD  . MET   I  1 31  ? -43.344 -64.306  -25.964 1.00 32.43 ? 31  MET   I SD  1 
ATOM   10419 C  CE  . MET   I  1 31  ? -43.648 -66.035  -25.669 1.00 38.03 ? 31  MET   I CE  1 
ATOM   10420 N  N   . TRP   I  1 32  ? -38.153 -65.806  -27.892 1.00 28.57 ? 32  TRP   I N   1 
ATOM   10421 C  CA  . TRP   I  1 32  ? -37.367 -66.822  -28.571 1.00 30.85 ? 32  TRP   I CA  1 
ATOM   10422 C  C   . TRP   I  1 32  ? -35.898 -66.753  -28.173 1.00 27.55 ? 32  TRP   I C   1 
ATOM   10423 O  O   . TRP   I  1 32  ? -35.254 -67.794  -27.986 1.00 31.61 ? 32  TRP   I O   1 
ATOM   10424 C  CB  . TRP   I  1 32  ? -37.550 -66.667  -30.080 1.00 29.72 ? 32  TRP   I CB  1 
ATOM   10425 C  CG  . TRP   I  1 32  ? -38.712 -67.488  -30.619 1.00 30.51 ? 32  TRP   I CG  1 
ATOM   10426 C  CD1 . TRP   I  1 32  ? -39.083 -68.757  -30.225 1.00 35.43 ? 32  TRP   I CD1 1 
ATOM   10427 C  CD2 . TRP   I  1 32  ? -39.647 -67.093  -31.624 1.00 24.15 ? 32  TRP   I CD2 1 
ATOM   10428 N  NE1 . TRP   I  1 32  ? -40.189 -69.172  -30.946 1.00 31.27 ? 32  TRP   I NE1 1 
ATOM   10429 C  CE2 . TRP   I  1 32  ? -40.547 -68.173  -31.813 1.00 27.34 ? 32  TRP   I CE2 1 
ATOM   10430 C  CE3 . TRP   I  1 32  ? -39.805 -65.942  -32.404 1.00 31.04 ? 32  TRP   I CE3 1 
ATOM   10431 C  CZ2 . TRP   I  1 32  ? -41.578 -68.130  -32.745 1.00 28.32 ? 32  TRP   I CZ2 1 
ATOM   10432 C  CZ3 . TRP   I  1 32  ? -40.832 -65.905  -33.333 1.00 31.42 ? 32  TRP   I CZ3 1 
ATOM   10433 C  CH2 . TRP   I  1 32  ? -41.714 -66.990  -33.482 1.00 34.23 ? 32  TRP   I CH2 1 
ATOM   10434 N  N   . ASN   I  1 33  ? -35.351 -65.540  -28.045 1.00 28.41 ? 33  ASN   I N   1 
ATOM   10435 C  CA  . ASN   I  1 33  ? -33.980 -65.395  -27.548 1.00 32.28 ? 33  ASN   I CA  1 
ATOM   10436 C  C   . ASN   I  1 33  ? -33.852 -65.917  -26.121 1.00 34.45 ? 33  ASN   I C   1 
ATOM   10437 O  O   . ASN   I  1 33  ? -32.880 -66.617  -25.789 1.00 29.02 ? 33  ASN   I O   1 
ATOM   10438 C  CB  . ASN   I  1 33  ? -33.541 -63.928  -27.606 1.00 35.42 ? 33  ASN   I CB  1 
ATOM   10439 C  CG  . ASN   I  1 33  ? -33.240 -63.457  -29.018 1.00 30.84 ? 33  ASN   I CG  1 
ATOM   10440 O  OD1 . ASN   I  1 33  ? -32.971 -64.254  -29.906 1.00 31.19 ? 33  ASN   I OD1 1 
ATOM   10441 N  ND2 . ASN   I  1 33  ? -33.285 -62.154  -29.225 1.00 28.48 ? 33  ASN   I ND2 1 
ATOM   10442 N  N   . ASP   I  1 34  ? -34.807 -65.561  -25.249 1.00 32.65 ? 34  ASP   I N   1 
ATOM   10443 C  CA  . ASP   I  1 34  ? -34.767 -66.087  -23.885 1.00 31.85 ? 34  ASP   I CA  1 
ATOM   10444 C  C   . ASP   I  1 34  ? -34.754 -67.615  -23.890 1.00 39.41 ? 34  ASP   I C   1 
ATOM   10445 O  O   . ASP   I  1 34  ? -34.055 -68.232  -23.078 1.00 32.20 ? 34  ASP   I O   1 
ATOM   10446 C  CB  . ASP   I  1 34  ? -35.936 -65.546  -23.064 1.00 33.73 ? 34  ASP   I CB  1 
ATOM   10447 C  CG  . ASP   I  1 34  ? -35.992 -66.122  -21.641 1.00 38.49 ? 34  ASP   I CG  1 
ATOM   10448 O  OD1 . ASP   I  1 34  ? -35.033 -65.963  -20.851 1.00 36.66 ? 34  ASP   I OD1 1 
ATOM   10449 O  OD2 . ASP   I  1 34  ? -37.021 -66.731  -21.316 1.00 37.28 ? 34  ASP   I OD2 1 
ATOM   10450 N  N   . TRP   I  1 35  ? -35.487 -68.249  -24.826 1.00 33.52 ? 35  TRP   I N   1 
ATOM   10451 C  CA  . TRP   I  1 35  ? -35.532 -69.712  -24.867 1.00 32.68 ? 35  TRP   I CA  1 
ATOM   10452 C  C   . TRP   I  1 35  ? -34.327 -70.323  -25.556 1.00 31.12 ? 35  TRP   I C   1 
ATOM   10453 O  O   . TRP   I  1 35  ? -34.231 -71.556  -25.630 1.00 35.15 ? 35  TRP   I O   1 
ATOM   10454 C  CB  . TRP   I  1 35  ? -36.820 -70.209  -25.566 1.00 32.62 ? 35  TRP   I CB  1 
ATOM   10455 C  CG  . TRP   I  1 35  ? -38.078 -69.793  -24.890 1.00 37.40 ? 35  TRP   I CG  1 
ATOM   10456 C  CD1 . TRP   I  1 35  ? -38.205 -69.313  -23.616 1.00 41.78 ? 35  TRP   I CD1 1 
ATOM   10457 C  CD2 . TRP   I  1 35  ? -39.401 -69.779  -25.455 1.00 41.36 ? 35  TRP   I CD2 1 
ATOM   10458 N  NE1 . TRP   I  1 35  ? -39.517 -69.008  -23.358 1.00 44.18 ? 35  TRP   I NE1 1 
ATOM   10459 C  CE2 . TRP   I  1 35  ? -40.272 -69.288  -24.466 1.00 36.22 ? 35  TRP   I CE2 1 
ATOM   10460 C  CE3 . TRP   I  1 35  ? -39.932 -70.144  -26.696 1.00 39.30 ? 35  TRP   I CE3 1 
ATOM   10461 C  CZ2 . TRP   I  1 35  ? -41.651 -69.141  -24.684 1.00 43.24 ? 35  TRP   I CZ2 1 
ATOM   10462 C  CZ3 . TRP   I  1 35  ? -41.305 -69.998  -26.910 1.00 46.82 ? 35  TRP   I CZ3 1 
ATOM   10463 C  CH2 . TRP   I  1 35  ? -42.142 -69.498  -25.910 1.00 38.79 ? 35  TRP   I CH2 1 
ATOM   10464 N  N   . GLY   I  1 36  ? -33.389 -69.511  -26.045 1.00 30.44 ? 36  GLY   I N   1 
ATOM   10465 C  CA  . GLY   I  1 36  ? -32.243 -70.055  -26.744 1.00 27.50 ? 36  GLY   I CA  1 
ATOM   10466 C  C   . GLY   I  1 36  ? -32.485 -70.355  -28.207 1.00 29.40 ? 36  GLY   I C   1 
ATOM   10467 O  O   . GLY   I  1 36  ? -31.657 -71.036  -28.838 1.00 32.43 ? 36  GLY   I O   1 
ATOM   10468 N  N   . LEU   I  1 37  ? -33.591 -69.866  -28.766 1.00 29.87 ? 37  LEU   I N   1 
ATOM   10469 C  CA  . LEU   I  1 37  ? -33.922 -70.034  -30.186 1.00 34.11 ? 37  LEU   I CA  1 
ATOM   10470 C  C   . LEU   I  1 37  ? -33.539 -68.745  -30.915 1.00 28.11 ? 37  LEU   I C   1 
ATOM   10471 O  O   . LEU   I  1 37  ? -34.373 -67.976  -31.412 1.00 26.53 ? 37  LEU   I O   1 
ATOM   10472 C  CB  . LEU   I  1 37  ? -35.413 -70.391  -30.346 1.00 30.49 ? 37  LEU   I CB  1 
ATOM   10473 C  CG  . LEU   I  1 37  ? -35.761 -71.672  -29.566 1.00 37.45 ? 37  LEU   I CG  1 
ATOM   10474 C  CD1 . LEU   I  1 37  ? -37.246 -71.942  -29.447 1.00 30.16 ? 37  LEU   I CD1 1 
ATOM   10475 C  CD2 . LEU   I  1 37  ? -35.086 -72.856  -30.228 1.00 34.32 ? 37  LEU   I CD2 1 
ATOM   10476 N  N   . LYS   I  1 38  ? -32.217 -68.522  -30.960 1.00 29.03 ? 38  LYS   I N   1 
ATOM   10477 C  CA  . LYS   I  1 38  ? -31.692 -67.213  -31.325 1.00 35.54 ? 38  LYS   I CA  1 
ATOM   10478 C  C   . LYS   I  1 38  ? -31.899 -66.896  -32.795 1.00 30.53 ? 38  LYS   I C   1 
ATOM   10479 O  O   . LYS   I  1 38  ? -31.969 -65.719  -33.153 1.00 31.12 ? 38  LYS   I O   1 
ATOM   10480 C  CB  . LYS   I  1 38  ? -30.195 -67.126  -31.006 1.00 36.47 ? 38  LYS   I CB  1 
ATOM   10481 C  CG  . LYS   I  1 38  ? -29.829 -67.500  -29.596 1.00 47.54 ? 38  LYS   I CG  1 
ATOM   10482 C  CD  . LYS   I  1 38  ? -30.194 -66.421  -28.614 1.00 45.28 ? 38  LYS   I CD  1 
ATOM   10483 C  CE  . LYS   I  1 38  ? -29.564 -66.722  -27.240 1.00 46.45 ? 38  LYS   I CE  1 
ATOM   10484 N  NZ  . LYS   I  1 38  ? -29.436 -65.511  -26.416 1.00 56.44 ? 38  LYS   I NZ  1 
ATOM   10485 N  N   . ARG   I  1 39  ? -31.948 -67.911  -33.669 1.00 30.88 ? 39  ARG   I N   1 
ATOM   10486 C  CA  . ARG   I  1 39  ? -32.202 -67.632  -35.084 1.00 29.26 ? 39  ARG   I CA  1 
ATOM   10487 C  C   . ARG   I  1 39  ? -33.631 -67.160  -35.297 1.00 33.18 ? 39  ARG   I C   1 
ATOM   10488 O  O   . ARG   I  1 39  ? -33.871 -66.234  -36.082 1.00 24.80 ? 39  ARG   I O   1 
ATOM   10489 C  CB  . ARG   I  1 39  ? -31.899 -68.868  -35.922 1.00 32.10 ? 39  ARG   I CB  1 
ATOM   10490 C  CG  . ARG   I  1 39  ? -31.949 -68.643  -37.410 1.00 42.54 ? 39  ARG   I CG  1 
ATOM   10491 C  CD  . ARG   I  1 39  ? -31.842 -69.976  -38.128 1.00 47.85 ? 39  ARG   I CD  1 
ATOM   10492 N  NE  . ARG   I  1 39  ? -31.430 -69.844  -39.518 1.00 62.89 ? 39  ARG   I NE  1 
ATOM   10493 C  CZ  . ARG   I  1 39  ? -30.178 -69.946  -39.943 1.00 57.05 ? 39  ARG   I CZ  1 
ATOM   10494 N  NH1 . ARG   I  1 39  ? -29.174 -70.168  -39.102 1.00 57.84 ? 39  ARG   I NH1 1 
ATOM   10495 N  NH2 . ARG   I  1 39  ? -29.928 -69.822  -41.243 1.00 54.80 ? 39  ARG   I NH2 1 
ATOM   10496 N  N   . LEU   I  1 40  ? -34.601 -67.764  -34.584 1.00 29.05 ? 40  LEU   I N   1 
ATOM   10497 C  CA  . LEU   I  1 40  ? -35.964 -67.228  -34.617 1.00 29.15 ? 40  LEU   I CA  1 
ATOM   10498 C  C   . LEU   I  1 40  ? -36.010 -65.834  -34.017 1.00 27.49 ? 40  LEU   I C   1 
ATOM   10499 O  O   . LEU   I  1 40  ? -36.686 -64.938  -34.544 1.00 29.89 ? 40  LEU   I O   1 
ATOM   10500 C  CB  . LEU   I  1 40  ? -36.941 -68.131  -33.853 1.00 28.61 ? 40  LEU   I CB  1 
ATOM   10501 C  CG  . LEU   I  1 40  ? -37.510 -69.327  -34.600 1.00 31.82 ? 40  LEU   I CG  1 
ATOM   10502 C  CD1 . LEU   I  1 40  ? -38.148 -70.333  -33.649 1.00 30.79 ? 40  LEU   I CD1 1 
ATOM   10503 C  CD2 . LEU   I  1 40  ? -38.525 -68.899  -35.648 1.00 31.57 ? 40  LEU   I CD2 1 
ATOM   10504 N  N   . GLY   I  1 41  ? -35.319 -65.637  -32.896 1.00 29.22 ? 41  GLY   I N   1 
ATOM   10505 C  CA  . GLY   I  1 41  ? -35.334 -64.329  -32.273 1.00 29.80 ? 41  GLY   I CA  1 
ATOM   10506 C  C   . GLY   I  1 41  ? -34.775 -63.259  -33.197 1.00 25.30 ? 41  GLY   I C   1 
ATOM   10507 O  O   . GLY   I  1 41  ? -35.360 -62.185  -33.345 1.00 31.85 ? 41  GLY   I O   1 
ATOM   10508 N  N   . ALA   I  1 42  ? -33.642 -63.551  -33.851 1.00 26.56 ? 42  ALA   I N   1 
ATOM   10509 C  CA  . ALA   I  1 42  ? -33.039 -62.567  -34.754 1.00 23.98 ? 42  ALA   I CA  1 
ATOM   10510 C  C   . ALA   I  1 42  ? -33.943 -62.263  -35.926 1.00 26.22 ? 42  ALA   I C   1 
ATOM   10511 O  O   . ALA   I  1 42  ? -34.125 -61.096  -36.301 1.00 27.54 ? 42  ALA   I O   1 
ATOM   10512 C  CB  . ALA   I  1 42  ? -31.686 -63.062  -35.273 1.00 29.94 ? 42  ALA   I CB  1 
ATOM   10513 N  N   . HIS   I  1 43  ? -34.528 -63.295  -36.531 1.00 28.12 ? 43  HIS   I N   1 
ATOM   10514 C  CA  . HIS   I  1 43  ? -35.423 -63.027  -37.648 1.00 26.32 ? 43  HIS   I CA  1 
ATOM   10515 C  C   . HIS   I  1 43  ? -36.631 -62.210  -37.204 1.00 32.08 ? 43  HIS   I C   1 
ATOM   10516 O  O   . HIS   I  1 43  ? -37.076 -61.282  -37.905 1.00 27.46 ? 43  HIS   I O   1 
ATOM   10517 C  CB  . HIS   I  1 43  ? -35.875 -64.339  -38.273 1.00 31.06 ? 43  HIS   I CB  1 
ATOM   10518 C  CG  . HIS   I  1 43  ? -36.603 -64.153  -39.554 1.00 33.46 ? 43  HIS   I CG  1 
ATOM   10519 N  ND1 . HIS   I  1 43  ? -35.991 -64.309  -40.781 1.00 44.58 ? 43  HIS   I ND1 1 
ATOM   10520 C  CD2 . HIS   I  1 43  ? -37.879 -63.784  -39.807 1.00 35.42 ? 43  HIS   I CD2 1 
ATOM   10521 C  CE1 . HIS   I  1 43  ? -36.865 -64.045  -41.736 1.00 44.59 ? 43  HIS   I CE1 1 
ATOM   10522 N  NE2 . HIS   I  1 43  ? -38.019 -63.729  -41.172 1.00 39.73 ? 43  HIS   I NE2 1 
ATOM   10523 N  N   . GLU   I  1 44  ? -37.189 -62.550  -36.048 1.00 28.47 ? 44  GLU   I N   1 
ATOM   10524 C  CA  . GLU   I  1 44  ? -38.404 -61.882  -35.614 1.00 29.15 ? 44  GLU   I CA  1 
ATOM   10525 C  C   . GLU   I  1 44  ? -38.109 -60.439  -35.243 1.00 24.83 ? 44  GLU   I C   1 
ATOM   10526 O  O   . GLU   I  1 44  ? -38.960 -59.560  -35.441 1.00 28.97 ? 44  GLU   I O   1 
ATOM   10527 C  CB  . GLU   I  1 44  ? -38.999 -62.660  -34.441 1.00 31.84 ? 44  GLU   I CB  1 
ATOM   10528 C  CG  . GLU   I  1 44  ? -40.352 -62.173  -34.000 1.00 36.10 ? 44  GLU   I CG  1 
ATOM   10529 C  CD  . GLU   I  1 44  ? -41.481 -62.697  -34.875 1.00 37.25 ? 44  GLU   I CD  1 
ATOM   10530 O  OE1 . GLU   I  1 44  ? -41.216 -63.185  -36.002 1.00 30.87 ? 44  GLU   I OE1 1 
ATOM   10531 O  OE2 . GLU   I  1 44  ? -42.630 -62.649  -34.390 1.00 33.11 ? 44  GLU   I OE2 1 
ATOM   10532 N  N   . TYR   I  1 45  ? -36.901 -60.194  -34.725 1.00 25.37 ? 45  TYR   I N   1 
ATOM   10533 C  CA  . TYR   I  1 45  ? -36.436 -58.834  -34.477 1.00 22.86 ? 45  TYR   I CA  1 
ATOM   10534 C  C   . TYR   I  1 45  ? -36.444 -58.023  -35.762 1.00 23.29 ? 45  TYR   I C   1 
ATOM   10535 O  O   . TYR   I  1 45  ? -36.949 -56.896  -35.790 1.00 26.70 ? 45  TYR   I O   1 
ATOM   10536 C  CB  . TYR   I  1 45  ? -35.040 -58.881  -33.829 1.00 27.95 ? 45  TYR   I CB  1 
ATOM   10537 C  CG  . TYR   I  1 45  ? -34.343 -57.548  -33.724 1.00 26.49 ? 45  TYR   I CG  1 
ATOM   10538 C  CD1 . TYR   I  1 45  ? -34.577 -56.700  -32.649 1.00 33.62 ? 45  TYR   I CD1 1 
ATOM   10539 C  CD2 . TYR   I  1 45  ? -33.455 -57.123  -34.714 1.00 30.79 ? 45  TYR   I CD2 1 
ATOM   10540 C  CE1 . TYR   I  1 45  ? -33.951 -55.470  -32.557 1.00 36.05 ? 45  TYR   I CE1 1 
ATOM   10541 C  CE2 . TYR   I  1 45  ? -32.813 -55.878  -34.612 1.00 31.94 ? 45  TYR   I CE2 1 
ATOM   10542 C  CZ  . TYR   I  1 45  ? -33.076 -55.073  -33.538 1.00 35.41 ? 45  TYR   I CZ  1 
ATOM   10543 O  OH  . TYR   I  1 45  ? -32.483 -53.845  -33.441 1.00 36.66 ? 45  TYR   I OH  1 
ATOM   10544 N  N   . HIS   I  1 46  ? -35.921 -58.592  -36.862 1.00 26.72 ? 46  HIS   I N   1 
ATOM   10545 C  CA  . HIS   I  1 46  ? -35.893 -57.836  -38.110 1.00 26.64 ? 46  HIS   I CA  1 
ATOM   10546 C  C   . HIS   I  1 46  ? -37.300 -57.629  -38.677 1.00 31.14 ? 46  HIS   I C   1 
ATOM   10547 O  O   . HIS   I  1 46  ? -37.564 -56.578  -39.267 1.00 29.63 ? 46  HIS   I O   1 
ATOM   10548 C  CB  . HIS   I  1 46  ? -34.941 -58.508  -39.110 1.00 30.85 ? 46  HIS   I CB  1 
ATOM   10549 C  CG  . HIS   I  1 46  ? -33.489 -58.364  -38.721 1.00 42.98 ? 46  HIS   I CG  1 
ATOM   10550 N  ND1 . HIS   I  1 46  ? -32.716 -59.421  -38.290 1.00 46.95 ? 46  HIS   I ND1 1 
ATOM   10551 C  CD2 . HIS   I  1 46  ? -32.693 -57.270  -38.645 1.00 44.66 ? 46  HIS   I CD2 1 
ATOM   10552 C  CE1 . HIS   I  1 46  ? -31.505 -58.992  -37.980 1.00 43.00 ? 46  HIS   I CE1 1 
ATOM   10553 N  NE2 . HIS   I  1 46  ? -31.462 -57.689  -38.191 1.00 45.53 ? 46  HIS   I NE2 1 
ATOM   10554 N  N   . GLU   I  1 47  ? -38.233 -58.570  -38.450 1.00 30.04 ? 47  GLU   I N   1 
ATOM   10555 C  CA  . GLU   I  1 47  ? -39.637 -58.329  -38.786 1.00 27.74 ? 47  GLU   I CA  1 
ATOM   10556 C  C   . GLU   I  1 47  ? -40.173 -57.119  -38.033 1.00 27.84 ? 47  GLU   I C   1 
ATOM   10557 O  O   . GLU   I  1 47  ? -40.823 -56.246  -38.612 1.00 30.38 ? 47  GLU   I O   1 
ATOM   10558 C  CB  . GLU   I  1 47  ? -40.484 -59.569  -38.451 1.00 33.30 ? 47  GLU   I CB  1 
ATOM   10559 C  CG  . GLU   I  1 47  ? -40.115 -60.853  -39.189 1.00 38.07 ? 47  GLU   I CG  1 
ATOM   10560 C  CD  . GLU   I  1 47  ? -40.312 -60.749  -40.697 1.00 49.14 ? 47  GLU   I CD  1 
ATOM   10561 O  OE1 . GLU   I  1 47  ? -40.757 -59.680  -41.139 1.00 54.12 ? 47  GLU   I OE1 1 
ATOM   10562 O  OE2 . GLU   I  1 47  ? -40.027 -61.725  -41.436 1.00 48.04 ? 47  GLU   I OE2 1 
ATOM   10563 N  N   . SER   I  1 48  ? -39.893 -57.053  -36.724 1.00 25.67 ? 48  SER   I N   1 
ATOM   10564 C  CA  . SER   I  1 48  ? -40.327 -55.929  -35.918 1.00 22.97 ? 48  SER   I CA  1 
ATOM   10565 C  C   . SER   I  1 48  ? -39.730 -54.617  -36.418 1.00 28.11 ? 48  SER   I C   1 
ATOM   10566 O  O   . SER   I  1 48  ? -40.443 -53.620  -36.573 1.00 26.73 ? 48  SER   I O   1 
ATOM   10567 C  CB  . SER   I  1 48  ? -39.966 -56.204  -34.447 1.00 27.49 ? 48  SER   I CB  1 
ATOM   10568 O  OG  . SER   I  1 48  ? -40.452 -55.163  -33.603 1.00 27.12 ? 48  SER   I OG  1 
ATOM   10569 N  N   . ILE   I  1 49  ? -38.416 -54.588  -36.693 1.00 26.17 ? 49  ILE   I N   1 
ATOM   10570 C  CA  . ILE   I  1 49  ? -37.834 -53.370  -37.271 1.00 25.96 ? 49  ILE   I CA  1 
ATOM   10571 C  C   . ILE   I  1 49  ? -38.504 -53.003  -38.596 1.00 23.08 ? 49  ILE   I C   1 
ATOM   10572 O  O   . ILE   I  1 49  ? -38.719 -51.825  -38.889 1.00 27.19 ? 49  ILE   I O   1 
ATOM   10573 C  CB  . ILE   I  1 49  ? -36.309 -53.531  -37.466 1.00 31.34 ? 49  ILE   I CB  1 
ATOM   10574 C  CG1 . ILE   I  1 49  ? -35.604 -53.784  -36.141 1.00 29.06 ? 49  ILE   I CG1 1 
ATOM   10575 C  CG2 . ILE   I  1 49  ? -35.749 -52.305  -38.209 1.00 30.81 ? 49  ILE   I CG2 1 
ATOM   10576 C  CD1 . ILE   I  1 49  ? -35.509 -52.553  -35.217 1.00 34.84 ? 49  ILE   I CD1 1 
ATOM   10577 N  N   . ASP   I  1 50  ? -38.760 -53.985  -39.457 1.00 28.94 ? 50  ASP   I N   1 
ATOM   10578 C  CA  . ASP   I  1 50  ? -39.424 -53.666  -40.716 1.00 27.74 ? 50  ASP   I CA  1 
ATOM   10579 C  C   . ASP   I  1 50  ? -40.751 -52.976  -40.461 1.00 34.44 ? 50  ASP   I C   1 
ATOM   10580 O  O   . ASP   I  1 50  ? -41.107 -52.018  -41.164 1.00 26.62 ? 50  ASP   I O   1 
ATOM   10581 C  CB  . ASP   I  1 50  ? -39.633 -54.925  -41.564 1.00 40.77 ? 50  ASP   I CB  1 
ATOM   10582 C  CG  . ASP   I  1 50  ? -38.370 -55.359  -42.289 1.00 55.96 ? 50  ASP   I CG  1 
ATOM   10583 O  OD1 . ASP   I  1 50  ? -37.441 -54.530  -42.451 1.00 55.66 ? 50  ASP   I OD1 1 
ATOM   10584 O  OD2 . ASP   I  1 50  ? -38.306 -56.538  -42.694 1.00 65.96 ? 50  ASP   I OD2 1 
ATOM   10585 N  N   . GLU   I  1 51  ? -41.502 -53.443  -39.452 1.00 25.65 ? 51  GLU   I N   1 
ATOM   10586 C  CA  . GLU   I  1 51  ? -42.792 -52.822  -39.198 1.00 28.57 ? 51  GLU   I CA  1 
ATOM   10587 C  C   . GLU   I  1 51  ? -42.609 -51.424  -38.616 1.00 30.30 ? 51  GLU   I C   1 
ATOM   10588 O  O   . GLU   I  1 51  ? -43.401 -50.524  -38.903 1.00 26.18 ? 51  GLU   I O   1 
ATOM   10589 C  CB  . GLU   I  1 51  ? -43.633 -53.714  -38.266 1.00 22.19 ? 51  GLU   I CB  1 
ATOM   10590 C  CG  . GLU   I  1 51  ? -43.961 -55.104  -38.823 1.00 31.18 ? 51  GLU   I CG  1 
ATOM   10591 C  CD  . GLU   I  1 51  ? -44.599 -55.049  -40.225 1.00 41.49 ? 51  GLU   I CD  1 
ATOM   10592 O  OE1 . GLU   I  1 51  ? -45.624 -54.385  -40.360 1.00 45.62 ? 51  GLU   I OE1 1 
ATOM   10593 O  OE2 . GLU   I  1 51  ? -44.057 -55.629  -41.193 1.00 55.34 ? 51  GLU   I OE2 1 
ATOM   10594 N  N   . MET   I  1 52  ? -41.553 -51.206  -37.820 1.00 26.20 ? 52  MET   I N   1 
ATOM   10595 C  CA  . MET   I  1 52  ? -41.254 -49.844  -37.373 1.00 25.11 ? 52  MET   I CA  1 
ATOM   10596 C  C   . MET   I  1 52  ? -41.003 -48.910  -38.558 1.00 24.86 ? 52  MET   I C   1 
ATOM   10597 O  O   . MET   I  1 52  ? -41.456 -47.755  -38.573 1.00 26.45 ? 52  MET   I O   1 
ATOM   10598 C  CB  . MET   I  1 52  ? -40.024 -49.858  -36.459 1.00 27.31 ? 52  MET   I CB  1 
ATOM   10599 C  CG  . MET   I  1 52  ? -40.207 -50.597  -35.142 1.00 29.88 ? 52  MET   I CG  1 
ATOM   10600 S  SD  . MET   I  1 52  ? -38.632 -50.870  -34.271 1.00 28.23 ? 52  MET   I SD  1 
ATOM   10601 C  CE  . MET   I  1 52  ? -39.050 -52.252  -33.196 1.00 28.93 ? 52  MET   I CE  1 
ATOM   10602 N  N   . LYS   I  1 53  ? -40.261 -49.378  -39.557 1.00 26.16 ? 53  LYS   I N   1 
ATOM   10603 C  CA  . LYS   I  1 53  ? -40.025 -48.533  -40.719 1.00 25.65 ? 53  LYS   I CA  1 
ATOM   10604 C  C   . LYS   I  1 53  ? -41.319 -48.249  -41.468 1.00 27.98 ? 53  LYS   I C   1 
ATOM   10605 O  O   . LYS   I  1 53  ? -41.543 -47.116  -41.908 1.00 26.44 ? 53  LYS   I O   1 
ATOM   10606 C  CB  . LYS   I  1 53  ? -38.990 -49.188  -41.640 1.00 24.50 ? 53  LYS   I CB  1 
ATOM   10607 C  CG  . LYS   I  1 53  ? -37.613 -49.225  -41.031 1.00 30.79 ? 53  LYS   I CG  1 
ATOM   10608 C  CD  . LYS   I  1 53  ? -36.664 -49.918  -41.997 1.00 39.45 ? 53  LYS   I CD  1 
ATOM   10609 C  CE  . LYS   I  1 53  ? -35.301 -50.175  -41.370 1.00 48.13 ? 53  LYS   I CE  1 
ATOM   10610 N  NZ  . LYS   I  1 53  ? -34.386 -50.711  -42.420 1.00 59.70 ? 53  LYS   I NZ  1 
ATOM   10611 N  N   . HIS   I  1 54  ? -42.191 -49.257  -41.616 1.00 27.10 ? 54  HIS   I N   1 
ATOM   10612 C  CA  . HIS   I  1 54  ? -43.477 -49.005  -42.265 1.00 26.73 ? 54  HIS   I CA  1 
ATOM   10613 C  C   . HIS   I  1 54  ? -44.259 -47.945  -41.493 1.00 27.36 ? 54  HIS   I C   1 
ATOM   10614 O  O   . HIS   I  1 54  ? -44.826 -47.015  -42.082 1.00 28.61 ? 54  HIS   I O   1 
ATOM   10615 C  CB  . HIS   I  1 54  ? -44.323 -50.288  -42.367 1.00 29.37 ? 54  HIS   I CB  1 
ATOM   10616 C  CG  . HIS   I  1 54  ? -43.685 -51.411  -43.123 1.00 26.48 ? 54  HIS   I CG  1 
ATOM   10617 N  ND1 . HIS   I  1 54  ? -42.812 -51.211  -44.169 1.00 29.94 ? 54  HIS   I ND1 1 
ATOM   10618 C  CD2 . HIS   I  1 54  ? -43.831 -52.754  -43.008 1.00 27.02 ? 54  HIS   I CD2 1 
ATOM   10619 C  CE1 . HIS   I  1 54  ? -42.405 -52.380  -44.630 1.00 32.99 ? 54  HIS   I CE1 1 
ATOM   10620 N  NE2 . HIS   I  1 54  ? -43.005 -53.334  -43.939 1.00 35.46 ? 54  HIS   I NE2 1 
ATOM   10621 N  N   . ALA   I  1 55  ? -44.279 -48.063  -40.159 1.00 27.28 ? 55  ALA   I N   1 
ATOM   10622 C  CA  . ALA   I  1 55  ? -45.009 -47.111  -39.339 1.00 26.17 ? 55  ALA   I CA  1 
ATOM   10623 C  C   . ALA   I  1 55  ? -44.464 -45.703  -39.502 1.00 29.02 ? 55  ALA   I C   1 
ATOM   10624 O  O   . ALA   I  1 55  ? -45.228 -44.728  -39.497 1.00 24.66 ? 55  ALA   I O   1 
ATOM   10625 C  CB  . ALA   I  1 55  ? -44.974 -47.545  -37.870 1.00 32.52 ? 55  ALA   I CB  1 
ATOM   10626 N  N   . ASP   I  1 56  ? -43.140 -45.561  -39.609 1.00 28.88 ? 56  ASP   I N   1 
ATOM   10627 C  CA  . ASP   I  1 56  ? -42.557 -44.235  -39.798 1.00 30.69 ? 56  ASP   I CA  1 
ATOM   10628 C  C   . ASP   I  1 56  ? -43.101 -43.596  -41.077 1.00 22.85 ? 56  ASP   I C   1 
ATOM   10629 O  O   . ASP   I  1 56  ? -43.506 -42.427  -41.095 1.00 26.66 ? 56  ASP   I O   1 
ATOM   10630 C  CB  . ASP   I  1 56  ? -41.022 -44.381  -39.843 1.00 28.73 ? 56  ASP   I CB  1 
ATOM   10631 C  CG  . ASP   I  1 56  ? -40.271 -43.070  -39.962 1.00 28.99 ? 56  ASP   I CG  1 
ATOM   10632 O  OD1 . ASP   I  1 56  ? -40.821 -41.992  -39.682 1.00 29.47 ? 56  ASP   I OD1 1 
ATOM   10633 O  OD2 . ASP   I  1 56  ? -39.070 -43.132  -40.338 1.00 33.11 ? 56  ASP   I OD2 1 
ATOM   10634 N  N   . LYS   I  1 57  ? -43.065 -44.347  -42.169 1.00 20.94 ? 57  LYS   I N   1 
ATOM   10635 C  CA  . LYS   I  1 57  ? -43.491 -43.806  -43.447 1.00 24.03 ? 57  LYS   I CA  1 
ATOM   10636 C  C   . LYS   I  1 57  ? -44.967 -43.432  -43.409 1.00 28.65 ? 57  LYS   I C   1 
ATOM   10637 O  O   . LYS   I  1 57  ? -45.365 -42.398  -43.958 1.00 26.71 ? 57  LYS   I O   1 
ATOM   10638 C  CB  . LYS   I  1 57  ? -43.225 -44.826  -44.551 1.00 28.46 ? 57  LYS   I CB  1 
ATOM   10639 C  CG  . LYS   I  1 57  ? -41.719 -45.165  -44.788 1.00 38.27 ? 57  LYS   I CG  1 
ATOM   10640 C  CD  . LYS   I  1 57  ? -41.148 -44.495  -46.032 1.00 55.99 ? 57  LYS   I CD  1 
ATOM   10641 C  CE  . LYS   I  1 57  ? -39.628 -44.560  -46.058 1.00 51.83 ? 57  LYS   I CE  1 
ATOM   10642 N  NZ  . LYS   I  1 57  ? -39.054 -43.715  -44.945 1.00 63.35 ? 57  LYS   I NZ  1 
ATOM   10643 N  N   . LEU   I  1 58  ? -45.783 -44.252  -42.745 1.00 24.97 ? 58  LEU   I N   1 
ATOM   10644 C  CA  . LEU   I  1 58  ? -47.203 -43.918  -42.603 1.00 26.22 ? 58  LEU   I CA  1 
ATOM   10645 C  C   . LEU   I  1 58  ? -47.393 -42.632  -41.812 1.00 24.76 ? 58  LEU   I C   1 
ATOM   10646 O  O   . LEU   I  1 58  ? -48.150 -41.744  -42.214 1.00 27.98 ? 58  LEU   I O   1 
ATOM   10647 C  CB  . LEU   I  1 58  ? -47.961 -45.076  -41.938 1.00 26.02 ? 58  LEU   I CB  1 
ATOM   10648 C  CG  . LEU   I  1 58  ? -48.144 -46.312  -42.825 1.00 28.03 ? 58  LEU   I CG  1 
ATOM   10649 C  CD1 . LEU   I  1 58  ? -48.532 -47.532  -42.011 1.00 30.37 ? 58  LEU   I CD1 1 
ATOM   10650 C  CD2 . LEU   I  1 58  ? -49.142 -46.069  -43.951 1.00 27.17 ? 58  LEU   I CD2 1 
ATOM   10651 N  N   . ILE   I  1 59  ? -46.690 -42.504  -40.685 1.00 28.17 ? 59  ILE   I N   1 
ATOM   10652 C  CA  . ILE   I  1 59  ? -46.785 -41.304  -39.862 1.00 26.66 ? 59  ILE   I CA  1 
ATOM   10653 C  C   . ILE   I  1 59  ? -46.409 -40.078  -40.673 1.00 29.41 ? 59  ILE   I C   1 
ATOM   10654 O  O   . ILE   I  1 59  ? -47.046 -39.015  -40.579 1.00 26.88 ? 59  ILE   I O   1 
ATOM   10655 C  CB  . ILE   I  1 59  ? -45.874 -41.457  -38.620 1.00 25.05 ? 59  ILE   I CB  1 
ATOM   10656 C  CG1 . ILE   I  1 59  ? -46.438 -42.516  -37.675 1.00 26.88 ? 59  ILE   I CG1 1 
ATOM   10657 C  CG2 . ILE   I  1 59  ? -45.721 -40.159  -37.894 1.00 24.82 ? 59  ILE   I CG2 1 
ATOM   10658 C  CD1 . ILE   I  1 59  ? -45.450 -42.963  -36.597 1.00 28.00 ? 59  ILE   I CD1 1 
ATOM   10659 N  N   . GLU   I  1 60  ? -45.315 -40.186  -41.434 1.00 26.79 ? 60  GLU   I N   1 
ATOM   10660 C  CA  . GLU   I  1 60  ? -44.879 -39.076  -42.269 1.00 25.91 ? 60  GLU   I CA  1 
ATOM   10661 C  C   . GLU   I  1 60  ? -45.929 -38.716  -43.322 1.00 23.83 ? 60  GLU   I C   1 
ATOM   10662 O  O   . GLU   I  1 60  ? -46.219 -37.538  -43.543 1.00 28.49 ? 60  GLU   I O   1 
ATOM   10663 C  CB  . GLU   I  1 60  ? -43.540 -39.427  -42.929 1.00 28.95 ? 60  GLU   I CB  1 
ATOM   10664 C  CG  . GLU   I  1 60  ? -42.415 -39.527  -41.878 1.00 25.54 ? 60  GLU   I CG  1 
ATOM   10665 C  CD  . GLU   I  1 60  ? -41.101 -40.018  -42.443 1.00 32.40 ? 60  GLU   I CD  1 
ATOM   10666 O  OE1 . GLU   I  1 60  ? -41.099 -40.880  -43.357 1.00 34.49 ? 60  GLU   I OE1 1 
ATOM   10667 O  OE2 . GLU   I  1 60  ? -40.072 -39.521  -41.947 1.00 31.42 ? 60  GLU   I OE2 1 
ATOM   10668 N  N   . ARG   I  1 61  ? -46.464 -39.711  -44.013 1.00 25.53 ? 61  ARG   I N   1 
ATOM   10669 C  CA  . ARG   I  1 61  ? -47.496 -39.441  -45.019 1.00 27.07 ? 61  ARG   I CA  1 
ATOM   10670 C  C   . ARG   I  1 61  ? -48.719 -38.765  -44.393 1.00 28.26 ? 61  ARG   I C   1 
ATOM   10671 O  O   . ARG   I  1 61  ? -49.247 -37.779  -44.928 1.00 26.88 ? 61  ARG   I O   1 
ATOM   10672 C  CB  . ARG   I  1 61  ? -47.902 -40.748  -45.691 1.00 27.11 ? 61  ARG   I CB  1 
ATOM   10673 C  CG  . ARG   I  1 61  ? -48.911 -40.577  -46.821 1.00 26.75 ? 61  ARG   I CG  1 
ATOM   10674 C  CD  . ARG   I  1 61  ? -48.253 -39.926  -47.973 1.00 27.76 ? 61  ARG   I CD  1 
ATOM   10675 N  NE  . ARG   I  1 61  ? -49.165 -39.805  -49.112 1.00 33.43 ? 61  ARG   I NE  1 
ATOM   10676 C  CZ  . ARG   I  1 61  ? -48.995 -38.932  -50.088 1.00 34.46 ? 61  ARG   I CZ  1 
ATOM   10677 N  NH1 . ARG   I  1 61  ? -47.904 -38.183  -50.158 1.00 26.63 ? 61  ARG   I NH1 1 
ATOM   10678 N  NH2 . ARG   I  1 61  ? -49.954 -38.786  -51.010 1.00 34.79 ? 61  ARG   I NH2 1 
ATOM   10679 N  N   . ILE   I  1 62  ? -49.188 -39.285  -43.251 1.00 30.27 ? 62  ILE   I N   1 
ATOM   10680 C  CA  . ILE   I  1 62  ? -50.361 -38.692  -42.600 1.00 27.82 ? 62  ILE   I CA  1 
ATOM   10681 C  C   . ILE   I  1 62  ? -50.121 -37.224  -42.297 1.00 30.48 ? 62  ILE   I C   1 
ATOM   10682 O  O   . ILE   I  1 62  ? -50.996 -36.378  -42.517 1.00 29.76 ? 62  ILE   I O   1 
ATOM   10683 C  CB  . ILE   I  1 62  ? -50.731 -39.481  -41.328 1.00 35.24 ? 62  ILE   I CB  1 
ATOM   10684 C  CG1 . ILE   I  1 62  ? -51.367 -40.820  -41.709 1.00 24.35 ? 62  ILE   I CG1 1 
ATOM   10685 C  CG2 . ILE   I  1 62  ? -51.694 -38.666  -40.470 1.00 29.12 ? 62  ILE   I CG2 1 
ATOM   10686 C  CD1 . ILE   I  1 62  ? -51.358 -41.882  -40.610 1.00 30.03 ? 62  ILE   I CD1 1 
ATOM   10687 N  N   . LEU   I  1 63  ? -48.940 -36.885  -41.769 1.00 30.63 ? 63  LEU   I N   1 
ATOM   10688 C  CA  . LEU   I  1 63  ? -48.692 -35.492  -41.430 1.00 26.58 ? 63  LEU   I CA  1 
ATOM   10689 C  C   . LEU   I  1 63  ? -48.607 -34.643  -42.679 1.00 28.42 ? 63  LEU   I C   1 
ATOM   10690 O  O   . LEU   I  1 63  ? -49.104 -33.517  -42.694 1.00 27.90 ? 63  LEU   I O   1 
ATOM   10691 C  CB  . LEU   I  1 63  ? -47.404 -35.347  -40.598 1.00 28.22 ? 63  LEU   I CB  1 
ATOM   10692 C  CG  . LEU   I  1 63  ? -47.411 -35.949  -39.196 1.00 27.31 ? 63  LEU   I CG  1 
ATOM   10693 C  CD1 . LEU   I  1 63  ? -45.937 -36.095  -38.657 1.00 27.69 ? 63  LEU   I CD1 1 
ATOM   10694 C  CD2 . LEU   I  1 63  ? -48.215 -35.085  -38.262 1.00 30.14 ? 63  LEU   I CD2 1 
ATOM   10695 N  N   . PHE   I  1 64  ? -47.956 -35.154  -43.738 1.00 27.16 ? 64  PHE   I N   1 
ATOM   10696 C  CA  . PHE   I  1 64  ? -47.964 -34.434  -45.004 1.00 29.64 ? 64  PHE   I CA  1 
ATOM   10697 C  C   . PHE   I  1 64  ? -49.396 -34.113  -45.436 1.00 27.42 ? 64  PHE   I C   1 
ATOM   10698 O  O   . PHE   I  1 64  ? -49.679 -33.001  -45.896 1.00 26.91 ? 64  PHE   I O   1 
ATOM   10699 C  CB  . PHE   I  1 64  ? -47.264 -35.247  -46.103 1.00 34.71 ? 64  PHE   I CB  1 
ATOM   10700 C  CG  . PHE   I  1 64  ? -47.412 -34.653  -47.485 1.00 28.28 ? 64  PHE   I CG  1 
ATOM   10701 C  CD1 . PHE   I  1 64  ? -46.975 -33.369  -47.745 1.00 29.91 ? 64  PHE   I CD1 1 
ATOM   10702 C  CD2 . PHE   I  1 64  ? -47.999 -35.378  -48.509 1.00 31.29 ? 64  PHE   I CD2 1 
ATOM   10703 C  CE1 . PHE   I  1 64  ? -47.116 -32.816  -49.029 1.00 34.80 ? 64  PHE   I CE1 1 
ATOM   10704 C  CE2 . PHE   I  1 64  ? -48.139 -34.841  -49.797 1.00 33.27 ? 64  PHE   I CE2 1 
ATOM   10705 C  CZ  . PHE   I  1 64  ? -47.701 -33.555  -50.050 1.00 28.90 ? 64  PHE   I CZ  1 
ATOM   10706 N  N   . LEU   I  1 65  ? -50.296 -35.084  -45.307 1.00 33.16 ? 65  LEU   I N   1 
ATOM   10707 C  CA  . LEU   I  1 65  ? -51.713 -34.919  -45.669 1.00 37.86 ? 65  LEU   I CA  1 
ATOM   10708 C  C   . LEU   I  1 65  ? -52.515 -34.134  -44.622 1.00 38.49 ? 65  LEU   I C   1 
ATOM   10709 O  O   . LEU   I  1 65  ? -53.752 -34.004  -44.748 1.00 31.26 ? 65  LEU   I O   1 
ATOM   10710 C  CB  . LEU   I  1 65  ? -52.364 -36.291  -45.905 1.00 29.24 ? 65  LEU   I CB  1 
ATOM   10711 C  CG  . LEU   I  1 65  ? -51.755 -37.116  -47.054 1.00 33.28 ? 65  LEU   I CG  1 
ATOM   10712 C  CD1 . LEU   I  1 65  ? -52.448 -38.491  -47.184 1.00 33.54 ? 65  LEU   I CD1 1 
ATOM   10713 C  CD2 . LEU   I  1 65  ? -51.801 -36.381  -48.366 1.00 34.77 ? 65  LEU   I CD2 1 
ATOM   10714 N  N   . GLU   I  1 66  ? -51.840 -33.592  -43.612 1.00 35.96 ? 66  GLU   I N   1 
ATOM   10715 C  CA  . GLU   I  1 66  ? -52.444 -32.702  -42.623 1.00 30.52 ? 66  GLU   I CA  1 
ATOM   10716 C  C   . GLU   I  1 66  ? -53.446 -33.432  -41.730 1.00 39.04 ? 66  GLU   I C   1 
ATOM   10717 O  O   . GLU   I  1 66  ? -54.387 -32.827  -41.215 1.00 34.17 ? 66  GLU   I O   1 
ATOM   10718 C  CB  . GLU   I  1 66  ? -53.084 -31.491  -43.321 1.00 37.19 ? 66  GLU   I CB  1 
ATOM   10719 C  CG  . GLU   I  1 66  ? -52.043 -30.754  -44.175 1.00 39.95 ? 66  GLU   I CG  1 
ATOM   10720 C  CD  . GLU   I  1 66  ? -52.478 -29.405  -44.718 1.00 39.02 ? 66  GLU   I CD  1 
ATOM   10721 O  OE1 . GLU   I  1 66  ? -53.340 -28.743  -44.115 1.00 45.47 ? 66  GLU   I OE1 1 
ATOM   10722 O  OE2 . GLU   I  1 66  ? -51.948 -28.998  -45.784 1.00 36.22 ? 66  GLU   I OE2 1 
ATOM   10723 N  N   . GLY   I  1 67  ? -53.265 -34.740  -41.563 1.00 27.70 ? 67  GLY   I N   1 
ATOM   10724 C  CA  . GLY   I  1 67  ? -53.964 -35.493  -40.550 1.00 26.98 ? 67  GLY   I CA  1 
ATOM   10725 C  C   . GLY   I  1 67  ? -53.140 -35.640  -39.273 1.00 41.71 ? 67  GLY   I C   1 
ATOM   10726 O  O   . GLY   I  1 67  ? -51.974 -35.253  -39.189 1.00 31.63 ? 67  GLY   I O   1 
ATOM   10727 N  N   . LEU   I  1 68  ? -53.779 -36.242  -38.279 1.00 31.15 ? 68  LEU   I N   1 
ATOM   10728 C  CA  . LEU   I  1 68  ? -53.168 -36.532  -36.994 1.00 29.33 ? 68  LEU   I CA  1 
ATOM   10729 C  C   . LEU   I  1 68  ? -52.883 -38.015  -36.886 1.00 34.11 ? 68  LEU   I C   1 
ATOM   10730 O  O   . LEU   I  1 68  ? -53.830 -38.814  -36.800 1.00 29.52 ? 68  LEU   I O   1 
ATOM   10731 C  CB  . LEU   I  1 68  ? -54.091 -36.088  -35.863 1.00 41.65 ? 68  LEU   I CB  1 
ATOM   10732 C  CG  . LEU   I  1 68  ? -54.269 -34.571  -35.811 1.00 47.12 ? 68  LEU   I CG  1 
ATOM   10733 C  CD1 . LEU   I  1 68  ? -55.218 -34.199  -34.687 1.00 61.03 ? 68  LEU   I CD1 1 
ATOM   10734 C  CD2 . LEU   I  1 68  ? -52.922 -33.853  -35.659 1.00 55.12 ? 68  LEU   I CD2 1 
ATOM   10735 N  N   . PRO   I  1 69  ? -51.622 -38.441  -36.866 1.00 29.11 ? 69  PRO   I N   1 
ATOM   10736 C  CA  . PRO   I  1 69  ? -51.347 -39.868  -36.721 1.00 28.88 ? 69  PRO   I CA  1 
ATOM   10737 C  C   . PRO   I  1 69  ? -51.746 -40.338  -35.339 1.00 31.12 ? 69  PRO   I C   1 
ATOM   10738 O  O   . PRO   I  1 69  ? -51.528 -39.646  -34.341 1.00 33.83 ? 69  PRO   I O   1 
ATOM   10739 C  CB  . PRO   I  1 69  ? -49.827 -39.965  -36.948 1.00 29.25 ? 69  PRO   I CB  1 
ATOM   10740 C  CG  . PRO   I  1 69  ? -49.413 -38.656  -37.441 1.00 30.99 ? 69  PRO   I CG  1 
ATOM   10741 C  CD  . PRO   I  1 69  ? -50.368 -37.671  -36.920 1.00 31.56 ? 69  PRO   I CD  1 
ATOM   10742 N  N   . ASN   I  1 70  ? -52.312 -41.534  -35.286 1.00 27.55 ? 70  ASN   I N   1 
ATOM   10743 C  CA  . ASN   I  1 70  ? -52.835 -42.101  -34.054 1.00 34.68 ? 70  ASN   I CA  1 
ATOM   10744 C  C   . ASN   I  1 70  ? -51.830 -43.131  -33.554 1.00 28.77 ? 70  ASN   I C   1 
ATOM   10745 O  O   . ASN   I  1 70  ? -51.788 -44.268  -34.033 1.00 28.76 ? 70  ASN   I O   1 
ATOM   10746 C  CB  . ASN   I  1 70  ? -54.222 -42.709  -34.284 1.00 37.79 ? 70  ASN   I CB  1 
ATOM   10747 C  CG  . ASN   I  1 70  ? -54.840 -43.242  -33.006 1.00 39.39 ? 70  ASN   I CG  1 
ATOM   10748 O  OD1 . ASN   I  1 70  ? -54.187 -43.287  -31.964 1.00 31.32 ? 70  ASN   I OD1 1 
ATOM   10749 N  ND2 . ASN   I  1 70  ? -56.108 -43.646  -33.076 1.00 29.36 ? 70  ASN   I ND2 1 
ATOM   10750 N  N   . LEU   I  1 71  ? -50.978 -42.705  -32.633 1.00 27.03 ? 71  LEU   I N   1 
ATOM   10751 C  CA  . LEU   I  1 71  ? -50.106 -43.619  -31.900 1.00 32.87 ? 71  LEU   I CA  1 
ATOM   10752 C  C   . LEU   I  1 71  ? -50.629 -43.905  -30.489 1.00 35.02 ? 71  LEU   I C   1 
ATOM   10753 O  O   . LEU   I  1 71  ? -49.894 -44.455  -29.652 1.00 31.00 ? 71  LEU   I O   1 
ATOM   10754 C  CB  . LEU   I  1 71  ? -48.680 -43.057  -31.828 1.00 37.16 ? 71  LEU   I CB  1 
ATOM   10755 C  CG  . LEU   I  1 71  ? -47.846 -43.051  -33.128 1.00 32.02 ? 71  LEU   I CG  1 
ATOM   10756 C  CD1 . LEU   I  1 71  ? -48.272 -41.914  -34.018 1.00 30.48 ? 71  LEU   I CD1 1 
ATOM   10757 C  CD2 . LEU   I  1 71  ? -46.326 -42.923  -32.785 1.00 30.26 ? 71  LEU   I CD2 1 
ATOM   10758 N  N   . GLN   I  1 72  ? -51.886 -43.547  -30.211 1.00 32.62 ? 72  GLN   I N   1 
ATOM   10759 C  CA  . GLN   I  1 72  ? -52.467 -43.735  -28.881 1.00 24.22 ? 72  GLN   I CA  1 
ATOM   10760 C  C   . GLN   I  1 72  ? -53.220 -45.054  -28.731 1.00 40.42 ? 72  GLN   I C   1 
ATOM   10761 O  O   . GLN   I  1 72  ? -53.205 -45.642  -27.642 1.00 38.77 ? 72  GLN   I O   1 
ATOM   10762 C  CB  . GLN   I  1 72  ? -53.398 -42.553  -28.563 1.00 35.91 ? 72  GLN   I CB  1 
ATOM   10763 C  CG  . GLN   I  1 72  ? -54.026 -42.577  -27.164 1.00 32.85 ? 72  GLN   I CG  1 
ATOM   10764 C  CD  . GLN   I  1 72  ? -53.003 -42.488  -26.041 1.00 29.37 ? 72  GLN   I CD  1 
ATOM   10765 O  OE1 . GLN   I  1 72  ? -52.669 -41.396  -25.568 1.00 32.16 ? 72  GLN   I OE1 1 
ATOM   10766 N  NE2 . GLN   I  1 72  ? -52.532 -43.647  -25.580 1.00 30.34 ? 72  GLN   I NE2 1 
ATOM   10767 N  N   . ASP   I  1 73  ? -53.865 -45.536  -29.796 1.00 37.17 ? 73  ASP   I N   1 
ATOM   10768 C  CA  . ASP   I  1 73  ? -54.754 -46.684  -29.731 1.00 34.31 ? 73  ASP   I CA  1 
ATOM   10769 C  C   . ASP   I  1 73  ? -54.012 -47.942  -30.147 1.00 39.69 ? 73  ASP   I C   1 
ATOM   10770 O  O   . ASP   I  1 73  ? -53.566 -48.067  -31.295 1.00 51.14 ? 73  ASP   I O   1 
ATOM   10771 C  CB  . ASP   I  1 73  ? -55.986 -46.436  -30.606 1.00 36.09 ? 73  ASP   I CB  1 
ATOM   10772 C  CG  . ASP   I  1 73  ? -56.819 -45.284  -30.086 1.00 34.63 ? 73  ASP   I CG  1 
ATOM   10773 O  OD1 . ASP   I  1 73  ? -56.721 -45.034  -28.874 1.00 43.55 ? 73  ASP   I OD1 1 
ATOM   10774 O  OD2 . ASP   I  1 73  ? -57.556 -44.627  -30.853 1.00 40.02 ? 73  ASP   I OD2 1 
ATOM   10775 N  N   . LEU   I  1 74  ? -53.880 -48.865  -29.205 1.00 31.37 ? 74  LEU   I N   1 
ATOM   10776 C  CA  . LEU   I  1 74  ? -53.150 -50.110  -29.383 1.00 31.72 ? 74  LEU   I CA  1 
ATOM   10777 C  C   . LEU   I  1 74  ? -54.134 -51.262  -29.271 1.00 34.27 ? 74  LEU   I C   1 
ATOM   10778 O  O   . LEU   I  1 74  ? -54.790 -51.422  -28.233 1.00 33.19 ? 74  LEU   I O   1 
ATOM   10779 C  CB  . LEU   I  1 74  ? -52.039 -50.248  -28.339 1.00 35.20 ? 74  LEU   I CB  1 
ATOM   10780 C  CG  . LEU   I  1 74  ? -51.195 -51.509  -28.503 1.00 31.21 ? 74  LEU   I CG  1 
ATOM   10781 C  CD1 . LEU   I  1 74  ? -50.531 -51.525  -29.918 1.00 42.19 ? 74  LEU   I CD1 1 
ATOM   10782 C  CD2 . LEU   I  1 74  ? -50.151 -51.651  -27.394 1.00 36.57 ? 74  LEU   I CD2 1 
ATOM   10783 N  N   . GLY   I  1 75  ? -54.274 -52.014  -30.360 1.00 38.02 ? 75  GLY   I N   1 
ATOM   10784 C  CA  . GLY   I  1 75  ? -55.159 -53.153  -30.420 1.00 31.78 ? 75  GLY   I CA  1 
ATOM   10785 C  C   . GLY   I  1 75  ? -54.561 -54.357  -29.741 1.00 37.30 ? 75  GLY   I C   1 
ATOM   10786 O  O   . GLY   I  1 75  ? -53.470 -54.326  -29.176 1.00 37.77 ? 75  GLY   I O   1 
ATOM   10787 N  N   . LYS   I  1 76  ? -55.295 -55.453  -29.821 1.00 33.05 ? 76  LYS   I N   1 
ATOM   10788 C  CA  . LYS   I  1 76  ? -54.970 -56.657  -29.071 1.00 33.96 ? 76  LYS   I CA  1 
ATOM   10789 C  C   . LYS   I  1 76  ? -53.787 -57.360  -29.710 1.00 37.22 ? 76  LYS   I C   1 
ATOM   10790 O  O   . LYS   I  1 76  ? -53.823 -57.695  -30.898 1.00 33.92 ? 76  LYS   I O   1 
ATOM   10791 C  CB  . LYS   I  1 76  ? -56.187 -57.598  -29.030 1.00 38.90 ? 76  LYS   I CB  1 
ATOM   10792 C  CG  . LYS   I  1 76  ? -55.898 -58.951  -28.378 1.00 41.46 ? 76  LYS   I CG  1 
ATOM   10793 N  N   . LEU   I  1 77  ? -52.745 -57.603  -28.916 1.00 31.58 ? 77  LEU   I N   1 
ATOM   10794 C  CA  . LEU   I  1 77  ? -51.636 -58.423  -29.361 1.00 38.11 ? 77  LEU   I CA  1 
ATOM   10795 C  C   . LEU   I  1 77  ? -52.009 -59.888  -29.239 1.00 37.11 ? 77  LEU   I C   1 
ATOM   10796 O  O   . LEU   I  1 77  ? -52.703 -60.294  -28.303 1.00 40.60 ? 77  LEU   I O   1 
ATOM   10797 C  CB  . LEU   I  1 77  ? -50.373 -58.154  -28.526 1.00 39.12 ? 77  LEU   I CB  1 
ATOM   10798 C  CG  . LEU   I  1 77  ? -50.079 -56.715  -28.096 1.00 38.78 ? 77  LEU   I CG  1 
ATOM   10799 C  CD1 . LEU   I  1 77  ? -48.804 -56.676  -27.233 1.00 38.18 ? 77  LEU   I CD1 1 
ATOM   10800 C  CD2 . LEU   I  1 77  ? -49.956 -55.813  -29.289 1.00 34.74 ? 77  LEU   I CD2 1 
ATOM   10801 N  N   . LEU   I  1 78  ? -51.531 -60.670  -30.179 1.00 32.57 ? 78  LEU   I N   1 
ATOM   10802 C  CA  . LEU   I  1 78  ? -51.711 -62.111  -30.231 1.00 36.79 ? 78  LEU   I CA  1 
ATOM   10803 C  C   . LEU   I  1 78  ? -50.358 -62.732  -29.897 1.00 40.00 ? 78  LEU   I C   1 
ATOM   10804 O  O   . LEU   I  1 78  ? -49.459 -62.789  -30.746 1.00 30.66 ? 78  LEU   I O   1 
ATOM   10805 C  CB  . LEU   I  1 78  ? -52.213 -62.531  -31.614 1.00 38.26 ? 78  LEU   I CB  1 
ATOM   10806 C  CG  . LEU   I  1 78  ? -53.310 -61.630  -32.219 1.00 55.19 ? 78  LEU   I CG  1 
ATOM   10807 C  CD1 . LEU   I  1 78  ? -53.625 -62.011  -33.659 1.00 42.89 ? 78  LEU   I CD1 1 
ATOM   10808 C  CD2 . LEU   I  1 78  ? -54.593 -61.659  -31.389 1.00 42.95 ? 78  LEU   I CD2 1 
ATOM   10809 N  N   . ILE   I  1 79  ? -50.215 -63.198  -28.659 1.00 40.91 ? 79  ILE   I N   1 
ATOM   10810 C  CA  . ILE   I  1 79  ? -48.964 -63.758  -28.159 1.00 29.46 ? 79  ILE   I CA  1 
ATOM   10811 C  C   . ILE   I  1 79  ? -49.147 -65.260  -28.019 1.00 40.13 ? 79  ILE   I C   1 
ATOM   10812 O  O   . ILE   I  1 79  ? -50.072 -65.713  -27.343 1.00 42.74 ? 79  ILE   I O   1 
ATOM   10813 C  CB  . ILE   I  1 79  ? -48.564 -63.120  -26.815 1.00 34.88 ? 79  ILE   I CB  1 
ATOM   10814 C  CG1 . ILE   I  1 79  ? -48.601 -61.582  -26.895 1.00 37.90 ? 79  ILE   I CG1 1 
ATOM   10815 C  CG2 . ILE   I  1 79  ? -47.210 -63.634  -26.355 1.00 40.46 ? 79  ILE   I CG2 1 
ATOM   10816 C  CD1 . ILE   I  1 79  ? -47.710 -60.966  -28.007 1.00 40.91 ? 79  ILE   I CD1 1 
ATOM   10817 N  N   . GLY   I  1 80  ? -48.276 -66.040  -28.651 1.00 30.49 ? 80  GLY   I N   1 
ATOM   10818 C  CA  . GLY   I  1 80  ? -48.367 -67.476  -28.475 1.00 40.04 ? 80  GLY   I CA  1 
ATOM   10819 C  C   . GLY   I  1 80  ? -47.721 -67.963  -27.176 1.00 43.71 ? 80  GLY   I C   1 
ATOM   10820 O  O   . GLY   I  1 80  ? -47.044 -67.228  -26.451 1.00 44.84 ? 80  GLY   I O   1 
ATOM   10821 N  N   . GLU   I  1 81  ? -47.934 -69.249  -26.891 1.00 33.69 ? 81  GLU   I N   1 
ATOM   10822 C  CA  . GLU   I  1 81  ? -47.327 -69.905  -25.743 1.00 45.23 ? 81  GLU   I CA  1 
ATOM   10823 C  C   . GLU   I  1 81  ? -46.268 -70.919  -26.129 1.00 41.24 ? 81  GLU   I C   1 
ATOM   10824 O  O   . GLU   I  1 81  ? -45.572 -71.437  -25.246 1.00 37.73 ? 81  GLU   I O   1 
ATOM   10825 C  CB  . GLU   I  1 81  ? -48.410 -70.593  -24.899 1.00 54.57 ? 81  GLU   I CB  1 
ATOM   10826 C  CG  . GLU   I  1 81  ? -49.270 -69.613  -24.137 1.00 67.52 ? 81  GLU   I CG  1 
ATOM   10827 C  CD  . GLU   I  1 81  ? -50.184 -70.287  -23.128 1.00 73.20 ? 81  GLU   I CD  1 
ATOM   10828 O  OE1 . GLU   I  1 81  ? -49.687 -71.039  -22.257 1.00 77.33 ? 81  GLU   I OE1 1 
ATOM   10829 O  OE2 . GLU   I  1 81  ? -51.403 -70.061  -23.219 1.00 55.97 ? 81  GLU   I OE2 1 
ATOM   10830 N  N   . ASN   I  1 82  ? -46.132 -71.219  -27.411 1.00 38.16 ? 82  ASN   I N   1 
ATOM   10831 C  CA  . ASN   I  1 82  ? -45.063 -72.056  -27.905 1.00 35.97 ? 82  ASN   I CA  1 
ATOM   10832 C  C   . ASN   I  1 82  ? -44.746 -71.591  -29.323 1.00 30.61 ? 82  ASN   I C   1 
ATOM   10833 O  O   . ASN   I  1 82  ? -45.415 -70.712  -29.866 1.00 28.37 ? 82  ASN   I O   1 
ATOM   10834 C  CB  . ASN   I  1 82  ? -45.453 -73.529  -27.860 1.00 39.50 ? 82  ASN   I CB  1 
ATOM   10835 C  CG  . ASN   I  1 82  ? -46.745 -73.785  -28.564 1.00 41.01 ? 82  ASN   I CG  1 
ATOM   10836 O  OD1 . ASN   I  1 82  ? -46.934 -73.349  -29.697 1.00 36.32 ? 82  ASN   I OD1 1 
ATOM   10837 N  ND2 . ASN   I  1 82  ? -47.673 -74.454  -27.883 1.00 40.22 ? 82  ASN   I ND2 1 
ATOM   10838 N  N   . THR   I  1 83  ? -43.692 -72.164  -29.905 1.00 33.80 ? 83  THR   I N   1 
ATOM   10839 C  CA  . THR   I  1 83  ? -43.206 -71.665  -31.194 1.00 40.50 ? 83  THR   I CA  1 
ATOM   10840 C  C   . THR   I  1 83  ? -44.294 -71.765  -32.255 1.00 30.99 ? 83  THR   I C   1 
ATOM   10841 O  O   . THR   I  1 83  ? -44.627 -70.769  -32.913 1.00 33.91 ? 83  THR   I O   1 
ATOM   10842 C  CB  . THR   I  1 83  ? -41.925 -72.408  -31.603 1.00 31.13 ? 83  THR   I CB  1 
ATOM   10843 O  OG1 . THR   I  1 83  ? -40.860 -72.036  -30.723 1.00 34.05 ? 83  THR   I OG1 1 
ATOM   10844 C  CG2 . THR   I  1 83  ? -41.487 -72.054  -33.024 1.00 31.12 ? 83  THR   I CG2 1 
ATOM   10845 N  N   . GLN   I  1 84  ? -44.923 -72.939  -32.391 1.00 38.12 ? 84  GLN   I N   1 
ATOM   10846 C  CA  . GLN   I  1 84  ? -45.973 -73.077  -33.407 1.00 33.61 ? 84  GLN   I CA  1 
ATOM   10847 C  C   . GLN   I  1 84  ? -47.057 -72.018  -33.242 1.00 32.39 ? 84  GLN   I C   1 
ATOM   10848 O  O   . GLN   I  1 84  ? -47.502 -71.408  -34.222 1.00 36.92 ? 84  GLN   I O   1 
ATOM   10849 C  CB  . GLN   I  1 84  ? -46.584 -74.484  -33.371 1.00 39.01 ? 84  GLN   I CB  1 
ATOM   10850 C  CG  . GLN   I  1 84  ? -47.432 -74.776  -34.617 1.00 49.06 ? 84  GLN   I CG  1 
ATOM   10851 C  CD  . GLN   I  1 84  ? -47.943 -76.211  -34.685 1.00 60.70 ? 84  GLN   I CD  1 
ATOM   10852 O  OE1 . GLN   I  1 84  ? -47.177 -77.151  -34.916 1.00 60.50 ? 84  GLN   I OE1 1 
ATOM   10853 N  NE2 . GLN   I  1 84  ? -49.244 -76.381  -34.497 1.00 71.80 ? 84  GLN   I NE2 1 
ATOM   10854 N  N   . GLU   I  1 85  ? -47.506 -71.783  -32.008 1.00 33.21 ? 85  GLU   I N   1 
ATOM   10855 C  CA  . GLU   I  1 85  ? -48.572 -70.807  -31.794 1.00 36.53 ? 85  GLU   I CA  1 
ATOM   10856 C  C   . GLU   I  1 85  ? -48.115 -69.396  -32.110 1.00 29.31 ? 85  GLU   I C   1 
ATOM   10857 O  O   . GLU   I  1 85  ? -48.891 -68.596  -32.630 1.00 32.91 ? 85  GLU   I O   1 
ATOM   10858 C  CB  . GLU   I  1 85  ? -49.086 -70.865  -30.344 1.00 38.86 ? 85  GLU   I CB  1 
ATOM   10859 C  CG  . GLU   I  1 85  ? -49.989 -72.034  -30.051 1.00 51.63 ? 85  GLU   I CG  1 
ATOM   10860 C  CD  . GLU   I  1 85  ? -50.441 -72.092  -28.598 1.00 62.05 ? 85  GLU   I CD  1 
ATOM   10861 O  OE1 . GLU   I  1 85  ? -50.272 -71.080  -27.857 1.00 47.90 ? 85  GLU   I OE1 1 
ATOM   10862 O  OE2 . GLU   I  1 85  ? -50.955 -73.167  -28.214 1.00 55.60 ? 85  GLU   I OE2 1 
ATOM   10863 N  N   . MET   I  1 86  ? -46.874 -69.052  -31.762 1.00 32.05 ? 86  MET   I N   1 
ATOM   10864 C  CA  . MET   I  1 86  ? -46.399 -67.695  -32.024 1.00 32.21 ? 86  MET   I CA  1 
ATOM   10865 C  C   . MET   I  1 86  ? -46.383 -67.418  -33.526 1.00 24.02 ? 86  MET   I C   1 
ATOM   10866 O  O   . MET   I  1 86  ? -46.852 -66.373  -33.987 1.00 29.28 ? 86  MET   I O   1 
ATOM   10867 C  CB  . MET   I  1 86  ? -45.010 -67.512  -31.404 1.00 30.86 ? 86  MET   I CB  1 
ATOM   10868 C  CG  . MET   I  1 86  ? -44.973 -67.696  -29.874 1.00 33.05 ? 86  MET   I CG  1 
ATOM   10869 S  SD  . MET   I  1 86  ? -43.405 -68.264  -29.173 1.00 33.56 ? 86  MET   I SD  1 
ATOM   10870 C  CE  . MET   I  1 86  ? -42.404 -66.776  -29.352 1.00 36.52 ? 86  MET   I CE  1 
ATOM   10871 N  N   . LEU   I  1 87  ? -45.870 -68.367  -34.302 1.00 28.86 ? 87  LEU   I N   1 
ATOM   10872 C  CA  . LEU   I  1 87  ? -45.909 -68.252  -35.757 1.00 31.46 ? 87  LEU   I CA  1 
ATOM   10873 C  C   . LEU   I  1 87  ? -47.334 -68.102  -36.272 1.00 31.24 ? 87  LEU   I C   1 
ATOM   10874 O  O   . LEU   I  1 87  ? -47.609 -67.258  -37.133 1.00 32.13 ? 87  LEU   I O   1 
ATOM   10875 C  CB  . LEU   I  1 87  ? -45.241 -69.480  -36.358 1.00 29.47 ? 87  LEU   I CB  1 
ATOM   10876 C  CG  . LEU   I  1 87  ? -43.739 -69.542  -36.125 1.00 29.03 ? 87  LEU   I CG  1 
ATOM   10877 C  CD1 . LEU   I  1 87  ? -43.214 -70.880  -36.562 1.00 29.60 ? 87  LEU   I CD1 1 
ATOM   10878 C  CD2 . LEU   I  1 87  ? -43.020 -68.401  -36.876 1.00 32.35 ? 87  LEU   I CD2 1 
ATOM   10879 N  N   . GLN   I  1 88  ? -48.259 -68.911  -35.757 1.00 30.48 ? 88  GLN   I N   1 
ATOM   10880 C  CA  . GLN   I  1 88  ? -49.653 -68.818  -36.204 1.00 27.87 ? 88  GLN   I CA  1 
ATOM   10881 C  C   . GLN   I  1 88  ? -50.264 -67.478  -35.797 1.00 27.42 ? 88  GLN   I C   1 
ATOM   10882 O  O   . GLN   I  1 88  ? -51.055 -66.895  -36.546 1.00 29.86 ? 88  GLN   I O   1 
ATOM   10883 C  CB  . GLN   I  1 88  ? -50.443 -70.008  -35.639 1.00 27.26 ? 88  GLN   I CB  1 
ATOM   10884 C  CG  . GLN   I  1 88  ? -51.898 -70.143  -36.165 1.00 49.53 ? 88  GLN   I CG  1 
ATOM   10885 C  CD  . GLN   I  1 88  ? -51.989 -70.334  -37.691 1.00 56.04 ? 88  GLN   I CD  1 
ATOM   10886 O  OE1 . GLN   I  1 88  ? -51.346 -71.219  -38.259 1.00 50.59 ? 88  GLN   I OE1 1 
ATOM   10887 N  NE2 . GLN   I  1 88  ? -52.793 -69.500  -38.349 1.00 42.38 ? 88  GLN   I NE2 1 
ATOM   10888 N  N   . CYS   I  1 89  ? -49.873 -66.945  -34.637 1.00 32.14 ? 89  CYS   I N   1 
ATOM   10889 C  CA  . CYS   I  1 89  ? -50.357 -65.628  -34.233 1.00 22.91 ? 89  CYS   I CA  1 
ATOM   10890 C  C   . CYS   I  1 89  ? -49.859 -64.542  -35.178 1.00 29.69 ? 89  CYS   I C   1 
ATOM   10891 O  O   . CYS   I  1 89  ? -50.623 -63.658  -35.572 1.00 29.21 ? 89  CYS   I O   1 
ATOM   10892 C  CB  . CYS   I  1 89  ? -49.920 -65.316  -32.806 1.00 30.85 ? 89  CYS   I CB  1 
ATOM   10893 S  SG  . CYS   I  1 89  ? -50.941 -66.101  -31.513 1.00 36.27 ? 89  CYS   I SG  1 
ATOM   10894 N  N   . ASP   I  1 90  ? -48.555 -64.560  -35.497 1.00 26.10 ? 90  ASP   I N   1 
ATOM   10895 C  CA  . ASP   I  1 90  ? -48.024 -63.633  -36.497 1.00 27.27 ? 90  ASP   I CA  1 
ATOM   10896 C  C   . ASP   I  1 90  ? -48.796 -63.770  -37.808 1.00 27.85 ? 90  ASP   I C   1 
ATOM   10897 O  O   . ASP   I  1 90  ? -49.205 -62.777  -38.428 1.00 28.10 ? 90  ASP   I O   1 
ATOM   10898 C  CB  . ASP   I  1 90  ? -46.533 -63.912  -36.738 1.00 31.50 ? 90  ASP   I CB  1 
ATOM   10899 C  CG  . ASP   I  1 90  ? -45.632 -63.511  -35.564 1.00 31.07 ? 90  ASP   I CG  1 
ATOM   10900 O  OD1 . ASP   I  1 90  ? -46.109 -62.975  -34.536 1.00 31.33 ? 90  ASP   I OD1 1 
ATOM   10901 O  OD2 . ASP   I  1 90  ? -44.413 -63.753  -35.687 1.00 31.37 ? 90  ASP   I OD2 1 
ATOM   10902 N  N   . LEU   I  1 91  ? -49.013 -65.006  -38.246 1.00 29.00 ? 91  LEU   I N   1 
ATOM   10903 C  CA  . LEU   I  1 91  ? -49.664 -65.199  -39.541 1.00 29.51 ? 91  LEU   I CA  1 
ATOM   10904 C  C   . LEU   I  1 91  ? -51.078 -64.632  -39.520 1.00 32.01 ? 91  LEU   I C   1 
ATOM   10905 O  O   . LEU   I  1 91  ? -51.493 -63.953  -40.465 1.00 35.81 ? 91  LEU   I O   1 
ATOM   10906 C  CB  . LEU   I  1 91  ? -49.648 -66.677  -39.912 1.00 30.32 ? 91  LEU   I CB  1 
ATOM   10907 C  CG  . LEU   I  1 91  ? -50.381 -67.057  -41.211 1.00 30.09 ? 91  LEU   I CG  1 
ATOM   10908 C  CD1 . LEU   I  1 91  ? -49.885 -66.249  -42.443 1.00 35.17 ? 91  LEU   I CD1 1 
ATOM   10909 C  CD2 . LEU   I  1 91  ? -50.165 -68.533  -41.424 1.00 32.60 ? 91  LEU   I CD2 1 
ATOM   10910 N  N   . ASN   I  1 92  ? -51.801 -64.828  -38.407 1.00 34.26 ? 92  ASN   I N   1 
ATOM   10911 C  CA  . ASN   I  1 92  ? -53.167 -64.319  -38.294 1.00 31.56 ? 92  ASN   I CA  1 
ATOM   10912 C  C   . ASN   I  1 92  ? -53.196 -62.806  -38.367 1.00 29.32 ? 92  ASN   I C   1 
ATOM   10913 O  O   . ASN   I  1 92  ? -54.006 -62.230  -39.097 1.00 27.91 ? 92  ASN   I O   1 
ATOM   10914 C  CB  . ASN   I  1 92  ? -53.815 -64.803  -36.987 1.00 35.24 ? 92  ASN   I CB  1 
ATOM   10915 C  CG  . ASN   I  1 92  ? -54.215 -66.267  -37.045 1.00 46.13 ? 92  ASN   I CG  1 
ATOM   10916 O  OD1 . ASN   I  1 92  ? -54.296 -66.867  -38.129 1.00 44.47 ? 92  ASN   I OD1 1 
ATOM   10917 N  ND2 . ASN   I  1 92  ? -54.466 -66.854  -35.881 1.00 51.74 ? 92  ASN   I ND2 1 
ATOM   10918 N  N   . LEU   I  1 93  ? -52.316 -62.138  -37.608 1.00 34.00 ? 93  LEU   I N   1 
ATOM   10919 C  CA  . LEU   I  1 93  ? -52.224 -60.683  -37.688 1.00 29.80 ? 93  LEU   I CA  1 
ATOM   10920 C  C   . LEU   I  1 93  ? -51.869 -60.215  -39.103 1.00 29.47 ? 93  LEU   I C   1 
ATOM   10921 O  O   . LEU   I  1 93  ? -52.402 -59.202  -39.576 1.00 31.34 ? 93  LEU   I O   1 
ATOM   10922 C  CB  . LEU   I  1 93  ? -51.179 -60.182  -36.687 1.00 29.77 ? 93  LEU   I CB  1 
ATOM   10923 C  CG  . LEU   I  1 93  ? -50.830 -58.689  -36.706 1.00 30.18 ? 93  LEU   I CG  1 
ATOM   10924 C  CD1 . LEU   I  1 93  ? -52.041 -57.836  -36.444 1.00 35.35 ? 93  LEU   I CD1 1 
ATOM   10925 C  CD2 . LEU   I  1 93  ? -49.792 -58.377  -35.669 1.00 31.57 ? 93  LEU   I CD2 1 
ATOM   10926 N  N   . GLU   I  1 94  ? -50.941 -60.917  -39.775 1.00 34.86 ? 94  GLU   I N   1 
ATOM   10927 C  CA  . GLU   I  1 94  ? -50.562 -60.536  -41.148 1.00 35.87 ? 94  GLU   I CA  1 
ATOM   10928 C  C   . GLU   I  1 94  ? -51.752 -60.606  -42.109 1.00 35.22 ? 94  GLU   I C   1 
ATOM   10929 O  O   . GLU   I  1 94  ? -51.930 -59.727  -42.958 1.00 33.45 ? 94  GLU   I O   1 
ATOM   10930 C  CB  . GLU   I  1 94  ? -49.429 -61.440  -41.648 1.00 35.03 ? 94  GLU   I CB  1 
ATOM   10931 C  CG  . GLU   I  1 94  ? -48.075 -61.129  -40.980 1.00 36.05 ? 94  GLU   I CG  1 
ATOM   10932 C  CD  . GLU   I  1 94  ? -47.422 -59.852  -41.519 1.00 39.33 ? 94  GLU   I CD  1 
ATOM   10933 O  OE1 . GLU   I  1 94  ? -47.974 -59.220  -42.429 1.00 34.49 ? 94  GLU   I OE1 1 
ATOM   10934 O  OE2 . GLU   I  1 94  ? -46.337 -59.481  -41.042 1.00 52.49 ? 94  GLU   I OE2 1 
ATOM   10935 N  N   . LEU   I  1 95  ? -52.585 -61.634  -41.986 1.00 35.89 ? 95  LEU   I N   1 
ATOM   10936 C  CA  . LEU   I  1 95  ? -53.742 -61.730  -42.881 1.00 34.02 ? 95  LEU   I CA  1 
ATOM   10937 C  C   . LEU   I  1 95  ? -54.738 -60.610  -42.624 1.00 37.47 ? 95  LEU   I C   1 
ATOM   10938 O  O   . LEU   I  1 95  ? -55.308 -60.046  -43.572 1.00 32.57 ? 95  LEU   I O   1 
ATOM   10939 C  CB  . LEU   I  1 95  ? -54.391 -63.091  -42.726 1.00 35.27 ? 95  LEU   I CB  1 
ATOM   10940 C  CG  . LEU   I  1 95  ? -53.429 -64.181  -43.140 1.00 36.70 ? 95  LEU   I CG  1 
ATOM   10941 C  CD1 . LEU   I  1 95  ? -53.894 -65.515  -42.624 1.00 42.23 ? 95  LEU   I CD1 1 
ATOM   10942 C  CD2 . LEU   I  1 95  ? -53.285 -64.195  -44.668 1.00 39.06 ? 95  LEU   I CD2 1 
ATOM   10943 N  N   . LYS   I  1 96  ? -54.943 -60.247  -41.358 1.00 33.77 ? 96  LYS   I N   1 
ATOM   10944 C  CA  . LYS   I  1 96  ? -55.741 -59.064  -41.087 1.00 31.90 ? 96  LYS   I CA  1 
ATOM   10945 C  C   . LYS   I  1 96  ? -55.121 -57.839  -41.730 1.00 37.11 ? 96  LYS   I C   1 
ATOM   10946 O  O   . LYS   I  1 96  ? -55.825 -57.047  -42.368 1.00 33.51 ? 96  LYS   I O   1 
ATOM   10947 C  CB  . LYS   I  1 96  ? -55.900 -58.855  -39.586 1.00 37.21 ? 96  LYS   I CB  1 
ATOM   10948 C  CG  . LYS   I  1 96  ? -56.485 -57.518  -39.206 1.00 41.67 ? 96  LYS   I CG  1 
ATOM   10949 N  N   . ALA   I  1 97  ? -53.791 -57.685  -41.624 1.00 33.87 ? 97  ALA   I N   1 
ATOM   10950 C  CA  . ALA   I  1 97  ? -53.176 -56.446  -42.104 1.00 37.63 ? 97  ALA   I CA  1 
ATOM   10951 C  C   . ALA   I  1 97  ? -53.264 -56.330  -43.626 1.00 24.48 ? 97  ALA   I C   1 
ATOM   10952 O  O   . ALA   I  1 97  ? -53.434 -55.230  -44.162 1.00 28.41 ? 97  ALA   I O   1 
ATOM   10953 C  CB  . ALA   I  1 97  ? -51.718 -56.373  -41.629 1.00 38.95 ? 97  ALA   I CB  1 
ATOM   10954 N  N   . THR   I  1 98  ? -53.099 -57.442  -44.346 1.00 27.12 ? 98  THR   I N   1 
ATOM   10955 C  CA  . THR   I  1 98  ? -53.117 -57.363  -45.805 1.00 34.72 ? 98  THR   I CA  1 
ATOM   10956 C  C   . THR   I  1 98  ? -54.542 -57.142  -46.317 1.00 34.16 ? 98  THR   I C   1 
ATOM   10957 O  O   . THR   I  1 98  ? -54.759 -56.398  -47.287 1.00 34.26 ? 98  THR   I O   1 
ATOM   10958 C  CB  . THR   I  1 98  ? -52.508 -58.628  -46.414 1.00 34.11 ? 98  THR   I CB  1 
ATOM   10959 O  OG1 . THR   I  1 98  ? -53.186 -59.779  -45.906 1.00 32.20 ? 98  THR   I OG1 1 
ATOM   10960 C  CG2 . THR   I  1 98  ? -51.025 -58.744  -46.078 1.00 31.74 ? 98  THR   I CG2 1 
ATOM   10961 N  N   . LYS   I  1 99  ? -55.533 -57.735  -45.642 1.00 36.29 ? 99  LYS   I N   1 
ATOM   10962 C  CA  . LYS   I  1 99  ? -56.918 -57.403  -45.952 1.00 33.53 ? 99  LYS   I CA  1 
ATOM   10963 C  C   . LYS   I  1 99  ? -57.109 -55.907  -45.834 1.00 30.94 ? 99  LYS   I C   1 
ATOM   10964 O  O   . LYS   I  1 99  ? -57.642 -55.263  -46.743 1.00 30.44 ? 99  LYS   I O   1 
ATOM   10965 C  CB  . LYS   I  1 99  ? -57.881 -58.150  -45.015 1.00 33.13 ? 99  LYS   I CB  1 
ATOM   10966 C  CG  . LYS   I  1 99  ? -59.328 -57.603  -45.021 1.00 50.17 ? 99  LYS   I CG  1 
ATOM   10967 C  CD  . LYS   I  1 99  ? -60.161 -58.211  -43.881 1.00 49.49 ? 99  LYS   I CD  1 
ATOM   10968 N  N   . ASP   I  1 100 ? -56.628 -55.323  -44.730 1.00 30.40 ? 100 ASP   I N   1 
ATOM   10969 C  CA  . ASP   I  1 100 ? -56.835 -53.896  -44.509 1.00 26.10 ? 100 ASP   I CA  1 
ATOM   10970 C  C   . ASP   I  1 100 ? -56.055 -53.052  -45.510 1.00 31.66 ? 100 ASP   I C   1 
ATOM   10971 O  O   . ASP   I  1 100 ? -56.504 -51.958  -45.890 1.00 29.28 ? 100 ASP   I O   1 
ATOM   10972 C  CB  . ASP   I  1 100 ? -56.431 -53.494  -43.102 1.00 35.60 ? 100 ASP   I CB  1 
ATOM   10973 C  CG  . ASP   I  1 100 ? -57.349 -54.094  -42.022 1.00 44.24 ? 100 ASP   I CG  1 
ATOM   10974 O  OD1 . ASP   I  1 100 ? -58.451 -54.560  -42.356 1.00 38.88 ? 100 ASP   I OD1 1 
ATOM   10975 O  OD2 . ASP   I  1 100 ? -56.960 -54.096  -40.844 1.00 37.17 ? 100 ASP   I OD2 1 
ATOM   10976 N  N   . LEU   I  1 101 ? -54.839 -53.492  -45.863 1.00 34.16 ? 101 LEU   I N   1 
ATOM   10977 C  CA  . LEU   I  1 101 ? -54.071 -52.798  -46.892 1.00 33.53 ? 101 LEU   I CA  1 
ATOM   10978 C  C   . LEU   I  1 101 ? -54.845 -52.761  -48.219 1.00 29.74 ? 101 LEU   I C   1 
ATOM   10979 O  O   . LEU   I  1 101 ? -54.942 -51.710  -48.859 1.00 30.14 ? 101 LEU   I O   1 
ATOM   10980 C  CB  . LEU   I  1 101 ? -52.711 -53.487  -47.064 1.00 33.52 ? 101 LEU   I CB  1 
ATOM   10981 C  CG  . LEU   I  1 101 ? -51.651 -53.090  -46.021 1.00 29.95 ? 101 LEU   I CG  1 
ATOM   10982 C  CD1 . LEU   I  1 101 ? -50.550 -54.125  -45.967 1.00 28.39 ? 101 LEU   I CD1 1 
ATOM   10983 C  CD2 . LEU   I  1 101 ? -51.050 -51.715  -46.335 1.00 29.23 ? 101 LEU   I CD2 1 
ATOM   10984 N  N   . ARG   I  1 102 ? -55.365 -53.916  -48.653 1.00 28.43 ? 102 ARG   I N   1 
ATOM   10985 C  CA  . ARG   I  1 102 ? -56.130 -53.988  -49.904 1.00 31.85 ? 102 ARG   I CA  1 
ATOM   10986 C  C   . ARG   I  1 102 ? -57.290 -53.003  -49.900 1.00 32.26 ? 102 ARG   I C   1 
ATOM   10987 O  O   . ARG   I  1 102 ? -57.537 -52.309  -50.900 1.00 33.65 ? 102 ARG   I O   1 
ATOM   10988 C  CB  . ARG   I  1 102 ? -56.631 -55.416  -50.123 1.00 27.63 ? 102 ARG   I CB  1 
ATOM   10989 C  CG  . ARG   I  1 102 ? -55.544 -56.393  -50.442 1.00 31.67 ? 102 ARG   I CG  1 
ATOM   10990 C  CD  . ARG   I  1 102 ? -56.036 -57.804  -50.638 1.00 32.48 ? 102 ARG   I CD  1 
ATOM   10991 N  NE  . ARG   I  1 102 ? -55.025 -58.777  -50.234 1.00 35.26 ? 102 ARG   I NE  1 
ATOM   10992 C  CZ  . ARG   I  1 102 ? -53.890 -59.028  -50.885 1.00 38.72 ? 102 ARG   I CZ  1 
ATOM   10993 N  NH1 . ARG   I  1 102 ? -53.601 -58.439  -52.036 1.00 32.14 ? 102 ARG   I NH1 1 
ATOM   10994 N  NH2 . ARG   I  1 102 ? -53.014 -59.883  -50.360 1.00 31.83 ? 102 ARG   I NH2 1 
ATOM   10995 N  N   . GLU   I  1 103 ? -58.024 -52.912  -48.775 1.00 36.32 ? 103 GLU   I N   1 
ATOM   10996 C  CA  . GLU   I  1 103 ? -59.164 -51.996  -48.726 1.00 20.76 ? 103 GLU   I CA  1 
ATOM   10997 C  C   . GLU   I  1 103 ? -58.718 -50.549  -48.771 1.00 29.61 ? 103 GLU   I C   1 
ATOM   10998 O  O   . GLU   I  1 103 ? -59.382 -49.707  -49.381 1.00 27.71 ? 103 GLU   I O   1 
ATOM   10999 C  CB  . GLU   I  1 103 ? -60.013 -52.234  -47.460 1.00 30.41 ? 103 GLU   I CB  1 
ATOM   11000 C  CG  . GLU   I  1 103 ? -60.762 -53.550  -47.476 1.00 41.48 ? 103 GLU   I CG  1 
ATOM   11001 C  CD  . GLU   I  1 103 ? -61.398 -53.907  -46.129 1.00 57.44 ? 103 GLU   I CD  1 
ATOM   11002 O  OE1 . GLU   I  1 103 ? -61.277 -53.120  -45.161 1.00 51.47 ? 103 GLU   I OE1 1 
ATOM   11003 O  OE2 . GLU   I  1 103 ? -62.010 -54.993  -46.044 1.00 61.08 ? 103 GLU   I OE2 1 
ATOM   11004 N  N   . ALA   I  1 104 ? -57.593 -50.225  -48.127 1.00 28.25 ? 104 ALA   I N   1 
ATOM   11005 C  CA  . ALA   I  1 104 ? -57.135 -48.843  -48.172 1.00 27.00 ? 104 ALA   I CA  1 
ATOM   11006 C  C   . ALA   I  1 104 ? -56.693 -48.469  -49.586 1.00 26.89 ? 104 ALA   I C   1 
ATOM   11007 O  O   . ALA   I  1 104 ? -56.888 -47.333  -50.038 1.00 31.60 ? 104 ALA   I O   1 
ATOM   11008 C  CB  . ALA   I  1 104 ? -55.982 -48.654  -47.170 1.00 31.49 ? 104 ALA   I CB  1 
ATOM   11009 N  N   . ILE   I  1 105 ? -56.103 -49.418  -50.293 1.00 29.49 ? 105 ILE   I N   1 
ATOM   11010 C  CA  . ILE   I  1 105 ? -55.631 -49.158  -51.647 1.00 33.22 ? 105 ILE   I CA  1 
ATOM   11011 C  C   . ILE   I  1 105 ? -56.811 -48.876  -52.569 1.00 31.51 ? 105 ILE   I C   1 
ATOM   11012 O  O   . ILE   I  1 105 ? -56.803 -47.907  -53.341 1.00 28.59 ? 105 ILE   I O   1 
ATOM   11013 C  CB  . ILE   I  1 105 ? -54.796 -50.343  -52.145 1.00 22.85 ? 105 ILE   I CB  1 
ATOM   11014 C  CG1 . ILE   I  1 105 ? -53.386 -50.307  -51.499 1.00 26.86 ? 105 ILE   I CG1 1 
ATOM   11015 C  CG2 . ILE   I  1 105 ? -54.717 -50.304  -53.680 1.00 26.89 ? 105 ILE   I CG2 1 
ATOM   11016 C  CD1 . ILE   I  1 105 ? -52.651 -51.628  -51.596 1.00 30.23 ? 105 ILE   I CD1 1 
ATOM   11017 N  N   . VAL   I  1 106 ? -57.854 -49.709  -52.482 1.00 36.62 ? 106 VAL   I N   1 
ATOM   11018 C  CA  . VAL   I  1 106 ? -59.090 -49.429  -53.219 1.00 31.02 ? 106 VAL   I CA  1 
ATOM   11019 C  C   . VAL   I  1 106 ? -59.499 -47.982  -53.015 1.00 24.26 ? 106 VAL   I C   1 
ATOM   11020 O  O   . VAL   I  1 106 ? -59.804 -47.259  -53.975 1.00 35.33 ? 106 VAL   I O   1 
ATOM   11021 C  CB  . VAL   I  1 106 ? -60.220 -50.382  -52.776 1.00 28.92 ? 106 VAL   I CB  1 
ATOM   11022 C  CG1 . VAL   I  1 106 ? -61.528 -49.947  -53.393 1.00 38.12 ? 106 VAL   I CG1 1 
ATOM   11023 C  CG2 . VAL   I  1 106 ? -59.924 -51.777  -53.161 1.00 31.04 ? 106 VAL   I CG2 1 
ATOM   11024 N  N   . HIS   I  1 107 ? -59.529 -47.536  -51.760 1.00 30.33 ? 107 HIS   I N   1 
ATOM   11025 C  CA  . HIS   I  1 107 ? -59.999 -46.181  -51.506 1.00 26.62 ? 107 HIS   I CA  1 
ATOM   11026 C  C   . HIS   I  1 107 ? -59.042 -45.130  -52.052 1.00 34.72 ? 107 HIS   I C   1 
ATOM   11027 O  O   . HIS   I  1 107 ? -59.484 -44.100  -52.579 1.00 32.14 ? 107 HIS   I O   1 
ATOM   11028 C  CB  . HIS   I  1 107 ? -60.238 -45.926  -50.022 1.00 33.97 ? 107 HIS   I CB  1 
ATOM   11029 C  CG  . HIS   I  1 107 ? -60.740 -44.540  -49.758 1.00 37.01 ? 107 HIS   I CG  1 
ATOM   11030 N  ND1 . HIS   I  1 107 ? -62.030 -44.148  -50.051 1.00 38.19 ? 107 HIS   I ND1 1 
ATOM   11031 C  CD2 . HIS   I  1 107 ? -60.103 -43.433  -49.315 1.00 34.33 ? 107 HIS   I CD2 1 
ATOM   11032 C  CE1 . HIS   I  1 107 ? -62.172 -42.867  -49.777 1.00 33.76 ? 107 HIS   I CE1 1 
ATOM   11033 N  NE2 . HIS   I  1 107 ? -61.020 -42.410  -49.318 1.00 41.67 ? 107 HIS   I NE2 1 
ATOM   11034 N  N   . CYS   I  1 108 ? -57.730 -45.319  -51.873 1.00 37.67 ? 108 CYS   I N   1 
ATOM   11035 C  CA  . CYS   I  1 108 ? -56.795 -44.352  -52.438 1.00 28.25 ? 108 CYS   I CA  1 
ATOM   11036 C  C   . CYS   I  1 108 ? -56.998 -44.216  -53.936 1.00 25.00 ? 108 CYS   I C   1 
ATOM   11037 O  O   . CYS   I  1 108 ? -56.947 -43.108  -54.480 1.00 28.08 ? 108 CYS   I O   1 
ATOM   11038 C  CB  . CYS   I  1 108 ? -55.352 -44.769  -52.146 1.00 36.25 ? 108 CYS   I CB  1 
ATOM   11039 S  SG  . CYS   I  1 108 ? -54.941 -44.664  -50.359 1.00 32.93 ? 108 CYS   I SG  1 
ATOM   11040 N  N   . GLU   I  1 109 ? -57.170 -45.346  -54.619 1.00 25.88 ? 109 GLU   I N   1 
ATOM   11041 C  CA  . GLU   I  1 109 ? -57.360 -45.331  -56.063 1.00 30.08 ? 109 GLU   I CA  1 
ATOM   11042 C  C   . GLU   I  1 109 ? -58.615 -44.552  -56.432 1.00 35.26 ? 109 GLU   I C   1 
ATOM   11043 O  O   . GLU   I  1 109 ? -58.608 -43.742  -57.368 1.00 31.58 ? 109 GLU   I O   1 
ATOM   11044 C  CB  . GLU   I  1 109 ? -57.458 -46.770  -56.573 1.00 30.06 ? 109 GLU   I CB  1 
ATOM   11045 C  CG  . GLU   I  1 109 ? -57.695 -46.901  -58.055 1.00 34.10 ? 109 GLU   I CG  1 
ATOM   11046 C  CD  . GLU   I  1 109 ? -56.442 -46.581  -58.864 1.00 38.69 ? 109 GLU   I CD  1 
ATOM   11047 O  OE1 . GLU   I  1 109 ? -55.308 -46.640  -58.293 1.00 29.13 ? 109 GLU   I OE1 1 
ATOM   11048 O  OE2 . GLU   I  1 109 ? -56.600 -46.272  -60.059 1.00 29.34 ? 109 GLU   I OE2 1 
ATOM   11049 N  N   . GLN   I  1 110 ? -59.693 -44.759  -55.677 1.00 33.99 ? 110 GLN   I N   1 
ATOM   11050 C  CA  . GLN   I  1 110 ? -60.954 -44.082  -55.967 1.00 30.39 ? 110 GLN   I CA  1 
ATOM   11051 C  C   . GLN   I  1 110 ? -60.818 -42.571  -55.840 1.00 33.99 ? 110 GLN   I C   1 
ATOM   11052 O  O   . GLN   I  1 110 ? -61.376 -41.820  -56.653 1.00 33.65 ? 110 GLN   I O   1 
ATOM   11053 C  CB  . GLN   I  1 110 ? -62.032 -44.635  -55.030 1.00 33.30 ? 110 GLN   I CB  1 
ATOM   11054 C  CG  . GLN   I  1 110 ? -62.345 -46.111  -55.292 1.00 31.41 ? 110 GLN   I CG  1 
ATOM   11055 N  N   . VAL   I  1 111 ? -60.050 -42.086  -54.866 1.00 27.01 ? 111 VAL   I N   1 
ATOM   11056 C  CA  . VAL   I  1 111 ? -59.935 -40.635  -54.741 1.00 23.04 ? 111 VAL   I CA  1 
ATOM   11057 C  C   . VAL   I  1 111 ? -58.670 -40.115  -55.431 1.00 26.25 ? 111 VAL   I C   1 
ATOM   11058 O  O   . VAL   I  1 111 ? -58.359 -38.926  -55.341 1.00 31.18 ? 111 VAL   I O   1 
ATOM   11059 C  CB  . VAL   I  1 111 ? -59.993 -40.153  -53.270 1.00 30.74 ? 111 VAL   I CB  1 
ATOM   11060 C  CG1 . VAL   I  1 111 ? -61.377 -40.437  -52.653 1.00 40.03 ? 111 VAL   I CG1 1 
ATOM   11061 C  CG2 . VAL   I  1 111 ? -58.925 -40.776  -52.376 1.00 34.33 ? 111 VAL   I CG2 1 
ATOM   11062 N  N   . HIS   I  1 112 ? -57.951 -40.976  -56.145 1.00 30.65 ? 112 HIS   I N   1 
ATOM   11063 C  CA  . HIS   I  1 112 ? -56.809 -40.565  -56.963 1.00 32.12 ? 112 HIS   I CA  1 
ATOM   11064 C  C   . HIS   I  1 112 ? -55.601 -40.148  -56.118 1.00 34.36 ? 112 HIS   I C   1 
ATOM   11065 O  O   . HIS   I  1 112 ? -54.787 -39.318  -56.554 1.00 27.88 ? 112 HIS   I O   1 
ATOM   11066 C  CB  . HIS   I  1 112 ? -57.156 -39.404  -57.893 1.00 34.07 ? 112 HIS   I CB  1 
ATOM   11067 C  CG  . HIS   I  1 112 ? -58.391 -39.614  -58.722 1.00 41.81 ? 112 HIS   I CG  1 
ATOM   11068 N  ND1 . HIS   I  1 112 ? -58.874 -40.862  -59.050 1.00 41.83 ? 112 HIS   I ND1 1 
ATOM   11069 C  CD2 . HIS   I  1 112 ? -59.225 -38.723  -59.304 1.00 44.33 ? 112 HIS   I CD2 1 
ATOM   11070 C  CE1 . HIS   I  1 112 ? -59.964 -40.730  -59.791 1.00 43.05 ? 112 HIS   I CE1 1 
ATOM   11071 N  NE2 . HIS   I  1 112 ? -60.201 -39.441  -59.956 1.00 46.97 ? 112 HIS   I NE2 1 
ATOM   11072 N  N   . ASP   I  1 113 ? -55.504 -40.643  -54.891 1.00 30.40 ? 113 ASP   I N   1 
ATOM   11073 C  CA  . ASP   I  1 113 ? -54.284 -40.484  -54.100 1.00 30.21 ? 113 ASP   I CA  1 
ATOM   11074 C  C   . ASP   I  1 113 ? -53.307 -41.600  -54.493 1.00 25.28 ? 113 ASP   I C   1 
ATOM   11075 O  O   . ASP   I  1 113 ? -53.099 -42.588  -53.795 1.00 30.79 ? 113 ASP   I O   1 
ATOM   11076 C  CB  . ASP   I  1 113 ? -54.622 -40.498  -52.624 1.00 28.65 ? 113 ASP   I CB  1 
ATOM   11077 C  CG  . ASP   I  1 113 ? -53.446 -40.083  -51.746 1.00 42.11 ? 113 ASP   I CG  1 
ATOM   11078 O  OD1 . ASP   I  1 113 ? -52.315 -39.871  -52.268 1.00 30.01 ? 113 ASP   I OD1 1 
ATOM   11079 O  OD2 . ASP   I  1 113 ? -53.670 -39.980  -50.534 1.00 31.15 ? 113 ASP   I OD2 1 
ATOM   11080 N  N   . TYR   I  1 114 ? -52.717 -41.434  -55.672 1.00 25.94 ? 114 TYR   I N   1 
ATOM   11081 C  CA  . TYR   I  1 114 ? -51.886 -42.491  -56.218 1.00 28.47 ? 114 TYR   I CA  1 
ATOM   11082 C  C   . TYR   I  1 114 ? -50.568 -42.648  -55.458 1.00 29.17 ? 114 TYR   I C   1 
ATOM   11083 O  O   . TYR   I  1 114 ? -50.006 -43.747  -55.434 1.00 26.04 ? 114 TYR   I O   1 
ATOM   11084 C  CB  . TYR   I  1 114 ? -51.628 -42.203  -57.675 1.00 25.08 ? 114 TYR   I CB  1 
ATOM   11085 C  CG  . TYR   I  1 114 ? -52.914 -42.106  -58.475 1.00 28.13 ? 114 TYR   I CG  1 
ATOM   11086 C  CD1 . TYR   I  1 114 ? -53.763 -43.188  -58.552 1.00 30.18 ? 114 TYR   I CD1 1 
ATOM   11087 C  CD2 . TYR   I  1 114 ? -53.282 -40.930  -59.119 1.00 29.03 ? 114 TYR   I CD2 1 
ATOM   11088 C  CE1 . TYR   I  1 114 ? -54.967 -43.121  -59.283 1.00 32.79 ? 114 TYR   I CE1 1 
ATOM   11089 C  CE2 . TYR   I  1 114 ? -54.469 -40.854  -59.859 1.00 30.23 ? 114 TYR   I CE2 1 
ATOM   11090 C  CZ  . TYR   I  1 114 ? -55.298 -41.954  -59.925 1.00 30.03 ? 114 TYR   I CZ  1 
ATOM   11091 O  OH  . TYR   I  1 114 ? -56.463 -41.870  -60.639 1.00 39.03 ? 114 TYR   I OH  1 
ATOM   11092 N  N   . VAL   I  1 115 ? -50.104 -41.591  -54.800 1.00 29.25 ? 115 VAL   I N   1 
ATOM   11093 C  CA  . VAL   I  1 115 ? -48.885 -41.698  -53.990 1.00 31.99 ? 115 VAL   I CA  1 
ATOM   11094 C  C   . VAL   I  1 115 ? -49.150 -42.500  -52.716 1.00 31.83 ? 115 VAL   I C   1 
ATOM   11095 O  O   . VAL   I  1 115 ? -48.395 -43.414  -52.374 1.00 25.22 ? 115 VAL   I O   1 
ATOM   11096 C  CB  . VAL   I  1 115 ? -48.325 -40.295  -53.700 1.00 33.39 ? 115 VAL   I CB  1 
ATOM   11097 C  CG1 . VAL   I  1 115 ? -47.031 -40.388  -52.859 1.00 30.75 ? 115 VAL   I CG1 1 
ATOM   11098 C  CG2 . VAL   I  1 115 ? -48.079 -39.561  -55.035 1.00 32.82 ? 115 VAL   I CG2 1 
ATOM   11099 N  N   . SER   I  1 116 ? -50.259 -42.233  -52.021 1.00 27.13 ? 116 SER   I N   1 
ATOM   11100 C  CA  . SER   I  1 116 ? -50.571 -43.087  -50.878 1.00 24.76 ? 116 SER   I CA  1 
ATOM   11101 C  C   . SER   I  1 116 ? -50.733 -44.536  -51.317 1.00 26.12 ? 116 SER   I C   1 
ATOM   11102 O  O   . SER   I  1 116 ? -50.240 -45.458  -50.652 1.00 30.27 ? 116 SER   I O   1 
ATOM   11103 C  CB  . SER   I  1 116 ? -51.833 -42.592  -50.154 1.00 26.06 ? 116 SER   I CB  1 
ATOM   11104 O  OG  . SER   I  1 116 ? -51.631 -41.316  -49.588 1.00 26.20 ? 116 SER   I OG  1 
ATOM   11105 N  N   . ARG   I  1 117 ? -51.399 -44.758  -52.454 1.00 27.50 ? 117 ARG   I N   1 
ATOM   11106 C  CA  . ARG   I  1 117 ? -51.533 -46.116  -52.963 1.00 30.24 ? 117 ARG   I CA  1 
ATOM   11107 C  C   . ARG   I  1 117 ? -50.166 -46.769  -53.156 1.00 28.67 ? 117 ARG   I C   1 
ATOM   11108 O  O   . ARG   I  1 117 ? -49.970 -47.935  -52.786 1.00 27.61 ? 117 ARG   I O   1 
ATOM   11109 C  CB  . ARG   I  1 117 ? -52.322 -46.132  -54.289 1.00 28.99 ? 117 ARG   I CB  1 
ATOM   11110 C  CG  . ARG   I  1 117 ? -52.174 -47.455  -55.027 1.00 23.31 ? 117 ARG   I CG  1 
ATOM   11111 C  CD  . ARG   I  1 117 ? -52.987 -47.576  -56.315 1.00 27.63 ? 117 ARG   I CD  1 
ATOM   11112 N  NE  . ARG   I  1 117 ? -52.695 -48.881  -56.909 1.00 31.55 ? 117 ARG   I NE  1 
ATOM   11113 C  CZ  . ARG   I  1 117 ? -53.562 -49.642  -57.561 1.00 32.22 ? 117 ARG   I CZ  1 
ATOM   11114 N  NH1 . ARG   I  1 117 ? -54.804 -49.228  -57.802 1.00 33.70 ? 117 ARG   I NH1 1 
ATOM   11115 N  NH2 . ARG   I  1 117 ? -53.187 -50.857  -57.954 1.00 33.94 ? 117 ARG   I NH2 1 
ATOM   11116 N  N   . ASP   I  1 118 ? -49.219 -46.041  -53.772 1.00 30.59 ? 118 ASP   I N   1 
ATOM   11117 C  CA  . ASP   I  1 118 ? -47.882 -46.602  -54.024 1.00 29.30 ? 118 ASP   I CA  1 
ATOM   11118 C  C   . ASP   I  1 118 ? -47.206 -47.002  -52.712 1.00 26.11 ? 118 ASP   I C   1 
ATOM   11119 O  O   . ASP   I  1 118 ? -46.677 -48.110  -52.585 1.00 25.53 ? 118 ASP   I O   1 
ATOM   11120 C  CB  . ASP   I  1 118 ? -47.044 -45.582  -54.811 1.00 32.18 ? 118 ASP   I CB  1 
ATOM   11121 C  CG  . ASP   I  1 118 ? -45.855 -46.209  -55.512 1.00 31.28 ? 118 ASP   I CG  1 
ATOM   11122 O  OD1 . ASP   I  1 118 ? -46.018 -47.305  -56.076 1.00 30.41 ? 118 ASP   I OD1 1 
ATOM   11123 O  OD2 . ASP   I  1 118 ? -44.775 -45.588  -55.505 1.00 32.52 ? 118 ASP   I OD2 1 
ATOM   11124 N  N   . LEU   I  1 119 ? -47.286 -46.148  -51.697 1.00 27.11 ? 119 LEU   I N   1 
ATOM   11125 C  CA  . LEU   I  1 119 ? -46.745 -46.517  -50.386 1.00 25.90 ? 119 LEU   I CA  1 
ATOM   11126 C  C   . LEU   I  1 119 ? -47.387 -47.792  -49.845 1.00 28.48 ? 119 LEU   I C   1 
ATOM   11127 O  O   . LEU   I  1 119 ? -46.702 -48.689  -49.338 1.00 24.54 ? 119 LEU   I O   1 
ATOM   11128 C  CB  . LEU   I  1 119 ? -46.947 -45.370  -49.409 1.00 23.20 ? 119 LEU   I CB  1 
ATOM   11129 C  CG  . LEU   I  1 119 ? -46.573 -45.675  -47.951 1.00 30.76 ? 119 LEU   I CG  1 
ATOM   11130 C  CD1 . LEU   I  1 119 ? -45.095 -46.111  -47.813 1.00 35.67 ? 119 LEU   I CD1 1 
ATOM   11131 C  CD2 . LEU   I  1 119 ? -46.865 -44.471  -47.095 1.00 27.42 ? 119 LEU   I CD2 1 
ATOM   11132 N  N   . LEU   I  1 120 ? -48.720 -47.895  -49.932 1.00 30.80 ? 120 LEU   I N   1 
ATOM   11133 C  CA  . LEU   I  1 120 ? -49.381 -49.041  -49.323 1.00 25.77 ? 120 LEU   I CA  1 
ATOM   11134 C  C   . LEU   I  1 120 ? -49.081 -50.307  -50.084 1.00 23.77 ? 120 LEU   I C   1 
ATOM   11135 O  O   . LEU   I  1 120 ? -48.947 -51.382  -49.482 1.00 26.03 ? 120 LEU   I O   1 
ATOM   11136 C  CB  . LEU   I  1 120 ? -50.898 -48.815  -49.261 1.00 27.43 ? 120 LEU   I CB  1 
ATOM   11137 C  CG  . LEU   I  1 120 ? -51.362 -47.600  -48.477 1.00 30.44 ? 120 LEU   I CG  1 
ATOM   11138 C  CD1 . LEU   I  1 120 ? -52.894 -47.424  -48.565 1.00 34.63 ? 120 LEU   I CD1 1 
ATOM   11139 C  CD2 . LEU   I  1 120 ? -50.930 -47.740  -47.043 1.00 28.78 ? 120 LEU   I CD2 1 
ATOM   11140 N  N   . LYS   I  1 121 ? -48.951 -50.198  -51.410 1.00 25.99 ? 121 LYS   I N   1 
ATOM   11141 C  CA  . LYS   I  1 121 ? -48.530 -51.347  -52.198 1.00 25.76 ? 121 LYS   I CA  1 
ATOM   11142 C  C   . LYS   I  1 121 ? -47.160 -51.853  -51.745 1.00 27.80 ? 121 LYS   I C   1 
ATOM   11143 O  O   . LYS   I  1 121 ? -46.951 -53.069  -51.627 1.00 23.63 ? 121 LYS   I O   1 
ATOM   11144 C  CB  . LYS   I  1 121 ? -48.530 -50.965  -53.688 1.00 28.19 ? 121 LYS   I CB  1 
ATOM   11145 C  CG  . LYS   I  1 121 ? -48.131 -52.063  -54.664 1.00 28.81 ? 121 LYS   I CG  1 
ATOM   11146 C  CD  . LYS   I  1 121 ? -46.600 -52.095  -54.911 1.00 30.61 ? 121 LYS   I CD  1 
ATOM   11147 C  CE  . LYS   I  1 121 ? -46.057 -50.841  -55.657 1.00 36.66 ? 121 LYS   I CE  1 
ATOM   11148 N  NZ  . LYS   I  1 121 ? -44.582 -51.021  -56.003 1.00 35.80 ? 121 LYS   I NZ  1 
ATOM   11149 N  N   . ASP   I  1 122 ? -46.220 -50.936  -51.487 1.00 33.92 ? 122 ASP   I N   1 
ATOM   11150 C  CA  . ASP   I  1 122 ? -44.876 -51.349  -51.057 1.00 28.36 ? 122 ASP   I CA  1 
ATOM   11151 C  C   . ASP   I  1 122 ? -44.956 -52.063  -49.715 1.00 27.20 ? 122 ASP   I C   1 
ATOM   11152 O  O   . ASP   I  1 122 ? -44.362 -53.137  -49.518 1.00 27.04 ? 122 ASP   I O   1 
ATOM   11153 C  CB  . ASP   I  1 122 ? -43.942 -50.133  -50.971 1.00 32.18 ? 122 ASP   I CB  1 
ATOM   11154 C  CG  . ASP   I  1 122 ? -43.552 -49.555  -52.340 1.00 42.37 ? 122 ASP   I CG  1 
ATOM   11155 O  OD1 . ASP   I  1 122 ? -43.710 -50.220  -53.389 1.00 33.14 ? 122 ASP   I OD1 1 
ATOM   11156 O  OD2 . ASP   I  1 122 ? -43.075 -48.398  -52.351 1.00 36.50 ? 122 ASP   I OD2 1 
ATOM   11157 N  N   . ILE   I  1 123 ? -45.739 -51.509  -48.794 1.00 28.25 ? 123 ILE   I N   1 
ATOM   11158 C  CA  . ILE   I  1 123 ? -45.958 -52.180  -47.516 1.00 26.07 ? 123 ILE   I CA  1 
ATOM   11159 C  C   . ILE   I  1 123 ? -46.578 -53.552  -47.737 1.00 27.86 ? 123 ILE   I C   1 
ATOM   11160 O  O   . ILE   I  1 123 ? -46.155 -54.547  -47.133 1.00 28.81 ? 123 ILE   I O   1 
ATOM   11161 C  CB  . ILE   I  1 123 ? -46.803 -51.278  -46.603 1.00 25.71 ? 123 ILE   I CB  1 
ATOM   11162 C  CG1 . ILE   I  1 123 ? -46.011 -50.006  -46.293 1.00 30.89 ? 123 ILE   I CG1 1 
ATOM   11163 C  CG2 . ILE   I  1 123 ? -47.184 -51.976  -45.251 1.00 27.03 ? 123 ILE   I CG2 1 
ATOM   11164 C  CD1 . ILE   I  1 123 ? -46.813 -48.964  -45.535 1.00 31.19 ? 123 ILE   I CD1 1 
ATOM   11165 N  N   . LEU   I  1 124 ? -47.553 -53.642  -48.648 1.00 27.57 ? 124 LEU   I N   1 
ATOM   11166 C  CA  . LEU   I  1 124 ? -48.200 -54.926  -48.908 1.00 20.37 ? 124 LEU   I CA  1 
ATOM   11167 C  C   . LEU   I  1 124 ? -47.231 -55.958  -49.456 1.00 27.42 ? 124 LEU   I C   1 
ATOM   11168 O  O   . LEU   I  1 124 ? -47.305 -57.144  -49.103 1.00 27.33 ? 124 LEU   I O   1 
ATOM   11169 C  CB  . LEU   I  1 124 ? -49.368 -54.709  -49.888 1.00 28.46 ? 124 LEU   I CB  1 
ATOM   11170 C  CG  . LEU   I  1 124 ? -50.164 -55.936  -50.339 1.00 29.06 ? 124 LEU   I CG  1 
ATOM   11171 C  CD1 . LEU   I  1 124 ? -50.840 -56.603  -49.140 1.00 32.28 ? 124 LEU   I CD1 1 
ATOM   11172 C  CD2 . LEU   I  1 124 ? -51.224 -55.526  -51.401 1.00 31.04 ? 124 LEU   I CD2 1 
ATOM   11173 N  N   . GLU   I  1 125 ? -46.323 -55.538  -50.350 1.00 28.87 ? 125 GLU   I N   1 
ATOM   11174 C  CA  . GLU   I  1 125 ? -45.305 -56.466  -50.826 1.00 28.86 ? 125 GLU   I CA  1 
ATOM   11175 C  C   . GLU   I  1 125 ? -44.472 -56.995  -49.676 1.00 24.97 ? 125 GLU   I C   1 
ATOM   11176 O  O   . GLU   I  1 125 ? -44.200 -58.201  -49.612 1.00 26.81 ? 125 GLU   I O   1 
ATOM   11177 C  CB  . GLU   I  1 125 ? -44.423 -55.796  -51.885 1.00 34.20 ? 125 GLU   I CB  1 
ATOM   11178 C  CG  . GLU   I  1 125 ? -45.237 -55.520  -53.153 1.00 41.10 ? 125 GLU   I CG  1 
ATOM   11179 C  CD  . GLU   I  1 125 ? -44.482 -54.783  -54.249 1.00 52.99 ? 125 GLU   I CD  1 
ATOM   11180 O  OE1 . GLU   I  1 125 ? -43.579 -53.959  -53.938 1.00 38.23 ? 125 GLU   I OE1 1 
ATOM   11181 O  OE2 . GLU   I  1 125 ? -44.817 -55.045  -55.430 1.00 46.75 ? 125 GLU   I OE2 1 
ATOM   11182 N  N   . SER   I  1 126 ? -44.104 -56.119  -48.731 1.00 27.11 ? 126 SER   I N   1 
ATOM   11183 C  CA  A SER   I  1 126 ? -43.347 -56.571  -47.563 0.50 30.57 ? 126 SER   I CA  1 
ATOM   11184 C  CA  B SER   I  1 126 ? -43.351 -56.564  -47.557 0.50 30.57 ? 126 SER   I CA  1 
