data_9BG5
# 
_entry.id   9BG5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BG5         pdb_00009bg5 10.2210/pdb9bg5/pdb 
WWPDB D_1000283226 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-19 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BG5 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-18 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jyano@revmed.com 
_pdbx_contact_author.name_first         Jason 
_pdbx_contact_author.name_last          Yano 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9774-2611 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tomlinson, A.C.A.' 1 0000-0002-9663-773X 
'Bieder, R.'        2 ?                   
'Chen, A.'          3 0000-0002-3259-5868 
'Knox, J.E.'        4 ?                   
'Yano, J.K.'        5 0000-0002-9774-2611 
# 
_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            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                6064 
_citation.page_last                 6083 
_citation.title                     
;Discovery of Daraxonrasib (RMC-6236), a Potent and Orally Bioavailable RAS(ON) Multi-selective, Noncovalent Tri-complex Inhibitor for the Treatment of Patients with Multiple RAS-Addicted Cancers.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02314 
_citation.pdbx_database_id_PubMed   40056080 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cregg, J.'         1  ? 
primary 'Edwards, A.V.'     2  ? 
primary 'Chang, S.'         3  ? 
primary 'Lee, B.J.'         4  ? 
primary 'Knox, J.E.'        5  ? 
primary 'Tomlinson, A.C.A.' 6  ? 
primary 'Marquez, A.'       7  ? 
primary 'Liu, Y.'           8  ? 
primary 'Freilich, R.'      9  ? 
primary 'Aay, N.'           10 ? 
primary 'Wang, Y.'          11 ? 
primary 'Jiang, L.'         12 ? 
primary 'Jiang, J.'         13 ? 
primary 'Wang, Z.'          14 ? 
primary 'Flagella, M.'      15 ? 
primary 'Wildes, D.'        16 ? 
primary 'Smith, J.A.M.'     17 ? 
primary 'Singh, M.'         18 ? 
primary 'Wang, Z.'          19 ? 
primary 'Gill, A.L.'        20 ? 
primary 'Koltun, E.S.'      21 ? 
# 
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 'GTPase KRas' 19416.873 2   3.6.5.2 G13D ? ? 
2 polymer     man 'Peptidyl-prolyl cis-trans isomerase A' 18123.582 2   5.2.1.8 ?    ? ? 
3 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' 522.196   2   ?       ?    ? ? 
4 non-polymer nat 'MAGNESIUM ION' 24.305    2   ?       ?    ? ? 
5 non-polymer syn 
;(1R,2S)-N-[(1P,7S,9S,13R,20M)-21-ethyl-20-{2-[(1R)-1-methoxyethyl]-5-(4-methylpiperazin-1-yl)pyridin-3-yl}-17,17-dimethyl-8,14-dioxo-15-oxa-4-thia-9,21,27,28-tetraazapentacyclo[17.5.2.1~2,5~.1~9,13~.0~22,26~]octacosa-1(24),2,5(28),19,22,25-hexaen-7-yl]-2-methylcyclopropane-1-carboxamide
;
811.047   2   ?       ?    ? ? 
6 water       nat water 18.015    539 ?       ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'K-Ras 2,Ki-Ras,c-K-ras,c-Ki-ras'                                 
2 'PPIase A,Cyclophilin A,Cyclosporin A-binding protein,Rotamase A' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;SMTEYKLVVVGAGDVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
;SMTEYKLVVVGAGDVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
A,B ? 
2 'polypeptide(L)' no no 
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' GNP   
4 'MAGNESIUM ION' MG    
5 
;(1R,2S)-N-[(1P,7S,9S,13R,20M)-21-ethyl-20-{2-[(1R)-1-methoxyethyl]-5-(4-methylpiperazin-1-yl)pyridin-3-yl}-17,17-dimethyl-8,14-dioxo-15-oxa-4-thia-9,21,27,28-tetraazapentacyclo[17.5.2.1~2,5~.1~9,13~.0~22,26~]octacosa-1(24),2,5(28),19,22,25-hexaen-7-yl]-2-methylcyclopropane-1-carboxamide
;
A1AHB 
6 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   THR n 
1 4   GLU n 
1 5   TYR n 
1 6   LYS n 
1 7   LEU n 
1 8   VAL n 
1 9   VAL n 
1 10  VAL n 
1 11  GLY n 
1 12  ALA n 
1 13  GLY n 
1 14  ASP n 
1 15  VAL n 
1 16  GLY n 
1 17  LYS n 
1 18  SER n 
1 19  ALA n 
1 20  LEU n 
1 21  THR n 
1 22  ILE n 
1 23  GLN n 
1 24  LEU n 
1 25  ILE n 
1 26  GLN n 
1 27  ASN n 
1 28  HIS n 
1 29  PHE n 
1 30  VAL n 
1 31  ASP n 
1 32  GLU n 
1 33  TYR n 
1 34  ASP n 
1 35  PRO n 
1 36  THR n 
1 37  ILE n 
1 38  GLU n 
1 39  ASP n 
1 40  SER n 
1 41  TYR n 
1 42  ARG n 
1 43  LYS n 
1 44  GLN n 
1 45  VAL n 
1 46  VAL n 
1 47  ILE n 
1 48  ASP n 
1 49  GLY n 
1 50  GLU n 
1 51  THR n 
1 52  CYS n 
1 53  LEU n 
1 54  LEU n 
1 55  ASP n 
1 56  ILE n 
1 57  LEU n 
1 58  ASP n 
1 59  THR n 
1 60  ALA n 
1 61  GLY n 
1 62  GLN n 
1 63  GLU n 
1 64  GLU n 
1 65  TYR n 
1 66  SER n 
1 67  ALA n 
1 68  MET n 
1 69  ARG n 
1 70  ASP n 
1 71  GLN n 
1 72  TYR n 
1 73  MET n 
1 74  ARG n 
1 75  THR n 
1 76  GLY n 
1 77  GLU n 
1 78  GLY n 
1 79  PHE n 
1 80  LEU n 
1 81  CYS n 
1 82  VAL n 
1 83  PHE n 
1 84  ALA n 
1 85  ILE n 
1 86  ASN n 
1 87  ASN n 
1 88  THR n 
1 89  LYS n 
1 90  SER n 
1 91  PHE n 
1 92  GLU n 
1 93  ASP n 
1 94  ILE n 
1 95  HIS n 
1 96  HIS n 
1 97  TYR n 
1 98  ARG n 
1 99  GLU n 
1 100 GLN n 
1 101 ILE n 
1 102 LYS n 
1 103 ARG n 
1 104 VAL n 
1 105 LYS n 
1 106 ASP n 
1 107 SER n 
1 108 GLU n 
1 109 ASP n 
1 110 VAL n 
1 111 PRO n 
1 112 MET n 
1 113 VAL n 
1 114 LEU n 
1 115 VAL n 
1 116 GLY n 
1 117 ASN n 
1 118 LYS n 
1 119 CYS n 
1 120 ASP n 
1 121 LEU n 
1 122 PRO n 
1 123 SER n 
1 124 ARG n 
1 125 THR n 
1 126 VAL n 
1 127 ASP n 
1 128 THR n 
1 129 LYS n 
1 130 GLN n 
1 131 ALA n 
1 132 GLN n 
1 133 ASP n 
1 134 LEU n 
1 135 ALA n 
1 136 ARG n 
1 137 SER n 
1 138 TYR n 
1 139 GLY n 
1 140 ILE n 
1 141 PRO n 
1 142 PHE n 
1 143 ILE n 
1 144 GLU n 
1 145 THR n 
1 146 SER n 
1 147 ALA n 
1 148 LYS n 
1 149 THR n 
1 150 ARG n 
1 151 GLN n 
1 152 GLY n 
1 153 VAL n 
1 154 ASP n 
1 155 ASP n 
1 156 ALA n 
1 157 PHE n 
1 158 TYR n 
1 159 THR n 
1 160 LEU n 
1 161 VAL n 
1 162 ARG n 
1 163 GLU n 
1 164 ILE n 
1 165 ARG n 
1 166 LYS n 
1 167 HIS n 
1 168 LYS n 
1 169 GLU n 
1 170 LYS n 
2 1   SER n 
2 2   MET n 
2 3   VAL n 
2 4   ASN n 
2 5   PRO n 
2 6   THR n 
2 7   VAL n 
2 8   PHE n 
2 9   PHE n 
2 10  ASP n 
2 11  ILE n 
2 12  ALA n 
2 13  VAL n 
2 14  ASP n 
2 15  GLY n 
2 16  GLU n 
2 17  PRO n 
2 18  LEU n 
2 19  GLY n 
2 20  ARG n 
2 21  VAL n 
2 22  SER n 
2 23  PHE n 
2 24  GLU n 
2 25  LEU n 
2 26  PHE n 
2 27  ALA n 
2 28  ASP n 
2 29  LYS n 
2 30  VAL n 
2 31  PRO n 
2 32  LYS n 
2 33  THR n 
2 34  ALA n 
2 35  GLU n 
2 36  ASN n 
2 37  PHE n 
2 38  ARG n 
2 39  ALA n 
2 40  LEU n 
2 41  SER n 
2 42  THR n 
2 43  GLY n 
2 44  GLU n 
2 45  LYS n 
2 46  GLY n 
2 47  PHE n 
2 48  GLY n 
2 49  TYR n 
2 50  LYS n 
2 51  GLY n 
2 52  SER n 
2 53  CYS n 
2 54  PHE n 
2 55  HIS n 
2 56  ARG n 
2 57  ILE n 
2 58  ILE n 
2 59  PRO n 
2 60  GLY n 
2 61  PHE n 
2 62  MET n 
2 63  CYS n 
2 64  GLN n 
2 65  GLY n 
2 66  GLY n 
2 67  ASP n 
2 68  PHE n 
2 69  THR n 
2 70  ARG n 
2 71  HIS n 
2 72  ASN n 
2 73  GLY n 
2 74  THR n 
2 75  GLY n 
2 76  GLY n 
2 77  LYS n 
2 78  SER n 
2 79  ILE n 
2 80  TYR n 
2 81  GLY n 
2 82  GLU n 
2 83  LYS n 
2 84  PHE n 
2 85  GLU n 
2 86  ASP n 
2 87  GLU n 
2 88  ASN n 
2 89  PHE n 
2 90  ILE n 
2 91  LEU n 
2 92  LYS n 
2 93  HIS n 
2 94  THR n 
2 95  GLY n 
2 96  PRO n 
2 97  GLY n 
2 98  ILE n 
2 99  LEU n 
2 100 SER n 
2 101 MET n 
2 102 ALA n 
2 103 ASN n 
2 104 ALA n 
2 105 GLY n 
2 106 PRO n 
2 107 ASN n 
2 108 THR n 
2 109 ASN n 
2 110 GLY n 
2 111 SER n 
2 112 GLN n 
2 113 PHE n 
2 114 PHE n 
2 115 ILE n 
2 116 CYS n 
2 117 THR n 
2 118 ALA n 
2 119 LYS n 
2 120 THR n 
2 121 GLU n 
2 122 TRP n 
2 123 LEU n 
2 124 ASP n 
2 125 GLY n 
2 126 LYS n 
2 127 HIS n 
2 128 VAL n 
2 129 VAL n 
2 130 PHE n 
2 131 GLY n 
2 132 LYS n 
2 133 VAL n 
2 134 LYS n 
2 135 GLU n 
2 136 GLY n 
2 137 MET n 
2 138 ASN n 
2 139 ILE n 
2 140 VAL n 
2 141 GLU n 
2 142 ALA n 
2 143 MET n 
2 144 GLU n 
2 145 ARG n 
2 146 PHE n 
2 147 GLY n 
2 148 SER n 
2 149 ARG n 
2 150 ASN n 
2 151 GLY n 
2 152 LYS n 
2 153 THR n 
2 154 SER n 
2 155 LYS n 
2 156 LYS n 
2 157 ILE n 
2 158 THR n 
2 159 ILE n 
2 160 ALA n 
2 161 ASP n 
2 162 CYS n 
2 163 GLY n 
2 164 GLN n 
2 165 LEU n 
2 166 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 170 human ? 'KRAS, KRAS2, RASK2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 166 human ? 'PPIA, CYPA'         ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1AHB non-polymer         . 
;(1R,2S)-N-[(1P,7S,9S,13R,20M)-21-ethyl-20-{2-[(1R)-1-methoxyethyl]-5-(4-methylpiperazin-1-yl)pyridin-3-yl}-17,17-dimethyl-8,14-dioxo-15-oxa-4-thia-9,21,27,28-tetraazapentacyclo[17.5.2.1~2,5~.1~9,13~.0~22,26~]octacosa-1(24),2,5(28),19,22,25-hexaen-7-yl]-2-methylcyclopropane-1-carboxamide
;
? 'C44 H58 N8 O5 S'   811.047 
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  
GNP   non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' ? 'C10 H17 N6 O13 P3' 522.196 
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'     149.211 
MG    non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'              24.305  
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   SER 1   0   0   SER SER A . n 
A 1 2   MET 2   1   1   MET MET A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   GLU 4   3   3   GLU GLU A . n 
A 1 5   TYR 5   4   4   TYR TYR A . n 
A 1 6   LYS 6   5   5   LYS LYS A . n 
A 1 7   LEU 7   6   6   LEU LEU A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   VAL 9   8   8   VAL VAL A . n 
A 1 10  VAL 10  9   9   VAL VAL A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ALA 12  11  11  ALA ALA A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  ASP 14  13  13  ASP ASP A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLY 16  15  15  GLY GLY A . n 
A 1 17  LYS 17  16  16  LYS LYS A . n 
A 1 18  SER 18  17  17  SER SER A . n 
A 1 19  ALA 19  18  18  ALA ALA A . n 
A 1 20  LEU 20  19  19  LEU LEU A . n 
A 1 21  THR 21  20  20  THR THR A . n 
A 1 22  ILE 22  21  21  ILE ILE A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LEU 24  23  23  LEU LEU A . n 
A 1 25  ILE 25  24  24  ILE ILE A . n 
A 1 26  GLN 26  25  25  GLN GLN A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  HIS 28  27  27  HIS HIS A . n 
A 1 29  PHE 29  28  28  PHE PHE A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  ASP 31  30  30  ASP ASP A . n 
A 1 32  GLU 32  31  31  GLU GLU A . n 
A 1 33  TYR 33  32  32  TYR TYR A . n 
A 1 34  ASP 34  33  33  ASP ASP A . n 
A 1 35  PRO 35  34  34  PRO PRO A . n 
A 1 36  THR 36  35  35  THR THR A . n 
A 1 37  ILE 37  36  36  ILE ILE A . n 
A 1 38  GLU 38  37  37  GLU GLU A . n 
A 1 39  ASP 39  38  38  ASP ASP A . n 
A 1 40  SER 40  39  39  SER SER A . n 
A 1 41  TYR 41  40  40  TYR TYR A . n 
A 1 42  ARG 42  41  41  ARG ARG A . n 
A 1 43  LYS 43  42  42  LYS LYS A . n 
A 1 44  GLN 44  43  43  GLN GLN A . n 
A 1 45  VAL 45  44  44  VAL VAL A . n 
A 1 46  VAL 46  45  45  VAL VAL A . n 
A 1 47  ILE 47  46  46  ILE ILE A . n 
A 1 48  ASP 48  47  47  ASP ASP A . n 
A 1 49  GLY 49  48  48  GLY GLY A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  THR 51  50  50  THR THR A . n 
A 1 52  CYS 52  51  51  CYS CYS A . n 
A 1 53  LEU 53  52  52  LEU LEU A . n 
A 1 54  LEU 54  53  53  LEU LEU A . n 
A 1 55  ASP 55  54  54  ASP ASP A . n 
A 1 56  ILE 56  55  55  ILE ILE A . n 
A 1 57  LEU 57  56  56  LEU LEU A . n 
A 1 58  ASP 58  57  57  ASP ASP A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  ALA 60  59  59  ALA ALA A . n 
A 1 61  GLY 61  60  60  GLY GLY A . n 
A 1 62  GLN 62  61  61  GLN GLN A . n 
A 1 63  GLU 63  62  62  GLU GLU A . n 
A 1 64  GLU 64  63  63  GLU GLU A . n 
A 1 65  TYR 65  64  64  TYR TYR A . n 
A 1 66  SER 66  65  65  SER SER A . n 
A 1 67  ALA 67  66  66  ALA ALA A . n 
A 1 68  MET 68  67  67  MET MET A . n 
A 1 69  ARG 69  68  68  ARG ARG A . n 
A 1 70  ASP 70  69  69  ASP ASP A . n 
A 1 71  GLN 71  70  70  GLN GLN A . n 
A 1 72  TYR 72  71  71  TYR TYR A . n 
A 1 73  MET 73  72  72  MET MET A . n 
A 1 74  ARG 74  73  73  ARG ARG A . n 
A 1 75  THR 75  74  74  THR THR A . n 
A 1 76  GLY 76  75  75  GLY GLY A . n 
A 1 77  GLU 77  76  76  GLU GLU A . n 
A 1 78  GLY 78  77  77  GLY GLY A . n 
A 1 79  PHE 79  78  78  PHE PHE A . n 
A 1 80  LEU 80  79  79  LEU LEU A . n 
A 1 81  CYS 81  80  80  CYS CYS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  PHE 83  82  82  PHE PHE A . n 
A 1 84  ALA 84  83  83  ALA ALA A . n 
A 1 85  ILE 85  84  84  ILE ILE A . n 
A 1 86  ASN 86  85  85  ASN ASN A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  THR 88  87  87  THR THR A . n 
A 1 89  LYS 89  88  88  LYS LYS A . n 
A 1 90  SER 90  89  89  SER SER A . n 
A 1 91  PHE 91  90  90  PHE PHE A . n 
A 1 92  GLU 92  91  91  GLU GLU A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  ILE 94  93  93  ILE ILE A . n 
A 1 95  HIS 95  94  94  HIS HIS A . n 
A 1 96  HIS 96  95  95  HIS HIS A . n 
A 1 97  TYR 97  96  96  TYR TYR A . n 
A 1 98  ARG 98  97  97  ARG ARG A . n 
A 1 99  GLU 99  98  98  GLU GLU A . n 
A 1 100 GLN 100 99  99  GLN GLN A . n 
A 1 101 ILE 101 100 100 ILE ILE A . n 
A 1 102 LYS 102 101 101 LYS LYS A . n 
A 1 103 ARG 103 102 102 ARG ARG A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 LYS 105 104 104 LYS LYS A . n 
A 1 106 ASP 106 105 105 ASP ASP A . n 
A 1 107 SER 107 106 106 SER SER A . n 
A 1 108 GLU 108 107 107 GLU GLU A . n 
A 1 109 ASP 109 108 108 ASP ASP A . n 
A 1 110 VAL 110 109 109 VAL VAL A . n 
A 1 111 PRO 111 110 110 PRO PRO A . n 
A 1 112 MET 112 111 111 MET MET A . n 
A 1 113 VAL 113 112 112 VAL VAL A . n 
A 1 114 LEU 114 113 113 LEU LEU A . n 
A 1 115 VAL 115 114 114 VAL VAL A . n 
A 1 116 GLY 116 115 115 GLY GLY A . n 
A 1 117 ASN 117 116 116 ASN ASN A . n 
A 1 118 LYS 118 117 117 LYS LYS A . n 
A 1 119 CYS 119 118 118 CYS CYS A . n 
A 1 120 ASP 120 119 119 ASP ASP A . n 
A 1 121 LEU 121 120 120 LEU LEU A . n 
A 1 122 PRO 122 121 121 PRO PRO A . n 
A 1 123 SER 123 122 122 SER SER A . n 
A 1 124 ARG 124 123 123 ARG ARG A . n 
A 1 125 THR 125 124 124 THR THR A . n 
A 1 126 VAL 126 125 125 VAL VAL A . n 
A 1 127 ASP 127 126 126 ASP ASP A . n 
A 1 128 THR 128 127 127 THR THR A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLN 130 129 129 GLN GLN A . n 
A 1 131 ALA 131 130 130 ALA ALA A . n 
A 1 132 GLN 132 131 131 GLN GLN A . n 
A 1 133 ASP 133 132 132 ASP ASP A . n 
A 1 134 LEU 134 133 133 LEU LEU A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 ARG 136 135 135 ARG ARG A . n 
A 1 137 SER 137 136 136 SER SER A . n 
A 1 138 TYR 138 137 137 TYR TYR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ILE 140 139 139 ILE ILE A . n 
A 1 141 PRO 141 140 140 PRO PRO A . n 
A 1 142 PHE 142 141 141 PHE PHE A . n 
A 1 143 ILE 143 142 142 ILE ILE A . n 
A 1 144 GLU 144 143 143 GLU GLU A . n 
A 1 145 THR 145 144 144 THR THR A . n 
A 1 146 SER 146 145 145 SER SER A . n 
A 1 147 ALA 147 146 146 ALA ALA A . n 
A 1 148 LYS 148 147 147 LYS LYS A . n 
A 1 149 THR 149 148 148 THR THR A . n 
A 1 150 ARG 150 149 149 ARG ARG A . n 
A 1 151 GLN 151 150 150 GLN GLN A . n 
A 1 152 GLY 152 151 151 GLY GLY A . n 
A 1 153 VAL 153 152 152 VAL VAL A . n 
A 1 154 ASP 154 153 153 ASP ASP A . n 
A 1 155 ASP 155 154 154 ASP ASP A . n 
A 1 156 ALA 156 155 155 ALA ALA A . n 
A 1 157 PHE 157 156 156 PHE PHE A . n 
A 1 158 TYR 158 157 157 TYR TYR A . n 
A 1 159 THR 159 158 158 THR THR A . n 
A 1 160 LEU 160 159 159 LEU LEU A . n 
A 1 161 VAL 161 160 160 VAL VAL A . n 
A 1 162 ARG 162 161 161 ARG ARG A . n 
A 1 163 GLU 163 162 162 GLU GLU A . n 
A 1 164 ILE 164 163 163 ILE ILE A . n 
A 1 165 ARG 165 164 164 ARG ARG A . n 
A 1 166 LYS 166 165 165 LYS LYS A . n 
A 1 167 HIS 167 166 166 HIS HIS A . n 
A 1 168 LYS 168 167 167 LYS LYS A . n 
A 1 169 GLU 169 168 168 GLU GLU A . n 
A 1 170 LYS 170 169 169 LYS LYS A . n 
B 1 1   SER 1   0   0   SER SER B . n 
B 1 2   MET 2   1   1   MET MET B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   GLU 4   3   3   GLU GLU B . n 
B 1 5   TYR 5   4   4   TYR TYR B . n 
B 1 6   LYS 6   5   5   LYS LYS B . n 
B 1 7   LEU 7   6   6   LEU LEU B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   VAL 9   8   8   VAL VAL B . n 
B 1 10  VAL 10  9   9   VAL VAL B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ALA 12  11  11  ALA ALA B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  ASP 14  13  13  ASP ASP B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  GLY 16  15  15  GLY GLY B . n 
B 1 17  LYS 17  16  16  LYS LYS B . n 
B 1 18  SER 18  17  17  SER SER B . n 
B 1 19  ALA 19  18  18  ALA ALA B . n 
B 1 20  LEU 20  19  19  LEU LEU B . n 
B 1 21  THR 21  20  20  THR THR B . n 
B 1 22  ILE 22  21  21  ILE ILE B . n 
B 1 23  GLN 23  22  22  GLN GLN B . n 
B 1 24  LEU 24  23  23  LEU LEU B . n 
B 1 25  ILE 25  24  24  ILE ILE B . n 
B 1 26  GLN 26  25  25  GLN GLN B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  HIS 28  27  27  HIS HIS B . n 
B 1 29  PHE 29  28  28  PHE PHE B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  ASP 31  30  30  ASP ASP B . n 
B 1 32  GLU 32  31  31  GLU GLU B . n 
B 1 33  TYR 33  32  32  TYR TYR B . n 
B 1 34  ASP 34  33  33  ASP ASP B . n 
B 1 35  PRO 35  34  34  PRO PRO B . n 
B 1 36  THR 36  35  35  THR THR B . n 
B 1 37  ILE 37  36  36  ILE ILE B . n 
B 1 38  GLU 38  37  37  GLU GLU B . n 
B 1 39  ASP 39  38  38  ASP ASP B . n 
B 1 40  SER 40  39  39  SER SER B . n 
B 1 41  TYR 41  40  40  TYR TYR B . n 
B 1 42  ARG 42  41  41  ARG ARG B . n 
B 1 43  LYS 43  42  42  LYS LYS B . n 
B 1 44  GLN 44  43  43  GLN GLN B . n 
B 1 45  VAL 45  44  44  VAL VAL B . n 
B 1 46  VAL 46  45  45  VAL VAL B . n 
B 1 47  ILE 47  46  46  ILE ILE B . n 
B 1 48  ASP 48  47  47  ASP ASP B . n 
B 1 49  GLY 49  48  48  GLY GLY B . n 
B 1 50  GLU 50  49  49  GLU GLU B . n 
B 1 51  THR 51  50  50  THR THR B . n 
B 1 52  CYS 52  51  51  CYS CYS B . n 
B 1 53  LEU 53  52  52  LEU LEU B . n 
B 1 54  LEU 54  53  53  LEU LEU B . n 
B 1 55  ASP 55  54  54  ASP ASP B . n 
B 1 56  ILE 56  55  55  ILE ILE B . n 
B 1 57  LEU 57  56  56  LEU LEU B . n 
B 1 58  ASP 58  57  57  ASP ASP B . n 
B 1 59  THR 59  58  58  THR THR B . n 
B 1 60  ALA 60  59  59  ALA ALA B . n 
B 1 61  GLY 61  60  60  GLY GLY B . n 
B 1 62  GLN 62  61  61  GLN GLN B . n 
B 1 63  GLU 63  62  62  GLU GLU B . n 
B 1 64  GLU 64  63  63  GLU GLU B . n 
B 1 65  TYR 65  64  64  TYR TYR B . n 
B 1 66  SER 66  65  65  SER SER B . n 
B 1 67  ALA 67  66  66  ALA ALA B . n 
B 1 68  MET 68  67  67  MET MET B . n 
B 1 69  ARG 69  68  68  ARG ARG B . n 
B 1 70  ASP 70  69  69  ASP ASP B . n 
B 1 71  GLN 71  70  70  GLN GLN B . n 
B 1 72  TYR 72  71  71  TYR TYR B . n 
B 1 73  MET 73  72  72  MET MET B . n 
B 1 74  ARG 74  73  73  ARG ARG B . n 
B 1 75  THR 75  74  74  THR THR B . n 
B 1 76  GLY 76  75  75  GLY GLY B . n 
B 1 77  GLU 77  76  76  GLU GLU B . n 
B 1 78  GLY 78  77  77  GLY GLY B . n 
B 1 79  PHE 79  78  78  PHE PHE B . n 
B 1 80  LEU 80  79  79  LEU LEU B . n 
B 1 81  CYS 81  80  80  CYS CYS B . n 
B 1 82  VAL 82  81  81  VAL VAL B . n 
B 1 83  PHE 83  82  82  PHE PHE B . n 
B 1 84  ALA 84  83  83  ALA ALA B . n 
B 1 85  ILE 85  84  84  ILE ILE B . n 
B 1 86  ASN 86  85  85  ASN ASN B . n 
B 1 87  ASN 87  86  86  ASN ASN B . n 
B 1 88  THR 88  87  87  THR THR B . n 
B 1 89  LYS 89  88  88  LYS LYS B . n 
B 1 90  SER 90  89  89  SER SER B . n 
B 1 91  PHE 91  90  90  PHE PHE B . n 
B 1 92  GLU 92  91  91  GLU GLU B . n 
B 1 93  ASP 93  92  92  ASP ASP B . n 
B 1 94  ILE 94  93  93  ILE ILE B . n 
B 1 95  HIS 95  94  94  HIS HIS B . n 
B 1 96  HIS 96  95  95  HIS HIS B . n 
B 1 97  TYR 97  96  96  TYR TYR B . n 
B 1 98  ARG 98  97  97  ARG ARG B . n 
B 1 99  GLU 99  98  98  GLU GLU B . n 
B 1 100 GLN 100 99  99  GLN GLN B . n 
B 1 101 ILE 101 100 100 ILE ILE B . n 
B 1 102 LYS 102 101 101 LYS LYS B . n 
B 1 103 ARG 103 102 102 ARG ARG B . n 
B 1 104 VAL 104 103 103 VAL VAL B . n 
B 1 105 LYS 105 104 104 LYS LYS B . n 
B 1 106 ASP 106 105 105 ASP ASP B . n 
B 1 107 SER 107 106 106 SER SER B . n 
B 1 108 GLU 108 107 107 GLU GLU B . n 
B 1 109 ASP 109 108 108 ASP ASP B . n 
B 1 110 VAL 110 109 109 VAL VAL B . n 
B 1 111 PRO 111 110 110 PRO PRO B . n 
B 1 112 MET 112 111 111 MET MET B . n 
B 1 113 VAL 113 112 112 VAL VAL B . n 
B 1 114 LEU 114 113 113 LEU LEU B . n 
B 1 115 VAL 115 114 114 VAL VAL B . n 
B 1 116 GLY 116 115 115 GLY GLY B . n 
B 1 117 ASN 117 116 116 ASN ASN B . n 
B 1 118 LYS 118 117 117 LYS LYS B . n 
B 1 119 CYS 119 118 118 CYS CYS B . n 
B 1 120 ASP 120 119 119 ASP ASP B . n 
B 1 121 LEU 121 120 120 LEU LEU B . n 
B 1 122 PRO 122 121 121 PRO PRO B . n 
B 1 123 SER 123 122 122 SER SER B . n 
B 1 124 ARG 124 123 123 ARG ARG B . n 
B 1 125 THR 125 124 124 THR THR B . n 
B 1 126 VAL 126 125 125 VAL VAL B . n 
B 1 127 ASP 127 126 126 ASP ASP B . n 
B 1 128 THR 128 127 127 THR THR B . n 
B 1 129 LYS 129 128 128 LYS LYS B . n 
B 1 130 GLN 130 129 129 GLN GLN B . n 
B 1 131 ALA 131 130 130 ALA ALA B . n 
B 1 132 GLN 132 131 131 GLN GLN B . n 
B 1 133 ASP 133 132 132 ASP ASP B . n 
B 1 134 LEU 134 133 133 LEU LEU B . n 
B 1 135 ALA 135 134 134 ALA ALA B . n 
B 1 136 ARG 136 135 135 ARG ARG B . n 
B 1 137 SER 137 136 136 SER SER B . n 
B 1 138 TYR 138 137 137 TYR TYR B . n 
B 1 139 GLY 139 138 138 GLY GLY B . n 
B 1 140 ILE 140 139 139 ILE ILE B . n 
B 1 141 PRO 141 140 140 PRO PRO B . n 
B 1 142 PHE 142 141 141 PHE PHE B . n 
B 1 143 ILE 143 142 142 ILE ILE B . n 
B 1 144 GLU 144 143 143 GLU GLU B . n 
B 1 145 THR 145 144 144 THR THR B . n 
B 1 146 SER 146 145 145 SER SER B . n 
B 1 147 ALA 147 146 146 ALA ALA B . n 
B 1 148 LYS 148 147 147 LYS LYS B . n 
B 1 149 THR 149 148 148 THR THR B . n 
B 1 150 ARG 150 149 149 ARG ARG B . n 
B 1 151 GLN 151 150 150 GLN GLN B . n 
B 1 152 GLY 152 151 151 GLY GLY B . n 
B 1 153 VAL 153 152 152 VAL VAL B . n 
B 1 154 ASP 154 153 153 ASP ASP B . n 
B 1 155 ASP 155 154 154 ASP ASP B . n 
B 1 156 ALA 156 155 155 ALA ALA B . n 
B 1 157 PHE 157 156 156 PHE PHE B . n 
B 1 158 TYR 158 157 157 TYR TYR B . n 
B 1 159 THR 159 158 158 THR THR B . n 
B 1 160 LEU 160 159 159 LEU LEU B . n 
B 1 161 VAL 161 160 160 VAL VAL B . n 
B 1 162 ARG 162 161 161 ARG ARG B . n 
B 1 163 GLU 163 162 162 GLU GLU B . n 
B 1 164 ILE 164 163 163 ILE ILE B . n 
B 1 165 ARG 165 164 164 ARG ARG B . n 
B 1 166 LYS 166 165 165 LYS LYS B . n 
B 1 167 HIS 167 166 166 HIS HIS B . n 
B 1 168 LYS 168 167 167 LYS LYS B . n 
B 1 169 GLU 169 168 168 GLU GLU B . n 
B 1 170 LYS 170 169 169 LYS LYS B . n 
C 2 1   SER 1   0   ?   ?   ?   C . n 
C 2 2   MET 2   1   ?   ?   ?   C . n 
C 2 3   VAL 3   2   2   VAL VAL C . n 
C 2 4   ASN 4   3   3   ASN ASN C . n 
C 2 5   PRO 5   4   4   PRO PRO C . n 
C 2 6   THR 6   5   5   THR THR C . n 
C 2 7   VAL 7   6   6   VAL VAL C . n 
C 2 8   PHE 8   7   7   PHE PHE C . n 
C 2 9   PHE 9   8   8   PHE PHE C . n 
C 2 10  ASP 10  9   9   ASP ASP C . n 
C 2 11  ILE 11  10  10  ILE ILE C . n 
C 2 12  ALA 12  11  11  ALA ALA C . n 
C 2 13  VAL 13  12  12  VAL VAL C . n 
C 2 14  ASP 14  13  13  ASP ASP C . n 
C 2 15  GLY 15  14  14  GLY GLY C . n 
C 2 16  GLU 16  15  15  GLU GLU C . n 
C 2 17  PRO 17  16  16  PRO PRO C . n 
C 2 18  LEU 18  17  17  LEU LEU C . n 
C 2 19  GLY 19  18  18  GLY GLY C . n 
C 2 20  ARG 20  19  19  ARG ARG C . n 
C 2 21  VAL 21  20  20  VAL VAL C . n 
C 2 22  SER 22  21  21  SER SER C . n 
C 2 23  PHE 23  22  22  PHE PHE C . n 
C 2 24  GLU 24  23  23  GLU GLU C . n 
C 2 25  LEU 25  24  24  LEU LEU C . n 
C 2 26  PHE 26  25  25  PHE PHE C . n 
C 2 27  ALA 27  26  26  ALA ALA C . n 
C 2 28  ASP 28  27  27  ASP ASP C . n 
C 2 29  LYS 29  28  28  LYS LYS C . n 
C 2 30  VAL 30  29  29  VAL VAL C . n 
C 2 31  PRO 31  30  30  PRO PRO C . n 
C 2 32  LYS 32  31  31  LYS LYS C . n 
C 2 33  THR 33  32  32  THR THR C . n 
C 2 34  ALA 34  33  33  ALA ALA C . n 
C 2 35  GLU 35  34  34  GLU GLU C . n 
C 2 36  ASN 36  35  35  ASN ASN C . n 
C 2 37  PHE 37  36  36  PHE PHE C . n 
C 2 38  ARG 38  37  37  ARG ARG C . n 
C 2 39  ALA 39  38  38  ALA ALA C . n 
C 2 40  LEU 40  39  39  LEU LEU C . n 
C 2 41  SER 41  40  40  SER SER C . n 
C 2 42  THR 42  41  41  THR THR C . n 
C 2 43  GLY 43  42  42  GLY GLY C . n 
C 2 44  GLU 44  43  43  GLU GLU C . n 
C 2 45  LYS 45  44  44  LYS LYS C . n 
C 2 46  GLY 46  45  45  GLY GLY C . n 
C 2 47  PHE 47  46  46  PHE PHE C . n 
C 2 48  GLY 48  47  47  GLY GLY C . n 
C 2 49  TYR 49  48  48  TYR TYR C . n 
C 2 50  LYS 50  49  49  LYS LYS C . n 
C 2 51  GLY 51  50  50  GLY GLY C . n 
C 2 52  SER 52  51  51  SER SER C . n 
C 2 53  CYS 53  52  52  CYS CYS C . n 
C 2 54  PHE 54  53  53  PHE PHE C . n 
C 2 55  HIS 55  54  54  HIS HIS C . n 
C 2 56  ARG 56  55  55  ARG ARG C . n 
C 2 57  ILE 57  56  56  ILE ILE C . n 
C 2 58  ILE 58  57  57  ILE ILE C . n 
C 2 59  PRO 59  58  58  PRO PRO C . n 
C 2 60  GLY 60  59  59  GLY GLY C . n 
C 2 61  PHE 61  60  60  PHE PHE C . n 
C 2 62  MET 62  61  61  MET MET C . n 
C 2 63  CYS 63  62  62  CYS CYS C . n 
C 2 64  GLN 64  63  63  GLN GLN C . n 
C 2 65  GLY 65  64  64  GLY GLY C . n 
C 2 66  GLY 66  65  65  GLY GLY C . n 
C 2 67  ASP 67  66  66  ASP ASP C . n 
C 2 68  PHE 68  67  67  PHE PHE C . n 
C 2 69  THR 69  68  68  THR THR C . n 
C 2 70  ARG 70  69  69  ARG ARG C . n 
C 2 71  HIS 71  70  70  HIS HIS C . n 
C 2 72  ASN 72  71  71  ASN ASN C . n 
C 2 73  GLY 73  72  72  GLY GLY C . n 
C 2 74  THR 74  73  73  THR THR C . n 
C 2 75  GLY 75  74  74  GLY GLY C . n 
C 2 76  GLY 76  75  75  GLY GLY C . n 
C 2 77  LYS 77  76  76  LYS LYS C . n 
C 2 78  SER 78  77  77  SER SER C . n 
C 2 79  ILE 79  78  78  ILE ILE C . n 
C 2 80  TYR 80  79  79  TYR TYR C . n 
C 2 81  GLY 81  80  80  GLY GLY C . n 
C 2 82  GLU 82  81  81  GLU GLU C . n 
C 2 83  LYS 83  82  82  LYS LYS C . n 
C 2 84  PHE 84  83  83  PHE PHE C . n 
C 2 85  GLU 85  84  84  GLU GLU C . n 
C 2 86  ASP 86  85  85  ASP ASP C . n 
C 2 87  GLU 87  86  86  GLU GLU C . n 
C 2 88  ASN 88  87  87  ASN ASN C . n 
C 2 89  PHE 89  88  88  PHE PHE C . n 
C 2 90  ILE 90  89  89  ILE ILE C . n 
C 2 91  LEU 91  90  90  LEU LEU C . n 
C 2 92  LYS 92  91  91  LYS LYS C . n 
C 2 93  HIS 93  92  92  HIS HIS C . n 
C 2 94  THR 94  93  93  THR THR C . n 
C 2 95  GLY 95  94  94  GLY GLY C . n 
C 2 96  PRO 96  95  95  PRO PRO C . n 
C 2 97  GLY 97  96  96  GLY GLY C . n 
C 2 98  ILE 98  97  97  ILE ILE C . n 
C 2 99  LEU 99  98  98  LEU LEU C . n 
C 2 100 SER 100 99  99  SER SER C . n 
C 2 101 MET 101 100 100 MET MET C . n 
C 2 102 ALA 102 101 101 ALA ALA C . n 
C 2 103 ASN 103 102 102 ASN ASN C . n 
C 2 104 ALA 104 103 103 ALA ALA C . n 
C 2 105 GLY 105 104 104 GLY GLY C . n 
C 2 106 PRO 106 105 105 PRO PRO C . n 
C 2 107 ASN 107 106 106 ASN ASN C . n 
C 2 108 THR 108 107 107 THR THR C . n 
C 2 109 ASN 109 108 108 ASN ASN C . n 
C 2 110 GLY 110 109 109 GLY GLY C . n 
C 2 111 SER 111 110 110 SER SER C . n 
C 2 112 GLN 112 111 111 GLN GLN C . n 
C 2 113 PHE 113 112 112 PHE PHE C . n 
C 2 114 PHE 114 113 113 PHE PHE C . n 
C 2 115 ILE 115 114 114 ILE ILE C . n 
C 2 116 CYS 116 115 115 CYS CYS C . n 
C 2 117 THR 117 116 116 THR THR C . n 
C 2 118 ALA 118 117 117 ALA ALA C . n 
C 2 119 LYS 119 118 118 LYS LYS C . n 
C 2 120 THR 120 119 119 THR THR C . n 
C 2 121 GLU 121 120 120 GLU GLU C . n 
C 2 122 TRP 122 121 121 TRP TRP C . n 
C 2 123 LEU 123 122 122 LEU LEU C . n 
C 2 124 ASP 124 123 123 ASP ASP C . n 
C 2 125 GLY 125 124 124 GLY GLY C . n 
C 2 126 LYS 126 125 125 LYS LYS C . n 
C 2 127 HIS 127 126 126 HIS HIS C . n 
C 2 128 VAL 128 127 127 VAL VAL C . n 
C 2 129 VAL 129 128 128 VAL VAL C . n 
C 2 130 PHE 130 129 129 PHE PHE C . n 
C 2 131 GLY 131 130 130 GLY GLY C . n 
C 2 132 LYS 132 131 131 LYS LYS C . n 
C 2 133 VAL 133 132 132 VAL VAL C . n 
C 2 134 LYS 134 133 133 LYS LYS C . n 
C 2 135 GLU 135 134 134 GLU GLU C . n 
C 2 136 GLY 136 135 135 GLY GLY C . n 
C 2 137 MET 137 136 136 MET MET C . n 
C 2 138 ASN 138 137 137 ASN ASN C . n 
C 2 139 ILE 139 138 138 ILE ILE C . n 
C 2 140 VAL 140 139 139 VAL VAL C . n 
C 2 141 GLU 141 140 140 GLU GLU C . n 
C 2 142 ALA 142 141 141 ALA ALA C . n 
C 2 143 MET 143 142 142 MET MET C . n 
C 2 144 GLU 144 143 143 GLU GLU C . n 
C 2 145 ARG 145 144 144 ARG ARG C . n 
C 2 146 PHE 146 145 145 PHE PHE C . n 
C 2 147 GLY 147 146 146 GLY GLY C . n 
C 2 148 SER 148 147 147 SER SER C . n 
C 2 149 ARG 149 148 148 ARG ARG C . n 
C 2 150 ASN 150 149 149 ASN ASN C . n 
C 2 151 GLY 151 150 150 GLY GLY C . n 
C 2 152 LYS 152 151 151 LYS LYS C . n 
C 2 153 THR 153 152 152 THR THR C . n 
C 2 154 SER 154 153 153 SER SER C . n 
C 2 155 LYS 155 154 154 LYS LYS C . n 
C 2 156 LYS 156 155 155 LYS LYS C . n 
C 2 157 ILE 157 156 156 ILE ILE C . n 
C 2 158 THR 158 157 157 THR THR C . n 
C 2 159 ILE 159 158 158 ILE ILE C . n 
C 2 160 ALA 160 159 159 ALA ALA C . n 
C 2 161 ASP 161 160 160 ASP ASP C . n 
C 2 162 CYS 162 161 161 CYS CYS C . n 
C 2 163 GLY 163 162 162 GLY GLY C . n 
C 2 164 GLN 164 163 163 GLN GLN C . n 
C 2 165 LEU 165 164 164 LEU LEU C . n 
C 2 166 GLU 166 165 ?   ?   ?   C . n 
D 2 1   SER 1   0   ?   ?   ?   D . n 
D 2 2   MET 2   1   ?   ?   ?   D . n 
D 2 3   VAL 3   2   2   VAL VAL D . n 
D 2 4   ASN 4   3   3   ASN ASN D . n 
D 2 5   PRO 5   4   4   PRO PRO D . n 
D 2 6   THR 6   5   5   THR THR D . n 
D 2 7   VAL 7   6   6   VAL VAL D . n 
D 2 8   PHE 8   7   7   PHE PHE D . n 
D 2 9   PHE 9   8   8   PHE PHE D . n 
D 2 10  ASP 10  9   9   ASP ASP D . n 
D 2 11  ILE 11  10  10  ILE ILE D . n 
D 2 12  ALA 12  11  11  ALA ALA D . n 
D 2 13  VAL 13  12  12  VAL VAL D . n 
D 2 14  ASP 14  13  13  ASP ASP D . n 
D 2 15  GLY 15  14  14  GLY GLY D . n 
D 2 16  GLU 16  15  15  GLU GLU D . n 
D 2 17  PRO 17  16  16  PRO PRO D . n 
D 2 18  LEU 18  17  17  LEU LEU D . n 
D 2 19  GLY 19  18  18  GLY GLY D . n 
D 2 20  ARG 20  19  19  ARG ARG D . n 
D 2 21  VAL 21  20  20  VAL VAL D . n 
D 2 22  SER 22  21  21  SER SER D . n 
D 2 23  PHE 23  22  22  PHE PHE D . n 
D 2 24  GLU 24  23  23  GLU GLU D . n 
D 2 25  LEU 25  24  24  LEU LEU D . n 
D 2 26  PHE 26  25  25  PHE PHE D . n 
D 2 27  ALA 27  26  26  ALA ALA D . n 
D 2 28  ASP 28  27  27  ASP ASP D . n 
D 2 29  LYS 29  28  28  LYS LYS D . n 
D 2 30  VAL 30  29  29  VAL VAL D . n 
D 2 31  PRO 31  30  30  PRO PRO D . n 
D 2 32  LYS 32  31  31  LYS LYS D . n 
D 2 33  THR 33  32  32  THR THR D . n 
D 2 34  ALA 34  33  33  ALA ALA D . n 
D 2 35  GLU 35  34  34  GLU GLU D . n 
D 2 36  ASN 36  35  35  ASN ASN D . n 
D 2 37  PHE 37  36  36  PHE PHE D . n 
D 2 38  ARG 38  37  37  ARG ARG D . n 
D 2 39  ALA 39  38  38  ALA ALA D . n 
D 2 40  LEU 40  39  39  LEU LEU D . n 
D 2 41  SER 41  40  40  SER SER D . n 
D 2 42  THR 42  41  41  THR THR D . n 
D 2 43  GLY 43  42  42  GLY GLY D . n 
D 2 44  GLU 44  43  43  GLU GLU D . n 
D 2 45  LYS 45  44  44  LYS LYS D . n 
D 2 46  GLY 46  45  45  GLY GLY D . n 
D 2 47  PHE 47  46  46  PHE PHE D . n 
D 2 48  GLY 48  47  47  GLY GLY D . n 
D 2 49  TYR 49  48  48  TYR TYR D . n 
D 2 50  LYS 50  49  49  LYS LYS D . n 
D 2 51  GLY 51  50  50  GLY GLY D . n 
D 2 52  SER 52  51  51  SER SER D . n 
D 2 53  CYS 53  52  52  CYS CYS D . n 
D 2 54  PHE 54  53  53  PHE PHE D . n 
D 2 55  HIS 55  54  54  HIS HIS D . n 
D 2 56  ARG 56  55  55  ARG ARG D . n 
D 2 57  ILE 57  56  56  ILE ILE D . n 
D 2 58  ILE 58  57  57  ILE ILE D . n 
D 2 59  PRO 59  58  58  PRO PRO D . n 
D 2 60  GLY 60  59  59  GLY GLY D . n 
D 2 61  PHE 61  60  60  PHE PHE D . n 
D 2 62  MET 62  61  61  MET MET D . n 
D 2 63  CYS 63  62  62  CYS CYS D . n 
D 2 64  GLN 64  63  63  GLN GLN D . n 
D 2 65  GLY 65  64  64  GLY GLY D . n 
D 2 66  GLY 66  65  65  GLY GLY D . n 
D 2 67  ASP 67  66  66  ASP ASP D . n 
D 2 68  PHE 68  67  67  PHE PHE D . n 
D 2 69  THR 69  68  68  THR THR D . n 
D 2 70  ARG 70  69  69  ARG ARG D . n 
D 2 71  HIS 71  70  70  HIS HIS D . n 
D 2 72  ASN 72  71  71  ASN ASN D . n 
D 2 73  GLY 73  72  72  GLY GLY D . n 
D 2 74  THR 74  73  73  THR THR D . n 
D 2 75  GLY 75  74  74  GLY GLY D . n 
D 2 76  GLY 76  75  75  GLY GLY D . n 
D 2 77  LYS 77  76  76  LYS LYS D . n 
D 2 78  SER 78  77  77  SER SER D . n 
D 2 79  ILE 79  78  78  ILE ILE D . n 
D 2 80  TYR 80  79  79  TYR TYR D . n 
D 2 81  GLY 81  80  80  GLY GLY D . n 
D 2 82  GLU 82  81  81  GLU GLU D . n 
D 2 83  LYS 83  82  82  LYS LYS D . n 
D 2 84  PHE 84  83  83  PHE PHE D . n 
D 2 85  GLU 85  84  84  GLU GLU D . n 
D 2 86  ASP 86  85  85  ASP ASP D . n 
D 2 87  GLU 87  86  86  GLU GLU D . n 
D 2 88  ASN 88  87  87  ASN ASN D . n 
D 2 89  PHE 89  88  88  PHE PHE D . n 
D 2 90  ILE 90  89  89  ILE ILE D . n 
D 2 91  LEU 91  90  90  LEU LEU D . n 
D 2 92  LYS 92  91  91  LYS LYS D . n 
D 2 93  HIS 93  92  92  HIS HIS D . n 
D 2 94  THR 94  93  93  THR THR D . n 
D 2 95  GLY 95  94  94  GLY GLY D . n 
D 2 96  PRO 96  95  95  PRO PRO D . n 
D 2 97  GLY 97  96  96  GLY GLY D . n 
D 2 98  ILE 98  97  97  ILE ILE D . n 
D 2 99  LEU 99  98  98  LEU LEU D . n 
D 2 100 SER 100 99  99  SER SER D . n 
D 2 101 MET 101 100 100 MET MET D . n 
D 2 102 ALA 102 101 101 ALA ALA D . n 
D 2 103 ASN 103 102 102 ASN ASN D . n 
D 2 104 ALA 104 103 103 ALA ALA D . n 
D 2 105 GLY 105 104 104 GLY GLY D . n 
D 2 106 PRO 106 105 105 PRO PRO D . n 
D 2 107 ASN 107 106 106 ASN ASN D . n 
D 2 108 THR 108 107 107 THR THR D . n 
D 2 109 ASN 109 108 108 ASN ASN D . n 
D 2 110 GLY 110 109 109 GLY GLY D . n 
D 2 111 SER 111 110 110 SER SER D . n 
D 2 112 GLN 112 111 111 GLN GLN D . n 
D 2 113 PHE 113 112 112 PHE PHE D . n 
D 2 114 PHE 114 113 113 PHE PHE D . n 
D 2 115 ILE 115 114 114 ILE ILE D . n 
D 2 116 CYS 116 115 115 CYS CYS D . n 
D 2 117 THR 117 116 116 THR THR D . n 
D 2 118 ALA 118 117 117 ALA ALA D . n 
D 2 119 LYS 119 118 118 LYS LYS D . n 
D 2 120 THR 120 119 119 THR THR D . n 
D 2 121 GLU 121 120 120 GLU GLU D . n 
D 2 122 TRP 122 121 121 TRP TRP D . n 
D 2 123 LEU 123 122 122 LEU LEU D . n 
D 2 124 ASP 124 123 123 ASP ASP D . n 
D 2 125 GLY 125 124 124 GLY GLY D . n 
D 2 126 LYS 126 125 125 LYS LYS D . n 
D 2 127 HIS 127 126 126 HIS HIS D . n 
D 2 128 VAL 128 127 127 VAL VAL D . n 
D 2 129 VAL 129 128 128 VAL VAL D . n 
D 2 130 PHE 130 129 129 PHE PHE D . n 
D 2 131 GLY 131 130 130 GLY GLY D . n 
D 2 132 LYS 132 131 131 LYS LYS D . n 
D 2 133 VAL 133 132 132 VAL VAL D . n 
D 2 134 LYS 134 133 133 LYS LYS D . n 
D 2 135 GLU 135 134 134 GLU GLU D . n 
D 2 136 GLY 136 135 135 GLY GLY D . n 
D 2 137 MET 137 136 136 MET MET D . n 
D 2 138 ASN 138 137 137 ASN ASN D . n 
D 2 139 ILE 139 138 138 ILE ILE D . n 
D 2 140 VAL 140 139 139 VAL VAL D . n 
D 2 141 GLU 141 140 140 GLU GLU D . n 
D 2 142 ALA 142 141 141 ALA ALA D . n 
D 2 143 MET 143 142 142 MET MET D . n 
D 2 144 GLU 144 143 143 GLU GLU D . n 
D 2 145 ARG 145 144 144 ARG ARG D . n 
D 2 146 PHE 146 145 145 PHE PHE D . n 
D 2 147 GLY 147 146 146 GLY GLY D . n 
D 2 148 SER 148 147 147 SER SER D . n 
D 2 149 ARG 149 148 148 ARG ARG D . n 
D 2 150 ASN 150 149 149 ASN ASN D . n 
D 2 151 GLY 151 150 150 GLY GLY D . n 
D 2 152 LYS 152 151 151 LYS LYS D . n 
D 2 153 THR 153 152 152 THR THR D . n 
D 2 154 SER 154 153 153 SER SER D . n 
D 2 155 LYS 155 154 154 LYS LYS D . n 
D 2 156 LYS 156 155 155 LYS LYS D . n 
D 2 157 ILE 157 156 156 ILE ILE D . n 
D 2 158 THR 158 157 157 THR THR D . n 
D 2 159 ILE 159 158 158 ILE ILE D . n 
D 2 160 ALA 160 159 159 ALA ALA D . n 
D 2 161 ASP 161 160 160 ASP ASP D . n 
D 2 162 CYS 162 161 161 CYS CYS D . n 
D 2 163 GLY 163 162 162 GLY GLY D . n 
D 2 164 GLN 164 163 163 GLN GLN D . n 
D 2 165 LEU 165 164 164 LEU LEU D . n 
D 2 166 GLU 166 165 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AHB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AHB 
_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 
E 3 GNP   1   201 201  GNP   GNP A . 
F 4 MG    1   202 301  MG    MG  A . 
G 3 GNP   1   201 201  GNP   GNP B . 
H 4 MG    1   202 301  MG    MG  B . 
I 5 A1AHB 1   201 6236 A1AHB RMC C . 
J 5 A1AHB 1   201 6236 A1AHB RMC D . 
K 6 HOH   1   301 146  HOH   HOH A . 
K 6 HOH   2   302 36   HOH   HOH A . 
K 6 HOH   3   303 257  HOH   HOH A . 
K 6 HOH   4   304 135  HOH   HOH A . 
K 6 HOH   5   305 423  HOH   HOH A . 
K 6 HOH   6   306 335  HOH   HOH A . 
K 6 HOH   7   307 37   HOH   HOH A . 
K 6 HOH   8   308 311  HOH   HOH A . 
K 6 HOH   9   309 456  HOH   HOH A . 
K 6 HOH   10  310 122  HOH   HOH A . 
K 6 HOH   11  311 93   HOH   HOH A . 
K 6 HOH   12  312 14   HOH   HOH A . 
K 6 HOH   13  313 180  HOH   HOH A . 
K 6 HOH   14  314 543  HOH   HOH A . 
K 6 HOH   15  315 105  HOH   HOH A . 
K 6 HOH   16  316 556  HOH   HOH A . 
K 6 HOH   17  317 465  HOH   HOH A . 
K 6 HOH   18  318 211  HOH   HOH A . 
K 6 HOH   19  319 553  HOH   HOH A . 
K 6 HOH   20  320 103  HOH   HOH A . 
K 6 HOH   21  321 295  HOH   HOH A . 
K 6 HOH   22  322 548  HOH   HOH A . 
K 6 HOH   23  323 154  HOH   HOH A . 
K 6 HOH   24  324 1    HOH   HOH A . 
K 6 HOH   25  325 179  HOH   HOH A . 
K 6 HOH   26  326 508  HOH   HOH A . 
K 6 HOH   27  327 83   HOH   HOH A . 
K 6 HOH   28  328 371  HOH   HOH A . 
K 6 HOH   29  329 394  HOH   HOH A . 
K 6 HOH   30  330 21   HOH   HOH A . 
K 6 HOH   31  331 449  HOH   HOH A . 
K 6 HOH   32  332 129  HOH   HOH A . 
K 6 HOH   33  333 400  HOH   HOH A . 
K 6 HOH   34  334 3    HOH   HOH A . 
K 6 HOH   35  335 488  HOH   HOH A . 
K 6 HOH   36  336 189  HOH   HOH A . 
K 6 HOH   37  337 328  HOH   HOH A . 
K 6 HOH   38  338 52   HOH   HOH A . 
K 6 HOH   39  339 450  HOH   HOH A . 
K 6 HOH   40  340 63   HOH   HOH A . 
K 6 HOH   41  341 156  HOH   HOH A . 
K 6 HOH   42  342 231  HOH   HOH A . 
K 6 HOH   43  343 249  HOH   HOH A . 
K 6 HOH   44  344 202  HOH   HOH A . 
K 6 HOH   45  345 150  HOH   HOH A . 
K 6 HOH   46  346 134  HOH   HOH A . 
K 6 HOH   47  347 434  HOH   HOH A . 
K 6 HOH   48  348 217  HOH   HOH A . 
K 6 HOH   49  349 443  HOH   HOH A . 
K 6 HOH   50  350 425  HOH   HOH A . 
K 6 HOH   51  351 95   HOH   HOH A . 
K 6 HOH   52  352 188  HOH   HOH A . 
K 6 HOH   53  353 337  HOH   HOH A . 
K 6 HOH   54  354 497  HOH   HOH A . 
K 6 HOH   55  355 307  HOH   HOH A . 
K 6 HOH   56  356 35   HOH   HOH A . 
K 6 HOH   57  357 72   HOH   HOH A . 
K 6 HOH   58  358 552  HOH   HOH A . 
K 6 HOH   59  359 367  HOH   HOH A . 
K 6 HOH   60  360 329  HOH   HOH A . 
K 6 HOH   61  361 11   HOH   HOH A . 
K 6 HOH   62  362 6    HOH   HOH A . 
K 6 HOH   63  363 10   HOH   HOH A . 
K 6 HOH   64  364 112  HOH   HOH A . 
K 6 HOH   65  365 152  HOH   HOH A . 
K 6 HOH   66  366 357  HOH   HOH A . 
K 6 HOH   67  367 117  HOH   HOH A . 
K 6 HOH   68  368 276  HOH   HOH A . 
K 6 HOH   69  369 525  HOH   HOH A . 
K 6 HOH   70  370 197  HOH   HOH A . 
K 6 HOH   71  371 518  HOH   HOH A . 
K 6 HOH   72  372 28   HOH   HOH A . 
K 6 HOH   73  373 426  HOH   HOH A . 
K 6 HOH   74  374 313  HOH   HOH A . 
K 6 HOH   75  375 421  HOH   HOH A . 
K 6 HOH   76  376 474  HOH   HOH A . 
K 6 HOH   77  377 29   HOH   HOH A . 
K 6 HOH   78  378 355  HOH   HOH A . 
K 6 HOH   79  379 448  HOH   HOH A . 
K 6 HOH   80  380 298  HOH   HOH A . 
K 6 HOH   81  381 201  HOH   HOH A . 
K 6 HOH   82  382 196  HOH   HOH A . 
K 6 HOH   83  383 98   HOH   HOH A . 
K 6 HOH   84  384 457  HOH   HOH A . 
K 6 HOH   85  385 278  HOH   HOH A . 
K 6 HOH   86  386 537  HOH   HOH A . 
K 6 HOH   87  387 332  HOH   HOH A . 
K 6 HOH   88  388 346  HOH   HOH A . 
K 6 HOH   89  389 454  HOH   HOH A . 