ATOM   11185 C  C   . SER   I  1 126 ? -44.157 -57.564  -46.738 1.00 30.46 ? 126 SER   I C   1 
ATOM   11186 O  O   . SER   I  1 126 ? -43.635 -58.601  -46.318 1.00 29.14 ? 126 SER   I O   1 
ATOM   11187 C  CB  A SER   I  1 126 ? -42.940 -55.375  -46.703 0.50 29.35 ? 126 SER   I CB  1 
ATOM   11188 C  CB  B SER   I  1 126 ? -42.968 -55.365  -46.692 0.50 29.34 ? 126 SER   I CB  1 
ATOM   11189 O  OG  A SER   I  1 126 ? -42.314 -55.798  -45.503 0.50 26.85 ? 126 SER   I OG  1 
ATOM   11190 O  OG  B SER   I  1 126 ? -42.072 -54.525  -47.384 0.50 33.88 ? 126 SER   I OG  1 
ATOM   11191 N  N   . GLU   I  1 127 ? -45.449 -57.266  -46.507 1.00 32.82 ? 127 GLU   I N   1 
ATOM   11192 C  CA  . GLU   I  1 127 ? -46.271 -58.140  -45.672 1.00 30.51 ? 127 GLU   I CA  1 
ATOM   11193 C  C   . GLU   I  1 127 ? -46.518 -59.486  -46.335 1.00 29.21 ? 127 GLU   I C   1 
ATOM   11194 O  O   . GLU   I  1 127 ? -46.526 -60.520  -45.658 1.00 31.41 ? 127 GLU   I O   1 
ATOM   11195 C  CB  . GLU   I  1 127 ? -47.599 -57.478  -45.344 1.00 28.12 ? 127 GLU   I CB  1 
ATOM   11196 C  CG  . GLU   I  1 127 ? -47.520 -56.133  -44.615 1.00 32.63 ? 127 GLU   I CG  1 
ATOM   11197 C  CD  . GLU   I  1 127 ? -46.616 -56.146  -43.383 1.00 41.41 ? 127 GLU   I CD  1 
ATOM   11198 O  OE1 . GLU   I  1 127 ? -46.441 -57.202  -42.735 1.00 33.75 ? 127 GLU   I OE1 1 
ATOM   11199 O  OE2 . GLU   I  1 127 ? -46.074 -55.069  -43.076 1.00 40.20 ? 127 GLU   I OE2 1 
ATOM   11200 N  N   . GLU   I  1 128 ? -46.708 -59.513  -47.660 1.00 31.50 ? 128 GLU   I N   1 
ATOM   11201 C  CA  . GLU   I  1 128 ? -46.824 -60.814  -48.315 1.00 30.30 ? 128 GLU   I CA  1 
ATOM   11202 C  C   . GLU   I  1 128 ? -45.531 -61.605  -48.232 1.00 32.11 ? 128 GLU   I C   1 
ATOM   11203 O  O   . GLU   I  1 128 ? -45.577 -62.836  -48.129 1.00 29.22 ? 128 GLU   I O   1 
ATOM   11204 C  CB  . GLU   I  1 128 ? -47.275 -60.654  -49.780 1.00 30.22 ? 128 GLU   I CB  1 
ATOM   11205 C  CG  . GLU   I  1 128 ? -48.705 -60.197  -49.897 1.00 30.55 ? 128 GLU   I CG  1 
ATOM   11206 C  CD  . GLU   I  1 128 ? -49.299 -60.310  -51.323 1.00 41.02 ? 128 GLU   I CD  1 
ATOM   11207 O  OE1 . GLU   I  1 128 ? -48.650 -60.880  -52.232 1.00 32.31 ? 128 GLU   I OE1 1 
ATOM   11208 O  OE2 . GLU   I  1 128 ? -50.429 -59.814  -51.530 1.00 34.94 ? 128 GLU   I OE2 1 
ATOM   11209 N  N   . GLU   I  1 129 ? -44.364 -60.936  -48.257 1.00 33.33 ? 129 GLU   I N   1 
ATOM   11210 C  CA  . GLU   I  1 129 ? -43.120 -61.652  -47.984 1.00 31.47 ? 129 GLU   I CA  1 
ATOM   11211 C  C   . GLU   I  1 129 ? -43.096 -62.229  -46.571 1.00 26.58 ? 129 GLU   I C   1 
ATOM   11212 O  O   . GLU   I  1 129 ? -42.631 -63.359  -46.381 1.00 25.62 ? 129 GLU   I O   1 
ATOM   11213 C  CB  . GLU   I  1 129 ? -41.905 -60.739  -48.202 1.00 40.38 ? 129 GLU   I CB  1 
ATOM   11214 C  CG  . GLU   I  1 129 ? -41.793 -60.290  -49.639 1.00 41.75 ? 129 GLU   I CG  1 
ATOM   11215 C  CD  . GLU   I  1 129 ? -40.614 -59.347  -49.887 1.00 63.21 ? 129 GLU   I CD  1 
ATOM   11216 O  OE1 . GLU   I  1 129 ? -39.633 -59.388  -49.104 1.00 52.55 ? 129 GLU   I OE1 1 
ATOM   11217 O  OE2 . GLU   I  1 129 ? -40.681 -58.566  -50.869 1.00 60.43 ? 129 GLU   I OE2 1 
ATOM   11218 N  N   . HIS   I  1 130 ? -43.572 -61.479  -45.569 1.00 29.08 ? 130 HIS   I N   1 
ATOM   11219 C  CA  A HIS   I  1 130 ? -43.662 -62.050  -44.226 0.50 32.57 ? 130 HIS   I CA  1 
ATOM   11220 C  CA  B HIS   I  1 130 ? -43.689 -62.032  -44.213 0.50 32.57 ? 130 HIS   I CA  1 
ATOM   11221 C  C   . HIS   I  1 130 ? -44.625 -63.240  -44.194 1.00 29.70 ? 130 HIS   I C   1 
ATOM   11222 O  O   . HIS   I  1 130 ? -44.353 -64.254  -43.533 1.00 30.62 ? 130 HIS   I O   1 
ATOM   11223 C  CB  A HIS   I  1 130 ? -44.081 -60.970  -43.228 0.50 31.53 ? 130 HIS   I CB  1 
ATOM   11224 C  CB  B HIS   I  1 130 ? -44.217 -60.982  -43.225 0.50 31.63 ? 130 HIS   I CB  1 
ATOM   11225 C  CG  A HIS   I  1 130 ? -43.873 -61.352  -41.795 0.50 35.67 ? 130 HIS   I CG  1 
ATOM   11226 C  CG  B HIS   I  1 130 ? -43.371 -59.750  -43.082 0.50 34.47 ? 130 HIS   I CG  1 
ATOM   11227 N  ND1 A HIS   I  1 130 ? -44.158 -60.502  -40.748 0.50 35.33 ? 130 HIS   I ND1 1 
ATOM   11228 N  ND1 B HIS   I  1 130 ? -42.081 -59.650  -43.560 0.50 33.27 ? 130 HIS   I ND1 1 
ATOM   11229 C  CD2 A HIS   I  1 130 ? -43.402 -62.492  -41.235 0.50 33.51 ? 130 HIS   I CD2 1 
ATOM   11230 C  CD2 B HIS   I  1 130 ? -43.642 -58.561  -42.488 0.50 34.49 ? 130 HIS   I CD2 1 
ATOM   11231 C  CE1 A HIS   I  1 130 ? -43.881 -61.105  -39.606 0.50 35.10 ? 130 HIS   I CE1 1 
ATOM   11232 C  CE1 B HIS   I  1 130 ? -41.604 -58.448  -43.288 0.50 33.64 ? 130 HIS   I CE1 1 
ATOM   11233 N  NE2 A HIS   I  1 130 ? -43.419 -62.311  -39.875 0.50 38.07 ? 130 HIS   I NE2 1 
ATOM   11234 N  NE2 B HIS   I  1 130 ? -42.527 -57.769  -42.634 0.50 36.75 ? 130 HIS   I NE2 1 
ATOM   11235 N  N   . ILE   I  1 131 ? -45.742 -63.156  -44.913 1.00 30.04 ? 131 ILE   I N   1 
ATOM   11236 C  CA  . ILE   I  1 131 ? -46.664 -64.293  -44.967 1.00 26.28 ? 131 ILE   I CA  1 
ATOM   11237 C  C   . ILE   I  1 131 ? -45.987 -65.515  -45.573 1.00 30.36 ? 131 ILE   I C   1 
ATOM   11238 O  O   . ILE   I  1 131 ? -46.105 -66.627  -45.047 1.00 33.40 ? 131 ILE   I O   1 
ATOM   11239 C  CB  . ILE   I  1 131 ? -47.954 -63.927  -45.723 1.00 32.97 ? 131 ILE   I CB  1 
ATOM   11240 C  CG1 . ILE   I  1 131 ? -48.791 -63.005  -44.845 1.00 31.54 ? 131 ILE   I CG1 1 
ATOM   11241 C  CG2 . ILE   I  1 131 ? -48.724 -65.209  -46.073 1.00 32.93 ? 131 ILE   I CG2 1 
ATOM   11242 C  CD1 . ILE   I  1 131 ? -49.863 -62.294  -45.554 1.00 34.43 ? 131 ILE   I CD1 1 
ATOM   11243 N  N   . ASP   I  1 132 ? -45.284 -65.344  -46.698 1.00 28.73 ? 132 ASP   I N   1 
ATOM   11244 C  CA  . ASP   I  1 132 ? -44.521 -66.468  -47.241 1.00 31.46 ? 132 ASP   I CA  1 
ATOM   11245 C  C   . ASP   I  1 132 ? -43.586 -67.059  -46.191 1.00 33.73 ? 132 ASP   I C   1 
ATOM   11246 O  O   . ASP   I  1 132 ? -43.470 -68.285  -46.049 1.00 30.71 ? 132 ASP   I O   1 
ATOM   11247 C  CB  . ASP   I  1 132 ? -43.727 -66.008  -48.467 1.00 35.40 ? 132 ASP   I CB  1 
ATOM   11248 C  CG  . ASP   I  1 132 ? -43.179 -67.168  -49.300 1.00 34.93 ? 132 ASP   I CG  1 
ATOM   11249 O  OD1 . ASP   I  1 132 ? -43.384 -68.345  -48.952 1.00 46.75 ? 132 ASP   I OD1 1 
ATOM   11250 O  OD2 . ASP   I  1 132 ? -42.526 -66.893  -50.327 1.00 45.56 ? 132 ASP   I OD2 1 
ATOM   11251 N  N   . TYR   I  1 133 ? -42.852 -66.197  -45.484 1.00 31.50 ? 133 TYR   I N   1 
ATOM   11252 C  CA  . TYR   I  1 133 ? -41.949 -66.697  -44.460 1.00 29.79 ? 133 TYR   I CA  1 
ATOM   11253 C  C   . TYR   I  1 133 ? -42.722 -67.492  -43.412 1.00 30.30 ? 133 TYR   I C   1 
ATOM   11254 O  O   . TYR   I  1 133 ? -42.340 -68.608  -43.056 1.00 31.59 ? 133 TYR   I O   1 
ATOM   11255 C  CB  . TYR   I  1 133 ? -41.208 -65.540  -43.805 1.00 27.64 ? 133 TYR   I CB  1 
ATOM   11256 C  CG  . TYR   I  1 133 ? -40.502 -65.952  -42.534 1.00 33.19 ? 133 TYR   I CG  1 
ATOM   11257 C  CD1 . TYR   I  1 133 ? -39.272 -66.576  -42.574 1.00 40.03 ? 133 TYR   I CD1 1 
ATOM   11258 C  CD2 . TYR   I  1 133 ? -41.085 -65.734  -41.294 1.00 40.01 ? 133 TYR   I CD2 1 
ATOM   11259 C  CE1 . TYR   I  1 133 ? -38.632 -66.956  -41.429 1.00 39.01 ? 133 TYR   I CE1 1 
ATOM   11260 C  CE2 . TYR   I  1 133 ? -40.450 -66.107  -40.142 1.00 37.20 ? 133 TYR   I CE2 1 
ATOM   11261 C  CZ  . TYR   I  1 133 ? -39.228 -66.723  -40.216 1.00 38.06 ? 133 TYR   I CZ  1 
ATOM   11262 O  OH  . TYR   I  1 133 ? -38.581 -67.103  -39.066 1.00 41.54 ? 133 TYR   I OH  1 
ATOM   11263 N  N   . LEU   I  1 134 ? -43.832 -66.941  -42.934 1.00 32.74 ? 134 LEU   I N   1 
ATOM   11264 C  CA  . LEU   I  1 134 ? -44.574 -67.602  -41.857 1.00 33.44 ? 134 LEU   I CA  1 
ATOM   11265 C  C   . LEU   I  1 134 ? -45.158 -68.934  -42.319 1.00 35.01 ? 134 LEU   I C   1 
ATOM   11266 O  O   . LEU   I  1 134 ? -45.041 -69.954  -41.624 1.00 29.73 ? 134 LEU   I O   1 
ATOM   11267 C  CB  . LEU   I  1 134 ? -45.676 -66.674  -41.375 1.00 31.48 ? 134 LEU   I CB  1 
ATOM   11268 C  CG  . LEU   I  1 134 ? -45.102 -65.515  -40.563 1.00 30.11 ? 134 LEU   I CG  1 
ATOM   11269 C  CD1 . LEU   I  1 134 ? -46.096 -64.396  -40.430 1.00 31.79 ? 134 LEU   I CD1 1 
ATOM   11270 C  CD2 . LEU   I  1 134 ? -44.621 -66.006  -39.196 1.00 35.62 ? 134 LEU   I CD2 1 
ATOM   11271 N  N   . GLU   I  1 135 ? -45.804 -68.937  -43.492 1.00 37.07 ? 135 GLU   I N   1 
ATOM   11272 C  CA  . GLU   I  1 135 ? -46.370 -70.176  -44.022 1.00 37.62 ? 135 GLU   I CA  1 
ATOM   11273 C  C   . GLU   I  1 135 ? -45.286 -71.219  -44.216 1.00 35.53 ? 135 GLU   I C   1 
ATOM   11274 O  O   . GLU   I  1 135 ? -45.491 -72.410  -43.945 1.00 36.16 ? 135 GLU   I O   1 
ATOM   11275 C  CB  . GLU   I  1 135 ? -47.079 -69.905  -45.352 1.00 36.96 ? 135 GLU   I CB  1 
ATOM   11276 C  CG  . GLU   I  1 135 ? -48.324 -69.041  -45.232 1.00 34.53 ? 135 GLU   I CG  1 
ATOM   11277 C  CD  . GLU   I  1 135 ? -48.983 -68.753  -46.570 1.00 38.37 ? 135 GLU   I CD  1 
ATOM   11278 O  OE1 . GLU   I  1 135 ? -48.293 -68.797  -47.623 1.00 39.23 ? 135 GLU   I OE1 1 
ATOM   11279 O  OE2 . GLU   I  1 135 ? -50.196 -68.474  -46.567 1.00 43.38 ? 135 GLU   I OE2 1 
ATOM   11280 N  N   . THR   I  1 136 ? -44.118 -70.788  -44.690 1.00 33.86 ? 136 THR   I N   1 
ATOM   11281 C  CA  . THR   I  1 136 ? -43.010 -71.718  -44.884 1.00 33.27 ? 136 THR   I CA  1 
ATOM   11282 C  C   . THR   I  1 136 ? -42.528 -72.326  -43.561 1.00 30.54 ? 136 THR   I C   1 
ATOM   11283 O  O   . THR   I  1 136 ? -42.244 -73.529  -43.489 1.00 30.96 ? 136 THR   I O   1 
ATOM   11284 C  CB  . THR   I  1 136 ? -41.875 -70.996  -45.621 1.00 38.29 ? 136 THR   I CB  1 
ATOM   11285 O  OG1 . THR   I  1 136 ? -42.383 -70.453  -46.849 1.00 30.95 ? 136 THR   I OG1 1 
ATOM   11286 C  CG2 . THR   I  1 136 ? -40.741 -71.947  -45.925 1.00 36.03 ? 136 THR   I CG2 1 
ATOM   11287 N  N   . GLN   I  1 137 ? -42.383 -71.518  -42.507 1.00 30.72 ? 137 GLN   I N   1 
ATOM   11288 C  CA  . GLN   I  1 137 ? -41.960 -72.076  -41.221 1.00 34.52 ? 137 GLN   I CA  1 
ATOM   11289 C  C   . GLN   I  1 137 ? -42.959 -73.123  -40.705 1.00 26.63 ? 137 GLN   I C   1 
ATOM   11290 O  O   . GLN   I  1 137 ? -42.567 -74.194  -40.212 1.00 33.54 ? 137 GLN   I O   1 
ATOM   11291 C  CB  . GLN   I  1 137 ? -41.787 -70.956  -40.183 1.00 33.18 ? 137 GLN   I CB  1 
ATOM   11292 C  CG  . GLN   I  1 137 ? -40.734 -69.904  -40.544 1.00 36.88 ? 137 GLN   I CG  1 
ATOM   11293 C  CD  . GLN   I  1 137 ? -39.548 -70.500  -41.245 1.00 30.70 ? 137 GLN   I CD  1 
ATOM   11294 O  OE1 . GLN   I  1 137 ? -39.365 -70.311  -42.456 1.00 38.77 ? 137 GLN   I OE1 1 
ATOM   11295 N  NE2 . GLN   I  1 137 ? -38.743 -71.218  -40.516 1.00 35.26 ? 137 GLN   I NE2 1 
ATOM   11296 N  N   . LEU   I  1 138 ? -44.250 -72.808  -40.771 1.00 32.42 ? 138 LEU   I N   1 
ATOM   11297 C  CA  . LEU   I  1 138 ? -45.258 -73.752  -40.277 1.00 33.15 ? 138 LEU   I CA  1 
ATOM   11298 C  C   . LEU   I  1 138 ? -45.241 -75.029  -41.102 1.00 39.51 ? 138 LEU   I C   1 
ATOM   11299 O  O   . LEU   I  1 138 ? -45.347 -76.131  -40.554 1.00 41.99 ? 138 LEU   I O   1 
ATOM   11300 C  CB  . LEU   I  1 138 ? -46.636 -73.104  -40.296 1.00 27.55 ? 138 LEU   I CB  1 
ATOM   11301 C  CG  . LEU   I  1 138 ? -46.834 -71.950  -39.305 1.00 29.58 ? 138 LEU   I CG  1 
ATOM   11302 C  CD1 . LEU   I  1 138 ? -47.913 -70.956  -39.780 1.00 38.76 ? 138 LEU   I CD1 1 
ATOM   11303 C  CD2 . LEU   I  1 138 ? -47.167 -72.451  -37.913 1.00 37.01 ? 138 LEU   I CD2 1 
ATOM   11304 N  N   . GLY   I  1 139 ? -45.038 -74.901  -42.420 1.00 36.25 ? 139 GLY   I N   1 
ATOM   11305 C  CA  . GLY   I  1 139 ? -44.840 -76.079  -43.246 1.00 33.88 ? 139 GLY   I CA  1 
ATOM   11306 C  C   . GLY   I  1 139 ? -43.608 -76.875  -42.882 1.00 37.29 ? 139 GLY   I C   1 
ATOM   11307 O  O   . GLY   I  1 139 ? -43.639 -78.108  -42.882 1.00 39.14 ? 139 GLY   I O   1 
ATOM   11308 N  N   . LEU   I  1 140 ? -42.498 -76.190  -42.570 1.00 36.91 ? 140 LEU   I N   1 
ATOM   11309 C  CA  . LEU   I  1 140 ? -41.277 -76.902  -42.197 1.00 35.91 ? 140 LEU   I CA  1 
ATOM   11310 C  C   . LEU   I  1 140 ? -41.447 -77.690  -40.901 1.00 29.66 ? 140 LEU   I C   1 
ATOM   11311 O  O   . LEU   I  1 140 ? -40.825 -78.746  -40.728 1.00 36.06 ? 140 LEU   I O   1 
ATOM   11312 C  CB  . LEU   I  1 140 ? -40.094 -75.924  -42.021 1.00 35.46 ? 140 LEU   I CB  1 
ATOM   11313 C  CG  . LEU   I  1 140 ? -39.465 -75.391  -43.318 1.00 39.91 ? 140 LEU   I CG  1 
ATOM   11314 C  CD1 . LEU   I  1 140 ? -38.379 -74.324  -43.080 1.00 36.35 ? 140 LEU   I CD1 1 
ATOM   11315 C  CD2 . LEU   I  1 140 ? -38.885 -76.542  -44.054 1.00 30.16 ? 140 LEU   I CD2 1 
ATOM   11316 N  N   . ILE   I  1 141 ? -42.216 -77.163  -39.955 1.00 31.15 ? 141 ILE   I N   1 
ATOM   11317 C  CA  . ILE   I  1 141 ? -42.405 -77.893  -38.702 1.00 33.73 ? 141 ILE   I CA  1 
ATOM   11318 C  C   . ILE   I  1 141 ? -43.017 -79.262  -38.980 1.00 40.01 ? 141 ILE   I C   1 
ATOM   11319 O  O   . ILE   I  1 141 ? -42.636 -80.264  -38.362 1.00 37.31 ? 141 ILE   I O   1 
ATOM   11320 C  CB  . ILE   I  1 141 ? -43.254 -77.075  -37.719 1.00 32.97 ? 141 ILE   I CB  1 
ATOM   11321 C  CG1 . ILE   I  1 141 ? -42.431 -75.919  -37.121 1.00 33.72 ? 141 ILE   I CG1 1 
ATOM   11322 C  CG2 . ILE   I  1 141 ? -43.758 -77.991  -36.599 1.00 38.19 ? 141 ILE   I CG2 1 
ATOM   11323 C  CD1 . ILE   I  1 141 ? -43.227 -74.828  -36.449 1.00 31.77 ? 141 ILE   I CD1 1 
ATOM   11324 N  N   . GLN   I  1 142 ? -43.949 -79.324  -39.943 1.00 38.84 ? 142 GLN   I N   1 
ATOM   11325 C  CA  . GLN   I  1 142 ? -44.579 -80.586  -40.331 1.00 40.06 ? 142 GLN   I CA  1 
ATOM   11326 C  C   . GLN   I  1 142 ? -43.605 -81.508  -41.050 1.00 40.08 ? 142 GLN   I C   1 
ATOM   11327 O  O   . GLN   I  1 142 ? -43.641 -82.727  -40.850 1.00 47.55 ? 142 GLN   I O   1 
ATOM   11328 C  CB  . GLN   I  1 142 ? -45.797 -80.301  -41.217 1.00 41.48 ? 142 GLN   I CB  1 
ATOM   11329 C  CG  . GLN   I  1 142 ? -46.881 -79.485  -40.517 1.00 38.23 ? 142 GLN   I CG  1 
ATOM   11330 C  CD  . GLN   I  1 142 ? -47.407 -80.168  -39.262 1.00 45.45 ? 142 GLN   I CD  1 
ATOM   11331 O  OE1 . GLN   I  1 142 ? -47.740 -81.350  -39.288 1.00 60.72 ? 142 GLN   I OE1 1 
ATOM   11332 N  NE2 . GLN   I  1 142 ? -47.470 -79.433  -38.157 1.00 44.33 ? 142 GLN   I NE2 1 
ATOM   11333 N  N   . LYS   I  1 143 ? -42.706 -80.950  -41.869 1.00 40.48 ? 143 LYS   I N   1 
ATOM   11334 C  CA  . LYS   I  1 143 ? -41.838 -81.773  -42.709 1.00 36.97 ? 143 LYS   I CA  1 
ATOM   11335 C  C   . LYS   I  1 143 ? -40.635 -82.306  -41.946 1.00 45.34 ? 143 LYS   I C   1 
ATOM   11336 O  O   . LYS   I  1 143 ? -40.239 -83.462  -42.139 1.00 44.25 ? 143 LYS   I O   1 
ATOM   11337 C  CB  . LYS   I  1 143 ? -41.340 -80.980  -43.933 1.00 38.83 ? 143 LYS   I CB  1 
ATOM   11338 C  CG  . LYS   I  1 143 ? -42.403 -80.620  -44.969 1.00 41.58 ? 143 LYS   I CG  1 
ATOM   11339 C  CD  . LYS   I  1 143 ? -41.812 -79.806  -46.128 1.00 50.21 ? 143 LYS   I CD  1 
ATOM   11340 C  CE  . LYS   I  1 143 ? -42.811 -79.650  -47.286 1.00 60.07 ? 143 LYS   I CE  1 
ATOM   11341 N  NZ  . LYS   I  1 143 ? -44.040 -78.862  -46.926 1.00 58.51 ? 143 LYS   I NZ  1 
ATOM   11342 N  N   . VAL   I  1 144 ? -40.006 -81.479  -41.109 1.00 40.23 ? 144 VAL   I N   1 
ATOM   11343 C  CA  . VAL   I  1 144 ? -38.818 -81.925  -40.401 1.00 31.50 ? 144 VAL   I CA  1 
ATOM   11344 C  C   . VAL   I  1 144 ? -39.125 -82.359  -38.976 1.00 35.91 ? 144 VAL   I C   1 
ATOM   11345 O  O   . VAL   I  1 144 ? -38.278 -83.013  -38.351 1.00 36.33 ? 144 VAL   I O   1 
ATOM   11346 C  CB  . VAL   I  1 144 ? -37.723 -80.839  -40.402 1.00 38.77 ? 144 VAL   I CB  1 
ATOM   11347 C  CG1 . VAL   I  1 144 ? -37.467 -80.350  -41.832 1.00 43.04 ? 144 VAL   I CG1 1 
ATOM   11348 C  CG2 . VAL   I  1 144 ? -38.082 -79.679  -39.479 1.00 37.99 ? 144 VAL   I CG2 1 
ATOM   11349 N  N   . GLY   I  1 145 ? -40.305 -82.046  -38.461 1.00 36.67 ? 145 GLY   I N   1 
ATOM   11350 C  CA  . GLY   I  1 145 ? -40.641 -82.302  -37.068 1.00 51.41 ? 145 GLY   I CA  1 
ATOM   11351 C  C   . GLY   I  1 145 ? -40.311 -81.113  -36.189 1.00 43.12 ? 145 GLY   I C   1 
ATOM   11352 O  O   . GLY   I  1 145 ? -39.424 -80.319  -36.481 1.00 35.75 ? 145 GLY   I O   1 
ATOM   11353 N  N   . LEU   I  1 146 ? -41.066 -80.973  -35.101 1.00 40.37 ? 146 LEU   I N   1 
ATOM   11354 C  CA  . LEU   I  1 146 ? -40.916 -79.783  -34.263 1.00 41.87 ? 146 LEU   I CA  1 
ATOM   11355 C  C   . LEU   I  1 146 ? -39.541 -79.733  -33.612 1.00 38.42 ? 146 LEU   I C   1 
ATOM   11356 O  O   . LEU   I  1 146 ? -38.948 -78.654  -33.491 1.00 34.62 ? 146 LEU   I O   1 
ATOM   11357 C  CB  . LEU   I  1 146 ? -42.001 -79.732  -33.188 1.00 30.30 ? 146 LEU   I CB  1 
ATOM   11358 C  CG  . LEU   I  1 146 ? -41.928 -78.478  -32.315 1.00 33.83 ? 146 LEU   I CG  1 
ATOM   11359 C  CD1 . LEU   I  1 146 ? -42.285 -77.293  -33.175 1.00 32.89 ? 146 LEU   I CD1 1 
ATOM   11360 C  CD2 . LEU   I  1 146 ? -42.837 -78.564  -31.057 1.00 39.93 ? 146 LEU   I CD2 1 
ATOM   11361 N  N   . GLU   I  1 147 ? -39.022 -80.887  -33.177 1.00 31.33 ? 147 GLU   I N   1 
ATOM   11362 C  CA  . GLU   I  1 147 ? -37.758 -80.884  -32.455 1.00 42.20 ? 147 GLU   I CA  1 
ATOM   11363 C  C   . GLU   I  1 147 ? -36.602 -80.518  -33.380 1.00 36.38 ? 147 GLU   I C   1 
ATOM   11364 O  O   . GLU   I  1 147 ? -35.697 -79.783  -32.980 1.00 29.21 ? 147 GLU   I O   1 
ATOM   11365 C  CB  . GLU   I  1 147 ? -37.512 -82.244  -31.809 1.00 44.94 ? 147 GLU   I CB  1 
ATOM   11366 C  CG  . GLU   I  1 147 ? -38.481 -82.579  -30.661 1.00 42.95 ? 147 GLU   I CG  1 
ATOM   11367 C  CD  . GLU   I  1 147 ? -37.996 -83.760  -29.854 1.00 51.56 ? 147 GLU   I CD  1 
ATOM   11368 O  OE1 . GLU   I  1 147 ? -37.304 -84.620  -30.434 1.00 48.61 ? 147 GLU   I OE1 1 
ATOM   11369 O  OE2 . GLU   I  1 147 ? -38.292 -83.822  -28.643 1.00 69.34 ? 147 GLU   I OE2 1 
ATOM   11370 N  N   . ASN   I  1 148 ? -36.610 -81.043  -34.605 1.00 32.80 ? 148 ASN   I N   1 
ATOM   11371 C  CA  . ASN   I  1 148 ? -35.612 -80.639  -35.593 1.00 38.24 ? 148 ASN   I CA  1 
ATOM   11372 C  C   . ASN   I  1 148 ? -35.782 -79.176  -35.965 1.00 32.57 ? 148 ASN   I C   1 
ATOM   11373 O  O   . ASN   I  1 148 ? -34.797 -78.449  -36.085 1.00 31.46 ? 148 ASN   I O   1 
ATOM   11374 C  CB  . ASN   I  1 148 ? -35.715 -81.507  -36.842 1.00 32.69 ? 148 ASN   I CB  1 
ATOM   11375 C  CG  . ASN   I  1 148 ? -34.846 -82.733  -36.770 1.00 28.30 ? 148 ASN   I CG  1 
ATOM   11376 O  OD1 . ASN   I  1 148 ? -34.210 -83.014  -35.753 1.00 37.22 ? 148 ASN   I OD1 1 
ATOM   11377 N  ND2 . ASN   I  1 148 ? -34.803 -83.483  -37.860 1.00 34.45 ? 148 ASN   I ND2 1 
ATOM   11378 N  N   . TYR   I  1 149 ? -37.027 -78.723  -36.145 1.00 28.48 ? 149 TYR   I N   1 
ATOM   11379 C  CA  . TYR   I  1 149 ? -37.242 -77.329  -36.509 1.00 37.74 ? 149 TYR   I CA  1 
ATOM   11380 C  C   . TYR   I  1 149 ? -36.674 -76.388  -35.452 1.00 39.50 ? 149 TYR   I C   1 
ATOM   11381 O  O   . TYR   I  1 149 ? -36.058 -75.367  -35.779 1.00 31.18 ? 149 TYR   I O   1 
ATOM   11382 C  CB  . TYR   I  1 149 ? -38.724 -77.043  -36.699 1.00 29.40 ? 149 TYR   I CB  1 
ATOM   11383 C  CG  . TYR   I  1 149 ? -38.956 -75.600  -37.070 1.00 33.07 ? 149 TYR   I CG  1 
ATOM   11384 C  CD1 . TYR   I  1 149 ? -38.772 -75.164  -38.377 1.00 37.91 ? 149 TYR   I CD1 1 
ATOM   11385 C  CD2 . TYR   I  1 149 ? -39.303 -74.664  -36.114 1.00 32.03 ? 149 TYR   I CD2 1 
ATOM   11386 C  CE1 . TYR   I  1 149 ? -38.961 -73.846  -38.719 1.00 32.73 ? 149 TYR   I CE1 1 
ATOM   11387 C  CE2 . TYR   I  1 149 ? -39.487 -73.343  -36.450 1.00 33.02 ? 149 TYR   I CE2 1 
ATOM   11388 C  CZ  . TYR   I  1 149 ? -39.303 -72.940  -37.745 1.00 34.38 ? 149 TYR   I CZ  1 
ATOM   11389 O  OH  . TYR   I  1 149 ? -39.472 -71.630  -38.088 1.00 33.77 ? 149 TYR   I OH  1 
ATOM   11390 N  N   . LEU   I  1 150 ? -36.896 -76.702  -34.174 1.00 30.99 ? 150 LEU   I N   1 
ATOM   11391 C  CA  . LEU   I  1 150 ? -36.375 -75.849  -33.118 1.00 31.00 ? 150 LEU   I CA  1 
ATOM   11392 C  C   . LEU   I  1 150 ? -34.866 -75.954  -33.065 1.00 31.08 ? 150 LEU   I C   1 
ATOM   11393 O  O   . LEU   I  1 150 ? -34.175 -74.939  -32.957 1.00 34.18 ? 150 LEU   I O   1 
ATOM   11394 C  CB  . LEU   I  1 150 ? -36.991 -76.222  -31.772 1.00 28.90 ? 150 LEU   I CB  1 
ATOM   11395 C  CG  . LEU   I  1 150 ? -38.522 -76.134  -31.692 1.00 38.25 ? 150 LEU   I CG  1 
ATOM   11396 C  CD1 . LEU   I  1 150 ? -39.030 -76.600  -30.311 1.00 36.19 ? 150 LEU   I CD1 1 
ATOM   11397 C  CD2 . LEU   I  1 150 ? -39.040 -74.739  -32.033 1.00 36.52 ? 150 LEU   I CD2 1 
ATOM   11398 N  N   . GLN   I  1 151 ? -34.343 -77.171  -33.212 1.00 31.31 ? 151 GLN   I N   1 
ATOM   11399 C  CA  . GLN   I  1 151 ? -32.909 -77.375  -33.216 1.00 32.37 ? 151 GLN   I CA  1 
ATOM   11400 C  C   . GLN   I  1 151 ? -32.238 -76.485  -34.258 1.00 36.87 ? 151 GLN   I C   1 
ATOM   11401 O  O   . GLN   I  1 151 ? -31.197 -75.878  -33.992 1.00 30.57 ? 151 GLN   I O   1 
ATOM   11402 C  CB  . GLN   I  1 151 ? -32.605 -78.845  -33.480 1.00 35.37 ? 151 GLN   I CB  1 
ATOM   11403 C  CG  . GLN   I  1 151 ? -31.139 -79.120  -33.580 1.00 31.99 ? 151 GLN   I CG  1 
ATOM   11404 C  CD  . GLN   I  1 151 ? -30.814 -80.533  -33.998 1.00 35.49 ? 151 GLN   I CD  1 
ATOM   11405 O  OE1 . GLN   I  1 151 ? -31.567 -81.180  -34.736 1.00 35.75 ? 151 GLN   I OE1 1 
ATOM   11406 N  NE2 . GLN   I  1 151 ? -29.687 -81.024  -33.526 1.00 34.72 ? 151 GLN   I NE2 1 
ATOM   11407 N  N   . SER   I  1 152 ? -32.842 -76.390  -35.446 1.00 33.33 ? 152 SER   I N   1 
ATOM   11408 C  CA  . SER   I  1 152 ? -32.333 -75.604  -36.560 1.00 33.63 ? 152 SER   I CA  1 
ATOM   11409 C  C   . SER   I  1 152 ? -32.437 -74.113  -36.312 1.00 37.44 ? 152 SER   I C   1 
ATOM   11410 O  O   . SER   I  1 152 ? -31.886 -73.331  -37.093 1.00 35.41 ? 152 SER   I O   1 
ATOM   11411 C  CB  . SER   I  1 152 ? -33.097 -75.969  -37.831 1.00 33.23 ? 152 SER   I CB  1 
ATOM   11412 O  OG  . SER   I  1 152 ? -32.576 -77.175  -38.364 1.00 36.03 ? 152 SER   I OG  1 
ATOM   11413 N  N   . HIS   I  1 153 ? -33.119 -73.701  -35.251 1.00 31.58 ? 153 HIS   I N   1 
ATOM   11414 C  CA  . HIS   I  1 153 ? -33.265 -72.286  -34.942 1.00 33.03 ? 153 HIS   I CA  1 
ATOM   11415 C  C   . HIS   I  1 153 ? -32.596 -71.909  -33.619 1.00 27.07 ? 153 HIS   I C   1 
ATOM   11416 O  O   . HIS   I  1 153 ? -32.832 -70.816  -33.110 1.00 31.37 ? 153 HIS   I O   1 
ATOM   11417 C  CB  . HIS   I  1 153 ? -34.742 -71.906  -34.990 1.00 28.21 ? 153 HIS   I CB  1 
ATOM   11418 C  CG  . HIS   I  1 153 ? -35.242 -71.774  -36.390 1.00 33.41 ? 153 HIS   I CG  1 
ATOM   11419 N  ND1 . HIS   I  1 153 ? -35.640 -72.862  -37.136 1.00 38.10 ? 153 HIS   I ND1 1 
ATOM   11420 C  CD2 . HIS   I  1 153 ? -35.275 -70.711  -37.230 1.00 38.99 ? 153 HIS   I CD2 1 
ATOM   11421 C  CE1 . HIS   I  1 153 ? -35.943 -72.467  -38.361 1.00 37.74 ? 153 HIS   I CE1 1 
ATOM   11422 N  NE2 . HIS   I  1 153 ? -35.731 -71.166  -38.445 1.00 35.38 ? 153 HIS   I NE2 1 
ATOM   11423 N  N   . MET   I  1 154 ? -31.708 -72.768  -33.105 1.00 28.40 ? 154 MET   I N   1 
ATOM   11424 C  CA  . MET   I  1 154 ? -30.970 -72.457  -31.884 1.00 37.93 ? 154 MET   I CA  1 
ATOM   11425 C  C   . MET   I  1 154 ? -29.894 -71.396  -32.130 1.00 41.37 ? 154 MET   I C   1 
ATOM   11426 O  O   . MET   I  1 154 ? -29.807 -70.400  -31.401 1.00 34.85 ? 154 MET   I O   1 
ATOM   11427 C  CB  . MET   I  1 154 ? -30.328 -73.726  -31.315 1.00 41.37 ? 154 MET   I CB  1 
ATOM   11428 C  CG  . MET   I  1 154 ? -31.264 -74.625  -30.502 1.00 43.68 ? 154 MET   I CG  1 
ATOM   11429 S  SD  . MET   I  1 154 ? -30.520 -76.204  -30.014 1.00 52.30 ? 154 MET   I SD  1 
ATOM   11430 C  CE  . MET   I  1 154 ? -28.928 -75.678  -29.400 1.00 41.24 ? 154 MET   I CE  1 
ATOM   11431 N  N   . HIS   I  1 155 ? -29.061 -71.590  -33.145 1.00 39.65 ? 155 HIS   I N   1 
ATOM   11432 C  CA  . HIS   I  1 155 ? -27.882 -70.758  -33.340 1.00 46.03 ? 155 HIS   I CA  1 
ATOM   11433 C  C   . HIS   I  1 155 ? -28.086 -69.856  -34.548 1.00 48.45 ? 155 HIS   I C   1 
ATOM   11434 O  O   . HIS   I  1 155 ? -28.697 -70.257  -35.544 1.00 52.93 ? 155 HIS   I O   1 
ATOM   11435 C  CB  . HIS   I  1 155 ? -26.632 -71.633  -33.505 1.00 43.64 ? 155 HIS   I CB  1 
ATOM   11436 C  CG  . HIS   I  1 155 ? -26.364 -72.521  -32.323 1.00 51.12 ? 155 HIS   I CG  1 
ATOM   11437 N  ND1 . HIS   I  1 155 ? -25.875 -73.808  -32.442 1.00 46.10 ? 155 HIS   I ND1 1 
ATOM   11438 C  CD2 . HIS   I  1 155 ? -26.521 -72.303  -30.993 1.00 58.85 ? 155 HIS   I CD2 1 
ATOM   11439 C  CE1 . HIS   I  1 155 ? -25.748 -74.343  -31.237 1.00 48.81 ? 155 HIS   I CE1 1 
ATOM   11440 N  NE2 . HIS   I  1 155 ? -26.134 -73.451  -30.341 1.00 53.72 ? 155 HIS   I NE2 1 
ATOM   11441 N  N   . GLU   I  1 156 ? -27.613 -68.622  -34.444 1.00 55.44 ? 156 GLU   I N   1 
ATOM   11442 C  CA  . GLU   I  1 156 ? -27.584 -67.755  -35.612 1.00 59.93 ? 156 GLU   I CA  1 
ATOM   11443 C  C   . GLU   I  1 156 ? -26.437 -68.198  -36.518 1.00 54.53 ? 156 GLU   I C   1 
ATOM   11444 O  O   . GLU   I  1 156 ? -26.621 -68.347  -37.722 1.00 63.28 ? 156 GLU   I O   1 
ATOM   11445 C  CB  . GLU   I  1 156 ? -27.415 -66.293  -35.214 1.00 53.16 ? 156 GLU   I CB  1 
ATOM   11446 C  CG  . GLU   I  1 156 ? -28.340 -65.846  -34.117 1.00 50.76 ? 156 GLU   I CG  1 
ATOM   11447 C  CD  . GLU   I  1 156 ? -28.414 -64.328  -33.992 1.00 72.39 ? 156 GLU   I CD  1 
ATOM   11448 O  OE1 . GLU   I  1 156 ? -28.218 -63.633  -35.016 1.00 77.18 ? 156 GLU   I OE1 1 
ATOM   11449 O  OE2 . GLU   I  1 156 ? -28.675 -63.826  -32.875 1.00 62.43 ? 156 GLU   I OE2 1 
ATOM   11450 N  N   . MET   J  1 1   ? 50.072  -68.718  -51.921 1.00 31.63 ? 1   MET   J N   1 
ATOM   11451 C  CA  . MET   J  1 1   ? 51.265  -67.852  -52.033 1.00 34.67 ? 1   MET   J CA  1 
ATOM   11452 C  C   . MET   J  1 1   ? 52.199  -68.155  -50.863 1.00 45.58 ? 1   MET   J C   1 
ATOM   11453 O  O   . MET   J  1 1   ? 51.801  -68.008  -49.728 1.00 43.60 ? 1   MET   J O   1 
ATOM   11454 C  CB  . MET   J  1 1   ? 50.841  -66.378  -52.024 1.00 34.66 ? 1   MET   J CB  1 
ATOM   11455 C  CG  . MET   J  1 1   ? 51.922  -65.387  -52.398 1.00 39.82 ? 1   MET   J CG  1 
ATOM   11456 S  SD  . MET   J  1 1   ? 51.330  -63.667  -52.384 1.00 48.55 ? 1   MET   J SD  1 
ATOM   11457 C  CE  . MET   J  1 1   ? 51.601  -63.166  -50.690 1.00 59.03 ? 1   MET   J CE  1 
ATOM   11458 N  N   . LYS   J  1 2   ? 53.447  -68.544  -51.112 1.00 42.15 ? 2   LYS   J N   1 
ATOM   11459 C  CA  . LYS   J  1 2   ? 54.296  -68.990  -50.009 1.00 45.87 ? 2   LYS   J CA  1 
ATOM   11460 C  C   . LYS   J  1 2   ? 54.567  -67.841  -49.049 1.00 36.21 ? 2   LYS   J C   1 
ATOM   11461 O  O   . LYS   J  1 2   ? 55.178  -66.839  -49.418 1.00 38.56 ? 2   LYS   J O   1 
ATOM   11462 C  CB  . LYS   J  1 2   ? 55.614  -69.560  -50.543 1.00 46.39 ? 2   LYS   J CB  1 
ATOM   11463 N  N   . GLY   J  1 3   ? 54.103  -67.971  -47.813 1.00 39.33 ? 3   GLY   J N   1 
ATOM   11464 C  CA  . GLY   J  1 3   ? 54.384  -66.962  -46.823 1.00 37.06 ? 3   GLY   J CA  1 
ATOM   11465 C  C   . GLY   J  1 3   ? 55.723  -67.187  -46.129 1.00 39.00 ? 3   GLY   J C   1 
ATOM   11466 O  O   . GLY   J  1 3   ? 56.329  -68.247  -46.220 1.00 39.66 ? 3   GLY   J O   1 
ATOM   11467 N  N   . ASP   J  1 4   ? 56.168  -66.141  -45.451 1.00 35.34 ? 4   ASP   J N   1 
ATOM   11468 C  CA  . ASP   J  1 4   ? 57.347  -66.190  -44.597 1.00 40.78 ? 4   ASP   J CA  1 
ATOM   11469 C  C   . ASP   J  1 4   ? 57.100  -67.120  -43.406 1.00 43.86 ? 4   ASP   J C   1 
ATOM   11470 O  O   . ASP   J  1 4   ? 56.044  -67.069  -42.768 1.00 38.92 ? 4   ASP   J O   1 
ATOM   11471 C  CB  . ASP   J  1 4   ? 57.675  -64.769  -44.143 1.00 36.27 ? 4   ASP   J CB  1 
ATOM   11472 C  CG  . ASP   J  1 4   ? 58.811  -64.710  -43.103 1.00 44.78 ? 4   ASP   J CG  1 
ATOM   11473 O  OD1 . ASP   J  1 4   ? 58.540  -64.802  -41.883 1.00 47.09 ? 4   ASP   J OD1 1 
ATOM   11474 O  OD2 . ASP   J  1 4   ? 59.977  -64.550  -43.506 1.00 44.96 ? 4   ASP   J OD2 1 
ATOM   11475 N  N   . LYS   J  1 5   ? 58.068  -67.993  -43.112 1.00 39.53 ? 5   LYS   J N   1 
ATOM   11476 C  CA  . LYS   J  1 5   ? 57.836  -69.013  -42.093 1.00 37.19 ? 5   LYS   J CA  1 
ATOM   11477 C  C   . LYS   J  1 5   ? 57.569  -68.382  -40.729 1.00 35.49 ? 5   LYS   J C   1 
ATOM   11478 O  O   . LYS   J  1 5   ? 56.700  -68.848  -39.982 1.00 35.56 ? 5   LYS   J O   1 
ATOM   11479 C  CB  . LYS   J  1 5   ? 59.030  -69.972  -42.031 1.00 45.15 ? 5   LYS   J CB  1 
ATOM   11480 C  CG  . LYS   J  1 5   ? 58.964  -70.996  -40.911 1.00 43.41 ? 5   LYS   J CG  1 
ATOM   11481 N  N   . LYS   J  1 6   ? 58.292  -67.314  -40.399 1.00 31.41 ? 6   LYS   J N   1 
ATOM   11482 C  CA  . LYS   J  1 6   ? 58.167  -66.694  -39.092 1.00 39.84 ? 6   LYS   J CA  1 
ATOM   11483 C  C   . LYS   J  1 6   ? 56.919  -65.824  -39.004 1.00 45.71 ? 6   LYS   J C   1 
ATOM   11484 O  O   . LYS   J  1 6   ? 56.376  -65.660  -37.911 1.00 35.13 ? 6   LYS   J O   1 
ATOM   11485 C  CB  . LYS   J  1 6   ? 59.405  -65.857  -38.785 1.00 38.67 ? 6   LYS   J CB  1 
ATOM   11486 C  CG  . LYS   J  1 6   ? 59.360  -65.022  -37.488 1.00 58.81 ? 6   LYS   J CG  1 
ATOM   11487 C  CD  . LYS   J  1 6   ? 59.559  -65.858  -36.203 1.00 61.24 ? 6   LYS   J CD  1 
ATOM   11488 C  CE  . LYS   J  1 6   ? 60.082  -64.982  -35.048 1.00 63.01 ? 6   LYS   J CE  1 
ATOM   11489 N  NZ  . LYS   J  1 6   ? 60.281  -65.726  -33.760 1.00 67.43 ? 6   LYS   J NZ  1 
ATOM   11490 N  N   . VAL   J  1 7   ? 56.475  -65.230  -40.121 1.00 40.79 ? 7   VAL   J N   1 
ATOM   11491 C  CA  . VAL   J  1 7   ? 55.143  -64.620  -40.138 1.00 35.00 ? 7   VAL   J CA  1 
ATOM   11492 C  C   . VAL   J  1 7   ? 54.100  -65.640  -39.727 1.00 30.12 ? 7   VAL   J C   1 
ATOM   11493 O  O   . VAL   J  1 7   ? 53.262  -65.398  -38.848 1.00 31.94 ? 7   VAL   J O   1 
ATOM   11494 C  CB  . VAL   J  1 7   ? 54.822  -64.033  -41.523 1.00 36.34 ? 7   VAL   J CB  1 
ATOM   11495 C  CG1 . VAL   J  1 7   ? 53.307  -63.760  -41.615 1.00 40.33 ? 7   VAL   J CG1 1 
ATOM   11496 C  CG2 . VAL   J  1 7   ? 55.594  -62.757  -41.717 1.00 33.42 ? 7   VAL   J CG2 1 
ATOM   11497 N  N   . ILE   J  1 8   ? 54.134  -66.800  -40.356 1.00 29.61 ? 8   ILE   J N   1 
ATOM   11498 C  CA  . ILE   J  1 8   ? 53.137  -67.816  -40.072 1.00 30.11 ? 8   ILE   J CA  1 
ATOM   11499 C  C   . ILE   J  1 8   ? 53.185  -68.254  -38.617 1.00 36.47 ? 8   ILE   J C   1 
ATOM   11500 O  O   . ILE   J  1 8   ? 52.152  -68.591  -38.017 1.00 29.96 ? 8   ILE   J O   1 
ATOM   11501 C  CB  . ILE   J  1 8   ? 53.346  -68.997  -41.024 1.00 28.89 ? 8   ILE   J CB  1 
ATOM   11502 C  CG1 . ILE   J  1 8   ? 52.992  -68.556  -42.445 1.00 40.03 ? 8   ILE   J CG1 1 
ATOM   11503 C  CG2 . ILE   J  1 8   ? 52.546  -70.172  -40.571 1.00 29.96 ? 8   ILE   J CG2 1 
ATOM   11504 C  CD1 . ILE   J  1 8   ? 53.353  -69.574  -43.499 1.00 42.36 ? 8   ILE   J CD1 1 
ATOM   11505 N  N   . GLN   J  1 9   ? 54.386  -68.340  -38.043 1.00 36.13 ? 9   GLN   J N   1 
ATOM   11506 C  CA  . GLN   J  1 9   ? 54.479  -68.712  -36.641 1.00 35.61 ? 9   GLN   J CA  1 
ATOM   11507 C  C   . GLN   J  1 9   ? 53.806  -67.659  -35.779 1.00 26.14 ? 9   GLN   J C   1 
ATOM   11508 O  O   . GLN   J  1 9   ? 53.097  -67.988  -34.831 1.00 31.44 ? 9   GLN   J O   1 
ATOM   11509 C  CB  . GLN   J  1 9   ? 55.954  -68.911  -36.237 1.00 39.30 ? 9   GLN   J CB  1 
ATOM   11510 C  CG  . GLN   J  1 9   ? 56.572  -70.167  -36.883 1.00 40.24 ? 9   GLN   J CG  1 
ATOM   11511 C  CD  . GLN   J  1 9   ? 58.077  -70.318  -36.641 1.00 45.08 ? 9   GLN   J CD  1 
ATOM   11512 O  OE1 . GLN   J  1 9   ? 58.836  -69.346  -36.626 1.00 43.49 ? 9   GLN   J OE1 1 
ATOM   11513 N  NE2 . GLN   J  1 9   ? 58.497  -71.545  -36.420 1.00 47.91 ? 9   GLN   J NE2 1 
ATOM   11514 N  N   . HIS   J  1 10  ? 54.067  -66.386  -36.068 1.00 30.35 ? 10  HIS   J N   1 
ATOM   11515 C  CA  . HIS   J  1 10  ? 53.418  -65.312  -35.338 1.00 35.53 ? 10  HIS   J CA  1 
ATOM   11516 C  C   . HIS   J  1 10  ? 51.900  -65.409  -35.473 1.00 33.34 ? 10  HIS   J C   1 
ATOM   11517 O  O   . HIS   J  1 10  ? 51.165  -65.356  -34.471 1.00 31.41 ? 10  HIS   J O   1 
ATOM   11518 C  CB  . HIS   J  1 10  ? 53.935  -63.965  -35.846 1.00 30.57 ? 10  HIS   J CB  1 
ATOM   11519 C  CG  . HIS   J  1 10  ? 55.194  -63.513  -35.183 1.00 35.97 ? 10  HIS   J CG  1 
ATOM   11520 N  ND1 . HIS   J  1 10  ? 55.229  -63.095  -33.868 1.00 36.01 ? 10  HIS   J ND1 1 
ATOM   11521 C  CD2 . HIS   J  1 10  ? 56.467  -63.425  -35.643 1.00 36.89 ? 10  HIS   J CD2 1 
ATOM   11522 C  CE1 . HIS   J  1 10  ? 56.473  -62.771  -33.545 1.00 43.08 ? 10  HIS   J CE1 1 
ATOM   11523 N  NE2 . HIS   J  1 10  ? 57.246  -62.967  -34.602 1.00 38.88 ? 10  HIS   J NE2 1 
ATOM   11524 N  N   . LEU   J  1 11  ? 51.411  -65.589  -36.704 1.00 34.41 ? 11  LEU   J N   1 
ATOM   11525 C  CA  . LEU   J  1 11  ? 49.967  -65.703  -36.910 1.00 30.08 ? 11  LEU   J CA  1 
ATOM   11526 C  C   . LEU   J  1 11  ? 49.401  -66.849  -36.106 1.00 37.90 ? 11  LEU   J C   1 
ATOM   11527 O  O   . LEU   J  1 11  ? 48.346  -66.704  -35.474 1.00 32.61 ? 11  LEU   J O   1 
ATOM   11528 C  CB  . LEU   J  1 11  ? 49.638  -65.882  -38.396 1.00 34.07 ? 11  LEU   J CB  1 
ATOM   11529 C  CG  . LEU   J  1 11  ? 50.043  -64.715  -39.300 1.00 33.31 ? 11  LEU   J CG  1 
ATOM   11530 C  CD1 . LEU   J  1 11  ? 49.650  -64.985  -40.762 1.00 37.13 ? 11  LEU   J CD1 1 
ATOM   11531 C  CD2 . LEU   J  1 11  ? 49.429  -63.422  -38.808 1.00 34.38 ? 11  LEU   J CD2 1 
ATOM   11532 N  N   . ASN   J  1 12  ? 50.097  -67.994  -36.082 1.00 28.91 ? 12  ASN   J N   1 
ATOM   11533 C  CA  . ASN   J  1 12  ? 49.588  -69.116  -35.288 1.00 33.44 ? 12  ASN   J CA  1 
ATOM   11534 C  C   . ASN   J  1 12  ? 49.626  -68.801  -33.795 1.00 33.73 ? 12  ASN   J C   1 
ATOM   11535 O  O   . ASN   J  1 12  ? 48.794  -69.306  -33.022 1.00 33.01 ? 12  ASN   J O   1 
ATOM   11536 C  CB  . ASN   J  1 12  ? 50.375  -70.398  -35.576 1.00 38.15 ? 12  ASN   J CB  1 
ATOM   11537 C  CG  . ASN   J  1 12  ? 49.645  -71.322  -36.524 1.00 43.10 ? 12  ASN   J CG  1 
ATOM   11538 O  OD1 . ASN   J  1 12  ? 48.418  -71.460  -36.465 1.00 38.93 ? 12  ASN   J OD1 1 
ATOM   11539 N  ND2 . ASN   J  1 12  ? 50.395  -71.972  -37.405 1.00 35.97 ? 12  ASN   J ND2 1 
ATOM   11540 N  N   . LYS   J  1 13  ? 50.572  -67.966  -33.374 1.00 31.73 ? 13  LYS   J N   1 
ATOM   11541 C  CA  . LYS   J  1 13  ? 50.593  -67.567  -31.976 1.00 36.74 ? 13  LYS   J CA  1 
ATOM   11542 C  C   . LYS   J  1 13  ? 49.387  -66.690  -31.645 1.00 35.85 ? 13  LYS   J C   1 
ATOM   11543 O  O   . LYS   J  1 13  ? 48.706  -66.898  -30.632 1.00 29.38 ? 13  LYS   J O   1 
ATOM   11544 C  CB  . LYS   J  1 13  ? 51.878  -66.818  -31.665 1.00 27.88 ? 13  LYS   J CB  1 
ATOM   11545 C  CG  . LYS   J  1 13  ? 52.111  -66.685  -30.173 1.00 30.35 ? 13  LYS   J CG  1 
ATOM   11546 C  CD  . LYS   J  1 13  ? 53.395  -65.924  -29.869 1.00 42.12 ? 13  LYS   J CD  1 
ATOM   11547 C  CE  . LYS   J  1 13  ? 53.669  -65.900  -28.380 1.00 50.50 ? 13  LYS   J CE  1 
ATOM   11548 N  NZ  . LYS   J  1 13  ? 54.876  -65.050  -28.083 1.00 60.73 ? 13  LYS   J NZ  1 
ATOM   11549 N  N   . ILE   J  1 14  ? 49.142  -65.673  -32.472 1.00 30.80 ? 14  ILE   J N   1 
ATOM   11550 C  CA  . ILE   J  1 14  ? 47.955  -64.840  -32.289 1.00 38.21 ? 14  ILE   J CA  1 
ATOM   11551 C  C   . ILE   J  1 14  ? 46.711  -65.713  -32.253 1.00 29.21 ? 14  ILE   J C   1 
ATOM   11552 O  O   . ILE   J  1 14  ? 45.863  -65.602  -31.359 1.00 36.13 ? 14  ILE   J O   1 
ATOM   11553 C  CB  . ILE   J  1 14  ? 47.851  -63.785  -33.404 1.00 32.33 ? 14  ILE   J CB  1 
ATOM   11554 C  CG1 . ILE   J  1 14  ? 49.151  -62.984  -33.558 1.00 29.26 ? 14  ILE   J CG1 1 
ATOM   11555 C  CG2 . ILE   J  1 14  ? 46.661  -62.861  -33.110 1.00 30.01 ? 14  ILE   J CG2 1 
ATOM   11556 C  CD1 . ILE   J  1 14  ? 49.680  -62.435  -32.232 1.00 41.81 ? 14  ILE   J CD1 1 
ATOM   11557 N  N   . LEU   J  1 15  ? 46.578  -66.605  -33.235 1.00 30.68 ? 15  LEU   J N   1 
ATOM   11558 C  CA  . LEU   J  1 15  ? 45.446  -67.516  -33.251 1.00 29.30 ? 15  LEU   J CA  1 
ATOM   11559 C  C   . LEU   J  1 15  ? 45.330  -68.314  -31.958 1.00 35.02 ? 15  LEU   J C   1 
ATOM   11560 O  O   . LEU   J  1 15  ? 44.222  -68.507  -31.426 1.00 30.53 ? 15  LEU   J O   1 
ATOM   11561 C  CB  . LEU   J  1 15  ? 45.563  -68.434  -34.459 1.00 28.74 ? 15  LEU   J CB  1 
ATOM   11562 C  CG  . LEU   J  1 15  ? 44.670  -69.634  -34.610 1.00 30.96 ? 15  LEU   J CG  1 
ATOM   11563 C  CD1 . LEU   J  1 15  ? 43.178  -69.194  -34.662 1.00 32.53 ? 15  LEU   J CD1 1 
ATOM   11564 C  CD2 . LEU   J  1 15  ? 45.088  -70.407  -35.879 1.00 34.12 ? 15  LEU   J CD2 1 
ATOM   11565 N  N   . GLY   J  1 16  ? 46.450  -68.844  -31.472 1.00 37.35 ? 16  GLY   J N   1 
ATOM   11566 C  CA  . GLY   J  1 16  ? 46.422  -69.559  -30.210 1.00 29.17 ? 16  GLY   J CA  1 
ATOM   11567 C  C   . GLY   J  1 16  ? 45.831  -68.722  -29.091 1.00 30.24 ? 16  GLY   J C   1 
ATOM   11568 O  O   . GLY   J  1 16  ? 45.047  -69.220  -28.283 1.00 32.06 ? 16  GLY   J O   1 
ATOM   11569 N  N   . ASN   J  1 17  ? 46.196  -67.433  -29.035 1.00 32.02 ? 17  ASN   J N   1 
ATOM   11570 C  CA  . ASN   J  1 17  ? 45.601  -66.536  -28.052 1.00 31.67 ? 17  ASN   J CA  1 
ATOM   11571 C  C   . ASN   J  1 17  ? 44.101  -66.374  -28.282 1.00 35.58 ? 17  ASN   J C   1 
ATOM   11572 O  O   . ASN   J  1 17  ? 43.331  -66.355  -27.315 1.00 29.15 ? 17  ASN   J O   1 
ATOM   11573 C  CB  . ASN   J  1 17  ? 46.278  -65.173  -28.090 1.00 26.97 ? 17  ASN   J CB  1 
ATOM   11574 C  CG  . ASN   J  1 17  ? 47.673  -65.211  -27.566 1.00 33.72 ? 17  ASN   J CG  1 
ATOM   11575 O  OD1 . ASN   J  1 17  ? 48.028  -66.108  -26.808 1.00 35.61 ? 17  ASN   J OD1 1 
ATOM   11576 N  ND2 . ASN   J  1 17  ? 48.474  -64.235  -27.950 1.00 35.32 ? 17  ASN   J ND2 1 
ATOM   11577 N  N   . GLU   J  1 18  ? 43.670  -66.288  -29.556 1.00 31.34 ? 18  GLU   J N   1 
ATOM   11578 C  CA  . GLU   J  1 18  ? 42.245  -66.157  -29.880 1.00 32.88 ? 18  GLU   J CA  1 
ATOM   11579 C  C   . GLU   J  1 18  ? 41.458  -67.379  -29.427 1.00 33.58 ? 18  GLU   J C   1 
ATOM   11580 O  O   . GLU   J  1 18  ? 40.327  -67.257  -28.922 1.00 29.03 ? 18  GLU   J O   1 
ATOM   11581 C  CB  . GLU   J  1 18  ? 42.057  -65.935  -31.394 1.00 28.88 ? 18  GLU   J CB  1 
ATOM   11582 C  CG  . GLU   J  1 18  ? 42.672  -64.668  -31.942 1.00 37.45 ? 18  GLU   J CG  1 
ATOM   11583 C  CD  . GLU   J  1 18  ? 41.910  -63.427  -31.564 1.00 46.68 ? 18  GLU   J CD  1 
ATOM   11584 O  OE1 . GLU   J  1 18  ? 40.778  -63.571  -31.032 1.00 41.34 ? 18  GLU   J OE1 1 
ATOM   11585 O  OE2 . GLU   J  1 18  ? 42.443  -62.311  -31.816 1.00 41.04 ? 18  GLU   J OE2 1 
ATOM   11586 N  N   . LEU   J  1 19  ? 42.037  -68.574  -29.579 1.00 31.88 ? 19  LEU   J N   1 
ATOM   11587 C  CA  . LEU   J  1 19  ? 41.330  -69.778  -29.142 1.00 29.95 ? 19  LEU   J CA  1 
ATOM   11588 C  C   . LEU   J  1 19  ? 41.133  -69.790  -27.631 1.00 28.47 ? 19  LEU   J C   1 
ATOM   11589 O  O   . LEU   J  1 19  ? 40.077  -70.219  -27.136 1.00 35.12 ? 19  LEU   J O   1 
ATOM   11590 C  CB  . LEU   J  1 19  ? 42.091  -71.028  -29.585 1.00 32.96 ? 19  LEU   J CB  1 
ATOM   11591 C  CG  . LEU   J  1 19  ? 42.208  -71.138  -31.116 1.00 41.11 ? 19  LEU   J CG  1 
ATOM   11592 C  CD1 . LEU   J  1 19  ? 43.058  -72.310  -31.563 1.00 42.51 ? 19  LEU   J CD1 1 
ATOM   11593 C  CD2 . LEU   J  1 19  ? 40.863  -71.261  -31.748 1.00 36.06 ? 19  LEU   J CD2 1 
ATOM   11594 N  N   . ILE   J  1 20  ? 42.139  -69.334  -26.882 1.00 29.43 ? 20  ILE   J N   1 
ATOM   11595 C  CA  . ILE   J  1 20  ? 41.980  -69.178  -25.438 1.00 31.49 ? 20  ILE   J CA  1 
ATOM   11596 C  C   . ILE   J  1 20  ? 40.836  -68.218  -25.158 1.00 28.26 ? 20  ILE   J C   1 
ATOM   11597 O  O   . ILE   J  1 20  ? 39.951  -68.498  -24.349 1.00 26.32 ? 20  ILE   J O   1 
ATOM   11598 C  CB  . ILE   J  1 20  ? 43.283  -68.668  -24.805 1.00 27.82 ? 20  ILE   J CB  1 
ATOM   11599 C  CG1 . ILE   J  1 20  ? 44.392  -69.705  -24.985 1.00 31.43 ? 20  ILE   J CG1 1 
ATOM   11600 C  CG2 . ILE   J  1 20  ? 43.084  -68.352  -23.320 1.00 28.32 ? 20  ILE   J CG2 1 
ATOM   11601 C  CD1 . ILE   J  1 20  ? 45.770  -69.215  -24.539 1.00 31.01 ? 20  ILE   J CD1 1 
ATOM   11602 N  N   . ALA   J  1 21  ? 40.869  -67.058  -25.815 1.00 29.30 ? 21  ALA   J N   1 
ATOM   11603 C  CA  . ALA   J  1 21  ? 39.878  -66.012  -25.567 1.00 37.61 ? 21  ALA   J CA  1 
ATOM   11604 C  C   . ALA   J  1 21  ? 38.466  -66.480  -25.911 1.00 30.11 ? 21  ALA   J C   1 
ATOM   11605 O  O   . ALA   J  1 21  ? 37.517  -66.209  -25.170 1.00 29.21 ? 21  ALA   J O   1 
ATOM   11606 C  CB  . ALA   J  1 21  ? 40.251  -64.757  -26.362 1.00 28.66 ? 21  ALA   J CB  1 
ATOM   11607 N  N   . ILE   J  1 22  ? 38.306  -67.203  -27.015 1.00 32.73 ? 22  ILE   J N   1 
ATOM   11608 C  CA  . ILE   J  1 22  ? 36.981  -67.700  -27.379 1.00 33.66 ? 22  ILE   J CA  1 
ATOM   11609 C  C   . ILE   J  1 22  ? 36.374  -68.511  -26.237 1.00 35.52 ? 22  ILE   J C   1 
ATOM   11610 O  O   . ILE   J  1 22  ? 35.212  -68.303  -25.854 1.00 26.67 ? 22  ILE   J O   1 
ATOM   11611 C  CB  . ILE   J  1 22  ? 37.054  -68.532  -28.670 1.00 29.13 ? 22  ILE   J CB  1 
ATOM   11612 C  CG1 . ILE   J  1 22  ? 37.314  -67.636  -29.882 1.00 28.45 ? 22  ILE   J CG1 1 
ATOM   11613 C  CG2 . ILE   J  1 22  ? 35.779  -69.295  -28.853 1.00 30.44 ? 22  ILE   J CG2 1 
ATOM   11614 C  CD1 . ILE   J  1 22  ? 37.797  -68.407  -31.072 1.00 33.04 ? 22  ILE   J CD1 1 
ATOM   11615 N  N   . ASN   J  1 23  ? 37.135  -69.461  -25.685 1.00 26.58 ? 23  ASN   J N   1 
ATOM   11616 C  CA  . ASN   J  1 23  ? 36.584  -70.329  -24.646 1.00 28.93 ? 23  ASN   J CA  1 
ATOM   11617 C  C   . ASN   J  1 23  ? 36.456  -69.622  -23.296 1.00 28.11 ? 23  ASN   J C   1 
ATOM   11618 O  O   . ASN   J  1 23  ? 35.451  -69.805  -22.595 1.00 28.72 ? 23  ASN   J O   1 
ATOM   11619 C  CB  . ASN   J  1 23  ? 37.435  -71.577  -24.514 1.00 29.59 ? 23  ASN   J CB  1 
ATOM   11620 C  CG  . ASN   J  1 23  ? 37.357  -72.460  -25.749 1.00 40.39 ? 23  ASN   J CG  1 
ATOM   11621 O  OD1 . ASN   J  1 23  ? 36.956  -71.998  -26.823 1.00 33.29 ? 23  ASN   J OD1 1 
ATOM   11622 N  ND2 . ASN   J  1 23  ? 37.717  -73.739  -25.602 1.00 37.11 ? 23  ASN   J ND2 1 
ATOM   11623 N  N   . GLN   J  1 24  ? 37.460  -68.831  -22.921 1.00 28.70 ? 24  GLN   J N   1 
ATOM   11624 C  CA  . GLN   J  1 24  ? 37.408  -68.081  -21.676 1.00 32.39 ? 24  GLN   J CA  1 
ATOM   11625 C  C   . GLN   J  1 24  ? 36.205  -67.136  -21.654 1.00 29.70 ? 24  GLN   J C   1 
ATOM   11626 O  O   . GLN   J  1 24  ? 35.472  -67.062  -20.661 1.00 25.87 ? 24  GLN   J O   1 
ATOM   11627 C  CB  . GLN   J  1 24  ? 38.696  -67.293  -21.509 1.00 26.99 ? 24  GLN   J CB  1 
ATOM   11628 C  CG  . GLN   J  1 24  ? 38.662  -66.299  -20.375 1.00 30.30 ? 24  GLN   J CG  1 
ATOM   11629 C  CD  . GLN   J  1 24  ? 40.038  -65.765  -20.058 1.00 30.73 ? 24  GLN   J CD  1 
ATOM   11630 O  OE1 . GLN   J  1 24  ? 41.031  -66.471  -20.200 1.00 35.30 ? 24  GLN   J OE1 1 
ATOM   11631 N  NE2 . GLN   J  1 24  ? 40.108  -64.496  -19.676 1.00 28.59 ? 24  GLN   J NE2 1 
ATOM   11632 N  N   . TYR   J  1 25  ? 36.017  -66.375  -22.734 1.00 29.62 ? 25  TYR   J N   1 
ATOM   11633 C  CA  . TYR   J  1 25  ? 34.873  -65.463  -22.810 1.00 31.65 ? 25  TYR   J CA  1 
ATOM   11634 C  C   . TYR   J  1 25  ? 33.559  -66.223  -22.896 1.00 28.31 ? 25  TYR   J C   1 
ATOM   11635 O  O   . TYR   J  1 25  ? 32.566  -65.814  -22.282 1.00 26.80 ? 25  TYR   J O   1 
ATOM   11636 C  CB  . TYR   J  1 25  ? 35.007  -64.494  -23.993 1.00 27.42 ? 25  TYR   J CB  1 
ATOM   11637 C  CG  . TYR   J  1 25  ? 36.277  -63.651  -23.984 1.00 33.80 ? 25  TYR   J CG  1 
ATOM   11638 C  CD1 . TYR   J  1 25  ? 37.116  -63.610  -22.857 1.00 34.50 ? 25  TYR   J CD1 1 
ATOM   11639 C  CD2 . TYR   J  1 25  ? 36.651  -62.910  -25.096 1.00 31.87 ? 25  TYR   J CD2 1 
ATOM   11640 C  CE1 . TYR   J  1 25  ? 38.282  -62.857  -22.854 1.00 30.34 ? 25  TYR   J CE1 1 
ATOM   11641 C  CE2 . TYR   J  1 25  ? 37.829  -62.159  -25.110 1.00 31.84 ? 25  TYR   J CE2 1 
ATOM   11642 C  CZ  . TYR   J  1 25  ? 38.643  -62.144  -23.973 1.00 38.09 ? 25  TYR   J CZ  1 
ATOM   11643 O  OH  . TYR   J  1 25  ? 39.815  -61.416  -23.933 1.00 40.23 ? 25  TYR   J OH  1 
ATOM   11644 N  N   . PHE   J  1 26  ? 33.510  -67.334  -23.639 1.00 27.08 ? 26  PHE   J N   1 
ATOM   11645 C  CA  . PHE   J  1 26  ? 32.240  -68.020  -23.764 1.00 28.50 ? 26  PHE   J CA  1 
ATOM   11646 C  C   . PHE   J  1 26  ? 31.820  -68.603  -22.420 1.00 31.56 ? 26  PHE   J C   1 
ATOM   11647 O  O   . PHE   J  1 26  ? 30.653  -68.492  -22.015 1.00 28.43 ? 26  PHE   J O   1 
ATOM   11648 C  CB  . PHE   J  1 26  ? 32.279  -69.107  -24.835 1.00 28.25 ? 26  PHE   J CB  1 
ATOM   11649 C  CG  . PHE   J  1 26  ? 30.936  -69.451  -25.346 1.00 28.67 ? 26  PHE   J CG  1 
ATOM   11650 C  CD1 . PHE   J  1 26  ? 30.145  -70.380  -24.698 1.00 31.62 ? 26  PHE   J CD1 1 
ATOM   11651 C  CD2 . PHE   J  1 26  ? 30.420  -68.800  -26.463 1.00 31.84 ? 26  PHE   J CD2 1 
ATOM   11652 C  CE1 . PHE   J  1 26  ? 28.868  -70.668  -25.162 1.00 31.95 ? 26  PHE   J CE1 1 
ATOM   11653 C  CE2 . PHE   J  1 26  ? 29.135  -69.085  -26.917 1.00 30.65 ? 26  PHE   J CE2 1 
ATOM   11654 C  CZ  . PHE   J  1 26  ? 28.362  -70.007  -26.270 1.00 28.55 ? 26  PHE   J CZ  1 
ATOM   11655 N  N   . LEU   J  1 27  ? 32.776  -69.167  -21.688 1.00 30.42 ? 27  LEU   J N   1 
ATOM   11656 C  CA  . LEU   J  1 27  ? 32.475  -69.698  -20.368 1.00 28.30 ? 27  LEU   J CA  1 
ATOM   11657 C  C   . LEU   J  1 27  ? 32.085  -68.581  -19.412 1.00 25.44 ? 27  LEU   J C   1 
ATOM   11658 O  O   . LEU   J  1 27  ? 31.142  -68.738  -18.641 1.00 23.81 ? 27  LEU   J O   1 
ATOM   11659 C  CB  . LEU   J  1 27  ? 33.666  -70.474  -19.819 1.00 28.70 ? 27  LEU   J CB  1 
ATOM   11660 C  CG  . LEU   J  1 27  ? 33.541  -71.030  -18.393 1.00 31.09 ? 27  LEU   J CG  1 
ATOM   11661 C  CD1 . LEU   J  1 27  ? 32.338  -71.928  -18.283 1.00 32.97 ? 27  LEU   J CD1 1 
ATOM   11662 C  CD2 . LEU   J  1 27  ? 34.795  -71.803  -17.977 1.00 34.99 ? 27  LEU   J CD2 1 
ATOM   11663 N  N   . HIS   J  1 28  ? 32.828  -67.472  -19.408 1.00 26.20 ? 28  HIS   J N   1 
ATOM   11664 C  CA  . HIS   J  1 28  ? 32.454  -66.371  -18.532 1.00 22.78 ? 28  HIS   J CA  1 
ATOM   11665 C  C   . HIS   J  1 28  ? 31.042  -65.895  -18.856 1.00 27.89 ? 28  HIS   J C   1 
ATOM   11666 O  O   . HIS   J  1 28  ? 30.263  -65.572  -17.954 1.00 27.80 ? 28  HIS   J O   1 
ATOM   11667 C  CB  . HIS   J  1 28  ? 33.457  -65.213  -18.657 1.00 25.10 ? 28  HIS   J CB  1 
ATOM   11668 C  CG  . HIS   J  1 28  ? 34.738  -65.413  -17.898 1.00 33.23 ? 28  HIS   J CG  1 
ATOM   11669 N  ND1 . HIS   J  1 28  ? 35.860  -64.628  -18.099 1.00 27.58 ? 28  HIS   J ND1 1 
ATOM   11670 C  CD2 . HIS   J  1 28  ? 35.065  -66.287  -16.918 1.00 24.37 ? 28  HIS   J CD2 1 
ATOM   11671 C  CE1 . HIS   J  1 28  ? 36.814  -65.006  -17.270 1.00 31.67 ? 28  HIS   J CE1 1 
ATOM   11672 N  NE2 . HIS   J  1 28  ? 36.366  -66.021  -16.553 1.00 27.23 ? 28  HIS   J NE2 1 
ATOM   11673 N  N   . SER   J  1 29  ? 30.691  -65.875  -20.151 1.00 25.74 ? 29  SER   J N   1 
ATOM   11674 C  CA  . SER   J  1 29  ? 29.370  -65.430  -20.565 1.00 24.30 ? 29  SER   J CA  1 
ATOM   11675 C  C   . SER   J  1 29  ? 28.294  -66.301  -19.952 1.00 29.79 ? 29  SER   J C   1 
ATOM   11676 O  O   . SER   J  1 29  ? 27.307  -65.801  -19.395 1.00 29.31 ? 29  SER   J O   1 
ATOM   11677 C  CB  . SER   J  1 29  ? 29.254  -65.445  -22.094 1.00 23.90 ? 29  SER   J CB  1 
ATOM   11678 O  OG  . SER   J  1 29  ? 27.888  -65.373  -22.508 1.00 26.50 ? 29  SER   J OG  1 
ATOM   11679 N  N   . ARG   J  1 30  ? 28.461  -67.617  -20.066 1.00 24.75 ? 30  ARG   J N   1 
ATOM   11680 C  CA  . ARG   J  1 30  ? 27.453  -68.536  -19.576 1.00 27.12 ? 30  ARG   J CA  1 
ATOM   11681 C  C   . ARG   J  1 30  ? 27.443  -68.610  -18.060 1.00 27.43 ? 30  ARG   J C   1 
ATOM   11682 O  O   . ARG   J  1 30  ? 26.401  -68.926  -17.475 1.00 27.62 ? 30  ARG   J O   1 
ATOM   11683 C  CB  . ARG   J  1 30  ? 27.682  -69.904  -20.210 1.00 26.62 ? 30  ARG   J CB  1 
ATOM   11684 C  CG  . ARG   J  1 30  ? 27.018  -70.077  -21.586 1.00 31.55 ? 30  ARG   J CG  1 
ATOM   11685 C  CD  . ARG   J  1 30  ? 27.139  -68.858  -22.548 1.00 27.77 ? 30  ARG   J CD  1 
ATOM   11686 N  NE  . ARG   J  1 30  ? 26.174  -69.013  -23.629 1.00 35.36 ? 30  ARG   J NE  1 
ATOM   11687 C  CZ  . ARG   J  1 30  ? 25.496  -68.020  -24.193 1.00 32.06 ? 30  ARG   J CZ  1 
ATOM   11688 N  NH1 . ARG   J  1 30  ? 25.716  -66.751  -23.864 1.00 30.61 ? 30  ARG   J NH1 1 
ATOM   11689 N  NH2 . ARG   J  1 30  ? 24.570  -68.308  -25.102 1.00 30.75 ? 30  ARG   J NH2 1 
ATOM   11690 N  N   . MET   J  1 31  ? 28.566  -68.288  -17.409 1.00 26.20 ? 31  MET   J N   1 
ATOM   11691 C  CA  . MET   J  1 31  ? 28.557  -68.224  -15.949 1.00 25.69 ? 31  MET   J CA  1 
ATOM   11692 C  C   . MET   J  1 31  ? 27.721  -67.042  -15.492 1.00 29.26 ? 31  MET   J C   1 
ATOM   11693 O  O   . MET   J  1 31  ? 26.858  -67.173  -14.609 1.00 26.74 ? 31  MET   J O   1 
ATOM   11694 C  CB  . MET   J  1 31  ? 29.993  -68.108  -15.404 1.00 30.25 ? 31  MET   J CB  1 
ATOM   11695 C  CG  . MET   J  1 31  ? 30.843  -69.414  -15.431 1.00 28.96 ? 31  MET   J CG  1 
ATOM   11696 S  SD  . MET   J  1 31  ? 32.631  -69.044  -15.289 1.00 28.72 ? 31  MET   J SD  1 
ATOM   11697 C  CE  . MET   J  1 31  ? 32.708  -68.646  -13.544 1.00 38.87 ? 31  MET   J CE  1 
ATOM   11698 N  N   . TRP   J  1 32  ? 27.913  -65.901  -16.151 1.00 29.71 ? 32  TRP   J N   1 
ATOM   11699 C  CA  . TRP   J  1 32  ? 27.159  -64.709  -15.801 1.00 28.28 ? 32  TRP   J CA  1 
ATOM   11700 C  C   . TRP   J  1 32  ? 25.667  -64.920  -16.032 1.00 31.78 ? 32  TRP   J C   1 
ATOM   11701 O  O   . TRP   J  1 32  ? 24.846  -64.571  -15.171 1.00 26.91 ? 32  TRP   J O   1 
ATOM   11702 C  CB  . TRP   J  1 32  ? 27.691  -63.509  -16.589 1.00 28.19 ? 32  TRP   J CB  1 
ATOM   11703 C  CG  . TRP   J  1 32  ? 28.809  -62.782  -15.874 1.00 31.62 ? 32  TRP   J CG  1 
ATOM   11704 C  CD1 . TRP   J  1 32  ? 28.886  -62.514  -14.550 1.00 34.52 ? 32  TRP   J CD1 1 
ATOM   11705 C  CD2 . TRP   J  1 32  ? 30.012  -62.251  -16.457 1.00 24.35 ? 32  TRP   J CD2 1 
ATOM   11706 N  NE1 . TRP   J  1 32  ? 30.058  -61.856  -14.264 1.00 27.45 ? 32  TRP   J NE1 1 
ATOM   11707 C  CE2 . TRP   J  1 32  ? 30.760  -61.671  -15.417 1.00 29.71 ? 32  TRP   J CE2 1 
ATOM   11708 C  CE3 . TRP   J  1 32  ? 30.523  -62.208  -17.754 1.00 28.99 ? 32  TRP   J CE3 1 
ATOM   11709 C  CZ2 . TRP   J  1 32  ? 32.001  -61.065  -15.628 1.00 27.95 ? 32  TRP   J CZ2 1 
ATOM   11710 C  CZ3 . TRP   J  1 32  ? 31.756  -61.588  -17.974 1.00 29.16 ? 32  TRP   J CZ3 1 
ATOM   11711 C  CH2 . TRP   J  1 32  ? 32.476  -61.028  -16.919 1.00 27.90 ? 32  TRP   J CH2 1 
ATOM   11712 N  N   . ASN   J  1 33  ? 25.300  -65.521  -17.173 1.00 26.35 ? 33  ASN   J N   1 
ATOM   11713 C  CA  . ASN   J  1 33  ? 23.909  -65.856  -17.422 1.00 30.78 ? 33  ASN   J CA  1 
ATOM   11714 C  C   . ASN   J  1 33  ? 23.353  -66.768  -16.345 1.00 37.79 ? 33  ASN   J C   1 
ATOM   11715 O  O   . ASN   J  1 33  ? 22.238  -66.552  -15.865 1.00 29.76 ? 33  ASN   J O   1 
ATOM   11716 C  CB  . ASN   J  1 33  ? 23.763  -66.508  -18.787 1.00 30.59 ? 33  ASN   J CB  1 
ATOM   11717 C  CG  . ASN   J  1 33  ? 23.843  -65.517  -19.909 1.00 32.17 ? 33  ASN   J CG  1 
ATOM   11718 O  OD1 . ASN   J  1 33  ? 23.678  -64.308  -19.702 1.00 33.17 ? 33  ASN   J OD1 1 
ATOM   11719 N  ND2 . ASN   J  1 33  ? 24.095  -66.016  -21.121 1.00 30.47 ? 33  ASN   J ND2 1 
ATOM   11720 N  N   . ASP   J  1 34  ? 24.108  -67.801  -15.965 1.00 30.40 ? 34  ASP   J N   1 
ATOM   11721 C  CA  . ASP   J  1 34  ? 23.673  -68.706  -14.902 1.00 28.79 ? 34  ASP   J CA  1 
ATOM   11722 C  C   . ASP   J  1 34  ? 23.402  -67.950  -13.604 1.00 29.04 ? 34  ASP   J C   1 
ATOM   11723 O  O   . ASP   J  1 34  ? 22.480  -68.291  -12.851 1.00 29.56 ? 34  ASP   J O   1 
ATOM   11724 C  CB  . ASP   J  1 34  ? 24.746  -69.781  -14.684 1.00 32.07 ? 34  ASP   J CB  1 
ATOM   11725 C  CG  . ASP   J  1 34  ? 24.457  -70.696  -13.473 1.00 39.68 ? 34  ASP   J CG  1 
ATOM   11726 O  OD1 . ASP   J  1 34  ? 23.439  -71.414  -13.476 1.00 38.00 ? 34  ASP   J OD1 1 
ATOM   11727 O  OD2 . ASP   J  1 34  ? 25.275  -70.716  -12.534 1.00 43.46 ? 34  ASP   J OD2 1 
ATOM   11728 N  N   . TRP   J  1 35  ? 24.205  -66.935  -13.320 1.00 27.28 ? 35  TRP   J N   1 
ATOM   11729 C  CA  . TRP   J  1 35  ? 24.072  -66.140  -12.106 1.00 33.03 ? 35  TRP   J CA  1 
ATOM   11730 C  C   . TRP   J  1 35  ? 22.997  -65.069  -12.202 1.00 28.36 ? 35  TRP   J C   1 
ATOM   11731 O  O   . TRP   J  1 35  ? 22.819  -64.316  -11.241 1.00 28.07 ? 35  TRP   J O   1 
ATOM   11732 C  CB  . TRP   J  1 35  ? 25.408  -65.463  -11.781 1.00 30.80 ? 35  TRP   J CB  1 
ATOM   11733 C  CG  . TRP   J  1 35  ? 26.523  -66.441  -11.504 1.00 29.89 ? 35  TRP   J CG  1 
ATOM   11734 C  CD1 . TRP   J  1 35  ? 26.402  -67.778  -11.262 1.00 35.70 ? 35  TRP   J CD1 1 
ATOM   11735 C  CD2 . TRP   J  1 35  ? 27.916  -66.145  -11.436 1.00 32.18 ? 35  TRP   J CD2 1 
ATOM   11736 N  NE1 . TRP   J  1 35  ? 27.638  -68.332  -11.047 1.00 43.38 ? 35  TRP   J NE1 1 
ATOM   11737 C  CE2 . TRP   J  1 35  ? 28.587  -67.353  -11.151 1.00 41.10 ? 35  TRP   J CE2 1 
ATOM   11738 C  CE3 . TRP   J  1 35  ? 28.665  -64.984  -11.600 1.00 30.73 ? 35  TRP   J CE3 1 
ATOM   11739 C  CZ2 . TRP   J  1 35  ? 29.971  -67.426  -11.024 1.00 40.72 ? 35  TRP   J CZ2 1 
ATOM   11740 C  CZ3 . TRP   J  1 35  ? 30.042  -65.061  -11.474 1.00 38.39 ? 35  TRP   J CZ3 1 
ATOM   11741 C  CH2 . TRP   J  1 35  ? 30.678  -66.267  -11.184 1.00 35.95 ? 35  TRP   J CH2 1 
ATOM   11742 N  N   . GLY   J  1 36  ? 22.304  -64.970  -13.337 1.00 27.41 ? 36  GLY   J N   1 
ATOM   11743 C  CA  . GLY   J  1 36  ? 21.317  -63.933  -13.527 1.00 28.61 ? 36  GLY   J CA  1 
ATOM   11744 C  C   . GLY   J  1 36  ? 21.885  -62.592  -13.885 1.00 29.22 ? 36  GLY   J C   1 
ATOM   11745 O  O   . GLY   J  1 36  ? 21.177  -61.590  -13.778 1.00 29.92 ? 36  GLY   J O   1 
ATOM   11746 N  N   . LEU   J  1 37  ? 23.155  -62.523  -14.277 1.00 26.87 ? 37  LEU   J N   1 
ATOM   11747 C  CA  . LEU   J  1 37  ? 23.740  -61.258  -14.692 1.00 24.68 ? 37  LEU   J CA  1 
ATOM   11748 C  C   . LEU   J  1 37  ? 23.738  -61.196  -16.223 1.00 30.07 ? 37  LEU   J C   1 
ATOM   11749 O  O   . LEU   J  1 37  ? 24.770  -61.145  -16.874 1.00 28.11 ? 37  LEU   J O   1 
ATOM   11750 C  CB  . LEU   J  1 37  ? 25.138  -61.101  -14.097 1.00 29.25 ? 37  LEU   J CB  1 
ATOM   11751 C  CG  . LEU   J  1 37  ? 25.110  -61.115  -12.566 1.00 29.28 ? 37  LEU   J CG  1 
ATOM   11752 C  CD1 . LEU   J  1 37  ? 26.500  -61.183  -11.963 1.00 28.49 ? 37  LEU   J CD1 1 
ATOM   11753 C  CD2 . LEU   J  1 37  ? 24.375  -59.884  -12.035 1.00 29.36 ? 37  LEU   J CD2 1 
ATOM   11754 N  N   . LYS   J  1 38  ? 22.525  -61.145  -16.784 1.00 26.38 ? 38  LYS   J N   1 
ATOM   11755 C  CA  . LYS   J  1 38  ? 22.330  -61.388  -18.219 1.00 26.77 ? 38  LYS   J CA  1 
ATOM   11756 C  C   . LYS   J  1 38  ? 22.944  -60.312  -19.091 1.00 24.30 ? 38  LYS   J C   1 
ATOM   11757 O  O   . LYS   J  1 38  ? 23.269  -60.563  -20.265 1.00 26.13 ? 38  LYS   J O   1 
ATOM   11758 C  CB  . LYS   J  1 38  ? 20.840  -61.470  -18.549 1.00 27.53 ? 38  LYS   J CB  1 
ATOM   11759 C  CG  . LYS   J  1 38  ? 20.064  -62.501  -17.749 1.00 47.80 ? 38  LYS   J CG  1 
ATOM   11760 C  CD  . LYS   J  1 38  ? 20.518  -63.912  -18.063 1.00 44.14 ? 38  LYS   J CD  1 
ATOM   11761 C  CE  . LYS   J  1 38  ? 19.619  -64.956  -17.385 1.00 46.06 ? 38  LYS   J CE  1 
ATOM   11762 N  NZ  . LYS   J  1 38  ? 19.020  -65.911  -18.360 1.00 56.65 ? 38  LYS   J NZ  1 
ATOM   11763 N  N   . ARG   J  1 39  ? 23.059  -59.091  -18.591 1.00 25.34 ? 39  ARG   J N   1 
ATOM   11764 C  CA  . ARG   J  1 39  ? 23.650  -58.067  -19.439 1.00 25.02 ? 39  ARG   J CA  1 
ATOM   11765 C  C   . ARG   J  1 39  ? 25.161  -58.277  -19.575 1.00 29.76 ? 39  ARG   J C   1 
ATOM   11766 O  O   . ARG   J  1 39  ? 25.729  -58.108  -20.666 1.00 26.48 ? 39  ARG   J O   1 
ATOM   11767 C  CB  . ARG   J  1 39  ? 23.335  -56.695  -18.870 1.00 27.14 ? 39  ARG   J CB  1 
ATOM   11768 C  CG  . ARG   J  1 39  ? 23.767  -55.538  -19.740 1.00 36.64 ? 39  ARG   J CG  1 
ATOM   11769 C  CD  . ARG   J  1 39  ? 23.618  -54.214  -18.985 1.00 49.62 ? 39  ARG   J CD  1 
ATOM   11770 N  NE  . ARG   J  1 39  ? 23.545  -53.049  -19.860 1.00 56.69 ? 39  ARG   J NE  1 
ATOM   11771 C  CZ  . ARG   J  1 39  ? 22.414  -52.431  -20.181 1.00 63.27 ? 39  ARG   J CZ  1 
ATOM   11772 N  NH1 . ARG   J  1 39  ? 21.235  -52.895  -19.789 1.00 53.38 ? 39  ARG   J NH1 1 
ATOM   11773 N  NH2 . ARG   J  1 39  ? 22.466  -51.312  -20.897 1.00 64.38 ? 39  ARG   J NH2 1 
ATOM   11774 N  N   . LEU   J  1 40  ? 25.831  -58.667  -18.486 1.00 27.03 ? 40  LEU   J N   1 
ATOM   11775 C  CA  . LEU   J  1 40  ? 27.229  -59.095  -18.609 1.00 28.98 ? 40  LEU   J CA  1 
ATOM   11776 C  C   . LEU   J  1 40  ? 27.334  -60.308  -19.512 1.00 22.54 ? 40  LEU   J C   1 
ATOM   11777 O  O   . LEU   J  1 40  ? 28.208  -60.372  -20.388 1.00 29.95 ? 40  LEU   J O   1 
ATOM   11778 C  CB  . LEU   J  1 40  ? 27.835  -59.426  -17.234 1.00 24.53 ? 40  LEU   J CB  1 
ATOM   11779 C  CG  . LEU   J  1 40  ? 28.330  -58.198  -16.491 1.00 25.40 ? 40  LEU   J CG  1 
ATOM   11780 C  CD1 . LEU   J  1 40  ? 28.523  -58.461  -14.986 1.00 27.47 ? 40  LEU   J CD1 1 
ATOM   11781 C  CD2 . LEU   J  1 40  ? 29.620  -57.677  -17.156 1.00 32.22 ? 40  LEU   J CD2 1 
ATOM   11782 N  N   . GLY   J  1 41  ? 26.443  -61.272  -19.314 1.00 25.81 ? 41  GLY   J N   1 
ATOM   11783 C  CA  . GLY   J  1 41  ? 26.490  -62.474  -20.118 1.00 30.45 ? 41  GLY   J CA  1 
ATOM   11784 C  C   . GLY   J  1 41  ? 26.306  -62.189  -21.596 1.00 30.12 ? 41  GLY   J C   1 
ATOM   11785 O  O   . GLY   J  1 41  ? 26.987  -62.783  -22.434 1.00 28.77 ? 41  GLY   J O   1 
ATOM   11786 N  N   . ALA   J  1 42  ? 25.411  -61.251  -21.937 1.00 27.74 ? 42  ALA   J N   1 
ATOM   11787 C  CA  . ALA   J  1 42  ? 25.206  -60.923  -23.355 1.00 27.41 ? 42  ALA   J CA  1 
ATOM   11788 C  C   . ALA   J  1 42  ? 26.444  -60.235  -23.926 1.00 31.00 ? 42  ALA   J C   1 
ATOM   11789 O  O   . ALA   J  1 42  ? 26.921  -60.576  -25.016 1.00 27.32 ? 42  ALA   J O   1 
ATOM   11790 C  CB  . ALA   J  1 42  ? 23.964  -60.035  -23.540 1.00 28.00 ? 42  ALA   J CB  1 
ATOM   11791 N  N   . HIS   J  1 43  ? 26.973  -59.247  -23.210 1.00 28.33 ? 43  HIS   J N   1 
ATOM   11792 C  CA  . HIS   J  1 43  ? 28.127  -58.531  -23.725 1.00 26.40 ? 43  HIS   J CA  1 
ATOM   11793 C  C   . HIS   J  1 43  ? 29.317  -59.472  -23.859 1.00 34.20 ? 43  HIS   J C   1 
ATOM   11794 O  O   . HIS   J  1 43  ? 30.087  -59.384  -24.828 1.00 28.18 ? 43  HIS   J O   1 
ATOM   11795 C  CB  . HIS   J  1 43  ? 28.464  -57.361  -22.804 1.00 28.68 ? 43  HIS   J CB  1 
ATOM   11796 C  CG  . HIS   J  1 43  ? 29.410  -56.382  -23.401 1.00 35.42 ? 43  HIS   J CG  1 
ATOM   11797 N  ND1 . HIS   J  1 43  ? 30.778  -56.573  -23.419 1.00 36.61 ? 43  HIS   J ND1 1 
ATOM   11798 C  CD2 . HIS   J  1 43  ? 29.188  -55.186  -23.995 1.00 49.25 ? 43  HIS   J CD2 1 
ATOM   11799 C  CE1 . HIS   J  1 43  ? 31.351  -55.546  -24.027 1.00 37.59 ? 43  HIS   J CE1 1 
ATOM   11800 N  NE2 . HIS   J  1 43  ? 30.410  -54.686  -24.373 1.00 47.73 ? 43  HIS   J NE2 1 
ATOM   11801 N  N   . GLU   J  1 44  ? 29.462  -60.403  -22.911 1.00 29.15 ? 44  GLU   J N   1 
ATOM   11802 C  CA  . GLU   J  1 44  ? 30.610  -61.310  -22.940 1.00 29.42 ? 44  GLU   J CA  1 
ATOM   11803 C  C   . GLU   J  1 44  ? 30.442  -62.328  -24.051 1.00 29.74 ? 44  GLU   J C   1 
ATOM   11804 O  O   . GLU   J  1 44  ? 31.419  -62.725  -24.681 1.00 30.34 ? 44  GLU   J O   1 
ATOM   11805 C  CB  . GLU   J  1 44  ? 30.790  -62.015  -21.586 1.00 28.70 ? 44  GLU   J CB  1 
ATOM   11806 C  CG  . GLU   J  1 44  ? 32.099  -62.866  -21.472 1.00 29.54 ? 44  GLU   J CG  1 
ATOM   11807 C  CD  . GLU   J  1 44  ? 33.359  -62.046  -21.215 1.00 35.66 ? 44  GLU   J CD  1 
ATOM   11808 O  OE1 . GLU   J  1 44  ? 33.334  -60.815  -21.381 1.00 33.14 ? 44  GLU   J OE1 1 
ATOM   11809 O  OE2 . GLU   J  1 44  ? 34.389  -62.643  -20.828 1.00 33.32 ? 44  GLU   J OE2 1 
ATOM   11810 N  N   . TYR   J  1 45  ? 29.199  -62.701  -24.343 1.00 26.99 ? 45  TYR   J N   1 
ATOM   11811 C  CA  . TYR   J  1 45  ? 28.923  -63.504  -25.522 1.00 31.63 ? 45  TYR   J CA  1 
ATOM   11812 C  C   . TYR   J  1 45  ? 29.417  -62.817  -26.787 1.00 30.20 ? 45  TYR   J C   1 
ATOM   11813 O  O   . TYR   J  1 45  ? 30.063  -63.454  -27.627 1.00 27.08 ? 45  TYR   J O   1 
ATOM   11814 C  CB  . TYR   J  1 45  ? 27.429  -63.788  -25.598 1.00 29.37 ? 45  TYR   J CB  1 
ATOM   11815 C  CG  . TYR   J  1 45  ? 26.973  -64.416  -26.888 1.00 28.08 ? 45  TYR   J CG  1 
ATOM   11816 C  CD1 . TYR   J  1 45  ? 27.001  -65.791  -27.054 1.00 32.21 ? 45  TYR   J CD1 1 
ATOM   11817 C  CD2 . TYR   J  1 45  ? 26.505  -63.631  -27.936 1.00 28.19 ? 45  TYR   J CD2 1 
ATOM   11818 C  CE1 . TYR   J  1 45  ? 26.571  -66.371  -28.217 1.00 34.62 ? 45  TYR   J CE1 1 
ATOM   11819 C  CE2 . TYR   J  1 45  ? 26.065  -64.203  -29.110 1.00 31.52 ? 45  TYR   J CE2 1 
ATOM   11820 C  CZ  . TYR   J  1 45  ? 26.106  -65.569  -29.251 1.00 31.48 ? 45  TYR   J CZ  1 
ATOM   11821 O  OH  . TYR   J  1 45  ? 25.678  -66.153  -30.422 1.00 37.51 ? 45  TYR   J OH  1 
ATOM   11822 N  N   . HIS   J  1 46  ? 29.146  -61.512  -26.943 1.00 28.57 ? 46  HIS   J N   1 
ATOM   11823 C  CA  . HIS   J  1 46  ? 29.546  -60.850  -28.185 1.00 31.88 ? 46  HIS   J CA  1 
ATOM   11824 C  C   . HIS   J  1 46  ? 31.068  -60.687  -28.259 1.00 32.81 ? 46  HIS   J C   1 
ATOM   11825 O  O   . HIS   J  1 46  ? 31.642  -60.699  -29.359 1.00 26.78 ? 46  HIS   J O   1 
ATOM   11826 C  CB  . HIS   J  1 46  ? 28.836  -59.495  -28.330 1.00 34.24 ? 46  HIS   J CB  1 
ATOM   11827 C  CG  . HIS   J  1 46  ? 27.349  -59.610  -28.495 1.00 36.53 ? 46  HIS   J CG  1 
ATOM   11828 N  ND1 . HIS   J  1 46  ? 26.755  -60.258  -29.562 1.00 40.70 ? 46  HIS   J ND1 1 
ATOM   11829 C  CD2 . HIS   J  1 46  ? 26.334  -59.172  -27.713 1.00 33.59 ? 46  HIS   J CD2 1 
ATOM   11830 C  CE1 . HIS   J  1 46  ? 25.441  -60.222  -29.423 1.00 35.30 ? 46  HIS   J CE1 1 
ATOM   11831 N  NE2 . HIS   J  1 46  ? 25.163  -59.575  -28.302 1.00 38.37 ? 46  HIS   J NE2 1 
ATOM   11832 N  N   . GLU   J  1 47  ? 31.740  -60.556  -27.115 1.00 30.46 ? 47  GLU   J N   1 
ATOM   11833 C  CA  . GLU   J  1 47  ? 33.205  -60.555  -27.133 1.00 26.90 ? 47  GLU   J CA  1 
ATOM   11834 C  C   . GLU   J  1 47  ? 33.736  -61.880  -27.664 1.00 24.15 ? 47  GLU   J C   1 
ATOM   11835 O  O   . GLU   J  1 47  ? 34.686  -61.905  -28.458 1.00 32.96 ? 47  GLU   J O   1 
ATOM   11836 C  CB  . GLU   J  1 47  ? 33.754  -60.291  -25.734 1.00 28.71 ? 47  GLU   J CB  1 
ATOM   11837 C  CG  . GLU   J  1 47  ? 33.360  -58.934  -25.130 1.00 38.28 ? 47  GLU   J CG  1 
ATOM   11838 C  CD  . GLU   J  1 47  ? 34.020  -57.787  -25.846 1.00 43.28 ? 47  GLU   J CD  1 
ATOM   11839 O  OE1 . GLU   J  1 47  ? 34.755  -58.074  -26.808 1.00 50.31 ? 47  GLU   J OE1 1 
ATOM   11840 O  OE2 . GLU   J  1 47  ? 33.806  -56.610  -25.465 1.00 39.86 ? 47  GLU   J OE2 1 
ATOM   11841 N  N   . SER   J  1 48  ? 33.150  -62.988  -27.212 1.00 25.53 ? 48  SER   J N   1 
ATOM   11842 C  CA  . SER   J  1 48  ? 33.535  -64.311  -27.694 1.00 26.42 ? 48  SER   J CA  1 
ATOM   11843 C  C   . SER   J  1 48  ? 33.324  -64.426  -29.198 1.00 31.66 ? 48  SER   J C   1 
ATOM   11844 O  O   . SER   J  1 48  ? 34.210  -64.900  -29.918 1.00 29.79 ? 48  SER   J O   1 
ATOM   11845 C  CB  . SER   J  1 48  ? 32.744  -65.368  -26.922 1.00 30.16 ? 48  SER   J CB  1 
ATOM   11846 O  OG  . SER   J  1 48  ? 33.086  -66.713  -27.259 1.00 29.46 ? 48  SER   J OG  1 
ATOM   11847 N  N   . ILE   J  1 49  ? 32.191  -63.926  -29.705 1.00 26.13 ? 49  ILE   J N   1 
ATOM   11848 C  CA  . ILE   J  1 49  ? 31.922  -63.987  -31.138 1.00 24.34 ? 49  ILE   J CA  1 
ATOM   11849 C  C   . ILE   J  1 49  ? 32.939  -63.166  -31.887 1.00 28.94 ? 49  ILE   J C   1 
ATOM   11850 O  O   . ILE   J  1 49  ? 33.435  -63.578  -32.952 1.00 31.25 ? 49  ILE   J O   1 
ATOM   11851 C  CB  . ILE   J  1 49  ? 30.484  -63.504  -31.447 1.00 26.71 ? 49  ILE   J CB  1 
ATOM   11852 C  CG1 . ILE   J  1 49  ? 29.439  -64.379  -30.756 1.00 30.91 ? 49  ILE   J CG1 1 
ATOM   11853 C  CG2 . ILE   J  1 49  ? 30.227  -63.424  -32.956 1.00 28.81 ? 49  ILE   J CG2 1 
ATOM   11854 C  CD1 . ILE   J  1 49  ? 29.268  -65.732  -31.323 1.00 30.82 ? 49  ILE   J CD1 1 
ATOM   11855 N  N   . ASP   J  1 50  ? 33.276  -61.991  -31.351 1.00 24.48 ? 50  ASP   J N   1 
ATOM   11856 C  CA  . ASP   J  1 50  ? 34.287  -61.166  -31.978 1.00 32.45 ? 50  ASP   J CA  1 
ATOM   11857 C  C   . ASP   J  1 50  ? 35.584  -61.941  -32.137 1.00 36.13 ? 50  ASP   J C   1 
ATOM   11858 O  O   . ASP   J  1 50  ? 36.235  -61.842  -33.177 1.00 25.39 ? 50  ASP   J O   1 
ATOM   11859 C  CB  . ASP   J  1 50  ? 34.558  -59.909  -31.149 1.00 33.22 ? 50  ASP   J CB  1 
ATOM   11860 C  CG  . ASP   J  1 50  ? 33.694  -58.730  -31.545 1.00 59.13 ? 50  ASP   J CG  1 
ATOM   11861 O  OD1 . ASP   J  1 50  ? 32.868  -58.866  -32.476 1.00 67.45 ? 50  ASP   J OD1 1 
ATOM   11862 O  OD2 . ASP   J  1 50  ? 33.845  -57.657  -30.909 1.00 70.68 ? 50  ASP   J OD2 1 
ATOM   11863 N  N   . GLU   J  1 51  ? 35.985  -62.700  -31.101 1.00 33.26 ? 51  GLU   J N   1 
ATOM   11864 C  CA  . GLU   J  1 51  ? 37.255  -63.429  -31.173 1.00 30.05 ? 51  GLU   J CA  1 
ATOM   11865 C  C   . GLU   J  1 51  ? 37.138  -64.604  -32.119 1.00 26.22 ? 51  GLU   J C   1 
ATOM   11866 O  O   . GLU   J  1 51  ? 38.107  -64.948  -32.813 1.00 30.23 ? 51  GLU   J O   1 
ATOM   11867 C  CB  . GLU   J  1 51  ? 37.687  -63.908  -29.776 1.00 27.88 ? 51  GLU   J CB  1 
ATOM   11868 C  CG  . GLU   J  1 51  ? 37.917  -62.772  -28.788 1.00 29.56 ? 51  GLU   J CG  1 
ATOM   11869 C  CD  . GLU   J  1 51  ? 39.024  -61.817  -29.241 1.00 36.39 ? 51  GLU   J CD  1 
ATOM   11870 O  OE1 . GLU   J  1 51  ? 40.190  -62.230  -29.261 1.00 57.22 ? 51  GLU   J OE1 1 
ATOM   11871 O  OE2 . GLU   J  1 51  ? 38.743  -60.652  -29.577 1.00 47.81 ? 51  GLU   J OE2 1 
ATOM   11872 N  N   . MET   J  1 52  ? 35.944  -65.190  -32.207 1.00 27.56 ? 52  MET   J N   1 
ATOM   11873 C  CA  . MET   J  1 52  ? 35.704  -66.222  -33.196 1.00 30.35 ? 52  MET   J CA  1 
ATOM   11874 C  C   . MET   J  1 52  ? 35.920  -65.693  -34.607 1.00 33.49 ? 52  MET   J C   1 
ATOM   11875 O  O   . MET   J  1 52  ? 36.519  -66.378  -35.450 1.00 28.29 ? 52  MET   J O   1 
ATOM   11876 C  CB  . MET   J  1 52  ? 34.298  -66.761  -33.042 1.00 28.45 ? 52  MET   J CB  1 
ATOM   11877 C  CG  . MET   J  1 52  ? 34.081  -67.579  -31.827 1.00 32.71 ? 52  MET   J CG  1 
ATOM   11878 S  SD  . MET   J  1 52  ? 32.345  -68.015  -31.719 1.00 29.18 ? 52  MET   J SD  1 
ATOM   11879 C  CE  . MET   J  1 52  ? 32.186  -68.168  -29.930 1.00 28.54 ? 52  MET   J CE  1 
ATOM   11880 N  N   . LYS   J  1 53  ? 35.483  -64.454  -34.872 1.00 26.92 ? 53  LYS   J N   1 
ATOM   11881 C  CA  . LYS   J  1 53  ? 35.652  -63.894  -36.216 1.00 32.41 ? 53  LYS   J CA  1 
ATOM   11882 C  C   . LYS   J  1 53  ? 37.111  -63.579  -36.503 1.00 33.78 ? 53  LYS   J C   1 
ATOM   11883 O  O   . LYS   J  1 53  ? 37.570  -63.757  -37.639 1.00 27.31 ? 53  LYS   J O   1 
ATOM   11884 C  CB  . LYS   J  1 53  ? 34.797  -62.637  -36.392 1.00 33.41 ? 53  LYS   J CB  1 
ATOM   11885 C  CG  . LYS   J  1 53  ? 33.277  -62.879  -36.447 1.00 37.67 ? 53  LYS   J CG  1 
ATOM   11886 C  CD  . LYS   J  1 53  ? 32.528  -61.579  -36.145 1.00 37.30 ? 53  LYS   J CD  1 
ATOM   11887 C  CE  . LYS   J  1 53  ? 31.099  -61.580  -36.668 1.00 54.90 ? 53  LYS   J CE  1 
ATOM   11888 N  NZ  . LYS   J  1 53  ? 30.324  -60.374  -36.195 1.00 58.18 ? 53  LYS   J NZ  1 
ATOM   11889 N  N   . HIS   J  1 54  ? 37.850  -63.078  -35.499 1.00 29.11 ? 54  HIS   J N   1 
ATOM   11890 C  CA  . HIS   J  1 54  ? 39.286  -62.853  -35.674 1.00 33.50 ? 54  HIS   J CA  1 
ATOM   11891 C  C   . HIS   J  1 54  ? 40.004  -64.156  -35.989 1.00 32.09 ? 54  HIS   J C   1 
ATOM   11892 O  O   . HIS   J  1 54  ? 40.887  -64.208  -36.861 1.00 33.74 ? 54  HIS   J O   1 
ATOM   11893 C  CB  . HIS   J  1 54  ? 39.918  -62.258  -34.417 1.00 29.32 ? 54  HIS   J CB  1 
ATOM   11894 C  CG  . HIS   J  1 54  ? 39.340  -60.948  -33.980 1.00 36.19 ? 54  HIS   J CG  1 
ATOM   11895 N  ND1 . HIS   J  1 54  ? 38.794  -60.035  -34.856 1.00 31.86 ? 54  HIS   J ND1 1 
ATOM   11896 C  CD2 . HIS   J  1 54  ? 39.231  -60.398  -32.744 1.00 32.20 ? 54  HIS   J CD2 1 
ATOM   11897 C  CE1 . HIS   J  1 54  ? 38.389  -58.970  -34.179 1.00 38.23 ? 54  HIS   J CE1 1 
ATOM   11898 N  NE2 . HIS   J  1 54  ? 38.636  -59.169  -32.896 1.00 38.49 ? 54  HIS   J NE2 1 
ATOM   11899 N  N   . ALA   J  1 55  ? 39.693  -65.199  -35.227 1.00 26.25 ? 55  ALA   J N   1 
ATOM   11900 C  CA  . ALA   J  1 55  ? 40.253  -66.514  -35.470 1.00 33.11 ? 55  ALA   J CA  1 
ATOM   11901 C  C   . ALA   J  1 55  ? 40.019  -66.940  -36.908 1.00 37.21 ? 55  ALA   J C   1 
ATOM   11902 O  O   . ALA   J  1 55  ? 40.932  -67.424  -37.586 1.00 28.48 ? 55  ALA   J O   1 
ATOM   11903 C  CB  . ALA   J  1 55  ? 39.621  -67.521  -34.518 1.00 30.84 ? 55  ALA   J CB  1 
ATOM   11904 N  N   . ASP   J  1 56  ? 38.783  -66.772  -37.384 1.00 30.94 ? 56  ASP   J N   1 
ATOM   11905 C  CA  . ASP   J  1 56  ? 38.459  -67.105  -38.765 1.00 27.73 ? 56  ASP   J CA  1 
ATOM   11906 C  C   . ASP   J  1 56  ? 39.411  -66.393  -39.725 1.00 28.58 ? 56  ASP   J C   1 
ATOM   11907 O  O   . ASP   J  1 56  ? 40.049  -67.024  -40.573 1.00 27.53 ? 56  ASP   J O   1 
ATOM   11908 C  CB  . ASP   J  1 56  ? 36.989  -66.746  -39.031 1.00 27.97 ? 56  ASP   J CB  1 
ATOM   11909 C  CG  . ASP   J  1 56  ? 36.519  -67.131  -40.405 1.00 31.61 ? 56  ASP   J CG  1 
ATOM   11910 O  OD1 . ASP   J  1 56  ? 37.170  -67.970  -41.063 1.00 34.12 ? 56  ASP   J OD1 1 
ATOM   11911 O  OD2 . ASP   J  1 56  ? 35.466  -66.597  -40.816 1.00 29.92 ? 56  ASP   J OD2 1 
ATOM   11912 N  N   . LYS   J  1 57  ? 39.575  -65.082  -39.560 1.00 25.47 ? 57  LYS   J N   1 
ATOM   11913 C  CA  . LYS   J  1 57  ? 40.398  -64.343  -40.498 1.00 28.06 ? 57  LYS   J CA  1 
ATOM   11914 C  C   . LYS   J  1 57  ? 41.849  -64.820  -40.447 1.00 30.17 ? 57  LYS   J C   1 
ATOM   11915 O  O   . LYS   J  1 57  ? 42.513  -64.889  -41.481 1.00 29.74 ? 57  LYS   J O   1 
ATOM   11916 C  CB  . LYS   J  1 57  ? 40.327  -62.837  -40.230 1.00 34.56 ? 57  LYS   J CB  1 
ATOM   11917 C  CG  . LYS   J  1 57  ? 38.961  -62.192  -40.541 1.00 33.49 ? 57  LYS   J CG  1 
ATOM   11918 C  CD  . LYS   J  1 57  ? 38.612  -62.334  -42.002 1.00 45.67 ? 57  LYS   J CD  1 
ATOM   11919 N  N   . LEU   J  1 58  ? 42.360  -65.129  -39.252 1.00 29.95 ? 58  LEU   J N   1 
ATOM   11920 C  CA  . LEU   J  1 58  ? 43.725  -65.654  -39.126 1.00 28.14 ? 58  LEU   J CA  1 
ATOM   11921 C  C   . LEU   J  1 58  ? 43.877  -66.999  -39.820 1.00 27.07 ? 58  LEU   J C   1 
ATOM   11922 O  O   . LEU   J  1 58  ? 44.850  -67.227  -40.543 1.00 31.96 ? 58  LEU   J O   1 
ATOM   11923 C  CB  . LEU   J  1 58  ? 44.093  -65.792  -37.658 1.00 24.97 ? 58  LEU   J CB  1 
ATOM   11924 C  CG  . LEU   J  1 58  ? 44.222  -64.459  -36.944 1.00 32.55 ? 58  LEU   J CG  1 
ATOM   11925 C  CD1 . LEU   J  1 58  ? 44.254  -64.664  -35.442 1.00 32.54 ? 58  LEU   J CD1 1 
ATOM   11926 C  CD2 . LEU   J  1 58  ? 45.433  -63.718  -37.405 1.00 32.30 ? 58  LEU   J CD2 1 
ATOM   11927 N  N   . ILE   J  1 59  ? 42.937  -67.911  -39.576 1.00 26.05 ? 59  ILE   J N   1 
ATOM   11928 C  CA  . ILE   J  1 59  ? 42.935  -69.208  -40.240 1.00 29.73 ? 59  ILE   J CA  1 
ATOM   11929 C  C   . ILE   J  1 59  ? 42.974  -69.021  -41.749 1.00 35.11 ? 59  ILE   J C   1 
ATOM   11930 O  O   . ILE   J  1 59  ? 43.801  -69.618  -42.452 1.00 30.53 ? 59  ILE   J O   1 
ATOM   11931 C  CB  . ILE   J  1 59  ? 41.715  -70.030  -39.790 1.00 28.75 ? 59  ILE   J CB  1 
ATOM   11932 C  CG1 . ILE   J  1 59  ? 41.816  -70.340  -38.286 1.00 28.13 ? 59  ILE   J CG1 1 
ATOM   11933 C  CG2 . ILE   J  1 59  ? 41.584  -71.320  -40.596 1.00 30.56 ? 59  ILE   J CG2 1 
ATOM   11934 C  CD1 . ILE   J  1 59  ? 40.666  -71.102  -37.731 1.00 29.01 ? 59  ILE   J CD1 1 
ATOM   11935 N  N   . GLU   J  1 60  ? 42.113  -68.149  -42.271 1.00 33.21 ? 60  GLU   J N   1 
ATOM   11936 C  CA  . GLU   J  1 60  ? 42.074  -67.963  -43.716 1.00 32.63 ? 60  GLU   J CA  1 
ATOM   11937 C  C   . GLU   J  1 60  ? 43.397  -67.416  -44.220 1.00 29.81 ? 60  GLU   J C   1 
ATOM   11938 O  O   . GLU   J  1 60  ? 43.889  -67.846  -45.263 1.00 31.57 ? 60  GLU   J O   1 
ATOM   11939 C  CB  . GLU   J  1 60  ? 40.912  -67.042  -44.106 1.00 32.86 ? 60  GLU   J CB  1 
ATOM   11940 C  CG  . GLU   J  1 60  ? 39.560  -67.686  -43.795 1.00 31.30 ? 60  GLU   J CG  1 
ATOM   11941 C  CD  . GLU   J  1 60  ? 38.366  -66.717  -43.954 1.00 39.55 ? 60  GLU   J CD  1 
ATOM   11942 O  OE1 . GLU   J  1 60  ? 38.533  -65.508  -43.711 1.00 36.12 ? 60  GLU   J OE1 1 
ATOM   11943 O  OE2 . GLU   J  1 60  ? 37.274  -67.180  -44.316 1.00 31.07 ? 60  GLU   J OE2 1 
ATOM   11944 N  N   . ARG   J  1 61  ? 43.988  -66.468  -43.489 1.00 31.76 ? 61  ARG   J N   1 
ATOM   11945 C  CA  . ARG   J  1 61  ? 45.242  -65.866  -43.924 1.00 30.88 ? 61  ARG   J CA  1 
ATOM   11946 C  C   . ARG   J  1 61  ? 46.374  -66.891  -43.893 1.00 32.74 ? 61  ARG   J C   1 
ATOM   11947 O  O   . ARG   J  1 61  ? 47.200  -66.955  -44.819 1.00 29.53 ? 61  ARG   J O   1 
ATOM   11948 C  CB  . ARG   J  1 61  ? 45.575  -64.666  -43.041 1.00 32.20 ? 61  ARG   J CB  1 
ATOM   11949 C  CG  . ARG   J  1 61  ? 46.869  -63.935  -43.404 1.00 31.06 ? 61  ARG   J CG  1 
ATOM   11950 C  CD  . ARG   J  1 61  ? 46.712  -63.199  -44.725 1.00 36.26 ? 61  ARG   J CD  1 
ATOM   11951 N  NE  . ARG   J  1 61  ? 47.956  -62.556  -45.126 1.00 35.95 ? 61  ARG   J NE  1 
ATOM   11952 C  CZ  . ARG   J  1 61  ? 48.196  -62.062  -46.333 1.00 36.85 ? 61  ARG   J CZ  1 
ATOM   11953 N  NH1 . ARG   J  1 61  ? 47.273  -62.081  -47.277 1.00 27.84 ? 61  ARG   J NH1 1 
ATOM   11954 N  NH2 . ARG   J  1 61  ? 49.396  -61.544  -46.600 1.00 28.70 ? 61  ARG   J NH2 1 
ATOM   11955 N  N   . ILE   J  1 62  ? 46.395  -67.732  -42.861 1.00 39.29 ? 62  ILE   J N   1 
ATOM   11956 C  CA  . ILE   J  1 62  ? 47.442  -68.745  -42.745 1.00 34.60 ? 62  ILE   J CA  1 
ATOM   11957 C  C   . ILE   J  1 62  ? 47.361  -69.740  -43.906 1.00 37.74 ? 62  ILE   J C   1 
ATOM   11958 O  O   . ILE   J  1 62  ? 48.386  -70.097  -44.506 1.00 33.97 ? 62  ILE   J O   1 
ATOM   11959 C  CB  . ILE   J  1 62  ? 47.340  -69.439  -41.376 1.00 29.91 ? 62  ILE   J CB  1 
ATOM   11960 C  CG1 . ILE   J  1 62  ? 47.791  -68.482  -40.275 1.00 26.86 ? 62  ILE   J CG1 1 
ATOM   11961 C  CG2 . ILE   J  1 62  ? 48.198  -70.721  -41.366 1.00 38.36 ? 62  ILE   J CG2 1 
ATOM   11962 C  CD1 . ILE   J  1 62  ? 47.443  -68.948  -38.871 1.00 31.60 ? 62  ILE   J CD1 1 
ATOM   11963 N  N   . LEU   J  1 63  ? 46.146  -70.194  -44.248 1.00 28.98 ? 63  LEU   J N   1 
ATOM   11964 C  CA  . LEU   J  1 63  ? 45.980  -71.123  -45.367 1.00 34.89 ? 63  LEU   J CA  1 
ATOM   11965 C  C   . LEU   J  1 63  ? 46.403  -70.486  -46.682 1.00 35.86 ? 63  LEU   J C   1 
ATOM   11966 O  O   . LEU   J  1 63  ? 47.032  -71.142  -47.517 1.00 38.09 ? 63  LEU   J O   1 
ATOM   11967 C  CB  . LEU   J  1 63  ? 44.532  -71.602  -45.468 1.00 31.67 ? 63  LEU   J CB  1 
ATOM   11968 C  CG  . LEU   J  1 63  ? 44.119  -72.481  -44.301 1.00 36.27 ? 63  LEU   J CG  1 
ATOM   11969 C  CD1 . LEU   J  1 63  ? 42.641  -72.696  -44.314 1.00 29.45 ? 63  LEU   J CD1 1 
ATOM   11970 C  CD2 . LEU   J  1 63  ? 44.847  -73.827  -44.341 1.00 36.89 ? 63  LEU   J CD2 1 
ATOM   11971 N  N   . PHE   J  1 64  ? 46.076  -69.210  -46.883 1.00 33.55 ? 64  PHE   J N   1 
ATOM   11972 C  CA  . PHE   J  1 64  ? 46.496  -68.543  -48.103 1.00 33.12 ? 64  PHE   J CA  1 
ATOM   11973 C  C   . PHE   J  1 64  ? 48.013  -68.500  -48.213 1.00 41.30 ? 64  PHE   J C   1 
ATOM   11974 O  O   . PHE   J  1 64  ? 48.565  -68.599  -49.322 1.00 33.41 ? 64  PHE   J O   1 
ATOM   11975 C  CB  . PHE   J  1 64  ? 45.942  -67.125  -48.172 1.00 31.88 ? 64  PHE   J CB  1 
ATOM   11976 C  CG  . PHE   J  1 64  ? 46.547  -66.303  -49.275 1.00 28.29 ? 64  PHE   J CG  1 
ATOM   11977 C  CD1 . PHE   J  1 64  ? 46.393  -66.680  -50.594 1.00 31.25 ? 64  PHE   J CD1 1 
ATOM   11978 C  CD2 . PHE   J  1 64  ? 47.259  -65.171  -48.999 1.00 28.59 ? 64  PHE   J CD2 1 
ATOM   11979 C  CE1 . PHE   J  1 64  ? 46.941  -65.931  -51.607 1.00 33.16 ? 64  PHE   J CE1 1 
ATOM   11980 C  CE2 . PHE   J  1 64  ? 47.812  -64.427  -50.009 1.00 36.08 ? 64  PHE   J CE2 1 
ATOM   11981 C  CZ  . PHE   J  1 64  ? 47.634  -64.805  -51.319 1.00 29.80 ? 64  PHE   J CZ  1 
ATOM   11982 N  N   . LEU   J  1 65  ? 48.702  -68.299  -47.085 1.00 33.15 ? 65  LEU   J N   1 
ATOM   11983 C  CA  . LEU   J  1 65  ? 50.165  -68.241  -47.060 1.00 37.26 ? 65  LEU   J CA  1 
ATOM   11984 C  C   . LEU   J  1 65  ? 50.808  -69.622  -47.016 1.00 34.25 ? 65  LEU   J C   1 
ATOM   11985 O  O   . LEU   J  1 65  ? 52.033  -69.711  -46.862 1.00 35.31 ? 65  LEU   J O   1 
ATOM   11986 C  CB  . LEU   J  1 65  ? 50.645  -67.407  -45.867 1.00 38.96 ? 65  LEU   J CB  1 
ATOM   11987 C  CG  . LEU   J  1 65  ? 50.309  -65.913  -45.883 1.00 37.74 ? 65  LEU   J CG  1 
ATOM   11988 C  CD1 . LEU   J  1 65  ? 50.752  -65.222  -44.598 1.00 34.36 ? 65  LEU   J CD1 1 
ATOM   11989 C  CD2 . LEU   J  1 65  ? 50.903  -65.242  -47.124 1.00 37.43 ? 65  LEU   J CD2 1 
ATOM   11990 N  N   . GLU   J  1 66  ? 49.998  -70.673  -47.136 1.00 30.21 ? 66  GLU   J N   1 
ATOM   11991 C  CA  . GLU   J  1 66  ? 50.431  -72.058  -47.301 1.00 37.55 ? 66  GLU   J CA  1 
ATOM   11992 C  C   . GLU   J  1 66  ? 50.988  -72.644  -46.011 1.00 44.72 ? 66  GLU   J C   1 
ATOM   11993 O  O   . GLU   J  1 66  ? 51.786  -73.576  -46.047 1.00 36.66 ? 66  GLU   J O   1 
ATOM   11994 C  CB  . GLU   J  1 66  ? 51.436  -72.177  -48.461 1.00 36.40 ? 66  GLU   J CB  1 
ATOM   11995 C  CG  . GLU   J  1 66  ? 50.783  -71.577  -49.729 1.00 37.97 ? 66  GLU   J CG  1 
ATOM   11996 C  CD  . GLU   J  1 66  ? 51.512  -71.862  -51.035 1.00 49.41 ? 66  GLU   J CD  1 
ATOM   11997 O  OE1 . GLU   J  1 66  ? 51.811  -73.042  -51.320 1.00 43.22 ? 66  GLU   J OE1 1 
ATOM   11998 O  OE2 . GLU   J  1 66  ? 51.762  -70.891  -51.780 1.00 53.78 ? 66  GLU   J OE2 1 
ATOM   11999 N  N   . GLY   J  1 67  ? 50.531  -72.127  -44.867 1.00 36.58 ? 67  GLY   J N   1 
ATOM   12000 C  CA  . GLY   J  1 67  ? 50.856  -72.683  -43.573 1.00 34.34 ? 67  GLY   J CA  1 
ATOM   12001 C  C   . GLY   J  1 67  ? 49.730  -73.522  -43.015 1.00 36.46 ? 67  GLY   J C   1 
ATOM   12002 O  O   . GLY   J  1 67  ? 48.631  -73.585  -43.561 1.00 37.33 ? 67  GLY   J O   1 
ATOM   12003 N  N   . LEU   J  1 68  ? 50.024  -74.185  -41.888 1.00 32.61 ? 68  LEU   J N   1 
ATOM   12004 C  CA  . LEU   J  1 68  ? 49.042  -75.032  -41.226 1.00 34.16 ? 68  LEU   J CA  1 
ATOM   12005 C  C   . LEU   J  1 68  ? 48.486  -74.285  -40.023 1.00 41.67 ? 68  LEU   J C   1 
ATOM   12006 O  O   . LEU   J  1 68  ? 49.227  -74.061  -39.054 1.00 36.35 ? 68  LEU   J O   1 
ATOM   12007 C  CB  . LEU   J  1 68  ? 49.657  -76.357  -40.773 1.00 44.18 ? 68  LEU   J CB  1 
ATOM   12008 C  CG  . LEU   J  1 68  ? 50.161  -77.317  -41.856 1.00 60.60 ? 68  LEU   J CG  1 
ATOM   12009 C  CD1 . LEU   J  1 68  ? 50.761  -78.555  -41.203 1.00 62.35 ? 68  LEU   J CD1 1 
ATOM   12010 C  CD2 . LEU   J  1 68  ? 49.039  -77.706  -42.816 1.00 54.52 ? 68  LEU   J CD2 1 
ATOM   12011 N  N   . PRO   J  1 69  ? 47.219  -73.879  -40.026 1.00 37.49 ? 69  PRO   J N   1 
ATOM   12012 C  CA  . PRO   J  1 69  ? 46.658  -73.236  -38.827 1.00 32.59 ? 69  PRO   J CA  1 
ATOM   12013 C  C   . PRO   J  1 69  ? 46.603  -74.206  -37.655 1.00 32.14 ? 69  PRO   J C   1 
ATOM   12014 O  O   . PRO   J  1 69  ? 46.081  -75.317  -37.774 1.00 33.10 ? 69  PRO   J O   1 
ATOM   12015 C  CB  . PRO   J  1 69  ? 45.247  -72.817  -39.269 1.00 30.30 ? 69  PRO   J CB  1 
ATOM   12016 C  CG  . PRO   J  1 69  ? 45.299  -72.770  -40.765 1.00 32.74 ? 69  PRO   J CG  1 
ATOM   12017 C  CD  . PRO   J  1 69  ? 46.286  -73.842  -41.165 1.00 39.64 ? 69  PRO   J CD  1 
ATOM   12018 N  N   . ASN   J  1 70  ? 47.100  -73.751  -36.504 1.00 36.89 ? 70  ASN   J N   1 
ATOM   12019 C  CA  . ASN   J  1 70  ? 47.155  -74.554  -35.274 1.00 39.91 ? 70  ASN   J CA  1 
ATOM   12020 C  C   . ASN   J  1 70  ? 45.889  -74.313  -34.446 1.00 30.41 ? 70  ASN   J C   1 
ATOM   12021 O  O   . ASN   J  1 70  ? 45.767  -73.302  -33.760 1.00 33.66 ? 70  ASN   J O   1 
ATOM   12022 C  CB  . ASN   J  1 70  ? 48.412  -74.203  -34.484 1.00 36.12 ? 70  ASN   J CB  1 
ATOM   12023 C  CG  . ASN   J  1 70  ? 48.662  -75.145  -33.308 1.00 39.90 ? 70  ASN   J CG  1 
ATOM   12024 O  OD1 . ASN   J  1 70  ? 47.831  -75.973  -32.973 1.00 36.83 ? 70  ASN   J OD1 1 
ATOM   12025 N  ND2 . ASN   J  1 70  ? 49.839  -75.021  -32.690 1.00 37.26 ? 70  ASN   J ND2 1 
ATOM   12026 N  N   . LEU   J  1 71  ? 44.945  -75.243  -34.532 1.00 26.87 ? 71  LEU   J N   1 
ATOM   12027 C  CA  . LEU   J  1 71  ? 43.733  -75.263  -33.732 1.00 39.05 ? 71  LEU   J CA  1 
ATOM   12028 C  C   . LEU   J  1 71  ? 43.752  -76.396  -32.720 1.00 41.04 ? 71  LEU   J C   1 
ATOM   12029 O  O   . LEU   J  1 71  ? 42.705  -76.727  -32.141 1.00 31.47 ? 71  LEU   J O   1 
ATOM   12030 C  CB  . LEU   J  1 71  ? 42.507  -75.420  -34.627 1.00 37.51 ? 71  LEU   J CB  1 
ATOM   12031 C  CG  . LEU   J  1 71  ? 41.976  -74.233  -35.438 1.00 37.15 ? 71  LEU   J CG  1 
ATOM   12032 C  CD1 . LEU   J  1 71  ? 42.751  -74.024  -36.721 1.00 38.70 ? 71  LEU   J CD1 1 
ATOM   12033 C  CD2 . LEU   J  1 71  ? 40.511  -74.481  -35.785 1.00 36.30 ? 71  LEU   J CD2 1 
ATOM   12034 N  N   . GLN   J  1 72  ? 44.922  -76.997  -32.500 1.00 37.24 ? 72  GLN   J N   1 
ATOM   12035 C  CA  . GLN   J  1 72  ? 45.063  -78.186  -31.674 1.00 43.63 ? 72  GLN   J CA  1 
ATOM   12036 C  C   . GLN   J  1 72  ? 45.560  -77.864  -30.276 1.00 33.10 ? 72  GLN   J C   1 
ATOM   12037 O  O   . GLN   J  1 72  ? 45.157  -78.526  -29.312 1.00 37.09 ? 72  GLN   J O   1 
ATOM   12038 C  CB  . GLN   J  1 72  ? 46.038  -79.166  -32.350 1.00 47.57 ? 72  GLN   J CB  1 
ATOM   12039 C  CG  . GLN   J  1 72  ? 46.315  -80.482  -31.613 1.00 36.93 ? 72  GLN   J CG  1 
ATOM   12040 C  CD  . GLN   J  1 72  ? 45.100  -81.323  -31.410 1.00 30.88 ? 72  GLN   J CD  1 
ATOM   12041 O  OE1 . GLN   J  1 72  ? 44.808  -82.220  -32.196 1.00 35.40 ? 72  GLN   J OE1 1 
ATOM   12042 N  NE2 . GLN   J  1 72  ? 44.353  -81.035  -30.335 1.00 44.16 ? 72  GLN   J NE2 1 
ATOM   12043 N  N   . ASP   J  1 73  ? 46.426  -76.870  -30.158 1.00 30.67 ? 73  ASP   J N   1 
ATOM   12044 C  CA  . ASP   J  1 73  ? 47.085  -76.541  -28.909 1.00 42.27 ? 73  ASP   J CA  1 
ATOM   12045 C  C   . ASP   J  1 73  ? 46.325  -75.404  -28.249 1.00 40.83 ? 73  ASP   J C   1 
ATOM   12046 O  O   . ASP   J  1 73  ? 46.183  -74.318  -28.825 1.00 47.46 ? 73  ASP   J O   1 
ATOM   12047 C  CB  . ASP   J  1 73  ? 48.543  -76.157  -29.128 1.00 39.91 ? 73  ASP   J CB  1 
ATOM   12048 C  CG  . ASP   J  1 73  ? 49.351  -77.280  -29.751 1.00 43.28 ? 73  ASP   J CG  1 
ATOM   12049 O  OD1 . ASP   J  1 73  ? 49.014  -78.463  -29.528 1.00 47.30 ? 73  ASP   J OD1 1 
ATOM   12050 O  OD2 . ASP   J  1 73  ? 50.301  -76.973  -30.481 1.00 43.39 ? 73  ASP   J OD2 1 
ATOM   12051 N  N   . LEU   J  1 74  ? 45.829  -75.667  -27.054 1.00 39.06 ? 74  LEU   J N   1 
ATOM   12052 C  CA  . LEU   J  1 74  ? 45.036  -74.705  -26.306 1.00 41.62 ? 74  LEU   J CA  1 
ATOM   12053 C  C   . LEU   J  1 74  ? 45.806  -74.340  -25.051 1.00 35.30 ? 74  LEU   J C   1 
ATOM   12054 O  O   . LEU   J  1 74  ? 46.023  -75.199  -24.197 1.00 37.58 ? 74  LEU   J O   1 
ATOM   12055 C  CB  . LEU   J  1 74  ? 43.671  -75.304  -25.960 1.00 35.58 ? 74  LEU   J CB  1 
ATOM   12056 C  CG  . LEU   J  1 74  ? 42.638  -74.417  -25.251 1.00 38.12 ? 74  LEU   J CG  1 
ATOM   12057 C  CD1 . LEU   J  1 74  ? 42.315  -73.157  -26.069 1.00 41.04 ? 74  LEU   J CD1 1 
ATOM   12058 C  CD2 . LEU   J  1 74  ? 41.384  -75.235  -25.051 1.00 31.92 ? 74  LEU   J CD2 1 
ATOM   12059 N  N   . GLY   J  1 75  ? 46.210  -73.077  -24.944 1.00 31.49 ? 75  GLY   J N   1 
ATOM   12060 C  CA  . GLY   J  1 75  ? 46.788  -72.556  -23.728 1.00 39.39 ? 75  GLY   J CA  1 
ATOM   12061 C  C   . GLY   J  1 75  ? 45.803  -72.502  -22.567 1.00 31.76 ? 75  GLY   J C   1 
ATOM   12062 O  O   . GLY   J  1 75  ? 44.636  -72.886  -22.653 1.00 33.76 ? 75  GLY   J O   1 
ATOM   12063 N  N   . LYS   J  1 76  ? 46.308  -72.011  -21.444 1.00 31.55 ? 76  LYS   J N   1 
ATOM   12064 C  CA  . LYS   J  1 76  ? 45.571  -72.061  -20.191 1.00 36.83 ? 76  LYS   J CA  1 
ATOM   12065 C  C   . LYS   J  1 76  ? 44.476  -70.990  -20.157 1.00 30.06 ? 76  LYS   J C   1 
ATOM   12066 O  O   . LYS   J  1 76  ? 44.750  -69.800  -20.336 1.00 28.20 ? 76  LYS   J O   1 
ATOM   12067 C  CB  . LYS   J  1 76  ? 46.546  -71.878  -19.029 1.00 38.98 ? 76  LYS   J CB  1 
ATOM   12068 C  CG  . LYS   J  1 76  ? 45.899  -71.966  -17.639 1.00 38.71 ? 76  LYS   J CG  1 
ATOM   12069 N  N   . LEU   J  1 77  ? 43.244  -71.406  -19.902 1.00 32.41 ? 77  LEU   J N   1 
ATOM   12070 C  CA  . LEU   J  1 77  ? 42.184  -70.434  -19.685 1.00 37.72 ? 77  LEU   J CA  1 
ATOM   12071 C  C   . LEU   J  1 77  ? 42.328  -69.788  -18.309 1.00 36.41 ? 77  LEU   J C   1 
ATOM   12072 O  O   . LEU   J  1 77  ? 42.652  -70.462  -17.328 1.00 34.67 ? 77  LEU   J O   1 
ATOM   12073 C  CB  . LEU   J  1 77  ? 40.813  -71.105  -19.789 1.00 31.36 ? 77  LEU   J CB  1 
ATOM   12074 C  CG  . LEU   J  1 77  ? 40.580  -72.052  -20.945 1.00 36.98 ? 77  LEU   J CG  1 
ATOM   12075 C  CD1 . LEU   J  1 77  ? 39.099  -72.466  -20.976 1.00 38.30 ? 77  LEU   J CD1 1 
ATOM   12076 C  CD2 . LEU   J  1 77  ? 41.016  -71.398  -22.237 1.00 33.86 ? 77  LEU   J CD2 1 
ATOM   12077 N  N   . LEU   J  1 78  ? 42.110  -68.466  -18.249 1.00 34.16 ? 78  LEU   J N   1 
ATOM   12078 C  CA  . LEU   J  1 78  ? 42.024  -67.710  -16.999 1.00 33.57 ? 78  LEU   J CA  1 
ATOM   12079 C  C   . LEU   J  1 78  ? 40.545  -67.483  -16.659 1.00 33.44 ? 78  LEU   J C   1 
ATOM   12080 O  O   . LEU   J  1 78  ? 39.918  -66.562  -17.185 1.00 31.97 ? 78  LEU   J O   1 
ATOM   12081 C  CB  . LEU   J  1 78  ? 42.778  -66.391  -17.140 1.00 28.48 ? 78  LEU   J CB  1 
ATOM   12082 C  CG  . LEU   J  1 78  ? 44.208  -66.600  -17.655 1.00 39.06 ? 78  LEU   J CG  1 
ATOM   12083 C  CD1 . LEU   J  1 78  ? 44.864  -65.289  -18.024 1.00 38.89 ? 78  LEU   J CD1 1 
ATOM   12084 C  CD2 . LEU   J  1 78  ? 45.034  -67.314  -16.607 1.00 38.31 ? 78  LEU   J CD2 1 
ATOM   12085 N  N   . ILE   J  1 79  ? 40.007  -68.315  -15.766 1.00 29.07 ? 79  ILE   J N   1 
ATOM   12086 C  CA  . ILE   J  1 79  ? 38.608  -68.297  -15.351 1.00 29.27 ? 79  ILE   J CA  1 
ATOM   12087 C  C   . ILE   J  1 79  ? 38.487  -67.701  -13.943 1.00 40.10 ? 79  ILE   J C   1 
ATOM   12088 O  O   . ILE   J  1 79  ? 38.987  -68.270  -12.960 1.00 34.54 ? 79  ILE   J O   1 
ATOM   12089 C  CB  . ILE   J  1 79  ? 38.003  -69.703  -15.381 1.00 29.94 ? 79  ILE   J CB  1 
ATOM   12090 C  CG1 . ILE   J  1 79  ? 38.297  -70.405  -16.714 1.00 33.09 ? 79  ILE   J CG1 1 
ATOM   12091 C  CG2 . ILE   J  1 79  ? 36.487  -69.626  -15.105 1.00 31.87 ? 79  ILE   J CG2 1 
ATOM   12092 C  CD1 . ILE   J  1 79  ? 37.851  -69.581  -17.920 1.00 30.17 ? 79  ILE   J CD1 1 
ATOM   12093 N  N   . GLY   J  1 80  ? 37.763  -66.601  -13.822 1.00 35.79 ? 80  GLY   J N   1 
ATOM   12094 C  CA  . GLY   J  1 80  ? 37.475  -66.064  -12.491 1.00 34.64 ? 80  GLY   J CA  1 
ATOM   12095 C  C   . GLY   J  1 80  ? 36.432  -66.869  -11.719 1.00 35.29 ? 80  GLY   J C   1 
ATOM   12096 O  O   . GLY   J  1 80  ? 35.698  -67.699  -12.264 1.00 35.54 ? 80  GLY   J O   1 
ATOM   12097 N  N   . GLU   J  1 81  ? 36.357  -66.597  -10.399 1.00 30.94 ? 81  GLU   J N   1 
ATOM   12098 C  CA  . GLU   J  1 81  ? 35.348  -67.186  -9.525  1.00 29.81 ? 81  GLU   J CA  1 
ATOM   12099 C  C   . GLU   J  1 81  ? 34.302  -66.172  -9.084  1.00 25.92 ? 81  GLU   J C   1 
ATOM   12100 O  O   . GLU   J  1 81  ? 33.330  -66.556  -8.434  1.00 34.36 ? 81  GLU   J O   1 
ATOM   12101 C  CB  . GLU   J  1 81  ? 36.007  -67.823  -8.278  1.00 38.01 ? 81  GLU   J CB  1 
ATOM   12102 C  CG  . GLU   J  1 81  ? 37.011  -68.931  -8.642  1.00 43.79 ? 81  GLU   J CG  1 
ATOM   12103 C  CD  . GLU   J  1 81  ? 37.721  -69.575  -7.443  1.00 50.57 ? 81  GLU   J CD  1 
ATOM   12104 O  OE1 . GLU   J  1 81  ? 37.792  -68.968  -6.350  1.00 34.06 ? 81  GLU   J OE1 1 
ATOM   12105 O  OE2 . GLU   J  1 81  ? 38.221  -70.705  -7.606  1.00 61.35 ? 81  GLU   J OE2 1 
ATOM   12106 N  N   . ASN   J  1 82  ? 34.479  -64.900  -9.423  1.00 26.61 ? 82  ASN   J N   1 
ATOM   12107 C  CA  . ASN   J  1 82  ? 33.463  -63.871  -9.239  1.00 35.48 ? 82  ASN   J CA  1 
ATOM   12108 C  C   . ASN   J  1 82  ? 33.631  -62.844  -10.358 1.00 31.49 ? 82  ASN   J C   1 
ATOM   12109 O  O   . ASN   J  1 82  ? 34.583  -62.907  -11.148 1.00 29.06 ? 82  ASN   J O   1 
ATOM   12110 C  CB  . ASN   J  1 82  ? 33.533  -63.229  -7.835  1.00 25.29 ? 82  ASN   J CB  1 
ATOM   12111 C  CG  . ASN   J  1 82  ? 34.860  -62.539  -7.546  1.00 22.20 ? 82  ASN   J CG  1 
ATOM   12112 O  OD1 . ASN   J  1 82  ? 35.526  -62.023  -8.429  1.00 26.87 ? 82  ASN   J OD1 1 
ATOM   12113 N  ND2 . ASN   J  1 82  ? 35.211  -62.484  -6.273  1.00 29.77 ? 82  ASN   J ND2 1 
ATOM   12114 N  N   . THR   J  1 83  ? 32.689  -61.891  -10.418 1.00 31.31 ? 83  THR   J N   1 
ATOM   12115 C  CA  . THR   J  1 83  ? 32.658  -60.935  -11.528 1.00 31.18 ? 83  THR   J CA  1 
ATOM   12116 C  C   . THR   J  1 83  ? 33.962  -60.159  -11.625 1.00 31.19 ? 83  THR   J C   1 
ATOM   12117 O  O   . THR   J  1 83  ? 34.526  -59.994  -12.713 1.00 26.04 ? 83  THR   J O   1 
ATOM   12118 C  CB  . THR   J  1 83  ? 31.455  -59.984  -11.367 1.00 23.51 ? 83  THR   J CB  1 
ATOM   12119 O  OG1 . THR   J  1 83  ? 30.240  -60.725  -11.571 1.00 28.92 ? 83  THR   J OG1 1 
ATOM   12120 C  CG2 . THR   J  1 83  ? 31.477  -58.823  -12.346 1.00 23.17 ? 83  THR   J CG2 1 
ATOM   12121 N  N   . GLN   J  1 84  ? 34.466  -59.667  -10.503 1.00 26.33 ? 84  GLN   J N   1 
ATOM   12122 C  CA  . GLN   J  1 84  ? 35.672  -58.857  -10.582 1.00 30.14 ? 84  GLN   J CA  1 
ATOM   12123 C  C   . GLN   J  1 84  ? 36.848  -59.672  -11.120 1.00 33.03 ? 84  GLN   J C   1 
ATOM   12124 O  O   . GLN   J  1 84  ? 37.650  -59.174  -11.922 1.00 30.98 ? 84  GLN   J O   1 
ATOM   12125 C  CB  . GLN   J  1 84  ? 36.013  -58.286  -9.217  1.00 38.05 ? 84  GLN   J CB  1 
ATOM   12126 C  CG  . GLN   J  1 84  ? 37.189  -57.363  -9.266  1.00 50.00 ? 84  GLN   J CG  1 
ATOM   12127 C  CD  . GLN   J  1 84  ? 37.041  -56.257  -8.280  1.00 46.05 ? 84  GLN   J CD  1 
ATOM   12128 O  OE1 . GLN   J  1 84  ? 36.628  -55.152  -8.617  1.00 48.91 ? 84  GLN   J OE1 1 
ATOM   12129 N  NE2 . GLN   J  1 84  ? 37.348  -56.557  -7.027  1.00 72.97 ? 84  GLN   J NE2 1 
ATOM   12130 N  N   . GLU   J  1 85  ? 36.987  -60.912  -10.654 1.00 28.79 ? 85  GLU   J N   1 
ATOM   12131 C  CA  . GLU   J  1 85  ? 38.065  -61.773  -11.142 1.00 32.82 ? 85  GLU   J CA  1 
ATOM   12132 C  C   . GLU   J  1 85  ? 37.904  -62.093  -12.621 1.00 32.07 ? 85  GLU   J C   1 
ATOM   12133 O  O   . GLU   J  1 85  ? 38.894  -62.181  -13.360 1.00 30.88 ? 85  GLU   J O   1 
ATOM   12134 C  CB  . GLU   J  1 85  ? 38.095  -63.070  -10.355 1.00 26.99 ? 85  GLU   J CB  1 
ATOM   12135 C  CG  . GLU   J  1 85  ? 38.700  -62.917  -8.969  1.00 32.54 ? 85  GLU   J CG  1 
ATOM   12136 C  CD  . GLU   J  1 85  ? 38.818  -64.244  -8.214  1.00 39.71 ? 85  GLU   J CD  1 
ATOM   12137 O  OE1 . GLU   J  1 85  ? 38.494  -65.305  -8.808  1.00 31.40 ? 85  GLU   J OE1 1 
ATOM   12138 O  OE2 . GLU   J  1 85  ? 39.248  -64.218  -7.027  1.00 35.80 ? 85  GLU   J OE2 1 
ATOM   12139 N  N   . MET   J  1 86  ? 36.669  -62.342  -13.056 1.00 28.81 ? 86  MET   J N   1 
ATOM   12140 C  CA  . MET   J  1 86  ? 36.458  -62.711  -14.455 1.00 30.54 ? 86  MET   J CA  1 
ATOM   12141 C  C   . MET   J  1 86  ? 36.906  -61.580  -15.367 1.00 31.57 ? 86  MET   J C   1 
ATOM   12142 O  O   . MET   J  1 86  ? 37.593  -61.813  -16.375 1.00 26.74 ? 86  MET   J O   1 
ATOM   12143 C  CB  . MET   J  1 86  ? 34.993  -63.066  -14.675 1.00 29.88 ? 86  MET   J CB  1 
ATOM   12144 C  CG  . MET   J  1 86  ? 34.574  -64.341  -13.951 1.00 31.78 ? 86  MET   J CG  1 
ATOM   12145 S  SD  . MET   J  1 86  ? 32.811  -64.379  -13.491 1.00 29.19 ? 86  MET   J SD  1 
ATOM   12146 C  CE  . MET   J  1 86  ? 32.056  -64.685  -15.111 1.00 30.50 ? 86  MET   J CE  1 
ATOM   12147 N  N   . LEU   J  1 87  ? 36.551  -60.341  -14.995 1.00 31.56 ? 87  LEU   J N   1 
ATOM   12148 C  CA  . LEU   J  1 87  ? 36.943  -59.159  -15.754 1.00 26.47 ? 87  LEU   J CA  1 
ATOM   12149 C  C   . LEU   J  1 87  ? 38.449  -58.948  -15.720 1.00 31.09 ? 87  LEU   J C   1 
ATOM   12150 O  O   . LEU   J  1 87  ? 39.046  -58.501  -16.709 1.00 25.20 ? 87  LEU   J O   1 
ATOM   12151 C  CB  . LEU   J  1 87  ? 36.237  -57.924  -15.197 1.00 28.54 ? 87  LEU   J CB  1 
ATOM   12152 C  CG  . LEU   J  1 87  ? 34.702  -57.831  -15.405 1.00 31.13 ? 87  LEU   J CG  1 
ATOM   12153 C  CD1 . LEU   J  1 87  ? 34.104  -56.762  -14.499 1.00 30.30 ? 87  LEU   J CD1 1 
ATOM   12154 C  CD2 . LEU   J  1 87  ? 34.343  -57.527  -16.849 1.00 26.07 ? 87  LEU   J CD2 1 
ATOM   12155 N  N   . GLN   J  1 88  ? 39.067  -59.186  -14.570 1.00 30.07 ? 88  GLN   J N   1 
ATOM   12156 C  CA  . GLN   J  1 88  ? 40.508  -59.048  -14.498 1.00 29.93 ? 88  GLN   J CA  1 
ATOM   12157 C  C   . GLN   J  1 88  ? 41.194  -60.128  -15.328 1.00 26.63 ? 88  GLN   J C   1 
ATOM   12158 O  O   . GLN   J  1 88  ? 42.222  -59.865  -15.957 1.00 29.71 ? 88  GLN   J O   1 
ATOM   12159 C  CB  . GLN   J  1 88  ? 40.973  -59.079  -13.027 1.00 30.59 ? 88  GLN   J CB  1 
ATOM   12160 C  CG  . GLN   J  1 88  ? 42.435  -58.682  -12.821 1.00 53.47 ? 88  GLN   J CG  1 
ATOM   12161 C  CD  . GLN   J  1 88  ? 42.750  -57.271  -13.301 1.00 60.49 ? 88  GLN   J CD  1 
ATOM   12162 O  OE1 . GLN   J  1 88  ? 42.098  -56.314  -12.882 1.00 64.83 ? 88  GLN   J OE1 1 
ATOM   12163 N  NE2 . GLN   J  1 88  ? 43.755  -57.136  -14.183 1.00 42.13 ? 88  GLN   J NE2 1 
ATOM   12164 N  N   . CYS   J  1 89  ? 40.641  -61.343  -15.344 1.00 24.07 ? 89  CYS   J N   1 
ATOM   12165 C  CA  . CYS   J  1 89  ? 41.234  -62.409  -16.145 1.00 30.89 ? 89  CYS   J CA  1 
ATOM   12166 C  C   . CYS   J  1 89  ? 41.127  -62.107  -17.631 1.00 31.51 ? 89  CYS   J C   1 
ATOM   12167 O  O   . CYS   J  1 89  ? 42.050  -62.414  -18.394 1.00 28.75 ? 89  CYS   J O   1 
ATOM   12168 C  CB  . CYS   J  1 89  ? 40.566  -63.751  -15.852 1.00 26.56 ? 89  CYS   J CB  1 
ATOM   12169 S  SG  . CYS   J  1 89  ? 40.992  -64.559  -14.258 1.00 31.91 ? 89  CYS   J SG  1 
ATOM   12170 N  N   . ASP   J  1 90  ? 39.998  -61.527  -18.063 1.00 27.64 ? 90  ASP   J N   1 
ATOM   12171 C  CA  . ASP   J  1 90  ? 39.880  -61.073  -19.450 1.00 30.99 ? 90  ASP   J CA  1 
ATOM   12172 C  C   . ASP   J  1 90  ? 40.924  -60.001  -19.759 1.00 29.59 ? 90  ASP   J C   1 
ATOM   12173 O  O   . ASP   J  1 90  ? 41.606  -60.053  -20.800 1.00 30.58 ? 90  ASP   J O   1 
ATOM   12174 C  CB  . ASP   J  1 90  ? 38.461  -60.524  -19.719 1.00 31.45 ? 90  ASP   J CB  1 
ATOM   12175 C  CG  . ASP   J  1 90  ? 37.375  -61.606  -19.775 1.00 31.37 ? 90  ASP   J CG  1 
ATOM   12176 O  OD1 . ASP   J  1 90  ? 37.653  -62.817  -19.631 1.00 29.43 ? 90  ASP   J OD1 1 
ATOM   12177 O  OD2 . ASP   J  1 90  ? 36.184  -61.235  -19.982 1.00 33.31 ? 90  ASP   J OD2 1 
ATOM   12178 N  N   . LEU   J  1 91  ? 41.101  -59.042  -18.843 1.00 23.46 ? 91  LEU   J N   1 
ATOM   12179 C  CA  . LEU   J  1 91  ? 42.021  -57.950  -19.114 1.00 27.18 ? 91  LEU   J CA  1 
ATOM   12180 C  C   . LEU   J  1 91  ? 43.465  -58.447  -19.165 1.00 33.88 ? 91  LEU   J C   1 
ATOM   12181 O  O   . LEU   J  1 91  ? 44.244  -58.027  -20.029 1.00 25.50 ? 91  LEU   J O   1 
ATOM   12182 C  CB  . LEU   J  1 91  ? 41.873  -56.869  -18.064 1.00 28.87 ? 91  LEU   J CB  1 
ATOM   12183 C  CG  . LEU   J  1 91  ? 42.796  -55.676  -18.194 1.00 30.05 ? 91  LEU   J CG  1 
ATOM   12184 C  CD1 . LEU   J  1 91  ? 42.674  -55.041  -19.530 1.00 34.94 ? 91  LEU   J CD1 1 
ATOM   12185 C  CD2 . LEU   J  1 91  ? 42.485  -54.692  -17.079 1.00 38.33 ? 91  LEU   J CD2 1 
ATOM   12186 N  N   . ASN   J  1 92  ? 43.837  -59.336  -18.247 1.00 31.23 ? 92  ASN   J N   1 
ATOM   12187 C  CA  . ASN   J  1 92  ? 45.188  -59.901  -18.295 1.00 38.01 ? 92  ASN   J CA  1 
ATOM   12188 C  C   . ASN   J  1 92  ? 45.415  -60.661  -19.599 1.00 31.46 ? 92  ASN   J C   1 
ATOM   12189 O  O   . ASN   J  1 92  ? 46.452  -60.490  -20.245 1.00 29.34 ? 92  ASN   J O   1 
ATOM   12190 C  CB  . ASN   J  1 92  ? 45.424  -60.794  -17.071 1.00 35.40 ? 92  ASN   J CB  1 
ATOM   12191 C  CG  . ASN   J  1 92  ? 45.443  -59.998  -15.762 1.00 40.26 ? 92  ASN   J CG  1 
ATOM   12192 O  OD1 . ASN   J  1 92  ? 45.703  -58.795  -15.755 1.00 38.54 ? 92  ASN   J OD1 1 
ATOM   12193 N  ND2 . ASN   J  1 92  ? 45.150  -60.670  -14.654 1.00 36.01 ? 92  ASN   J ND2 1 
ATOM   12194 N  N   . LEU   J  1 93  ? 44.431  -61.454  -20.042 1.00 32.08 ? 93  LEU   J N   1 
ATOM   12195 C  CA  . LEU   J  1 93  ? 44.575  -62.135  -21.329 1.00 39.44 ? 93  LEU   J CA  1 
ATOM   12196 C  C   . LEU   J  1 93  ? 44.688  -61.137  -22.488 1.00 39.61 ? 93  LEU   J C   1 
ATOM   12197 O  O   . LEU   J  1 93  ? 45.506  -61.325  -23.394 1.00 30.19 ? 93  LEU   J O   1 
ATOM   12198 C  CB  . LEU   J  1 93  ? 43.418  -63.113  -21.559 1.00 31.52 ? 93  LEU   J CB  1 
ATOM   12199 C  CG  . LEU   J  1 93  ? 43.365  -63.851  -22.914 1.00 32.90 ? 93  LEU   J CG  1 
ATOM   12200 C  CD1 . LEU   J  1 93  ? 44.574  -64.777  -23.141 1.00 37.52 ? 93  LEU   J CD1 1 
ATOM   12201 C  CD2 . LEU   J  1 93  ? 42.045  -64.652  -23.087 1.00 32.79 ? 93  LEU   J CD2 1 
ATOM   12202 N  N   . GLU   J  1 94  ? 43.907  -60.052  -22.462 1.00 32.05 ? 94  GLU   J N   1 
ATOM   12203 C  CA  . GLU   J  1 94  ? 43.992  -59.057  -23.534 1.00 31.39 ? 94  GLU   J CA  1 
ATOM   12204 C  C   . GLU   J  1 94  ? 45.362  -58.386  -23.578 1.00 36.91 ? 94  GLU   J C   1 
ATOM   12205 O  O   . GLU   J  1 94  ? 45.861  -58.044  -24.657 1.00 34.86 ? 94  GLU   J O   1 
ATOM   12206 C  CB  . GLU   J  1 94  ? 42.908  -58.000  -23.356 1.00 32.27 ? 94  GLU   J CB  1 
ATOM   12207 C  CG  . GLU   J  1 94  ? 41.483  -58.530  -23.591 1.00 30.40 ? 94  GLU   J CG  1 
ATOM   12208 C  CD  . GLU   J  1 94  ? 41.152  -58.713  -25.078 1.00 38.23 ? 94  GLU   J CD  1 
ATOM   12209 O  OE1 . GLU   J  1 94  ? 41.923  -58.250  -25.916 1.00 35.55 ? 94  GLU   J OE1 1 
ATOM   12210 O  OE2 . GLU   J  1 94  ? 40.128  -59.338  -25.404 1.00 45.39 ? 94  GLU   J OE2 1 
ATOM   12211 N  N   . LEU   J  1 95  ? 45.975  -58.156  -22.415 1.00 32.88 ? 95  LEU   J N   1 
ATOM   12212 C  CA  . LEU   J  1 95  ? 47.236  -57.418  -22.402 1.00 28.65 ? 95  LEU   J CA  1 
ATOM   12213 C  C   . LEU   J  1 95  ? 48.369  -58.258  -22.968 1.00 30.95 ? 95  LEU   J C   1 
ATOM   12214 O  O   . LEU   J  1 95  ? 49.269  -57.731  -23.638 1.00 35.41 ? 95  LEU   J O   1 
ATOM   12215 C  CB  . LEU   J  1 95  ? 47.549  -56.960  -20.984 1.00 33.82 ? 95  LEU   J CB  1 
ATOM   12216 C  CG  . LEU   J  1 95  ? 46.644  -55.805  -20.521 1.00 35.38 ? 95  LEU   J CG  1 
ATOM   12217 C  CD1 . LEU   J  1 95  ? 46.725  -55.599  -19.013 1.00 38.69 ? 95  LEU   J CD1 1 
ATOM   12218 C  CD2 . LEU   J  1 95  ? 47.017  -54.508  -21.229 1.00 40.06 ? 95  LEU   J CD2 1 
ATOM   12219 N  N   . LYS   J  1 96  ? 48.317  -59.564  -22.733 1.00 32.15 ? 96  LYS   J N   1 
ATOM   12220 C  CA  . LYS   J  1 96  ? 49.237  -60.485  -23.380 1.00 34.34 ? 96  LYS   J CA  1 
ATOM   12221 C  C   . LYS   J  1 96  ? 48.924  -60.635  -24.866 1.00 39.45 ? 96  LYS   J C   1 
ATOM   12222 O  O   . LYS   J  1 96  ? 49.845  -60.807  -25.672 1.00 31.88 ? 96  LYS   J O   1 
ATOM   12223 C  CB  . LYS   J  1 96  ? 49.172  -61.819  -22.633 1.00 37.31 ? 96  LYS   J CB  1 
ATOM   12224 C  CG  . LYS   J  1 96  ? 49.230  -63.083  -23.442 1.00 41.46 ? 96  LYS   J CG  1 
ATOM   12225 C  CD  . LYS   J  1 96  ? 50.590  -63.391  -23.970 1.00 52.82 ? 96  LYS   J CD  1 
ATOM   12226 C  CE  . LYS   J  1 96  ? 50.751  -64.906  -24.092 1.00 54.59 ? 96  LYS   J CE  1 
ATOM   12227 N  NZ  . LYS   J  1 96  ? 51.760  -65.268  -25.110 1.00 56.24 ? 96  LYS   J NZ  1 
ATOM   12228 N  N   . ALA   J  1 97  ? 47.636  -60.584  -25.260 1.00 34.71 ? 97  ALA   J N   1 
ATOM   12229 C  CA  . ALA   J  1 97  ? 47.306  -60.652  -26.691 1.00 28.89 ? 97  ALA   J CA  1 
ATOM   12230 C  C   . ALA   J  1 97  ? 47.850  -59.446  -27.436 1.00 31.20 ? 97  ALA   J C   1 
ATOM   12231 O  O   . ALA   J  1 97  ? 48.354  -59.565  -28.558 1.00 32.40 ? 97  ALA   J O   1 
ATOM   12232 C  CB  . ALA   J  1 97  ? 45.789  -60.747  -26.900 1.00 27.17 ? 97  ALA   J CB  1 
ATOM   12233 N  N   . THR   J  1 98  ? 47.717  -58.265  -26.854 1.00 26.12 ? 98  THR   J N   1 
ATOM   12234 C  CA  . THR   J  1 98  ? 48.131  -57.104  -27.587 1.00 29.06 ? 98  THR   J CA  1 
ATOM   12235 C  C   . THR   J  1 98  ? 49.651  -57.029  -27.636 1.00 36.22 ? 98  THR   J C   1 
ATOM   12236 O  O   . THR   J  1 98  ? 50.201  -56.596  -28.646 1.00 29.16 ? 98  THR   J O   1 
ATOM   12237 C  CB  . THR   J  1 98  ? 47.523  -55.842  -26.986 1.00 31.50 ? 98  THR   J CB  1 
ATOM   12238 O  OG1 . THR   J  1 98  ? 47.885  -55.740  -25.611 1.00 31.69 ? 98  THR   J OG1 1 
ATOM   12239 C  CG2 . THR   J  1 98  ? 45.993  -55.885  -27.129 1.00 28.62 ? 98  THR   J CG2 1 
ATOM   12240 N  N   . LYS   J  1 99  ? 50.336  -57.457  -26.572 1.00 32.62 ? 99  LYS   J N   1 
ATOM   12241 C  CA  . LYS   J  1 99  ? 51.790  -57.621  -26.647 1.00 30.56 ? 99  LYS   J CA  1 
ATOM   12242 C  C   . LYS   J  1 99  ? 52.170  -58.498  -27.829 1.00 22.73 ? 99  LYS   J C   1 
ATOM   12243 O  O   . LYS   J  1 99  ? 53.020  -58.132  -28.647 1.00 30.94 ? 99  LYS   J O   1 
ATOM   12244 C  CB  . LYS   J  1 99  ? 52.316  -58.234  -25.339 1.00 31.54 ? 99  LYS   J CB  1 
ATOM   12245 C  CG  . LYS   J  1 99  ? 53.787  -58.621  -25.352 1.00 36.46 ? 99  LYS   J CG  1 
ATOM   12246 C  CD  . LYS   J  1 99  ? 54.195  -59.238  -24.006 1.00 37.34 ? 99  LYS   J CD  1 
ATOM   12247 N  N   . ASP   J  1 100 ? 51.574  -59.685  -27.911 1.00 30.32 ? 100 ASP   J N   1 
ATOM   12248 C  CA  . ASP   J  1 100 ? 51.902  -60.596  -28.994 1.00 28.14 ? 100 ASP   J CA  1 
ATOM   12249 C  C   . ASP   J  1 100 ? 51.565  -59.983  -30.350 1.00 38.86 ? 100 ASP   J C   1 
ATOM   12250 O  O   . ASP   J  1 100 ? 52.321  -60.146  -31.322 1.00 32.60 ? 100 ASP   J O   1 
ATOM   12251 C  CB  . ASP   J  1 100 ? 51.184  -61.930  -28.800 1.00 30.99 ? 100 ASP   J CB  1 
ATOM   12252 C  CG  . ASP   J  1 100 ? 51.729  -62.732  -27.603 1.00 38.18 ? 100 ASP   J CG  1 
ATOM   12253 O  OD1 . ASP   J  1 100 ? 52.726  -62.292  -27.013 1.00 41.08 ? 100 ASP   J OD1 1 
ATOM   12254 O  OD2 . ASP   J  1 100 ? 51.174  -63.797  -27.266 1.00 33.52 ? 100 ASP   J OD2 1 
ATOM   12255 N  N   . LEU   J  1 101 ? 50.449  -59.251  -30.433 1.00 35.32 ? 101 LEU   J N   1 
ATOM   12256 C  CA  . LEU   J  1 101 ? 50.090  -58.613  -31.698 1.00 31.30 ? 101 LEU   J CA  1 
ATOM   12257 C  C   . LEU   J  1 101 ? 51.141  -57.597  -32.112 1.00 29.99 ? 101 LEU   J C   1 
ATOM   12258 O  O   . LEU   J  1 101 ? 51.527  -57.534  -33.288 1.00 30.20 ? 101 LEU   J O   1 
ATOM   12259 C  CB  . LEU   J  1 101 ? 48.691  -57.960  -31.590 1.00 33.86 ? 101 LEU   J CB  1 
ATOM   12260 C  CG  . LEU   J  1 101 ? 47.479  -58.899  -31.701 1.00 33.74 ? 101 LEU   J CG  1 
ATOM   12261 C  CD1 . LEU   J  1 101 ? 46.173  -58.255  -31.174 1.00 30.01 ? 101 LEU   J CD1 1 
ATOM   12262 C  CD2 . LEU   J  1 101 ? 47.250  -59.314  -33.134 1.00 32.65 ? 101 LEU   J CD2 1 
ATOM   12263 N  N   . ARG   J  1 102 ? 51.639  -56.797  -31.160 1.00 27.59 ? 102 ARG   J N   1 
ATOM   12264 C  CA  . ARG   J  1 102 ? 52.655  -55.808  -31.507 1.00 33.06 ? 102 ARG   J CA  1 
ATOM   12265 C  C   . ARG   J  1 102 ? 53.908  -56.487  -32.052 1.00 36.41 ? 102 ARG   J C   1 
ATOM   12266 O  O   . ARG   J  1 102 ? 54.486  -56.029  -33.050 1.00 30.69 ? 102 ARG   J O   1 
ATOM   12267 C  CB  . ARG   J  1 102 ? 53.005  -54.944  -30.297 1.00 34.56 ? 102 ARG   J CB  1 
ATOM   12268 C  CG  . ARG   J  1 102 ? 51.878  -54.011  -29.877 1.00 28.93 ? 102 ARG   J CG  1 
ATOM   12269 C  CD  . ARG   J  1 102 ? 52.115  -53.278  -28.575 1.00 32.27 ? 102 ARG   J CD  1 
ATOM   12270 N  NE  . ARG   J  1 102 ? 50.839  -53.067  -27.870 1.00 32.25 ? 102 ARG   J NE  1 
ATOM   12271 C  CZ  . ARG   J  1 102 ? 49.903  -52.203  -28.268 1.00 37.45 ? 102 ARG   J CZ  1 
ATOM   12272 N  NH1 . ARG   J  1 102 ? 50.102  -51.395  -29.295 1.00 30.77 ? 102 ARG   J NH1 1 
ATOM   12273 N  NH2 . ARG   J  1 102 ? 48.733  -52.156  -27.626 1.00 30.44 ? 102 ARG   J NH2 1 
ATOM   12274 N  N   . GLU   J  1 103 ? 54.328  -57.595  -31.431 1.00 34.97 ? 103 GLU   J N   1 
ATOM   12275 C  CA  . GLU   J  1 103 ? 55.541  -58.267  -31.894 1.00 40.88 ? 103 GLU   J CA  1 
ATOM   12276 C  C   . GLU   J  1 103 ? 55.339  -58.885  -33.272 1.00 32.99 ? 103 GLU   J C   1 
ATOM   12277 O  O   . GLU   J  1 103 ? 56.281  -58.948  -34.066 1.00 32.14 ? 103 GLU   J O   1 
ATOM   12278 C  CB  . GLU   J  1 103 ? 55.971  -59.332  -30.889 1.00 33.37 ? 103 GLU   J CB  1 
ATOM   12279 C  CG  . GLU   J  1 103 ? 56.236  -58.765  -29.477 1.00 39.70 ? 103 GLU   J CG  1 
ATOM   12280 N  N   . ALA   J  1 104 ? 54.129  -59.349  -33.571 1.00 27.33 ? 104 ALA   J N   1 
ATOM   12281 C  CA  . ALA   J  1 104 ? 53.856  -59.905  -34.881 1.00 29.90 ? 104 ALA   J CA  1 
ATOM   12282 C  C   . ALA   J  1 104 ? 53.916  -58.824  -35.953 1.00 33.98 ? 104 ALA   J C   1 
ATOM   12283 O  O   . ALA   J  1 104 ? 54.519  -59.025  -37.010 1.00 33.65 ? 104 ALA   J O   1 
ATOM   12284 C  CB  . ALA   J  1 104 ? 52.503  -60.614  -34.882 1.00 32.12 ? 104 ALA   J CB  1 
ATOM   12285 N  N   . ILE   J  1 105 ? 53.348  -57.650  -35.679 1.00 34.57 ? 105 ILE   J N   1 
ATOM   12286 C  CA  . ILE   J  1 105 ? 53.385  -56.547  -36.642 1.00 34.14 ? 105 ILE   J CA  1 
ATOM   12287 C  C   . ILE   J  1 105 ? 54.825  -56.131  -36.935 1.00 36.92 ? 105 ILE   J C   1 
ATOM   12288 O  O   . ILE   J  1 105 ? 55.191  -55.872  -38.085 1.00 32.08 ? 105 ILE   J O   1 
ATOM   12289 C  CB  . ILE   J  1 105 ? 52.532  -55.371  -36.118 1.00 29.17 ? 105 ILE   J CB  1 
ATOM   12290 C  CG1 . ILE   J  1 105 ? 51.063  -55.794  -36.167 1.00 26.00 ? 105 ILE   J CG1 1 
ATOM   12291 C  CG2 . ILE   J  1 105 ? 52.736  -54.121  -36.936 1.00 28.07 ? 105 ILE   J CG2 1 
ATOM   12292 C  CD1 . ILE   J  1 105 ? 50.079  -55.001  -35.226 1.00 32.70 ? 105 ILE   J CD1 1 
ATOM   12293 N  N   . VAL   J  1 106 ? 55.653  -56.015  -35.897 1.00 34.20 ? 106 VAL   J N   1 
ATOM   12294 C  CA  . VAL   J  1 106 ? 57.064  -55.712  -36.110 1.00 34.84 ? 106 VAL   J CA  1 
ATOM   12295 C  C   . VAL   J  1 106 ? 57.632  -56.624  -37.183 1.00 29.84 ? 106 VAL   J C   1 
ATOM   12296 O  O   . VAL   J  1 106 ? 58.246  -56.174  -38.150 1.00 32.89 ? 106 VAL   J O   1 
ATOM   12297 C  CB  . VAL   J  1 106 ? 57.857  -55.850  -34.797 1.00 31.88 ? 106 VAL   J CB  1 
ATOM   12298 C  CG1 . VAL   J  1 106 ? 59.394  -55.905  -35.109 1.00 31.05 ? 106 VAL   J CG1 1 
ATOM   12299 C  CG2 . VAL   J  1 106 ? 57.556  -54.702  -33.906 1.00 32.27 ? 106 VAL   J CG2 1 
ATOM   12300 N  N   . HIS   J  1 107 ? 57.425  -57.923  -37.032 1.00 32.04 ? 107 HIS   J N   1 
ATOM   12301 C  CA  . HIS   J  1 107 ? 58.036  -58.843  -37.969 1.00 33.44 ? 107 HIS   J CA  1 
ATOM   12302 C  C   . HIS   J  1 107 ? 57.405  -58.730  -39.356 1.00 35.98 ? 107 HIS   J C   1 
ATOM   12303 O  O   . HIS   J  1 107 ? 58.124  -58.657  -40.361 1.00 30.15 ? 107 HIS   J O   1 
ATOM   12304 C  CB  . HIS   J  1 107 ? 57.951  -60.282  -37.469 1.00 31.42 ? 107 HIS   J CB  1 
ATOM   12305 C  CG  . HIS   J  1 107 ? 58.785  -61.201  -38.293 1.00 47.61 ? 107 HIS   J CG  1 
ATOM   12306 N  ND1 . HIS   J  1 107 ? 60.163  -61.121  -38.306 1.00 47.51 ? 107 HIS   J ND1 1 
ATOM   12307 C  CD2 . HIS   J  1 107 ? 58.451  -62.138  -39.210 1.00 48.80 ? 107 HIS   J CD2 1 
ATOM   12308 C  CE1 . HIS   J  1 107 ? 60.643  -62.017  -39.147 1.00 50.36 ? 107 HIS   J CE1 1 
ATOM   12309 N  NE2 . HIS   J  1 107 ? 59.627  -62.643  -39.714 1.00 48.89 ? 107 HIS   J NE2 1 
ATOM   12310 N  N   . CYS   J  1 108 ? 56.061  -58.721  -39.432 1.00 26.89 ? 108 CYS   J N   1 
ATOM   12311 C  CA  . CYS   J  1 108 ? 55.387  -58.488  -40.712 1.00 26.82 ? 108 CYS   J CA  1 
ATOM   12312 C  C   . CYS   J  1 108 ? 55.951  -57.269  -41.408 1.00 25.40 ? 108 CYS   J C   1 
ATOM   12313 O  O   . CYS   J  1 108 ? 56.204  -57.292  -42.624 1.00 35.56 ? 108 CYS   J O   1 
ATOM   12314 C  CB  . CYS   J  1 108 ? 53.860  -58.337  -40.498 1.00 25.58 ? 108 CYS   J CB  1 
ATOM   12315 S  SG  . CYS   J  1 108 ? 53.071  -59.828  -40.021 1.00 31.67 ? 108 CYS   J SG  1 
ATOM   12316 N  N   . GLU   J  1 109 ? 56.158  -56.186  -40.663 1.00 24.63 ? 109 GLU   J N   1 
ATOM   12317 C  CA  . GLU   J  1 109 ? 56.720  -54.997  -41.280 1.00 27.37 ? 109 GLU   J CA  1 
ATOM   12318 C  C   . GLU   J  1 109 ? 58.122  -55.296  -41.818 1.00 39.50 ? 109 GLU   J C   1 
ATOM   12319 O  O   . GLU   J  1 109 ? 58.463  -54.891  -42.933 1.00 31.62 ? 109 GLU   J O   1 
ATOM   12320 C  CB  . GLU   J  1 109 ? 56.766  -53.847  -40.286 1.00 26.61 ? 109 GLU   J CB  1 
ATOM   12321 C  CG  . GLU   J  1 109 ? 57.330  -52.544  -40.846 1.00 30.80 ? 109 GLU   J CG  1 
ATOM   12322 C  CD  . GLU   J  1 109 ? 56.395  -51.829  -41.851 1.00 32.40 ? 109 GLU   J CD  1 
ATOM   12323 O  OE1 . GLU   J  1 109 ? 55.204  -52.176  -41.924 1.00 31.59 ? 109 GLU   J OE1 1 
ATOM   12324 O  OE2 . GLU   J  1 109 ? 56.851  -50.876  -42.532 1.00 32.93 ? 109 GLU   J OE2 1 
ATOM   12325 N  N   . GLN   J  1 110 ? 58.925  -56.057  -41.056 1.00 36.39 ? 110 GLN   J N   1 
ATOM   12326 C  CA  . GLN   J  1 110 ? 60.323  -56.277  -41.444 1.00 35.80 ? 110 GLN   J CA  1 
ATOM   12327 C  C   . GLN   J  1 110 ? 60.415  -57.085  -42.724 1.00 32.39 ? 110 GLN   J C   1 
ATOM   12328 O  O   . GLN   J  1 110 ? 61.278  -56.813  -43.561 1.00 36.94 ? 110 GLN   J O   1 
ATOM   12329 C  CB  . GLN   J  1 110 ? 61.100  -56.975  -40.313 1.00 37.97 ? 110 GLN   J CB  1 
ATOM   12330 C  CG  . GLN   J  1 110 ? 61.724  -55.975  -39.314 1.00 53.26 ? 110 GLN   J CG  1 
ATOM   12331 C  CD  . GLN   J  1 110 ? 62.236  -56.614  -38.020 1.00 56.50 ? 110 GLN   J CD  1 
ATOM   12332 O  OE1 . GLN   J  1 110 ? 62.385  -57.842  -37.910 1.00 53.01 ? 110 GLN   J OE1 1 
ATOM   12333 N  NE2 . GLN   J  1 110 ? 62.498  -55.772  -37.026 1.00 55.62 ? 110 GLN   J NE2 1 
ATOM   12334 N  N   . VAL   J  1 111 ? 59.556  -58.090  -42.897 1.00 32.73 ? 111 VAL   J N   1 
ATOM   12335 C  CA  . VAL   J  1 111 ? 59.623  -58.913  -44.105 1.00 35.83 ? 111 VAL   J CA  1 
ATOM   12336 C  C   . VAL   J  1 111 ? 58.646  -58.466  -45.183 1.00 36.93 ? 111 VAL   J C   1 
ATOM   12337 O  O   . VAL   J  1 111 ? 58.489  -59.173  -46.178 1.00 33.64 ? 111 VAL   J O   1 
ATOM   12338 C  CB  . VAL   J  1 111 ? 59.399  -60.403  -43.795 1.00 34.66 ? 111 VAL   J CB  1 
ATOM   12339 C  CG1 . VAL   J  1 111 ? 60.450  -60.876  -42.790 1.00 38.46 ? 111 VAL   J CG1 1 
ATOM   12340 C  CG2 . VAL   J  1 111 ? 57.987  -60.663  -43.283 1.00 35.21 ? 111 VAL   J CG2 1 
ATOM   12341 N  N   . HIS   J  1 112 ? 57.993  -57.309  -45.004 1.00 37.60 ? 112 HIS   J N   1 
ATOM   12342 C  CA  . HIS   J  1 112 ? 57.172  -56.660  -46.032 1.00 39.55 ? 112 HIS   J CA  1 
ATOM   12343 C  C   . HIS   J  1 112 ? 55.847  -57.365  -46.303 1.00 33.97 ? 112 HIS   J C   1 
ATOM   12344 O  O   . HIS   J  1 112 ? 55.265  -57.234  -47.405 1.00 27.75 ? 112 HIS   J O   1 
ATOM   12345 C  CB  . HIS   J  1 112 ? 57.952  -56.547  -47.341 1.00 40.96 ? 112 HIS   J CB  1 
ATOM   12346 C  CG  . HIS   J  1 112 ? 59.309  -55.942  -47.177 1.00 45.20 ? 112 HIS   J CG  1 
ATOM   12347 N  ND1 . HIS   J  1 112 ? 59.528  -54.795  -46.446 1.00 44.63 ? 112 HIS   J ND1 1 
ATOM   12348 C  CD2 . HIS   J  1 112 ? 60.514  -56.310  -47.670 1.00 43.74 ? 112 HIS   J CD2 1 
ATOM   12349 C  CE1 . HIS   J  1 112 ? 60.810  -54.485  -46.492 1.00 39.07 ? 112 HIS   J CE1 1 
ATOM   12350 N  NE2 . HIS   J  1 112 ? 61.430  -55.391  -47.222 1.00 52.03 ? 112 HIS   J NE2 1 
ATOM   12351 N  N   . ASP   J  1 113 ? 55.347  -58.110  -45.320 1.00 30.31 ? 113 ASP   J N   1 
ATOM   12352 C  CA  . ASP   J  1 113 ? 54.028  -58.722  -45.425 1.00 30.16 ? 113 ASP   J CA  1 
ATOM   12353 C  C   . ASP   J  1 113 ? 53.000  -57.707  -44.926 1.00 31.41 ? 113 ASP   J C   1 
ATOM   12354 O  O   . ASP   J  1 113 ? 52.481  -57.770  -43.808 1.00 29.08 ? 113 ASP   J O   1 
ATOM   12355 C  CB  . ASP   J  1 113 ? 53.989  -60.033  -44.660 1.00 31.17 ? 113 ASP   J CB  1 
ATOM   12356 C  CG  . ASP   J  1 113 ? 52.694  -60.776  -44.856 1.00 28.52 ? 113 ASP   J CG  1 
ATOM   12357 O  OD1 . ASP   J  1 113 ? 51.762  -60.188  -45.454 1.00 32.12 ? 113 ASP   J OD1 1 
ATOM   12358 O  OD2 . ASP   J  1 113 ? 52.588  -61.944  -44.427 1.00 30.30 ? 113 ASP   J OD2 1 
ATOM   12359 N  N   . TYR   J  1 114 ? 52.766  -56.710  -45.774 1.00 27.50 ? 114 TYR   J N   1 
ATOM   12360 C  CA  . TYR   J  1 114 ? 51.987  -55.556  -45.336 1.00 29.88 ? 114 TYR   J CA  1 
ATOM   12361 C  C   . TYR   J  1 114 ? 50.516  -55.893  -45.162 1.00 32.80 ? 114 TYR   J C   1 
ATOM   12362 O  O   . TYR   J  1 114 ? 49.843  -55.253  -44.335 1.00 30.98 ? 114 TYR   J O   1 
ATOM   12363 C  CB  . TYR   J  1 114 ? 52.146  -54.412  -46.313 1.00 28.37 ? 114 TYR   J CB  1 
ATOM   12364 C  CG  . TYR   J  1 114 ? 53.555  -53.931  -46.382 1.00 29.97 ? 114 TYR   J CG  1 
ATOM   12365 C  CD1 . TYR   J  1 114 ? 54.165  -53.402  -45.273 1.00 31.53 ? 114 TYR   J CD1 1 
ATOM   12366 C  CD2 . TYR   J  1 114 ? 54.292  -54.024  -47.567 1.00 30.22 ? 114 TYR   J CD2 1 
ATOM   12367 C  CE1 . TYR   J  1 114 ? 55.486  -52.947  -45.317 1.00 32.49 ? 114 TYR   J CE1 1 
ATOM   12368 C  CE2 . TYR   J  1 114 ? 55.591  -53.577  -47.633 1.00 33.47 ? 114 TYR   J CE2 1 
ATOM   12369 C  CZ  . TYR   J  1 114 ? 56.192  -53.046  -46.510 1.00 31.80 ? 114 TYR   J CZ  1 
ATOM   12370 O  OH  . TYR   J  1 114 ? 57.481  -52.593  -46.594 1.00 36.95 ? 114 TYR   J OH  1 
ATOM   12371 N  N   . VAL   J  1 115 ? 50.018  -56.899  -45.902 1.00 33.54 ? 115 VAL   J N   1 
ATOM   12372 C  CA  . VAL   J  1 115 ? 48.627  -57.351  -45.745 1.00 29.87 ? 115 VAL   J CA  1 
ATOM   12373 C  C   . VAL   J  1 115 ? 48.443  -58.107  -44.427 1.00 37.91 ? 115 VAL   J C   1 
ATOM   12374 O  O   . VAL   J  1 115 ? 47.409  -57.974  -43.760 1.00 29.29 ? 115 VAL   J O   1 
ATOM   12375 C  CB  . VAL   J  1 115 ? 48.196  -58.214  -46.945 1.00 29.15 ? 115 VAL   J CB  1 
ATOM   12376 C  CG1 . VAL   J  1 115 ? 46.789  -58.726  -46.778 1.00 32.78 ? 115 VAL   J CG1 1 
ATOM   12377 C  CG2 . VAL   J  1 115 ? 48.294  -57.423  -48.252 1.00 28.01 ? 115 VAL   J CG2 1 
ATOM   12378 N  N   . SER   J  1 116 ? 49.408  -58.947  -44.039 1.00 30.07 ? 116 SER   J N   1 
ATOM   12379 C  CA  . SER   J  1 116 ? 49.328  -59.537  -42.703 1.00 28.52 ? 116 SER   J CA  1 
ATOM   12380 C  C   . SER   J  1 116 ? 49.367  -58.448  -41.635 1.00 28.04 ? 116 SER   J C   1 
ATOM   12381 O  O   . SER   J  1 116 ? 48.581  -58.478  -40.675 1.00 30.76 ? 116 SER   J O   1 
ATOM   12382 C  CB  . SER   J  1 116 ? 50.445  -60.576  -42.500 1.00 33.48 ? 116 SER   J CB  1 
ATOM   12383 O  OG  . SER   J  1 116 ? 50.187  -61.748  -43.290 1.00 28.35 ? 116 SER   J OG  1 
ATOM   12384 N  N   . ARG   J  1 117 ? 50.217  -57.440  -41.812 1.00 28.29 ? 117 ARG   J N   1 
ATOM   12385 C  CA  . ARG   J  1 117 ? 50.247  -56.361  -40.831 1.00 33.50 ? 117 ARG   J CA  1 
ATOM   12386 C  C   . ARG   J  1 117 ? 48.896  -55.647  -40.714 1.00 35.52 ? 117 ARG   J C   1 
ATOM   12387 O  O   . ARG   J  1 117 ? 48.485  -55.274  -39.609 1.00 28.78 ? 117 ARG   J O   1 
ATOM   12388 C  CB  . ARG   J  1 117 ? 51.314  -55.348  -41.182 1.00 24.81 ? 117 ARG   J CB  1 
ATOM   12389 C  CG  . ARG   J  1 117 ? 51.123  -54.033  -40.445 1.00 22.83 ? 117 ARG   J CG  1 
ATOM   12390 C  CD  . ARG   J  1 117 ? 52.281  -53.125  -40.544 1.00 27.23 ? 117 ARG   J CD  1 
ATOM   12391 N  NE  . ARG   J  1 117 ? 51.971  -51.863  -39.886 1.00 32.12 ? 117 ARG   J NE  1 
ATOM   12392 C  CZ  . ARG   J  1 117 ? 52.864  -51.033  -39.376 1.00 38.90 ? 117 ARG   J CZ  1 
ATOM   12393 N  NH1 . ARG   J  1 117 ? 54.166  -51.262  -39.494 1.00 37.22 ? 117 ARG   J NH1 1 
ATOM   12394 N  NH2 . ARG   J  1 117 ? 52.441  -49.941  -38.740 1.00 36.33 ? 117 ARG   J NH2 1 
ATOM   12395 N  N   . ASP   J  1 118 ? 48.235  -55.371  -41.851 1.00 35.49 ? 118 ASP   J N   1 
ATOM   12396 C  CA  . ASP   J  1 118 ? 46.948  -54.669  -41.819 1.00 32.79 ? 118 ASP   J CA  1 
ATOM   12397 C  C   . ASP   J  1 118 ? 45.889  -55.492  -41.089 1.00 29.96 ? 118 ASP   J C   1 
ATOM   12398 O  O   . ASP   J  1 118 ? 45.092  -54.951  -40.308 1.00 30.31 ? 118 ASP   J O   1 
ATOM   12399 C  CB  . ASP   J  1 118 ? 46.509  -54.365  -43.251 1.00 25.79 ? 118 ASP   J CB  1 
ATOM   12400 C  CG  . ASP   J  1 118 ? 45.449  -53.285  -43.339 1.00 33.06 ? 118 ASP   J CG  1 
ATOM   12401 O  OD1 . ASP   J  1 118 ? 45.633  -52.227  -42.725 1.00 33.64 ? 118 ASP   J OD1 1 
ATOM   12402 O  OD2 . ASP   J  1 118 ? 44.479  -53.472  -44.105 1.00 31.11 ? 118 ASP   J OD2 1 
ATOM   12403 N  N   . LEU   J  1 119 ? 45.866  -56.806  -41.324 1.00 27.97 ? 119 LEU   J N   1 
ATOM   12404 C  CA  . LEU   J  1 119 ? 44.950  -57.667  -40.594 1.00 29.29 ? 119 LEU   J CA  1 
ATOM   12405 C  C   . LEU   J  1 119 ? 45.199  -57.599  -39.090 1.00 30.90 ? 119 LEU   J C   1 
ATOM   12406 O  O   . LEU   J  1 119 ? 44.267  -57.427  -38.288 1.00 29.02 ? 119 LEU   J O   1 
ATOM   12407 C  CB  . LEU   J  1 119 ? 45.095  -59.104  -41.083 1.00 27.77 ? 119 LEU   J CB  1 
ATOM   12408 C  CG  . LEU   J  1 119 ? 44.230  -60.115  -40.304 1.00 34.43 ? 119 LEU   J CG  1 
ATOM   12409 C  CD1 . LEU   J  1 119 ? 42.703  -59.808  -40.404 1.00 36.69 ? 119 LEU   J CD1 1 
ATOM   12410 C  CD2 . LEU   J  1 119 ? 44.520  -61.544  -40.769 1.00 32.41 ? 119 LEU   J CD2 1 
ATOM   12411 N  N   . LEU   J  1 120 ? 46.457  -57.781  -38.684 1.00 31.73 ? 120 LEU   J N   1 
ATOM   12412 C  CA  . LEU   J  1 120 ? 46.787  -57.768  -37.264 1.00 27.73 ? 120 LEU   J CA  1 
ATOM   12413 C  C   . LEU   J  1 120 ? 46.484  -56.414  -36.649 1.00 23.31 ? 120 LEU   J C   1 
ATOM   12414 O  O   . LEU   J  1 120 ? 46.066  -56.340  -35.499 1.00 28.58 ? 120 LEU   J O   1 
ATOM   12415 C  CB  . LEU   J  1 120 ? 48.273  -58.115  -37.064 1.00 26.86 ? 120 LEU   J CB  1 
ATOM   12416 C  CG  . LEU   J  1 120 ? 48.656  -59.543  -37.455 1.00 32.44 ? 120 LEU   J CG  1 
ATOM   12417 C  CD1 . LEU   J  1 120 ? 50.179  -59.819  -37.248 1.00 36.61 ? 120 LEU   J CD1 1 
ATOM   12418 C  CD2 . LEU   J  1 120 ? 47.814  -60.587  -36.699 1.00 37.20 ? 120 LEU   J CD2 1 
ATOM   12419 N  N   . LYS   J  1 121 ? 46.720  -55.327  -37.394 1.00 24.49 ? 121 LYS   J N   1 
ATOM   12420 C  CA  . LYS   J  1 121 ? 46.396  -54.011  -36.874 1.00 26.17 ? 121 LYS   J CA  1 
ATOM   12421 C  C   . LYS   J  1 121 ? 44.882  -53.879  -36.656 1.00 29.99 ? 121 LYS   J C   1 
ATOM   12422 O  O   . LYS   J  1 121 ? 44.441  -53.319  -35.650 1.00 31.20 ? 121 LYS   J O   1 
ATOM   12423 C  CB  . LYS   J  1 121 ? 46.906  -52.939  -37.821 1.00 26.81 ? 121 LYS   J CB  1 
ATOM   12424 C  CG  . LYS   J  1 121 ? 46.597  -51.499  -37.404 1.00 31.14 ? 121 LYS   J CG  1 
ATOM   12425 C  CD  . LYS   J  1 121 ? 45.189  -50.997  -37.866 1.00 36.63 ? 121 LYS   J CD  1 
ATOM   12426 C  CE  . LYS   J  1 121 ? 45.079  -50.812  -39.387 1.00 39.01 ? 121 LYS   J CE  1 
ATOM   12427 N  NZ  . LYS   J  1 121 ? 43.707  -50.265  -39.749 1.00 44.88 ? 121 LYS   J NZ  1 
ATOM   12428 N  N   . ASP   J  1 122 ? 44.077  -54.427  -37.559 1.00 30.77 ? 122 ASP   J N   1 
ATOM   12429 C  CA  . ASP   J  1 122 ? 42.631  -54.376  -37.341 1.00 33.92 ? 122 ASP   J CA  1 
ATOM   12430 C  C   . ASP   J  1 122 ? 42.246  -55.189  -36.109 1.00 27.44 ? 122 ASP   J C   1 
ATOM   12431 O  O   . ASP   J  1 122 ? 41.430  -54.741  -35.299 1.00 26.44 ? 122 ASP   J O   1 
ATOM   12432 C  CB  . ASP   J  1 122 ? 41.872  -54.897  -38.555 1.00 30.57 ? 122 ASP   J CB  1 
ATOM   12433 C  CG  . ASP   J  1 122 ? 41.966  -53.982  -39.775 1.00 32.04 ? 122 ASP   J CG  1 
ATOM   12434 O  OD1 . ASP   J  1 122 ? 42.282  -52.778  -39.679 1.00 28.99 ? 122 ASP   J OD1 1 
ATOM   12435 O  OD2 . ASP   J  1 122 ? 41.718  -54.515  -40.869 1.00 31.09 ? 122 ASP   J OD2 1 
ATOM   12436 N  N   . ILE   J  1 123 ? 42.828  -56.384  -35.939 1.00 28.53 ? 123 ILE   J N   1 
ATOM   12437 C  CA  . ILE   J  1 123 ? 42.549  -57.160  -34.726 1.00 30.34 ? 123 ILE   J CA  1 
ATOM   12438 C  C   . ILE   J  1 123 ? 42.973  -56.378  -33.487 1.00 27.08 ? 123 ILE   J C   1 
ATOM   12439 O  O   . ILE   J  1 123 ? 42.242  -56.342  -32.476 1.00 28.60 ? 123 ILE   J O   1 
ATOM   12440 C  CB  . ILE   J  1 123 ? 43.222  -58.548  -34.784 1.00 28.19 ? 123 ILE   J CB  1 
ATOM   12441 C  CG1 . ILE   J  1 123 ? 42.639  -59.385  -35.926 1.00 36.90 ? 123 ILE   J CG1 1 
ATOM   12442 C  CG2 . ILE   J  1 123 ? 43.071  -59.309  -33.448 1.00 31.50 ? 123 ILE   J CG2 1 
ATOM   12443 C  CD1 . ILE   J  1 123 ? 43.362  -60.748  -36.149 1.00 36.92 ? 123 ILE   J CD1 1 
ATOM   12444 N  N   . LEU   J  1 124 ? 44.151  -55.731  -33.547 1.00 30.65 ? 124 LEU   J N   1 
ATOM   12445 C  CA  . LEU   J  1 124 ? 44.662  -54.966  -32.408 1.00 27.61 ? 124 LEU   J CA  1 
ATOM   12446 C  C   . LEU   J  1 124 ? 43.720  -53.824  -32.023 1.00 26.06 ? 124 LEU   J C   1 
ATOM   12447 O  O   . LEU   J  1 124 ? 43.562  -53.510  -30.836 1.00 28.59 ? 124 LEU   J O   1 
ATOM   12448 C  CB  . LEU   J  1 124 ? 46.047  -54.401  -32.717 1.00 26.24 ? 124 LEU   J CB  1 
ATOM   12449 C  CG  . LEU   J  1 124 ? 46.749  -53.576  -31.630 1.00 30.42 ? 124 LEU   J CG  1 
ATOM   12450 C  CD1 . LEU   J  1 124 ? 47.066  -54.442  -30.392 1.00 31.89 ? 124 LEU   J CD1 1 
ATOM   12451 C  CD2 . LEU   J  1 124 ? 48.027  -52.911  -32.143 1.00 28.49 ? 124 LEU   J CD2 1 
ATOM   12452 N  N   . GLU   J  1 125 ? 43.112  -53.171  -33.013 1.00 25.73 ? 125 GLU   J N   1 
ATOM   12453 C  CA  . GLU   J  1 125 ? 42.115  -52.144  -32.713 1.00 28.88 ? 125 GLU   J CA  1 
ATOM   12454 C  C   . GLU   J  1 125 ? 40.925  -52.739  -31.961 1.00 24.44 ? 125 GLU   J C   1 
ATOM   12455 O  O   . GLU   J  1 125 ? 40.419  -52.142  -30.996 1.00 25.35 ? 125 GLU   J O   1 
ATOM   12456 C  CB  . GLU   J  1 125 ? 41.665  -51.466  -34.013 1.00 29.68 ? 125 GLU   J CB  1 
ATOM   12457 C  CG  . GLU   J  1 125 ? 42.770  -50.589  -34.584 1.00 36.37 ? 125 GLU   J CG  1 
ATOM   12458 C  CD  . GLU   J  1 125 ? 42.466  -49.892  -35.920 1.00 42.66 ? 125 GLU   J CD  1 
ATOM   12459 O  OE1 . GLU   J  1 125 ? 41.698  -50.417  -36.771 1.00 37.17 ? 125 GLU   J OE1 1 
ATOM   12460 O  OE2 . GLU   J  1 125 ? 43.032  -48.793  -36.109 1.00 39.88 ? 125 GLU   J OE2 1 
ATOM   12461 N  N   . SER   J  1 126 ? 40.459  -53.912  -32.386 1.00 28.24 ? 126 SER   J N   1 
ATOM   12462 C  CA  A SER   J  1 126 ? 39.385  -54.577  -31.666 0.50 29.60 ? 126 SER   J CA  1 
ATOM   12463 C  CA  B SER   J  1 126 ? 39.382  -54.580  -31.661 0.50 29.60 ? 126 SER   J CA  1 
ATOM   12464 C  C   . SER   J  1 126 ? 39.801  -54.852  -30.222 1.00 33.28 ? 126 SER   J C   1 
ATOM   12465 O  O   . SER   J  1 126 ? 39.067  -54.539  -29.270 1.00 28.69 ? 126 SER   J O   1 
ATOM   12466 C  CB  A SER   J  1 126 ? 39.014  -55.867  -32.391 0.50 26.56 ? 126 SER   J CB  1 
ATOM   12467 C  CB  B SER   J  1 126 ? 38.995  -55.889  -32.353 0.50 26.55 ? 126 SER   J CB  1 
ATOM   12468 O  OG  A SER   J  1 126 ? 38.051  -56.575  -31.657 0.50 23.84 ? 126 SER   J OG  1 
ATOM   12469 O  OG  B SER   J  1 126 ? 38.454  -55.651  -33.632 0.50 31.33 ? 126 SER   J OG  1 
ATOM   12470 N  N   . GLU   J  1 127 ? 40.994  -55.412  -30.037 1.00 28.49 ? 127 GLU   J N   1 
ATOM   12471 C  CA  . GLU   J  1 127 ? 41.425  -55.756  -28.686 1.00 23.84 ? 127 GLU   J CA  1 
ATOM   12472 C  C   . GLU   J  1 127 ? 41.592  -54.518  -27.810 1.00 24.99 ? 127 GLU   J C   1 
ATOM   12473 O  O   . GLU   J  1 127 ? 41.259  -54.559  -26.620 1.00 27.18 ? 127 GLU   J O   1 
ATOM   12474 C  CB  . GLU   J  1 127 ? 42.708  -56.580  -28.738 1.00 30.51 ? 127 GLU   J CB  1 
ATOM   12475 C  CG  . GLU   J  1 127 ? 42.622  -57.847  -29.576 1.00 29.66 ? 127 GLU   J CG  1 
ATOM   12476 C  CD  . GLU   J  1 127 ? 41.428  -58.696  -29.261 1.00 40.81 ? 127 GLU   J CD  1 
ATOM   12477 O  OE1 . GLU   J  1 127 ? 40.961  -58.688  -28.106 1.00 40.56 ? 127 GLU   J OE1 1 
ATOM   12478 O  OE2 . GLU   J  1 127 ? 40.948  -59.387  -30.182 1.00 46.76 ? 127 GLU   J OE2 1 
ATOM   12479 N  N   . GLU   J  1 128 ? 42.110  -53.407  -28.351 1.00 24.68 ? 128 GLU   J N   1 
ATOM   12480 C  CA  . GLU   J  1 128 ? 42.207  -52.211  -27.508 1.00 26.20 ? 128 GLU   J CA  1 
ATOM   12481 C  C   . GLU   J  1 128 ? 40.814  -51.681  -27.155 1.00 31.03 ? 128 GLU   J C   1 
ATOM   12482 O  O   . GLU   J  1 128 ? 40.617  -51.106  -26.073 1.00 27.35 ? 128 GLU   J O   1 
ATOM   12483 C  CB  . GLU   J  1 128 ? 43.058  -51.128  -28.177 1.00 27.15 ? 128 GLU   J CB  1 
ATOM   12484 C  CG  . GLU   J  1 128 ? 44.595  -51.470  -28.179 1.00 31.71 ? 128 GLU   J CG  1 
ATOM   12485 C  CD  . GLU   J  1 128 ? 45.485  -50.326  -28.608 1.00 31.12 ? 128 GLU   J CD  1 
ATOM   12486 O  OE1 . GLU   J  1 128 ? 44.985  -49.201  -28.748 1.00 31.31 ? 128 GLU   J OE1 1 
ATOM   12487 O  OE2 . GLU   J  1 128 ? 46.708  -50.554  -28.828 1.00 36.56 ? 128 GLU   J OE2 1 
ATOM   12488 N  N   . GLU   J  1 129 ? 39.825  -51.914  -28.024 1.00 25.24 ? 129 GLU   J N   1 
ATOM   12489 C  CA  . GLU   J  1 129 ? 38.446  -51.570  -27.661 1.00 33.03 ? 129 GLU   J CA  1 
ATOM   12490 C  C   . GLU   J  1 129 ? 37.951  -52.465  -26.523 1.00 28.37 ? 129 GLU   J C   1 
ATOM   12491 O  O   . GLU   J  1 129 ? 37.310  -51.983  -25.584 1.00 26.06 ? 129 GLU   J O   1 
ATOM   12492 C  CB  . GLU   J  1 129 ? 37.527  -51.651  -28.906 1.00 27.68 ? 129 GLU   J CB  1 
ATOM   12493 N  N   . HIS   J  1 130 ? 38.295  -53.756  -26.548 1.00 26.65 ? 130 HIS   J N   1 
ATOM   12494 C  CA  A HIS   J  1 130 ? 37.909  -54.634  -25.451 0.50 30.45 ? 130 HIS   J CA  1 
ATOM   12495 C  CA  B HIS   J  1 130 ? 37.917  -54.640  -25.453 0.50 30.45 ? 130 HIS   J CA  1 
ATOM   12496 C  C   . HIS   J  1 130 ? 38.600  -54.221  -24.151 1.00 37.39 ? 130 HIS   J C   1 
ATOM   12497 O  O   . HIS   J  1 130 ? 37.991  -54.273  -23.073 1.00 25.84 ? 130 HIS   J O   1 
ATOM   12498 C  CB  A HIS   J  1 130 ? 38.223  -56.092  -25.810 0.50 26.62 ? 130 HIS   J CB  1 
ATOM   12499 C  CB  B HIS   J  1 130 ? 38.263  -56.096  -25.792 0.50 26.61 ? 130 HIS   J CB  1 
ATOM   12500 C  CG  A HIS   J  1 130 ? 37.647  -57.093  -24.849 0.50 32.95 ? 130 HIS   J CG  1 
ATOM   12501 C  CG  B HIS   J  1 130 ? 37.548  -56.645  -26.990 0.50 31.89 ? 130 HIS   J CG  1 
ATOM   12502 N  ND1 A HIS   J  1 130 ? 38.109  -58.388  -24.752 0.50 37.79 ? 130 HIS   J ND1 1 
ATOM   12503 N  ND1 B HIS   J  1 130 ? 36.516  -55.981  -27.621 0.50 34.37 ? 130 HIS   J ND1 1 
ATOM   12504 C  CD2 A HIS   J  1 130 ? 36.646  -56.986  -23.942 0.50 34.58 ? 130 HIS   J CD2 1 
ATOM   12505 C  CD2 B HIS   J  1 130 ? 37.724  -57.801  -27.676 0.50 36.97 ? 130 HIS   J CD2 1 
ATOM   12506 C  CE1 A HIS   J  1 130 ? 37.425  -59.031  -23.823 0.50 31.63 ? 130 HIS   J CE1 1 
ATOM   12507 C  CE1 B HIS   J  1 130 ? 36.106  -56.690  -28.659 0.50 34.05 ? 130 HIS   J CE1 1 
ATOM   12508 N  NE2 A HIS   J  1 130 ? 36.531  -58.203  -23.318 0.50 34.43 ? 130 HIS   J NE2 1 
ATOM   12509 N  NE2 B HIS   J  1 130 ? 36.810  -57.807  -28.704 0.50 32.40 ? 130 HIS   J NE2 1 
ATOM   12510 N  N   . ILE   J  1 131 ? 39.867  -53.802  -24.233 1.00 28.34 ? 131 ILE   J N   1 
ATOM   12511 C  CA  . ILE   J  1 131 ? 40.598  -53.353  -23.054 1.00 29.39 ? 131 ILE   J CA  1 
ATOM   12512 C  C   . ILE   J  1 131 ? 39.960  -52.100  -22.476 1.00 28.52 ? 131 ILE   J C   1 
ATOM   12513 O  O   . ILE   J  1 131 ? 39.814  -51.962  -21.256 1.00 29.10 ? 131 ILE   J O   1 
ATOM   12514 C  CB  . ILE   J  1 131 ? 42.076  -53.128  -23.424 1.00 31.16 ? 131 ILE   J CB  1 
ATOM   12515 C  CG1 . ILE   J  1 131 ? 42.757  -54.479  -23.644 1.00 30.32 ? 131 ILE   J CG1 1 
ATOM   12516 C  CG2 . ILE   J  1 131 ? 42.784  -52.288  -22.365 1.00 26.64 ? 131 ILE   J CG2 1 
ATOM   12517 C  CD1 . ILE   J  1 131 ? 44.232  -54.340  -24.175 1.00 36.34 ? 131 ILE   J CD1 1 
ATOM   12518 N  N   . ASP   J  1 132 ? 39.616  -51.148  -23.335 1.00 29.07 ? 132 ASP   J N   1 
ATOM   12519 C  CA  . ASP   J  1 132 ? 38.871  -49.972  -22.904 1.00 31.01 ? 132 ASP   J CA  1 
ATOM   12520 C  C   . ASP   J  1 132 ? 37.600  -50.383  -22.147 1.00 32.32 ? 132 ASP   J C   1 
ATOM   12521 O  O   . ASP   J  1 132 ? 37.309  -49.862  -21.071 1.00 29.27 ? 132 ASP   J O   1 
ATOM   12522 C  CB  . ASP   J  1 132 ? 38.533  -49.120  -24.131 1.00 32.12 ? 132 ASP   J CB  1 
ATOM   12523 C  CG  . ASP   J  1 132 ? 38.033  -47.711  -23.765 1.00 29.47 ? 132 ASP   J CG  1 
ATOM   12524 O  OD1 . ASP   J  1 132 ? 38.052  -47.333  -22.580 1.00 33.49 ? 132 ASP   J OD1 1 
ATOM   12525 O  OD2 . ASP   J  1 132 ? 37.655  -46.971  -24.683 1.00 41.15 ? 132 ASP   J OD2 1 
ATOM   12526 N  N   . TYR   J  1 133 ? 36.842  -51.335  -22.699 1.00 29.37 ? 133 TYR   J N   1 
ATOM   12527 C  CA  . TYR   J  1 133 ? 35.626  -51.799  -22.042 1.00 31.55 ? 133 TYR   J CA  1 
ATOM   12528 C  C   . TYR   J  1 133 ? 35.930  -52.419  -20.679 1.00 32.69 ? 133 TYR   J C   1 
ATOM   12529 O  O   . TYR   J  1 133 ? 35.220  -52.171  -19.687 1.00 25.75 ? 133 TYR   J O   1 
ATOM   12530 C  CB  . TYR   J  1 133 ? 34.919  -52.807  -22.944 1.00 29.09 ? 133 TYR   J CB  1 
ATOM   12531 C  CG  . TYR   J  1 133 ? 33.901  -53.610  -22.215 1.00 28.70 ? 133 TYR   J CG  1 
ATOM   12532 C  CD1 . TYR   J  1 133 ? 32.620  -53.114  -21.977 1.00 36.06 ? 133 TYR   J CD1 1 
ATOM   12533 C  CD2 . TYR   J  1 133 ? 34.221  -54.857  -21.727 1.00 38.18 ? 133 TYR   J CD2 1 
ATOM   12534 C  CE1 . TYR   J  1 133 ? 31.697  -53.861  -21.280 1.00 29.55 ? 133 TYR   J CE1 1 
ATOM   12535 C  CE2 . TYR   J  1 133 ? 33.318  -55.599  -21.042 1.00 34.91 ? 133 TYR   J CE2 1 
ATOM   12536 C  CZ  . TYR   J  1 133 ? 32.061  -55.103  -20.811 1.00 33.00 ? 133 TYR   J CZ  1 
ATOM   12537 O  OH  . TYR   J  1 133 ? 31.176  -55.900  -20.124 1.00 36.08 ? 133 TYR   J OH  1 
ATOM   12538 N  N   . LEU   J  1 134 ? 36.960  -53.270  -20.618 1.00 34.98 ? 134 LEU   J N   1 
ATOM   12539 C  CA  . LEU   J  1 134 ? 37.267  -53.971  -19.366 1.00 33.13 ? 134 LEU   J CA  1 
ATOM   12540 C  C   . LEU   J  1 134 ? 37.771  -53.011  -18.291 1.00 27.61 ? 134 LEU   J C   1 
ATOM   12541 O  O   . LEU   J  1 134 ? 37.353  -53.092  -17.113 1.00 27.98 ? 134 LEU   J O   1 
ATOM   12542 C  CB  . LEU   J  1 134 ? 38.299  -55.065  -19.623 1.00 26.29 ? 134 LEU   J CB  1 
ATOM   12543 C  CG  . LEU   J  1 134 ? 37.827  -56.223  -20.480 1.00 31.13 ? 134 LEU   J CG  1 
ATOM   12544 C  CD1 . LEU   J  1 134 ? 39.007  -57.021  -21.057 1.00 30.61 ? 134 LEU   J CD1 1 
ATOM   12545 C  CD2 . LEU   J  1 134 ? 36.919  -57.126  -19.655 1.00 24.81 ? 134 LEU   J CD2 1 
ATOM   12546 N  N   . GLU   J  1 135 ? 38.678  -52.109  -18.670 1.00 28.68 ? 135 GLU   J N   1 
ATOM   12547 C  CA  . GLU   J  1 135 ? 39.182  -51.113  -17.733 1.00 30.98 ? 135 GLU   J CA  1 
ATOM   12548 C  C   . GLU   J  1 135 ? 38.052  -50.243  -17.197 1.00 32.59 ? 135 GLU   J C   1 
ATOM   12549 O  O   . GLU   J  1 135 ? 38.002  -49.929  -15.996 1.00 28.18 ? 135 GLU   J O   1 
ATOM   12550 C  CB  . GLU   J  1 135 ? 40.239  -50.256  -18.423 1.00 30.19 ? 135 GLU   J CB  1 
ATOM   12551 C  CG  . GLU   J  1 135 ? 41.575  -50.993  -18.675 1.00 30.64 ? 135 GLU   J CG  1 
ATOM   12552 C  CD  . GLU   J  1 135 ? 42.564  -50.153  -19.432 1.00 32.33 ? 135 GLU   J CD  1 
ATOM   12553 O  OE1 . GLU   J  1 135 ? 42.145  -49.233  -20.172 1.00 34.08 ? 135 GLU   J OE1 1 
ATOM   12554 O  OE2 . GLU   J  1 135 ? 43.771  -50.408  -19.270 1.00 40.51 ? 135 GLU   J OE2 1 
ATOM   12555 N  N   . THR   J  1 136 ? 37.143  -49.835  -18.085 1.00 27.40 ? 136 THR   J N   1 
ATOM   12556 C  CA  . THR   J  1 136 ? 35.977  -49.054  -17.683 1.00 28.60 ? 136 THR   J CA  1 
ATOM   12557 C  C   . THR   J  1 136 ? 35.070  -49.831  -16.720 1.00 26.48 ? 136 THR   J C   1 
ATOM   12558 O  O   . THR   J  1 136 ? 34.577  -49.264  -15.732 1.00 31.56 ? 136 THR   J O   1 
ATOM   12559 C  CB  . THR   J  1 136 ? 35.236  -48.620  -18.954 1.00 33.30 ? 136 THR   J CB  1 
ATOM   12560 O  OG1 . THR   J  1 136 ? 36.097  -47.769  -19.726 1.00 36.37 ? 136 THR   J OG1 1 
ATOM   12561 C  CG2 . THR   J  1 136 ? 33.961  -47.849  -18.645 1.00 29.30 ? 136 THR   J CG2 1 
ATOM   12562 N  N   . GLN   J  1 137 ? 34.839  -51.124  -16.974 1.00 26.53 ? 137 GLN   J N   1 
ATOM   12563 C  CA  . GLN   J  1 137 ? 34.017  -51.914  -16.065 1.00 22.58 ? 137 GLN   J CA  1 
ATOM   12564 C  C   . GLN   J  1 137 ? 34.651  -51.982  -14.678 1.00 36.18 ? 137 GLN   J C   1 
ATOM   12565 O  O   . GLN   J  1 137 ? 33.966  -51.854  -13.655 1.00 27.36 ? 137 GLN   J O   1 
ATOM   12566 C  CB  . GLN   J  1 137 ? 33.793  -53.330  -16.594 1.00 27.92 ? 137 GLN   J CB  1 
ATOM   12567 C  CG  . GLN   J  1 137 ? 32.988  -53.469  -17.930 1.00 32.79 ? 137 GLN   J CG  1 
ATOM   12568 C  CD  . GLN   J  1 137 ? 31.963  -52.368  -18.147 1.00 30.16 ? 137 GLN   J CD  1 
ATOM   12569 O  OE1 . GLN   J  1 137 ? 32.174  -51.460  -18.944 1.00 36.34 ? 137 GLN   J OE1 1 
ATOM   12570 N  NE2 . GLN   J  1 137 ? 30.859  -52.443  -17.431 1.00 23.93 ? 137 GLN   J NE2 1 
ATOM   12571 N  N   . LEU   J  1 138 ? 35.959  -52.240  -14.620 1.00 31.29 ? 138 LEU   J N   1 
ATOM   12572 C  CA  . LEU   J  1 138 ? 36.611  -52.330  -13.322 1.00 31.31 ? 138 LEU   J CA  1 
ATOM   12573 C  C   . LEU   J  1 138 ? 36.539  -50.995  -12.614 1.00 25.20 ? 138 LEU   J C   1 
ATOM   12574 O  O   . LEU   J  1 138 ? 36.368  -50.941  -11.395 1.00 29.48 ? 138 LEU   J O   1 
ATOM   12575 C  CB  . LEU   J  1 138 ? 38.064  -52.791  -13.506 1.00 29.26 ? 138 LEU   J CB  1 
ATOM   12576 C  CG  . LEU   J  1 138 ? 38.124  -54.240  -13.990 1.00 29.13 ? 138 LEU   J CG  1 
ATOM   12577 C  CD1 . LEU   J  1 138 ? 39.493  -54.593  -14.607 1.00 37.96 ? 138 LEU   J CD1 1 
ATOM   12578 C  CD2 . LEU   J  1 138 ? 37.791  -55.185  -12.867 1.00 28.85 ? 138 LEU   J CD2 1 
ATOM   12579 N  N   . GLY   J  1 139 ? 36.633  -49.902  -13.373 1.00 25.66 ? 139 GLY   J N   1 
ATOM   12580 C  CA  . GLY   J  1 139 ? 36.507  -48.582  -12.777 1.00 25.35 ? 139 GLY   J CA  1 
ATOM   12581 C  C   . GLY   J  1 139 ? 35.101  -48.312  -12.271 1.00 28.89 ? 139 GLY   J C   1 
ATOM   12582 O  O   . GLY   J  1 139 ? 34.927  -47.714  -11.210 1.00 27.03 ? 139 GLY   J O   1 
ATOM   12583 N  N   . LEU   J  1 140 ? 34.080  -48.766  -13.021 1.00 28.47 ? 140 LEU   J N   1 
ATOM   12584 C  CA  . LEU   J  1 140 ? 32.691  -48.598  -12.595 1.00 27.33 ? 140 LEU   J CA  1 
ATOM   12585 C  C   . LEU   J  1 140 ? 32.415  -49.335  -11.291 1.00 31.85 ? 140 LEU   J C   1 
ATOM   12586 O  O   . LEU   J  1 140 ? 31.674  -48.835  -10.438 1.00 27.43 ? 140 LEU   J O   1 
ATOM   12587 C  CB  . LEU   J  1 140 ? 31.736  -49.093  -13.695 1.00 27.96 ? 140 LEU   J CB  1 
ATOM   12588 C  CG  . LEU   J  1 140 ? 31.573  -48.130  -14.862 1.00 28.07 ? 140 LEU   J CG  1 
ATOM   12589 C  CD1 . LEU   J  1 140 ? 30.738  -48.753  -15.995 1.00 25.36 ? 140 LEU   J CD1 1 
ATOM   12590 C  CD2 . LEU   J  1 140 ? 30.935  -46.833  -14.413 1.00 29.42 ? 140 LEU   J CD2 1 
ATOM   12591 N  N   . ILE   J  1 141 ? 32.966  -50.545  -11.139 1.00 29.36 ? 141 ILE   J N   1 
ATOM   12592 C  CA  . ILE   J  1 141 ? 32.801  -51.286  -9.893  1.00 31.58 ? 141 ILE   J CA  1 
ATOM   12593 C  C   . ILE   J  1 141 ? 33.252  -50.427  -8.720  1.00 29.53 ? 141 ILE   J C   1 
ATOM   12594 O  O   . ILE   J  1 141 ? 32.610  -50.400  -7.661  1.00 27.81 ? 141 ILE   J O   1 
ATOM   12595 C  CB  . ILE   J  1 141 ? 33.556  -52.630  -9.973  1.00 29.09 ? 141 ILE   J CB  1 
ATOM   12596 C  CG1 . ILE   J  1 141 ? 32.783  -53.577  -10.874 1.00 31.83 ? 141 ILE   J CG1 1 
ATOM   12597 C  CG2 . ILE   J  1 141 ? 33.727  -53.299  -8.589  1.00 28.32 ? 141 ILE   J CG2 1 
ATOM   12598 C  CD1 . ILE   J  1 141 ? 33.476  -54.888  -11.108 1.00 34.54 ? 141 ILE   J CD1 1 
ATOM   12599 N  N   . GLN   J  1 142 ? 34.325  -49.653  -8.913  1.00 28.60 ? 142 GLN   J N   1 
ATOM   12600 C  CA  . GLN   J  1 142 ? 34.757  -48.732  -7.868  1.00 31.67 ? 142 GLN   J CA  1 
ATOM   12601 C  C   . GLN   J  1 142 ? 33.798  -47.559  -7.729  1.00 29.97 ? 142 GLN   J C   1 
ATOM   12602 O  O   . GLN   J  1 142 ? 33.465  -47.165  -6.616  1.00 29.92 ? 142 GLN   J O   1 
ATOM   12603 C  CB  . GLN   J  1 142 ? 36.154  -48.189  -8.151  1.00 33.88 ? 142 GLN   J CB  1 
ATOM   12604 C  CG  . GLN   J  1 142 ? 37.194  -49.202  -8.319  1.00 29.43 ? 142 GLN   J CG  1 
ATOM   12605 C  CD  . GLN   J  1 142 ? 38.571  -48.534  -8.432  1.00 44.58 ? 142 GLN   J CD  1 
ATOM   12606 O  OE1 . GLN   J  1 142 ? 38.796  -47.685  -9.297  1.00 49.00 ? 142 GLN   J OE1 1 
ATOM   12607 N  NE2 . GLN   J  1 142 ? 39.460  -48.871  -7.529  1.00 34.15 ? 142 GLN   J NE2 1 
ATOM   12608 N  N   . LYS   J  1 143 ? 33.373  -46.961  -8.838  1.00 30.44 ? 143 LYS   J N   1 
ATOM   12609 C  CA  . LYS   J  1 143 ? 32.611  -45.721  -8.734  1.00 27.04 ? 143 LYS   J CA  1 
ATOM   12610 C  C   . LYS   J  1 143 ? 31.183  -45.962  -8.218  1.00 28.97 ? 143 LYS   J C   1 
ATOM   12611 O  O   . LYS   J  1 143 ? 30.672  -45.176  -7.425  1.00 29.92 ? 143 LYS   J O   1 
ATOM   12612 C  CB  . LYS   J  1 143 ? 32.592  -45.012  -10.081 1.00 26.64 ? 143 LYS   J CB  1 
ATOM   12613 C  CG  . LYS   J  1 143 ? 33.993  -44.477  -10.494 1.00 37.50 ? 143 LYS   J CG  1 
ATOM   12614 C  CD  . LYS   J  1 143 ? 33.941  -43.524  -11.684 1.00 41.38 ? 143 LYS   J CD  1 
ATOM   12615 C  CE  . LYS   J  1 143 ? 35.305  -42.821  -11.892 1.00 40.75 ? 143 LYS   J CE  1 
ATOM   12616 N  NZ  . LYS   J  1 143 ? 36.315  -43.763  -12.456 1.00 38.02 ? 143 LYS   J NZ  1 
ATOM   12617 N  N   . VAL   J  1 144 ? 30.514  -47.030  -8.650  1.00 29.44 ? 144 VAL   J N   1 
ATOM   12618 C  CA  . VAL   J  1 144 ? 29.129  -47.232  -8.233  1.00 32.76 ? 144 VAL   J CA  1 
ATOM   12619 C  C   . VAL   J  1 144 ? 29.010  -48.253  -7.111  1.00 35.99 ? 144 VAL   J C   1 
ATOM   12620 O  O   . VAL   J  1 144 ? 27.967  -48.300  -6.438  1.00 26.70 ? 144 VAL   J O   1 
ATOM   12621 C  CB  . VAL   J  1 144 ? 28.226  -47.607  -9.432  1.00 25.97 ? 144 VAL   J CB  1 
ATOM   12622 C  CG1 . VAL   J  1 144 ? 28.430  -46.609  -10.548 1.00 32.60 ? 144 VAL   J CG1 1 
ATOM   12623 C  CG2 . VAL   J  1 144 ? 28.438  -49.071  -9.909  1.00 26.59 ? 144 VAL   J CG2 1 
ATOM   12624 N  N   . GLY   J  1 145 ? 30.071  -48.986  -6.814  1.00 29.50 ? 145 GLY   J N   1 
ATOM   12625 C  CA  . GLY   J  1 145 ? 29.984  -50.032  -5.811  1.00 28.15 ? 145 GLY   J CA  1 
ATOM   12626 C  C   . GLY   J  1 145 ? 29.623  -51.358  -6.438  1.00 23.42 ? 145 GLY   J C   1 
ATOM   12627 O  O   . GLY   J  1 145 ? 28.950  -51.434  -7.462  1.00 25.91 ? 145 GLY   J O   1 
ATOM   12628 N  N   . LEU   J  1 146 ? 30.116  -52.433  -5.838  1.00 26.16 ? 146 LEU   J N   1 
ATOM   12629 C  CA  . LEU   J  1 146 ? 29.918  -53.724  -6.478  1.00 30.06 ? 146 LEU   J CA  1 
ATOM   12630 C  C   . LEU   J  1 146 ? 28.437  -54.065  -6.582  1.00 24.21 ? 146 LEU   J C   1 
ATOM   12631 O  O   . LEU   J  1 146 ? 27.989  -54.543  -7.633  1.00 23.91 ? 146 LEU   J O   1 
ATOM   12632 C  CB  . LEU   J  1 146 ? 30.685  -54.823  -5.748  1.00 26.76 ? 146 LEU   J CB  1 
ATOM   12633 C  CG  . LEU   J  1 146 ? 30.531  -56.221  -6.379  1.00 25.54 ? 146 LEU   J CG  1 
ATOM   12634 C  CD1 . LEU   J  1 146 ? 31.000  -56.268  -7.832  1.00 26.44 ? 146 LEU   J CD1 1 
ATOM   12635 C  CD2 . LEU   J  1 146 ? 31.242  -57.280  -5.547  1.00 29.95 ? 146 LEU   J CD2 1 
ATOM   12636 N  N   . GLU   J  1 147 ? 27.642  -53.811  -5.517  1.00 24.68 ? 147 GLU   J N   1 
ATOM   12637 C  CA  . GLU   J  1 147 ? 26.233  -54.235  -5.548  1.00 23.58 ? 147 GLU   J CA  1 
ATOM   12638 C  C   . GLU   J  1 147 ? 25.461  -53.524  -6.659  1.00 22.17 ? 147 GLU   J C   1 
ATOM   12639 O  O   . GLU   J  1 147 ? 24.661  -54.148  -7.363  1.00 23.45 ? 147 GLU   J O   1 
ATOM   12640 C  CB  . GLU   J  1 147 ? 25.550  -53.968  -4.208  1.00 27.78 ? 147 GLU   J CB  1 
ATOM   12641 C  CG  . GLU   J  1 147 ? 25.885  -54.970  -3.110  1.00 34.01 ? 147 GLU   J CG  1 
ATOM   12642 C  CD  . GLU   J  1 147 ? 27.053  -54.548  -2.238  1.00 44.75 ? 147 GLU   J CD  1 
ATOM   12643 O  OE1 . GLU   J  1 147 ? 27.864  -53.673  -2.665  1.00 36.62 ? 147 GLU   J OE1 1 
ATOM   12644 O  OE2 . GLU   J  1 147 ? 27.139  -55.104  -1.111  1.00 43.77 ? 147 GLU   J OE2 1 
ATOM   12645 N  N   . ASN   J  1 148 ? 25.678  -52.215  -6.801  1.00 24.44 ? 148 ASN   J N   1 
ATOM   12646 C  CA  . ASN   J  1 148 ? 25.075  -51.452  -7.885  1.00 22.73 ? 148 ASN   J CA  1 
ATOM   12647 C  C   . ASN   J  1 148 ? 25.587  -51.913  -9.237  1.00 29.04 ? 148 ASN   J C   1 
ATOM   12648 O  O   . ASN   J  1 148 ? 24.809  -52.023  -10.201 1.00 24.45 ? 148 ASN   J O   1 
ATOM   12649 C  CB  . ASN   J  1 148 ? 25.362  -49.966  -7.705  1.00 24.39 ? 148 ASN   J CB  1 
ATOM   12650 C  CG  . ASN   J  1 148 ? 24.386  -49.290  -6.721  1.00 29.01 ? 148 ASN   J CG  1 
ATOM   12651 O  OD1 . ASN   J  1 148 ? 23.458  -49.910  -6.178  1.00 24.02 ? 148 ASN   J OD1 1 
ATOM   12652 N  ND2 . ASN   J  1 148 ? 24.611  -48.023  -6.488  1.00 25.52 ? 148 ASN   J ND2 1 
ATOM   12653 N  N   . TYR   J  1 149 ? 26.899  -52.147  -9.346  1.00 21.67 ? 149 TYR   J N   1 
ATOM   12654 C  CA  . TYR   J  1 149 ? 27.446  -52.615  -10.614 1.00 24.52 ? 149 TYR   J CA  1 
ATOM   12655 C  C   . TYR   J  1 149 ? 26.767  -53.905  -11.049 1.00 24.09 ? 149 TYR   J C   1 
ATOM   12656 O  O   . TYR   J  1 149 ? 26.344  -54.040  -12.202 1.00 27.41 ? 149 TYR   J O   1 
ATOM   12657 C  CB  . TYR   J  1 149 ? 28.966  -52.819  -10.512 1.00 24.30 ? 149 TYR   J CB  1 
ATOM   12658 C  CG  . TYR   J  1 149 ? 29.500  -53.284  -11.850 1.00 30.44 ? 149 TYR   J CG  1 
ATOM   12659 C  CD1 . TYR   J  1 149 ? 29.773  -52.372  -12.841 1.00 26.30 ? 149 TYR   J CD1 1 
ATOM   12660 C  CD2 . TYR   J  1 149 ? 29.661  -54.638  -12.136 1.00 27.35 ? 149 TYR   J CD2 1 
ATOM   12661 C  CE1 . TYR   J  1 149 ? 30.207  -52.782  -14.100 1.00 26.25 ? 149 TYR   J CE1 1 
ATOM   12662 C  CE2 . TYR   J  1 149 ? 30.087  -55.050  -13.392 1.00 26.86 ? 149 TYR   J CE2 1 
ATOM   12663 C  CZ  . TYR   J  1 149 ? 30.332  -54.115  -14.365 1.00 28.22 ? 149 TYR   J CZ  1 
ATOM   12664 O  OH  . TYR   J  1 149 ? 30.743  -54.509  -15.622 1.00 32.69 ? 149 TYR   J OH  1 
ATOM   12665 N  N   . LEU   J  1 150 ? 26.622  -54.851  -10.130 1.00 23.06 ? 150 LEU   J N   1 
ATOM   12666 C  CA  . LEU   J  1 150 ? 26.011  -56.124  -10.487 1.00 24.59 ? 150 LEU   J CA  1 
ATOM   12667 C  C   . LEU   J  1 150 ? 24.528  -55.939  -10.800 1.00 28.15 ? 150 LEU   J C   1 
ATOM   12668 O  O   . LEU   J  1 150 ? 24.016  -56.526  -11.754 1.00 24.35 ? 150 LEU   J O   1 
ATOM   12669 C  CB  . LEU   J  1 150 ? 26.177  -57.132  -9.358  1.00 25.68 ? 150 LEU   J CB  1 
ATOM   12670 C  CG  . LEU   J  1 150 ? 27.617  -57.560  -8.988  1.00 26.38 ? 150 LEU   J CG  1 
ATOM   12671 C  CD1 . LEU   J  1 150 ? 27.619  -58.546  -7.823  1.00 24.44 ? 150 LEU   J CD1 1 
ATOM   12672 C  CD2 . LEU   J  1 150 ? 28.333  -58.209  -10.218 1.00 29.54 ? 150 LEU   J CD2 1 
ATOM   12673 N  N   . GLN   J  1 151 ? 23.841  -55.127  -9.992  1.00 24.27 ? 151 GLN   J N   1 
ATOM   12674 C  CA  . GLN   J  1 151 ? 22.427  -54.827  -10.216 1.00 26.90 ? 151 GLN   J CA  1 
ATOM   12675 C  C   . GLN   J  1 151 ? 22.206  -54.292  -11.621 1.00 26.75 ? 151 GLN   J C   1 
ATOM   12676 O  O   . GLN   J  1 151 ? 21.283  -54.715  -12.328 1.00 26.12 ? 151 GLN   J O   1 
ATOM   12677 C  CB  . GLN   J  1 151 ? 21.950  -53.801  -9.195  1.00 22.90 ? 151 GLN   J CB  1 
ATOM   12678 C  CG  . GLN   J  1 151 ? 20.453  -53.440  -9.328  1.00 25.66 ? 151 GLN   J CG  1 
ATOM   12679 C  CD  . GLN   J  1 151 ? 20.042  -52.271  -8.443  1.00 26.46 ? 151 GLN   J CD  1 
ATOM   12680 O  OE1 . GLN   J  1 151 ? 20.833  -51.366  -8.163  1.00 26.31 ? 151 GLN   J OE1 1 
ATOM   12681 N  NE2 . GLN   J  1 151 ? 18.799  -52.285  -8.006  1.00 25.07 ? 151 GLN   J NE2 1 
ATOM   12682 N  N   . SER   J  1 152 ? 23.062  -53.358  -12.043 1.00 27.46 ? 152 SER   J N   1 
ATOM   12683 C  CA  . SER   J  1 152 ? 22.945  -52.746  -13.354 1.00 27.81 ? 152 SER   J CA  1 
ATOM   12684 C  C   . SER   J  1 152 ? 23.204  -53.720  -14.492 1.00 32.96 ? 152 SER   J C   1 
ATOM   12685 O  O   . SER   J  1 152 ? 23.026  -53.326  -15.649 1.00 33.22 ? 152 SER   J O   1 
ATOM   12686 C  CB  . SER   J  1 152 ? 23.901  -51.571  -13.495 1.00 29.11 ? 152 SER   J CB  1 
ATOM   12687 O  OG  . SER   J  1 152 ? 23.516  -50.461  -12.711 1.00 29.88 ? 152 SER   J OG  1 
ATOM   12688 N  N   . HIS   J  1 153 ? 23.617  -54.961  -14.205 1.00 30.78 ? 153 HIS   J N   1 
ATOM   12689 C  CA  . HIS   J  1 153 ? 23.884  -55.958  -15.241 1.00 30.77 ? 153 HIS   J CA  1 
ATOM   12690 C  C   . HIS   J  1 153 ? 23.007  -57.198  -15.120 1.00 27.02 ? 153 HIS   J C   1 
ATOM   12691 O  O   . HIS   J  1 153 ? 23.299  -58.221  -15.762 1.00 27.74 ? 153 HIS   J O   1 
ATOM   12692 C  CB  . HIS   J  1 153 ? 25.371  -56.340  -15.230 1.00 32.29 ? 153 HIS   J CB  1 
ATOM   12693 C  CG  . HIS   J  1 153 ? 26.235  -55.258  -15.765 1.00 24.31 ? 153 HIS   J CG  1 
ATOM   12694 N  ND1 . HIS   J  1 153 ? 26.649  -54.186  -15.005 1.00 29.52 ? 153 HIS   J ND1 1 
ATOM   12695 C  CD2 . HIS   J  1 153 ? 26.674  -55.020  -17.024 1.00 27.75 ? 153 HIS   J CD2 1 
ATOM   12696 C  CE1 . HIS   J  1 153 ? 27.337  -53.354  -15.765 1.00 25.48 ? 153 HIS   J CE1 1 
ATOM   12697 N  NE2 . HIS   J  1 153 ? 27.360  -53.835  -16.994 1.00 24.23 ? 153 HIS   J NE2 1 
ATOM   12698 N  N   . MET   J  1 154 ? 21.923  -57.122  -14.341 1.00 22.83 ? 154 MET   J N   1 
ATOM   12699 C  CA  . MET   J  1 154 ? 20.996  -58.240  -14.232 1.00 27.01 ? 154 MET   J CA  1 
ATOM   12700 C  C   . MET   J  1 154 ? 20.163  -58.375  -15.499 1.00 31.49 ? 154 MET   J C   1 
ATOM   12701 O  O   . MET   J  1 154 ? 20.033  -59.471  -16.055 1.00 32.92 ? 154 MET   J O   1 
ATOM   12702 C  CB  . MET   J  1 154 ? 20.084  -58.056  -13.016 1.00 31.60 ? 154 MET   J CB  1 
ATOM   12703 C  CG  . MET   J  1 154 ? 20.728  -58.273  -11.652 1.00 35.29 ? 154 MET   J CG  1 
ATOM   12704 S  SD  . MET   J  1 154 ? 19.655  -57.813  -10.256 1.00 38.93 ? 154 MET   J SD  1 
ATOM   12705 C  CE  . MET   J  1 154 ? 18.067  -58.461  -10.800 1.00 30.03 ? 154 MET   J CE  1 
ATOM   12706 N  N   . HIS   J  1 155 ? 19.607  -57.270  -15.980 1.00 32.27 ? 155 HIS   J N   1 
ATOM   12707 C  CA  . HIS   J  1 155 ? 18.635  -57.301  -17.061 1.00 39.38 ? 155 HIS   J CA  1 
ATOM   12708 C  C   . HIS   J  1 155 ? 19.260  -56.751  -18.335 1.00 44.58 ? 155 HIS   J C   1 
ATOM   12709 O  O   . HIS   J  1 155 ? 19.971  -55.740  -18.308 1.00 49.39 ? 155 HIS   J O   1 
ATOM   12710 C  CB  . HIS   J  1 155 ? 17.380  -56.500  -16.692 1.00 36.14 ? 155 HIS   J CB  1 
ATOM   12711 C  CG  . HIS   J  1 155 ? 16.675  -57.002  -15.461 1.00 45.69 ? 155 HIS   J CG  1 
ATOM   12712 N  ND1 . HIS   J  1 155 ? 16.171  -56.155  -14.498 1.00 41.03 ? 155 HIS   J ND1 1 
ATOM   12713 C  CD2 . HIS   J  1 155 ? 16.397  -58.261  -15.035 1.00 42.41 ? 155 HIS   J CD2 1 
ATOM   12714 C  CE1 . HIS   J  1 155 ? 15.613  -56.868  -13.532 1.00 45.42 ? 155 HIS   J CE1 1 
ATOM   12715 N  NE2 . HIS   J  1 155 ? 15.743  -58.149  -13.831 1.00 53.60 ? 155 HIS   J NE2 1 
ATOM   12716 N  N   . GLU   J  1 156 ? 19.014  -57.431  -19.446 1.00 52.27 ? 156 GLU   J N   1 
ATOM   12717 C  CA  . GLU   J  1 156 ? 19.408  -56.907  -20.757 1.00 64.41 ? 156 GLU   J CA  1 
ATOM   12718 C  C   . GLU   J  1 156 ? 18.561  -55.684  -21.107 1.00 58.68 ? 156 GLU   J C   1 
ATOM   12719 O  O   . GLU   J  1 156 ? 17.459  -55.526  -20.578 1.00 55.95 ? 156 GLU   J O   1 