K 6 HOH   90  390 235  HOH   HOH A . 
K 6 HOH   91  391 256  HOH   HOH A . 
K 6 HOH   92  392 314  HOH   HOH A . 
K 6 HOH   93  393 39   HOH   HOH A . 
K 6 HOH   94  394 198  HOH   HOH A . 
K 6 HOH   95  395 471  HOH   HOH A . 
K 6 HOH   96  396 208  HOH   HOH A . 
K 6 HOH   97  397 462  HOH   HOH A . 
K 6 HOH   98  398 489  HOH   HOH A . 
K 6 HOH   99  399 395  HOH   HOH A . 
K 6 HOH   100 400 187  HOH   HOH A . 
K 6 HOH   101 401 385  HOH   HOH A . 
K 6 HOH   102 402 203  HOH   HOH A . 
K 6 HOH   103 403 511  HOH   HOH A . 
K 6 HOH   104 404 224  HOH   HOH A . 
K 6 HOH   105 405 356  HOH   HOH A . 
K 6 HOH   106 406 430  HOH   HOH A . 
K 6 HOH   107 407 168  HOH   HOH A . 
K 6 HOH   108 408 499  HOH   HOH A . 
K 6 HOH   109 409 58   HOH   HOH A . 
K 6 HOH   110 410 160  HOH   HOH A . 
K 6 HOH   111 411 319  HOH   HOH A . 
K 6 HOH   112 412 538  HOH   HOH A . 
K 6 HOH   113 413 30   HOH   HOH A . 
K 6 HOH   114 414 559  HOH   HOH A . 
K 6 HOH   115 415 239  HOH   HOH A . 
K 6 HOH   116 416 517  HOH   HOH A . 
K 6 HOH   117 417 370  HOH   HOH A . 
K 6 HOH   118 418 139  HOH   HOH A . 
K 6 HOH   119 419 399  HOH   HOH A . 
K 6 HOH   120 420 393  HOH   HOH A . 
K 6 HOH   121 421 530  HOH   HOH A . 
K 6 HOH   122 422 555  HOH   HOH A . 
K 6 HOH   123 423 558  HOH   HOH A . 
K 6 HOH   124 424 296  HOH   HOH A . 
K 6 HOH   125 425 415  HOH   HOH A . 
K 6 HOH   126 426 428  HOH   HOH A . 
K 6 HOH   127 427 478  HOH   HOH A . 
K 6 HOH   128 428 258  HOH   HOH A . 
K 6 HOH   129 429 259  HOH   HOH A . 
K 6 HOH   130 430 375  HOH   HOH A . 
K 6 HOH   131 431 368  HOH   HOH A . 
K 6 HOH   132 432 446  HOH   HOH A . 
K 6 HOH   133 433 437  HOH   HOH A . 
K 6 HOH   134 434 342  HOH   HOH A . 
K 6 HOH   135 435 177  HOH   HOH A . 
K 6 HOH   136 436 251  HOH   HOH A . 
K 6 HOH   137 437 534  HOH   HOH A . 
K 6 HOH   138 438 380  HOH   HOH A . 
K 6 HOH   139 439 263  HOH   HOH A . 
K 6 HOH   140 440 557  HOH   HOH A . 
K 6 HOH   141 441 31   HOH   HOH A . 
K 6 HOH   142 442 330  HOH   HOH A . 
K 6 HOH   143 443 289  HOH   HOH A . 
K 6 HOH   144 444 138  HOH   HOH A . 
K 6 HOH   145 445 502  HOH   HOH A . 
K 6 HOH   146 446 402  HOH   HOH A . 
K 6 HOH   147 447 514  HOH   HOH A . 
K 6 HOH   148 448 532  HOH   HOH A . 
K 6 HOH   149 449 216  HOH   HOH A . 
K 6 HOH   150 450 205  HOH   HOH A . 
K 6 HOH   151 451 483  HOH   HOH A . 
K 6 HOH   152 452 411  HOH   HOH A . 
K 6 HOH   153 453 262  HOH   HOH A . 
L 6 HOH   1   301 491  HOH   HOH B . 
L 6 HOH   2   302 76   HOH   HOH B . 
L 6 HOH   3   303 165  HOH   HOH B . 
L 6 HOH   4   304 422  HOH   HOH B . 
L 6 HOH   5   305 46   HOH   HOH B . 
L 6 HOH   6   306 254  HOH   HOH B . 
L 6 HOH   7   307 516  HOH   HOH B . 
L 6 HOH   8   308 253  HOH   HOH B . 
L 6 HOH   9   309 174  HOH   HOH B . 
L 6 HOH   10  310 376  HOH   HOH B . 
L 6 HOH   11  311 495  HOH   HOH B . 
L 6 HOH   12  312 563  HOH   HOH B . 
L 6 HOH   13  313 128  HOH   HOH B . 
L 6 HOH   14  314 67   HOH   HOH B . 
L 6 HOH   15  315 209  HOH   HOH B . 
L 6 HOH   16  316 199  HOH   HOH B . 
L 6 HOH   17  317 130  HOH   HOH B . 
L 6 HOH   18  318 65   HOH   HOH B . 
L 6 HOH   19  319 22   HOH   HOH B . 
L 6 HOH   20  320 234  HOH   HOH B . 
L 6 HOH   21  321 218  HOH   HOH B . 
L 6 HOH   22  322 121  HOH   HOH B . 
L 6 HOH   23  323 533  HOH   HOH B . 
L 6 HOH   24  324 255  HOH   HOH B . 
L 6 HOH   25  325 75   HOH   HOH B . 
L 6 HOH   26  326 339  HOH   HOH B . 
L 6 HOH   27  327 163  HOH   HOH B . 
L 6 HOH   28  328 348  HOH   HOH B . 
L 6 HOH   29  329 287  HOH   HOH B . 
L 6 HOH   30  330 547  HOH   HOH B . 
L 6 HOH   31  331 354  HOH   HOH B . 
L 6 HOH   32  332 562  HOH   HOH B . 
L 6 HOH   33  333 45   HOH   HOH B . 
L 6 HOH   34  334 269  HOH   HOH B . 
L 6 HOH   35  335 327  HOH   HOH B . 
L 6 HOH   36  336 347  HOH   HOH B . 
L 6 HOH   37  337 184  HOH   HOH B . 
L 6 HOH   38  338 107  HOH   HOH B . 
L 6 HOH   39  339 244  HOH   HOH B . 
L 6 HOH   40  340 520  HOH   HOH B . 
L 6 HOH   41  341 331  HOH   HOH B . 
L 6 HOH   42  342 77   HOH   HOH B . 
L 6 HOH   43  343 494  HOH   HOH B . 
L 6 HOH   44  344 91   HOH   HOH B . 
L 6 HOH   45  345 219  HOH   HOH B . 
L 6 HOH   46  346 19   HOH   HOH B . 
L 6 HOH   47  347 88   HOH   HOH B . 
L 6 HOH   48  348 210  HOH   HOH B . 
L 6 HOH   49  349 73   HOH   HOH B . 
L 6 HOH   50  350 294  HOH   HOH B . 
L 6 HOH   51  351 94   HOH   HOH B . 
L 6 HOH   52  352 175  HOH   HOH B . 
L 6 HOH   53  353 41   HOH   HOH B . 
L 6 HOH   54  354 469  HOH   HOH B . 
L 6 HOH   55  355 396  HOH   HOH B . 
L 6 HOH   56  356 372  HOH   HOH B . 
L 6 HOH   57  357 416  HOH   HOH B . 
L 6 HOH   58  358 522  HOH   HOH B . 
L 6 HOH   59  359 250  HOH   HOH B . 
L 6 HOH   60  360 212  HOH   HOH B . 
L 6 HOH   61  361 80   HOH   HOH B . 
L 6 HOH   62  362 116  HOH   HOH B . 
L 6 HOH   63  363 232  HOH   HOH B . 
L 6 HOH   64  364 500  HOH   HOH B . 
L 6 HOH   65  365 280  HOH   HOH B . 
L 6 HOH   66  366 301  HOH   HOH B . 
L 6 HOH   67  367 420  HOH   HOH B . 
L 6 HOH   68  368 323  HOH   HOH B . 
L 6 HOH   69  369 106  HOH   HOH B . 
L 6 HOH   70  370 167  HOH   HOH B . 
L 6 HOH   71  371 159  HOH   HOH B . 
L 6 HOH   72  372 433  HOH   HOH B . 
L 6 HOH   73  373 338  HOH   HOH B . 
L 6 HOH   74  374 575  HOH   HOH B . 
L 6 HOH   75  375 377  HOH   HOH B . 
L 6 HOH   76  376 452  HOH   HOH B . 
L 6 HOH   77  377 477  HOH   HOH B . 
L 6 HOH   78  378 466  HOH   HOH B . 
L 6 HOH   79  379 561  HOH   HOH B . 
L 6 HOH   80  380 124  HOH   HOH B . 
L 6 HOH   81  381 267  HOH   HOH B . 
L 6 HOH   82  382 207  HOH   HOH B . 
L 6 HOH   83  383 74   HOH   HOH B . 
L 6 HOH   84  384 266  HOH   HOH B . 
L 6 HOH   85  385 407  HOH   HOH B . 
L 6 HOH   86  386 493  HOH   HOH B . 
L 6 HOH   87  387 455  HOH   HOH B . 
L 6 HOH   88  388 268  HOH   HOH B . 
M 6 HOH   1   301 182  HOH   HOH C . 
M 6 HOH   2   302 78   HOH   HOH C . 
M 6 HOH   3   303 326  HOH   HOH C . 
M 6 HOH   4   304 245  HOH   HOH C . 
M 6 HOH   5   305 358  HOH   HOH C . 
M 6 HOH   6   306 310  HOH   HOH C . 
M 6 HOH   7   307 57   HOH   HOH C . 
M 6 HOH   8   308 131  HOH   HOH C . 
M 6 HOH   9   309 458  HOH   HOH C . 
M 6 HOH   10  310 401  HOH   HOH C . 
M 6 HOH   11  311 26   HOH   HOH C . 
M 6 HOH   12  312 54   HOH   HOH C . 
M 6 HOH   13  313 136  HOH   HOH C . 
M 6 HOH   14  314 379  HOH   HOH C . 
M 6 HOH   15  315 284  HOH   HOH C . 
M 6 HOH   16  316 468  HOH   HOH C . 
M 6 HOH   17  317 227  HOH   HOH C . 
M 6 HOH   18  318 155  HOH   HOH C . 
M 6 HOH   19  319 195  HOH   HOH C . 
M 6 HOH   20  320 170  HOH   HOH C . 
M 6 HOH   21  321 363  HOH   HOH C . 
M 6 HOH   22  322 66   HOH   HOH C . 
M 6 HOH   23  323 306  HOH   HOH C . 
M 6 HOH   24  324 68   HOH   HOH C . 
M 6 HOH   25  325 61   HOH   HOH C . 
M 6 HOH   26  326 60   HOH   HOH C . 
M 6 HOH   27  327 302  HOH   HOH C . 
M 6 HOH   28  328 17   HOH   HOH C . 
M 6 HOH   29  329 48   HOH   HOH C . 
M 6 HOH   30  330 304  HOH   HOH C . 
M 6 HOH   31  331 413  HOH   HOH C . 
M 6 HOH   32  332 229  HOH   HOH C . 
M 6 HOH   33  333 32   HOH   HOH C . 
M 6 HOH   34  334 151  HOH   HOH C . 
M 6 HOH   35  335 492  HOH   HOH C . 
M 6 HOH   36  336 436  HOH   HOH C . 
M 6 HOH   37  337 362  HOH   HOH C . 
M 6 HOH   38  338 50   HOH   HOH C . 
M 6 HOH   39  339 193  HOH   HOH C . 
M 6 HOH   40  340 16   HOH   HOH C . 
M 6 HOH   41  341 279  HOH   HOH C . 
M 6 HOH   42  342 215  HOH   HOH C . 
M 6 HOH   43  343 97   HOH   HOH C . 
M 6 HOH   44  344 12   HOH   HOH C . 
M 6 HOH   45  345 119  HOH   HOH C . 
M 6 HOH   46  346 4    HOH   HOH C . 
M 6 HOH   47  347 524  HOH   HOH C . 
M 6 HOH   48  348 503  HOH   HOH C . 
M 6 HOH   49  349 70   HOH   HOH C . 
M 6 HOH   50  350 43   HOH   HOH C . 
M 6 HOH   51  351 479  HOH   HOH C . 
M 6 HOH   52  352 127  HOH   HOH C . 
M 6 HOH   53  353 109  HOH   HOH C . 
M 6 HOH   54  354 308  HOH   HOH C . 
M 6 HOH   55  355 578  HOH   HOH C . 
M 6 HOH   56  356 387  HOH   HOH C . 
M 6 HOH   57  357 114  HOH   HOH C . 
M 6 HOH   58  358 38   HOH   HOH C . 
M 6 HOH   59  359 439  HOH   HOH C . 
M 6 HOH   60  360 270  HOH   HOH C . 
M 6 HOH   61  361 200  HOH   HOH C . 
M 6 HOH   62  362 527  HOH   HOH C . 
M 6 HOH   63  363 571  HOH   HOH C . 
M 6 HOH   64  364 274  HOH   HOH C . 
M 6 HOH   65  365 221  HOH   HOH C . 
M 6 HOH   66  366 213  HOH   HOH C . 
M 6 HOH   67  367 62   HOH   HOH C . 
M 6 HOH   68  368 336  HOH   HOH C . 
M 6 HOH   69  369 9    HOH   HOH C . 
M 6 HOH   70  370 275  HOH   HOH C . 
M 6 HOH   71  371 71   HOH   HOH C . 
M 6 HOH   72  372 523  HOH   HOH C . 
M 6 HOH   73  373 506  HOH   HOH C . 
M 6 HOH   74  374 161  HOH   HOH C . 
M 6 HOH   75  375 526  HOH   HOH C . 
M 6 HOH   76  376 484  HOH   HOH C . 
M 6 HOH   77  377 272  HOH   HOH C . 
M 6 HOH   78  378 386  HOH   HOH C . 
M 6 HOH   79  379 403  HOH   HOH C . 
M 6 HOH   80  380 513  HOH   HOH C . 
M 6 HOH   81  381 463  HOH   HOH C . 
M 6 HOH   82  382 429  HOH   HOH C . 
M 6 HOH   83  383 55   HOH   HOH C . 
M 6 HOH   84  384 118  HOH   HOH C . 
M 6 HOH   85  385 573  HOH   HOH C . 
M 6 HOH   86  386 277  HOH   HOH C . 
M 6 HOH   87  387 408  HOH   HOH C . 
M 6 HOH   88  388 566  HOH   HOH C . 
M 6 HOH   89  389 486  HOH   HOH C . 
M 6 HOH   90  390 297  HOH   HOH C . 
M 6 HOH   91  391 334  HOH   HOH C . 
M 6 HOH   92  392 409  HOH   HOH C . 
M 6 HOH   93  393 509  HOH   HOH C . 
M 6 HOH   94  394 570  HOH   HOH C . 
M 6 HOH   95  395 350  HOH   HOH C . 
M 6 HOH   96  396 461  HOH   HOH C . 
M 6 HOH   97  397 414  HOH   HOH C . 
M 6 HOH   98  398 560  HOH   HOH C . 
M 6 HOH   99  399 222  HOH   HOH C . 
M 6 HOH   100 400 490  HOH   HOH C . 
M 6 HOH   101 401 459  HOH   HOH C . 
M 6 HOH   102 402 293  HOH   HOH C . 
M 6 HOH   103 403 564  HOH   HOH C . 
M 6 HOH   104 404 322  HOH   HOH C . 
M 6 HOH   105 405 360  HOH   HOH C . 
M 6 HOH   106 406 464  HOH   HOH C . 
M 6 HOH   107 407 572  HOH   HOH C . 
M 6 HOH   108 408 238  HOH   HOH C . 
M 6 HOH   109 409 384  HOH   HOH C . 
M 6 HOH   110 410 473  HOH   HOH C . 
M 6 HOH   111 411 432  HOH   HOH C . 
M 6 HOH   112 412 233  HOH   HOH C . 
M 6 HOH   113 413 125  HOH   HOH C . 
M 6 HOH   114 414 485  HOH   HOH C . 
M 6 HOH   115 415 265  HOH   HOH C . 
M 6 HOH   116 416 286  HOH   HOH C . 
M 6 HOH   117 417 550  HOH   HOH C . 
M 6 HOH   118 418 482  HOH   HOH C . 
M 6 HOH   119 419 419  HOH   HOH C . 
M 6 HOH   120 420 536  HOH   HOH C . 
M 6 HOH   121 421 576  HOH   HOH C . 
M 6 HOH   122 422 391  HOH   HOH C . 
M 6 HOH   123 423 531  HOH   HOH C . 
N 6 HOH   1   301 115  HOH   HOH D . 
N 6 HOH   2   302 382  HOH   HOH D . 
N 6 HOH   3   303 467  HOH   HOH D . 
N 6 HOH   4   304 87   HOH   HOH D . 
N 6 HOH   5   305 15   HOH   HOH D . 
N 6 HOH   6   306 498  HOH   HOH D . 
N 6 HOH   7   307 181  HOH   HOH D . 
N 6 HOH   8   308 540  HOH   HOH D . 
N 6 HOH   9   309 281  HOH   HOH D . 
N 6 HOH   10  310 145  HOH   HOH D . 
N 6 HOH   11  311 225  HOH   HOH D . 
N 6 HOH   12  312 149  HOH   HOH D . 
N 6 HOH   13  313 252  HOH   HOH D . 
N 6 HOH   14  314 92   HOH   HOH D . 
N 6 HOH   15  315 178  HOH   HOH D . 
N 6 HOH   16  316 56   HOH   HOH D . 
N 6 HOH   17  317 318  HOH   HOH D . 
N 6 HOH   18  318 444  HOH   HOH D . 
N 6 HOH   19  319 2    HOH   HOH D . 
N 6 HOH   20  320 69   HOH   HOH D . 
N 6 HOH   21  321 237  HOH   HOH D . 
N 6 HOH   22  322 84   HOH   HOH D . 
N 6 HOH   23  323 185  HOH   HOH D . 
N 6 HOH   24  324 104  HOH   HOH D . 
N 6 HOH   25  325 487  HOH   HOH D . 
N 6 HOH   26  326 49   HOH   HOH D . 
N 6 HOH   27  327 325  HOH   HOH D . 
N 6 HOH   28  328 20   HOH   HOH D . 
N 6 HOH   29  329 53   HOH   HOH D . 
N 6 HOH   30  330 8    HOH   HOH D . 
N 6 HOH   31  331 345  HOH   HOH D . 
N 6 HOH   32  332 153  HOH   HOH D . 
N 6 HOH   33  333 194  HOH   HOH D . 
N 6 HOH   34  334 392  HOH   HOH D . 
N 6 HOH   35  335 7    HOH   HOH D . 
N 6 HOH   36  336 341  HOH   HOH D . 
N 6 HOH   37  337 85   HOH   HOH D . 
N 6 HOH   38  338 110  HOH   HOH D . 
N 6 HOH   39  339 51   HOH   HOH D . 
N 6 HOH   40  340 435  HOH   HOH D . 
N 6 HOH   41  341 549  HOH   HOH D . 
N 6 HOH   42  342 82   HOH   HOH D . 
N 6 HOH   43  343 172  HOH   HOH D . 
N 6 HOH   44  344 162  HOH   HOH D . 
N 6 HOH   45  345 59   HOH   HOH D . 
N 6 HOH   46  346 96   HOH   HOH D . 
N 6 HOH   47  347 79   HOH   HOH D . 
N 6 HOH   48  348 246  HOH   HOH D . 
N 6 HOH   49  349 81   HOH   HOH D . 
N 6 HOH   50  350 288  HOH   HOH D . 
N 6 HOH   51  351 23   HOH   HOH D . 
N 6 HOH   52  352 440  HOH   HOH D . 
N 6 HOH   53  353 18   HOH   HOH D . 
N 6 HOH   54  354 510  HOH   HOH D . 
N 6 HOH   55  355 33   HOH   HOH D . 
N 6 HOH   56  356 89   HOH   HOH D . 
N 6 HOH   57  357 126  HOH   HOH D . 
N 6 HOH   58  358 309  HOH   HOH D . 
N 6 HOH   59  359 343  HOH   HOH D . 
N 6 HOH   60  360 176  HOH   HOH D . 
N 6 HOH   61  361 102  HOH   HOH D . 
N 6 HOH   62  362 369  HOH   HOH D . 
N 6 HOH   63  363 64   HOH   HOH D . 
N 6 HOH   64  364 157  HOH   HOH D . 
N 6 HOH   65  365 108  HOH   HOH D . 
N 6 HOH   66  366 42   HOH   HOH D . 
N 6 HOH   67  367 24   HOH   HOH D . 
N 6 HOH   68  368 132  HOH   HOH D . 
N 6 HOH   69  369 47   HOH   HOH D . 
N 6 HOH   70  370 5    HOH   HOH D . 
N 6 HOH   71  371 236  HOH   HOH D . 
N 6 HOH   72  372 351  HOH   HOH D . 
N 6 HOH   73  373 305  HOH   HOH D . 
N 6 HOH   74  374 34   HOH   HOH D . 
N 6 HOH   75  375 226  HOH   HOH D . 
N 6 HOH   76  376 191  HOH   HOH D . 
N 6 HOH   77  377 243  HOH   HOH D . 
N 6 HOH   78  378 13   HOH   HOH D . 
N 6 HOH   79  379 141  HOH   HOH D . 
N 6 HOH   80  380 228  HOH   HOH D . 
N 6 HOH   81  381 292  HOH   HOH D . 
N 6 HOH   82  382 545  HOH   HOH D . 
N 6 HOH   83  383 579  HOH   HOH D . 
N 6 HOH   84  384 366  HOH   HOH D . 
N 6 HOH   85  385 164  HOH   HOH D . 
N 6 HOH   86  386 99   HOH   HOH D . 
N 6 HOH   87  387 460  HOH   HOH D . 
N 6 HOH   88  388 291  HOH   HOH D . 
N 6 HOH   89  389 101  HOH   HOH D . 
N 6 HOH   90  390 120  HOH   HOH D . 
N 6 HOH   91  391 312  HOH   HOH D . 
N 6 HOH   92  392 283  HOH   HOH D . 
N 6 HOH   93  393 501  HOH   HOH D . 
N 6 HOH   94  394 261  HOH   HOH D . 
N 6 HOH   95  395 27   HOH   HOH D . 
N 6 HOH   96  396 214  HOH   HOH D . 
N 6 HOH   97  397 186  HOH   HOH D . 
N 6 HOH   98  398 25   HOH   HOH D . 
N 6 HOH   99  399 273  HOH   HOH D . 
N 6 HOH   100 400 148  HOH   HOH D . 
N 6 HOH   101 401 190  HOH   HOH D . 
N 6 HOH   102 402 100  HOH   HOH D . 
N 6 HOH   103 403 113  HOH   HOH D . 
N 6 HOH   104 404 206  HOH   HOH D . 
N 6 HOH   105 405 90   HOH   HOH D . 
N 6 HOH   106 406 133  HOH   HOH D . 
N 6 HOH   107 407 40   HOH   HOH D . 
N 6 HOH   108 408 147  HOH   HOH D . 
N 6 HOH   109 409 144  HOH   HOH D . 
N 6 HOH   110 410 441  HOH   HOH D . 
N 6 HOH   111 411 427  HOH   HOH D . 
N 6 HOH   112 412 529  HOH   HOH D . 
N 6 HOH   113 413 442  HOH   HOH D . 
N 6 HOH   114 414 158  HOH   HOH D . 
N 6 HOH   115 415 365  HOH   HOH D . 
N 6 HOH   116 416 324  HOH   HOH D . 
N 6 HOH   117 417 44   HOH   HOH D . 
N 6 HOH   118 418 123  HOH   HOH D . 
N 6 HOH   119 419 173  HOH   HOH D . 
N 6 HOH   120 420 521  HOH   HOH D . 
N 6 HOH   121 421 349  HOH   HOH D . 
N 6 HOH   122 422 248  HOH   HOH D . 
N 6 HOH   123 423 476  HOH   HOH D . 
N 6 HOH   124 424 333  HOH   HOH D . 
N 6 HOH   125 425 223  HOH   HOH D . 
N 6 HOH   126 426 542  HOH   HOH D . 
N 6 HOH   127 427 317  HOH   HOH D . 
N 6 HOH   128 428 204  HOH   HOH D . 
N 6 HOH   129 429 344  HOH   HOH D . 
N 6 HOH   130 430 359  HOH   HOH D . 
N 6 HOH   131 431 315  HOH   HOH D . 
N 6 HOH   132 432 321  HOH   HOH D . 
N 6 HOH   133 433 247  HOH   HOH D . 
N 6 HOH   134 434 381  HOH   HOH D . 
N 6 HOH   135 435 290  HOH   HOH D . 
N 6 HOH   136 436 353  HOH   HOH D . 
N 6 HOH   137 437 390  HOH   HOH D . 
N 6 HOH   138 438 241  HOH   HOH D . 
N 6 HOH   139 439 242  HOH   HOH D . 
N 6 HOH   140 440 340  HOH   HOH D . 
N 6 HOH   141 441 504  HOH   HOH D . 
N 6 HOH   142 442 515  HOH   HOH D . 
N 6 HOH   143 443 169  HOH   HOH D . 
N 6 HOH   144 444 496  HOH   HOH D . 
N 6 HOH   145 445 389  HOH   HOH D . 
N 6 HOH   146 446 410  HOH   HOH D . 
N 6 HOH   147 447 412  HOH   HOH D . 
N 6 HOH   148 448 166  HOH   HOH D . 
N 6 HOH   149 449 220  HOH   HOH D . 
N 6 HOH   150 450 352  HOH   HOH D . 
N 6 HOH   151 451 424  HOH   HOH D . 
N 6 HOH   152 452 142  HOH   HOH D . 
N 6 HOH   153 453 264  HOH   HOH D . 
N 6 HOH   154 454 388  HOH   HOH D . 
N 6 HOH   155 455 137  HOH   HOH D . 
N 6 HOH   156 456 405  HOH   HOH D . 
N 6 HOH   157 457 480  HOH   HOH D . 
N 6 HOH   158 458 373  HOH   HOH D . 
N 6 HOH   159 459 303  HOH   HOH D . 
N 6 HOH   160 460 580  HOH   HOH D . 
N 6 HOH   161 461 544  HOH   HOH D . 
N 6 HOH   162 462 285  HOH   HOH D . 
N 6 HOH   163 463 565  HOH   HOH D . 
N 6 HOH   164 464 397  HOH   HOH D . 
N 6 HOH   165 465 417  HOH   HOH D . 
N 6 HOH   166 466 361  HOH   HOH D . 
N 6 HOH   167 467 431  HOH   HOH D . 
N 6 HOH   168 468 230  HOH   HOH D . 
N 6 HOH   169 469 404  HOH   HOH D . 
N 6 HOH   170 470 528  HOH   HOH D . 
N 6 HOH   171 471 171  HOH   HOH D . 
N 6 HOH   172 472 111  HOH   HOH D . 
N 6 HOH   173 473 577  HOH   HOH D . 
N 6 HOH   174 474 481  HOH   HOH D . 
N 6 HOH   175 475 567  HOH   HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BG5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.280 
_cell.length_a_esd                 ? 
_cell.length_b                     84.530 
_cell.length_b_esd                 ? 
_cell.length_c                     128.280 
_cell.length_c_esd                 ? 
_cell.volume                       718707.737 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9BG5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 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                   9BG5 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.42 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.08 
_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              7 
_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    '24% PEG4000, 0.1 M imidazole, pH 7' 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-22 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97946 
_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                        'CLSI BEAMLINE 08ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08ID-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          28.88 
_reflns.entry_id                                       9BG5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.67 
_reflns.d_resolution_low                               40.47 
_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                                     84194 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.88 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.53 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.1033 
_reflns.pdbx_Rpim_I_all                                0.0378 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.09597 
_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                                    1.67 
_reflns_shell.d_res_low                                     1.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.86 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8308 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               7.1 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               2.668 
_reflns_shell.pdbx_Rpim_I_all                               0.9926 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.342 
_reflns_shell.pdbx_CC_star                                  0.714 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.64 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.471 
_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                               39.30 
_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                                 9BG5 
_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                            1.67 
_refine.ls_d_res_low                             40.47 
_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                     84174 
_refine.ls_number_reflns_R_free                  4211 
_refine.ls_number_reflns_R_work                  79963 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2253 
_refine.ls_R_factor_R_free                       0.2664 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2232 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 30.3450 
_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                            0.3112 
_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                       1.67 
_refine_hist.d_res_low                        40.47 
_refine_hist.number_atoms_solvent             539 
_refine_hist.number_atoms_total               5937 
_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        5216 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         182 
_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' ? 0.0063  ? 5551 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8268  ? 7508 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0543  ? 800  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0063  ? 968  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.5515 ? 2114 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.67 1.69  . . 145 2633 99.53  . . . . 0.4339 . . . . . . . . . . . 0.4560 
'X-RAY DIFFRACTION' 1.69 1.71  . . 139 2620 99.42  . . . . 0.4017 . . . . . . . . . . . 0.4698 
'X-RAY DIFFRACTION' 1.71 1.73  . . 135 2623 99.96  . . . . 0.3884 . . . . . . . . . . . 0.3876 
'X-RAY DIFFRACTION' 1.73 1.75  . . 119 2641 99.64  . . . . 0.3582 . . . . . . . . . . . 0.4302 
'X-RAY DIFFRACTION' 1.75 1.77  . . 134 2619 99.93  . . . . 0.3427 . . . . . . . . . . . 0.3479 
'X-RAY DIFFRACTION' 1.77 1.80  . . 149 2659 99.86  . . . . 0.3175 . . . . . . . . . . . 0.3460 
'X-RAY DIFFRACTION' 1.80 1.82  . . 131 2625 99.93  . . . . 0.3177 . . . . . . . . . . . 0.3766 
'X-RAY DIFFRACTION' 1.82 1.85  . . 149 2644 99.86  . . . . 0.3055 . . . . . . . . . . . 0.3352 
'X-RAY DIFFRACTION' 1.85 1.88  . . 146 2631 99.96  . . . . 0.2935 . . . . . . . . . . . 0.3725 
'X-RAY DIFFRACTION' 1.88 1.91  . . 130 2622 99.96  . . . . 0.2793 . . . . . . . . . . . 0.3311 
'X-RAY DIFFRACTION' 1.91 1.94  . . 121 2692 99.93  . . . . 0.2689 . . . . . . . . . . . 0.3061 
'X-RAY DIFFRACTION' 1.94 1.98  . . 131 2617 99.96  . . . . 0.2665 . . . . . . . . . . . 0.3028 
'X-RAY DIFFRACTION' 1.98 2.02  . . 149 2675 100.00 . . . . 0.2733 . . . . . . . . . . . 0.3010 
'X-RAY DIFFRACTION' 2.02 2.06  . . 151 2630 100.00 . . . . 0.2623 . . . . . . . . . . . 0.3069 
'X-RAY DIFFRACTION' 2.06 2.10  . . 139 2634 99.93  . . . . 0.2587 . . . . . . . . . . . 0.3117 
'X-RAY DIFFRACTION' 2.10 2.15  . . 149 2653 99.96  . . . . 0.2640 . . . . . . . . . . . 0.3067 
'X-RAY DIFFRACTION' 2.15 2.21  . . 128 2668 99.96  . . . . 0.2440 . . . . . . . . . . . 0.2910 
'X-RAY DIFFRACTION' 2.21 2.27  . . 167 2604 100.00 . . . . 0.2492 . . . . . . . . . . . 0.3066 
'X-RAY DIFFRACTION' 2.27 2.33  . . 151 2667 100.00 . . . . 0.2498 . . . . . . . . . . . 0.2957 
'X-RAY DIFFRACTION' 2.33 2.41  . . 140 2657 100.00 . . . . 0.2522 . . . . . . . . . . . 0.2794 
'X-RAY DIFFRACTION' 2.41 2.49  . . 156 2662 100.00 . . . . 0.2469 . . . . . . . . . . . 0.2899 
'X-RAY DIFFRACTION' 2.49 2.59  . . 133 2654 100.00 . . . . 0.2474 . . . . . . . . . . . 0.2849 
'X-RAY DIFFRACTION' 2.59 2.71  . . 153 2677 100.00 . . . . 0.2441 . . . . . . . . . . . 0.3056 
'X-RAY DIFFRACTION' 2.71 2.86  . . 144 2673 100.00 . . . . 0.2351 . . . . . . . . . . . 0.2946 
'X-RAY DIFFRACTION' 2.86 3.03  . . 126 2708 99.89  . . . . 0.2278 . . . . . . . . . . . 0.2946 
'X-RAY DIFFRACTION' 3.03 3.27  . . 130 2716 99.96  . . . . 0.2215 . . . . . . . . . . . 0.2853 
'X-RAY DIFFRACTION' 3.27 3.60  . . 137 2691 99.93  . . . . 0.2074 . . . . . . . . . . . 0.2482 
'X-RAY DIFFRACTION' 3.60 4.12  . . 132 2741 99.79  . . . . 0.1871 . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 4.12 5.19  . . 141 2757 99.97  . . . . 0.1590 . . . . . . . . . . . 0.1918 
'X-RAY DIFFRACTION' 5.19 40.47 . . 156 2870 99.44  . . . . 0.1722 . . . . . . . . . . . 0.1944 
# 
_struct.entry_id                     9BG5 
_struct.title                        'Tri-complex of Daraxonrasib (RMC-6236), KRAS G13D, and CypA' 
_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        9BG5 
_struct_keywords.text            'inhibitor, complex, small GTPase, cancer, tri-complex, SIGNALING PROTEIN-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN/INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
K N N 6 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP RASK_HUMAN P01116 ? 1 
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLV
REIR
;
1 
2 UNP PPIA_HUMAN P62937 ? 2 
;MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG
EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD
CGQLE
;
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 9BG5 A 2 ? 165 ? P01116 1 ? 164 ? 1 164 
2 1 9BG5 B 2 ? 165 ? P01116 1 ? 164 ? 1 164 
3 2 9BG5 C 2 ? 166 ? P62937 1 ? 165 ? 1 165 
4 2 9BG5 D 2 ? 166 ? P62937 1 ? 165 ? 1 165 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9BG5 SER A 1   ? UNP P01116 ?   ?   'expression tag'      0   1  
1 9BG5 ASP A 14  ? UNP P01116 GLY 13  'engineered mutation' 13  2  
1 9BG5 GLY A 152 ? UNP P01116 ARG 151 conflict              151 3  
1 9BG5 ASP A 154 ? UNP P01116 GLU 153 conflict              153 4  
1 9BG5 LYS A 166 ? UNP P01116 ?   ?   'expression tag'      165 5  
1 9BG5 HIS A 167 ? UNP P01116 ?   ?   'expression tag'      166 6  
1 9BG5 LYS A 168 ? UNP P01116 ?   ?   'expression tag'      167 7  
1 9BG5 GLU A 169 ? UNP P01116 ?   ?   'expression tag'      168 8  
1 9BG5 LYS A 170 ? UNP P01116 ?   ?   'expression tag'      169 9  
2 9BG5 SER B 1   ? UNP P01116 ?   ?   'expression tag'      0   10 
2 9BG5 ASP B 14  ? UNP P01116 GLY 13  'engineered mutation' 13  11 
2 9BG5 GLY B 152 ? UNP P01116 ARG 151 conflict              151 12 
2 9BG5 ASP B 154 ? UNP P01116 GLU 153 conflict              153 13 
2 9BG5 LYS B 166 ? UNP P01116 ?   ?   'expression tag'      165 14 
2 9BG5 HIS B 167 ? UNP P01116 ?   ?   'expression tag'      166 15 
2 9BG5 LYS B 168 ? UNP P01116 ?   ?   'expression tag'      167 16 
2 9BG5 GLU B 169 ? UNP P01116 ?   ?   'expression tag'      168 17 
2 9BG5 LYS B 170 ? UNP P01116 ?   ?   'expression tag'      169 18 
3 9BG5 SER C 1   ? UNP P62937 ?   ?   'expression tag'      0   19 
4 9BG5 SER D 1   ? UNP P62937 ?   ?   'expression tag'      0   20 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,J,K,N 
2 1 B,C,G,H,I,L,M 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 16  ? ASN A 27  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2  AA2 GLN A 62  ? MET A 68  ? GLN A 61  MET A 67  5 ? 7  
HELX_P HELX_P3  AA3 ARG A 69  ? GLY A 76  ? ARG A 68  GLY A 75  1 ? 8  
HELX_P HELX_P4  AA4 ASN A 87  ? ASP A 106 ? ASN A 86  ASP A 105 1 ? 20 
HELX_P HELX_P5  AA5 ASP A 127 ? GLY A 139 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P6  AA6 GLY A 152 ? GLU A 169 ? GLY A 151 GLU A 168 1 ? 18 
HELX_P HELX_P7  AA7 GLY B 16  ? ASN B 27  ? GLY B 15  ASN B 26  1 ? 12 
HELX_P HELX_P8  AA8 TYR B 65  ? MET B 68  ? TYR B 64  MET B 67  5 ? 4  
HELX_P HELX_P9  AA9 ARG B 69  ? GLY B 76  ? ARG B 68  GLY B 75  1 ? 8  
HELX_P HELX_P10 AB1 ASN B 87  ? ASP B 106 ? ASN B 86  ASP B 105 1 ? 20 
HELX_P HELX_P11 AB2 ASP B 127 ? GLY B 139 ? ASP B 126 GLY B 138 1 ? 13 
HELX_P HELX_P12 AB3 GLY B 152 ? LYS B 170 ? GLY B 151 LYS B 169 1 ? 19 
HELX_P HELX_P13 AB4 VAL C 30  ? GLY C 43  ? VAL C 29  GLY C 42  1 ? 14 
HELX_P HELX_P14 AB5 THR C 120 ? ASP C 124 ? THR C 119 ASP C 123 5 ? 5  
HELX_P HELX_P15 AB6 GLY C 136 ? GLU C 144 ? GLY C 135 GLU C 143 1 ? 9  
HELX_P HELX_P16 AB7 ARG C 145 ? GLY C 147 ? ARG C 144 GLY C 146 5 ? 3  
HELX_P HELX_P17 AB8 VAL D 30  ? GLY D 43  ? VAL D 29  GLY D 42  1 ? 14 
HELX_P HELX_P18 AB9 THR D 120 ? ASP D 124 ? THR D 119 ASP D 123 5 ? 5  
HELX_P HELX_P19 AC1 GLY D 136 ? GLU D 144 ? GLY D 135 GLU D 143 1 ? 9  
HELX_P HELX_P20 AC2 ARG D 145 ? GLY D 147 ? ARG D 144 GLY D 146 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A SER 18 OG  ? ? ? 1_555 F MG  . MG ? ? A SER 17  A MG  202 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc2  metalc ? ? A THR 36 OG1 ? ? ? 1_555 F MG  . MG ? ? A THR 35  A MG  202 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc3  metalc ? ? E GNP .  O1G ? ? ? 1_555 F MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 1.932 ? ? 
metalc4  metalc ? ? E GNP .  O1B ? ? ? 1_555 F MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc5  metalc ? ? F MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 312 1_555 ? ? ? ? ? ? ? 2.214 ? ? 
metalc6  metalc ? ? F MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 324 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
metalc7  metalc ? ? B SER 18 OG  ? ? ? 1_555 H MG  . MG ? ? B SER 17  B MG  202 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc8  metalc ? ? B THR 36 OG1 ? ? ? 1_555 H MG  . MG ? ? B THR 35  B MG  202 1_555 ? ? ? ? ? ? ? 2.226 ? ? 
metalc9  metalc ? ? G GNP .  O2G ? ? ? 1_555 H MG  . MG ? ? B GNP 201 B MG  202 1_555 ? ? ? ? ? ? ? 1.884 ? ? 
metalc10 metalc ? ? G GNP .  O1B ? ? ? 1_555 H MG  . MG ? ? B GNP 201 B MG  202 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
metalc11 metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  202 B HOH 312 1_555 ? ? ? ? ? ? ? 1.937 ? ? 
metalc12 metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  202 B HOH 343 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
# 
_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  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 OG1 ? A THR 36 ? A THR 35  ? 1_555 80.5  ? 
2  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1G ? E GNP .  ? A GNP 201 ? 1_555 172.2 ? 
3  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1G ? E GNP .  ? A GNP 201 ? 1_555 91.8  ? 
4  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1B ? E GNP .  ? A GNP 201 ? 1_555 93.3  ? 
5  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1B ? E GNP .  ? A GNP 201 ? 1_555 173.8 ? 
6  O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1B ? E GNP .  ? A GNP 201 ? 1_555 94.4  ? 
7  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 312 ? 1_555 85.1  ? 
8  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 312 ? 1_555 87.4  ? 
9  O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 312 ? 1_555 93.4  ? 
10 O1B ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 312 ? 1_555 91.7  ? 
11 OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 324 ? 1_555 90.9  ? 
12 OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 324 ? 1_555 87.1  ? 
13 O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 324 ? 1_555 89.9  ? 
14 O1B ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 324 ? 1_555 93.4  ? 
15 O   ? K HOH .  ? A HOH 312 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 324 ? 1_555 173.7 ? 
16 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 OG1 ? B THR 36 ? B THR 35  ? 1_555 81.1  ? 
17 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O2G ? G GNP .  ? B GNP 201 ? 1_555 171.4 ? 
18 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O2G ? G GNP .  ? B GNP 201 ? 1_555 90.7  ? 
19 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O1B ? G GNP .  ? B GNP 201 ? 1_555 91.4  ? 
20 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O1B ? G GNP .  ? B GNP 201 ? 1_555 171.3 ? 
21 O2G ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O1B ? G GNP .  ? B GNP 201 ? 1_555 97.0  ? 
22 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 312 ? 1_555 84.0  ? 
23 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 312 ? 1_555 86.8  ? 
24 O2G ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 312 ? 1_555 93.2  ? 
25 O1B ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 312 ? 1_555 96.8  ? 
26 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 343 ? 1_555 82.6  ? 
27 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 343 ? 1_555 88.3  ? 
28 O2G ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 343 ? 1_555 99.6  ? 
29 O1B ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 343 ? 1_555 86.4  ? 
30 O   ? L HOH .  ? B HOH 312 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 343 ? 1_555 166.3 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 8 ? 
AA4 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA4 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 38  ? ILE A 47  ? GLU A 37  ILE A 46  
AA1 2 GLU A 50  ? THR A 59  ? GLU A 49  THR A 58  
AA1 3 THR A 3   ? GLY A 11  ? THR A 2   GLY A 10  
AA1 4 GLY A 78  ? ALA A 84  ? GLY A 77  ALA A 83  
AA1 5 MET A 112 ? ASN A 117 ? MET A 111 ASN A 116 
AA1 6 PHE A 142 ? GLU A 144 ? PHE A 141 GLU A 143 
AA2 1 GLU B 38  ? ILE B 47  ? GLU B 37  ILE B 46  
AA2 2 GLU B 50  ? THR B 59  ? GLU B 49  THR B 58  
AA2 3 THR B 3   ? GLY B 11  ? THR B 2   GLY B 10  
AA2 4 GLY B 78  ? ALA B 84  ? GLY B 77  ALA B 83  
AA2 5 MET B 112 ? ASN B 117 ? MET B 111 ASN B 116 
AA2 6 PHE B 142 ? GLU B 144 ? PHE B 141 GLU B 143 
AA3 1 PHE C 54  ? ILE C 58  ? PHE C 53  ILE C 57  
AA3 2 MET C 62  ? GLY C 65  ? MET C 61  GLY C 64  
AA3 3 PHE C 113 ? CYS C 116 ? PHE C 112 CYS C 115 
AA3 4 ILE C 98  ? MET C 101 ? ILE C 97  MET C 100 
AA3 5 VAL C 129 ? GLU C 135 ? VAL C 128 GLU C 134 
AA3 6 GLU C 16  ? LEU C 25  ? GLU C 15  LEU C 24  
AA3 7 THR C 6   ? VAL C 13  ? THR C 5   VAL C 12  
AA3 8 ILE C 157 ? GLN C 164 ? ILE C 156 GLN C 163 
AA4 1 ARG D 56  ? ILE D 58  ? ARG D 55  ILE D 57  
AA4 2 MET D 62  ? GLY D 65  ? MET D 61  GLY D 64  
AA4 3 PHE D 113 ? CYS D 116 ? PHE D 112 CYS D 115 
AA4 4 ILE D 98  ? MET D 101 ? ILE D 97  MET D 100 
AA4 5 VAL D 129 ? GLU D 135 ? VAL D 128 GLU D 134 
AA4 6 GLU D 16  ? LEU D 25  ? GLU D 15  LEU D 24  
AA4 7 THR D 6   ? VAL D 13  ? THR D 5   VAL D 12  
AA4 8 ILE D 157 ? GLN D 164 ? ILE D 156 GLN D 163 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 43  ? N LYS A 42  O LEU A 54  ? O LEU A 53  
AA1 2 3 O LEU A 57  ? O LEU A 56  N VAL A 9   ? N VAL A 8   
AA1 3 4 N VAL A 10  ? N VAL A 9   O VAL A 82  ? O VAL A 81  
AA1 4 5 N PHE A 83  ? N PHE A 82  O ASN A 117 ? O ASN A 116 
AA1 5 6 N LEU A 114 ? N LEU A 113 O ILE A 143 ? O ILE A 142 
AA2 1 2 N LYS B 43  ? N LYS B 42  O LEU B 54  ? O LEU B 53  
AA2 2 3 O LEU B 57  ? O LEU B 56  N VAL B 9   ? N VAL B 8   
AA2 3 4 N VAL B 10  ? N VAL B 9   O VAL B 82  ? O VAL B 81  
AA2 4 5 N PHE B 83  ? N PHE B 82  O ASN B 117 ? O ASN B 116 
AA2 5 6 N LEU B 114 ? N LEU B 113 O ILE B 143 ? O ILE B 142 
AA3 1 2 N ARG C 56  ? N ARG C 55  O GLN C 64  ? O GLN C 63  
AA3 2 3 N CYS C 63  ? N CYS C 62  O ILE C 115 ? O ILE C 114 
AA3 3 4 O CYS C 116 ? O CYS C 115 N ILE C 98  ? N ILE C 97  
AA3 4 5 N LEU C 99  ? N LEU C 98  O GLY C 131 ? O GLY C 130 
AA3 5 6 O LYS C 134 ? O LYS C 133 N SER C 22  ? N SER C 21  
AA3 6 7 O VAL C 21  ? O VAL C 20  N PHE C 9   ? N PHE C 8   
AA3 7 8 N ASP C 10  ? N ASP C 9   O ASP C 161 ? O ASP C 160 
AA4 1 2 N ARG D 56  ? N ARG D 55  O GLN D 64  ? O GLN D 63  
AA4 2 3 N CYS D 63  ? N CYS D 62  O ILE D 115 ? O ILE D 114 
AA4 3 4 O PHE D 114 ? O PHE D 113 N SER D 100 ? N SER D 99  
AA4 4 5 N LEU D 99  ? N LEU D 98  O GLY D 131 ? O GLY D 130 
AA4 5 6 O LYS D 132 ? O LYS D 131 N GLU D 24  ? N GLU D 23  
AA4 6 7 O VAL D 21  ? O VAL D 20  N PHE D 9   ? N PHE D 8   
AA4 7 8 N ASP D 10  ? N ASP D 9   O ASP D 161 ? O ASP D 160 
# 
_pdbx_entry_details.entry_id                   9BG5 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 30  ? ? -95.64  50.24  
2  1 LYS A 117 ? ? 73.51   31.40  
3  1 SER A 122 ? ? -91.45  49.07  
4  1 GLU B 37  ? ? -172.56 130.04 
5  1 ASP B 108 ? ? -117.03 61.29  
6  1 CYS B 118 ? ? -69.02  3.55   
7  1 CYS B 118 ? ? -67.35  1.80   
8  1 ARG B 123 ? ? -10.99  100.93 
9  1 PHE C 60  ? ? -132.30 -70.52 
10 1 LYS C 133 ? ? -91.47  -63.28 
11 1 PHE D 60  ? ? -136.40 -67.95 
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 N3 ? C A1AHB 201 ? PLANAR . 