ATOM   12720 C  CB  . GLU   J  1 156 ? 19.261  -57.980  -21.843 1.00 56.91 ? 156 GLU   J CB  1 
ATOM   12721 C  CG  . GLU   J  1 156 ? 20.138  -59.199  -21.615 1.00 46.50 ? 156 GLU   J CG  1 
ATOM   12722 C  CD  . GLU   J  1 156 ? 20.201  -60.128  -22.806 1.00 61.65 ? 156 GLU   J CD  1 
ATOM   12723 O  OE1 . GLU   J  1 156 ? 20.174  -59.640  -23.957 1.00 59.68 ? 156 GLU   J OE1 1 
ATOM   12724 O  OE2 . GLU   J  1 156 ? 20.284  -61.356  -22.584 1.00 59.99 ? 156 GLU   J OE2 1 
ATOM   12725 N  N   . MET   K  1 1   ? -9.201  -94.924  -23.940 1.00 40.39 ? 1   MET   K N   1 
ATOM   12726 C  CA  . MET   K  1 1   ? -8.220  -96.036  -23.937 1.00 41.72 ? 1   MET   K CA  1 
ATOM   12727 C  C   . MET   K  1 1   ? -7.905  -96.366  -22.483 1.00 44.69 ? 1   MET   K C   1 
ATOM   12728 O  O   . MET   K  1 1   ? -7.363  -95.538  -21.755 1.00 46.98 ? 1   MET   K O   1 
ATOM   12729 C  CB  . MET   K  1 1   ? -6.962  -95.655  -24.700 1.00 44.81 ? 1   MET   K CB  1 
ATOM   12730 C  CG  . MET   K  1 1   ? -6.034  -96.824  -24.974 1.00 49.91 ? 1   MET   K CG  1 
ATOM   12731 S  SD  . MET   K  1 1   ? -4.516  -96.335  -25.824 1.00 52.94 ? 1   MET   K SD  1 
ATOM   12732 C  CE  . MET   K  1 1   ? -3.584  -95.644  -24.460 1.00 50.87 ? 1   MET   K CE  1 
ATOM   12733 N  N   . LYS   K  1 2   ? -8.278  -97.560  -22.046 1.00 49.43 ? 2   LYS   K N   1 
ATOM   12734 C  CA  . LYS   K  1 2   ? -8.097  -97.922  -20.648 1.00 45.04 ? 2   LYS   K CA  1 
ATOM   12735 C  C   . LYS   K  1 2   ? -6.620  -97.871  -20.295 1.00 41.86 ? 2   LYS   K C   1 
ATOM   12736 O  O   . LYS   K  1 2   ? -5.802  -98.569  -20.897 1.00 49.41 ? 2   LYS   K O   1 
ATOM   12737 C  CB  . LYS   K  1 2   ? -8.678  -99.312  -20.377 1.00 50.05 ? 2   LYS   K CB  1 
ATOM   12738 N  N   . GLY   K  1 3   ? -6.275  -97.043  -19.304 1.00 42.93 ? 3   GLY   K N   1 
ATOM   12739 C  CA  . GLY   K  1 3   ? -4.902  -96.890  -18.879 1.00 46.46 ? 3   GLY   K CA  1 
ATOM   12740 C  C   . GLY   K  1 3   ? -4.532  -97.768  -17.680 1.00 39.02 ? 3   GLY   K C   1 
ATOM   12741 O  O   . GLY   K  1 3   ? -5.361  -98.426  -17.070 1.00 46.19 ? 3   GLY   K O   1 
ATOM   12742 N  N   . ASP   K  1 4   ? -3.238  -97.776  -17.387 1.00 43.88 ? 4   ASP   K N   1 
ATOM   12743 C  CA  . ASP   K  1 4   ? -2.703  -98.456  -16.215 1.00 42.99 ? 4   ASP   K CA  1 
ATOM   12744 C  C   . ASP   K  1 4   ? -3.177  -97.734  -14.957 1.00 51.20 ? 4   ASP   K C   1 
ATOM   12745 O  O   . ASP   K  1 4   ? -3.117  -96.504  -14.877 1.00 46.53 ? 4   ASP   K O   1 
ATOM   12746 C  CB  . ASP   K  1 4   ? -1.178  -98.467  -16.304 1.00 43.17 ? 4   ASP   K CB  1 
ATOM   12747 C  CG  . ASP   K  1 4   ? -0.504  -99.136  -15.123 1.00 47.63 ? 4   ASP   K CG  1 
ATOM   12748 O  OD1 . ASP   K  1 4   ? -0.337  -100.373 -15.144 1.00 47.28 ? 4   ASP   K OD1 1 
ATOM   12749 O  OD2 . ASP   K  1 4   ? -0.083  -98.414  -14.201 1.00 48.88 ? 4   ASP   K OD2 1 
ATOM   12750 N  N   . LYS   K  1 5   ? -3.666  -98.496  -13.976 1.00 43.15 ? 5   LYS   K N   1 
ATOM   12751 C  CA  . LYS   K  1 5   ? -4.240  -97.879  -12.783 1.00 46.86 ? 5   LYS   K CA  1 
ATOM   12752 C  C   . LYS   K  1 5   ? -3.202  -97.039  -12.050 1.00 40.45 ? 5   LYS   K C   1 
ATOM   12753 O  O   . LYS   K  1 5   ? -3.473  -95.907  -11.635 1.00 36.96 ? 5   LYS   K O   1 
ATOM   12754 C  CB  . LYS   K  1 5   ? -4.815  -98.954  -11.852 1.00 43.76 ? 5   LYS   K CB  1 
ATOM   12755 C  CG  . LYS   K  1 5   ? -5.676  -98.402  -10.731 1.00 49.65 ? 5   LYS   K CG  1 
ATOM   12756 N  N   . LYS   K  1 6   ? -2.008  -97.585  -11.859 1.00 40.38 ? 6   LYS   K N   1 
ATOM   12757 C  CA  . LYS   K  1 6   ? -1.000  -96.854  -11.115 1.00 37.80 ? 6   LYS   K CA  1 
ATOM   12758 C  C   . LYS   K  1 6   ? -0.484  -95.649  -11.897 1.00 48.73 ? 6   LYS   K C   1 
ATOM   12759 O  O   . LYS   K  1 6   ? -0.137  -94.630  -11.291 1.00 42.67 ? 6   LYS   K O   1 
ATOM   12760 C  CB  . LYS   K  1 6   ? 0.142   -97.800  -10.732 1.00 41.66 ? 6   LYS   K CB  1 
ATOM   12761 C  CG  . LYS   K  1 6   ? 1.234   -97.163  -9.923  1.00 46.47 ? 6   LYS   K CG  1 
ATOM   12762 C  CD  . LYS   K  1 6   ? 0.755   -96.801  -8.532  1.00 48.69 ? 6   LYS   K CD  1 
ATOM   12763 N  N   . VAL   K  1 7   ? -0.408  -95.731  -13.229 1.00 49.50 ? 7   VAL   K N   1 
ATOM   12764 C  CA  . VAL   K  1 7   ? -0.030  -94.543  -13.996 1.00 47.27 ? 7   VAL   K CA  1 
ATOM   12765 C  C   . VAL   K  1 7   ? -0.992  -93.407  -13.694 1.00 33.47 ? 7   VAL   K C   1 
ATOM   12766 O  O   . VAL   K  1 7   ? -0.580  -92.272  -13.429 1.00 38.63 ? 7   VAL   K O   1 
ATOM   12767 C  CB  . VAL   K  1 7   ? 0.019   -94.848  -15.505 1.00 47.65 ? 7   VAL   K CB  1 
ATOM   12768 C  CG1 . VAL   K  1 7   ? -0.003  -93.547  -16.320 1.00 41.98 ? 7   VAL   K CG1 1 
ATOM   12769 C  CG2 . VAL   K  1 7   ? 1.278   -95.635  -15.824 1.00 47.83 ? 7   VAL   K CG2 1 
ATOM   12770 N  N   . ILE   K  1 8   ? -2.293  -93.712  -13.687 1.00 39.25 ? 8   ILE   K N   1 
ATOM   12771 C  CA  . ILE   K  1 8   ? -3.301  -92.687  -13.440 1.00 43.98 ? 8   ILE   K CA  1 
ATOM   12772 C  C   . ILE   K  1 8   ? -3.144  -92.117  -12.043 1.00 41.62 ? 8   ILE   K C   1 
ATOM   12773 O  O   . ILE   K  1 8   ? -3.286  -90.908  -11.838 1.00 32.60 ? 8   ILE   K O   1 
ATOM   12774 C  CB  . ILE   K  1 8   ? -4.714  -93.252  -13.673 1.00 38.16 ? 8   ILE   K CB  1 
ATOM   12775 C  CG1 . ILE   K  1 8   ? -4.931  -93.517  -15.166 1.00 39.52 ? 8   ILE   K CG1 1 
ATOM   12776 C  CG2 . ILE   K  1 8   ? -5.780  -92.289  -13.120 1.00 46.78 ? 8   ILE   K CG2 1 
ATOM   12777 C  CD1 . ILE   K  1 8   ? -6.219  -94.283  -15.484 1.00 39.41 ? 8   ILE   K CD1 1 
ATOM   12778 N  N   . GLN   K  1 9   ? -2.824  -92.970  -11.061 1.00 37.33 ? 9   GLN   K N   1 
ATOM   12779 C  CA  . GLN   K  1 9   ? -2.599  -92.477  -9.708  1.00 36.75 ? 9   GLN   K CA  1 
ATOM   12780 C  C   . GLN   K  1 9   ? -1.400  -91.537  -9.666  1.00 39.84 ? 9   GLN   K C   1 
ATOM   12781 O  O   . GLN   K  1 9   ? -1.446  -90.485  -9.014  1.00 37.44 ? 9   GLN   K O   1 
ATOM   12782 C  CB  . GLN   K  1 9   ? -2.415  -93.657  -8.739  1.00 37.45 ? 9   GLN   K CB  1 
ATOM   12783 C  CG  . GLN   K  1 9   ? -3.655  -94.536  -8.631  1.00 37.12 ? 9   GLN   K CG  1 
ATOM   12784 C  CD  . GLN   K  1 9   ? -3.419  -95.799  -7.803  1.00 45.80 ? 9   GLN   K CD  1 
ATOM   12785 O  OE1 . GLN   K  1 9   ? -2.329  -96.367  -7.799  1.00 44.91 ? 9   GLN   K OE1 1 
ATOM   12786 N  NE2 . GLN   K  1 9   ? -4.444  -96.231  -7.094  1.00 50.94 ? 9   GLN   K NE2 1 
ATOM   12787 N  N   . HIS   K  1 10  ? -0.324  -91.891  -10.371 1.00 39.81 ? 10  HIS   K N   1 
ATOM   12788 C  CA  . HIS   K  1 10  ? 0.807   -90.983  -10.503 1.00 34.00 ? 10  HIS   K CA  1 
ATOM   12789 C  C   . HIS   K  1 10  ? 0.362   -89.668  -11.145 1.00 33.71 ? 10  HIS   K C   1 
ATOM   12790 O  O   . HIS   K  1 10  ? 0.684   -88.584  -10.644 1.00 31.56 ? 10  HIS   K O   1 
ATOM   12791 C  CB  . HIS   K  1 10  ? 1.923   -91.645  -11.318 1.00 40.44 ? 10  HIS   K CB  1 
ATOM   12792 C  CG  . HIS   K  1 10  ? 2.858   -92.493  -10.507 1.00 40.24 ? 10  HIS   K CG  1 
ATOM   12793 N  ND1 . HIS   K  1 10  ? 3.727   -91.959  -9.577  1.00 37.38 ? 10  HIS   K ND1 1 
ATOM   12794 C  CD2 . HIS   K  1 10  ? 3.072   -93.833  -10.501 1.00 33.91 ? 10  HIS   K CD2 1 
ATOM   12795 C  CE1 . HIS   K  1 10  ? 4.424   -92.937  -9.023  1.00 44.73 ? 10  HIS   K CE1 1 
ATOM   12796 N  NE2 . HIS   K  1 10  ? 4.047   -94.082  -9.567  1.00 46.86 ? 10  HIS   K NE2 1 
ATOM   12797 N  N   . LEU   K  1 11  ? -0.409  -89.745  -12.243 1.00 38.10 ? 11  LEU   K N   1 
ATOM   12798 C  CA  . LEU   K  1 11  ? -0.856  -88.524  -12.911 1.00 33.15 ? 11  LEU   K CA  1 
ATOM   12799 C  C   . LEU   K  1 11  ? -1.694  -87.663  -11.975 1.00 35.82 ? 11  LEU   K C   1 
ATOM   12800 O  O   . LEU   K  1 11  ? -1.548  -86.436  -11.949 1.00 36.55 ? 11  LEU   K O   1 
ATOM   12801 C  CB  . LEU   K  1 11  ? -1.637  -88.855  -14.182 1.00 33.29 ? 11  LEU   K CB  1 
ATOM   12802 C  CG  . LEU   K  1 11  ? -0.871  -89.567  -15.310 1.00 38.08 ? 11  LEU   K CG  1 
ATOM   12803 C  CD1 . LEU   K  1 11  ? -1.820  -89.839  -16.517 1.00 38.01 ? 11  LEU   K CD1 1 
ATOM   12804 C  CD2 . LEU   K  1 11  ? 0.361   -88.806  -15.739 1.00 39.58 ? 11  LEU   K CD2 1 
ATOM   12805 N  N   . ASN   K  1 12  ? -2.577  -88.282  -11.192 1.00 38.40 ? 12  ASN   K N   1 
ATOM   12806 C  CA  . ASN   K  1 12  ? -3.362  -87.491  -10.250 1.00 38.32 ? 12  ASN   K CA  1 
ATOM   12807 C  C   . ASN   K  1 12  ? -2.503  -86.928  -9.131  1.00 34.76 ? 12  ASN   K C   1 
ATOM   12808 O  O   . ASN   K  1 12  ? -2.814  -85.858  -8.596  1.00 38.33 ? 12  ASN   K O   1 
ATOM   12809 C  CB  . ASN   K  1 12  ? -4.513  -88.324  -9.678  1.00 32.99 ? 12  ASN   K CB  1 
ATOM   12810 C  CG  . ASN   K  1 12  ? -5.802  -88.066  -10.395 1.00 37.59 ? 12  ASN   K CG  1 
ATOM   12811 O  OD1 . ASN   K  1 12  ? -6.074  -86.932  -10.810 1.00 38.29 ? 12  ASN   K OD1 1 
ATOM   12812 N  ND2 . ASN   K  1 12  ? -6.613  -89.112  -10.565 1.00 36.59 ? 12  ASN   K ND2 1 
ATOM   12813 N  N   . LYS   K  1 13  ? -1.427  -87.613  -8.755  1.00 37.94 ? 13  LYS   K N   1 
ATOM   12814 C  CA  . LYS   K  1 13  ? -0.537  -87.030  -7.764  1.00 35.27 ? 13  LYS   K CA  1 
ATOM   12815 C  C   . LYS   K  1 13  ? 0.149   -85.788  -8.321  1.00 42.41 ? 13  LYS   K C   1 
ATOM   12816 O  O   . LYS   K  1 13  ? 0.218   -84.757  -7.639  1.00 35.60 ? 13  LYS   K O   1 
ATOM   12817 C  CB  . LYS   K  1 13  ? 0.496   -88.052  -7.296  1.00 34.31 ? 13  LYS   K CB  1 
ATOM   12818 C  CG  . LYS   K  1 13  ? 1.435   -87.491  -6.262  1.00 35.72 ? 13  LYS   K CG  1 
ATOM   12819 C  CD  . LYS   K  1 13  ? 2.369   -88.533  -5.638  1.00 42.36 ? 13  LYS   K CD  1 
ATOM   12820 C  CE  . LYS   K  1 13  ? 3.156   -87.901  -4.504  1.00 44.56 ? 13  LYS   K CE  1 
ATOM   12821 N  NZ  . LYS   K  1 13  ? 4.152   -88.781  -3.809  1.00 53.98 ? 13  LYS   K NZ  1 
ATOM   12822 N  N   . ILE   K  1 14  ? 0.682   -85.875  -9.554  1.00 38.45 ? 14  ILE   K N   1 
ATOM   12823 C  CA  . ILE   K  1 14  ? 1.347   -84.725  -10.178 1.00 36.01 ? 14  ILE   K CA  1 
ATOM   12824 C  C   . ILE   K  1 14  ? 0.363   -83.569  -10.326 1.00 34.75 ? 14  ILE   K C   1 
ATOM   12825 O  O   . ILE   K  1 14  ? 0.704   -82.404  -10.078 1.00 34.80 ? 14  ILE   K O   1 
ATOM   12826 C  CB  . ILE   K  1 14  ? 1.952   -85.116  -11.545 1.00 39.26 ? 14  ILE   K CB  1 
ATOM   12827 C  CG1 . ILE   K  1 14  ? 2.929   -86.298  -11.416 1.00 35.21 ? 14  ILE   K CG1 1 
ATOM   12828 C  CG2 . ILE   K  1 14  ? 2.670   -83.918  -12.188 1.00 37.00 ? 14  ILE   K CG2 1 
ATOM   12829 C  CD1 . ILE   K  1 14  ? 4.050   -86.086  -10.444 1.00 40.17 ? 14  ILE   K CD1 1 
ATOM   12830 N  N   . LEU   K  1 15  ? -0.865  -83.877  -10.748 1.00 36.01 ? 15  LEU   K N   1 
ATOM   12831 C  CA  . LEU   K  1 15  ? -1.926  -82.873  -10.821 1.00 34.24 ? 15  LEU   K CA  1 
ATOM   12832 C  C   . LEU   K  1 15  ? -2.157  -82.208  -9.464  1.00 42.92 ? 15  LEU   K C   1 
ATOM   12833 O  O   . LEU   K  1 15  ? -2.346  -80.984  -9.385  1.00 33.18 ? 15  LEU   K O   1 
ATOM   12834 C  CB  . LEU   K  1 15  ? -3.204  -83.536  -11.328 1.00 31.47 ? 15  LEU   K CB  1 
ATOM   12835 C  CG  . LEU   K  1 15  ? -4.503  -82.705  -11.393 1.00 28.25 ? 15  LEU   K CG  1 
ATOM   12836 C  CD1 . LEU   K  1 15  ? -4.284  -81.475  -12.238 1.00 29.50 ? 15  LEU   K CD1 1 
ATOM   12837 C  CD2 . LEU   K  1 15  ? -5.660  -83.536  -11.943 1.00 33.85 ? 15  LEU   K CD2 1 
ATOM   12838 N  N   . GLY   K  1 16  ? -2.155  -82.997  -8.384  1.00 37.41 ? 16  GLY   K N   1 
ATOM   12839 C  CA  . GLY   K  1 16  ? -2.279  -82.414  -7.063  1.00 31.99 ? 16  GLY   K CA  1 
ATOM   12840 C  C   . GLY   K  1 16  ? -1.204  -81.381  -6.782  1.00 36.81 ? 16  GLY   K C   1 
ATOM   12841 O  O   . GLY   K  1 16  ? -1.489  -80.296  -6.254  1.00 35.64 ? 16  GLY   K O   1 
ATOM   12842 N  N   . ASN   K  1 17  ? 0.053   -81.712  -7.106  1.00 32.75 ? 17  ASN   K N   1 
ATOM   12843 C  CA  . ASN   K  1 17  ? 1.146   -80.756  -6.952  1.00 34.52 ? 17  ASN   K CA  1 
ATOM   12844 C  C   . ASN   K  1 17  ? 0.913   -79.510  -7.788  1.00 34.42 ? 17  ASN   K C   1 
ATOM   12845 O  O   . ASN   K  1 17  ? 1.227   -78.400  -7.349  1.00 32.56 ? 17  ASN   K O   1 
ATOM   12846 C  CB  . ASN   K  1 17  ? 2.488   -81.381  -7.362  1.00 32.39 ? 17  ASN   K CB  1 
ATOM   12847 C  CG  . ASN   K  1 17  ? 2.913   -82.496  -6.445  1.00 40.29 ? 17  ASN   K CG  1 
ATOM   12848 O  OD1 . ASN   K  1 17  ? 2.490   -82.549  -5.294  1.00 36.30 ? 17  ASN   K OD1 1 
ATOM   12849 N  ND2 . ASN   K  1 17  ? 3.761   -83.400  -6.949  1.00 40.58 ? 17  ASN   K ND2 1 
ATOM   12850 N  N   . GLU   K  1 18  ? 0.398   -79.682  -9.013  1.00 30.03 ? 18  GLU   K N   1 
ATOM   12851 C  CA  . GLU   K  1 18  ? 0.098   -78.534  -9.869  1.00 42.29 ? 18  GLU   K CA  1 
ATOM   12852 C  C   . GLU   K  1 18  ? -0.958  -77.637  -9.246  1.00 31.12 ? 18  GLU   K C   1 
ATOM   12853 O  O   . GLU   K  1 18  ? -0.873  -76.404  -9.343  1.00 30.86 ? 18  GLU   K O   1 
ATOM   12854 C  CB  . GLU   K  1 18  ? -0.371  -79.011  -11.245 1.00 38.41 ? 18  GLU   K CB  1 
ATOM   12855 C  CG  . GLU   K  1 18  ? 0.703   -79.807  -12.003 1.00 45.15 ? 18  GLU   K CG  1 
ATOM   12856 C  CD  . GLU   K  1 18  ? 1.813   -78.935  -12.526 1.00 48.17 ? 18  GLU   K CD  1 
ATOM   12857 O  OE1 . GLU   K  1 18  ? 1.734   -77.704  -12.308 1.00 49.95 ? 18  GLU   K OE1 1 
ATOM   12858 O  OE2 . GLU   K  1 18  ? 2.756   -79.473  -13.154 1.00 47.49 ? 18  GLU   K OE2 1 
ATOM   12859 N  N   . LEU   K  1 19  ? -1.972  -78.232  -8.614  1.00 29.14 ? 19  LEU   K N   1 
ATOM   12860 C  CA  . LEU   K  1 19  ? -3.032  -77.415  -8.048  1.00 32.02 ? 19  LEU   K CA  1 
ATOM   12861 C  C   . LEU   K  1 19  ? -2.499  -76.552  -6.915  1.00 36.19 ? 19  LEU   K C   1 
ATOM   12862 O  O   . LEU   K  1 19  ? -2.898  -75.388  -6.776  1.00 32.82 ? 19  LEU   K O   1 
ATOM   12863 C  CB  . LEU   K  1 19  ? -4.181  -78.297  -7.571  1.00 33.63 ? 19  LEU   K CB  1 
ATOM   12864 C  CG  . LEU   K  1 19  ? -4.894  -79.040  -8.699  1.00 35.71 ? 19  LEU   K CG  1 
ATOM   12865 C  CD1 . LEU   K  1 19  ? -5.948  -79.960  -8.107  1.00 45.35 ? 19  LEU   K CD1 1 
ATOM   12866 C  CD2 . LEU   K  1 19  ? -5.530  -78.074  -9.691  1.00 39.97 ? 19  LEU   K CD2 1 
ATOM   12867 N  N   . ILE   K  1 20  ? -1.601  -77.110  -6.093  1.00 29.02 ? 20  ILE   K N   1 
ATOM   12868 C  CA  . ILE   K  1 20  ? -0.953  -76.330  -5.047  1.00 31.91 ? 20  ILE   K CA  1 
ATOM   12869 C  C   . ILE   K  1 20  ? -0.174  -75.190  -5.669  1.00 27.34 ? 20  ILE   K C   1 
ATOM   12870 O  O   . ILE   K  1 20  ? -0.296  -74.026  -5.274  1.00 31.25 ? 20  ILE   K O   1 
ATOM   12871 C  CB  . ILE   K  1 20  ? -0.025  -77.228  -4.215  1.00 30.27 ? 20  ILE   K CB  1 
ATOM   12872 C  CG1 . ILE   K  1 20  ? -0.830  -78.254  -3.426  1.00 30.52 ? 20  ILE   K CG1 1 
ATOM   12873 C  CG2 . ILE   K  1 20  ? 0.851   -76.369  -3.282  1.00 30.03 ? 20  ILE   K CG2 1 
ATOM   12874 C  CD1 . ILE   K  1 20  ? 0.032   -79.384  -2.844  1.00 38.20 ? 20  ILE   K CD1 1 
ATOM   12875 N  N   . ALA   K  1 21  ? 0.646   -75.525  -6.660  1.00 31.19 ? 21  ALA   K N   1 
ATOM   12876 C  CA  . ALA   K  1 21  ? 1.510   -74.545  -7.307  1.00 30.46 ? 21  ALA   K CA  1 
ATOM   12877 C  C   . ALA   K  1 21  ? 0.705   -73.412  -7.930  1.00 26.62 ? 21  ALA   K C   1 
ATOM   12878 O  O   . ALA   K  1 21  ? 1.067   -72.239  -7.793  1.00 26.14 ? 21  ALA   K O   1 
ATOM   12879 C  CB  . ALA   K  1 21  ? 2.356   -75.256  -8.363  1.00 32.02 ? 21  ALA   K CB  1 
ATOM   12880 N  N   . ILE   K  1 22  ? -0.386  -73.739  -8.621  1.00 27.37 ? 22  ILE   K N   1 
ATOM   12881 C  CA  . ILE   K  1 22  ? -1.202  -72.694  -9.241  1.00 28.52 ? 22  ILE   K CA  1 
ATOM   12882 C  C   . ILE   K  1 22  ? -1.596  -71.658  -8.196  1.00 31.22 ? 22  ILE   K C   1 
ATOM   12883 O  O   . ILE   K  1 22  ? -1.381  -70.447  -8.361  1.00 27.95 ? 22  ILE   K O   1 
ATOM   12884 C  CB  . ILE   K  1 22  ? -2.445  -73.307  -9.908  1.00 29.05 ? 22  ILE   K CB  1 
ATOM   12885 C  CG1 . ILE   K  1 22  ? -2.088  -74.089  -11.177 1.00 33.66 ? 22  ILE   K CG1 1 
ATOM   12886 C  CG2 . ILE   K  1 22  ? -3.434  -72.205  -10.274 1.00 26.53 ? 22  ILE   K CG2 1 
ATOM   12887 C  CD1 . ILE   K  1 22  ? -3.166  -75.059  -11.584 1.00 26.67 ? 22  ILE   K CD1 1 
ATOM   12888 N  N   . ASN   K  1 23  ? -2.145  -72.134  -7.080  1.00 26.58 ? 23  ASN   K N   1 
ATOM   12889 C  CA  . ASN   K  1 23  ? -2.651  -71.233  -6.043  1.00 32.03 ? 23  ASN   K CA  1 
ATOM   12890 C  C   . ASN   K  1 23  ? -1.532  -70.526  -5.297  1.00 25.95 ? 23  ASN   K C   1 
ATOM   12891 O  O   . ASN   K  1 23  ? -1.646  -69.331  -4.988  1.00 27.18 ? 23  ASN   K O   1 
ATOM   12892 C  CB  . ASN   K  1 23  ? -3.533  -72.008  -5.059  1.00 32.11 ? 23  ASN   K CB  1 
ATOM   12893 C  CG  . ASN   K  1 23  ? -4.885  -72.349  -5.652  1.00 33.54 ? 23  ASN   K CG  1 
ATOM   12894 O  OD1 . ASN   K  1 23  ? -5.049  -72.352  -6.876  1.00 31.84 ? 23  ASN   K OD1 1 
ATOM   12895 N  ND2 . ASN   K  1 23  ? -5.866  -72.650  -4.781  1.00 30.15 ? 23  ASN   K ND2 1 
ATOM   12896 N  N   . GLN   K  1 24  ? -0.461  -71.243  -4.957  1.00 26.65 ? 24  GLN   K N   1 
ATOM   12897 C  CA  . GLN   K  1 24  ? 0.652   -70.603  -4.259  1.00 23.90 ? 24  GLN   K CA  1 
ATOM   12898 C  C   . GLN   K  1 24  ? 1.295   -69.517  -5.123  1.00 30.55 ? 24  GLN   K C   1 
ATOM   12899 O  O   . GLN   K  1 24  ? 1.576   -68.408  -4.644  1.00 26.79 ? 24  GLN   K O   1 
ATOM   12900 C  CB  . GLN   K  1 24  ? 1.678   -71.666  -3.861  1.00 30.07 ? 24  GLN   K CB  1 
ATOM   12901 C  CG  . GLN   K  1 24  ? 2.952   -71.148  -3.203  1.00 30.18 ? 24  GLN   K CG  1 
ATOM   12902 C  CD  . GLN   K  1 24  ? 3.842   -72.309  -2.768  1.00 35.87 ? 24  GLN   K CD  1 
ATOM   12903 O  OE1 . GLN   K  1 24  ? 3.342   -73.308  -2.253  1.00 34.13 ? 24  GLN   K OE1 1 
ATOM   12904 N  NE2 . GLN   K  1 24  ? 5.149   -72.193  -2.992  1.00 31.28 ? 24  GLN   K NE2 1 
ATOM   12905 N  N   . TYR   K  1 25  ? 1.557   -69.825  -6.397  1.00 26.96 ? 25  TYR   K N   1 
ATOM   12906 C  CA  . TYR   K  1 25  ? 2.170   -68.822  -7.270  1.00 28.30 ? 25  TYR   K CA  1 
ATOM   12907 C  C   . TYR   K  1 25  ? 1.212   -67.664  -7.550  1.00 25.71 ? 25  TYR   K C   1 
ATOM   12908 O  O   . TYR   K  1 25  ? 1.641   -66.507  -7.610  1.00 27.49 ? 25  TYR   K O   1 
ATOM   12909 C  CB  . TYR   K  1 25  ? 2.644   -69.450  -8.584  1.00 29.35 ? 25  TYR   K CB  1 
ATOM   12910 C  CG  . TYR   K  1 25  ? 3.613   -70.603  -8.422  1.00 32.57 ? 25  TYR   K CG  1 
ATOM   12911 C  CD1 . TYR   K  1 25  ? 4.251   -70.852  -7.197  1.00 31.53 ? 25  TYR   K CD1 1 
ATOM   12912 C  CD2 . TYR   K  1 25  ? 3.871   -71.467  -9.471  1.00 32.45 ? 25  TYR   K CD2 1 
ATOM   12913 C  CE1 . TYR   K  1 25  ? 5.099   -71.917  -7.036  1.00 30.78 ? 25  TYR   K CE1 1 
ATOM   12914 C  CE2 . TYR   K  1 25  ? 4.738   -72.545  -9.319  1.00 39.22 ? 25  TYR   K CE2 1 
ATOM   12915 C  CZ  . TYR   K  1 25  ? 5.352   -72.761  -8.094  1.00 36.85 ? 25  TYR   K CZ  1 
ATOM   12916 O  OH  . TYR   K  1 25  ? 6.216   -73.830  -7.911  1.00 37.47 ? 25  TYR   K OH  1 
ATOM   12917 N  N   . PHE   K  1 26  ? -0.089  -67.936  -7.693  1.00 27.37 ? 26  PHE   K N   1 
ATOM   12918 C  CA  . PHE   K  1 26  ? -1.003  -66.827  -7.959  1.00 24.75 ? 26  PHE   K CA  1 
ATOM   12919 C  C   . PHE   K  1 26  ? -1.090  -65.899  -6.758  1.00 22.28 ? 26  PHE   K C   1 
ATOM   12920 O  O   . PHE   K  1 26  ? -1.048  -64.669  -6.908  1.00 25.58 ? 26  PHE   K O   1 
ATOM   12921 C  CB  . PHE   K  1 26  ? -2.387  -67.342  -8.363  1.00 24.83 ? 26  PHE   K CB  1 
ATOM   12922 C  CG  . PHE   K  1 26  ? -3.157  -66.354  -9.163  1.00 23.36 ? 26  PHE   K CG  1 
ATOM   12923 C  CD1 . PHE   K  1 26  ? -3.884  -65.349  -8.549  1.00 27.74 ? 26  PHE   K CD1 1 
ATOM   12924 C  CD2 . PHE   K  1 26  ? -3.096  -66.381  -10.531 1.00 25.16 ? 26  PHE   K CD2 1 
ATOM   12925 C  CE1 . PHE   K  1 26  ? -4.558  -64.401  -9.306  1.00 28.73 ? 26  PHE   K CE1 1 
ATOM   12926 C  CE2 . PHE   K  1 26  ? -3.772  -65.448  -11.294 1.00 26.99 ? 26  PHE   K CE2 1 
ATOM   12927 C  CZ  . PHE   K  1 26  ? -4.492  -64.443  -10.674 1.00 26.77 ? 26  PHE   K CZ  1 
ATOM   12928 N  N   . LEU   K  1 27  ? -1.119  -66.458  -5.550  1.00 26.99 ? 27  LEU   K N   1 
ATOM   12929 C  CA  . LEU   K  1 27  ? -1.131  -65.605  -4.366  1.00 24.16 ? 27  LEU   K CA  1 
ATOM   12930 C  C   . LEU   K  1 27  ? 0.187   -64.848  -4.217  1.00 26.97 ? 27  LEU   K C   1 
ATOM   12931 O  O   . LEU   K  1 27  ? 0.185   -63.639  -3.948  1.00 30.35 ? 27  LEU   K O   1 
ATOM   12932 C  CB  . LEU   K  1 27  ? -1.447  -66.434  -3.115  1.00 23.22 ? 27  LEU   K CB  1 
ATOM   12933 C  CG  . LEU   K  1 27  ? -1.491  -65.627  -1.803  1.00 29.51 ? 27  LEU   K CG  1 
ATOM   12934 C  CD1 . LEU   K  1 27  ? -2.485  -64.484  -1.917  1.00 29.04 ? 27  LEU   K CD1 1 
ATOM   12935 C  CD2 . LEU   K  1 27  ? -1.842  -66.515  -0.581  1.00 30.72 ? 27  LEU   K CD2 1 
ATOM   12936 N  N   . HIS   K  1 28  ? 1.334   -65.534  -4.363  1.00 25.18 ? 28  HIS   K N   1 
ATOM   12937 C  CA  . HIS   K  1 28  ? 2.615   -64.820  -4.335  1.00 26.11 ? 28  HIS   K CA  1 
ATOM   12938 C  C   . HIS   K  1 28  ? 2.642   -63.677  -5.350  1.00 24.59 ? 28  HIS   K C   1 
ATOM   12939 O  O   . HIS   K  1 28  ? 3.081   -62.566  -5.036  1.00 26.72 ? 28  HIS   K O   1 
ATOM   12940 C  CB  . HIS   K  1 28  ? 3.776   -65.795  -4.590  1.00 27.89 ? 28  HIS   K CB  1 
ATOM   12941 C  CG  . HIS   K  1 28  ? 4.153   -66.613  -3.386  1.00 26.55 ? 28  HIS   K CG  1 
ATOM   12942 N  ND1 . HIS   K  1 28  ? 4.907   -67.761  -3.474  1.00 29.49 ? 28  HIS   K ND1 1 
ATOM   12943 C  CD2 . HIS   K  1 28  ? 3.873   -66.448  -2.072  1.00 33.50 ? 28  HIS   K CD2 1 
ATOM   12944 C  CE1 . HIS   K  1 28  ? 5.084   -68.267  -2.269  1.00 29.09 ? 28  HIS   K CE1 1 
ATOM   12945 N  NE2 . HIS   K  1 28  ? 4.464   -67.493  -1.395  1.00 33.99 ? 28  HIS   K NE2 1 
ATOM   12946 N  N   . SER   K  1 29  ? 2.154   -63.932  -6.567  1.00 24.21 ? 29  SER   K N   1 
ATOM   12947 C  CA  . SER   K  1 29  ? 2.109   -62.895  -7.595  1.00 28.38 ? 29  SER   K CA  1 
ATOM   12948 C  C   . SER   K  1 29  ? 1.354   -61.672  -7.101  1.00 30.04 ? 29  SER   K C   1 
ATOM   12949 O  O   . SER   K  1 29  ? 1.846   -60.534  -7.184  1.00 24.75 ? 29  SER   K O   1 
ATOM   12950 C  CB  . SER   K  1 29  ? 1.442   -63.448  -8.852  1.00 26.34 ? 29  SER   K CB  1 
ATOM   12951 O  OG  . SER   K  1 29  ? 1.102   -62.413  -9.772  1.00 25.59 ? 29  SER   K OG  1 
ATOM   12952 N  N   . ARG   K  1 30  ? 0.148   -61.894  -6.575  1.00 24.53 ? 30  ARG   K N   1 
ATOM   12953 C  CA  . ARG   K  1 30  ? -0.701  -60.772  -6.184  1.00 27.37 ? 30  ARG   K CA  1 
ATOM   12954 C  C   . ARG   K  1 30  ? -0.182  -60.075  -4.922  1.00 27.14 ? 30  ARG   K C   1 
ATOM   12955 O  O   . ARG   K  1 30  ? -0.367  -58.859  -4.762  1.00 24.20 ? 30  ARG   K O   1 
ATOM   12956 C  CB  . ARG   K  1 30  ? -2.125  -61.283  -6.034  1.00 26.37 ? 30  ARG   K CB  1 
ATOM   12957 C  CG  . ARG   K  1 30  ? -2.888  -61.151  -7.369  1.00 26.20 ? 30  ARG   K CG  1 
ATOM   12958 C  CD  . ARG   K  1 30  ? -2.152  -61.727  -8.585  1.00 31.32 ? 30  ARG   K CD  1 
ATOM   12959 N  NE  . ARG   K  1 30  ? -2.890  -61.380  -9.789  1.00 28.30 ? 30  ARG   K NE  1 
ATOM   12960 C  CZ  . ARG   K  1 30  ? -2.355  -61.007  -10.948 1.00 27.85 ? 30  ARG   K CZ  1 
ATOM   12961 N  NH1 . ARG   K  1 30  ? -1.040  -60.970  -11.137 1.00 28.49 ? 30  ARG   K NH1 1 
ATOM   12962 N  NH2 . ARG   K  1 30  ? -3.159  -60.624  -11.934 1.00 28.46 ? 30  ARG   K NH2 1 
ATOM   12963 N  N   . MET   K  1 31  ? 0.492   -60.808  -4.033  1.00 25.67 ? 31  MET   K N   1 
ATOM   12964 C  CA  . MET   K  1 31  ? 1.175   -60.167  -2.915  1.00 28.12 ? 31  MET   K CA  1 
ATOM   12965 C  C   . MET   K  1 31  ? 2.256   -59.221  -3.419  1.00 27.83 ? 31  MET   K C   1 
ATOM   12966 O  O   . MET   K  1 31  ? 2.347   -58.077  -2.960  1.00 27.24 ? 31  MET   K O   1 
ATOM   12967 C  CB  . MET   K  1 31  ? 1.780   -61.220  -1.974  1.00 24.39 ? 31  MET   K CB  1 
ATOM   12968 C  CG  . MET   K  1 31  ? 0.748   -62.052  -1.164  1.00 28.73 ? 31  MET   K CG  1 
ATOM   12969 S  SD  . MET   K  1 31  ? 1.416   -63.580  -0.446  1.00 28.86 ? 31  MET   K SD  1 
ATOM   12970 C  CE  . MET   K  1 31  ? 2.594   -62.979  0.742   1.00 26.46 ? 31  MET   K CE  1 
ATOM   12971 N  N   . TRP   K  1 32  ? 3.095   -59.687  -4.363  1.00 26.05 ? 32  TRP   K N   1 
ATOM   12972 C  CA  . TRP   K  1 32  ? 4.178   -58.850  -4.865  1.00 23.50 ? 32  TRP   K CA  1 
ATOM   12973 C  C   . TRP   K  1 32  ? 3.624   -57.622  -5.563  1.00 26.02 ? 32  TRP   K C   1 
ATOM   12974 O  O   . TRP   K  1 32  ? 4.120   -56.506  -5.351  1.00 25.55 ? 32  TRP   K O   1 
ATOM   12975 C  CB  . TRP   K  1 32  ? 5.123   -59.643  -5.806  1.00 25.99 ? 32  TRP   K CB  1 
ATOM   12976 C  CG  . TRP   K  1 32  ? 6.230   -60.403  -5.073  1.00 28.69 ? 32  TRP   K CG  1 
ATOM   12977 C  CD1 . TRP   K  1 32  ? 6.999   -59.930  -4.052  1.00 25.05 ? 32  TRP   K CD1 1 
ATOM   12978 C  CD2 . TRP   K  1 32  ? 6.673   -61.750  -5.310  1.00 24.72 ? 32  TRP   K CD2 1 
ATOM   12979 N  NE1 . TRP   K  1 32  ? 7.890   -60.887  -3.646  1.00 26.18 ? 32  TRP   K NE1 1 
ATOM   12980 C  CE2 . TRP   K  1 32  ? 7.713   -62.013  -4.397  1.00 29.72 ? 32  TRP   K CE2 1 
ATOM   12981 C  CE3 . TRP   K  1 32  ? 6.295   -62.752  -6.205  1.00 28.55 ? 32  TRP   K CE3 1 
ATOM   12982 C  CZ2 . TRP   K  1 32  ? 8.375   -63.247  -4.342  1.00 24.36 ? 32  TRP   K CZ2 1 
ATOM   12983 C  CZ3 . TRP   K  1 32  ? 6.954   -63.975  -6.147  1.00 25.75 ? 32  TRP   K CZ3 1 
ATOM   12984 C  CH2 . TRP   K  1 32  ? 7.981   -64.209  -5.223  1.00 29.30 ? 32  TRP   K CH2 1 
ATOM   12985 N  N   . ASN   K  1 33  ? 2.565   -57.798  -6.366  1.00 29.38 ? 33  ASN   K N   1 
ATOM   12986 C  CA  . ASN   K  1 33  ? 1.947   -56.646  -7.021  1.00 27.35 ? 33  ASN   K CA  1 
ATOM   12987 C  C   . ASN   K  1 33  ? 1.408   -55.661  -5.992  1.00 26.80 ? 33  ASN   K C   1 
ATOM   12988 O  O   . ASN   K  1 33  ? 1.606   -54.451  -6.115  1.00 30.57 ? 33  ASN   K O   1 
ATOM   12989 C  CB  . ASN   K  1 33  ? 0.820   -57.094  -7.941  1.00 28.14 ? 33  ASN   K CB  1 
ATOM   12990 C  CG  . ASN   K  1 33  ? 1.312   -57.660  -9.257  1.00 29.86 ? 33  ASN   K CG  1 
ATOM   12991 O  OD1 . ASN   K  1 33  ? 2.465   -57.465  -9.641  1.00 28.07 ? 33  ASN   K OD1 1 
ATOM   12992 N  ND2 . ASN   K  1 33  ? 0.407   -58.319  -9.992  1.00 26.75 ? 33  ASN   K ND2 1 
ATOM   12993 N  N   . ASP   K  1 34  ? 0.727   -56.167  -4.964  1.00 25.53 ? 34  ASP   K N   1 
ATOM   12994 C  CA  . ASP   K  1 34  ? 0.232   -55.304  -3.883  1.00 28.90 ? 34  ASP   K CA  1 
ATOM   12995 C  C   . ASP   K  1 34  ? 1.369   -54.533  -3.201  1.00 27.70 ? 34  ASP   K C   1 
ATOM   12996 O  O   . ASP   K  1 34  ? 1.185   -53.381  -2.796  1.00 30.94 ? 34  ASP   K O   1 
ATOM   12997 C  CB  . ASP   K  1 34  ? -0.517  -56.160  -2.862  1.00 27.41 ? 34  ASP   K CB  1 
ATOM   12998 C  CG  . ASP   K  1 34  ? -1.010  -55.364  -1.657  1.00 32.41 ? 34  ASP   K CG  1 
ATOM   12999 O  OD1 . ASP   K  1 34  ? -1.716  -54.374  -1.853  1.00 40.09 ? 34  ASP   K OD1 1 
ATOM   13000 O  OD2 . ASP   K  1 34  ? -0.714  -55.767  -0.521  1.00 35.14 ? 34  ASP   K OD2 1 
ATOM   13001 N  N   . TRP   K  1 35  ? 2.555   -55.147  -3.064  1.00 27.32 ? 35  TRP   K N   1 
ATOM   13002 C  CA  . TRP   K  1 35  ? 3.715   -54.464  -2.483  1.00 24.77 ? 35  TRP   K CA  1 
ATOM   13003 C  C   . TRP   K  1 35  ? 4.431   -53.519  -3.462  1.00 27.10 ? 35  TRP   K C   1 
ATOM   13004 O  O   . TRP   K  1 35  ? 5.403   -52.853  -3.072  1.00 29.00 ? 35  TRP   K O   1 
ATOM   13005 C  CB  . TRP   K  1 35  ? 4.724   -55.498  -1.940  1.00 27.74 ? 35  TRP   K CB  1 
ATOM   13006 C  CG  . TRP   K  1 35  ? 4.139   -56.386  -0.855  1.00 33.18 ? 35  TRP   K CG  1 
ATOM   13007 C  CD1 . TRP   K  1 35  ? 2.983   -56.180  -0.160  1.00 37.32 ? 35  TRP   K CD1 1 
ATOM   13008 C  CD2 . TRP   K  1 35  ? 4.667   -57.644  -0.384  1.00 34.16 ? 35  TRP   K CD2 1 
ATOM   13009 N  NE1 . TRP   K  1 35  ? 2.759   -57.223  0.722   1.00 37.48 ? 35  TRP   K NE1 1 
ATOM   13010 C  CE2 . TRP   K  1 35  ? 3.782   -58.129  0.607   1.00 35.75 ? 35  TRP   K CE2 1 
ATOM   13011 C  CE3 . TRP   K  1 35  ? 5.799   -58.396  -0.698  1.00 34.97 ? 35  TRP   K CE3 1 
ATOM   13012 C  CZ2 . TRP   K  1 35  ? 3.994   -59.338  1.277   1.00 38.56 ? 35  TRP   K CZ2 1 
ATOM   13013 C  CZ3 . TRP   K  1 35  ? 6.007   -59.599  -0.033  1.00 38.93 ? 35  TRP   K CZ3 1 
ATOM   13014 C  CH2 . TRP   K  1 35  ? 5.108   -60.056  0.941   1.00 32.93 ? 35  TRP   K CH2 1 
ATOM   13015 N  N   . GLY   K  1 36  ? 4.007   -53.451  -4.714  1.00 25.08 ? 36  GLY   K N   1 
ATOM   13016 C  CA  . GLY   K  1 36  ? 4.676   -52.610  -5.693  1.00 25.59 ? 36  GLY   K CA  1 
ATOM   13017 C  C   . GLY   K  1 36  ? 5.904   -53.225  -6.327  1.00 29.08 ? 36  GLY   K C   1 
ATOM   13018 O  O   . GLY   K  1 36  ? 6.687   -52.517  -6.973  1.00 29.46 ? 36  GLY   K O   1 
ATOM   13019 N  N   . LEU   K  1 37  ? 6.107   -54.513  -6.147  1.00 27.34 ? 37  LEU   K N   1 
ATOM   13020 C  CA  . LEU   K  1 37  ? 7.160   -55.247  -6.843  1.00 26.81 ? 37  LEU   K CA  1 
ATOM   13021 C  C   . LEU   K  1 37  ? 6.572   -55.922  -8.084  1.00 26.57 ? 37  LEU   K C   1 
ATOM   13022 O  O   . LEU   K  1 37  ? 6.411   -57.136  -8.166  1.00 27.16 ? 37  LEU   K O   1 
ATOM   13023 C  CB  . LEU   K  1 37  ? 7.803   -56.246  -5.877  1.00 24.29 ? 37  LEU   K CB  1 
ATOM   13024 C  CG  . LEU   K  1 37  ? 8.332   -55.505  -4.646  1.00 26.02 ? 37  LEU   K CG  1 
ATOM   13025 C  CD1 . LEU   K  1 37  ? 8.632   -56.435  -3.512  1.00 29.28 ? 37  LEU   K CD1 1 
ATOM   13026 C  CD2 . LEU   K  1 37  ? 9.562   -54.664  -5.037  1.00 28.24 ? 37  LEU   K CD2 1 
ATOM   13027 N  N   . LYS   K  1 38  ? 6.278   -55.093  -9.094  1.00 24.51 ? 38  LYS   K N   1 
ATOM   13028 C  CA  . LYS   K  1 38  ? 5.452   -55.551  -10.213 1.00 30.38 ? 38  LYS   K CA  1 
ATOM   13029 C  C   . LYS   K  1 38  ? 6.192   -56.498  -11.148 1.00 28.79 ? 38  LYS   K C   1 
ATOM   13030 O  O   . LYS   K  1 38  ? 5.563   -57.329  -11.813 1.00 28.01 ? 38  LYS   K O   1 
ATOM   13031 C  CB  . LYS   K  1 38  ? 4.931   -54.337  -10.983 1.00 32.37 ? 38  LYS   K CB  1 
ATOM   13032 C  CG  . LYS   K  1 38  ? 4.232   -53.304  -10.086 1.00 38.72 ? 38  LYS   K CG  1 
ATOM   13033 C  CD  . LYS   K  1 38  ? 2.736   -53.523  -10.015 1.00 42.24 ? 38  LYS   K CD  1 
ATOM   13034 C  CE  . LYS   K  1 38  ? 2.034   -52.472  -9.130  1.00 50.59 ? 38  LYS   K CE  1 
ATOM   13035 N  NZ  . LYS   K  1 38  ? 0.746   -52.001  -9.711  1.00 62.96 ? 38  LYS   K NZ  1 
ATOM   13036 N  N   . ARG   K  1 39  ? 7.515   -56.398  -11.232 1.00 24.83 ? 39  ARG   K N   1 
ATOM   13037 C  CA  . ARG   K  1 39  ? 8.238   -57.333  -12.085 1.00 27.25 ? 39  ARG   K CA  1 
ATOM   13038 C  C   . ARG   K  1 39  ? 8.199   -58.739  -11.498 1.00 24.19 ? 39  ARG   K C   1 
ATOM   13039 O  O   . ARG   K  1 39  ? 8.059   -59.725  -12.234 1.00 23.66 ? 39  ARG   K O   1 
ATOM   13040 C  CB  . ARG   K  1 39  ? 9.668   -56.850  -12.270 1.00 26.78 ? 39  ARG   K CB  1 
ATOM   13041 C  CG  . ARG   K  1 39  ? 10.385  -57.484  -13.420 1.00 38.90 ? 39  ARG   K CG  1 
ATOM   13042 C  CD  . ARG   K  1 39  ? 11.885  -57.254  -13.283 1.00 43.12 ? 39  ARG   K CD  1 
ATOM   13043 N  NE  . ARG   K  1 39  ? 12.616  -57.566  -14.502 1.00 48.92 ? 39  ARG   K NE  1 
ATOM   13044 C  CZ  . ARG   K  1 39  ? 12.920  -56.686  -15.448 1.00 44.79 ? 39  ARG   K CZ  1 
ATOM   13045 N  NH1 . ARG   K  1 39  ? 12.565  -55.409  -15.361 1.00 51.38 ? 39  ARG   K NH1 1 
ATOM   13046 N  NH2 . ARG   K  1 39  ? 13.590  -57.099  -16.513 1.00 44.23 ? 39  ARG   K NH2 1 
ATOM   13047 N  N   . LEU   K  1 40  ? 8.342   -58.851  -10.176 1.00 25.46 ? 40  LEU   K N   1 
ATOM   13048 C  CA  . LEU   K  1 40  ? 8.151   -60.139  -9.522  1.00 23.60 ? 40  LEU   K CA  1 
ATOM   13049 C  C   . LEU   K  1 40  ? 6.720   -60.622  -9.691  1.00 24.53 ? 40  LEU   K C   1 
ATOM   13050 O  O   . LEU   K  1 40  ? 6.463   -61.798  -10.001 1.00 25.90 ? 40  LEU   K O   1 
ATOM   13051 C  CB  . LEU   K  1 40  ? 8.491   -60.018  -8.040  1.00 28.21 ? 40  LEU   K CB  1 
ATOM   13052 C  CG  . LEU   K  1 40  ? 9.967   -60.173  -7.690  1.00 28.95 ? 40  LEU   K CG  1 
ATOM   13053 C  CD1 . LEU   K  1 40  ? 10.255  -59.742  -6.233  1.00 22.72 ? 40  LEU   K CD1 1 
ATOM   13054 C  CD2 . LEU   K  1 40  ? 10.321  -61.623  -7.940  1.00 34.95 ? 40  LEU   K CD2 1 
ATOM   13055 N  N   . GLY   K  1 41  ? 5.766   -59.721  -9.478  1.00 27.32 ? 41  GLY   K N   1 
ATOM   13056 C  CA  . GLY   K  1 41  ? 4.365   -60.099  -9.649  1.00 28.84 ? 41  GLY   K CA  1 
ATOM   13057 C  C   . GLY   K  1 41  ? 4.079   -60.657  -11.027 1.00 28.49 ? 41  GLY   K C   1 
ATOM   13058 O  O   . GLY   K  1 41  ? 3.438   -61.700  -11.164 1.00 27.97 ? 41  GLY   K O   1 
ATOM   13059 N  N   . ALA   K  1 42  ? 4.578   -59.981  -12.073 1.00 29.35 ? 42  ALA   K N   1 
ATOM   13060 C  CA  . ALA   K  1 42  ? 4.291   -60.428  -13.425 1.00 28.45 ? 42  ALA   K CA  1 
ATOM   13061 C  C   . ALA   K  1 42  ? 4.937   -61.776  -13.697 1.00 27.95 ? 42  ALA   K C   1 
ATOM   13062 O  O   . ALA   K  1 42  ? 4.317   -62.657  -14.305 1.00 25.21 ? 42  ALA   K O   1 
ATOM   13063 C  CB  . ALA   K  1 42  ? 4.777   -59.396  -14.446 1.00 30.24 ? 42  ALA   K CB  1 
ATOM   13064 N  N   . HIS   K  1 43  ? 6.201   -61.947  -13.279 1.00 28.47 ? 43  HIS   K N   1 
ATOM   13065 C  CA  . HIS   K  1 43  ? 6.885   -63.210  -13.526 1.00 26.35 ? 43  HIS   K CA  1 
ATOM   13066 C  C   . HIS   K  1 43  ? 6.202   -64.357  -12.786 1.00 23.49 ? 43  HIS   K C   1 
ATOM   13067 O  O   . HIS   K  1 43  ? 5.988   -65.438  -13.352 1.00 29.09 ? 43  HIS   K O   1 
ATOM   13068 C  CB  . HIS   K  1 43  ? 8.363   -63.100  -13.114 1.00 30.07 ? 43  HIS   K CB  1 
ATOM   13069 C  CG  . HIS   K  1 43  ? 9.192   -64.230  -13.611 1.00 36.96 ? 43  HIS   K CG  1 
ATOM   13070 N  ND1 . HIS   K  1 43  ? 10.067  -64.099  -14.671 1.00 40.67 ? 43  HIS   K ND1 1 
ATOM   13071 C  CD2 . HIS   K  1 43  ? 9.252   -65.526  -13.227 1.00 35.99 ? 43  HIS   K CD2 1 
ATOM   13072 C  CE1 . HIS   K  1 43  ? 10.634  -65.268  -14.913 1.00 38.78 ? 43  HIS   K CE1 1 
ATOM   13073 N  NE2 . HIS   K  1 43  ? 10.154  -66.151  -14.057 1.00 40.62 ? 43  HIS   K NE2 1 
ATOM   13074 N  N   . GLU   K  1 44  ? 5.841   -64.135  -11.524 1.00 26.32 ? 44  GLU   K N   1 
ATOM   13075 C  CA  . GLU   K  1 44  ? 5.154   -65.167  -10.758 1.00 28.03 ? 44  GLU   K CA  1 
ATOM   13076 C  C   . GLU   K  1 44  ? 3.781   -65.494  -11.359 1.00 28.73 ? 44  GLU   K C   1 
ATOM   13077 O  O   . GLU   K  1 44  ? 3.359   -66.656  -11.355 1.00 26.98 ? 44  GLU   K O   1 
ATOM   13078 C  CB  . GLU   K  1 44  ? 5.045   -64.695  -9.302  1.00 28.35 ? 44  GLU   K CB  1 
ATOM   13079 C  CG  . GLU   K  1 44  ? 4.531   -65.742  -8.312  1.00 27.45 ? 44  GLU   K CG  1 
ATOM   13080 C  CD  . GLU   K  1 44  ? 5.587   -66.772  -7.937  1.00 33.58 ? 44  GLU   K CD  1 
ATOM   13081 O  OE1 . GLU   K  1 44  ? 6.576   -66.882  -8.664  1.00 31.19 ? 44  GLU   K OE1 1 
ATOM   13082 O  OE2 . GLU   K  1 44  ? 5.428   -67.477  -6.924  1.00 30.73 ? 44  GLU   K OE2 1 
ATOM   13083 N  N   . TYR   K  1 45  ? 3.092   -64.495  -11.913 1.00 28.58 ? 45  TYR   K N   1 
ATOM   13084 C  CA  . TYR   K  1 45  ? 1.819   -64.746  -12.597 1.00 27.06 ? 45  TYR   K CA  1 
ATOM   13085 C  C   . TYR   K  1 45  ? 2.017   -65.712  -13.761 1.00 31.46 ? 45  TYR   K C   1 
ATOM   13086 O  O   . TYR   K  1 45  ? 1.303   -66.719  -13.883 1.00 26.65 ? 45  TYR   K O   1 
ATOM   13087 C  CB  . TYR   K  1 45  ? 1.223   -63.412  -13.069 1.00 26.02 ? 45  TYR   K CB  1 
ATOM   13088 C  CG  . TYR   K  1 45  ? 0.039   -63.502  -14.030 1.00 25.82 ? 45  TYR   K CG  1 
ATOM   13089 C  CD1 . TYR   K  1 45  ? -1.248  -63.605  -13.560 1.00 33.45 ? 45  TYR   K CD1 1 
ATOM   13090 C  CD2 . TYR   K  1 45  ? 0.230   -63.481  -15.410 1.00 29.42 ? 45  TYR   K CD2 1 
ATOM   13091 C  CE1 . TYR   K  1 45  ? -2.321  -63.691  -14.428 1.00 29.33 ? 45  TYR   K CE1 1 
ATOM   13092 C  CE2 . TYR   K  1 45  ? -0.843  -63.558  -16.290 1.00 32.44 ? 45  TYR   K CE2 1 
ATOM   13093 C  CZ  . TYR   K  1 45  ? -2.115  -63.656  -15.785 1.00 35.42 ? 45  TYR   K CZ  1 
ATOM   13094 O  OH  . TYR   K  1 45  ? -3.205  -63.755  -16.632 1.00 35.50 ? 45  TYR   K OH  1 
ATOM   13095 N  N   . HIS   K  1 46  ? 3.028   -65.448  -14.602 1.00 30.31 ? 46  HIS   K N   1 
ATOM   13096 C  CA  . HIS   K  1 46  ? 3.317   -66.335  -15.725 1.00 27.84 ? 46  HIS   K CA  1 
ATOM   13097 C  C   . HIS   K  1 46  ? 3.699   -67.736  -15.254 1.00 31.70 ? 46  HIS   K C   1 
ATOM   13098 O  O   . HIS   K  1 46  ? 3.378   -68.716  -15.929 1.00 29.07 ? 46  HIS   K O   1 
ATOM   13099 C  CB  . HIS   K  1 46  ? 4.415   -65.707  -16.593 1.00 28.24 ? 46  HIS   K CB  1 
ATOM   13100 C  CG  . HIS   K  1 46  ? 3.938   -64.486  -17.320 1.00 41.15 ? 46  HIS   K CG  1 
ATOM   13101 N  ND1 . HIS   K  1 46  ? 2.874   -64.517  -18.200 1.00 43.88 ? 46  HIS   K ND1 1 
ATOM   13102 C  CD2 . HIS   K  1 46  ? 4.335   -63.192  -17.258 1.00 41.54 ? 46  HIS   K CD2 1 
ATOM   13103 C  CE1 . HIS   K  1 46  ? 2.654   -63.302  -18.670 1.00 39.84 ? 46  HIS   K CE1 1 
ATOM   13104 N  NE2 . HIS   K  1 46  ? 3.519   -62.476  -18.104 1.00 47.79 ? 46  HIS   K NE2 1 
ATOM   13105 N  N   . GLU   K  1 47  ? 4.378   -67.855  -14.109 1.00 29.64 ? 47  GLU   K N   1 
ATOM   13106 C  CA  . GLU   K  1 47  ? 4.634   -69.184  -13.545 1.00 34.76 ? 47  GLU   K CA  1 
ATOM   13107 C  C   . GLU   K  1 47  ? 3.334   -69.886  -13.155 1.00 32.51 ? 47  GLU   K C   1 
ATOM   13108 O  O   . GLU   K  1 47  ? 3.182   -71.096  -13.380 1.00 28.81 ? 47  GLU   K O   1 
ATOM   13109 C  CB  . GLU   K  1 47  ? 5.545   -69.080  -12.328 1.00 33.00 ? 47  GLU   K CB  1 
ATOM   13110 C  CG  . GLU   K  1 47  ? 6.897   -68.420  -12.589 1.00 39.05 ? 47  GLU   K CG  1 
ATOM   13111 C  CD  . GLU   K  1 47  ? 7.867   -69.336  -13.298 1.00 47.69 ? 47  GLU   K CD  1 
ATOM   13112 O  OE1 . GLU   K  1 47  ? 7.446   -70.424  -13.742 1.00 53.51 ? 47  GLU   K OE1 1 
ATOM   13113 O  OE2 . GLU   K  1 47  ? 9.059   -68.973  -13.403 1.00 55.55 ? 47  GLU   K OE2 1 
ATOM   13114 N  N   . SER   K  1 48  ? 2.384   -69.147  -12.569 1.00 28.20 ? 48  SER   K N   1 
ATOM   13115 C  CA  . SER   K  1 48  ? 1.074   -69.725  -12.254 1.00 28.77 ? 48  SER   K CA  1 
ATOM   13116 C  C   . SER   K  1 48  ? 0.360   -70.203  -13.519 1.00 28.39 ? 48  SER   K C   1 
ATOM   13117 O  O   . SER   K  1 48  ? -0.222  -71.297  -13.553 1.00 25.58 ? 48  SER   K O   1 
ATOM   13118 C  CB  . SER   K  1 48  ? 0.208   -68.699  -11.502 1.00 29.43 ? 48  SER   K CB  1 
ATOM   13119 O  OG  . SER   K  1 48  ? -1.011  -69.280  -10.999 1.00 28.19 ? 48  SER   K OG  1 
ATOM   13120 N  N   . ILE   K  1 49  ? 0.373   -69.377  -14.571 1.00 30.68 ? 49  ILE   K N   1 
ATOM   13121 C  CA  . ILE   K  1 49  ? -0.269  -69.760  -15.827 1.00 28.04 ? 49  ILE   K CA  1 
ATOM   13122 C  C   . ILE   K  1 49  ? 0.360   -71.033  -16.381 1.00 28.84 ? 49  ILE   K C   1 
ATOM   13123 O  O   . ILE   K  1 49  ? -0.346  -71.925  -16.875 1.00 30.03 ? 49  ILE   K O   1 
ATOM   13124 C  CB  . ILE   K  1 49  ? -0.160  -68.615  -16.858 1.00 31.03 ? 49  ILE   K CB  1 
ATOM   13125 C  CG1 . ILE   K  1 49  ? -0.851  -67.350  -16.375 1.00 32.11 ? 49  ILE   K CG1 1 
ATOM   13126 C  CG2 . ILE   K  1 49  ? -0.670  -69.075  -18.212 1.00 31.11 ? 49  ILE   K CG2 1 
ATOM   13127 C  CD1 . ILE   K  1 49  ? -2.342  -67.504  -16.193 1.00 33.03 ? 49  ILE   K CD1 1 
ATOM   13128 N  N   . ASP   K  1 50  ? 1.695   -71.126  -16.335 1.00 28.33 ? 50  ASP   K N   1 
ATOM   13129 C  CA  . ASP   K  1 50  ? 2.373   -72.319  -16.848 1.00 28.14 ? 50  ASP   K CA  1 
ATOM   13130 C  C   . ASP   K  1 50  ? 1.884   -73.575  -16.138 1.00 28.55 ? 50  ASP   K C   1 
ATOM   13131 O  O   . ASP   K  1 50  ? 1.652   -74.601  -16.783 1.00 32.09 ? 50  ASP   K O   1 
ATOM   13132 C  CB  . ASP   K  1 50  ? 3.893   -72.208  -16.684 1.00 38.63 ? 50  ASP   K CB  1 
ATOM   13133 C  CG  . ASP   K  1 50  ? 4.503   -71.196  -17.603 1.00 53.27 ? 50  ASP   K CG  1 
ATOM   13134 O  OD1 . ASP   K  1 50  ? 3.939   -70.970  -18.705 1.00 55.77 ? 50  ASP   K OD1 1 
ATOM   13135 O  OD2 . ASP   K  1 50  ? 5.555   -70.632  -17.209 1.00 59.40 ? 50  ASP   K OD2 1 
ATOM   13136 N  N   . GLU   K  1 51  ? 1.736   -73.518  -14.801 1.00 29.01 ? 51  GLU   K N   1 
ATOM   13137 C  CA  . GLU   K  1 51  ? 1.175   -74.659  -14.064 1.00 31.21 ? 51  GLU   K CA  1 
ATOM   13138 C  C   . GLU   K  1 51  ? -0.292  -74.923  -14.415 1.00 26.96 ? 51  GLU   K C   1 
ATOM   13139 O  O   . GLU   K  1 51  ? -0.740  -76.083  -14.420 1.00 29.70 ? 51  GLU   K O   1 
ATOM   13140 C  CB  . GLU   K  1 51  ? 1.321   -74.427  -12.564 1.00 32.25 ? 51  GLU   K CB  1 
ATOM   13141 C  CG  . GLU   K  1 51  ? 2.753   -74.207  -12.107 1.00 35.97 ? 51  GLU   K CG  1 
ATOM   13142 C  CD  . GLU   K  1 51  ? 3.669   -75.388  -12.400 1.00 39.05 ? 51  GLU   K CD  1 
ATOM   13143 O  OE1 . GLU   K  1 51  ? 3.574   -76.415  -11.709 1.00 66.09 ? 51  GLU   K OE1 1 
ATOM   13144 O  OE2 . GLU   K  1 51  ? 4.501   -75.289  -13.302 1.00 42.98 ? 51  GLU   K OE2 1 
ATOM   13145 N  N   . MET   K  1 52  ? -1.077  -73.870  -14.664 1.00 27.95 ? 52  MET   K N   1 
ATOM   13146 C  CA  . MET   K  1 52  ? -2.435  -74.086  -15.166 1.00 30.71 ? 52  MET   K CA  1 
ATOM   13147 C  C   . MET   K  1 52  ? -2.430  -74.874  -16.476 1.00 32.49 ? 52  MET   K C   1 
ATOM   13148 O  O   . MET   K  1 52  ? -3.260  -75.764  -16.680 1.00 28.23 ? 52  MET   K O   1 
ATOM   13149 C  CB  . MET   K  1 52  ? -3.148  -72.749  -15.368 1.00 31.22 ? 52  MET   K CB  1 
ATOM   13150 C  CG  . MET   K  1 52  ? -3.413  -71.985  -14.084 1.00 29.27 ? 52  MET   K CG  1 
ATOM   13151 S  SD  . MET   K  1 52  ? -4.020  -70.343  -14.449 1.00 31.25 ? 52  MET   K SD  1 
ATOM   13152 C  CE  . MET   K  1 52  ? -3.578  -69.450  -12.959 1.00 25.16 ? 52  MET   K CE  1 
ATOM   13153 N  N   . LYS   K  1 53  ? -1.515  -74.548  -17.387 1.00 30.10 ? 53  LYS   K N   1 
ATOM   13154 C  CA  . LYS   K  1 53  ? -1.435  -75.280  -18.648 1.00 30.32 ? 53  LYS   K CA  1 
ATOM   13155 C  C   . LYS   K  1 53  ? -0.985  -76.724  -18.426 1.00 29.90 ? 53  LYS   K C   1 
ATOM   13156 O  O   . LYS   K  1 53  ? -1.485  -77.645  -19.091 1.00 29.66 ? 53  LYS   K O   1 
ATOM   13157 C  CB  . LYS   K  1 53  ? -0.482  -74.552  -19.604 1.00 31.32 ? 53  LYS   K CB  1 
ATOM   13158 C  CG  . LYS   K  1 53  ? -0.984  -73.161  -20.046 1.00 29.78 ? 53  LYS   K CG  1 
ATOM   13159 C  CD  . LYS   K  1 53  ? 0.128   -72.360  -20.697 1.00 46.45 ? 53  LYS   K CD  1 
ATOM   13160 C  CE  . LYS   K  1 53  ? -0.399  -71.334  -21.711 1.00 56.10 ? 53  LYS   K CE  1 
ATOM   13161 N  NZ  . LYS   K  1 53  ? 0.742   -70.623  -22.400 1.00 62.62 ? 53  LYS   K NZ  1 
ATOM   13162 N  N   . HIS   K  1 54  ? -0.032  -76.940  -17.508 1.00 30.33 ? 54  HIS   K N   1 
ATOM   13163 C  CA  . HIS   K  1 54  ? 0.363   -78.309  -17.168 1.00 31.20 ? 54  HIS   K CA  1 
ATOM   13164 C  C   . HIS   K  1 54  ? -0.815  -79.105  -16.631 1.00 29.69 ? 54  HIS   K C   1 
ATOM   13165 O  O   . HIS   K  1 54  ? -0.952  -80.293  -16.934 1.00 29.60 ? 54  HIS   K O   1 
ATOM   13166 C  CB  . HIS   K  1 54  ? 1.487   -78.320  -16.123 1.00 28.78 ? 54  HIS   K CB  1 
ATOM   13167 C  CG  . HIS   K  1 54  ? 2.746   -77.630  -16.558 1.00 28.29 ? 54  HIS   K CG  1 
ATOM   13168 N  ND1 . HIS   K  1 54  ? 3.108   -77.485  -17.875 1.00 32.17 ? 54  HIS   K ND1 1 
ATOM   13169 C  CD2 . HIS   K  1 54  ? 3.730   -77.051  -15.831 1.00 29.06 ? 54  HIS   K CD2 1 
ATOM   13170 C  CE1 . HIS   K  1 54  ? 4.256   -76.834  -17.946 1.00 32.81 ? 54  HIS   K CE1 1 
ATOM   13171 N  NE2 . HIS   K  1 54  ? 4.658   -76.569  -16.715 1.00 37.11 ? 54  HIS   K NE2 1 
ATOM   13172 N  N   . ALA   K  1 55  ? -1.656  -78.477  -15.795 1.00 29.96 ? 55  ALA   K N   1 
ATOM   13173 C  CA  . ALA   K  1 55  ? -2.769  -79.189  -15.175 1.00 33.74 ? 55  ALA   K CA  1 
ATOM   13174 C  C   . ALA   K  1 55  ? -3.831  -79.539  -16.200 1.00 35.35 ? 55  ALA   K C   1 
ATOM   13175 O  O   . ALA   K  1 55  ? -4.476  -80.592  -16.117 1.00 30.89 ? 55  ALA   K O   1 
ATOM   13176 C  CB  . ALA   K  1 55  ? -3.374  -78.336  -14.056 1.00 28.36 ? 55  ALA   K CB  1 
ATOM   13177 N  N   . ASP   K  1 56  ? -4.067  -78.633  -17.140 1.00 29.59 ? 56  ASP   K N   1 
ATOM   13178 C  CA  . ASP   K  1 56  ? -4.931  -78.937  -18.261 1.00 30.09 ? 56  ASP   K CA  1 
ATOM   13179 C  C   . ASP   K  1 56  ? -4.468  -80.213  -18.973 1.00 27.55 ? 56  ASP   K C   1 
ATOM   13180 O  O   . ASP   K  1 56  ? -5.275  -81.119  -19.234 1.00 31.56 ? 56  ASP   K O   1 
ATOM   13181 C  CB  . ASP   K  1 56  ? -4.933  -77.726  -19.205 1.00 30.64 ? 56  ASP   K CB  1 
ATOM   13182 C  CG  . ASP   K  1 56  ? -5.963  -77.828  -20.302 1.00 30.90 ? 56  ASP   K CG  1 
ATOM   13183 O  OD1 . ASP   K  1 56  ? -6.891  -78.653  -20.192 1.00 29.79 ? 56  ASP   K OD1 1 
ATOM   13184 O  OD2 . ASP   K  1 56  ? -5.845  -77.058  -21.279 1.00 37.23 ? 56  ASP   K OD2 1 
ATOM   13185 N  N   . LYS   K  1 57  ? -3.175  -80.286  -19.326 1.00 29.53 ? 57  LYS   K N   1 
ATOM   13186 C  CA  . LYS   K  1 57  ? -2.681  -81.440  -20.073 1.00 31.94 ? 57  LYS   K CA  1 
ATOM   13187 C  C   . LYS   K  1 57  ? -2.837  -82.717  -19.263 1.00 35.46 ? 57  LYS   K C   1 
ATOM   13188 O  O   . LYS   K  1 57  ? -3.201  -83.763  -19.812 1.00 33.51 ? 57  LYS   K O   1 
ATOM   13189 C  CB  . LYS   K  1 57  ? -1.214  -81.234  -20.491 1.00 32.22 ? 57  LYS   K CB  1 
ATOM   13190 C  CG  . LYS   K  1 57  ? -1.019  -80.180  -21.574 1.00 36.52 ? 57  LYS   K CG  1 
ATOM   13191 C  CD  . LYS   K  1 57  ? -2.065  -80.285  -22.675 1.00 47.09 ? 57  LYS   K CD  1 
ATOM   13192 C  CE  . LYS   K  1 57  ? -1.715  -79.434  -23.902 1.00 59.55 ? 57  LYS   K CE  1 
ATOM   13193 N  NZ  . LYS   K  1 57  ? -2.943  -79.216  -24.760 1.00 68.88 ? 57  LYS   K NZ  1 
ATOM   13194 N  N   . LEU   K  1 58  ? -2.596  -82.646  -17.949 1.00 31.57 ? 58  LEU   K N   1 
ATOM   13195 C  CA  . LEU   K  1 58  ? -2.747  -83.835  -17.114 1.00 30.15 ? 58  LEU   K CA  1 
ATOM   13196 C  C   . LEU   K  1 58  ? -4.199  -84.255  -17.025 1.00 30.68 ? 58  LEU   K C   1 
ATOM   13197 O  O   . LEU   K  1 58  ? -4.513  -85.447  -17.112 1.00 31.08 ? 58  LEU   K O   1 
ATOM   13198 C  CB  . LEU   K  1 58  ? -2.179  -83.587  -15.717 1.00 29.41 ? 58  LEU   K CB  1 
ATOM   13199 C  CG  . LEU   K  1 58  ? -0.680  -83.306  -15.601 1.00 32.37 ? 58  LEU   K CG  1 
ATOM   13200 C  CD1 . LEU   K  1 58  ? -0.378  -82.692  -14.255 1.00 41.17 ? 58  LEU   K CD1 1 
ATOM   13201 C  CD2 . LEU   K  1 58  ? 0.150   -84.560  -15.806 1.00 31.62 ? 58  LEU   K CD2 1 
ATOM   13202 N  N   . ILE   K  1 59  ? -5.099  -83.286  -16.840 1.00 28.17 ? 59  ILE   K N   1 
ATOM   13203 C  CA  . ILE   K  1 59  ? -6.516  -83.586  -16.810 1.00 32.16 ? 59  ILE   K CA  1 
ATOM   13204 C  C   . ILE   K  1 59  ? -6.929  -84.252  -18.110 1.00 40.59 ? 59  ILE   K C   1 
ATOM   13205 O  O   . ILE   K  1 59  ? -7.706  -85.218  -18.112 1.00 29.85 ? 59  ILE   K O   1 
ATOM   13206 C  CB  . ILE   K  1 59  ? -7.317  -82.300  -16.541 1.00 32.75 ? 59  ILE   K CB  1 
ATOM   13207 C  CG1 . ILE   K  1 59  ? -7.047  -81.818  -15.107 1.00 34.81 ? 59  ILE   K CG1 1 
ATOM   13208 C  CG2 . ILE   K  1 59  ? -8.753  -82.526  -16.789 1.00 29.64 ? 59  ILE   K CG2 1 
ATOM   13209 C  CD1 . ILE   K  1 59  ? -7.498  -80.418  -14.854 1.00 32.62 ? 59  ILE   K CD1 1 
ATOM   13210 N  N   . GLU   K  1 60  ? -6.399  -83.755  -19.235 1.00 31.88 ? 60  GLU   K N   1 
ATOM   13211 C  CA  . GLU   K  1 60  ? -6.773  -84.297  -20.533 1.00 29.31 ? 60  GLU   K CA  1 
ATOM   13212 C  C   . GLU   K  1 60  ? -6.223  -85.709  -20.709 1.00 27.28 ? 60  GLU   K C   1 
ATOM   13213 O  O   . GLU   K  1 60  ? -6.909  -86.596  -21.234 1.00 33.34 ? 60  GLU   K O   1 
ATOM   13214 C  CB  . GLU   K  1 60  ? -6.272  -83.351  -21.644 1.00 29.05 ? 60  GLU   K CB  1 
ATOM   13215 C  CG  . GLU   K  1 60  ? -7.049  -82.014  -21.632 1.00 32.91 ? 60  GLU   K CG  1 
ATOM   13216 C  CD  . GLU   K  1 60  ? -6.504  -81.004  -22.613 1.00 36.32 ? 60  GLU   K CD  1 
ATOM   13217 O  OE1 . GLU   K  1 60  ? -5.288  -80.984  -22.787 1.00 35.66 ? 60  GLU   K OE1 1 
ATOM   13218 O  OE2 . GLU   K  1 60  ? -7.285  -80.227  -23.198 1.00 34.61 ? 60  GLU   K OE2 1 
ATOM   13219 N  N   . ARG   K  1 61  ? -5.010  -85.945  -20.239 1.00 27.45 ? 61  ARG   K N   1 
ATOM   13220 C  CA  . ARG   K  1 61  ? -4.435  -87.278  -20.349 1.00 35.50 ? 61  ARG   K CA  1 
ATOM   13221 C  C   . ARG   K  1 61  ? -5.192  -88.274  -19.472 1.00 38.33 ? 61  ARG   K C   1 
ATOM   13222 O  O   . ARG   K  1 61  ? -5.510  -89.384  -19.921 1.00 35.61 ? 61  ARG   K O   1 
ATOM   13223 C  CB  . ARG   K  1 61  ? -2.957  -87.227  -19.975 1.00 32.06 ? 61  ARG   K CB  1 
ATOM   13224 C  CG  . ARG   K  1 61  ? -2.224  -88.546  -20.139 1.00 34.72 ? 61  ARG   K CG  1 
ATOM   13225 C  CD  . ARG   K  1 61  ? -2.222  -88.989  -21.580 1.00 38.84 ? 61  ARG   K CD  1 
ATOM   13226 N  NE  . ARG   K  1 61  ? -1.320  -90.114  -21.806 1.00 37.18 ? 61  ARG   K NE  1 
ATOM   13227 C  CZ  . ARG   K  1 61  ? -1.329  -90.858  -22.904 1.00 32.74 ? 61  ARG   K CZ  1 
ATOM   13228 N  NH1 . ARG   K  1 61  ? -2.073  -90.535  -23.955 1.00 37.19 ? 61  ARG   K NH1 1 
ATOM   13229 N  NH2 . ARG   K  1 61  ? -0.592  -91.963  -22.942 1.00 39.56 ? 61  ARG   K NH2 1 
ATOM   13230 N  N   . ILE   K  1 62  ? -5.486  -87.891  -18.217 1.00 31.54 ? 62  ILE   K N   1 
ATOM   13231 C  CA  . ILE   K  1 62  ? -6.213  -88.777  -17.302 1.00 36.89 ? 62  ILE   K CA  1 
ATOM   13232 C  C   . ILE   K  1 62  ? -7.544  -89.192  -17.902 1.00 36.77 ? 62  ILE   K C   1 
ATOM   13233 O  O   . ILE   K  1 62  ? -7.936  -90.368  -17.845 1.00 36.31 ? 62  ILE   K O   1 
ATOM   13234 C  CB  . ILE   K  1 62  ? -6.419  -88.102  -15.935 1.00 34.56 ? 62  ILE   K CB  1 
ATOM   13235 C  CG1 . ILE   K  1 62  ? -5.093  -87.949  -15.210 1.00 27.93 ? 62  ILE   K CG1 1 
ATOM   13236 C  CG2 . ILE   K  1 62  ? -7.431  -88.897  -15.101 1.00 40.39 ? 62  ILE   K CG2 1 
ATOM   13237 C  CD1 . ILE   K  1 62  ? -5.127  -86.957  -14.067 1.00 30.61 ? 62  ILE   K CD1 1 
ATOM   13238 N  N   . LEU   K  1 63  ? -8.281  -88.228  -18.457 1.00 33.40 ? 63  LEU   K N   1 
ATOM   13239 C  CA  . LEU   K  1 63  ? -9.580  -88.548  -19.013 1.00 30.03 ? 63  LEU   K CA  1 
ATOM   13240 C  C   . LEU   K  1 63  ? -9.437  -89.480  -20.211 1.00 37.89 ? 63  LEU   K C   1 
ATOM   13241 O  O   . LEU   K  1 63  ? -10.228 -90.409  -20.375 1.00 35.04 ? 63  LEU   K O   1 
ATOM   13242 C  CB  . LEU   K  1 63  ? -10.326 -87.265  -19.405 1.00 37.89 ? 63  LEU   K CB  1 
ATOM   13243 C  CG  . LEU   K  1 63  ? -10.878 -86.414  -18.257 1.00 32.08 ? 63  LEU   K CG  1 
ATOM   13244 C  CD1 . LEU   K  1 63  ? -11.323 -85.029  -18.731 1.00 33.53 ? 63  LEU   K CD1 1 
ATOM   13245 C  CD2 . LEU   K  1 63  ? -12.046 -87.128  -17.550 1.00 35.43 ? 63  LEU   K CD2 1 
ATOM   13246 N  N   . PHE   K  1 64  ? -8.408  -89.276  -21.038 1.00 38.18 ? 64  PHE   K N   1 
ATOM   13247 C  CA  . PHE   K  1 64  ? -8.235  -90.149  -22.199 1.00 40.78 ? 64  PHE   K CA  1 
ATOM   13248 C  C   . PHE   K  1 64  ? -7.921  -91.572  -21.755 1.00 35.48 ? 64  PHE   K C   1 
ATOM   13249 O  O   . PHE   K  1 64  ? -8.433  -92.537  -22.338 1.00 39.15 ? 64  PHE   K O   1 
ATOM   13250 C  CB  . PHE   K  1 64  ? -7.133  -89.611  -23.113 1.00 39.16 ? 64  PHE   K CB  1 
ATOM   13251 C  CG  . PHE   K  1 64  ? -6.647  -90.613  -24.132 1.00 35.28 ? 64  PHE   K CG  1 
ATOM   13252 C  CD1 . PHE   K  1 64  ? -7.501  -91.100  -25.106 1.00 31.56 ? 64  PHE   K CD1 1 
ATOM   13253 C  CD2 . PHE   K  1 64  ? -5.358  -91.067  -24.093 1.00 33.09 ? 64  PHE   K CD2 1 
ATOM   13254 C  CE1 . PHE   K  1 64  ? -7.056  -92.023  -26.042 1.00 40.07 ? 64  PHE   K CE1 1 
ATOM   13255 C  CE2 . PHE   K  1 64  ? -4.889  -91.997  -25.034 1.00 42.98 ? 64  PHE   K CE2 1 
ATOM   13256 C  CZ  . PHE   K  1 64  ? -5.728  -92.468  -26.005 1.00 32.80 ? 64  PHE   K CZ  1 
ATOM   13257 N  N   . LEU   K  1 65  ? -7.090  -91.713  -20.711 1.00 35.43 ? 65  LEU   K N   1 
ATOM   13258 C  CA  . LEU   K  1 65  ? -6.777  -93.007  -20.115 1.00 36.57 ? 65  LEU   K CA  1 
ATOM   13259 C  C   . LEU   K  1 65  ? -7.936  -93.570  -19.264 1.00 41.25 ? 65  LEU   K C   1 
ATOM   13260 O  O   . LEU   K  1 65  ? -7.767  -94.618  -18.639 1.00 39.46 ? 65  LEU   K O   1 
ATOM   13261 C  CB  . LEU   K  1 65  ? -5.484  -92.881  -19.298 1.00 37.09 ? 65  LEU   K CB  1 
ATOM   13262 C  CG  . LEU   K  1 65  ? -4.206  -92.633  -20.137 1.00 36.01 ? 65  LEU   K CG  1 
ATOM   13263 C  CD1 . LEU   K  1 65  ? -2.986  -92.404  -19.278 1.00 37.12 ? 65  LEU   K CD1 1 
ATOM   13264 C  CD2 . LEU   K  1 65  ? -3.979  -93.780  -21.088 1.00 38.76 ? 65  LEU   K CD2 1 
ATOM   13265 N  N   . GLU   K  1 66  ? -9.087  -92.892  -19.254 1.00 35.57 ? 66  GLU   K N   1 
ATOM   13266 C  CA  . GLU   K  1 66  ? -10.337 -93.300  -18.607 1.00 42.20 ? 66  GLU   K CA  1 
ATOM   13267 C  C   . GLU   K  1 66  ? -10.260 -93.292  -17.081 1.00 42.60 ? 66  GLU   K C   1 
ATOM   13268 O  O   . GLU   K  1 66  ? -11.018 -94.010  -16.409 1.00 39.97 ? 66  GLU   K O   1 
ATOM   13269 C  CB  . GLU   K  1 66  ? -10.801 -94.666  -19.128 1.00 42.55 ? 66  GLU   K CB  1 
ATOM   13270 C  CG  . GLU   K  1 66  ? -10.964 -94.633  -20.647 1.00 42.72 ? 66  GLU   K CG  1 
ATOM   13271 C  CD  . GLU   K  1 66  ? -11.484 -95.923  -21.235 1.00 48.71 ? 66  GLU   K CD  1 
ATOM   13272 O  OE1 . GLU   K  1 66  ? -12.122 -96.715  -20.507 1.00 47.87 ? 66  GLU   K OE1 1 
ATOM   13273 O  OE2 . GLU   K  1 66  ? -11.257 -96.132  -22.442 1.00 46.78 ? 66  GLU   K OE2 1 
ATOM   13274 N  N   . GLY   K  1 67  ? -9.366  -92.481  -16.515 1.00 39.72 ? 67  GLY   K N   1 
ATOM   13275 C  CA  . GLY   K  1 67  ? -9.378  -92.195  -15.097 1.00 39.60 ? 67  GLY   K CA  1 
ATOM   13276 C  C   . GLY   K  1 67  ? -10.216 -90.969  -14.755 1.00 40.52 ? 67  GLY   K C   1 
ATOM   13277 O  O   . GLY   K  1 67  ? -10.766 -90.290  -15.623 1.00 36.59 ? 67  GLY   K O   1 
ATOM   13278 N  N   . LEU   K  1 68  ? -10.306 -90.699  -13.449 1.00 39.10 ? 68  LEU   K N   1 
ATOM   13279 C  CA  . LEU   K  1 68  ? -11.022 -89.544  -12.911 1.00 38.47 ? 68  LEU   K CA  1 
ATOM   13280 C  C   . LEU   K  1 68  ? -10.025 -88.510  -12.404 1.00 41.80 ? 68  LEU   K C   1 
ATOM   13281 O  O   . LEU   K  1 68  ? -9.310  -88.778  -11.426 1.00 33.98 ? 68  LEU   K O   1 
ATOM   13282 C  CB  . LEU   K  1 68  ? -11.949 -89.977  -11.778 1.00 40.32 ? 68  LEU   K CB  1 
ATOM   13283 C  CG  . LEU   K  1 68  ? -13.139 -90.821  -12.223 1.00 47.36 ? 68  LEU   K CG  1 
ATOM   13284 C  CD1 . LEU   K  1 68  ? -13.885 -91.383  -11.002 1.00 58.73 ? 68  LEU   K CD1 1 
ATOM   13285 C  CD2 . LEU   K  1 68  ? -14.088 -89.999  -13.114 1.00 62.90 ? 68  LEU   K CD2 1 
ATOM   13286 N  N   . PRO   K  1 69  ? -9.924  -87.333  -13.020 1.00 33.69 ? 69  PRO   K N   1 
ATOM   13287 C  CA  . PRO   K  1 69  ? -8.990  -86.318  -12.509 1.00 38.36 ? 69  PRO   K CA  1 
ATOM   13288 C  C   . PRO   K  1 69  ? -9.436  -85.844  -11.140 1.00 32.78 ? 69  PRO   K C   1 
ATOM   13289 O  O   . PRO   K  1 69  ? -10.612 -85.546  -10.938 1.00 38.57 ? 69  PRO   K O   1 
ATOM   13290 C  CB  . PRO   K  1 69  ? -9.085  -85.184  -13.539 1.00 35.70 ? 69  PRO   K CB  1 
ATOM   13291 C  CG  . PRO   K  1 69  ? -9.802  -85.783  -14.741 1.00 37.14 ? 69  PRO   K CG  1 
ATOM   13292 C  CD  . PRO   K  1 69  ? -10.686 -86.841  -14.179 1.00 30.29 ? 69  PRO   K CD  1 
ATOM   13293 N  N   . ASN   K  1 70  ? -8.491  -85.743  -10.211 1.00 35.05 ? 70  ASN   K N   1 
ATOM   13294 C  CA  . ASN   K  1 70  ? -8.790  -85.260  -8.864  1.00 36.90 ? 70  ASN   K CA  1 
ATOM   13295 C  C   . ASN   K  1 70  ? -8.520  -83.759  -8.799  1.00 28.64 ? 70  ASN   K C   1 
ATOM   13296 O  O   . ASN   K  1 70  ? -7.375  -83.336  -8.651  1.00 29.68 ? 70  ASN   K O   1 
ATOM   13297 C  CB  . ASN   K  1 70  ? -7.960  -86.015  -7.830  1.00 33.81 ? 70  ASN   K CB  1 
ATOM   13298 C  CG  . ASN   K  1 70  ? -8.304  -85.627  -6.405  1.00 33.35 ? 70  ASN   K CG  1 
ATOM   13299 O  OD1 . ASN   K  1 70  ? -8.953  -84.601  -6.142  1.00 36.27 ? 70  ASN   K OD1 1 
ATOM   13300 N  ND2 . ASN   K  1 70  ? -7.880  -86.449  -5.477  1.00 36.15 ? 70  ASN   K ND2 1 
ATOM   13301 N  N   . LEU   K  1 71  ? -9.579  -82.956  -8.899  1.00 32.10 ? 71  LEU   K N   1 
ATOM   13302 C  CA  . LEU   K  1 71  ? -9.521  -81.518  -8.657  1.00 33.88 ? 71  LEU   K CA  1 
ATOM   13303 C  C   . LEU   K  1 71  ? -10.116 -81.126  -7.307  1.00 42.80 ? 71  LEU   K C   1 
ATOM   13304 O  O   . LEU   K  1 71  ? -10.303 -79.932  -7.043  1.00 35.28 ? 71  LEU   K O   1 
ATOM   13305 C  CB  . LEU   K  1 71  ? -10.252 -80.762  -9.763  1.00 30.43 ? 71  LEU   K CB  1 
ATOM   13306 C  CG  . LEU   K  1 71  ? -9.547  -80.731  -11.123 1.00 41.61 ? 71  LEU   K CG  1 
ATOM   13307 C  CD1 . LEU   K  1 71  ? -9.710  -82.055  -11.815 1.00 41.83 ? 71  LEU   K CD1 1 
ATOM   13308 C  CD2 . LEU   K  1 71  ? -10.112 -79.616  -11.986 1.00 37.76 ? 71  LEU   K CD2 1 
ATOM   13309 N  N   . GLN   K  1 72  ? -10.400 -82.105  -6.446  1.00 37.59 ? 72  GLN   K N   1 
ATOM   13310 C  CA  . GLN   K  1 72  ? -11.044 -81.876  -5.159  1.00 35.81 ? 72  GLN   K CA  1 
ATOM   13311 C  C   . GLN   K  1 72  ? -10.043 -81.714  -4.014  1.00 35.51 ? 72  GLN   K C   1 
ATOM   13312 O  O   . GLN   K  1 72  ? -10.250 -80.885  -3.124  1.00 38.65 ? 72  GLN   K O   1 
ATOM   13313 C  CB  . GLN   K  1 72  ? -11.979 -83.041  -4.863  1.00 36.85 ? 72  GLN   K CB  1 
ATOM   13314 C  CG  . GLN   K  1 72  ? -12.704 -82.935  -3.545  1.00 33.76 ? 72  GLN   K CG  1 
ATOM   13315 C  CD  . GLN   K  1 72  ? -13.693 -81.822  -3.544  1.00 33.61 ? 72  GLN   K CD  1 
ATOM   13316 O  OE1 . GLN   K  1 72  ? -14.814 -81.961  -4.041  1.00 38.73 ? 72  GLN   K OE1 1 
ATOM   13317 N  NE2 . GLN   K  1 72  ? -13.278 -80.685  -3.018  1.00 34.92 ? 72  GLN   K NE2 1 
ATOM   13318 N  N   . ASP   K  1 73  ? -8.970  -82.495  -4.017  1.00 35.72 ? 73  ASP   K N   1 
ATOM   13319 C  CA  . ASP   K  1 73  ? -8.020  -82.541  -2.909  1.00 38.22 ? 73  ASP   K CA  1 
ATOM   13320 C  C   . ASP   K  1 73  ? -6.856  -81.584  -3.151  1.00 36.92 ? 73  ASP   K C   1 
ATOM   13321 O  O   . ASP   K  1 73  ? -6.091  -81.739  -4.112  1.00 40.58 ? 73  ASP   K O   1 
ATOM   13322 C  CB  . ASP   K  1 73  ? -7.514  -83.967  -2.727  1.00 39.51 ? 73  ASP   K CB  1 
ATOM   13323 C  CG  . ASP   K  1 73  ? -8.617  -84.902  -2.324  1.00 37.10 ? 73  ASP   K CG  1 
ATOM   13324 O  OD1 . ASP   K  1 73  ? -9.535  -84.433  -1.623  1.00 42.81 ? 73  ASP   K OD1 1 
ATOM   13325 O  OD2 . ASP   K  1 73  ? -8.586  -86.079  -2.735  1.00 42.23 ? 73  ASP   K OD2 1 
ATOM   13326 N  N   . LEU   K  1 74  ? -6.727  -80.607  -2.269  1.00 36.34 ? 74  LEU   K N   1 
ATOM   13327 C  CA  . LEU   K  1 74  ? -5.746  -79.541  -2.381  1.00 39.79 ? 74  LEU   K CA  1 
ATOM   13328 C  C   . LEU   K  1 74  ? -4.794  -79.619  -1.190  1.00 34.30 ? 74  LEU   K C   1 
ATOM   13329 O  O   . LEU   K  1 74  ? -5.223  -79.462  -0.044  1.00 33.64 ? 74  LEU   K O   1 
ATOM   13330 C  CB  . LEU   K  1 74  ? -6.462  -78.195  -2.419  1.00 30.44 ? 74  LEU   K CB  1 
ATOM   13331 C  CG  . LEU   K  1 74  ? -5.557  -76.975  -2.523  1.00 34.92 ? 74  LEU   K CG  1 
ATOM   13332 C  CD1 . LEU   K  1 74  ? -4.747  -77.063  -3.825  1.00 33.82 ? 74  LEU   K CD1 1 
ATOM   13333 C  CD2 . LEU   K  1 74  ? -6.392  -75.717  -2.487  1.00 32.46 ? 74  LEU   K CD2 1 
ATOM   13334 N  N   . GLY   K  1 75  ? -3.519  -79.880  -1.456  1.00 34.05 ? 75  GLY   K N   1 
ATOM   13335 C  CA  . GLY   K  1 75  ? -2.528  -79.955  -0.404  1.00 36.22 ? 75  GLY   K CA  1 
ATOM   13336 C  C   . GLY   K  1 75  ? -2.171  -78.583  0.142   1.00 36.93 ? 75  GLY   K C   1 
ATOM   13337 O  O   . GLY   K  1 75  ? -2.763  -77.557  -0.190  1.00 36.45 ? 75  GLY   K O   1 
ATOM   13338 N  N   . LYS   K  1 76  ? -1.150  -78.579  0.991   1.00 33.29 ? 76  LYS   K N   1 
ATOM   13339 C  CA  . LYS   K  1 76  ? -0.808  -77.403  1.785   1.00 38.62 ? 76  LYS   K CA  1 
ATOM   13340 C  C   . LYS   K  1 76  ? -0.029  -76.387  0.945   1.00 36.66 ? 76  LYS   K C   1 
ATOM   13341 O  O   . LYS   K  1 76  ? 1.041   -76.697  0.431   1.00 32.04 ? 76  LYS   K O   1 
ATOM   13342 C  CB  . LYS   K  1 76  ? 0.014   -77.819  3.011   1.00 38.49 ? 76  LYS   K CB  1 
ATOM   13343 C  CG  . LYS   K  1 76  ? 0.481   -76.642  3.847   1.00 43.73 ? 76  LYS   K CG  1 
ATOM   13344 N  N   . LEU   K  1 77  ? -0.564  -75.177  0.822   1.00 33.65 ? 77  LEU   K N   1 
ATOM   13345 C  CA  . LEU   K  1 77  ? 0.176   -74.058  0.250   1.00 31.67 ? 77  LEU   K CA  1 
ATOM   13346 C  C   . LEU   K  1 77  ? 1.327   -73.645  1.166   1.00 38.77 ? 77  LEU   K C   1 
ATOM   13347 O  O   . LEU   K  1 77  ? 1.173   -73.576  2.381   1.00 34.08 ? 77  LEU   K O   1 
ATOM   13348 C  CB  . LEU   K  1 77  ? -0.776  -72.864  0.049   1.00 34.82 ? 77  LEU   K CB  1 
ATOM   13349 C  CG  . LEU   K  1 77  ? -1.694  -72.778  -1.182  1.00 44.83 ? 77  LEU   K CG  1 
ATOM   13350 C  CD1 . LEU   K  1 77  ? -2.137  -74.138  -1.676  1.00 39.51 ? 77  LEU   K CD1 1 
ATOM   13351 C  CD2 . LEU   K  1 77  ? -2.918  -71.888  -0.892  1.00 36.24 ? 77  LEU   K CD2 1 
ATOM   13352 N  N   . LEU   K  1 78  ? 2.484   -73.346  0.578   1.00 29.06 ? 78  LEU   K N   1 
ATOM   13353 C  CA  . LEU   K  1 78  ? 3.622   -72.768  1.300   1.00 33.39 ? 78  LEU   K CA  1 
ATOM   13354 C  C   . LEU   K  1 78  ? 3.681   -71.287  0.931   1.00 36.26 ? 78  LEU   K C   1 
ATOM   13355 O  O   . LEU   K  1 78  ? 4.168   -70.919  -0.143  1.00 32.79 ? 78  LEU   K O   1 
ATOM   13356 C  CB  . LEU   K  1 78  ? 4.932   -73.474  0.941   1.00 32.32 ? 78  LEU   K CB  1 
ATOM   13357 C  CG  . LEU   K  1 78  ? 4.966   -75.013  0.946   1.00 41.26 ? 78  LEU   K CG  1 
ATOM   13358 C  CD1 . LEU   K  1 78  ? 6.361   -75.514  0.454   1.00 37.48 ? 78  LEU   K CD1 1 
ATOM   13359 C  CD2 . LEU   K  1 78  ? 4.619   -75.568  2.338   1.00 42.46 ? 78  LEU   K CD2 1 
ATOM   13360 N  N   . ILE   K  1 79  ? 3.195   -70.433  1.822   1.00 31.51 ? 79  ILE   K N   1 
ATOM   13361 C  CA  . ILE   K  1 79  ? 3.096   -69.005  1.554   1.00 32.16 ? 79  ILE   K CA  1 
ATOM   13362 C  C   . ILE   K  1 79  ? 4.164   -68.290  2.364   1.00 38.66 ? 79  ILE   K C   1 
ATOM   13363 O  O   . ILE   K  1 79  ? 4.196   -68.386  3.600   1.00 37.38 ? 79  ILE   K O   1 
ATOM   13364 C  CB  . ILE   K  1 79  ? 1.704   -68.462  1.894   1.00 35.85 ? 79  ILE   K CB  1 
ATOM   13365 C  CG1 . ILE   K  1 79  ? 0.614   -69.233  1.121   1.00 41.13 ? 79  ILE   K CG1 1 
ATOM   13366 C  CG2 . ILE   K  1 79  ? 1.673   -66.957  1.636   1.00 37.48 ? 79  ILE   K CG2 1 
ATOM   13367 C  CD1 . ILE   K  1 79  ? 0.788   -69.273  -0.434  1.00 35.17 ? 79  ILE   K CD1 1 
ATOM   13368 N  N   . GLY   K  1 80  ? 5.011   -67.553  1.697   1.00 35.01 ? 80  GLY   K N   1 
ATOM   13369 C  CA  . GLY   K  1 80  ? 6.026   -66.834  2.436   1.00 38.34 ? 80  GLY   K CA  1 
ATOM   13370 C  C   . GLY   K  1 80  ? 5.477   -65.552  3.051   1.00 34.61 ? 80  GLY   K C   1 
ATOM   13371 O  O   . GLY   K  1 80  ? 4.406   -65.064  2.693   1.00 38.00 ? 80  GLY   K O   1 
ATOM   13372 N  N   . GLU   K  1 81  ? 6.269   -64.974  3.949   1.00 34.56 ? 81  GLU   K N   1 
ATOM   13373 C  CA  . GLU   K  1 81  ? 5.933   -63.709  4.578   1.00 38.72 ? 81  GLU   K CA  1 
ATOM   13374 C  C   . GLU   K  1 81  ? 6.825   -62.569  4.104   1.00 38.62 ? 81  GLU   K C   1 
ATOM   13375 O  O   . GLU   K  1 81  ? 6.593   -61.420  4.476   1.00 36.71 ? 81  GLU   K O   1 
ATOM   13376 C  CB  . GLU   K  1 81  ? 5.993   -63.864  6.103   1.00 37.06 ? 81  GLU   K CB  1 
ATOM   13377 C  CG  . GLU   K  1 81  ? 4.992   -64.900  6.583   1.00 55.48 ? 81  GLU   K CG  1 
ATOM   13378 C  CD  . GLU   K  1 81  ? 4.877   -64.969  8.087   1.00 66.76 ? 81  GLU   K CD  1 
ATOM   13379 O  OE1 . GLU   K  1 81  ? 5.673   -64.294  8.774   1.00 51.76 ? 81  GLU   K OE1 1 
ATOM   13380 O  OE2 . GLU   K  1 81  ? 3.983   -65.697  8.573   1.00 76.35 ? 81  GLU   K OE2 1 
ATOM   13381 N  N   . ASN   K  1 82  ? 7.813   -62.853  3.263   1.00 29.93 ? 82  ASN   K N   1 
ATOM   13382 C  CA  . ASN   K  1 82  ? 8.632   -61.818  2.652   1.00 28.81 ? 82  ASN   K CA  1 
ATOM   13383 C  C   . ASN   K  1 82  ? 9.207   -62.411  1.371   1.00 27.76 ? 82  ASN   K C   1 
ATOM   13384 O  O   . ASN   K  1 82  ? 9.043   -63.600  1.085   1.00 29.78 ? 82  ASN   K O   1 
ATOM   13385 C  CB  . ASN   K  1 82  ? 9.715   -61.293  3.612   1.00 29.96 ? 82  ASN   K CB  1 
ATOM   13386 C  CG  . ASN   K  1 82  ? 10.747  -62.355  4.020   1.00 34.79 ? 82  ASN   K CG  1 
ATOM   13387 O  OD1 . ASN   K  1 82  ? 11.130  -63.228  3.248   1.00 38.98 ? 82  ASN   K OD1 1 
ATOM   13388 N  ND2 . ASN   K  1 82  ? 11.209  -62.258  5.242   1.00 42.11 ? 82  ASN   K ND2 1 
ATOM   13389 N  N   . THR   K  1 83  ? 9.839   -61.559  0.570   1.00 30.84 ? 83  THR   K N   1 
ATOM   13390 C  CA  . THR   K  1 83  ? 10.247  -62.000  -0.764  1.00 29.22 ? 83  THR   K CA  1 
ATOM   13391 C  C   . THR   K  1 83  ? 11.147  -63.232  -0.709  1.00 32.48 ? 83  THR   K C   1 
ATOM   13392 O  O   . THR   K  1 83  ? 10.895  -64.227  -1.409  1.00 27.58 ? 83  THR   K O   1 
ATOM   13393 C  CB  . THR   K  1 83  ? 10.924  -60.851  -1.507  1.00 31.82 ? 83  THR   K CB  1 
ATOM   13394 O  OG1 . THR   K  1 83  ? 9.940   -59.863  -1.848  1.00 29.90 ? 83  THR   K OG1 1 
ATOM   13395 C  CG2 . THR   K  1 83  ? 11.532  -61.338  -2.802  1.00 27.40 ? 83  THR   K CG2 1 
ATOM   13396 N  N   . GLN   K  1 84  ? 12.205  -63.193  0.114   1.00 31.24 ? 84  GLN   K N   1 
ATOM   13397 C  CA  . GLN   K  1 84  ? 13.121  -64.330  0.174   1.00 31.50 ? 84  GLN   K CA  1 
ATOM   13398 C  C   . GLN   K  1 84  ? 12.385  -65.605  0.570   1.00 30.82 ? 84  GLN   K C   1 
ATOM   13399 O  O   . GLN   K  1 84  ? 12.602  -66.669  -0.024  1.00 29.07 ? 84  GLN   K O   1 
ATOM   13400 C  CB  . GLN   K  1 84  ? 14.258  -64.031  1.160   1.00 30.16 ? 84  GLN   K CB  1 
ATOM   13401 C  CG  . GLN   K  1 84  ? 15.369  -65.068  1.166   1.00 41.76 ? 84  GLN   K CG  1 
ATOM   13402 C  CD  . GLN   K  1 84  ? 16.662  -64.490  1.732   1.00 50.28 ? 84  GLN   K CD  1 
ATOM   13403 O  OE1 . GLN   K  1 84  ? 16.680  -63.355  2.216   1.00 55.05 ? 84  GLN   K OE1 1 
ATOM   13404 N  NE2 . GLN   K  1 84  ? 17.745  -65.258  1.661   1.00 53.08 ? 84  GLN   K NE2 1 
ATOM   13405 N  N   . GLU   K  1 85  ? 11.508  -65.518  1.576   1.00 32.48 ? 85  GLU   K N   1 
ATOM   13406 C  CA  . GLU   K  1 85  ? 10.735  -66.686  1.987   1.00 35.67 ? 85  GLU   K CA  1 
ATOM   13407 C  C   . GLU   K  1 85  ? 9.816   -67.169  0.879   1.00 28.75 ? 85  GLU   K C   1 
ATOM   13408 O  O   . GLU   K  1 85  ? 9.608   -68.377  0.716   1.00 25.79 ? 85  GLU   K O   1 
ATOM   13409 C  CB  . GLU   K  1 85  ? 9.886   -66.376  3.230   1.00 38.40 ? 85  GLU   K CB  1 
ATOM   13410 C  CG  . GLU   K  1 85  ? 10.636  -66.402  4.543   1.00 44.86 ? 85  GLU   K CG  1 
ATOM   13411 C  CD  . GLU   K  1 85  ? 9.737   -66.069  5.738   1.00 51.85 ? 85  GLU   K CD  1 
ATOM   13412 O  OE1 . GLU   K  1 85  ? 8.482   -66.059  5.576   1.00 33.82 ? 85  GLU   K OE1 1 
ATOM   13413 O  OE2 . GLU   K  1 85  ? 10.300  -65.820  6.834   1.00 46.40 ? 85  GLU   K OE2 1 
ATOM   13414 N  N   . MET   K  1 86  ? 9.194   -66.242  0.152   1.00 29.07 ? 86  MET   K N   1 
ATOM   13415 C  CA  . MET   K  1 86  ? 8.277   -66.669  -0.895  1.00 28.00 ? 86  MET   K CA  1 
ATOM   13416 C  C   . MET   K  1 86  ? 9.026   -67.436  -1.979  1.00 30.33 ? 86  MET   K C   1 
ATOM   13417 O  O   . MET   K  1 86  ? 8.562   -68.485  -2.452  1.00 27.36 ? 86  MET   K O   1 
ATOM   13418 C  CB  . MET   K  1 86  ? 7.548   -65.449  -1.461  1.00 25.73 ? 86  MET   K CB  1 
ATOM   13419 C  CG  . MET   K  1 86  ? 6.637   -64.748  -0.474  1.00 31.60 ? 86  MET   K CG  1 
ATOM   13420 S  SD  . MET   K  1 86  ? 6.432   -62.974  -0.770  1.00 29.58 ? 86  MET   K SD  1 
ATOM   13421 C  CE  . MET   K  1 86  ? 5.350   -63.005  -2.226  1.00 29.87 ? 86  MET   K CE  1 
ATOM   13422 N  N   . LEU   K  1 87  ? 10.202  -66.937  -2.366  1.00 28.08 ? 87  LEU   K N   1 
ATOM   13423 C  CA  . LEU   K  1 87  ? 11.016  -67.650  -3.340  1.00 26.40 ? 87  LEU   K CA  1 
ATOM   13424 C  C   . LEU   K  1 87  ? 11.424  -69.026  -2.819  1.00 32.88 ? 87  LEU   K C   1 
ATOM   13425 O  O   . LEU   K  1 87  ? 11.368  -70.020  -3.556  1.00 28.71 ? 87  LEU   K O   1 
ATOM   13426 C  CB  . LEU   K  1 87  ? 12.234  -66.807  -3.698  1.00 25.96 ? 87  LEU   K CB  1 
ATOM   13427 C  CG  . LEU   K  1 87  ? 11.885  -65.529  -4.464  1.00 26.98 ? 87  LEU   K CG  1 
ATOM   13428 C  CD1 . LEU   K  1 87  ? 13.044  -64.557  -4.465  1.00 27.55 ? 87  LEU   K CD1 1 
ATOM   13429 C  CD2 . LEU   K  1 87  ? 11.479  -65.862  -5.911  1.00 28.65 ? 87  LEU   K CD2 1 
ATOM   13430 N  N   . GLN   K  1 88  ? 11.794  -69.114  -1.539  1.00 33.54 ? 88  GLN   K N   1 
ATOM   13431 C  CA  . GLN   K  1 88  ? 12.223  -70.399  -0.998  1.00 31.54 ? 88  GLN   K CA  1 
ATOM   13432 C  C   . GLN   K  1 88  ? 11.057  -71.364  -0.875  1.00 24.52 ? 88  GLN   K C   1 
ATOM   13433 O  O   . GLN   K  1 88  ? 11.212  -72.566  -1.123  1.00 31.02 ? 88  GLN   K O   1 
ATOM   13434 C  CB  . GLN   K  1 88  ? 12.917  -70.187  0.350   1.00 35.98 ? 88  GLN   K CB  1 
ATOM   13435 C  CG  . GLN   K  1 88  ? 13.447  -71.484  0.951   1.00 49.87 ? 88  GLN   K CG  1 
ATOM   13436 C  CD  . GLN   K  1 88  ? 14.616  -72.091  0.180   1.00 44.25 ? 88  GLN   K CD  1 
ATOM   13437 O  OE1 . GLN   K  1 88  ? 15.656  -71.450  0.010   1.00 43.05 ? 88  GLN   K OE1 1 
ATOM   13438 N  NE2 . GLN   K  1 88  ? 14.465  -73.347  -0.251  1.00 40.38 ? 88  GLN   K NE2 1 
ATOM   13439 N  N   . CYS   K  1 89  ? 9.869   -70.858  -0.521  1.00 24.98 ? 89  CYS   K N   1 
ATOM   13440 C  CA  . CYS   K  1 89  ? 8.671   -71.687  -0.541  1.00 29.25 ? 89  CYS   K CA  1 
ATOM   13441 C  C   . CYS   K  1 89  ? 8.373   -72.204  -1.944  1.00 34.58 ? 89  CYS   K C   1 
ATOM   13442 O  O   . CYS   K  1 89  ? 7.973   -73.359  -2.109  1.00 28.18 ? 89  CYS   K O   1 
ATOM   13443 C  CB  . CYS   K  1 89  ? 7.477   -70.893  -0.035  1.00 33.21 ? 89  CYS   K CB  1 
ATOM   13444 S  SG  . CYS   K  1 89  ? 7.408   -70.733  1.747   1.00 35.59 ? 89  CYS   K SG  1 
ATOM   13445 N  N   . ASP   K  1 90  ? 8.507   -71.348  -2.966  1.00 28.71 ? 90  ASP   K N   1 
ATOM   13446 C  CA  . ASP   K  1 90  ? 8.323   -71.835  -4.331  1.00 33.15 ? 90  ASP   K CA  1 
ATOM   13447 C  C   . ASP   K  1 90  ? 9.336   -72.922  -4.633  1.00 28.19 ? 90  ASP   K C   1 
ATOM   13448 O  O   . ASP   K  1 90  ? 9.009   -73.948  -5.245  1.00 27.52 ? 90  ASP   K O   1 
ATOM   13449 C  CB  . ASP   K  1 90  ? 8.480   -70.698  -5.350  1.00 29.69 ? 90  ASP   K CB  1 
ATOM   13450 C  CG  . ASP   K  1 90  ? 7.312   -69.716  -5.358  1.00 31.92 ? 90  ASP   K CG  1 
ATOM   13451 O  OD1 . ASP   K  1 90  ? 6.315   -69.908  -4.637  1.00 30.41 ? 90  ASP   K OD1 1 
ATOM   13452 O  OD2 . ASP   K  1 90  ? 7.408   -68.718  -6.111  1.00 33.39 ? 90  ASP   K OD2 1 
ATOM   13453 N  N   . LEU   K  1 91  ? 10.588  -72.700  -4.223  1.00 31.24 ? 91  LEU   K N   1 
ATOM   13454 C  CA  . LEU   K  1 91  ? 11.641  -73.661  -4.529  1.00 32.02 ? 91  LEU   K CA  1 
ATOM   13455 C  C   . LEU   K  1 91  ? 11.380  -74.992  -3.829  1.00 36.98 ? 91  LEU   K C   1 
ATOM   13456 O  O   . LEU   K  1 91  ? 11.496  -76.057  -4.445  1.00 30.97 ? 91  LEU   K O   1 
ATOM   13457 C  CB  . LEU   K  1 91  ? 12.990  -73.064  -4.142  1.00 30.06 ? 91  LEU   K CB  1 
ATOM   13458 C  CG  . LEU   K  1 91  ? 14.279  -73.869  -4.400  1.00 33.55 ? 91  LEU   K CG  1 
ATOM   13459 C  CD1 . LEU   K  1 91  ? 14.347  -74.459  -5.807  1.00 34.43 ? 91  LEU   K CD1 1 
ATOM   13460 C  CD2 . LEU   K  1 91  ? 15.480  -72.996  -4.144  1.00 39.07 ? 91  LEU   K CD2 1 
ATOM   13461 N  N   . ASN   K  1 92  ? 10.979  -74.952  -2.556  1.00 33.30 ? 92  ASN   K N   1 
ATOM   13462 C  CA  . ASN   K  1 92  ? 10.672  -76.194  -1.849  1.00 32.29 ? 92  ASN   K CA  1 
ATOM   13463 C  C   . ASN   K  1 92  ? 9.584   -76.986  -2.558  1.00 31.26 ? 92  ASN   K C   1 
ATOM   13464 O  O   . ASN   K  1 92  ? 9.709   -78.205  -2.750  1.00 32.57 ? 92  ASN   K O   1 
ATOM   13465 C  CB  . ASN   K  1 92  ? 10.280  -75.888  -0.403  1.00 33.58 ? 92  ASN   K CB  1 
ATOM   13466 C  CG  . ASN   K  1 92  ? 11.444  -75.356  0.396   1.00 40.28 ? 92  ASN   K CG  1 
ATOM   13467 O  OD1 . ASN   K  1 92  ? 12.605  -75.525  0.001   1.00 45.26 ? 92  ASN   K OD1 1 
ATOM   13468 N  ND2 . ASN   K  1 92  ? 11.153  -74.698  1.519   1.00 45.05 ? 92  ASN   K ND2 1 
ATOM   13469 N  N   . LEU   K  1 93  ? 8.504   -76.309  -2.965  1.00 30.66 ? 93  LEU   K N   1 
ATOM   13470 C  CA  . LEU   K  1 93  ? 7.449   -76.983  -3.716  1.00 29.39 ? 93  LEU   K CA  1 
ATOM   13471 C  C   . LEU   K  1 93  ? 7.963   -77.577  -5.029  1.00 33.14 ? 93  LEU   K C   1 
ATOM   13472 O  O   . LEU   K  1 93  ? 7.578   -78.694  -5.408  1.00 29.40 ? 93  LEU   K O   1 
ATOM   13473 C  CB  . LEU   K  1 93  ? 6.308   -75.995  -3.979  1.00 33.16 ? 93  LEU   K CB  1 
ATOM   13474 C  CG  . LEU   K  1 93  ? 5.131   -76.551  -4.773  1.00 28.47 ? 93  LEU   K CG  1 
ATOM   13475 C  CD1 . LEU   K  1 93  ? 4.452   -77.672  -4.014  1.00 40.58 ? 93  LEU   K CD1 1 
ATOM   13476 C  CD2 . LEU   K  1 93  ? 4.133   -75.466  -5.060  1.00 32.62 ? 93  LEU   K CD2 1 
ATOM   13477 N  N   . GLU   K  1 94  ? 8.804   -76.841  -5.760  1.00 29.23 ? 94  GLU   K N   1 
ATOM   13478 C  CA  . GLU   K  1 94  ? 9.312   -77.382  -7.026  1.00 37.28 ? 94  GLU   K CA  1 
ATOM   13479 C  C   . GLU   K  1 94  ? 10.136  -78.646  -6.802  1.00 37.74 ? 94  GLU   K C   1 
ATOM   13480 O  O   . GLU   K  1 94  ? 10.040  -79.602  -7.577  1.00 31.71 ? 94  GLU   K O   1 
ATOM   13481 C  CB  . GLU   K  1 94  ? 10.168  -76.353  -7.769  1.00 32.05 ? 94  GLU   K CB  1 
ATOM   13482 C  CG  . GLU   K  1 94  ? 9.393   -75.198  -8.337  1.00 32.85 ? 94  GLU   K CG  1 
ATOM   13483 C  CD  . GLU   K  1 94  ? 8.604   -75.576  -9.564  1.00 40.36 ? 94  GLU   K CD  1 
ATOM   13484 O  OE1 . GLU   K  1 94  ? 8.768   -76.698  -10.086 1.00 36.99 ? 94  GLU   K OE1 1 
ATOM   13485 O  OE2 . GLU   K  1 94  ? 7.800   -74.746  -10.004 1.00 46.84 ? 94  GLU   K OE2 1 
ATOM   13486 N  N   . LEU   K  1 95  ? 10.984  -78.658  -5.769  1.00 38.24 ? 95  LEU   K N   1 
ATOM   13487 C  CA  . LEU   K  1 95  ? 11.823  -79.832  -5.548  1.00 37.82 ? 95  LEU   K CA  1 
ATOM   13488 C  C   . LEU   K  1 95  ? 10.985  -81.060  -5.218  1.00 35.36 ? 95  LEU   K C   1 
ATOM   13489 O  O   . LEU   K  1 95  ? 11.277  -82.166  -5.700  1.00 37.82 ? 95  LEU   K O   1 
ATOM   13490 C  CB  . LEU   K  1 95  ? 12.840  -79.542  -4.447  1.00 35.77 ? 95  LEU   K CB  1 
ATOM   13491 C  CG  . LEU   K  1 95  ? 13.910  -78.563  -4.875  1.00 36.64 ? 95  LEU   K CG  1 
ATOM   13492 C  CD1 . LEU   K  1 95  ? 14.628  -78.022  -3.657  1.00 41.09 ? 95  LEU   K CD1 1 
ATOM   13493 C  CD2 . LEU   K  1 95  ? 14.888  -79.249  -5.828  1.00 46.78 ? 95  LEU   K CD2 1 
ATOM   13494 N  N   . LYS   K  1 96  ? 9.912   -80.883  -4.446  1.00 34.31 ? 96  LYS   K N   1 
ATOM   13495 C  CA  . LYS   K  1 96  ? 8.958   -81.967  -4.261  1.00 30.50 ? 96  LYS   K CA  1 
ATOM   13496 C  C   . LYS   K  1 96  ? 8.318   -82.366  -5.580  1.00 36.62 ? 96  LYS   K C   1 
ATOM   13497 O  O   . LYS   K  1 96  ? 8.164   -83.561  -5.874  1.00 32.44 ? 96  LYS   K O   1 
ATOM   13498 C  CB  . LYS   K  1 96  ? 7.890   -81.562  -3.242  1.00 41.22 ? 96  LYS   K CB  1 
ATOM   13499 C  CG  . LYS   K  1 96  ? 6.643   -82.448  -3.251  1.00 34.86 ? 96  LYS   K CG  1 
ATOM   13500 N  N   . ALA   K  1 97  ? 7.929   -81.380  -6.394  1.00 35.18 ? 97  ALA   K N   1 
ATOM   13501 C  CA  . ALA   K  1 97  ? 7.276   -81.703  -7.656  1.00 34.40 ? 97  ALA   K CA  1 
ATOM   13502 C  C   . ALA   K  1 97  ? 8.214   -82.468  -8.591  1.00 31.31 ? 97  ALA   K C   1 
ATOM   13503 O  O   . ALA   K  1 97  ? 7.799   -83.432  -9.248  1.00 33.98 ? 97  ALA   K O   1 
ATOM   13504 C  CB  . ALA   K  1 97  ? 6.761   -80.421  -8.322  1.00 38.40 ? 97  ALA   K CB  1 
ATOM   13505 N  N   . THR   K  1 98  ? 9.478   -82.061  -8.678  1.00 32.68 ? 98  THR   K N   1 
ATOM   13506 C  CA  . THR   K  1 98  ? 10.354  -82.776  -9.604  1.00 33.01 ? 98  THR   K CA  1 
ATOM   13507 C  C   . THR   K  1 98  ? 10.640  -84.192  -9.090  1.00 43.51 ? 98  THR   K C   1 
ATOM   13508 O  O   . THR   K  1 98  ? 10.733  -85.140  -9.884  1.00 33.97 ? 98  THR   K O   1 
ATOM   13509 C  CB  . THR   K  1 98  ? 11.651  -82.004  -9.865  1.00 35.68 ? 98  THR   K CB  1 
ATOM   13510 O  OG1 . THR   K  1 98  ? 12.307  -81.677  -8.647  1.00 37.65 ? 98  THR   K OG1 1 
ATOM   13511 C  CG2 . THR   K  1 98  ? 11.392  -80.714  -10.658 1.00 39.21 ? 98  THR   K CG2 1 
ATOM   13512 N  N   . LYS   K  1 99  ? 10.740  -84.373  -7.768  1.00 37.63 ? 99  LYS   K N   1 
ATOM   13513 C  CA  . LYS   K  1 99  ? 10.841  -85.732  -7.227  1.00 36.30 ? 99  LYS   K CA  1 
ATOM   13514 C  C   . LYS   K  1 99  ? 9.666   -86.583  -7.680  1.00 33.71 ? 99  LYS   K C   1 
ATOM   13515 O  O   . LYS   K  1 99  ? 9.848   -87.697  -8.185  1.00 37.03 ? 99  LYS   K O   1 
ATOM   13516 C  CB  . LYS   K  1 99  ? 10.921  -85.698  -5.698  1.00 40.96 ? 99  LYS   K CB  1 
ATOM   13517 C  CG  . LYS   K  1 99  ? 11.035  -87.070  -5.017  1.00 45.76 ? 99  LYS   K CG  1 
ATOM   13518 C  CD  . LYS   K  1 99  ? 11.308  -86.920  -3.503  1.00 42.53 ? 99  LYS   K CD  1 
ATOM   13519 N  N   . ASP   K  1 100 ? 8.444   -86.065  -7.531  1.00 32.19 ? 100 ASP   K N   1 
ATOM   13520 C  CA  . ASP   K  1 100 ? 7.276   -86.858  -7.888  1.00 33.70 ? 100 ASP   K CA  1 
ATOM   13521 C  C   . ASP   K  1 100 ? 7.215   -87.135  -9.386  1.00 33.82 ? 100 ASP   K C   1 
ATOM   13522 O  O   . ASP   K  1 100 ? 6.721   -88.191  -9.801  1.00 35.20 ? 100 ASP   K O   1 
ATOM   13523 C  CB  . ASP   K  1 100 ? 6.006   -86.156  -7.425  1.00 40.86 ? 100 ASP   K CB  1 
ATOM   13524 C  CG  . ASP   K  1 100 ? 5.857   -86.168  -5.913  1.00 45.72 ? 100 ASP   K CG  1 
ATOM   13525 O  OD1 . ASP   K  1 100 ? 6.523   -87.002  -5.259  1.00 39.84 ? 100 ASP   K OD1 1 
ATOM   13526 O  OD2 . ASP   K  1 100 ? 5.072   -85.351  -5.386  1.00 42.57 ? 100 ASP   K OD2 1 
ATOM   13527 N  N   . LEU   K  1 101 ? 7.683   -86.202  -10.213 1.00 40.73 ? 101 LEU   K N   1 
ATOM   13528 C  CA  . LEU   K  1 101 ? 7.685   -86.441  -11.658 1.00 41.59 ? 101 LEU   K CA  1 
ATOM   13529 C  C   . LEU   K  1 101 ? 8.643   -87.577  -12.032 1.00 32.31 ? 101 LEU   K C   1 
ATOM   13530 O  O   . LEU   K  1 101 ? 8.316   -88.421  -12.880 1.00 30.22 ? 101 LEU   K O   1 
ATOM   13531 C  CB  . LEU   K  1 101 ? 8.044   -85.143  -12.396 1.00 38.61 ? 101 LEU   K CB  1 
ATOM   13532 C  CG  . LEU   K  1 101 ? 6.941   -84.054  -12.456 1.00 37.47 ? 101 LEU   K CG  1 
ATOM   13533 C  CD1 . LEU   K  1 101 ? 7.514   -82.664  -12.736 1.00 37.25 ? 101 LEU   K CD1 1 
ATOM   13534 C  CD2 . LEU   K  1 101 ? 5.924   -84.397  -13.526 1.00 41.84 ? 101 LEU   K CD2 1 
ATOM   13535 N  N   . ARG   K  1 102 ? 9.818   -87.620  -11.406 1.00 29.68 ? 102 ARG   K N   1 
ATOM   13536 C  CA  . ARG   K  1 102 ? 10.779  -88.682  -11.701 1.00 37.18 ? 102 ARG   K CA  1 
ATOM   13537 C  C   . ARG   K  1 102 ? 10.220  -90.063  -11.361 1.00 39.54 ? 102 ARG   K C   1 
ATOM   13538 O  O   . ARG   K  1 102 ? 10.356  -91.003  -12.154 1.00 33.49 ? 102 ARG   K O   1 
ATOM   13539 C  CB  . ARG   K  1 102 ? 12.084  -88.415  -10.961 1.00 34.30 ? 102 ARG   K CB  1 
ATOM   13540 C  CG  . ARG   K  1 102 ? 12.771  -87.129  -11.412 1.00 33.81 ? 102 ARG   K CG  1 
ATOM   13541 C  CD  . ARG   K  1 102 ? 14.105  -86.924  -10.747 1.00 34.24 ? 102 ARG   K CD  1 
ATOM   13542 N  NE  . ARG   K  1 102 ? 14.454  -85.507  -10.706 1.00 35.12 ? 102 ARG   K NE  1 
ATOM   13543 C  CZ  . ARG   K  1 102 ? 14.931  -84.831  -11.745 1.00 38.62 ? 102 ARG   K CZ  1 
ATOM   13544 N  NH1 . ARG   K  1 102 ? 15.220  -85.433  -12.888 1.00 36.02 ? 102 ARG   K NH1 1 
ATOM   13545 N  NH2 . ARG   K  1 102 ? 15.106  -83.514  -11.643 1.00 34.41 ? 102 ARG   K NH2 1 
ATOM   13546 N  N   . GLU   K  1 103 ? 9.582   -90.210  -10.188 1.00 42.17 ? 103 GLU   K N   1 
ATOM   13547 C  CA  . GLU   K  1 103 ? 9.016   -91.510  -9.808  1.00 34.89 ? 103 GLU   K CA  1 
ATOM   13548 C  C   . GLU   K  1 103 ? 7.918   -91.939  -10.770 1.00 37.67 ? 103 GLU   K C   1 
ATOM   13549 O  O   . GLU   K  1 103 ? 7.839   -93.115  -11.150 1.00 37.10 ? 103 GLU   K O   1 
ATOM   13550 C  CB  . GLU   K  1 103 ? 8.485   -91.463  -8.361  1.00 35.23 ? 103 GLU   K CB  1 
ATOM   13551 C  CG  . GLU   K  1 103 ? 9.615   -91.418  -7.321  1.00 44.70 ? 103 GLU   K CG  1 
ATOM   13552 C  CD  . GLU   K  1 103 ? 9.144   -91.060  -5.915  1.00 62.00 ? 103 GLU   K CD  1 
ATOM   13553 O  OE1 . GLU   K  1 103 ? 7.918   -91.047  -5.664  1.00 59.34 ? 103 GLU   K OE1 1 
ATOM   13554 O  OE2 . GLU   K  1 103 ? 10.013  -90.780  -5.059  1.00 59.87 ? 103 GLU   K OE2 1 
ATOM   13555 N  N   . ALA   K  1 104 ? 7.064   -90.996  -11.183 1.00 33.07 ? 104 ALA   K N   1 
ATOM   13556 C  CA  . ALA   K  1 104 ? 6.023   -91.298  -12.158 1.00 33.79 ? 104 ALA   K CA  1 
ATOM   13557 C  C   . ALA   K  1 104 ? 6.613   -91.702  -13.516 1.00 33.09 ? 104 ALA   K C   1 
ATOM   13558 O  O   . ALA   K  1 104 ? 6.103   -92.614  -14.180 1.00 34.24 ? 104 ALA   K O   1 
ATOM   13559 C  CB  . ALA   K  1 104 ? 5.109   -90.083  -12.314 1.00 35.90 ? 104 ALA   K CB  1 
ATOM   13560 N  N   . ILE   K  1 105 ? 7.667   -91.024  -13.960 1.00 33.88 ? 105 ILE   K N   1 
ATOM   13561 C  CA  . ILE   K  1 105 ? 8.280   -91.400  -15.233 1.00 36.41 ? 105 ILE   K CA  1 
ATOM   13562 C  C   . ILE   K  1 105 ? 8.799   -92.830  -15.163 1.00 40.44 ? 105 ILE   K C   1 
ATOM   13563 O  O   . ILE   K  1 105 ? 8.549   -93.643  -16.063 1.00 37.33 ? 105 ILE   K O   1 
ATOM   13564 C  CB  . ILE   K  1 105 ? 9.392   -90.415  -15.614 1.00 33.35 ? 105 ILE   K CB  1 
ATOM   13565 C  CG1 . ILE   K  1 105 ? 8.775   -89.108  -16.119 1.00 28.46 ? 105 ILE   K CG1 1 
ATOM   13566 C  CG2 . ILE   K  1 105 ? 10.256  -91.009  -16.686 1.00 33.50 ? 105 ILE   K CG2 1 
ATOM   13567 C  CD1 . ILE   K  1 105 ? 9.767   -87.975  -16.318 1.00 28.09 ? 105 ILE   K CD1 1 
ATOM   13568 N  N   . VAL   K  1 106 ? 9.513   -93.161  -14.078 1.00 37.71 ? 106 VAL   K N   1 
ATOM   13569 C  CA  . VAL   K  1 106 ? 9.951   -94.543  -13.863 1.00 37.83 ? 106 VAL   K CA  1 
ATOM   13570 C  C   . VAL   K  1 106 ? 8.796   -95.510  -14.082 1.00 37.94 ? 106 VAL   K C   1 
ATOM   13571 O  O   . VAL   K  1 106 ? 8.923   -96.500  -14.814 1.00 34.75 ? 106 VAL   K O   1 
ATOM   13572 C  CB  . VAL   K  1 106 ? 10.552  -94.709  -12.455 1.00 38.03 ? 106 VAL   K CB  1 
ATOM   13573 C  CG1 . VAL   K  1 106 ? 10.726  -96.173  -12.140 1.00 41.74 ? 106 VAL   K CG1 1 
ATOM   13574 C  CG2 . VAL   K  1 106 ? 11.856  -94.000  -12.363 1.00 37.57 ? 106 VAL   K CG2 1 
ATOM   13575 N  N   . HIS   K  1 107 ? 7.639   -95.237  -13.464 1.00 37.77 ? 107 HIS   K N   1 
ATOM   13576 C  CA  . HIS   K  1 107 ? 6.546   -96.202  -13.567 1.00 34.32 ? 107 HIS   K CA  1 
ATOM   13577 C  C   . HIS   K  1 107 ? 5.923   -96.226  -14.966 1.00 41.05 ? 107 HIS   K C   1 
ATOM   13578 O  O   . HIS   K  1 107 ? 5.480   -97.283  -15.426 1.00 36.24 ? 107 HIS   K O   1 
ATOM   13579 C  CB  . HIS   K  1 107 ? 5.464   -95.943  -12.524 1.00 41.93 ? 107 HIS   K CB  1 
ATOM   13580 C  CG  . HIS   K  1 107 ? 4.338   -96.922  -12.614 1.00 45.57 ? 107 HIS   K CG  1 
ATOM   13581 N  ND1 . HIS   K  1 107 ? 4.460   -98.226  -12.182 1.00 46.03 ? 107 HIS   K ND1 1 
ATOM   13582 C  CD2 . HIS   K  1 107 ? 3.102   -96.819  -13.160 1.00 44.38 ? 107 HIS   K CD2 1 
ATOM   13583 C  CE1 . HIS   K  1 107 ? 3.333   -98.872  -12.425 1.00 49.19 ? 107 HIS   K CE1 1 
ATOM   13584 N  NE2 . HIS   K  1 107 ? 2.496   -98.042  -13.023 1.00 46.43 ? 107 HIS   K NE2 1 
ATOM   13585 N  N   . CYS   K  1 108 ? 5.823   -95.074  -15.639 1.00 40.52 ? 108 CYS   K N   1 
ATOM   13586 C  CA  . CYS   K  1 108 ? 5.349   -95.079  -17.025 1.00 37.42 ? 108 CYS   K CA  1 
ATOM   13587 C  C   . CYS   K  1 108 ? 6.262   -95.900  -17.924 1.00 34.87 ? 108 CYS   K C   1 
ATOM   13588 O  O   . CYS   K  1 108 ? 5.788   -96.622  -18.806 1.00 40.01 ? 108 CYS   K O   1 
ATOM   13589 C  CB  . CYS   K  1 108 ? 5.252   -93.655  -17.566 1.00 36.96 ? 108 CYS   K CB  1 
ATOM   13590 S  SG  . CYS   K  1 108 ? 3.908   -92.720  -16.834 1.00 37.64 ? 108 CYS   K SG  1 
ATOM   13591 N  N   . GLU   K  1 109 ? 7.574   -95.772  -17.738 1.00 34.79 ? 109 GLU   K N   1 
ATOM   13592 C  CA  . GLU   K  1 109 ? 8.505   -96.551  -18.538 1.00 36.56 ? 109 GLU   K CA  1 
ATOM   13593 C  C   . GLU   K  1 109 ? 8.264   -98.040  -18.333 1.00 43.40 ? 109 GLU   K C   1 
ATOM   13594 O  O   . GLU   K  1 109 ? 8.182   -98.799  -19.302 1.00 42.81 ? 109 GLU   K O   1 
ATOM   13595 C  CB  . GLU   K  1 109 ? 9.931   -96.164  -18.172 1.00 37.29 ? 109 GLU   K CB  1 
ATOM   13596 C  CG  . GLU   K  1 109 ? 11.032  -96.846  -19.006 1.00 40.57 ? 109 GLU   K CG  1 
ATOM   13597 C  CD  . GLU   K  1 109 ? 11.112  -96.347  -20.443 1.00 44.67 ? 109 GLU   K CD  1 
ATOM   13598 O  OE1 . GLU   K  1 109 ? 10.614  -95.238  -20.715 1.00 40.66 ? 109 GLU   K OE1 1 
ATOM   13599 O  OE2 . GLU   K  1 109 ? 11.688  -97.068  -21.296 1.00 38.80 ? 109 GLU   K OE2 1 
ATOM   13600 N  N   . GLN   K  1 110 ? 8.077   -98.457  -17.076 1.00 45.18 ? 110 GLN   K N   1 
ATOM   13601 C  CA  . GLN   K  1 110 ? 7.987   -99.877  -16.753 1.00 39.52 ? 110 GLN   K CA  1 
ATOM   13602 C  C   . GLN   K  1 110 ? 6.776   -100.525 -17.396 1.00 37.92 ? 110 GLN   K C   1 
ATOM   13603 O  O   . GLN   K  1 110 ? 6.842   -101.687 -17.813 1.00 43.93 ? 110 GLN   K O   1 
ATOM   13604 C  CB  . GLN   K  1 110 ? 7.942   -100.077 -15.230 1.00 44.23 ? 110 GLN   K CB  1 
ATOM   13605 C  CG  . GLN   K  1 110 ? 9.236   -99.762  -14.512 1.00 45.45 ? 110 GLN   K CG  1 
ATOM   13606 N  N   . VAL   K  1 111 ? 5.652   -99.812  -17.477 1.00 40.07 ? 111 VAL   K N   1 
ATOM   13607 C  CA  . VAL   K  1 111 ? 4.477   -100.365 -18.128 1.00 36.91 ? 111 VAL   K CA  1 
ATOM   13608 C  C   . VAL   K  1 111 ? 4.312   -99.841  -19.553 1.00 36.30 ? 111 VAL   K C   1 
ATOM   13609 O  O   . VAL   K  1 111 ? 3.246   -99.996  -20.143 1.00 37.65 ? 111 VAL   K O   1 
ATOM   13610 C  CB  . VAL   K  1 111 ? 3.203   -100.130 -17.304 1.00 40.00 ? 111 VAL   K CB  1 
ATOM   13611 C  CG1 . VAL   K  1 111 ? 3.424   -100.595 -15.870 1.00 46.29 ? 111 VAL   K CG1 1 
ATOM   13612 C  CG2 . VAL   K  1 111 ? 2.776   -98.683  -17.337 1.00 41.56 ? 111 VAL   K CG2 1 
ATOM   13613 N  N   . HIS   K  1 112 ? 5.347   -99.235  -20.120 1.00 36.49 ? 112 HIS   K N   1 
ATOM   13614 C  CA  . HIS   K  1 112 ? 5.387   -98.907  -21.540 1.00 37.33 ? 112 HIS   K CA  1 
ATOM   13615 C  C   . HIS   K  1 112 ? 4.404   -97.809  -21.928 1.00 42.78 ? 112 HIS   K C   1 
ATOM   13616 O  O   . HIS   K  1 112 ? 4.004   -97.722  -23.096 1.00 38.08 ? 112 HIS   K O   1 
ATOM   13617 C  CB  . HIS   K  1 112 ? 5.145   -100.178 -22.368 1.00 36.86 ? 112 HIS   K CB  1 
ATOM   13618 C  CG  . HIS   K  1 112 ? 6.079   -101.292 -22.000 1.00 46.93 ? 112 HIS   K CG  1 
ATOM   13619 N  ND1 . HIS   K  1 112 ? 7.365   -101.058 -21.557 1.00 49.94 ? 112 HIS   K ND1 1 
ATOM   13620 C  CD2 . HIS   K  1 112 ? 5.911   -102.633 -21.970 1.00 52.20 ? 112 HIS   K CD2 1 
ATOM   13621 C  CE1 . HIS   K  1 112 ? 7.956   -102.209 -21.289 1.00 46.61 ? 112 HIS   K CE1 1 
ATOM   13622 N  NE2 . HIS   K  1 112 ? 7.096   -103.181 -21.534 1.00 58.22 ? 112 HIS   K NE2 1 
ATOM   13623 N  N   . ASP   K  1 113 ? 4.001   -96.960  -20.977 1.00 36.88 ? 113 ASP   K N   1 
ATOM   13624 C  CA  . ASP   K  1 113 ? 3.118   -95.838  -21.284 1.00 34.16 ? 113 ASP   K CA  1 
ATOM   13625 C  C   . ASP   K  1 113 ? 4.001   -94.666  -21.695 1.00 38.95 ? 113 ASP   K C   1 
ATOM   13626 O  O   . ASP   K  1 113 ? 4.211   -93.713  -20.942 1.00 33.59 ? 113 ASP   K O   1 
ATOM   13627 C  CB  . ASP   K  1 113 ? 2.243   -95.482  -20.096 1.00 35.42 ? 113 ASP   K CB  1 
ATOM   13628 C  CG  . ASP   K  1 113 ? 1.276   -94.366  -20.430 1.00 41.58 ? 113 ASP   K CG  1 
ATOM   13629 O  OD1 . ASP   K  1 113 ? 1.508   -93.667  -21.445 1.00 39.17 ? 113 ASP   K OD1 1 
ATOM   13630 O  OD2 . ASP   K  1 113 ? 0.295   -94.187  -19.694 1.00 35.25 ? 113 ASP   K OD2 1 
ATOM   13631 N  N   . TYR   K  1 114 ? 4.513   -94.748  -22.932 1.00 36.48 ? 114 TYR   K N   1 
ATOM   13632 C  CA  . TYR   K  1 114 ? 5.574   -93.846  -23.376 1.00 40.46 ? 114 TYR   K CA  1 
ATOM   13633 C  C   . TYR   K  1 114 ? 5.054   -92.439  -23.649 1.00 30.03 ? 114 TYR   K C   1 
ATOM   13634 O  O   . TYR   K  1 114 ? 5.802   -91.465  -23.493 1.00 36.00 ? 114 TYR   K O   1 
ATOM   13635 C  CB  . TYR   K  1 114 ? 6.263   -94.435  -24.617 1.00 37.75 ? 114 TYR   K CB  1 
ATOM   13636 C  CG  . TYR   K  1 114 ? 6.958   -95.762  -24.340 1.00 36.65 ? 114 TYR   K CG  1 
ATOM   13637 C  CD1 . TYR   K  1 114 ? 8.054   -95.841  -23.483 1.00 37.50 ? 114 TYR   K CD1 1 
ATOM   13638 C  CD2 . TYR   K  1 114 ? 6.507   -96.937  -24.922 1.00 41.37 ? 114 TYR   K CD2 1 
ATOM   13639 C  CE1 . TYR   K  1 114 ? 8.689   -97.057  -23.226 1.00 36.17 ? 114 TYR   K CE1 1 
ATOM   13640 C  CE2 . TYR   K  1 114 ? 7.138   -98.160  -24.669 1.00 39.48 ? 114 TYR   K CE2 1 
ATOM   13641 C  CZ  . TYR   K  1 114 ? 8.209   -98.213  -23.817 1.00 38.85 ? 114 TYR   K CZ  1 
ATOM   13642 O  OH  . TYR   K  1 114 ? 8.814   -99.429  -23.593 1.00 46.34 ? 114 TYR   K OH  1 
ATOM   13643 N  N   . VAL   K  1 115 ? 3.785   -92.313  -24.029 1.00 35.29 ? 115 VAL   K N   1 
ATOM   13644 C  CA  . VAL   K  1 115 ? 3.205   -90.995  -24.250 1.00 34.15 ? 115 VAL   K CA  1 
ATOM   13645 C  C   . VAL   K  1 115 ? 3.064   -90.255  -22.922 1.00 40.32 ? 115 VAL   K C   1 
ATOM   13646 O  O   . VAL   K  1 115 ? 3.517   -89.112  -22.786 1.00 32.43 ? 115 VAL   K O   1 
ATOM   13647 C  CB  . VAL   K  1 115 ? 1.876   -91.135  -25.005 1.00 34.14 ? 115 VAL   K CB  1 
ATOM   13648 C  CG1 . VAL   K  1 115 ? 1.184   -89.797  -25.150 1.00 31.12 ? 115 VAL   K CG1 1 
ATOM   13649 C  CG2 . VAL   K  1 115 ? 2.149   -91.733  -26.392 1.00 40.95 ? 115 VAL   K CG2 1 
ATOM   13650 N  N   . SER   K  1 116 ? 2.490   -90.911  -21.901 1.00 35.62 ? 116 SER   K N   1 
ATOM   13651 C  CA  . SER   K  1 116 ? 2.447   -90.290  -20.580 1.00 34.91 ? 116 SER   K CA  1 
ATOM   13652 C  C   . SER   K  1 116 ? 3.834   -89.883  -20.131 1.00 34.47 ? 116 SER   K C   1 
ATOM   13653 O  O   . SER   K  1 116 ? 4.013   -88.808  -19.542 1.00 33.17 ? 116 SER   K O   1 
ATOM   13654 C  CB  . SER   K  1 116 ? 1.822   -91.229  -19.552 1.00 35.81 ? 116 SER   K CB  1 
ATOM   13655 O  OG  . SER   K  1 116 ? 0.445   -91.355  -19.799 1.00 35.39 ? 116 SER   K OG  1 
ATOM   13656 N  N   . ARG   K  1 117 ? 4.844   -90.725  -20.416 1.00 37.66 ? 117 ARG   K N   1 
ATOM   13657 C  CA  . ARG   K  1 117 ? 6.203   -90.380  -20.022 1.00 35.57 ? 117 ARG   K CA  1 
ATOM   13658 C  C   . ARG   K  1 117 ? 6.644   -89.084  -20.690 1.00 38.75 ? 117 ARG   K C   1 
ATOM   13659 O  O   . ARG   K  1 117 ? 7.275   -88.228  -20.055 1.00 32.81 ? 117 ARG   K O   1 
ATOM   13660 C  CB  . ARG   K  1 117 ? 7.194   -91.499  -20.384 1.00 33.43 ? 117 ARG   K CB  1 
ATOM   13661 C  CG  . ARG   K  1 117 ? 8.626   -91.011  -20.302 1.00 30.06 ? 117 ARG   K CG  1 
ATOM   13662 C  CD  . ARG   K  1 117 ? 9.705   -92.067  -20.551 1.00 35.91 ? 117 ARG   K CD  1 
ATOM   13663 N  NE  . ARG   K  1 117 ? 11.018  -91.449  -20.537 1.00 36.71 ? 117 ARG   K NE  1 
ATOM   13664 C  CZ  . ARG   K  1 117 ? 12.132  -92.040  -20.122 1.00 35.26 ? 117 ARG   K CZ  1 
ATOM   13665 N  NH1 . ARG   K  1 117 ? 12.127  -93.276  -19.638 1.00 36.10 ? 117 ARG   K NH1 1 
ATOM   13666 N  NH2 . ARG   K  1 117 ? 13.279  -91.381  -20.205 1.00 35.40 ? 117 ARG   K NH2 1 
ATOM   13667 N  N   . ASP   K  1 118 ? 6.345   -88.945  -21.983 1.00 36.65 ? 118 ASP   K N   1 
ATOM   13668 C  CA  . ASP   K  1 118 ? 6.761   -87.764  -22.733 1.00 36.07 ? 118 ASP   K CA  1 
ATOM   13669 C  C   . ASP   K  1 118 ? 6.094   -86.504  -22.175 1.00 29.68 ? 118 ASP   K C   1 
ATOM   13670 O  O   . ASP   K  1 118 ? 6.726   -85.452  -22.058 1.00 32.64 ? 118 ASP   K O   1 
ATOM   13671 C  CB  . ASP   K  1 118 ? 6.406   -87.980  -24.207 1.00 33.30 ? 118 ASP   K CB  1 
ATOM   13672 C  CG  . ASP   K  1 118 ? 7.174   -87.075  -25.157 1.00 32.15 ? 118 ASP   K CG  1 
ATOM   13673 O  OD1 . ASP   K  1 118 ? 8.373   -86.899  -24.969 1.00 30.49 ? 118 ASP   K OD1 1 
ATOM   13674 O  OD2 . ASP   K  1 118 ? 6.564   -86.592  -26.123 1.00 39.10 ? 118 ASP   K OD2 1 
ATOM   13675 N  N   . LEU   K  1 119 ? 4.814   -86.594  -21.844 1.00 31.49 ? 119 LEU   K N   1 
ATOM   13676 C  CA  . LEU   K  1 119 ? 4.136   -85.462  -21.221 1.00 40.56 ? 119 LEU   K CA  1 
ATOM   13677 C  C   . LEU   K  1 119 ? 4.827   -85.063  -19.924 1.00 36.65 ? 119 LEU   K C   1 
ATOM   13678 O  O   . LEU   K  1 119 ? 5.113   -83.877  -19.684 1.00 29.36 ? 119 LEU   K O   1 
ATOM   13679 C  CB  . LEU   K  1 119 ? 2.676   -85.821  -20.960 1.00 30.41 ? 119 LEU   K CB  1 
ATOM   13680 C  CG  . LEU   K  1 119 ? 1.834   -84.794  -20.198 1.00 33.37 ? 119 LEU   K CG  1 
ATOM   13681 C  CD1 . LEU   K  1 119 ? 1.783   -83.472  -20.961 1.00 35.68 ? 119 LEU   K CD1 1 
ATOM   13682 C  CD2 . LEU   K  1 119 ? 0.423   -85.313  -19.958 1.00 33.00 ? 119 LEU   K CD2 1 
ATOM   13683 N  N   . LEU   K  1 120 ? 5.102   -86.050  -19.068 1.00 34.60 ? 120 LEU   K N   1 
ATOM   13684 C  CA  . LEU   K  1 120 ? 5.755   -85.764  -17.797 1.00 28.39 ? 120 LEU   K CA  1 
ATOM   13685 C  C   . LEU   K  1 120 ? 7.150   -85.203  -18.000 1.00 28.79 ? 120 LEU   K C   1 
ATOM   13686 O  O   . LEU   K  1 120 ? 7.592   -84.332  -17.237 1.00 32.60 ? 120 LEU   K O   1 
ATOM   13687 C  CB  . LEU   K  1 120 ? 5.796   -87.041  -16.943 1.00 38.63 ? 120 LEU   K CB  1 
ATOM   13688 C  CG  . LEU   K  1 120 ? 4.410   -87.580  -16.544 1.00 34.38 ? 120 LEU   K CG  1 
ATOM   13689 C  CD1 . LEU   K  1 120 ? 4.474   -88.824  -15.681 1.00 39.37 ? 120 LEU   K CD1 1 
ATOM   13690 C  CD2 . LEU   K  1 120 ? 3.653   -86.507  -15.808 1.00 42.27 ? 120 LEU   K CD2 1 
ATOM   13691 N  N   . LYS   K  1 121 ? 7.884   -85.715  -18.993 1.00 33.75 ? 121 LYS   K N   1 
ATOM   13692 C  CA  . LYS   K  1 121 ? 9.220   -85.191  -19.247 1.00 31.68 ? 121 LYS   K CA  1 
ATOM   13693 C  C   . LYS   K  1 121 ? 9.146   -83.721  -19.660 1.00 30.85 ? 121 LYS   K C   1 
ATOM   13694 O  O   . LYS   K  1 121 ? 9.951   -82.899  -19.212 1.00 29.28 ? 121 LYS   K O   1 
ATOM   13695 C  CB  . LYS   K  1 121 ? 9.920   -86.039  -20.320 1.00 30.80 ? 121 LYS   K CB  1 
ATOM   13696 C  CG  . LYS   K  1 121 ? 11.339  -85.567  -20.695 1.00 33.65 ? 121 LYS   K CG  1 
ATOM   13697 C  CD  . LYS   K  1 121 ? 11.362  -84.510  -21.805 1.00 35.22 ? 121 LYS   K CD  1 
ATOM   13698 C  CE  . LYS   K  1 121 ? 10.678  -85.023  -23.068 1.00 43.81 ? 121 LYS   K CE  1 
ATOM   13699 N  NZ  . LYS   K  1 121 ? 10.825  -84.065  -24.216 1.00 44.28 ? 121 LYS   K NZ  1 
ATOM   13700 N  N   . ASP   K  1 122 ? 8.159   -83.376  -20.495 1.00 30.20 ? 122 ASP   K N   1 
ATOM   13701 C  CA  . ASP   K  1 122 ? 7.952   -81.980  -20.880 1.00 33.48 ? 122 ASP   K CA  1 
ATOM   13702 C  C   . ASP   K  1 122 ? 7.655   -81.113  -19.663 1.00 30.45 ? 122 ASP   K C   1 
ATOM   13703 O  O   . ASP   K  1 122 ? 8.195   -80.010  -19.526 1.00 26.50 ? 122 ASP   K O   1 
ATOM   13704 C  CB  . ASP   K  1 122 ? 6.817   -81.892  -21.904 1.00 35.88 ? 122 ASP   K CB  1 
ATOM   13705 C  CG  . ASP   K  1 122 ? 7.250   -82.375  -23.271 1.00 37.15 ? 122 ASP   K CG  1 
ATOM   13706 O  OD1 . ASP   K  1 122 ? 8.474   -82.422  -23.496 1.00 37.94 ? 122 ASP   K OD1 1 
ATOM   13707 O  OD2 . ASP   K  1 122 ? 6.391   -82.717  -24.110 1.00 38.65 ? 122 ASP   K OD2 1 
ATOM   13708 N  N   . ILE   K  1 123 ? 6.815   -81.606  -18.757 1.00 31.88 ? 123 ILE   K N   1 
ATOM   13709 C  CA  . ILE   K  1 123 ? 6.517   -80.853  -17.539 1.00 30.62 ? 123 ILE   K CA  1 
ATOM   13710 C  C   . ILE   K  1 123 ? 7.764   -80.729  -16.679 1.00 26.23 ? 123 ILE   K C   1 
ATOM   13711 O  O   . ILE   K  1 123 ? 8.079   -79.644  -16.161 1.00 30.40 ? 123 ILE   K O   1 
ATOM   13712 C  CB  . ILE   K  1 123 ? 5.346   -81.515  -16.781 1.00 28.72 ? 123 ILE   K CB  1 
ATOM   13713 C  CG1 . ILE   K  1 123 ? 4.083   -81.411  -17.604 1.00 25.88 ? 123 ILE   K CG1 1 
ATOM   13714 C  CG2 . ILE   K  1 123 ? 5.128   -80.873  -15.391 1.00 31.45 ? 123 ILE   K CG2 1 
ATOM   13715 C  CD1 . ILE   K  1 123 ? 2.873   -82.169  -17.038 1.00 28.05 ? 123 ILE   K CD1 1 
ATOM   13716 N  N   . LEU   K  1 124 ? 8.526   -81.827  -16.538 1.00 27.08 ? 124 LEU   K N   1 
ATOM   13717 C  CA  . LEU   K  1 124 ? 9.766   -81.774  -15.765 1.00 26.50 ? 124 LEU   K CA  1 
ATOM   13718 C  C   . LEU   K  1 124 ? 10.730  -80.744  -16.334 1.00 30.21 ? 124 LEU   K C   1 
ATOM   13719 O  O   . LEU   K  1 124 ? 11.441  -80.057  -15.581 1.00 29.36 ? 124 LEU   K O   1 
ATOM   13720 C  CB  . LEU   K  1 124 ? 10.423  -83.165  -15.727 1.00 29.83 ? 124 LEU   K CB  1 
ATOM   13721 C  CG  . LEU   K  1 124 ? 11.811  -83.287  -15.105 1.00 33.29 ? 124 LEU   K CG  1 
ATOM   13722 C  CD1 . LEU   K  1 124 ? 11.764  -82.916  -13.648 1.00 34.55 ? 124 LEU   K CD1 1 
ATOM   13723 C  CD2 . LEU   K  1 124 ? 12.315  -84.703  -15.266 1.00 33.91 ? 124 LEU   K CD2 1 
ATOM   13724 N  N   . GLU   K  1 125 ? 10.790  -80.630  -17.666 1.00 33.03 ? 125 GLU   K N   1 
ATOM   13725 C  CA  . GLU   K  1 125 ? 11.644  -79.606  -18.269 1.00 32.18 ? 125 GLU   K CA  1 
ATOM   13726 C  C   . GLU   K  1 125 ? 11.229  -78.208  -17.837 1.00 30.96 ? 125 GLU   K C   1 
ATOM   13727 O  O   . GLU   K  1 125 ? 12.081  -77.390  -17.467 1.00 28.94 ? 125 GLU   K O   1 
ATOM   13728 C  CB  . GLU   K  1 125 ? 11.631  -79.733  -19.794 1.00 29.98 ? 125 GLU   K CB  1 
ATOM   13729 C  CG  . GLU   K  1 125 ? 12.655  -80.751  -20.229 1.00 34.88 ? 125 GLU   K CG  1 
ATOM   13730 C  CD  . GLU   K  1 125 ? 12.575  -81.202  -21.688 1.00 50.81 ? 125 GLU   K CD  1 
ATOM   13731 O  OE1 . GLU   K  1 125 ? 11.553  -80.940  -22.386 1.00 36.93 ? 125 GLU   K OE1 1 
ATOM   13732 O  OE2 . GLU   K  1 125 ? 13.565  -81.864  -22.110 1.00 39.87 ? 125 GLU   K OE2 1 
ATOM   13733 N  N   . SER   K  1 126 ? 9.924   -77.903  -17.878 1.00 29.33 ? 126 SER   K N   1 
ATOM   13734 C  CA  A SER   K  1 126 ? 9.477   -76.592  -17.416 0.50 31.25 ? 126 SER   K CA  1 
ATOM   13735 C  CA  B SER   K  1 126 ? 9.490   -76.589  -17.418 0.50 31.25 ? 126 SER   K CA  1 
ATOM   13736 C  C   . SER   K  1 126 ? 9.804   -76.392  -15.939 1.00 30.58 ? 126 SER   K C   1 
ATOM   13737 O  O   . SER   K  1 126 ? 10.287  -75.323  -15.534 1.00 26.76 ? 126 SER   K O   1 
ATOM   13738 C  CB  A SER   K  1 126 ? 7.976   -76.429  -17.667 0.50 34.04 ? 126 SER   K CB  1 
ATOM   13739 C  CB  B SER   K  1 126 ? 8.000   -76.400  -17.684 0.50 34.04 ? 126 SER   K CB  1 
ATOM   13740 O  OG  A SER   K  1 126 ? 7.455   -75.299  -16.986 0.50 39.37 ? 126 SER   K OG  1 
ATOM   13741 O  OG  B SER   K  1 126 ? 7.784   -76.078  -19.039 0.50 38.30 ? 126 SER   K OG  1 
ATOM   13742 N  N   . GLU   K  1 127 ? 9.555   -77.416  -15.115 1.00 32.27 ? 127 GLU   K N   1 
ATOM   13743 C  CA  . GLU   K  1 127 ? 9.827   -77.286  -13.684 1.00 30.48 ? 127 GLU   K CA  1 
ATOM   13744 C  C   . GLU   K  1 127 ? 11.322  -77.093  -13.395 1.00 29.58 ? 127 GLU   K C   1 
ATOM   13745 O  O   . GLU   K  1 127 ? 11.688  -76.331  -12.487 1.00 29.05 ? 127 GLU   K O   1 
ATOM   13746 C  CB  . GLU   K  1 127 ? 9.275   -78.509  -12.931 1.00 31.22 ? 127 GLU   K CB  1 
ATOM   13747 C  CG  . GLU   K  1 127 ? 7.784   -78.787  -13.086 1.00 35.28 ? 127 GLU   K CG  1 
ATOM   13748 C  CD  . GLU   K  1 127 ? 6.894   -77.570  -12.854 1.00 38.55 ? 127 GLU   K CD  1 
ATOM   13749 O  OE1 . GLU   K  1 127 ? 7.307   -76.637  -12.143 1.00 37.11 ? 127 GLU   K OE1 1 
ATOM   13750 O  OE2 . GLU   K  1 127 ? 5.779   -77.540  -13.405 1.00 49.72 ? 127 GLU   K OE2 1 
ATOM   13751 N  N   . GLU   K  1 128 ? 12.214  -77.771  -14.134 1.00 26.42 ? 128 GLU   K N   1 
ATOM   13752 C  CA  . GLU   K  1 128 ? 13.634  -77.480  -13.934 1.00 27.14 ? 128 GLU   K CA  1 
ATOM   13753 C  C   . GLU   K  1 128 ? 14.002  -76.057  -14.356 1.00 31.87 ? 128 GLU   K C   1 
ATOM   13754 O  O   . GLU   K  1 128 ? 14.866  -75.436  -13.729 1.00 26.98 ? 128 GLU   K O   1 
ATOM   13755 C  CB  . GLU   K  1 128 ? 14.520  -78.500  -14.662 1.00 26.81 ? 128 GLU   K CB  1 
ATOM   13756 C  CG  . GLU   K  1 128 ? 14.570  -79.818  -13.948 1.00 32.34 ? 128 GLU   K CG  1 
ATOM   13757 C  CD  . GLU   K  1 128 ? 15.649  -80.796  -14.442 1.00 36.91 ? 128 GLU   K CD  1 
ATOM   13758 O  OE1 . GLU   K  1 128 ? 16.581  -80.403  -15.169 1.00 33.53 ? 128 GLU   K OE1 1 
ATOM   13759 O  OE2 . GLU   K  1 128 ? 15.545  -81.984  -14.078 1.00 36.58 ? 128 GLU   K OE2 1 
ATOM   13760 N  N   . GLU   K  1 129 ? 13.358  -75.506  -15.392 1.00 33.51 ? 129 GLU   K N   1 
ATOM   13761 C  CA  . GLU   K  1 129 ? 13.612  -74.106  -15.725 1.00 26.87 ? 129 GLU   K CA  1 
ATOM   13762 C  C   . GLU   K  1 129 ? 13.145  -73.179  -14.602 1.00 25.84 ? 129 GLU   K C   1 
ATOM   13763 O  O   . GLU   K  1 129 ? 13.833  -72.210  -14.269 1.00 28.93 ? 129 GLU   K O   1 
ATOM   13764 C  CB  . GLU   K  1 129 ? 12.936  -73.730  -17.058 1.00 28.75 ? 129 GLU   K CB  1 
ATOM   13765 N  N   . HIS   K  1 130 ? 12.005  -73.467  -13.986 1.00 29.78 ? 130 HIS   K N   1 
ATOM   13766 C  CA  . HIS   K  1 130 ? 11.578  -72.658  -12.836 1.00 37.15 ? 130 HIS   K CA  1 
ATOM   13767 C  C   . HIS   K  1 130 ? 12.556  -72.778  -11.660 1.00 32.96 ? 130 HIS   K C   1 
ATOM   13768 O  O   . HIS   K  1 130 ? 12.890  -71.774  -11.007 1.00 30.19 ? 130 HIS   K O   1 
ATOM   13769 C  CB  . HIS   K  1 130 ? 10.167  -73.056  -12.413 1.00 34.43 ? 130 HIS   K CB  1 
ATOM   13770 C  CG  . HIS   K  1 130 ? 9.504   -72.069  -11.494 1.00 57.11 ? 130 HIS   K CG  1 
ATOM   13771 N  ND1 . HIS   K  1 130 ? 8.349   -72.358  -10.797 1.00 60.24 ? 130 HIS   K ND1 1 
ATOM   13772 C  CD2 . HIS   K  1 130 ? 9.826   -70.792  -11.169 1.00 57.42 ? 130 HIS   K CD2 1 
ATOM   13773 C  CE1 . HIS   K  1 130 ? 7.996   -71.310  -10.071 1.00 51.36 ? 130 HIS   K CE1 1 
ATOM   13774 N  NE2 . HIS   K  1 130 ? 8.874   -70.345  -10.280 1.00 60.21 ? 130 HIS   K NE2 1 
ATOM   13775 N  N   . ILE   K  1 131 ? 13.026  -73.994  -11.370 1.00 28.28 ? 131 ILE   K N   1 
ATOM   13776 C  CA  . ILE   K  1 131 ? 14.045  -74.166  -10.335 1.00 28.46 ? 131 ILE   K CA  1 
ATOM   13777 C  C   . ILE   K  1 131 ? 15.266  -73.309  -10.636 1.00 30.67 ? 131 ILE   K C   1 
ATOM   13778 O  O   . ILE   K  1 131 ? 15.819  -72.644  -9.745  1.00 29.77 ? 131 ILE   K O   1 
ATOM   13779 C  CB  . ILE   K  1 131 ? 14.429  -75.650  -10.192 1.00 32.65 ? 131 ILE   K CB  1 
ATOM   13780 C  CG1 . ILE   K  1 131 ? 13.305  -76.418  -9.517  1.00 30.36 ? 131 ILE   K CG1 1 
ATOM   13781 C  CG2 . ILE   K  1 131 ? 15.739  -75.778  -9.396  1.00 38.50 ? 131 ILE   K CG2 1 
ATOM   13782 C  CD1 . ILE   K  1 131 ? 13.445  -77.933  -9.586  1.00 38.30 ? 131 ILE   K CD1 1 
ATOM   13783 N  N   . ASP   K  1 132 ? 15.727  -73.333  -11.891 1.00 30.01 ? 132 ASP   K N   1 
ATOM   13784 C  CA  . ASP   K  1 132 ? 16.837  -72.458  -12.298 1.00 28.60 ? 132 ASP   K CA  1 
ATOM   13785 C  C   . ASP   K  1 132 ? 16.533  -71.000  -11.965 1.00 28.50 ? 132 ASP   K C   1 
ATOM   13786 O  O   . ASP   K  1 132 ? 17.376  -70.272  -11.424 1.00 29.96 ? 132 ASP   K O   1 
ATOM   13787 C  CB  . ASP   K  1 132 ? 17.083  -72.620  -13.807 1.00 32.44 ? 132 ASP   K CB  1 
ATOM   13788 C  CG  . ASP   K  1 132 ? 18.436  -72.042  -14.276 1.00 41.71 ? 132 ASP   K CG  1 
ATOM   13789 O  OD1 . ASP   K  1 132 ? 19.274  -71.636  -13.458 1.00 37.68 ? 132 ASP   K OD1 1 
ATOM   13790 O  OD2 . ASP   K  1 132 ? 18.661  -72.013  -15.497 1.00 42.48 ? 132 ASP   K OD2 1 
ATOM   13791 N  N   . TYR   K  1 133 ? 15.347  -70.541  -12.352 1.00 27.92 ? 133 TYR   K N   1 
ATOM   13792 C  CA  . TYR   K  1 133 ? 14.953  -69.167  -12.078 1.00 31.81 ? 133 TYR   K CA  1 
ATOM   13793 C  C   . TYR   K  1 133 ? 14.992  -68.872  -10.583 1.00 30.06 ? 133 TYR   K C   1 
ATOM   13794 O  O   . TYR   K  1 133 ? 15.557  -67.861  -10.146 1.00 29.43 ? 133 TYR   K O   1 
ATOM   13795 C  CB  . TYR   K  1 133 ? 13.551  -68.912  -12.634 1.00 29.89 ? 133 TYR   K CB  1 
ATOM   13796 C  CG  . TYR   K  1 133 ? 12.950  -67.665  -12.087 1.00 29.17 ? 133 TYR   K CG  1 
ATOM   13797 C  CD1 . TYR   K  1 133 ? 13.307  -66.429  -12.590 1.00 33.01 ? 133 TYR   K CD1 1 
ATOM   13798 C  CD2 . TYR   K  1 133 ? 12.041  -67.715  -11.040 1.00 32.18 ? 133 TYR   K CD2 1 
ATOM   13799 C  CE1 . TYR   K  1 133 ? 12.761  -65.260  -12.055 1.00 31.55 ? 133 TYR   K CE1 1 
ATOM   13800 C  CE2 . TYR   K  1 133 ? 11.487  -66.566  -10.516 1.00 38.24 ? 133 TYR   K CE2 1 
ATOM   13801 C  CZ  . TYR   K  1 133 ? 11.858  -65.342  -11.018 1.00 38.39 ? 133 TYR   K CZ  1 
ATOM   13802 O  OH  . TYR   K  1 133 ? 11.304  -64.193  -10.481 1.00 39.31 ? 133 TYR   K OH  1 
ATOM   13803 N  N   . LEU   K  1 134 ? 14.392  -69.748  -9.781  1.00 27.43 ? 134 LEU   K N   1 
ATOM   13804 C  CA  . LEU   K  1 134 ? 14.302  -69.496  -8.348  1.00 26.47 ? 134 LEU   K CA  1 
ATOM   13805 C  C   . LEU   K  1 134 ? 15.678  -69.528  -7.672  1.00 35.15 ? 134 LEU   K C   1 
ATOM   13806 O  O   . LEU   K  1 134 ? 15.968  -68.690  -6.809  1.00 29.12 ? 134 LEU   K O   1 
ATOM   13807 C  CB  . LEU   K  1 134 ? 13.368  -70.519  -7.706  1.00 26.29 ? 134 LEU   K CB  1 
ATOM   13808 C  CG  . LEU   K  1 134 ? 11.884  -70.427  -8.083  1.00 32.04 ? 134 LEU   K CG  1 
ATOM   13809 C  CD1 . LEU   K  1 134 ? 11.124  -71.698  -7.714  1.00 32.51 ? 134 LEU   K CD1 1 
ATOM   13810 C  CD2 . LEU   K  1 134 ? 11.229  -69.195  -7.443  1.00 29.09 ? 134 LEU   K CD2 1 
ATOM   13811 N  N   . GLU   K  1 135 ? 16.530  -70.491  -8.031  1.00 30.40 ? 135 GLU   K N   1 
ATOM   13812 C  CA  . GLU   K  1 135 ? 17.877  -70.537  -7.453  1.00 30.29 ? 135 GLU   K CA  1 
ATOM   13813 C  C   . GLU   K  1 135 ? 18.648  -69.284  -7.810  1.00 35.14 ? 135 GLU   K C   1 
ATOM   13814 O  O   . GLU   K  1 135 ? 19.358  -68.718  -6.974  1.00 31.61 ? 135 GLU   K O   1 
ATOM   13815 C  CB  . GLU   K  1 135 ? 18.625  -71.789  -7.943  1.00 34.71 ? 135 GLU   K CB  1 
ATOM   13816 C  CG  . GLU   K  1 135 ? 18.121  -73.098  -7.328  1.00 37.50 ? 135 GLU   K CG  1 
ATOM   13817 C  CD  . GLU   K  1 135 ? 18.749  -74.341  -7.967  1.00 39.88 ? 135 GLU   K CD  1 
ATOM   13818 O  OE1 . GLU   K  1 135 ? 19.248  -74.244  -9.106  1.00 35.14 ? 135 GLU   K OE1 1 
ATOM   13819 O  OE2 . GLU   K  1 135 ? 18.723  -75.420  -7.333  1.00 39.06 ? 135 GLU   K OE2 1 
ATOM   13820 N  N   . THR   K  1 136 ? 18.499  -68.824  -9.055  1.00 31.80 ? 136 THR   K N   1 
ATOM   13821 C  CA  . THR   K  1 136 ? 19.188  -67.627  -9.498  1.00 26.44 ? 136 THR   K CA  1 
ATOM   13822 C  C   . THR   K  1 136 ? 18.727  -66.410  -8.713  1.00 24.36 ? 136 THR   K C   1 
ATOM   13823 O  O   . THR   K  1 136 ? 19.552  -65.582  -8.309  1.00 30.44 ? 136 THR   K O   1 
ATOM   13824 C  CB  . THR   K  1 136 ? 18.953  -67.444  -11.001 1.00 36.28 ? 136 THR   K CB  1 
ATOM   13825 O  OG1 . THR   K  1 136 ? 19.353  -68.626  -11.700 1.00 32.93 ? 136 THR   K OG1 1 
ATOM   13826 C  CG2 . THR   K  1 136 ? 19.723  -66.285  -11.540 1.00 32.93 ? 136 THR   K CG2 1 
ATOM   13827 N  N   . GLN   K  1 137 ? 17.410  -66.276  -8.487  1.00 29.39 ? 137 GLN   K N   1 
ATOM   13828 C  CA  . GLN   K  1 137 ? 16.913  -65.128  -7.731  1.00 31.20 ? 137 GLN   K CA  1 
ATOM   13829 C  C   . GLN   K  1 137 ? 17.479  -65.121  -6.311  1.00 25.49 ? 137 GLN   K C   1 
ATOM   13830 O  O   . GLN   K  1 137 ? 17.884  -64.073  -5.794  1.00 24.21 ? 137 GLN   K O   1 
ATOM   13831 C  CB  . GLN   K  1 137 ? 15.375  -65.129  -7.672  1.00 27.65 ? 137 GLN   K CB  1 
ATOM   13832 C  CG  . GLN   K  1 137 ? 14.651  -65.119  -9.046  1.00 24.25 ? 137 GLN   K CG  1 
ATOM   13833 C  CD  . GLN   K  1 137 ? 15.358  -64.294  -10.083 1.00 27.61 ? 137 GLN   K CD  1 
ATOM   13834 O  OE1 . GLN   K  1 137 ? 15.835  -64.808  -11.096 1.00 32.74 ? 137 GLN   K OE1 1 
ATOM   13835 N  NE2 . GLN   K  1 137 ? 15.421  -63.012  -9.851  1.00 26.37 ? 137 GLN   K NE2 1 
ATOM   13836 N  N   . LEU   K  1 138 ? 17.428  -66.262  -5.635  1.00 27.35 ? 138 LEU   K N   1 
ATOM   13837 C  CA  . LEU   K  1 138 ? 18.011  -66.355  -4.300  1.00 30.06 ? 138 LEU   K CA  1 
ATOM   13838 C  C   . LEU   K  1 138 ? 19.488  -65.971  -4.313  1.00 33.16 ? 138 LEU   K C   1 
ATOM   13839 O  O   . LEU   K  1 138 ? 19.949  -65.252  -3.422  1.00 33.95 ? 138 LEU   K O   1 
ATOM   13840 C  CB  . LEU   K  1 138 ? 17.805  -67.761  -3.740  1.00 32.20 ? 138 LEU   K CB  1 
ATOM   13841 C  CG  . LEU   K  1 138 ? 16.333  -68.012  -3.418  1.00 30.77 ? 138 LEU   K CG  1 
ATOM   13842 C  CD1 . LEU   K  1 138 ? 16.035  -69.486  -3.227  1.00 37.99 ? 138 LEU   K CD1 1 
ATOM   13843 C  CD2 . LEU   K  1 138 ? 15.853  -67.225  -2.201  1.00 37.44 ? 138 LEU   K CD2 1 
ATOM   13844 N  N   . GLY   K  1 139 ? 20.238  -66.385  -5.346  1.00 33.87 ? 139 GLY   K N   1 
ATOM   13845 C  CA  . GLY   K  1 139 ? 21.633  -65.972  -5.429  1.00 27.38 ? 139 GLY   K CA  1 
ATOM   13846 C  C   . GLY   K  1 139 ? 21.794  -64.482  -5.650  1.00 34.02 ? 139 GLY   K C   1 
ATOM   13847 O  O   . GLY   K  1 139 ? 22.705  -63.855  -5.098  1.00 34.36 ? 139 GLY   K O   1 
ATOM   13848 N  N   . LEU   K  1 140 ? 20.928  -63.889  -6.479  1.00 29.37 ? 140 LEU   K N   1 
ATOM   13849 C  CA  . LEU   K  1 140 ? 21.061  -62.462  -6.747  1.00 28.01 ? 140 LEU   K CA  1 
ATOM   13850 C  C   . LEU   K  1 140 ? 20.848  -61.660  -5.475  1.00 24.91 ? 140 LEU   K C   1 
ATOM   13851 O  O   . LEU   K  1 140 ? 21.485  -60.626  -5.273  1.00 29.29 ? 140 LEU   K O   1 
ATOM   13852 C  CB  . LEU   K  1 140 ? 20.074  -62.016  -7.827  1.00 26.01 ? 140 LEU   K CB  1 
ATOM   13853 C  CG  . LEU   K  1 140 ? 20.479  -62.346  -9.263  1.00 26.82 ? 140 LEU   K CG  1 
ATOM   13854 C  CD1 . LEU   K  1 140 ? 19.239  -62.127  -10.209 1.00 32.84 ? 140 LEU   K CD1 1 
ATOM   13855 C  CD2 . LEU   K  1 140 ? 21.695  -61.529  -9.732  1.00 33.02 ? 140 LEU   K CD2 1 
ATOM   13856 N  N   . ILE   K  1 141 ? 19.937  -62.104  -4.624  1.00 27.45 ? 141 ILE   K N   1 
ATOM   13857 C  CA  . ILE   K  1 141 ? 19.696  -61.386  -3.383  1.00 32.05 ? 141 ILE   K CA  1 
ATOM   13858 C  C   . ILE   K  1 141 ? 20.985  -61.302  -2.584  1.00 34.11 ? 141 ILE   K C   1 
ATOM   13859 O  O   . ILE   K  1 141 ? 21.344  -60.240  -2.050  1.00 30.41 ? 141 ILE   K O   1 
ATOM   13860 C  CB  . ILE   K  1 141 ? 18.570  -62.067  -2.592  1.00 28.62 ? 141 ILE   K CB  1 
ATOM   13861 C  CG1 . ILE   K  1 141 ? 17.209  -61.741  -3.242  1.00 33.68 ? 141 ILE   K CG1 1 
ATOM   13862 C  CG2 . ILE   K  1 141 ? 18.606  -61.600  -1.143  1.00 32.14 ? 141 ILE   K CG2 1 
ATOM   13863 C  CD1 . ILE   K  1 141 ? 16.036  -62.519  -2.671  1.00 28.21 ? 141 ILE   K CD1 1 
ATOM   13864 N  N   . GLN   K  1 142 ? 21.715  -62.412  -2.523  1.00 31.70 ? 142 GLN   K N   1 
ATOM   13865 C  CA  . GLN   K  1 142 ? 23.012  -62.410  -1.837  1.00 33.03 ? 142 GLN   K CA  1 
ATOM   13866 C  C   . GLN   K  1 142 ? 24.022  -61.540  -2.565  1.00 36.71 ? 142 GLN   K C   1 
ATOM   13867 O  O   . GLN   K  1 142 ? 24.812  -60.842  -1.924  1.00 41.28 ? 142 GLN   K O   1 
ATOM   13868 C  CB  . GLN   K  1 142 ? 23.540  -63.829  -1.720  1.00 30.49 ? 142 GLN   K CB  1 
ATOM   13869 C  CG  . GLN   K  1 142 ? 22.641  -64.780  -0.956  1.00 34.38 ? 142 GLN   K CG  1 
ATOM   13870 C  CD  . GLN   K  1 142 ? 22.307  -64.319  0.459   1.00 45.87 ? 142 GLN   K CD  1 
ATOM   13871 O  OE1 . GLN   K  1 142 ? 23.184  -63.870  1.207   1.00 49.37 ? 142 GLN   K OE1 1 
ATOM   13872 N  NE2 . GLN   K  1 142 ? 21.019  -64.436  0.835   1.00 41.17 ? 142 GLN   K NE2 1 
ATOM   13873 N  N   . LYS   K  1 143 ? 24.010  -61.544  -3.905  1.00 32.84 ? 143 LYS   K N   1 
ATOM   13874 C  CA  . LYS   K  1 143 ? 25.060  -60.825  -4.625  1.00 30.63 ? 143 LYS   K CA  1 
ATOM   13875 C  C   . LYS   K  1 143 ? 24.807  -59.327  -4.666  1.00 37.88 ? 143 LYS   K C   1 
ATOM   13876 O  O   . LYS   K  1 143 ? 25.746  -58.548  -4.523  1.00 36.55 ? 143 LYS   K O   1 
ATOM   13877 C  CB  . LYS   K  1 143 ? 25.218  -61.350  -6.056  1.00 34.65 ? 143 LYS   K CB  1 
ATOM   13878 C  CG  . LYS   K  1 143 ? 25.711  -62.799  -6.139  1.00 41.33 ? 143 LYS   K CG  1 
ATOM   13879 C  CD  . LYS   K  1 143 ? 26.093  -63.232  -7.571  1.00 45.88 ? 143 LYS   K CD  1 
ATOM   13880 C  CE  . LYS   K  1 143 ? 26.575  -64.695  -7.606  1.00 41.74 ? 143 LYS   K CE  1 
ATOM   13881 N  NZ  . LYS   K  1 143 ? 25.504  -65.625  -7.137  1.00 55.28 ? 143 LYS   K NZ  1 
ATOM   13882 N  N   . VAL   K  1 144 ? 23.565  -58.879  -4.892  1.00 32.98 ? 144 VAL   K N   1 
ATOM   13883 C  CA  . VAL   K  1 144 ? 23.332  -57.437  -5.021  1.00 23.07 ? 144 VAL   K CA  1 
ATOM   13884 C  C   . VAL   K  1 144 ? 22.732  -56.851  -3.761  1.00 25.69 ? 144 VAL   K C   1 
ATOM   13885 O  O   . VAL   K  1 144 ? 22.651  -55.615  -3.646  1.00 30.93 ? 144 VAL   K O   1 
ATOM   13886 C  CB  . VAL   K  1 144 ? 22.451  -57.108  -6.253  1.00 28.28 ? 144 VAL   K CB  1 
ATOM   13887 C  CG1 . VAL   K  1 144 ? 22.933  -57.896  -7.462  1.00 29.16 ? 144 VAL   K CG1 1 
ATOM   13888 C  CG2 . VAL   K  1 144 ? 20.981  -57.400  -5.985  1.00 27.76 ? 144 VAL   K CG2 1 
ATOM   13889 N  N   . GLY   K  1 145 ? 22.326  -57.680  -2.813  1.00 27.54 ? 145 GLY   K N   1 
ATOM   13890 C  CA  . GLY   K  1 145 ? 21.694  -57.203  -1.582  1.00 31.52 ? 145 GLY   K CA  1 
ATOM   13891 C  C   . GLY   K  1 145 ? 20.191  -57.093  -1.754  1.00 31.63 ? 145 GLY   K C   1 
ATOM   13892 O  O   . GLY   K  1 145 ? 19.676  -56.888  -2.853  1.00 26.51 ? 145 GLY   K O   1 
ATOM   13893 N  N   . LEU   K  1 146 ? 19.464  -57.261  -0.646  1.00 27.86 ? 146 LEU   K N   1 
ATOM   13894 C  CA  . LEU   K  1 146 ? 18.006  -57.357  -0.751  1.00 28.19 ? 146 LEU   K CA  1 
ATOM   13895 C  C   . LEU   K  1 146 ? 17.385  -56.066  -1.278  1.00 28.50 ? 146 LEU   K C   1 
ATOM   13896 O  O   . LEU   K  1 146 ? 16.456  -56.099  -2.101  1.00 28.97 ? 146 LEU   K O   1 
ATOM   13897 C  CB  . LEU   K  1 146 ? 17.394  -57.711  0.609   1.00 34.90 ? 146 LEU   K CB  1 
ATOM   13898 C  CG  . LEU   K  1 146 ? 15.880  -57.940  0.618   1.00 33.66 ? 146 LEU   K CG  1 
ATOM   13899 C  CD1 . LEU   K  1 146 ? 15.533  -59.068  -0.325  1.00 36.65 ? 146 LEU   K CD1 1 
ATOM   13900 C  CD2 . LEU   K  1 146 ? 15.403  -58.249  2.040   1.00 34.67 ? 146 LEU   K CD2 1 
ATOM   13901 N  N   . GLU   K  1 147 ? 17.869  -54.917  -0.814  1.00 25.74 ? 147 GLU   K N   1 
ATOM   13902 C  CA  . GLU   K  1 147 ? 17.242  -53.670  -1.228  1.00 29.07 ? 147 GLU   K CA  1 
ATOM   13903 C  C   . GLU   K  1 147 ? 17.413  -53.436  -2.724  1.00 30.14 ? 147 GLU   K C   1 
ATOM   13904 O  O   . GLU   K  1 147 ? 16.463  -53.015  -3.392  1.00 25.98 ? 147 GLU   K O   1 
ATOM   13905 C  CB  . GLU   K  1 147 ? 17.795  -52.493  -0.440  1.00 28.18 ? 147 GLU   K CB  1 
ATOM   13906 C  CG  . GLU   K  1 147 ? 17.367  -52.485  1.011   1.00 32.82 ? 147 GLU   K CG  1 
ATOM   13907 C  CD  . GLU   K  1 147 ? 17.807  -51.220  1.734   1.00 45.74 ? 147 GLU   K CD  1 
ATOM   13908 O  OE1 . GLU   K  1 147 ? 18.903  -50.709  1.423   1.00 47.19 ? 147 GLU   K OE1 1 
ATOM   13909 O  OE2 . GLU   K  1 147 ? 17.047  -50.728  2.597   1.00 47.25 ? 147 GLU   K OE2 1 
ATOM   13910 N  N   . ASN   K  1 148 ? 18.620  -53.676  -3.265  1.00 24.85 ? 148 ASN   K N   1 
ATOM   13911 C  CA  . ASN   K  1 148 ? 18.812  -53.577  -4.701  1.00 25.90 ? 148 ASN   K CA  1 
ATOM   13912 C  C   . ASN   K  1 148 ? 18.005  -54.637  -5.431  1.00 25.71 ? 148 ASN   K C   1 
ATOM   13913 O  O   . ASN   K  1 148 ? 17.489  -54.393  -6.530  1.00 26.84 ? 148 ASN   K O   1 
ATOM   13914 C  CB  . ASN   K  1 148 ? 20.294  -53.738  -5.057  1.00 27.36 ? 148 ASN   K CB  1 
ATOM   13915 C  CG  . ASN   K  1 148 ? 21.079  -52.425  -5.028  1.00 27.66 ? 148 ASN   K CG  1 
ATOM   13916 O  OD1 . ASN   K  1 148 ? 20.553  -51.343  -4.748  1.00 23.32 ? 148 ASN   K OD1 1 
ATOM   13917 N  ND2 . ASN   K  1 148 ? 22.363  -52.526  -5.372  1.00 28.21 ? 148 ASN   K ND2 1 
ATOM   13918 N  N   . TYR   K  1 149 ? 17.914  -55.836  -4.866  1.00 21.86 ? 149 TYR   K N   1 
ATOM   13919 C  CA  . TYR   K  1 149 ? 17.149  -56.870  -5.530  1.00 28.10 ? 149 TYR   K CA  1 
ATOM   13920 C  C   . TYR   K  1 149 ? 15.684  -56.447  -5.671  1.00 25.21 ? 149 TYR   K C   1 
ATOM   13921 O  O   . TYR   K  1 149 ? 15.091  -56.557  -6.753  1.00 25.35 ? 149 TYR   K O   1 
ATOM   13922 C  CB  . TYR   K  1 149 ? 17.258  -58.190  -4.778  1.00 27.98 ? 149 TYR   K CB  1 
ATOM   13923 C  CG  . TYR   K  1 149 ? 16.487  -59.236  -5.501  1.00 24.63 ? 149 TYR   K CG  1 
ATOM   13924 C  CD1 . TYR   K  1 149 ? 17.026  -59.884  -6.620  1.00 31.54 ? 149 TYR   K CD1 1 
ATOM   13925 C  CD2 . TYR   K  1 149 ? 15.177  -59.533  -5.128  1.00 31.83 ? 149 TYR   K CD2 1 
ATOM   13926 C  CE1 . TYR   K  1 149 ? 16.285  -60.825  -7.313  1.00 28.96 ? 149 TYR   K CE1 1 
ATOM   13927 C  CE2 . TYR   K  1 149 ? 14.451  -60.462  -5.790  1.00 25.34 ? 149 TYR   K CE2 1 
ATOM   13928 C  CZ  . TYR   K  1 149 ? 14.978  -61.091  -6.895  1.00 30.59 ? 149 TYR   K CZ  1 
ATOM   13929 O  OH  . TYR   K  1 149 ? 14.197  -62.008  -7.561  1.00 33.50 ? 149 TYR   K OH  1 
ATOM   13930 N  N   . LEU   K  1 150 ? 15.102  -55.936  -4.582  1.00 27.93 ? 150 LEU   K N   1 
ATOM   13931 C  CA  . LEU   K  1 150 ? 13.706  -55.492  -4.597  1.00 27.38 ? 150 LEU   K CA  1 
ATOM   13932 C  C   . LEU   K  1 150 ? 13.528  -54.306  -5.541  1.00 23.26 ? 150 LEU   K C   1 
ATOM   13933 O  O   . LEU   K  1 150 ? 12.575  -54.266  -6.330  1.00 26.10 ? 150 LEU   K O   1 
ATOM   13934 C  CB  . LEU   K  1 150 ? 13.262  -55.129  -3.175  1.00 23.54 ? 150 LEU   K CB  1 
ATOM   13935 C  CG  . LEU   K  1 150 ? 13.221  -56.319  -2.203  1.00 23.37 ? 150 LEU   K CG  1 
ATOM   13936 C  CD1 . LEU   K  1 150 ? 12.763  -55.907  -0.821  1.00 27.89 ? 150 LEU   K CD1 1 
ATOM   13937 C  CD2 . LEU   K  1 150 ? 12.378  -57.474  -2.750  1.00 30.17 ? 150 LEU   K CD2 1 
ATOM   13938 N  N   . GLN   K  1 151 ? 14.445  -53.331  -5.464  1.00 25.39 ? 151 GLN   K N   1 
ATOM   13939 C  CA  . GLN   K  1 151 ? 14.417  -52.178  -6.364  1.00 24.94 ? 151 GLN   K CA  1 
ATOM   13940 C  C   . GLN   K  1 151 ? 14.316  -52.597  -7.820  1.00 30.34 ? 151 GLN   K C   1 
ATOM   13941 O  O   . GLN   K  1 151 ? 13.572  -51.986  -8.599  1.00 27.28 ? 151 GLN   K O   1 
ATOM   13942 C  CB  . GLN   K  1 151 ? 15.667  -51.318  -6.188  1.00 27.22 ? 151 GLN   K CB  1 
ATOM   13943 C  CG  . GLN   K  1 151 ? 15.655  -50.049  -7.030  1.00 26.45 ? 151 GLN   K CG  1 
ATOM   13944 C  CD  . GLN   K  1 151 ? 16.974  -49.313  -6.964  1.00 27.47 ? 151 GLN   K CD  1 
ATOM   13945 O  OE1 . GLN   K  1 151 ? 18.000  -49.910  -6.676  1.00 26.07 ? 151 GLN   K OE1 1 
ATOM   13946 N  NE2 . GLN   K  1 151 ? 16.950  -48.014  -7.222  1.00 25.49 ? 151 GLN   K NE2 1 
ATOM   13947 N  N   . SER   K  1 152 ? 15.094  -53.615  -8.215  1.00 24.82 ? 152 SER   K N   1 
ATOM   13948 C  CA  . SER   K  1 152 ? 15.148  -54.055  -9.595  1.00 26.12 ? 152 SER   K CA  1 
ATOM   13949 C  C   . SER   K  1 152 ? 13.883  -54.796  -10.012 1.00 26.92 ? 152 SER   K C   1 
ATOM   13950 O  O   . SER   K  1 152 ? 13.753  -55.158  -11.189 1.00 28.76 ? 152 SER   K O   1 
ATOM   13951 C  CB  . SER   K  1 152 ? 16.363  -54.959  -9.807  1.00 28.60 ? 152 SER   K CB  1 
ATOM   13952 O  OG  . SER   K  1 152 ? 17.587  -54.225  -9.768  1.00 28.73 ? 152 SER   K OG  1 
ATOM   13953 N  N   . HIS   K  1 153 ? 12.992  -55.085  -9.077  1.00 28.62 ? 153 HIS   K N   1 
ATOM   13954 C  CA  . HIS   K  1 153 ? 11.752  -55.793  -9.392  1.00 27.72 ? 153 HIS   K CA  1 
ATOM   13955 C  C   . HIS   K  1 153 ? 10.515  -54.948  -9.117  1.00 25.77 ? 153 HIS   K C   1 
ATOM   13956 O  O   . HIS   K  1 153 ? 9.389   -55.484  -9.064  1.00 26.63 ? 153 HIS   K O   1 
ATOM   13957 C  CB  . HIS   K  1 153 ? 11.707  -57.111  -8.642  1.00 23.00 ? 153 HIS   K CB  1 
ATOM   13958 C  CG  . HIS   K  1 153 ? 12.655  -58.105  -9.204  1.00 32.52 ? 153 HIS   K CG  1 
ATOM   13959 N  ND1 . HIS   K  1 153 ? 13.993  -58.122  -8.868  1.00 27.70 ? 153 HIS   K ND1 1 
ATOM   13960 C  CD2 . HIS   K  1 153 ? 12.485  -59.060  -10.143 1.00 29.98 ? 153 HIS   K CD2 1 
ATOM   13961 C  CE1 . HIS   K  1 153 ? 14.603  -59.060  -9.571  1.00 33.89 ? 153 HIS   K CE1 1 
ATOM   13962 N  NE2 . HIS   K  1 153 ? 13.708  -59.655  -10.340 1.00 32.09 ? 153 HIS   K NE2 1 
ATOM   13963 N  N   . MET   K  1 154 ? 10.701  -53.635  -9.011  1.00 24.78 ? 154 MET   K N   1 
ATOM   13964 C  CA  . MET   K  1 154 ? 9.581   -52.725  -8.800  1.00 34.32 ? 154 MET   K CA  1 
ATOM   13965 C  C   . MET   K  1 154 ? 8.789   -52.503  -10.082 1.00 37.50 ? 154 MET   K C   1 
ATOM   13966 O  O   . MET   K  1 154 ? 7.547   -52.515  -10.062 1.00 33.37 ? 154 MET   K O   1 
ATOM   13967 C  CB  . MET   K  1 154 ? 10.083  -51.376  -8.294  1.00 28.87 ? 154 MET   K CB  1 
ATOM   13968 C  CG  . MET   K  1 154 ? 10.289  -51.266  -6.806  1.00 37.24 ? 154 MET   K CG  1 
ATOM   13969 S  SD  . MET   K  1 154 ? 11.091  -49.704  -6.355  1.00 45.41 ? 154 MET   K SD  1 
ATOM   13970 C  CE  . MET   K  1 154 ? 10.088  -48.499  -7.230  1.00 38.31 ? 154 MET   K CE  1 
ATOM   13971 N  N   . HIS   K  1 155 ? 9.496   -52.286  -11.188 1.00 36.57 ? 155 HIS   K N   1 
ATOM   13972 C  CA  . HIS   K  1 155 ? 8.932   -51.891  -12.473 1.00 46.36 ? 155 HIS   K CA  1 
ATOM   13973 C  C   . HIS   K  1 155 ? 9.124   -53.009  -13.501 1.00 49.39 ? 155 HIS   K C   1 
ATOM   13974 O  O   . HIS   K  1 155 ? 10.093  -53.773  -13.452 1.00 42.15 ? 155 HIS   K O   1 
ATOM   13975 C  CB  . HIS   K  1 155 ? 9.606   -50.582  -12.971 1.00 42.45 ? 155 HIS   K CB  1 
ATOM   13976 C  CG  . HIS   K  1 155 ? 9.409   -49.402  -12.061 1.00 49.08 ? 155 HIS   K CG  1 
ATOM   13977 N  ND1 . HIS   K  1 155 ? 10.393  -48.457  -11.831 1.00 52.05 ? 155 HIS   K ND1 1 
ATOM   13978 C  CD2 . HIS   K  1 155 ? 8.338   -49.011  -11.325 1.00 60.82 ? 155 HIS   K CD2 1 
ATOM   13979 C  CE1 . HIS   K  1 155 ? 9.934   -47.538  -10.997 1.00 45.37 ? 155 HIS   K CE1 1 
ATOM   13980 N  NE2 . HIS   K  1 155 ? 8.692   -47.853  -10.668 1.00 51.02 ? 155 HIS   K NE2 1 
ATOM   13981 N  N   . GLU   K  1 156 ? 8.207   -53.107  -14.451 1.00 63.18 ? 156 GLU   K N   1 
ATOM   13982 C  CA  . GLU   K  1 156 ? 8.360   -54.097  -15.525 1.00 58.69 ? 156 GLU   K CA  1 
ATOM   13983 C  C   . GLU   K  1 156 ? 9.129   -53.543  -16.726 1.00 51.43 ? 156 GLU   K C   1 
ATOM   13984 O  O   . GLU   K  1 156 ? 9.404   -52.339  -16.808 1.00 61.77 ? 156 GLU   K O   1 
ATOM   13985 C  CB  . GLU   K  1 156 ? 6.990   -54.590  -15.968 1.00 60.95 ? 156 GLU   K CB  1 
ATOM   13986 C  CG  . GLU   K  1 156 ? 5.985   -54.583  -14.830 1.00 55.41 ? 156 GLU   K CG  1 
ATOM   13987 C  CD  . GLU   K  1 156 ? 4.707   -55.314  -15.168 1.00 75.33 ? 156 GLU   K CD  1 
ATOM   13988 O  OE1 . GLU   K  1 156 ? 4.705   -56.096  -16.148 1.00 75.59 ? 156 GLU   K OE1 1 
ATOM   13989 O  OE2 . GLU   K  1 156 ? 3.702   -55.102  -14.455 1.00 64.61 ? 156 GLU   K OE2 1 
ATOM   13990 N  N   . MET   L  1 1   ? 8.907   -1.806   -75.292 1.00 38.15 ? 1   MET   L N   1 
ATOM   13991 C  CA  . MET   L  1 1   ? 8.128   -1.374   -76.514 1.00 40.11 ? 1   MET   L CA  1 
ATOM   13992 C  C   . MET   L  1 1   ? 7.509   -0.011   -76.180 1.00 41.46 ? 1   MET   L C   1 
ATOM   13993 O  O   . MET   L  1 1   ? 6.947   0.157    -75.101 1.00 42.31 ? 1   MET   L O   1 
ATOM   13994 C  CB  . MET   L  1 1   ? 7.069   -2.424   -76.881 1.00 38.15 ? 1   MET   L CB  1 
ATOM   13995 C  CG  . MET   L  1 1   ? 6.495   -2.344   -78.307 1.00 43.63 ? 1   MET   L CG  1 
ATOM   13996 S  SD  . MET   L  1 1   ? 5.161   -3.529   -78.563 1.00 43.22 ? 1   MET   L SD  1 
ATOM   13997 C  CE  . MET   L  1 1   ? 3.766   -2.618   -77.935 1.00 54.31 ? 1   MET   L CE  1 
ATOM   13998 N  N   . LYS   L  1 2   ? 7.629   0.984    -77.053 1.00 40.31 ? 2   LYS   L N   1 
ATOM   13999 C  CA  . LYS   L  1 2   ? 7.283   2.345    -76.642 1.00 38.70 ? 2   LYS   L CA  1 
ATOM   14000 C  C   . LYS   L  1 2   ? 5.773   2.506    -76.785 1.00 34.99 ? 2   LYS   L C   1 
ATOM   14001 O  O   . LYS   L  1 2   ? 5.228   2.433    -77.890 1.00 40.54 ? 2   LYS   L O   1 
ATOM   14002 C  CB  . LYS   L  1 2   ? 8.071   3.385    -77.444 1.00 35.37 ? 2   LYS   L CB  1 
ATOM   14003 N  N   . GLY   L  1 3   ? 5.078   2.662    -75.655 1.00 34.37 ? 3   GLY   L N   1 
ATOM   14004 C  CA  . GLY   L  1 3   ? 3.649   2.832    -75.698 1.00 33.88 ? 3   GLY   L CA  1 
ATOM   14005 C  C   . GLY   L  1 3   ? 3.211   4.260    -76.001 1.00 34.89 ? 3   GLY   L C   1 
ATOM   14006 O  O   . GLY   L  1 3   ? 3.991   5.212    -75.960 1.00 40.44 ? 3   GLY   L O   1 
ATOM   14007 N  N   . ASP   L  1 4   ? 1.927   4.351    -76.321 1.00 34.77 ? 4   ASP   L N   1 
ATOM   14008 C  CA  . ASP   L  1 4   ? 1.206   5.604    -76.485 1.00 38.89 ? 4   ASP   L CA  1 
ATOM   14009 C  C   . ASP   L  1 4   ? 1.154   6.352    -75.163 1.00 48.94 ? 4   ASP   L C   1 
ATOM   14010 O  O   . ASP   L  1 4   ? 0.785   5.783    -74.126 1.00 37.73 ? 4   ASP   L O   1 
ATOM   14011 C  CB  . ASP   L  1 4   ? -0.195  5.276    -77.008 1.00 34.69 ? 4   ASP   L CB  1 
ATOM   14012 C  CG  . ASP   L  1 4   ? -1.118  6.496    -77.110 1.00 44.66 ? 4   ASP   L CG  1 
ATOM   14013 O  OD1 . ASP   L  1 4   ? -1.799  6.833    -76.119 1.00 41.11 ? 4   ASP   L OD1 1 
ATOM   14014 O  OD2 . ASP   L  1 4   ? -1.205  7.103    -78.195 1.00 44.20 ? 4   ASP   L OD2 1 
ATOM   14015 N  N   . LYS   L  1 5   ? 1.560   7.626    -75.199 1.00 38.32 ? 5   LYS   L N   1 
ATOM   14016 C  CA  . LYS   L  1 5   ? 1.716   8.391    -73.965 1.00 39.53 ? 5   LYS   L CA  1 
ATOM   14017 C  C   . LYS   L  1 5   ? 0.410   8.456    -73.196 1.00 37.25 ? 5   LYS   L C   1 
ATOM   14018 O  O   . LYS   L  1 5   ? 0.397   8.296    -71.972 1.00 40.92 ? 5   LYS   L O   1 
ATOM   14019 C  CB  . LYS   L  1 5   ? 2.232   9.807    -74.263 1.00 43.88 ? 5   LYS   L CB  1 
ATOM   14020 C  CG  . LYS   L  1 5   ? 2.433   10.686   -73.019 1.00 46.46 ? 5   LYS   L CG  1 
ATOM   14021 N  N   . LYS   L  1 6   ? -0.699  8.688    -73.889 1.00 35.36 ? 6   LYS   L N   1 
ATOM   14022 C  CA  . LYS   L  1 6   ? -1.956  8.823    -73.178 1.00 37.89 ? 6   LYS   L CA  1 
ATOM   14023 C  C   . LYS   L  1 6   ? -2.468  7.471    -72.679 1.00 39.63 ? 6   LYS   L C   1 
ATOM   14024 O  O   . LYS   L  1 6   ? -3.141  7.413    -71.643 1.00 34.53 ? 6   LYS   L O   1 
ATOM   14025 C  CB  . LYS   L  1 6   ? -2.987  9.512    -74.077 1.00 42.76 ? 6   LYS   L CB  1 
ATOM   14026 C  CG  . LYS   L  1 6   ? -4.319  9.799    -73.394 1.00 50.27 ? 6   LYS   L CG  1 
ATOM   14027 C  CD  . LYS   L  1 6   ? -4.160  10.610   -72.090 1.00 56.13 ? 6   LYS   L CD  1 
ATOM   14028 C  CE  . LYS   L  1 6   ? -5.516  11.148   -71.561 1.00 59.82 ? 6   LYS   L CE  1 
ATOM   14029 N  NZ  . LYS   L  1 6   ? -5.671  11.027   -70.046 1.00 65.74 ? 6   LYS   L NZ  1 
ATOM   14030 N  N   . VAL   L  1 7   ? -2.160  6.374    -73.382 1.00 38.68 ? 7   VAL   L N   1 
ATOM   14031 C  CA  . VAL   L  1 7   ? -2.485  5.059    -72.837 1.00 35.93 ? 7   VAL   L CA  1 
ATOM   14032 C  C   . VAL   L  1 7   ? -1.784  4.868    -71.491 1.00 30.25 ? 7   VAL   L C   1 
ATOM   14033 O  O   . VAL   L  1 7   ? -2.405  4.468    -70.502 1.00 32.25 ? 7   VAL   L O   1 
ATOM   14034 C  CB  . VAL   L  1 7   ? -2.124  3.943    -73.834 1.00 38.52 ? 7   VAL   L CB  1 
ATOM   14035 C  CG1 . VAL   L  1 7   ? -2.045  2.609    -73.113 1.00 42.00 ? 7   VAL   L CG1 1 
ATOM   14036 C  CG2 . VAL   L  1 7   ? -3.171  3.854    -74.954 1.00 39.54 ? 7   VAL   L CG2 1 
ATOM   14037 N  N   . ILE   L  1 8   ? -0.492  5.188    -71.422 1.00 32.28 ? 8   ILE   L N   1 
ATOM   14038 C  CA  . ILE   L  1 8   ? 0.230   5.045    -70.160 1.00 38.65 ? 8   ILE   L CA  1 
ATOM   14039 C  C   . ILE   L  1 8   ? -0.366  5.936    -69.071 1.00 38.18 ? 8   ILE   L C   1 
ATOM   14040 O  O   . ILE   L  1 8   ? -0.412  5.548    -67.897 1.00 32.55 ? 8   ILE   L O   1 
ATOM   14041 C  CB  . ILE   L  1 8   ? 1.714   5.336    -70.396 1.00 36.70 ? 8   ILE   L CB  1 
ATOM   14042 C  CG1 . ILE   L  1 8   ? 2.279   4.242    -71.291 1.00 37.39 ? 8   ILE   L CG1 1 
ATOM   14043 C  CG2 . ILE   L  1 8   ? 2.466   5.451    -69.075 1.00 31.85 ? 8   ILE   L CG2 1 
ATOM   14044 C  CD1 . ILE   L  1 8   ? 3.629   4.597    -71.891 1.00 40.08 ? 8   ILE   L CD1 1 
ATOM   14045 N  N   . GLN   L  1 9   ? -0.836  7.130    -69.431 1.00 35.37 ? 9   GLN   L N   1 
ATOM   14046 C  CA  . GLN   L  1 9   ? -1.483  7.992    -68.447 1.00 35.41 ? 9   GLN   L CA  1 
ATOM   14047 C  C   . GLN   L  1 9   ? -2.783  7.374    -67.936 1.00 36.74 ? 9   GLN   L C   1 
ATOM   14048 O  O   . GLN   L  1 9   ? -3.049  7.380    -66.724 1.00 35.31 ? 9   GLN   L O   1 
ATOM   14049 C  CB  . GLN   L  1 9   ? -1.730  9.373    -69.068 1.00 35.92 ? 9   GLN   L CB  1 
ATOM   14050 C  CG  . GLN   L  1 9   ? -0.436  10.129   -69.304 1.00 34.44 ? 9   GLN   L CG  1 
ATOM   14051 C  CD  . GLN   L  1 9   ? -0.635  11.491   -69.944 1.00 44.61 ? 9   GLN   L CD  1 
ATOM   14052 O  OE1 . GLN   L  1 9   ? -1.589  11.711   -70.687 1.00 46.10 ? 9   GLN   L OE1 1 
ATOM   14053 N  NE2 . GLN   L  1 9   ? 0.278   12.415   -69.649 1.00 53.23 ? 9   GLN   L NE2 1 
ATOM   14054 N  N   . HIS   L  1 10  ? -3.594  6.824    -68.839 1.00 31.46 ? 10  HIS   L N   1 
ATOM   14055 C  CA  . HIS   L  1 10  ? -4.774  6.077    -68.416 1.00 35.84 ? 10  HIS   L CA  1 
ATOM   14056 C  C   . HIS   L  1 10  ? -4.405  4.920    -67.488 1.00 30.93 ? 10  HIS   L C   1 
ATOM   14057 O  O   . HIS   L  1 10  ? -5.090  4.673    -66.489 1.00 31.78 ? 10  HIS   L O   1 
ATOM   14058 C  CB  . HIS   L  1 10  ? -5.498  5.543    -69.638 1.00 33.26 ? 10  HIS   L CB  1 
ATOM   14059 C  CG  . HIS   L  1 10  ? -6.497  6.491    -70.225 1.00 35.60 ? 10  HIS   L CG  1 
ATOM   14060 N  ND1 . HIS   L  1 10  ? -7.627  6.891    -69.551 1.00 33.13 ? 10  HIS   L ND1 1 
ATOM   14061 C  CD2 . HIS   L  1 10  ? -6.556  7.078    -71.447 1.00 37.44 ? 10  HIS   L CD2 1 
ATOM   14062 C  CE1 . HIS   L  1 10  ? -8.328  7.704    -70.320 1.00 43.41 ? 10  HIS   L CE1 1 
ATOM   14063 N  NE2 . HIS   L  1 10  ? -7.694  7.840    -71.474 1.00 39.99 ? 10  HIS   L NE2 1 
ATOM   14064 N  N   . LEU   L  1 11  ? -3.347  4.175    -67.825 1.00 36.04 ? 11  LEU   L N   1 
ATOM   14065 C  CA  . LEU   L  1 11  ? -2.954  3.030    -67.006 1.00 35.55 ? 11  LEU   L CA  1 
ATOM   14066 C  C   . LEU   L  1 11  ? -2.509  3.474    -65.619 1.00 31.52 ? 11  LEU   L C   1 
ATOM   14067 O  O   . LEU   L  1 11  ? -2.833  2.825    -64.615 1.00 32.06 ? 11  LEU   L O   1 
ATOM   14068 C  CB  . LEU   L  1 11  ? -1.838  2.241    -67.701 1.00 26.96 ? 11  LEU   L CB  1 
ATOM   14069 C  CG  . LEU   L  1 11  ? -2.241  1.484    -68.986 1.00 26.02 ? 11  LEU   L CG  1 
ATOM   14070 C  CD1 . LEU   L  1 11  ? -1.031  0.804    -69.627 1.00 37.42 ? 11  LEU   L CD1 1 
ATOM   14071 C  CD2 . LEU   L  1 11  ? -3.344  0.484    -68.724 1.00 30.55 ? 11  LEU   L CD2 1 
ATOM   14072 N  N   . ASN   L  1 12  ? -1.744  4.563    -65.535 1.00 33.34 ? 12  ASN   L N   1 
ATOM   14073 C  CA  . ASN   L  1 12  ? -1.377  5.080    -64.220 1.00 38.12 ? 12  ASN   L CA  1 
ATOM   14074 C  C   . ASN   L  1 12  ? -2.599  5.553    -63.444 1.00 32.86 ? 12  ASN   L C   1 
ATOM   14075 O  O   . ASN   L  1 12  ? -2.657  5.394    -62.220 1.00 28.96 ? 12  ASN   L O   1 
ATOM   14076 C  CB  . ASN   L  1 12  ? -0.341  6.201    -64.359 1.00 28.80 ? 12  ASN   L CB  1 
ATOM   14077 C  CG  . ASN   L  1 12  ? 1.067   5.700    -64.164 1.00 36.92 ? 12  ASN   L CG  1 
ATOM   14078 O  OD1 . ASN   L  1 12  ? 1.308   4.831    -63.325 1.00 32.52 ? 12  ASN   L OD1 1 
ATOM   14079 N  ND2 . ASN   L  1 12  ? 2.004   6.209    -64.960 1.00 38.10 ? 12  ASN   L ND2 1 
ATOM   14080 N  N   . LYS   L  1 13  ? -3.617  6.075    -64.129 1.00 35.03 ? 13  LYS   L N   1 
ATOM   14081 C  CA  . LYS   L  1 13  ? -4.819  6.482    -63.407 1.00 31.32 ? 13  LYS   L CA  1 
ATOM   14082 C  C   . LYS   L  1 13  ? -5.572  5.270    -62.862 1.00 37.32 ? 13  LYS   L C   1 
ATOM   14083 O  O   . LYS   L  1 13  ? -6.084  5.302    -61.731 1.00 29.77 ? 13  LYS   L O   1 
ATOM   14084 C  CB  . LYS   L  1 13  ? -5.728  7.312    -64.320 1.00 36.84 ? 13  LYS   L CB  1 
ATOM   14085 C  CG  . LYS   L  1 13  ? -7.012  7.815    -63.639 1.00 39.01 ? 13  LYS   L CG  1 
ATOM   14086 C  CD  . LYS   L  1 13  ? -7.852  8.710    -64.573 1.00 46.48 ? 13  LYS   L CD  1 
ATOM   14087 C  CE  . LYS   L  1 13  ? -8.964  9.422    -63.802 1.00 49.96 ? 13  LYS   L CE  1 
ATOM   14088 N  NZ  . LYS   L  1 13  ? -9.908  10.172   -64.679 1.00 45.80 ? 13  LYS   L NZ  1 
ATOM   14089 N  N   . ILE   L  1 14  ? -5.685  4.205    -63.662 1.00 34.39 ? 14  ILE   L N   1 
ATOM   14090 C  CA  . ILE   L  1 14  ? -6.307  2.977    -63.176 1.00 31.93 ? 14  ILE   L CA  1 
ATOM   14091 C  C   . ILE   L  1 14  ? -5.518  2.437    -61.992 1.00 27.45 ? 14  ILE   L C   1 
ATOM   14092 O  O   . ILE   L  1 14  ? -6.097  2.039    -60.973 1.00 30.99 ? 14  ILE   L O   1 
ATOM   14093 C  CB  . ILE   L  1 14  ? -6.411  1.931    -64.307 1.00 31.43 ? 14  ILE   L CB  1 
ATOM   14094 C  CG1 . ILE   L  1 14  ? -7.192  2.476    -65.511 1.00 31.60 ? 14  ILE   L CG1 1 
ATOM   14095 C  CG2 . ILE   L  1 14  ? -7.065  0.647    -63.806 1.00 33.00 ? 14  ILE   L CG2 1 
ATOM   14096 C  CD1 . ILE   L  1 14  ? -8.540  3.125    -65.187 1.00 41.14 ? 14  ILE   L CD1 1 
ATOM   14097 N  N   . LEU   L  1 15  ? -4.182  2.447    -62.103 1.00 31.56 ? 15  LEU   L N   1 
ATOM   14098 C  CA  . LEU   L  1 15  ? -3.314  2.007    -61.013 1.00 35.10 ? 15  LEU   L CA  1 
ATOM   14099 C  C   . LEU   L  1 15  ? -3.544  2.829    -59.754 1.00 39.33 ? 15  LEU   L C   1 
ATOM   14100 O  O   . LEU   L  1 15  ? -3.563  2.283    -58.639 1.00 33.68 ? 15  LEU   L O   1 
ATOM   14101 C  CB  . LEU   L  1 15  ? -1.851  2.104    -61.439 1.00 35.34 ? 15  LEU   L CB  1 
ATOM   14102 C  CG  . LEU   L  1 15  ? -0.746  1.838    -60.410 1.00 31.88 ? 15  LEU   L CG  1 
ATOM   14103 C  CD1 . LEU   L  1 15  ? -0.911  0.490    -59.766 1.00 36.04 ? 15  LEU   L CD1 1 
ATOM   14104 C  CD2 . LEU   L  1 15  ? 0.595   1.930    -61.101 1.00 33.40 ? 15  LEU   L CD2 1 
ATOM   14105 N  N   . GLY   L  1 16  ? -3.668  4.148    -59.908 1.00 33.60 ? 16  GLY   L N   1 
ATOM   14106 C  CA  . GLY   L  1 16  ? -3.967  4.989    -58.761 1.00 34.44 ? 16  GLY   L CA  1 
ATOM   14107 C  C   . GLY   L  1 16  ? -5.251  4.588    -58.062 1.00 31.22 ? 16  GLY   L C   1 
ATOM   14108 O  O   . GLY   L  1 16  ? -5.337  4.628    -56.825 1.00 34.82 ? 16  GLY   L O   1 
ATOM   14109 N  N   . ASN   L  1 17  ? -6.283  4.246    -58.841 1.00 31.49 ? 17  ASN   L N   1 
ATOM   14110 C  CA  . ASN   L  1 17  ? -7.506  3.714    -58.255 1.00 34.02 ? 17  ASN   L CA  1 
ATOM   14111 C  C   . ASN   L  1 17  ? -7.227  2.426    -57.497 1.00 33.69 ? 17  ASN   L C   1 
ATOM   14112 O  O   . ASN   L  1 17  ? -7.796  2.192    -56.429 1.00 29.13 ? 17  ASN   L O   1 
ATOM   14113 C  CB  . ASN   L  1 17  ? -8.548  3.453    -59.333 1.00 35.87 ? 17  ASN   L CB  1 
ATOM   14114 C  CG  . ASN   L  1 17  ? -9.139  4.718    -59.888 1.00 43.15 ? 17  ASN   L CG  1 
ATOM   14115 O  OD1 . ASN   L  1 17  ? -9.106  5.757    -59.245 1.00 36.84 ? 17  ASN   L OD1 1 
ATOM   14116 N  ND2 . ASN   L  1 17  ? -9.713  4.632    -61.080 1.00 31.84 ? 17  ASN   L ND2 1 
ATOM   14117 N  N   . GLU   L  1 18  ? -6.352  1.573    -58.038 1.00 30.43 ? 18  GLU   L N   1 
ATOM   14118 C  CA  . GLU   L  1 18  ? -6.090  0.295    -57.384 1.00 33.24 ? 18  GLU   L CA  1 
ATOM   14119 C  C   . GLU   L  1 18  ? -5.390  0.510    -56.056 1.00 27.24 ? 18  GLU   L C   1 
ATOM   14120 O  O   . GLU   L  1 18  ? -5.675  -0.194   -55.080 1.00 28.78 ? 18  GLU   L O   1 
ATOM   14121 C  CB  . GLU   L  1 18  ? -5.253  -0.617   -58.292 1.00 33.44 ? 18  GLU   L CB  1 
ATOM   14122 C  CG  . GLU   L  1 18  ? -5.955  -0.986   -59.605 1.00 37.57 ? 18  GLU   L CG  1 
ATOM   14123 C  CD  . GLU   L  1 18  ? -7.037  -1.972   -59.409 1.00 36.83 ? 18  GLU   L CD  1 
ATOM   14124 O  OE1 . GLU   L  1 18  ? -7.237  -2.412   -58.249 1.00 42.45 ? 18  GLU   L OE1 1 
ATOM   14125 O  OE2 . GLU   L  1 18  ? -7.675  -2.334   -60.412 1.00 42.38 ? 18  GLU   L OE2 1 
ATOM   14126 N  N   . LEU   L  1 19  ? -4.492  1.502    -55.984 1.00 29.05 ? 19  LEU   L N   1 
ATOM   14127 C  CA  . LEU   L  1 19  ? -3.753  1.730    -54.748 1.00 28.08 ? 19  LEU   L CA  1 
ATOM   14128 C  C   . LEU   L  1 19  ? -4.674  2.227    -53.641 1.00 34.54 ? 19  LEU   L C   1 
ATOM   14129 O  O   . LEU   L  1 19  ? -4.510  1.860    -52.467 1.00 29.74 ? 19  LEU   L O   1 
ATOM   14130 C  CB  . LEU   L  1 19  ? -2.620  2.723    -54.978 1.00 29.56 ? 19  LEU   L CB  1 
ATOM   14131 C  CG  . LEU   L  1 19  ? -1.565  2.277    -55.979 1.00 38.51 ? 19  LEU   L CG  1 
ATOM   14132 C  CD1 . LEU   L  1 19  ? -0.724  3.478    -56.417 1.00 50.11 ? 19  LEU   L CD1 1 
ATOM   14133 C  CD2 . LEU   L  1 19  ? -0.679  1.193    -55.372 1.00 39.67 ? 19  LEU   L CD2 1 
ATOM   14134 N  N   . ILE   L  1 20  ? -5.646  3.058    -54.001 1.00 29.42 ? 20  ILE   L N   1 
ATOM   14135 C  CA  . ILE   L  1 20  ? -6.693  3.455    -53.072 1.00 31.42 ? 20  ILE   L CA  1 
ATOM   14136 C  C   . ILE   L  1 20  ? -7.448  2.233    -52.572 1.00 28.59 ? 20  ILE   L C   1 
ATOM   14137 O  O   . ILE   L  1 20  ? -7.615  2.033    -51.363 1.00 31.82 ? 20  ILE   L O   1 
ATOM   14138 C  CB  . ILE   L  1 20  ? -7.657  4.444    -53.756 1.00 28.22 ? 20  ILE   L CB  1 
ATOM   14139 C  CG1 . ILE   L  1 20  ? -6.941  5.758    -54.086 1.00 31.69 ? 20  ILE   L CG1 1 
ATOM   14140 C  CG2 . ILE   L  1 20  ? -8.869  4.708    -52.856 1.00 31.91 ? 20  ILE   L CG2 1 
ATOM   14141 C  CD1 . ILE   L  1 20  ? -7.729  6.649    -55.043 1.00 33.33 ? 20  ILE   L CD1 1 
ATOM   14142 N  N   . ALA   L  1 21  ? -7.923  1.405    -53.502 1.00 26.56 ? 21  ALA   L N   1 
ATOM   14143 C  CA  . ALA   L  1 21  ? -8.778  0.282    -53.128 1.00 32.65 ? 21  ALA   L CA  1 
ATOM   14144 C  C   . ALA   L  1 21  ? -8.029  -0.714   -52.244 1.00 27.64 ? 21  ALA   L C   1 
ATOM   14145 O  O   . ALA   L  1 21  ? -8.575  -1.192   -51.241 1.00 29.74 ? 21  ALA   L O   1 
ATOM   14146 C  CB  . ALA   L  1 21  ? -9.310  -0.409   -54.382 1.00 27.96 ? 21  ALA   L CB  1 
ATOM   14147 N  N   . ILE   L  1 22  ? -6.775  -1.022   -52.594 1.00 25.81 ? 22  ILE   L N   1 
ATOM   14148 C  CA  . ILE   L  1 22  ? -5.950  -1.908   -51.766 1.00 28.07 ? 22  ILE   L CA  1 
ATOM   14149 C  C   . ILE   L  1 22  ? -5.975  -1.459   -50.308 1.00 29.56 ? 22  ILE   L C   1 
ATOM   14150 O  O   . ILE   L  1 22  ? -6.263  -2.248   -49.397 1.00 24.53 ? 22  ILE   L O   1 
ATOM   14151 C  CB  . ILE   L  1 22  ? -4.502  -1.952   -52.290 1.00 30.11 ? 22  ILE   L CB  1 
ATOM   14152 C  CG1 . ILE   L  1 22  ? -4.394  -2.711   -53.626 1.00 27.32 ? 22  ILE   L CG1 1 
ATOM   14153 C  CG2 . ILE   L  1 22  ? -3.612  -2.600   -51.281 1.00 28.17 ? 22  ILE   L CG2 1 
ATOM   14154 C  CD1 . ILE   L  1 22  ? -3.048  -2.528   -54.296 1.00 29.55 ? 22  ILE   L CD1 1 
ATOM   14155 N  N   . ASN   L  1 23  ? -5.616  -0.193   -50.062 1.00 29.69 ? 23  ASN   L N   1 
ATOM   14156 C  CA  . ASN   L  1 23  ? -5.520  0.294    -48.684 1.00 32.29 ? 23  ASN   L CA  1 
ATOM   14157 C  C   . ASN   L  1 23  ? -6.885  0.374    -48.036 1.00 28.10 ? 23  ASN   L C   1 
ATOM   14158 O  O   . ASN   L  1 23  ? -7.046  0.052    -46.844 1.00 26.40 ? 23  ASN   L O   1 
ATOM   14159 C  CB  . ASN   L  1 23  ? -4.850  1.669    -48.641 1.00 29.28 ? 23  ASN   L CB  1 
ATOM   14160 C  CG  . ASN   L  1 23  ? -3.376  1.589    -48.868 1.00 36.05 ? 23  ASN   L CG  1 
ATOM   14161 O  OD1 . ASN   L  1 23  ? -2.873  0.543    -49.254 1.00 33.82 ? 23  ASN   L OD1 1 
ATOM   14162 N  ND2 . ASN   L  1 23  ? -2.663  2.691    -48.635 1.00 39.39 ? 23  ASN   L ND2 1 
ATOM   14163 N  N   . GLN   L  1 24  ? -7.875  0.835    -48.797 1.00 26.74 ? 24  GLN   L N   1 
ATOM   14164 C  CA  . GLN   L  1 24  ? -9.214  0.985    -48.258 1.00 33.74 ? 24  GLN   L CA  1 
ATOM   14165 C  C   . GLN   L  1 24  ? -9.807  -0.361   -47.880 1.00 28.44 ? 24  GLN   L C   1 
ATOM   14166 O  O   . GLN   L  1 24  ? -10.393 -0.516   -46.802 1.00 26.16 ? 24  GLN   L O   1 
ATOM   14167 C  CB  . GLN   L  1 24  ? -10.099 1.689    -49.277 1.00 30.03 ? 24  GLN   L CB  1 
ATOM   14168 C  CG  . GLN   L  1 24  ? -11.523 1.890    -48.843 1.00 30.33 ? 24  GLN   L CG  1 
ATOM   14169 C  CD  . GLN   L  1 24  ? -12.332 2.682    -49.898 1.00 29.63 ? 24  GLN   L CD  1 
ATOM   14170 O  OE1 . GLN   L  1 24  ? -11.879 3.712    -50.389 1.00 32.66 ? 24  GLN   L OE1 1 
ATOM   14171 N  NE2 . GLN   L  1 24  ? -13.486 2.176    -50.265 1.00 28.36 ? 24  GLN   L NE2 1 
ATOM   14172 N  N   . TYR   L  1 25  ? -9.698  -1.343   -48.771 1.00 30.82 ? 25  TYR   L N   1 
ATOM   14173 C  CA  . TYR   L  1 25  ? -10.245 -2.653   -48.449 1.00 28.19 ? 25  TYR   L CA  1 
ATOM   14174 C  C   . TYR   L  1 25  ? -9.450  -3.308   -47.328 1.00 25.97 ? 25  TYR   L C   1 
ATOM   14175 O  O   . TYR   L  1 25  ? -10.034 -3.960   -46.448 1.00 29.23 ? 25  TYR   L O   1 
ATOM   14176 C  CB  . TYR   L  1 25  ? -10.291 -3.559   -49.698 1.00 27.85 ? 25  TYR   L CB  1 
ATOM   14177 C  CG  . TYR   L  1 25  ? -11.048 -2.986   -50.873 1.00 33.25 ? 25  TYR   L CG  1 
ATOM   14178 C  CD1 . TYR   L  1 25  ? -11.842 -1.852   -50.731 1.00 30.57 ? 25  TYR   L CD1 1 
ATOM   14179 C  CD2 . TYR   L  1 25  ? -10.932 -3.552   -52.142 1.00 31.72 ? 25  TYR   L CD2 1 
ATOM   14180 C  CE1 . TYR   L  1 25  ? -12.514 -1.307   -51.813 1.00 29.89 ? 25  TYR   L CE1 1 
ATOM   14181 C  CE2 . TYR   L  1 25  ? -11.614 -3.018   -53.239 1.00 31.18 ? 25  TYR   L CE2 1 
ATOM   14182 C  CZ  . TYR   L  1 25  ? -12.397 -1.893   -53.071 1.00 35.92 ? 25  TYR   L CZ  1 
ATOM   14183 O  OH  . TYR   L  1 25  ? -13.058 -1.361   -54.167 1.00 38.82 ? 25  TYR   L OH  1 
ATOM   14184 N  N   . PHE   L  1 26  ? -8.128  -3.125   -47.304 1.00 27.63 ? 26  PHE   L N   1 
ATOM   14185 C  CA  . PHE   L  1 26  ? -7.357  -3.760   -46.236 1.00 29.87 ? 26  PHE   L CA  1 
ATOM   14186 C  C   . PHE   L  1 26  ? -7.755  -3.203   -44.871 1.00 28.55 ? 26  PHE   L C   1 
ATOM   14187 O  O   . PHE   L  1 26  ? -7.929  -3.958   -43.897 1.00 27.81 ? 26  PHE   L O   1 
ATOM   14188 C  CB  . PHE   L  1 26  ? -5.839  -3.598   -46.467 1.00 28.76 ? 26  PHE   L CB  1 
ATOM   14189 C  CG  . PHE   L  1 26  ? -5.025  -4.670   -45.792 1.00 24.43 ? 26  PHE   L CG  1 
ATOM   14190 C  CD1 . PHE   L  1 26  ? -4.621  -4.521   -44.473 1.00 26.13 ? 26  PHE   L CD1 1 
ATOM   14191 C  CD2 . PHE   L  1 26  ? -4.721  -5.865   -46.444 1.00 23.95 ? 26  PHE   L CD2 1 
ATOM   14192 C  CE1 . PHE   L  1 26  ? -3.939  -5.530   -43.807 1.00 25.41 ? 26  PHE   L CE1 1 
ATOM   14193 C  CE2 . PHE   L  1 26  ? -4.037  -6.891   -45.771 1.00 31.40 ? 26  PHE   L CE2 1 
ATOM   14194 C  CZ  . PHE   L  1 26  ? -3.644  -6.710   -44.450 1.00 27.92 ? 26  PHE   L CZ  1 
ATOM   14195 N  N   . LEU   L  1 27  ? -7.886  -1.880   -44.769 1.00 28.08 ? 27  LEU   L N   1 
ATOM   14196 C  CA  . LEU   L  1 27  ? -8.298  -1.293   -43.497 1.00 29.41 ? 27  LEU   L CA  1 
ATOM   14197 C  C   . LEU   L  1 27  ? -9.702  -1.747   -43.115 1.00 26.93 ? 27  LEU   L C   1 
ATOM   14198 O  O   . LEU   L  1 27  ? -9.960  -2.077   -41.948 1.00 28.66 ? 27  LEU   L O   1 
ATOM   14199 C  CB  . LEU   L  1 27  ? -8.221  0.233    -43.556 1.00 31.09 ? 27  LEU   L CB  1 
ATOM   14200 C  CG  . LEU   L  1 27  ? -8.596  0.987    -42.261 1.00 31.48 ? 27  LEU   L CG  1 
ATOM   14201 C  CD1 . LEU   L  1 27  ? -7.817  0.444    -41.103 1.00 27.13 ? 27  LEU   L CD1 1 
ATOM   14202 C  CD2 . LEU   L  1 27  ? -8.328  2.506    -42.406 1.00 35.62 ? 27  LEU   L CD2 1 
ATOM   14203 N  N   . HIS   L  1 28  ? -10.627 -1.772   -44.078 1.00 30.29 ? 28  HIS   L N   1 
ATOM   14204 C  CA  . HIS   L  1 28  ? -11.970 -2.240   -43.756 1.00 27.32 ? 28  HIS   L CA  1 
ATOM   14205 C  C   . HIS   L  1 28  ? -11.938 -3.678   -43.256 1.00 30.15 ? 28  HIS   L C   1 
ATOM   14206 O  O   . HIS   L  1 28  ? -12.677 -4.035   -42.331 1.00 26.32 ? 28  HIS   L O   1 
ATOM   14207 C  CB  . HIS   L  1 28  ? -12.893 -2.140   -44.974 1.00 33.67 ? 28  HIS   L CB  1 
ATOM   14208 C  CG  . HIS   L  1 28  ? -13.404 -0.755   -45.237 1.00 33.63 ? 28  HIS   L CG  1 
ATOM   14209 N  ND1 . HIS   L  1 28  ? -13.933 -0.387   -46.449 1.00 29.22 ? 28  HIS   L ND1 1 
ATOM   14210 C  CD2 . HIS   L  1 28  ? -13.442 0.352    -44.459 1.00 25.84 ? 28  HIS   L CD2 1 
ATOM   14211 C  CE1 . HIS   L  1 28  ? -14.302 0.882    -46.403 1.00 29.13 ? 28  HIS   L CE1 1 
ATOM   14212 N  NE2 . HIS   L  1 28  ? -14.004 1.356    -45.209 1.00 28.65 ? 28  HIS   L NE2 1 
ATOM   14213 N  N   . SER   L  1 29  ? -11.132 -4.530   -43.901 1.00 26.67 ? 29  SER   L N   1 
ATOM   14214 C  CA  . SER   L  1 29  ? -10.980 -5.914   -43.447 1.00 26.28 ? 29  SER   L CA  1 
ATOM   14215 C  C   . SER   L  1 29  ? -10.571 -5.965   -41.989 1.00 25.31 ? 29  SER   L C   1 
ATOM   14216 O  O   . SER   L  1 29  ? -11.141 -6.715   -41.182 1.00 29.77 ? 29  SER   L O   1 
ATOM   14217 C  CB  . SER   L  1 29  ? -9.921  -6.627   -44.306 1.00 32.28 ? 29  SER   L CB  1 
ATOM   14218 O  OG  . SER   L  1 29  ? -9.539  -7.868   -43.731 1.00 25.56 ? 29  SER   L OG  1 
ATOM   14219 N  N   . ARG   L  1 30  ? -9.535  -5.206   -41.647 1.00 23.97 ? 30  ARG   L N   1 
ATOM   14220 C  CA  . ARG   L  1 30  ? -8.973  -5.307   -40.319 1.00 24.06 ? 30  ARG   L CA  1 
ATOM   14221 C  C   . ARG   L  1 30  ? -9.889  -4.644   -39.289 1.00 28.62 ? 30  ARG   L C   1 
ATOM   14222 O  O   . ARG   L  1 30  ? -9.968  -5.098   -38.139 1.00 23.31 ? 30  ARG   L O   1 
ATOM   14223 C  CB  . ARG   L  1 30  ? -7.567  -4.710   -40.317 1.00 27.42 ? 30  ARG   L CB  1 
ATOM   14224 C  CG  . ARG   L  1 30  ? -6.460  -5.747   -40.574 1.00 31.21 ? 30  ARG   L CG  1 
ATOM   14225 C  CD  . ARG   L  1 30  ? -6.750  -6.705   -41.758 1.00 28.11 ? 30  ARG   L CD  1 
ATOM   14226 N  NE  . ARG   L  1 30  ? -5.778  -7.786   -41.788 1.00 32.02 ? 30  ARG   L NE  1 
ATOM   14227 C  CZ  . ARG   L  1 30  ? -6.030  -9.031   -42.171 1.00 31.80 ? 30  ARG   L CZ  1 
ATOM   14228 N  NH1 . ARG   L  1 30  ? -7.228  -9.399   -42.594 1.00 28.26 ? 30  ARG   L NH1 1 
ATOM   14229 N  NH2 . ARG   L  1 30  ? -5.048  -9.933   -42.129 1.00 30.09 ? 30  ARG   L NH2 1 
ATOM   14230 N  N   . MET   L  1 31  ? -10.616 -3.599   -39.700 1.00 27.32 ? 31  MET   L N   1 
ATOM   14231 C  CA  . MET   L  1 31  ? -11.676 -3.061   -38.858 1.00 27.59 ? 31  MET   L CA  1 
ATOM   14232 C  C   . MET   L  1 31  ? -12.728 -4.133   -38.565 1.00 29.50 ? 31  MET   L C   1 
ATOM   14233 O  O   . MET   L  1 31  ? -13.083 -4.377   -37.405 1.00 29.48 ? 31  MET   L O   1 
ATOM   14234 C  CB  . MET   L  1 31  ? -12.314 -1.845   -39.538 1.00 29.01 ? 31  MET   L CB  1 
ATOM   14235 C  CG  . MET   L  1 31  ? -11.442 -0.572   -39.543 1.00 26.48 ? 31  MET   L CG  1 
ATOM   14236 S  SD  . MET   L  1 31  ? -12.060 0.690    -40.728 1.00 29.55 ? 31  MET   L SD  1 
ATOM   14237 C  CE  . MET   L  1 31  ? -13.571 1.141    -39.951 1.00 32.96 ? 31  MET   L CE  1 
ATOM   14238 N  N   . TRP   L  1 32  ? -13.230 -4.794   -39.613 1.00 23.88 ? 32  TRP   L N   1 
ATOM   14239 C  CA  . TRP   L  1 32  ? -14.245 -5.819   -39.413 1.00 24.72 ? 32  TRP   L CA  1 
ATOM   14240 C  C   . TRP   L  1 32  ? -13.728 -6.959   -38.526 1.00 25.92 ? 32  TRP   L C   1 
ATOM   14241 O  O   . TRP   L  1 32  ? -14.464 -7.463   -37.668 1.00 26.94 ? 32  TRP   L O   1 
ATOM   14242 C  CB  . TRP   L  1 32  ? -14.730 -6.316   -40.779 1.00 25.23 ? 32  TRP   L CB  1 
ATOM   14243 C  CG  . TRP   L  1 32  ? -15.885 -5.517   -41.331 1.00 27.09 ? 32  TRP   L CG  1 
ATOM   14244 C  CD1 . TRP   L  1 32  ? -16.942 -5.008   -40.640 1.00 23.69 ? 32  TRP   L CD1 1 
ATOM   14245 C  CD2 . TRP   L  1 32  ? -16.079 -5.135   -42.698 1.00 22.64 ? 32  TRP   L CD2 1 
ATOM   14246 N  NE1 . TRP   L  1 32  ? -17.790 -4.335   -41.494 1.00 27.25 ? 32  TRP   L NE1 1 
ATOM   14247 C  CE2 . TRP   L  1 32  ? -17.282 -4.404   -42.763 1.00 29.17 ? 32  TRP   L CE2 1 
ATOM   14248 C  CE3 . TRP   L  1 32  ? -15.362 -5.350   -43.866 1.00 23.83 ? 32  TRP   L CE3 1 
ATOM   14249 C  CZ2 . TRP   L  1 32  ? -17.771 -3.887   -43.955 1.00 26.89 ? 32  TRP   L CZ2 1 
ATOM   14250 C  CZ3 . TRP   L  1 32  ? -15.844 -4.834   -45.049 1.00 24.02 ? 32  TRP   L CZ3 1 
ATOM   14251 C  CH2 . TRP   L  1 32  ? -17.042 -4.111   -45.086 1.00 35.04 ? 32  TRP   L CH2 1 
ATOM   14252 N  N   . ASN   L  1 33  ? -12.462 -7.372   -38.699 1.00 27.51 ? 33  ASN   L N   1 
ATOM   14253 C  CA  . ASN   L  1 33  ? -11.902 -8.391   -37.809 1.00 29.41 ? 33  ASN   L CA  1 