2 1 N3 ? D A1AHB 201 ? PLANAR . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 C SER 0   ? C SER 1   
2 1 Y 1 C MET 1   ? C MET 2   
3 1 Y 1 C GLU 165 ? C GLU 166 
4 1 Y 1 D SER 0   ? D SER 1   
5 1 Y 1 D MET 1   ? D MET 2   
6 1 Y 1 D GLU 165 ? D GLU 166 
# 
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 
A1AHB C1     C  N N 1   
A1AHB C10    C  Y N 2   
A1AHB C11    C  Y N 3   
A1AHB C12    C  N N 4   
A1AHB C13    C  N S 5   
A1AHB C14    C  N N 6   
A1AHB C15    C  N S 7   
A1AHB C16    C  N N 8   
A1AHB C17    C  N S 9   
A1AHB C18    C  N N 10  
A1AHB C19    C  N N 11  
A1AHB C2     C  N N 12  
A1AHB C20    C  N N 13  
A1AHB C21    C  N N 14  
A1AHB C22    C  N N 15  
A1AHB C23    C  N S 16  
A1AHB C24    C  N N 17  
A1AHB C25    C  N N 18  
A1AHB C26    C  N N 19  
A1AHB C27    C  N N 20  
A1AHB C28    C  N N 21  
A1AHB C29    C  N N 22  
A1AHB C3     C  Y N 23  
A1AHB C30    C  Y N 24  
A1AHB C31    C  Y N 25  
A1AHB C32    C  Y N 26  
A1AHB C33    C  Y N 27  
A1AHB C34    C  Y N 28  
A1AHB C35    C  Y N 29  
A1AHB C36    C  Y N 30  
A1AHB C37    C  N N 31  
A1AHB C38    C  N N 32  
A1AHB C39    C  N N 33  
A1AHB C4     C  Y N 34  
A1AHB C40    C  N N 35  
A1AHB C41    C  N N 36  
A1AHB C42    C  N S 37  
A1AHB C43    C  N N 38  
A1AHB C44    C  N N 39  
A1AHB C5     C  Y N 40  
A1AHB C6     C  Y N 41  
A1AHB C7     C  Y N 42  
A1AHB C8     C  Y N 43  
A1AHB C9     C  Y N 44  
A1AHB N1     N  Y N 45  
A1AHB N2     N  N N 46  
A1AHB N3     N  N S 47  
A1AHB N4     N  N N 48  
A1AHB N5     N  Y N 49  
A1AHB N6     N  N N 50  
A1AHB N7     N  N N 51  
A1AHB N8     N  Y N 52  
A1AHB O1     O  N N 53  
A1AHB O2     O  N N 54  
A1AHB O3     O  N N 55  
A1AHB O4     O  N N 56  
A1AHB O5     O  N N 57  
A1AHB S1     S  Y N 58  
A1AHB H2     H  N N 59  
A1AHB H1     H  N N 60  
A1AHB H3     H  N N 61  
A1AHB H9     H  N N 62  
A1AHB H11    H  N N 63  
A1AHB H10    H  N N 64  
A1AHB H12    H  N N 65  
A1AHB H14    H  N N 66  
A1AHB H15    H  N N 67  
A1AHB H16    H  N N 68  
A1AHB H17    H  N N 69  
A1AHB H20    H  N N 70  
A1AHB H18    H  N N 71  
A1AHB H19    H  N N 72  
A1AHB H4     H  N N 73  
A1AHB H5     H  N N 74  
A1AHB H21    H  N N 75  
A1AHB H22    H  N N 76  
A1AHB H23    H  N N 77  
A1AHB H24    H  N N 78  
A1AHB H25    H  N N 79  
A1AHB H26    H  N N 80  
A1AHB H27    H  N N 81  
A1AHB H30    H  N N 82  
A1AHB H29    H  N N 83  
A1AHB H31    H  N N 84  
A1AHB H32    H  N N 85  
A1AHB H33    H  N N 86  
A1AHB H34    H  N N 87  
A1AHB H36    H  N N 88  
A1AHB H35    H  N N 89  
A1AHB H37    H  N N 90  
A1AHB H38    H  N N 91  
A1AHB H39    H  N N 92  
A1AHB H40    H  N N 93  
A1AHB H41    H  N N 94  
A1AHB H42    H  N N 95  
A1AHB H43    H  N N 96  
A1AHB H44    H  N N 97  
A1AHB H47    H  N N 98  
A1AHB H46    H  N N 99  
A1AHB H45    H  N N 100 
A1AHB H48    H  N N 101 
A1AHB H49    H  N N 102 
A1AHB H50    H  N N 103 
A1AHB H51    H  N N 104 
A1AHB H52    H  N N 105 
A1AHB H53    H  N N 106 
A1AHB H55    H  N N 107 
A1AHB H54    H  N N 108 
A1AHB H57    H  N N 109 
A1AHB H58    H  N N 110 
A1AHB H56    H  N N 111 
A1AHB H6     H  N N 112 
A1AHB H7     H  N N 113 
A1AHB H8     H  N N 114 
A1AHB H13    H  N N 115 
A1AHB H28    H  N N 116 
ALA   N      N  N N 117 
ALA   CA     C  N S 118 
ALA   C      C  N N 119 
ALA   O      O  N N 120 
ALA   CB     C  N N 121 
ALA   OXT    O  N N 122 
ALA   H      H  N N 123 
ALA   H2     H  N N 124 
ALA   HA     H  N N 125 
ALA   HB1    H  N N 126 
ALA   HB2    H  N N 127 
ALA   HB3    H  N N 128 
ALA   HXT    H  N N 129 
ARG   N      N  N N 130 
ARG   CA     C  N S 131 
ARG   C      C  N N 132 
ARG   O      O  N N 133 
ARG   CB     C  N N 134 
ARG   CG     C  N N 135 
ARG   CD     C  N N 136 
ARG   NE     N  N N 137 
ARG   CZ     C  N N 138 
ARG   NH1    N  N N 139 
ARG   NH2    N  N N 140 
ARG   OXT    O  N N 141 
ARG   H      H  N N 142 
ARG   H2     H  N N 143 
ARG   HA     H  N N 144 
ARG   HB2    H  N N 145 
ARG   HB3    H  N N 146 
ARG   HG2    H  N N 147 
ARG   HG3    H  N N 148 
ARG   HD2    H  N N 149 
ARG   HD3    H  N N 150 
ARG   HE     H  N N 151 
ARG   HH11   H  N N 152 
ARG   HH12   H  N N 153 
ARG   HH21   H  N N 154 
ARG   HH22   H  N N 155 
ARG   HXT    H  N N 156 
ASN   N      N  N N 157 
ASN   CA     C  N S 158 
ASN   C      C  N N 159 
ASN   O      O  N N 160 
ASN   CB     C  N N 161 
ASN   CG     C  N N 162 
ASN   OD1    O  N N 163 
ASN   ND2    N  N N 164 
ASN   OXT    O  N N 165 
ASN   H      H  N N 166 
ASN   H2     H  N N 167 
ASN   HA     H  N N 168 
ASN   HB2    H  N N 169 
ASN   HB3    H  N N 170 
ASN   HD21   H  N N 171 
ASN   HD22   H  N N 172 
ASN   HXT    H  N N 173 
ASP   N      N  N N 174 
ASP   CA     C  N S 175 
ASP   C      C  N N 176 
ASP   O      O  N N 177 
ASP   CB     C  N N 178 
ASP   CG     C  N N 179 
ASP   OD1    O  N N 180 
ASP   OD2    O  N N 181 
ASP   OXT    O  N N 182 
ASP   H      H  N N 183 
ASP   H2     H  N N 184 
ASP   HA     H  N N 185 
ASP   HB2    H  N N 186 
ASP   HB3    H  N N 187 
ASP   HD2    H  N N 188 
ASP   HXT    H  N N 189 
CYS   N      N  N N 190 
CYS   CA     C  N R 191 
CYS   C      C  N N 192 
CYS   O      O  N N 193 
CYS   CB     C  N N 194 
CYS   SG     S  N N 195 
CYS   OXT    O  N N 196 
CYS   H      H  N N 197 
CYS   H2     H  N N 198 
CYS   HA     H  N N 199 
CYS   HB2    H  N N 200 
CYS   HB3    H  N N 201 
CYS   HG     H  N N 202 
CYS   HXT    H  N N 203 
GLN   N      N  N N 204 
GLN   CA     C  N S 205 
GLN   C      C  N N 206 
GLN   O      O  N N 207 
GLN   CB     C  N N 208 
GLN   CG     C  N N 209 
GLN   CD     C  N N 210 
GLN   OE1    O  N N 211 
GLN   NE2    N  N N 212 
GLN   OXT    O  N N 213 
GLN   H      H  N N 214 
GLN   H2     H  N N 215 
GLN   HA     H  N N 216 
GLN   HB2    H  N N 217 
GLN   HB3    H  N N 218 
GLN   HG2    H  N N 219 
GLN   HG3    H  N N 220 
GLN   HE21   H  N N 221 
GLN   HE22   H  N N 222 
GLN   HXT    H  N N 223 
GLU   N      N  N N 224 
GLU   CA     C  N S 225 
GLU   C      C  N N 226 
GLU   O      O  N N 227 
GLU   CB     C  N N 228 
GLU   CG     C  N N 229 
GLU   CD     C  N N 230 
GLU   OE1    O  N N 231 
GLU   OE2    O  N N 232 
GLU   OXT    O  N N 233 
GLU   H      H  N N 234 
GLU   H2     H  N N 235 
GLU   HA     H  N N 236 
GLU   HB2    H  N N 237 
GLU   HB3    H  N N 238 
GLU   HG2    H  N N 239 
GLU   HG3    H  N N 240 
GLU   HE2    H  N N 241 
GLU   HXT    H  N N 242 
GLY   N      N  N N 243 
GLY   CA     C  N N 244 
GLY   C      C  N N 245 
GLY   O      O  N N 246 
GLY   OXT    O  N N 247 
GLY   H      H  N N 248 
GLY   H2     H  N N 249 
GLY   HA2    H  N N 250 
GLY   HA3    H  N N 251 
GLY   HXT    H  N N 252 
GNP   PG     P  N N 253 
GNP   O1G    O  N N 254 
GNP   O2G    O  N N 255 
GNP   O3G    O  N N 256 
GNP   N3B    N  N N 257 
GNP   PB     P  N R 258 
GNP   O1B    O  N N 259 
GNP   O2B    O  N N 260 
GNP   O3A    O  N N 261 
GNP   PA     P  N S 262 
GNP   O1A    O  N N 263 
GNP   O2A    O  N N 264 
GNP   "O5'"  O  N N 265 
GNP   "C5'"  C  N N 266 
GNP   "C4'"  C  N R 267 
GNP   "O4'"  O  N N 268 
GNP   "C3'"  C  N S 269 
GNP   "O3'"  O  N N 270 
GNP   "C2'"  C  N R 271 
GNP   "O2'"  O  N N 272 
GNP   "C1'"  C  N R 273 
GNP   N9     N  Y N 274 
GNP   C8     C  Y N 275 
GNP   N7     N  Y N 276 
GNP   C5     C  Y N 277 
GNP   C6     C  Y N 278 
GNP   O6     O  N N 279 
GNP   N1     N  Y N 280 
GNP   C2     C  Y N 281 
GNP   N2     N  N N 282 
GNP   N3     N  Y N 283 
GNP   C4     C  Y N 284 
GNP   HOG2   H  N N 285 
GNP   HOG3   H  N N 286 
GNP   HNB3   H  N N 287 
GNP   HOB2   H  N N 288 
GNP   HOA2   H  N N 289 
GNP   "H5'2" H  N N 290 
GNP   "H5'1" H  N N 291 
GNP   "H4'"  H  N N 292 
GNP   "H3'"  H  N N 293 
GNP   "HO3'" H  N N 294 
GNP   "H2'"  H  N N 295 
GNP   "HO2'" H  N N 296 
GNP   "H1'"  H  N N 297 
GNP   H8     H  N N 298 
GNP   HN1    H  N N 299 
GNP   HN21   H  N N 300 
GNP   HN22   H  N N 301 
HIS   N      N  N N 302 
HIS   CA     C  N S 303 
HIS   C      C  N N 304 
HIS   O      O  N N 305 
HIS   CB     C  N N 306 
HIS   CG     C  Y N 307 
HIS   ND1    N  Y N 308 
HIS   CD2    C  Y N 309 
HIS   CE1    C  Y N 310 
HIS   NE2    N  Y N 311 
HIS   OXT    O  N N 312 
HIS   H      H  N N 313 
HIS   H2     H  N N 314 
HIS   HA     H  N N 315 
HIS   HB2    H  N N 316 
HIS   HB3    H  N N 317 
HIS   HD1    H  N N 318 
HIS   HD2    H  N N 319 
HIS   HE1    H  N N 320 
HIS   HE2    H  N N 321 
HIS   HXT    H  N N 322 
HOH   O      O  N N 323 
HOH   H1     H  N N 324 
HOH   H2     H  N N 325 
ILE   N      N  N N 326 
ILE   CA     C  N S 327 
ILE   C      C  N N 328 
ILE   O      O  N N 329 
ILE   CB     C  N S 330 
ILE   CG1    C  N N 331 
ILE   CG2    C  N N 332 
ILE   CD1    C  N N 333 
ILE   OXT    O  N N 334 
ILE   H      H  N N 335 
ILE   H2     H  N N 336 
ILE   HA     H  N N 337 
ILE   HB     H  N N 338 
ILE   HG12   H  N N 339 
ILE   HG13   H  N N 340 
ILE   HG21   H  N N 341 
ILE   HG22   H  N N 342 
ILE   HG23   H  N N 343 
ILE   HD11   H  N N 344 
ILE   HD12   H  N N 345 
ILE   HD13   H  N N 346 
ILE   HXT    H  N N 347 
LEU   N      N  N N 348 
LEU   CA     C  N S 349 
LEU   C      C  N N 350 
LEU   O      O  N N 351 
LEU   CB     C  N N 352 
LEU   CG     C  N N 353 
LEU   CD1    C  N N 354 
LEU   CD2    C  N N 355 
LEU   OXT    O  N N 356 
LEU   H      H  N N 357 
LEU   H2     H  N N 358 
LEU   HA     H  N N 359 
LEU   HB2    H  N N 360 
LEU   HB3    H  N N 361 
LEU   HG     H  N N 362 
LEU   HD11   H  N N 363 
LEU   HD12   H  N N 364 
LEU   HD13   H  N N 365 
LEU   HD21   H  N N 366 
LEU   HD22   H  N N 367 
LEU   HD23   H  N N 368 
LEU   HXT    H  N N 369 
LYS   N      N  N N 370 
LYS   CA     C  N S 371 
LYS   C      C  N N 372 
LYS   O      O  N N 373 
LYS   CB     C  N N 374 
LYS   CG     C  N N 375 
LYS   CD     C  N N 376 
LYS   CE     C  N N 377 
LYS   NZ     N  N N 378 
LYS   OXT    O  N N 379 
LYS   H      H  N N 380 
LYS   H2     H  N N 381 
LYS   HA     H  N N 382 
LYS   HB2    H  N N 383 
LYS   HB3    H  N N 384 
LYS   HG2    H  N N 385 
LYS   HG3    H  N N 386 
LYS   HD2    H  N N 387 
LYS   HD3    H  N N 388 
LYS   HE2    H  N N 389 
LYS   HE3    H  N N 390 
LYS   HZ1    H  N N 391 
LYS   HZ2    H  N N 392 
LYS   HZ3    H  N N 393 
LYS   HXT    H  N N 394 
MET   N      N  N N 395 
MET   CA     C  N S 396 
MET   C      C  N N 397 
MET   O      O  N N 398 
MET   CB     C  N N 399 
MET   CG     C  N N 400 
MET   SD     S  N N 401 
MET   CE     C  N N 402 
MET   OXT    O  N N 403 
MET   H      H  N N 404 
MET   H2     H  N N 405 
MET   HA     H  N N 406 
MET   HB2    H  N N 407 
MET   HB3    H  N N 408 
MET   HG2    H  N N 409 
MET   HG3    H  N N 410 
MET   HE1    H  N N 411 
MET   HE2    H  N N 412 
MET   HE3    H  N N 413 
MET   HXT    H  N N 414 
MG    MG     MG N N 415 
PHE   N      N  N N 416 
PHE   CA     C  N S 417 
PHE   C      C  N N 418 
PHE   O      O  N N 419 
PHE   CB     C  N N 420 
PHE   CG     C  Y N 421 
PHE   CD1    C  Y N 422 
PHE   CD2    C  Y N 423 
PHE   CE1    C  Y N 424 
PHE   CE2    C  Y N 425 
PHE   CZ     C  Y N 426 
PHE   OXT    O  N N 427 
PHE   H      H  N N 428 
PHE   H2     H  N N 429 
PHE   HA     H  N N 430 
PHE   HB2    H  N N 431 
PHE   HB3    H  N N 432 
PHE   HD1    H  N N 433 
PHE   HD2    H  N N 434 
PHE   HE1    H  N N 435 
PHE   HE2    H  N N 436 
PHE   HZ     H  N N 437 
PHE   HXT    H  N N 438 
PRO   N      N  N N 439 
PRO   CA     C  N S 440 
PRO   C      C  N N 441 
PRO   O      O  N N 442 
PRO   CB     C  N N 443 
PRO   CG     C  N N 444 
PRO   CD     C  N N 445 
PRO   OXT    O  N N 446 
PRO   H      H  N N 447 
PRO   HA     H  N N 448 
PRO   HB2    H  N N 449 
PRO   HB3    H  N N 450 
PRO   HG2    H  N N 451 
PRO   HG3    H  N N 452 
PRO   HD2    H  N N 453 
PRO   HD3    H  N N 454 
PRO   HXT    H  N N 455 
SER   N      N  N N 456 
SER   CA     C  N S 457 
SER   C      C  N N 458 
SER   O      O  N N 459 
SER   CB     C  N N 460 
SER   OG     O  N N 461 
SER   OXT    O  N N 462 
SER   H      H  N N 463 
SER   H2     H  N N 464 
SER   HA     H  N N 465 
SER   HB2    H  N N 466 
SER   HB3    H  N N 467 
SER   HG     H  N N 468 
SER   HXT    H  N N 469 
THR   N      N  N N 470 
THR   CA     C  N S 471 
THR   C      C  N N 472 
THR   O      O  N N 473 
THR   CB     C  N R 474 
THR   OG1    O  N N 475 
THR   CG2    C  N N 476 
THR   OXT    O  N N 477 
THR   H      H  N N 478 
THR   H2     H  N N 479 
THR   HA     H  N N 480 
THR   HB     H  N N 481 
THR   HG1    H  N N 482 
THR   HG21   H  N N 483 
THR   HG22   H  N N 484 
THR   HG23   H  N N 485 
THR   HXT    H  N N 486 
TRP   N      N  N N 487 
TRP   CA     C  N S 488 
TRP   C      C  N N 489 
TRP   O      O  N N 490 
TRP   CB     C  N N 491 
TRP   CG     C  Y N 492 
TRP   CD1    C  Y N 493 
TRP   CD2    C  Y N 494 
TRP   NE1    N  Y N 495 
TRP   CE2    C  Y N 496 
TRP   CE3    C  Y N 497 
TRP   CZ2    C  Y N 498 
TRP   CZ3    C  Y N 499 
TRP   CH2    C  Y N 500 
TRP   OXT    O  N N 501 
TRP   H      H  N N 502 
TRP   H2     H  N N 503 
TRP   HA     H  N N 504 
TRP   HB2    H  N N 505 
TRP   HB3    H  N N 506 
TRP   HD1    H  N N 507 
TRP   HE1    H  N N 508 
TRP   HE3    H  N N 509 
TRP   HZ2    H  N N 510 
TRP   HZ3    H  N N 511 
TRP   HH2    H  N N 512 
TRP   HXT    H  N N 513 
TYR   N      N  N N 514 
TYR   CA     C  N S 515 
TYR   C      C  N N 516 
TYR   O      O  N N 517 
TYR   CB     C  N N 518 
TYR   CG     C  Y N 519 
TYR   CD1    C  Y N 520 
TYR   CD2    C  Y N 521 
TYR   CE1    C  Y N 522 
TYR   CE2    C  Y N 523 
TYR   CZ     C  Y N 524 
TYR   OH     O  N N 525 
TYR   OXT    O  N N 526 
TYR   H      H  N N 527 
TYR   H2     H  N N 528 
TYR   HA     H  N N 529 
TYR   HB2    H  N N 530 
TYR   HB3    H  N N 531 
TYR   HD1    H  N N 532 
TYR   HD2    H  N N 533 
TYR   HE1    H  N N 534 
TYR   HE2    H  N N 535 
TYR   HH     H  N N 536 
TYR   HXT    H  N N 537 
VAL   N      N  N N 538 
VAL   CA     C  N S 539 
VAL   C      C  N N 540 
VAL   O      O  N N 541 
VAL   CB     C  N N 542 
VAL   CG1    C  N N 543 
VAL   CG2    C  N N 544 
VAL   OXT    O  N N 545 
VAL   H      H  N N 546 
VAL   H2     H  N N 547 
VAL   HA     H  N N 548 
VAL   HB     H  N N 549 
VAL   HG11   H  N N 550 
VAL   HG12   H  N N 551 
VAL   HG13   H  N N 552 
VAL   HG21   H  N N 553 
VAL   HG22   H  N N 554 
VAL   HG23   H  N N 555 
VAL   HXT    H  N N 556 
# 
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 
A1AHB C1    C2     sing N N 1   
A1AHB C2    N1     sing N N 2   
A1AHB N1    C3     sing Y N 3   
A1AHB C3    C4     doub Y N 4   
A1AHB C4    C5     sing Y N 5   
A1AHB C5    C6     doub Y N 6   
A1AHB C6    C7     sing Y N 7   
A1AHB C7    C8     doub Y N 8   
A1AHB C6    C9     sing N N 9   
A1AHB C9    C10    doub Y N 10  
A1AHB C10   S1     sing Y N 11  
A1AHB S1    C11    sing Y N 12  
A1AHB C11   C12    sing N N 13  
A1AHB C12   C13    sing N N 14  
A1AHB C13   N2     sing N N 15  
A1AHB N2    C14    sing N N 16  
A1AHB C14   O1     doub N N 17  
A1AHB C14   C15    sing N N 18  
A1AHB C15   C16    sing N N 19  
A1AHB C16   C17    sing N N 20  
A1AHB C17   C18    sing N N 21  
A1AHB C13   C19    sing N N 22  
A1AHB C19   O2     doub N N 23  
A1AHB C19   N3     sing N N 24  
A1AHB N3    C20    sing N N 25  
A1AHB C20   C21    sing N N 26  
A1AHB C21   C22    sing N N 27  
A1AHB C22   C23    sing N N 28  
A1AHB C23   N4     sing N N 29  
A1AHB C23   C24    sing N N 30  
A1AHB C24   O3     doub N N 31  
A1AHB C24   O4     sing N N 32  
A1AHB O4    C25    sing N N 33  
A1AHB C25   C26    sing N N 34  
A1AHB C26   C27    sing N N 35  
A1AHB C26   C28    sing N N 36  
A1AHB C26   C29    sing N N 37  
A1AHB C29   C30    sing N N 38  
A1AHB C30   C31    doub Y N 39  
A1AHB C31   C32    sing N N 40  
A1AHB C32   C33    doub Y N 41  
A1AHB C33   N5     sing Y N 42  
A1AHB N5    C34    doub Y N 43  
A1AHB C34   C35    sing Y N 44  
A1AHB C35   C36    doub Y N 45  
A1AHB C35   N6     sing N N 46  
A1AHB N6    C37    sing N N 47  
A1AHB C37   C38    sing N N 48  
A1AHB C38   N7     sing N N 49  
A1AHB N7    C39    sing N N 50  
A1AHB N7    C40    sing N N 51  
A1AHB C40   C41    sing N N 52  
A1AHB C33   C42    sing N N 53  
A1AHB C42   C43    sing N N 54  
A1AHB C42   O5     sing N N 55  
A1AHB O5    C44    sing N N 56  
A1AHB C11   N8     doub Y N 57  
A1AHB N1    C31    sing Y N 58  
A1AHB C32   C36    sing Y N 59  
A1AHB N6    C41    sing N N 60  
A1AHB C3    C8     sing Y N 61  
A1AHB C9    N8     sing Y N 62  
A1AHB C4    C30    sing Y N 63  
A1AHB C15   C17    sing N N 64  
A1AHB N3    N4     sing N N 65  
A1AHB C1    H2     sing N N 66  
A1AHB C1    H1     sing N N 67  
A1AHB C1    H3     sing N N 68  
A1AHB C10   H9     sing N N 69  
A1AHB C12   H11    sing N N 70  
A1AHB C12   H10    sing N N 71  
A1AHB C13   H12    sing N N 72  
A1AHB C15   H14    sing N N 73  
A1AHB C16   H15    sing N N 74  
A1AHB C16   H16    sing N N 75  
A1AHB C17   H17    sing N N 76  
A1AHB C18   H20    sing N N 77  
A1AHB C18   H18    sing N N 78  
A1AHB C18   H19    sing N N 79  
A1AHB C2    H4     sing N N 80  
A1AHB C2    H5     sing N N 81  
A1AHB C20   H21    sing N N 82  
A1AHB C20   H22    sing N N 83  
A1AHB C21   H23    sing N N 84  
A1AHB C21   H24    sing N N 85  
A1AHB C22   H25    sing N N 86  
A1AHB C22   H26    sing N N 87  
A1AHB C23   H27    sing N N 88  
A1AHB C25   H30    sing N N 89  
A1AHB C25   H29    sing N N 90  
A1AHB C27   H31    sing N N 91  
A1AHB C27   H32    sing N N 92  
A1AHB C27   H33    sing N N 93  
A1AHB C28   H34    sing N N 94  
A1AHB C28   H36    sing N N 95  
A1AHB C28   H35    sing N N 96  
A1AHB C29   H37    sing N N 97  
A1AHB C29   H38    sing N N 98  
A1AHB C34   H39    sing N N 99  
A1AHB C36   H40    sing N N 100 
A1AHB C37   H41    sing N N 101 
A1AHB C37   H42    sing N N 102 
A1AHB C38   H43    sing N N 103 
A1AHB C38   H44    sing N N 104 
A1AHB C39   H47    sing N N 105 
A1AHB C39   H46    sing N N 106 
A1AHB C39   H45    sing N N 107 
A1AHB C40   H48    sing N N 108 
A1AHB C40   H49    sing N N 109 
A1AHB C41   H50    sing N N 110 
A1AHB C41   H51    sing N N 111 
A1AHB C42   H52    sing N N 112 
A1AHB C43   H53    sing N N 113 
A1AHB C43   H55    sing N N 114 
A1AHB C43   H54    sing N N 115 
A1AHB C44   H57    sing N N 116 
A1AHB C44   H58    sing N N 117 
A1AHB C44   H56    sing N N 118 
A1AHB C5    H6     sing N N 119 
A1AHB C7    H7     sing N N 120 
A1AHB C8    H8     sing N N 121 
A1AHB N2    H13    sing N N 122 
A1AHB N4    H28    sing N N 123 
ALA   N     CA     sing N N 124 
ALA   N     H      sing N N 125 
ALA   N     H2     sing N N 126 
ALA   CA    C      sing N N 127 
ALA   CA    CB     sing N N 128 
ALA   CA    HA     sing N N 129 
ALA   C     O      doub N N 130 
ALA   C     OXT    sing N N 131 
ALA   CB    HB1    sing N N 132 
ALA   CB    HB2    sing N N 133 
ALA   CB    HB3    sing N N 134 
ALA   OXT   HXT    sing N N 135 
ARG   N     CA     sing N N 136 
ARG   N     H      sing N N 137 
ARG   N     H2     sing N N 138 
ARG   CA    C      sing N N 139 
ARG   CA    CB     sing N N 140 
ARG   CA    HA     sing N N 141 
ARG   C     O      doub N N 142 
ARG   C     OXT    sing N N 143 
ARG   CB    CG     sing N N 144 
ARG   CB    HB2    sing N N 145 
ARG   CB    HB3    sing N N 146 
ARG   CG    CD     sing N N 147 
ARG   CG    HG2    sing N N 148 
ARG   CG    HG3    sing N N 149 
ARG   CD    NE     sing N N 150 
ARG   CD    HD2    sing N N 151 
ARG   CD    HD3    sing N N 152 
ARG   NE    CZ     sing N N 153 
ARG   NE    HE     sing N N 154 
ARG   CZ    NH1    sing N N 155 
ARG   CZ    NH2    doub N N 156 
ARG   NH1   HH11   sing N N 157 
ARG   NH1   HH12   sing N N 158 
ARG   NH2   HH21   sing N N 159 
ARG   NH2   HH22   sing N N 160 
ARG   OXT   HXT    sing N N 161 
ASN   N     CA     sing N N 162 
ASN   N     H      sing N N 163 
ASN   N     H2     sing N N 164 
ASN   CA    C      sing N N 165 
ASN   CA    CB     sing N N 166 
ASN   CA    HA     sing N N 167 
ASN   C     O      doub N N 168 
ASN   C     OXT    sing N N 169 
ASN   CB    CG     sing N N 170 
ASN   CB    HB2    sing N N 171 
ASN   CB    HB3    sing N N 172 
ASN   CG    OD1    doub N N 173 
ASN   CG    ND2    sing N N 174 
ASN   ND2   HD21   sing N N 175 
ASN   ND2   HD22   sing N N 176 
ASN   OXT   HXT    sing N N 177 
ASP   N     CA     sing N N 178 
ASP   N     H      sing N N 179 
ASP   N     H2     sing N N 180 
ASP   CA    C      sing N N 181 
ASP   CA    CB     sing N N 182 
ASP   CA    HA     sing N N 183 
ASP   C     O      doub N N 184 
ASP   C     OXT    sing N N 185 
ASP   CB    CG     sing N N 186 
ASP   CB    HB2    sing N N 187 
ASP   CB    HB3    sing N N 188 
ASP   CG    OD1    doub N N 189 
ASP   CG    OD2    sing N N 190 
ASP   OD2   HD2    sing N N 191 
ASP   OXT   HXT    sing N N 192 
CYS   N     CA     sing N N 193 
CYS   N     H      sing N N 194 
CYS   N     H2     sing N N 195 
CYS   CA    C      sing N N 196 
CYS   CA    CB     sing N N 197 
CYS   CA    HA     sing N N 198 
CYS   C     O      doub N N 199 
CYS   C     OXT    sing N N 200 
CYS   CB    SG     sing N N 201 
CYS   CB    HB2    sing N N 202 
CYS   CB    HB3    sing N N 203 
CYS   SG    HG     sing N N 204 
CYS   OXT   HXT    sing N N 205 
GLN   N     CA     sing N N 206 
GLN   N     H      sing N N 207 
GLN   N     H2     sing N N 208 
GLN   CA    C      sing N N 209 
GLN   CA    CB     sing N N 210 
GLN   CA    HA     sing N N 211 
GLN   C     O      doub N N 212 
GLN   C     OXT    sing N N 213 
GLN   CB    CG     sing N N 214 
GLN   CB    HB2    sing N N 215 
GLN   CB    HB3    sing N N 216 
GLN   CG    CD     sing N N 217 
GLN   CG    HG2    sing N N 218 
GLN   CG    HG3    sing N N 219 
GLN   CD    OE1    doub N N 220 
GLN   CD    NE2    sing N N 221 
GLN   NE2   HE21   sing N N 222 
GLN   NE2   HE22   sing N N 223 
GLN   OXT   HXT    sing N N 224 
GLU   N     CA     sing N N 225 
GLU   N     H      sing N N 226 
GLU   N     H2     sing N N 227 
GLU   CA    C      sing N N 228 
GLU   CA    CB     sing N N 229 
GLU   CA    HA     sing N N 230 
GLU   C     O      doub N N 231 
GLU   C     OXT    sing N N 232 
GLU   CB    CG     sing N N 233 
GLU   CB    HB2    sing N N 234 
GLU   CB    HB3    sing N N 235 
GLU   CG    CD     sing N N 236 
GLU   CG    HG2    sing N N 237 
GLU   CG    HG3    sing N N 238 
GLU   CD    OE1    doub N N 239 
GLU   CD    OE2    sing N N 240 
GLU   OE2   HE2    sing N N 241 
GLU   OXT   HXT    sing N N 242 
GLY   N     CA     sing N N 243 
GLY   N     H      sing N N 244 
GLY   N     H2     sing N N 245 
GLY   CA    C      sing N N 246 
GLY   CA    HA2    sing N N 247 
GLY   CA    HA3    sing N N 248 
GLY   C     O      doub N N 249 
GLY   C     OXT    sing N N 250 
GLY   OXT   HXT    sing N N 251 
GNP   PG    O1G    doub N N 252 
GNP   PG    O2G    sing N N 253 
GNP   PG    O3G    sing N N 254 
GNP   PG    N3B    sing N N 255 
GNP   O2G   HOG2   sing N N 256 
GNP   O3G   HOG3   sing N N 257 
GNP   N3B   PB     sing N N 258 
GNP   N3B   HNB3   sing N N 259 
GNP   PB    O1B    doub N N 260 
GNP   PB    O2B    sing N N 261 
GNP   PB    O3A    sing N N 262 
GNP   O2B   HOB2   sing N N 263 
GNP   O3A   PA     sing N N 264 
GNP   PA    O1A    doub N N 265 
GNP   PA    O2A    sing N N 266 
GNP   PA    "O5'"  sing N N 267 
GNP   O2A   HOA2   sing N N 268 
GNP   "O5'" "C5'"  sing N N 269 
GNP   "C5'" "C4'"  sing N N 270 
GNP   "C5'" "H5'2" sing N N 271 
GNP   "C5'" "H5'1" sing N N 272 
GNP   "C4'" "O4'"  sing N N 273 
GNP   "C4'" "C3'"  sing N N 274 
GNP   "C4'" "H4'"  sing N N 275 
GNP   "O4'" "C1'"  sing N N 276 
GNP   "C3'" "O3'"  sing N N 277 
GNP   "C3'" "C2'"  sing N N 278 
GNP   "C3'" "H3'"  sing N N 279 
GNP   "O3'" "HO3'" sing N N 280 
GNP   "C2'" "O2'"  sing N N 281 
GNP   "C2'" "C1'"  sing N N 282 
GNP   "C2'" "H2'"  sing N N 283 
GNP   "O2'" "HO2'" sing N N 284 
GNP   "C1'" N9     sing N N 285 
GNP   "C1'" "H1'"  sing N N 286 
GNP   N9    C8     sing Y N 287 
GNP   N9    C4     sing Y N 288 
GNP   C8    N7     doub Y N 289 
GNP   C8    H8     sing N N 290 
GNP   N7    C5     sing Y N 291 
GNP   C5    C6     sing Y N 292 
GNP   C5    C4     doub Y N 293 
GNP   C6    O6     doub N N 294 
GNP   C6    N1     sing Y N 295 
GNP   N1    C2     sing Y N 296 
GNP   N1    HN1    sing N N 297 
GNP   C2    N2     sing N N 298 
GNP   C2    N3     doub Y N 299 
GNP   N2    HN21   sing N N 300 
GNP   N2    HN22   sing N N 301 
GNP   N3    C4     sing Y N 302 
HIS   N     CA     sing N N 303 
HIS   N     H      sing N N 304 
HIS   N     H2     sing N N 305 
HIS   CA    C      sing N N 306 
HIS   CA    CB     sing N N 307 
HIS   CA    HA     sing N N 308 
HIS   C     O      doub N N 309 
HIS   C     OXT    sing N N 310 
HIS   CB    CG     sing N N 311 
HIS   CB    HB2    sing N N 312 
HIS   CB    HB3    sing N N 313 
HIS   CG    ND1    sing Y N 314 
HIS   CG    CD2    doub Y N 315 
HIS   ND1   CE1    doub Y N 316 
HIS   ND1   HD1    sing N N 317 
HIS   CD2   NE2    sing Y N 318 
HIS   CD2   HD2    sing N N 319 
HIS   CE1   NE2    sing Y N 320 
HIS   CE1   HE1    sing N N 321 
HIS   NE2   HE2    sing N N 322 
HIS   OXT   HXT    sing N N 323 
HOH   O     H1     sing N N 324 
HOH   O     H2     sing N N 325 
ILE   N     CA     sing N N 326 
ILE   N     H      sing N N 327 
ILE   N     H2     sing N N 328 
ILE   CA    C      sing N N 329 
ILE   CA    CB     sing N N 330 
ILE   CA    HA     sing N N 331 
ILE   C     O      doub N N 332 
ILE   C     OXT    sing N N 333 
ILE   CB    CG1    sing N N 334 
ILE   CB    CG2    sing N N 335 
ILE   CB    HB     sing N N 336 
ILE   CG1   CD1    sing N N 337 
ILE   CG1   HG12   sing N N 338 
ILE   CG1   HG13   sing N N 339 
ILE   CG2   HG21   sing N N 340 
ILE   CG2   HG22   sing N N 341 
ILE   CG2   HG23   sing N N 342 
ILE   CD1   HD11   sing N N 343 
ILE   CD1   HD12   sing N N 344 
ILE   CD1   HD13   sing N N 345 
ILE   OXT   HXT    sing N N 346 
LEU   N     CA     sing N N 347 
LEU   N     H      sing N N 348 
LEU   N     H2     sing N N 349 
LEU   CA    C      sing N N 350 
LEU   CA    CB     sing N N 351 
LEU   CA    HA     sing N N 352 
LEU   C     O      doub N N 353 
LEU   C     OXT    sing N N 354 
LEU   CB    CG     sing N N 355 
LEU   CB    HB2    sing N N 356 
LEU   CB    HB3    sing N N 357 
LEU   CG    CD1    sing N N 358 
LEU   CG    CD2    sing N N 359 
LEU   CG    HG     sing N N 360 
LEU   CD1   HD11   sing N N 361 
LEU   CD1   HD12   sing N N 362 
LEU   CD1   HD13   sing N N 363 
LEU   CD2   HD21   sing N N 364 
LEU   CD2   HD22   sing N N 365 
LEU   CD2   HD23   sing N N 366 
LEU   OXT   HXT    sing N N 367 
LYS   N     CA     sing N N 368 
LYS   N     H      sing N N 369 
LYS   N     H2     sing N N 370 
LYS   CA    C      sing N N 371 
LYS   CA    CB     sing N N 372 
LYS   CA    HA     sing N N 373 
LYS   C     O      doub N N 374 
LYS   C     OXT    sing N N 375 
LYS   CB    CG     sing N N 376 
LYS   CB    HB2    sing N N 377 
LYS   CB    HB3    sing N N 378 
LYS   CG    CD     sing N N 379 
LYS   CG    HG2    sing N N 380 
LYS   CG    HG3    sing N N 381 
LYS   CD    CE     sing N N 382 
LYS   CD    HD2    sing N N 383 
LYS   CD    HD3    sing N N 384 
LYS   CE    NZ     sing N N 385 
LYS   CE    HE2    sing N N 386 
LYS   CE    HE3    sing N N 387 
LYS   NZ    HZ1    sing N N 388 
LYS   NZ    HZ2    sing N N 389 
LYS   NZ    HZ3    sing N N 390 
LYS   OXT   HXT    sing N N 391 
MET   N     CA     sing N N 392 
MET   N     H      sing N N 393 
MET   N     H2     sing N N 394 
MET   CA    C      sing N N 395 
MET   CA    CB     sing N N 396 
MET   CA    HA     sing N N 397 
MET   C     O      doub N N 398 
MET   C     OXT    sing N N 399 
MET   CB    CG     sing N N 400 
MET   CB    HB2    sing N N 401 
MET   CB    HB3    sing N N 402 
MET   CG    SD     sing N N 403 
MET   CG    HG2    sing N N 404 
MET   CG    HG3    sing N N 405 
MET   SD    CE     sing N N 406 
MET   CE    HE1    sing N N 407 
MET   CE    HE2    sing N N 408 
MET   CE    HE3    sing N N 409 
MET   OXT   HXT    sing N N 410 
PHE   N     CA     sing N N 411 
PHE   N     H      sing N N 412 
PHE   N     H2     sing N N 413 
PHE   CA    C      sing N N 414 
PHE   CA    CB     sing N N 415 
PHE   CA    HA     sing N N 416 
PHE   C     O      doub N N 417 
PHE   C     OXT    sing N N 418 
PHE   CB    CG     sing N N 419 
PHE   CB    HB2    sing N N 420 
PHE   CB    HB3    sing N N 421 
PHE   CG    CD1    doub Y N 422 
PHE   CG    CD2    sing Y N 423 
PHE   CD1   CE1    sing Y N 424 
PHE   CD1   HD1    sing N N 425 
PHE   CD2   CE2    doub Y N 426 
PHE   CD2   HD2    sing N N 427 
PHE   CE1   CZ     doub Y N 428 
PHE   CE1   HE1    sing N N 429 
PHE   CE2   CZ     sing Y N 430 
PHE   CE2   HE2    sing N N 431 
PHE   CZ    HZ     sing N N 432 
PHE   OXT   HXT    sing N N 433 
PRO   N     CA     sing N N 434 
PRO   N     CD     sing N N 435 
PRO   N     H      sing N N 436 
PRO   CA    C      sing N N 437 
PRO   CA    CB     sing N N 438 
PRO   CA    HA     sing N N 439 
PRO   C     O      doub N N 440 
PRO   C     OXT    sing N N 441 
PRO   CB    CG     sing N N 442 
PRO   CB    HB2    sing N N 443 
PRO   CB    HB3    sing N N 444 
PRO   CG    CD     sing N N 445 
PRO   CG    HG2    sing N N 446 
PRO   CG    HG3    sing N N 447 
PRO   CD    HD2    sing N N 448 
PRO   CD    HD3    sing N N 449 
PRO   OXT   HXT    sing N N 450 
SER   N     CA     sing N N 451 
SER   N     H      sing N N 452 
SER   N     H2     sing N N 453 
SER   CA    C      sing N N 454 
SER   CA    CB     sing N N 455 
SER   CA    HA     sing N N 456 
SER   C     O      doub N N 457 
SER   C     OXT    sing N N 458 
SER   CB    OG     sing N N 459 
SER   CB    HB2    sing N N 460 
SER   CB    HB3    sing N N 461 
SER   OG    HG     sing N N 462 
SER   OXT   HXT    sing N N 463 
THR   N     CA     sing N N 464 
THR   N     H      sing N N 465 
THR   N     H2     sing N N 466 
THR   CA    C      sing N N 467 
THR   CA    CB     sing N N 468 
THR   CA    HA     sing N N 469 
THR   C     O      doub N N 470 
THR   C     OXT    sing N N 471 
THR   CB    OG1    sing N N 472 
THR   CB    CG2    sing N N 473 
THR   CB    HB     sing N N 474 
THR   OG1   HG1    sing N N 475 
THR   CG2   HG21   sing N N 476 
THR   CG2   HG22   sing N N 477 
THR   CG2   HG23   sing N N 478 
THR   OXT   HXT    sing N N 479 
TRP   N     CA     sing N N 480 
TRP   N     H      sing N N 481 
TRP   N     H2     sing N N 482 
TRP   CA    C      sing N N 483 
TRP   CA    CB     sing N N 484 
TRP   CA    HA     sing N N 485 
TRP   C     O      doub N N 486 
TRP   C     OXT    sing N N 487 
TRP   CB    CG     sing N N 488 
TRP   CB    HB2    sing N N 489 
TRP   CB    HB3    sing N N 490 
TRP   CG    CD1    doub Y N 491 
TRP   CG    CD2    sing Y N 492 
TRP   CD1   NE1    sing Y N 493 
TRP   CD1   HD1    sing N N 494 
TRP   CD2   CE2    doub Y N 495 
TRP   CD2   CE3    sing Y N 496 
TRP   NE1   CE2    sing Y N 497 
TRP   NE1   HE1    sing N N 498 
TRP   CE2   CZ2    sing Y N 499 
TRP   CE3   CZ3    doub Y N 500 
TRP   CE3   HE3    sing N N 501 
TRP   CZ2   CH2    doub Y N 502 
TRP   CZ2   HZ2    sing N N 503 
TRP   CZ3   CH2    sing Y N 504 
TRP   CZ3   HZ3    sing N N 505 
TRP   CH2   HH2    sing N N 506 
TRP   OXT   HXT    sing N N 507 
TYR   N     CA     sing N N 508 
TYR   N     H      sing N N 509 
TYR   N     H2     sing N N 510 
TYR   CA    C      sing N N 511 
TYR   CA    CB     sing N N 512 
TYR   CA    HA     sing N N 513 
TYR   C     O      doub N N 514 
TYR   C     OXT    sing N N 515 
TYR   CB    CG     sing N N 516 
TYR   CB    HB2    sing N N 517 
TYR   CB    HB3    sing N N 518 
TYR   CG    CD1    doub Y N 519 
TYR   CG    CD2    sing Y N 520 
TYR   CD1   CE1    sing Y N 521 
TYR   CD1   HD1    sing N N 522 
TYR   CD2   CE2    doub Y N 523 
TYR   CD2   HD2    sing N N 524 
TYR   CE1   CZ     doub Y N 525 
TYR   CE1   HE1    sing N N 526 
TYR   CE2   CZ     sing Y N 527 
TYR   CE2   HE2    sing N N 528 
TYR   CZ    OH     sing N N 529 
TYR   OH    HH     sing N N 530 
TYR   OXT   HXT    sing N N 531 
VAL   N     CA     sing N N 532 
VAL   N     H      sing N N 533 
VAL   N     H2     sing N N 534 
VAL   CA    C      sing N N 535 
VAL   CA    CB     sing N N 536 
VAL   CA    HA     sing N N 537 
VAL   C     O      doub N N 538 
VAL   C     OXT    sing N N 539 
VAL   CB    CG1    sing N N 540 
VAL   CB    CG2    sing N N 541 
VAL   CB    HB     sing N N 542 
VAL   CG1   HG11   sing N N 543 
VAL   CG1   HG12   sing N N 544 
VAL   CG1   HG13   sing N N 545 
VAL   CG2   HG21   sing N N 546 
VAL   CG2   HG22   sing N N 547 
VAL   CG2   HG23   sing N N 548 
VAL   OXT   HXT    sing N N 549 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          in-house 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BG5 
_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]   0.015088 
_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]   0.011830 
_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]   0.007795 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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     . SER   A 1 1   ? 5.54854   0.43829   30.83594  1.000 53.96584  ? 0   SER   A N     1 
ATOM   2    C  CA    . SER   A 1 1   ? 5.13253   1.06944   29.59286  1.000 50.60755  ? 0   SER   A CA    1 
ATOM   3    C  C     . SER   A 1 1   ? 6.03244   0.59419   28.43524  1.000 52.48409  ? 0   SER   A C     1 
ATOM   4    O  O     . SER   A 1 1   ? 6.97120   -0.18391  28.65113  1.000 50.92337  ? 0   SER   A O     1 
ATOM   5    C  CB    . SER   A 1 1   ? 5.13153   2.60455   29.73713  1.000 53.38257  ? 0   SER   A CB    1 
ATOM   6    O  OG    . SER   A 1 1   ? 6.43303   3.17778   29.81296  1.000 65.86505  ? 0   SER   A OG    1 
ATOM   7    N  N     . MET   A 1 2   ? 5.73340   1.03998   27.21627  1.000 42.35393  ? 1   MET   A N     1 
ATOM   8    C  CA    . MET   A 1 2   ? 6.44383   0.52404   26.05768  1.000 38.08230  ? 1   MET   A CA    1 
ATOM   9    C  C     . MET   A 1 2   ? 7.92468   0.87007   26.14712  1.000 36.74799  ? 1   MET   A C     1 
ATOM   10   O  O     . MET   A 1 2   ? 8.31770   1.88769   26.72098  1.000 35.65466  ? 1   MET   A O     1 
ATOM   11   C  CB    . MET   A 1 2   ? 5.84519   1.08830   24.77188  1.000 44.16274  ? 1   MET   A CB    1 
ATOM   12   C  CG    . MET   A 1 2   ? 6.20450   2.54316   24.51259  1.000 37.43548  ? 1   MET   A CG    1 
ATOM   13   S  SD    . MET   A 1 2   ? 5.35896   3.21340   23.07993  1.000 35.57890  ? 1   MET   A SD    1 
ATOM   14   C  CE    . MET   A 1 2   ? 3.66119   3.32541   23.70012  1.000 30.35317  ? 1   MET   A CE    1 
ATOM   15   N  N     . THR   A 1 3   ? 8.74915   0.00305   25.57847  1.000 30.94999  ? 2   THR   A N     1 
ATOM   16   C  CA    . THR   A 1 3   ? 10.18922  0.20413   25.63470  1.000 33.58509  ? 2   THR   A CA    1 
ATOM   17   C  C     . THR   A 1 3   ? 10.58959  1.36027   24.72653  1.000 28.13117  ? 2   THR   A C     1 
ATOM   18   O  O     . THR   A 1 3   ? 10.08738  1.49364   23.61704  1.000 29.30374  ? 2   THR   A O     1 
ATOM   19   C  CB    . THR   A 1 3   ? 10.90462  -1.08075  25.22536  1.000 36.18606  ? 2   THR   A CB    1 
ATOM   20   O  OG1   . THR   A 1 3   ? 10.47712  -2.14380  26.09057  1.000 39.01958  ? 2   THR   A OG1   1 
ATOM   21   C  CG2   . THR   A 1 3   ? 12.41665  -0.91959  25.32559  1.000 34.72633  ? 2   THR   A CG2   1 
ATOM   22   N  N     . GLU   A 1 4   ? 11.46055  2.22574   25.21352  1.000 37.76345  ? 3   GLU   A N     1 
ATOM   23   C  CA    . GLU   A 1 4   ? 11.98086  3.30129   24.38321  1.000 33.48135  ? 3   GLU   A CA    1 
ATOM   24   C  C     . GLU   A 1 4   ? 13.33912  2.89304   23.83272  1.000 34.55586  ? 3   GLU   A C     1 
ATOM   25   O  O     . GLU   A 1 4   ? 14.12239  2.22703   24.51840  1.000 30.22820  ? 3   GLU   A O     1 
ATOM   26   C  CB    . GLU   A 1 4   ? 12.08325  4.59748   25.17772  1.000 36.46383  ? 3   GLU   A CB    1 
ATOM   27   C  CG    . GLU   A 1 4   ? 10.77764  4.98418   25.85462  1.000 39.87356  ? 3   GLU   A CG    1 
ATOM   28   C  CD    . GLU   A 1 4   ? 10.92605  6.20898   26.73865  1.000 51.88342  ? 3   GLU   A CD    1 
ATOM   29   O  OE1   . GLU   A 1 4   ? 11.99297  6.86317   26.67072  1.000 55.78504  ? 3   GLU   A OE1   1 
ATOM   30   O  OE2   . GLU   A 1 4   ? 9.98470   6.51026   27.51114  1.000 53.26084  ? 3   GLU   A OE2   1 
ATOM   31   N  N     . TYR   A 1 5   ? 13.60808  3.27510   22.58458  1.000 35.92273  ? 4   TYR   A N     1 
ATOM   32   C  CA    . TYR   A 1 5   ? 14.87291  2.96878   21.92270  1.000 29.14160  ? 4   TYR   A CA    1 
ATOM   33   C  C     . TYR   A 1 5   ? 15.56066  4.27114   21.52890  1.000 31.33914  ? 4   TYR   A C     1 
ATOM   34   O  O     . TYR   A 1 5   ? 14.94535  5.13460   20.90019  1.000 28.72631  ? 4   TYR   A O     1 
ATOM   35   C  CB    . TYR   A 1 5   ? 14.64113  2.06270   20.69798  1.000 29.39567  ? 4   TYR   A CB    1 
ATOM   36   C  CG    . TYR   A 1 5   ? 14.13476  0.69018   21.09902  1.000 29.21064  ? 4   TYR   A CG    1 
ATOM   37   C  CD1   . TYR   A 1 5   ? 14.99984  -0.28718  21.54583  1.000 33.78515  ? 4   TYR   A CD1   1 
ATOM   38   C  CD2   . TYR   A 1 5   ? 12.78175  0.39496   21.08412  1.000 32.85111  ? 4   TYR   A CD2   1 
ATOM   39   C  CE1   . TYR   A 1 5   ? 14.53654  -1.53827  21.93815  1.000 37.09578  ? 4   TYR   A CE1   1 
ATOM   40   C  CE2   . TYR   A 1 5   ? 12.31520  -0.85057  21.46647  1.000 36.29393  ? 4   TYR   A CE2   1 
ATOM   41   C  CZ    . TYR   A 1 5   ? 13.19713  -1.81108  21.89680  1.000 38.71298  ? 4   TYR   A CZ    1 
ATOM   42   O  OH    . TYR   A 1 5   ? 12.72135  -3.04940  22.29273  1.000 38.70016  ? 4   TYR   A OH    1 
ATOM   43   N  N     . LYS   A 1 6   ? 16.83023  4.42269   21.90814  1.000 26.60882  ? 5   LYS   A N     1 
ATOM   44   C  CA    . LYS   A 1 6   ? 17.56640  5.65014   21.61860  1.000 24.28022  ? 5   LYS   A CA    1 
ATOM   45   C  C     . LYS   A 1 6   ? 18.35365  5.42971   20.33250  1.000 27.17672  ? 5   LYS   A C     1 
ATOM   46   O  O     . LYS   A 1 6   ? 19.41708  4.80613   20.34058  1.000 25.59033  ? 5   LYS   A O     1 
ATOM   47   C  CB    . LYS   A 1 6   ? 18.47879  6.02440   22.78671  1.000 26.28374  ? 5   LYS   A CB    1 
ATOM   48   C  CG    . LYS   A 1 6   ? 17.75671  6.49587   24.05657  1.000 31.52152  ? 5   LYS   A CG    1 
ATOM   49   C  CD    . LYS   A 1 6   ? 18.78168  6.85491   25.11608  1.000 32.92711  ? 5   LYS   A CD    1 
ATOM   50   C  CE    . LYS   A 1 6   ? 18.14899  7.32015   26.41526  1.000 43.32454  ? 5   LYS   A CE    1 
ATOM   51   N  NZ    . LYS   A 1 6   ? 19.19670  7.69202   27.42958  1.000 57.40441  ? 5   LYS   A NZ    1 
ATOM   52   N  N     . LEU   A 1 7   ? 17.81747  5.92403   19.21865  1.000 21.17772  ? 6   LEU   A N     1 
ATOM   53   C  CA    . LEU   A 1 7   ? 18.42442  5.80228   17.90469  1.000 22.64420  ? 6   LEU   A CA    1 
ATOM   54   C  C     . LEU   A 1 7   ? 19.13653  7.09927   17.55233  1.000 23.64766  ? 6   LEU   A C     1 
ATOM   55   O  O     . LEU   A 1 7   ? 18.63247  8.19060   17.84615  1.000 24.67986  ? 6   LEU   A O     1 
ATOM   56   C  CB    . LEU   A 1 7   ? 17.36250  5.50113   16.83077  1.000 21.89447  ? 6   LEU   A CB    1 
ATOM   57   C  CG    . LEU   A 1 7   ? 16.29911  4.42498   17.10750  1.000 26.78623  ? 6   LEU   A CG    1 
ATOM   58   C  CD1   . LEU   A 1 7   ? 15.41539  4.20581   15.86279  1.000 23.57502  ? 6   LEU   A CD1   1 
ATOM   59   C  CD2   . LEU   A 1 7   ? 16.93206  3.12030   17.55098  1.000 27.29094  ? 6   LEU   A CD2   1 
ATOM   60   N  N     . VAL   A 1 8   ? 20.30800  6.98525   16.92830  1.000 18.11270  ? 7   VAL   A N     1 
ATOM   61   C  CA    . VAL   A 1 8   ? 21.09646  8.14351   16.52096  1.000 19.29027  ? 7   VAL   A CA    1 
ATOM   62   C  C     . VAL   A 1 8   ? 21.41766  7.99942   15.03952  1.000 19.03773  ? 7   VAL   A C     1 
ATOM   63   O  O     . VAL   A 1 8   ? 21.89176  6.94652   14.60626  1.000 20.28418  ? 7   VAL   A O     1 
ATOM   64   C  CB    . VAL   A 1 8   ? 22.38783  8.27162   17.36248  1.000 22.23569  ? 7   VAL   A CB    1 
ATOM   65   C  CG1   . VAL   A 1 8   ? 23.13104  9.51628   16.97077  1.000 18.83289  ? 7   VAL   A CG1   1 
ATOM   66   C  CG2   . VAL   A 1 8   ? 22.03472  8.30657   18.83065  1.000 20.73614  ? 7   VAL   A CG2   1 
ATOM   67   N  N     . VAL   A 1 9   ? 21.13123  9.03682   14.26185  1.000 18.79255  ? 8   VAL   A N     1 
ATOM   68   C  CA    . VAL   A 1 9   ? 21.35594  9.02139   12.82062  1.000 19.73624  ? 8   VAL   A CA    1 
ATOM   69   C  C     . VAL   A 1 9   ? 22.63763  9.79657   12.53838  1.000 19.24496  ? 8   VAL   A C     1 
ATOM   70   O  O     . VAL   A 1 9   ? 22.71080  10.99448  12.82990  1.000 20.15664  ? 8   VAL   A O     1 
ATOM   71   C  CB    . VAL   A 1 9   ? 20.16107  9.62483   12.07023  1.000 17.31967  ? 8   VAL   A CB    1 
ATOM   72   C  CG1   . VAL   A 1 9   ? 20.37862  9.48649   10.55225  1.000 21.83469  ? 8   VAL   A CG1   1 
ATOM   73   C  CG2   . VAL   A 1 9   ? 18.88539  8.91689   12.53154  1.000 19.66551  ? 8   VAL   A CG2   1 
ATOM   74   N  N     . VAL   A 1 10  ? 23.64417  9.12345   11.97002  1.000 19.88362  ? 9   VAL   A N     1 
ATOM   75   C  CA    . VAL   A 1 10  ? 24.95510  9.72782   11.73049  1.000 19.86190  ? 9   VAL   A CA    1 
ATOM   76   C  C     . VAL   A 1 10  ? 25.37209  9.52297   10.27569  1.000 22.65066  ? 9   VAL   A C     1 
ATOM   77   O  O     . VAL   A 1 10  ? 24.88971  8.62748   9.57819   1.000 20.91058  ? 9   VAL   A O     1 
ATOM   78   C  CB    . VAL   A 1 10  ? 26.05577  9.16720   12.66852  1.000 21.14588  ? 9   VAL   A CB    1 
ATOM   79   C  CG1   . VAL   A 1 10  ? 25.68757  9.38633   14.14648  1.000 21.21779  ? 9   VAL   A CG1   1 
ATOM   80   C  CG2   . VAL   A 1 10  ? 26.30127  7.68325   12.37903  1.000 22.30440  ? 9   VAL   A CG2   1 
ATOM   81   N  N     . GLY   A 1 11  ? 26.31185  10.34335  9.83712   1.000 21.90578  ? 10  GLY   A N     1 
ATOM   82   C  CA    . GLY   A 1 11  ? 26.83752  10.23911  8.48789   1.000 23.96072  ? 10  GLY   A CA    1 
ATOM   83   C  C     . GLY   A 1 11  ? 27.26043  11.59332  7.96431   1.000 23.83328  ? 10  GLY   A C     1 