ATOM   14254 C  C   . ASN   L  1 33  ? -11.840 -7.889   -36.367 1.00 32.55 ? 33  ASN   L C   1 
ATOM   14255 O  O   . ASN   L  1 33  ? -12.205 -8.602   -35.427 1.00 28.40 ? 33  ASN   L O   1 
ATOM   14256 C  CB  . ASN   L  1 33  ? -10.508 -8.817   -38.280 1.00 30.51 ? 33  ASN   L CB  1 
ATOM   14257 C  CG  . ASN   L  1 33  ? -10.548 -9.718   -39.496 1.00 27.33 ? 33  ASN   L CG  1 
ATOM   14258 O  OD1 . ASN   L  1 33  ? -11.574 -10.340  -39.823 1.00 28.09 ? 33  ASN   L OD1 1 
ATOM   14259 N  ND2 . ASN   L  1 33  ? -9.422  -9.807   -40.168 1.00 27.46 ? 33  ASN   L ND2 1 
ATOM   14260 N  N   . ASP   L  1 34  ? -11.375 -6.656   -36.176 1.00 30.17 ? 34  ASP   L N   1 
ATOM   14261 C  CA  . ASP   L  1 34  ? -11.364 -6.062   -34.850 1.00 27.52 ? 34  ASP   L CA  1 
ATOM   14262 C  C   . ASP   L  1 34  ? -12.758 -6.073   -34.209 1.00 30.14 ? 34  ASP   L C   1 
ATOM   14263 O  O   . ASP   L  1 34  ? -12.892 -6.321   -33.005 1.00 28.80 ? 34  ASP   L O   1 
ATOM   14264 C  CB  . ASP   L  1 34  ? -10.802 -4.636   -34.939 1.00 27.68 ? 34  ASP   L CB  1 
ATOM   14265 C  CG  . ASP   L  1 34  ? -10.851 -3.881   -33.585 1.00 36.70 ? 34  ASP   L CG  1 
ATOM   14266 O  OD1 . ASP   L  1 34  ? -10.389 -4.405   -32.547 1.00 38.10 ? 34  ASP   L OD1 1 
ATOM   14267 O  OD2 . ASP   L  1 34  ? -11.329 -2.739   -33.570 1.00 40.58 ? 34  ASP   L OD2 1 
ATOM   14268 N  N   . TRP   L  1 35  ? -13.810 -5.830   -34.994 1.00 27.77 ? 35  TRP   L N   1 
ATOM   14269 C  CA  . TRP   L  1 35  ? -15.164 -5.764   -34.447 1.00 27.10 ? 35  TRP   L CA  1 
ATOM   14270 C  C   . TRP   L  1 35  ? -15.787 -7.136   -34.258 1.00 31.24 ? 35  TRP   L C   1 
ATOM   14271 O  O   . TRP   L  1 35  ? -16.884 -7.228   -33.708 1.00 28.71 ? 35  TRP   L O   1 
ATOM   14272 C  CB  . TRP   L  1 35  ? -16.082 -4.921   -35.341 1.00 32.20 ? 35  TRP   L CB  1 
ATOM   14273 C  CG  . TRP   L  1 35  ? -15.638 -3.505   -35.510 1.00 34.74 ? 35  TRP   L CG  1 
ATOM   14274 C  CD1 . TRP   L  1 35  ? -14.689 -2.844   -34.779 1.00 38.14 ? 35  TRP   L CD1 1 
ATOM   14275 C  CD2 . TRP   L  1 35  ? -16.102 -2.575   -36.503 1.00 31.80 ? 35  TRP   L CD2 1 
ATOM   14276 N  NE1 . TRP   L  1 35  ? -14.526 -1.566   -35.271 1.00 33.18 ? 35  TRP   L NE1 1 
ATOM   14277 C  CE2 . TRP   L  1 35  ? -15.384 -1.377   -36.320 1.00 34.94 ? 35  TRP   L CE2 1 
ATOM   14278 C  CE3 . TRP   L  1 35  ? -17.047 -2.646   -37.531 1.00 36.66 ? 35  TRP   L CE3 1 
ATOM   14279 C  CZ2 . TRP   L  1 35  ? -15.579 -0.254   -37.124 1.00 43.98 ? 35  TRP   L CZ2 1 
ATOM   14280 C  CZ3 . TRP   L  1 35  ? -17.242 -1.526   -38.336 1.00 38.50 ? 35  TRP   L CZ3 1 
ATOM   14281 C  CH2 . TRP   L  1 35  ? -16.509 -0.344   -38.120 1.00 35.21 ? 35  TRP   L CH2 1 
ATOM   14282 N  N   . GLY   L  1 36  ? -15.111 -8.199   -34.675 1.00 28.92 ? 36  GLY   L N   1 
ATOM   14283 C  CA  . GLY   L  1 36  ? -15.626 -9.535   -34.522 1.00 28.58 ? 36  GLY   L CA  1 
ATOM   14284 C  C   . GLY   L  1 36  ? -16.488 -10.001  -35.671 1.00 29.32 ? 36  GLY   L C   1 
ATOM   14285 O  O   . GLY   L  1 36  ? -17.201 -10.997  -35.524 1.00 28.87 ? 36  GLY   L O   1 
ATOM   14286 N  N   . LEU   L  1 37  ? -16.479 -9.286   -36.790 1.00 25.41 ? 37  LEU   L N   1 
ATOM   14287 C  CA  . LEU   L  1 37  ? -17.252 -9.670   -37.963 1.00 23.70 ? 37  LEU   L CA  1 
ATOM   14288 C  C   . LEU   L  1 37  ? -16.340 -10.369  -38.976 1.00 27.01 ? 37  LEU   L C   1 
ATOM   14289 O  O   . LEU   L  1 37  ? -16.039 -9.860   -40.053 1.00 26.33 ? 37  LEU   L O   1 
ATOM   14290 C  CB  . LEU   L  1 37  ? -17.927 -8.443   -38.547 1.00 32.11 ? 37  LEU   L CB  1 
ATOM   14291 C  CG  . LEU   L  1 37  ? -18.917 -7.827   -37.541 1.00 33.24 ? 37  LEU   L CG  1 
ATOM   14292 C  CD1 . LEU   L  1 37  ? -19.322 -6.449   -38.015 1.00 35.21 ? 37  LEU   L CD1 1 
ATOM   14293 C  CD2 . LEU   L  1 37  ? -20.126 -8.726   -37.406 1.00 28.51 ? 37  LEU   L CD2 1 
ATOM   14294 N  N   . LYS   L  1 38  ? -15.906 -11.574  -38.599 1.00 28.58 ? 38  LYS   L N   1 
ATOM   14295 C  CA  . LYS   L  1 38  ? -14.764 -12.200  -39.275 1.00 31.06 ? 38  LYS   L CA  1 
ATOM   14296 C  C   . LYS   L  1 38  ? -15.073 -12.621  -40.699 1.00 31.35 ? 38  LYS   L C   1 
ATOM   14297 O  O   . LYS   L  1 38  ? -14.152 -12.713  -41.533 1.00 33.35 ? 38  LYS   L O   1 
ATOM   14298 C  CB  . LYS   L  1 38  ? -14.288 -13.447  -38.537 1.00 35.38 ? 38  LYS   L CB  1 
ATOM   14299 C  CG  . LYS   L  1 38  ? -13.959 -13.262  -37.103 1.00 48.86 ? 38  LYS   L CG  1 
ATOM   14300 C  CD  . LYS   L  1 38  ? -12.786 -12.384  -36.916 1.00 43.13 ? 38  LYS   L CD  1 
ATOM   14301 C  CE  . LYS   L  1 38  ? -12.216 -12.666  -35.534 1.00 52.16 ? 38  LYS   L CE  1 
ATOM   14302 N  NZ  . LYS   L  1 38  ? -11.391 -11.572  -35.025 1.00 51.09 ? 38  LYS   L NZ  1 
ATOM   14303 N  N   . ARG   L  1 39  ? -16.321 -12.969  -40.986 1.00 28.32 ? 39  ARG   L N   1 
ATOM   14304 C  CA  . ARG   L  1 39  ? -16.638 -13.367  -42.350 1.00 26.40 ? 39  ARG   L CA  1 
ATOM   14305 C  C   . ARG   L  1 39  ? -16.501 -12.183  -43.296 1.00 26.77 ? 39  ARG   L C   1 
ATOM   14306 O  O   . ARG   L  1 39  ? -16.051 -12.340  -44.437 1.00 30.00 ? 39  ARG   L O   1 
ATOM   14307 C  CB  . ARG   L  1 39  ? -18.036 -13.961  -42.400 1.00 30.11 ? 39  ARG   L CB  1 
ATOM   14308 C  CG  . ARG   L  1 39  ? -18.379 -14.634  -43.716 1.00 35.66 ? 39  ARG   L CG  1 
ATOM   14309 C  CD  . ARG   L  1 39  ? -19.874 -14.923  -43.764 1.00 42.13 ? 39  ARG   L CD  1 
ATOM   14310 N  NE  . ARG   L  1 39  ? -20.199 -16.056  -44.621 1.00 52.88 ? 39  ARG   L NE  1 
ATOM   14311 C  CZ  . ARG   L  1 39  ? -20.215 -17.314  -44.204 1.00 55.44 ? 39  ARG   L CZ  1 
ATOM   14312 N  NH1 . ARG   L  1 39  ? -19.844 -17.639  -42.975 1.00 63.57 ? 39  ARG   L NH1 1 
ATOM   14313 N  NH2 . ARG   L  1 39  ? -20.619 -18.267  -45.036 1.00 54.75 ? 39  ARG   L NH2 1 
ATOM   14314 N  N   . LEU   L  1 40  ? -16.885 -10.988  -42.837 1.00 29.52 ? 40  LEU   L N   1 
ATOM   14315 C  CA  . LEU   L  1 40  ? -16.655 -9.784   -43.625 1.00 32.02 ? 40  LEU   L CA  1 
ATOM   14316 C  C   . LEU   L  1 40  ? -15.172 -9.465   -43.691 1.00 26.18 ? 40  LEU   L C   1 
ATOM   14317 O  O   . LEU   L  1 40  ? -14.666 -9.025   -44.728 1.00 27.45 ? 40  LEU   L O   1 
ATOM   14318 C  CB  . LEU   L  1 40  ? -17.419 -8.597   -43.033 1.00 27.86 ? 40  LEU   L CB  1 
ATOM   14319 C  CG  . LEU   L  1 40  ? -18.895 -8.483   -43.386 1.00 29.05 ? 40  LEU   L CG  1 
ATOM   14320 C  CD1 . LEU   L  1 40  ? -19.544 -7.442   -42.477 1.00 28.20 ? 40  LEU   L CD1 1 
ATOM   14321 C  CD2 . LEU   L  1 40  ? -19.053 -8.112   -44.876 1.00 30.71 ? 40  LEU   L CD2 1 
ATOM   14322 N  N   . GLY   L  1 41  ? -14.456 -9.660   -42.590 1.00 24.21 ? 41  GLY   L N   1 
ATOM   14323 C  CA  . GLY   L  1 41  ? -13.054 -9.324   -42.600 1.00 27.90 ? 41  GLY   L CA  1 
ATOM   14324 C  C   . GLY   L  1 41  ? -12.278 -10.193  -43.561 1.00 25.60 ? 41  GLY   L C   1 
ATOM   14325 O  O   . GLY   L  1 41  ? -11.342 -9.729   -44.212 1.00 26.13 ? 41  GLY   L O   1 
ATOM   14326 N  N   . ALA   L  1 42  ? -12.654 -11.470  -43.653 1.00 25.09 ? 42  ALA   L N   1 
ATOM   14327 C  CA  . ALA   L  1 42  ? -11.968 -12.388  -44.554 1.00 26.74 ? 42  ALA   L CA  1 
ATOM   14328 C  C   . ALA   L  1 42  ? -12.311 -12.078  -45.993 1.00 27.39 ? 42  ALA   L C   1 
ATOM   14329 O  O   . ALA   L  1 42  ? -11.439 -12.082  -46.873 1.00 25.24 ? 42  ALA   L O   1 
ATOM   14330 C  CB  . ALA   L  1 42  ? -12.342 -13.837  -44.218 1.00 31.84 ? 42  ALA   L CB  1 
ATOM   14331 N  N   . HIS   L  1 43  ? -13.584 -11.805  -46.256 1.00 25.29 ? 43  HIS   L N   1 
ATOM   14332 C  CA  . HIS   L  1 43  ? -13.981 -11.518  -47.625 1.00 27.99 ? 43  HIS   L CA  1 
ATOM   14333 C  C   . HIS   L  1 43  ? -13.324 -10.237  -48.127 1.00 28.29 ? 43  HIS   L C   1 
ATOM   14334 O  O   . HIS   L  1 43  ? -12.852 -10.184  -49.270 1.00 28.92 ? 43  HIS   L O   1 
ATOM   14335 C  CB  . HIS   L  1 43  ? -15.508 -11.426  -47.734 1.00 25.60 ? 43  HIS   L CB  1 
ATOM   14336 C  CG  . HIS   L  1 43  ? -15.969 -11.302  -49.136 1.00 29.07 ? 43  HIS   L CG  1 
ATOM   14337 N  ND1 . HIS   L  1 43  ? -16.471 -12.370  -49.852 1.00 40.54 ? 43  HIS   L ND1 1 
ATOM   14338 C  CD2 . HIS   L  1 43  ? -15.933 -10.255  -49.989 1.00 27.25 ? 43  HIS   L CD2 1 
ATOM   14339 C  CE1 . HIS   L  1 43  ? -16.741 -11.978  -51.085 1.00 31.84 ? 43  HIS   L CE1 1 
ATOM   14340 N  NE2 . HIS   L  1 43  ? -16.411 -10.703  -51.196 1.00 33.61 ? 43  HIS   L NE2 1 
ATOM   14341 N  N   . GLU   L  1 44  ? -13.267 -9.201   -47.276 1.00 28.08 ? 44  GLU   L N   1 
ATOM   14342 C  CA  . GLU   L  1 44  ? -12.663 -7.926   -47.656 1.00 29.05 ? 44  GLU   L CA  1 
ATOM   14343 C  C   . GLU   L  1 44  ? -11.152 -8.057   -47.846 1.00 26.09 ? 44  GLU   L C   1 
ATOM   14344 O  O   . GLU   L  1 44  ? -10.569 -7.391   -48.707 1.00 27.87 ? 44  GLU   L O   1 
ATOM   14345 C  CB  . GLU   L  1 44  ? -12.987 -6.870   -46.595 1.00 25.87 ? 44  GLU   L CB  1 
ATOM   14346 C  CG  . GLU   L  1 44  ? -12.577 -5.465   -46.976 1.00 28.05 ? 44  GLU   L CG  1 
ATOM   14347 C  CD  . GLU   L  1 44  ? -13.596 -4.820   -47.911 1.00 32.79 ? 44  GLU   L CD  1 
ATOM   14348 O  OE1 . GLU   L  1 44  ? -14.332 -5.567   -48.562 1.00 30.88 ? 44  GLU   L OE1 1 
ATOM   14349 O  OE2 . GLU   L  1 44  ? -13.651 -3.583   -47.995 1.00 30.65 ? 44  GLU   L OE2 1 
ATOM   14350 N  N   . TYR   L  1 45  ? -10.519 -8.929   -47.065 1.00 25.59 ? 45  TYR   L N   1 
ATOM   14351 C  CA  . TYR   L  1 45  ? -9.107  -9.222   -47.243 1.00 24.97 ? 45  TYR   L CA  1 
ATOM   14352 C  C   . TYR   L  1 45  ? -8.849  -9.779   -48.638 1.00 23.60 ? 45  TYR   L C   1 
ATOM   14353 O  O   . TYR   L  1 45  ? -7.928  -9.331   -49.323 1.00 26.74 ? 45  TYR   L O   1 
ATOM   14354 C  CB  . TYR   L  1 45  ? -8.646  -10.183  -46.138 1.00 29.82 ? 45  TYR   L CB  1 
ATOM   14355 C  CG  . TYR   L  1 45  ? -7.280  -10.798  -46.363 1.00 27.46 ? 45  TYR   L CG  1 
ATOM   14356 C  CD1 . TYR   L  1 45  ? -6.119  -10.145  -45.960 1.00 26.38 ? 45  TYR   L CD1 1 
ATOM   14357 C  CD2 . TYR   L  1 45  ? -7.156  -12.031  -46.992 1.00 31.46 ? 45  TYR   L CD2 1 
ATOM   14358 C  CE1 . TYR   L  1 45  ? -4.867  -10.714  -46.173 1.00 31.34 ? 45  TYR   L CE1 1 
ATOM   14359 C  CE2 . TYR   L  1 45  ? -5.909  -12.610  -47.211 1.00 31.56 ? 45  TYR   L CE2 1 
ATOM   14360 C  CZ  . TYR   L  1 45  ? -4.763  -11.950  -46.800 1.00 33.69 ? 45  TYR   L CZ  1 
ATOM   14361 O  OH  . TYR   L  1 45  ? -3.517  -12.525  -47.026 1.00 37.47 ? 45  TYR   L OH  1 
ATOM   14362 N  N   . HIS   L  1 46  ? -9.692  -10.707  -49.102 1.00 25.58 ? 46  HIS   L N   1 
ATOM   14363 C  CA  . HIS   L  1 46  ? -9.520  -11.273  -50.430 1.00 26.62 ? 46  HIS   L CA  1 
ATOM   14364 C  C   . HIS   L  1 46  ? -9.788  -10.249  -51.521 1.00 30.13 ? 46  HIS   L C   1 
ATOM   14365 O  O   . HIS   L  1 46  ? -9.136  -10.285  -52.570 1.00 27.50 ? 46  HIS   L O   1 
ATOM   14366 C  CB  . HIS   L  1 46  ? -10.423 -12.507  -50.604 1.00 32.19 ? 46  HIS   L CB  1 
ATOM   14367 C  CG  . HIS   L  1 46  ? -9.991  -13.653  -49.745 1.00 35.55 ? 46  HIS   L CG  1 
ATOM   14368 N  ND1 . HIS   L  1 46  ? -8.751  -14.249  -49.870 1.00 45.26 ? 46  HIS   L ND1 1 
ATOM   14369 C  CD2 . HIS   L  1 46  ? -10.598 -14.261  -48.699 1.00 36.69 ? 46  HIS   L CD2 1 
ATOM   14370 C  CE1 . HIS   L  1 46  ? -8.626  -15.192  -48.952 1.00 42.15 ? 46  HIS   L CE1 1 
ATOM   14371 N  NE2 . HIS   L  1 46  ? -9.730  -15.210  -48.223 1.00 39.04 ? 46  HIS   L NE2 1 
ATOM   14372 N  N   . GLU   L  1 47  ? -10.724 -9.334   -51.299 1.00 26.38 ? 47  GLU   L N   1 
ATOM   14373 C  CA  . GLU   L  1 47  ? -10.898 -8.240   -52.250 1.00 30.99 ? 47  GLU   L CA  1 
ATOM   14374 C  C   . GLU   L  1 47  ? -9.637  -7.395   -52.323 1.00 21.41 ? 47  GLU   L C   1 
ATOM   14375 O  O   . GLU   L  1 47  ? -9.227  -6.965   -53.407 1.00 26.38 ? 47  GLU   L O   1 
ATOM   14376 C  CB  . GLU   L  1 47  ? -12.094 -7.366   -51.849 1.00 27.71 ? 47  GLU   L CB  1 
ATOM   14377 C  CG  . GLU   L  1 47  ? -13.411 -8.114   -51.733 1.00 32.55 ? 47  GLU   L CG  1 
ATOM   14378 C  CD  . GLU   L  1 47  ? -14.006 -8.426   -53.065 1.00 38.52 ? 47  GLU   L CD  1 
ATOM   14379 O  OE1 . GLU   L  1 47  ? -13.253 -8.372   -54.054 1.00 48.12 ? 47  GLU   L OE1 1 
ATOM   14380 O  OE2 . GLU   L  1 47  ? -15.219 -8.718   -53.131 1.00 44.11 ? 47  GLU   L OE2 1 
ATOM   14381 N  N   . SER   L  1 48  ? -9.022  -7.122   -51.178 1.00 24.17 ? 48  SER   L N   1 
ATOM   14382 C  CA  . SER   L  1 48  ? -7.783  -6.350   -51.163 1.00 25.80 ? 48  SER   L CA  1 
ATOM   14383 C  C   . SER   L  1 48  ? -6.677  -7.054   -51.956 1.00 28.89 ? 48  SER   L C   1 
ATOM   14384 O  O   . SER   L  1 48  ? -6.005  -6.443   -52.794 1.00 25.45 ? 48  SER   L O   1 
ATOM   14385 C  CB  . SER   L  1 48  ? -7.351  -6.116   -49.713 1.00 25.34 ? 48  SER   L CB  1 
ATOM   14386 O  OG  . SER   L  1 48  ? -6.200  -5.291   -49.644 1.00 31.33 ? 48  SER   L OG  1 
ATOM   14387 N  N   . ILE   L  1 49  ? -6.476  -8.348   -51.703 1.00 29.26 ? 49  ILE   L N   1 
ATOM   14388 C  CA  . ILE   L  1 49  ? -5.483  -9.126   -52.445 1.00 29.26 ? 49  ILE   L CA  1 
ATOM   14389 C  C   . ILE   L  1 49  ? -5.748  -9.064   -53.945 1.00 28.62 ? 49  ILE   L C   1 
ATOM   14390 O  O   . ILE   L  1 49  ? -4.806  -8.985   -54.753 1.00 25.93 ? 49  ILE   L O   1 
ATOM   14391 C  CB  . ILE   L  1 49  ? -5.491  -10.591  -51.956 1.00 32.67 ? 49  ILE   L CB  1 
ATOM   14392 C  CG1 . ILE   L  1 49  ? -5.110  -10.668  -50.471 1.00 30.86 ? 49  ILE   L CG1 1 
ATOM   14393 C  CG2 . ILE   L  1 49  ? -4.576  -11.464  -52.848 1.00 31.88 ? 49  ILE   L CG2 1 
ATOM   14394 C  CD1 . ILE   L  1 49  ? -3.735  -10.180  -50.191 1.00 36.42 ? 49  ILE   L CD1 1 
ATOM   14395 N  N   . ASP   L  1 50  ? -7.025  -9.188   -54.341 1.00 30.63 ? 50  ASP   L N   1 
ATOM   14396 C  CA  . ASP   L  1 50  ? -7.404  -9.126   -55.754 1.00 32.29 ? 50  ASP   L CA  1 
ATOM   14397 C  C   . ASP   L  1 50  ? -6.989  -7.803   -56.392 1.00 29.78 ? 50  ASP   L C   1 
ATOM   14398 O  O   . ASP   L  1 50  ? -6.563  -7.769   -57.556 1.00 25.76 ? 50  ASP   L O   1 
ATOM   14399 C  CB  . ASP   L  1 50  ? -8.917  -9.288   -55.915 1.00 33.06 ? 50  ASP   L CB  1 
ATOM   14400 C  CG  . ASP   L  1 50  ? -9.408  -10.720  -55.753 1.00 50.03 ? 50  ASP   L CG  1 
ATOM   14401 O  OD1 . ASP   L  1 50  ? -8.600  -11.656  -55.554 1.00 59.61 ? 50  ASP   L OD1 1 
ATOM   14402 O  OD2 . ASP   L  1 50  ? -10.648 -10.896  -55.835 1.00 68.39 ? 50  ASP   L OD2 1 
ATOM   14403 N  N   . GLU   L  1 51  ? -7.182  -6.692   -55.678 1.00 30.01 ? 51  GLU   L N   1 
ATOM   14404 C  CA  . GLU   L  1 51  ? -6.732  -5.405   -56.208 1.00 33.24 ? 51  GLU   L CA  1 
ATOM   14405 C  C   . GLU   L  1 51  ? -5.206  -5.328   -56.241 1.00 29.36 ? 51  GLU   L C   1 
ATOM   14406 O  O   . GLU   L  1 51  ? -4.633  -4.725   -57.156 1.00 28.36 ? 51  GLU   L O   1 
ATOM   14407 C  CB  . GLU   L  1 51  ? -7.347  -4.253   -55.388 1.00 26.85 ? 51  GLU   L CB  1 
ATOM   14408 C  CG  . GLU   L  1 51  ? -8.873  -4.242   -55.393 1.00 28.35 ? 51  GLU   L CG  1 
ATOM   14409 C  CD  . GLU   L  1 51  ? -9.462  -4.083   -56.791 1.00 35.53 ? 51  GLU   L CD  1 
ATOM   14410 O  OE1 . GLU   L  1 51  ? -9.360  -2.980   -57.346 1.00 52.99 ? 51  GLU   L OE1 1 
ATOM   14411 O  OE2 . GLU   L  1 51  ? -9.989  -5.056   -57.342 1.00 40.28 ? 51  GLU   L OE2 1 
ATOM   14412 N  N   . MET   L  1 52  ? -4.527  -5.954   -55.276 1.00 28.94 ? 52  MET   L N   1 
ATOM   14413 C  CA  . MET   L  1 52  ? -3.071  -6.049   -55.325 1.00 27.47 ? 52  MET   L CA  1 
ATOM   14414 C  C   . MET   L  1 52  ? -2.604  -6.727   -56.610 1.00 25.60 ? 52  MET   L C   1 
ATOM   14415 O  O   . MET   L  1 52  ? -1.691  -6.243   -57.291 1.00 25.28 ? 52  MET   L O   1 
ATOM   14416 C  CB  . MET   L  1 52  ? -2.562  -6.818   -54.112 1.00 29.93 ? 52  MET   L CB  1 
ATOM   14417 C  CG  . MET   L  1 52  ? -2.790  -6.109   -52.789 1.00 29.12 ? 52  MET   L CG  1 
ATOM   14418 S  SD  . MET   L  1 52  ? -2.264  -7.086   -51.371 1.00 28.87 ? 52  MET   L SD  1 
ATOM   14419 C  CE  . MET   L  1 52  ? -3.162  -6.365   -49.982 1.00 27.59 ? 52  MET   L CE  1 
ATOM   14420 N  N   . LYS   L  1 53  ? -3.246  -7.838   -56.971 1.00 24.01 ? 53  LYS   L N   1 
ATOM   14421 C  CA  . LYS   L  1 53  ? -2.883  -8.556   -58.193 1.00 27.86 ? 53  LYS   L CA  1 
ATOM   14422 C  C   . LYS   L  1 53  ? -3.115  -7.701   -59.434 1.00 31.92 ? 53  LYS   L C   1 
ATOM   14423 O  O   . LYS   L  1 53  ? -2.297  -7.704   -60.368 1.00 28.90 ? 53  LYS   L O   1 
ATOM   14424 C  CB  . LYS   L  1 53  ? -3.695  -9.850   -58.289 1.00 24.33 ? 53  LYS   L CB  1 
ATOM   14425 C  CG  . LYS   L  1 53  ? -3.324  -10.937  -57.250 1.00 27.25 ? 53  LYS   L CG  1 
ATOM   14426 C  CD  . LYS   L  1 53  ? -4.145  -12.219  -57.499 1.00 37.90 ? 53  LYS   L CD  1 
ATOM   14427 C  CE  . LYS   L  1 53  ? -3.980  -13.259  -56.406 1.00 38.03 ? 53  LYS   L CE  1 
ATOM   14428 N  NZ  . LYS   L  1 53  ? -5.043  -14.324  -56.501 1.00 51.90 ? 53  LYS   L NZ  1 
ATOM   14429 N  N   . HIS   L  1 54  ? -4.259  -7.011   -59.494 1.00 27.75 ? 54  HIS   L N   1 
ATOM   14430 C  CA  . HIS   L  1 54  ? -4.505  -6.075   -60.589 1.00 30.83 ? 54  HIS   L CA  1 
ATOM   14431 C  C   . HIS   L  1 54  ? -3.422  -5.003   -60.657 1.00 32.10 ? 54  HIS   L C   1 
ATOM   14432 O  O   . HIS   L  1 54  ? -2.957  -4.648   -61.744 1.00 31.11 ? 54  HIS   L O   1 
ATOM   14433 C  CB  . HIS   L  1 54  ? -5.858  -5.383   -60.435 1.00 28.39 ? 54  HIS   L CB  1 
ATOM   14434 C  CG  . HIS   L  1 54  ? -7.028  -6.301   -60.348 1.00 36.69 ? 54  HIS   L CG  1 
ATOM   14435 N  ND1 . HIS   L  1 54  ? -7.064  -7.543   -60.945 1.00 33.77 ? 54  HIS   L ND1 1 
ATOM   14436 C  CD2 . HIS   L  1 54  ? -8.236  -6.130   -59.755 1.00 36.24 ? 54  HIS   L CD2 1 
ATOM   14437 C  CE1 . HIS   L  1 54  ? -8.236  -8.105   -60.707 1.00 36.76 ? 54  HIS   L CE1 1 
ATOM   14438 N  NE2 . HIS   L  1 54  ? -8.965  -7.267   -59.990 1.00 33.41 ? 54  HIS   L NE2 1 
ATOM   14439 N  N   . ALA   L  1 55  ? -3.033  -4.438   -59.505 1.00 28.49 ? 55  ALA   L N   1 
ATOM   14440 C  CA  . ALA   L  1 55  ? -1.993  -3.417   -59.546 1.00 27.23 ? 55  ALA   L CA  1 
ATOM   14441 C  C   . ALA   L  1 55  ? -0.695  -3.992   -60.089 1.00 30.38 ? 55  ALA   L C   1 
ATOM   14442 O  O   . ALA   L  1 55  ? -0.003  -3.338   -60.880 1.00 30.04 ? 55  ALA   L O   1 
ATOM   14443 C  CB  . ALA   L  1 55  ? -1.783  -2.805   -58.172 1.00 24.23 ? 55  ALA   L CB  1 
ATOM   14444 N  N   . ASP   L  1 56  ? -0.343  -5.212   -59.670 1.00 27.37 ? 56  ASP   L N   1 
ATOM   14445 C  CA  . ASP   L  1 56  ? 0.828   -5.892   -60.231 1.00 25.38 ? 56  ASP   L CA  1 
ATOM   14446 C  C   . ASP   L  1 56  ? 0.772   -5.909   -61.760 1.00 27.13 ? 56  ASP   L C   1 
ATOM   14447 O  O   . ASP   L  1 56  ? 1.715   -5.475   -62.436 1.00 26.26 ? 56  ASP   L O   1 
ATOM   14448 C  CB  . ASP   L  1 56  ? 0.924   -7.323   -59.662 1.00 28.57 ? 56  ASP   L CB  1 
ATOM   14449 C  CG  . ASP   L  1 56  ? 2.265   -8.003   -59.985 1.00 35.99 ? 56  ASP   L CG  1 
ATOM   14450 O  OD1 . ASP   L  1 56  ? 3.195   -7.306   -60.431 1.00 30.20 ? 56  ASP   L OD1 1 
ATOM   14451 O  OD2 . ASP   L  1 56  ? 2.398   -9.230   -59.781 1.00 35.10 ? 56  ASP   L OD2 1 
ATOM   14452 N  N   . LYS   L  1 57  ? -0.351  -6.357   -62.330 1.00 24.14 ? 57  LYS   L N   1 
ATOM   14453 C  CA  . LYS   L  1 57  ? -0.418  -6.488   -63.784 1.00 25.29 ? 57  LYS   L CA  1 
ATOM   14454 C  C   . LYS   L  1 57  ? -0.302  -5.133   -64.477 1.00 32.19 ? 57  LYS   L C   1 
ATOM   14455 O  O   . LYS   L  1 57  ? 0.330   -5.017   -65.530 1.00 29.49 ? 57  LYS   L O   1 
ATOM   14456 C  CB  . LYS   L  1 57  ? -1.706  -7.189   -64.196 1.00 31.39 ? 57  LYS   L CB  1 
ATOM   14457 C  CG  . LYS   L  1 57  ? -1.781  -8.646   -63.775 1.00 31.02 ? 57  LYS   L CG  1 
ATOM   14458 C  CD  . LYS   L  1 57  ? -1.022  -9.551   -64.723 1.00 43.05 ? 57  LYS   L CD  1 
ATOM   14459 C  CE  . LYS   L  1 57  ? -0.449  -10.809  -64.038 1.00 58.79 ? 57  LYS   L CE  1 
ATOM   14460 N  NZ  . LYS   L  1 57  ? 1.074   -10.839  -64.052 1.00 64.27 ? 57  LYS   L NZ  1 
ATOM   14461 N  N   . LEU   L  1 58  ? -0.882  -4.090   -63.892 1.00 27.84 ? 58  LEU   L N   1 
ATOM   14462 C  CA  . LEU   L  1 58  ? -0.794  -2.770   -64.513 1.00 34.47 ? 58  LEU   L CA  1 
ATOM   14463 C  C   . LEU   L  1 58  ? 0.631   -2.231   -64.461 1.00 25.14 ? 58  LEU   L C   1 
ATOM   14464 O  O   . LEU   L  1 58  ? 1.102   -1.627   -65.420 1.00 28.68 ? 58  LEU   L O   1 
ATOM   14465 C  CB  . LEU   L  1 58  ? -1.746  -1.800   -63.814 1.00 31.74 ? 58  LEU   L CB  1 
ATOM   14466 C  CG  . LEU   L  1 58  ? -3.225  -2.039   -64.077 1.00 27.95 ? 58  LEU   L CG  1 
ATOM   14467 C  CD1 . LEU   L  1 58  ? -4.049  -1.412   -62.944 1.00 33.23 ? 58  LEU   L CD1 1 
ATOM   14468 C  CD2 . LEU   L  1 58  ? -3.628  -1.485   -65.396 1.00 32.89 ? 58  LEU   L CD2 1 
ATOM   14469 N  N   . ILE   L  1 59  ? 1.307   -2.427   -63.330 1.00 27.45 ? 59  ILE   L N   1 
ATOM   14470 C  CA  . ILE   L  1 59  ? 2.694   -2.014   -63.169 1.00 25.31 ? 59  ILE   L CA  1 
ATOM   14471 C  C   . ILE   L  1 59  ? 3.555   -2.696   -64.209 1.00 32.64 ? 59  ILE   L C   1 
ATOM   14472 O  O   . ILE   L  1 59  ? 4.433   -2.071   -64.815 1.00 29.11 ? 59  ILE   L O   1 
ATOM   14473 C  CB  . ILE   L  1 59  ? 3.177   -2.345   -61.745 1.00 28.67 ? 59  ILE   L CB  1 
ATOM   14474 C  CG1 . ILE   L  1 59  ? 2.469   -1.463   -60.708 1.00 30.88 ? 59  ILE   L CG1 1 
ATOM   14475 C  CG2 . ILE   L  1 59  ? 4.698   -2.190   -61.605 1.00 26.66 ? 59  ILE   L CG2 1 
ATOM   14476 C  CD1 . ILE   L  1 59  ? 2.674   -1.928   -59.257 1.00 30.93 ? 59  ILE   L CD1 1 
ATOM   14477 N  N   . GLU   L  1 60  ? 3.324   -3.996   -64.414 1.00 28.80 ? 60  GLU   L N   1 
ATOM   14478 C  CA  . GLU   L  1 60  ? 4.089   -4.755   -65.401 1.00 25.78 ? 60  GLU   L CA  1 
ATOM   14479 C  C   . GLU   L  1 60  ? 3.792   -4.269   -66.813 1.00 24.81 ? 60  GLU   L C   1 
ATOM   14480 O  O   . GLU   L  1 60  ? 4.702   -4.152   -67.640 1.00 29.51 ? 60  GLU   L O   1 
ATOM   14481 C  CB  . GLU   L  1 60  ? 3.777   -6.255   -65.256 1.00 30.43 ? 60  GLU   L CB  1 
ATOM   14482 C  CG  . GLU   L  1 60  ? 4.256   -6.838   -63.928 1.00 32.16 ? 60  GLU   L CG  1 
ATOM   14483 C  CD  . GLU   L  1 60  ? 3.779   -8.278   -63.686 1.00 37.67 ? 60  GLU   L CD  1 
ATOM   14484 O  OE1 . GLU   L  1 60  ? 2.651   -8.627   -64.083 1.00 34.41 ? 60  GLU   L OE1 1 
ATOM   14485 O  OE2 . GLU   L  1 60  ? 4.535   -9.053   -63.080 1.00 32.86 ? 60  GLU   L OE2 1 
ATOM   14486 N  N   . ARG   L  1 61  ? 2.521   -4.002   -67.125 1.00 25.48 ? 61  ARG   L N   1 
ATOM   14487 C  CA  . ARG   L  1 61  ? 2.196   -3.474   -68.448 1.00 27.78 ? 61  ARG   L CA  1 
ATOM   14488 C  C   . ARG   L  1 61  ? 2.848   -2.109   -68.685 1.00 31.48 ? 61  ARG   L C   1 
ATOM   14489 O  O   . ARG   L  1 61  ? 3.393   -1.843   -69.777 1.00 25.56 ? 61  ARG   L O   1 
ATOM   14490 C  CB  . ARG   L  1 61  ? 0.682   -3.375   -68.620 1.00 28.49 ? 61  ARG   L CB  1 
ATOM   14491 C  CG  . ARG   L  1 61  ? 0.280   -2.892   -69.987 1.00 27.70 ? 61  ARG   L CG  1 
ATOM   14492 C  CD  . ARG   L  1 61  ? 0.552   -3.963   -70.989 1.00 26.27 ? 61  ARG   L CD  1 
ATOM   14493 N  NE  . ARG   L  1 61  ? 0.013   -3.654   -72.311 1.00 29.16 ? 61  ARG   L NE  1 
ATOM   14494 C  CZ  . ARG   L  1 61  ? 0.503   -4.182   -73.425 1.00 34.34 ? 61  ARG   L CZ  1 
ATOM   14495 N  NH1 . ARG   L  1 61  ? 1.460   -5.107   -73.386 1.00 30.86 ? 61  ARG   L NH1 1 
ATOM   14496 N  NH2 . ARG   L  1 61  ? 0.072   -3.736   -74.602 1.00 30.76 ? 61  ARG   L NH2 1 
ATOM   14497 N  N   . ILE   L  1 62  ? 2.787   -1.228   -67.685 1.00 29.75 ? 62  ILE   L N   1 
ATOM   14498 C  CA  . ILE   L  1 62  ? 3.353   0.114    -67.829 1.00 32.90 ? 62  ILE   L CA  1 
ATOM   14499 C  C   . ILE   L  1 62  ? 4.856   0.048    -68.087 1.00 34.65 ? 62  ILE   L C   1 
ATOM   14500 O  O   . ILE   L  1 62  ? 5.387   0.758    -68.950 1.00 33.34 ? 62  ILE   L O   1 
ATOM   14501 C  CB  . ILE   L  1 62  ? 3.047   0.965    -66.586 1.00 29.99 ? 62  ILE   L CB  1 
ATOM   14502 C  CG1 . ILE   L  1 62  ? 1.576   1.269    -66.505 1.00 28.87 ? 62  ILE   L CG1 1 
ATOM   14503 C  CG2 . ILE   L  1 62  ? 3.871   2.262    -66.627 1.00 31.42 ? 62  ILE   L CG2 1 
ATOM   14504 C  CD1 . ILE   L  1 62  ? 1.139   1.865    -65.121 1.00 34.16 ? 62  ILE   L CD1 1 
ATOM   14505 N  N   . LEU   L  1 63  ? 5.573   -0.771   -67.311 1.00 27.87 ? 63  LEU   L N   1 
ATOM   14506 C  CA  . LEU   L  1 63  ? 7.002   -0.934   -67.533 1.00 33.54 ? 63  LEU   L CA  1 
ATOM   14507 C  C   . LEU   L  1 63  ? 7.288   -1.480   -68.930 1.00 35.62 ? 63  LEU   L C   1 
ATOM   14508 O  O   . LEU   L  1 63  ? 8.194   -0.995   -69.622 1.00 30.91 ? 63  LEU   L O   1 
ATOM   14509 C  CB  . LEU   L  1 63  ? 7.598   -1.842   -66.448 1.00 28.87 ? 63  LEU   L CB  1 
ATOM   14510 C  CG  . LEU   L  1 63  ? 7.720   -1.189   -65.072 1.00 33.62 ? 63  LEU   L CG  1 
ATOM   14511 C  CD1 . LEU   L  1 63  ? 8.024   -2.224   -63.982 1.00 29.56 ? 63  LEU   L CD1 1 
ATOM   14512 C  CD2 . LEU   L  1 63  ? 8.799   -0.100   -65.110 1.00 31.37 ? 63  LEU   L CD2 1 
ATOM   14513 N  N   . PHE   L  1 64  ? 6.499   -2.451   -69.386 1.00 29.30 ? 64  PHE   L N   1 
ATOM   14514 C  CA  . PHE   L  1 64  ? 6.719   -2.981   -70.723 1.00 34.09 ? 64  PHE   L CA  1 
ATOM   14515 C  C   . PHE   L  1 64  ? 6.555   -1.890   -71.765 1.00 31.65 ? 64  PHE   L C   1 
ATOM   14516 O  O   . PHE   L  1 64  ? 7.305   -1.850   -72.742 1.00 30.16 ? 64  PHE   L O   1 
ATOM   14517 C  CB  . PHE   L  1 64  ? 5.753   -4.131   -71.023 1.00 26.78 ? 64  PHE   L CB  1 
ATOM   14518 C  CG  . PHE   L  1 64  ? 5.743   -4.539   -72.459 1.00 24.08 ? 64  PHE   L CG  1 
ATOM   14519 C  CD1 . PHE   L  1 64  ? 6.862   -5.095   -73.051 1.00 34.81 ? 64  PHE   L CD1 1 
ATOM   14520 C  CD2 . PHE   L  1 64  ? 4.599   -4.374   -73.228 1.00 32.86 ? 64  PHE   L CD2 1 
ATOM   14521 C  CE1 . PHE   L  1 64  ? 6.838   -5.466   -74.388 1.00 33.59 ? 64  PHE   L CE1 1 
ATOM   14522 C  CE2 . PHE   L  1 64  ? 4.574   -4.746   -74.544 1.00 33.03 ? 64  PHE   L CE2 1 
ATOM   14523 C  CZ  . PHE   L  1 64  ? 5.691   -5.294   -75.127 1.00 30.02 ? 64  PHE   L CZ  1 
ATOM   14524 N  N   . LEU   L  1 65  ? 5.566   -1.003   -71.577 1.00 29.34 ? 65  LEU   L N   1 
ATOM   14525 C  CA  . LEU   L  1 65  ? 5.314   0.091    -72.509 1.00 31.82 ? 65  LEU   L CA  1 
ATOM   14526 C  C   . LEU   L  1 65  ? 6.300   1.247    -72.328 1.00 34.55 ? 65  LEU   L C   1 
ATOM   14527 O  O   . LEU   L  1 65  ? 6.171   2.257    -73.027 1.00 34.68 ? 65  LEU   L O   1 
ATOM   14528 C  CB  . LEU   L  1 65  ? 3.869   0.600    -72.354 1.00 31.78 ? 65  LEU   L CB  1 
ATOM   14529 C  CG  . LEU   L  1 65  ? 2.758   -0.357   -72.797 1.00 28.28 ? 65  LEU   L CG  1 
ATOM   14530 C  CD1 . LEU   L  1 65  ? 1.356   0.234    -72.660 1.00 36.07 ? 65  LEU   L CD1 1 
ATOM   14531 C  CD2 . LEU   L  1 65  ? 2.934   -0.850   -74.209 1.00 35.13 ? 65  LEU   L CD2 1 
ATOM   14532 N  N   . GLU   L  1 66  ? 7.261   1.109    -71.407 1.00 31.35 ? 66  GLU   L N   1 
ATOM   14533 C  CA  . GLU   L  1 66  ? 8.342   2.070    -71.155 1.00 32.88 ? 66  GLU   L CA  1 
ATOM   14534 C  C   . GLU   L  1 66  ? 7.814   3.354    -70.511 1.00 35.22 ? 66  GLU   L C   1 
ATOM   14535 O  O   . GLU   L  1 66  ? 8.272   4.456    -70.796 1.00 37.22 ? 66  GLU   L O   1 
ATOM   14536 C  CB  . GLU   L  1 66  ? 9.142   2.363    -72.431 1.00 36.07 ? 66  GLU   L CB  1 
ATOM   14537 C  CG  . GLU   L  1 66  ? 9.853   1.111    -72.954 1.00 41.32 ? 66  GLU   L CG  1 
ATOM   14538 C  CD  . GLU   L  1 66  ? 10.490  1.286    -74.338 1.00 46.66 ? 66  GLU   L CD  1 
ATOM   14539 O  OE1 . GLU   L  1 66  ? 10.838  2.413    -74.702 1.00 43.35 ? 66  GLU   L OE1 1 
ATOM   14540 O  OE2 . GLU   L  1 66  ? 10.634  0.286    -75.064 1.00 33.87 ? 66  GLU   L OE2 1 
ATOM   14541 N  N   . GLY   L  1 67  ? 6.843   3.205    -69.618 1.00 31.01 ? 67  GLY   L N   1 
ATOM   14542 C  CA  . GLY   L  1 67  ? 6.359   4.296    -68.805 1.00 35.95 ? 67  GLY   L CA  1 
ATOM   14543 C  C   . GLY   L  1 67  ? 6.838   4.120    -67.377 1.00 33.42 ? 67  GLY   L C   1 
ATOM   14544 O  O   . GLY   L  1 67  ? 7.473   3.123    -67.037 1.00 30.52 ? 67  GLY   L O   1 
ATOM   14545 N  N   . LEU   L  1 68  ? 6.548   5.142    -66.542 1.00 28.93 ? 68  LEU   L N   1 
ATOM   14546 C  CA  . LEU   L  1 68  ? 6.884   5.101    -65.129 1.00 35.99 ? 68  LEU   L CA  1 
ATOM   14547 C  C   . LEU   L  1 68  ? 5.622   4.803    -64.339 1.00 31.26 ? 68  LEU   L C   1 
ATOM   14548 O  O   . LEU   L  1 68  ? 4.695   5.629    -64.336 1.00 36.77 ? 68  LEU   L O   1 
ATOM   14549 C  CB  . LEU   L  1 68  ? 7.506   6.421    -64.664 1.00 35.93 ? 68  LEU   L CB  1 
ATOM   14550 C  CG  . LEU   L  1 68  ? 8.819   6.771    -65.362 1.00 43.61 ? 68  LEU   L CG  1 
ATOM   14551 C  CD1 . LEU   L  1 68  ? 9.348   8.143    -64.942 1.00 55.99 ? 68  LEU   L CD1 1 
ATOM   14552 C  CD2 . LEU   L  1 68  ? 9.863   5.712    -65.080 1.00 51.68 ? 68  LEU   L CD2 1 
ATOM   14553 N  N   . PRO   L  1 69  ? 5.513   3.639    -63.693 1.00 33.00 ? 69  PRO   L N   1 
ATOM   14554 C  CA  . PRO   L  1 69  ? 4.343   3.376    -62.843 1.00 36.04 ? 69  PRO   L CA  1 
ATOM   14555 C  C   . PRO   L  1 69  ? 4.326   4.342    -61.666 1.00 26.30 ? 69  PRO   L C   1 
ATOM   14556 O  O   . PRO   L  1 69  ? 5.326   4.488    -60.957 1.00 33.96 ? 69  PRO   L O   1 
ATOM   14557 C  CB  . PRO   L  1 69  ? 4.555   1.925    -62.381 1.00 34.01 ? 69  PRO   L CB  1 
ATOM   14558 C  CG  . PRO   L  1 69  ? 5.647   1.375    -63.209 1.00 32.73 ? 69  PRO   L CG  1 
ATOM   14559 C  CD  . PRO   L  1 69  ? 6.489   2.544    -63.631 1.00 33.03 ? 69  PRO   L CD  1 
ATOM   14560 N  N   . ASN   L  1 70  ? 3.180   4.981    -61.449 1.00 29.46 ? 70  ASN   L N   1 
ATOM   14561 C  CA  . ASN   L  1 70  ? 3.039   5.933    -60.351 1.00 37.91 ? 70  ASN   L CA  1 
ATOM   14562 C  C   . ASN   L  1 70  ? 2.519   5.201    -59.111 1.00 29.41 ? 70  ASN   L C   1 
ATOM   14563 O  O   . ASN   L  1 70  ? 1.323   4.940    -58.981 1.00 29.10 ? 70  ASN   L O   1 
ATOM   14564 C  CB  . ASN   L  1 70  ? 2.121   7.073    -60.768 1.00 31.13 ? 70  ASN   L CB  1 
ATOM   14565 C  CG  . ASN   L  1 70  ? 2.039   8.173    -59.721 1.00 33.41 ? 70  ASN   L CG  1 
ATOM   14566 O  OD1 . ASN   L  1 70  ? 2.513   8.013    -58.602 1.00 34.93 ? 70  ASN   L OD1 1 
ATOM   14567 N  ND2 . ASN   L  1 70  ? 1.425   9.292    -60.085 1.00 34.34 ? 70  ASN   L ND2 1 
ATOM   14568 N  N   . LEU   L  1 71  ? 3.420   4.887    -58.189 1.00 29.82 ? 71  LEU   L N   1 
ATOM   14569 C  CA  . LEU   L  1 71  ? 3.048   4.357    -56.885 1.00 32.45 ? 71  LEU   L CA  1 
ATOM   14570 C  C   . LEU   L  1 71  ? 3.251   5.374    -55.776 1.00 37.94 ? 71  LEU   L C   1 
ATOM   14571 O  O   . LEU   L  1 71  ? 3.328   4.992    -54.601 1.00 32.78 ? 71  LEU   L O   1 
ATOM   14572 C  CB  . LEU   L  1 71  ? 3.852   3.102    -56.564 1.00 26.45 ? 71  LEU   L CB  1 
ATOM   14573 C  CG  . LEU   L  1 71  ? 3.529   1.841    -57.367 1.00 33.61 ? 71  LEU   L CG  1 
ATOM   14574 C  CD1 . LEU   L  1 71  ? 4.326   1.804    -58.649 1.00 32.66 ? 71  LEU   L CD1 1 
ATOM   14575 C  CD2 . LEU   L  1 71  ? 3.905   0.634    -56.531 1.00 39.11 ? 71  LEU   L CD2 1 
ATOM   14576 N  N   . GLN   L  1 72  ? 3.380   6.654    -56.126 1.00 35.97 ? 72  GLN   L N   1 
ATOM   14577 C  CA  . GLN   L  1 72  ? 3.666   7.717    -55.160 1.00 37.86 ? 72  GLN   L CA  1 
ATOM   14578 C  C   . GLN   L  1 72  ? 2.410   8.487    -54.772 1.00 39.29 ? 72  GLN   L C   1 
ATOM   14579 O  O   . GLN   L  1 72  ? 2.247   8.880    -53.605 1.00 38.28 ? 72  GLN   L O   1 
ATOM   14580 C  CB  . GLN   L  1 72  ? 4.710   8.686    -55.742 1.00 35.94 ? 72  GLN   L CB  1 
ATOM   14581 C  CG  . GLN   L  1 72  ? 5.069   9.876    -54.855 1.00 37.14 ? 72  GLN   L CG  1 
ATOM   14582 C  CD  . GLN   L  1 72  ? 5.791   9.469    -53.600 1.00 35.63 ? 72  GLN   L CD  1 
ATOM   14583 O  OE1 . GLN   L  1 72  ? 7.016   9.409    -53.570 1.00 39.14 ? 72  GLN   L OE1 1 
ATOM   14584 N  NE2 . GLN   L  1 72  ? 5.033   9.195    -52.548 1.00 33.78 ? 72  GLN   L NE2 1 
ATOM   14585 N  N   . ASP   L  1 73  ? 1.504   8.666    -55.723 1.00 34.66 ? 73  ASP   L N   1 
ATOM   14586 C  CA  . ASP   L  1 73  ? 0.332   9.510    -55.547 1.00 39.94 ? 73  ASP   L CA  1 
ATOM   14587 C  C   . ASP   L  1 73  ? -0.859  8.652    -55.135 1.00 42.08 ? 73  ASP   L C   1 
ATOM   14588 O  O   . ASP   L  1 73  ? -1.355  7.824    -55.907 1.00 52.20 ? 73  ASP   L O   1 
ATOM   14589 C  CB  . ASP   L  1 73  ? 0.060   10.296   -56.827 1.00 41.10 ? 73  ASP   L CB  1 
ATOM   14590 C  CG  . ASP   L  1 73  ? 1.183   11.274   -57.139 1.00 43.06 ? 73  ASP   L CG  1 
ATOM   14591 O  OD1 . ASP   L  1 73  ? 1.875   11.686   -56.188 1.00 43.75 ? 73  ASP   L OD1 1 
ATOM   14592 O  OD2 . ASP   L  1 73  ? 1.393   11.611   -58.317 1.00 42.30 ? 73  ASP   L OD2 1 
ATOM   14593 N  N   . LEU   L  1 74  ? -1.305  8.847    -53.912 1.00 37.40 ? 74  LEU   L N   1 
ATOM   14594 C  CA  . LEU   L  1 74  ? -2.403  8.092    -53.327 1.00 37.03 ? 74  LEU   L CA  1 
ATOM   14595 C  C   . LEU   L  1 74  ? -3.561  9.051    -53.111 1.00 37.13 ? 74  LEU   L C   1 
ATOM   14596 O  O   . LEU   L  1 74  ? -3.442  9.994    -52.324 1.00 39.66 ? 74  LEU   L O   1 
ATOM   14597 C  CB  . LEU   L  1 74  ? -1.971  7.459    -52.006 1.00 37.42 ? 74  LEU   L CB  1 
ATOM   14598 C  CG  . LEU   L  1 74  ? -3.032  6.656    -51.248 1.00 35.31 ? 74  LEU   L CG  1 
ATOM   14599 C  CD1 . LEU   L  1 74  ? -3.571  5.534    -52.103 1.00 38.71 ? 74  LEU   L CD1 1 
ATOM   14600 C  CD2 . LEU   L  1 74  ? -2.446  6.095    -49.969 1.00 41.23 ? 74  LEU   L CD2 1 
ATOM   14601 N  N   . GLY   L  1 75  ? -4.655  8.827    -53.829 1.00 36.86 ? 75  GLY   L N   1 
ATOM   14602 C  CA  . GLY   L  1 75  ? -5.858  9.602    -53.655 1.00 40.69 ? 75  GLY   L CA  1 
ATOM   14603 C  C   . GLY   L  1 75  ? -6.498  9.335    -52.312 1.00 37.31 ? 75  GLY   L C   1 
ATOM   14604 O  O   . GLY   L  1 75  ? -5.942  8.682    -51.428 1.00 37.31 ? 75  GLY   L O   1 
ATOM   14605 N  N   . LYS   L  1 76  ? -7.726  9.848    -52.185 1.00 35.73 ? 76  LYS   L N   1 
ATOM   14606 C  CA  . LYS   L  1 76  ? -8.474  9.867    -50.932 1.00 39.74 ? 76  LYS   L CA  1 
ATOM   14607 C  C   . LYS   L  1 76  ? -9.120  8.511    -50.690 1.00 32.79 ? 76  LYS   L C   1 
ATOM   14608 O  O   . LYS   L  1 76  ? -9.887  8.025    -51.526 1.00 30.92 ? 76  LYS   L O   1 
ATOM   14609 C  CB  . LYS   L  1 76  ? -9.552  10.958   -50.956 1.00 40.72 ? 76  LYS   L CB  1 
ATOM   14610 C  CG  . LYS   L  1 76  ? -10.418 11.035   -49.666 1.00 37.67 ? 76  LYS   L CG  1 
ATOM   14611 N  N   . LEU   L  1 77  ? -8.785  7.902    -49.556 1.00 32.00 ? 77  LEU   L N   1 
ATOM   14612 C  CA  . LEU   L  1 77  ? -9.472  6.704    -49.104 1.00 32.86 ? 77  LEU   L CA  1 
ATOM   14613 C  C   . LEU   L  1 77  ? -10.877 7.034    -48.629 1.00 38.02 ? 77  LEU   L C   1 
ATOM   14614 O  O   . LEU   L  1 77  ? -11.100 8.042    -47.959 1.00 43.38 ? 77  LEU   L O   1 
ATOM   14615 C  CB  . LEU   L  1 77  ? -8.700  6.068    -47.952 1.00 33.04 ? 77  LEU   L CB  1 
ATOM   14616 C  CG  . LEU   L  1 77  ? -7.479  5.195    -48.252 1.00 46.85 ? 77  LEU   L CG  1 
ATOM   14617 C  CD1 . LEU   L  1 77  ? -6.631  5.742    -49.364 1.00 39.65 ? 77  LEU   L CD1 1 
ATOM   14618 C  CD2 . LEU   L  1 77  ? -6.654  5.029    -46.987 1.00 39.34 ? 77  LEU   L CD2 1 
ATOM   14619 N  N   . LEU   L  1 78  ? -11.821 6.156    -48.949 1.00 35.05 ? 78  LEU   L N   1 
ATOM   14620 C  CA  . LEU   L  1 78  ? -13.191 6.237    -48.450 1.00 35.88 ? 78  LEU   L CA  1 
ATOM   14621 C  C   . LEU   L  1 78  ? -13.363 5.209    -47.332 1.00 34.05 ? 78  LEU   L C   1 
ATOM   14622 O  O   . LEU   L  1 78  ? -13.664 4.043    -47.598 1.00 37.06 ? 78  LEU   L O   1 
ATOM   14623 C  CB  . LEU   L  1 78  ? -14.182 5.980    -49.581 1.00 36.25 ? 78  LEU   L CB  1 
ATOM   14624 C  CG  . LEU   L  1 78  ? -13.963 6.761    -50.869 1.00 46.60 ? 78  LEU   L CG  1 
ATOM   14625 C  CD1 . LEU   L  1 78  ? -15.178 6.624    -51.806 1.00 44.54 ? 78  LEU   L CD1 1 
ATOM   14626 C  CD2 . LEU   L  1 78  ? -13.647 8.223    -50.538 1.00 44.87 ? 78  LEU   L CD2 1 
ATOM   14627 N  N   . ILE   L  1 79  ? -13.224 5.646    -46.080 1.00 35.29 ? 79  ILE   L N   1 
ATOM   14628 C  CA  . ILE   L  1 79  ? -13.322 4.761    -44.921 1.00 33.49 ? 79  ILE   L CA  1 
ATOM   14629 C  C   . ILE   L  1 79  ? -14.685 4.942    -44.261 1.00 37.82 ? 79  ILE   L C   1 
ATOM   14630 O  O   . ILE   L  1 79  ? -15.028 6.041    -43.815 1.00 42.29 ? 79  ILE   L O   1 
ATOM   14631 C  CB  . ILE   L  1 79  ? -12.192 5.030    -43.916 1.00 37.17 ? 79  ILE   L CB  1 
ATOM   14632 C  CG1 . ILE   L  1 79  ? -10.830 5.020    -44.605 1.00 39.85 ? 79  ILE   L CG1 1 
ATOM   14633 C  CG2 . ILE   L  1 79  ? -12.234 3.987    -42.784 1.00 39.30 ? 79  ILE   L CG2 1 
ATOM   14634 C  CD1 . ILE   L  1 79  ? -10.535 3.745    -45.360 1.00 38.57 ? 79  ILE   L CD1 1 
ATOM   14635 N  N   . GLY   L  1 80  ? -15.462 3.871    -44.171 1.00 35.21 ? 80  GLY   L N   1 
ATOM   14636 C  CA  . GLY   L  1 80  ? -16.746 3.977    -43.491 1.00 43.84 ? 80  GLY   L CA  1 
ATOM   14637 C  C   . GLY   L  1 80  ? -16.593 3.967    -41.967 1.00 35.15 ? 80  GLY   L C   1 
ATOM   14638 O  O   . GLY   L  1 80  ? -15.540 3.657    -41.423 1.00 35.34 ? 80  GLY   L O   1 
ATOM   14639 N  N   . GLU   L  1 81  ? -17.662 4.339    -41.264 1.00 36.28 ? 81  GLU   L N   1 
ATOM   14640 C  CA  . GLU   L  1 81  ? -17.663 4.299    -39.803 1.00 41.39 ? 81  GLU   L CA  1 
ATOM   14641 C  C   . GLU   L  1 81  ? -18.594 3.226    -39.254 1.00 35.66 ? 81  GLU   L C   1 
ATOM   14642 O  O   . GLU   L  1 81  ? -18.721 3.073    -38.031 1.00 41.51 ? 81  GLU   L O   1 
ATOM   14643 C  CB  . GLU   L  1 81  ? -18.020 5.680    -39.241 1.00 44.57 ? 81  GLU   L CB  1 
ATOM   14644 C  CG  . GLU   L  1 81  ? -16.946 6.717    -39.534 1.00 51.69 ? 81  GLU   L CG  1 
ATOM   14645 C  CD  . GLU   L  1 81  ? -17.072 7.980    -38.713 1.00 66.10 ? 81  GLU   L CD  1 
ATOM   14646 O  OE1 . GLU   L  1 81  ? -17.111 7.890    -37.467 1.00 73.11 ? 81  GLU   L OE1 1 
ATOM   14647 O  OE2 . GLU   L  1 81  ? -17.113 9.070    -39.322 1.00 78.57 ? 81  GLU   L OE2 1 
ATOM   14648 N  N   . ASN   L  1 82  ? -19.209 2.456    -40.129 1.00 26.76 ? 82  ASN   L N   1 
ATOM   14649 C  CA  . ASN   L  1 82  ? -20.015 1.306    -39.751 1.00 31.09 ? 82  ASN   L CA  1 
ATOM   14650 C  C   . ASN   L  1 82  ? -20.135 0.436    -40.995 1.00 26.18 ? 82  ASN   L C   1 
ATOM   14651 O  O   . ASN   L  1 82  ? -19.695 0.817    -42.080 1.00 30.59 ? 82  ASN   L O   1 
ATOM   14652 C  CB  . ASN   L  1 82  ? -21.375 1.718    -39.169 1.00 37.67 ? 82  ASN   L CB  1 
ATOM   14653 C  CG  . ASN   L  1 82  ? -22.269 2.432    -40.180 1.00 41.51 ? 82  ASN   L CG  1 
ATOM   14654 O  OD1 . ASN   L  1 82  ? -22.405 2.014    -41.334 1.00 36.22 ? 82  ASN   L OD1 1 
ATOM   14655 N  ND2 . ASN   L  1 82  ? -22.891 3.518    -39.736 1.00 41.53 ? 82  ASN   L ND2 1 
ATOM   14656 N  N   . THR   L  1 83  ? -20.709 -0.749   -40.817 1.00 29.58 ? 83  THR   L N   1 
ATOM   14657 C  CA  . THR   L  1 83  ? -20.646 -1.765   -41.863 1.00 29.29 ? 83  THR   L CA  1 
ATOM   14658 C  C   . THR   L  1 83  ? -21.330 -1.281   -43.133 1.00 33.26 ? 83  THR   L C   1 
ATOM   14659 O  O   . THR   L  1 83  ? -20.786 -1.425   -44.227 1.00 29.31 ? 83  THR   L O   1 
ATOM   14660 C  CB  . THR   L  1 83  ? -21.258 -3.065   -41.346 1.00 26.14 ? 83  THR   L CB  1 
ATOM   14661 O  OG1 . THR   L  1 83  ? -20.403 -3.605   -40.333 1.00 33.56 ? 83  THR   L OG1 1 
ATOM   14662 C  CG2 . THR   L  1 83  ? -21.451 -4.112   -42.449 1.00 33.44 ? 83  THR   L CG2 1 
ATOM   14663 N  N   . GLN   L  1 84  ? -22.513 -0.684   -43.006 1.00 29.12 ? 84  GLN   L N   1 
ATOM   14664 C  CA  . GLN   L  1 84  ? -23.222 -0.165   -44.174 1.00 26.63 ? 84  GLN   L CA  1 
ATOM   14665 C  C   . GLN   L  1 84  ? -22.391 0.873    -44.906 1.00 26.33 ? 84  GLN   L C   1 
ATOM   14666 O  O   . GLN   L  1 84  ? -22.250 0.822    -46.137 1.00 30.30 ? 84  GLN   L O   1 
ATOM   14667 C  CB  . GLN   L  1 84  ? -24.562 0.446    -43.747 1.00 33.23 ? 84  GLN   L CB  1 
ATOM   14668 C  CG  . GLN   L  1 84  ? -25.394 1.008    -44.937 1.00 40.54 ? 84  GLN   L CG  1 
ATOM   14669 C  CD  . GLN   L  1 84  ? -26.801 1.365    -44.512 1.00 41.42 ? 84  GLN   L CD  1 
ATOM   14670 O  OE1 . GLN   L  1 84  ? -27.781 0.968    -45.140 1.00 41.23 ? 84  GLN   L OE1 1 
ATOM   14671 N  NE2 . GLN   L  1 84  ? -26.905 2.102    -43.426 1.00 43.13 ? 84  GLN   L NE2 1 
ATOM   14672 N  N   . GLU   L  1 85  ? -21.819 1.819    -44.166 1.00 27.36 ? 85  GLU   L N   1 
ATOM   14673 C  CA  . GLU   L  1 85  ? -21.007 2.846    -44.799 1.00 33.15 ? 85  GLU   L CA  1 
ATOM   14674 C  C   . GLU   L  1 85  ? -19.786 2.244    -45.466 1.00 32.25 ? 85  GLU   L C   1 
ATOM   14675 O  O   . GLU   L  1 85  ? -19.375 2.690    -46.538 1.00 31.59 ? 85  GLU   L O   1 
ATOM   14676 C  CB  . GLU   L  1 85  ? -20.580 3.905    -43.780 1.00 34.63 ? 85  GLU   L CB  1 
ATOM   14677 C  CG  . GLU   L  1 85  ? -21.666 4.911    -43.418 1.00 44.73 ? 85  GLU   L CG  1 
ATOM   14678 C  CD  . GLU   L  1 85  ? -21.145 6.076    -42.574 1.00 50.55 ? 85  GLU   L CD  1 
ATOM   14679 O  OE1 . GLU   L  1 85  ? -19.948 6.059    -42.204 1.00 35.88 ? 85  GLU   L OE1 1 
ATOM   14680 O  OE2 . GLU   L  1 85  ? -21.935 7.008    -42.276 1.00 54.65 ? 85  GLU   L OE2 1 
ATOM   14681 N  N   . MET   L  1 86  ? -19.157 1.254    -44.831 1.00 27.54 ? 86  MET   L N   1 
ATOM   14682 C  CA  . MET   L  1 86  ? -17.936 0.726    -45.424 1.00 28.62 ? 86  MET   L CA  1 
ATOM   14683 C  C   . MET   L  1 86  ? -18.268 0.052    -46.739 1.00 25.15 ? 86  MET   L C   1 
ATOM   14684 O  O   . MET   L  1 86  ? -17.563 0.246    -47.736 1.00 33.63 ? 86  MET   L O   1 
ATOM   14685 C  CB  . MET   L  1 86  ? -17.227 -0.241   -44.456 1.00 24.73 ? 86  MET   L CB  1 
ATOM   14686 C  CG  . MET   L  1 86  ? -16.765 0.406    -43.148 1.00 25.31 ? 86  MET   L CG  1 
ATOM   14687 S  SD  . MET   L  1 86  ? -16.859 -0.706   -41.699 1.00 31.18 ? 86  MET   L SD  1 
ATOM   14688 C  CE  . MET   L  1 86  ? -15.357 -1.686   -42.003 1.00 30.41 ? 86  MET   L CE  1 
ATOM   14689 N  N   . LEU   L  1 87  ? -19.354 -0.716   -46.761 1.00 27.08 ? 87  LEU   L N   1 
ATOM   14690 C  CA  . LEU   L  1 87  ? -19.769 -1.367   -47.993 1.00 29.29 ? 87  LEU   L CA  1 
ATOM   14691 C  C   . LEU   L  1 87  ? -20.080 -0.331   -49.063 1.00 37.68 ? 87  LEU   L C   1 
ATOM   14692 O  O   . LEU   L  1 87  ? -19.619 -0.445   -50.207 1.00 28.00 ? 87  LEU   L O   1 
ATOM   14693 C  CB  . LEU   L  1 87  ? -20.971 -2.261   -47.728 1.00 30.26 ? 87  LEU   L CB  1 
ATOM   14694 C  CG  . LEU   L  1 87  ? -20.739 -3.492   -46.846 1.00 25.44 ? 87  LEU   L CG  1 
ATOM   14695 C  CD1 . LEU   L  1 87  ? -22.048 -4.117   -46.488 1.00 26.69 ? 87  LEU   L CD1 1 
ATOM   14696 C  CD2 . LEU   L  1 87  ? -19.829 -4.498   -47.558 1.00 28.57 ? 87  LEU   L CD2 1 
ATOM   14697 N  N   . GLN   L  1 88  ? -20.833 0.714    -48.690 1.00 33.95 ? 88  GLN   L N   1 
ATOM   14698 C  CA  A GLN   L  1 88  ? -21.140 1.779    -49.640 0.50 33.16 ? 88  GLN   L CA  1 
ATOM   14699 C  CA  B GLN   L  1 88  ? -21.133 1.791    -49.631 0.50 33.16 ? 88  GLN   L CA  1 
ATOM   14700 C  C   . GLN   L  1 88  ? -19.868 2.506    -50.077 1.00 31.83 ? 88  GLN   L C   1 
ATOM   14701 O  O   . GLN   L  1 88  ? -19.720 2.858    -51.257 1.00 32.53 ? 88  GLN   L O   1 
ATOM   14702 C  CB  A GLN   L  1 88  ? -22.173 2.743    -49.023 0.50 27.58 ? 88  GLN   L CB  1 
ATOM   14703 C  CB  B GLN   L  1 88  ? -22.122 2.776    -48.996 0.50 27.60 ? 88  GLN   L CB  1 
ATOM   14704 C  CG  A GLN   L  1 88  ? -22.667 3.839    -49.949 0.50 36.38 ? 88  GLN   L CG  1 
ATOM   14705 C  CG  B GLN   L  1 88  ? -23.462 2.170    -48.891 0.50 22.81 ? 88  GLN   L CG  1 
ATOM   14706 C  CD  A GLN   L  1 88  ? -23.540 3.329    -51.102 0.50 41.28 ? 88  GLN   L CD  1 
ATOM   14707 C  CD  B GLN   L  1 88  ? -24.420 2.924    -48.004 0.50 25.44 ? 88  GLN   L CD  1 
ATOM   14708 O  OE1 A GLN   L  1 88  ? -24.342 2.407    -50.938 0.50 47.50 ? 88  GLN   L OE1 1 
ATOM   14709 O  OE1 B GLN   L  1 88  ? -24.083 3.906    -47.334 0.50 23.95 ? 88  GLN   L OE1 1 
ATOM   14710 N  NE2 A GLN   L  1 88  ? -23.401 3.952    -52.262 0.50 27.87 ? 88  GLN   L NE2 1 
ATOM   14711 N  NE2 B GLN   L  1 88  ? -25.627 2.441    -47.984 0.50 24.39 ? 88  GLN   L NE2 1 
ATOM   14712 N  N   . CYS   L  1 89  ? -18.932 2.720    -49.153 1.00 27.64 ? 89  CYS   L N   1 
ATOM   14713 C  CA  . CYS   L  1 89  ? -17.668 3.331    -49.530 1.00 32.50 ? 89  CYS   L CA  1 
ATOM   14714 C  C   . CYS   L  1 89  ? -16.946 2.507    -50.603 1.00 39.80 ? 89  CYS   L C   1 
ATOM   14715 O  O   . CYS   L  1 89  ? -16.410 3.064    -51.572 1.00 32.32 ? 89  CYS   L O   1 
ATOM   14716 C  CB  . CYS   L  1 89  ? -16.783 3.493    -48.300 1.00 37.75 ? 89  CYS   L CB  1 
ATOM   14717 S  SG  . CYS   L  1 89  ? -17.077 5.003    -47.322 1.00 35.86 ? 89  CYS   L SG  1 
ATOM   14718 N  N   . ASP   L  1 90  ? -16.894 1.179    -50.436 1.00 33.70 ? 90  ASP   L N   1 
ATOM   14719 C  CA  . ASP   L  1 90  ? -16.279 0.350    -51.467 1.00 34.69 ? 90  ASP   L CA  1 
ATOM   14720 C  C   . ASP   L  1 90  ? -17.038 0.485    -52.786 1.00 32.21 ? 90  ASP   L C   1 
ATOM   14721 O  O   . ASP   L  1 90  ? -16.432 0.557    -53.863 1.00 30.67 ? 90  ASP   L O   1 
ATOM   14722 C  CB  . ASP   L  1 90  ? -16.248 -1.112   -51.034 1.00 28.71 ? 90  ASP   L CB  1 
ATOM   14723 C  CG  . ASP   L  1 90  ? -15.309 -1.378   -49.887 1.00 24.88 ? 90  ASP   L CG  1 
ATOM   14724 O  OD1 . ASP   L  1 90  ? -14.523 -0.503   -49.470 1.00 28.39 ? 90  ASP   L OD1 1 
ATOM   14725 O  OD2 . ASP   L  1 90  ? -15.359 -2.522   -49.397 1.00 33.68 ? 90  ASP   L OD2 1 
ATOM   14726 N  N   . LEU   L  1 91  ? -18.366 0.524    -52.717 1.00 28.36 ? 91  LEU   L N   1 
ATOM   14727 C  CA  . LEU   L  1 91  ? -19.164 0.616    -53.939 1.00 31.43 ? 91  LEU   L CA  1 
ATOM   14728 C  C   . LEU   L  1 91  ? -18.902 1.932    -54.671 1.00 38.17 ? 91  LEU   L C   1 
ATOM   14729 O  O   . LEU   L  1 91  ? -18.680 1.943    -55.887 1.00 34.12 ? 91  LEU   L O   1 
ATOM   14730 C  CB  . LEU   L  1 91  ? -20.642 0.451    -53.600 1.00 33.79 ? 91  LEU   L CB  1 
ATOM   14731 C  CG  . LEU   L  1 91  ? -21.664 0.554    -54.735 1.00 33.81 ? 91  LEU   L CG  1 
ATOM   14732 C  CD1 . LEU   L  1 91  ? -21.344 -0.438   -55.852 1.00 37.63 ? 91  LEU   L CD1 1 
ATOM   14733 C  CD2 . LEU   L  1 91  ? -23.046 0.319    -54.179 1.00 35.48 ? 91  LEU   L CD2 1 
ATOM   14734 N  N   . ASN   L  1 92  ? -18.875 3.049    -53.939 1.00 37.88 ? 92  ASN   L N   1 
ATOM   14735 C  CA  . ASN   L  1 92  ? -18.583 4.340    -54.564 1.00 37.00 ? 92  ASN   L CA  1 
ATOM   14736 C  C   . ASN   L  1 92  ? -17.222 4.332    -55.258 1.00 37.34 ? 92  ASN   L C   1 
ATOM   14737 O  O   . ASN   L  1 92  ? -17.081 4.813    -56.388 1.00 32.38 ? 92  ASN   L O   1 
ATOM   14738 C  CB  . ASN   L  1 92  ? -18.650 5.453    -53.512 1.00 28.21 ? 92  ASN   L CB  1 
ATOM   14739 C  CG  . ASN   L  1 92  ? -20.061 5.681    -52.977 1.00 40.69 ? 92  ASN   L CG  1 
ATOM   14740 O  OD1 . ASN   L  1 92  ? -21.031 5.041    -53.413 1.00 40.10 ? 92  ASN   L OD1 1 
ATOM   14741 N  ND2 . ASN   L  1 92  ? -20.183 6.613    -52.027 1.00 41.09 ? 92  ASN   L ND2 1 
ATOM   14742 N  N   . LEU   L  1 93  ? -16.194 3.813    -54.592 1.00 29.16 ? 93  LEU   L N   1 
ATOM   14743 C  CA  . LEU   L  1 93  ? -14.898 3.685    -55.245 1.00 28.03 ? 93  LEU   L CA  1 
ATOM   14744 C  C   . LEU   L  1 93  ? -14.985 2.787    -56.483 1.00 27.78 ? 93  LEU   L C   1 
ATOM   14745 O  O   . LEU   L  1 93  ? -14.404 3.105    -57.526 1.00 29.15 ? 93  LEU   L O   1 
ATOM   14746 C  CB  . LEU   L  1 93  ? -13.852 3.165    -54.248 1.00 35.37 ? 93  LEU   L CB  1 
ATOM   14747 C  CG  . LEU   L  1 93  ? -12.402 2.983    -54.747 1.00 26.95 ? 93  LEU   L CG  1 
ATOM   14748 C  CD1 . LEU   L  1 93  ? -11.800 4.298    -55.207 1.00 34.15 ? 93  LEU   L CD1 1 
ATOM   14749 C  CD2 . LEU   L  1 93  ? -11.500 2.373    -53.680 1.00 29.68 ? 93  LEU   L CD2 1 
ATOM   14750 N  N   . GLU   L  1 94  ? -15.715 1.668    -56.402 1.00 33.94 ? 94  GLU   L N   1 
ATOM   14751 C  CA  . GLU   L  1 94  ? -15.771 0.764    -57.548 1.00 30.78 ? 94  GLU   L CA  1 
ATOM   14752 C  C   . GLU   L  1 94  ? -16.433 1.433    -58.751 1.00 36.19 ? 94  GLU   L C   1 
ATOM   14753 O  O   . GLU   L  1 94  ? -15.999 1.241    -59.891 1.00 31.19 ? 94  GLU   L O   1 
ATOM   14754 C  CB  . GLU   L  1 94  ? -16.523 -0.518   -57.198 1.00 28.93 ? 94  GLU   L CB  1 
ATOM   14755 C  CG  . GLU   L  1 94  ? -15.762 -1.501   -56.278 1.00 29.74 ? 94  GLU   L CG  1 
ATOM   14756 C  CD  . GLU   L  1 94  ? -14.651 -2.258   -56.988 1.00 36.93 ? 94  GLU   L CD  1 
ATOM   14757 O  OE1 . GLU   L  1 94  ? -14.501 -2.116   -58.215 1.00 36.26 ? 94  GLU   L OE1 1 
ATOM   14758 O  OE2 . GLU   L  1 94  ? -13.909 -2.981   -56.307 1.00 42.12 ? 94  GLU   L OE2 1 
ATOM   14759 N  N   . LEU   L  1 95  ? -17.493 2.215    -58.522 1.00 31.86 ? 95  LEU   L N   1 
ATOM   14760 C  CA  . LEU   L  1 95  ? -18.173 2.867    -59.640 1.00 32.31 ? 95  LEU   L CA  1 
ATOM   14761 C  C   . LEU   L  1 95  ? -17.282 3.923    -60.285 1.00 30.93 ? 95  LEU   L C   1 
ATOM   14762 O  O   . LEU   L  1 95  ? -17.262 4.055    -61.512 1.00 36.43 ? 95  LEU   L O   1 
ATOM   14763 C  CB  . LEU   L  1 95  ? -19.510 3.453    -59.172 1.00 36.72 ? 95  LEU   L CB  1 
ATOM   14764 C  CG  . LEU   L  1 95  ? -20.545 2.408    -58.756 1.00 35.43 ? 95  LEU   L CG  1 
ATOM   14765 C  CD1 . LEU   L  1 95  ? -21.625 3.036    -57.905 1.00 42.71 ? 95  LEU   L CD1 1 
ATOM   14766 C  CD2 . LEU   L  1 95  ? -21.184 1.701    -59.922 1.00 34.90 ? 95  LEU   L CD2 1 
ATOM   14767 N  N   . LYS   L  1 96  ? -16.484 4.642    -59.491 1.00 32.43 ? 96  LYS   L N   1 
ATOM   14768 C  CA  . LYS   L  1 96  ? -15.494 5.539    -60.078 1.00 30.81 ? 96  LYS   L CA  1 
ATOM   14769 C  C   . LYS   L  1 96  ? -14.451 4.761    -60.870 1.00 41.46 ? 96  LYS   L C   1 
ATOM   14770 O  O   . LYS   L  1 96  ? -14.070 5.167    -61.974 1.00 33.74 ? 96  LYS   L O   1 
ATOM   14771 C  CB  . LYS   L  1 96  ? -14.829 6.380    -58.983 1.00 36.67 ? 96  LYS   L CB  1 
ATOM   14772 C  CG  . LYS   L  1 96  ? -13.448 7.053    -59.318 1.00 36.15 ? 96  LYS   L CG  1 
ATOM   14773 C  CD  . LYS   L  1 96  ? -13.517 8.176    -60.336 1.00 55.84 ? 96  LYS   L CD  1 
ATOM   14774 C  CE  . LYS   L  1 96  ? -12.275 9.085    -60.241 1.00 59.99 ? 96  LYS   L CE  1 
ATOM   14775 N  NZ  . LYS   L  1 96  ? -10.956 8.356    -60.033 1.00 47.02 ? 96  LYS   L NZ  1 
ATOM   14776 N  N   . ALA   L  1 97  ? -13.988 3.627    -60.335 1.00 33.63 ? 97  ALA   L N   1 
ATOM   14777 C  CA  . ALA   L  1 97  ? -12.935 2.871    -61.020 1.00 37.51 ? 97  ALA   L CA  1 
ATOM   14778 C  C   . ALA   L  1 97  ? -13.432 2.270    -62.332 1.00 30.03 ? 97  ALA   L C   1 
ATOM   14779 O  O   . ALA   L  1 97  ? -12.663 2.171    -63.299 1.00 32.53 ? 97  ALA   L O   1 
ATOM   14780 C  CB  . ALA   L  1 97  ? -12.387 1.758    -60.116 1.00 31.54 ? 97  ALA   L CB  1 
ATOM   14781 N  N   . THR   L  1 98  ? -14.698 1.855    -62.393 1.00 29.85 ? 98  THR   L N   1 
ATOM   14782 C  CA  . THR   L  1 98  ? -15.181 1.245    -63.623 1.00 31.87 ? 98  THR   L CA  1 
ATOM   14783 C  C   . THR   L  1 98  ? -15.428 2.300    -64.698 1.00 38.58 ? 98  THR   L C   1 
ATOM   14784 O  O   . THR   L  1 98  ? -15.179 2.049    -65.884 1.00 29.57 ? 98  THR   L O   1 
ATOM   14785 C  CB  . THR   L  1 98  ? -16.440 0.417    -63.370 1.00 35.60 ? 98  THR   L CB  1 
ATOM   14786 O  OG1 . THR   L  1 98  ? -17.429 1.191    -62.672 1.00 36.52 ? 98  THR   L OG1 1 
ATOM   14787 C  CG2 . THR   L  1 98  ? -16.075 -0.800   -62.564 1.00 37.68 ? 98  THR   L CG2 1 
ATOM   14788 N  N   . LYS   L  1 99  ? -15.907 3.481    -64.299 1.00 38.58 ? 99  LYS   L N   1 
ATOM   14789 C  CA  . LYS   L  1 99  ? -15.961 4.620    -65.209 1.00 35.80 ? 99  LYS   L CA  1 
ATOM   14790 C  C   . LYS   L  1 99  ? -14.594 4.862    -65.830 1.00 31.13 ? 99  LYS   L C   1 
ATOM   14791 O  O   . LYS   L  1 99  ? -14.453 4.921    -67.058 1.00 34.09 ? 99  LYS   L O   1 
ATOM   14792 C  CB  . LYS   L  1 99  ? -16.437 5.859    -64.446 1.00 39.39 ? 99  LYS   L CB  1 
ATOM   14793 C  CG  . LYS   L  1 99  ? -16.621 7.143    -65.256 1.00 46.02 ? 99  LYS   L CG  1 
ATOM   14794 C  CD  . LYS   L  1 99  ? -17.178 8.284    -64.337 1.00 41.88 ? 99  LYS   L CD  1 
ATOM   14795 N  N   . ASP   L  1 100 ? -13.567 4.977    -64.984 1.00 33.02 ? 100 ASP   L N   1 
ATOM   14796 C  CA  . ASP   L  1 100 ? -12.202 5.198    -65.457 1.00 27.24 ? 100 ASP   L CA  1 
ATOM   14797 C  C   . ASP   L  1 100 ? -11.724 4.073    -66.378 1.00 35.01 ? 100 ASP   L C   1 
ATOM   14798 O  O   . ASP   L  1 100 ? -11.069 4.334    -67.396 1.00 32.78 ? 100 ASP   L O   1 
ATOM   14799 C  CB  . ASP   L  1 100 ? -11.268 5.354    -64.264 1.00 29.38 ? 100 ASP   L CB  1 
ATOM   14800 C  CG  . ASP   L  1 100 ? -11.494 6.668    -63.504 1.00 32.79 ? 100 ASP   L CG  1 
ATOM   14801 O  OD1 . ASP   L  1 100 ? -12.306 7.492    -63.964 1.00 41.98 ? 100 ASP   L OD1 1 
ATOM   14802 O  OD2 . ASP   L  1 100 ? -10.875 6.874    -62.443 1.00 34.17 ? 100 ASP   L OD2 1 
ATOM   14803 N  N   . LEU   L  1 101 ? -12.015 2.815    -66.029 1.00 36.80 ? 101 LEU   L N   1 
ATOM   14804 C  CA  . LEU   L  1 101 ? -11.659 1.700    -66.909 1.00 31.57 ? 101 LEU   L CA  1 
ATOM   14805 C  C   . LEU   L  1 101 ? -12.305 1.863    -68.289 1.00 29.27 ? 101 LEU   L C   1 
ATOM   14806 O  O   . LEU   L  1 101 ? -11.649 1.675    -69.310 1.00 29.74 ? 101 LEU   L O   1 
ATOM   14807 C  CB  . LEU   L  1 101 ? -12.070 0.357    -66.283 1.00 33.89 ? 101 LEU   L CB  1 
ATOM   14808 C  CG  . LEU   L  1 101 ? -11.156 -0.143   -65.144 1.00 28.22 ? 101 LEU   L CG  1 
ATOM   14809 C  CD1 . LEU   L  1 101 ? -11.900 -1.124   -64.236 1.00 31.71 ? 101 LEU   L CD1 1 
ATOM   14810 C  CD2 . LEU   L  1 101 ? -9.841  -0.762   -65.686 1.00 38.80 ? 101 LEU   L CD2 1 
ATOM   14811 N  N   . ARG   L  1 102 ? -13.608 2.172    -68.332 1.00 30.86 ? 102 ARG   L N   1 
ATOM   14812 C  CA  . ARG   L  1 102 ? -14.298 2.326    -69.608 1.00 29.81 ? 102 ARG   L CA  1 
ATOM   14813 C  C   . ARG   L  1 102 ? -13.626 3.391    -70.473 1.00 31.12 ? 102 ARG   L C   1 
ATOM   14814 O  O   . ARG   L  1 102 ? -13.386 3.180    -71.668 1.00 32.82 ? 102 ARG   L O   1 
ATOM   14815 C  CB  . ARG   L  1 102 ? -15.771 2.658    -69.356 1.00 29.80 ? 102 ARG   L CB  1 
ATOM   14816 C  CG  . ARG   L  1 102 ? -16.601 1.455    -68.907 1.00 32.19 ? 102 ARG   L CG  1 
ATOM   14817 C  CD  . ARG   L  1 102 ? -18.017 1.841    -68.481 1.00 33.58 ? 102 ARG   L CD  1 
ATOM   14818 N  NE  . ARG   L  1 102 ? -18.523 1.013    -67.382 1.00 35.77 ? 102 ARG   L NE  1 
ATOM   14819 C  CZ  . ARG   L  1 102 ? -18.835 -0.273   -67.489 1.00 31.21 ? 102 ARG   L CZ  1 
ATOM   14820 N  NH1 . ARG   L  1 102 ? -18.692 -0.925   -68.626 1.00 35.82 ? 102 ARG   L NH1 1 
ATOM   14821 N  NH2 . ARG   L  1 102 ? -19.289 -0.928   -66.420 1.00 34.50 ? 102 ARG   L NH2 1 
ATOM   14822 N  N   . GLU   L  1 103 ? -13.299 4.539    -69.880 1.00 33.53 ? 103 GLU   L N   1 
ATOM   14823 C  CA  . GLU   L  1 103 ? -12.637 5.599    -70.639 1.00 41.66 ? 103 GLU   L CA  1 
ATOM   14824 C  C   . GLU   L  1 103 ? -11.265 5.162    -71.143 1.00 37.47 ? 103 GLU   L C   1 
ATOM   14825 O  O   . GLU   L  1 103 ? -10.858 5.535    -72.247 1.00 34.36 ? 103 GLU   L O   1 
ATOM   14826 C  CB  . GLU   L  1 103 ? -12.510 6.856    -69.778 1.00 32.25 ? 103 GLU   L CB  1 
ATOM   14827 C  CG  . GLU   L  1 103 ? -13.858 7.462    -69.395 1.00 35.84 ? 103 GLU   L CG  1 
ATOM   14828 N  N   . ALA   L  1 104 ? -10.511 4.423    -70.323 1.00 32.58 ? 104 ALA   L N   1 
ATOM   14829 C  CA  . ALA   L  1 104 ? -9.200  3.954    -70.755 1.00 26.65 ? 104 ALA   L CA  1 
ATOM   14830 C  C   . ALA   L  1 104 ? -9.319  2.970    -71.915 1.00 25.77 ? 104 ALA   L C   1 
ATOM   14831 O  O   . ALA   L  1 104 ? -8.521  3.013    -72.859 1.00 34.25 ? 104 ALA   L O   1 
ATOM   14832 C  CB  . ALA   L  1 104 ? -8.465  3.314    -69.575 1.00 33.24 ? 104 ALA   L CB  1 
ATOM   14833 N  N   . ILE   L  1 105 ? -10.329 2.101    -71.881 1.00 32.06 ? 105 ILE   L N   1 
ATOM   14834 C  CA  . ILE   L  1 105 ? -10.515 1.130    -72.955 1.00 27.40 ? 105 ILE   L CA  1 
ATOM   14835 C  C   . ILE   L  1 105 ? -10.844 1.848    -74.261 1.00 40.83 ? 105 ILE   L C   1 
ATOM   14836 O  O   . ILE   L  1 105 ? -10.338 1.479    -75.328 1.00 33.52 ? 105 ILE   L O   1 
ATOM   14837 C  CB  . ILE   L  1 105 ? -11.601 0.114    -72.556 1.00 24.54 ? 105 ILE   L CB  1 
ATOM   14838 C  CG1 . ILE   L  1 105 ? -11.057 -0.858   -71.487 1.00 31.14 ? 105 ILE   L CG1 1 
ATOM   14839 C  CG2 . ILE   L  1 105 ? -12.151 -0.648   -73.756 1.00 29.28 ? 105 ILE   L CG2 1 
ATOM   14840 C  CD1 . ILE   L  1 105 ? -12.179 -1.659   -70.772 1.00 35.08 ? 105 ILE   L CD1 1 
ATOM   14841 N  N   . VAL   L  1 106 ? -11.684 2.888    -74.200 1.00 30.06 ? 106 VAL   L N   1 
ATOM   14842 C  CA  . VAL   L  1 106 ? -11.985 3.681    -75.397 1.00 31.48 ? 106 VAL   L CA  1 
ATOM   14843 C  C   . VAL   L  1 106 ? -10.697 4.153    -76.064 1.00 29.88 ? 106 VAL   L C   1 
ATOM   14844 O  O   . VAL   L  1 106 ? -10.500 3.992    -77.274 1.00 34.18 ? 106 VAL   L O   1 
ATOM   14845 C  CB  . VAL   L  1 106 ? -12.875 4.890    -75.042 1.00 34.89 ? 106 VAL   L CB  1 
ATOM   14846 C  CG1 . VAL   L  1 106 ? -12.937 5.858    -76.238 1.00 34.19 ? 106 VAL   L CG1 1 
ATOM   14847 C  CG2 . VAL   L  1 106 ? -14.253 4.456    -74.665 1.00 35.95 ? 106 VAL   L CG2 1 
ATOM   14848 N  N   . HIS   L  1 107 ? -9.807  4.772    -75.285 1.00 28.85 ? 107 HIS   L N   1 
ATOM   14849 C  CA  . HIS   L  1 107 ? -8.580  5.283    -75.875 1.00 33.26 ? 107 HIS   L CA  1 
ATOM   14850 C  C   . HIS   L  1 107 ? -7.658  4.157    -76.343 1.00 38.43 ? 107 HIS   L C   1 
ATOM   14851 O  O   . HIS   L  1 107 ? -7.027  4.280    -77.396 1.00 34.14 ? 107 HIS   L O   1 
ATOM   14852 C  CB  . HIS   L  1 107 ? -7.844  6.191    -74.901 1.00 32.53 ? 107 HIS   L CB  1 
ATOM   14853 C  CG  . HIS   L  1 107 ? -6.576  6.752    -75.462 1.00 44.14 ? 107 HIS   L CG  1 
ATOM   14854 N  ND1 . HIS   L  1 107 ? -6.564  7.694    -76.468 1.00 38.77 ? 107 HIS   L ND1 1 
ATOM   14855 C  CD2 . HIS   L  1 107 ? -5.279  6.499    -75.166 1.00 40.64 ? 107 HIS   L CD2 1 
ATOM   14856 C  CE1 . HIS   L  1 107 ? -5.314  7.996    -76.770 1.00 36.73 ? 107 HIS   L CE1 1 
ATOM   14857 N  NE2 . HIS   L  1 107 ? -4.513  7.283    -75.995 1.00 39.92 ? 107 HIS   L NE2 1 
ATOM   14858 N  N   . CYS   L  1 108 ? -7.547  3.065    -75.577 1.00 30.72 ? 108 CYS   L N   1 
ATOM   14859 C  CA  . CYS   L  1 108 ? -6.791  1.908    -76.061 1.00 35.53 ? 108 CYS   L CA  1 
ATOM   14860 C  C   . CYS   L  1 108 ? -7.271  1.466    -77.438 1.00 30.40 ? 108 CYS   L C   1 
ATOM   14861 O  O   . CYS   L  1 108 ? -6.457  1.195    -78.336 1.00 32.48 ? 108 CYS   L O   1 
ATOM   14862 C  CB  . CYS   L  1 108 ? -6.910  0.745    -75.074 1.00 28.39 ? 108 CYS   L CB  1 
ATOM   14863 S  SG  . CYS   L  1 108 ? -5.949  1.000    -73.591 1.00 33.05 ? 108 CYS   L SG  1 
ATOM   14864 N  N   . GLU   L  1 109 ? -8.593  1.390    -77.617 1.00 34.13 ? 109 GLU   L N   1 
ATOM   14865 C  CA  . GLU   L  1 109 ? -9.157  0.930    -78.883 1.00 36.84 ? 109 GLU   L CA  1 
ATOM   14866 C  C   . GLU   L  1 109 ? -8.807  1.893    -80.009 1.00 41.40 ? 109 GLU   L C   1 
ATOM   14867 O  O   . GLU   L  1 109 ? -8.439  1.468    -81.111 1.00 30.66 ? 109 GLU   L O   1 
ATOM   14868 C  CB  . GLU   L  1 109 ? -10.671 0.790    -78.750 1.00 30.55 ? 109 GLU   L CB  1 
ATOM   14869 C  CG  . GLU   L  1 109 ? -11.416 0.260    -79.996 1.00 34.10 ? 109 GLU   L CG  1 
ATOM   14870 C  CD  . GLU   L  1 109 ? -11.135 -1.207   -80.300 1.00 31.85 ? 109 GLU   L CD  1 
ATOM   14871 O  OE1 . GLU   L  1 109 ? -10.620 -1.906   -79.407 1.00 32.10 ? 109 GLU   L OE1 1 
ATOM   14872 O  OE2 . GLU   L  1 109 ? -11.430 -1.651   -81.438 1.00 32.70 ? 109 GLU   L OE2 1 
ATOM   14873 N  N   . GLN   L  1 110 ? -8.871  3.196    -79.726 1.00 37.91 ? 110 GLN   L N   1 
ATOM   14874 C  CA  . GLN   L  1 110 ? -8.610  4.206    -80.740 1.00 36.78 ? 110 GLN   L CA  1 
ATOM   14875 C  C   . GLN   L  1 110 ? -7.155  4.191    -81.206 1.00 39.06 ? 110 GLN   L C   1 
ATOM   14876 O  O   . GLN   L  1 110 ? -6.890  4.478    -82.376 1.00 41.35 ? 110 GLN   L O   1 
ATOM   14877 C  CB  . GLN   L  1 110 ? -8.997  5.588    -80.197 1.00 42.12 ? 110 GLN   L CB  1 
ATOM   14878 C  CG  . GLN   L  1 110 ? -10.526 5.840    -80.116 1.00 39.90 ? 110 GLN   L CG  1 
ATOM   14879 N  N   . VAL   L  1 111 ? -6.197  3.870    -80.333 1.00 36.83 ? 111 VAL   L N   1 
ATOM   14880 C  CA  . VAL   L  1 111 ? -4.800  3.827    -80.744 1.00 33.39 ? 111 VAL   L CA  1 
ATOM   14881 C  C   . VAL   L  1 111 ? -4.321  2.394    -80.989 1.00 34.36 ? 111 VAL   L C   1 
ATOM   14882 O  O   . VAL   L  1 111 ? -3.126  2.166    -81.194 1.00 33.36 ? 111 VAL   L O   1 
ATOM   14883 C  CB  . VAL   L  1 111 ? -3.887  4.594    -79.757 1.00 35.46 ? 111 VAL   L CB  1 
ATOM   14884 C  CG1 . VAL   L  1 111 ? -4.421  6.021    -79.560 1.00 39.13 ? 111 VAL   L CG1 1 
ATOM   14885 C  CG2 . VAL   L  1 111 ? -3.727  3.906    -78.392 1.00 34.30 ? 111 VAL   L CG2 1 
ATOM   14886 N  N   . HIS   L  1 112 ? -5.240  1.432    -81.026 1.00 30.24 ? 112 HIS   L N   1 
ATOM   14887 C  CA  . HIS   L  1 112 ? -4.958  0.063    -81.445 1.00 30.96 ? 112 HIS   L CA  1 
ATOM   14888 C  C   . HIS   L  1 112 ? -4.076  -0.697   -80.457 1.00 32.59 ? 112 HIS   L C   1 
ATOM   14889 O  O   . HIS   L  1 112 ? -3.376  -1.637   -80.838 1.00 32.51 ? 112 HIS   L O   1 
ATOM   14890 C  CB  . HIS   L  1 112 ? -4.340  0.046    -82.835 1.00 33.34 ? 112 HIS   L CB  1 
ATOM   14891 C  CG  . HIS   L  1 112 ? -5.061  0.924    -83.807 1.00 35.89 ? 112 HIS   L CG  1 
ATOM   14892 N  ND1 . HIS   L  1 112 ? -6.422  0.847    -84.007 1.00 44.08 ? 112 HIS   L ND1 1 
ATOM   14893 C  CD2 . HIS   L  1 112 ? -4.616  1.913    -84.615 1.00 45.56 ? 112 HIS   L CD2 1 
ATOM   14894 C  CE1 . HIS   L  1 112 ? -6.782  1.735    -84.915 1.00 44.53 ? 112 HIS   L CE1 1 
ATOM   14895 N  NE2 . HIS   L  1 112 ? -5.704  2.395    -85.299 1.00 46.28 ? 112 HIS   L NE2 1 
ATOM   14896 N  N   . ASP   L  1 113 ? -4.122  -0.316   -79.186 1.00 33.76 ? 113 ASP   L N   1 
ATOM   14897 C  CA  . ASP   L  1 113 ? -3.432  -1.052   -78.128 1.00 31.31 ? 113 ASP   L CA  1 
ATOM   14898 C  C   . ASP   L  1 113 ? -4.398  -2.098   -77.568 1.00 29.52 ? 113 ASP   L C   1 
ATOM   14899 O  O   . ASP   L  1 113 ? -4.965  -1.980   -76.482 1.00 31.37 ? 113 ASP   L O   1 
ATOM   14900 C  CB  . ASP   L  1 113 ? -2.927  -0.089   -77.062 1.00 31.73 ? 113 ASP   L CB  1 
ATOM   14901 C  CG  . ASP   L  1 113 ? -2.047  -0.758   -76.033 1.00 29.91 ? 113 ASP   L CG  1 
ATOM   14902 O  OD1 . ASP   L  1 113 ? -1.936  -2.000   -76.054 1.00 29.18 ? 113 ASP   L OD1 1 
ATOM   14903 O  OD2 . ASP   L  1 113 ? -1.472  -0.042   -75.188 1.00 32.03 ? 113 ASP   L OD2 1 
ATOM   14904 N  N   . TYR   L  1 114 ? -4.586  -3.148   -78.363 1.00 25.89 ? 114 TYR   L N   1 
ATOM   14905 C  CA  . TYR   L  1 114 ? -5.588  -4.159   -78.046 1.00 27.75 ? 114 TYR   L CA  1 
ATOM   14906 C  C   . TYR   L  1 114 ? -5.215  -5.011   -76.843 1.00 21.88 ? 114 TYR   L C   1 
ATOM   14907 O  O   . TYR   L  1 114 ? -6.107  -5.527   -76.165 1.00 30.72 ? 114 TYR   L O   1 
ATOM   14908 C  CB  . TYR   L  1 114 ? -5.801  -5.029   -79.262 1.00 29.77 ? 114 TYR   L CB  1 
ATOM   14909 C  CG  . TYR   L  1 114 ? -6.269  -4.228   -80.458 1.00 33.21 ? 114 TYR   L CG  1 
ATOM   14910 C  CD1 . TYR   L  1 114 ? -7.456  -3.534   -80.411 1.00 30.23 ? 114 TYR   L CD1 1 
ATOM   14911 C  CD2 . TYR   L  1 114 ? -5.512  -4.164   -81.628 1.00 32.39 ? 114 TYR   L CD2 1 
ATOM   14912 C  CE1 . TYR   L  1 114 ? -7.907  -2.794   -81.489 1.00 36.76 ? 114 TYR   L CE1 1 
ATOM   14913 C  CE2 . TYR   L  1 114 ? -5.949  -3.419   -82.716 1.00 33.54 ? 114 TYR   L CE2 1 
ATOM   14914 C  CZ  . TYR   L  1 114 ? -7.147  -2.735   -82.635 1.00 38.08 ? 114 TYR   L CZ  1 
ATOM   14915 O  OH  . TYR   L  1 114 ? -7.600  -2.001   -83.703 1.00 34.12 ? 114 TYR   L OH  1 
ATOM   14916 N  N   . VAL   L  1 115 ? -3.924  -5.221   -76.598 1.00 27.19 ? 115 VAL   L N   1 
ATOM   14917 C  CA  . VAL   L  1 115 ? -3.515  -6.006   -75.428 1.00 26.34 ? 115 VAL   L CA  1 
ATOM   14918 C  C   . VAL   L  1 115 ? -3.829  -5.251   -74.145 1.00 29.55 ? 115 VAL   L C   1 
ATOM   14919 O  O   . VAL   L  1 115 ? -4.346  -5.830   -73.180 1.00 24.07 ? 115 VAL   L O   1 
ATOM   14920 C  CB  . VAL   L  1 115 ? -2.022  -6.369   -75.532 1.00 24.21 ? 115 VAL   L CB  1 
ATOM   14921 C  CG1 . VAL   L  1 115 ? -1.538  -7.116   -74.290 1.00 28.08 ? 115 VAL   L CG1 1 
ATOM   14922 C  CG2 . VAL   L  1 115 ? -1.797  -7.218   -76.796 1.00 28.50 ? 115 VAL   L CG2 1 
ATOM   14923 N  N   . SER   L  1 116 ? -3.488  -3.954   -74.092 1.00 29.70 ? 116 SER   L N   1 
ATOM   14924 C  CA  . SER   L  1 116 ? -3.891  -3.151   -72.934 1.00 33.68 ? 116 SER   L CA  1 
ATOM   14925 C  C   . SER   L  1 116 ? -5.398  -3.171   -72.748 1.00 24.78 ? 116 SER   L C   1 
ATOM   14926 O  O   . SER   L  1 116 ? -5.892  -3.309   -71.619 1.00 28.92 ? 116 SER   L O   1 
ATOM   14927 C  CB  . SER   L  1 116 ? -3.426  -1.718   -73.071 1.00 28.67 ? 116 SER   L CB  1 
ATOM   14928 O  OG  . SER   L  1 116 ? -2.042  -1.647   -72.888 1.00 28.14 ? 116 SER   L OG  1 
ATOM   14929 N  N   . ARG   L  1 117 ? -6.154  -3.000   -73.840 1.00 27.82 ? 117 ARG   L N   1 
ATOM   14930 C  CA  . ARG   L  1 117 ? -7.600  -3.107   -73.743 1.00 31.77 ? 117 ARG   L CA  1 
ATOM   14931 C  C   . ARG   L  1 117 ? -7.992  -4.421   -73.082 1.00 31.04 ? 117 ARG   L C   1 
ATOM   14932 O  O   . ARG   L  1 117 ? -8.851  -4.448   -72.192 1.00 31.20 ? 117 ARG   L O   1 
ATOM   14933 C  CB  . ARG   L  1 117 ? -8.256  -2.994   -75.122 1.00 30.66 ? 117 ARG   L CB  1 
ATOM   14934 C  CG  . ARG   L  1 117 ? -9.709  -3.465   -75.111 1.00 30.72 ? 117 ARG   L CG  1 
ATOM   14935 C  CD  . ARG   L  1 117 ? -10.458 -3.157   -76.371 1.00 27.80 ? 117 ARG   L CD  1 
ATOM   14936 N  NE  . ARG   L  1 117 ? -11.822 -3.653   -76.270 1.00 33.03 ? 117 ARG   L NE  1 
ATOM   14937 C  CZ  . ARG   L  1 117 ? -12.866 -3.093   -76.863 1.00 38.63 ? 117 ARG   L CZ  1 
ATOM   14938 N  NH1 . ARG   L  1 117 ? -12.736 -2.026   -77.640 1.00 32.01 ? 117 ARG   L NH1 1 
ATOM   14939 N  NH2 . ARG   L  1 117 ? -14.065 -3.617   -76.678 1.00 31.44 ? 117 ARG   L NH2 1 
ATOM   14940 N  N   . ASP   L  1 118 ? -7.365  -5.526   -73.513 1.00 29.79 ? 118 ASP   L N   1 
ATOM   14941 C  CA  . ASP   L  1 118 ? -7.727  -6.847   -73.000 1.00 32.84 ? 118 ASP   L CA  1 
ATOM   14942 C  C   . ASP   L  1 118 ? -7.445  -6.927   -71.507 1.00 25.07 ? 118 ASP   L C   1 
ATOM   14943 O  O   . ASP   L  1 118 ? -8.276  -7.412   -70.729 1.00 27.40 ? 118 ASP   L O   1 
ATOM   14944 C  CB  . ASP   L  1 118 ? -6.956  -7.931   -73.771 1.00 34.28 ? 118 ASP   L CB  1 
ATOM   14945 C  CG  . ASP   L  1 118 ? -7.570  -9.314   -73.633 1.00 29.19 ? 118 ASP   L CG  1 
ATOM   14946 O  OD1 . ASP   L  1 118 ? -8.794  -9.426   -73.754 1.00 30.36 ? 118 ASP   L OD1 1 
ATOM   14947 O  OD2 . ASP   L  1 118 ? -6.823  -10.291  -73.433 1.00 29.71 ? 118 ASP   L OD2 1 
ATOM   14948 N  N   . LEU   L  1 119 ? -6.294  -6.416   -71.080 1.00 24.49 ? 119 LEU   L N   1 
ATOM   14949 C  CA  . LEU   L  1 119 ? -6.000  -6.408   -69.656 1.00 28.30 ? 119 LEU   L CA  1 
ATOM   14950 C  C   . LEU   L  1 119 ? -7.028  -5.577   -68.881 1.00 30.74 ? 119 LEU   L C   1 
ATOM   14951 O  O   . LEU   L  1 119 ? -7.481  -5.980   -67.804 1.00 24.27 ? 119 LEU   L O   1 
ATOM   14952 C  CB  . LEU   L  1 119 ? -4.578  -5.884   -69.429 1.00 28.54 ? 119 LEU   L CB  1 
ATOM   14953 C  CG  . LEU   L  1 119 ? -4.247  -5.575   -67.980 1.00 33.38 ? 119 LEU   L CG  1 
ATOM   14954 C  CD1 . LEU   L  1 119 ? -4.351  -6.868   -67.206 1.00 36.15 ? 119 LEU   L CD1 1 
ATOM   14955 C  CD2 . LEU   L  1 119 ? -2.840  -4.946   -67.846 1.00 32.75 ? 119 LEU   L CD2 1 
ATOM   14956 N  N   . LEU   L  1 120 ? -7.405  -4.411   -69.409 1.00 29.59 ? 120 LEU   L N   1 
ATOM   14957 C  CA  . LEU   L  1 120 ? -8.355  -3.565   -68.702 1.00 29.00 ? 120 LEU   L CA  1 
ATOM   14958 C  C   . LEU   L  1 120 ? -9.735  -4.207   -68.666 1.00 26.98 ? 120 LEU   L C   1 
ATOM   14959 O  O   . LEU   L  1 120 ? -10.450 -4.084   -67.667 1.00 26.20 ? 120 LEU   L O   1 
ATOM   14960 C  CB  . LEU   L  1 120 ? -8.431  -2.187   -69.360 1.00 31.87 ? 120 LEU   L CB  1 
ATOM   14961 C  CG  . LEU   L  1 120 ? -7.165  -1.351   -69.249 1.00 24.49 ? 120 LEU   L CG  1 
ATOM   14962 C  CD1 . LEU   L  1 120 ? -7.336  0.044    -69.874 1.00 36.18 ? 120 LEU   L CD1 1 
ATOM   14963 C  CD2 . LEU   L  1 120 ? -6.689  -1.204   -67.833 1.00 31.74 ? 120 LEU   L CD2 1 
ATOM   14964 N  N   . LYS   L  1 121 ? -10.122 -4.896   -69.746 1.00 25.43 ? 121 LYS   L N   1 
ATOM   14965 C  CA  . LYS   L  1 121 ? -11.391 -5.611   -69.771 1.00 30.89 ? 121 LYS   L CA  1 
ATOM   14966 C  C   . LYS   L  1 121 ? -11.443 -6.699   -68.698 1.00 27.81 ? 121 LYS   L C   1 
ATOM   14967 O  O   . LYS   L  1 121 ? -12.462 -6.851   -68.004 1.00 26.01 ? 121 LYS   L O   1 
ATOM   14968 C  CB  . LYS   L  1 121 ? -11.609 -6.203   -71.157 1.00 27.85 ? 121 LYS   L CB  1 
ATOM   14969 C  CG  . LYS   L  1 121 ? -12.904 -6.911   -71.325 1.00 32.01 ? 121 LYS   L CG  1 
ATOM   14970 C  CD  . LYS   L  1 121 ? -12.856 -8.390   -70.952 1.00 36.86 ? 121 LYS   L CD  1 
ATOM   14971 C  CE  . LYS   L  1 121 ? -11.999 -9.232   -71.922 1.00 37.59 ? 121 LYS   L CE  1 
ATOM   14972 N  NZ  . LYS   L  1 121 ? -11.900 -10.648  -71.402 1.00 41.16 ? 121 LYS   L NZ  1 
ATOM   14973 N  N   . ASP   L  1 122 ? -10.361 -7.474   -68.550 1.00 29.23 ? 122 ASP   L N   1 
ATOM   14974 C  CA  . ASP   L  1 122 ? -10.325 -8.475   -67.483 1.00 26.88 ? 122 ASP   L CA  1 
ATOM   14975 C  C   . ASP   L  1 122 ? -10.465 -7.830   -66.105 1.00 28.87 ? 122 ASP   L C   1 
ATOM   14976 O  O   . ASP   L  1 122 ? -11.164 -8.357   -65.236 1.00 29.35 ? 122 ASP   L O   1 
ATOM   14977 C  CB  . ASP   L  1 122 ? -9.035  -9.282   -67.551 1.00 25.57 ? 122 ASP   L CB  1 
ATOM   14978 C  CG  . ASP   L  1 122 ? -8.958  -10.199  -68.777 1.00 28.35 ? 122 ASP   L CG  1 
ATOM   14979 O  OD1 . ASP   L  1 122 ? -9.999  -10.492  -69.405 1.00 30.12 ? 122 ASP   L OD1 1 
ATOM   14980 O  OD2 . ASP   L  1 122 ? -7.830  -10.635  -69.111 1.00 35.14 ? 122 ASP   L OD2 1 
ATOM   14981 N  N   . ILE   L  1 123 ? -9.775  -6.708   -65.875 1.00 25.07 ? 123 ILE   L N   1 
ATOM   14982 C  CA  . ILE   L  1 123 ? -9.904  -5.994   -64.609 1.00 25.08 ? 123 ILE   L CA  1 
ATOM   14983 C  C   . ILE   L  1 123 ? -11.325 -5.495   -64.427 1.00 28.18 ? 123 ILE   L C   1 
ATOM   14984 O  O   . ILE   L  1 123 ? -11.914 -5.646   -63.352 1.00 30.04 ? 123 ILE   L O   1 
ATOM   14985 C  CB  . ILE   L  1 123 ? -8.881  -4.846   -64.539 1.00 23.64 ? 123 ILE   L CB  1 
ATOM   14986 C  CG1 . ILE   L  1 123 ? -7.470  -5.410   -64.456 1.00 27.03 ? 123 ILE   L CG1 1 
ATOM   14987 C  CG2 . ILE   L  1 123 ? -9.167  -3.951   -63.320 1.00 30.13 ? 123 ILE   L CG2 1 
ATOM   14988 C  CD1 . ILE   L  1 123 ? -6.403  -4.361   -64.482 1.00 27.92 ? 123 ILE   L CD1 1 
ATOM   14989 N  N   . LEU   L  1 124 ? -11.920 -4.946   -65.497 1.00 28.80 ? 124 LEU   L N   1 
ATOM   14990 C  CA  . LEU   L  1 124 ? -13.302 -4.477   -65.443 1.00 25.48 ? 124 LEU   L CA  1 
ATOM   14991 C  C   . LEU   L  1 124 ? -14.261 -5.604   -65.060 1.00 31.78 ? 124 LEU   L C   1 
ATOM   14992 O  O   . LEU   L  1 124 ? -15.200 -5.402   -64.278 1.00 27.60 ? 124 LEU   L O   1 
ATOM   14993 C  CB  . LEU   L  1 124 ? -13.704 -3.889   -66.810 1.00 24.19 ? 124 LEU   L CB  1 
ATOM   14994 C  CG  . LEU   L  1 124 ? -15.122 -3.319   -66.913 1.00 28.83 ? 124 LEU   L CG  1 
ATOM   14995 C  CD1 . LEU   L  1 124 ? -15.347 -2.178   -65.934 1.00 29.81 ? 124 LEU   L CD1 1 
ATOM   14996 C  CD2 . LEU   L  1 124 ? -15.430 -2.865   -68.367 1.00 35.37 ? 124 LEU   L CD2 1 
ATOM   14997 N  N   . GLU   L  1 125 ? -14.048 -6.797   -65.611 1.00 27.20 ? 125 GLU   L N   1 
ATOM   14998 C  CA  . GLU   L  1 125 ? -14.878 -7.939   -65.251 1.00 32.24 ? 125 GLU   L CA  1 
ATOM   14999 C  C   . GLU   L  1 125 ? -14.779 -8.249   -63.755 1.00 26.49 ? 125 GLU   L C   1 
ATOM   15000 O  O   . GLU   L  1 125 ? -15.798 -8.513   -63.099 1.00 30.12 ? 125 GLU   L O   1 
ATOM   15001 C  CB  . GLU   L  1 125 ? -14.476 -9.153   -66.090 1.00 29.08 ? 125 GLU   L CB  1 
ATOM   15002 C  CG  . GLU   L  1 125 ? -15.098 -9.149   -67.445 1.00 42.30 ? 125 GLU   L CG  1 
ATOM   15003 C  CD  . GLU   L  1 125 ? -14.636 -10.282  -68.376 1.00 46.96 ? 125 GLU   L CD  1 
ATOM   15004 O  OE1 . GLU   L  1 125 ? -13.548 -10.880  -68.162 1.00 36.12 ? 125 GLU   L OE1 1 
ATOM   15005 O  OE2 . GLU   L  1 125 ? -15.379 -10.549  -69.349 1.00 38.50 ? 125 GLU   L OE2 1 
ATOM   15006 N  N   . SER   L  1 126 ? -13.564 -8.247   -63.213 1.00 26.99 ? 126 SER   L N   1 
ATOM   15007 C  CA  A SER   L  1 126 ? -13.393 -8.463   -61.780 0.50 30.34 ? 126 SER   L CA  1 
ATOM   15008 C  CA  B SER   L  1 126 ? -13.396 -8.461   -61.776 0.50 30.35 ? 126 SER   L CA  1 
ATOM   15009 C  C   . SER   L  1 126 ? -14.116 -7.379   -60.980 1.00 33.05 ? 126 SER   L C   1 
ATOM   15010 O  O   . SER   L  1 126 ? -14.822 -7.680   -60.016 1.00 26.20 ? 126 SER   L O   1 
ATOM   15011 C  CB  A SER   L  1 126 ? -11.905 -8.490   -61.441 0.50 28.77 ? 126 SER   L CB  1 
ATOM   15012 C  CB  B SER   L  1 126 ? -11.918 -8.474   -61.405 0.50 28.75 ? 126 SER   L CB  1 
ATOM   15013 O  OG  A SER   L  1 126 ? -11.690 -8.301   -60.060 0.50 27.18 ? 126 SER   L OG  1 
ATOM   15014 O  OG  B SER   L  1 126 ? -11.290 -9.647   -61.872 0.50 31.28 ? 126 SER   L OG  1 
ATOM   15015 N  N   . GLU   L  1 127 ? -13.955 -6.114   -61.368 1.00 33.00 ? 127 GLU   L N   1 
ATOM   15016 C  CA  . GLU   L  1 127 ? -14.620 -5.042   -60.633 1.00 30.33 ? 127 GLU   L CA  1 
ATOM   15017 C  C   . GLU   L  1 127 ? -16.149 -5.145   -60.718 1.00 29.79 ? 127 GLU   L C   1 
ATOM   15018 O  O   . GLU   L  1 127 ? -16.840 -4.868   -59.734 1.00 31.46 ? 127 GLU   L O   1 
ATOM   15019 C  CB  . GLU   L  1 127 ? -14.135 -3.683   -61.123 1.00 29.79 ? 127 GLU   L CB  1 
ATOM   15020 C  CG  . GLU   L  1 127 ? -12.638 -3.449   -61.028 1.00 35.34 ? 127 GLU   L CG  1 
ATOM   15021 C  CD  . GLU   L  1 127 ? -12.026 -3.786   -59.687 1.00 38.82 ? 127 GLU   L CD  1 