ATOM   84   O  O     . GLY   A 1 11  ? 26.96861  12.63468  8.54142   1.000 22.39821  ? 10  GLY   A O     1 
ATOM   85   N  N     . ALA   A 1 12  ? 27.94494  11.56358  6.82205   1.000 25.20554  ? 11  ALA   A N     1 
ATOM   86   C  CA    . ALA   A 1 12  ? 28.48457  12.78531  6.24854   1.000 28.16597  ? 11  ALA   A CA    1 
ATOM   87   C  C     . ALA   A 1 12  ? 27.36965  13.76657  5.90222   1.000 34.24669  ? 11  ALA   A C     1 
ATOM   88   O  O     . ALA   A 1 12  ? 26.19200  13.40285  5.78233   1.000 29.22048  ? 11  ALA   A O     1 
ATOM   89   C  CB    . ALA   A 1 12  ? 29.31030  12.46913  4.99850   1.000 33.37961  ? 11  ALA   A CB    1 
ATOM   90   N  N     . GLY   A 1 13  ? 27.74814  15.02904  5.74790   1.000 26.33379  ? 12  GLY   A N     1 
ATOM   91   C  CA    . GLY   A 1 13  ? 26.76629  16.03148  5.37506   1.000 27.12178  ? 12  GLY   A CA    1 
ATOM   92   C  C     . GLY   A 1 13  ? 26.13829  15.71134  4.02475   1.000 32.21372  ? 12  GLY   A C     1 
ATOM   93   O  O     . GLY   A 1 13  ? 26.78497  15.15518  3.13701   1.000 31.84921  ? 12  GLY   A O     1 
ATOM   94   N  N     A ASP   A 1 14  ? 24.85155  16.05049  3.89847   0.500 29.79894  ? 13  ASP   A N     1 
ATOM   95   N  N     B ASP   A 1 14  ? 24.85107  16.04816  3.89330   0.500 29.74044  ? 13  ASP   A N     1 
ATOM   96   C  CA    A ASP   A 1 14  ? 24.05672  15.98908  2.66458   0.500 29.96946  ? 13  ASP   A CA    1 
ATOM   97   C  CA    B ASP   A 1 14  ? 24.08917  15.98281  2.64319   0.500 29.97597  ? 13  ASP   A CA    1 
ATOM   98   C  C     A ASP   A 1 14  ? 23.67622  14.57377  2.24427   0.500 29.35039  ? 13  ASP   A C     1 
ATOM   99   C  C     B ASP   A 1 14  ? 23.74213  14.55833  2.21083   0.500 29.36933  ? 13  ASP   A C     1 
ATOM   100  O  O     A ASP   A 1 14  ? 23.15322  14.39755  1.12601   0.500 31.13581  ? 13  ASP   A O     1 
ATOM   101  O  O     B ASP   A 1 14  ? 23.30780  14.35571  1.06560   0.500 31.15145  ? 13  ASP   A O     1 
ATOM   102  C  CB    A ASP   A 1 14  ? 24.78030  16.67495  1.49963   0.500 31.33817  ? 13  ASP   A CB    1 
ATOM   103  C  CB    B ASP   A 1 14  ? 24.83616  16.69961  1.50616   0.500 31.31096  ? 13  ASP   A CB    1 
ATOM   104  C  CG    A ASP   A 1 14  ? 25.16677  18.10631  1.82056   0.500 31.73752  ? 13  ASP   A CG    1 
ATOM   105  C  CG    B ASP   A 1 14  ? 23.92012  17.14147  0.37634   0.500 34.11004  ? 13  ASP   A CG    1 
ATOM   106  O  OD1   A ASP   A 1 14  ? 24.27552  18.89149  2.19916   0.500 36.20052  ? 13  ASP   A OD1   1 
ATOM   107  O  OD1   B ASP   A 1 14  ? 23.15441  18.11348  0.55975   0.500 36.93418  ? 13  ASP   A OD1   1 
ATOM   108  O  OD2   A ASP   A 1 14  ? 26.36422  18.44219  1.70856   0.500 36.51000  ? 13  ASP   A OD2   1 
ATOM   109  O  OD2   B ASP   A 1 14  ? 23.97856  16.52168  -0.70392  0.500 41.18273  ? 13  ASP   A OD2   1 
ATOM   110  N  N     . VAL   A 1 15  ? 23.89875  13.55853  3.08197   1.000 26.27931  ? 14  VAL   A N     1 
ATOM   111  C  CA    . VAL   A 1 15  ? 23.55097  12.19934  2.67831   1.000 26.83971  ? 14  VAL   A CA    1 
ATOM   112  C  C     . VAL   A 1 15  ? 22.06270  11.90928  2.83922   1.000 25.92473  ? 14  VAL   A C     1 
ATOM   113  O  O     . VAL   A 1 15  ? 21.57115  10.92269  2.27704   1.000 26.92583  ? 14  VAL   A O     1 
ATOM   114  C  CB    . VAL   A 1 15  ? 24.34577  11.12118  3.43396   1.000 27.82614  ? 14  VAL   A CB    1 
ATOM   115  C  CG1   . VAL   A 1 15  ? 25.82977  11.23139  3.13872   1.000 28.26462  ? 14  VAL   A CG1   1 
ATOM   116  C  CG2   . VAL   A 1 15  ? 24.08088  11.19364  4.95981   1.000 23.27454  ? 14  VAL   A CG2   1 
ATOM   117  N  N     . GLY   A 1 16  ? 21.33406  12.72120  3.58490   1.000 23.46546  ? 15  GLY   A N     1 
ATOM   118  C  CA    . GLY   A 1 16  ? 19.91620  12.51290  3.77104   1.000 21.35766  ? 15  GLY   A CA    1 
ATOM   119  C  C     . GLY   A 1 16  ? 19.48051  12.07320  5.17268   1.000 24.32463  ? 15  GLY   A C     1 
ATOM   120  O  O     . GLY   A 1 16  ? 18.39883  11.49103  5.30802   1.000 21.20940  ? 15  GLY   A O     1 
ATOM   121  N  N     . LYS   A 1 17  ? 20.28677  12.33025  6.20649   1.000 23.65779  ? 16  LYS   A N     1 
ATOM   122  C  CA    . LYS   A 1 17  ? 19.89513  11.94152  7.55277   1.000 20.20477  ? 16  LYS   A CA    1 
ATOM   123  C  C     . LYS   A 1 17  ? 18.58036  12.59486  7.94839   1.000 20.26059  ? 16  LYS   A C     1 
ATOM   124  O  O     . LYS   A 1 17  ? 17.68808  11.93405  8.48184   1.000 20.17201  ? 16  LYS   A O     1 
ATOM   125  C  CB    . LYS   A 1 17  ? 21.00401  12.31833  8.55100   1.000 19.23710  ? 16  LYS   A CB    1 
ATOM   126  C  CG    . LYS   A 1 17  ? 22.34258  11.69180  8.24570   1.000 21.81505  ? 16  LYS   A CG    1 
ATOM   127  C  CD    . LYS   A 1 17  ? 23.36537  12.09144  9.31969   1.000 20.87706  ? 16  LYS   A CD    1 
ATOM   128  C  CE    . LYS   A 1 17  ? 23.71472  13.56514  9.27768   1.000 22.64403  ? 16  LYS   A CE    1 
ATOM   129  N  NZ    . LYS   A 1 17  ? 24.35888  13.98483  7.98502   1.000 25.98844  ? 16  LYS   A NZ    1 
ATOM   130  N  N     . SER   A 1 18  ? 18.44917  13.90174  7.70004   1.000 19.73018  ? 17  SER   A N     1 
ATOM   131  C  CA    . SER   A 1 18  ? 17.25023  14.62472  8.10435   1.000 21.68831  ? 17  SER   A CA    1 
ATOM   132  C  C     . SER   A 1 18  ? 16.05848  14.23692  7.24163   1.000 21.59035  ? 17  SER   A C     1 
ATOM   133  O  O     . SER   A 1 18  ? 14.93902  14.08068  7.75230   1.000 21.00955  ? 17  SER   A O     1 
ATOM   134  C  CB    . SER   A 1 18  ? 17.48963  16.13269  8.02492   1.000 18.98523  ? 17  SER   A CB    1 
ATOM   135  O  OG    . SER   A 1 18  ? 18.46675  16.54887  8.98066   1.000 21.31506  ? 17  SER   A OG    1 
ATOM   136  N  N     . ALA   A 1 19  ? 16.27769  14.07931  5.93698   1.000 21.55059  ? 18  ALA   A N     1 
ATOM   137  C  CA    . ALA   A 1 19  ? 15.18254  13.68910  5.05711   1.000 23.92630  ? 18  ALA   A CA    1 
ATOM   138  C  C     . ALA   A 1 19  ? 14.62171  12.33546  5.46391   1.000 22.75175  ? 18  ALA   A C     1 
ATOM   139  O  O     . ALA   A 1 19  ? 13.39841  12.14890  5.48469   1.000 22.37896  ? 18  ALA   A O     1 
ATOM   140  C  CB    . ALA   A 1 19  ? 15.66254  13.67789  3.60022   1.000 18.39641  ? 18  ALA   A CB    1 
ATOM   141  N  N     . LEU   A 1 20  ? 15.49278  11.39372  5.84198   1.000 20.95055  ? 19  LEU   A N     1 
ATOM   142  C  CA    . LEU   A 1 20  ? 15.01819  10.09186  6.30997   1.000 19.00169  ? 19  LEU   A CA    1 
ATOM   143  C  C     . LEU   A 1 20  ? 14.21341  10.22438  7.59365   1.000 18.87801  ? 19  LEU   A C     1 
ATOM   144  O  O     . LEU   A 1 20  ? 13.12807  9.65275   7.72157   1.000 20.56812  ? 19  LEU   A O     1 
ATOM   145  C  CB    . LEU   A 1 20  ? 16.19056  9.13012   6.51200   1.000 21.15964  ? 19  LEU   A CB    1 
ATOM   146  C  CG    . LEU   A 1 20  ? 16.81782  8.56287   5.23693   1.000 22.67509  ? 19  LEU   A CG    1 
ATOM   147  C  CD1   . LEU   A 1 20  ? 18.12519  7.83175   5.53505   1.000 22.60033  ? 19  LEU   A CD1   1 
ATOM   148  C  CD2   . LEU   A 1 20  ? 15.86135  7.63829   4.50956   1.000 22.93881  ? 19  LEU   A CD2   1 
ATOM   149  N  N     . THR   A 1 21  ? 14.73743  10.96750  8.56198   1.000 20.50440  ? 20  THR   A N     1 
ATOM   150  C  CA    . THR   A 1 21  ? 14.04321  11.11709  9.83085   1.000 20.38532  ? 20  THR   A CA    1 
ATOM   151  C  C     . THR   A 1 21  ? 12.70538  11.84000  9.65381   1.000 19.92222  ? 20  THR   A C     1 
ATOM   152  O  O     . THR   A 1 21  ? 11.70415  11.44963  10.25644  1.000 23.18369  ? 20  THR   A O     1 
ATOM   153  C  CB    . THR   A 1 21  ? 14.95515  11.85741  10.80502  1.000 24.09497  ? 20  THR   A CB    1 
ATOM   154  O  OG1   . THR   A 1 21  ? 16.17725  11.11663  10.97731  1.000 22.51441  ? 20  THR   A OG1   1 
ATOM   155  C  CG2   . THR   A 1 21  ? 14.29615  12.03700  12.15647  1.000 21.89311  ? 20  THR   A CG2   1 
ATOM   156  N  N     . ILE   A 1 22  ? 12.67605  12.90831  8.84880   1.000 20.97589  ? 21  ILE   A N     1 
ATOM   157  C  CA    . ILE   A 1 22  ? 11.42400  13.64021  8.65203   1.000 22.33385  ? 21  ILE   A CA    1 
ATOM   158  C  C     . ILE   A 1 22  ? 10.43608  12.80934  7.83770   1.000 25.94094  ? 21  ILE   A C     1 
ATOM   159  O  O     . ILE   A 1 22  ? 9.21710   12.92358  8.03055   1.000 21.00271  ? 21  ILE   A O     1 
ATOM   160  C  CB    . ILE   A 1 22  ? 11.70382  15.01467  8.01801   1.000 25.96978  ? 21  ILE   A CB    1 
ATOM   161  C  CG1   . ILE   A 1 22  ? 12.40672  15.94091  9.01381   1.000 31.21528  ? 21  ILE   A CG1   1 
ATOM   162  C  CG2   . ILE   A 1 22  ? 10.41756  15.68171  7.51815   1.000 28.73025  ? 21  ILE   A CG2   1 
ATOM   163  C  CD1   . ILE   A 1 22  ? 12.84723  17.24310  8.40192   1.000 33.99441  ? 21  ILE   A CD1   1 
ATOM   164  N  N     . GLN   A 1 23  ? 10.91800  11.93987  6.94316   1.000 22.04954  ? 22  GLN   A N     1 
ATOM   165  C  CA    . GLN   A 1 23  ? 9.98623   11.01177  6.29889   1.000 27.20922  ? 22  GLN   A CA    1 
ATOM   166  C  C     . GLN   A 1 23  ? 9.35261   10.07557  7.31595   1.000 29.13356  ? 22  GLN   A C     1 
ATOM   167  O  O     . GLN   A 1 23  ? 8.14144   9.82475   7.28750   1.000 24.60008  ? 22  GLN   A O     1 
ATOM   168  C  CB    . GLN   A 1 23  ? 10.68342  10.19823  5.22261   1.000 25.65069  ? 22  GLN   A CB    1 
ATOM   169  C  CG    . GLN   A 1 23  ? 10.54326  10.79993  3.86377   1.000 28.53604  ? 22  GLN   A CG    1 
ATOM   170  C  CD    . GLN   A 1 23  ? 9.12527   10.72534  3.27042   1.000 29.04443  ? 22  GLN   A CD    1 
ATOM   171  O  OE1   . GLN   A 1 23  ? 8.13801   10.42740  3.94671   1.000 30.20120  ? 22  GLN   A OE1   1 
ATOM   172  N  NE2   . GLN   A 1 23  ? 9.04431   10.99093  1.98721   1.000 26.31515  ? 22  GLN   A NE2   1 
ATOM   173  N  N     . LEU   A 1 24  ? 10.16939  9.51853   8.20315   1.000 22.97975  ? 23  LEU   A N     1 
ATOM   174  C  CA    . LEU   A 1 24  ? 9.65032   8.62323   9.22554   1.000 24.95359  ? 23  LEU   A CA    1 
ATOM   175  C  C     . LEU   A 1 24  ? 8.63936   9.33285   10.12629  1.000 27.63958  ? 23  LEU   A C     1 
ATOM   176  O  O     . LEU   A 1 24  ? 7.54836   8.80835   10.38374  1.000 30.49167  ? 23  LEU   A O     1 
ATOM   177  C  CB    . LEU   A 1 24  ? 10.81059  8.06951   10.05165  1.000 22.90903  ? 23  LEU   A CB    1 
ATOM   178  C  CG    . LEU   A 1 24  ? 10.34728  7.12487   11.14690  1.000 26.80372  ? 23  LEU   A CG    1 
ATOM   179  C  CD1   . LEU   A 1 24  ? 10.13997  5.72210   10.61289  1.000 28.99632  ? 23  LEU   A CD1   1 
ATOM   180  C  CD2   . LEU   A 1 24  ? 11.35660  7.13024   12.26146  1.000 27.23594  ? 23  LEU   A CD2   1 
ATOM   181  N  N     . ILE   A 1 25  ? 8.97450   10.54376  10.58582  1.000 26.22639  ? 24  ILE   A N     1 
ATOM   182  C  CA    . ILE   A 1 25  ? 8.16264   11.23424  11.58642  1.000 29.06839  ? 24  ILE   A CA    1 
ATOM   183  C  C     . ILE   A 1 25  ? 6.95454   11.89354  10.93501  1.000 30.68834  ? 24  ILE   A C     1 
ATOM   184  O  O     . ILE   A 1 25  ? 5.83098   11.79464  11.43926  1.000 33.08798  ? 24  ILE   A O     1 
ATOM   185  C  CB    . ILE   A 1 25  ? 8.99533   12.28301  12.35891  1.000 29.30859  ? 24  ILE   A CB    1 
ATOM   186  C  CG1   . ILE   A 1 25  ? 10.20607  11.67650  13.08865  1.000 27.15047  ? 24  ILE   A CG1   1 
ATOM   187  C  CG2   . ILE   A 1 25  ? 8.10347   13.07675  13.31736  1.000 32.04484  ? 24  ILE   A CG2   1 
ATOM   188  C  CD1   . ILE   A 1 25  ? 9.90986   10.56961  14.00655  1.000 28.12008  ? 24  ILE   A CD1   1 
ATOM   189  N  N     . GLN   A 1 26  ? 7.16608   12.57646  9.81285   1.000 26.64130  ? 25  GLN   A N     1 
ATOM   190  C  CA    . GLN   A 1 26  ? 6.15348   13.45106  9.24137   1.000 35.56146  ? 25  GLN   A CA    1 
ATOM   191  C  C     . GLN   A 1 26  ? 5.58154   12.95407  7.91896   1.000 33.59100  ? 25  GLN   A C     1 
ATOM   192  O  O     . GLN   A 1 26  ? 4.59316   13.52392  7.44297   1.000 32.39979  ? 25  GLN   A O     1 
ATOM   193  C  CB    . GLN   A 1 26  ? 6.73979   14.86170  9.07721   1.000 35.11127  ? 25  GLN   A CB    1 
ATOM   194  C  CG    . GLN   A 1 26  ? 6.92586   15.53803  10.42326  1.000 38.30736  ? 25  GLN   A CG    1 
ATOM   195  C  CD    . GLN   A 1 26  ? 7.80710   16.76367  10.38651  1.000 43.33897  ? 25  GLN   A CD    1 
ATOM   196  O  OE1   . GLN   A 1 26  ? 8.17971   17.25290  9.32251   1.000 46.72991  ? 25  GLN   A OE1   1 
ATOM   197  N  NE2   . GLN   A 1 26  ? 8.15506   17.26713  11.56907  1.000 55.65530  ? 25  GLN   A NE2   1 
ATOM   198  N  N     . ASN   A 1 27  ? 6.15571   11.90130  7.33433   1.000 31.19453  ? 26  ASN   A N     1 
ATOM   199  C  CA    . ASN   A 1 27  ? 5.66160   11.27365  6.09950   1.000 27.61733  ? 26  ASN   A CA    1 
ATOM   200  C  C     . ASN   A 1 27  ? 5.64820   12.23506  4.90438   1.000 38.28579  ? 26  ASN   A C     1 
ATOM   201  O  O     . ASN   A 1 27  ? 4.74765   12.18974  4.06140   1.000 30.71118  ? 26  ASN   A O     1 
ATOM   202  C  CB    . ASN   A 1 27  ? 4.28039   10.64180  6.30112   1.000 26.08799  ? 26  ASN   A CB    1 
ATOM   203  C  CG    . ASN   A 1 27  ? 4.11088   9.36949   5.49143   1.000 37.20212  ? 26  ASN   A CG    1 
ATOM   204  O  OD1   . ASN   A 1 27  ? 4.24520   8.26531   6.02352   1.000 33.29754  ? 26  ASN   A OD1   1 
ATOM   205  N  ND2   . ASN   A 1 27  ? 3.84566   9.51671   4.18446   1.000 30.81938  ? 26  ASN   A ND2   1 
ATOM   206  N  N     . HIS   A 1 28  ? 6.65741   13.09979  4.80632   1.000 31.22539  ? 27  HIS   A N     1 
ATOM   207  C  CA    . HIS   A 1 28  ? 6.81388   13.93246  3.61794   1.000 37.19428  ? 27  HIS   A CA    1 
ATOM   208  C  C     . HIS   A 1 28  ? 8.29032   14.24144  3.38935   1.000 36.62789  ? 27  HIS   A C     1 
ATOM   209  O  O     . HIS   A 1 28  ? 9.13071   14.04246  4.26858   1.000 30.47249  ? 27  HIS   A O     1 
ATOM   210  C  CB    . HIS   A 1 28  ? 5.99777   15.21802  3.73126   1.000 36.45982  ? 27  HIS   A CB    1 
ATOM   211  C  CG    . HIS   A 1 28  ? 6.65400   16.27846  4.55208   1.000 39.76302  ? 27  HIS   A CG    1 
ATOM   212  N  ND1   . HIS   A 1 28  ? 7.38656   17.30177  3.99037   1.000 53.60730  ? 27  HIS   A ND1   1 
ATOM   213  C  CD2   . HIS   A 1 28  ? 6.68685   16.47979  5.88901   1.000 43.96728  ? 27  HIS   A CD2   1 
ATOM   214  C  CE1   . HIS   A 1 28  ? 7.84610   18.08650  4.94847   1.000 49.24790  ? 27  HIS   A CE1   1 
ATOM   215  N  NE2   . HIS   A 1 28  ? 7.43678   17.60934  6.11030   1.000 52.61632  ? 27  HIS   A NE2   1 
ATOM   216  N  N     . PHE   A 1 29  ? 8.58949   14.73866  2.18758   1.000 36.49496  ? 28  PHE   A N     1 
ATOM   217  C  CA    . PHE   A 1 29  ? 9.94845   14.98257  1.70594   1.000 33.73973  ? 28  PHE   A CA    1 
ATOM   218  C  C     . PHE   A 1 29  ? 9.97669   16.31117  0.96968   1.000 38.96809  ? 28  PHE   A C     1 
ATOM   219  O  O     . PHE   A 1 29  ? 9.14947   16.54136  0.08109   1.000 47.79745  ? 28  PHE   A O     1 
ATOM   220  C  CB    . PHE   A 1 29  ? 10.41801  13.85614  0.76409   1.000 32.50011  ? 28  PHE   A CB    1 
ATOM   221  C  CG    . PHE   A 1 29  ? 11.70927  14.15807  0.02229   1.000 35.50143  ? 28  PHE   A CG    1 
ATOM   222  C  CD1   . PHE   A 1 29  ? 12.93635  13.88172  0.59907   1.000 31.10191  ? 28  PHE   A CD1   1 
ATOM   223  C  CD2   . PHE   A 1 29  ? 11.68982  14.68833  -1.26465  1.000 33.44496  ? 28  PHE   A CD2   1 
ATOM   224  C  CE1   . PHE   A 1 29  ? 14.12301  14.15339  -0.08235  1.000 28.76719  ? 28  PHE   A CE1   1 
ATOM   225  C  CE2   . PHE   A 1 29  ? 12.86123  14.96387  -1.94568  1.000 37.80976  ? 28  PHE   A CE2   1 
ATOM   226  C  CZ    . PHE   A 1 29  ? 14.08577  14.69027  -1.35980  1.000 35.60382  ? 28  PHE   A CZ    1 
ATOM   227  N  N     . VAL   A 1 30  ? 10.92870  17.17293  1.31763   1.000 46.20922  ? 29  VAL   A N     1 
ATOM   228  C  CA    . VAL   A 1 30  ? 11.17826  18.40498  0.57679   1.000 45.38221  ? 29  VAL   A CA    1 
ATOM   229  C  C     . VAL   A 1 30  ? 12.64680  18.43939  0.17347   1.000 46.71026  ? 29  VAL   A C     1 
ATOM   230  O  O     . VAL   A 1 30  ? 13.52435  18.01992  0.93759   1.000 41.17270  ? 29  VAL   A O     1 
ATOM   231  C  CB    . VAL   A 1 30  ? 10.80716  19.66355  1.39012   1.000 54.28807  ? 29  VAL   A CB    1 
ATOM   232  C  CG1   . VAL   A 1 30  ? 10.76899  20.89047  0.48074   1.000 55.31524  ? 29  VAL   A CG1   1 
ATOM   233  C  CG2   . VAL   A 1 30  ? 9.47308   19.47555  2.09447   1.000 52.85677  ? 29  VAL   A CG2   1 
ATOM   234  N  N     . ASP   A 1 31  ? 12.91327  18.93328  -1.03213  1.000 46.97906  ? 30  ASP   A N     1 
ATOM   235  C  CA    . ASP   A 1 31  ? 14.25891  18.88640  -1.59906  1.000 43.00400  ? 30  ASP   A CA    1 
ATOM   236  C  C     . ASP   A 1 31  ? 15.01282  20.18806  -1.35229  1.000 46.51667  ? 30  ASP   A C     1 
ATOM   237  O  O     . ASP   A 1 31  ? 15.59284  20.78403  -2.25923  1.000 57.72156  ? 30  ASP   A O     1 
ATOM   238  C  CB    . ASP   A 1 31  ? 14.18274  18.55776  -3.08635  1.000 48.57309  ? 30  ASP   A CB    1 
ATOM   239  C  CG    . ASP   A 1 31  ? 15.54734  18.27862  -3.70073  1.000 56.23116  ? 30  ASP   A CG    1 
ATOM   240  O  OD1   . ASP   A 1 31  ? 16.32823  17.49533  -3.11408  1.000 45.85961  ? 30  ASP   A OD1   1 
ATOM   241  O  OD2   . ASP   A 1 31  ? 15.83137  18.83965  -4.78078  1.000 61.98786  ? 30  ASP   A OD2   1 
ATOM   242  N  N     . GLU   A 1 32  ? 15.01856  20.63587  -0.10278  1.000 42.30554  ? 31  GLU   A N     1 
ATOM   243  C  CA    . GLU   A 1 32  ? 15.71284  21.85577  0.27094   1.000 41.56204  ? 31  GLU   A CA    1 
ATOM   244  C  C     . GLU   A 1 32  ? 16.91745  21.53742  1.14276   1.000 41.10156  ? 31  GLU   A C     1 
ATOM   245  O  O     . GLU   A 1 32  ? 16.98122  20.49771  1.80226   1.000 44.40038  ? 31  GLU   A O     1 
ATOM   246  C  CB    . GLU   A 1 32  ? 14.78671  22.82000  1.00791   1.000 43.71870  ? 31  GLU   A CB    1 
ATOM   247  C  CG    . GLU   A 1 32  ? 13.94169  23.67445  0.09195   1.000 54.14773  ? 31  GLU   A CG    1 
ATOM   248  C  CD    . GLU   A 1 32  ? 12.84833  24.39328  0.84546   1.000 61.27679  ? 31  GLU   A CD    1 
ATOM   249  O  OE1   . GLU   A 1 32  ? 12.58296  24.00296  2.00512   1.000 61.72242  ? 31  GLU   A OE1   1 
ATOM   250  O  OE2   . GLU   A 1 32  ? 12.25855  25.34342  0.28366   1.000 64.34712  ? 31  GLU   A OE2   1 
ATOM   251  N  N     . TYR   A 1 33  ? 17.86129  22.47185  1.14711   1.000 37.54473  ? 32  TYR   A N     1 
ATOM   252  C  CA    . TYR   A 1 33  ? 19.10682  22.35996  1.90505   1.000 44.52961  ? 32  TYR   A CA    1 
ATOM   253  C  C     . TYR   A 1 33  ? 18.91065  23.02061  3.26965   1.000 38.45786  ? 32  TYR   A C     1 
ATOM   254  O  O     . TYR   A 1 33  ? 18.86591  24.24808  3.37637   1.000 37.66822  ? 32  TYR   A O     1 
ATOM   255  C  CB    . TYR   A 1 33  ? 20.23779  23.00957  1.11622   1.000 44.04553  ? 32  TYR   A CB    1 
ATOM   256  C  CG    . TYR   A 1 33  ? 21.57814  23.02691  1.81431   1.000 46.34914  ? 32  TYR   A CG    1 
ATOM   257  C  CD1   . TYR   A 1 33  ? 22.39635  21.90050  1.81993   1.000 43.73304  ? 32  TYR   A CD1   1 
ATOM   258  C  CD2   . TYR   A 1 33  ? 22.03997  24.17732  2.44992   1.000 44.70421  ? 32  TYR   A CD2   1 
ATOM   259  C  CE1   . TYR   A 1 33  ? 23.63421  21.91567  2.45296   1.000 43.09115  ? 32  TYR   A CE1   1 
ATOM   260  C  CE2   . TYR   A 1 33  ? 23.27340  24.19746  3.09646   1.000 39.31659  ? 32  TYR   A CE2   1 
ATOM   261  C  CZ    . TYR   A 1 33  ? 24.06700  23.06498  3.09325   1.000 40.51160  ? 32  TYR   A CZ    1 
ATOM   262  O  OH    . TYR   A 1 33  ? 25.29856  23.08370  3.72469   1.000 41.81202  ? 32  TYR   A OH    1 
ATOM   263  N  N     . ASP   A 1 34  ? 18.78020  22.21065  4.31987   1.000 36.53112  ? 33  ASP   A N     1 
ATOM   264  C  CA    . ASP   A 1 34  ? 18.53748  22.70964  5.67718   1.000 34.44743  ? 33  ASP   A CA    1 
ATOM   265  C  C     . ASP   A 1 34  ? 19.50904  22.00969  6.61964   1.000 31.48593  ? 33  ASP   A C     1 
ATOM   266  O  O     . ASP   A 1 34  ? 19.12956  21.07194  7.33323   1.000 26.04428  ? 33  ASP   A O     1 
ATOM   267  C  CB    . ASP   A 1 34  ? 17.08667  22.48492  6.10961   1.000 33.50575  ? 33  ASP   A CB    1 
ATOM   268  C  CG    . ASP   A 1 34  ? 16.73811  23.20909  7.40873   1.000 40.04900  ? 33  ASP   A CG    1 
ATOM   269  O  OD1   . ASP   A 1 34  ? 17.56247  24.00972  7.91146   1.000 33.51259  ? 33  ASP   A OD1   1 
ATOM   270  O  OD2   . ASP   A 1 34  ? 15.62949  22.97241  7.94019   1.000 49.00222  ? 33  ASP   A OD2   1 
ATOM   271  N  N     . PRO   A 1 35  ? 20.77040  22.44221  6.64386   1.000 28.75516  ? 34  PRO   A N     1 
ATOM   272  C  CA    . PRO   A 1 35  ? 21.79477  21.70097  7.39620   1.000 25.44324  ? 34  PRO   A CA    1 
ATOM   273  C  C     . PRO   A 1 35  ? 21.51231  21.71660  8.89309   1.000 25.46500  ? 34  PRO   A C     1 
ATOM   274  O  O     . PRO   A 1 35  ? 21.14294  22.73915  9.47006   1.000 25.99906  ? 34  PRO   A O     1 
ATOM   275  C  CB    . PRO   A 1 35  ? 23.09861  22.43635  7.05138   1.000 29.65537  ? 34  PRO   A CB    1 
ATOM   276  C  CG    . PRO   A 1 35  ? 22.68434  23.78641  6.59543   1.000 28.46332  ? 34  PRO   A CG    1 
ATOM   277  C  CD    . PRO   A 1 35  ? 21.31142  23.64418  5.98568   1.000 34.82014  ? 34  PRO   A CD    1 
ATOM   278  N  N     . THR   A 1 36  ? 21.70518  20.56360  9.51663   1.000 21.95224  ? 35  THR   A N     1 
ATOM   279  C  CA    . THR   A 1 36  ? 21.26796  20.33366  10.88977  1.000 20.46865  ? 35  THR   A CA    1 
ATOM   280  C  C     . THR   A 1 36  ? 22.30543  20.81307  11.89665  1.000 23.13093  ? 35  THR   A C     1 
ATOM   281  O  O     . THR   A 1 36  ? 23.51022  20.63391  11.69468  1.000 20.64025  ? 35  THR   A O     1 
ATOM   282  C  CB    . THR   A 1 36  ? 21.01028  18.84109  11.08741  1.000 21.38107  ? 35  THR   A CB    1 
ATOM   283  O  OG1   . THR   A 1 36  ? 20.02390  18.40893  10.12837  1.000 21.62570  ? 35  THR   A OG1   1 
ATOM   284  C  CG2   . THR   A 1 36  ? 20.54891  18.51758  12.53351  1.000 22.18120  ? 35  THR   A CG2   1 
ATOM   285  N  N     . ILE   A 1 37  ? 21.82912  21.44324  12.96947  1.000 22.53161  ? 36  ILE   A N     1 
ATOM   286  C  CA    . ILE   A 1 37  ? 22.64542  21.60732  14.16834  1.000 22.72220  ? 36  ILE   A CA    1 
ATOM   287  C  C     . ILE   A 1 37  ? 22.47637  20.33860  15.00348  1.000 23.92336  ? 36  ILE   A C     1 
ATOM   288  O  O     . ILE   A 1 37  ? 23.41798  19.55207  15.18070  1.000 22.02915  ? 36  ILE   A O     1 
ATOM   289  C  CB    . ILE   A 1 37  ? 22.25658  22.85071  14.98620  1.000 23.29145  ? 36  ILE   A CB    1 
ATOM   290  C  CG1   . ILE   A 1 37  ? 22.25999  24.14102  14.15837  1.000 26.41026  ? 36  ILE   A CG1   1 
ATOM   291  C  CG2   . ILE   A 1 37  ? 23.12285  22.94564  16.23685  1.000 25.75117  ? 36  ILE   A CG2   1 
ATOM   292  C  CD1   . ILE   A 1 37  ? 23.60251  24.51111  13.55344  1.000 25.59358  ? 36  ILE   A CD1   1 
ATOM   293  N  N     . GLU   A 1 38  ? 21.27715  20.14243  15.53714  1.000 18.00812  ? 37  GLU   A N     1 
ATOM   294  C  CA    . GLU   A 1 38  ? 20.92339  18.89842  16.20288  1.000 19.64929  ? 37  GLU   A CA    1 
ATOM   295  C  C     . GLU   A 1 38  ? 19.42841  18.89506  16.44324  1.000 22.24214  ? 37  GLU   A C     1 
ATOM   296  O  O     . GLU   A 1 38  ? 18.88037  19.89985  16.90065  1.000 25.08796  ? 37  GLU   A O     1 
ATOM   297  C  CB    . GLU   A 1 38  ? 21.65329  18.74789  17.54676  1.000 26.87036  ? 37  GLU   A CB    1 
ATOM   298  C  CG    . GLU   A 1 38  ? 21.54003  17.35933  18.14313  1.000 30.28146  ? 37  GLU   A CG    1 
ATOM   299  C  CD    . GLU   A 1 38  ? 22.31999  17.22756  19.43903  1.000 40.19511  ? 37  GLU   A CD    1 
ATOM   300  O  OE1   . GLU   A 1 38  ? 21.77235  17.58096  20.49456  1.000 39.69707  ? 37  GLU   A OE1   1 
ATOM   301  O  OE2   . GLU   A 1 38  ? 23.48943  16.78848  19.39443  1.000 46.17660  ? 37  GLU   A OE2   1 
ATOM   302  N  N     . ASP   A 1 39  ? 18.75625  17.79109  16.14390  1.000 19.62851  ? 38  ASP   A N     1 
ATOM   303  C  CA    . ASP   A 1 39  ? 17.31814  17.72834  16.32473  1.000 20.93763  ? 38  ASP   A CA    1 
ATOM   304  C  C     . ASP   A 1 39  ? 16.95613  16.38742  16.93516  1.000 23.72350  ? 38  ASP   A C     1 
ATOM   305  O  O     . ASP   A 1 39  ? 17.62313  15.38015  16.68120  1.000 21.17078  ? 38  ASP   A O     1 
ATOM   306  C  CB    . ASP   A 1 39  ? 16.59348  17.93453  14.98341  1.000 21.25451  ? 38  ASP   A CB    1 
ATOM   307  C  CG    . ASP   A 1 39  ? 16.58876  19.39283  14.55087  1.000 26.09352  ? 38  ASP   A CG    1 
ATOM   308  O  OD1   . ASP   A 1 39  ? 15.91196  20.22565  15.19614  1.000 31.76031  ? 38  ASP   A OD1   1 
ATOM   309  O  OD2   . ASP   A 1 39  ? 17.29971  19.72042  13.60159  1.000 28.87101  ? 38  ASP   A OD2   1 
ATOM   310  N  N     . SER   A 1 40  ? 15.88630  16.38141  17.73734  1.000 20.36337  ? 39  SER   A N     1 
ATOM   311  C  CA    . SER   A 1 40  ? 15.42095  15.17467  18.40449  1.000 23.96200  ? 39  SER   A CA    1 
ATOM   312  C  C     . SER   A 1 40  ? 13.93063  15.01793  18.16361  1.000 23.56856  ? 39  SER   A C     1 
ATOM   313  O  O     . SER   A 1 40  ? 13.19450  16.01055  18.05838  1.000 25.09141  ? 39  SER   A O     1 
ATOM   314  C  CB    . SER   A 1 40  ? 15.68616  15.19913  19.94034  1.000 24.38161  ? 39  SER   A CB    1 
ATOM   315  O  OG    . SER   A 1 40  ? 17.06597  15.40003  20.21228  1.000 42.15734  ? 39  SER   A OG    1 
ATOM   316  N  N     . TYR   A 1 41  ? 13.49877  13.76660  18.05869  1.000 22.83051  ? 40  TYR   A N     1 
ATOM   317  C  CA    . TYR   A 1 41  ? 12.12404  13.44602  17.69006  1.000 21.26360  ? 40  TYR   A CA    1 
ATOM   318  C  C     . TYR   A 1 41  ? 11.69866  12.22296  18.47898  1.000 26.34194  ? 40  TYR   A C     1 
ATOM   319  O  O     . TYR   A 1 41  ? 12.52930  11.43817  18.93374  1.000 26.92686  ? 40  TYR   A O     1 
ATOM   320  C  CB    . TYR   A 1 41  ? 11.98045  13.16172  16.18937  1.000 22.76316  ? 40  TYR   A CB    1 
ATOM   321  C  CG    . TYR   A 1 41  ? 12.44806  14.28520  15.28821  1.000 24.23513  ? 40  TYR   A CG    1 
ATOM   322  C  CD1   . TYR   A 1 41  ? 11.58967  15.30996  14.93211  1.000 26.44843  ? 40  TYR   A CD1   1 
ATOM   323  C  CD2   . TYR   A 1 41  ? 13.75091  14.31977  14.79406  1.000 23.47236  ? 40  TYR   A CD2   1 
ATOM   324  C  CE1   . TYR   A 1 41  ? 12.00052  16.33606  14.10796  1.000 27.82850  ? 40  TYR   A CE1   1 
ATOM   325  C  CE2   . TYR   A 1 41  ? 14.17827  15.36023  13.96117  1.000 21.15084  ? 40  TYR   A CE2   1 
ATOM   326  C  CZ    . TYR   A 1 41  ? 13.29660  16.36098  13.62357  1.000 26.21224  ? 40  TYR   A CZ    1 
ATOM   327  O  OH    . TYR   A 1 41  ? 13.70159  17.39376  12.79472  1.000 28.77599  ? 40  TYR   A OH    1 
ATOM   328  N  N     A ARG   A 1 42  ? 10.38566  12.07217  18.66408  0.500 25.44009  ? 41  ARG   A N     1 
ATOM   329  N  N     B ARG   A 1 42  ? 10.38642  12.06151  18.62615  0.500 25.56468  ? 41  ARG   A N     1 
ATOM   330  C  CA    A ARG   A 1 42  ? 9.82859   10.86685  19.26338  0.500 25.11242  ? 41  ARG   A CA    1 
ATOM   331  C  CA    B ARG   A 1 42  ? 9.82278   10.86983  19.23732  0.500 25.15153  ? 41  ARG   A CA    1 
ATOM   332  C  C     A ARG   A 1 42  ? 8.70439   10.34702  18.38420  0.500 24.20772  ? 41  ARG   A C     1 
ATOM   333  C  C     B ARG   A 1 42  ? 8.70195   10.34477  18.36432  0.500 24.84450  ? 41  ARG   A C     1 
ATOM   334  O  O     A ARG   A 1 42  ? 7.94528   11.13275  17.81428  0.500 23.55233  ? 41  ARG   A O     1 
ATOM   335  O  O     B ARG   A 1 42  ? 7.94078   11.12365  17.78763  0.500 23.53765  ? 41  ARG   A O     1 
ATOM   336  C  CB    A ARG   A 1 42  ? 9.30911   11.11587  20.69161  0.500 25.48109  ? 41  ARG   A CB    1 
ATOM   337  C  CB    B ARG   A 1 42  ? 9.29962   11.15522  20.63646  0.500 25.35950  ? 41  ARG   A CB    1 
ATOM   338  C  CG    A ARG   A 1 42  ? 10.14078  10.41753  21.77437  0.500 28.50746  ? 41  ARG   A CG    1 
ATOM   339  C  CG    B ARG   A 1 42  ? 10.39036  11.57024  21.57615  0.500 25.49674  ? 41  ARG   A CG    1 
ATOM   340  C  CD    A ARG   A 1 42  ? 10.89668  11.41700  22.61759  0.500 31.03020  ? 41  ARG   A CD    1 
ATOM   341  C  CD    B ARG   A 1 42  ? 9.81312   12.05674  22.85860  0.500 26.71804  ? 41  ARG   A CD    1 
ATOM   342  N  NE    A ARG   A 1 42  ? 11.84616  10.79010  23.53318  0.500 26.23548  ? 41  ARG   A NE    1 
ATOM   343  N  NE    B ARG   A 1 42  ? 10.25153  11.23831  23.97920  0.500 35.18250  ? 41  ARG   A NE    1 
ATOM   344  C  CZ    A ARG   A 1 42  ? 11.51256  10.25225  24.69976  0.500 32.11393  ? 41  ARG   A CZ    1 
ATOM   345  C  CZ    B ARG   A 1 42  ? 9.45814   10.42297  24.65323  0.500 30.27147  ? 41  ARG   A CZ    1 
ATOM   346  N  NH1   A ARG   A 1 42  ? 10.25487  10.18291  25.09174  0.500 27.48972  ? 41  ARG   A NH1   1 
ATOM   347  N  NH1   B ARG   A 1 42  ? 8.16313   10.35327  24.39302  0.500 29.44045  ? 41  ARG   A NH1   1 
ATOM   348  N  NH2   A ARG   A 1 42  ? 12.46848  9.78281   25.49619  0.500 31.60421  ? 41  ARG   A NH2   1 
ATOM   349  N  NH2   B ARG   A 1 42  ? 9.97586   9.67049   25.61737  0.500 34.19731  ? 41  ARG   A NH2   1 
ATOM   350  N  N     . LYS   A 1 43  ? 8.60444   9.02230   18.27003  1.000 24.78257  ? 42  LYS   A N     1 
ATOM   351  C  CA    . LYS   A 1 43  ? 7.52942   8.40114   17.50710  1.000 24.58923  ? 42  LYS   A CA    1 
ATOM   352  C  C     . LYS   A 1 43  ? 7.25003   7.00568   18.03855  1.000 29.97918  ? 42  LYS   A C     1 
ATOM   353  O  O     . LYS   A 1 43  ? 8.18208   6.22435   18.24608  1.000 27.81291  ? 42  LYS   A O     1 
ATOM   354  C  CB    . LYS   A 1 43  ? 7.88363   8.31484   16.01569  1.000 23.99877  ? 42  LYS   A CB    1 
ATOM   355  C  CG    . LYS   A 1 43  ? 6.79703   7.66244   15.15880  1.000 23.01651  ? 42  LYS   A CG    1 
ATOM   356  C  CD    . LYS   A 1 43  ? 7.25870   7.45963   13.69136  1.000 26.21773  ? 42  LYS   A CD    1 
ATOM   357  C  CE    . LYS   A 1 43  ? 6.14403   6.86143   12.80812  1.000 30.16152  ? 42  LYS   A CE    1 
ATOM   358  N  NZ    . LYS   A 1 43  ? 5.00985   7.82205   12.64149  1.000 40.18349  ? 42  LYS   A NZ    1 
ATOM   359  N  N     . GLN   A 1 44  ? 5.97840   6.67080   18.23407  1.000 25.87864  ? 43  GLN   A N     1 
ATOM   360  C  CA    . GLN   A 1 44  ? 5.65478   5.30404   18.61716  1.000 25.74912  ? 43  GLN   A CA    1 
ATOM   361  C  C     . GLN   A 1 44  ? 5.29883   4.50091   17.37585  1.000 24.99132  ? 43  GLN   A C     1 
ATOM   362  O  O     . GLN   A 1 44  ? 4.68715   5.01557   16.43311  1.000 26.91984  ? 43  GLN   A O     1 
ATOM   363  C  CB    . GLN   A 1 44  ? 4.53032   5.24719   19.66837  1.000 25.93612  ? 43  GLN   A CB    1 
ATOM   364  C  CG    . GLN   A 1 44  ? 3.13064   5.52408   19.18317  1.000 32.23970  ? 43  GLN   A CG    1 
ATOM   365  C  CD    . GLN   A 1 44  ? 2.09194   5.16058   20.24348  1.000 32.17728  ? 43  GLN   A CD    1 
ATOM   366  O  OE1   . GLN   A 1 44  ? 1.85474   3.98220   20.51851  1.000 30.79791  ? 43  GLN   A OE1   1 
ATOM   367  N  NE2   . GLN   A 1 44  ? 1.50220   6.17670   20.86675  1.000 28.13166  ? 43  GLN   A NE2   1 
ATOM   368  N  N     . VAL   A 1 45  ? 5.72973   3.24283   17.37083  1.000 27.07777  ? 44  VAL   A N     1 
ATOM   369  C  CA    . VAL   A 1 45  ? 5.58019   2.33253   16.24412  1.000 29.99363  ? 44  VAL   A CA    1 
ATOM   370  C  C     . VAL   A 1 45  ? 5.31160   0.93106   16.77974  1.000 34.83106  ? 44  VAL   A C     1 
ATOM   371  O  O     . VAL   A 1 45  ? 5.41045   0.66916   17.98117  1.000 35.54427  ? 44  VAL   A O     1 
ATOM   372  C  CB    . VAL   A 1 45  ? 6.83655   2.31495   15.35299  1.000 32.55795  ? 44  VAL   A CB    1 
ATOM   373  C  CG1   . VAL   A 1 45  ? 7.06436   3.68470   14.72683  1.000 25.49664  ? 44  VAL   A CG1   1 
ATOM   374  C  CG2   . VAL   A 1 45  ? 8.02523   1.89224   16.18113  1.000 31.23016  ? 44  VAL   A CG2   1 
ATOM   375  N  N     . VAL   A 1 46  ? 4.96085   0.02557   15.86702  1.000 32.36873  ? 45  VAL   A N     1 
ATOM   376  C  CA    . VAL   A 1 46  ? 4.84504   -1.39817  16.16320  1.000 40.07657  ? 45  VAL   A CA    1 
ATOM   377  C  C     . VAL   A 1 46  ? 5.90301   -2.13191  15.35441  1.000 30.60583  ? 45  VAL   A C     1 
ATOM   378  O  O     . VAL   A 1 46  ? 6.01885   -1.92381  14.14324  1.000 36.06897  ? 45  VAL   A O     1 
ATOM   379  C  CB    . VAL   A 1 46  ? 3.43365   -1.93328  15.85364  1.000 34.88095  ? 45  VAL   A CB    1 
ATOM   380  C  CG1   . VAL   A 1 46  ? 3.35104   -3.42541  16.15204  1.000 38.91259  ? 45  VAL   A CG1   1 
ATOM   381  C  CG2   . VAL   A 1 46  ? 2.40188   -1.16505  16.67280  1.000 36.51340  ? 45  VAL   A CG2   1 
ATOM   382  N  N     . ILE   A 1 47  ? 6.70839   -2.95068  16.02658  1.000 37.22084  ? 46  ILE   A N     1 
ATOM   383  C  CA    . ILE   A 1 47  ? 7.79184   -3.66791  15.36979  1.000 38.23096  ? 46  ILE   A CA    1 
ATOM   384  C  C     . ILE   A 1 47  ? 7.72507   -5.12496  15.79435  1.000 42.31889  ? 46  ILE   A C     1 
ATOM   385  O  O     . ILE   A 1 47  ? 7.81306   -5.42945  16.99098  1.000 46.73695  ? 46  ILE   A O     1 
ATOM   386  C  CB    . ILE   A 1 47  ? 9.16780   -3.06201  15.69440  1.000 38.65137  ? 46  ILE   A CB    1 
ATOM   387  C  CG1   . ILE   A 1 47  ? 9.23140   -1.61438  15.20864  1.000 36.96485  ? 46  ILE   A CG1   1 
ATOM   388  C  CG2   . ILE   A 1 47  ? 10.28417  -3.86358  15.03889  1.000 37.94054  ? 46  ILE   A CG2   1 
ATOM   389  C  CD1   . ILE   A 1 47  ? 10.52694  -0.92339  15.59654  1.000 33.96844  ? 46  ILE   A CD1   1 
ATOM   390  N  N     . ASP   A 1 48  ? 7.57515   -6.02060  14.81428  1.000 46.98073  ? 47  ASP   A N     1 
ATOM   391  C  CA    . ASP   A 1 48  ? 7.47889   -7.45574  15.07064  1.000 49.70165  ? 47  ASP   A CA    1 
ATOM   392  C  C     . ASP   A 1 48  ? 6.42075   -7.73446  16.13135  1.000 45.27151  ? 47  ASP   A C     1 
ATOM   393  O  O     . ASP   A 1 48  ? 6.61852   -8.53350  17.04759  1.000 52.56676  ? 47  ASP   A O     1 
ATOM   394  C  CB    . ASP   A 1 48  ? 8.83774   -8.03841  15.47130  1.000 45.55876  ? 47  ASP   A CB    1 
ATOM   395  C  CG    . ASP   A 1 48  ? 9.85681   -7.97236  14.34325  1.000 50.64733  ? 47  ASP   A CG    1 
ATOM   396  O  OD1   . ASP   A 1 48  ? 9.44994   -7.92210  13.15937  1.000 45.32196  ? 47  ASP   A OD1   1 
ATOM   397  O  OD2   . ASP   A 1 48  ? 11.06987  -7.98113  14.63859  1.000 53.64310  ? 47  ASP   A OD2   1 
ATOM   398  N  N     . GLY   A 1 49  ? 5.29502   -7.02965  16.02056  1.000 46.89299  ? 48  GLY   A N     1 
ATOM   399  C  CA    . GLY   A 1 49  ? 4.19394   -7.17222  16.94418  1.000 49.80346  ? 48  GLY   A CA    1 
ATOM   400  C  C     . GLY   A 1 49  ? 4.30227   -6.38146  18.22997  1.000 49.99120  ? 48  GLY   A C     1 
ATOM   401  O  O     . GLY   A 1 49  ? 3.32297   -6.32978  18.98377  1.000 45.66991  ? 48  GLY   A O     1 
ATOM   402  N  N     . GLU   A 1 50  ? 5.44273   -5.75541  18.51284  1.000 44.97340  ? 49  GLU   A N     1 
ATOM   403  C  CA    . GLU   A 1 50  ? 5.66581   -5.10293  19.79625  1.000 44.23047  ? 49  GLU   A CA    1 
ATOM   404  C  C     . GLU   A 1 50  ? 5.68721   -3.59127  19.62772  1.000 47.14369  ? 49  GLU   A C     1 
ATOM   405  O  O     . GLU   A 1 50  ? 6.42164   -3.06343  18.78429  1.000 43.29283  ? 49  GLU   A O     1 
ATOM   406  C  CB    . GLU   A 1 50  ? 6.97087   -5.57437  20.43666  1.000 50.70917  ? 49  GLU   A CB    1 
ATOM   407  C  CG    . GLU   A 1 50  ? 7.19689   -5.00319  21.81974  1.000 48.93182  ? 49  GLU   A CG    1 
ATOM   408  C  CD    . GLU   A 1 50  ? 8.25026   -5.76403  22.59491  1.000 58.02159  ? 49  GLU   A CD    1 
ATOM   409  O  OE1   . GLU   A 1 50  ? 9.26127   -6.17314  21.98278  1.000 60.37760  ? 49  GLU   A OE1   1 
ATOM   410  O  OE2   . GLU   A 1 50  ? 8.05951   -5.96181  23.81384  1.000 65.44958  ? 49  GLU   A OE2   1 
ATOM   411  N  N     . THR   A 1 51  ? 4.89521   -2.90424  20.44598  1.000 43.39710  ? 50  THR   A N     1 
ATOM   412  C  CA    . THR   A 1 51  ? 4.84301   -1.44996  20.42811  1.000 46.26769  ? 50  THR   A CA    1 
ATOM   413  C  C     . THR   A 1 51  ? 6.04268   -0.86689  21.17151  1.000 44.24820  ? 50  THR   A C     1 
ATOM   414  O  O     . THR   A 1 51  ? 6.42937   -1.35728  22.23862  1.000 40.12988  ? 50  THR   A O     1 
ATOM   415  C  CB    . THR   A 1 51  ? 3.53037   -0.97098  21.04761  1.000 44.84884  ? 50  THR   A CB    1 
ATOM   416  O  OG1   . THR   A 1 51  ? 2.43987   -1.46232  20.25728  1.000 42.12758  ? 50  THR   A OG1   1 
ATOM   417  C  CG2   . THR   A 1 51  ? 3.46622   0.55333   21.09295  1.000 42.77119  ? 50  THR   A CG2   1 
ATOM   418  N  N     . CYS   A 1 52  ? 6.63804   0.17700   20.60232  1.000 36.33923  ? 51  CYS   A N     1 
ATOM   419  C  CA    . CYS   A 1 52  ? 7.81025   0.78522   21.20857  1.000 34.83431  ? 51  CYS   A CA    1 
ATOM   420  C  C     . CYS   A 1 52  ? 7.88174   2.24828   20.79776  1.000 31.74469  ? 51  CYS   A C     1 
ATOM   421  O  O     . CYS   A 1 52  ? 7.22550   2.68611   19.85303  1.000 30.57143  ? 51  CYS   A O     1 
ATOM   422  C  CB    . CYS   A 1 52  ? 9.08451   0.02639   20.82716  1.000 35.77283  ? 51  CYS   A CB    1 
ATOM   423  S  SG    . CYS   A 1 52  ? 9.43327   -0.06717  19.07460  1.000 41.70172  ? 51  CYS   A SG    1 
ATOM   424  N  N     . LEU   A 1 53  ? 8.68192   3.00588   21.53744  1.000 29.39016  ? 52  LEU   A N     1 
ATOM   425  C  CA    . LEU   A 1 53  ? 8.83479   4.44052   21.33776  1.000 30.54727  ? 52  LEU   A CA    1 
ATOM   426  C  C     . LEU   A 1 53  ? 10.22633  4.69416   20.77629  1.000 34.63286  ? 52  LEU   A C     1 
ATOM   427  O  O     . LEU   A 1 53  ? 11.22406  4.32024   21.40131  1.000 31.45052  ? 52  LEU   A O     1 
ATOM   428  C  CB    . LEU   A 1 53  ? 8.64392   5.18448   22.65919  1.000 30.28331  ? 52  LEU   A CB    1 
ATOM   429  C  CG    . LEU   A 1 53  ? 8.61378   6.71214   22.66607  1.000 30.13187  ? 52  LEU   A CG    1 
ATOM   430  C  CD1   . LEU   A 1 53  ? 7.55639   7.23279   21.70538  1.000 25.79678  ? 52  LEU   A CD1   1 
ATOM   431  C  CD2   . LEU   A 1 53  ? 8.31216   7.17702   24.08301  1.000 39.69807  ? 52  LEU   A CD2   1 
ATOM   432  N  N     . LEU   A 1 54  ? 10.29471  5.32755   19.61041  1.000 26.12695  ? 53  LEU   A N     1 
ATOM   433  C  CA    . LEU   A 1 54  ? 11.57779  5.68998   19.01749  1.000 28.94081  ? 53  LEU   A CA    1 
ATOM   434  C  C     . LEU   A 1 54  ? 11.97498  7.08865   19.47345  1.000 29.73448  ? 53  LEU   A C     1 
ATOM   435  O  O     . LEU   A 1 54  ? 11.23295  8.05239   19.27319  1.000 26.77993  ? 53  LEU   A O     1 
ATOM   436  C  CB    . LEU   A 1 54  ? 11.51775  5.62397   17.49289  1.000 26.75062  ? 53  LEU   A CB    1 
ATOM   437  C  CG    . LEU   A 1 54  ? 10.99220  4.34067   16.84466  1.000 29.12289  ? 53  LEU   A CG    1 
ATOM   438  C  CD1   . LEU   A 1 54  ? 11.26893  4.36566   15.34563  1.000 31.15685  ? 53  LEU   A CD1   1 
ATOM   439  C  CD2   . LEU   A 1 54  ? 11.58215  3.10363   17.51234  1.000 31.26004  ? 53  LEU   A CD2   1 
ATOM   440  N  N     . ASP   A 1 55  ? 13.14114  7.19978   20.08124  1.000 24.39274  ? 54  ASP   A N     1 
ATOM   441  C  CA    . ASP   A 1 55  ? 13.74409  8.48050   20.40648  1.000 25.11931  ? 54  ASP   A CA    1 
ATOM   442  C  C     . ASP   A 1 55  ? 14.88414  8.64954   19.41274  1.000 24.50942  ? 54  ASP   A C     1 
ATOM   443  O  O     . ASP   A 1 55  ? 15.87272  7.91796   19.48861  1.000 27.10826  ? 54  ASP   A O     1 
ATOM   444  C  CB    . ASP   A 1 55  ? 14.22153  8.46318   21.85968  1.000 28.31487  ? 54  ASP   A CB    1 
ATOM   445  C  CG    . ASP   A 1 55  ? 14.79883  9.78587   22.32865  1.000 34.89495  ? 54  ASP   A CG    1 
ATOM   446  O  OD1   . ASP   A 1 55  ? 15.59116  10.41908  21.59968  1.000 40.29209  ? 54  ASP   A OD1   1 
ATOM   447  O  OD2   . ASP   A 1 55  ? 14.48414  10.17150  23.47153  1.000 40.46701  ? 54  ASP   A OD2   1 
ATOM   448  N  N     . ILE   A 1 56  ? 14.73059  9.56774   18.45222  1.000 23.00397  ? 55  ILE   A N     1 
ATOM   449  C  CA    . ILE   A 1 56  ? 15.65197  9.68578   17.32536  1.000 23.80297  ? 55  ILE   A CA    1 
ATOM   450  C  C     . ILE   A 1 56  ? 16.45377  10.97025  17.46525  1.000 21.48862  ? 55  ILE   A C     1 
ATOM   451  O  O     . ILE   A 1 56  ? 15.89138  12.06477  17.57654  1.000 22.18332  ? 55  ILE   A O     1 
ATOM   452  C  CB    . ILE   A 1 56  ? 14.89737  9.64427   15.98360  1.000 22.36109  ? 55  ILE   A CB    1 
ATOM   453  C  CG1   . ILE   A 1 56  ? 14.07659  8.36341   15.92270  1.000 22.79858  ? 55  ILE   A CG1   1 
ATOM   454  C  CG2   . ILE   A 1 56  ? 15.88251  9.69252   14.78316  1.000 22.02667  ? 55  ILE   A CG2   1 
ATOM   455  C  CD1   . ILE   A 1 56  ? 13.13671  8.35965   14.81048  1.000 29.88406  ? 55  ILE   A CD1   1 
ATOM   456  N  N     . LEU   A 1 57  ? 17.77059  10.84140  17.44112  1.000 19.51112  ? 56  LEU   A N     1 
ATOM   457  C  CA    . LEU   A 1 57  ? 18.64930  11.99418  17.43275  1.000 18.70447  ? 56  LEU   A CA    1 
ATOM   458  C  C     . LEU   A 1 57  ? 19.19319  12.15235  16.01979  1.000 20.93653  ? 56  LEU   A C     1 
ATOM   459  O  O     . LEU   A 1 57  ? 19.84652  11.23913  15.49589  1.000 22.28267  ? 56  LEU   A O     1 
ATOM   460  C  CB    . LEU   A 1 57  ? 19.78600  11.80921  18.43868  1.000 19.26904  ? 56  LEU   A CB    1 
ATOM   461  C  CG    . LEU   A 1 57  ? 20.67988  13.02827  18.56000  1.000 23.33145  ? 56  LEU   A CG    1 
ATOM   462  C  CD1   . LEU   A 1 57  ? 19.89436  14.20201  19.07308  1.000 28.06626  ? 56  LEU   A CD1   1 
ATOM   463  C  CD2   . LEU   A 1 57  ? 21.83705  12.69371  19.51546  1.000 23.43704  ? 56  LEU   A CD2   1 
ATOM   464  N  N     . ASP   A 1 58  ? 18.90544  13.30092  15.39867  1.000 20.37515  ? 57  ASP   A N     1 
ATOM   465  C  CA    . ASP   A 1 58  ? 19.36455  13.62920  14.05668  1.000 20.69912  ? 57  ASP   A CA    1 
ATOM   466  C  C     . ASP   A 1 58  ? 20.57030  14.55148  14.19848  1.000 20.96697  ? 57  ASP   A C     1 
ATOM   467  O  O     . ASP   A 1 58  ? 20.42987  15.70213  14.62163  1.000 20.88140  ? 57  ASP   A O     1 
ATOM   468  C  CB    . ASP   A 1 58  ? 18.23170  14.30299  13.28404  1.000 23.42073  ? 57  ASP   A CB    1 
ATOM   469  C  CG    . ASP   A 1 58  ? 18.60078  14.64449  11.84795  1.000 24.46707  ? 57  ASP   A CG    1 
ATOM   470  O  OD1   . ASP   A 1 58  ? 19.58639  14.09592  11.29350  1.000 23.88217  ? 57  ASP   A OD1   1 
ATOM   471  O  OD2   . ASP   A 1 58  ? 17.87457  15.48378  11.26312  1.000 22.44603  ? 57  ASP   A OD2   1 
ATOM   472  N  N     . THR   A 1 59  ? 21.75327  14.05128  13.85644  1.000 20.42637  ? 58  THR   A N     1 
ATOM   473  C  CA    . THR   A 1 59  ? 22.98041  14.75216  14.19074  1.000 22.20383  ? 58  THR   A CA    1 
ATOM   474  C  C     . THR   A 1 59  ? 23.50370  15.54057  12.99042  1.000 24.84277  ? 58  THR   A C     1 
ATOM   475  O  O     . THR   A 1 59  ? 23.07187  15.35506  11.85341  1.000 22.07890  ? 58  THR   A O     1 
ATOM   476  C  CB    . THR   A 1 59  ? 24.03666  13.76141  14.68448  1.000 21.88073  ? 58  THR   A CB    1 
ATOM   477  O  OG1   . THR   A 1 59  ? 24.44920  12.93029  13.59671  1.000 23.49377  ? 58  THR   A OG1   1 
ATOM   478  C  CG2   . THR   A 1 59  ? 23.45348  12.88645  15.79394  1.000 21.93732  ? 58  THR   A CG2   1 
ATOM   479  N  N     . ALA   A 1 60  ? 24.46088  16.42177  13.26334  1.000 20.31460  ? 59  ALA   A N     1 
ATOM   480  C  CA    . ALA   A 1 60  ? 25.08470  17.24785  12.23636  1.000 21.91134  ? 59  ALA   A CA    1 
ATOM   481  C  C     . ALA   A 1 60  ? 26.16322  16.48490  11.46635  1.000 25.20356  ? 59  ALA   A C     1 
ATOM   482  O  O     . ALA   A 1 60  ? 27.08936  15.93508  12.06403  1.000 27.61202  ? 59  ALA   A O     1 
ATOM   483  C  CB    . ALA   A 1 60  ? 25.70897  18.48904  12.87631  1.000 23.96840  ? 59  ALA   A CB    1 
ATOM   484  N  N     . GLY   A 1 61  ? 26.04657  16.46683  10.14015  1.000 25.74930  ? 60  GLY   A N     1 
ATOM   485  C  CA    . GLY   A 1 61  ? 27.12279  15.95857  9.32042   1.000 26.08773  ? 60  GLY   A CA    1 
ATOM   486  C  C     . GLY   A 1 61  ? 28.27307  16.91984  9.16341   1.000 34.45287  ? 60  GLY   A C     1 
ATOM   487  O  O     . GLY   A 1 61  ? 29.33280  16.52091  8.66553   1.000 35.93434  ? 60  GLY   A O     1 
ATOM   488  N  N     . GLN   A 1 62  ? 28.08196  18.17517  9.59015   1.000 30.37622  ? 61  GLN   A N     1 
ATOM   489  C  CA    . GLN   A 1 62  ? 29.05032  19.24925  9.38954   1.000 34.63434  ? 61  GLN   A CA    1 
ATOM   490  C  C     . GLN   A 1 62  ? 30.42775  18.81161  9.90346   1.000 31.46841  ? 61  GLN   A C     1 
ATOM   491  O  O     . GLN   A 1 62  ? 30.63991  18.62574  11.10859  1.000 35.09253  ? 61  GLN   A O     1 
ATOM   492  C  CB    . GLN   A 1 62  ? 28.54997  20.53461  10.05986  1.000 32.19345  ? 61  GLN   A CB    1 
ATOM   493  C  CG    . GLN   A 1 62  ? 29.27209  21.81084  9.60494   1.000 37.15235  ? 61  GLN   A CG    1 
ATOM   494  C  CD    . GLN   A 1 62  ? 28.99522  22.16849  8.15448   1.000 39.82912  ? 61  GLN   A CD    1 
ATOM   495  O  OE1   . GLN   A 1 62  ? 27.89483  21.93083  7.63962   1.000 37.34601  ? 61  GLN   A OE1   1 
ATOM   496  N  NE2   . GLN   A 1 62  ? 29.99211  22.74702  7.48205   1.000 43.29311  ? 61  GLN   A NE2   1 
ATOM   497  N  N     . GLU   A 1 63  ? 31.35996  18.60489  8.96534   1.000 37.36122  ? 62  GLU   A N     1 
ATOM   498  C  CA    . GLU   A 1 63  ? 32.57592  17.83566  9.23768   1.000 36.81642  ? 62  GLU   A CA    1 
ATOM   499  C  C     . GLU   A 1 63  ? 33.51707  18.52223  10.24243  1.000 36.78510  ? 62  GLU   A C     1 
ATOM   500  O  O     . GLU   A 1 63  ? 34.30751  17.84759  10.90949  1.000 35.70313  ? 62  GLU   A O     1 
ATOM   501  C  CB    . GLU   A 1 63  ? 33.29567  17.56493  7.91057   1.000 52.47796  ? 62  GLU   A CB    1 
ATOM   502  C  CG    . GLU   A 1 63  ? 32.58564  16.58889  6.89550   1.000 52.06412  ? 62  GLU   A CG    1 
ATOM   503  C  CD    . GLU   A 1 63  ? 31.30161  17.10968  6.19480   1.000 51.00799  ? 62  GLU   A CD    1 
ATOM   504  O  OE1   . GLU   A 1 63  ? 31.00936  18.34863  6.17536   1.000 47.67309  ? 62  GLU   A OE1   1 
ATOM   505  O  OE2   . GLU   A 1 63  ? 30.54478  16.24397  5.65746   1.000 42.03935  ? 62  GLU   A OE2   1 
ATOM   506  N  N     . GLU   A 1 64  ? 33.43433  19.84724  10.39472  1.000 36.32474  ? 63  GLU   A N     1 
ATOM   507  C  CA    . GLU   A 1 64  ? 34.35755  20.58456  11.26341  1.000 31.92636  ? 63  GLU   A CA    1 
ATOM   508  C  C     . GLU   A 1 64  ? 34.17763  20.28152  12.74948  1.000 36.31629  ? 63  GLU   A C     1 
ATOM   509  O  O     . GLU   A 1 64  ? 35.06500  20.59813  13.54213  1.000 33.94187  ? 63  GLU   A O     1 
ATOM   510  C  CB    . GLU   A 1 64  ? 34.18759  22.09830  11.07398  1.000 35.89262  ? 63  GLU   A CB    1 
ATOM   511  C  CG    . GLU   A 1 64  ? 34.33231  22.58308  9.63573   1.000 47.44664  ? 63  GLU   A CG    1 
ATOM   512  C  CD    . GLU   A 1 64  ? 32.99178  22.64754  8.92714   1.000 51.60537  ? 63  GLU   A CD    1 
ATOM   513  O  OE1   . GLU   A 1 64  ? 32.46295  21.57179  8.57944   1.000 47.05431  ? 63  GLU   A OE1   1 
ATOM   514  O  OE2   . GLU   A 1 64  ? 32.45897  23.76662  8.72653   1.000 54.03164  ? 63  GLU   A OE2   1 
ATOM   515  N  N     . TYR   A 1 65  ? 33.05145  19.68747  13.15405  1.000 32.84712  ? 64  TYR   A N     1 
ATOM   516  C  CA    . TYR   A 1 65  ? 32.72179  19.44243  14.55435  1.000 33.27915  ? 64  TYR   A CA    1 
ATOM   517  C  C     . TYR   A 1 65  ? 32.85393  17.96409  14.91270  1.000 31.19469  ? 64  TYR   A C     1 
ATOM   518  O  O     . TYR   A 1 65  ? 32.19333  17.48340  15.83393  1.000 29.31517  ? 64  TYR   A O     1 
ATOM   519  C  CB    . TYR   A 1 65  ? 31.31430  19.98355  14.86103  1.000 31.14003  ? 64  TYR   A CB    1 
ATOM   520  C  CG    . TYR   A 1 65  ? 31.21747  21.45742  14.50317  1.000 25.87275  ? 64  TYR   A CG    1 
ATOM   521  C  CD1   . TYR   A 1 65  ? 31.79975  22.41253  15.31430  1.000 26.56519  ? 64  TYR   A CD1   1 
ATOM   522  C  CD2   . TYR   A 1 65  ? 30.59557  21.88472  13.32960  1.000 29.75183  ? 64  TYR   A CD2   1 
ATOM   523  C  CE1   . TYR   A 1 65  ? 31.75789  23.75201  14.99935  1.000 28.69176  ? 64  TYR   A CE1   1 
ATOM   524  C  CE2   . TYR   A 1 65  ? 30.54415  23.23636  12.99772  1.000 29.39271  ? 64  TYR   A CE2   1 
ATOM   525  C  CZ    . TYR   A 1 65  ? 31.12984  24.16686  13.84314  1.000 28.62070  ? 64  TYR   A CZ    1 
ATOM   526  O  OH    . TYR   A 1 65  ? 31.08843  25.50483  13.53591  1.000 31.13153  ? 64  TYR   A OH    1 
ATOM   527  N  N     . SER   A 1 66  ? 33.75761  17.24753  14.22980  1.000 34.42403  ? 65  SER   A N     1 
ATOM   528  C  CA    . SER   A 1 66  ? 33.92411  15.82126  14.48321  1.000 32.90806  ? 65  SER   A CA    1 
ATOM   529  C  C     . SER   A 1 66  ? 34.38866  15.52215  15.90150  1.000 30.14924  ? 65  SER   A C     1 
ATOM   530  O  O     . SER   A 1 66  ? 34.20930  14.39314  16.36215  1.000 34.41876  ? 65  SER   A O     1 
ATOM   531  C  CB    . SER   A 1 66  ? 34.89671  15.20585  13.47221  1.000 36.44931  ? 65  SER   A CB    1 
ATOM   532  O  OG    . SER   A 1 66  ? 36.13688  15.88101  13.48120  1.000 34.25361  ? 65  SER   A OG    1 
ATOM   533  N  N     . ALA   A 1 67  ? 34.96312  16.49205  16.61181  1.000 35.52381  ? 66  ALA   A N     1 
ATOM   534  C  CA    . ALA   A 1 67  ? 35.35870  16.25539  17.99760  1.000 37.07297  ? 66  ALA   A CA    1 
ATOM   535  C  C     . ALA   A 1 67  ? 34.21526  16.46071  18.98948  1.000 36.71582  ? 66  ALA   A C     1 
ATOM   536  O  O     . ALA   A 1 67  ? 34.43325  16.33877  20.19929  1.000 41.11430  ? 66  ALA   A O     1 
ATOM   537  C  CB    . ALA   A 1 67  ? 36.54209  17.15447  18.37933  1.000 38.92125  ? 66  ALA   A CB    1 
ATOM   538  N  N     . MET   A 1 68  ? 33.00449  16.75035  18.50965  1.000 38.50050  ? 67  MET   A N     1 
ATOM   539  C  CA    . MET   A 1 68  ? 31.84825  17.03747  19.35154  1.000 35.67170  ? 67  MET   A CA    1 
ATOM   540  C  C     . MET   A 1 68  ? 30.88615  15.86105  19.46340  1.000 38.26431  ? 67  MET   A C     1 
ATOM   541  O  O     . MET   A 1 68  ? 29.74701  16.05635  19.89410  1.000 33.83010  ? 67  MET   A O     1 
ATOM   542  C  CB    . MET   A 1 68  ? 31.07433  18.24274  18.80388  1.000 33.56629  ? 67  MET   A CB    1 
ATOM   543  C  CG    . MET   A 1 68  ? 31.90643  19.47430  18.51479  1.000 38.87524  ? 67  MET   A CG    1 
ATOM   544  S  SD    . MET   A 1 68  ? 32.18244  20.37295  20.02217  1.000 49.38781  ? 67  MET   A SD    1 
ATOM   545  C  CE    . MET   A 1 68  ? 30.48605  20.72799  20.51501  1.000 34.25477  ? 67  MET   A CE    1 
ATOM   546  N  N     . ARG   A 1 69  ? 31.29394  14.65761  19.05009  1.000 32.34599  ? 68  ARG   A N     1 
ATOM   547  C  CA    . ARG   A 1 69  ? 30.35460  13.55065  18.88790  1.000 28.34172  ? 68  ARG   A CA    1 
ATOM   548  C  C     . ARG   A 1 69  ? 30.36904  12.55846  20.03508  1.000 32.13951  ? 68  ARG   A C     1 
ATOM   549  O  O     . ARG   A 1 69  ? 29.47486  11.71130  20.10883  1.000 26.70731  ? 68  ARG   A O     1 
ATOM   550  C  CB    . ARG   A 1 69  ? 30.64730  12.79581  17.59000  1.000 26.54940  ? 68  ARG   A CB    1 
ATOM   551  C  CG    . ARG   A 1 69  ? 30.74429  13.68531  16.38318  1.000 29.38921  ? 68  ARG   A CG    1 
ATOM   552  C  CD    . ARG   A 1 69  ? 30.71769  12.88063  15.10209  1.000 31.49790  ? 68  ARG   A CD    1 
ATOM   553  N  NE    . ARG   A 1 69  ? 30.85643  13.74573  13.94153  1.000 31.59631  ? 68  ARG   A NE    1 
ATOM   554  C  CZ    . ARG   A 1 69  ? 31.75787  13.57905  12.98384  1.000 30.71014  ? 68  ARG   A CZ    1 
ATOM   555  N  NH1   . ARG   A 1 69  ? 32.62268  12.57605  13.01114  1.000 30.82096  ? 68  ARG   A NH1   1 
ATOM   556  N  NH2   . ARG   A 1 69  ? 31.79385  14.43890  11.97215  1.000 32.81435  ? 68  ARG   A NH2   1 
ATOM   557  N  N     . ASP   A 1 70  ? 31.35388  12.63467  20.92949  1.000 28.51843  ? 69  ASP   A N     1 
ATOM   558  C  CA    . ASP   A 1 70  ? 31.52731  11.56637  21.90053  1.000 31.19732  ? 69  ASP   A CA    1 
ATOM   559  C  C     . ASP   A 1 70  ? 30.30137  11.41203  22.78668  1.000 28.77335  ? 69  ASP   A C     1 
ATOM   560  O  O     . ASP   A 1 70  ? 29.87503  10.28663  23.06309  1.000 30.02188  ? 69  ASP   A O     1 
ATOM   561  C  CB    . ASP   A 1 70  ? 32.77220  11.81327  22.75956  1.000 33.30412  ? 69  ASP   A CB    1 
ATOM   562  C  CG    . ASP   A 1 70  ? 34.07052  11.54911  22.01577  1.000 44.79775  ? 69  ASP   A CG    1 
ATOM   563  O  OD1   . ASP   A 1 70  ? 34.04263  11.42179  20.76834  1.000 41.77754  ? 69  ASP   A OD1   1 
ATOM   564  O  OD2   . ASP   A 1 70  ? 35.12329  11.47020  22.69604  1.000 42.35289  ? 69  ASP   A OD2   1 
ATOM   565  N  N     . GLN   A 1 71  ? 29.71854  12.52352  23.24948  1.000 28.64237  ? 70  GLN   A N     1 
ATOM   566  C  CA    . GLN   A 1 71  ? 28.64283  12.39973  24.22963  1.000 30.84465  ? 70  GLN   A CA    1 
ATOM   567  C  C     . GLN   A 1 71  ? 27.39001  11.78944  23.61194  1.000 29.41027  ? 70  GLN   A C     1 
ATOM   568  O  O     . GLN   A 1 71  ? 26.76872  10.90560  24.20843  1.000 27.17579  ? 70  GLN   A O     1 
ATOM   569  C  CB    . GLN   A 1 71  ? 28.30285  13.74400  24.85690  1.000 35.94526  ? 70  GLN   A CB    1 
ATOM   570  C  CG    . GLN   A 1 71  ? 27.24412  13.59392  25.94339  1.000 38.09239  ? 70  GLN   A CG    1 
ATOM   571  C  CD    . GLN   A 1 71  ? 27.65065  12.59102  27.01385  1.000 44.90985  ? 70  GLN   A CD    1 
ATOM   572  O  OE1   . GLN   A 1 71  ? 28.72903  12.69968  27.61123  1.000 52.52726  ? 70  GLN   A OE1   1 
ATOM   573  N  NE2   . GLN   A 1 71  ? 26.79947  11.60189  27.25098  1.000 41.43642  ? 70  GLN   A NE2   1 
ATOM   574  N  N     . TYR   A 1 72  ? 27.00274  12.22137  22.41219  1.000 28.91472  ? 71  TYR   A N     1 
ATOM   575  C  CA    . TYR   A 1 72  ? 25.80142  11.59883  21.87750  1.000 31.15578  ? 71  TYR   A CA    1 
ATOM   576  C  C     . TYR   A 1 72  ? 26.06783  10.14514  21.50819  1.000 24.13644  ? 71  TYR   A C     1 
ATOM   577  O  O     . TYR   A 1 72  ? 25.15198  9.31735   21.56568  1.000 27.15477  ? 71  TYR   A O     1 
ATOM   578  C  CB    . TYR   A 1 72  ? 25.22797  12.41909  20.71786  1.000 28.34782  ? 71  TYR   A CB    1 
ATOM   579  C  CG    . TYR   A 1 72  ? 25.90284  12.38686  19.36501  1.000 24.86829  ? 71  TYR   A CG    1 
ATOM   580  C  CD1   . TYR   A 1 72  ? 26.07869  11.19358  18.66165  1.000 25.25737  ? 71  TYR   A CD1   1 
ATOM   581  C  CD2   . TYR   A 1 72  ? 26.27344  13.57022  18.73449  1.000 23.65032  ? 71  TYR   A CD2   1 
ATOM   582  C  CE1   . TYR   A 1 72  ? 26.66959  11.17417  17.39882  1.000 23.91456  ? 71  TYR   A CE1   1 
ATOM   583  C  CE2   . TYR   A 1 72  ? 26.84454  13.55225  17.45386  1.000 22.75785  ? 71  TYR   A CE2   1 
ATOM   584  C  CZ    . TYR   A 1 72  ? 27.02968  12.35234  16.80217  1.000 22.79632  ? 71  TYR   A CZ    1 
ATOM   585  O  OH    . TYR   A 1 72  ? 27.59038  12.32186  15.54811  1.000 26.21664  ? 71  TYR   A OH    1 
ATOM   586  N  N     . MET   A 1 73  ? 27.32008  9.80264   21.19023  1.000 25.05815  ? 72  MET   A N     1 
ATOM   587  C  CA    . MET   A 1 73  ? 27.64223  8.40341   20.92408  1.000 24.73227  ? 72  MET   A CA    1 
ATOM   588  C  C     . MET   A 1 73  ? 27.61151  7.56426   22.19257  1.000 26.14370  ? 72  MET   A C     1 
ATOM   589  O  O     . MET   A 1 73  ? 27.23386  6.38765   22.14032  1.000 27.00638  ? 72  MET   A O     1 
ATOM   590  C  CB    . MET   A 1 73  ? 29.00157  8.27952   20.23282  1.000 23.49521  ? 72  MET   A CB    1 
ATOM   591  C  CG    . MET   A 1 73  ? 28.98207  8.81038   18.82815  1.000 25.03992  ? 72  MET   A CG    1 
ATOM   592  S  SD    . MET   A 1 73  ? 30.57004  8.65897   17.99776  1.000 27.30021  ? 72  MET   A SD    1 
ATOM   593  C  CE    . MET   A 1 73  ? 30.10630  9.21989   16.37131  1.000 25.41253  ? 72  MET   A CE    1 
ATOM   594  N  N     . ARG   A 1 74  ? 28.00586  8.13391   23.33741  1.000 26.56179  ? 73  ARG   A N     1 
ATOM   595  C  CA    . ARG   A 1 74  ? 27.85697  7.39534   24.59104  1.000 27.06788  ? 73  ARG   A CA    1 
ATOM   596  C  C     . ARG   A 1 74  ? 26.39134  7.20722   24.95964  1.000 27.59637  ? 73  ARG   A C     1 
ATOM   597  O  O     . ARG   A 1 74  ? 26.00209  6.14857   25.45936  1.000 30.43647  ? 73  ARG   A O     1 
ATOM   598  C  CB    . ARG   A 1 74  ? 28.60515  8.10255   25.72589  1.000 32.22398  ? 73  ARG   A CB    1 
ATOM   599  C  CG    . ARG   A 1 74  ? 30.11258  7.89941   25.67825  1.000 36.44957  ? 73  ARG   A CG    1 
ATOM   600  C  CD    . ARG   A 1 74  ? 30.80299  8.34973   26.96411  1.000 36.92773  ? 73  ARG   A CD    1 
ATOM   601  N  NE    . ARG   A 1 74  ? 30.58641  9.76818   27.20883  1.000 42.47762  ? 73  ARG   A NE    1 
ATOM   602  C  CZ    . ARG   A 1 74  ? 31.28796  10.74073  26.64318  1.000 46.47810  ? 73  ARG   A CZ    1 
ATOM   603  N  NH1   . ARG   A 1 74  ? 32.25832  10.48192  25.77728  1.000 44.00939  ? 73  ARG   A NH1   1 
ATOM   604  N  NH2   . ARG   A 1 74  ? 31.01192  12.00573  26.95705  1.000 48.86713  ? 73  ARG   A NH2   1 
ATOM   605  N  N     . THR   A 1 75  ? 25.56653  8.22355   24.72952  1.000 26.29596  ? 74  THR   A N     1 
ATOM   606  C  CA    . THR   A 1 75  ? 24.16458  8.13732   25.12517  1.000 26.39675  ? 74  THR   A CA    1 
ATOM   607  C  C     . THR   A 1 75  ? 23.37434  7.20421   24.21128  1.000 27.71688  ? 74  THR   A C     1 
ATOM   608  O  O     . THR   A 1 75  ? 22.46204  6.51215   24.67130  1.000 32.82538  ? 74  THR   A O     1 
ATOM   609  C  CB    . THR   A 1 75  ? 23.54218  9.53717   25.13866  1.000 28.37385  ? 74  THR   A CB    1 
ATOM   610  O  OG1   . THR   A 1 75  ? 24.25126  10.36121  26.07432  1.000 42.19886  ? 74  THR   A OG1   1 
ATOM   611  C  CG2   . THR   A 1 75  ? 22.08796  9.48108   25.55541  1.000 31.21459  ? 74  THR   A CG2   1 
ATOM   612  N  N     . GLY   A 1 76  ? 23.69708  7.17006   22.91848  1.000 25.29836  ? 75  GLY   A N     1 
ATOM   613  C  CA    . GLY   A 1 76  ? 22.86320  6.43031   21.97751  1.000 24.65627  ? 75  GLY   A CA    1 
ATOM   614  C  C     . GLY   A 1 76  ? 22.96328  4.92312   22.15293  1.000 29.51346  ? 75  GLY   A C     1 
ATOM   615  O  O     . GLY   A 1 76  ? 24.00866  4.37879   22.51327  1.000 32.17409  ? 75  GLY   A O     1 
ATOM   616  N  N     . GLU   A 1 77  ? 21.85190  4.23489   21.87635  1.000 24.79681  ? 76  GLU   A N     1 
ATOM   617  C  CA    . GLU   A 1 77  ? 21.79464  2.77447   21.90829  1.000 25.90029  ? 76  GLU   A CA    1 
ATOM   618  C  C     . GLU   A 1 77  ? 22.03981  2.11529   20.55815  1.000 29.79858  ? 76  GLU   A C     1 
ATOM   619  O  O     . GLU   A 1 77  ? 22.57085  0.99926   20.51765  1.000 29.17125  ? 76  GLU   A O     1 
ATOM   620  C  CB    . GLU   A 1 77  ? 20.43818  2.31082   22.44182  1.000 28.19848  ? 76  GLU   A CB    1 
ATOM   621  C  CG    . GLU   A 1 77  ? 20.25849  2.57440   23.92708  1.000 37.27026  ? 76  GLU   A CG    1 
ATOM   622  C  CD    . GLU   A 1 77  ? 18.86073  2.26237   24.42651  1.000 38.00231  ? 76  GLU   A CD    1 
ATOM   623  O  OE1   . GLU   A 1 77  ? 17.88582  2.46792   23.67187  1.000 33.48892  ? 76  GLU   A OE1   1 
ATOM   624  O  OE2   . GLU   A 1 77  ? 18.73794  1.82346   25.58834  1.000 46.33653  ? 76  GLU   A OE2   1 
ATOM   625  N  N     . GLY   A 1 78  ? 21.67699  2.76879   19.46287  1.000 23.44910  ? 77  GLY   A N     1 
ATOM   626  C  CA    . GLY   A 1 78  ? 21.85662  2.19584   18.13614  1.000 22.66944  ? 77  GLY   A CA    1 
ATOM   627  C  C     . GLY   A 1 78  ? 22.06046  3.28076   17.10241  1.000 22.80901  ? 77  GLY   A C     1 
ATOM   628  O  O     . GLY   A 1 78  ? 21.57129  4.40718   17.25156  1.000 22.81352  ? 77  GLY   A O     1 
ATOM   629  N  N     . PHE   A 1 79  ? 22.81440  2.95288   16.06024  1.000 22.77861  ? 78  PHE   A N     1 
ATOM   630  C  CA    . PHE   A 1 79  ? 23.25106  3.96333   15.11675  1.000 21.09634  ? 78  PHE   A CA    1 
ATOM   631  C  C     . PHE   A 1 79  ? 22.84965  3.60035   13.70699  1.000 25.72895  ? 78  PHE   A C     1 
ATOM   632  O  O     . PHE   A 1 79  ? 23.16794  2.51420   13.21551  1.000 26.40135  ? 78  PHE   A O     1 
ATOM   633  C  CB    . PHE   A 1 79  ? 24.76219  4.18116   15.22454  1.000 25.98664  ? 78  PHE   A CB    1 
ATOM   634  C  CG    . PHE   A 1 79  ? 25.14971  4.65549   16.58194  1.000 19.20555  ? 78  PHE   A CG    1 
ATOM   635  C  CD1   . PHE   A 1 79  ? 25.26526  3.75462   17.61025  1.000 22.74959  ? 78  PHE   A CD1   1 
ATOM   636  C  CD2   . PHE   A 1 79  ? 25.29509  6.00628   16.84281  1.000 21.31573  ? 78  PHE   A CD2   1 
ATOM   637  C  CE1   . PHE   A 1 79  ? 25.56392  4.17855   18.88792  1.000 23.18110  ? 78  PHE   A CE1   1 
ATOM   638  C  CE2   . PHE   A 1 79  ? 25.61381  6.43869   18.12437  1.000 22.38861  ? 78  PHE   A CE2   1 
ATOM   639  C  CZ    . PHE   A 1 79  ? 25.73193  5.52387   19.14261  1.000 23.26702  ? 78  PHE   A CZ    1 
ATOM   640  N  N     . LEU   A 1 80  ? 22.14589  4.52496   13.06909  1.000 22.98974  ? 79  LEU   A N     1 
ATOM   641  C  CA    . LEU   A 1 80  ? 21.85812  4.45432   11.64403  1.000 21.42820  ? 79  LEU   A CA    1 
ATOM   642  C  C     . LEU   A 1 80  ? 23.00169  5.16495   10.92949  1.000 22.20673  ? 79  LEU   A C     1 
ATOM   643  O  O     . LEU   A 1 80  ? 23.16738  6.38366   11.06088  1.000 21.03578  ? 79  LEU   A O     1 
ATOM   644  C  CB    . LEU   A 1 80  ? 20.50868  5.10652   11.35051  1.000 26.69547  ? 79  LEU   A CB    1 
ATOM   645  C  CG    . LEU   A 1 80  ? 19.63408  4.43895   10.30150  1.000 30.20976  ? 79  LEU   A CG    1 
ATOM   646  C  CD1   . LEU   A 1 80  ? 19.28862  3.04103   10.75455  1.000 27.67465  ? 79  LEU   A CD1   1 
ATOM   647  C  CD2   . LEU   A 1 80  ? 18.37362  5.28242   10.09832  1.000 25.87382  ? 79  LEU   A CD2   1 
ATOM   648  N  N     . CYS   A 1 81  ? 23.82673  4.39978   10.22258  1.000 22.68879  ? 80  CYS   A N     1 
ATOM   649  C  CA    . CYS   A 1 81  ? 25.04552  4.92782   9.61671   1.000 24.58615  ? 80  CYS   A CA    1 
ATOM   650  C  C     . CYS   A 1 81  ? 24.74946  5.13833   8.14415   1.000 23.46852  ? 80  CYS   A C     1 
ATOM   651  O  O     . CYS   A 1 81  ? 24.72286  4.17912   7.37131   1.000 25.32140  ? 80  CYS   A O     1 
ATOM   652  C  CB    . CYS   A 1 81  ? 26.22289  3.97580   9.80244   1.000 23.06735  ? 80  CYS   A CB    1 
ATOM   653  S  SG    . CYS   A 1 81  ? 26.73770  3.78296   11.51136  1.000 27.93489  ? 80  CYS   A SG    1 
ATOM   654  N  N     . VAL   A 1 82  ? 24.56849  6.39369   7.74889   1.000 20.28378  ? 81  VAL   A N     1 
ATOM   655  C  CA    . VAL   A 1 82  ? 23.97711  6.73118   6.45381   1.000 21.49188  ? 81  VAL   A CA    1 
ATOM   656  C  C     . VAL   A 1 82  ? 25.04368  7.26790   5.51170   1.000 22.62188  ? 81  VAL   A C     1 
ATOM   657  O  O     . VAL   A 1 82  ? 25.83466  8.14229   5.87814   1.000 22.22863  ? 81  VAL   A O     1 
ATOM   658  C  CB    . VAL   A 1 82  ? 22.83533  7.75015   6.60870   1.000 21.68029  ? 81  VAL   A CB    1 
ATOM   659  C  CG1   . VAL   A 1 82  ? 22.10440  7.91653   5.28208   1.000 19.86344  ? 81  VAL   A CG1   1 
ATOM   660  C  CG2   . VAL   A 1 82  ? 21.86076  7.30829   7.71409   1.000 23.84860  ? 81  VAL   A CG2   1 
ATOM   661  N  N     . PHE   A 1 83  ? 25.02995  6.76922   4.27752   1.000 23.00042  ? 82  PHE   A N     1 
ATOM   662  C  CA    . PHE   A 1 83  ? 25.76672  7.36094   3.17740   1.000 26.84031  ? 82  PHE   A CA    1 
ATOM   663  C  C     . PHE   A 1 83  ? 24.79365  7.48958   2.01240   1.000 23.77984  ? 82  PHE   A C     1 
ATOM   664  O  O     . PHE   A 1 83  ? 23.68922  6.94178   2.05038   1.000 23.81281  ? 82  PHE   A O     1 
ATOM   665  C  CB    . PHE   A 1 83  ? 26.99452  6.50688   2.79701   1.000 26.33484  ? 82  PHE   A CB    1 
ATOM   666  C  CG    . PHE   A 1 83  ? 26.64406  5.18834   2.15392   1.000 25.12554  ? 82  PHE   A CG    1 
ATOM   667  C  CD1   . PHE   A 1 83  ? 26.35356  4.07964   2.92410   1.000 25.30451  ? 82  PHE   A CD1   1 
ATOM   668  C  CD2   . PHE   A 1 83  ? 26.61693  5.06069   0.76293   1.000 25.85195  ? 82  PHE   A CD2   1 
ATOM   669  C  CE1   . PHE   A 1 83  ? 26.01765  2.86483   2.33143   1.000 23.66484  ? 82  PHE   A CE1   1 
ATOM   670  C  CE2   . PHE   A 1 83  ? 26.28373  3.85761   0.17215   1.000 28.26803  ? 82  PHE   A CE2   1 
ATOM   671  C  CZ    . PHE   A 1 83  ? 25.98268  2.75902   0.95022   1.000 29.19445  ? 82  PHE   A CZ    1 
ATOM   672  N  N     . ALA   A 1 84  ? 25.19517  8.23255   0.98637   1.000 25.88680  ? 83  ALA   A N     1 
ATOM   673  C  CA    . ALA   A 1 84  ? 24.39113  8.37200   -0.22053  1.000 27.73902  ? 83  ALA   A CA    1 
ATOM   674  C  C     . ALA   A 1 84  ? 25.03214  7.57894   -1.35064  1.000 29.85601  ? 83  ALA   A C     1 
ATOM   675  O  O     . ALA   A 1 84  ? 26.24746  7.64237   -1.54934  1.000 28.65746  ? 83  ALA   A O     1 
ATOM   676  C  CB    . ALA   A 1 84  ? 24.23895  9.83839   -0.62763  1.000 24.90710  ? 83  ALA   A CB    1 
ATOM   677  N  N     . ILE   A 1 85  ? 24.20447  6.84568   -2.09895  1.000 29.25595  ? 84  ILE   A N     1 
ATOM   678  C  CA    . ILE   A 1 85  ? 24.72843  5.91241   -3.09196  1.000 33.66334  ? 84  ILE   A CA    1 
ATOM   679  C  C     . ILE   A 1 85  ? 25.31631  6.61374   -4.30363  1.000 32.70803  ? 84  ILE   A C     1 
ATOM   680  O  O     . ILE   A 1 85  ? 25.91320  5.94979   -5.15771  1.000 38.19290  ? 84  ILE   A O     1 
ATOM   681  C  CB    . ILE   A 1 85  ? 23.64097  4.89960   -3.51584  1.000 33.92923  ? 84  ILE   A CB    1 
ATOM   682  C  CG1   . ILE   A 1 85  ? 22.38563  5.60406   -4.04331  1.000 40.29877  ? 84  ILE   A CG1   1 
ATOM   683  C  CG2   . ILE   A 1 85  ? 23.28775  3.97339   -2.35802  1.000 34.35025  ? 84  ILE   A CG2   1 
ATOM   684  C  CD1   . ILE   A 1 85  ? 22.38574  5.84345   -5.53549  1.000 43.17644  ? 84  ILE   A CD1   1 
ATOM   685  N  N     . ASN   A 1 86  ? 25.16922  7.93488   -4.39607  1.000 34.09785  ? 85  ASN   A N     1 
ATOM   686  C  CA    . ASN   A 1 86  ? 25.75778  8.72993   -5.46650  1.000 40.17450  ? 85  ASN   A CA    1 
ATOM   687  C  C     . ASN   A 1 86  ? 26.90321  9.60504   -4.97174  1.000 37.65863  ? 85  ASN   A C     1 
ATOM   688  O  O     . ASN   A 1 86  ? 27.22099  10.61629  -5.60457  1.000 36.34268  ? 85  ASN   A O     1 
ATOM   689  C  CB    . ASN   A 1 86  ? 24.69643  9.60833   -6.12275  1.000 40.64443  ? 85  ASN   A CB    1 
ATOM   690  C  CG    . ASN   A 1 86  ? 24.22881  10.72160  -5.21199  1.000 40.64526  ? 85  ASN   A CG    1 
ATOM   691  O  OD1   . ASN   A 1 86  ? 24.23231  10.57447  -3.99192  1.000 34.83219  ? 85  ASN   A OD1   1 
ATOM   692  N  ND2   . ASN   A 1 86  ? 23.83278  11.84407  -5.79495  1.000 40.04468  ? 85  ASN   A ND2   1 
ATOM   693  N  N     . ASN   A 1 87  ? 27.49938  9.27435   -3.82577  1.000 32.56591  ? 86  ASN   A N     1 
ATOM   694  C  CA    . ASN   A 1 87  ? 28.59934  10.07508  -3.29020  1.000 35.92762  ? 86  ASN   A CA    1 
ATOM   695  C  C     . ASN   A 1 87  ? 29.58725  9.12092   -2.62401  1.000 40.46483  ? 86  ASN   A C     1 
ATOM   696  O  O     . ASN   A 1 87  ? 29.36283  8.64864   -1.50472  1.000 36.64271  ? 86  ASN   A O     1 
ATOM   697  C  CB    . ASN   A 1 87  ? 28.10402  11.14676  -2.32851  1.000 39.09967  ? 86  ASN   A CB    1 
ATOM   698  C  CG    . ASN   A 1 87  ? 29.20397  12.10980  -1.92321  1.000 41.22221  ? 86  ASN   A CG    1 
ATOM   699  O  OD1   . ASN   A 1 87  ? 30.14301  11.72801  -1.23911  1.000 41.66549  ? 86  ASN   A OD1   1 
ATOM   700  N  ND2   . ASN   A 1 87  ? 29.09455  13.36003  -2.35197  1.000 46.59128  ? 86  ASN   A ND2   1 
ATOM   701  N  N     . THR   A 1 88  ? 30.68545  8.83755   -3.32522  1.000 36.29318  ? 87  THR   A N     1 
ATOM   702  C  CA    . THR   A 1 88  ? 31.62106  7.82661   -2.84927  1.000 38.31923  ? 87  THR   A CA    1 
ATOM   703  C  C     . THR   A 1 88  ? 32.34022  8.29034   -1.58738  1.000 38.68243  ? 87  THR   A C     1 
ATOM   704  O  O     . THR   A 1 88  ? 32.66433  7.47944   -0.71533  1.000 37.65599  ? 87  THR   A O     1 
ATOM   705  C  CB    . THR   A 1 88  ? 32.61272  7.47799   -3.96575  1.000 43.44190  ? 87  THR   A CB    1 
ATOM   706  O  OG1   . THR   A 1 88  ? 31.88525  6.98559   -5.10087  1.000 42.52237  ? 87  THR   A OG1   1 
ATOM   707  C  CG2   . THR   A 1 88  ? 33.59682  6.40910   -3.50001  1.000 42.12758  ? 87  THR   A CG2   1 
ATOM   708  N  N     . LYS   A 1 89  ? 32.56289  9.59501   -1.45212  1.000 38.20343  ? 88  LYS   A N     1 
ATOM   709  C  CA    . LYS   A 1 89  ? 33.22317  10.09373  -0.25447  1.000 39.55096  ? 88  LYS   A CA    1 
ATOM   710  C  C     . LYS   A 1 89  ? 32.37939  9.83327   0.98962   1.000 35.77821  ? 88  LYS   A C     1 
ATOM   711  O  O     . LYS   A 1 89  ? 32.91374  9.47063   2.04170   1.000 36.78747  ? 88  LYS   A O     1 
ATOM   712  C  CB    . LYS   A 1 89  ? 33.52276  11.58322  -0.39727  1.000 47.06276  ? 88  LYS   A CB    1 
ATOM   713  C  CG    . LYS   A 1 89  ? 34.47278  12.11048  0.66849   1.000 48.68363  ? 88  LYS   A CG    1 
ATOM   714  C  CD    . LYS   A 1 89  ? 33.88445  13.30984  1.39252   1.000 52.45903  ? 88  LYS   A CD    1 
ATOM   715  C  CE    . LYS   A 1 89  ? 34.92531  14.00505  2.26110   1.000 60.62362  ? 88  LYS   A CE    1 
ATOM   716  N  NZ    . LYS   A 1 89  ? 35.47352  13.12388  3.33349   1.000 50.66545  ? 88  LYS   A NZ    1 
ATOM   717  N  N     . SER   A 1 90  ? 31.05483  10.00282  0.88842   1.000 35.54124  ? 89  SER   A N     1 
ATOM   718  C  CA    . SER   A 1 90  ? 30.19326  9.70462   2.03205   1.000 31.27891  ? 89  SER   A CA    1 
ATOM   719  C  C     . SER   A 1 90  ? 30.25840  8.23252   2.41397   1.000 33.31863  ? 89  SER   A C     1 
ATOM   720  O  O     . SER   A 1 90  ? 30.12755  7.89377   3.59395   1.000 32.08678  ? 89  SER   A O     1 
ATOM   721  C  CB    . SER   A 1 90  ? 28.74732  10.10073  1.72781   1.000 30.58672  ? 89  SER   A CB    1 
ATOM   722  O  OG    . SER   A 1 90  ? 28.14191  9.18791   0.83266   1.000 31.32441  ? 89  SER   A OG    1 
ATOM   723  N  N     . PHE   A 1 91  ? 30.45842  7.34821   1.43524   1.000 30.47092  ? 90  PHE   A N     1 
ATOM   724  C  CA    . PHE   A 1 91  ? 30.64790  5.93029   1.72342   1.000 31.61053  ? 90  PHE   A CA    1 
ATOM   725  C  C     . PHE   A 1 91  ? 31.97399  5.68740   2.43581   1.000 35.70544  ? 90  PHE   A C     1 
ATOM   726  O  O     . PHE   A 1 91  ? 32.05377  4.86999   3.36205   1.000 32.91069  ? 90  PHE   A O     1 
ATOM   727  C  CB    . PHE   A 1 91  ? 30.58522  5.13192   0.41837   1.000 33.83185  ? 90  PHE   A CB    1 
ATOM   728  C  CG    . PHE   A 1 91  ? 30.71458  3.64614   0.60152   1.000 34.91413  ? 90  PHE   A CG    1 
ATOM   729  C  CD1   . PHE   A 1 91  ? 29.73483  2.92414   1.26228   1.000 32.54749  ? 90  PHE   A CD1   1 
ATOM   730  C  CD2   . PHE   A 1 91  ? 31.80858  2.96279   0.09190   1.000 38.81140  ? 90  PHE   A CD2   1 
ATOM   731  C  CE1   . PHE   A 1 91  ? 29.84726  1.55610   1.42291   1.000 31.60571  ? 90  PHE   A CE1   1 
ATOM   732  C  CE2   . PHE   A 1 91  ? 31.92146  1.59068   0.25074   1.000 38.81140  ? 90  PHE   A CE2   1 
ATOM   733  C  CZ    . PHE   A 1 91  ? 30.93774  0.88578   0.91198   1.000 35.31098  ? 90  PHE   A CZ    1 
ATOM   734  N  N     . GLU   A 1 92  ? 33.02595  6.38568   2.01170   1.000 36.53766  ? 91  GLU   A N     1 
ATOM   735  C  CA    . GLU   A 1 92  ? 34.31188  6.26644   2.69261   1.000 38.98456  ? 91  GLU   A CA    1 
ATOM   736  C  C     . GLU   A 1 92  ? 34.26291  6.86673   4.08903   1.000 40.50197  ? 91  GLU   A C     1 
ATOM   737  O  O     . GLU   A 1 92  ? 34.93614  6.36680   4.99726   1.000 38.40769  ? 91  GLU   A O     1 
ATOM   738  C  CB    . GLU   A 1 92  ? 35.40348  6.94047   1.86317   1.000 40.80515  ? 91  GLU   A CB    1 
ATOM   739  C  CG    . GLU   A 1 92  ? 35.50160  6.39981   0.45758   1.000 46.60052  ? 91  GLU   A CG    1 
ATOM   740  C  CD    . GLU   A 1 92  ? 36.50404  7.15707   -0.38772  1.000 57.14628  ? 91  GLU   A CD    1 
ATOM   741  O  OE1   . GLU   A 1 92  ? 36.90855  8.26805   0.02171   1.000 56.51010  ? 91  GLU   A OE1   1 
ATOM   742  O  OE2   . GLU   A 1 92  ? 36.88364  6.64018   -1.46064  1.000 60.76093  ? 91  GLU   A OE2   1 
ATOM   743  N  N     . ASP   A 1 93  ? 33.47404  7.93163   4.27654   1.000 41.85804  ? 92  ASP   A N     1 
ATOM   744  C  CA    . ASP   A 1 93  ? 33.33209  8.54594   5.59041   1.000 41.18359  ? 92  ASP   A CA    1 
ATOM   745  C  C     . ASP   A 1 93  ? 32.67905  7.61288   6.59845   1.000 39.35435  ? 92  ASP   A C     1 
ATOM   746  O  O     . ASP   A 1 93  ? 32.82520  7.83235   7.80332   1.000 34.02661  ? 92  ASP   A O     1 
ATOM   747  C  CB    . ASP   A 1 93  ? 32.51535  9.83556   5.48755   1.000 38.96425  ? 92  ASP   A CB    1 
ATOM   748  C  CG    . ASP   A 1 93  ? 33.24287  10.93237  4.73754   1.000 45.17400  ? 92  ASP   A CG    1 
ATOM   749  O  OD1   . ASP   A 1 93  ? 34.43673  10.74416  4.40035   1.000 44.52073  ? 92  ASP   A OD1   1 
ATOM   750  O  OD2   . ASP   A 1 93  ? 32.62209  11.98736  4.47759   1.000 43.83487  ? 92  ASP   A OD2   1 
ATOM   751  N  N     . ILE   A 1 94  ? 31.97176  6.57962   6.13115   1.000 38.59998  ? 93  ILE   A N     1 
ATOM   752  C  CA    . ILE   A 1 94  ? 31.24762  5.68377   7.03323   1.000 38.42724  ? 93  ILE   A CA    1 
ATOM   753  C  C     . ILE   A 1 94  ? 32.20325  4.99861   7.99558   1.000 42.26027  ? 93  ILE   A C     1 
ATOM   754  O  O     . ILE   A 1 94  ? 31.91806  4.86402   9.19381   1.000 36.36637  ? 93  ILE   A O     1 
ATOM   755  C  CB    . ILE   A 1 94  ? 30.44219  4.65329   6.22006   1.000 37.79962  ? 93  ILE   A CB    1 
ATOM   756  C  CG1   . ILE   A 1 94  ? 29.10356  5.24948   5.81458   1.000 37.81422  ? 93  ILE   A CG1   1 
ATOM   757  C  CG2   . ILE   A 1 94  ? 30.23781  3.37913   7.02575   1.000 40.33537  ? 93  ILE   A CG2   1 
ATOM   758  C  CD1   . ILE   A 1 94  ? 28.29256  5.67546   7.01077   1.000 29.06011  ? 93  ILE   A CD1   1 
ATOM   759  N  N     . HIS   A 1 95  ? 33.34536  4.54361   7.47963   1.000 37.48495  ? 94  HIS   A N     1 
ATOM   760  C  CA    . HIS   A 1 95  ? 34.31541  3.83862   8.30281   1.000 41.24779  ? 94  HIS   A CA    1 
ATOM   761  C  C     . HIS   A 1 95  ? 34.70934  4.66099   9.51955   1.000 37.82443  ? 94  HIS   A C     1 
ATOM   762  O  O     . HIS   A 1 95  ? 34.74233  4.14442   10.64123  1.000 37.55598  ? 94  HIS   A O     1 
ATOM   763  C  CB    . HIS   A 1 95  ? 35.54343  3.49708   7.45976   1.000 48.65490  ? 94  HIS   A CB    1 
ATOM   764  C  CG    . HIS   A 1 95  ? 36.60907  2.77274   8.21494   1.000 53.74146  ? 94  HIS   A CG    1 
ATOM   765  N  ND1   . HIS   A 1 95  ? 37.68488  3.41799   8.78657   1.000 57.13446  ? 94  HIS   A ND1   1 
ATOM   766  C  CD2   . HIS   A 1 95  ? 36.76036  1.45831   8.50112   1.000 53.19747  ? 94  HIS   A CD2   1 
ATOM   767  C  CE1   . HIS   A 1 95  ? 38.45653  2.53103   9.38864   1.000 58.63462  ? 94  HIS   A CE1   1 
ATOM   768  N  NE2   . HIS   A 1 95  ? 37.91733  1.33487   9.23182   1.000 60.49721  ? 94  HIS   A NE2   1 
ATOM   769  N  N     . HIS   A 1 96  ? 34.99129  5.95024   9.32260   1.000 39.67680  ? 95  HIS   A N     1 
ATOM   770  C  CA    . HIS   A 1 96  ? 35.40017  6.79013   10.44216  1.000 38.89825  ? 95  HIS   A CA    1 
ATOM   771  C  C     . HIS   A 1 96  ? 34.28553  6.94148   11.46666  1.000 38.36724  ? 95  HIS   A C     1 
ATOM   772  O  O     . HIS   A 1 96  ? 34.55465  7.03326   12.67251  1.000 32.87984  ? 95  HIS   A O     1 
ATOM   773  C  CB    . HIS   A 1 96  ? 35.84728  8.15571   9.92797   1.000 46.54820  ? 95  HIS   A CB    1 
ATOM   774  C  CG    . HIS   A 1 96  ? 36.93486  8.08026   8.90126   1.000 53.93467  ? 95  HIS   A CG    1 
ATOM   775  N  ND1   . HIS   A 1 96  ? 38.24073  7.76525   9.22005   1.000 62.02637  ? 95  HIS   A ND1   1 
ATOM   776  C  CD2   . HIS   A 1 96  ? 36.90932  8.26412   7.55992   1.000 53.30189  ? 95  HIS   A CD2   1 
ATOM   777  C  CE1   . HIS   A 1 96  ? 38.97320  7.76695   8.12064   1.000 54.72306  ? 95  HIS   A CE1   1 
ATOM   778  N  NE2   . HIS   A 1 96  ? 38.19016  8.06731   7.09921   1.000 58.98681  ? 95  HIS   A NE2   1 
ATOM   779  N  N     . TYR   A 1 97  ? 33.02963  6.96602   11.01776  1.000 33.78975  ? 96  TYR   A N     1 
ATOM   780  C  CA    . TYR   A 1 97  ? 31.93376  7.02151   11.97848  1.000 30.77982  ? 96  TYR   A CA    1 
ATOM   781  C  C     . TYR   A 1 97  ? 31.86274  5.74416   12.78846  1.000 29.52081  ? 96  TYR   A C     1 
ATOM   782  O  O     . TYR   A 1 97  ? 31.68255  5.78508   14.01058  1.000 28.33884  ? 96  TYR   A O     1 
ATOM   783  C  CB    . TYR   A 1 97  ? 30.60817  7.29734   11.26640  1.000 30.25774  ? 96  TYR   A CB    1 
ATOM   784  C  CG    . TYR   A 1 97  ? 30.27501  8.76410   11.23087  1.000 24.73339  ? 96  TYR   A CG    1 
ATOM   785  C  CD1   . TYR   A 1 97  ? 29.73809  9.39754   12.34877  1.000 27.42980  ? 96  TYR   A CD1   1 
ATOM   786  C  CD2   . TYR   A 1 97  ? 30.50014  9.52222   10.09289  1.000 29.21288  ? 96  TYR   A CD2   1 
ATOM   787  C  CE1   . TYR   A 1 97  ? 29.44489  10.74282  12.32811  1.000 28.94999  ? 96  TYR   A CE1   1 
ATOM   788  C  CE2   . TYR   A 1 97  ? 30.20240  10.86910  10.06296  1.000 26.10461  ? 96  TYR   A CE2   1 
ATOM   789  C  CZ    . TYR   A 1 97  ? 29.66735  11.47137  11.18212  1.000 29.29446  ? 96  TYR   A CZ    1 
ATOM   790  O  OH    . TYR   A 1 97  ? 29.36985  12.81477  11.17372  1.000 32.64090  ? 96  TYR   A OH    1 
ATOM   791  N  N     . ARG   A 1 98  ? 32.02152  4.58539   12.14722  1.000 31.19015  ? 97  ARG   A N     1 
ATOM   792  C  CA    A ARG   A 1 98  ? 31.94042  3.33045   12.87195  0.500 33.26560  ? 97  ARG   A CA    1 
ATOM   793  C  CA    B ARG   A 1 98  ? 31.94864  3.32984   12.87307  0.500 33.26766  ? 97  ARG   A CA    1 
ATOM   794  C  C     . ARG   A 1 98  ? 33.10753  3.17975   13.85520  1.000 35.81893  ? 97  ARG   A C     1 
ATOM   795  O  O     . ARG   A 1 98  ? 32.92189  2.72809   14.98377  1.000 31.61580  ? 97  ARG   A O     1 
ATOM   796  C  CB    A ARG   A 1 98  ? 31.92199  2.14135   11.90789  0.500 37.23942  ? 97  ARG   A CB    1 
ATOM   797  C  CB    B ARG   A 1 98  ? 31.89630  2.14016   11.91572  0.500 37.24228  ? 97  ARG   A CB    1 
ATOM   798  C  CG    A ARG   A 1 98  ? 31.86697  0.80590   12.63328  0.500 40.22832  ? 97  ARG   A CG    1 
ATOM   799  C  CG    B ARG   A 1 98  ? 31.90730  0.81058   12.65985  0.500 40.23004  ? 97  ARG   A CG    1 
ATOM   800  C  CD    A ARG   A 1 98  ? 32.06907  -0.36795  11.69532  0.500 42.44078  ? 97  ARG   A CD    1 
ATOM   801  C  CD    B ARG   A 1 98  ? 31.79611  -0.37215  11.73091  0.500 42.44078  ? 97  ARG   A CD    1 
ATOM   802  N  NE    A ARG   A 1 98  ? 32.05809  -1.64963  12.39402  0.500 43.43740  ? 97  ARG   A NE    1 
ATOM   803  N  NE    B ARG   A 1 98  ? 31.74925  -1.64471  12.44517  0.500 43.74241  ? 97  ARG   A NE    1 
ATOM   804  C  CZ    A ARG   A 1 98  ? 33.13073  -2.39359  12.62650  0.500 47.75720  ? 97  ARG   A CZ    1 
ATOM   805  C  CZ    B ARG   A 1 98  ? 30.64943  -2.18068  12.96012  0.500 47.75720  ? 97  ARG   A CZ    1 
ATOM   806  N  NH1   A ARG   A 1 98  ? 34.33285  -2.01805  12.22494  0.500 41.64858  ? 97  ARG   A NH1   1 
ATOM   807  N  NH1   B ARG   A 1 98  ? 29.48058  -1.56678  12.88877  0.500 41.64858  ? 97  ARG   A NH1   1 
ATOM   808  N  NH2   A ARG   A 1 98  ? 32.99173  -3.54668  13.27393  0.500 52.36039  ? 97  ARG   A NH2   1 
ATOM   809  N  NH2   B ARG   A 1 98  ? 30.72554  -3.36243  13.56387  0.500 52.36039  ? 97  ARG   A NH2   1 
ATOM   810  N  N     . GLU   A 1 99  ? 34.31446  3.54129   13.41018  1.000 36.17325  ? 98  GLU   A N     1 
ATOM   811  C  CA    . GLU   A 1 99  ? 35.46155  3.45173   14.31551  1.000 35.61916  ? 98  GLU   A CA    1 
ATOM   812  C  C     . GLU   A 1 99  ? 35.28775  4.37293   15.51063  1.000 35.82088  ? 98  GLU   A C     1 
ATOM   813  O  O     . GLU   A 1 99  ? 35.60680  4.00532   16.64756  1.000 30.76569  ? 98  GLU   A O     1 
ATOM   814  C  CB    . GLU   A 1 99  ? 36.75976  3.78057   13.57394  1.000 41.55624  ? 98  GLU   A CB    1 
ATOM   815  C  CG    . GLU   A 1 99  ? 37.15699  2.71072   12.57024  1.000 40.49581  ? 98  GLU   A CG    1 
ATOM   816  C  CD    . GLU   A 1 99  ? 37.27349  1.33597   13.21160  1.000 49.09385  ? 98  GLU   A CD    1 
ATOM   817  O  OE1   . GLU   A 1 99  ? 37.73144  1.25118   14.37482  1.000 47.58350  ? 98  GLU   A OE1   1 
ATOM   818  O  OE2   . GLU   A 1 99  ? 36.89760  0.34155   12.55222  1.000 52.89647  ? 98  GLU   A OE2   1 
ATOM   819  N  N     . GLN   A 1 100 ? 34.75110  5.56686   15.27799  1.000 32.80977  ? 99  GLN   A N     1 
ATOM   820  C  CA    . GLN   A 1 100 ? 34.52594  6.49368   16.37659  1.000 33.55024  ? 99  GLN   A CA    1 
ATOM   821  C  C     . GLN   A 1 100 ? 33.48596  5.94465   17.34251  1.000 30.96835  ? 99  GLN   A C     1 
ATOM   822  O  O     . GLN   A 1 100 ? 33.65203  6.03701   18.55674  1.000 30.77049  ? 99  GLN   A O     1 
ATOM   823  C  CB    . GLN   A 1 100 ? 34.10936  7.85190   15.81433  1.000 36.82030  ? 99  GLN   A CB    1 
ATOM   824  C  CG    . GLN   A 1 100 ? 34.07822  9.01073   16.77666  1.000 34.93198  ? 99  GLN   A CG    1 
ATOM   825  C  CD    . GLN   A 1 100 ? 33.90422  10.33006  16.03389  1.000 42.21735  ? 99  GLN   A CD    1 
ATOM   826  O  OE1   . GLN   A 1 100 ? 33.29589  10.37756  14.95640  1.000 38.14033  ? 99  GLN   A OE1   1 
ATOM   827  N  NE2   . GLN   A 1 100 ? 34.45115  11.40346  16.59539  1.000 37.23489  ? 99  GLN   A NE2   1 
ATOM   828  N  N     . ILE   A 1 101 ? 32.41051  5.34258   16.82429  1.000 27.75337  ? 100 ILE   A N     1 
ATOM   829  C  CA    . ILE   A 1 101 ? 31.39685  4.77860   17.71303  1.000 24.46494  ? 100 ILE   A CA    1 
ATOM   830  C  C     . ILE   A 1 101 ? 31.97881  3.63627   18.53932  1.000 30.01004  ? 100 ILE   A C     1 
ATOM   831  O  O     . ILE   A 1 101 ? 31.78823  3.57354   19.75971  1.000 32.21390  ? 100 ILE   A O     1 
ATOM   832  C  CB    . ILE   A 1 101 ? 30.17428  4.31654   16.90593  1.000 27.57872  ? 100 ILE   A CB    1 
ATOM   833  C  CG1   . ILE   A 1 101 ? 29.53906  5.52617   16.23924  1.000 26.22409  ? 100 ILE   A CG1   1 
ATOM   834  C  CG2   . ILE   A 1 101 ? 29.19082  3.59813   17.81621  1.000 27.46285  ? 100 ILE   A CG2   1 
ATOM   835  C  CD1   . ILE   A 1 101 ? 28.56924  5.15452   15.10656  1.000 27.63096  ? 100 ILE   A CD1   1 
ATOM   836  N  N     . LYS   A 1 102 ? 32.67157  2.70101   17.87955  1.000 31.90986  ? 101 LYS   A N     1 
ATOM   837  C  CA    . LYS   A 1 102 ? 33.26126  1.57049   18.59522  1.000 37.42934  ? 101 LYS   A CA    1 
ATOM   838  C  C     . LYS   A 1 102 ? 34.25355  2.04078   19.64562  1.000 32.67382  ? 101 LYS   A C     1 
ATOM   839  O  O     . LYS   A 1 102 ? 34.27213  1.52118   20.76962  1.000 32.58960  ? 101 LYS   A O     1 
ATOM   840  C  CB    . LYS   A 1 102 ? 33.95187  0.61982   17.61957  1.000 35.95195  ? 101 LYS   A CB    1 
ATOM   841  C  CG    . LYS   A 1 102 ? 33.00193  -0.07638  16.66378  1.000 43.44566  ? 101 LYS   A CG    1 
ATOM   842  C  CD    . LYS   A 1 102 ? 33.64956  -1.28146  15.98446  1.000 49.69546  ? 101 LYS   A CD    1 
ATOM   843  C  CE    . LYS   A 1 102 ? 34.92640  -0.90652  15.26075  1.000 46.22211  ? 101 LYS   A CE    1 
ATOM   844  N  NZ    . LYS   A 1 102 ? 35.67314  -2.11401  14.80845  1.000 50.00742  ? 101 LYS   A NZ    1 
ATOM   845  N  N     . ARG   A 1 103 ? 35.08869  3.02006   19.29482  1.000 35.59769  ? 102 ARG   A N     1 
ATOM   846  C  CA    . ARG   A 1 103 ? 36.06510  3.54519   20.24606  1.000 37.02479  ? 102 ARG   A CA    1 
ATOM   847  C  C     . ARG   A 1 103 ? 35.37332  4.19171   21.43675  1.000 43.09736  ? 102 ARG   A C     1 
ATOM   848  O  O     . ARG   A 1 103 ? 35.71199  3.91672   22.59507  1.000 37.69547  ? 102 ARG   A O     1 
ATOM   849  C  CB    . ARG   A 1 103 ? 36.98647  4.54862   19.54819  1.000 44.50628  ? 102 ARG   A CB    1 
ATOM   850  C  CG    . ARG   A 1 103 ? 37.85998  5.34859   20.49463  1.000 48.13620  ? 102 ARG   A CG    1 
ATOM   851  C  CD    . ARG   A 1 103 ? 38.78518  6.30423   19.74588  1.000 54.20176  ? 102 ARG   A CD    1 
ATOM   852  N  NE    . ARG   A 1 103 ? 38.11042  7.52526   19.31477  1.000 52.48765  ? 102 ARG   A NE    1 
ATOM   853  C  CZ    . ARG   A 1 103 ? 37.97152  7.90543   18.05085  1.000 53.34177  ? 102 ARG   A CZ    1 
ATOM   854  N  NH1   . ARG   A 1 103 ? 38.45422  7.18179   17.05204  1.000 52.50391  ? 102 ARG   A NH1   1 
ATOM   855  N  NH2   . ARG   A 1 103 ? 37.33559  9.04328   17.78273  1.000 55.18983  ? 102 ARG   A NH2   1 
ATOM   856  N  N     . VAL   A 1 104 ? 34.39149  5.05639   21.16896  1.000 38.46343  ? 103 VAL   A N     1 