ATOM   15022 O  OE1 . GLU   L  1 127 ? -12.693 -3.650   -58.648 1.00 39.01 ? 127 GLU   L OE1 1 
ATOM   15023 O  OE2 . GLU   L  1 127 ? -10.845 -4.174   -59.686 1.00 44.36 ? 127 GLU   L OE2 1 
ATOM   15024 N  N   . GLU   L  1 128 ? -16.715 -5.551   -61.860 1.00 27.96 ? 128 GLU   L N   1 
ATOM   15025 C  CA  . GLU   L  1 128 ? -18.170 -5.652   -61.882 1.00 28.46 ? 128 GLU   L CA  1 
ATOM   15026 C  C   . GLU   L  1 128 ? -18.635 -6.779   -60.978 1.00 32.75 ? 128 GLU   L C   1 
ATOM   15027 O  O   . GLU   L  1 128 ? -19.699 -6.675   -60.355 1.00 29.22 ? 128 GLU   L O   1 
ATOM   15028 C  CB  . GLU   L  1 128 ? -18.712 -5.829   -63.309 1.00 26.09 ? 128 GLU   L CB  1 
ATOM   15029 C  CG  . GLU   L  1 128 ? -18.626 -4.526   -64.118 1.00 34.61 ? 128 GLU   L CG  1 
ATOM   15030 C  CD  . GLU   L  1 128 ? -19.316 -4.579   -65.473 1.00 30.16 ? 128 GLU   L CD  1 
ATOM   15031 O  OE1 . GLU   L  1 128 ? -19.981 -5.584   -65.796 1.00 26.96 ? 128 GLU   L OE1 1 
ATOM   15032 O  OE2 . GLU   L  1 128 ? -19.153 -3.598   -66.234 1.00 36.33 ? 128 GLU   L OE2 1 
ATOM   15033 N  N   . GLU   L  1 129 ? -17.822 -7.829   -60.839 1.00 30.29 ? 129 GLU   L N   1 
ATOM   15034 C  CA  . GLU   L  1 129 ? -18.157 -8.872   -59.871 1.00 33.78 ? 129 GLU   L CA  1 
ATOM   15035 C  C   . GLU   L  1 129 ? -18.090 -8.337   -58.440 1.00 24.31 ? 129 GLU   L C   1 
ATOM   15036 O  O   . GLU   L  1 129 ? -18.913 -8.716   -57.596 1.00 26.28 ? 129 GLU   L O   1 
ATOM   15037 C  CB  . GLU   L  1 129 ? -17.237 -10.090  -60.049 1.00 32.66 ? 129 GLU   L CB  1 
ATOM   15038 C  CG  . GLU   L  1 129 ? -17.613 -11.266  -59.161 1.00 47.24 ? 129 GLU   L CG  1 
ATOM   15039 N  N   . HIS   L  1 130 ? -17.123 -7.473   -58.139 1.00 26.36 ? 130 HIS   L N   1 
ATOM   15040 C  CA  A HIS   L  1 130 ? -17.108 -6.840   -56.828 0.50 27.73 ? 130 HIS   L CA  1 
ATOM   15041 C  CA  B HIS   L  1 130 ? -17.098 -6.834   -56.824 0.50 27.73 ? 130 HIS   L CA  1 
ATOM   15042 C  C   . HIS   L  1 130 ? -18.330 -5.949   -56.637 1.00 29.71 ? 130 HIS   L C   1 
ATOM   15043 O  O   . HIS   L  1 130 ? -18.947 -5.947   -55.567 1.00 28.07 ? 130 HIS   L O   1 
ATOM   15044 C  CB  A HIS   L  1 130 ? -15.827 -6.032   -56.644 0.50 30.89 ? 130 HIS   L CB  1 
ATOM   15045 C  CB  B HIS   L  1 130 ? -15.823 -5.993   -56.617 0.50 30.89 ? 130 HIS   L CB  1 
ATOM   15046 C  CG  A HIS   L  1 130 ? -15.542 -5.684   -55.220 0.50 32.85 ? 130 HIS   L CG  1 
ATOM   15047 C  CG  B HIS   L  1 130 ? -14.531 -6.760   -56.697 0.50 32.13 ? 130 HIS   L CG  1 
ATOM   15048 N  ND1 A HIS   L  1 130 ? -14.529 -4.829   -54.850 0.50 34.65 ? 130 HIS   L ND1 1 
ATOM   15049 N  ND1 B HIS   L  1 130 ? -14.461 -8.138   -56.654 0.50 33.35 ? 130 HIS   L ND1 1 
ATOM   15050 C  CD2 A HIS   L  1 130 ? -16.123 -6.099   -54.070 0.50 32.11 ? 130 HIS   L CD2 1 
ATOM   15051 C  CD2 B HIS   L  1 130 ? -13.252 -6.326   -56.846 0.50 34.74 ? 130 HIS   L CD2 1 
ATOM   15052 C  CE1 A HIS   L  1 130 ? -14.506 -4.722   -53.536 0.50 28.82 ? 130 HIS   L CE1 1 
ATOM   15053 C  CE1 B HIS   L  1 130 ? -13.199 -8.518   -56.779 0.50 32.53 ? 130 HIS   L CE1 1 
ATOM   15054 N  NE2 A HIS   L  1 130 ? -15.459 -5.487   -53.039 0.50 33.53 ? 130 HIS   L NE2 1 
ATOM   15055 N  NE2 B HIS   L  1 130 ? -12.446 -7.439   -56.895 0.50 28.72 ? 130 HIS   L NE2 1 
ATOM   15056 N  N   . ILE   L  1 131 ? -18.699 -5.184   -57.661 1.00 27.45 ? 131 ILE   L N   1 
ATOM   15057 C  CA  . ILE   L  1 131 ? -19.915 -4.373   -57.570 1.00 27.89 ? 131 ILE   L CA  1 
ATOM   15058 C  C   . ILE   L  1 131 ? -21.137 -5.245   -57.291 1.00 26.91 ? 131 ILE   L C   1 
ATOM   15059 O  O   . ILE   L  1 131 ? -21.980 -4.908   -56.446 1.00 30.01 ? 131 ILE   L O   1 
ATOM   15060 C  CB  . ILE   L  1 131 ? -20.085 -3.533   -58.854 1.00 26.61 ? 131 ILE   L CB  1 
ATOM   15061 C  CG1 . ILE   L  1 131 ? -19.086 -2.357   -58.832 1.00 26.92 ? 131 ILE   L CG1 1 
ATOM   15062 C  CG2 . ILE   L  1 131 ? -21.561 -3.072   -58.978 1.00 29.93 ? 131 ILE   L CG2 1 
ATOM   15063 C  CD1 . ILE   L  1 131 ? -18.882 -1.654   -60.208 1.00 34.13 ? 131 ILE   L CD1 1 
ATOM   15064 N  N   . ASP   L  1 132 ? -21.265 -6.371   -58.001 1.00 25.39 ? 132 ASP   L N   1 
ATOM   15065 C  CA  . ASP   L  1 132 ? -22.371 -7.291   -57.752 1.00 26.15 ? 132 ASP   L CA  1 
ATOM   15066 C  C   . ASP   L  1 132 ? -22.403 -7.722   -56.286 1.00 30.47 ? 132 ASP   L C   1 
ATOM   15067 O  O   . ASP   L  1 132 ? -23.453 -7.681   -55.624 1.00 30.58 ? 132 ASP   L O   1 
ATOM   15068 C  CB  . ASP   L  1 132 ? -22.231 -8.512   -58.680 1.00 29.55 ? 132 ASP   L CB  1 
ATOM   15069 C  CG  . ASP   L  1 132 ? -23.473 -9.422   -58.693 1.00 35.88 ? 132 ASP   L CG  1 
ATOM   15070 O  OD1 . ASP   L  1 132 ? -24.524 -9.133   -58.069 1.00 40.00 ? 132 ASP   L OD1 1 
ATOM   15071 O  OD2 . ASP   L  1 132 ? -23.366 -10.460  -59.356 1.00 36.86 ? 132 ASP   L OD2 1 
ATOM   15072 N  N   . TYR   L  1 133 ? -21.259 -8.150   -55.764 1.00 26.96 ? 133 TYR   L N   1 
ATOM   15073 C  CA  . TYR   L  1 133 ? -21.193 -8.562   -54.368 1.00 30.50 ? 133 TYR   L CA  1 
ATOM   15074 C  C   . TYR   L  1 133 ? -21.641 -7.444   -53.434 1.00 34.06 ? 133 TYR   L C   1 
ATOM   15075 O  O   . TYR   L  1 133 ? -22.463 -7.665   -52.536 1.00 26.60 ? 133 TYR   L O   1 
ATOM   15076 C  CB  . TYR   L  1 133 ? -19.766 -8.993   -54.015 1.00 30.30 ? 133 TYR   L CB  1 
ATOM   15077 C  CG  . TYR   L  1 133 ? -19.533 -9.091   -52.541 1.00 29.92 ? 133 TYR   L CG  1 
ATOM   15078 C  CD1 . TYR   L  1 133 ? -19.943 -10.211  -51.812 1.00 31.56 ? 133 TYR   L CD1 1 
ATOM   15079 C  CD2 . TYR   L  1 133 ? -18.939 -8.051   -51.862 1.00 34.24 ? 133 TYR   L CD2 1 
ATOM   15080 C  CE1 . TYR   L  1 133 ? -19.730 -10.283  -50.431 1.00 36.13 ? 133 TYR   L CE1 1 
ATOM   15081 C  CE2 . TYR   L  1 133 ? -18.710 -8.115   -50.491 1.00 39.58 ? 133 TYR   L CE2 1 
ATOM   15082 C  CZ  . TYR   L  1 133 ? -19.104 -9.222   -49.780 1.00 41.13 ? 133 TYR   L CZ  1 
ATOM   15083 O  OH  . TYR   L  1 133 ? -18.867 -9.238   -48.412 1.00 36.73 ? 133 TYR   L OH  1 
ATOM   15084 N  N   . LEU   L  1 134 ? -21.075 -6.243   -53.605 1.00 28.01 ? 134 LEU   L N   1 
ATOM   15085 C  CA  . LEU   L  1 134 ? -21.391 -5.127   -52.712 1.00 29.12 ? 134 LEU   L CA  1 
ATOM   15086 C  C   . LEU   L  1 134 ? -22.873 -4.768   -52.776 1.00 25.63 ? 134 LEU   L C   1 
ATOM   15087 O  O   . LEU   L  1 134 ? -23.542 -4.604   -51.747 1.00 30.77 ? 134 LEU   L O   1 
ATOM   15088 C  CB  . LEU   L  1 134 ? -20.551 -3.919   -53.083 1.00 26.66 ? 134 LEU   L CB  1 
ATOM   15089 C  CG  . LEU   L  1 134 ? -19.060 -4.063   -52.851 1.00 27.78 ? 134 LEU   L CG  1 
ATOM   15090 C  CD1 . LEU   L  1 134 ? -18.242 -3.038   -53.616 1.00 28.04 ? 134 LEU   L CD1 1 
ATOM   15091 C  CD2 . LEU   L  1 134 ? -18.832 -3.922   -51.374 1.00 32.37 ? 134 LEU   L CD2 1 
ATOM   15092 N  N   . GLU   L  1 135 ? -23.411 -4.650   -53.983 1.00 29.97 ? 135 GLU   L N   1 
ATOM   15093 C  CA  . GLU   L  1 135 ? -24.825 -4.322   -54.120 1.00 32.49 ? 135 GLU   L CA  1 
ATOM   15094 C  C   . GLU   L  1 135 ? -25.696 -5.381   -53.445 1.00 37.14 ? 135 GLU   L C   1 
ATOM   15095 O  O   . GLU   L  1 135 ? -26.721 -5.060   -52.823 1.00 28.61 ? 135 GLU   L O   1 
ATOM   15096 C  CB  . GLU   L  1 135 ? -25.182 -4.175   -55.598 1.00 34.42 ? 135 GLU   L CB  1 
ATOM   15097 C  CG  . GLU   L  1 135 ? -24.563 -2.947   -56.307 1.00 22.90 ? 135 GLU   L CG  1 
ATOM   15098 C  CD  . GLU   L  1 135 ? -24.922 -2.924   -57.793 1.00 35.90 ? 135 GLU   L CD  1 
ATOM   15099 O  OE1 . GLU   L  1 135 ? -25.287 -3.994   -58.352 1.00 35.95 ? 135 GLU   L OE1 1 
ATOM   15100 O  OE2 . GLU   L  1 135 ? -24.846 -1.834   -58.391 1.00 41.12 ? 135 GLU   L OE2 1 
ATOM   15101 N  N   . THR   L  1 136 ? -25.296 -6.652   -53.548 1.00 28.37 ? 136 THR   L N   1 
ATOM   15102 C  CA  . THR   L  1 136 ? -26.049 -7.728   -52.904 1.00 28.22 ? 136 THR   L CA  1 
ATOM   15103 C  C   . THR   L  1 136 ? -25.991 -7.593   -51.382 1.00 25.06 ? 136 THR   L C   1 
ATOM   15104 O  O   . THR   L  1 136 ? -27.012 -7.733   -50.704 1.00 29.51 ? 136 THR   L O   1 
ATOM   15105 C  CB  . THR   L  1 136 ? -25.495 -9.082   -53.376 1.00 34.97 ? 136 THR   L CB  1 
ATOM   15106 O  OG1 . THR   L  1 136 ? -25.670 -9.191   -54.790 1.00 39.91 ? 136 THR   L OG1 1 
ATOM   15107 C  CG2 . THR   L  1 136 ? -26.186 -10.251  -52.708 1.00 30.19 ? 136 THR   L CG2 1 
ATOM   15108 N  N   . GLN   L  1 137 ? -24.810 -7.313   -50.830 1.00 27.64 ? 137 GLN   L N   1 
ATOM   15109 C  CA  . GLN   L  1 137 ? -24.705 -7.199   -49.374 1.00 34.02 ? 137 GLN   L CA  1 
ATOM   15110 C  C   . GLN   L  1 137 ? -25.592 -6.070   -48.859 1.00 33.39 ? 137 GLN   L C   1 
ATOM   15111 O  O   . GLN   L  1 137 ? -26.263 -6.221   -47.841 1.00 30.30 ? 137 GLN   L O   1 
ATOM   15112 C  CB  . GLN   L  1 137 ? -23.256 -6.959   -48.946 1.00 26.59 ? 137 GLN   L CB  1 
ATOM   15113 C  CG  . GLN   L  1 137 ? -22.264 -8.063   -49.322 1.00 30.78 ? 137 GLN   L CG  1 
ATOM   15114 C  CD  . GLN   L  1 137 ? -22.813 -9.453   -49.057 1.00 28.87 ? 137 GLN   L CD  1 
ATOM   15115 O  OE1 . GLN   L  1 137 ? -23.080 -10.216  -49.974 1.00 40.80 ? 137 GLN   L OE1 1 
ATOM   15116 N  NE2 . GLN   L  1 137 ? -23.000 -9.765   -47.825 1.00 31.74 ? 137 GLN   L NE2 1 
ATOM   15117 N  N   . LEU   L  1 138 ? -25.626 -4.943   -49.576 1.00 33.62 ? 138 LEU   L N   1 
ATOM   15118 C  CA  . LEU   L  1 138 ? -26.425 -3.804   -49.140 1.00 31.49 ? 138 LEU   L CA  1 
ATOM   15119 C  C   . LEU   L  1 138 ? -27.911 -4.100   -49.247 1.00 30.28 ? 138 LEU   L C   1 
ATOM   15120 O  O   . LEU   L  1 138 ? -28.692 -3.660   -48.394 1.00 30.10 ? 138 LEU   L O   1 
ATOM   15121 C  CB  . LEU   L  1 138 ? -26.053 -2.566   -49.952 1.00 34.23 ? 138 LEU   L CB  1 
ATOM   15122 C  CG  . LEU   L  1 138 ? -24.672 -2.013   -49.629 1.00 32.32 ? 138 LEU   L CG  1 
ATOM   15123 C  CD1 . LEU   L  1 138 ? -24.130 -1.157   -50.788 1.00 38.48 ? 138 LEU   L CD1 1 
ATOM   15124 C  CD2 . LEU   L  1 138 ? -24.673 -1.169   -48.353 1.00 33.65 ? 138 LEU   L CD2 1 
ATOM   15125 N  N   . GLY   L  1 139 ? -28.312 -4.861   -50.268 1.00 28.31 ? 139 GLY   L N   1 
ATOM   15126 C  CA  . GLY   L  1 139 ? -29.683 -5.339   -50.349 1.00 30.10 ? 139 GLY   L CA  1 
ATOM   15127 C  C   . GLY   L  1 139 ? -30.050 -6.337   -49.251 1.00 36.36 ? 139 GLY   L C   1 
ATOM   15128 O  O   . GLY   L  1 139 ? -31.186 -6.344   -48.757 1.00 29.24 ? 139 GLY   L O   1 
ATOM   15129 N  N   . LEU   L  1 140 ? -29.112 -7.207   -48.867 1.00 28.87 ? 140 LEU   L N   1 
ATOM   15130 C  CA  . LEU   L  1 140 ? -29.384 -8.151   -47.772 1.00 32.87 ? 140 LEU   L CA  1 
ATOM   15131 C  C   . LEU   L  1 140 ? -29.619 -7.434   -46.445 1.00 26.97 ? 140 LEU   L C   1 
ATOM   15132 O  O   . LEU   L  1 140 ? -30.438 -7.879   -45.640 1.00 28.37 ? 140 LEU   L O   1 
ATOM   15133 C  CB  . LEU   L  1 140 ? -28.230 -9.144   -47.610 1.00 31.98 ? 140 LEU   L CB  1 
ATOM   15134 C  CG  . LEU   L  1 140 ? -28.170 -10.268  -48.649 1.00 30.36 ? 140 LEU   L CG  1 
ATOM   15135 C  CD1 . LEU   L  1 140 ? -26.822 -11.067  -48.596 1.00 34.81 ? 140 LEU   L CD1 1 
ATOM   15136 C  CD2 . LEU   L  1 140 ? -29.378 -11.175  -48.459 1.00 31.83 ? 140 LEU   L CD2 1 
ATOM   15137 N  N   . ILE   L  1 141 ? -28.851 -6.380   -46.169 1.00 26.72 ? 141 ILE   L N   1 
ATOM   15138 C  CA  . ILE   L  1 141 ? -29.065 -5.581   -44.967 1.00 30.04 ? 141 ILE   L CA  1 
ATOM   15139 C  C   . ILE   L  1 141 ? -30.522 -5.160   -44.857 1.00 35.22 ? 141 ILE   L C   1 
ATOM   15140 O  O   . ILE   L  1 141 ? -31.134 -5.255   -43.780 1.00 30.34 ? 141 ILE   L O   1 
ATOM   15141 C  CB  . ILE   L  1 141 ? -28.129 -4.360   -44.962 1.00 31.26 ? 141 ILE   L CB  1 
ATOM   15142 C  CG1 . ILE   L  1 141 ? -26.714 -4.816   -44.622 1.00 33.37 ? 141 ILE   L CG1 1 
ATOM   15143 C  CG2 . ILE   L  1 141 ? -28.643 -3.294   -43.971 1.00 36.27 ? 141 ILE   L CG2 1 
ATOM   15144 C  CD1 . ILE   L  1 141 ? -25.640 -3.740   -44.702 1.00 34.16 ? 141 ILE   L CD1 1 
ATOM   15145 N  N   . GLN   L  1 142 ? -31.103 -4.705   -45.974 1.00 33.74 ? 142 GLN   L N   1 
ATOM   15146 C  CA  . GLN   L  1 142 ? -32.514 -4.308   -46.004 1.00 32.23 ? 142 GLN   L CA  1 
ATOM   15147 C  C   . GLN   L  1 142 ? -33.434 -5.509   -45.856 1.00 33.93 ? 142 GLN   L C   1 
ATOM   15148 O  O   . GLN   L  1 142 ? -34.470 -5.434   -45.192 1.00 33.86 ? 142 GLN   L O   1 
ATOM   15149 C  CB  . GLN   L  1 142 ? -32.834 -3.591   -47.322 1.00 35.66 ? 142 GLN   L CB  1 
ATOM   15150 C  CG  . GLN   L  1 142 ? -32.028 -2.356   -47.577 1.00 33.82 ? 142 GLN   L CG  1 
ATOM   15151 C  CD  . GLN   L  1 142 ? -32.301 -1.283   -46.529 1.00 50.64 ? 142 GLN   L CD  1 
ATOM   15152 O  OE1 . GLN   L  1 142 ? -33.442 -1.093   -46.095 1.00 56.73 ? 142 GLN   L OE1 1 
ATOM   15153 N  NE2 . GLN   L  1 142 ? -31.261 -0.594   -46.114 1.00 37.60 ? 142 GLN   L NE2 1 
ATOM   15154 N  N   . LYS   L  1 143 ? -33.083 -6.622   -46.489 1.00 33.92 ? 143 LYS   L N   1 
ATOM   15155 C  CA  . LYS   L  1 143 ? -33.965 -7.776   -46.481 1.00 28.70 ? 143 LYS   L CA  1 
ATOM   15156 C  C   . LYS   L  1 143 ? -33.949 -8.521   -45.147 1.00 30.64 ? 143 LYS   L C   1 
ATOM   15157 O  O   . LYS   L  1 143 ? -35.003 -8.961   -44.687 1.00 33.04 ? 143 LYS   L O   1 
ATOM   15158 C  CB  . LYS   L  1 143 ? -33.588 -8.731   -47.618 1.00 34.50 ? 143 LYS   L CB  1 
ATOM   15159 C  CG  . LYS   L  1 143 ? -33.920 -8.218   -49.009 1.00 44.80 ? 143 LYS   L CG  1 
ATOM   15160 C  CD  . LYS   L  1 143 ? -33.780 -9.320   -50.093 1.00 40.44 ? 143 LYS   L CD  1 
ATOM   15161 C  CE  . LYS   L  1 143 ? -34.296 -8.839   -51.458 1.00 54.42 ? 143 LYS   L CE  1 
ATOM   15162 N  NZ  . LYS   L  1 143 ? -33.452 -7.750   -52.064 1.00 52.06 ? 143 LYS   L NZ  1 
ATOM   15163 N  N   . VAL   L  1 144 ? -32.781 -8.728   -44.521 1.00 28.53 ? 144 VAL   L N   1 
ATOM   15164 C  CA  . VAL   L  1 144 ? -32.749 -9.504   -43.272 1.00 32.92 ? 144 VAL   L CA  1 
ATOM   15165 C  C   . VAL   L  1 144 ? -32.655 -8.615   -42.035 1.00 34.36 ? 144 VAL   L C   1 
ATOM   15166 O  O   . VAL   L  1 144 ? -32.845 -9.113   -40.907 1.00 34.37 ? 144 VAL   L O   1 
ATOM   15167 C  CB  . VAL   L  1 144 ? -31.616 -10.570  -43.262 1.00 28.17 ? 144 VAL   L CB  1 
ATOM   15168 C  CG1 . VAL   L  1 144 ? -31.675 -11.439  -44.508 1.00 34.14 ? 144 VAL   L CG1 1 
ATOM   15169 C  CG2 . VAL   L  1 144 ? -30.217 -9.954   -43.085 1.00 25.66 ? 144 VAL   L CG2 1 
ATOM   15170 N  N   . GLY   L  1 145 ? -32.422 -7.327   -42.205 1.00 29.39 ? 145 GLY   L N   1 
ATOM   15171 C  CA  . GLY   L  1 145 ? -32.209 -6.414   -41.094 1.00 27.36 ? 145 GLY   L CA  1 
ATOM   15172 C  C   . GLY   L  1 145 ? -30.756 -6.383   -40.691 1.00 33.64 ? 145 GLY   L C   1 
ATOM   15173 O  O   . GLY   L  1 145 ? -30.013 -7.350   -40.856 1.00 29.16 ? 145 GLY   L O   1 
ATOM   15174 N  N   . LEU   L  1 146 ? -30.335 -5.231   -40.172 1.00 29.76 ? 146 LEU   L N   1 
ATOM   15175 C  CA  . LEU   L  1 146 ? -28.922 -5.030   -39.900 1.00 36.06 ? 146 LEU   L CA  1 
ATOM   15176 C  C   . LEU   L  1 146 ? -28.405 -6.019   -38.854 1.00 37.60 ? 146 LEU   L C   1 
ATOM   15177 O  O   . LEU   L  1 146 ? -27.319 -6.594   -39.017 1.00 28.62 ? 146 LEU   L O   1 
ATOM   15178 C  CB  . LEU   L  1 146 ? -28.694 -3.594   -39.443 1.00 37.31 ? 146 LEU   L CB  1 
ATOM   15179 C  CG  . LEU   L  1 146 ? -27.244 -3.214   -39.196 1.00 33.04 ? 146 LEU   L CG  1 
ATOM   15180 C  CD1 . LEU   L  1 146 ? -26.454 -3.293   -40.439 1.00 29.52 ? 146 LEU   L CD1 1 
ATOM   15181 C  CD2 . LEU   L  1 146 ? -27.140 -1.816   -38.586 1.00 41.07 ? 146 LEU   L CD2 1 
ATOM   15182 N  N   . GLU   L  1 147 ? -29.157 -6.221   -37.765 1.00 26.48 ? 147 GLU   L N   1 
ATOM   15183 C  CA  . GLU   L  1 147 ? -28.676 -7.103   -36.703 1.00 30.79 ? 147 GLU   L CA  1 
ATOM   15184 C  C   . GLU   L  1 147 ? -28.453 -8.525   -37.214 1.00 29.36 ? 147 GLU   L C   1 
ATOM   15185 O  O   . GLU   L  1 147 ? -27.453 -9.165   -36.875 1.00 27.14 ? 147 GLU   L O   1 
ATOM   15186 C  CB  . GLU   L  1 147 ? -29.657 -7.107   -35.527 1.00 33.92 ? 147 GLU   L CB  1 
ATOM   15187 C  CG  . GLU   L  1 147 ? -29.566 -5.887   -34.607 1.00 37.70 ? 147 GLU   L CG  1 
ATOM   15188 C  CD  . GLU   L  1 147 ? -30.498 -5.992   -33.368 1.00 43.54 ? 147 GLU   L CD  1 
ATOM   15189 O  OE1 . GLU   L  1 147 ? -31.469 -6.763   -33.401 1.00 44.63 ? 147 GLU   L OE1 1 
ATOM   15190 O  OE2 . GLU   L  1 147 ? -30.251 -5.318   -32.352 1.00 51.38 ? 147 GLU   L OE2 1 
ATOM   15191 N  N   . ASN   L  1 148 ? -29.388 -9.046   -37.999 1.00 28.72 ? 148 ASN   L N   1 
ATOM   15192 C  CA  . ASN   L  1 148 ? -29.225 -10.372  -38.591 1.00 31.72 ? 148 ASN   L CA  1 
ATOM   15193 C  C   . ASN   L  1 148 ? -28.078 -10.395  -39.587 1.00 35.07 ? 148 ASN   L C   1 
ATOM   15194 O  O   . ASN   L  1 148 ? -27.335 -11.380  -39.644 1.00 31.01 ? 148 ASN   L O   1 
ATOM   15195 C  CB  . ASN   L  1 148 ? -30.504 -10.818  -39.286 1.00 29.90 ? 148 ASN   L CB  1 
ATOM   15196 C  CG  . ASN   L  1 148 ? -31.481 -11.550  -38.356 1.00 29.31 ? 148 ASN   L CG  1 
ATOM   15197 O  OD1 . ASN   L  1 148 ? -31.237 -11.732  -37.158 1.00 26.78 ? 148 ASN   L OD1 1 
ATOM   15198 N  ND2 . ASN   L  1 148 ? -32.598 -11.987  -38.930 1.00 29.42 ? 148 ASN   L ND2 1 
ATOM   15199 N  N   . TYR   L  1 149 ? -27.912 -9.313   -40.366 1.00 25.89 ? 149 TYR   L N   1 
ATOM   15200 C  CA  . TYR   L  1 149 ? -26.860 -9.274   -41.376 1.00 30.75 ? 149 TYR   L CA  1 
ATOM   15201 C  C   . TYR   L  1 149 ? -25.498 -9.350   -40.722 1.00 31.67 ? 149 TYR   L C   1 
ATOM   15202 O  O   . TYR   L  1 149 ? -24.629 -10.121  -41.141 1.00 29.10 ? 149 TYR   L O   1 
ATOM   15203 C  CB  . TYR   L  1 149 ? -26.961 -8.007   -42.228 1.00 31.45 ? 149 TYR   L CB  1 
ATOM   15204 C  CG  . TYR   L  1 149 ? -25.847 -7.966   -43.243 1.00 29.47 ? 149 TYR   L CG  1 
ATOM   15205 C  CD1 . TYR   L  1 149 ? -25.961 -8.652   -44.444 1.00 31.79 ? 149 TYR   L CD1 1 
ATOM   15206 C  CD2 . TYR   L  1 149 ? -24.668 -7.321   -42.972 1.00 27.74 ? 149 TYR   L CD2 1 
ATOM   15207 C  CE1 . TYR   L  1 149 ? -24.937 -8.660   -45.349 1.00 37.45 ? 149 TYR   L CE1 1 
ATOM   15208 C  CE2 . TYR   L  1 149 ? -23.629 -7.319   -43.888 1.00 32.66 ? 149 TYR   L CE2 1 
ATOM   15209 C  CZ  . TYR   L  1 149 ? -23.770 -7.997   -45.061 1.00 35.00 ? 149 TYR   L CZ  1 
ATOM   15210 O  OH  . TYR   L  1 149 ? -22.724 -8.011   -45.969 1.00 36.78 ? 149 TYR   L OH  1 
ATOM   15211 N  N   . LEU   L  1 150 ? -25.300 -8.543   -39.683 1.00 29.54 ? 150 LEU   L N   1 
ATOM   15212 C  CA  . LEU   L  1 150 ? -24.062 -8.568   -38.926 1.00 27.67 ? 150 LEU   L CA  1 
ATOM   15213 C  C   . LEU   L  1 150 ? -23.851 -9.923   -38.269 1.00 29.37 ? 150 LEU   L C   1 
ATOM   15214 O  O   . LEU   L  1 150 ? -22.745 -10.485  -38.312 1.00 30.33 ? 150 LEU   L O   1 
ATOM   15215 C  CB  . LEU   L  1 150 ? -24.096 -7.459   -37.887 1.00 26.79 ? 150 LEU   L CB  1 
ATOM   15216 C  CG  . LEU   L  1 150 ? -24.178 -6.047   -38.476 1.00 32.75 ? 150 LEU   L CG  1 
ATOM   15217 C  CD1 . LEU   L  1 150 ? -24.140 -5.011   -37.388 1.00 32.31 ? 150 LEU   L CD1 1 
ATOM   15218 C  CD2 . LEU   L  1 150 ? -23.058 -5.808   -39.452 1.00 31.36 ? 150 LEU   L CD2 1 
ATOM   15219 N  N   . GLN   L  1 151 ? -24.897 -10.448  -37.641 1.00 27.90 ? 151 GLN   L N   1 
ATOM   15220 C  CA  . GLN   L  1 151 ? -24.823 -11.769  -37.025 1.00 29.80 ? 151 GLN   L CA  1 
ATOM   15221 C  C   . GLN   L  1 151 ? -24.266 -12.807  -37.997 1.00 32.59 ? 151 GLN   L C   1 
ATOM   15222 O  O   . GLN   L  1 151 ? -23.389 -13.598  -37.640 1.00 28.69 ? 151 GLN   L O   1 
ATOM   15223 C  CB  . GLN   L  1 151 ? -26.212 -12.193  -36.551 1.00 24.39 ? 151 GLN   L CB  1 
ATOM   15224 C  CG  . GLN   L  1 151 ? -26.206 -13.520  -35.766 1.00 26.63 ? 151 GLN   L CG  1 
ATOM   15225 C  CD  . GLN   L  1 151 ? -27.594 -14.068  -35.512 1.00 29.58 ? 151 GLN   L CD  1 
ATOM   15226 O  OE1 . GLN   L  1 151 ? -28.558 -13.757  -36.233 1.00 27.49 ? 151 GLN   L OE1 1 
ATOM   15227 N  NE2 . GLN   L  1 151 ? -27.701 -14.902  -34.493 1.00 25.80 ? 151 GLN   L NE2 1 
ATOM   15228 N  N   . SER   L  1 152 ? -24.774 -12.813  -39.234 1.00 27.71 ? 152 SER   L N   1 
ATOM   15229 C  CA  . SER   L  1 152 ? -24.396 -13.794  -40.237 1.00 29.35 ? 152 SER   L CA  1 
ATOM   15230 C  C   . SER   L  1 152 ? -22.971 -13.630  -40.734 1.00 30.66 ? 152 SER   L C   1 
ATOM   15231 O  O   . SER   L  1 152 ? -22.521 -14.465  -41.521 1.00 32.06 ? 152 SER   L O   1 
ATOM   15232 C  CB  . SER   L  1 152 ? -25.322 -13.719  -41.447 1.00 29.98 ? 152 SER   L CB  1 
ATOM   15233 O  OG  . SER   L  1 152 ? -26.608 -14.204  -41.154 1.00 30.32 ? 152 SER   L OG  1 
ATOM   15234 N  N   . HIS   L  1 153 ? -22.275 -12.578  -40.324 1.00 28.31 ? 153 HIS   L N   1 
ATOM   15235 C  CA  . HIS   L  1 153 ? -20.913 -12.313  -40.759 1.00 31.03 ? 153 HIS   L CA  1 
ATOM   15236 C  C   . HIS   L  1 153 ? -19.947 -12.311  -39.573 1.00 31.01 ? 153 HIS   L C   1 
ATOM   15237 O  O   . HIS   L  1 153 ? -18.806 -11.865  -39.692 1.00 29.37 ? 153 HIS   L O   1 
ATOM   15238 C  CB  . HIS   L  1 153 ? -20.887 -11.009  -41.567 1.00 31.20 ? 153 HIS   L CB  1 
ATOM   15239 C  CG  . HIS   L  1 153 ? -21.508 -11.162  -42.925 1.00 28.59 ? 153 HIS   L CG  1 
ATOM   15240 N  ND1 . HIS   L  1 153 ? -22.847 -10.950  -43.165 1.00 33.52 ? 153 HIS   L ND1 1 
ATOM   15241 C  CD2 . HIS   L  1 153 ? -20.976 -11.566  -44.109 1.00 29.05 ? 153 HIS   L CD2 1 
ATOM   15242 C  CE1 . HIS   L  1 153 ? -23.117 -11.216  -44.433 1.00 37.51 ? 153 HIS   L CE1 1 
ATOM   15243 N  NE2 . HIS   L  1 153 ? -21.996 -11.592  -45.031 1.00 32.61 ? 153 HIS   L NE2 1 
ATOM   15244 N  N   . MET   L  1 154 ? -20.386 -12.849  -38.433 1.00 26.93 ? 154 MET   L N   1 
ATOM   15245 C  CA  . MET   L  1 154 ? -19.511 -12.978  -37.266 1.00 35.00 ? 154 MET   L CA  1 
ATOM   15246 C  C   . MET   L  1 154 ? -18.460 -14.065  -37.464 1.00 37.90 ? 154 MET   L C   1 
ATOM   15247 O  O   . MET   L  1 154 ? -17.270 -13.850  -37.213 1.00 33.68 ? 154 MET   L O   1 
ATOM   15248 C  CB  . MET   L  1 154 ? -20.344 -13.287  -36.023 1.00 33.08 ? 154 MET   L CB  1 
ATOM   15249 C  CG  . MET   L  1 154 ? -20.956 -12.082  -35.361 1.00 45.63 ? 154 MET   L CG  1 
ATOM   15250 S  SD  . MET   L  1 154 ? -22.154 -12.528  -34.072 1.00 44.34 ? 154 MET   L SD  1 
ATOM   15251 C  CE  . MET   L  1 154 ? -21.094 -13.514  -33.008 1.00 38.72 ? 154 MET   L CE  1 
ATOM   15252 N  N   . HIS   L  1 155 ? -18.883 -15.239  -37.910 1.00 43.92 ? 155 HIS   L N   1 
ATOM   15253 C  CA  . HIS   L  1 155 ? -18.032 -16.416  -37.955 1.00 43.89 ? 155 HIS   L CA  1 
ATOM   15254 C  C   . HIS   L  1 155 ? -17.701 -16.789  -39.398 1.00 37.62 ? 155 HIS   L C   1 
ATOM   15255 O  O   . HIS   L  1 155 ? -18.521 -16.632  -40.312 1.00 42.32 ? 155 HIS   L O   1 
ATOM   15256 C  CB  . HIS   L  1 155 ? -18.729 -17.586  -37.251 1.00 44.00 ? 155 HIS   L CB  1 
ATOM   15257 C  CG  . HIS   L  1 155 ? -19.126 -17.298  -35.832 1.00 58.28 ? 155 HIS   L CG  1 
ATOM   15258 N  ND1 . HIS   L  1 155 ? -20.288 -17.790  -35.268 1.00 57.88 ? 155 HIS   L ND1 1 
ATOM   15259 C  CD2 . HIS   L  1 155 ? -18.504 -16.591  -34.855 1.00 51.69 ? 155 HIS   L CD2 1 
ATOM   15260 C  CE1 . HIS   L  1 155 ? -20.365 -17.395  -34.009 1.00 50.85 ? 155 HIS   L CE1 1 
ATOM   15261 N  NE2 . HIS   L  1 155 ? -19.298 -16.664  -33.734 1.00 68.50 ? 155 HIS   L NE2 1 
ATOM   15262 N  N   . GLU   L  1 156 ? -16.490 -17.281  -39.608 1.00 47.69 ? 156 GLU   L N   1 
ATOM   15263 C  CA  . GLU   L  1 156 ? -16.150 -17.849  -40.912 1.00 48.94 ? 156 GLU   L CA  1 
ATOM   15264 C  C   . GLU   L  1 156 ? -16.658 -19.292  -40.978 1.00 55.95 ? 156 GLU   L C   1 
ATOM   15265 O  O   . GLU   L  1 156 ? -17.164 -19.733  -42.011 1.00 60.62 ? 156 GLU   L O   1 
ATOM   15266 C  CB  . GLU   L  1 156 ? -14.645 -17.798  -41.155 1.00 52.56 ? 156 GLU   L CB  1 
ATOM   15267 C  CG  . GLU   L  1 156 ? -14.024 -16.438  -40.857 1.00 56.17 ? 156 GLU   L CG  1 
ATOM   15268 C  CD  . GLU   L  1 156 ? -12.518 -16.382  -41.136 1.00 63.42 ? 156 GLU   L CD  1 
ATOM   15269 O  OE1 . GLU   L  1 156 ? -12.064 -17.026  -42.106 1.00 61.61 ? 156 GLU   L OE1 1 
ATOM   15270 O  OE2 . GLU   L  1 156 ? -11.786 -15.688  -40.392 1.00 63.23 ? 156 GLU   L OE2 1 
HETATM 15271 K  K   . K     M  2 .   ? 20.746  -49.029  -6.424  1.00 24.09 ? 201 K     A K   1 
HETATM 15272 C  CHA . HEM   N  3 .   ? 29.278  -29.512  -34.124 1.00 29.17 ? 202 HEM   A CHA 1 
HETATM 15273 C  CHB . HEM   N  3 .   ? 33.146  -30.844  -31.520 1.00 25.14 ? 202 HEM   A CHB 1 
HETATM 15274 C  CHC . HEM   N  3 .   ? 34.272  -26.189  -31.217 1.00 29.18 ? 202 HEM   A CHC 1 
HETATM 15275 C  CHD . HEM   N  3 .   ? 30.423  -24.828  -33.787 1.00 31.56 ? 202 HEM   A CHD 1 
HETATM 15276 C  C1A . HEM   N  3 .   ? 30.245  -30.238  -33.461 1.00 29.67 ? 202 HEM   A C1A 1 
HETATM 15277 C  C2A . HEM   N  3 .   ? 30.265  -31.683  -33.366 1.00 35.15 ? 202 HEM   A C2A 1 
HETATM 15278 C  C3A . HEM   N  3 .   ? 31.332  -32.060  -32.661 1.00 31.44 ? 202 HEM   A C3A 1 
HETATM 15279 C  C4A . HEM   N  3 .   ? 32.007  -30.869  -32.260 1.00 31.06 ? 202 HEM   A C4A 1 
HETATM 15280 C  CMA . HEM   N  3 .   ? 31.781  -33.482  -32.295 1.00 34.87 ? 202 HEM   A CMA 1 
HETATM 15281 C  CAA . HEM   N  3 .   ? 29.237  -32.603  -34.008 1.00 34.68 ? 202 HEM   A CAA 1 
HETATM 15282 C  CBA . HEM   N  3 .   ? 29.614  -32.767  -35.463 1.00 42.72 ? 202 HEM   A CBA 1 
HETATM 15283 C  CGA . HEM   N  3 .   ? 28.443  -33.384  -36.169 1.00 53.96 ? 202 HEM   A CGA 1 
HETATM 15284 O  O1A . HEM   N  3 .   ? 28.597  -34.546  -36.598 1.00 41.13 ? 202 HEM   A O1A 1 
HETATM 15285 O  O2A . HEM   N  3 .   ? 27.370  -32.726  -36.277 1.00 63.29 ? 202 HEM   A O2A 1 
HETATM 15286 C  C1B . HEM   N  3 .   ? 33.766  -29.690  -31.215 1.00 27.01 ? 202 HEM   A C1B 1 
HETATM 15287 C  C2B . HEM   N  3 .   ? 34.989  -29.612  -30.447 1.00 26.69 ? 202 HEM   A C2B 1 
HETATM 15288 C  C3B . HEM   N  3 .   ? 35.297  -28.304  -30.381 1.00 31.68 ? 202 HEM   A C3B 1 
HETATM 15289 C  C4B . HEM   N  3 .   ? 34.285  -27.543  -31.083 1.00 27.12 ? 202 HEM   A C4B 1 
HETATM 15290 C  CMB . HEM   N  3 .   ? 35.693  -30.878  -29.902 1.00 31.92 ? 202 HEM   A CMB 1 
HETATM 15291 C  CAB . HEM   N  3 .   ? 36.479  -27.660  -29.664 1.00 36.87 ? 202 HEM   A CAB 1 
HETATM 15292 C  CBB . HEM   N  3 .   ? 37.093  -28.398  -28.740 1.00 44.14 ? 202 HEM   A CBB 1 
HETATM 15293 C  C1C . HEM   N  3 .   ? 33.359  -25.429  -31.881 1.00 32.32 ? 202 HEM   A C1C 1 
HETATM 15294 C  C2C . HEM   N  3 .   ? 33.408  -23.987  -31.976 1.00 32.73 ? 202 HEM   A C2C 1 
HETATM 15295 C  C3C . HEM   N  3 .   ? 32.333  -23.596  -32.661 1.00 27.86 ? 202 HEM   A C3C 1 
HETATM 15296 C  C4C . HEM   N  3 .   ? 31.583  -24.786  -33.048 1.00 30.41 ? 202 HEM   A C4C 1 
HETATM 15297 C  CMC . HEM   N  3 .   ? 34.528  -23.112  -31.346 1.00 37.28 ? 202 HEM   A CMC 1 
HETATM 15298 C  CAC . HEM   N  3 .   ? 31.915  -22.168  -33.067 1.00 33.67 ? 202 HEM   A CAC 1 
HETATM 15299 C  CBC . HEM   N  3 .   ? 32.800  -21.172  -32.974 1.00 56.30 ? 202 HEM   A CBC 1 
HETATM 15300 C  C1D . HEM   N  3 .   ? 29.740  -25.980  -34.096 1.00 28.86 ? 202 HEM   A C1D 1 
HETATM 15301 C  C2D . HEM   N  3 .   ? 28.453  -26.083  -34.749 1.00 31.01 ? 202 HEM   A C2D 1 
HETATM 15302 C  C3D . HEM   N  3 .   ? 28.123  -27.373  -34.840 1.00 28.62 ? 202 HEM   A C3D 1 
HETATM 15303 C  C4D . HEM   N  3 .   ? 29.193  -28.141  -34.220 1.00 26.77 ? 202 HEM   A C4D 1 
HETATM 15304 C  CMD . HEM   N  3 .   ? 27.624  -24.878  -35.242 1.00 35.87 ? 202 HEM   A CMD 1 
HETATM 15305 C  CAD . HEM   N  3 .   ? 26.825  -27.941  -35.489 1.00 31.45 ? 202 HEM   A CAD 1 
HETATM 15306 C  CBD . HEM   N  3 .   ? 25.882  -28.356  -34.365 1.00 39.68 ? 202 HEM   A CBD 1 
HETATM 15307 C  CGD . HEM   N  3 .   ? 24.505  -28.728  -34.876 1.00 47.53 ? 202 HEM   A CGD 1 
HETATM 15308 O  O1D . HEM   N  3 .   ? 24.055  -29.872  -34.647 1.00 59.72 ? 202 HEM   A O1D 1 
HETATM 15309 O  O2D . HEM   N  3 .   ? 23.845  -27.872  -35.497 1.00 43.76 ? 202 HEM   A O2D 1 
HETATM 15310 N  NA  . HEM   N  3 .   ? 31.350  -29.769  -32.774 1.00 25.37 ? 202 HEM   A NA  1 
HETATM 15311 N  NB  . HEM   N  3 .   ? 33.358  -28.430  -31.570 1.00 26.68 ? 202 HEM   A NB  1 
HETATM 15312 N  NC  . HEM   N  3 .   ? 32.226  -25.894  -32.528 1.00 28.73 ? 202 HEM   A NC  1 
HETATM 15313 N  ND  . HEM   N  3 .   ? 30.153  -27.257  -33.791 1.00 28.87 ? 202 HEM   A ND  1 
HETATM 15314 FE FE  . HEM   N  3 .   ? 31.783  -27.856  -32.593 1.00 30.30 ? 202 HEM   A FE  1 
HETATM 15315 K  K   . K     O  2 .   ? -31.425 -14.306  -36.012 1.00 24.20 ? 201 K     B K   1 
HETATM 15316 O  O1  . PG4   P  4 .   ? -21.379 -30.223  -23.709 1.00 52.89 ? 202 PG4   B O1  1 
HETATM 15317 C  C1  . PG4   P  4 .   ? -20.786 -29.595  -22.584 1.00 53.63 ? 202 PG4   B C1  1 
HETATM 15318 C  C2  . PG4   P  4 .   ? -21.388 -30.103  -21.312 1.00 53.94 ? 202 PG4   B C2  1 
HETATM 15319 O  O2  . PG4   P  4 .   ? -22.738 -29.656  -21.232 1.00 51.31 ? 202 PG4   B O2  1 
HETATM 15320 C  C3  . PG4   P  4 .   ? -23.382 -30.066  -20.030 1.00 50.89 ? 202 PG4   B C3  1 
HETATM 15321 C  C4  . PG4   P  4 .   ? -24.713 -29.401  -19.882 1.00 46.80 ? 202 PG4   B C4  1 
HETATM 15322 O  O3  . PG4   P  4 .   ? -25.503 -29.565  -21.058 1.00 46.47 ? 202 PG4   B O3  1 
HETATM 15323 C  C5  . PG4   P  4 .   ? -26.718 -28.825  -20.899 1.00 38.60 ? 202 PG4   B C5  1 
HETATM 15324 C  C6  . PG4   P  4 .   ? -27.727 -29.353  -21.871 1.00 41.94 ? 202 PG4   B C6  1 
HETATM 15325 O  O4  . PG4   P  4 .   ? -27.360 -28.906  -23.174 1.00 50.80 ? 202 PG4   B O4  1 
HETATM 15326 C  C7  . PG4   P  4 .   ? -28.096 -29.609  -24.159 1.00 49.70 ? 202 PG4   B C7  1 
HETATM 15327 C  C8  . PG4   P  4 .   ? -27.873 -28.921  -25.475 1.00 59.59 ? 202 PG4   B C8  1 
HETATM 15328 O  O5  . PG4   P  4 .   ? -28.565 -27.669  -25.515 1.00 48.22 ? 202 PG4   B O5  1 
HETATM 15329 C  C13 . A1BYB Q  5 .   ? 10.201  -25.764  2.758   1.00 65.02 ? 203 A1BYB B C13 1 
HETATM 15330 C  C17 . A1BYB Q  5 .   ? 2.811   -24.889  3.036   1.00 54.63 ? 203 A1BYB B C17 1 
HETATM 15331 C  C02 . A1BYB Q  5 .   ? 1.669   -23.095  -0.703  1.00 31.41 ? 203 A1BYB B C02 1 
HETATM 15332 C  C04 . A1BYB Q  5 .   ? 3.967   -23.654  -0.465  1.00 46.84 ? 203 A1BYB B C04 1 
HETATM 15333 C  C05 . A1BYB Q  5 .   ? 3.268   -24.045  0.818   1.00 48.59 ? 203 A1BYB B C05 1 
HETATM 15334 C  C06 . A1BYB Q  5 .   ? 3.767   -24.636  1.974   1.00 58.87 ? 203 A1BYB B C06 1 
HETATM 15335 C  C08 . A1BYB Q  5 .   ? 5.800   -25.752  3.192   1.00 60.94 ? 203 A1BYB B C08 1 
HETATM 15336 C  C09 . A1BYB Q  5 .   ? 7.326   -25.762  3.051   1.00 80.35 ? 203 A1BYB B C09 1 
HETATM 15337 C  C10 . A1BYB Q  5 .   ? 7.967   -26.631  2.171   1.00 62.99 ? 203 A1BYB B C10 1 
HETATM 15338 C  C11 . A1BYB Q  5 .   ? 9.361   -26.642  2.032   1.00 81.87 ? 203 A1BYB B C11 1 
HETATM 15339 C  C14 . A1BYB Q  5 .   ? 9.590   -24.862  3.643   1.00 63.84 ? 203 A1BYB B C14 1 
HETATM 15340 C  C15 . A1BYB Q  5 .   ? 8.183   -24.880  3.764   1.00 82.29 ? 203 A1BYB B C15 1 
HETATM 15341 C  C18 . A1BYB Q  5 .   ? 1.453   -24.558  2.894   1.00 50.97 ? 203 A1BYB B C18 1 
HETATM 15342 C  C19 . A1BYB Q  5 .   ? 0.962   -23.948  1.681   1.00 47.37 ? 203 A1BYB B C19 1 
HETATM 15343 C  C20 . A1BYB Q  5 .   ? 1.887   -23.707  0.675   1.00 51.01 ? 203 A1BYB B C20 1 
HETATM 15344 N  N03 . A1BYB Q  5 .   ? 2.948   -23.099  -1.298  1.00 49.56 ? 203 A1BYB B N03 1 
HETATM 15345 N  N07 . A1BYB Q  5 .   ? 5.155   -24.984  2.136   1.00 61.37 ? 203 A1BYB B N07 1 
HETATM 15346 O  O01 . A1BYB Q  5 .   ? 0.728   -22.659  -1.291  1.00 38.10 ? 203 A1BYB B O01 1 
HETATM 15347 O  O16 . A1BYB Q  5 .   ? 7.559   -23.991  4.641   1.00 75.17 ? 203 A1BYB B O16 1 
HETATM 15348 O  O21 . A1BYB Q  5 .   ? 5.105   -23.720  -0.828  1.00 44.19 ? 203 A1BYB B O21 1 
HETATM 15349 CL CL1 . A1BYB Q  5 .   ? 10.062  -27.792  0.909   1.00 85.16 ? 203 A1BYB B CL1 1 
HETATM 15350 C  C13 . A1BYB R  5 .   ? -47.315 -67.885  -20.999 1.00 86.99 ? 201 A1BYB C C13 1 
HETATM 15351 C  C17 . A1BYB R  5 .   ? -50.766 -62.119  -24.023 1.00 62.47 ? 201 A1BYB C C17 1 
HETATM 15352 C  C02 . A1BYB R  5 .   ? -48.262 -58.726  -23.399 1.00 41.37 ? 201 A1BYB C C02 1 
HETATM 15353 C  C04 . A1BYB R  5 .   ? -47.444 -60.808  -22.565 1.00 58.88 ? 201 A1BYB C C04 1 
HETATM 15354 C  C05 . A1BYB R  5 .   ? -48.788 -61.051  -23.208 1.00 61.12 ? 201 A1BYB C C05 1 
HETATM 15355 C  C06 . A1BYB R  5 .   ? -49.505 -62.215  -23.357 1.00 63.30 ? 201 A1BYB C C06 1 
HETATM 15356 C  C08 . A1BYB R  5 .   ? -49.452 -64.778  -23.268 1.00 61.53 ? 201 A1BYB C C08 1 
HETATM 15357 C  C09 . A1BYB R  5 .   ? -48.723 -65.862  -22.480 1.00 84.74 ? 201 A1BYB C C09 1 
HETATM 15358 C  C10 . A1BYB R  5 .   ? -47.623 -66.522  -23.015 1.00 68.79 ? 201 A1BYB C C10 1 
HETATM 15359 C  C11 . A1BYB R  5 .   ? -46.942 -67.511  -22.302 1.00 79.09 ? 201 A1BYB C C11 1 
HETATM 15360 C  C14 . A1BYB R  5 .   ? -48.408 -67.229  -20.416 1.00 69.81 ? 201 A1BYB C C14 1 
HETATM 15361 C  C15 . A1BYB R  5 .   ? -49.078 -66.242  -21.155 1.00 87.92 ? 201 A1BYB C C15 1 
HETATM 15362 C  C18 . A1BYB R  5 .   ? -51.243 -60.900  -24.504 1.00 60.32 ? 201 A1BYB C C18 1 
HETATM 15363 C  C19 . A1BYB R  5 .   ? -50.478 -59.700  -24.343 1.00 56.25 ? 201 A1BYB C C19 1 
HETATM 15364 C  C20 . A1BYB R  5 .   ? -49.270 -59.814  -23.692 1.00 52.44 ? 201 A1BYB C C20 1 
HETATM 15365 N  N03 . A1BYB R  5 .   ? -47.211 -59.395  -22.725 1.00 53.77 ? 201 A1BYB C N03 1 
HETATM 15366 N  N07 . A1BYB R  5 .   ? -49.049 -63.453  -22.879 1.00 52.27 ? 201 A1BYB C N07 1 
HETATM 15367 O  O01 . A1BYB R  5 .   ? -48.229 -57.551  -23.616 1.00 36.63 ? 201 A1BYB C O01 1 
HETATM 15368 O  O16 . A1BYB R  5 .   ? -50.169 -65.584  -20.576 1.00 68.04 ? 201 A1BYB C O16 1 
HETATM 15369 O  O21 . A1BYB R  5 .   ? -46.658 -61.531  -22.025 1.00 53.23 ? 201 A1BYB C O21 1 
HETATM 15370 CL CL1 . A1BYB R  5 .   ? -45.584 -68.302  -23.066 1.00 75.46 ? 201 A1BYB C CL1 1 
HETATM 15371 K  K   . K     S  2 .   ? -31.369 -83.718  -35.973 1.00 30.66 ? 201 K     D K   1 
HETATM 15372 C  CHA . HEM   T  3 .   ? -0.010  -87.874  -50.764 0.50 36.08 ? 202 HEM   D CHA 1 
HETATM 15373 C  CHB . HEM   T  3 .   ? -3.197  -91.244  -52.130 0.50 37.39 ? 202 HEM   D CHB 1 
HETATM 15374 C  CHC . HEM   T  3 .   ? 0.022   -94.585  -50.747 0.50 38.84 ? 202 HEM   D CHC 1 
HETATM 15375 C  CHD . HEM   T  3 .   ? 3.225   -91.224  -49.394 0.50 37.39 ? 202 HEM   D CHD 1 
HETATM 15376 C  C1A . HEM   T  3 .   ? -1.123  -88.484  -51.294 0.50 38.85 ? 202 HEM   D C1A 1 
HETATM 15377 C  C2A . HEM   T  3 .   ? -2.238  -87.810  -51.933 0.50 38.59 ? 202 HEM   D C2A 1 
HETATM 15378 C  C3A . HEM   T  3 .   ? -3.117  -88.733  -52.317 0.50 39.71 ? 202 HEM   D C3A 1 
HETATM 15379 C  C4A . HEM   T  3 .   ? -2.600  -90.027  -51.922 0.50 38.79 ? 202 HEM   D C4A 1 
HETATM 15380 C  CMA . HEM   T  3 .   ? -4.449  -88.467  -53.053 0.50 39.69 ? 202 HEM   D CMA 1 
HETATM 15381 C  CAA . HEM   T  3 .   ? -2.387  -86.285  -52.160 0.50 40.93 ? 202 HEM   D CAA 1 
HETATM 15382 C  CBA . HEM   T  3 .   ? -1.717  -85.926  -53.477 0.50 41.75 ? 202 HEM   D CBA 1 
HETATM 15383 C  CGA . HEM   T  3 .   ? -1.931  -84.465  -53.764 0.50 43.27 ? 202 HEM   D CGA 1 
HETATM 15384 O  O1A . HEM   T  3 .   ? -3.115  -84.053  -53.870 0.50 44.91 ? 202 HEM   D O1A 1 
HETATM 15385 O  O2A . HEM   T  3 .   ? -0.914  -83.729  -53.895 0.50 40.51 ? 202 HEM   D O2A 1 
HETATM 15386 C  C1B . HEM   T  3 .   ? -2.590  -92.447  -51.886 0.50 37.69 ? 202 HEM   D C1B 1 
HETATM 15387 C  C2B . HEM   T  3 .   ? -3.149  -93.746  -52.170 0.50 38.00 ? 202 HEM   D C2B 1 
HETATM 15388 C  C3B . HEM   T  3 .   ? -2.252  -94.670  -51.794 0.50 38.88 ? 202 HEM   D C3B 1 
HETATM 15389 C  C4B . HEM   T  3 .   ? -1.109  -93.979  -51.243 0.50 38.31 ? 202 HEM   D C4B 1 
HETATM 15390 C  CMB . HEM   T  3 .   ? -4.533  -93.954  -52.807 0.50 40.20 ? 202 HEM   D CMB 1 
HETATM 15391 C  CAB . HEM   T  3 .   ? -2.379  -96.212  -51.869 0.50 44.30 ? 202 HEM   D CAB 1 
HETATM 15392 C  CBB . HEM   T  3 .   ? -3.572  -96.809  -51.968 0.50 38.36 ? 202 HEM   D CBB 1 
HETATM 15393 C  C1C . HEM   T  3 .   ? 1.144   -93.979  -50.234 0.50 38.30 ? 202 HEM   D C1C 1 
HETATM 15394 C  C2C . HEM   T  3 .   ? 2.257   -94.662  -49.614 0.50 38.90 ? 202 HEM   D C2C 1 
HETATM 15395 C  C3C . HEM   T  3 .   ? 3.150   -93.735  -49.226 0.50 37.91 ? 202 HEM   D C3C 1 
HETATM 15396 C  C4C . HEM   T  3 .   ? 2.621   -92.439  -49.600 0.50 37.69 ? 202 HEM   D C4C 1 
HETATM 15397 C  CMC . HEM   T  3 .   ? 2.349   -96.198  -49.448 0.50 44.33 ? 202 HEM   D CMC 1 
HETATM 15398 C  CAC . HEM   T  3 .   ? 4.516   -93.928  -48.532 0.50 40.29 ? 202 HEM   D CAC 1 
HETATM 15399 C  CBC . HEM   T  3 .   ? 5.088   -95.132  -48.389 0.50 43.67 ? 202 HEM   D CBC 1 
HETATM 15400 C  C1D . HEM   T  3 .   ? 2.615   -90.012  -49.623 0.50 38.79 ? 202 HEM   D C1D 1 
HETATM 15401 C  C2D . HEM   T  3 .   ? 3.141   -88.703  -49.290 0.50 39.71 ? 202 HEM   D C2D 1 
HETATM 15402 C  C3D . HEM   T  3 .   ? 2.246   -87.790  -49.672 0.50 38.57 ? 202 HEM   D C3D 1 
HETATM 15403 C  C4D . HEM   T  3 .   ? 1.115   -88.483  -50.254 0.50 38.86 ? 202 HEM   D C4D 1 
HETATM 15404 C  CMD . HEM   T  3 .   ? 4.498   -88.421  -48.606 0.50 39.76 ? 202 HEM   D CMD 1 
HETATM 15405 C  CAD . HEM   T  3 .   ? 2.376   -86.253  -49.520 0.50 40.88 ? 202 HEM   D CAD 1 
HETATM 15406 C  CBD . HEM   T  3 .   ? 1.831   -85.816  -48.170 0.50 41.66 ? 202 HEM   D CBD 1 
HETATM 15407 C  CGD . HEM   T  3 .   ? 1.786   -84.311  -48.109 0.50 43.02 ? 202 HEM   D CGD 1 
HETATM 15408 O  O1D . HEM   T  3 .   ? 1.212   -83.669  -49.028 0.50 39.43 ? 202 HEM   D O1D 1 
HETATM 15409 O  O2D . HEM   T  3 .   ? 2.319   -83.759  -47.116 0.50 43.81 ? 202 HEM   D O2D 1 
HETATM 15410 N  NA  . HEM   T  3 .   ? -1.379  -89.841  -51.299 0.50 35.89 ? 202 HEM   D NA  1 
HETATM 15411 N  NB  . HEM   T  3 .   ? -1.347  -92.620  -51.321 0.50 37.03 ? 202 HEM   D NB  1 
HETATM 15412 N  NC  . HEM   T  3 .   ? 1.399   -92.622  -50.207 0.50 37.01 ? 202 HEM   D NC  1 
HETATM 15413 N  ND  . HEM   T  3 .   ? 1.374   -89.840  -50.212 0.50 35.89 ? 202 HEM   D ND  1 
HETATM 15414 FE FE  . HEM   T  3 .   ? 0.016   -91.252  -50.752 0.50 38.34 ? 202 HEM   D FE  1 
HETATM 15415 O  O1  . PG4   U  4 .   ? -15.812 -83.465  -51.201 1.00 87.98 ? 203 PG4   D O1  1 
HETATM 15416 C  C1  . PG4   U  4 .   ? -16.357 -84.177  -52.300 1.00 63.02 ? 203 PG4   D C1  1 
HETATM 15417 C  C2  . PG4   U  4 .   ? -15.542 -85.389  -52.612 1.00 64.14 ? 203 PG4   D C2  1 
HETATM 15418 O  O2  . PG4   U  4 .   ? -16.410 -86.473  -52.930 1.00 69.71 ? 203 PG4   D O2  1 
HETATM 15419 C  C3  . PG4   U  4 .   ? -16.274 -86.921  -54.272 1.00 58.16 ? 203 PG4   D C3  1 
HETATM 15420 C  C4  . PG4   U  4 .   ? -17.024 -88.195  -54.468 1.00 46.25 ? 203 PG4   D C4  1 
HETATM 15421 O  O3  . PG4   U  4 .   ? -18.386 -87.905  -54.814 1.00 60.41 ? 203 PG4   D O3  1 
HETATM 15422 C  C5  . PG4   U  4 .   ? -19.226 -88.568  -53.889 1.00 51.09 ? 203 PG4   D C5  1 
HETATM 15423 C  C6  . PG4   U  4 .   ? -20.677 -88.447  -54.247 1.00 49.68 ? 203 PG4   D C6  1 
HETATM 15424 O  O4  . PG4   U  4 .   ? -21.031 -87.066  -54.324 1.00 59.20 ? 203 PG4   D O4  1 
HETATM 15425 C  C7  . PG4   U  4 .   ? -22.309 -86.892  -53.751 1.00 50.66 ? 203 PG4   D C7  1 
HETATM 15426 C  C8  . PG4   U  4 .   ? -22.609 -85.440  -53.538 1.00 53.01 ? 203 PG4   D C8  1 
HETATM 15427 O  O5  . PG4   U  4 .   ? -23.085 -85.253  -52.201 1.00 60.69 ? 203 PG4   D O5  1 
HETATM 15428 C  CHA . HEM   V  3 .   ? -5.905  -29.425  -17.606 1.00 28.80 ? 201 HEM   E CHA 1 
HETATM 15429 C  CHB . HEM   V  3 .   ? -9.734  -28.453  -14.817 1.00 20.63 ? 201 HEM   E CHB 1 
HETATM 15430 C  CHC . HEM   V  3 .   ? -6.963  -26.025  -11.690 1.00 27.54 ? 201 HEM   E CHC 1 
HETATM 15431 C  CHD . HEM   V  3 .   ? -3.111  -27.007  -14.466 1.00 23.41 ? 201 HEM   E CHD 1 
HETATM 15432 C  C1A . HEM   V  3 .   ? -7.191  -29.428  -17.116 1.00 24.27 ? 201 HEM   E C1A 1 
HETATM 15433 C  C2A . HEM   V  3 .   ? -8.346  -30.105  -17.689 1.00 28.10 ? 201 HEM   E C2A 1 
HETATM 15434 C  C3A . HEM   V  3 .   ? -9.400  -29.831  -16.909 1.00 28.66 ? 201 HEM   E C3A 1 
HETATM 15435 C  C4A . HEM   V  3 .   ? -8.958  -28.964  -15.836 1.00 22.36 ? 201 HEM   E C4A 1 
HETATM 15436 C  CMA . HEM   V  3 .   ? -10.823 -30.367  -17.087 1.00 28.23 ? 201 HEM   E CMA 1 
HETATM 15437 C  CAA . HEM   V  3 .   ? -8.337  -31.008  -18.939 1.00 34.10 ? 201 HEM   E CAA 1 
HETATM 15438 C  CBA . HEM   V  3 .   ? -7.829  -32.384  -18.516 1.00 33.78 ? 201 HEM   E CBA 1 
HETATM 15439 C  CGA . HEM   V  3 .   ? -7.840  -33.331  -19.699 1.00 46.02 ? 201 HEM   E CGA 1 
HETATM 15440 O  O1A . HEM   V  3 .   ? -8.878  -33.407  -20.402 1.00 51.39 ? 201 HEM   E O1A 1 
HETATM 15441 O  O2A . HEM   V  3 .   ? -6.827  -34.042  -19.922 1.00 51.55 ? 201 HEM   E O2A 1 
HETATM 15442 C  C1B . HEM   V  3 .   ? -9.319  -27.718  -13.739 1.00 24.73 ? 201 HEM   E C1B 1 
HETATM 15443 C  C2B . HEM   V  3 .   ? -10.178 -27.230  -12.646 1.00 25.58 ? 201 HEM   E C2B 1 
HETATM 15444 C  C3B . HEM   V  3 .   ? -9.388  -26.575  -11.779 1.00 20.98 ? 201 HEM   E C3B 1 
HETATM 15445 C  C4B . HEM   V  3 .   ? -8.028  -26.605  -12.296 1.00 24.28 ? 201 HEM   E C4B 1 
HETATM 15446 C  CMB . HEM   V  3 .   ? -11.707 -27.499  -12.529 1.00 32.31 ? 201 HEM   E CMB 1 
HETATM 15447 C  CAB . HEM   V  3 .   ? -9.812  -25.861  -10.499 1.00 28.78 ? 201 HEM   E CAB 1 
HETATM 15448 C  CBB . HEM   V  3 .   ? -11.090 -25.469  -10.424 1.00 42.10 ? 201 HEM   E CBB 1 
HETATM 15449 C  C1C . HEM   V  3 .   ? -5.681  -26.080  -12.158 1.00 26.63 ? 201 HEM   E C1C 1 
HETATM 15450 C  C2C . HEM   V  3 .   ? -4.529  -25.475  -11.531 1.00 25.79 ? 201 HEM   E C2C 1 
HETATM 15451 C  C3C . HEM   V  3 .   ? -3.493  -25.745  -12.322 1.00 28.79 ? 201 HEM   E C3C 1 
HETATM 15452 C  C4C . HEM   V  3 .   ? -3.928  -26.540  -13.444 1.00 28.06 ? 201 HEM   E C4C 1 
HETATM 15453 C  CMC . HEM   V  3 .   ? -4.527  -24.655  -10.213 1.00 31.36 ? 201 HEM   E CMC 1 
HETATM 15454 C  CAC . HEM   V  3 .   ? -2.028  -25.344  -12.118 1.00 30.56 ? 201 HEM   E CAC 1 
HETATM 15455 C  CBC . HEM   V  3 .   ? -1.619  -24.882  -10.932 1.00 46.88 ? 201 HEM   E CBC 1 
HETATM 15456 C  C1D . HEM   V  3 .   ? -3.510  -27.710  -15.575 1.00 24.91 ? 201 HEM   E C1D 1 
HETATM 15457 C  C2D . HEM   V  3 .   ? -2.691  -28.088  -16.714 1.00 25.94 ? 201 HEM   E C2D 1 
HETATM 15458 C  C3D . HEM   V  3 .   ? -3.472  -28.738  -17.582 1.00 27.10 ? 201 HEM   E C3D 1 
HETATM 15459 C  C4D . HEM   V  3 .   ? -4.811  -28.819  -17.020 1.00 26.00 ? 201 HEM   E C4D 1 
HETATM 15460 C  CMD . HEM   V  3 .   ? -1.202  -27.761  -16.917 1.00 28.26 ? 201 HEM   E CMD 1 
HETATM 15461 C  CAD . HEM   V  3 .   ? -3.056  -29.357  -18.938 1.00 26.69 ? 201 HEM   E CAD 1 
HETATM 15462 C  CBD . HEM   V  3 .   ? -3.275  -28.352  -20.055 1.00 32.42 ? 201 HEM   E CBD 1 
HETATM 15463 C  CGD . HEM   V  3 .   ? -2.763  -28.872  -21.383 1.00 36.52 ? 201 HEM   E CGD 1 
HETATM 15464 O  O1D . HEM   V  3 .   ? -3.488  -29.632  -22.068 1.00 40.80 ? 201 HEM   E O1D 1 
HETATM 15465 O  O2D . HEM   V  3 .   ? -1.627  -28.512  -21.766 1.00 45.37 ? 201 HEM   E O2D 1 
HETATM 15466 N  NA  . HEM   V  3 .   ? -7.598  -28.733  -16.013 1.00 23.77 ? 201 HEM   E NA  1 
HETATM 15467 N  NB  . HEM   V  3 .   ? -8.032  -27.316  -13.484 1.00 23.55 ? 201 HEM   E NB  1 
HETATM 15468 N  NC  . HEM   V  3 .   ? -5.279  -26.735  -13.306 1.00 28.29 ? 201 HEM   E NC  1 
HETATM 15469 N  ND  . HEM   V  3 .   ? -4.787  -28.173  -15.820 1.00 24.59 ? 201 HEM   E ND  1 
HETATM 15470 FE FE  . HEM   V  3 .   ? -6.420  -27.726  -14.625 1.00 26.63 ? 201 HEM   E FE  1 
HETATM 15471 O  O1  . PG4   W  4 .   ? 10.823  -31.679  -16.792 1.00 65.36 ? 202 PG4   E O1  1 
HETATM 15472 C  C1  . PG4   W  4 .   ? 9.775   -30.972  -16.137 1.00 76.33 ? 202 PG4   E C1  1 
HETATM 15473 C  C2  . PG4   W  4 .   ? 10.181  -29.568  -15.818 1.00 58.12 ? 202 PG4   E C2  1 
HETATM 15474 O  O2  . PG4   W  4 .   ? 11.132  -29.583  -14.771 1.00 45.90 ? 202 PG4   E O2  1 
HETATM 15475 C  C3  . PG4   W  4 .   ? 11.671  -28.302  -14.485 1.00 55.97 ? 202 PG4   E C3  1 
HETATM 15476 C  C4  . PG4   W  4 .   ? 12.799  -28.467  -13.522 1.00 48.93 ? 202 PG4   E C4  1 
HETATM 15477 O  O3  . PG4   W  4 .   ? 13.776  -29.350  -14.060 1.00 53.31 ? 202 PG4   E O3  1 
HETATM 15478 C  C5  . PG4   W  4 .   ? 14.808  -29.521  -13.080 1.00 41.45 ? 202 PG4   E C5  1 
HETATM 15479 C  C6  . PG4   W  4 .   ? 16.093  -29.739  -13.808 1.00 45.88 ? 202 PG4   E C6  1 
HETATM 15480 O  O4  . PG4   W  4 .   ? 15.924  -30.732  -14.821 1.00 54.06 ? 202 PG4   E O4  1 
HETATM 15481 C  C7  . PG4   W  4 .   ? 16.967  -31.709  -14.821 1.00 54.09 ? 202 PG4   E C7  1 
HETATM 15482 C  C8  . PG4   W  4 .   ? 16.472  -32.963  -14.155 1.00 56.18 ? 202 PG4   E C8  1 
HETATM 15483 O  O5  . PG4   W  4 .   ? 17.507  -33.897  -13.853 1.00 41.77 ? 202 PG4   E O5  1 
HETATM 15484 C  C13 . A1BYB X  5 .   ? -27.123 -16.662  -9.422  1.00 79.83 ? 203 A1BYB E C13 1 
HETATM 15485 C  C17 . A1BYB X  5 .   ? -20.309 -15.479  -6.777  1.00 51.07 ? 203 A1BYB E C17 1 
HETATM 15486 C  C02 . A1BYB X  5 .   ? -18.490 -19.377  -6.472  1.00 38.89 ? 203 A1BYB E C02 1 
HETATM 15487 C  C04 . A1BYB X  5 .   ? -20.695 -19.275  -7.444  1.00 57.26 ? 203 A1BYB E C04 1 
HETATM 15488 C  C05 . A1BYB X  5 .   ? -20.282 -17.867  -7.071  1.00 56.00 ? 203 A1BYB E C05 1 
HETATM 15489 C  C06 . A1BYB X  5 .   ? -20.970 -16.667  -7.227  1.00 59.47 ? 203 A1BYB E C06 1 
HETATM 15490 C  C08 . A1BYB X  5 .   ? -23.042 -15.458  -8.262  1.00 58.00 ? 203 A1BYB E C08 1 
HETATM 15491 C  C09 . A1BYB X  5 .   ? -24.448 -15.860  -8.680  1.00 71.51 ? 203 A1BYB E C09 1 
HETATM 15492 C  C10 . A1BYB X  5 .   ? -24.745 -16.310  -9.969  1.00 67.66 ? 203 A1BYB E C10 1 
HETATM 15493 C  C11 . A1BYB X  5 .   ? -26.051 -16.696  -10.336 1.00 82.07 ? 203 A1BYB E C11 1 
HETATM 15494 C  C14 . A1BYB X  5 .   ? -26.848 -16.229  -8.112  1.00 82.65 ? 203 A1BYB E C14 1 
HETATM 15495 C  C15 . A1BYB X  5 .   ? -25.530 -15.852  -7.780  1.00 81.37 ? 203 A1BYB E C15 1 
HETATM 15496 C  C18 . A1BYB X  5 .   ? -19.026 -15.530  -6.216  1.00 56.89 ? 203 A1BYB E C18 1 
HETATM 15497 C  C19 . A1BYB X  5 .   ? -18.320 -16.789  -6.065  1.00 47.81 ? 203 A1BYB E C19 1 
HETATM 15498 C  C20 . A1BYB X  5 .   ? -18.972 -17.926  -6.500  1.00 43.50 ? 203 A1BYB E C20 1 
HETATM 15499 N  N03 . A1BYB X  5 .   ? -19.573 -20.120  -7.041  1.00 47.23 ? 203 A1BYB E N03 1 
HETATM 15500 N  N07 . A1BYB X  5 .   ? -22.281 -16.602  -7.794  1.00 66.69 ? 203 A1BYB E N07 1 
HETATM 15501 O  O01 . A1BYB X  5 .   ? -17.484 -19.913  -6.114  1.00 36.49 ? 203 A1BYB E O01 1 
HETATM 15502 O  O16 . A1BYB X  5 .   ? -25.234 -15.423  -6.488  1.00 73.07 ? 203 A1BYB E O16 1 
HETATM 15503 O  O21 . A1BYB X  5 .   ? -21.690 -19.716  -7.941  1.00 46.95 ? 203 A1BYB E O21 1 
HETATM 15504 CL CL1 . A1BYB X  5 .   ? -26.344 -17.230  -11.981 1.00 76.84 ? 203 A1BYB E CL1 1 
HETATM 15505 C  CHA . HEM   Y  3 .   ? -5.852  -68.592  -17.459 1.00 32.57 ? 201 HEM   F CHA 1 
HETATM 15506 C  CHB . HEM   Y  3 .   ? -6.335  -73.270  -16.324 1.00 31.18 ? 201 HEM   F CHB 1 
HETATM 15507 C  CHC . HEM   Y  3 .   ? -6.861  -72.017  -11.655 1.00 30.08 ? 201 HEM   F CHC 1 
HETATM 15508 C  CHD . HEM   Y  3 .   ? -6.414  -67.341  -12.838 1.00 30.46 ? 201 HEM   F CHD 1 
HETATM 15509 C  C1A . HEM   Y  3 .   ? -5.910  -69.970  -17.540 1.00 35.81 ? 201 HEM   F C1A 1 
HETATM 15510 C  C2A . HEM   Y  3 .   ? -5.759  -70.739  -18.756 1.00 32.73 ? 201 HEM   F C2A 1 
HETATM 15511 C  C3A . HEM   Y  3 .   ? -5.878  -72.035  -18.443 1.00 34.36 ? 201 HEM   F C3A 1 
HETATM 15512 C  C4A . HEM   Y  3 .   ? -6.152  -72.121  -17.031 1.00 29.71 ? 201 HEM   F C4A 1 
HETATM 15513 C  CMA . HEM   Y  3 .   ? -5.800  -73.249  -19.398 1.00 34.20 ? 201 HEM   F CMA 1 
HETATM 15514 C  CAA . HEM   Y  3 .   ? -5.462  -70.135  -20.153 1.00 32.12 ? 201 HEM   F CAA 1 
HETATM 15515 C  CBA . HEM   Y  3 .   ? -3.979  -69.772  -20.118 1.00 31.39 ? 201 HEM   F CBA 1 
HETATM 15516 C  CGA . HEM   Y  3 .   ? -3.538  -69.444  -21.528 1.00 47.98 ? 201 HEM   F CGA 1 
HETATM 15517 O  O1A . HEM   Y  3 .   ? -3.388  -70.373  -22.363 1.00 55.14 ? 201 HEM   F O1A 1 
HETATM 15518 O  O2A . HEM   Y  3 .   ? -3.325  -68.246  -21.811 1.00 45.62 ? 201 HEM   F O2A 1 
HETATM 15519 C  C1B . HEM   Y  3 .   ? -6.524  -73.339  -14.969 1.00 30.82 ? 201 HEM   F C1B 1 
HETATM 15520 C  C2B . HEM   Y  3 .   ? -6.784  -74.541  -14.202 1.00 34.12 ? 201 HEM   F C2B 1 
HETATM 15521 C  C3B . HEM   Y  3 .   ? -6.908  -74.178  -12.915 1.00 34.66 ? 201 HEM   F C3B 1 
HETATM 15522 C  C4B . HEM   Y  3 .   ? -6.759  -72.745  -12.824 1.00 32.17 ? 201 HEM   F C4B 1 
HETATM 15523 C  CMB . HEM   Y  3 .   ? -6.834  -75.961  -14.796 1.00 32.15 ? 201 HEM   F CMB 1 
HETATM 15524 C  CAB . HEM   Y  3 .   ? -7.220  -75.055  -11.693 1.00 39.56 ? 201 HEM   F CAB 1 
HETATM 15525 C  CBB . HEM   Y  3 .   ? -8.088  -76.056  -11.877 1.00 52.57 ? 201 HEM   F CBB 1 
HETATM 15526 C  C1C . HEM   Y  3 .   ? -6.798  -70.647  -11.558 1.00 28.16 ? 201 HEM   F C1C 1 
HETATM 15527 C  C2C . HEM   Y  3 .   ? -6.906  -69.866  -10.351 1.00 26.13 ? 201 HEM   F C2C 1 
HETATM 15528 C  C3C . HEM   Y  3 .   ? -6.806  -68.589  -10.702 1.00 29.10 ? 201 HEM   F C3C 1 
HETATM 15529 C  C4C . HEM   Y  3 .   ? -6.599  -68.506  -12.128 1.00 30.56 ? 201 HEM   F C4C 1 
HETATM 15530 C  CMC . HEM   Y  3 .   ? -7.151  -70.418  -8.924  1.00 36.82 ? 201 HEM   F CMC 1 
HETATM 15531 C  CAC . HEM   Y  3 .   ? -6.857  -67.362  -9.780  1.00 31.27 ? 201 HEM   F CAC 1 
HETATM 15532 C  CBC . HEM   Y  3 .   ? -6.778  -67.524  -8.454  1.00 45.53 ? 201 HEM   F CBC 1 
HETATM 15533 C  C1D . HEM   Y  3 .   ? -6.234  -67.231  -14.188 1.00 28.58 ? 201 HEM   F C1D 1 
HETATM 15534 C  C2D . HEM   Y  3 .   ? -6.119  -66.013  -14.974 1.00 30.47 ? 201 HEM   F C2D 1 
HETATM 15535 C  C3D . HEM   Y  3 .   ? -5.987  -66.370  -16.254 1.00 28.16 ? 201 HEM   F C3D 1 
HETATM 15536 C  C4D . HEM   Y  3 .   ? -5.990  -67.824  -16.320 1.00 33.46 ? 201 HEM   F C4D 1 
HETATM 15537 C  CMD . HEM   Y  3 .   ? -6.165  -64.565  -14.426 1.00 32.18 ? 201 HEM   F CMD 1 
HETATM 15538 C  CAD . HEM   Y  3 .   ? -5.817  -65.435  -17.478 1.00 32.89 ? 201 HEM   F CAD 1 
HETATM 15539 C  CBD . HEM   Y  3 .   ? -7.181  -65.198  -18.120 1.00 41.53 ? 201 HEM   F CBD 1 
HETATM 15540 C  CGD . HEM   Y  3 .   ? -7.038  -64.246  -19.280 1.00 47.84 ? 201 HEM   F CGD 1 
HETATM 15541 O  O1D . HEM   Y  3 .   ? -6.772  -64.720  -20.409 1.00 46.47 ? 201 HEM   F O1D 1 
HETATM 15542 O  O2D . HEM   Y  3 .   ? -7.182  -63.019  -19.061 1.00 55.13 ? 201 HEM   F O2D 1 
HETATM 15543 N  NA  . HEM   Y  3 .   ? -6.167  -70.853  -16.501 1.00 30.35 ? 201 HEM   F NA  1 
HETATM 15544 N  NB  . HEM   Y  3 .   ? -6.517  -72.269  -14.096 1.00 30.70 ? 201 HEM   F NB  1 
HETATM 15545 N  NC  . HEM   Y  3 .   ? -6.596  -69.782  -12.619 1.00 28.16 ? 201 HEM   F NC  1 
HETATM 15546 N  ND  . HEM   Y  3 .   ? -6.162  -68.304  -15.040 1.00 30.96 ? 201 HEM   F ND  1 
HETATM 15547 FE FE  . HEM   Y  3 .   ? -6.420  -70.289  -14.551 1.00 31.27 ? 201 HEM   F FE  1 
HETATM 15548 C  C13 . A1BYB Z  5 .   ? 1.200   -62.499  6.734   1.00 69.98 ? 202 A1BYB F C13 1 
HETATM 15549 C  C17 . A1BYB Z  5 .   ? -0.504  -69.362  4.592   1.00 51.84 ? 202 A1BYB F C17 1 
HETATM 15550 C  C02 . A1BYB Z  5 .   ? -3.860  -68.953  1.953   1.00 44.00 ? 202 A1BYB F C02 1 
HETATM 15551 C  C04 . A1BYB Z  5 .   ? -2.924  -66.900  2.798   1.00 55.18 ? 202 A1BYB F C04 1 
HETATM 15552 C  C05 . A1BYB Z  5 .   ? -2.131  -68.064  3.370   1.00 50.88 ? 202 A1BYB F C05 1 
HETATM 15553 C  C06 . A1BYB Z  5 .   ? -1.044  -68.069  4.225   1.00 60.93 ? 202 A1BYB F C06 1 
HETATM 15554 C  C08 . A1BYB Z  5 .   ? 0.843   -66.626  5.277   1.00 63.44 ? 202 A1BYB F C08 1 
HETATM 15555 C  C09 . A1BYB Z  5 .   ? 0.992   -65.196  5.764   1.00 67.13 ? 202 A1BYB F C09 1 
HETATM 15556 C  C10 . A1BYB Z  5 .   ? 1.661   -64.215  5.044   1.00 65.93 ? 202 A1BYB F C10 1 
HETATM 15557 C  C11 . A1BYB Z  5 .   ? 1.772   -62.899  5.518   1.00 79.59 ? 202 A1BYB F C11 1 
HETATM 15558 C  C14 . A1BYB Z  5 .   ? 0.506   -63.465  7.472   1.00 68.68 ? 202 A1BYB F C14 1 
HETATM 15559 C  C15 . A1BYB Z  5 .   ? 0.419   -64.772  6.962   1.00 72.52 ? 202 A1BYB F C15 1 
HETATM 15560 C  C18 . A1BYB Z  5 .   ? -1.055  -70.554  4.093   1.00 50.86 ? 202 A1BYB F C18 1 
HETATM 15561 C  C19 . A1BYB Z  5 .   ? -2.185  -70.531  3.202   1.00 49.84 ? 202 A1BYB F C19 1 
HETATM 15562 C  C20 . A1BYB Z  5 .   ? -2.691  -69.280  2.865   1.00 51.14 ? 202 A1BYB F C20 1 
HETATM 15563 N  N03 . A1BYB Z  5 .   ? -3.941  -67.510  1.973   1.00 52.43 ? 202 A1BYB F N03 1 
HETATM 15564 N  N07 . A1BYB Z  5 .   ? -0.481  -66.872  4.738   1.00 66.79 ? 202 A1BYB F N07 1 
HETATM 15565 O  O01 . A1BYB Z  5 .   ? -4.609  -69.618  1.304   1.00 43.14 ? 202 A1BYB F O01 1 
HETATM 15566 O  O16 . A1BYB Z  5 .   ? -0.273  -65.753  7.669   1.00 69.31 ? 202 A1BYB F O16 1 
HETATM 15567 O  O21 . A1BYB Z  5 .   ? -2.833  -65.714  2.921   1.00 46.62 ? 202 A1BYB F O21 1 
HETATM 15568 CL CL1 . A1BYB Z  5 .   ? 2.658   -61.722  4.558   1.00 89.52 ? 202 A1BYB F CL1 1 
HETATM 15569 O  O2  . PG4   AA 4 .   ? -24.601 -16.426  -58.082 1.00 46.59 ? 201 PG4   G O2  1 
HETATM 15570 C  C3  . PG4   AA 4 .   ? -24.320 -15.284  -58.891 1.00 47.31 ? 201 PG4   G C3  1 
HETATM 15571 C  C4  . PG4   AA 4 .   ? -24.908 -14.045  -58.283 1.00 47.46 ? 201 PG4   G C4  1 
HETATM 15572 O  O3  . PG4   AA 4 .   ? -24.063 -13.520  -57.249 1.00 55.08 ? 201 PG4   G O3  1 
HETATM 15573 C  C5  . PG4   AA 4 .   ? -24.774 -12.503  -56.535 1.00 43.91 ? 201 PG4   G C5  1 
HETATM 15574 C  C6  . PG4   AA 4 .   ? -23.869 -11.652  -55.690 1.00 44.80 ? 201 PG4   G C6  1 
HETATM 15575 O  O4  . PG4   AA 4 .   ? -22.950 -12.443  -54.956 1.00 53.60 ? 201 PG4   G O4  1 
HETATM 15576 C  C7  . PG4   AA 4 .   ? -22.976 -12.008  -53.604 1.00 51.75 ? 201 PG4   G C7  1 
HETATM 15577 C  C8  . PG4   AA 4 .   ? -23.201 -13.173  -52.687 1.00 59.56 ? 201 PG4   G C8  1 
HETATM 15578 O  O5  . PG4   AA 4 .   ? -23.551 -12.706  -51.389 1.00 58.78 ? 201 PG4   G O5  1 
HETATM 15579 C  C2  . PG4   BA 4 .   ? 35.590  -67.608  -48.998 1.00 59.93 ? 201 PG4   H C2  1 
HETATM 15580 O  O2  . PG4   BA 4 .   ? 36.728  -68.258  -49.556 1.00 54.92 ? 201 PG4   H O2  1 
HETATM 15581 C  C3  . PG4   BA 4 .   ? 37.960  -67.654  -49.195 1.00 42.74 ? 201 PG4   H C3  1 
HETATM 15582 C  C4  . PG4   BA 4 .   ? 39.068  -68.347  -49.927 1.00 49.98 ? 201 PG4   H C4  1 
HETATM 15583 O  O3  . PG4   BA 4 .   ? 39.063  -67.937  -51.302 1.00 59.22 ? 201 PG4   H O3  1 
HETATM 15584 C  C5  . PG4   BA 4 .   ? 39.921  -68.778  -52.074 1.00 52.95 ? 201 PG4   H C5  1 
HETATM 15585 C  C6  . PG4   BA 4 .   ? 39.966  -68.261  -53.480 1.00 47.07 ? 201 PG4   H C6  1 
HETATM 15586 O  O4  . PG4   BA 4 .   ? 38.641  -68.368  -53.990 1.00 66.97 ? 201 PG4   H O4  1 
HETATM 15587 C  C7  . PG4   BA 4 .   ? 38.632  -68.855  -55.323 1.00 59.00 ? 201 PG4   H C7  1 
HETATM 15588 C  C8  . PG4   BA 4 .   ? 37.311  -69.497  -55.622 1.00 59.91 ? 201 PG4   H C8  1 
HETATM 15589 O  O5  . PG4   BA 4 .   ? 37.431  -70.255  -56.825 1.00 55.35 ? 201 PG4   H O5  1 
HETATM 15590 C  CHA . HEM   CA 3 .   ? 29.192  -68.430  -34.102 1.00 29.87 ? 202 HEM   H CHA 1 
HETATM 15591 C  CHB . HEM   CA 3 .   ? 33.801  -69.338  -35.435 1.00 34.55 ? 202 HEM   H CHB 1 
HETATM 15592 C  CHC . HEM   CA 3 .   ? 34.341  -71.678  -31.239 1.00 30.57 ? 202 HEM   H CHC 1 
HETATM 15593 C  CHD . HEM   CA 3 .   ? 29.714  -70.905  -29.987 1.00 27.85 ? 202 HEM   H CHD 1 
HETATM 15594 C  C1A . HEM   CA 3 .   ? 30.393  -68.424  -34.793 1.00 30.94 ? 202 HEM   H C1A 1 
HETATM 15595 C  C2A . HEM   CA 3 .   ? 30.660  -67.677  -35.999 1.00 36.14 ? 202 HEM   H C2A 1 
HETATM 15596 C  C3A . HEM   CA 3 .   ? 31.933  -67.917  -36.374 1.00 37.80 ? 202 HEM   H C3A 1 
HETATM 15597 C  C4A . HEM   CA 3 .   ? 32.512  -68.840  -35.423 1.00 37.86 ? 202 HEM   H C4A 1 
HETATM 15598 C  CMA . HEM   CA 3 .   ? 32.705  -67.343  -37.582 1.00 35.27 ? 202 HEM   H CMA 1 
HETATM 15599 C  CAA . HEM   CA 3 .   ? 29.606  -66.756  -36.677 1.00 38.90 ? 202 HEM   H CAA 1 
HETATM 15600 C  CBA . HEM   CA 3 .   ? 30.014  -65.304  -36.438 1.00 41.84 ? 202 HEM   H CBA 1 
HETATM 15601 C  CGA . HEM   CA 3 .   ? 29.065  -64.423  -37.206 1.00 54.41 ? 202 HEM   H CGA 1 
HETATM 15602 O  O1A . HEM   CA 3 .   ? 29.535  -63.618  -38.052 1.00 55.93 ? 202 HEM   H O1A 1 
HETATM 15603 O  O2A . HEM   CA 3 .   ? 27.836  -64.565  -36.995 1.00 48.43 ? 202 HEM   H O2A 1 
HETATM 15604 C  C1B . HEM   CA 3 .   ? 34.396  -70.058  -34.415 1.00 32.68 ? 202 HEM   H C1B 1 
HETATM 15605 C  C2B . HEM   CA 3 .   ? 35.779  -70.528  -34.325 1.00 34.29 ? 202 HEM   H C2B 1 
HETATM 15606 C  C3B . HEM   CA 3 .   ? 35.900  -71.164  -33.151 1.00 35.38 ? 202 HEM   H C3B 1 
HETATM 15607 C  C4B . HEM   CA 3 .   ? 34.616  -71.134  -32.468 1.00 34.44 ? 202 HEM   H C4B 1 
HETATM 15608 C  CMB . HEM   CA 3 .   ? 36.874  -70.306  -35.400 1.00 35.05 ? 202 HEM   H CMB 1 
HETATM 15609 C  CAB . HEM   CA 3 .   ? 37.132  -71.872  -32.587 1.00 46.47 ? 202 HEM   H CAB 1 
HETATM 15610 C  CBB . HEM   CA 3 .   ? 38.022  -72.364  -33.448 1.00 50.34 ? 202 HEM   H CBB 1 
HETATM 15611 C  C1C . HEM   CA 3 .   ? 33.152  -71.676  -30.550 1.00 34.19 ? 202 HEM   H C1C 1 
HETATM 15612 C  C2C . HEM   CA 3 .   ? 32.916  -72.319  -29.277 1.00 29.63 ? 202 HEM   H C2C 1 
HETATM 15613 C  C3C . HEM   CA 3 .   ? 31.634  -72.118  -28.938 1.00 32.83 ? 202 HEM   H C3C 1 
HETATM 15614 C  C4C . HEM   CA 3 .   ? 31.016  -71.344  -29.986 1.00 32.42 ? 202 HEM   H C4C 1 
HETATM 15615 C  CMC . HEM   CA 3 .   ? 33.979  -73.103  -28.497 1.00 31.14 ? 202 HEM   H CMC 1 
HETATM 15616 C  CAC . HEM   CA 3 .   ? 30.863  -72.579  -27.681 1.00 42.55 ? 202 HEM   H CAC 1 
HETATM 15617 C  CBC . HEM   CA 3 .   ? 31.506  -73.178  -26.676 1.00 59.51 ? 202 HEM   H CBC 1 
HETATM 15618 C  C1D . HEM   CA 3 .   ? 29.139  -70.171  -30.988 1.00 34.59 ? 202 HEM   H C1D 1 
HETATM 15619 C  C2D . HEM   CA 3 .   ? 27.768  -69.719  -31.077 1.00 31.90 ? 202 HEM   H C2D 1 
HETATM 15620 C  C3D . HEM   CA 3 .   ? 27.634  -69.030  -32.212 1.00 34.19 ? 202 HEM   H C3D 1 
HETATM 15621 C  C4D . HEM   CA 3 .   ? 28.915  -69.021  -32.895 1.00 32.06 ? 202 HEM   H C4D 1 
HETATM 15622 C  CMD . HEM   CA 3 .   ? 26.675  -69.997  -30.038 1.00 37.04 ? 202 HEM   H CMD 1 
HETATM 15623 C  CAD . HEM   CA 3 .   ? 26.343  -68.372  -32.745 1.00 35.96 ? 202 HEM   H CAD 1 
HETATM 15624 C  CBD . HEM   CA 3 .   ? 25.548  -69.450  -33.461 1.00 40.34 ? 202 HEM   H CBD 1 
HETATM 15625 C  CGD . HEM   CA 3 .   ? 24.435  -68.808  -34.247 1.00 51.65 ? 202 HEM   H CGD 1 
HETATM 15626 O  O1D . HEM   CA 3 .   ? 24.639  -67.716  -34.832 1.00 57.41 ? 202 HEM   H O1D 1 
HETATM 15627 O  O2D . HEM   CA 3 .   ? 23.347  -69.412  -34.288 1.00 58.46 ? 202 HEM   H O2D 1 
HETATM 15628 N  NA  . HEM   CA 3 .   ? 31.544  -69.105  -34.473 1.00 30.22 ? 202 HEM   H NA  1 
HETATM 15629 N  NB  . HEM   CA 3 .   ? 33.749  -70.448  -33.272 1.00 33.49 ? 202 HEM   H NB  1 
HETATM 15630 N  NC  . HEM   CA 3 .   ? 31.974  -71.083  -30.941 1.00 35.31 ? 202 HEM   H NC  1 
HETATM 15631 N  ND  . HEM   CA 3 .   ? 29.799  -69.727  -32.108 1.00 34.00 ? 202 HEM   H ND  1 
HETATM 15632 FE FE  . HEM   CA 3 .   ? 31.790  -70.053  -32.665 1.00 31.86 ? 202 HEM   H FE  1 
HETATM 15633 C  C13 . A1BYB DA 5 .   ? 34.736  -72.016  -8.631  1.00 73.01 ? 203 A1BYB H C13 1 
HETATM 15634 C  C17 . A1BYB DA 5 .   ? 39.460  -72.915  -14.359 1.00 50.59 ? 203 A1BYB H C17 1 
HETATM 15635 C  C02 . A1BYB DA 5 .   ? 37.389  -74.880  -17.512 1.00 39.17 ? 203 A1BYB H C02 1 
HETATM 15636 C  C04 . A1BYB DA 5 .   ? 36.082  -74.424  -15.535 1.00 58.11 ? 203 A1BYB H C04 1 
HETATM 15637 C  C05 . A1BYB DA 5 .   ? 37.496  -73.909  -15.314 1.00 55.83 ? 203 A1BYB H C05 1 
HETATM 15638 C  C06 . A1BYB DA 5 .   ? 38.067  -73.256  -14.225 1.00 55.16 ? 203 A1BYB H C06 1 
HETATM 15639 C  C08 . A1BYB DA 5 .   ? 36.844  -71.682  -12.478 1.00 59.43 ? 203 A1BYB H C08 1 
HETATM 15640 C  C09 . A1BYB DA 5 .   ? 36.110  -71.782  -11.159 1.00 66.38 ? 203 A1BYB H C09 1 
HETATM 15641 C  C10 . A1BYB DA 5 .   ? 34.953  -71.053  -10.893 1.00 65.97 ? 203 A1BYB H C10 1 
HETATM 15642 C  C11 . A1BYB DA 5 .   ? 34.283  -71.162  -9.658  1.00 75.84 ? 203 A1BYB H C11 1 
HETATM 15643 C  C14 . A1BYB DA 5 .   ? 35.895  -72.772  -8.868  1.00 68.72 ? 203 A1BYB H C14 1 
HETATM 15644 C  C15 . A1BYB DA 5 .   ? 36.547  -72.636  -10.115 1.00 79.89 ? 203 A1BYB H C15 1 
HETATM 15645 C  C18 . A1BYB DA 5 .   ? 40.182  -73.197  -15.513 1.00 52.13 ? 203 A1BYB H C18 1 
HETATM 15646 C  C19 . A1BYB DA 5 .   ? 39.573  -73.851  -16.617 1.00 42.82 ? 203 A1BYB H C19 1 
HETATM 15647 C  C20 . A1BYB DA 5 .   ? 38.254  -74.188  -16.496 1.00 44.80 ? 203 A1BYB H C20 1 
HETATM 15648 N  N03 . A1BYB DA 5 .   ? 36.098  -74.995  -16.863 1.00 45.28 ? 203 A1BYB H N03 1 
HETATM 15649 N  N07 . A1BYB DA 5 .   ? 37.383  -72.962  -12.981 1.00 60.19 ? 203 A1BYB H N07 1 
HETATM 15650 O  O01 . A1BYB DA 5 .   ? 37.584  -75.291  -18.617 1.00 43.59 ? 203 A1BYB H O01 1 
HETATM 15651 O  O16 . A1BYB DA 5 .   ? 37.708  -73.371  -10.377 1.00 69.73 ? 203 A1BYB H O16 1 
HETATM 15652 O  O21 . A1BYB DA 5 .   ? 35.097  -74.413  -14.854 1.00 41.50 ? 203 A1BYB H O21 1 
HETATM 15653 CL CL1 . A1BYB DA 5 .   ? 32.840  -70.201  -9.390  1.00 80.27 ? 203 A1BYB H CL1 1 
HETATM 15654 C  CHA . HEM   EA 3 .   ? -35.199 -49.028  -34.270 1.00 33.95 ? 201 HEM   I CHA 1 
HETATM 15655 C  CHB . HEM   EA 3 .   ? -39.375 -46.742  -35.169 1.00 29.31 ? 201 HEM   I CHB 1 
HETATM 15656 C  CHC . HEM   EA 3 .   ? -41.273 -49.046  -31.388 1.00 32.41 ? 201 HEM   I CHC 1 
HETATM 15657 C  CHD . HEM   EA 3 .   ? -37.096 -51.341  -30.455 1.00 31.39 ? 201 HEM   I CHD 1 
HETATM 15658 C  C1A . HEM   EA 3 .   ? -36.159 -48.239  -34.882 1.00 30.55 ? 201 HEM   I C1A 1 
HETATM 15659 C  C2A . HEM   EA 3 .   ? -36.012 -47.507  -36.135 1.00 28.95 ? 201 HEM   I C2A 1 
HETATM 15660 C  C3A . HEM   EA 3 .   ? -37.163 -46.868  -36.389 1.00 31.34 ? 201 HEM   I C3A 1 
HETATM 15661 C  C4A . HEM   EA 3 .   ? -38.080 -47.170  -35.302 1.00 32.19 ? 201 HEM   I C4A 1 
HETATM 15662 C  CMA . HEM   EA 3 .   ? -37.534 -45.960  -37.585 1.00 33.14 ? 201 HEM   I CMA 1 
HETATM 15663 C  CAA . HEM   EA 3 .   ? -34.718 -47.485  -36.981 1.00 34.03 ? 201 HEM   I CAA 1 
HETATM 15664 C  CBA . HEM   EA 3 .   ? -34.579 -48.781  -37.773 1.00 39.54 ? 201 HEM   I CBA 1 
HETATM 15665 C  CGA . HEM   EA 3 .   ? -33.428 -48.664  -38.760 1.00 38.00 ? 201 HEM   I CGA 1 
HETATM 15666 O  O1A . HEM   EA 3 .   ? -33.613 -48.097  -39.854 1.00 47.51 ? 201 HEM   I O1A 1 
HETATM 15667 O  O2A . HEM   EA 3 .   ? -32.315 -49.120  -38.450 1.00 45.62 ? 201 HEM   I O2A 1 
HETATM 15668 C  C1B . HEM   EA 3 .   ? -40.277 -47.192  -34.233 1.00 31.32 ? 201 HEM   I C1B 1 
HETATM 15669 C  C2B . HEM   EA 3 .   ? -41.676 -46.827  -34.156 1.00 34.89 ? 201 HEM   I C2B 1 
HETATM 15670 C  C3B . HEM   EA 3 .   ? -42.207 -47.471  -33.103 1.00 31.55 ? 201 HEM   I C3B 1 
HETATM 15671 C  C4B . HEM   EA 3 .   ? -41.154 -48.248  -32.488 1.00 32.03 ? 201 HEM   I C4B 1 
HETATM 15672 C  CMB . HEM   EA 3 .   ? -42.342 -45.862  -35.169 1.00 35.17 ? 201 HEM   I CMB 1 
HETATM 15673 C  CAB . HEM   EA 3 .   ? -43.666 -47.392  -32.591 1.00 40.80 ? 201 HEM   I CAB 1 
HETATM 15674 C  CBB . HEM   EA 3 .   ? -44.403 -46.353  -33.000 1.00 43.75 ? 201 HEM   I CBB 1 
HETATM 15675 C  C1C . HEM   EA 3 .   ? -40.307 -49.837  -30.804 1.00 32.03 ? 201 HEM   I C1C 1 
HETATM 15676 C  C2C . HEM   EA 3 .   ? -40.511 -50.634  -29.609 1.00 30.63 ? 201 HEM   I C2C 1 
HETATM 15677 C  C3C . HEM   EA 3 .   ? -39.361 -51.265  -29.346 1.00 32.99 ? 201 HEM   I C3C 1 
HETATM 15678 C  C4C . HEM   EA 3 .   ? -38.391 -50.890  -30.370 1.00 27.90 ? 201 HEM   I C4C 1 
HETATM 15679 C  CMC . HEM   EA 3 .   ? -41.849 -50.697  -28.797 1.00 36.10 ? 201 HEM   I CMC 1 
HETATM 15680 C  CAC . HEM   EA 3 .   ? -39.028 -52.236  -28.190 1.00 34.42 ? 201 HEM   I CAC 1 
HETATM 15681 C  CBC . HEM   EA 3 .   ? -40.009 -52.838  -27.506 1.00 51.14 ? 201 HEM   I CBC 1 
HETATM 15682 C  C1D . HEM   EA 3 .   ? -36.190 -50.897  -31.384 1.00 32.84 ? 201 HEM   I C1D 1 
HETATM 15683 C  C2D . HEM   EA 3 .   ? -34.780 -51.204  -31.447 1.00 34.79 ? 201 HEM   I C2D 1 
HETATM 15684 C  C3D . HEM   EA 3 .   ? -34.267 -50.560  -32.507 1.00 29.40 ? 201 HEM   I C3D 1 
HETATM 15685 C  C4D . HEM   EA 3 .   ? -35.336 -49.819  -33.142 1.00 34.06 ? 201 HEM   I C4D 1 
HETATM 15686 C  CMD . HEM   EA 3 .   ? -34.048 -52.107  -30.423 1.00 36.20 ? 201 HEM   I CMD 1 
HETATM 15687 C  CAD . HEM   EA 3 .   ? -32.791 -50.563  -33.024 1.00 30.34 ? 201 HEM   I CAD 1 
HETATM 15688 C  CBD . HEM   EA 3 .   ? -32.019 -49.460  -32.331 1.00 41.96 ? 201 HEM   I CBD 1 
HETATM 15689 C  CGD . HEM   EA 3 .   ? -30.556 -49.603  -32.684 1.00 41.03 ? 201 HEM   I CGD 1 
HETATM 15690 O  O1D . HEM   EA 3 .   ? -30.221 -49.417  -33.866 1.00 48.35 ? 201 HEM   I O1D 1 
HETATM 15691 O  O2D . HEM   EA 3 .   ? -29.749 -49.915  -31.787 1.00 57.22 ? 201 HEM   I O2D 1 
HETATM 15692 N  NA  . HEM   EA 3 .   ? -37.438 -48.002  -34.427 1.00 30.69 ? 201 HEM   I NA  1 
HETATM 15693 N  NB  . HEM   EA 3 .   ? -39.994 -48.051  -33.204 1.00 35.65 ? 201 HEM   I NB  1 
HETATM 15694 N  NC  . HEM   EA 3 .   ? -39.005 -50.008  -31.229 1.00 31.53 ? 201 HEM   I NC  1 
HETATM 15695 N  ND  . HEM   EA 3 .   ? -36.498 -50.042  -32.415 1.00 31.77 ? 201 HEM   I ND  1 
HETATM 15696 FE FE  . HEM   EA 3 .   ? -38.268 -49.016  -32.828 1.00 29.73 ? 201 HEM   I FE  1 
HETATM 15697 O  O1  . PG4   FA 4 .   ? -28.941 -61.910  -28.792 1.00 77.17 ? 202 PG4   I O1  1 
HETATM 15698 C  C1  . PG4   FA 4 .   ? -28.944 -63.001  -27.892 1.00 72.17 ? 202 PG4   I C1  1 
HETATM 15699 C  C2  . PG4   FA 4 .   ? -29.132 -62.541  -26.478 1.00 69.39 ? 202 PG4   I C2  1 
HETATM 15700 O  O2  . PG4   FA 4 .   ? -30.433 -62.898  -26.032 1.00 61.34 ? 202 PG4   I O2  1 
HETATM 15701 C  C3  . PG4   FA 4 .   ? -30.662 -62.644  -24.649 1.00 50.81 ? 202 PG4   I C3  1 
HETATM 15702 C  C4  . PG4   FA 4 .   ? -31.253 -63.851  -24.009 1.00 47.65 ? 202 PG4   I C4  1 
HETATM 15703 O  O3  . PG4   FA 4 .   ? -30.258 -64.861  -23.823 1.00 54.29 ? 202 PG4   I O3  1 
HETATM 15704 C  C5  . PG4   FA 4 .   ? -30.854 -66.002  -23.205 1.00 53.19 ? 202 PG4   I C5  1 
HETATM 15705 C  C6  . PG4   FA 4 .   ? -29.804 -67.026  -22.925 1.00 48.60 ? 202 PG4   I C6  1 
HETATM 15706 O  O4  . PG4   FA 4 .   ? -29.237 -67.441  -24.155 1.00 58.46 ? 202 PG4   I O4  1 
HETATM 15707 C  C7  . PG4   FA 4 .   ? -28.475 -68.637  -24.036 1.00 51.44 ? 202 PG4   I C7  1 
HETATM 15708 C  C8  . PG4   FA 4 .   ? -28.621 -69.314  -25.375 1.00 63.50 ? 202 PG4   I C8  1 
HETATM 15709 O  O5  . PG4   FA 4 .   ? -28.048 -70.608  -25.439 1.00 60.92 ? 202 PG4   I O5  1 
HETATM 15710 C  C13 . A1BYB GA 5 .   ? -53.051 -30.032  -33.442 1.00 74.40 ? 203 A1BYB I C13 1 
HETATM 15711 C  C17 . A1BYB GA 5 .   ? -52.942 -35.756  -28.692 1.00 53.70 ? 203 A1BYB I C17 1 
HETATM 15712 C  C02 . A1BYB GA 5 .   ? -51.888 -39.081  -31.191 1.00 42.00 ? 203 A1BYB I C02 1 
HETATM 15713 C  C04 . A1BYB GA 5 .   ? -51.980 -36.942  -32.237 1.00 52.44 ? 203 A1BYB I C04 1 
HETATM 15714 C  C05 . A1BYB GA 5 .   ? -52.335 -36.758  -30.780 1.00 51.61 ? 203 A1BYB I C05 1 
HETATM 15715 C  C06 . A1BYB GA 5 .   ? -52.654 -35.607  -30.087 1.00 51.47 ? 203 A1BYB I C06 1 
HETATM 15716 C  C08 . A1BYB GA 5 .   ? -52.537 -32.994  -30.198 1.00 51.78 ? 203 A1BYB I C08 1 
HETATM 15717 C  C09 . A1BYB GA 5 .   ? -52.691 -31.943  -31.315 1.00 66.02 ? 203 A1BYB I C09 1 
HETATM 15718 C  C10 . A1BYB GA 5 .   ? -51.604 -31.298  -31.914 1.00 61.73 ? 203 A1BYB I C10 1 
HETATM 15719 C  C11 . A1BYB GA 5 .   ? -51.787 -30.355  -32.949 1.00 69.89 ? 203 A1BYB I C11 1 
HETATM 15720 C  C14 . A1BYB GA 5 .   ? -54.155 -30.671  -32.880 1.00 80.09 ? 203 A1BYB I C14 1 
HETATM 15721 C  C15 . A1BYB GA 5 .   ? -53.954 -31.598  -31.856 1.00 84.85 ? 203 A1BYB I C15 1 
HETATM 15722 C  C18 . A1BYB GA 5 .   ? -52.882 -37.008  -28.066 1.00 51.17 ? 203 A1BYB I C18 1 
HETATM 15723 C  C19 . A1BYB GA 5 .   ? -52.541 -38.194  -28.814 1.00 49.66 ? 203 A1BYB I C19 1 
HETATM 15724 C  C20 . A1BYB GA 5 .   ? -52.266 -38.031  -30.154 1.00 46.57 ? 203 A1BYB I C20 1 
HETATM 15725 N  N03 . A1BYB GA 5 .   ? -51.750 -38.342  -32.398 1.00 46.78 ? 203 A1BYB I N03 1 
HETATM 15726 N  N07 . A1BYB GA 5 .   ? -52.716 -34.337  -30.725 1.00 49.95 ? 203 A1BYB I N07 1 
HETATM 15727 O  O01 . A1BYB GA 5 .   ? -51.701 -40.262  -31.161 1.00 38.51 ? 203 A1BYB I O01 1 
HETATM 15728 O  O16 . A1BYB GA 5 .   ? -55.063 -32.234  -31.306 1.00 82.55 ? 203 A1BYB I O16 1 
HETATM 15729 O  O21 . A1BYB GA 5 .   ? -51.899 -36.182  -33.155 1.00 53.95 ? 203 A1BYB I O21 1 
HETATM 15730 CL CL1 . A1BYB GA 5 .   ? -50.401 -29.547  -33.660 1.00 71.28 ? 203 A1BYB I CL1 1 
HETATM 15731 C  C2  . PG4   HA 4 .   ? 20.251  -67.323  -21.088 1.00 45.56 ? 201 PG4   J C2  1 
HETATM 15732 O  O2  . PG4   HA 4 .   ? 20.534  -67.528  -19.705 1.00 57.11 ? 201 PG4   J O2  1 
HETATM 15733 C  C3  . PG4   HA 4 .   ? 20.235  -68.848  -19.259 1.00 48.18 ? 201 PG4   J C3  1 
HETATM 15734 C  C4  . PG4   HA 4 .   ? 20.556  -68.992  -17.807 1.00 50.18 ? 201 PG4   J C4  1 
HETATM 15735 O  O3  . PG4   HA 4 .   ? 19.421  -68.633  -17.032 1.00 54.23 ? 201 PG4   J O3  1 
HETATM 15736 C  C5  . PG4   HA 4 .   ? 19.797  -68.527  -15.658 1.00 52.10 ? 201 PG4   J C5  1 
HETATM 15737 C  C6  . PG4   HA 4 .   ? 18.594  -68.332  -14.790 1.00 53.26 ? 201 PG4   J C6  1 
HETATM 15738 O  O4  . PG4   HA 4 .   ? 17.800  -67.282  -15.333 1.00 57.91 ? 201 PG4   J O4  1 
HETATM 15739 C  C7  . PG4   HA 4 .   ? 17.211  -66.479  -14.318 1.00 49.84 ? 201 PG4   J C7  1 
HETATM 15740 C  C8  . PG4   HA 4 .   ? 17.266  -65.052  -14.769 1.00 53.80 ? 201 PG4   J C8  1 
HETATM 15741 O  O5  . PG4   HA 4 .   ? 17.209  -64.188  -13.645 1.00 43.69 ? 201 PG4   J O5  1 
HETATM 15742 C  C13 . A1BYB IA 5 .   ? 48.653  -80.825  -45.328 1.00 68.51 ? 202 A1BYB J C13 1 
HETATM 15743 C  C17 . A1BYB IA 5 .   ? 46.780  -82.467  -38.198 1.00 61.89 ? 202 A1BYB J C17 1 
HETATM 15744 C  C02 . A1BYB IA 5 .   ? 45.795  -78.570  -36.731 1.00 58.00 ? 202 A1BYB J C02 1 
HETATM 15745 C  C04 . A1BYB IA 5 .   ? 46.534  -78.687  -39.017 1.00 67.75 ? 202 A1BYB J C04 1 
HETATM 15746 C  C05 . A1BYB IA 5 .   ? 46.539  -80.088  -38.436 1.00 69.36 ? 202 A1BYB J C05 1 
HETATM 15747 C  C06 . A1BYB IA 5 .   ? 46.874  -81.294  -39.029 1.00 70.61 ? 202 A1BYB J C06 1 
HETATM 15748 C  C08 . A1BYB IA 5 .   ? 46.946  -82.252  -41.482 1.00 54.14 ? 202 A1BYB J C08 1 
HETATM 15749 C  C09 . A1BYB IA 5 .   ? 47.522  -81.764  -42.833 1.00 72.07 ? 202 A1BYB J C09 1 
HETATM 15750 C  C10 . A1BYB IA 5 .   ? 46.712  -81.436  -43.919 1.00 65.52 ? 202 A1BYB J C10 1 
HETATM 15751 C  C11 . A1BYB IA 5 .   ? 47.269  -80.988  -45.138 1.00 79.54 ? 202 A1BYB J C11 1 
HETATM 15752 C  C14 . A1BYB IA 5 .   ? 49.492  -81.119  -44.261 1.00 70.30 ? 202 A1BYB J C14 1 
HETATM 15753 C  C15 . A1BYB IA 5 .   ? 48.928  -81.570  -43.058 1.00 80.27 ? 202 A1BYB J C15 1 
HETATM 15754 C  C18 . A1BYB IA 5 .   ? 46.353  -82.392  -36.878 1.00 59.73 ? 202 A1BYB J C18 1 
HETATM 15755 C  C19 . A1BYB IA 5 .   ? 45.997  -81.136  -36.288 1.00 60.54 ? 202 A1BYB J C19 1 
HETATM 15756 C  C20 . A1BYB IA 5 .   ? 46.102  -80.012  -37.086 1.00 60.77 ? 202 A1BYB J C20 1 
HETATM 15757 N  N03 . A1BYB IA 5 .   ? 46.084  -77.836  -37.936 1.00 58.90 ? 202 A1BYB J N03 1 
HETATM 15758 N  N07 . A1BYB IA 5 .   ? 47.350  -81.387  -40.382 1.00 65.97 ? 202 A1BYB J N07 1 
HETATM 15759 O  O01 . A1BYB IA 5 .   ? 45.405  -78.026  -35.741 1.00 51.14 ? 202 A1BYB J O01 1 
HETATM 15760 O  O16 . A1BYB IA 5 .   ? 49.786  -81.862  -42.003 1.00 67.47 ? 202 A1BYB J O16 1 
HETATM 15761 O  O21 . A1BYB IA 5 .   ? 46.817  -78.260  -40.099 1.00 51.50 ? 202 A1BYB J O21 1 
HETATM 15762 CL CL1 . A1BYB IA 5 .   ? 46.215  -80.625  -46.473 1.00 81.19 ? 202 A1BYB J CL1 1 
HETATM 15763 C  C13 . A1BYB JA 5 .   ? -18.122 -91.110  -13.728 1.00 82.87 ? 201 A1BYB K C13 1 
HETATM 15764 C  C17 . A1BYB JA 5 .   ? -17.072 -86.176  -8.220  1.00 55.47 ? 201 A1BYB K C17 1 
HETATM 15765 C  C02 . A1BYB JA 5 .   ? -13.095 -84.741  -8.927  1.00 47.65 ? 201 A1BYB K C02 1 
HETATM 15766 C  C04 . A1BYB JA 5 .   ? -13.929 -86.416  -10.428 1.00 62.86 ? 201 A1BYB K C04 1 
HETATM 15767 C  C05 . A1BYB JA 5 .   ? -15.002 -86.121  -9.418  1.00 61.19 ? 201 A1BYB K C05 1 
HETATM 15768 C  C06 . A1BYB JA 5 .   ? -16.269 -86.662  -9.299  1.00 66.05 ? 201 A1BYB K C06 1 
HETATM 15769 C  C08 . A1BYB JA 5 .   ? -18.114 -87.968  -10.613 1.00 68.19 ? 201 A1BYB K C08 1 
HETATM 15770 C  C09 . A1BYB JA 5 .   ? -18.136 -89.056  -11.704 1.00 81.62 ? 201 A1BYB K C09 1 
HETATM 15771 C  C10 . A1BYB JA 5 .   ? -18.454 -88.777  -13.037 1.00 72.73 ? 201 A1BYB K C10 1 
HETATM 15772 C  C11 . A1BYB JA 5 .   ? -18.453 -89.784  -14.017 1.00 81.04 ? 201 A1BYB K C11 1 
HETATM 15773 C  C14 . A1BYB JA 5 .   ? -17.782 -91.426  -12.408 1.00 74.29 ? 201 A1BYB K C14 1 
HETATM 15774 C  C15 . A1BYB JA 5 .   ? -17.788 -90.410  -11.442 1.00 82.39 ? 201 A1BYB K C15 1 
HETATM 15775 C  C18 . A1BYB JA 5 .   ? -16.596 -85.200  -7.341  1.00 59.41 ? 201 A1BYB K C18 1 
HETATM 15776 C  C19 . A1BYB JA 5 .   ? -15.270 -84.651  -7.481  1.00 60.73 ? 201 A1BYB K C19 1 
HETATM 15777 C  C20 . A1BYB JA 5 .   ? -14.510 -85.125  -8.527  1.00 51.80 ? 201 A1BYB K C20 1 
HETATM 15778 N  N03 . A1BYB JA 5 .   ? -12.824 -85.555  -10.067 1.00 60.85 ? 201 A1BYB K N03 1 
HETATM 15779 N  N07 . A1BYB JA 5 .   ? -16.758 -87.669  -10.190 1.00 61.67 ? 201 A1BYB K N07 1 
HETATM 15780 O  O01 . A1BYB JA 5 .   ? -12.282 -83.977  -8.494  1.00 40.44 ? 201 A1BYB K O01 1 
HETATM 15781 O  O16 . A1BYB JA 5 .   ? -17.448 -90.730  -10.125 1.00 71.07 ? 201 A1BYB K O16 1 
HETATM 15782 O  O21 . A1BYB JA 5 .   ? -13.882 -87.164  -11.359 1.00 56.89 ? 201 A1BYB K O21 1 
HETATM 15783 CL CL1 . A1BYB JA 5 .   ? -18.882 -89.393  -15.648 1.00 91.35 ? 201 A1BYB K CL1 1 
HETATM 15784 C  CHA . HEM   KA 3 .   ? -0.008  -10.295  -50.697 0.50 26.81 ? 201 HEM   L CHA 1 
HETATM 15785 C  CHB . HEM   KA 3 .   ? -0.859  -6.884   -47.348 0.50 31.29 ? 201 HEM   L CHB 1 
HETATM 15786 C  CHC . HEM   KA 3 .   ? -0.035  -3.437   -50.660 0.50 32.54 ? 201 HEM   L CHC 1 
HETATM 15787 C  CHD . HEM   KA 3 .   ? 0.816   -6.851   -54.029 0.50 31.26 ? 201 HEM   L CHD 1 
HETATM 15788 C  C1A . HEM   KA 3 .   ? -0.272  -9.680   -49.487 0.50 34.11 ? 201 HEM   L C1A 1 