ATOM   857  C  CA    . VAL   A 1 104 ? 33.75289  5.80155   22.24516  1.000 36.22951  ? 103 VAL   A CA    1 
ATOM   858  C  C     . VAL   A 1 104 ? 33.00138  4.86421   23.17894  1.000 34.26611  ? 103 VAL   A C     1 
ATOM   859  O  O     . VAL   A 1 104 ? 33.03178  5.03565   24.40215  1.000 37.64347  ? 103 VAL   A O     1 
ATOM   860  C  CB    . VAL   A 1 104 ? 32.83783  6.88915   21.65644  1.000 36.43479  ? 103 VAL   A CB    1 
ATOM   861  C  CG1   . VAL   A 1 104 ? 31.91958  7.43032   22.71679  1.000 32.76363  ? 103 VAL   A CG1   1 
ATOM   862  C  CG2   . VAL   A 1 104 ? 33.68208  8.00180   21.04201  1.000 37.88431  ? 103 VAL   A CG2   1 
ATOM   863  N  N     . LYS   A 1 105 ? 32.32865  3.85386   22.63079  1.000 34.27891  ? 104 LYS   A N     1 
ATOM   864  C  CA    . LYS   A 1 105 ? 31.58858  2.89285   23.43981  1.000 36.69052  ? 104 LYS   A CA    1 
ATOM   865  C  C     . LYS   A 1 105 ? 32.44271  1.70647   23.87207  1.000 37.12961  ? 104 LYS   A C     1 
ATOM   866  O  O     . LYS   A 1 105 ? 31.94837  0.83763   24.59717  1.000 40.65109  ? 104 LYS   A O     1 
ATOM   867  C  CB    . LYS   A 1 105 ? 30.34459  2.40209   22.68074  1.000 38.63513  ? 104 LYS   A CB    1 
ATOM   868  C  CG    . LYS   A 1 105 ? 29.38800  3.54313   22.30277  1.000 41.81503  ? 104 LYS   A CG    1 
ATOM   869  C  CD    . LYS   A 1 105 ? 28.05475  3.07010   21.72085  1.000 34.87131  ? 104 LYS   A CD    1 
ATOM   870  C  CE    . LYS   A 1 105 ? 27.03211  2.67650   22.78627  1.000 34.67932  ? 104 LYS   A CE    1 
ATOM   871  N  NZ    . LYS   A 1 105 ? 26.54550  3.81392   23.62490  1.000 31.55781  ? 104 LYS   A NZ    1 
ATOM   872  N  N     . ASP   A 1 106 ? 33.70573  1.66135   23.44681  1.000 39.70887  ? 105 ASP   A N     1 
ATOM   873  C  CA    . ASP   A 1 106 ? 34.66247  0.63130   23.85836  1.000 41.51610  ? 105 ASP   A CA    1 
ATOM   874  C  C     . ASP   A 1 106 ? 34.06148  -0.76769  23.73841  1.000 44.28241  ? 105 ASP   A C     1 
ATOM   875  O  O     . ASP   A 1 106 ? 34.04992  -1.55591  24.68812  1.000 40.30175  ? 105 ASP   A O     1 
ATOM   876  C  CB    . ASP   A 1 106 ? 35.16618  0.89242   25.27748  1.000 43.03607  ? 105 ASP   A CB    1 
ATOM   877  C  CG    . ASP   A 1 106 ? 36.47716  0.17470   25.57009  1.000 49.48069  ? 105 ASP   A CG    1 
ATOM   878  O  OD1   . ASP   A 1 106 ? 37.18115  -0.21065  24.61009  1.000 42.59343  ? 105 ASP   A OD1   1 
ATOM   879  O  OD2   . ASP   A 1 106 ? 36.79150  -0.00851  26.76135  1.000 53.95735  ? 105 ASP   A OD2   1 
ATOM   880  N  N     . SER   A 1 107 ? 33.55173  -1.07210  22.54701  1.000 36.77694  ? 106 SER   A N     1 
ATOM   881  C  CA    . SER   A 1 107 ? 32.86530  -2.33002  22.31984  1.000 37.35333  ? 106 SER   A CA    1 
ATOM   882  C  C     . SER   A 1 107 ? 32.85522  -2.63177  20.83146  1.000 44.63965  ? 106 SER   A C     1 
ATOM   883  O  O     . SER   A 1 107 ? 32.76034  -1.72019  20.00373  1.000 41.39855  ? 106 SER   A O     1 
ATOM   884  C  CB    . SER   A 1 107 ? 31.42983  -2.28513  22.85398  1.000 40.88950  ? 106 SER   A CB    1 
ATOM   885  O  OG    . SER   A 1 107 ? 30.73674  -3.48159  22.55655  1.000 40.96031  ? 106 SER   A OG    1 
ATOM   886  N  N     . GLU   A 1 108 ? 32.95474  -3.91697  20.50802  1.000 48.77519  ? 107 GLU   A N     1 
ATOM   887  C  CA    . GLU   A 1 108 ? 32.80505  -4.41832  19.15113  1.000 48.96250  ? 107 GLU   A CA    1 
ATOM   888  C  C     . GLU   A 1 108 ? 31.36280  -4.76040  18.82805  1.000 49.44642  ? 107 GLU   A C     1 
ATOM   889  O  O     . GLU   A 1 108 ? 31.05853  -5.13054  17.68918  1.000 53.03094  ? 107 GLU   A O     1 
ATOM   890  C  CB    . GLU   A 1 108 ? 33.68180  -5.65814  18.95493  1.000 53.34730  ? 107 GLU   A CB    1 
ATOM   891  C  CG    . GLU   A 1 108 ? 35.16458  -5.37544  19.04748  1.000 53.27658  ? 107 GLU   A CG    1 
ATOM   892  C  CD    . GLU   A 1 108 ? 35.68215  -4.64444  17.83024  1.000 56.34492  ? 107 GLU   A CD    1 
ATOM   893  O  OE1   . GLU   A 1 108 ? 35.22772  -4.96451  16.71328  1.000 61.86734  ? 107 GLU   A OE1   1 
ATOM   894  O  OE2   . GLU   A 1 108 ? 36.53351  -3.74574  17.98827  1.000 57.24255  ? 107 GLU   A OE2   1 
ATOM   895  N  N     . ASP   A 1 109 ? 30.47547  -4.64222  19.80213  1.000 47.71126  ? 108 ASP   A N     1 
ATOM   896  C  CA    . ASP   A 1 109 ? 29.11175  -5.12712  19.69341  1.000 51.03452  ? 108 ASP   A CA    1 
ATOM   897  C  C     . ASP   A 1 109 ? 28.16200  -3.95538  19.92978  1.000 50.30747  ? 108 ASP   A C     1 
ATOM   898  O  O     . ASP   A 1 109 ? 27.45888  -3.90902  20.94534  1.000 48.80175  ? 108 ASP   A O     1 
ATOM   899  C  CB    . ASP   A 1 109 ? 28.89092  -6.25836  20.69297  1.000 53.80755  ? 108 ASP   A CB    1 
ATOM   900  C  CG    . ASP   A 1 109 ? 27.53850  -6.90727  20.54725  1.000 63.64667  ? 108 ASP   A CG    1 
ATOM   901  O  OD1   . ASP   A 1 109 ? 26.85243  -6.62852  19.54259  1.000 61.09671  ? 108 ASP   A OD1   1 
ATOM   902  O  OD2   . ASP   A 1 109 ? 27.16194  -7.69402  21.44192  1.000 70.82232  ? 108 ASP   A OD2   1 
ATOM   903  N  N     . VAL   A 1 110 ? 28.15526  -3.00134  19.00555  1.000 40.81355  ? 109 VAL   A N     1 
ATOM   904  C  CA    . VAL   A 1 110 ? 27.25742  -1.85319  19.07471  1.000 38.43419  ? 109 VAL   A CA    1 
ATOM   905  C  C     . VAL   A 1 110 ? 26.20160  -2.01230  17.97908  1.000 31.27140  ? 109 VAL   A C     1 
ATOM   906  O  O     . VAL   A 1 110 ? 26.56794  -2.15913  16.81403  1.000 29.82790  ? 109 VAL   A O     1 
ATOM   907  C  CB    . VAL   A 1 110 ? 27.99926  -0.52053  18.90979  1.000 30.49224  ? 109 VAL   A CB    1 
ATOM   908  C  CG1   . VAL   A 1 110 ? 27.01703  0.63581   19.10669  1.000 28.32158  ? 109 VAL   A CG1   1 
ATOM   909  C  CG2   . VAL   A 1 110 ? 29.14276  -0.42667  19.90113  1.000 31.66317  ? 109 VAL   A CG2   1 
ATOM   910  N  N     . PRO   A 1 111 ? 24.91164  -1.97797  18.31014  1.000 29.16287  ? 110 PRO   A N     1 
ATOM   911  C  CA    . PRO   A 1 111 ? 23.86278  -2.04466  17.27011  1.000 29.88920  ? 110 PRO   A CA    1 
ATOM   912  C  C     . PRO   A 1 111 ? 24.00815  -0.93121  16.24263  1.000 28.68453  ? 110 PRO   A C     1 
ATOM   913  O  O     . PRO   A 1 111 ? 24.05427  0.25364   16.58115  1.000 26.57365  ? 110 PRO   A O     1 
ATOM   914  C  CB    . PRO   A 1 111 ? 22.56901  -1.90601  18.07662  1.000 32.65931  ? 110 PRO   A CB    1 
ATOM   915  C  CG    . PRO   A 1 111 ? 22.94681  -2.37063  19.45720  1.000 34.64883  ? 110 PRO   A CG    1 
ATOM   916  C  CD    . PRO   A 1 111 ? 24.34258  -1.91229  19.66495  1.000 32.39484  ? 110 PRO   A CD    1 
ATOM   917  N  N     . MET   A 1 112 ? 24.10801  -1.32473  14.97546  1.000 29.42522  ? 111 MET   A N     1 
ATOM   918  C  CA    . MET   A 1 112 ? 24.21532  -0.37594  13.87939  1.000 27.23286  ? 111 MET   A CA    1 
ATOM   919  C  C     . MET   A 1 112 ? 23.53988  -0.96448  12.65323  1.000 27.89817  ? 111 MET   A C     1 
ATOM   920  O  O     . MET   A 1 112 ? 23.37343  -2.17959  12.52862  1.000 29.18229  ? 111 MET   A O     1 
ATOM   921  C  CB    . MET   A 1 112 ? 25.66794  -0.03040  13.49738  1.000 27.61294  ? 111 MET   A CB    1 
ATOM   922  C  CG    . MET   A 1 112 ? 26.59685  0.37860   14.61552  1.000 30.98560  ? 111 MET   A CG    1 
ATOM   923  S  SD    . MET   A 1 112 ? 28.14534  0.93155   13.87838  1.000 33.28970  ? 111 MET   A SD    1 
ATOM   924  C  CE    . MET   A 1 112 ? 29.15085  1.03871   15.37622  1.000 33.01087  ? 111 MET   A CE    1 
ATOM   925  N  N     . VAL   A 1 113 ? 23.16887  -0.07674  11.73954  1.000 23.78128  ? 112 VAL   A N     1 
ATOM   926  C  CA    . VAL   A 1 113 ? 22.63084  -0.45376  10.43724  1.000 26.88670  ? 112 VAL   A CA    1 
ATOM   927  C  C     . VAL   A 1 113 ? 23.26856  0.45442   9.41023   1.000 24.55076  ? 112 VAL   A C     1 
ATOM   928  O  O     . VAL   A 1 113 ? 23.30068  1.67579   9.59227   1.000 25.23940  ? 112 VAL   A O     1 
ATOM   929  C  CB    . VAL   A 1 113 ? 21.09430  -0.33595  10.37271  1.000 22.86091  ? 112 VAL   A CB    1 
ATOM   930  C  CG1   . VAL   A 1 113 ? 20.61165  -0.54287  8.95731   1.000 24.94559  ? 112 VAL   A CG1   1 
ATOM   931  C  CG2   . VAL   A 1 113 ? 20.45410  -1.33736  11.29216  1.000 25.18733  ? 112 VAL   A CG2   1 
ATOM   932  N  N     . LEU   A 1 114 ? 23.81401  -0.13480  8.35418   1.000 24.24288  ? 113 LEU   A N     1 
ATOM   933  C  CA    . LEU   A 1 114 ? 24.35938  0.63551   7.25373   1.000 25.03924  ? 113 LEU   A CA    1 
ATOM   934  C  C     . LEU   A 1 114 ? 23.22637  0.94508   6.29118   1.000 25.87675  ? 113 LEU   A C     1 
ATOM   935  O  O     . LEU   A 1 114 ? 22.48641  0.04491   5.89882   1.000 27.24332  ? 113 LEU   A O     1 
ATOM   936  C  CB    . LEU   A 1 114 ? 25.46762  -0.13320  6.53920   1.000 30.63969  ? 113 LEU   A CB    1 
ATOM   937  C  CG    . LEU   A 1 114 ? 26.11112  0.59526   5.35788   1.000 30.21609  ? 113 LEU   A CG    1 
ATOM   938  C  CD1   . LEU   A 1 114 ? 26.91598  1.80230   5.82542   1.000 28.67167  ? 113 LEU   A CD1   1 
ATOM   939  C  CD2   . LEU   A 1 114 ? 27.00357  -0.35374  4.55590   1.000 32.22771  ? 113 LEU   A CD2   1 
ATOM   940  N  N     . VAL   A 1 115 ? 23.08657  2.21562   5.93900   1.000 25.75505  ? 114 VAL   A N     1 
ATOM   941  C  CA    . VAL   A 1 115 ? 21.97468  2.69784   5.13324   1.000 24.90046  ? 114 VAL   A CA    1 
ATOM   942  C  C     . VAL   A 1 115 ? 22.56341  3.38791   3.91443   1.000 27.33454  ? 114 VAL   A C     1 
ATOM   943  O  O     . VAL   A 1 115 ? 23.32577  4.35137   4.04363   1.000 26.86943  ? 114 VAL   A O     1 
ATOM   944  C  CB    . VAL   A 1 115 ? 21.04989  3.64374   5.92275   1.000 24.07142  ? 114 VAL   A CB    1 
ATOM   945  C  CG1   . VAL   A 1 115 ? 19.99741  4.27602   4.98284   1.000 23.46475  ? 114 VAL   A CG1   1 
ATOM   946  C  CG2   . VAL   A 1 115 ? 20.36337  2.88610   7.03280   1.000 23.82115  ? 114 VAL   A CG2   1 
ATOM   947  N  N     . GLY   A 1 116 ? 22.22546  2.88966   2.73690   1.000 25.52985  ? 115 GLY   A N     1 
ATOM   948  C  CA    . GLY   A 1 116 ? 22.60160  3.57810   1.52249   1.000 27.14131  ? 115 GLY   A CA    1 
ATOM   949  C  C     . GLY   A 1 116 ? 21.39513  4.33066   1.00542   1.000 23.57799  ? 115 GLY   A C     1 
ATOM   950  O  O     . GLY   A 1 116 ? 20.46301  3.70263   0.50838   1.000 28.56169  ? 115 GLY   A O     1 
ATOM   951  N  N     . ASN   A 1 117 ? 21.40153  5.65367   1.13337   1.000 22.53965  ? 116 ASN   A N     1 
ATOM   952  C  CA    . ASN   A 1 117 ? 20.25283  6.49264   0.83968   1.000 26.28080  ? 116 ASN   A CA    1 
ATOM   953  C  C     . ASN   A 1 117 ? 20.34480  7.06879   -0.56999  1.000 27.66090  ? 116 ASN   A C     1 
ATOM   954  O  O     . ASN   A 1 117 ? 21.38833  7.01530   -1.22563  1.000 30.47675  ? 116 ASN   A O     1 
ATOM   955  C  CB    . ASN   A 1 117 ? 20.13668  7.62444   1.86510   1.000 24.64227  ? 116 ASN   A CB    1 
ATOM   956  C  CG    . ASN   A 1 117 ? 18.81916  8.36532   1.74859   1.000 24.01078  ? 116 ASN   A CG    1 
ATOM   957  O  OD1   . ASN   A 1 117 ? 17.76899  7.73557   1.60911   1.000 25.06801  ? 116 ASN   A OD1   1 
ATOM   958  N  ND2   . ASN   A 1 117 ? 18.86643  9.69296   1.78414   1.000 23.48821  ? 116 ASN   A ND2   1 
ATOM   959  N  N     . LYS   A 1 118 ? 19.21448  7.62032   -1.03015  1.000 30.24688  ? 117 LYS   A N     1 
ATOM   960  C  CA    . LYS   A 1 118 ? 19.06448  8.25469   -2.33985  1.000 23.78304  ? 117 LYS   A CA    1 
ATOM   961  C  C     . LYS   A 1 118 ? 19.02847  7.22296   -3.45852  1.000 28.08518  ? 117 LYS   A C     1 
ATOM   962  O  O     . LYS   A 1 118 ? 19.47535  7.49445   -4.57290  1.000 30.54653  ? 117 LYS   A O     1 
ATOM   963  C  CB    . LYS   A 1 118 ? 20.15757  9.29684   -2.62065  1.000 24.95639  ? 117 LYS   A CB    1 
ATOM   964  C  CG    . LYS   A 1 118 ? 20.40251  10.30428  -1.51203  1.000 25.12301  ? 117 LYS   A CG    1 
ATOM   965  C  CD    . LYS   A 1 118 ? 20.93802  11.61875  -2.04786  1.000 24.76005  ? 117 LYS   A CD    1 
ATOM   966  C  CE    . LYS   A 1 118 ? 21.15809  12.63824  -0.92594  1.000 27.12126  ? 117 LYS   A CE    1 
ATOM   967  N  NZ    . LYS   A 1 118 ? 22.08583  13.76741  -1.29921  1.000 27.81287  ? 117 LYS   A NZ    1 
ATOM   968  N  N     . CYS   A 1 119 ? 18.50357  6.03095   -3.17974  1.000 30.25484  ? 118 CYS   A N     1 
ATOM   969  C  CA    . CYS   A 1 119 ? 18.50756  5.00444   -4.21290  1.000 30.87623  ? 118 CYS   A CA    1 
ATOM   970  C  C     . CYS   A 1 119 ? 17.50587  5.28595   -5.32011  1.000 36.52703  ? 118 CYS   A C     1 
ATOM   971  O  O     . CYS   A 1 119 ? 17.45094  4.52501   -6.29148  1.000 37.64921  ? 118 CYS   A O     1 
ATOM   972  C  CB    . CYS   A 1 119 ? 18.24412  3.63115   -3.60313  1.000 32.50538  ? 118 CYS   A CB    1 
ATOM   973  S  SG    . CYS   A 1 119 ? 16.57876  3.38093   -3.02625  1.000 46.53701  ? 118 CYS   A SG    1 
ATOM   974  N  N     . ASP   A 1 120 ? 16.72153  6.35529   -5.20405  1.000 32.31482  ? 119 ASP   A N     1 
ATOM   975  C  CA    . ASP   A 1 120 ? 15.89813  6.80631   -6.31920  1.000 39.26697  ? 119 ASP   A CA    1 
ATOM   976  C  C     . ASP   A 1 120 ? 16.71117  7.44914   -7.43647  1.000 37.92755  ? 119 ASP   A C     1 
ATOM   977  O  O     . ASP   A 1 120 ? 16.15840  7.68795   -8.51787  1.000 40.59571  ? 119 ASP   A O     1 
ATOM   978  C  CB    . ASP   A 1 120 ? 14.87220  7.81959   -5.82995  1.000 33.11598  ? 119 ASP   A CB    1 
ATOM   979  C  CG    . ASP   A 1 120 ? 15.52587  9.02082   -5.20614  1.000 34.79538  ? 119 ASP   A CG    1 
ATOM   980  O  OD1   . ASP   A 1 120 ? 16.07696  8.85696   -4.08442  1.000 30.45525  ? 119 ASP   A OD1   1 
ATOM   981  O  OD2   . ASP   A 1 120 ? 15.52359  10.10960  -5.83529  1.000 32.58776  ? 119 ASP   A OD2   1 
ATOM   982  N  N     . LEU   A 1 121 ? 17.98826  7.75555   -7.20085  1.000 36.20056  ? 120 LEU   A N     1 
ATOM   983  C  CA    . LEU   A 1 121 ? 18.77320  8.58723   -8.11081  1.000 46.37089  ? 120 LEU   A CA    1 
ATOM   984  C  C     . LEU   A 1 121 ? 19.54057  7.72977   -9.11522  1.000 42.91452  ? 120 LEU   A C     1 
ATOM   985  O  O     . LEU   A 1 121 ? 20.04798  6.66168   -8.76273  1.000 45.40955  ? 120 LEU   A O     1 
ATOM   986  C  CB    . LEU   A 1 121 ? 19.75901  9.46510   -7.33819  1.000 38.56458  ? 120 LEU   A CB    1 
ATOM   987  C  CG    . LEU   A 1 121 ? 19.18460  10.72288  -6.67930  1.000 38.37923  ? 120 LEU   A CG    1 
ATOM   988  C  CD1   . LEU   A 1 121 ? 20.27583  11.53314  -6.01150  1.000 34.87145  ? 120 LEU   A CD1   1 
ATOM   989  C  CD2   . LEU   A 1 121 ? 18.43130  11.57520  -7.68994  1.000 38.59690  ? 120 LEU   A CD2   1 
ATOM   990  N  N     . PRO   A 1 122 ? 19.65479  8.19749   -10.36235 1.000 55.46976  ? 121 PRO   A N     1 
ATOM   991  C  CA    . PRO   A 1 122 ? 20.29391  7.37982   -11.40548 1.000 58.67522  ? 121 PRO   A CA    1 
ATOM   992  C  C     . PRO   A 1 122 ? 21.81541  7.36826   -11.35679 1.000 61.86097  ? 121 PRO   A C     1 
ATOM   993  O  O     . PRO   A 1 122 ? 22.42789  6.47301   -11.95725 1.000 60.84677  ? 121 PRO   A O     1 
ATOM   994  C  CB    . PRO   A 1 122 ? 19.79797  8.03453   -12.70127 1.000 59.53639  ? 121 PRO   A CB    1 
ATOM   995  C  CG    . PRO   A 1 122 ? 19.62015  9.48090   -12.32525 1.000 57.66323  ? 121 PRO   A CG    1 
ATOM   996  C  CD    . PRO   A 1 122 ? 19.17871  9.49526   -10.87927 1.000 50.38882  ? 121 PRO   A CD    1 
ATOM   997  N  N     . SER   A 1 123 ? 22.43969  8.31474   -10.66194 1.000 59.82707  ? 122 SER   A N     1 
ATOM   998  C  CA    . SER   A 1 123 ? 23.88982  8.50590   -10.71891 1.000 64.66894  ? 122 SER   A CA    1 
ATOM   999  C  C     . SER   A 1 123 ? 24.62646  7.71306   -9.64199  1.000 62.49845  ? 122 SER   A C     1 
ATOM   1000 O  O     . SER   A 1 123 ? 25.49036  8.24197   -8.94915  1.000 63.62226  ? 122 SER   A O     1 
ATOM   1001 C  CB    . SER   A 1 123 ? 24.20706  9.99192   -10.61018 1.000 69.89282  ? 122 SER   A CB    1 
ATOM   1002 O  OG    . SER   A 1 123 ? 23.63472  10.54760  -9.43626  1.000 64.01459  ? 122 SER   A OG    1 
ATOM   1003 N  N     . ARG   A 1 124 ? 24.30994  6.42761   -9.51647  1.000 54.22918  ? 123 ARG   A N     1 
ATOM   1004 C  CA    . ARG   A 1 124 ? 24.88607  5.60472   -8.46097  1.000 49.50191  ? 123 ARG   A CA    1 
ATOM   1005 C  C     . ARG   A 1 124 ? 26.37414  5.36209   -8.69770  1.000 54.97503  ? 123 ARG   A C     1 
ATOM   1006 O  O     . ARG   A 1 124 ? 26.77539  4.89325   -9.76789  1.000 54.62088  ? 123 ARG   A O     1 
ATOM   1007 C  CB    . ARG   A 1 124 ? 24.14396  4.27501   -8.38010  1.000 51.93537  ? 123 ARG   A CB    1 
ATOM   1008 C  CG    . ARG   A 1 124 ? 24.91455  3.19447   -7.66626  1.000 50.96440  ? 123 ARG   A CG    1 
ATOM   1009 C  CD    . ARG   A 1 124 ? 24.23911  1.85344   -7.81244  1.000 50.97874  ? 123 ARG   A CD    1 
ATOM   1010 N  NE    . ARG   A 1 124 ? 22.92641  1.83366   -7.18188  1.000 56.70347  ? 123 ARG   A NE    1 
ATOM   1011 C  CZ    . ARG   A 1 124 ? 22.70577  1.53220   -5.90773  1.000 56.07340  ? 123 ARG   A CZ    1 
ATOM   1012 N  NH1   . ARG   A 1 124 ? 23.69896  1.25997   -5.07674  1.000 51.29274  ? 123 ARG   A NH1   1 
ATOM   1013 N  NH2   . ARG   A 1 124 ? 21.45617  1.49965   -5.45760  1.000 48.83891  ? 123 ARG   A NH2   1 
ATOM   1014 N  N     . THR   A 1 125 ? 27.19495  5.67743   -7.68946  1.000 45.36783  ? 124 THR   A N     1 
ATOM   1015 C  CA    . THR   A 1 125 ? 28.63064  5.42513   -7.73474  1.000 46.97290  ? 124 THR   A CA    1 
ATOM   1016 C  C     . THR   A 1 125 ? 29.09907  4.38506   -6.72518  1.000 48.59227  ? 124 THR   A C     1 
ATOM   1017 O  O     . THR   A 1 125 ? 30.27188  4.00153   -6.75925  1.000 45.08720  ? 124 THR   A O     1 
ATOM   1018 C  CB    . THR   A 1 125 ? 29.41785  6.72699   -7.50849  1.000 51.91037  ? 124 THR   A CB    1 
ATOM   1019 O  OG1   . THR   A 1 125 ? 29.12781  7.25471   -6.20642  1.000 43.51459  ? 124 THR   A OG1   1 
ATOM   1020 C  CG2   . THR   A 1 125 ? 29.04690  7.75995   -8.55408  1.000 53.38946  ? 124 THR   A CG2   1 
ATOM   1021 N  N     . VAL   A 1 126 ? 28.22655  3.92800   -5.83032  1.000 44.08834  ? 125 VAL   A N     1 
ATOM   1022 C  CA    . VAL   A 1 126 ? 28.52379  2.85420   -4.88898  1.000 44.74632  ? 125 VAL   A CA    1 
ATOM   1023 C  C     . VAL   A 1 126 ? 27.58232  1.69713   -5.19915  1.000 48.34938  ? 125 VAL   A C     1 
ATOM   1024 O  O     . VAL   A 1 126 ? 26.35701  1.84631   -5.10594  1.000 43.74620  ? 125 VAL   A O     1 
ATOM   1025 C  CB    . VAL   A 1 126 ? 28.37077  3.31429   -3.42707  1.000 40.36684  ? 125 VAL   A CB    1 
ATOM   1026 C  CG1   . VAL   A 1 126 ? 28.70404  2.17230   -2.47588  1.000 41.94861  ? 125 VAL   A CG1   1 
ATOM   1027 C  CG2   . VAL   A 1 126 ? 29.24183  4.53351   -3.15639  1.000 37.92181  ? 125 VAL   A CG2   1 
ATOM   1028 N  N     . ASP   A 1 127 ? 28.14865  0.55128   -5.57084  1.000 49.52321  ? 126 ASP   A N     1 
ATOM   1029 C  CA    . ASP   A 1 127 ? 27.32906  -0.59507  -5.92567  1.000 51.35237  ? 126 ASP   A CA    1 
ATOM   1030 C  C     . ASP   A 1 127 ? 26.71867  -1.22337  -4.68605  1.000 48.92043  ? 126 ASP   A C     1 
ATOM   1031 O  O     . ASP   A 1 127 ? 27.22752  -1.09802  -3.56631  1.000 49.00999  ? 126 ASP   A O     1 
ATOM   1032 C  CB    . ASP   A 1 127 ? 28.14436  -1.66258  -6.64665  1.000 56.93113  ? 126 ASP   A CB    1 
ATOM   1033 C  CG    . ASP   A 1 127 ? 29.45769  -1.15366  -7.09557  1.000 63.18959  ? 126 ASP   A CG    1 
ATOM   1034 O  OD1   . ASP   A 1 127 ? 29.45386  -0.11668  -7.81194  1.000 74.18919  ? 126 ASP   A OD1   1 
ATOM   1035 O  OD2   . ASP   A 1 127 ? 30.50192  -1.75651  -6.72345  1.000 74.27900  ? 126 ASP   A OD2   1 
ATOM   1036 N  N     . THR   A 1 128 ? 25.62600  -1.94927  -4.91979  1.000 47.33675  ? 127 THR   A N     1 
ATOM   1037 C  CA    . THR   A 1 128 ? 24.97861  -2.69352  -3.85015  1.000 51.61011  ? 127 THR   A CA    1 
ATOM   1038 C  C     . THR   A 1 128 ? 25.92739  -3.71728  -3.24270  1.000 53.59193  ? 127 THR   A C     1 
ATOM   1039 O  O     . THR   A 1 128 ? 25.99644  -3.85495  -2.01638  1.000 46.73495  ? 127 THR   A O     1 
ATOM   1040 C  CB    . THR   A 1 128 ? 23.71130  -3.36082  -4.38621  1.000 52.79795  ? 127 THR   A CB    1 
ATOM   1041 O  OG1   . THR   A 1 128 ? 22.80420  -2.34517  -4.83141  1.000 52.96564  ? 127 THR   A OG1   1 
ATOM   1042 C  CG2   . THR   A 1 128 ? 23.03646  -4.19494  -3.32544  1.000 52.57578  ? 127 THR   A CG2   1 
ATOM   1043 N  N     . LYS   A 1 129 ? 26.67504  -4.44149  -4.08202  1.000 53.25067  ? 128 LYS   A N     1 
ATOM   1044 C  CA    . LYS   A 1 129 ? 27.60824  -5.43299  -3.55266  1.000 55.73239  ? 128 LYS   A CA    1 
ATOM   1045 C  C     . LYS   A 1 129 ? 28.70205  -4.76842  -2.72846  1.000 47.78418  ? 128 LYS   A C     1 
ATOM   1046 O  O     . LYS   A 1 129 ? 29.13772  -5.30764  -1.70366  1.000 49.49440  ? 128 LYS   A O     1 
ATOM   1047 C  CB    . LYS   A 1 129 ? 28.21728  -6.24850  -4.69446  1.000 59.03789  ? 128 LYS   A CB    1 
ATOM   1048 C  CG    . LYS   A 1 129 ? 27.21019  -7.10780  -5.44482  1.000 65.82849  ? 128 LYS   A CG    1 
ATOM   1049 C  CD    . LYS   A 1 129 ? 27.85891  -7.83652  -6.62020  1.000 70.10109  ? 128 LYS   A CD    1 
ATOM   1050 C  CE    . LYS   A 1 129 ? 26.86896  -8.77210  -7.30408  1.000 69.77822  ? 128 LYS   A CE    1 
ATOM   1051 N  NZ    . LYS   A 1 129 ? 27.49411  -9.51103  -8.43788  1.000 72.23048  ? 128 LYS   A NZ    1 
ATOM   1052 N  N     . GLN   A 1 130 ? 29.14957  -3.59169  -3.16315  1.000 48.82839  ? 129 GLN   A N     1 
ATOM   1053 C  CA    . GLN   A 1 130 ? 30.16974  -2.84902  -2.43547  1.000 44.97266  ? 129 GLN   A CA    1 
ATOM   1054 C  C     . GLN   A 1 130 ? 29.73151  -2.57921  -1.00340  1.000 47.21821  ? 129 GLN   A C     1 
ATOM   1055 O  O     . GLN   A 1 130 ? 30.49254  -2.79131  -0.05179  1.000 40.93834  ? 129 GLN   A O     1 
ATOM   1056 C  CB    . GLN   A 1 130 ? 30.44272  -1.54321  -3.17106  1.000 50.36278  ? 129 GLN   A CB    1 
ATOM   1057 C  CG    . GLN   A 1 130 ? 31.79613  -0.93053  -2.94748  1.000 54.36063  ? 129 GLN   A CG    1 
ATOM   1058 C  CD    . GLN   A 1 130 ? 32.02923  0.22274   -3.89777  1.000 57.49258  ? 129 GLN   A CD    1 
ATOM   1059 O  OE1   . GLN   A 1 130 ? 31.51537  0.22891   -5.01968  1.000 58.33479  ? 129 GLN   A OE1   1 
ATOM   1060 N  NE2   . GLN   A 1 130 ? 32.79029  1.21384   -3.45250  1.000 58.19751  ? 129 GLN   A NE2   1 
ATOM   1061 N  N     . ALA   A 1 131 ? 28.49375  -2.11853  -0.83283  1.000 44.67949  ? 130 ALA   A N     1 
ATOM   1062 C  CA    . ALA   A 1 131 ? 27.99754  -1.81633  0.50222   1.000 39.07840  ? 130 ALA   A CA    1 
ATOM   1063 C  C     . ALA   A 1 131 ? 27.63341  -3.08554  1.25722   1.000 40.04049  ? 130 ALA   A C     1 
ATOM   1064 O  O     . ALA   A 1 131 ? 27.85681  -3.17540  2.46789   1.000 37.10109  ? 130 ALA   A O     1 
ATOM   1065 C  CB    . ALA   A 1 131 ? 26.79965  -0.87965  0.40169   1.000 36.73082  ? 130 ALA   A CB    1 
ATOM   1066 N  N     . GLN   A 1 132 ? 27.06613  -4.07718  0.56400   1.000 40.80111  ? 131 GLN   A N     1 
ATOM   1067 C  CA    . GLN   A 1 132 ? 26.75840  -5.34332  1.22174   1.000 47.30239  ? 131 GLN   A CA    1 
ATOM   1068 C  C     . GLN   A 1 132 ? 28.02066  -5.98786  1.77847   1.000 46.70386  ? 131 GLN   A C     1 
ATOM   1069 O  O     . GLN   A 1 132 ? 28.00788  -6.53996  2.88412   1.000 49.27687  ? 131 GLN   A O     1 
ATOM   1070 C  CB    . GLN   A 1 132 ? 26.05355  -6.29482  0.25159   1.000 51.33785  ? 131 GLN   A CB    1 
ATOM   1071 C  CG    . GLN   A 1 132 ? 24.58242  -5.98236  0.01177   1.000 49.11950  ? 131 GLN   A CG    1 
ATOM   1072 C  CD    . GLN   A 1 132 ? 23.94398  -6.89495  -1.02857  1.000 55.10548  ? 131 GLN   A CD    1 
ATOM   1073 O  OE1   . GLN   A 1 132 ? 24.60954  -7.37467  -1.94434  1.000 58.59259  ? 131 GLN   A OE1   1 
ATOM   1074 N  NE2   . GLN   A 1 132 ? 22.64694  -7.13523  -0.88842  1.000 57.49594  ? 131 GLN   A NE2   1 
ATOM   1075 N  N     . ASP   A 1 133 ? 29.12377  -5.92377  1.02787   1.000 49.91022  ? 132 ASP   A N     1 
ATOM   1076 C  CA    . ASP   A 1 133 ? 30.37480  -6.50001  1.51088   1.000 50.82096  ? 132 ASP   A CA    1 
ATOM   1077 C  C     . ASP   A 1 133 ? 30.85142  -5.78886  2.76690   1.000 46.54030  ? 132 ASP   A C     1 
ATOM   1078 O  O     . ASP   A 1 133 ? 31.28581  -6.43502  3.72918   1.000 46.51237  ? 132 ASP   A O     1 
ATOM   1079 C  CB    . ASP   A 1 133 ? 31.44646  -6.43137  0.42378   1.000 55.48492  ? 132 ASP   A CB    1 
ATOM   1080 C  CG    . ASP   A 1 133 ? 31.19132  -7.40135  -0.71810  1.000 52.83364  ? 132 ASP   A CG    1 
ATOM   1081 O  OD1   . ASP   A 1 133 ? 30.32426  -8.28946  -0.57381  1.000 52.62884  ? 132 ASP   A OD1   1 
ATOM   1082 O  OD2   . ASP   A 1 133 ? 31.86462  -7.26328  -1.76196  1.000 55.49830  ? 132 ASP   A OD2   1 
ATOM   1083 N  N     . LEU   A 1 134 ? 30.77061  -4.45433  2.77702   1.000 47.90595  ? 133 LEU   A N     1 
ATOM   1084 C  CA    . LEU   A 1 134 ? 31.15591  -3.69154  3.96153   1.000 45.04915  ? 133 LEU   A CA    1 
ATOM   1085 C  C     . LEU   A 1 134 ? 30.29796  -4.07164  5.15954   1.000 40.29315  ? 133 LEU   A C     1 
ATOM   1086 O  O     . LEU   A 1 134 ? 30.81829  -4.35944  6.24342   1.000 40.58472  ? 133 LEU   A O     1 
ATOM   1087 C  CB    . LEU   A 1 134 ? 31.05175  -2.19057  3.68268   1.000 41.55120  ? 133 LEU   A CB    1 
ATOM   1088 C  CG    . LEU   A 1 134 ? 31.58677  -1.29411  4.79686   1.000 42.43437  ? 133 LEU   A CG    1 
ATOM   1089 C  CD1   . LEU   A 1 134 ? 33.09039  -1.52517  4.97406   1.000 43.99277  ? 133 LEU   A CD1   1 
ATOM   1090 C  CD2   . LEU   A 1 134 ? 31.29886  0.17524   4.54114   1.000 33.90866  ? 133 LEU   A CD2   1 
ATOM   1091 N  N     . ALA   A 1 135 ? 28.97356  -4.07784  4.98108   1.000 42.08497  ? 134 ALA   A N     1 
ATOM   1092 C  CA    . ALA   A 1 135 ? 28.07837  -4.44062  6.07292   1.000 40.53466  ? 134 ALA   A CA    1 
ATOM   1093 C  C     . ALA   A 1 135 ? 28.36890  -5.84582  6.58828   1.000 47.19565  ? 134 ALA   A C     1 
ATOM   1094 O  O     . ALA   A 1 135 ? 28.32607  -6.09286  7.80234   1.000 39.55622  ? 134 ALA   A O     1 
ATOM   1095 C  CB    . ALA   A 1 135 ? 26.62438  -4.32292  5.61481   1.000 35.97159  ? 134 ALA   A CB    1 
ATOM   1096 N  N     . ARG   A 1 136 ? 28.66372  -6.78098  5.67881   1.000 44.19464  ? 135 ARG   A N     1 
ATOM   1097 C  CA    . ARG   A 1 136 ? 29.02515  -8.13624  6.08889   1.000 48.45175  ? 135 ARG   A CA    1 
ATOM   1098 C  C     . ARG   A 1 136 ? 30.29791  -8.13762  6.92700   1.000 42.41709  ? 135 ARG   A C     1 
ATOM   1099 O  O     . ARG   A 1 136 ? 30.38037  -8.83200  7.94854   1.000 47.17165  ? 135 ARG   A O     1 
ATOM   1100 C  CB    . ARG   A 1 136 ? 29.19789  -9.02146  4.85700   1.000 46.45442  ? 135 ARG   A CB    1 
ATOM   1101 C  CG    . ARG   A 1 136 ? 29.43033  -10.49527 5.15699   1.000 55.92713  ? 135 ARG   A CG    1 
ATOM   1102 C  CD    . ARG   A 1 136 ? 29.69317  -11.27620 3.86703   1.000 58.44479  ? 135 ARG   A CD    1 
ATOM   1103 N  NE    . ARG   A 1 136 ? 28.65360  -11.03617 2.87169   1.000 63.23470  ? 135 ARG   A NE    1 
ATOM   1104 C  CZ    . ARG   A 1 136 ? 28.82281  -10.33881 1.75422   1.000 62.43943  ? 135 ARG   A CZ    1 
ATOM   1105 N  NH1   . ARG   A 1 136 ? 30.00083  -9.83219  1.42459   1.000 60.94194  ? 135 ARG   A NH1   1 
ATOM   1106 N  NH2   . ARG   A 1 136 ? 27.78304  -10.14410 0.94709   1.000 63.24822  ? 135 ARG   A NH2   1 
ATOM   1107 N  N     . SER   A 1 137 ? 31.30138  -7.36016  6.51353   1.000 42.83821  ? 136 SER   A N     1 
ATOM   1108 C  CA    . SER   A 1 137 ? 32.53139  -7.26783  7.28888   1.000 46.48293  ? 136 SER   A CA    1 
ATOM   1109 C  C     . SER   A 1 137 ? 32.30847  -6.59342  8.63623   1.000 46.55674  ? 136 SER   A C     1 
ATOM   1110 O  O     . SER   A 1 137 ? 33.07089  -6.84028  9.57671   1.000 49.49305  ? 136 SER   A O     1 
ATOM   1111 C  CB    . SER   A 1 137 ? 33.60235  -6.51916  6.49394   1.000 47.27905  ? 136 SER   A CB    1 
ATOM   1112 O  OG    . SER   A 1 137 ? 33.40123  -5.12050  6.54186   1.000 44.01948  ? 136 SER   A OG    1 
ATOM   1113 N  N     . TYR   A 1 138 ? 31.28495  -5.75281  8.75522   1.000 41.90696  ? 137 TYR   A N     1 
ATOM   1114 C  CA    . TYR   A 1 138 ? 30.93352  -5.16522  10.03871  1.000 40.14577  ? 137 TYR   A CA    1 
ATOM   1115 C  C     . TYR   A 1 138 ? 30.04222  -6.06595  10.88185  1.000 41.79013  ? 137 TYR   A C     1 
ATOM   1116 O  O     . TYR   A 1 138 ? 29.93218  -5.84606  12.09157  1.000 42.20391  ? 137 TYR   A O     1 
ATOM   1117 C  CB    . TYR   A 1 138 ? 30.22040  -3.82807  9.83826   1.000 39.73790  ? 137 TYR   A CB    1 
ATOM   1118 C  CG    . TYR   A 1 138 ? 31.06861  -2.70551  9.28520   1.000 43.92502  ? 137 TYR   A CG    1 
ATOM   1119 C  CD1   . TYR   A 1 138 ? 32.45788  -2.78509  9.25450   1.000 41.23537  ? 137 TYR   A CD1   1 
ATOM   1120 C  CD2   . TYR   A 1 138 ? 30.46928  -1.55591  8.79361   1.000 41.20472  ? 137 TYR   A CD2   1 
ATOM   1121 C  CE1   . TYR   A 1 138 ? 33.21557  -1.74222  8.75104   1.000 39.86657  ? 137 TYR   A CE1   1 
ATOM   1122 C  CE2   . TYR   A 1 138 ? 31.21030  -0.52175  8.29387   1.000 39.12965  ? 137 TYR   A CE2   1 
ATOM   1123 C  CZ    . TYR   A 1 138 ? 32.58221  -0.61324  8.27317   1.000 41.04735  ? 137 TYR   A CZ    1 
ATOM   1124 O  OH    . TYR   A 1 138 ? 33.28848  0.44862   7.76698   1.000 41.00736  ? 137 TYR   A OH    1 
ATOM   1125 N  N     . GLY   A 1 139 ? 29.39749  -7.05923  10.27813  1.000 38.64033  ? 138 GLY   A N     1 
ATOM   1126 C  CA    . GLY   A 1 139 ? 28.45187  -7.87895  11.00782  1.000 38.25125  ? 138 GLY   A CA    1 
ATOM   1127 C  C     . GLY   A 1 139 ? 27.11887  -7.20708  11.25016  1.000 36.30596  ? 138 GLY   A C     1 
ATOM   1128 O  O     . GLY   A 1 139 ? 26.42433  -7.55227  12.20953  1.000 41.06613  ? 138 GLY   A O     1 
ATOM   1129 N  N     . ILE   A 1 140 ? 26.73996  -6.25434  10.40082  1.000 36.03387  ? 139 ILE   A N     1 
ATOM   1130 C  CA    . ILE   A 1 140 ? 25.52676  -5.46655  10.60347  1.000 35.79038  ? 139 ILE   A CA    1 
ATOM   1131 C  C     . ILE   A 1 140 ? 24.68058  -5.53812  9.33619   1.000 38.01024  ? 139 ILE   A C     1 
ATOM   1132 O  O     . ILE   A 1 140 ? 25.18173  -5.87421  8.25333   1.000 36.60859  ? 139 ILE   A O     1 
ATOM   1133 C  CB    . ILE   A 1 140 ? 25.85084  -3.99656  10.96567  1.000 34.00639  ? 139 ILE   A CB    1 
ATOM   1134 C  CG1   . ILE   A 1 140 ? 26.44175  -3.26142  9.76395   1.000 36.70171  ? 139 ILE   A CG1   1 
ATOM   1135 C  CG2   . ILE   A 1 140 ? 26.78531  -3.93273  12.17070  1.000 32.63182  ? 139 ILE   A CG2   1 
ATOM   1136 C  CD1   . ILE   A 1 140 ? 26.67094  -1.78002  10.00506  1.000 35.00843  ? 139 ILE   A CD1   1 
ATOM   1137 N  N     . PRO   A 1 141 ? 23.38690  -5.23766  9.44249   1.000 35.50381  ? 140 PRO   A N     1 
ATOM   1138 C  CA    . PRO   A 1 141 ? 22.54238  -5.21612  8.24283   1.000 33.25810  ? 140 PRO   A CA    1 
ATOM   1139 C  C     . PRO   A 1 141 ? 22.85269  -4.03612  7.33873   1.000 32.65489  ? 140 PRO   A C     1 
ATOM   1140 O  O     . PRO   A 1 141 ? 23.37257  -3.00621  7.77274   1.000 31.60818  ? 140 PRO   A O     1 
ATOM   1141 C  CB    . PRO   A 1 141 ? 21.12249  -5.10448  8.80830   1.000 29.95166  ? 140 PRO   A CB    1 
ATOM   1142 C  CG    . PRO   A 1 141 ? 21.22979  -5.52189  10.22427  1.000 31.19848  ? 140 PRO   A CG    1 
ATOM   1143 C  CD    . PRO   A 1 141 ? 22.59014  -5.12794  10.67290  1.000 33.36653  ? 140 PRO   A CD    1 
ATOM   1144 N  N     . PHE   A 1 142 ? 22.51894  -4.20334  6.05696   1.000 32.68171  ? 141 PHE   A N     1 
ATOM   1145 C  CA    . PHE   A 1 142 ? 22.55768  -3.13245  5.06856   1.000 28.14169  ? 141 PHE   A CA    1 
ATOM   1146 C  C     . PHE   A 1 142 ? 21.17103  -2.98375  4.46921   1.000 31.46006  ? 141 PHE   A C     1 
ATOM   1147 O  O     . PHE   A 1 142 ? 20.52893  -3.98402  4.13756   1.000 37.38806  ? 141 PHE   A O     1 
ATOM   1148 C  CB    . PHE   A 1 142 ? 23.57371  -3.41435  3.95659   1.000 35.36493  ? 141 PHE   A CB    1 
ATOM   1149 C  CG    . PHE   A 1 142 ? 23.49523  -2.44799  2.79858   1.000 35.25042  ? 141 PHE   A CG    1 
ATOM   1150 C  CD1   . PHE   A 1 142 ? 23.75218  -1.09535  2.98185   1.000 26.67709  ? 141 PHE   A CD1   1 
ATOM   1151 C  CD2   . PHE   A 1 142 ? 23.17835  -2.89650  1.52134   1.000 37.30332  ? 141 PHE   A CD2   1 
ATOM   1152 C  CE1   . PHE   A 1 142 ? 23.68060  -0.20788  1.92952   1.000 28.65289  ? 141 PHE   A CE1   1 
ATOM   1153 C  CE2   . PHE   A 1 142 ? 23.10721  -2.01086  0.45732   1.000 37.12578  ? 141 PHE   A CE2   1 
ATOM   1154 C  CZ    . PHE   A 1 142 ? 23.36067  -0.66703  0.65869   1.000 36.61550  ? 141 PHE   A CZ    1 
ATOM   1155 N  N     . ILE   A 1 143 ? 20.70990  -1.74326  4.33513   1.000 33.05389  ? 142 ILE   A N     1 
ATOM   1156 C  CA    . ILE   A 1 143 ? 19.39725  -1.44666  3.76581   1.000 32.19349  ? 142 ILE   A CA    1 
ATOM   1157 C  C     . ILE   A 1 143 ? 19.54383  -0.25807  2.83037   1.000 28.77335  ? 142 ILE   A C     1 
ATOM   1158 O  O     . ILE   A 1 143 ? 20.20274  0.72820   3.17561   1.000 29.89974  ? 142 ILE   A O     1 
ATOM   1159 C  CB    . ILE   A 1 143 ? 18.35464  -1.14782  4.85986   1.000 30.48480  ? 142 ILE   A CB    1 
ATOM   1160 C  CG1   . ILE   A 1 143 ? 18.06963  -2.40447  5.67758   1.000 32.35935  ? 142 ILE   A CG1   1 
ATOM   1161 C  CG2   . ILE   A 1 143 ? 17.03913  -0.60431  4.24262   1.000 36.86910  ? 142 ILE   A CG2   1 
ATOM   1162 C  CD1   . ILE   A 1 143 ? 17.36026  -2.12056  6.95050   1.000 42.02987  ? 142 ILE   A CD1   1 
ATOM   1163 N  N     . GLU   A 1 144 ? 18.95179  -0.35507  1.64254   1.000 28.58346  ? 143 GLU   A N     1 
ATOM   1164 C  CA    . GLU   A 1 144 ? 18.94799  0.75982   0.71065   1.000 27.07163  ? 143 GLU   A CA    1 
ATOM   1165 C  C     . GLU   A 1 144 ? 17.64847  1.52256   0.88130   1.000 29.83137  ? 143 GLU   A C     1 
ATOM   1166 O  O     . GLU   A 1 144 ? 16.58808  0.92597   1.09968   1.000 32.10576  ? 143 GLU   A O     1 
ATOM   1167 C  CB    . GLU   A 1 144 ? 19.10114  0.29307   -0.74040  1.000 36.97189  ? 143 GLU   A CB    1 
ATOM   1168 C  CG    . GLU   A 1 144 ? 20.50544  -0.16742  -1.07403  1.000 44.74342  ? 143 GLU   A CG    1 
ATOM   1169 C  CD    . GLU   A 1 144 ? 20.76415  -0.29530  -2.57132  1.000 52.62865  ? 143 GLU   A CD    1 
ATOM   1170 O  OE1   . GLU   A 1 144 ? 19.83000  -0.04775  -3.36620  1.000 56.69830  ? 143 GLU   A OE1   1 
ATOM   1171 O  OE2   . GLU   A 1 144 ? 21.90886  -0.63665  -2.94700  1.000 51.84375  ? 143 GLU   A OE2   1 
ATOM   1172 N  N     . THR   A 1 145 ? 17.73200  2.84316   0.80488   1.000 29.27201  ? 144 THR   A N     1 
ATOM   1173 C  CA    . THR   A 1 145 ? 16.57295  3.66850   1.09604   1.000 24.66400  ? 144 THR   A CA    1 
ATOM   1174 C  C     . THR   A 1 145 ? 16.46717  4.80276   0.10224   1.000 24.51549  ? 144 THR   A C     1 
ATOM   1175 O  O     . THR   A 1 145 ? 17.42663  5.16479   -0.57329  1.000 25.84931  ? 144 THR   A O     1 
ATOM   1176 C  CB    . THR   A 1 145 ? 16.62770  4.27028   2.51646   1.000 23.24101  ? 144 THR   A CB    1 
ATOM   1177 O  OG1   . THR   A 1 145 ? 17.77289  5.13349   2.62352   1.000 24.75855  ? 144 THR   A OG1   1 
ATOM   1178 C  CG2   . THR   A 1 145 ? 16.68468  3.17297   3.56031   1.000 24.24650  ? 144 THR   A CG2   1 
ATOM   1179 N  N     . SER   A 1 146 ? 15.26238  5.36561   0.03600   1.000 25.39959  ? 145 SER   A N     1 
ATOM   1180 C  CA    . SER   A 1 146 ? 15.04243  6.66568   -0.57974  1.000 23.45166  ? 145 SER   A CA    1 
ATOM   1181 C  C     . SER   A 1 146 ? 14.14451  7.47194   0.34738   1.000 24.51494  ? 145 SER   A C     1 
ATOM   1182 O  O     . SER   A 1 146 ? 12.98952  7.09646   0.58231   1.000 23.99769  ? 145 SER   A O     1 
ATOM   1183 C  CB    . SER   A 1 146 ? 14.39975  6.54169   -1.95973  1.000 23.45609  ? 145 SER   A CB    1 
ATOM   1184 O  OG    . SER   A 1 146 ? 14.09417  7.82686   -2.42731  1.000 24.89337  ? 145 SER   A OG    1 
ATOM   1185 N  N     . ALA   A 1 147 ? 14.66864  8.58428   0.86883   1.000 27.17527  ? 146 ALA   A N     1 
ATOM   1186 C  CA    . ALA   A 1 147 ? 13.80490  9.50068   1.59610   1.000 29.14648  ? 146 ALA   A CA    1 
ATOM   1187 C  C     . ALA   A 1 147 ? 12.77408  10.12364  0.66675   1.000 26.23626  ? 146 ALA   A C     1 
ATOM   1188 O  O     . ALA   A 1 147 ? 11.69783  10.51003  1.12110   1.000 28.08385  ? 146 ALA   A O     1 
ATOM   1189 C  CB    . ALA   A 1 147 ? 14.62584  10.59231  2.27317   1.000 25.12086  ? 146 ALA   A CB    1 
ATOM   1190 N  N     . LYS   A 1 148 ? 13.07819  10.21303  -0.63394  1.000 27.82075  ? 147 LYS   A N     1 
ATOM   1191 C  CA    . LYS   A 1 148 ? 12.15267  10.84633  -1.57456  1.000 27.89411  ? 147 LYS   A CA    1 
ATOM   1192 C  C     . LYS   A 1 148 ? 10.95630  9.94696   -1.90418  1.000 28.53708  ? 147 LYS   A C     1 
ATOM   1193 O  O     . LYS   A 1 148 ? 9.80885   10.41278  -1.93664  1.000 29.49484  ? 147 LYS   A O     1 
ATOM   1194 C  CB    . LYS   A 1 148 ? 12.91022  11.23290  -2.85076  1.000 26.74416  ? 147 LYS   A CB    1 
ATOM   1195 C  CG    . LYS   A 1 148 ? 12.06728  11.96985  -3.91107  1.000 27.79674  ? 147 LYS   A CG    1 
ATOM   1196 C  CD    . LYS   A 1 148 ? 12.91967  12.33511  -5.14065  1.000 36.80575  ? 147 LYS   A CD    1 
ATOM   1197 C  CE    . LYS   A 1 148 ? 12.15181  13.20809  -6.13244  1.000 43.18075  ? 147 LYS   A CE    1 
ATOM   1198 N  NZ    . LYS   A 1 148 ? 12.11705  14.64247  -5.72055  1.000 51.13129  ? 147 LYS   A NZ    1 
ATOM   1199 N  N     . THR   A 1 149 ? 11.19462  8.66342   -2.15953  1.000 28.36389  ? 148 THR   A N     1 
ATOM   1200 C  CA    . THR   A 1 149 ? 10.10560  7.75227   -2.48218  1.000 25.04569  ? 148 THR   A CA    1 
ATOM   1201 C  C     . THR   A 1 149 ? 9.57326   7.00111   -1.26989  1.000 28.30173  ? 148 THR   A C     1 
ATOM   1202 O  O     . THR   A 1 149 ? 8.57084   6.28716   -1.39315  1.000 26.38503  ? 148 THR   A O     1 
ATOM   1203 C  CB    . THR   A 1 149 ? 10.55858  6.73191   -3.53155  1.000 24.20438  ? 148 THR   A CB    1 
ATOM   1204 O  OG1   . THR   A 1 149 ? 11.54289  5.85571   -2.95171  1.000 29.20796  ? 148 THR   A OG1   1 
ATOM   1205 C  CG2   . THR   A 1 149 ? 11.13105  7.43876   -4.75626  1.000 27.64427  ? 148 THR   A CG2   1 
ATOM   1206 N  N     . ARG   A 1 150 ? 10.23193  7.12273   -0.11209  1.000 23.90260  ? 149 ARG   A N     1 
ATOM   1207 C  CA    . ARG   A 1 150 ? 9.98149   6.37825   1.12179   1.000 26.23620  ? 149 ARG   A CA    1 
ATOM   1208 C  C     . ARG   A 1 150 ? 10.41470  4.92314   1.03456   1.000 25.52296  ? 149 ARG   A C     1 
ATOM   1209 O  O     . ARG   A 1 150 ? 10.19876  4.18364   1.99061   1.000 31.17443  ? 149 ARG   A O     1 
ATOM   1210 C  CB    . ARG   A 1 150 ? 8.50916   6.42488   1.58483   1.000 27.47933  ? 149 ARG   A CB    1 
ATOM   1211 C  CG    . ARG   A 1 150 ? 7.98727   7.83621   1.83504   1.000 35.99008  ? 149 ARG   A CG    1 
ATOM   1212 C  CD    . ARG   A 1 150 ? 6.61458   7.86168   2.53076   1.000 33.86870  ? 149 ARG   A CD    1 
ATOM   1213 N  NE    . ARG   A 1 150 ? 6.41171   6.71441   3.40873   1.000 34.95041  ? 149 ARG   A NE    1 
ATOM   1214 C  CZ    . ARG   A 1 150 ? 6.75780   6.66206   4.68740   1.000 37.36227  ? 149 ARG   A CZ    1 
ATOM   1215 N  NH1   . ARG   A 1 150 ? 7.29992   7.70155   5.30387   1.000 32.70637  ? 149 ARG   A NH1   1 
ATOM   1216 N  NH2   . ARG   A 1 150 ? 6.57856   5.52837   5.35987   1.000 43.35709  ? 149 ARG   A NH2   1 
ATOM   1217 N  N     . GLN   A 1 151 ? 11.02018  4.48389   -0.07186  1.000 27.35165  ? 150 GLN   A N     1 
ATOM   1218 C  CA    . GLN   A 1 151 ? 11.52738  3.12160   -0.13067  1.000 28.30685  ? 150 GLN   A CA    1 
ATOM   1219 C  C     . GLN   A 1 151 ? 12.44911  2.85019   1.05350   1.000 24.95577  ? 150 GLN   A C     1 
ATOM   1220 O  O     . GLN   A 1 151 ? 13.38894  3.60063   1.29196   1.000 27.69003  ? 150 GLN   A O     1 
ATOM   1221 C  CB    . GLN   A 1 151 ? 12.28917  2.89363   -1.43092  1.000 28.69966  ? 150 GLN   A CB    1 
ATOM   1222 C  CG    . GLN   A 1 151 ? 12.89795  1.51538   -1.52048  1.000 30.02350  ? 150 GLN   A CG    1 
ATOM   1223 C  CD    . GLN   A 1 151 ? 13.74566  1.34261   -2.75806  1.000 44.96171  ? 150 GLN   A CD    1 
ATOM   1224 O  OE1   . GLN   A 1 151 ? 13.43525  1.88665   -3.82111  1.000 39.67025  ? 150 GLN   A OE1   1 
ATOM   1225 N  NE2   . GLN   A 1 151 ? 14.83084  0.58861   -2.62743  1.000 46.65634  ? 150 GLN   A NE2   1 
ATOM   1226 N  N     . GLY   A 1 152 ? 12.15438  1.79507   1.80585   1.000 27.00066  ? 151 GLY   A N     1 
ATOM   1227 C  CA    . GLY   A 1 152 ? 13.05645  1.30519   2.83535   1.000 29.20663  ? 151 GLY   A CA    1 
ATOM   1228 C  C     . GLY   A 1 152 ? 13.16686  2.14138   4.09679   1.000 28.84505  ? 151 GLY   A C     1 
ATOM   1229 O  O     . GLY   A 1 152 ? 13.94855  1.77453   4.98274   1.000 28.68392  ? 151 GLY   A O     1 
ATOM   1230 N  N     . VAL   A 1 153 ? 12.41013  3.23503   4.21507   1.000 28.06873  ? 152 VAL   A N     1 
ATOM   1231 C  CA    . VAL   A 1 153 ? 12.56145  4.14754   5.34582   1.000 29.75211  ? 152 VAL   A CA    1 
ATOM   1232 C  C     . VAL   A 1 153 ? 12.15287  3.46085   6.64194   1.000 31.11431  ? 152 VAL   A C     1 
ATOM   1233 O  O     . VAL   A 1 153 ? 12.91305  3.43414   7.62042   1.000 26.65169  ? 152 VAL   A O     1 
ATOM   1234 C  CB    . VAL   A 1 153 ? 11.75126  5.43307   5.10474   1.000 28.02090  ? 152 VAL   A CB    1 
ATOM   1235 C  CG1   . VAL   A 1 153 ? 11.51307  6.17540   6.43085   1.000 27.20445  ? 152 VAL   A CG1   1 
ATOM   1236 C  CG2   . VAL   A 1 153 ? 12.44860  6.30650   4.08693   1.000 30.98280  ? 152 VAL   A CG2   1 
ATOM   1237 N  N     . ASP   A 1 154 ? 10.93831  2.90518   6.67906   1.000 30.34959  ? 153 ASP   A N     1 
ATOM   1238 C  CA    . ASP   A 1 154 ? 10.52519  2.15535   7.85834   1.000 28.60221  ? 153 ASP   A CA    1 
ATOM   1239 C  C     . ASP   A 1 154 ? 11.46895  0.98926   8.10977   1.000 34.03151  ? 153 ASP   A C     1 
ATOM   1240 O  O     . ASP   A 1 154 ? 11.85241  0.72139   9.25633   1.000 34.54565  ? 153 ASP   A O     1 
ATOM   1241 C  CB    . ASP   A 1 154 ? 9.08654   1.64928   7.70227   1.000 29.03196  ? 153 ASP   A CB    1 
ATOM   1242 C  CG    . ASP   A 1 154 ? 8.04347   2.73117   7.96326   1.000 40.25453  ? 153 ASP   A CG    1 
ATOM   1243 O  OD1   . ASP   A 1 154 ? 8.40554   3.85806   8.36900   1.000 34.57697  ? 153 ASP   A OD1   1 
ATOM   1244 O  OD2   . ASP   A 1 154 ? 6.84370   2.45566   7.75910   1.000 37.81353  ? 153 ASP   A OD2   1 
ATOM   1245 N  N     . ASP   A 1 155 ? 11.87149  0.29726   7.04528   1.000 30.11343  ? 154 ASP   A N     1 
ATOM   1246 C  CA    . ASP   A 1 155 ? 12.69252  -0.89236  7.21144   1.000 31.81042  ? 154 ASP   A CA    1 
ATOM   1247 C  C     . ASP   A 1 155 ? 14.00554  -0.56378  7.91767   1.000 30.24364  ? 154 ASP   A C     1 
ATOM   1248 O  O     . ASP   A 1 155 ? 14.42754  -1.29278  8.82301   1.000 30.93252  ? 154 ASP   A O     1 
ATOM   1249 C  CB    . ASP   A 1 155 ? 12.95839  -1.53743  5.85283   1.000 35.66552  ? 154 ASP   A CB    1 
ATOM   1250 C  CG    . ASP   A 1 155 ? 13.60123  -2.90606  5.97459   1.000 40.21555  ? 154 ASP   A CG    1 
ATOM   1251 O  OD1   . ASP   A 1 155 ? 13.35648  -3.60582  6.98393   1.000 46.12947  ? 154 ASP   A OD1   1 
ATOM   1252 O  OD2   . ASP   A 1 155 ? 14.36987  -3.27668  5.06347   1.000 44.67762  ? 154 ASP   A OD2   1 
ATOM   1253 N  N     . ALA   A 1 156 ? 14.64179  0.54882   7.54606   1.000 27.15655  ? 155 ALA   A N     1 
ATOM   1254 C  CA    . ALA   A 1 156 ? 15.91995  0.90716   8.16170   1.000 24.26072  ? 155 ALA   A CA    1 
ATOM   1255 C  C     . ALA   A 1 156 ? 15.76843  1.15909   9.66377   1.000 26.15458  ? 155 ALA   A C     1 
ATOM   1256 O  O     . ALA   A 1 156 ? 16.46408  0.54054   10.47701  1.000 30.83138  ? 155 ALA   A O     1 
ATOM   1257 C  CB    . ALA   A 1 156 ? 16.52369  2.11990   7.44868   1.000 26.47207  ? 155 ALA   A CB    1 
ATOM   1258 N  N     . PHE   A 1 157 ? 14.84424  2.03998   10.05760  1.000 23.66273  ? 156 PHE   A N     1 
ATOM   1259 C  CA    . PHE   A 1 157 ? 14.66469  2.31581   11.47823  1.000 24.10114  ? 156 PHE   A CA    1 
ATOM   1260 C  C     . PHE   A 1 157 ? 14.23789  1.06649   12.23991  1.000 28.96598  ? 156 PHE   A C     1 
ATOM   1261 O  O     . PHE   A 1 157 ? 14.80029  0.76979   13.29864  1.000 25.65170  ? 156 PHE   A O     1 
ATOM   1262 C  CB    . PHE   A 1 157 ? 13.66187  3.45087   11.68403  1.000 23.46873  ? 156 PHE   A CB    1 
ATOM   1263 C  CG    . PHE   A 1 157 ? 14.21384  4.80023   11.34979  1.000 24.38616  ? 156 PHE   A CG    1 
ATOM   1264 C  CD1   . PHE   A 1 157 ? 14.99715  5.49050   12.26451  1.000 21.24042  ? 156 PHE   A CD1   1 
ATOM   1265 C  CD2   . PHE   A 1 157 ? 13.97025  5.37841   10.10928  1.000 22.15343  ? 156 PHE   A CD2   1 
ATOM   1266 C  CE1   . PHE   A 1 157 ? 15.52864  6.73261   11.93920  1.000 22.63618  ? 156 PHE   A CE1   1 
ATOM   1267 C  CE2   . PHE   A 1 157 ? 14.47499  6.61764   9.78658   1.000 22.40229  ? 156 PHE   A CE2   1 
ATOM   1268 C  CZ    . PHE   A 1 157 ? 15.25769  7.30160   10.70065  1.000 27.08091  ? 156 PHE   A CZ    1 
ATOM   1269 N  N     . TYR   A 1 158 ? 13.27288  0.29792   11.69881  1.000 25.45623  ? 157 TYR   A N     1 
ATOM   1270 C  CA    . TYR   A 1 158 ? 12.79857  -0.90129  12.39094  1.000 32.96528  ? 157 TYR   A CA    1 
ATOM   1271 C  C     . TYR   A 1 158 ? 13.90725  -1.93160  12.56340  1.000 29.61299  ? 157 TYR   A C     1 
ATOM   1272 O  O     . TYR   A 1 158 ? 14.01225  -2.56466  13.61968  1.000 32.26542  ? 157 TYR   A O     1 
ATOM   1273 C  CB    . TYR   A 1 158 ? 11.63305  -1.55365  11.63928  1.000 29.78444  ? 157 TYR   A CB    1 
ATOM   1274 C  CG    . TYR   A 1 158 ? 10.33428  -0.76960  11.63653  1.000 33.32241  ? 157 TYR   A CG    1 
ATOM   1275 C  CD1   . TYR   A 1 158 ? 10.26309  0.51646   12.15634  1.000 25.60582  ? 157 TYR   A CD1   1 
ATOM   1276 C  CD2   . TYR   A 1 158 ? 9.17648   -1.32908  11.11526  1.000 39.03582  ? 157 TYR   A CD2   1 
ATOM   1277 C  CE1   . TYR   A 1 158 ? 9.07264   1.23009   12.14374  1.000 32.58635  ? 157 TYR   A CE1   1 
ATOM   1278 C  CE2   . TYR   A 1 158 ? 7.98376   -0.63254  11.09395  1.000 37.58332  ? 157 TYR   A CE2   1 
ATOM   1279 C  CZ    . TYR   A 1 158 ? 7.93058   0.64333   11.61460  1.000 38.48950  ? 157 TYR   A CZ    1 
ATOM   1280 O  OH    . TYR   A 1 158 ? 6.73223   1.32815   11.59046  1.000 34.25347  ? 157 TYR   A OH    1 
ATOM   1281 N  N     . THR   A 1 159 ? 14.69985  -2.16122  11.51484  1.000 29.96186  ? 158 THR   A N     1 
ATOM   1282 C  CA    . THR   A 1 159 ? 15.80028  -3.11654  11.60902  1.000 36.17114  ? 158 THR   A CA    1 
ATOM   1283 C  C     . THR   A 1 159 ? 16.79888  -2.70719  12.68831  1.000 31.49230  ? 158 THR   A C     1 
ATOM   1284 O  O     . THR   A 1 159 ? 17.31165  -3.56031  13.42780  1.000 31.33871  ? 158 THR   A O     1 
ATOM   1285 C  CB    . THR   A 1 159 ? 16.50151  -3.24481  10.25894  1.000 33.12817  ? 158 THR   A CB    1 
ATOM   1286 O  OG1   . THR   A 1 159 ? 15.59159  -3.76247  9.27823   1.000 35.24852  ? 158 THR   A OG1   1 
ATOM   1287 C  CG2   . THR   A 1 159 ? 17.71405  -4.16335  10.36242  1.000 31.93998  ? 158 THR   A CG2   1 
ATOM   1288 N  N     . LEU   A 1 160 ? 17.08958  -1.40375  12.79489  1.000 28.42101  ? 159 LEU   A N     1 
ATOM   1289 C  CA    . LEU   A 1 160 ? 17.98939  -0.93862  13.84499  1.000 29.04923  ? 159 LEU   A CA    1 
ATOM   1290 C  C     . LEU   A 1 160 ? 17.43010  -1.28105  15.21633  1.000 28.42125  ? 159 LEU   A C     1 
ATOM   1291 O  O     . LEU   A 1 160 ? 18.17086  -1.71110  16.10759  1.000 30.36429  ? 159 LEU   A O     1 
ATOM   1292 C  CB    . LEU   A 1 160 ? 18.23034  0.56809   13.71416  1.000 25.66764  ? 159 LEU   A CB    1 
ATOM   1293 C  CG    . LEU   A 1 160 ? 19.07485  1.16324   14.86151  1.000 25.78758  ? 159 LEU   A CG    1 
ATOM   1294 C  CD1   . LEU   A 1 160 ? 20.40993  0.44890   14.96287  1.000 22.86876  ? 159 LEU   A CD1   1 
ATOM   1295 C  CD2   . LEU   A 1 160 ? 19.30316  2.67064   14.69844  1.000 24.19423  ? 159 LEU   A CD2   1 
ATOM   1296 N  N     . VAL   A 1 161 ? 16.11491  -1.13003  15.39308  1.000 28.80698  ? 160 VAL   A N     1 
ATOM   1297 C  CA    . VAL   A 1 161 ? 15.47173  -1.54689  16.63603  1.000 30.95488  ? 160 VAL   A CA    1 
ATOM   1298 C  C     . VAL   A 1 161 ? 15.64151  -3.04633  16.85068  1.000 31.48140  ? 160 VAL   A C     1 
ATOM   1299 O  O     . VAL   A 1 161 ? 15.97046  -3.49335  17.95392  1.000 33.88084  ? 160 VAL   A O     1 
ATOM   1300 C  CB    . VAL   A 1 161 ? 13.98598  -1.13947  16.63168  1.000 29.56085  ? 160 VAL   A CB    1 
ATOM   1301 C  CG1   . VAL   A 1 161 ? 13.25431  -1.77387  17.80922  1.000 31.56640  ? 160 VAL   A CG1   1 
ATOM   1302 C  CG2   . VAL   A 1 161 ? 13.86063  0.36202   16.68793  1.000 24.59030  ? 160 VAL   A CG2   1 
ATOM   1303 N  N     . ARG   A 1 162 ? 15.42738  -3.84748  15.80383  1.000 33.92317  ? 161 ARG   A N     1 
ATOM   1304 C  CA    . ARG   A 1 162 ? 15.66655  -5.28449  15.92808  1.000 38.23842  ? 161 ARG   A CA    1 
ATOM   1305 C  C     . ARG   A 1 162 ? 17.10291  -5.57404  16.36151  1.000 40.19897  ? 161 ARG   A C     1 
ATOM   1306 O  O     . ARG   A 1 162 ? 17.34685  -6.49888  17.14597  1.000 40.94629  ? 161 ARG   A O     1 
ATOM   1307 C  CB    . ARG   A 1 162 ? 15.35464  -5.99530  14.60892  1.000 37.91866  ? 161 ARG   A CB    1 
ATOM   1308 C  CG    . ARG   A 1 162 ? 13.90381  -5.87379  14.15335  1.000 41.42804  ? 161 ARG   A CG    1 
ATOM   1309 C  CD    . ARG   A 1 162 ? 13.61807  -6.75346  12.94260  1.000 43.29559  ? 161 ARG   A CD    1 
ATOM   1310 N  NE    . ARG   A 1 162 ? 12.24661  -6.57115  12.48206  1.000 44.71067  ? 161 ARG   A NE    1 
ATOM   1311 C  CZ    . ARG   A 1 162 ? 11.88664  -5.82179  11.44765  1.000 39.35199  ? 161 ARG   A CZ    1 
ATOM   1312 N  NH1   . ARG   A 1 162 ? 12.78303  -5.23691  10.66698  1.000 42.80249  ? 161 ARG   A NH1   1 
ATOM   1313 N  NH2   . ARG   A 1 162 ? 10.59374  -5.65440  11.19065  1.000 44.37385  ? 161 ARG   A NH2   1 
ATOM   1314 N  N     . GLU   A 1 163 ? 18.06714  -4.78994  15.86609  1.000 37.48788  ? 162 GLU   A N     1 
ATOM   1315 C  CA    . GLU   A 1 163 ? 19.46288  -4.99933  16.24369  1.000 34.70598  ? 162 GLU   A CA    1 
ATOM   1316 C  C     . GLU   A 1 163 ? 19.70491  -4.64280  17.70939  1.000 38.99941  ? 162 GLU   A C     1 
ATOM   1317 O  O     . GLU   A 1 163 ? 20.49759  -5.30643  18.38648  1.000 39.79864  ? 162 GLU   A O     1 
ATOM   1318 C  CB    . GLU   A 1 163 ? 20.38251  -4.19073  15.33182  1.000 32.98866  ? 162 GLU   A CB    1 
ATOM   1319 C  CG    . GLU   A 1 163 ? 20.41063  -4.68273  13.88871  1.000 36.96873  ? 162 GLU   A CG    1 
ATOM   1320 C  CD    . GLU   A 1 163 ? 20.96460  -6.09724  13.77570  1.000 41.92651  ? 162 GLU   A CD    1 
ATOM   1321 O  OE1   . GLU   A 1 163 ? 22.14557  -6.29807  14.12085  1.000 35.71278  ? 162 GLU   A OE1   1 
ATOM   1322 O  OE2   . GLU   A 1 163 ? 20.21405  -7.00338  13.36597  1.000 35.26623  ? 162 GLU   A OE2   1 
ATOM   1323 N  N     . ILE   A 1 164 ? 19.03171  -3.60449  18.22084  1.000 34.60042  ? 163 ILE   A N     1 
ATOM   1324 C  CA    . ILE   A 1 164 ? 19.17249  -3.25733  19.63344  1.000 35.27692  ? 163 ILE   A CA    1 
ATOM   1325 C  C     . ILE   A 1 164 ? 18.53335  -4.32816  20.50676  1.000 42.41127  ? 163 ILE   A C     1 
ATOM   1326 O  O     . ILE   A 1 164 ? 19.04154  -4.65558  21.58821  1.000 39.43309  ? 163 ILE   A O     1 
ATOM   1327 C  CB    . ILE   A 1 164 ? 18.56661  -1.87009  19.92120  1.000 34.70740  ? 163 ILE   A CB    1 
ATOM   1328 C  CG1   . ILE   A 1 164 ? 19.35404  -0.76446  19.22053  1.000 32.17866  ? 163 ILE   A CG1   1 
ATOM   1329 C  CG2   . ILE   A 1 164 ? 18.56111  -1.59117  21.42287  1.000 32.46606  ? 163 ILE   A CG2   1 
ATOM   1330 C  CD1   . ILE   A 1 164 ? 18.67122  0.59746   19.31347  1.000 30.03711  ? 163 ILE   A CD1   1 
ATOM   1331 N  N     . ARG   A 1 165 ? 17.40820  -4.88371  20.05523  1.000 36.07707  ? 164 ARG   A N     1 
ATOM   1332 C  CA    . ARG   A 1 165 ? 16.75071  -5.95188  20.80256  1.000 44.77335  ? 164 ARG   A CA    1 
ATOM   1333 C  C     . ARG   A 1 165 ? 17.66407  -7.16287  20.93849  1.000 50.60138  ? 164 ARG   A C     1 
ATOM   1334 O  O     . ARG   A 1 165 ? 17.82618  -7.71513  22.03322  1.000 60.63962  ? 164 ARG   A O     1 
ATOM   1335 C  CB    . ARG   A 1 165 ? 15.43734  -6.34190  20.11900  1.000 43.28493  ? 164 ARG   A CB    1 
ATOM   1336 C  CG    . ARG   A 1 165 ? 14.30399  -5.35912  20.34637  1.000 42.08200  ? 164 ARG   A CG    1 
ATOM   1337 C  CD    . ARG   A 1 165 ? 13.06771  -5.73560  19.54914  1.000 42.30300  ? 164 ARG   A CD    1 
ATOM   1338 N  NE    . ARG   A 1 165 ? 11.97028  -4.80119  19.78078  1.000 41.84330  ? 164 ARG   A NE    1 
ATOM   1339 C  CZ    . ARG   A 1 165 ? 10.82407  -4.81017  19.11334  1.000 40.41948  ? 164 ARG   A CZ    1 
ATOM   1340 N  NH1   . ARG   A 1 165 ? 10.58750  -5.69362  18.15742  1.000 44.88075  ? 164 ARG   A NH1   1 
ATOM   1341 N  NH2   . ARG   A 1 165 ? 9.89622   -3.90369  19.40501  1.000 40.04312  ? 164 ARG   A NH2   1 
ATOM   1342 N  N     . LYS   A 1 166 ? 18.28236  -7.57838  19.83078  1.000 55.02960  ? 165 LYS   A N     1 
ATOM   1343 C  CA    . LYS   A 1 166 ? 19.20852  -8.70678  19.84048  1.000 59.25589  ? 165 LYS   A CA    1 
ATOM   1344 C  C     . LYS   A 1 166 ? 20.42008  -8.46871  20.73942  1.000 64.36330  ? 165 LYS   A C     1 
ATOM   1345 O  O     . LYS   A 1 166 ? 21.07131  -9.43663  21.14725  1.000 73.00207  ? 165 LYS   A O     1 
ATOM   1346 C  CB    . LYS   A 1 166 ? 19.65647  -9.01215  18.40571  1.000 51.72081  ? 165 LYS   A CB    1 
ATOM   1347 C  CG    . LYS   A 1 166 ? 18.55345  -9.61825  17.54215  1.000 57.56139  ? 165 LYS   A CG    1 
ATOM   1348 C  CD    . LYS   A 1 166 ? 18.71742  -9.28690  16.05810  1.000 52.89828  ? 165 LYS   A CD    1 
ATOM   1349 C  CE    . LYS   A 1 166 ? 20.03671  -9.80153  15.49379  1.000 56.21644  ? 165 LYS   A CE    1 
ATOM   1350 N  NZ    . LYS   A 1 166 ? 20.17303  -9.50604  14.03846  1.000 49.70717  ? 165 LYS   A NZ    1 
ATOM   1351 N  N     . HIS   A 1 167 ? 20.73273  -7.21160  21.06355  1.000 56.78458  ? 166 HIS   A N     1 
ATOM   1352 C  CA    . HIS   A 1 167 ? 21.87003  -6.87177  21.91429  1.000 57.58706  ? 166 HIS   A CA    1 
ATOM   1353 C  C     . HIS   A 1 167 ? 21.49658  -6.83591  23.39255  1.000 63.95265  ? 166 HIS   A C     1 
ATOM   1354 O  O     . HIS   A 1 167 ? 22.29098  -7.25765  24.23940  1.000 67.67469  ? 166 HIS   A O     1 
ATOM   1355 C  CB    . HIS   A 1 167 ? 22.45300  -5.52201  21.47491  1.000 53.80430  ? 166 HIS   A CB    1 
ATOM   1356 C  CG    . HIS   A 1 167 ? 23.48999  -4.95711  22.40119  1.000 58.30759  ? 166 HIS   A CG    1 
ATOM   1357 N  ND1   . HIS   A 1 167 ? 24.83207  -5.26013  22.29682  1.000 60.66849  ? 166 HIS   A ND1   1 
ATOM   1358 C  CD2   . HIS   A 1 167 ? 23.38436  -4.07476  23.42402  1.000 58.44240  ? 166 HIS   A CD2   1 
ATOM   1359 C  CE1   . HIS   A 1 167 ? 25.50478  -4.60062  23.22401  1.000 57.68010  ? 166 HIS   A CE1   1 
ATOM   1360 N  NE2   . HIS   A 1 167 ? 24.64930  -3.87561  23.92221  1.000 59.21102  ? 166 HIS   A NE2   1 
ATOM   1361 N  N     . LYS   A 1 168 ? 20.29594  -6.35303  23.72207  1.000 63.03965  ? 167 LYS   A N     1 
ATOM   1362 C  CA    . LYS   A 1 168 ? 19.87507  -6.22778  25.11349  1.000 68.05841  ? 167 LYS   A CA    1 
ATOM   1363 C  C     . LYS   A 1 168 ? 19.43939  -7.55160  25.72705  1.000 76.21625  ? 167 LYS   A C     1 
ATOM   1364 O  O     . LYS   A 1 168 ? 19.33089  -7.63648  26.95527  1.000 76.78975  ? 167 LYS   A O     1 
ATOM   1365 C  CB    . LYS   A 1 168 ? 18.73921  -5.20671  25.23636  1.000 63.47449  ? 167 LYS   A CB    1 
ATOM   1366 C  CG    . LYS   A 1 168 ? 19.12697  -3.78675  24.83382  1.000 58.16742  ? 167 LYS   A CG    1 
ATOM   1367 C  CD    . LYS   A 1 168 ? 19.43023  -2.91743  26.04693  1.000 61.69998  ? 167 LYS   A CD    1 
ATOM   1368 C  CE    . LYS   A 1 168 ? 19.77716  -1.49124  25.62918  1.000 58.88421  ? 167 LYS   A CE    1 
ATOM   1369 N  NZ    . LYS   A 1 168 ? 19.82207  -0.54235  26.77971  1.000 54.56320  ? 167 LYS   A NZ    1 
ATOM   1370 N  N     . GLU   A 1 169 ? 19.17796  -8.57366  24.91348  1.000 84.44845  ? 168 GLU   A N     1 
ATOM   1371 C  CA    . GLU   A 1 169 ? 18.96899  -9.92924  25.40529  1.000 89.00162  ? 168 GLU   A CA    1 
ATOM   1372 C  C     . GLU   A 1 169 ? 20.25175  -10.75584 25.38962  1.000 93.32181  ? 168 GLU   A C     1 
ATOM   1373 O  O     . GLU   A 1 169 ? 20.20325  -11.95989 25.66341  1.000 97.17713  ? 168 GLU   A O     1 
ATOM   1374 C  CB    . GLU   A 1 169 ? 17.87126  -10.63365 24.59227  1.000 87.58568  ? 168 GLU   A CB    1 
ATOM   1375 C  CG    . GLU   A 1 169 ? 18.10241  -10.67647 23.08139  1.000 88.00242  ? 168 GLU   A CG    1 
ATOM   1376 C  CD    . GLU   A 1 169 ? 18.77956  -11.95473 22.61186  1.000 92.02533  ? 168 GLU   A CD    1 
ATOM   1377 O  OE1   . GLU   A 1 169 ? 18.79496  -12.93914 23.38090  1.000 90.56249  ? 168 GLU   A OE1   1 
ATOM   1378 O  OE2   . GLU   A 1 169 ? 19.29066  -11.97519 21.47040  1.000 89.94384  ? 168 GLU   A OE2   1 
ATOM   1379 N  N     . LYS   A 1 170 ? 21.39175  -10.13559 25.09018  1.000 88.29415  ? 169 LYS   A N     1 
ATOM   1380 C  CA    . LYS   A 1 170 ? 22.67048  -10.83920 25.03210  1.000 91.26194  ? 169 LYS   A CA    1 
ATOM   1381 C  C     . LYS   A 1 170 ? 23.39094  -10.77937 26.37433  1.000 95.50472  ? 169 LYS   A C     1 
ATOM   1382 O  O     . LYS   A 1 170 ? 23.52411  -11.79092 27.06324  1.000 97.16777  ? 169 LYS   A O     1 
ATOM   1383 C  CB    . LYS   A 1 170 ? 23.55968  -10.25043 23.93206  1.000 88.96003  ? 169 LYS   A CB    1 
ATOM   1384 C  CG    . LYS   A 1 170 ? 24.89997  -10.95257 23.76849  1.000 92.92640  ? 169 LYS   A CG    1 
ATOM   1385 C  CD    . LYS   A 1 170 ? 25.78668  -10.23494 22.76023  1.000 92.93600  ? 169 LYS   A CD    1 
ATOM   1386 C  CE    . LYS   A 1 170 ? 25.22479  -10.30728 21.34293  1.000 91.42835  ? 169 LYS   A CE    1 
ATOM   1387 N  NZ    . LYS   A 1 170 ? 25.49244  -11.62041 20.68548  1.000 95.00312  ? 169 LYS   A NZ    1 
ATOM   1388 N  N     . SER   B 1 1   ? 36.62627  28.82360  23.50787  1.000 47.13799  ? 0   SER   B N     1 
ATOM   1389 C  CA    . SER   B 1 1   ? 35.26304  29.25788  23.80645  1.000 34.80966  ? 0   SER   B CA    1 
ATOM   1390 C  C     . SER   B 1 1   ? 35.03556  29.29517  25.30243  1.000 38.06725  ? 0   SER   B C     1 
ATOM   1391 O  O     . SER   B 1 1   ? 35.69173  28.56592  26.05022  1.000 35.02947  ? 0   SER   B O     1 
ATOM   1392 C  CB    . SER   B 1 1   ? 34.23990  28.33181  23.15538  1.000 37.50435  ? 0   SER   B CB    1 
ATOM   1393 O  OG    . SER   B 1 1   ? 34.20871  28.52164  21.75666  1.000 40.25894  ? 0   SER   B OG    1 
ATOM   1394 N  N     . MET   B 1 2   ? 34.09708  30.14866  25.72173  1.000 32.49135  ? 1   MET   B N     1 
ATOM   1395 C  CA    . MET   B 1 2   ? 33.73720  30.23352  27.12660  1.000 30.36536  ? 1   MET   B CA    1 
ATOM   1396 C  C     . MET   B 1 2   ? 33.32004  28.86336  27.64042  1.000 34.85226  ? 1   MET   B C     1 
ATOM   1397 O  O     . MET   B 1 2   ? 32.75668  28.04048  26.90921  1.000 30.89186  ? 1   MET   B O     1 
ATOM   1398 C  CB    . MET   B 1 2   ? 32.60841  31.25000  27.33362  1.000 25.26350  ? 1   MET   B CB    1 
ATOM   1399 C  CG    . MET   B 1 2   ? 31.22861  30.78967  26.87972  1.000 29.30520  ? 1   MET   B CG    1 
ATOM   1400 S  SD    . MET   B 1 2   ? 29.96090  32.07152  27.02753  1.000 32.94745  ? 1   MET   B SD    1 
ATOM   1401 C  CE    . MET   B 1 2   ? 30.38597  33.10302  25.61510  1.000 30.47114  ? 1   MET   B CE    1 
ATOM   1402 N  N     . THR   B 1 3   ? 33.63883  28.61203  28.90740  1.000 29.34272  ? 2   THR   B N     1 
ATOM   1403 C  CA    . THR   B 1 3   ? 33.24878  27.36825  29.55300  1.000 30.86095  ? 2   THR   B CA    1 
ATOM   1404 C  C     . THR   B 1 3   ? 31.73271  27.30048  29.70776  1.000 29.11676  ? 2   THR   B C     1 
ATOM   1405 O  O     . THR   B 1 3   ? 31.06944  28.31505  29.95542  1.000 30.84784  ? 2   THR   B O     1 
ATOM   1406 C  CB    . THR   B 1 3   ? 33.94817  27.25573  30.91225  1.000 31.02733  ? 2   THR   B CB    1 
ATOM   1407 O  OG1   . THR   B 1 3   ? 35.35791  27.37116  30.69324  1.000 34.26875  ? 2   THR   B OG1   1 
ATOM   1408 C  CG2   . THR   B 1 3   ? 33.67009  25.92245  31.57378  1.000 32.40536  ? 2   THR   B CG2   1 
ATOM   1409 N  N     . GLU   B 1 4   ? 31.18850  26.09706  29.52695  1.000 30.33068  ? 3   GLU   B N     1 
ATOM   1410 C  CA    . GLU   B 1 4   ? 29.76802  25.82892  29.68726  1.000 27.74827  ? 3   GLU   B CA    1 
ATOM   1411 C  C     . GLU   B 1 4   ? 29.55469  25.02873  30.96274  1.000 31.31430  ? 3   GLU   B C     1 
ATOM   1412 O  O     . GLU   B 1 4   ? 30.30615  24.09343  31.24559  1.000 34.27117  ? 3   GLU   B O     1 
ATOM   1413 C  CB    . GLU   B 1 4   ? 29.20121  25.03844  28.50011  1.000 32.05647  ? 3   GLU   B CB    1 
ATOM   1414 C  CG    . GLU   B 1 4   ? 29.45110  25.66207  27.12778  1.000 33.37237  ? 3   GLU   B CG    1 
ATOM   1415 C  CD    . GLU   B 1 4   ? 28.71807  24.93272  26.01240  1.000 44.47284  ? 3   GLU   B CD    1 
ATOM   1416 O  OE1   . GLU   B 1 4   ? 27.94619  23.98996  26.30645  1.000 50.28300  ? 3   GLU   B OE1   1 
ATOM   1417 O  OE2   . GLU   B 1 4   ? 28.91309  25.31249  24.84300  1.000 44.29744  ? 3   GLU   B OE2   1 
ATOM   1418 N  N     . TYR   B 1 5   ? 28.51839  25.38943  31.71575  1.000 29.83491  ? 4   TYR   B N     1 
ATOM   1419 C  CA    . TYR   B 1 5   ? 28.18784  24.74521  32.98154  1.000 29.83082  ? 4   TYR   B CA    1 
ATOM   1420 C  C     . TYR   B 1 5   ? 26.78691  24.16380  32.89911  1.000 29.31289  ? 4   TYR   B C     1 
ATOM   1421 O  O     . TYR   B 1 5   ? 25.81634  24.89966  32.68218  1.000 32.06694  ? 4   TYR   B O     1 
ATOM   1422 C  CB    . TYR   B 1 5   ? 28.27657  25.73285  34.14661  1.000 32.54396  ? 4   TYR   B CB    1 
ATOM   1423 C  CG    . TYR   B 1 5   ? 29.66575  26.27476  34.37422  1.000 37.69674  ? 4   TYR   B CG    1 
ATOM   1424 C  CD1   . TYR   B 1 5   ? 30.61907  25.54011  35.07654  1.000 40.36019  ? 4   TYR   B CD1   1 
ATOM   1425 C  CD2   . TYR   B 1 5   ? 30.02612  27.51970  33.89269  1.000 35.41463  ? 4   TYR   B CD2   1 
ATOM   1426 C  CE1   . TYR   B 1 5   ? 31.89600  26.03968  35.28055  1.000 39.87884  ? 4   TYR   B CE1   1 
ATOM   1427 C  CE2   . TYR   B 1 5   ? 31.29160  28.02206  34.08777  1.000 39.72680  ? 4   TYR   B CE2   1 
ATOM   1428 C  CZ    . TYR   B 1 5   ? 32.22033  27.28617  34.78694  1.000 43.27594  ? 4   TYR   B CZ    1 
ATOM   1429 O  OH    . TYR   B 1 5   ? 33.47389  27.81629  34.96814  1.000 46.28014  ? 4   TYR   B OH    1 
ATOM   1430 N  N     . LYS   B 1 6   ? 26.68158  22.85767  33.11176  1.000 28.99443  ? 5   LYS   B N     1 
ATOM   1431 C  CA    . LYS   B 1 6   ? 25.40250  22.15358  33.07544  1.000 32.78870  ? 5   LYS   B CA    1 
ATOM   1432 C  C     . LYS   B 1 6   ? 24.79338  22.15290  34.47255  1.000 32.29356  ? 5   LYS   B C     1 
ATOM   1433 O  O     . LYS   B 1 6   ? 25.13845  21.32910  35.32187  1.000 33.93734  ? 5   LYS   B O     1 
ATOM   1434 C  CB    . LYS   B 1 6   ? 25.60246  20.74698  32.53102  1.000 33.85757  ? 5   LYS   B CB    1 
ATOM   1435 C  CG    . LYS   B 1 6   ? 26.03216  20.74893  31.08216  1.000 37.83552  ? 5   LYS   B CG    1 
ATOM   1436 C  CD    . LYS   B 1 6   ? 26.62437  19.41886  30.65131  1.000 40.49753  ? 5   LYS   B CD    1 
ATOM   1437 C  CE    . LYS   B 1 6   ? 26.89445  19.42165  29.15375  1.000 45.24461  ? 5   LYS   B CE    1 
ATOM   1438 N  NZ    . LYS   B 1 6   ? 27.83176  20.52696  28.76194  1.000 43.95343  ? 5   LYS   B NZ    1 
ATOM   1439 N  N     . LEU   B 1 7   ? 23.88660  23.08965  34.71118  1.000 29.07526  ? 6   LEU   B N     1 
ATOM   1440 C  CA    . LEU   B 1 7   ? 23.19714  23.24646  35.98044  1.000 28.28799  ? 6   LEU   B CA    1 
ATOM   1441 C  C     . LEU   B 1 7   ? 21.84542  22.55198  35.90523  1.000 32.03411  ? 6   LEU   B C     1 
ATOM   1442 O  O     . LEU   B 1 7   ? 21.16001  22.62112  34.87998  1.000 31.32140  ? 6   LEU   B O     1 
ATOM   1443 C  CB    . LEU   B 1 7   ? 23.00256  24.73200  36.30420  1.000 28.27240  ? 6   LEU   B CB    1 
ATOM   1444 C  CG    . LEU   B 1 7   ? 24.25356  25.61645  36.14197  1.000 29.02486  ? 6   LEU   B CG    1 
ATOM   1445 C  CD1   . LEU   B 1 7   ? 24.01102  27.04407  36.59835  1.000 30.36956  ? 6   LEU   B CD1   1 
ATOM   1446 C  CD2   . LEU   B 1 7   ? 25.41906  25.01580  36.85790  1.000 36.27619  ? 6   LEU   B CD2   1 
ATOM   1447 N  N     . VAL   B 1 8   ? 21.45660  21.88248  36.98978  1.000 27.49270  ? 7   VAL   B N     1 
ATOM   1448 C  CA    . VAL   B 1 8   ? 20.16434  21.21034  37.05766  1.000 26.03092  ? 7   VAL   B CA    1 
ATOM   1449 C  C     . VAL   B 1 8   ? 19.42347  21.69172  38.30011  1.000 33.83892  ? 7   VAL   B C     1 
ATOM   1450 O  O     . VAL   B 1 8   ? 19.98145  21.67802  39.40352  1.000 33.62644  ? 7   VAL   B O     1 
ATOM   1451 C  CB    . VAL   B 1 8   ? 20.31948  19.67874  37.06501  1.000 26.72018  ? 7   VAL   B CB    1 
ATOM   1452 C  CG1   . VAL   B 1 8   ? 18.95267  19.01181  37.08810  1.000 26.50758  ? 7   VAL   B CG1   1 
ATOM   1453 C  CG2   . VAL   B 1 8   ? 21.14470  19.21945  35.84942  1.000 28.30477  ? 7   VAL   B CG2   1 
ATOM   1454 N  N     . VAL   B 1 9   ? 18.17795  22.12417  38.12344  1.000 27.25802  ? 8   VAL   B N     1 
ATOM   1455 C  CA    . VAL   B 1 9   ? 17.37536  22.66275  39.21866  1.000 31.37007  ? 8   VAL   B CA    1 
ATOM   1456 C  C     . VAL   B 1 9   ? 16.41495  21.57057  39.66794  1.000 33.35402  ? 8   VAL   B C     1 
ATOM   1457 O  O     . VAL   B 1 9   ? 15.49637  21.20384  38.92552  1.000 28.38234  ? 8   VAL   B O     1 
ATOM   1458 C  CB    . VAL   B 1 9   ? 16.61255  23.92740  38.79257  1.000 37.66257  ? 8   VAL   B CB    1 
ATOM   1459 C  CG1   . VAL   B 1 9   ? 15.88781  24.53985  39.97865  1.000 32.42995  ? 8   VAL   B CG1   1 
ATOM   1460 C  CG2   . VAL   B 1 9   ? 17.54252  24.95426  38.17640  1.000 28.96001  ? 8   VAL   B CG2   1 
ATOM   1461 N  N     . VAL   B 1 10  ? 16.61162  21.05671  40.88895  1.000 33.37145  ? 9   VAL   B N     1 
ATOM   1462 C  CA    . VAL   B 1 10  ? 15.79515  19.97142  41.42151  1.000 31.10850  ? 9   VAL   B CA    1 
ATOM   1463 C  C     . VAL   B 1 10  ? 15.18629  20.36843  42.76222  1.000 40.49088  ? 9   VAL   B C     1 
ATOM   1464 O  O     . VAL   B 1 10  ? 15.67752  21.25773  43.46372  1.000 35.36643  ? 9   VAL   B O     1 
ATOM   1465 C  CB    . VAL   B 1 10  ? 16.59228  18.66379  41.58785  1.000 35.80543  ? 9   VAL   B CB    1 
ATOM   1466 C  CG1   . VAL   B 1 10  ? 17.29354  18.31092  40.30384  1.000 36.64591  ? 9   VAL   B CG1   1 
ATOM   1467 C  CG2   . VAL   B 1 10  ? 17.59419  18.77708  42.74037  1.000 39.98229  ? 9   VAL   B CG2   1 
ATOM   1468 N  N     . GLY   B 1 11  ? 14.11779  19.67372  43.11486  1.000 36.44335  ? 10  GLY   B N     1 
ATOM   1469 C  CA    . GLY   B 1 11  ? 13.36854  19.92881  44.33036  1.000 39.86672  ? 10  GLY   B CA    1 
ATOM   1470 C  C     . GLY   B 1 11  ? 11.94217  19.44027  44.19235  1.000 43.42516  ? 10  GLY   B C     1 
ATOM   1471 O  O     . GLY   B 1 11  ? 11.44950  19.14770  43.10219  1.000 38.91559  ? 10  GLY   B O     1 
ATOM   1472 N  N     . ALA   B 1 12  ? 11.26228  19.34522  45.33446  1.000 38.40872  ? 11  ALA   B N     1 
ATOM   1473 C  CA    . ALA   B 1 12  ? 9.87187   18.91389  45.34979  1.000 40.64583  ? 11  ALA   B CA    1 
ATOM   1474 C  C     . ALA   B 1 12  ? 8.99777   19.89958  44.58510  1.000 41.84860  ? 11  ALA   B C     1 
ATOM   1475 O  O     . ALA   B 1 12  ? 9.40211   21.01724  44.27060  1.000 42.84276  ? 11  ALA   B O     1 
ATOM   1476 C  CB    . ALA   B 1 12  ? 9.36381   18.77553  46.78475  1.000 43.93260  ? 11  ALA   B CB    1 
ATOM   1477 N  N     . GLY   B 1 13  ? 7.77752   19.46478  44.28500  1.000 38.36924  ? 12  GLY   B N     1 
ATOM   1478 C  CA    . GLY   B 1 13  ? 6.86667   20.31434  43.53693  1.000 41.65384  ? 12  GLY   B CA    1 
ATOM   1479 C  C     . GLY   B 1 13  ? 6.55897   21.60039  44.28593  1.000 49.08482  ? 12  GLY   B C     1 
ATOM   1480 O  O     . GLY   B 1 13  ? 6.50675   21.62815  45.51836  1.000 41.19063  ? 12  GLY   B O     1 
ATOM   1481 N  N     . ASP   B 1 14  ? 6.40021   22.68482  43.52231  1.000 45.38276  ? 13  ASP   B N     1 
ATOM   1482 C  CA    . ASP   B 1 14  ? 5.96683   24.00581  43.97767  1.000 45.85142  ? 13  ASP   B CA    1 
ATOM   1483 C  C     . ASP   B 1 14  ? 6.98220   24.74028  44.85493  1.000 44.83244  ? 13  ASP   B C     1 
ATOM   1484 O  O     . ASP   B 1 14  ? 6.62682   25.74568  45.46890  1.000 43.42247  ? 13  ASP   B O     1 
ATOM   1485 C  CB    . ASP   B 1 14  ? 4.62374   23.92529  44.71501  1.000 52.31272  ? 13  ASP   B CB    1 
ATOM   1486 C  CG    . ASP   B 1 14  ? 3.44118   24.09558  43.78572  1.000 58.16108  ? 13  ASP   B CG    1 
ATOM   1487 O  OD1   . ASP   B 1 14  ? 3.16442   23.17411  42.99446  1.000 57.97538  ? 13  ASP   B OD1   1 
ATOM   1488 O  OD2   . ASP   B 1 14  ? 2.78687   25.15551  43.84488  1.000 65.20140  ? 13  ASP   B OD2   1 
ATOM   1489 N  N     . VAL   B 1 15  ? 8.23639   24.29034  44.92623  1.000 41.59331  ? 14  VAL   B N     1 
ATOM   1490 C  CA    . VAL   B 1 15  ? 9.21703   25.02123  45.72933  1.000 45.58180  ? 14  VAL   B CA    1 
ATOM   1491 C  C     . VAL   B 1 15  ? 9.73102   26.27144  45.02402  1.000 49.66703  ? 14  VAL   B C     1 
ATOM   1492 O  O     . VAL   B 1 15  ? 10.35054  27.12502  45.67531  1.000 44.20152  ? 14  VAL   B O     1 
ATOM   1493 C  CB    . VAL   B 1 15  ? 10.41763  24.14442  46.12701  1.000 45.52485  ? 14  VAL   B CB    1 
ATOM   1494 C  CG1   . VAL   B 1 15  ? 9.96234   22.96973  46.97932  1.000 45.27865  ? 14  VAL   B CG1   1 
ATOM   1495 C  CG2   . VAL   B 1 15  ? 11.17219  23.66407  44.89454  1.000 40.89064  ? 14  VAL   B CG2   1 
ATOM   1496 N  N     . GLY   B 1 16  ? 9.50269   26.39976  43.72410  1.000 43.41356  ? 15  GLY   B N     1 
ATOM   1497 C  CA    . GLY   B 1 16  ? 9.92290   27.55323  42.96719  1.000 39.79311  ? 15  GLY   B CA    1 
ATOM   1498 C  C     . GLY   B 1 16  ? 11.08944  27.32045  42.00982  1.000 43.68784  ? 15  GLY   B C     1 
ATOM   1499 O  O     . GLY   B 1 16  ? 11.82825  28.27554  41.72621  1.000 36.43102  ? 15  GLY   B O     1 
ATOM   1500 N  N     . LYS   B 1 17  ? 11.28225  26.09142  41.52432  1.000 34.40297  ? 16  LYS   B N     1 
ATOM   1501 C  CA    . LYS   B 1 17  ? 12.40095  25.81711  40.62533  1.000 35.07261  ? 16  LYS   B CA    1 
ATOM   1502 C  C     . LYS   B 1 17  ? 12.29969  26.65357  39.35739  1.000 37.56458  ? 16  LYS   B C     1 
ATOM   1503 O  O     . LYS   B 1 17  ? 13.28295  27.26711  38.92249  1.000 31.74519  ? 16  LYS   B O     1 
ATOM   1504 C  CB    . LYS   B 1 17  ? 12.44030  24.32508  40.29363  1.000 34.89939  ? 16  LYS   B CB    1 
ATOM   1505 C  CG    . LYS   B 1 17  ? 12.77647  23.43385  41.48035  1.000 29.09444  ? 16  LYS   B CG    1 
ATOM   1506 C  CD    . LYS   B 1 17  ? 12.75163  21.97252  41.06772  1.000 35.97471  ? 16  LYS   B CD    1 
ATOM   1507 C  CE    . LYS   B 1 17  ? 11.39856  21.61880  40.45423  1.000 32.25197  ? 16  LYS   B CE    1 
ATOM   1508 N  NZ    . LYS   B 1 17  ? 10.31803  21.55014  41.47062  1.000 37.86680  ? 16  LYS   B NZ    1 
ATOM   1509 N  N     . SER   B 1 18  ? 11.10635  26.69919  38.76445  1.000 32.38450  ? 17  SER   B N     1 
ATOM   1510 C  CA    . SER   B 1 18  ? 10.90720  27.42892  37.52129  1.000 39.20415  ? 17  SER   B CA    1 
ATOM   1511 C  C     . SER   B 1 18  ? 10.88188  28.93205  37.75861  1.000 41.52702  ? 17  SER   B C     1 
ATOM   1512 O  O     . SER   B 1 18  ? 11.41066  29.70377  36.95231  1.000 33.11129  ? 17  SER   B O     1 
ATOM   1513 C  CB    . SER   B 1 18  ? 9.61048   26.96936  36.85534  1.000 30.68586  ? 17  SER   B CB    1 
ATOM   1514 O  OG    . SER   B 1 18  ? 9.61598   25.55697  36.62853  1.000 30.00551  ? 17  SER   B OG    1 
ATOM   1515 N  N     . ALA   B 1 19  ? 10.23925  29.37170  38.84199  1.000 39.96748  ? 18  ALA   B N     1 
ATOM   1516 C  CA    . ALA   B 1 19  ? 10.20951  30.79817  39.13055  1.000 38.72425  ? 18  ALA   B CA    1 
ATOM   1517 C  C     . ALA   B 1 19  ? 11.61992  31.35361  39.24242  1.000 34.98199  ? 18  ALA   B C     1 
ATOM   1518 O  O     . ALA   B 1 19  ? 11.89905  32.45903  38.76751  1.000 46.88514  ? 18  ALA   B O     1 
ATOM   1519 C  CB    . ALA   B 1 19  ? 9.41519   31.05812  40.41319  1.000 39.82117  ? 18  ALA   B CB    1 
ATOM   1520 N  N     . LEU   B 1 20  ? 12.52576  30.59942  39.86287  1.000 32.22903  ? 19  LEU   B N     1 
ATOM   1521 C  CA    . LEU   B 1 20  ? 13.91336  31.02779  39.93270  1.000 33.16072  ? 19  LEU   B CA    1 
ATOM   1522 C  C     . LEU   B 1 20  ? 14.53021  31.05558  38.53857  1.000 38.48467  ? 19  LEU   B C     1 
ATOM   1523 O  O     . LEU   B 1 20  ? 15.17052  32.03770  38.14326  1.000 35.69602  ? 19  LEU   B O     1 
ATOM   1524 C  CB    . LEU   B 1 20  ? 14.69739  30.09905  40.85599  1.000 33.10610  ? 19  LEU   B CB    1 
ATOM   1525 C  CG    . LEU   B 1 20  ? 14.27796  30.16887  42.33337  1.000 39.99479  ? 19  LEU   B CG    1 
ATOM   1526 C  CD1   . LEU   B 1 20  ? 14.93732  29.06936  43.15086  1.000 37.74285  ? 19  LEU   B CD1   1 
ATOM   1527 C  CD2   . LEU   B 1 20  ? 14.64170  31.53157  42.88514  1.000 47.50133  ? 19  LEU   B CD2   1 
ATOM   1528 N  N     . THR   B 1 21  ? 14.30131  29.99440  37.76739  1.000 35.56140  ? 20  THR   B N     1 
ATOM   1529 C  CA    . THR   B 1 21  ? 14.89683  29.89373  36.44066  1.000 31.39171  ? 20  THR   B CA    1 
ATOM   1530 C  C     . THR   B 1 21  ? 14.35674  30.97463  35.51434  1.000 33.64950  ? 20  THR   B C     1 
ATOM   1531 O  O     . THR   B 1 21  ? 15.12862  31.64951  34.82129  1.000 36.93137  ? 20  THR   B O     1 
ATOM   1532 C  CB    . THR   B 1 21  ? 14.64053  28.48722  35.88730  1.000 30.17350  ? 20  THR   B CB    1 
ATOM   1533 O  OG1   . THR   B 1 21  ? 15.28288  27.53233  36.75060  1.000 31.45943  ? 20  THR   B OG1   1 
ATOM   1534 C  CG2   . THR   B 1 21  ? 15.19142  28.33951  34.45470  1.000 32.99493  ? 20  THR   B CG2   1 
ATOM   1535 N  N     . ILE   B 1 22  ? 13.03801  31.18969  35.52901  1.000 34.63195  ? 21  ILE   B N     1 
ATOM   1536 C  CA    . ILE   B 1 22  ? 12.41945  32.16012  34.62989  1.000 39.49292  ? 21  ILE   B CA    1 
ATOM   1537 C  C     . ILE   B 1 22  ? 12.84024  33.58475  34.98433  1.000 40.07935  ? 21  ILE   B C     1 
ATOM   1538 O  O     . ILE   B 1 22  ? 13.05070  34.41775  34.09244  1.000 34.86169  ? 21  ILE   B O     1 
ATOM   1539 C  CB    . ILE   B 1 22  ? 10.89212  31.98742  34.64078  1.000 38.19669  ? 21  ILE   B CB    1 
ATOM   1540 C  CG1   . ILE   B 1 22  ? 10.52219  30.66869  33.96053  1.000 34.79980  ? 21  ILE   B CG1   1 
ATOM   1541 C  CG2   . ILE   B 1 22  ? 10.19105  33.18408  33.99143  1.000 37.60862  ? 21  ILE   B CG2   1 
ATOM   1542 C  CD1   . ILE   B 1 22  ? 10.90710  30.60366  32.48050  1.000 36.53045  ? 21  ILE   B CD1   1 
ATOM   1543 N  N     . GLN   B 1 23  ? 12.98305  33.88894  36.27736  1.000 37.70126  ? 22  GLN   B N     1 
ATOM   1544 C  CA    . GLN   B 1 23  ? 13.55710  35.17598  36.66111  1.000 37.93407  ? 22  GLN   B CA    1 
ATOM   1545 C  C     . GLN   B 1 23  ? 14.92547  35.36840  36.01876  1.000 39.22976  ? 22  GLN   B C     1 
ATOM   1546 O  O     . GLN   B 1 23  ? 15.19133  36.39996  35.39082  1.000 36.62673  ? 22  GLN   B O     1 
ATOM   1547 C  CB    . GLN   B 1 23  ? 13.66655  35.28416  38.18328  1.000 47.06687  ? 22  GLN   B CB    1 
ATOM   1548 C  CG    . GLN   B 1 23  ? 12.44357  35.88438  38.85889  1.000 44.90750  ? 22  GLN   B CG    1 
ATOM   1549 C  CD    . GLN   B 1 23  ? 12.30874  37.39156  38.64166  1.000 56.62477  ? 22  GLN   B CD    1 
ATOM   1550 O  OE1   . GLN   B 1 23  ? 12.88712  37.96226  37.70916  1.000 46.40965  ? 22  GLN   B OE1   1 
ATOM   1551 N  NE2   . GLN   B 1 23  ? 11.53746  38.04361  39.51344  1.000 48.55870  ? 22  GLN   B NE2   1 
ATOM   1552 N  N     . LEU   B 1 24  ? 15.80143  34.36980  36.15812  1.000 36.52773  ? 23  LEU   B N     1 
ATOM   1553 C  CA    . LEU   B 1 24  ? 17.15337  34.47559  35.62039  1.000 30.51973  ? 23  LEU   B CA    1 
ATOM   1554 C  C     . LEU   B 1 24  ? 17.13912  34.64957  34.10393  1.000 35.59623  ? 23  LEU   B C     1 
ATOM   1555 O  O     . LEU   B 1 24  ? 17.87700  35.47978  33.55978  1.000 33.39494  ? 23  LEU   B O     1 
ATOM   1556 C  CB    . LEU   B 1 24  ? 17.96277  33.24017  36.01074  1.000 30.48369  ? 23  LEU   B CB    1 
ATOM   1557 C  CG    . LEU   B 1 24  ? 19.43665  33.24110  35.60927  1.000 38.35999  ? 23  LEU   B CG    1 
ATOM   1558 C  CD1   . LEU   B 1 24  ? 20.26845  34.10020  36.55756  1.000 37.10749  ? 23  LEU   B CD1   1 
ATOM   1559 C  CD2   . LEU   B 1 24  ? 19.97873  31.82385  35.54483  1.000 34.61207  ? 23  LEU   B CD2   1 
ATOM   1560 N  N     . ILE   B 1 25  ? 16.30616  33.88476  33.40888  1.000 30.96891  ? 24  ILE   B N     1 
ATOM   1561 C  CA    . ILE   B 1 25  ? 16.36346  33.84582  31.95083  1.000 29.69625  ? 24  ILE   B CA    1 
ATOM   1562 C  C     . ILE   B 1 25  ? 15.55022  34.96713  31.32421  1.000 35.27046  ? 24  ILE   B C     1 
ATOM   1563 O  O     . ILE   B 1 25  ? 15.98628  35.58352  30.34616  1.000 37.18052  ? 24  ILE   B O     1 
ATOM   1564 C  CB    . ILE   B 1 25  ? 15.89204  32.46905  31.44922  1.000 33.48483  ? 24  ILE   B CB    1 
ATOM   1565 C  CG1   . ILE   B 1 25  ? 16.82795  31.35755  31.94201  1.000 29.76543  ? 24  ILE   B CG1   1 
ATOM   1566 C  CG2   . ILE   B 1 25  ? 15.72358  32.47348  29.92943  1.000 39.38285  ? 24  ILE   B CG2   1 
ATOM   1567 C  CD1   . ILE   B 1 25  ? 18.26767  31.45695  31.47567  1.000 31.07568  ? 24  ILE   B CD1   1 
ATOM   1568 N  N     . GLN   B 1 26  ? 14.36152  35.25032  31.86290  1.000 32.63810  ? 25  GLN   B N     1 
ATOM   1569 C  CA    . GLN   B 1 26  ? 13.42587  36.15112  31.20590  1.000 35.48731  ? 25  GLN   B CA    1 
ATOM   1570 C  C     . GLN   B 1 26  ? 13.09237  37.38552  32.02919  1.000 40.82573  ? 25  GLN   B C     1 
ATOM   1571 O  O     . GLN   B 1 26  ? 12.31865  38.23280  31.55976  1.000 42.30668  ? 25  GLN   B O     1 
ATOM   1572 C  CB    . GLN   B 1 26  ? 12.14251  35.39727  30.84863  1.000 39.67327  ? 25  GLN   B CB    1 
ATOM   1573 C  CG    . GLN   B 1 26  ? 12.39287  34.27416  29.86847  1.000 40.34136  ? 25  GLN   B CG    1 
ATOM   1574 C  CD    . GLN   B 1 26  ? 11.20767  33.34775  29.72536  1.000 43.28555  ? 25  GLN   B CD    1 
ATOM   1575 O  OE1   . GLN   B 1 26  ? 10.06781  33.72803  29.99659  1.000 43.63212  ? 25  GLN   B OE1   1 
ATOM   1576 N  NE2   . GLN   B 1 26  ? 11.47187  32.11568  29.30298  1.000 44.32731  ? 25  GLN   B NE2   1 
ATOM   1577 N  N     . ASN   B 1 27  ? 13.66041  37.50999  33.22971  1.000 40.11758  ? 26  ASN   B N     1 
ATOM   1578 C  CA    . ASN   B 1 27  ? 13.56801  38.72360  34.04421  1.000 48.36783  ? 26  ASN   B CA    1 
ATOM   1579 C  C     . ASN   B 1 27  ? 12.11624  39.09251  34.35228  1.000 49.84091  ? 26  ASN   B C     1 
ATOM   1580 O  O     . ASN   B 1 27  ? 11.70621  40.24788  34.21208  1.000 42.77503  ? 26  ASN   B O     1 
ATOM   1581 C  CB    . ASN   B 1 27  ? 14.29048  39.89522  33.37425  1.000 43.36676  ? 26  ASN   B CB    1 
ATOM   1582 C  CG    . ASN   B 1 27  ? 14.50341  41.05559  34.31838  1.000 43.75109  ? 26  ASN   B CG    1 
ATOM   1583 O  OD1   . ASN   B 1 27  ? 14.91485  40.86252  35.46035  1.000 45.32797  ? 26  ASN   B OD1   1 
ATOM   1584 N  ND2   . ASN   B 1 27  ? 14.20413  42.26898  33.85367  1.000 45.92277  ? 26  ASN   B ND2   1 
ATOM   1585 N  N     . HIS   B 1 28  ? 11.32434  38.10264  34.75945  1.000 41.85661  ? 27  HIS   B N     1 
ATOM   1586 C  CA    . HIS   B 1 28  ? 9.99798   38.38255  35.28785  1.000 49.06060  ? 27  HIS   B CA    1 
ATOM   1587 C  C     . HIS   B 1 28  ? 9.56217   37.22006  36.16497  1.000 50.05376  ? 27  HIS   B C     1 
ATOM   1588 O  O     . HIS   B 1 28  ? 10.14361  36.13282  36.13579  1.000 39.10648  ? 27  HIS   B O     1 
ATOM   1589 C  CB    . HIS   B 1 28  ? 8.97991   38.66193  34.17461  1.000 43.14613  ? 27  HIS   B CB    1 
ATOM   1590 C  CG    . HIS   B 1 28  ? 8.64872   37.47456  33.32712  1.000 52.59540  ? 27  HIS   B CG    1 
ATOM   1591 N  ND1   . HIS   B 1 28  ? 7.86654   36.43213  33.77677  1.000 52.13342  ? 27  HIS   B ND1   1 
ATOM   1592 C  CD2   . HIS   B 1 28  ? 8.96444   37.18105  32.04310  1.000 43.03887  ? 27  HIS   B CD2   1 
ATOM   1593 C  CE1   . HIS   B 1 28  ? 7.73041   35.53915  32.81238  1.000 50.96824  ? 27  HIS   B CE1   1 
ATOM   1594 N  NE2   . HIS   B 1 28  ? 8.38520   35.97070  31.74930  1.000 46.86859  ? 27  HIS   B NE2   1 
ATOM   1595 N  N     . PHE   B 1 29  ? 8.54107   37.48617  36.97546  1.000 54.98785  ? 28  PHE   B N     1 
ATOM   1596 C  CA    . PHE   B 1 29  ? 7.96723   36.52862  37.90889  1.000 57.08710  ? 28  PHE   B CA    1 
ATOM   1597 C  C     . PHE   B 1 29  ? 6.46019   36.57879  37.73692  1.000 57.38580  ? 28  PHE   B C     1 
ATOM   1598 O  O     . PHE   B 1 29  ? 5.87479   37.66430  37.75327  1.000 60.21711  ? 28  PHE   B O     1 
ATOM   1599 C  CB    . PHE   B 1 29  ? 8.36298   36.86623  39.35670  1.000 53.38653  ? 28  PHE   B CB    1 
ATOM   1600 C  CG    . PHE   B 1 29  ? 7.60261   36.09204  40.40123  1.000 60.21178  ? 28  PHE   B CG    1 
ATOM   1601 C  CD1   . PHE   B 1 29  ? 8.06376   34.86303  40.83943  1.000 57.87423  ? 28  PHE   B CD1   1 
ATOM   1602 C  CD2   . PHE   B 1 29  ? 6.43962   36.60329  40.96044  1.000 64.06203  ? 28  PHE   B CD2   1 
ATOM   1603 C  CE1   . PHE   B 1 29  ? 7.37251   34.14567  41.80395  1.000 55.69983  ? 28  PHE   B CE1   1 
ATOM   1604 C  CE2   . PHE   B 1 29  ? 5.74108   35.89073  41.92182  1.000 68.25042  ? 28  PHE   B CE2   1 
ATOM   1605 C  CZ    . PHE   B 1 29  ? 6.21002   34.66008  42.34537  1.000 64.29821  ? 28  PHE   B CZ    1 
ATOM   1606 N  N     . VAL   B 1 30  ? 5.83568   35.42008  37.54840  1.000 66.10891  ? 29  VAL   B N     1 
ATOM   1607 C  CA    . VAL   B 1 30  ? 4.38337   35.32872  37.44925  1.000 73.08403  ? 29  VAL   B CA    1 
ATOM   1608 C  C     . VAL   B 1 30  ? 3.89703   34.32304  38.47839  1.000 72.00466  ? 29  VAL   B C     1 
ATOM   1609 O  O     . VAL   B 1 30  ? 4.36451   33.17933  38.50443  1.000 68.74242  ? 29  VAL   B O     1 
ATOM   1610 C  CB    . VAL   B 1 30  ? 3.91725   34.92726  36.03824  1.000 74.48316  ? 29  VAL   B CB    1 
ATOM   1611 C  CG1   . VAL   B 1 30  ? 2.41529   34.66665  36.03882  1.000 73.33376  ? 29  VAL   B CG1   1 
ATOM   1612 C  CG2   . VAL   B 1 30  ? 4.27394   36.01958  35.03996  1.000 68.45468  ? 29  VAL   B CG2   1 
ATOM   1613 N  N     . ASP   B 1 31  ? 2.95968   34.74983  39.32224  1.000 78.59820  ? 30  ASP   B N     1 
ATOM   1614 C  CA    . ASP   B 1 31  ? 2.43573   33.89898  40.38230  1.000 80.84327  ? 30  ASP   B CA    1 
ATOM   1615 C  C     . ASP   B 1 31  ? 1.34933   32.98151  39.83792  1.000 80.06123  ? 30  ASP   B C     1 
ATOM   1616 O  O     . ASP   B 1 31  ? 0.25335   32.89923  40.40133  1.000 88.03835  ? 30  ASP   B O     1 
ATOM   1617 C  CB    . ASP   B 1 31  ? 1.90168   34.75559  41.53514  1.000 86.99387  ? 30  ASP   B CB    1 
ATOM   1618 C  CG    . ASP   B 1 31  ? 1.81028   33.99002  42.84386  1.000 86.18023  ? 30  ASP   B CG    1 
ATOM   1619 O  OD1   . ASP   B 1 31  ? 2.80555   33.33807  43.22968  1.000 83.00880  ? 30  ASP   B OD1   1 
ATOM   1620 O  OD2   . ASP   B 1 31  ? 0.74623   34.05377  43.49496  1.000 94.03381  ? 30  ASP   B OD2   1 
ATOM   1621 N  N     . GLU   B 1 32  ? 1.64132   32.29793  38.73963  1.000 74.43070  ? 31  GLU   B N     1 
ATOM   1622 C  CA    . GLU   B 1 32  ? 0.71926   31.34451  38.14874  1.000 74.84013  ? 31  GLU   B CA    1 
ATOM   1623 C  C     . GLU   B 1 32  ? 1.12026   29.92352  38.52826  1.000 74.09458  ? 31  GLU   B C     1 
ATOM   1624 O  O     . GLU   B 1 32  ? 2.16686   29.67998  39.13536  1.000 71.47924  ? 31  GLU   B O     1 
ATOM   1625 C  CB    . GLU   B 1 32  ? 0.67741   31.50843  36.62721  1.000 71.95594  ? 31  GLU   B CB    1 
ATOM   1626 C  CG    . GLU   B 1 32  ? -0.71344  31.75661  36.08355  1.000 68.42966  ? 31  GLU   B CG    1 
ATOM   1627 C  CD    . GLU   B 1 32  ? -0.71054  32.23185  34.64233  1.000 72.42770  ? 31  GLU   B CD    1 
ATOM   1628 O  OE1   . GLU   B 1 32  ? 0.21776   31.86429  33.88775  1.000 64.50242  ? 31  GLU   B OE1   1 
ATOM   1629 O  OE2   . GLU   B 1 32  ? -1.64040  32.97947  34.26496  1.000 73.68173  ? 31  GLU   B OE2   1 