HETATM 15789 C  C2A . HEM   KA 3 .   ? -0.500  -10.345  -48.218 0.50 31.73 ? 201 HEM   L C2A 1 
HETATM 15790 C  C3A . HEM   KA 3 .   ? -0.727  -9.408   -47.292 0.50 30.95 ? 201 HEM   L C3A 1 
HETATM 15791 C  C4A . HEM   KA 3 .   ? -0.665  -8.114   -47.941 0.50 33.00 ? 201 HEM   L C4A 1 
HETATM 15792 C  CMA . HEM   KA 3 .   ? -1.017  -9.628   -45.791 0.50 32.27 ? 201 HEM   L CMA 1 
HETATM 15793 C  CAA . HEM   KA 3 .   ? -0.449  -11.874  -47.999 0.50 36.22 ? 201 HEM   L CAA 1 
HETATM 15794 C  CBA . HEM   KA 3 .   ? 1.011   -12.281  -47.805 0.50 32.82 ? 201 HEM   L CBA 1 
HETATM 15795 C  CGA . HEM   KA 3 .   ? 1.143   -13.726  -47.388 0.50 39.12 ? 201 HEM   L CGA 1 
HETATM 15796 O  O1A . HEM   KA 3 .   ? 0.331   -14.208  -46.549 0.50 44.45 ? 201 HEM   L O1A 1 
HETATM 15797 O  O2A . HEM   KA 3 .   ? 2.084   -14.396  -47.879 0.50 36.71 ? 201 HEM   L O2A 1 
HETATM 15798 C  C1B . HEM   KA 3 .   ? -0.728  -5.664   -47.968 0.50 33.67 ? 201 HEM   L C1B 1 
HETATM 15799 C  C2B . HEM   KA 3 .   ? -0.964  -4.385   -47.340 0.50 31.42 ? 201 HEM   L C2B 1 
HETATM 15800 C  C3B . HEM   KA 3 .   ? -0.728  -3.425   -48.244 0.50 32.46 ? 201 HEM   L C3B 1 
HETATM 15801 C  C4B . HEM   KA 3 .   ? -0.347  -4.072   -49.483 0.50 32.73 ? 201 HEM   L C4B 1 
HETATM 15802 C  CMB . HEM   KA 3 .   ? -1.388  -4.234   -45.864 0.50 33.35 ? 201 HEM   L CMB 1 
HETATM 15803 C  CAB . HEM   KA 3 .   ? -0.853  -1.896   -48.069 0.50 35.36 ? 201 HEM   L CAB 1 
HETATM 15804 C  CBB . HEM   KA 3 .   ? -1.541  -1.366   -47.043 0.50 38.45 ? 201 HEM   L CBB 1 
HETATM 15805 C  C1C . HEM   KA 3 .   ? 0.250   -4.065   -51.852 0.50 32.58 ? 201 HEM   L C1C 1 
HETATM 15806 C  C2C . HEM   KA 3 .   ? 0.520   -3.396   -53.103 0.50 32.62 ? 201 HEM   L C2C 1 
HETATM 15807 C  C3C . HEM   KA 3 .   ? 0.749   -4.338   -54.036 0.50 31.41 ? 201 HEM   L C3C 1 
HETATM 15808 C  C4C . HEM   KA 3 .   ? 0.642   -5.634   -53.400 0.50 33.78 ? 201 HEM   L C4C 1 
HETATM 15809 C  CMC . HEM   KA 3 .   ? 0.512   -1.862   -53.247 0.50 34.27 ? 201 HEM   L CMC 1 
HETATM 15810 C  CAC . HEM   KA 3 .   ? 1.094   -4.178   -55.535 0.50 33.25 ? 201 HEM   L CAC 1 
HETATM 15811 C  CBC . HEM   KA 3 .   ? 1.510   -3.010   -56.026 0.50 36.11 ? 201 HEM   L CBC 1 
HETATM 15812 C  C1D . HEM   KA 3 .   ? 0.642   -8.091   -53.442 0.50 32.89 ? 201 HEM   L C1D 1 
HETATM 15813 C  C2D . HEM   KA 3 .   ? 0.748   -9.390   -54.085 0.50 30.97 ? 201 HEM   L C2D 1 
HETATM 15814 C  C3D . HEM   KA 3 .   ? 0.525   -10.332  -53.161 0.50 31.73 ? 201 HEM   L C3D 1 
HETATM 15815 C  C4D . HEM   KA 3 .   ? 0.262   -9.670   -51.900 0.50 34.07 ? 201 HEM   L C4D 1 
HETATM 15816 C  CMD . HEM   KA 3 .   ? 1.068   -9.606   -55.580 0.50 32.26 ? 201 HEM   L CMD 1 
HETATM 15817 C  CAD . HEM   KA 3 .   ? 0.517   -11.866  -53.356 0.50 36.12 ? 201 HEM   L CAD 1 
HETATM 15818 C  CBD . HEM   KA 3 .   ? -0.893  -12.330  -53.714 0.50 32.86 ? 201 HEM   L CBD 1 
HETATM 15819 C  CGD . HEM   KA 3 .   ? -0.864  -13.799  -54.059 0.50 39.28 ? 201 HEM   L CGD 1 
HETATM 15820 O  O1D . HEM   KA 3 .   ? -0.858  -14.641  -53.123 0.50 37.05 ? 201 HEM   L O1D 1 
HETATM 15821 O  O2D . HEM   KA 3 .   ? -0.835  -14.128  -55.280 0.50 45.17 ? 201 HEM   L O2D 1 
HETATM 15822 N  NA  . HEM   KA 3 .   ? -0.378  -8.317   -49.268 0.50 29.68 ? 201 HEM   L NA  1 
HETATM 15823 N  NB  . HEM   KA 3 .   ? -0.347  -5.440   -49.280 0.50 29.22 ? 201 HEM   L NB  1 
HETATM 15824 N  NC  . HEM   KA 3 .   ? 0.327   -5.432   -52.066 0.50 29.14 ? 201 HEM   L NC  1 
HETATM 15825 N  ND  . HEM   KA 3 .   ? 0.337   -8.304   -52.120 0.50 29.75 ? 201 HEM   L ND  1 
HETATM 15826 FE FE  . HEM   KA 3 .   ? -0.012  -6.868   -50.652 0.50 28.61 ? 201 HEM   L FE  1 
HETATM 15827 O  O1  . PG4   LA 4 .   ? -9.053  -13.208  -36.533 1.00 61.85 ? 202 PG4   L O1  1 
HETATM 15828 C  C1  . PG4   LA 4 .   ? -8.708  -12.115  -37.368 1.00 82.36 ? 202 PG4   L C1  1 
HETATM 15829 C  C2  . PG4   LA 4 .   ? -7.827  -11.136  -36.655 1.00 59.47 ? 202 PG4   L C2  1 
HETATM 15830 O  O2  . PG4   LA 4 .   ? -8.344  -10.908  -35.359 1.00 63.94 ? 202 PG4   L O2  1 
HETATM 15831 C  C3  . PG4   LA 4 .   ? -7.849  -9.733   -34.734 1.00 56.21 ? 202 PG4   L C3  1 
HETATM 15832 C  C4  . PG4   LA 4 .   ? -8.971  -9.134   -33.951 1.00 48.60 ? 202 PG4   L C4  1 
HETATM 15833 O  O3  . PG4   LA 4 .   ? -9.666  -10.152  -33.223 1.00 48.42 ? 202 PG4   L O3  1 
HETATM 15834 C  C5  . PG4   LA 4 .   ? -10.754 -9.543   -32.515 1.00 50.42 ? 202 PG4   L C5  1 
HETATM 15835 C  C6  . PG4   LA 4 .   ? -11.082 -10.289  -31.255 1.00 47.19 ? 202 PG4   L C6  1 
HETATM 15836 O  O4  . PG4   LA 4 .   ? -11.419 -11.638  -31.579 1.00 53.95 ? 202 PG4   L O4  1 
HETATM 15837 C  C7  . PG4   LA 4 .   ? -12.697 -12.017  -31.090 1.00 51.57 ? 202 PG4   L C7  1 
HETATM 15838 C  C8  . PG4   LA 4 .   ? -13.570 -12.345  -32.263 1.00 61.95 ? 202 PG4   L C8  1 
HETATM 15839 O  O5  . PG4   LA 4 .   ? -14.895 -12.646  -31.832 1.00 55.58 ? 202 PG4   L O5  1 
HETATM 15840 C  C13 . A1BYB MA 5 .   ? 13.457  6.749    -65.023 1.00 69.38 ? 203 A1BYB L C13 1 
HETATM 15841 C  C17 . A1BYB MA 5 .   ? 10.700  8.327    -58.299 1.00 53.77 ? 203 A1BYB L C17 1 
HETATM 15842 C  C02 . A1BYB MA 5 .   ? 6.904   6.345    -58.671 1.00 41.02 ? 203 A1BYB L C02 1 
HETATM 15843 C  C04 . A1BYB MA 5 .   ? 8.540   5.855    -60.347 1.00 51.71 ? 203 A1BYB L C04 1 
HETATM 15844 C  C05 . A1BYB MA 5 .   ? 9.150   6.842    -59.388 1.00 54.56 ? 203 A1BYB L C05 1 
HETATM 15845 C  C06 . A1BYB MA 5 .   ? 10.419  7.428    -59.376 1.00 60.87 ? 203 A1BYB L C06 1 
HETATM 15846 C  C08 . A1BYB MA 5 .   ? 12.445  8.000    -60.910 1.00 59.81 ? 203 A1BYB L C08 1 
HETATM 15847 C  C09 . A1BYB MA 5 .   ? 12.808  7.577    -62.333 1.00 72.49 ? 203 A1BYB L C09 1 
HETATM 15848 C  C10 . A1BYB MA 5 .   ? 13.324  6.303    -62.609 1.00 69.91 ? 203 A1BYB L C10 1 
HETATM 15849 C  C11 . A1BYB MA 5 .   ? 13.645  5.897    -63.918 1.00 85.43 ? 203 A1BYB L C11 1 
HETATM 15850 C  C14 . A1BYB MA 5 .   ? 12.926  8.026    -64.780 1.00 75.62 ? 203 A1BYB L C14 1 
HETATM 15851 C  C15 . A1BYB MA 5 .   ? 12.611  8.400    -63.457 1.00 77.92 ? 203 A1BYB L C15 1 
HETATM 15852 C  C18 . A1BYB MA 5 .   ? 9.748   8.613    -57.318 1.00 56.42 ? 203 A1BYB L C18 1 
HETATM 15853 C  C19 . A1BYB MA 5 .   ? 8.440   8.004    -57.348 1.00 53.22 ? 203 A1BYB L C19 1 
HETATM 15854 C  C20 . A1BYB MA 5 .   ? 8.176   7.129    -58.384 1.00 47.73 ? 203 A1BYB L C20 1 
HETATM 15855 N  N03 . A1BYB MA 5 .   ? 7.201   5.623    -59.862 1.00 52.30 ? 203 A1BYB L N03 1 
HETATM 15856 N  N07 . A1BYB MA 5 .   ? 11.420  7.144    -60.347 1.00 64.52 ? 203 A1BYB L N07 1 
HETATM 15857 O  O01 . A1BYB MA 5 .   ? 5.842   6.248    -58.133 1.00 37.42 ? 203 A1BYB L O01 1 
HETATM 15858 O  O16 . A1BYB MA 5 .   ? 12.080  9.667    -63.201 1.00 69.27 ? 203 A1BYB L O16 1 
HETATM 15859 O  O21 . A1BYB MA 5 .   ? 8.956   5.325    -61.333 1.00 54.14 ? 203 A1BYB L O21 1 
HETATM 15860 CL CL1 . A1BYB MA 5 .   ? 14.309  4.272    -64.173 1.00 77.70 ? 203 A1BYB L CL1 1 
HETATM 15861 O  O   . HOH   NA 6 .   ? 28.111  -21.350  -20.346 1.00 47.75 ? 301 HOH   A O   1 
HETATM 15862 O  O   . HOH   NA 6 .   ? 20.649  -28.159  -19.751 1.00 41.74 ? 302 HOH   A O   1 
HETATM 15863 O  O   . HOH   NA 6 .   ? 16.232  -27.658  -9.660  1.00 47.16 ? 303 HOH   A O   1 
HETATM 15864 O  O   . HOH   NA 6 .   ? 30.702  -7.791   -18.018 1.00 37.22 ? 304 HOH   A O   1 
HETATM 15865 O  O   . HOH   NA 6 .   ? 36.255  -23.484  -27.646 1.00 32.17 ? 305 HOH   A O   1 
HETATM 15866 O  O   . HOH   NA 6 .   ? 37.446  -19.347  -16.127 1.00 50.38 ? 306 HOH   A O   1 
HETATM 15867 O  O   . HOH   NA 6 .   ? 26.128  0.912    -20.341 1.00 43.18 ? 307 HOH   A O   1 
HETATM 15868 O  O   . HOH   NA 6 .   ? 14.073  -14.430  -29.778 1.00 41.22 ? 308 HOH   A O   1 
HETATM 15869 O  O   . HOH   NA 6 .   ? 25.183  -2.053   -31.474 1.00 35.59 ? 309 HOH   A O   1 
HETATM 15870 O  O   . HOH   NA 6 .   ? 14.952  1.465    -24.144 1.00 41.10 ? 310 HOH   A O   1 
HETATM 15871 O  O   . HOH   NA 6 .   ? 17.451  -25.479  -9.502  1.00 44.45 ? 311 HOH   A O   1 
HETATM 15872 O  O   . HOH   NA 6 .   ? 28.482  2.959    -25.837 1.00 42.87 ? 312 HOH   A O   1 
HETATM 15873 O  O   . HOH   NA 6 .   ? 29.200  -6.972   -41.892 1.00 45.43 ? 313 HOH   A O   1 
HETATM 15874 O  O   . HOH   NA 6 .   ? 16.913  -13.711  -15.677 1.00 28.21 ? 314 HOH   A O   1 
HETATM 15875 O  O   . HOH   NA 6 .   ? 35.181  -46.034  -14.697 1.00 34.99 ? 315 HOH   A O   1 
HETATM 15876 O  O   . HOH   NA 6 .   ? 27.098  -17.517  -41.090 1.00 31.20 ? 316 HOH   A O   1 
HETATM 15877 O  O   . HOH   NA 6 .   ? 27.225  -17.257  -22.199 1.00 40.66 ? 317 HOH   A O   1 
HETATM 15878 O  O   . HOH   NA 6 .   ? 27.528  -43.302  -2.719  1.00 38.09 ? 318 HOH   A O   1 
HETATM 15879 O  O   . HOH   NA 6 .   ? 35.632  -7.795   -24.901 1.00 42.08 ? 319 HOH   A O   1 
HETATM 15880 O  O   . HOH   NA 6 .   ? 29.431  -8.527   -20.267 1.00 33.02 ? 320 HOH   A O   1 
HETATM 15881 O  O   . HOH   NA 6 .   ? 26.103  -32.558  -4.282  1.00 37.44 ? 321 HOH   A O   1 
HETATM 15882 O  O   . HOH   NA 6 .   ? 28.667  -47.916  -19.122 1.00 40.39 ? 322 HOH   A O   1 
HETATM 15883 O  O   . HOH   NA 6 .   ? 22.043  -19.796  -29.893 1.00 42.83 ? 323 HOH   A O   1 
HETATM 15884 O  O   . HOH   NA 6 .   ? 31.858  -36.953  -7.422  1.00 30.71 ? 324 HOH   A O   1 
HETATM 15885 O  O   . HOH   NA 6 .   ? 35.950  -40.454  -24.190 1.00 25.12 ? 325 HOH   A O   1 
HETATM 15886 O  O   . HOH   NA 6 .   ? 24.476  -22.445  -34.913 1.00 44.93 ? 326 HOH   A O   1 
HETATM 15887 O  O   . HOH   NA 6 .   ? 28.513  -15.105  -20.941 1.00 32.97 ? 327 HOH   A O   1 
HETATM 15888 O  O   . HOH   NA 6 .   ? 28.790  -1.528   -20.364 1.00 45.38 ? 328 HOH   A O   1 
HETATM 15889 O  O   . HOH   NA 6 .   ? 27.773  -40.829  -24.367 1.00 37.56 ? 329 HOH   A O   1 
HETATM 15890 O  O   . HOH   NA 6 .   ? 40.270  -16.871  -17.463 1.00 47.78 ? 330 HOH   A O   1 
HETATM 15891 O  O   . HOH   NA 6 .   ? 27.125  -12.553  -39.971 1.00 27.76 ? 331 HOH   A O   1 
HETATM 15892 O  O   . HOH   NA 6 .   ? 37.839  -17.138  -23.534 1.00 32.78 ? 332 HOH   A O   1 
HETATM 15893 O  O   . HOH   NA 6 .   ? 23.891  -44.081  -3.489  1.00 25.74 ? 333 HOH   A O   1 
HETATM 15894 O  O   . HOH   NA 6 .   ? 39.818  -24.218  -28.499 1.00 30.62 ? 334 HOH   A O   1 
HETATM 15895 O  O   . HOH   NA 6 .   ? 35.810  -5.514   -32.983 1.00 40.48 ? 335 HOH   A O   1 
HETATM 15896 O  O   . HOH   NA 6 .   ? 29.873  -49.302  -1.740  1.00 44.66 ? 336 HOH   A O   1 
HETATM 15897 O  O   . HOH   NA 6 .   ? 14.894  -9.042   -23.378 1.00 34.52 ? 337 HOH   A O   1 
HETATM 15898 O  O   . HOH   NA 6 .   ? 26.859  -40.165  -1.402  1.00 35.09 ? 338 HOH   A O   1 
HETATM 15899 O  O   . HOH   NA 6 .   ? 23.230  -13.758  -35.051 1.00 34.93 ? 339 HOH   A O   1 
HETATM 15900 O  O   . HOH   NA 6 .   ? 22.396  -46.560  -16.195 1.00 34.23 ? 340 HOH   A O   1 
HETATM 15901 O  O   . HOH   NA 6 .   ? 15.103  -6.292   -26.855 1.00 28.39 ? 341 HOH   A O   1 
HETATM 15902 O  O   . HOH   NA 6 .   ? 25.510  -33.565  -32.900 1.00 48.89 ? 342 HOH   A O   1 
HETATM 15903 O  O   . HOH   NA 6 .   ? 14.083  -9.043   -25.775 1.00 48.88 ? 343 HOH   A O   1 
HETATM 15904 O  O   . HOH   NA 6 .   ? 33.041  -39.560  -10.271 1.00 29.61 ? 344 HOH   A O   1 
HETATM 15905 O  O   . HOH   NA 6 .   ? 19.940  -23.007  -27.143 1.00 48.19 ? 345 HOH   A O   1 
HETATM 15906 O  O   . HOH   NA 6 .   ? 33.301  -10.712  -15.329 1.00 52.49 ? 346 HOH   A O   1 
HETATM 15907 O  O   . HOH   NA 6 .   ? 39.990  -13.969  -33.521 1.00 35.33 ? 347 HOH   A O   1 
HETATM 15908 O  O   . HOH   NA 6 .   ? 15.728  -29.570  -2.265  1.00 55.20 ? 348 HOH   A O   1 
HETATM 15909 O  O   . HOH   NA 6 .   ? 28.287  -38.639  -26.129 1.00 30.94 ? 349 HOH   A O   1 
HETATM 15910 O  O   . HOH   NA 6 .   ? 41.277  -44.907  -19.647 1.00 43.85 ? 350 HOH   A O   1 
HETATM 15911 O  O   . HOH   NA 6 .   ? 28.763  -38.334  -28.465 1.00 49.97 ? 351 HOH   A O   1 
HETATM 15912 O  O   . HOH   NA 6 .   ? 26.341  -46.100  -0.647  1.00 51.18 ? 352 HOH   A O   1 
HETATM 15913 O  O   . HOH   NA 6 .   ? 35.712  -6.072   -29.114 1.00 41.75 ? 353 HOH   A O   1 
HETATM 15914 O  O   . HOH   NA 6 .   ? 23.908  -13.666  -12.288 1.00 47.04 ? 354 HOH   A O   1 
HETATM 15915 O  O   . HOH   NA 6 .   ? 24.540  -38.602  0.386   1.00 51.07 ? 355 HOH   A O   1 
HETATM 15916 O  O   . HOH   NA 6 .   ? 27.129  -48.146  -21.273 1.00 47.36 ? 356 HOH   A O   1 
HETATM 15917 O  O   . HOH   NA 6 .   ? 20.253  -18.507  -29.196 1.00 46.92 ? 357 HOH   A O   1 
HETATM 15918 O  O   . HOH   NA 6 .   ? 26.381  -29.840  -3.781  1.00 47.10 ? 358 HOH   A O   1 
HETATM 15919 O  O   . HOH   OA 6 .   ? -23.994 -16.694  -35.968 1.00 41.45 ? 301 HOH   B O   1 
HETATM 15920 O  O   . HOH   OA 6 .   ? 1.628   -26.447  -18.442 1.00 39.80 ? 302 HOH   B O   1 
HETATM 15921 O  O   . HOH   OA 6 .   ? 18.106  -3.449   -18.005 1.00 36.44 ? 303 HOH   B O   1 
HETATM 15922 O  O   . HOH   OA 6 .   ? 1.440   -4.059   -23.573 1.00 31.00 ? 304 HOH   B O   1 
HETATM 15923 O  O   . HOH   OA 6 .   ? -26.757 -28.936  -16.964 1.00 40.16 ? 305 HOH   B O   1 
HETATM 15924 O  O   . HOH   OA 6 .   ? -22.331 -5.044   -24.168 1.00 36.56 ? 306 HOH   B O   1 
HETATM 15925 O  O   . HOH   OA 6 .   ? 9.362   -15.849  -25.094 1.00 47.97 ? 307 HOH   B O   1 
HETATM 15926 O  O   . HOH   OA 6 .   ? -29.696 -26.592  -18.079 1.00 37.28 ? 308 HOH   B O   1 
HETATM 15927 O  O   . HOH   OA 6 .   ? -17.323 -0.362   -33.583 1.00 52.37 ? 309 HOH   B O   1 
HETATM 15928 O  O   . HOH   OA 6 .   ? -2.025  -12.981  -15.006 1.00 38.10 ? 310 HOH   B O   1 
HETATM 15929 O  O   . HOH   OA 6 .   ? -16.828 -6.643   -11.839 1.00 49.45 ? 311 HOH   B O   1 
HETATM 15930 O  O   . HOH   OA 6 .   ? -21.954 -27.408  -17.146 1.00 25.11 ? 312 HOH   B O   1 
HETATM 15931 O  O   . HOH   OA 6 .   ? 7.660   -28.980  -13.507 1.00 33.40 ? 313 HOH   B O   1 
HETATM 15932 O  O   . HOH   OA 6 .   ? -10.863 -4.457   -28.651 1.00 46.82 ? 314 HOH   B O   1 
HETATM 15933 O  O   . HOH   OA 6 .   ? -27.490 -25.606  -27.216 1.00 36.58 ? 315 HOH   B O   1 
HETATM 15934 O  O   . HOH   OA 6 .   ? -7.385  -22.107  -9.232  1.00 30.88 ? 316 HOH   B O   1 
HETATM 15935 O  O   . HOH   OA 6 .   ? 8.235   -3.646   -7.212  1.00 37.71 ? 317 HOH   B O   1 
HETATM 15936 O  O   . HOH   OA 6 .   ? 1.540   -5.276   -8.359  1.00 44.31 ? 318 HOH   B O   1 
HETATM 15937 O  O   . HOH   OA 6 .   ? 2.969   -11.889  -3.295  1.00 37.97 ? 319 HOH   B O   1 
HETATM 15938 O  O   . HOH   OA 6 .   ? 13.660  -9.628   -20.908 1.00 32.47 ? 320 HOH   B O   1 
HETATM 15939 O  O   . HOH   OA 6 .   ? 10.869  -25.601  -11.680 1.00 26.71 ? 321 HOH   B O   1 
HETATM 15940 O  O   . HOH   OA 6 .   ? -3.099  -4.816   -7.330  1.00 53.11 ? 322 HOH   B O   1 
HETATM 15941 O  O   . HOH   OA 6 .   ? 8.695   -21.332  -16.066 1.00 34.19 ? 323 HOH   B O   1 
HETATM 15942 O  O   . HOH   OA 6 .   ? -8.349  -29.716  -22.792 1.00 45.78 ? 324 HOH   B O   1 
HETATM 15943 O  O   . HOH   OA 6 .   ? 8.889   -17.584  -1.224  1.00 33.65 ? 325 HOH   B O   1 
HETATM 15944 O  O   . HOH   OA 6 .   ? -1.616  -10.776  -13.356 1.00 32.17 ? 326 HOH   B O   1 
HETATM 15945 O  O   . HOH   OA 6 .   ? -30.977 -22.155  -21.039 1.00 40.18 ? 327 HOH   B O   1 
HETATM 15946 O  O   . HOH   OA 6 .   ? 15.108  -12.765  -9.480  1.00 30.60 ? 328 HOH   B O   1 
HETATM 15947 O  O   . HOH   OA 6 .   ? 2.656   -7.166   -9.542  1.00 29.82 ? 329 HOH   B O   1 
HETATM 15948 O  O   . HOH   OA 6 .   ? -26.543 -10.844  -20.646 1.00 33.66 ? 330 HOH   B O   1 
HETATM 15949 O  O   . HOH   OA 6 .   ? -5.582  -15.562  -5.429  1.00 30.00 ? 331 HOH   B O   1 
HETATM 15950 O  O   . HOH   OA 6 .   ? -18.955 -26.529  -24.827 1.00 34.05 ? 332 HOH   B O   1 
HETATM 15951 O  O   . HOH   OA 6 .   ? -9.598  -10.701  -3.384  1.00 47.37 ? 333 HOH   B O   1 
HETATM 15952 O  O   . HOH   OA 6 .   ? -19.998 -28.221  -18.972 1.00 28.94 ? 334 HOH   B O   1 
HETATM 15953 O  O   . HOH   OA 6 .   ? 10.026  -8.015   -22.672 1.00 38.47 ? 335 HOH   B O   1 
HETATM 15954 O  O   . HOH   OA 6 .   ? 14.522  -5.995   -5.033  1.00 38.86 ? 336 HOH   B O   1 
HETATM 15955 O  O   . HOH   OA 6 .   ? 16.139  -9.985   -2.722  1.00 37.17 ? 337 HOH   B O   1 
HETATM 15956 O  O   . HOH   OA 6 .   ? -30.754 -9.654   -31.366 1.00 36.15 ? 338 HOH   B O   1 
HETATM 15957 O  O   . HOH   OA 6 .   ? -25.249 -21.381  -32.531 1.00 32.22 ? 339 HOH   B O   1 
HETATM 15958 O  O   . HOH   OA 6 .   ? -15.271 -17.144  -23.709 1.00 45.58 ? 340 HOH   B O   1 
HETATM 15959 O  O   . HOH   OA 6 .   ? -6.692  -13.531  -16.649 1.00 44.47 ? 341 HOH   B O   1 
HETATM 15960 O  O   . HOH   OA 6 .   ? -4.877  -13.687  -15.098 1.00 45.04 ? 342 HOH   B O   1 
HETATM 15961 O  O   . HOH   OA 6 .   ? 4.388   -18.280  -0.456  1.00 48.90 ? 343 HOH   B O   1 
HETATM 15962 O  O   . HOH   OA 6 .   ? -16.688 -24.507  -30.380 1.00 53.44 ? 344 HOH   B O   1 
HETATM 15963 O  O   . HOH   OA 6 .   ? 11.554  -9.786   -22.956 1.00 40.42 ? 345 HOH   B O   1 
HETATM 15964 O  O   . HOH   OA 6 .   ? -8.992  -23.578  -6.277  1.00 28.16 ? 346 HOH   B O   1 
HETATM 15965 O  O   . HOH   OA 6 .   ? 11.775  -23.750  -3.363  1.00 44.62 ? 347 HOH   B O   1 
HETATM 15966 O  O   . HOH   OA 6 .   ? -32.015 -8.840   -28.087 1.00 38.86 ? 348 HOH   B O   1 
HETATM 15967 O  O   . HOH   OA 6 .   ? -1.551  -18.701  -24.012 1.00 52.28 ? 349 HOH   B O   1 
HETATM 15968 O  O   . HOH   OA 6 .   ? -2.756  -11.882  -6.100  1.00 47.46 ? 350 HOH   B O   1 
HETATM 15969 O  O   . HOH   OA 6 .   ? 6.248   -14.417  -2.088  1.00 41.48 ? 351 HOH   B O   1 
HETATM 15970 O  O   . HOH   OA 6 .   ? -26.115 -2.188   -34.971 1.00 48.01 ? 352 HOH   B O   1 
HETATM 15971 O  O   . HOH   OA 6 .   ? -27.360 -14.660  -20.440 1.00 25.12 ? 353 HOH   B O   1 
HETATM 15972 O  O   . HOH   OA 6 .   ? 2.968   -15.440  -0.920  1.00 46.62 ? 354 HOH   B O   1 
HETATM 15973 O  O   . HOH   OA 6 .   ? 14.208  -8.005   -3.167  1.00 40.80 ? 355 HOH   B O   1 
HETATM 15974 O  O   . HOH   OA 6 .   ? -29.842 -6.071   -27.119 1.00 46.05 ? 356 HOH   B O   1 
HETATM 15975 O  O   . HOH   OA 6 .   ? -7.820  -18.993  0.619   1.00 44.18 ? 357 HOH   B O   1 
HETATM 15976 O  O   . HOH   OA 6 .   ? -16.421 -27.224  -22.985 1.00 35.48 ? 358 HOH   B O   1 
HETATM 15977 O  O   . HOH   OA 6 .   ? -30.043 -26.920  -14.694 1.00 44.32 ? 359 HOH   B O   1 
HETATM 15978 O  O   . HOH   OA 6 .   ? -18.986 -12.542  -7.306  1.00 46.22 ? 360 HOH   B O   1 
HETATM 15979 O  O   . HOH   OA 6 .   ? -5.939  -24.208  -24.573 1.00 52.41 ? 361 HOH   B O   1 
HETATM 15980 O  O   . HOH   OA 6 .   ? -15.132 -29.036  -22.508 1.00 46.39 ? 362 HOH   B O   1 
HETATM 15981 O  O   . HOH   OA 6 .   ? 20.334  -1.014   -14.454 1.00 53.44 ? 363 HOH   B O   1 
HETATM 15982 O  O   . HOH   OA 6 .   ? -25.807 -27.445  -28.541 1.00 49.73 ? 364 HOH   B O   1 
HETATM 15983 O  O   . HOH   OA 6 .   ? -4.986  -12.715  -4.609  1.00 48.83 ? 365 HOH   B O   1 
HETATM 15984 O  O   . HOH   PA 6 .   ? -43.910 -46.517  -8.865  1.00 35.73 ? 301 HOH   C O   1 
HETATM 15985 O  O   . HOH   PA 6 .   ? -24.073 -50.503  -15.945 1.00 46.29 ? 302 HOH   C O   1 
HETATM 15986 O  O   . HOH   PA 6 .   ? -29.170 -41.512  -23.230 1.00 47.66 ? 303 HOH   C O   1 
HETATM 15987 O  O   . HOH   PA 6 .   ? -44.823 -29.647  -44.076 1.00 41.60 ? 304 HOH   C O   1 
HETATM 15988 O  O   . HOH   PA 6 .   ? -30.532 -39.262  -9.453  1.00 24.70 ? 305 HOH   C O   1 
HETATM 15989 O  O   . HOH   PA 6 .   ? -38.941 -42.517  -20.220 1.00 46.59 ? 306 HOH   C O   1 
HETATM 15990 O  O   . HOH   PA 6 .   ? -30.768 -36.017  -24.495 1.00 44.61 ? 307 HOH   C O   1 
HETATM 15991 O  O   . HOH   PA 6 .   ? -28.577 -53.944  0.143   1.00 41.10 ? 308 HOH   C O   1 
HETATM 15992 O  O   . HOH   PA 6 .   ? -39.430 -21.488  -22.353 1.00 34.73 ? 309 HOH   C O   1 
HETATM 15993 O  O   . HOH   PA 6 .   ? -28.948 -44.293  -23.174 1.00 48.12 ? 310 HOH   C O   1 
HETATM 15994 O  O   . HOH   PA 6 .   ? -41.295 -58.163  -2.647  1.00 42.52 ? 311 HOH   C O   1 
HETATM 15995 O  O   . HOH   PA 6 .   ? -53.425 -55.226  -17.938 1.00 54.56 ? 312 HOH   C O   1 
HETATM 15996 O  O   . HOH   PA 6 .   ? -25.857 -50.015  -9.460  1.00 42.68 ? 313 HOH   C O   1 
HETATM 15997 O  O   . HOH   PA 6 .   ? -34.160 -62.224  -21.800 1.00 31.36 ? 314 HOH   C O   1 
HETATM 15998 O  O   . HOH   PA 6 .   ? -35.705 -26.883  -42.731 1.00 35.85 ? 315 HOH   C O   1 
HETATM 15999 O  O   . HOH   PA 6 .   ? -29.560 -50.617  1.023   1.00 39.63 ? 316 HOH   C O   1 
HETATM 16000 O  O   . HOH   PA 6 .   ? -34.059 -24.700  -45.703 1.00 44.05 ? 317 HOH   C O   1 
HETATM 16001 O  O   . HOH   PA 6 .   ? -31.695 -52.638  -27.808 1.00 36.48 ? 318 HOH   C O   1 
HETATM 16002 O  O   . HOH   PA 6 .   ? -41.996 -47.838  -10.240 1.00 31.87 ? 319 HOH   C O   1 
HETATM 16003 O  O   . HOH   PA 6 .   ? -23.294 -49.422  -13.588 1.00 35.47 ? 320 HOH   C O   1 
HETATM 16004 O  O   . HOH   PA 6 .   ? -38.184 -44.877  -18.038 1.00 40.10 ? 321 HOH   C O   1 
HETATM 16005 O  O   . HOH   PA 6 .   ? -48.107 -47.517  -21.076 1.00 34.13 ? 322 HOH   C O   1 
HETATM 16006 O  O   . HOH   PA 6 .   ? -43.359 -25.178  -41.488 1.00 40.04 ? 323 HOH   C O   1 
HETATM 16007 O  O   . HOH   PA 6 .   ? -32.258 -12.184  -23.727 1.00 49.74 ? 324 HOH   C O   1 
HETATM 16008 O  O   . HOH   PA 6 .   ? -44.407 -47.765  -27.864 1.00 36.25 ? 325 HOH   C O   1 
HETATM 16009 O  O   . HOH   PA 6 .   ? -42.619 -50.933  -4.042  1.00 47.81 ? 326 HOH   C O   1 
HETATM 16010 O  O   . HOH   PA 6 .   ? -39.918 -15.116  -27.637 1.00 43.19 ? 327 HOH   C O   1 
HETATM 16011 O  O   . HOH   PA 6 .   ? -34.525 -34.465  -39.195 1.00 42.38 ? 328 HOH   C O   1 
HETATM 16012 O  O   . HOH   PA 6 .   ? -42.447 -36.137  -40.805 1.00 28.10 ? 329 HOH   C O   1 
HETATM 16013 O  O   . HOH   PA 6 .   ? -36.148 -60.006  -8.670  1.00 33.16 ? 330 HOH   C O   1 
HETATM 16014 O  O   . HOH   PA 6 .   ? -43.628 -22.789  -29.302 1.00 33.56 ? 331 HOH   C O   1 
HETATM 16015 O  O   . HOH   PA 6 .   ? -31.835 -29.785  -30.546 1.00 46.12 ? 332 HOH   C O   1 
HETATM 16016 O  O   . HOH   PA 6 .   ? -26.984 -52.387  -7.729  1.00 29.52 ? 333 HOH   C O   1 
HETATM 16017 O  O   . HOH   PA 6 .   ? -39.752 -14.553  -31.239 1.00 36.55 ? 334 HOH   C O   1 
HETATM 16018 O  O   . HOH   PA 6 .   ? -30.823 -24.090  -38.425 1.00 37.48 ? 335 HOH   C O   1 
HETATM 16019 O  O   . HOH   PA 6 .   ? -39.998 -44.796  -15.736 1.00 33.07 ? 336 HOH   C O   1 
HETATM 16020 O  O   . HOH   PA 6 .   ? -47.254 -51.315  -17.657 1.00 40.06 ? 337 HOH   C O   1 
HETATM 16021 O  O   . HOH   PA 6 .   ? -31.299 -55.855  3.435   1.00 41.29 ? 338 HOH   C O   1 
HETATM 16022 O  O   . HOH   PA 6 .   ? -27.001 -48.240  -8.486  1.00 35.14 ? 339 HOH   C O   1 
HETATM 16023 O  O   . HOH   PA 6 .   ? -45.429 -61.593  -14.901 1.00 35.27 ? 340 HOH   C O   1 
HETATM 16024 O  O   . HOH   PA 6 .   ? -33.366 -60.934  -26.503 1.00 36.22 ? 341 HOH   C O   1 
HETATM 16025 O  O   . HOH   PA 6 .   ? -36.027 -14.451  -31.337 1.00 30.10 ? 342 HOH   C O   1 
HETATM 16026 O  O   . HOH   PA 6 .   ? -35.813 -24.022  -18.011 1.00 39.58 ? 343 HOH   C O   1 
HETATM 16027 O  O   . HOH   PA 6 .   ? -31.577 -56.718  -19.793 1.00 38.99 ? 344 HOH   C O   1 
HETATM 16028 O  O   . HOH   PA 6 .   ? -30.379 -56.364  -26.777 1.00 45.22 ? 345 HOH   C O   1 
HETATM 16029 O  O   . HOH   PA 6 .   ? -46.649 -47.270  -16.479 1.00 46.28 ? 346 HOH   C O   1 
HETATM 16030 O  O   . HOH   PA 6 .   ? -43.691 -24.097  -33.022 1.00 28.63 ? 347 HOH   C O   1 
HETATM 16031 O  O   . HOH   PA 6 .   ? -43.030 -59.706  -4.526  1.00 40.29 ? 348 HOH   C O   1 
HETATM 16032 O  O   . HOH   PA 6 .   ? -38.034 -37.704  -9.515  1.00 43.93 ? 349 HOH   C O   1 
HETATM 16033 O  O   . HOH   PA 6 .   ? -47.478 -48.633  -29.850 1.00 36.16 ? 350 HOH   C O   1 
HETATM 16034 O  O   . HOH   PA 6 .   ? -43.483 -24.566  -20.895 1.00 50.10 ? 351 HOH   C O   1 
HETATM 16035 O  O   . HOH   PA 6 .   ? -48.973 -30.752  -37.879 1.00 46.33 ? 352 HOH   C O   1 
HETATM 16036 O  O   . HOH   PA 6 .   ? -31.210 -45.494  -35.863 1.00 40.06 ? 353 HOH   C O   1 
HETATM 16037 O  O   . HOH   PA 6 .   ? -53.919 -49.707  -24.509 1.00 46.38 ? 354 HOH   C O   1 
HETATM 16038 O  O   . HOH   PA 6 .   ? -34.353 -26.989  -46.343 1.00 53.69 ? 355 HOH   C O   1 
HETATM 16039 O  O   . HOH   PA 6 .   ? -28.847 -46.904  -24.820 1.00 54.38 ? 356 HOH   C O   1 
HETATM 16040 O  O   . HOH   QA 6 .   ? 1.171   -86.978  -37.645 1.00 48.78 ? 301 HOH   D O   1 
HETATM 16041 O  O   . HOH   QA 6 .   ? 18.819  -96.908  -21.938 1.00 41.61 ? 302 HOH   D O   1 
HETATM 16042 O  O   . HOH   QA 6 .   ? -16.916 -84.830  -36.236 1.00 42.32 ? 303 HOH   D O   1 
HETATM 16043 O  O   . HOH   QA 6 .   ? 1.699   -94.236  -24.356 1.00 33.23 ? 304 HOH   D O   1 
HETATM 16044 O  O   . HOH   QA 6 .   ? 10.390  -85.827  -29.306 1.00 44.59 ? 305 HOH   D O   1 
HETATM 16045 O  O   . HOH   QA 6 .   ? 12.475  -107.246 -29.806 1.00 51.29 ? 306 HOH   D O   1 
HETATM 16046 O  O   . HOH   QA 6 .   ? 6.239   -87.627  -45.438 1.00 46.79 ? 307 HOH   D O   1 
HETATM 16047 O  O   . HOH   QA 6 .   ? -0.306  -98.804  -48.452 1.00 47.92 ? 308 HOH   D O   1 
HETATM 16048 O  O   . HOH   QA 6 .   ? -3.802  -83.335  -49.470 1.00 49.86 ? 309 HOH   D O   1 
HETATM 16049 O  O   . HOH   QA 6 .   ? 1.842   -97.582  -36.729 1.00 45.92 ? 310 HOH   D O   1 
HETATM 16050 O  O   . HOH   QA 6 .   ? 1.652   -105.016 -44.040 1.00 44.79 ? 311 HOH   D O   1 
HETATM 16051 O  O   . HOH   QA 6 .   ? -23.315 -82.214  -41.833 1.00 40.37 ? 312 HOH   D O   1 
HETATM 16052 O  O   . HOH   QA 6 .   ? -23.266 -84.695  -48.640 1.00 44.78 ? 313 HOH   D O   1 
HETATM 16053 O  O   . HOH   QA 6 .   ? 17.020  -105.212 -44.119 1.00 50.25 ? 314 HOH   D O   1 
HETATM 16054 O  O   . HOH   QA 6 .   ? -23.181 -97.639  -38.660 1.00 42.72 ? 315 HOH   D O   1 
HETATM 16055 O  O   . HOH   QA 6 .   ? 10.613  -103.973 -50.693 1.00 48.66 ? 316 HOH   D O   1 
HETATM 16056 O  O   . HOH   QA 6 .   ? -25.849 -92.142  -49.589 1.00 47.11 ? 317 HOH   D O   1 
HETATM 16057 O  O   . HOH   QA 6 .   ? -1.058  -100.746 -51.707 1.00 43.91 ? 318 HOH   D O   1 
HETATM 16058 O  O   . HOH   QA 6 .   ? -0.819  -97.517  -37.822 1.00 48.90 ? 319 HOH   D O   1 
HETATM 16059 O  O   . HOH   QA 6 .   ? -15.661 -91.494  -53.451 1.00 34.55 ? 320 HOH   D O   1 
HETATM 16060 O  O   . HOH   QA 6 .   ? -12.419 -105.730 -36.971 1.00 53.91 ? 321 HOH   D O   1 
HETATM 16061 O  O   . HOH   QA 6 .   ? 13.968  -89.439  -48.629 1.00 34.99 ? 322 HOH   D O   1 
HETATM 16062 O  O   . HOH   QA 6 .   ? 2.740   -100.170 -35.669 1.00 42.57 ? 323 HOH   D O   1 
HETATM 16063 O  O   . HOH   QA 6 .   ? -17.775 -85.725  -34.058 1.00 49.76 ? 324 HOH   D O   1 
HETATM 16064 O  O   . HOH   QA 6 .   ? 19.774  -99.713  -34.629 1.00 39.12 ? 325 HOH   D O   1 
HETATM 16065 O  O   . HOH   QA 6 .   ? 19.108  -107.172 -31.128 1.00 49.26 ? 326 HOH   D O   1 
HETATM 16066 O  O   . HOH   QA 6 .   ? -14.692 -84.956  -48.430 1.00 40.92 ? 327 HOH   D O   1 
HETATM 16067 O  O   . HOH   QA 6 .   ? 15.016  -91.965  -27.023 1.00 41.91 ? 328 HOH   D O   1 
HETATM 16068 O  O   . HOH   QA 6 .   ? -30.261 -89.875  -34.102 1.00 40.32 ? 329 HOH   D O   1 
HETATM 16069 O  O   . HOH   QA 6 .   ? -29.149 -94.664  -32.648 1.00 47.11 ? 330 HOH   D O   1 
HETATM 16070 O  O   . HOH   QA 6 .   ? -23.332 -95.970  -42.448 1.00 41.68 ? 331 HOH   D O   1 
HETATM 16071 O  O   . HOH   QA 6 .   ? 10.300  -86.823  -45.037 1.00 55.15 ? 332 HOH   D O   1 
HETATM 16072 O  O   . HOH   QA 6 .   ? 1.364   -108.276 -33.296 1.00 56.31 ? 333 HOH   D O   1 
HETATM 16073 O  O   . HOH   QA 6 .   ? -4.523  -106.597 -39.888 1.00 50.27 ? 334 HOH   D O   1 
HETATM 16074 O  O   . HOH   QA 6 .   ? -7.809  -87.195  -35.286 1.00 48.08 ? 335 HOH   D O   1 
HETATM 16075 O  O   . HOH   QA 6 .   ? -11.414 -91.524  -25.578 1.00 50.81 ? 336 HOH   D O   1 
HETATM 16076 O  O   . HOH   QA 6 .   ? -13.429 -83.318  -41.490 1.00 44.54 ? 337 HOH   D O   1 
HETATM 16077 O  O   . HOH   QA 6 .   ? -31.002 -93.035  -35.325 1.00 48.84 ? 338 HOH   D O   1 
HETATM 16078 O  O   . HOH   QA 6 .   ? -18.548 -101.306 -32.609 1.00 51.73 ? 339 HOH   D O   1 
HETATM 16079 O  O   . HOH   QA 6 .   ? -19.979 -90.839  -21.005 1.00 48.18 ? 340 HOH   D O   1 
HETATM 16080 O  O   . HOH   QA 6 .   ? 12.033  -90.644  -26.832 1.00 53.70 ? 341 HOH   D O   1 
HETATM 16081 O  O   . HOH   QA 6 .   ? -3.035  -83.868  -44.284 1.00 58.08 ? 342 HOH   D O   1 
HETATM 16082 O  O   . HOH   RA 6 .   ? -19.107 -34.943  5.259   1.00 37.45 ? 301 HOH   E O   1 
HETATM 16083 O  O   . HOH   RA 6 .   ? -20.961 -27.840  1.431   1.00 36.57 ? 302 HOH   E O   1 
HETATM 16084 O  O   . HOH   RA 6 .   ? 7.709   -45.095  4.411   1.00 33.97 ? 303 HOH   E O   1 
HETATM 16085 O  O   . HOH   RA 6 .   ? -32.610 -47.005  -2.152  1.00 29.74 ? 304 HOH   E O   1 
HETATM 16086 O  O   . HOH   RA 6 .   ? -20.636 -45.078  -13.532 1.00 34.83 ? 305 HOH   E O   1 
HETATM 16087 O  O   . HOH   RA 6 .   ? -24.315 -38.888  5.361   1.00 42.00 ? 306 HOH   E O   1 
HETATM 16088 O  O   . HOH   RA 6 .   ? -15.161 -48.581  -0.642  1.00 22.50 ? 307 HOH   E O   1 
HETATM 16089 O  O   . HOH   RA 6 .   ? -3.579  -45.888  5.073   1.00 46.64 ? 308 HOH   E O   1 
HETATM 16090 O  O   . HOH   RA 6 .   ? -13.478 -33.175  -17.357 1.00 37.89 ? 309 HOH   E O   1 
HETATM 16091 O  O   . HOH   RA 6 .   ? 3.995   -54.053  3.319   1.00 53.41 ? 310 HOH   E O   1 
HETATM 16092 O  O   . HOH   RA 6 .   ? -27.258 -22.959  -10.681 1.00 39.83 ? 311 HOH   E O   1 
HETATM 16093 O  O   . HOH   RA 6 .   ? -19.190 -30.586  7.137   1.00 51.94 ? 312 HOH   E O   1 
HETATM 16094 O  O   . HOH   RA 6 .   ? -9.912  -35.793  -3.558  1.00 43.74 ? 313 HOH   E O   1 
HETATM 16095 O  O   . HOH   RA 6 .   ? 6.991   -46.156  -9.319  1.00 33.82 ? 314 HOH   E O   1 
HETATM 16096 O  O   . HOH   RA 6 .   ? -12.904 -36.303  -3.689  1.00 36.67 ? 315 HOH   E O   1 
HETATM 16097 O  O   . HOH   RA 6 .   ? -21.216 -47.385  -12.229 1.00 44.66 ? 316 HOH   E O   1 
HETATM 16098 O  O   . HOH   RA 6 .   ? -2.886  -43.693  -8.828  1.00 48.53 ? 317 HOH   E O   1 
HETATM 16099 O  O   . HOH   RA 6 .   ? 17.632  -32.419  -6.404  1.00 36.63 ? 318 HOH   E O   1 
HETATM 16100 O  O   . HOH   RA 6 .   ? -19.453 -35.412  2.635   1.00 27.70 ? 319 HOH   E O   1 
HETATM 16101 O  O   . HOH   RA 6 .   ? 16.389  -36.335  -13.206 1.00 39.08 ? 320 HOH   E O   1 
HETATM 16102 O  O   . HOH   RA 6 .   ? -11.466 -26.339  -0.409  1.00 26.00 ? 321 HOH   E O   1 
HETATM 16103 O  O   . HOH   RA 6 .   ? 15.072  -43.255  -12.622 1.00 35.71 ? 322 HOH   E O   1 
HETATM 16104 O  O   . HOH   RA 6 .   ? -17.131 -32.335  -19.319 1.00 49.57 ? 323 HOH   E O   1 
HETATM 16105 O  O   . HOH   RA 6 .   ? -26.283 -23.832  -4.194  1.00 36.00 ? 324 HOH   E O   1 
HETATM 16106 O  O   . HOH   RA 6 .   ? -14.482 -37.755  -12.771 1.00 43.13 ? 325 HOH   E O   1 
HETATM 16107 O  O   . HOH   RA 6 .   ? -33.148 -45.137  -0.282  1.00 41.45 ? 326 HOH   E O   1 
HETATM 16108 O  O   . HOH   RA 6 .   ? -11.528 -33.135  -19.541 1.00 50.10 ? 327 HOH   E O   1 
HETATM 16109 O  O   . HOH   RA 6 .   ? 8.944   -27.618  -11.478 1.00 26.06 ? 328 HOH   E O   1 
HETATM 16110 O  O   . HOH   RA 6 .   ? 14.456  -54.715  2.915   1.00 46.51 ? 329 HOH   E O   1 
HETATM 16111 O  O   . HOH   RA 6 .   ? 8.044   -35.044  -15.030 1.00 36.48 ? 330 HOH   E O   1 
HETATM 16112 O  O   . HOH   RA 6 .   ? -24.079 -28.768  -16.024 1.00 28.91 ? 331 HOH   E O   1 
HETATM 16113 O  O   . HOH   RA 6 .   ? -14.067 -35.903  -1.020  1.00 28.02 ? 332 HOH   E O   1 
HETATM 16114 O  O   . HOH   RA 6 .   ? -30.632 -34.223  -5.487  1.00 28.47 ? 333 HOH   E O   1 
HETATM 16115 O  O   . HOH   RA 6 .   ? 18.535  -44.682  1.831   1.00 36.69 ? 334 HOH   E O   1 
HETATM 16116 O  O   . HOH   RA 6 .   ? -12.770 -43.896  4.526   1.00 42.75 ? 335 HOH   E O   1 
HETATM 16117 O  O   . HOH   RA 6 .   ? 18.220  -47.542  -0.578  1.00 26.54 ? 336 HOH   E O   1 
HETATM 16118 O  O   . HOH   RA 6 .   ? -24.216 -46.431  -8.111  1.00 42.74 ? 337 HOH   E O   1 
HETATM 16119 O  O   . HOH   RA 6 .   ? 2.741   -39.425  -7.503  1.00 41.48 ? 338 HOH   E O   1 
HETATM 16120 O  O   . HOH   RA 6 .   ? -30.723 -48.194  0.569   1.00 44.77 ? 339 HOH   E O   1 
HETATM 16121 O  O   . HOH   RA 6 .   ? -2.230  -50.901  -0.293  1.00 38.70 ? 340 HOH   E O   1 
HETATM 16122 O  O   . HOH   RA 6 .   ? -7.157  -29.856  4.599   1.00 44.63 ? 341 HOH   E O   1 
HETATM 16123 O  O   . HOH   RA 6 .   ? -14.217 -34.083  6.893   1.00 54.16 ? 342 HOH   E O   1 
HETATM 16124 O  O   . HOH   RA 6 .   ? -34.040 -29.943  -0.671  1.00 34.19 ? 343 HOH   E O   1 
HETATM 16125 O  O   . HOH   RA 6 .   ? -7.925  -25.744  -7.066  1.00 33.14 ? 344 HOH   E O   1 
HETATM 16126 O  O   . HOH   RA 6 .   ? 5.244   -41.563  -13.713 1.00 41.26 ? 345 HOH   E O   1 
HETATM 16127 O  O   . HOH   RA 6 .   ? -21.474 -34.627  -14.072 1.00 33.55 ? 346 HOH   E O   1 
HETATM 16128 O  O   . HOH   RA 6 .   ? -26.667 -45.481  -7.498  1.00 27.62 ? 347 HOH   E O   1 
HETATM 16129 O  O   . HOH   RA 6 .   ? -24.041 -25.703  -1.274  1.00 40.13 ? 348 HOH   E O   1 
HETATM 16130 O  O   . HOH   RA 6 .   ? 11.840  -38.399  2.133   1.00 25.74 ? 349 HOH   E O   1 
HETATM 16131 O  O   . HOH   RA 6 .   ? -11.162 -40.991  -12.884 1.00 47.83 ? 350 HOH   E O   1 
HETATM 16132 O  O   . HOH   RA 6 .   ? 13.118  -36.025  -0.842  1.00 25.34 ? 351 HOH   E O   1 
HETATM 16133 O  O   . HOH   RA 6 .   ? -9.197  -26.934  5.605   1.00 40.61 ? 352 HOH   E O   1 
HETATM 16134 O  O   . HOH   RA 6 .   ? -16.743 -26.153  -0.268  1.00 44.02 ? 353 HOH   E O   1 
HETATM 16135 O  O   . HOH   RA 6 .   ? -32.131 -31.047  1.699   1.00 36.49 ? 354 HOH   E O   1 
HETATM 16136 O  O   . HOH   RA 6 .   ? -6.839  -22.245  -6.611  1.00 30.10 ? 355 HOH   E O   1 
HETATM 16137 O  O   . HOH   RA 6 .   ? -22.931 -47.225  -6.182  1.00 32.63 ? 356 HOH   E O   1 
HETATM 16138 O  O   . HOH   RA 6 .   ? -20.985 -23.416  -0.528  1.00 43.45 ? 357 HOH   E O   1 
HETATM 16139 O  O   . HOH   RA 6 .   ? -27.372 -26.140  -1.128  1.00 46.28 ? 358 HOH   E O   1 
HETATM 16140 O  O   . HOH   RA 6 .   ? -10.517 -19.310  0.370   1.00 43.32 ? 359 HOH   E O   1 
HETATM 16141 O  O   . HOH   RA 6 .   ? -3.042  -41.304  -11.674 1.00 54.60 ? 360 HOH   E O   1 
HETATM 16142 O  O   . HOH   RA 6 .   ? -36.540 -37.989  -1.763  1.00 47.59 ? 361 HOH   E O   1 
HETATM 16143 O  O   . HOH   RA 6 .   ? 5.302   -33.607  -15.325 1.00 38.00 ? 362 HOH   E O   1 
HETATM 16144 O  O   . HOH   RA 6 .   ? -27.841 -44.946  2.856   1.00 40.83 ? 363 HOH   E O   1 
HETATM 16145 O  O   . HOH   RA 6 .   ? 15.275  -37.066  -15.673 1.00 47.67 ? 364 HOH   E O   1 
HETATM 16146 O  O   . HOH   RA 6 .   ? -15.607 -39.661  -12.371 1.00 40.28 ? 365 HOH   E O   1 
HETATM 16147 O  O   . HOH   RA 6 .   ? -28.569 -25.012  -2.880  1.00 44.02 ? 366 HOH   E O   1 
HETATM 16148 O  O   . HOH   SA 6 .   ? -9.582  -87.471  -24.479 1.00 43.29 ? 301 HOH   F O   1 
HETATM 16149 O  O   . HOH   SA 6 .   ? -39.673 -72.521  -21.600 1.00 55.37 ? 302 HOH   F O   1 
HETATM 16150 O  O   . HOH   SA 6 .   ? -23.888 -69.749  1.779   1.00 51.85 ? 303 HOH   F O   1 
HETATM 16151 O  O   . HOH   SA 6 .   ? -18.042 -51.524  -12.258 1.00 46.12 ? 304 HOH   F O   1 
HETATM 16152 O  O   . HOH   SA 6 .   ? -22.606 -67.530  -19.895 1.00 43.85 ? 305 HOH   F O   1 
HETATM 16153 O  O   . HOH   SA 6 .   ? -23.113 -65.454  3.246   1.00 39.71 ? 306 HOH   F O   1 
HETATM 16154 O  O   . HOH   SA 6 .   ? -29.783 -59.153  -9.171  1.00 24.71 ? 307 HOH   F O   1 
HETATM 16155 O  O   . HOH   SA 6 .   ? -25.289 -46.426  2.142   1.00 33.26 ? 308 HOH   F O   1 
HETATM 16156 O  O   . HOH   SA 6 .   ? -19.048 -66.094  -7.224  1.00 42.90 ? 309 HOH   F O   1 
HETATM 16157 O  O   . HOH   SA 6 .   ? -32.765 -72.064  -12.075 1.00 53.29 ? 310 HOH   F O   1 
HETATM 16158 O  O   . HOH   SA 6 .   ? -13.289 -90.127  -25.575 1.00 45.02 ? 311 HOH   F O   1 
HETATM 16159 O  O   . HOH   SA 6 .   ? -40.660 -80.039  -28.657 1.00 46.98 ? 312 HOH   F O   1 
HETATM 16160 O  O   . HOH   SA 6 .   ? -13.826 -73.203  -1.649  1.00 32.50 ? 313 HOH   F O   1 
HETATM 16161 O  O   . HOH   SA 6 .   ? -20.586 -50.409  -11.968 1.00 38.23 ? 314 HOH   F O   1 
HETATM 16162 O  O   . HOH   SA 6 .   ? -33.692 -80.543  -19.020 1.00 35.37 ? 315 HOH   F O   1 
HETATM 16163 O  O   . HOH   SA 6 .   ? -21.610 -64.134  1.536   1.00 32.31 ? 316 HOH   F O   1 
HETATM 16164 O  O   . HOH   SA 6 .   ? -18.689 -54.958  10.324  1.00 39.94 ? 317 HOH   F O   1 
HETATM 16165 O  O   . HOH   SA 6 .   ? -7.934  -68.735  -22.745 1.00 43.50 ? 318 HOH   F O   1 
HETATM 16166 O  O   . HOH   SA 6 .   ? -27.419 -51.757  10.056  1.00 41.96 ? 319 HOH   F O   1 
HETATM 16167 O  O   . HOH   SA 6 .   ? -16.971 -61.167  -16.219 1.00 51.98 ? 320 HOH   F O   1 
HETATM 16168 O  O   . HOH   SA 6 .   ? -16.961 -83.806  -32.045 1.00 42.54 ? 321 HOH   F O   1 
HETATM 16169 O  O   . HOH   SA 6 .   ? -20.413 -66.208  -4.575  1.00 32.87 ? 322 HOH   F O   1 
HETATM 16170 O  O   . HOH   SA 6 .   ? -18.184 -89.793  -26.890 1.00 46.94 ? 323 HOH   F O   1 
HETATM 16171 O  O   . HOH   SA 6 .   ? -10.379 -83.418  -22.422 1.00 33.25 ? 324 HOH   F O   1 
HETATM 16172 O  O   . HOH   SA 6 .   ? -38.398 -85.052  -20.146 1.00 49.03 ? 325 HOH   F O   1 
HETATM 16173 O  O   . HOH   SA 6 .   ? -13.584 -77.434  -27.196 1.00 39.30 ? 326 HOH   F O   1 
HETATM 16174 O  O   . HOH   SA 6 .   ? -2.234  -57.906  -8.777  1.00 32.02 ? 327 HOH   F O   1 
HETATM 16175 O  O   . HOH   SA 6 .   ? -9.621  -73.406  -7.993  1.00 35.26 ? 328 HOH   F O   1 
HETATM 16176 O  O   . HOH   SA 6 .   ? -4.179  -73.015  -22.948 1.00 45.07 ? 329 HOH   F O   1 
HETATM 16177 O  O   . HOH   SA 6 .   ? -14.037 -52.794  4.037   1.00 29.14 ? 330 HOH   F O   1 
HETATM 16178 O  O   . HOH   SA 6 .   ? -4.010  -55.831  -4.634  1.00 25.17 ? 331 HOH   F O   1 
HETATM 16179 O  O   . HOH   SA 6 .   ? -13.269 -54.529  11.136  1.00 40.83 ? 332 HOH   F O   1 
HETATM 16180 O  O   . HOH   SA 6 .   ? -13.045 -69.386  1.520   1.00 43.56 ? 333 HOH   F O   1 
HETATM 16181 O  O   . HOH   SA 6 .   ? -33.352 -68.085  -18.202 1.00 41.22 ? 334 HOH   F O   1 
HETATM 16182 O  O   . HOH   SA 6 .   ? -27.550 -85.977  -20.177 1.00 33.76 ? 335 HOH   F O   1 
HETATM 16183 O  O   . HOH   SA 6 .   ? -33.650 -85.111  -29.984 1.00 39.75 ? 336 HOH   F O   1 
HETATM 16184 O  O   . HOH   SA 6 .   ? -11.495 -61.201  8.073   1.00 45.91 ? 337 HOH   F O   1 
HETATM 16185 O  O   . HOH   SA 6 .   ? -21.561 -49.214  -4.421  1.00 31.15 ? 338 HOH   F O   1 
HETATM 16186 O  O   . HOH   SA 6 .   ? -22.370 -50.120  -7.153  1.00 46.29 ? 339 HOH   F O   1 
HETATM 16187 O  O   . HOH   SA 6 .   ? -24.348 -51.632  -6.829  1.00 32.46 ? 340 HOH   F O   1 
HETATM 16188 O  O   . HOH   SA 6 .   ? -7.831  -61.387  -14.309 1.00 41.36 ? 341 HOH   F O   1 
HETATM 16189 O  O   . HOH   SA 6 .   ? -22.920 -59.851  7.311   1.00 46.47 ? 342 HOH   F O   1 
HETATM 16190 O  O   . HOH   SA 6 .   ? -11.353 -63.990  6.155   1.00 42.63 ? 343 HOH   F O   1 
HETATM 16191 O  O   . HOH   SA 6 .   ? -19.193 -68.391  -8.754  1.00 46.85 ? 344 HOH   F O   1 
HETATM 16192 O  O   . HOH   SA 6 .   ? -7.770  -61.859  6.683   1.00 35.38 ? 345 HOH   F O   1 
HETATM 16193 O  O   . HOH   SA 6 .   ? -6.425  -61.378  -16.700 1.00 51.09 ? 346 HOH   F O   1 
HETATM 16194 O  O   . HOH   SA 6 .   ? -24.332 -86.763  -21.948 1.00 31.11 ? 347 HOH   F O   1 
HETATM 16195 O  O   . HOH   SA 6 .   ? -22.636 -79.359  -33.730 1.00 44.90 ? 348 HOH   F O   1 
HETATM 16196 O  O   . HOH   SA 6 .   ? -16.137 -56.461  10.935  1.00 38.69 ? 349 HOH   F O   1 
HETATM 16197 O  O   . HOH   SA 6 .   ? -2.538  -53.278  1.065   1.00 43.34 ? 350 HOH   F O   1 
HETATM 16198 O  O   . HOH   SA 6 .   ? -9.857  -55.765  -7.527  1.00 38.28 ? 351 HOH   F O   1 
HETATM 16199 O  O   . HOH   SA 6 .   ? -15.452 -78.898  -33.193 1.00 54.19 ? 352 HOH   F O   1 
HETATM 16200 O  O   . HOH   SA 6 .   ? -38.641 -83.869  -25.358 1.00 53.14 ? 353 HOH   F O   1 
HETATM 16201 O  O   . HOH   SA 6 .   ? -7.292  -76.183  -6.962  1.00 37.99 ? 354 HOH   F O   1 
HETATM 16202 O  O   . HOH   SA 6 .   ? -33.226 -87.876  -27.296 1.00 43.54 ? 355 HOH   F O   1 
HETATM 16203 O  O   . HOH   SA 6 .   ? -13.605 -65.316  -20.583 1.00 48.76 ? 356 HOH   F O   1 
HETATM 16204 O  O   . HOH   SA 6 .   ? -35.118 -85.899  -24.373 1.00 50.57 ? 357 HOH   F O   1 
HETATM 16205 O  O   . HOH   SA 6 .   ? -9.397  -78.165  1.054   1.00 43.82 ? 358 HOH   F O   1 
HETATM 16206 O  O   . HOH   SA 6 .   ? -30.067 -65.784  -5.080  1.00 48.68 ? 359 HOH   F O   1 
HETATM 16207 O  O   . HOH   SA 6 .   ? -15.751 -90.681  -25.585 1.00 50.24 ? 360 HOH   F O   1 
HETATM 16208 O  O   . HOH   SA 6 .   ? -9.796  -69.602  -26.252 1.00 55.20 ? 361 HOH   F O   1 
HETATM 16209 O  O   . HOH   TA 6 .   ? -56.711 -46.487  -76.600 1.00 45.72 ? 301 HOH   G O   1 
HETATM 16210 O  O   . HOH   TA 6 .   ? -38.387 -30.628  -53.349 1.00 38.04 ? 302 HOH   G O   1 
HETATM 16211 O  O   . HOH   TA 6 .   ? -33.214 -36.995  -68.224 1.00 42.63 ? 303 HOH   G O   1 
HETATM 16212 O  O   . HOH   TA 6 .   ? -58.950 -43.093  -75.515 1.00 41.04 ? 304 HOH   G O   1 
HETATM 16213 O  O   . HOH   TA 6 .   ? -44.601 -29.659  -62.837 1.00 41.13 ? 305 HOH   G O   1 
HETATM 16214 O  O   . HOH   TA 6 .   ? -45.821 -17.679  -45.193 1.00 38.70 ? 306 HOH   G O   1 
HETATM 16215 O  O   . HOH   TA 6 .   ? -48.468 -23.542  -81.582 1.00 47.65 ? 307 HOH   G O   1 
HETATM 16216 O  O   . HOH   TA 6 .   ? -48.530 -16.754  -49.995 1.00 50.13 ? 308 HOH   G O   1 
HETATM 16217 O  O   . HOH   TA 6 .   ? -38.989 -24.675  -70.604 1.00 33.53 ? 309 HOH   G O   1 
HETATM 16218 O  O   . HOH   TA 6 .   ? -29.994 -8.582   -51.837 1.00 36.07 ? 310 HOH   G O   1 
HETATM 16219 O  O   . HOH   TA 6 .   ? -52.154 -31.627  -75.067 1.00 41.84 ? 311 HOH   G O   1 
HETATM 16220 O  O   . HOH   TA 6 .   ? -34.756 -31.050  -55.830 1.00 54.72 ? 312 HOH   G O   1 
HETATM 16221 O  O   . HOH   TA 6 .   ? -25.072 -14.549  -49.682 1.00 39.39 ? 313 HOH   G O   1 
HETATM 16222 O  O   . HOH   TA 6 .   ? -28.233 -14.797  -60.698 1.00 29.54 ? 314 HOH   G O   1 
HETATM 16223 O  O   . HOH   TA 6 .   ? -53.954 -33.962  -67.658 1.00 33.12 ? 315 HOH   G O   1 
HETATM 16224 O  O   . HOH   TA 6 .   ? -46.480 -24.847  -71.618 1.00 34.17 ? 316 HOH   G O   1 
HETATM 16225 O  O   . HOH   TA 6 .   ? -49.752 -20.897  -65.650 1.00 40.13 ? 317 HOH   G O   1 
HETATM 16226 O  O   . HOH   TA 6 .   ? -48.452 -31.700  -64.550 1.00 31.65 ? 318 HOH   G O   1 
HETATM 16227 O  O   . HOH   TA 6 .   ? -41.279 -12.418  -49.032 1.00 38.70 ? 319 HOH   G O   1 
HETATM 16228 O  O   . HOH   TA 6 .   ? -46.604 -30.164  -45.885 1.00 43.28 ? 320 HOH   G O   1 
HETATM 16229 O  O   . HOH   TA 6 .   ? -51.223 -45.150  -75.035 1.00 31.35 ? 321 HOH   G O   1 
HETATM 16230 O  O   . HOH   TA 6 .   ? -38.045 -42.166  -77.228 1.00 29.92 ? 322 HOH   G O   1 
HETATM 16231 O  O   . HOH   TA 6 .   ? -26.573 -20.783  -55.319 1.00 42.53 ? 323 HOH   G O   1 
HETATM 16232 O  O   . HOH   TA 6 .   ? -37.369 -11.512  -50.590 1.00 32.88 ? 324 HOH   G O   1 
HETATM 16233 O  O   . HOH   TA 6 .   ? -39.719 -42.287  -70.737 1.00 40.65 ? 325 HOH   G O   1 
HETATM 16234 O  O   . HOH   TA 6 .   ? -55.996 -33.434  -72.426 1.00 47.24 ? 326 HOH   G O   1 
HETATM 16235 O  O   . HOH   TA 6 .   ? -59.238 -37.960  -70.310 1.00 41.38 ? 327 HOH   G O   1 
HETATM 16236 O  O   . HOH   TA 6 .   ? -49.477 -48.655  -63.694 1.00 32.32 ? 328 HOH   G O   1 
HETATM 16237 O  O   . HOH   TA 6 .   ? -33.677 -40.124  -75.769 1.00 32.36 ? 329 HOH   G O   1 
HETATM 16238 O  O   . HOH   TA 6 .   ? -48.978 -36.056  -81.533 1.00 40.49 ? 330 HOH   G O   1 
HETATM 16239 O  O   . HOH   TA 6 .   ? -37.491 -13.039  -38.252 1.00 33.17 ? 331 HOH   G O   1 
HETATM 16240 O  O   . HOH   TA 6 .   ? -27.497 -18.888  -44.262 1.00 39.28 ? 332 HOH   G O   1 
HETATM 16241 O  O   . HOH   TA 6 .   ? -56.325 -43.555  -80.029 1.00 44.55 ? 333 HOH   G O   1 
HETATM 16242 O  O   . HOH   TA 6 .   ? -45.935 -31.951  -63.909 1.00 37.08 ? 334 HOH   G O   1 
HETATM 16243 O  O   . HOH   TA 6 .   ? -39.044 -10.454  -39.963 1.00 37.33 ? 335 HOH   G O   1 
HETATM 16244 O  O   . HOH   TA 6 .   ? -42.256 -11.917  -40.372 1.00 41.34 ? 336 HOH   G O   1 
HETATM 16245 O  O   . HOH   TA 6 .   ? -57.956 -41.207  -77.771 1.00 40.01 ? 337 HOH   G O   1 
HETATM 16246 O  O   . HOH   TA 6 .   ? -36.234 -23.486  -53.540 1.00 41.53 ? 338 HOH   G O   1 
HETATM 16247 O  O   . HOH   TA 6 .   ? -49.512 -46.194  -60.066 1.00 34.85 ? 339 HOH   G O   1 
HETATM 16248 O  O   . HOH   TA 6 .   ? -38.516 -21.809  -73.175 1.00 37.20 ? 340 HOH   G O   1 
HETATM 16249 O  O   . HOH   TA 6 .   ? -56.076 -27.876  -66.168 1.00 54.00 ? 341 HOH   G O   1 
HETATM 16250 O  O   . HOH   TA 6 .   ? -26.719 -30.036  -62.490 1.00 42.15 ? 342 HOH   G O   1 
HETATM 16251 O  O   . HOH   TA 6 .   ? -23.019 -19.317  -49.713 1.00 46.39 ? 343 HOH   G O   1 
HETATM 16252 O  O   . HOH   TA 6 .   ? -25.967 -23.243  -59.752 1.00 40.69 ? 344 HOH   G O   1 
HETATM 16253 O  O   . HOH   TA 6 .   ? -23.522 -16.482  -49.646 1.00 53.62 ? 345 HOH   G O   1 
HETATM 16254 O  O   . HOH   TA 6 .   ? -27.174 -22.402  -57.810 1.00 40.59 ? 346 HOH   G O   1 
HETATM 16255 O  O   . HOH   TA 6 .   ? -28.462 -7.196   -56.404 1.00 51.13 ? 347 HOH   G O   1 
HETATM 16256 O  O   . HOH   UA 6 .   ? 26.058  -96.662  -51.871 1.00 56.35 ? 301 HOH   H O   1 
HETATM 16257 O  O   . HOH   UA 6 .   ? 24.544  -82.478  -41.656 1.00 46.43 ? 302 HOH   H O   1 
HETATM 16258 O  O   . HOH   UA 6 .   ? 23.830  -92.975  -44.762 1.00 47.66 ? 303 HOH   H O   1 
HETATM 16259 O  O   . HOH   UA 6 .   ? 43.863  -70.993  -52.581 1.00 43.02 ? 304 HOH   H O   1 
HETATM 16260 O  O   . HOH   UA 6 .   ? 26.960  -67.569  -39.493 1.00 46.79 ? 305 HOH   H O   1 
HETATM 16261 O  O   . HOH   UA 6 .   ? 23.727  -71.496  -28.899 1.00 37.69 ? 306 HOH   H O   1 
HETATM 16262 O  O   . HOH   UA 6 .   ? 29.734  -90.854  -22.608 1.00 37.72 ? 307 HOH   H O   1 
HETATM 16263 O  O   . HOH   UA 6 .   ? 19.866  -93.758  -32.338 1.00 34.67 ? 308 HOH   H O   1 
HETATM 16264 O  O   . HOH   UA 6 .   ? 16.360  -84.226  -15.231 1.00 33.76 ? 309 HOH   H O   1 
HETATM 16265 O  O   . HOH   UA 6 .   ? 30.078  -76.760  -58.690 1.00 39.83 ? 310 HOH   H O   1 
HETATM 16266 O  O   . HOH   UA 6 .   ? 13.785  -94.713  -15.788 1.00 46.05 ? 311 HOH   H O   1 
HETATM 16267 O  O   . HOH   UA 6 .   ? 38.213  -82.421  -26.193 1.00 38.32 ? 312 HOH   H O   1 
HETATM 16268 O  O   . HOH   UA 6 .   ? 39.739  -70.291  -46.261 1.00 30.96 ? 313 HOH   H O   1 
HETATM 16269 O  O   . HOH   UA 6 .   ? 34.532  -92.718  -50.871 1.00 32.87 ? 314 HOH   H O   1 
HETATM 16270 O  O   . HOH   UA 6 .   ? 26.092  -67.513  -37.124 1.00 54.42 ? 315 HOH   H O   1 
HETATM 16271 O  O   . HOH   UA 6 .   ? 23.598  -69.102  -21.015 1.00 32.44 ? 316 HOH   H O   1 
HETATM 16272 O  O   . HOH   UA 6 .   ? 25.863  -91.789  -10.255 1.00 42.65 ? 317 HOH   H O   1 
HETATM 16273 O  O   . HOH   UA 6 .   ? 31.340  -64.493  -39.917 1.00 53.75 ? 318 HOH   H O   1 
HETATM 16274 O  O   . HOH   UA 6 .   ? 21.985  -85.232  -12.750 1.00 37.67 ? 319 HOH   H O   1 
HETATM 16275 O  O   . HOH   UA 6 .   ? 32.376  -80.378  -12.451 1.00 42.23 ? 320 HOH   H O   1 
HETATM 16276 O  O   . HOH   UA 6 .   ? 21.121  -76.379  -21.850 1.00 42.28 ? 321 HOH   H O   1 
HETATM 16277 O  O   . HOH   UA 6 .   ? 42.455  -76.006  -55.533 1.00 42.19 ? 322 HOH   H O   1 
HETATM 16278 O  O   . HOH   UA 6 .   ? 22.774  -73.997  -10.652 1.00 45.41 ? 323 HOH   H O   1 
HETATM 16279 O  O   . HOH   UA 6 .   ? 23.066  -72.351  -17.320 1.00 35.62 ? 324 HOH   H O   1 
HETATM 16280 O  O   . HOH   UA 6 .   ? 36.617  -75.535  -29.854 1.00 43.20 ? 325 HOH   H O   1 
HETATM 16281 O  O   . HOH   UA 6 .   ? 26.194  -82.064  -52.209 1.00 44.60 ? 326 HOH   H O   1 
HETATM 16282 O  O   . HOH   UA 6 .   ? 14.622  -90.435  -8.505  1.00 55.25 ? 327 HOH   H O   1 
HETATM 16283 O  O   . HOH   UA 6 .   ? 31.922  -71.320  -48.867 1.00 41.04 ? 328 HOH   H O   1 
HETATM 16284 O  O   . HOH   UA 6 .   ? 37.856  -88.873  -60.976 1.00 43.11 ? 329 HOH   H O   1 
HETATM 16285 O  O   . HOH   UA 6 .   ? 34.736  -88.197  -62.029 1.00 39.12 ? 330 HOH   H O   1 
HETATM 16286 O  O   . HOH   UA 6 .   ? 29.579  -87.057  -27.925 1.00 39.84 ? 331 HOH   H O   1 
HETATM 16287 O  O   . HOH   UA 6 .   ? 39.227  -70.895  -10.337 1.00 55.79 ? 332 HOH   H O   1 
HETATM 16288 O  O   . HOH   UA 6 .   ? 39.926  -74.176  -29.326 1.00 38.70 ? 333 HOH   H O   1 
HETATM 16289 O  O   . HOH   UA 6 .   ? 14.080  -88.359  -21.164 1.00 36.77 ? 334 HOH   H O   1 
HETATM 16290 O  O   . HOH   UA 6 .   ? 42.166  -87.353  -28.084 1.00 50.17 ? 335 HOH   H O   1 
HETATM 16291 O  O   . HOH   UA 6 .   ? 28.234  -94.347  -16.263 1.00 50.34 ? 336 HOH   H O   1 
HETATM 16292 O  O   . HOH   UA 6 .   ? 26.451  -87.584  -7.449  1.00 43.16 ? 337 HOH   H O   1 
HETATM 16293 O  O   . HOH   UA 6 .   ? 40.648  -82.881  -52.600 1.00 35.61 ? 338 HOH   H O   1 
HETATM 16294 O  O   . HOH   UA 6 .   ? 39.796  -86.820  -52.106 1.00 36.65 ? 339 HOH   H O   1 
HETATM 16295 O  O   . HOH   UA 6 .   ? 13.077  -82.946  -27.226 1.00 49.86 ? 340 HOH   H O   1 
HETATM 16296 O  O   . HOH   UA 6 .   ? 35.536  -93.465  -25.007 1.00 53.78 ? 341 HOH   H O   1 
HETATM 16297 O  O   . HOH   UA 6 .   ? 31.818  -70.491  -45.676 1.00 37.81 ? 342 HOH   H O   1 
HETATM 16298 O  O   . HOH   UA 6 .   ? 30.383  -84.229  -31.826 1.00 47.31 ? 343 HOH   H O   1 
HETATM 16299 O  O   . HOH   UA 6 .   ? 47.272  -89.086  -45.033 1.00 44.13 ? 344 HOH   H O   1 
HETATM 16300 O  O   . HOH   UA 6 .   ? 14.982  -89.725  -25.094 1.00 42.91 ? 345 HOH   H O   1 
HETATM 16301 O  O   . HOH   UA 6 .   ? 27.717  -90.080  -9.513  1.00 48.87 ? 346 HOH   H O   1 
HETATM 16302 O  O   . HOH   UA 6 .   ? 36.209  -92.229  -20.576 1.00 53.97 ? 347 HOH   H O   1 
HETATM 16303 O  O   . HOH   UA 6 .   ? 25.396  -78.742  -49.344 1.00 52.48 ? 348 HOH   H O   1 
HETATM 16304 O  O   . HOH   UA 6 .   ? 34.995  -94.283  -48.486 1.00 45.22 ? 349 HOH   H O   1 
HETATM 16305 O  O   . HOH   UA 6 .   ? 17.321  -87.134  -36.983 1.00 54.07 ? 350 HOH   H O   1 
HETATM 16306 O  O   . HOH   UA 6 .   ? 26.251  -76.047  -49.068 1.00 44.96 ? 351 HOH   H O   1 
HETATM 16307 O  O   . HOH   UA 6 .   ? 31.247  -68.752  -44.322 1.00 47.80 ? 352 HOH   H O   1 
HETATM 16308 O  O   . HOH   UA 6 .   ? 25.805  -74.155  -50.990 1.00 54.73 ? 353 HOH   H O   1 
HETATM 16309 O  O   . HOH   UA 6 .   ? 25.607  -74.917  -47.043 1.00 44.44 ? 354 HOH   H O   1 
HETATM 16310 O  O   . HOH   VA 6 .   ? -33.247 -64.463  -20.803 1.00 42.40 ? 301 HOH   I O   1 
HETATM 16311 O  O   . HOH   VA 6 .   ? -40.132 -61.772  -43.902 1.00 41.39 ? 302 HOH   I O   1 
HETATM 16312 O  O   . HOH   VA 6 .   ? -25.518 -73.460  -27.907 1.00 41.49 ? 303 HOH   I O   1 
HETATM 16313 O  O   . HOH   VA 6 .   ? -60.299 -51.414  -43.590 1.00 35.91 ? 304 HOH   I O   1 
HETATM 16314 O  O   . HOH   VA 6 .   ? -30.689 -76.772  -39.992 1.00 46.17 ? 305 HOH   I O   1 
HETATM 16315 O  O   . HOH   VA 6 .   ? -39.893 -37.335  -40.674 1.00 28.68 ? 306 HOH   I O   1 
HETATM 16316 O  O   . HOH   VA 6 .   ? -35.064 -70.850  -40.875 1.00 43.13 ? 307 HOH   I O   1 
HETATM 16317 O  O   . HOH   VA 6 .   ? -42.333 -47.303  -54.533 1.00 44.33 ? 308 HOH   I O   1 
HETATM 16318 O  O   . HOH   VA 6 .   ? -33.655 -68.166  -20.511 1.00 46.88 ? 309 HOH   I O   1 
HETATM 16319 O  O   . HOH   VA 6 .   ? -60.524 -54.794  -40.185 1.00 52.89 ? 310 HOH   I O   1 
HETATM 16320 O  O   . HOH   VA 6 .   ? -39.871 -54.055  -46.071 1.00 46.80 ? 311 HOH   I O   1 
HETATM 16321 O  O   . HOH   VA 6 .   ? -51.397 -58.723  -53.700 1.00 31.99 ? 312 HOH   I O   1 
HETATM 16322 O  O   . HOH   VA 6 .   ? -51.164 -38.973  -54.446 1.00 27.34 ? 313 HOH   I O   1 
HETATM 16323 O  O   . HOH   VA 6 .   ? -46.923 -76.515  -38.485 1.00 35.41 ? 314 HOH   I O   1 
HETATM 16324 O  O   . HOH   VA 6 .   ? -37.934 -45.393  -41.074 1.00 40.07 ? 315 HOH   I O   1 
HETATM 16325 O  O   . HOH   VA 6 .   ? -51.887 -69.284  -44.715 1.00 47.01 ? 316 HOH   I O   1 
HETATM 16326 O  O   . HOH   VA 6 .   ? -58.751 -44.958  -38.598 1.00 40.14 ? 317 HOH   I O   1 
HETATM 16327 O  O   . HOH   VA 6 .   ? -30.935 -63.460  -31.514 1.00 33.99 ? 318 HOH   I O   1 
HETATM 16328 O  O   . HOH   VA 6 .   ? -45.899 -50.450  -31.310 1.00 33.58 ? 319 HOH   I O   1 
HETATM 16329 O  O   . HOH   VA 6 .   ? -55.619 -58.083  -32.835 1.00 43.15 ? 320 HOH   I O   1 
HETATM 16330 O  O   . HOH   VA 6 .   ? -49.480 -53.436  -42.420 1.00 40.93 ? 321 HOH   I O   1 
HETATM 16331 O  O   . HOH   VA 6 .   ? -34.870 -61.840  -24.527 1.00 28.25 ? 322 HOH   I O   1 
HETATM 16332 O  O   . HOH   VA 6 .   ? -50.188 -49.980  -56.967 1.00 39.15 ? 323 HOH   I O   1 
HETATM 16333 O  O   . HOH   VA 6 .   ? -57.979 -50.394  -44.189 1.00 35.36 ? 324 HOH   I O   1 
HETATM 16334 O  O   . HOH   VA 6 .   ? -39.344 -65.176  -37.235 1.00 43.66 ? 325 HOH   I O   1 
HETATM 16335 O  O   . HOH   VA 6 .   ? -54.316 -66.125  -33.213 1.00 50.52 ? 326 HOH   I O   1 
HETATM 16336 O  O   . HOH   VA 6 .   ? -62.912 -46.966  -48.037 1.00 41.44 ? 327 HOH   I O   1 
HETATM 16337 O  O   . HOH   VA 6 .   ? -34.848 -73.001  -23.339 1.00 43.31 ? 328 HOH   I O   1 
HETATM 16338 O  O   . HOH   VA 6 .   ? -46.472 -49.596  -27.599 1.00 30.45 ? 329 HOH   I O   1 
HETATM 16339 O  O   . HOH   VA 6 .   ? -28.977 -71.096  -28.079 1.00 41.67 ? 330 HOH   I O   1 
HETATM 16340 O  O   . HOH   VA 6 .   ? -44.104 -41.213  -46.166 1.00 33.50 ? 331 HOH   I O   1 
HETATM 16341 O  O   . HOH   VA 6 .   ? -29.148 -73.816  -34.870 1.00 40.28 ? 332 HOH   I O   1 
HETATM 16342 O  O   . HOH   VA 6 .   ? -53.571 -50.616  -32.751 1.00 31.63 ? 333 HOH   I O   1 
HETATM 16343 O  O   . HOH   VA 6 .   ? -55.446 -37.705  -49.858 1.00 32.86 ? 334 HOH   I O   1 
HETATM 16344 O  O   . HOH   VA 6 .   ? -45.850 -69.736  -48.890 1.00 45.63 ? 335 HOH   I O   1 
HETATM 16345 O  O   . HOH   VA 6 .   ? -41.381 -73.777  -28.497 1.00 35.04 ? 336 HOH   I O   1 
HETATM 16346 O  O   . HOH   VA 6 .   ? -57.652 -55.168  -38.269 1.00 50.66 ? 337 HOH   I O   1 
HETATM 16347 O  O   . HOH   VA 6 .   ? -56.641 -36.699  -38.577 1.00 31.62 ? 338 HOH   I O   1 
HETATM 16348 O  O   . HOH   VA 6 .   ? -55.396 -60.564  -47.960 1.00 47.36 ? 339 HOH   I O   1 
HETATM 16349 O  O   . HOH   VA 6 .   ? -38.076 -83.439  -35.472 1.00 37.78 ? 340 HOH   I O   1 
HETATM 16350 O  O   . HOH   VA 6 .   ? -48.581 -48.036  -57.300 1.00 43.33 ? 341 HOH   I O   1 
HETATM 16351 O  O   . HOH   VA 6 .   ? -44.018 -35.678  -42.949 1.00 31.37 ? 342 HOH   I O   1 
HETATM 16352 O  O   . HOH   VA 6 .   ? -44.274 -75.330  -30.795 1.00 35.97 ? 343 HOH   I O   1 
HETATM 16353 O  O   . HOH   VA 6 .   ? -50.533 -45.776  -57.506 1.00 32.12 ? 344 HOH   I O   1 
HETATM 16354 O  O   . HOH   VA 6 .   ? -52.408 -53.079  -42.339 1.00 35.71 ? 345 HOH   I O   1 
HETATM 16355 O  O   . HOH   VA 6 .   ? -62.259 -50.085  -39.015 1.00 50.16 ? 346 HOH   I O   1 
HETATM 16356 O  O   . HOH   VA 6 .   ? -48.652 -79.794  -35.151 1.00 50.17 ? 347 HOH   I O   1 
HETATM 16357 O  O   . HOH   VA 6 .   ? -52.815 -63.252  -27.045 1.00 47.79 ? 348 HOH   I O   1 
HETATM 16358 O  O   . HOH   VA 6 .   ? -43.305 -83.065  -34.798 1.00 43.80 ? 349 HOH   I O   1 
HETATM 16359 O  O   . HOH   VA 6 .   ? -54.443 -48.405  -26.209 1.00 42.13 ? 350 HOH   I O   1 
HETATM 16360 O  O   . HOH   VA 6 .   ? -40.533 -83.619  -32.934 1.00 44.26 ? 351 HOH   I O   1 
HETATM 16361 O  O   . HOH   VA 6 .   ? -48.520 -55.589  -40.019 1.00 43.31 ? 352 HOH   I O   1 
HETATM 16362 O  O   . HOH   VA 6 .   ? -48.090 -30.741  -44.212 1.00 54.82 ? 353 HOH   I O   1 
HETATM 16363 O  O   . HOH   VA 6 .   ? -52.724 -67.292  -28.434 1.00 49.73 ? 354 HOH   I O   1 
HETATM 16364 O  O   . HOH   VA 6 .   ? -50.952 -72.781  -34.950 1.00 54.38 ? 355 HOH   I O   1 
HETATM 16365 O  O   . HOH   VA 6 .   ? -53.717 -65.131  -28.566 1.00 51.98 ? 356 HOH   I O   1 
HETATM 16366 O  O   . HOH   VA 6 .   ? -35.394 -71.270  -21.012 1.00 49.65 ? 357 HOH   I O   1 
HETATM 16367 O  O   . HOH   VA 6 .   ? -56.114 -50.616  -33.678 1.00 47.23 ? 358 HOH   I O   1 
HETATM 16368 O  O   . HOH   WA 6 .   ? 31.392  -58.307  -20.609 1.00 45.73 ? 301 HOH   J O   1 
HETATM 16369 O  O   . HOH   WA 6 .   ? 21.660  -72.010  -15.093 1.00 47.28 ? 302 HOH   J O   1 
HETATM 16370 O  O   . HOH   WA 6 .   ? 39.988  -71.864  -6.314  1.00 49.07 ? 303 HOH   J O   1 
HETATM 16371 O  O   . HOH   WA 6 .   ? 38.434  -71.965  -28.890 1.00 39.23 ? 304 HOH   J O   1 
HETATM 16372 O  O   . HOH   WA 6 .   ? 55.306  -62.934  -29.425 1.00 49.26 ? 305 HOH   J O   1 
HETATM 16373 O  O   . HOH   WA 6 .   ? 22.161  -49.158  -14.452 1.00 47.54 ? 306 HOH   J O   1 
HETATM 16374 O  O   . HOH   WA 6 .   ? 48.336  -49.384  -30.424 1.00 28.11 ? 307 HOH   J O   1 
HETATM 16375 O  O   . HOH   WA 6 .   ? 44.501  -61.827  -30.335 1.00 40.20 ? 308 HOH   J O   1 
HETATM 16376 O  O   . HOH   WA 6 .   ? 38.688  -62.096  -5.651  1.00 34.05 ? 309 HOH   J O   1 
HETATM 16377 O  O   . HOH   WA 6 .   ? 41.814  -53.271  -43.147 1.00 46.63 ? 310 HOH   J O   1 
HETATM 16378 O  O   . HOH   WA 6 .   ? 34.164  -64.706  -39.592 1.00 42.25 ? 311 HOH   J O   1 
HETATM 16379 O  O   . HOH   WA 6 .   ? 37.284  -52.911  -9.785  1.00 45.37 ? 312 HOH   J O   1 
HETATM 16380 O  O   . HOH   WA 6 .   ? 18.381  -61.838  -13.817 1.00 37.57 ? 313 HOH   J O   1 
HETATM 16381 O  O   . HOH   WA 6 .   ? 30.413  -53.503  -2.022  1.00 32.10 ? 314 HOH   J O   1 
HETATM 16382 O  O   . HOH   WA 6 .   ? 40.372  -47.285  -20.345 1.00 42.87 ? 315 HOH   J O   1 
HETATM 16383 O  O   . HOH   WA 6 .   ? 46.892  -73.036  -31.031 1.00 48.61 ? 316 HOH   J O   1 
HETATM 16384 O  O   . HOH   WA 6 .   ? 21.530  -70.346  -11.429 1.00 44.88 ? 317 HOH   J O   1 
HETATM 16385 O  O   . HOH   WA 6 .   ? 22.296  -62.925  -21.741 1.00 35.19 ? 318 HOH   J O   1 
HETATM 16386 O  O   . HOH   WA 6 .   ? 37.269  -69.361  -45.891 1.00 33.66 ? 319 HOH   J O   1 
HETATM 16387 O  O   . HOH   WA 6 .   ? 34.552  -54.285  -26.604 1.00 43.29 ? 320 HOH   J O   1 
HETATM 16388 O  O   . HOH   WA 6 .   ? 24.451  -70.325  -18.701 1.00 30.09 ? 321 HOH   J O   1 
HETATM 16389 O  O   . HOH   WA 6 .   ? 22.845  -65.669  -8.891  1.00 40.11 ? 322 HOH   J O   1 
HETATM 16390 O  O   . HOH   WA 6 .   ? 46.079  -71.613  -27.529 1.00 33.70 ? 323 HOH   J O   1 
HETATM 16391 O  O   . HOH   WA 6 .   ? 54.467  -63.730  -45.256 1.00 35.51 ? 324 HOH   J O   1 
HETATM 16392 O  O   . HOH   WA 6 .   ? 42.710  -62.246  -28.220 1.00 37.99 ? 325 HOH   J O   1 
HETATM 16393 O  O   . HOH   WA 6 .   ? 53.739  -62.608  -31.636 1.00 36.74 ? 326 HOH   J O   1 
HETATM 16394 O  O   . HOH   WA 6 .   ? 58.690  -51.166  -44.594 1.00 38.14 ? 327 HOH   J O   1 
HETATM 16395 O  O   . HOH   WA 6 .   ? 25.214  -64.527  -32.582 1.00 46.38 ? 328 HOH   J O   1 
HETATM 16396 O  O   . HOH   WA 6 .   ? 42.017  -68.872  -47.013 1.00 34.76 ? 329 HOH   J O   1 
HETATM 16397 O  O   . HOH   WA 6 .   ? 40.291  -67.401  -8.760  1.00 49.89 ? 330 HOH   J O   1 
HETATM 16398 O  O   . HOH   WA 6 .   ? 50.654  -54.257  -25.331 1.00 51.07 ? 331 HOH   J O   1 
HETATM 16399 O  O   . HOH   WA 6 .   ? 50.527  -75.632  -37.098 1.00 47.52 ? 332 HOH   J O   1 
HETATM 16400 O  O   . HOH   WA 6 .   ? 42.015  -63.416  -43.861 1.00 40.71 ? 333 HOH   J O   1 
HETATM 16401 O  O   . HOH   WA 6 .   ? 47.384  -61.923  -29.847 1.00 32.47 ? 334 HOH   J O   1 
HETATM 16402 O  O   . HOH   WA 6 .   ? 61.740  -63.990  -41.305 1.00 44.03 ? 335 HOH   J O   1 
HETATM 16403 O  O   . HOH   WA 6 .   ? 19.628  -54.507  -14.677 1.00 41.98 ? 336 HOH   J O   1 
HETATM 16404 O  O   . HOH   WA 6 .   ? 27.407  -51.645  -18.885 1.00 43.90 ? 337 HOH   J O   1 
HETATM 16405 O  O   . HOH   WA 6 .   ? 21.322  -49.043  -22.314 1.00 55.04 ? 338 HOH   J O   1 
HETATM 16406 O  O   . HOH   WA 6 .   ? 45.089  -52.290  -17.485 1.00 48.60 ? 339 HOH   J O   1 
HETATM 16407 O  O   . HOH   WA 6 .   ? 52.715  -73.878  -40.824 1.00 45.65 ? 340 HOH   J O   1 
HETATM 16408 O  O   . HOH   WA 6 .   ? 33.420  -63.910  -4.476  1.00 36.02 ? 341 HOH   J O   1 
HETATM 16409 O  O   . HOH   WA 6 .   ? 26.886  -50.500  -4.778  1.00 27.89 ? 342 HOH   J O   1 
HETATM 16410 O  O   . HOH   WA 6 .   ? 50.480  -52.526  -43.522 1.00 34.57 ? 343 HOH   J O   1 
HETATM 16411 O  O   . HOH   WA 6 .   ? 59.946  -61.999  -35.145 1.00 41.72 ? 344 HOH   J O   1 
HETATM 16412 O  O   . HOH   WA 6 .   ? 48.309  -51.336  -41.951 1.00 43.79 ? 345 HOH   J O   1 
HETATM 16413 O  O   . HOH   WA 6 .   ? 33.089  -59.693  -7.871  1.00 26.66 ? 346 HOH   J O   1 
HETATM 16414 O  O   . HOH   WA 6 .   ? 46.777  -71.429  -50.463 1.00 47.32 ? 347 HOH   J O   1 
HETATM 16415 O  O   . HOH   WA 6 .   ? 31.911  -52.209  -3.480  1.00 32.18 ? 348 HOH   J O   1 
HETATM 16416 O  O   . HOH   WA 6 .   ? 30.906  -49.121  -20.278 1.00 36.41 ? 349 HOH   J O   1 
HETATM 16417 O  O   . HOH   WA 6 .   ? 60.522  -68.113  -44.799 1.00 43.17 ? 350 HOH   J O   1 
HETATM 16418 O  O   . HOH   WA 6 .   ? 38.283  -75.714  -27.777 1.00 36.63 ? 351 HOH   J O   1 
HETATM 16419 O  O   . HOH   WA 6 .   ? 49.201  -50.717  -39.942 1.00 32.99 ? 352 HOH   J O   1 
HETATM 16420 O  O   . HOH   WA 6 .   ? 33.461  -52.062  -5.308  1.00 44.31 ? 353 HOH   J O   1 
HETATM 16421 O  O   . HOH   WA 6 .   ? 23.787  -64.444  -24.149 1.00 42.32 ? 354 HOH   J O   1 
HETATM 16422 O  O   . HOH   WA 6 .   ? 29.985  -62.000  -8.838  1.00 29.14 ? 355 HOH   J O   1 
HETATM 16423 O  O   . HOH   WA 6 .   ? 54.276  -63.583  -24.700 1.00 60.44 ? 356 HOH   J O   1 
HETATM 16424 O  O   . HOH   WA 6 .   ? 35.713  -54.716  -31.008 1.00 54.03 ? 357 HOH   J O   1 
HETATM 16425 O  O   . HOH   WA 6 .   ? 45.908  -78.653  -26.268 1.00 47.80 ? 358 HOH   J O   1 
HETATM 16426 O  O   . HOH   WA 6 .   ? 40.965  -57.623  -10.155 1.00 40.09 ? 359 HOH   J O   1 
HETATM 16427 O  O   . HOH   WA 6 .   ? 22.074  -60.103  -27.382 1.00 47.76 ? 360 HOH   J O   1 
HETATM 16428 O  O   . HOH   WA 6 .   ? 35.465  -57.302  -34.118 1.00 53.47 ? 361 HOH   J O   1 
HETATM 16429 O  O   . HOH   WA 6 .   ? 48.852  -70.463  -26.845 1.00 48.48 ? 362 HOH   J O   1 
HETATM 16430 O  O   . HOH   XA 6 .   ? 15.449  -51.223  4.067   1.00 51.06 ? 301 HOH   K O   1 
HETATM 16431 O  O   . HOH   XA 6 .   ? -0.191  -52.001  -1.512  1.00 46.57 ? 302 HOH   K O   1 
HETATM 16432 O  O   . HOH   XA 6 .   ? 7.136   -83.310  -26.346 1.00 45.55 ? 303 HOH   K O   1 
HETATM 16433 O  O   . HOH   XA 6 .   ? 18.089  -53.897  -12.156 1.00 42.57 ? 304 HOH   K O   1 
HETATM 16434 O  O   . HOH   XA 6 .   ? 17.881  -75.986  -5.063  1.00 50.94 ? 305 HOH   K O   1 
HETATM 16435 O  O   . HOH   XA 6 .   ? -5.595  -83.363  -5.938  1.00 43.06 ? 306 HOH   K O   1 
HETATM 16436 O  O   . HOH   XA 6 .   ? -3.903  -75.532  -21.637 1.00 40.62 ? 307 HOH   K O   1 
HETATM 16437 O  O   . HOH   XA 6 .   ? 5.754   -74.936  -19.945 1.00 48.27 ? 308 HOH   K O   1 
HETATM 16438 O  O   . HOH   XA 6 .   ? -1.153  -96.135  -19.031 1.00 42.56 ? 309 HOH   K O   1 
HETATM 16439 O  O   . HOH   XA 6 .   ? 9.297   -84.515  -26.235 1.00 46.01 ? 310 HOH   K O   1 
HETATM 16440 O  O   . HOH   XA 6 .   ? 10.738  -69.912  -15.126 1.00 43.01 ? 311 HOH   K O   1 
HETATM 16441 O  O   . HOH   XA 6 .   ? 18.941  -65.444  -0.699  1.00 39.37 ? 312 HOH   K O   1 
HETATM 16442 O  O   . HOH   XA 6 .   ? -5.448  -74.725  -7.996  1.00 34.25 ? 313 HOH   K O   1 
HETATM 16443 O  O   . HOH   XA 6 .   ? 0.998   -101.061 -12.888 1.00 48.63 ? 314 HOH   K O   1 
HETATM 16444 O  O   . HOH   XA 6 .   ? -0.812  -68.719  -23.593 1.00 60.44 ? 315 HOH   K O   1 
HETATM 16445 O  O   . HOH   XA 6 .   ? 6.049   -50.152  -8.190  1.00 35.34 ? 316 HOH   K O   1 
HETATM 16446 O  O   . HOH   XA 6 .   ? 4.569   -80.687  -11.499 1.00 46.91 ? 317 HOH   K O   1 
HETATM 16447 O  O   . HOH   XA 6 .   ? 5.509   -76.552  -9.775  1.00 44.39 ? 318 HOH   K O   1 
HETATM 16448 O  O   . HOH   XA 6 .   ? -9.968  -80.787  -23.424 1.00 33.70 ? 319 HOH   K O   1 
HETATM 16449 O  O   . HOH   XA 6 .   ? 4.958   -51.704  -0.584  1.00 39.33 ? 320 HOH   K O   1 
HETATM 16450 O  O   . HOH   XA 6 .   ? 12.880  -61.012  1.698   1.00 29.76 ? 321 HOH   K O   1 
HETATM 16451 O  O   . HOH   XA 6 .   ? 4.965   -96.675  -9.163  1.00 48.83 ? 322 HOH   K O   1 
HETATM 16452 O  O   . HOH   XA 6 .   ? -5.373  -77.889  -24.372 1.00 48.76 ? 323 HOH   K O   1 
HETATM 16453 O  O   . HOH   XA 6 .   ? -2.563  -57.684  -6.046  1.00 27.07 ? 324 HOH   K O   1 
HETATM 16454 O  O   . HOH   XA 6 .   ? 4.583   -89.468  -8.493  1.00 39.85 ? 325 HOH   K O   1 
HETATM 16455 O  O   . HOH   XA 6 .   ? 2.646   -57.010  -12.413 1.00 35.12 ? 326 HOH   K O   1 
HETATM 16456 O  O   . HOH   XA 6 .   ? 0.888   -71.994  -24.864 1.00 59.03 ? 327 HOH   K O   1 
HETATM 16457 O  O   . HOH   XA 6 .   ? -2.875  -90.268  -6.587  1.00 40.47 ? 328 HOH   K O   1 
HETATM 16458 O  O   . HOH   XA 6 .   ? -3.163  -80.995  -4.081  1.00 33.13 ? 329 HOH   K O   1 
HETATM 16459 O  O   . HOH   XA 6 .   ? 8.604   -91.761  -23.810 1.00 34.00 ? 330 HOH   K O   1 
HETATM 16460 O  O   . HOH   XA 6 .   ? 6.082   -87.413  -2.226  1.00 53.41 ? 331 HOH   K O   1 
HETATM 16461 O  O   . HOH   XA 6 .   ? 4.769   -83.052  -9.599  1.00 32.95 ? 332 HOH   K O   1 
HETATM 16462 O  O   . HOH   XA 6 .   ? 12.345  -51.936  -11.362 1.00 36.18 ? 333 HOH   K O   1 
HETATM 16463 O  O   . HOH   XA 6 .   ? -2.870  -84.260  -22.642 1.00 43.32 ? 334 HOH   K O   1 
HETATM 16464 O  O   . HOH   XA 6 .   ? 8.607   -65.129  -9.892  1.00 42.02 ? 335 HOH   K O   1 
HETATM 16465 O  O   . HOH   XA 6 .   ? 14.431  -84.371  -8.020  1.00 44.01 ? 336 HOH   K O   1 
HETATM 16466 O  O   . HOH   XA 6 .   ? 21.232  -53.772  -1.871  1.00 27.05 ? 337 HOH   K O   1 
HETATM 16467 O  O   . HOH   XA 6 .   ? -3.949  -101.375 -14.423 1.00 47.56 ? 338 HOH   K O   1 
HETATM 16468 O  O   . HOH   XA 6 .   ? 2.846   -79.012  0.185   1.00 43.87 ? 339 HOH   K O   1 
HETATM 16469 O  O   . HOH   XA 6 .   ? -9.088  -85.714  -23.022 1.00 37.75 ? 340 HOH   K O   1 
HETATM 16470 O  O   . HOH   XA 6 .   ? 14.813  -69.969  -15.948 1.00 48.01 ? 341 HOH   K O   1 
HETATM 16471 O  O   . HOH   XA 6 .   ? -8.348  -73.901  -5.831  1.00 35.05 ? 342 HOH   K O   1 
HETATM 16472 O  O   . HOH   XA 6 .   ? 20.688  -58.204  1.907   1.00 38.42 ? 343 HOH   K O   1 
HETATM 16473 O  O   . HOH   XA 6 .   ? 11.584  -88.976  -22.141 1.00 44.38 ? 344 HOH   K O   1 
HETATM 16474 O  O   . HOH   XA 6 .   ? 8.552   -60.219  -15.161 1.00 40.49 ? 345 HOH   K O   1 
HETATM 16475 O  O   . HOH   XA 6 .   ? 7.248   -98.931  -11.232 1.00 54.29 ? 346 HOH   K O   1 
HETATM 16476 O  O   . HOH   XA 6 .   ? 11.226  -80.113  -0.938  1.00 46.89 ? 347 HOH   K O   1 
HETATM 16477 O  O   . HOH   XA 6 .   ? -9.157  -92.844  -11.602 1.00 43.84 ? 348 HOH   K O   1 
HETATM 16478 O  O   . HOH   XA 6 .   ? 10.121  -58.531  0.908   1.00 35.48 ? 349 HOH   K O   1 
HETATM 16479 O  O   . HOH   XA 6 .   ? -6.062  -91.903  -9.424  1.00 44.55 ? 350 HOH   K O   1 
HETATM 16480 O  O   . HOH   XA 6 .   ? 10.257  -89.091  -23.927 1.00 48.63 ? 351 HOH   K O   1 
HETATM 16481 O  O   . HOH   XA 6 .   ? 0.210   -81.311  1.403   1.00 52.80 ? 352 HOH   K O   1 
HETATM 16482 O  O   . HOH   XA 6 .   ? 19.968  -54.563  1.431   1.00 43.06 ? 353 HOH   K O   1 
HETATM 16483 O  O   . HOH   XA 6 .   ? 7.653   -68.321  -16.817 1.00 54.08 ? 354 HOH   K O   1 
HETATM 16484 O  O   . HOH   XA 6 .   ? 5.586   -51.499  -13.685 1.00 50.22 ? 355 HOH   K O   1 
HETATM 16485 O  O   . HOH   XA 6 .   ? -0.110  -84.575  -4.466  1.00 49.22 ? 356 HOH   K O   1 
HETATM 16486 O  O   . HOH   XA 6 .   ? 16.070  -68.932  1.950   1.00 48.41 ? 357 HOH   K O   1 
HETATM 16487 O  O   . HOH   XA 6 .   ? -9.037  -80.154  -0.082  1.00 46.65 ? 358 HOH   K O   1 
HETATM 16488 O  O   . HOH   XA 6 .   ? 5.448   -50.216  -11.026 1.00 50.07 ? 359 HOH   K O   1 
HETATM 16489 O  O   . HOH   XA 6 .   ? 14.433  -98.056  -19.834 1.00 47.68 ? 360 HOH   K O   1 
HETATM 16490 O  O   . HOH   XA 6 .   ? 2.469   -52.014  0.380   1.00 52.97 ? 361 HOH   K O   1 
HETATM 16491 O  O   . HOH   XA 6 .   ? 13.985  -68.502  2.869   1.00 47.74 ? 362 HOH   K O   1 
HETATM 16492 O  O   . HOH   XA 6 .   ? 11.170  -82.855  -1.399  1.00 47.62 ? 363 HOH   K O   1 
HETATM 16493 O  O   . HOH   XA 6 .   ? 4.946   -104.142 -24.784 1.00 58.95 ? 364 HOH   K O   1 
HETATM 16494 O  O   . HOH   YA 6 .   ? -15.778 -4.816   -50.844 1.00 43.89 ? 301 HOH   L O   1 
HETATM 16495 O  O   . HOH   YA 6 .   ? -26.666 -8.658   -56.951 1.00 44.29 ? 302 HOH   L O   1 
HETATM 16496 O  O   . HOH   YA 6 .   ? -22.186 -13.384  -46.688 1.00 39.68 ? 303 HOH   L O   1 
HETATM 16497 O  O   . HOH   YA 6 .   ? -11.913 -5.684   -30.849 1.00 40.25 ? 304 HOH   L O   1 
HETATM 16498 O  O   . HOH   YA 6 .   ? -7.804  -12.182  -71.031 1.00 46.37 ? 305 HOH   L O   1 
HETATM 16499 O  O   . HOH   YA 6 .   ? -0.788  6.786    -58.189 1.00 44.87 ? 306 HOH   L O   1 
HETATM 16500 O  O   . HOH   YA 6 .   ? -31.258 -4.800   -37.083 1.00 43.49 ? 307 HOH   L O   1 
HETATM 16501 O  O   . HOH   YA 6 .   ? -16.316 -10.110  -55.089 1.00 38.64 ? 308 HOH   L O   1 
HETATM 16502 O  O   . HOH   YA 6 .   ? -11.821 -1.413   -56.716 1.00 49.58 ? 309 HOH   L O   1 
HETATM 16503 O  O   . HOH   YA 6 .   ? -17.495 -5.732   -31.608 1.00 39.02 ? 310 HOH   L O   1 
HETATM 16504 O  O   . HOH   YA 6 .   ? 0.079   1.888    -76.137 1.00 35.06 ? 311 HOH   L O   1 
HETATM 16505 O  O   . HOH   YA 6 .   ? 0.250   -12.975  -57.409 1.00 46.89 ? 312 HOH   L O   1 
HETATM 16506 O  O   . HOH   YA 6 .   ? -10.469 -0.820   -58.419 1.00 43.52 ? 313 HOH   L O   1 
HETATM 16507 O  O   . HOH   YA 6 .   ? 0.155   -10.472  -59.068 1.00 40.34 ? 314 HOH   L O   1 
HETATM 16508 O  O   . HOH   YA 6 .   ? -2.784  9.261    -78.018 1.00 53.21 ? 315 HOH   L O   1 
HETATM 16509 O  O   . HOH   YA 6 .   ? -16.841 -13.000  -33.751 1.00 36.29 ? 316 HOH   L O   1 
HETATM 16510 O  O   . HOH   YA 6 .   ? -19.189 -3.672   -68.949 1.00 27.78 ? 317 HOH   L O   1 
HETATM 16511 O  O   . HOH   YA 6 .   ? -10.040 -0.804   -83.615 1.00 34.92 ? 318 HOH   L O   1 
HETATM 16512 O  O   . HOH   YA 6 .   ? 7.240   -8.696   -62.892 1.00 30.96 ? 319 HOH   L O   1 
HETATM 16513 O  O   . HOH   YA 6 .   ? -10.189 -7.669   -75.336 1.00 44.43 ? 320 HOH   L O   1 
HETATM 16514 O  O   . HOH   YA 6 .   ? -11.131 -12.871  -40.802 1.00 35.72 ? 321 HOH   L O   1 
HETATM 16515 O  O   . HOH   YA 6 .   ? -9.142  6.402    -67.302 1.00 36.94 ? 322 HOH   L O   1 
HETATM 16516 O  O   . HOH   YA 6 .   ? 2.374   8.799    -77.557 1.00 41.23 ? 323 HOH   L O   1 
HETATM 16517 O  O   . HOH   YA 6 .   ? -10.519 8.701    -66.929 1.00 38.59 ? 324 HOH   L O   1 
HETATM 16518 O  O   . HOH   YA 6 .   ? -12.351 -12.071  -54.004 1.00 53.68 ? 325 HOH   L O   1 
HETATM 16519 O  O   . HOH   YA 6 .   ? -7.721  -6.284   -37.029 1.00 27.16 ? 326 HOH   L O   1 
HETATM 16520 O  O   . HOH   YA 6 .   ? -26.212 -6.601   -58.162 1.00 41.23 ? 327 HOH   L O   1 
HETATM 16521 O  O   . HOH   YA 6 .   ? -11.087 8.644    -53.963 1.00 41.22 ? 328 HOH   L O   1 
HETATM 16522 O  O   . HOH   YA 6 .   ? -2.341  9.506    -65.047 1.00 42.09 ? 329 HOH   L O   1 
HETATM 16523 O  O   . HOH   YA 6 .   ? -1.917  0.879    -51.975 1.00 37.21 ? 330 HOH   L O   1 
HETATM 16524 O  O   . HOH   YA 6 .   ? -21.299 -2.220   -38.049 1.00 33.21 ? 331 HOH   L O   1 
HETATM 16525 O  O   . HOH   YA 6 .   ? -9.979  2.108    -62.315 1.00 32.89 ? 332 HOH   L O   1 
HETATM 16526 O  O   . HOH   YA 6 .   ? 6.988   -5.717   -67.061 1.00 28.48 ? 333 HOH   L O   1 
HETATM 16527 O  O   . HOH   YA 6 .   ? 5.609   7.423    -67.940 1.00 39.95 ? 334 HOH   L O   1 
HETATM 16528 O  O   . HOH   YA 6 .   ? -4.108  7.053    -55.997 1.00 33.94 ? 335 HOH   L O   1 
HETATM 16529 O  O   . HOH   YA 6 .   ? -28.254 -1.047   -47.342 1.00 34.48 ? 336 HOH   L O   1 
HETATM 16530 O  O   . HOH   YA 6 .   ? -8.681  -5.919   -77.336 1.00 34.95 ? 337 HOH   L O   1 
HETATM 16531 O  O   . HOH   YA 6 .   ? -32.190 -8.314   -38.244 1.00 31.76 ? 338 HOH   L O   1 
HETATM 16532 O  O   . HOH   YA 6 .   ? -7.208  -13.903  -52.257 1.00 52.06 ? 339 HOH   L O   1 
HETATM 16533 O  O   . HOH   YA 6 .   ? 0.706   -7.254   -67.314 1.00 36.09 ? 340 HOH   L O   1 
HETATM 16534 O  O   . HOH   YA 6 .   ? -16.263 -7.741   -48.086 1.00 44.46 ? 341 HOH   L O   1 
HETATM 16535 O  O   . HOH   YA 6 .   ? -8.444  9.494    -73.801 1.00 47.06 ? 342 HOH   L O   1 
HETATM 16536 O  O   . HOH   YA 6 .   ? -21.760 -16.032  -38.200 1.00 41.29 ? 343 HOH   L O   1 
HETATM 16537 O  O   . HOH   YA 6 .   ? -24.079 -0.519   -40.460 1.00 33.42 ? 344 HOH   L O   1 
HETATM 16538 O  O   . HOH   YA 6 .   ? -0.764  9.848    -76.663 1.00 44.07 ? 345 HOH   L O   1 
HETATM 16539 O  O   . HOH   YA 6 .   ? 0.187   2.974    -49.575 1.00 34.19 ? 346 HOH   L O   1 
HETATM 16540 O  O   . HOH   YA 6 .   ? -19.288 2.628    -64.954 1.00 44.24 ? 347 HOH   L O   1 
HETATM 16541 O  O   . HOH   YA 6 .   ? -12.587 -6.131   -74.685 1.00 43.08 ? 348 HOH   L O   1 
HETATM 16542 O  O   . HOH   YA 6 .   ? -9.906  -11.122  -59.596 1.00 56.07 ? 349 HOH   L O   1 
HETATM 16543 O  O   . HOH   YA 6 .   ? -18.249 7.803    -49.968 1.00 54.86 ? 350 HOH   L O   1 
HETATM 16544 O  O   . HOH   YA 6 .   ? -20.093 9.044    -40.795 1.00 51.24 ? 351 HOH   L O   1 
HETATM 16545 O  O   . HOH   YA 6 .   ? -24.977 4.200    -42.122 1.00 45.88 ? 352 HOH   L O   1 
HETATM 16546 O  O   . HOH   YA 6 .   ? 4.799   8.517    -62.970 1.00 42.49 ? 353 HOH   L O   1 
HETATM 16547 O  O   . HOH   YA 6 .   ? -12.771 10.533   -63.078 1.00 54.88 ? 354 HOH   L O   1 
HETATM 16548 O  O   . HOH   YA 6 .   ? -11.592 -11.538  -65.371 1.00 46.16 ? 355 HOH   L O   1 
HETATM 16549 O  O   . HOH   YA 6 .   ? -36.075 -7.867   -53.976 1.00 56.13 ? 356 HOH   L O   1 
HETATM 16550 O  O   . HOH   YA 6 .   ? -8.724  -12.301  -42.556 1.00 39.19 ? 357 HOH   L O   1 
HETATM 16551 O  O   . HOH   YA 6 .   ? -28.321 0.880    -49.178 1.00 41.34 ? 358 HOH   L O   1 
HETATM 16552 O  O   . HOH   YA 6 .   ? -14.530 -0.398   -81.929 1.00 50.55 ? 359 HOH   L O   1 
HETATM 16553 O  O   . HOH   YA 6 .   ? -13.003 -12.299  -63.798 1.00 54.21 ? 360 HOH   L O   1 
HETATM 16554 O  O   . HOH   YA 6 .   ? -10.070 -12.855  -66.458 1.00 51.49 ? 361 HOH   L O   1 
HETATM 16555 O  O   . HOH   YA 6 .   ? -29.691 -6.941   -54.461 1.00 47.00 ? 362 HOH   L O   1 
# 