ATOM   1630 N  N     . TYR   B 1 33  ? 0.25448   28.98039  38.17410  1.000 72.93552  ? 32  TYR   B N     1 
ATOM   1631 C  CA    . TYR   B 1 33  ? 0.49045   27.55797  38.39065  1.000 67.25893  ? 32  TYR   B CA    1 
ATOM   1632 C  C     . TYR   B 1 33  ? 0.74623   26.91538  37.03256  1.000 61.99479  ? 32  TYR   B C     1 
ATOM   1633 O  O     . TYR   B 1 33  ? -0.16647  26.80504  36.20615  1.000 57.49852  ? 32  TYR   B O     1 
ATOM   1634 C  CB    . TYR   B 1 33  ? -0.69295  26.90470  39.10158  1.000 68.01396  ? 32  TYR   B CB    1 
ATOM   1635 C  CG    . TYR   B 1 33  ? -0.57041  25.40228  39.21663  1.000 69.12205  ? 32  TYR   B CG    1 
ATOM   1636 C  CD1   . TYR   B 1 33  ? 0.27514   24.82438  40.16120  1.000 62.86981  ? 32  TYR   B CD1   1 
ATOM   1637 C  CD2   . TYR   B 1 33  ? -1.29455  24.55910  38.37568  1.000 62.35632  ? 32  TYR   B CD2   1 
ATOM   1638 C  CE1   . TYR   B 1 33  ? 0.39522   23.45038  40.26766  1.000 59.69548  ? 32  TYR   B CE1   1 
ATOM   1639 C  CE2   . TYR   B 1 33  ? -1.18018  23.18251  38.47428  1.000 57.36888  ? 32  TYR   B CE2   1 
ATOM   1640 C  CZ    . TYR   B 1 33  ? -0.33413  22.63256  39.42411  1.000 62.16053  ? 32  TYR   B CZ    1 
ATOM   1641 O  OH    . TYR   B 1 33  ? -0.21267  21.26255  39.53210  1.000 57.00790  ? 32  TYR   B OH    1 
ATOM   1642 N  N     . ASP   B 1 34  ? 1.98532   26.49703  36.80146  1.000 56.68200  ? 33  ASP   B N     1 
ATOM   1643 C  CA    . ASP   B 1 34  ? 2.38482   25.90084  35.52664  1.000 53.16031  ? 33  ASP   B CA    1 
ATOM   1644 C  C     . ASP   B 1 34  ? 3.39993   24.80190  35.79480  1.000 49.38076  ? 33  ASP   B C     1 
ATOM   1645 O  O     . ASP   B 1 34  ? 4.61591   25.01057  35.68911  1.000 44.92920  ? 33  ASP   B O     1 
ATOM   1646 C  CB    . ASP   B 1 34  ? 2.95325   26.95709  34.57805  1.000 54.70906  ? 33  ASP   B CB    1 
ATOM   1647 C  CG    . ASP   B 1 34  ? 3.19423   26.41307  33.19622  1.000 55.17882  ? 33  ASP   B CG    1 
ATOM   1648 O  OD1   . ASP   B 1 34  ? 2.63677   25.33748  32.88258  1.000 56.41319  ? 33  ASP   B OD1   1 
ATOM   1649 O  OD2   . ASP   B 1 34  ? 3.94321   27.05177  32.42776  1.000 64.26878  ? 33  ASP   B OD2   1 
ATOM   1650 N  N     . PRO   B 1 35  ? 2.93191   23.60504  36.14077  1.000 41.28553  ? 34  PRO   B N     1 
ATOM   1651 C  CA    . PRO   B 1 35  ? 3.86110   22.52402  36.48053  1.000 39.84231  ? 34  PRO   B CA    1 
ATOM   1652 C  C     . PRO   B 1 35  ? 4.68611   22.08787  35.27306  1.000 30.98151  ? 34  PRO   B C     1 
ATOM   1653 O  O     . PRO   B 1 35  ? 4.17870   21.95863  34.15540  1.000 34.27442  ? 34  PRO   B O     1 
ATOM   1654 C  CB    . PRO   B 1 35  ? 2.93397   21.40532  36.97367  1.000 42.40513  ? 34  PRO   B CB    1 
ATOM   1655 C  CG    . PRO   B 1 35  ? 1.62138   21.67493  36.27159  1.000 43.77373  ? 34  PRO   B CG    1 
ATOM   1656 C  CD    . PRO   B 1 35  ? 1.52265   23.17694  36.20814  1.000 52.92281  ? 34  PRO   B CD    1 
ATOM   1657 N  N     . THR   B 1 36  ? 5.97101   21.85600  35.52922  1.000 35.03040  ? 35  THR   B N     1 
ATOM   1658 C  CA    . THR   B 1 36  ? 6.97684   21.57734  34.50731  1.000 30.45493  ? 35  THR   B CA    1 
ATOM   1659 C  C     . THR   B 1 36  ? 7.00288   20.10001  34.12965  1.000 32.11842  ? 35  THR   B C     1 
ATOM   1660 O  O     . THR   B 1 36  ? 6.84135   19.22402  34.98482  1.000 30.68338  ? 35  THR   B O     1 
ATOM   1661 C  CB    . THR   B 1 36  ? 8.35112   21.99922  35.03761  1.000 30.60162  ? 35  THR   B CB    1 
ATOM   1662 O  OG1   . THR   B 1 36  ? 8.32665   23.39030  35.38137  1.000 35.38637  ? 35  THR   B OG1   1 
ATOM   1663 C  CG2   . THR   B 1 36  ? 9.49060   21.70971  34.05200  1.000 24.91895  ? 35  THR   B CG2   1 
ATOM   1664 N  N     . ILE   B 1 37  ? 7.22203   19.82484  32.83973  1.000 27.93236  ? 36  ILE   B N     1 
ATOM   1665 C  CA    . ILE   B 1 37  ? 7.61835   18.48610  32.41556  1.000 27.13714  ? 36  ILE   B CA    1 
ATOM   1666 C  C     . ILE   B 1 37  ? 9.13853   18.43473  32.46994  1.000 24.30631  ? 36  ILE   B C     1 
ATOM   1667 O  O     . ILE   B 1 37  ? 9.72213   17.69099  33.26142  1.000 25.05228  ? 36  ILE   B O     1 
ATOM   1668 C  CB    . ILE   B 1 37  ? 7.10194   18.14412  31.00263  1.000 28.52946  ? 36  ILE   B CB    1 
ATOM   1669 C  CG1   . ILE   B 1 37  ? 5.57971   18.38674  30.88745  1.000 33.97664  ? 36  ILE   B CG1   1 
ATOM   1670 C  CG2   . ILE   B 1 37  ? 7.49606   16.70743  30.62598  1.000 25.10835  ? 36  ILE   B CG2   1 
ATOM   1671 C  CD1   . ILE   B 1 37  ? 4.72924   17.38929  31.63985  1.000 31.53583  ? 36  ILE   B CD1   1 
ATOM   1672 N  N     . GLU   B 1 38  ? 9.78320   19.23087  31.61274  1.000 23.63345  ? 37  GLU   B N     1 
ATOM   1673 C  CA    . GLU   B 1 38  ? 11.22539  19.42669  31.59942  1.000 23.79260  ? 37  GLU   B CA    1 
ATOM   1674 C  C     . GLU   B 1 38  ? 11.50656  20.53877  30.60286  1.000 25.23107  ? 37  GLU   B C     1 
ATOM   1675 O  O     . GLU   B 1 38  ? 10.98771  20.49398  29.48337  1.000 26.20940  ? 37  GLU   B O     1 
ATOM   1676 C  CB    . GLU   B 1 38  ? 11.97342  18.14553  31.20724  1.000 23.79420  ? 37  GLU   B CB    1 
ATOM   1677 C  CG    . GLU   B 1 38  ? 13.49552  18.25703  31.29349  1.000 26.33092  ? 37  GLU   B CG    1 
ATOM   1678 C  CD    . GLU   B 1 38  ? 14.18473  16.92605  31.05126  1.000 30.49423  ? 37  GLU   B CD    1 
ATOM   1679 O  OE1   . GLU   B 1 38  ? 14.16981  16.05855  31.95386  1.000 41.44396  ? 37  GLU   B OE1   1 
ATOM   1680 O  OE2   . GLU   B 1 38  ? 14.73447  16.74763  29.95498  1.000 38.96737  ? 37  GLU   B OE2   1 
ATOM   1681 N  N     . ASP   B 1 39  ? 12.28943  21.54731  30.99800  1.000 24.01012  ? 38  ASP   B N     1 
ATOM   1682 C  CA    . ASP   B 1 39  ? 12.64020  22.65161  30.11377  1.000 24.74674  ? 38  ASP   B CA    1 
ATOM   1683 C  C     . ASP   B 1 39  ? 14.13275  22.92242  30.20598  1.000 24.93430  ? 38  ASP   B C     1 
ATOM   1684 O  O     . ASP   B 1 39  ? 14.74999  22.68930  31.24674  1.000 24.79531  ? 38  ASP   B O     1 
ATOM   1685 C  CB    . ASP   B 1 39  ? 11.85785  23.92463  30.47127  1.000 23.60247  ? 38  ASP   B CB    1 
ATOM   1686 C  CG    . ASP   B 1 39  ? 10.38057  23.81005  30.15982  1.000 26.48470  ? 38  ASP   B CG    1 
ATOM   1687 O  OD1   . ASP   B 1 39  ? 10.02777  23.56725  28.98606  1.000 32.02795  ? 38  ASP   B OD1   1 
ATOM   1688 O  OD2   . ASP   B 1 39  ? 9.56687   23.98134  31.09272  1.000 37.87786  ? 38  ASP   B OD2   1 
ATOM   1689 N  N     . SER   B 1 40  ? 14.71800  23.40612  29.10195  1.000 23.95349  ? 39  SER   B N     1 
ATOM   1690 C  CA    . SER   B 1 40  ? 16.14100  23.73975  29.04275  1.000 25.02096  ? 39  SER   B CA    1 
ATOM   1691 C  C     . SER   B 1 40  ? 16.32723  25.18213  28.59058  1.000 26.09723  ? 39  SER   B C     1 
ATOM   1692 O  O     . SER   B 1 40  ? 15.58018  25.68323  27.74851  1.000 25.07487  ? 39  SER   B O     1 
ATOM   1693 C  CB    . SER   B 1 40  ? 16.89384  22.82508  28.06775  1.000 28.14586  ? 39  SER   B CB    1 
ATOM   1694 O  OG    . SER   B 1 40  ? 16.91812  21.49899  28.54079  1.000 39.90513  ? 39  SER   B OG    1 
ATOM   1695 N  N     . TYR   B 1 41  ? 17.34442  25.83941  29.13474  1.000 22.14412  ? 40  TYR   B N     1 
ATOM   1696 C  CA    . TYR   B 1 41  ? 17.64887  27.22708  28.81051  1.000 26.82293  ? 40  TYR   B CA    1 
ATOM   1697 C  C     . TYR   B 1 41  ? 19.15768  27.40236  28.71159  1.000 24.75688  ? 40  TYR   B C     1 
ATOM   1698 O  O     . TYR   B 1 41  ? 19.91644  26.69513  29.37103  1.000 29.00233  ? 40  TYR   B O     1 
ATOM   1699 C  CB    . TYR   B 1 41  ? 17.08537  28.19494  29.85803  1.000 27.91031  ? 40  TYR   B CB    1 
ATOM   1700 C  CG    . TYR   B 1 41  ? 15.60573  28.01209  30.07012  1.000 32.36430  ? 40  TYR   B CG    1 
ATOM   1701 C  CD1   . TYR   B 1 41  ? 14.68628  28.64355  29.24788  1.000 26.73766  ? 40  TYR   B CD1   1 
ATOM   1702 C  CD2   . TYR   B 1 41  ? 15.12421  27.18857  31.08853  1.000 29.78524  ? 40  TYR   B CD2   1 
ATOM   1703 C  CE1   . TYR   B 1 41  ? 13.31169  28.46842  29.44443  1.000 36.42227  ? 40  TYR   B CE1   1 
ATOM   1704 C  CE2   . TYR   B 1 41  ? 13.76949  27.00101  31.28067  1.000 29.68420  ? 40  TYR   B CE2   1 
ATOM   1705 C  CZ    . TYR   B 1 41  ? 12.86447  27.64594  30.46546  1.000 33.97117  ? 40  TYR   B CZ    1 
ATOM   1706 O  OH    . TYR   B 1 41  ? 11.50574  27.46133  30.66424  1.000 31.24811  ? 40  TYR   B OH    1 
ATOM   1707 N  N     . ARG   B 1 42  ? 19.58385  28.36121  27.89392  1.000 24.44370  ? 41  ARG   B N     1 
ATOM   1708 C  CA    . ARG   B 1 42  ? 20.98831  28.75250  27.80156  1.000 26.27993  ? 41  ARG   B CA    1 
ATOM   1709 C  C     . ARG   B 1 42  ? 21.08400  30.25222  27.99331  1.000 24.27596  ? 41  ARG   B C     1 
ATOM   1710 O  O     . ARG   B 1 42  ? 20.31894  31.00433  27.38574  1.000 23.56484  ? 41  ARG   B O     1 
ATOM   1711 C  CB    . ARG   B 1 42  ? 21.61639  28.40337  26.44800  1.000 29.47088  ? 41  ARG   B CB    1 
ATOM   1712 C  CG    . ARG   B 1 42  ? 21.62054  26.94752  26.12545  1.000 29.10044  ? 41  ARG   B CG    1 
ATOM   1713 C  CD    . ARG   B 1 42  ? 22.34236  26.70612  24.82870  1.000 37.72473  ? 41  ARG   B CD    1 
ATOM   1714 N  NE    . ARG   B 1 42  ? 23.16329  25.51743  24.98127  1.000 47.54252  ? 41  ARG   B NE    1 
ATOM   1715 C  CZ    . ARG   B 1 42  ? 24.44524  25.44861  24.66701  1.000 30.58782  ? 41  ARG   B CZ    1 
ATOM   1716 N  NH1   . ARG   B 1 42  ? 25.06657  26.46068  24.08473  1.000 39.12586  ? 41  ARG   B NH1   1 
ATOM   1717 N  NH2   . ARG   B 1 42  ? 25.10639  24.32815  24.91956  1.000 41.94520  ? 41  ARG   B NH2   1 
ATOM   1718 N  N     . LYS   B 1 43  ? 22.03794  30.68342  28.80735  1.000 23.31648  ? 42  LYS   B N     1 
ATOM   1719 C  CA    . LYS   B 1 43  ? 22.29179  32.10531  28.98619  1.000 26.86182  ? 42  LYS   B CA    1 
ATOM   1720 C  C     . LYS   B 1 43  ? 23.77529  32.30977  29.23077  1.000 28.13573  ? 42  LYS   B C     1 
ATOM   1721 O  O     . LYS   B 1 43  ? 24.35745  31.61850  30.07001  1.000 27.68658  ? 42  LYS   B O     1 
ATOM   1722 C  CB    . LYS   B 1 43  ? 21.50553  32.66598  30.16288  1.000 32.71636  ? 42  LYS   B CB    1 
ATOM   1723 C  CG    . LYS   B 1 43  ? 21.70634  34.14393  30.35402  1.000 27.79806  ? 42  LYS   B CG    1 
ATOM   1724 C  CD    . LYS   B 1 43  ? 21.08410  34.58823  31.66342  1.000 28.00198  ? 42  LYS   B CD    1 
ATOM   1725 C  CE    . LYS   B 1 43  ? 20.96886  36.09205  31.70428  1.000 31.58415  ? 42  LYS   B CE    1 
ATOM   1726 N  NZ    . LYS   B 1 43  ? 20.54359  36.50822  33.06562  1.000 46.60757  ? 42  LYS   B NZ    1 
ATOM   1727 N  N     . GLN   B 1 44  ? 24.38627  33.24782  28.51481  1.000 25.52237  ? 43  GLN   B N     1 
ATOM   1728 C  CA    . GLN   B 1 44  ? 25.76743  33.59322  28.81942  1.000 28.19071  ? 43  GLN   B CA    1 
ATOM   1729 C  C     . GLN   B 1 44  ? 25.78567  34.70260  29.86383  1.000 27.48824  ? 43  GLN   B C     1 
ATOM   1730 O  O     . GLN   B 1 44  ? 24.95140  35.61125  29.83970  1.000 29.10469  ? 43  GLN   B O     1 
ATOM   1731 C  CB    . GLN   B 1 44  ? 26.54776  33.99874  27.56149  1.000 29.62525  ? 43  GLN   B CB    1 
ATOM   1732 C  CG    . GLN   B 1 44  ? 26.16623  35.30397  26.89253  1.000 27.93123  ? 43  GLN   B CG    1 
ATOM   1733 C  CD    . GLN   B 1 44  ? 27.24200  35.73708  25.89549  1.000 26.55227  ? 43  GLN   B CD    1 
ATOM   1734 O  OE1   . GLN   B 1 44  ? 28.35534  36.08832  26.29043  1.000 26.25510  ? 43  GLN   B OE1   1 
ATOM   1735 N  NE2   . GLN   B 1 44  ? 26.92427  35.67910  24.60093  1.000 32.05896  ? 43  GLN   B NE2   1 
ATOM   1736 N  N     . VAL   B 1 45  ? 26.71594  34.58840  30.81159  1.000 29.27929  ? 44  VAL   B N     1 
ATOM   1737 C  CA    . VAL   B 1 45  ? 26.80353  35.46806  31.96866  1.000 33.21166  ? 44  VAL   B CA    1 
ATOM   1738 C  C     . VAL   B 1 45  ? 28.27275  35.76737  32.22899  1.000 37.32175  ? 44  VAL   B C     1 
ATOM   1739 O  O     . VAL   B 1 45  ? 29.17099  35.14215  31.66213  1.000 31.90643  ? 44  VAL   B O     1 
ATOM   1740 C  CB    . VAL   B 1 45  ? 26.15542  34.84690  33.22659  1.000 33.59498  ? 44  VAL   B CB    1 
ATOM   1741 C  CG1   . VAL   B 1 45  ? 24.65829  34.65128  33.01301  1.000 34.10921  ? 44  VAL   B CG1   1 
ATOM   1742 C  CG2   . VAL   B 1 45  ? 26.81334  33.52453  33.54841  1.000 33.33758  ? 44  VAL   B CG2   1 
ATOM   1743 N  N     . VAL   B 1 46  ? 28.51538  36.74746  33.09146  1.000 30.60146  ? 45  VAL   B N     1 
ATOM   1744 C  CA    . VAL   B 1 46  ? 29.85999  37.03500  33.57013  1.000 32.97649  ? 45  VAL   B CA    1 
ATOM   1745 C  C     . VAL   B 1 46  ? 29.85281  36.84005  35.07762  1.000 35.16359  ? 45  VAL   B C     1 
ATOM   1746 O  O     . VAL   B 1 46  ? 29.06152  37.47716  35.78480  1.000 37.63231  ? 45  VAL   B O     1 
ATOM   1747 C  CB    . VAL   B 1 46  ? 30.32360  38.44912  33.19698  1.000 34.83679  ? 45  VAL   B CB    1 
ATOM   1748 C  CG1   . VAL   B 1 46  ? 31.72898  38.66947  33.70180  1.000 39.09951  ? 45  VAL   B CG1   1 
ATOM   1749 C  CG2   . VAL   B 1 46  ? 30.28204  38.64635  31.68710  1.000 37.33277  ? 45  VAL   B CG2   1 
ATOM   1750 N  N     . ILE   B 1 47  ? 30.71850  35.95043  35.55856  1.000 35.89789  ? 46  ILE   B N     1 
ATOM   1751 C  CA    . ILE   B 1 47  ? 30.78342  35.56219  36.96332  1.000 38.23238  ? 46  ILE   B CA    1 
ATOM   1752 C  C     . ILE   B 1 47  ? 32.21417  35.76065  37.44494  1.000 41.31170  ? 46  ILE   B C     1 
ATOM   1753 O  O     . ILE   B 1 47  ? 33.12826  35.06174  36.98786  1.000 40.91165  ? 46  ILE   B O     1 
ATOM   1754 C  CB    . ILE   B 1 47  ? 30.34085  34.10592  37.18434  1.000 40.80224  ? 46  ILE   B CB    1 
ATOM   1755 C  CG1   . ILE   B 1 47  ? 28.84685  33.94695  36.87538  1.000 39.51316  ? 46  ILE   B CG1   1 
ATOM   1756 C  CG2   . ILE   B 1 47  ? 30.63302  33.67025  38.62734  1.000 45.24626  ? 46  ILE   B CG2   1 
ATOM   1757 C  CD1   . ILE   B 1 47  ? 28.37056  32.52198  36.94099  1.000 35.80893  ? 46  ILE   B CD1   1 
ATOM   1758 N  N     . ASP   B 1 48  ? 32.40445  36.69615  38.37526  1.000 44.71737  ? 47  ASP   B N     1 
ATOM   1759 C  CA    . ASP   B 1 48  ? 33.73861  37.02560  38.87282  1.000 48.25463  ? 47  ASP   B CA    1 
ATOM   1760 C  C     . ASP   B 1 48  ? 34.67613  37.33536  37.70743  1.000 47.54665  ? 47  ASP   B C     1 
ATOM   1761 O  O     . ASP   B 1 48  ? 35.80269  36.84486  37.63565  1.000 48.97577  ? 47  ASP   B O     1 
ATOM   1762 C  CB    . ASP   B 1 48  ? 34.29592  35.89924  39.74706  1.000 49.88114  ? 47  ASP   B CB    1 
ATOM   1763 C  CG    . ASP   B 1 48  ? 33.42329  35.60941  40.96151  1.000 51.08918  ? 47  ASP   B CG    1 
ATOM   1764 O  OD1   . ASP   B 1 48  ? 32.71246  36.52665  41.42395  1.000 52.34986  ? 47  ASP   B OD1   1 
ATOM   1765 O  OD2   . ASP   B 1 48  ? 33.45042  34.46410  41.45117  1.000 51.07866  ? 47  ASP   B OD2   1 
ATOM   1766 N  N     . GLY   B 1 49  ? 34.17633  38.12067  36.75616  1.000 45.56747  ? 48  GLY   B N     1 
ATOM   1767 C  CA    . GLY   B 1 49  ? 34.95052  38.54675  35.61197  1.000 45.07530  ? 48  GLY   B CA    1 
ATOM   1768 C  C     . GLY   B 1 49  ? 35.13402  37.51745  34.50678  1.000 45.26126  ? 48  GLY   B C     1 
ATOM   1769 O  O     . GLY   B 1 49  ? 35.77684  37.83106  33.49782  1.000 46.58179  ? 48  GLY   B O     1 
ATOM   1770 N  N     . GLU   B 1 50  ? 34.60772  36.30075  34.64376  1.000 40.10102  ? 49  GLU   B N     1 
ATOM   1771 C  CA    . GLU   B 1 50  ? 34.79895  35.25579  33.64189  1.000 38.02972  ? 49  GLU   B CA    1 
ATOM   1772 C  C     . GLU   B 1 50  ? 33.48658  34.98648  32.92599  1.000 42.01498  ? 49  GLU   B C     1 
ATOM   1773 O  O     . GLU   B 1 50  ? 32.48794  34.61023  33.55447  1.000 36.88222  ? 49  GLU   B O     1 
ATOM   1774 C  CB    . GLU   B 1 50  ? 35.32024  33.96333  34.26002  1.000 53.64283  ? 49  GLU   B CB    1 
ATOM   1775 C  CG    . GLU   B 1 50  ? 35.74396  32.92018  33.21859  1.000 47.73843  ? 49  GLU   B CG    1 
ATOM   1776 C  CD    . GLU   B 1 50  ? 36.69521  31.90457  33.80234  1.000 60.59914  ? 49  GLU   B CD    1 
ATOM   1777 O  OE1   . GLU   B 1 50  ? 36.64096  31.69345  35.04169  1.000 72.28972  ? 49  GLU   B OE1   1 
ATOM   1778 O  OE2   . GLU   B 1 50  ? 37.52255  31.32870  33.04824  1.000 71.67120  ? 49  GLU   B OE2   1 
ATOM   1779 N  N     . THR   B 1 51  ? 33.50394  35.16768  31.61307  1.000 36.06696  ? 50  THR   B N     1 
ATOM   1780 C  CA    . THR   B 1 51  ? 32.33703  34.87125  30.80045  1.000 38.43272  ? 50  THR   B CA    1 
ATOM   1781 C  C     . THR   B 1 51  ? 32.12840  33.36376  30.72414  1.000 36.40921  ? 50  THR   B C     1 
ATOM   1782 O  O     . THR   B 1 51  ? 33.07125  32.60618  30.49149  1.000 35.75577  ? 50  THR   B O     1 
ATOM   1783 C  CB    . THR   B 1 51  ? 32.52069  35.45220  29.39937  1.000 33.94201  ? 50  THR   B CB    1 
ATOM   1784 O  OG1   . THR   B 1 51  ? 32.73540  36.86517  29.50573  1.000 37.24147  ? 50  THR   B OG1   1 
ATOM   1785 C  CG2   . THR   B 1 51  ? 31.28869  35.18913  28.54841  1.000 31.73786  ? 50  THR   B CG2   1 
ATOM   1786 N  N     . CYS   B 1 52  ? 30.89269  32.92247  30.94656  1.000 34.32971  ? 51  CYS   B N     1 
ATOM   1787 C  CA    . CYS   B 1 52  ? 30.58910  31.50555  30.82460  1.000 34.23364  ? 51  CYS   B CA    1 
ATOM   1788 C  C     . CYS   B 1 52  ? 29.15527  31.34550  30.33433  1.000 27.22843  ? 51  CYS   B C     1 
ATOM   1789 O  O     . CYS   B 1 52  ? 28.36649  32.29148  30.32704  1.000 28.78655  ? 51  CYS   B O     1 
ATOM   1790 C  CB    . CYS   B 1 52  ? 30.81956  30.75955  32.14404  1.000 31.70265  ? 51  CYS   B CB    1 
ATOM   1791 S  SG    . CYS   B 1 52  ? 29.83220  31.30753  33.54989  1.000 38.76402  ? 51  CYS   B SG    1 
ATOM   1792 N  N     . LEU   B 1 53  ? 28.84250  30.13061  29.89508  1.000 28.16935  ? 52  LEU   B N     1 
ATOM   1793 C  CA    . LEU   B 1 53  ? 27.54733  29.79406  29.30532  1.000 27.09945  ? 52  LEU   B CA    1 
ATOM   1794 C  C     . LEU   B 1 53  ? 26.81593  28.87093  30.26846  1.000 26.11890  ? 52  LEU   B C     1 
ATOM   1795 O  O     . LEU   B 1 53  ? 27.31009  27.78562  30.58810  1.000 28.85301  ? 52  LEU   B O     1 
ATOM   1796 C  CB    . LEU   B 1 53  ? 27.75152  29.11954  27.95020  1.000 24.68525  ? 52  LEU   B CB    1 
ATOM   1797 C  CG    . LEU   B 1 53  ? 26.53093  28.86097  27.06551  1.000 23.20016  ? 52  LEU   B CG    1 
ATOM   1798 C  CD1   . LEU   B 1 53  ? 25.83348  30.16511  26.80879  1.000 27.78110  ? 52  LEU   B CD1   1 
ATOM   1799 C  CD2   . LEU   B 1 53  ? 27.00131  28.23905  25.75987  1.000 35.02160  ? 52  LEU   B CD2   1 
ATOM   1800 N  N     . LEU   B 1 54  ? 25.66098  29.30416  30.75293  1.000 27.03385  ? 53  LEU   B N     1 
ATOM   1801 C  CA    . LEU   B 1 54  ? 24.88904  28.50520  31.69568  1.000 29.88863  ? 53  LEU   B CA    1 
ATOM   1802 C  C     . LEU   B 1 54  ? 23.89429  27.67088  30.90574  1.000 30.18549  ? 53  LEU   B C     1 
ATOM   1803 O  O     . LEU   B 1 54  ? 23.07381  28.22113  30.17187  1.000 27.32356  ? 53  LEU   B O     1 
ATOM   1804 C  CB    . LEU   B 1 54  ? 24.14600  29.37385  32.70789  1.000 27.50119  ? 53  LEU   B CB    1 
ATOM   1805 C  CG    . LEU   B 1 54  ? 24.99346  30.36075  33.51021  1.000 29.13224  ? 53  LEU   B CG    1 
ATOM   1806 C  CD1   . LEU   B 1 54  ? 24.17814  30.95495  34.62319  1.000 32.99580  ? 53  LEU   B CD1   1 
ATOM   1807 C  CD2   . LEU   B 1 54  ? 26.26149  29.70103  34.03286  1.000 29.44094  ? 53  LEU   B CD2   1 
ATOM   1808 N  N     . ASP   B 1 55  ? 23.98303  26.35839  31.05507  1.000 28.04750  ? 54  ASP   B N     1 
ATOM   1809 C  CA    . ASP   B 1 55  ? 23.08012  25.38879  30.43924  1.000 27.65029  ? 54  ASP   B CA    1 
ATOM   1810 C  C     . ASP   B 1 55  ? 22.20734  24.85373  31.56990  1.000 27.50716  ? 54  ASP   B C     1 
ATOM   1811 O  O     . ASP   B 1 55  ? 22.68571  24.07465  32.39163  1.000 31.55164  ? 54  ASP   B O     1 
ATOM   1812 C  CB    . ASP   B 1 55  ? 23.91353  24.28811  29.79275  1.000 29.40900  ? 54  ASP   B CB    1 
ATOM   1813 C  CG    . ASP   B 1 55  ? 23.12270  23.41502  28.87280  1.000 39.98714  ? 54  ASP   B CG    1 
ATOM   1814 O  OD1   . ASP   B 1 55  ? 21.91134  23.24707  29.10797  1.000 45.94683  ? 54  ASP   B OD1   1 
ATOM   1815 O  OD2   . ASP   B 1 55  ? 23.72627  22.89088  27.91396  1.000 42.76277  ? 54  ASP   B OD2   1 
ATOM   1816 N  N     . ILE   B 1 56  ? 20.93763  25.25714  31.61693  1.000 24.98249  ? 55  ILE   B N     1 
ATOM   1817 C  CA    . ILE   B 1 56  ? 20.09403  25.07084  32.79765  1.000 24.52669  ? 55  ILE   B CA    1 
ATOM   1818 C  C     . ILE   B 1 56  ? 18.93884  24.13443  32.48028  1.000 26.47574  ? 55  ILE   B C     1 
ATOM   1819 O  O     . ILE   B 1 56  ? 18.16594  24.36382  31.53429  1.000 29.46903  ? 55  ILE   B O     1 
ATOM   1820 C  CB    . ILE   B 1 56  ? 19.59425  26.41880  33.33979  1.000 28.96465  ? 55  ILE   B CB    1 
ATOM   1821 C  CG1   . ILE   B 1 56  ? 20.80784  27.25955  33.74713  1.000 32.29246  ? 55  ILE   B CG1   1 
ATOM   1822 C  CG2   . ILE   B 1 56  ? 18.65696  26.19780  34.54187  1.000 30.26438  ? 55  ILE   B CG2   1 
ATOM   1823 C  CD1   . ILE   B 1 56  ? 20.46176  28.63257  34.21818  1.000 35.39125  ? 55  ILE   B CD1   1 
ATOM   1824 N  N     . LEU   B 1 57  ? 18.82345  23.07196  33.26876  1.000 22.25967  ? 56  LEU   B N     1 
ATOM   1825 C  CA    . LEU   B 1 57  ? 17.73255  22.12244  33.15000  1.000 22.95777  ? 56  LEU   B CA    1 
ATOM   1826 C  C     . LEU   B 1 57  ? 16.77103  22.36250  34.30139  1.000 25.48394  ? 56  LEU   B C     1 
ATOM   1827 O  O     . LEU   B 1 57  ? 17.15899  22.24204  35.46845  1.000 26.86944  ? 56  LEU   B O     1 
ATOM   1828 C  CB    . LEU   B 1 57  ? 18.25392  20.69291  33.18061  1.000 23.88598  ? 56  LEU   B CB    1 
ATOM   1829 C  CG    . LEU   B 1 57  ? 17.17704  19.66570  32.83975  1.000 22.79606  ? 56  LEU   B CG    1 
ATOM   1830 C  CD1   . LEU   B 1 57  ? 16.75043  19.83546  31.37820  1.000 27.23597  ? 56  LEU   B CD1   1 
ATOM   1831 C  CD2   . LEU   B 1 57  ? 17.69441  18.26602  33.08030  1.000 25.12538  ? 56  LEU   B CD2   1 
ATOM   1832 N  N     . ASP   B 1 58  ? 15.53942  22.71530  33.97273  1.000 22.18463  ? 57  ASP   B N     1 
ATOM   1833 C  CA    . ASP   B 1 58  ? 14.48307  22.92051  34.95849  1.000 21.82338  ? 57  ASP   B CA    1 
ATOM   1834 C  C     . ASP   B 1 58  ? 13.64405  21.64829  34.97210  1.000 25.41730  ? 57  ASP   B C     1 
ATOM   1835 O  O     . ASP   B 1 58  ? 13.00646  21.31133  33.96824  1.000 25.70767  ? 57  ASP   B O     1 
ATOM   1836 C  CB    . ASP   B 1 58  ? 13.66003  24.15361  34.58969  1.000 23.74864  ? 57  ASP   B CB    1 
ATOM   1837 C  CG    . ASP   B 1 58  ? 12.51504  24.41818  35.53851  1.000 27.84533  ? 57  ASP   B CG    1 
ATOM   1838 O  OD1   . ASP   B 1 58  ? 12.52997  23.88734  36.66466  1.000 29.29426  ? 57  ASP   B OD1   1 
ATOM   1839 O  OD2   . ASP   B 1 58  ? 11.61092  25.16980  35.14013  1.000 32.42167  ? 57  ASP   B OD2   1 
ATOM   1840 N  N     . THR   B 1 59  ? 13.65942  20.92724  36.09296  1.000 24.28771  ? 58  THR   B N     1 
ATOM   1841 C  CA    . THR   B 1 59  ? 13.06132  19.60130  36.13924  1.000 24.00535  ? 58  THR   B CA    1 
ATOM   1842 C  C     . THR   B 1 59  ? 11.72168  19.62533  36.86093  1.000 29.27960  ? 58  THR   B C     1 
ATOM   1843 O  O     . THR   B 1 59  ? 11.35241  20.59597  37.52820  1.000 31.50448  ? 58  THR   B O     1 
ATOM   1844 C  CB    . THR   B 1 59  ? 13.99453  18.59515  36.81271  1.000 27.47633  ? 58  THR   B CB    1 
ATOM   1845 O  OG1   . THR   B 1 59  ? 14.02347  18.84557  38.23027  1.000 25.97323  ? 58  THR   B OG1   1 
ATOM   1846 C  CG2   . THR   B 1 59  ? 15.39786  18.69545  36.25038  1.000 26.46717  ? 58  THR   B CG2   1 
ATOM   1847 N  N     . ALA   B 1 60  ? 11.00121  18.51430  36.73062  1.000 27.93522  ? 59  ALA   B N     1 
ATOM   1848 C  CA    . ALA   B 1 60  ? 9.67823   18.37688  37.31515  1.000 32.82527  ? 59  ALA   B CA    1 
ATOM   1849 C  C     . ALA   B 1 60  ? 9.76779   17.91199  38.76334  1.000 33.06334  ? 59  ALA   B C     1 
ATOM   1850 O  O     . ALA   B 1 60  ? 10.54777  17.01897  39.10277  1.000 29.36075  ? 59  ALA   B O     1 
ATOM   1851 C  CB    . ALA   B 1 60  ? 8.83540   17.38596  36.50667  1.000 30.50985  ? 59  ALA   B CB    1 
ATOM   1852 N  N     . GLY   B 1 61  ? 8.94190   18.51054  39.61301  1.000 32.55275  ? 60  GLY   B N     1 
ATOM   1853 C  CA    . GLY   B 1 61  ? 8.83559   18.04894  40.98465  1.000 38.81140  ? 60  GLY   B CA    1 
ATOM   1854 C  C     . GLY   B 1 61  ? 7.75273   17.00042  41.14050  1.000 40.89586  ? 60  GLY   B C     1 
ATOM   1855 O  O     . GLY   B 1 61  ? 6.65490   17.30342  41.61342  1.000 47.87405  ? 60  GLY   B O     1 
ATOM   1856 N  N     . GLN   B 1 62  ? 8.03703   15.76423  40.74007  1.000 48.84418  ? 61  GLN   B N     1 
ATOM   1857 C  CA    . GLN   B 1 62  ? 7.07184   14.67859  40.86231  1.000 50.03789  ? 61  GLN   B CA    1 
ATOM   1858 C  C     . GLN   B 1 62  ? 7.70547   13.49731  41.56763  1.000 56.08978  ? 61  GLN   B C     1 
ATOM   1859 O  O     . GLN   B 1 62  ? 8.76282   13.01484  41.14854  1.000 62.58003  ? 61  GLN   B O     1 
ATOM   1860 C  CB    . GLN   B 1 62  ? 6.56620   14.20948  39.51017  1.000 56.72150  ? 61  GLN   B CB    1 
ATOM   1861 C  CG    . GLN   B 1 62  ? 6.12397   15.32586  38.58810  1.000 58.45611  ? 61  GLN   B CG    1 
ATOM   1862 C  CD    . GLN   B 1 62  ? 4.72815   15.78153  38.84455  1.000 48.95783  ? 61  GLN   B CD    1 
ATOM   1863 O  OE1   . GLN   B 1 62  ? 3.86549   15.01264  39.30378  1.000 64.65288  ? 61  GLN   B OE1   1 
ATOM   1864 N  NE2   . GLN   B 1 62  ? 4.46682   17.04590  38.53944  1.000 52.85469  ? 61  GLN   B NE2   1 
ATOM   1865 N  N     . GLU   B 1 63  ? 7.04871   13.02749  42.62722  1.000 57.36215  ? 62  GLU   B N     1 
ATOM   1866 C  CA    . GLU   B 1 63  ? 7.45648   11.79152  43.27397  1.000 62.16302  ? 62  GLU   B CA    1 
ATOM   1867 C  C     . GLU   B 1 63  ? 7.02042   10.56924  42.47835  1.000 54.09065  ? 62  GLU   B C     1 
ATOM   1868 O  O     . GLU   B 1 63  ? 7.66774   9.51940   42.57001  1.000 51.88069  ? 62  GLU   B O     1 
ATOM   1869 C  CB    . GLU   B 1 63  ? 6.90000   11.74693  44.70450  1.000 64.59662  ? 62  GLU   B CB    1 
ATOM   1870 C  CG    . GLU   B 1 63  ? 7.52573   12.77748  45.63134  1.000 70.95870  ? 62  GLU   B CG    1 
ATOM   1871 C  CD    . GLU   B 1 63  ? 8.95074   12.42871  46.02109  1.000 75.49047  ? 62  GLU   B CD    1 
ATOM   1872 O  OE1   . GLU   B 1 63  ? 9.22787   11.22623  46.23620  1.000 76.33114  ? 62  GLU   B OE1   1 
ATOM   1873 O  OE2   . GLU   B 1 63  ? 9.79801   13.35193  46.09804  1.000 78.85830  ? 62  GLU   B OE2   1 
ATOM   1874 N  N     . GLU   B 1 64  ? 5.95441   10.68850  41.68155  1.000 53.40391  ? 63  GLU   B N     1 
ATOM   1875 C  CA    . GLU   B 1 64  ? 5.51049   9.56205   40.86690  1.000 53.38375  ? 63  GLU   B CA    1 
ATOM   1876 C  C     . GLU   B 1 64  ? 6.57250   9.10280   39.87194  1.000 48.11239  ? 63  GLU   B C     1 
ATOM   1877 O  O     . GLU   B 1 64  ? 6.54214   7.94234   39.44556  1.000 47.45276  ? 63  GLU   B O     1 
ATOM   1878 C  CB    . GLU   B 1 64  ? 4.22954   9.91039   40.09317  1.000 48.89849  ? 63  GLU   B CB    1 
ATOM   1879 C  CG    . GLU   B 1 64  ? 3.13011   10.58716  40.89408  1.000 60.24943  ? 63  GLU   B CG    1 
ATOM   1880 C  CD    . GLU   B 1 64  ? 3.27562   12.09500  40.93315  1.000 65.32510  ? 63  GLU   B CD    1 
ATOM   1881 O  OE1   . GLU   B 1 64  ? 4.31177   12.57972  41.44087  1.000 62.10264  ? 63  GLU   B OE1   1 
ATOM   1882 O  OE2   . GLU   B 1 64  ? 2.36374   12.79678  40.43798  1.000 62.85375  ? 63  GLU   B OE2   1 
ATOM   1883 N  N     . TYR   B 1 65  ? 7.51110   9.97251   39.49548  1.000 44.31995  ? 64  TYR   B N     1 
ATOM   1884 C  CA    . TYR   B 1 65  ? 8.48103   9.67024   38.44717  1.000 41.18372  ? 64  TYR   B CA    1 
ATOM   1885 C  C     . TYR   B 1 65  ? 9.91674   9.68784   38.98503  1.000 47.40692  ? 64  TYR   B C     1 
ATOM   1886 O  O     . TYR   B 1 65  ? 10.83075  10.22223  38.35623  1.000 41.59454  ? 64  TYR   B O     1 
ATOM   1887 C  CB    . TYR   B 1 65  ? 8.30275   10.63032  37.26528  1.000 37.47966  ? 64  TYR   B CB    1 
ATOM   1888 C  CG    . TYR   B 1 65  ? 6.86384   10.67875  36.74436  1.000 34.57700  ? 64  TYR   B CG    1 
ATOM   1889 C  CD1   . TYR   B 1 65  ? 6.23919   9.53585   36.26584  1.000 30.51830  ? 64  TYR   B CD1   1 
ATOM   1890 C  CD2   . TYR   B 1 65  ? 6.13130   11.86121  36.75822  1.000 30.37091  ? 64  TYR   B CD2   1 
ATOM   1891 C  CE1   . TYR   B 1 65  ? 4.92074   9.56864   35.80847  1.000 29.04180  ? 64  TYR   B CE1   1 
ATOM   1892 C  CE2   . TYR   B 1 65  ? 4.81093   11.90592  36.30856  1.000 27.71796  ? 64  TYR   B CE2   1 
ATOM   1893 C  CZ    . TYR   B 1 65  ? 4.21381   10.75536  35.82429  1.000 28.73387  ? 64  TYR   B CZ    1 
ATOM   1894 O  OH    . TYR   B 1 65  ? 2.90392   10.79423  35.38383  1.000 29.86032  ? 64  TYR   B OH    1 
ATOM   1895 N  N     . SER   B 1 66  ? 10.14035  9.05801   40.14688  1.000 50.49867  ? 65  SER   B N     1 
ATOM   1896 C  CA    . SER   B 1 66  ? 11.45614  9.10460   40.79000  1.000 46.45520  ? 65  SER   B CA    1 
ATOM   1897 C  C     . SER   B 1 66  ? 12.54259  8.48597   39.91540  1.000 49.21213  ? 65  SER   B C     1 
ATOM   1898 O  O     . SER   B 1 66  ? 13.65598  9.02040   39.82603  1.000 49.24978  ? 65  SER   B O     1 
ATOM   1899 C  CB    . SER   B 1 66  ? 11.40182  8.39675   42.14539  1.000 55.18718  ? 65  SER   B CB    1 
ATOM   1900 O  OG    . SER   B 1 66  ? 10.40510  8.96109   42.98697  1.000 51.97613  ? 65  SER   B OG    1 
ATOM   1901 N  N     . ALA   B 1 67  ? 12.24324  7.36125   39.25907  1.000 48.58951  ? 66  ALA   B N     1 
ATOM   1902 C  CA    . ALA   B 1 67  ? 13.23482  6.69006   38.42294  1.000 44.21346  ? 66  ALA   B CA    1 
ATOM   1903 C  C     . ALA   B 1 67  ? 13.55949  7.45432   37.14647  1.000 48.10812  ? 66  ALA   B C     1 
ATOM   1904 O  O     . ALA   B 1 67  ? 14.56992  7.15174   36.49448  1.000 46.76106  ? 66  ALA   B O     1 
ATOM   1905 C  CB    . ALA   B 1 67  ? 12.75576  5.28342   38.06779  1.000 53.99204  ? 66  ALA   B CB    1 
ATOM   1906 N  N     . MET   B 1 68  ? 12.73951  8.42828   36.76512  1.000 45.51088  ? 67  MET   B N     1 
ATOM   1907 C  CA    . MET   B 1 68  ? 13.06303  9.21555   35.59028  1.000 45.84909  ? 67  MET   B CA    1 
ATOM   1908 C  C     . MET   B 1 68  ? 14.18171  10.21601  35.84698  1.000 40.74361  ? 67  MET   B C     1 
ATOM   1909 O  O     . MET   B 1 68  ? 14.73125  10.76604  34.88822  1.000 45.41092  ? 67  MET   B O     1 
ATOM   1910 C  CB    . MET   B 1 68  ? 11.82061  9.94680   35.08224  1.000 43.12700  ? 67  MET   B CB    1 
ATOM   1911 C  CG    . MET   B 1 68  ? 10.55718  9.09425   34.97855  1.000 45.73251  ? 67  MET   B CG    1 
ATOM   1912 S  SD    . MET   B 1 68  ? 10.78308  7.47788   34.23778  1.000 54.74948  ? 67  MET   B SD    1 
ATOM   1913 C  CE    . MET   B 1 68  ? 11.60696  7.89497   32.71398  1.000 30.79433  ? 67  MET   B CE    1 
ATOM   1914 N  N     . ARG   B 1 69  ? 14.54692  10.45148  37.10651  1.000 39.07422  ? 68  ARG   B N     1 
ATOM   1915 C  CA    . ARG   B 1 69  ? 15.54379  11.47049  37.40078  1.000 41.90157  ? 68  ARG   B CA    1 
ATOM   1916 C  C     . ARG   B 1 69  ? 16.96278  10.99718  37.14181  1.000 40.36701  ? 68  ARG   B C     1 
ATOM   1917 O  O     . ARG   B 1 69  ? 17.84970  11.83564  36.94969  1.000 36.75852  ? 68  ARG   B O     1 
ATOM   1918 C  CB    . ARG   B 1 69  ? 15.42529  11.92979  38.85511  1.000 39.35620  ? 68  ARG   B CB    1 
ATOM   1919 C  CG    . ARG   B 1 69  ? 14.05350  12.43139  39.23275  1.000 42.36218  ? 68  ARG   B CG    1 
ATOM   1920 C  CD    . ARG   B 1 69  ? 13.98910  12.71126  40.71589  1.000 44.05413  ? 68  ARG   B CD    1 
ATOM   1921 N  NE    . ARG   B 1 69  ? 12.62427  12.95908  41.15391  1.000 52.93657  ? 68  ARG   B NE    1 
ATOM   1922 C  CZ    . ARG   B 1 69  ? 12.17401  12.68068  42.36907  1.000 51.42527  ? 68  ARG   B CZ    1 
ATOM   1923 N  NH1   . ARG   B 1 69  ? 12.95327  12.12716  43.28296  1.000 48.81705  ? 68  ARG   B NH1   1 
ATOM   1924 N  NH2   . ARG   B 1 69  ? 10.90993  12.95843  42.67162  1.000 56.35031  ? 68  ARG   B NH2   1 
ATOM   1925 N  N     . ASP   B 1 70  ? 17.18997  9.68130   37.12181  1.000 40.53911  ? 69  ASP   B N     1 
ATOM   1926 C  CA    . ASP   B 1 70  ? 18.55042  9.15588   37.03198  1.000 42.84031  ? 69  ASP   B CA    1 
ATOM   1927 C  C     . ASP   B 1 70  ? 19.29783  9.70533   35.82443  1.000 43.59991  ? 69  ASP   B C     1 
ATOM   1928 O  O     . ASP   B 1 70  ? 20.47423  10.07806  35.92897  1.000 40.70930  ? 69  ASP   B O     1 
ATOM   1929 C  CB    . ASP   B 1 70  ? 18.52458  7.62605   36.97847  1.000 49.30736  ? 69  ASP   B CB    1 
ATOM   1930 C  CG    . ASP   B 1 70  ? 18.00751  6.99984   38.26262  1.000 53.32452  ? 69  ASP   B CG    1 
ATOM   1931 O  OD1   . ASP   B 1 70  ? 17.33850  7.70019   39.05254  1.000 51.35878  ? 69  ASP   B OD1   1 
ATOM   1932 O  OD2   . ASP   B 1 70  ? 18.28044  5.80087   38.48226  1.000 62.17172  ? 69  ASP   B OD2   1 
ATOM   1933 N  N     . GLN   B 1 71  ? 18.62770  9.77833   34.67032  1.000 46.97726  ? 70  GLN   B N     1 
ATOM   1934 C  CA    . GLN   B 1 71  ? 19.33006  10.11473  33.43608  1.000 46.17888  ? 70  GLN   B CA    1 
ATOM   1935 C  C     . GLN   B 1 71  ? 19.82685  11.55620  33.44712  1.000 40.66820  ? 70  GLN   B C     1 
ATOM   1936 O  O     . GLN   B 1 71  ? 20.95501  11.82402  33.02457  1.000 42.41260  ? 70  GLN   B O     1 
ATOM   1937 C  CB    . GLN   B 1 71  ? 18.43719  9.84009   32.21945  1.000 42.31854  ? 70  GLN   B CB    1 
ATOM   1938 C  CG    . GLN   B 1 71  ? 17.08788  10.56113  32.19507  1.000 45.97107  ? 70  GLN   B CG    1 
ATOM   1939 C  CD    . GLN   B 1 71  ? 17.14304  11.88017  31.44495  1.000 39.12930  ? 70  GLN   B CD    1 
ATOM   1940 O  OE1   . GLN   B 1 71  ? 18.11972  12.17344  30.74374  1.000 50.24407  ? 70  GLN   B OE1   1 
ATOM   1941 N  NE2   . GLN   B 1 71  ? 16.10020  12.68359  31.58754  1.000 41.27155  ? 70  GLN   B NE2   1 
ATOM   1942 N  N     . TYR   B 1 72  ? 19.02291  12.50253  33.94082  1.000 40.10945  ? 71  TYR   B N     1 
ATOM   1943 C  CA    . TYR   B 1 72  ? 19.52726  13.86886  33.95077  1.000 35.53886  ? 71  TYR   B CA    1 
ATOM   1944 C  C     . TYR   B 1 72  ? 20.49935  14.12711  35.10070  1.000 35.29309  ? 71  TYR   B C     1 
ATOM   1945 O  O     . TYR   B 1 72  ? 21.36383  14.99852  34.97013  1.000 36.92366  ? 71  TYR   B O     1 
ATOM   1946 C  CB    . TYR   B 1 72  ? 18.37684  14.88898  33.94649  1.000 38.63589  ? 71  TYR   B CB    1 
ATOM   1947 C  CG    . TYR   B 1 72  ? 17.46011  14.98270  35.14935  1.000 37.75382  ? 71  TYR   B CG    1 
ATOM   1948 C  CD1   . TYR   B 1 72  ? 17.91331  15.44304  36.38144  1.000 35.58627  ? 71  TYR   B CD1   1 
ATOM   1949 C  CD2   . TYR   B 1 72  ? 16.10431  14.70276  35.02002  1.000 35.95483  ? 71  TYR   B CD2   1 
ATOM   1950 C  CE1   . TYR   B 1 72  ? 17.04192  15.56047  37.46999  1.000 33.97661  ? 71  TYR   B CE1   1 
ATOM   1951 C  CE2   . TYR   B 1 72  ? 15.24068  14.81703  36.08629  1.000 36.23427  ? 71  TYR   B CE2   1 
ATOM   1952 C  CZ    . TYR   B 1 72  ? 15.70700  15.24721  37.30548  1.000 33.62578  ? 71  TYR   B CZ    1 
ATOM   1953 O  OH    . TYR   B 1 72  ? 14.83323  15.36090  38.35851  1.000 43.62616  ? 71  TYR   B OH    1 
ATOM   1954 N  N     . MET   B 1 73  ? 20.40674  13.37140  36.19948  1.000 38.95458  ? 72  MET   B N     1 
ATOM   1955 C  CA    . MET   B 1 73  ? 21.39953  13.49956  37.26720  1.000 37.78114  ? 72  MET   B CA    1 
ATOM   1956 C  C     . MET   B 1 73  ? 22.78313  13.03840  36.82525  1.000 40.77144  ? 72  MET   B C     1 
ATOM   1957 O  O     . MET   B 1 73  ? 23.78753  13.62408  37.24427  1.000 46.61758  ? 72  MET   B O     1 
ATOM   1958 C  CB    . MET   B 1 73  ? 20.95646  12.71582  38.49907  1.000 36.60742  ? 72  MET   B CB    1 
ATOM   1959 C  CG    . MET   B 1 73  ? 19.74761  13.31307  39.17035  1.000 36.90776  ? 72  MET   B CG    1 
ATOM   1960 S  SD    . MET   B 1 73  ? 19.14836  12.35589  40.55976  1.000 43.61888  ? 72  MET   B SD    1 
ATOM   1961 C  CE    . MET   B 1 73  ? 17.97288  13.50583  41.27210  1.000 41.94861  ? 72  MET   B CE    1 
ATOM   1962 N  N     . ARG   B 1 74  ? 22.86087  11.99269  35.99820  1.000 42.61775  ? 73  ARG   B N     1 
ATOM   1963 C  CA    . ARG   B 1 74  ? 24.15345  11.56357  35.46811  1.000 43.79175  ? 73  ARG   B CA    1 
ATOM   1964 C  C     . ARG   B 1 74  ? 24.77850  12.64717  34.60225  1.000 44.89518  ? 73  ARG   B C     1 
ATOM   1965 O  O     . ARG   B 1 74  ? 25.99759  12.85028  34.62956  1.000 43.44839  ? 73  ARG   B O     1 
ATOM   1966 C  CB    . ARG   B 1 74  ? 23.99847  10.26648  34.66928  1.000 49.09371  ? 73  ARG   B CB    1 
ATOM   1967 C  CG    . ARG   B 1 74  ? 24.27068  8.99475   35.46775  1.000 55.29739  ? 73  ARG   B CG    1 
ATOM   1968 C  CD    . ARG   B 1 74  ? 24.19106  7.74431   34.59860  1.000 54.88488  ? 73  ARG   B CD    1 
ATOM   1969 N  NE    . ARG   B 1 74  ? 22.88286  7.58549   33.97274  1.000 60.42920  ? 73  ARG   B NE    1 
ATOM   1970 C  CZ    . ARG   B 1 74  ? 21.91307  6.80657   34.43569  1.000 57.86581  ? 73  ARG   B CZ    1 
ATOM   1971 N  NH1   . ARG   B 1 74  ? 22.06442  6.09456   35.54057  1.000 60.13305  ? 73  ARG   B NH1   1 
ATOM   1972 N  NH2   . ARG   B 1 74  ? 20.76353  6.73580   33.76972  1.000 54.10595  ? 73  ARG   B NH2   1 
ATOM   1973 N  N     . THR   B 1 75  ? 23.95215  13.36736  33.84013  1.000 42.46600  ? 74  THR   B N     1 
ATOM   1974 C  CA    . THR   B 1 75  ? 24.44700  14.37787  32.91658  1.000 35.64217  ? 74  THR   B CA    1 
ATOM   1975 C  C     . THR   B 1 75  ? 24.79095  15.69260  33.60769  1.000 36.51290  ? 74  THR   B C     1 
ATOM   1976 O  O     . THR   B 1 75  ? 25.73050  16.37758  33.18543  1.000 41.81718  ? 74  THR   B O     1 
ATOM   1977 C  CB    . THR   B 1 75  ? 23.40250  14.62240  31.82713  1.000 44.32015  ? 74  THR   B CB    1 
ATOM   1978 O  OG1   . THR   B 1 75  ? 23.01343  13.36514  31.25969  1.000 41.53899  ? 74  THR   B OG1   1 
ATOM   1979 C  CG2   . THR   B 1 75  ? 23.96005  15.52059  30.74380  1.000 40.40264  ? 74  THR   B CG2   1 
ATOM   1980 N  N     . GLY   B 1 76  ? 24.05075  16.06221  34.64999  1.000 35.96735  ? 75  GLY   B N     1 
ATOM   1981 C  CA    . GLY   B 1 76  ? 24.25948  17.35281  35.28065  1.000 34.52823  ? 75  GLY   B CA    1 
ATOM   1982 C  C     . GLY   B 1 76  ? 25.61998  17.44779  35.94754  1.000 38.43954  ? 75  GLY   B C     1 
ATOM   1983 O  O     . GLY   B 1 76  ? 26.17830  16.45922  36.41889  1.000 36.92193  ? 75  GLY   B O     1 
ATOM   1984 N  N     . GLU   B 1 77  ? 26.16575  18.66550  35.96704  1.000 34.99444  ? 76  GLU   B N     1 
ATOM   1985 C  CA    . GLU   B 1 77  ? 27.43285  18.94601  36.63879  1.000 39.83826  ? 76  GLU   B CA    1 
ATOM   1986 C  C     . GLU   B 1 77  ? 27.23311  19.42644  38.06618  1.000 47.43570  ? 76  GLU   B C     1 
ATOM   1987 O  O     . GLU   B 1 77  ? 27.99355  19.04197  38.96479  1.000 45.58319  ? 76  GLU   B O     1 
ATOM   1988 C  CB    . GLU   B 1 77  ? 28.21973  20.01019  35.87699  1.000 37.89813  ? 76  GLU   B CB    1 
ATOM   1989 C  CG    . GLU   B 1 77  ? 28.98760  19.50763  34.68701  1.000 45.22105  ? 76  GLU   B CG    1 
ATOM   1990 C  CD    . GLU   B 1 77  ? 29.75485  20.63033  34.01728  1.000 45.60507  ? 76  GLU   B CD    1 
ATOM   1991 O  OE1   . GLU   B 1 77  ? 29.10399  21.59435  33.56929  1.000 43.39910  ? 76  GLU   B OE1   1 
ATOM   1992 O  OE2   . GLU   B 1 77  ? 31.00239  20.57010  33.97259  1.000 50.34991  ? 76  GLU   B OE2   1 
ATOM   1993 N  N     . GLY   B 1 78  ? 26.25153  20.29404  38.26736  1.000 36.51311  ? 77  GLY   B N     1 
ATOM   1994 C  CA    . GLY   B 1 78  ? 25.95829  20.83375  39.57873  1.000 43.99413  ? 77  GLY   B CA    1 
ATOM   1995 C  C     . GLY   B 1 78  ? 24.46263  20.99898  39.70530  1.000 42.55600  ? 77  GLY   B C     1 
ATOM   1996 O  O     . GLY   B 1 78  ? 23.74997  21.12098  38.70743  1.000 41.04146  ? 77  GLY   B O     1 
ATOM   1997 N  N     . PHE   B 1 79  ? 23.98457  20.99457  40.94688  1.000 34.26300  ? 78  PHE   B N     1 
ATOM   1998 C  CA    . PHE   B 1 79  ? 22.55576  20.89383  41.21275  1.000 32.60276  ? 78  PHE   B CA    1 
ATOM   1999 C  C     . PHE   B 1 79  ? 22.11883  21.95564  42.20366  1.000 39.83446  ? 78  PHE   B C     1 
ATOM   2000 O  O     . PHE   B 1 79  ? 22.70281  22.07676  43.28705  1.000 46.93505  ? 78  PHE   B O     1 
ATOM   2001 C  CB    . PHE   B 1 79  ? 22.20440  19.50008  41.74060  1.000 33.37127  ? 78  PHE   B CB    1 
ATOM   2002 C  CG    . PHE   B 1 79  ? 22.56177  18.39356  40.79314  1.000 39.42652  ? 78  PHE   B CG    1 
ATOM   2003 C  CD1   . PHE   B 1 79  ? 23.86113  17.92184  40.71278  1.000 36.68341  ? 78  PHE   B CD1   1 
ATOM   2004 C  CD2   . PHE   B 1 79  ? 21.60180  17.83790  39.96132  1.000 34.52567  ? 78  PHE   B CD2   1 
ATOM   2005 C  CE1   . PHE   B 1 79  ? 24.20064  16.91005  39.83109  1.000 41.24846  ? 78  PHE   B CE1   1 
ATOM   2006 C  CE2   . PHE   B 1 79  ? 21.93561  16.82535  39.08744  1.000 30.96309  ? 78  PHE   B CE2   1 
ATOM   2007 C  CZ    . PHE   B 1 79  ? 23.23082  16.36264  39.01973  1.000 36.51638  ? 78  PHE   B CZ    1 
ATOM   2008 N  N     . LEU   B 1 80  ? 21.10806  22.72874  41.81993  1.000 34.10030  ? 79  LEU   B N     1 
ATOM   2009 C  CA    . LEU   B 1 80  ? 20.36106  23.57215  42.74399  1.000 39.60521  ? 79  LEU   B CA    1 
ATOM   2010 C  C     . LEU   B 1 80  ? 19.29864  22.71577  43.41630  1.000 44.71835  ? 79  LEU   B C     1 
ATOM   2011 O  O     . LEU   B 1 80  ? 18.24882  22.43680  42.82378  1.000 40.19850  ? 79  LEU   B O     1 
ATOM   2012 C  CB    . LEU   B 1 80  ? 19.70004  24.74241  42.02188  1.000 42.36097  ? 79  LEU   B CB    1 
ATOM   2013 C  CG    . LEU   B 1 80  ? 20.45104  26.03308  41.69630  1.000 44.00655  ? 79  LEU   B CG    1 
ATOM   2014 C  CD1   . LEU   B 1 80  ? 19.42969  27.14259  41.47696  1.000 40.21420  ? 79  LEU   B CD1   1 
ATOM   2015 C  CD2   . LEU   B 1 80  ? 21.46175  26.41287  42.78419  1.000 42.93153  ? 79  LEU   B CD2   1 
ATOM   2016 N  N     . CYS   B 1 81  ? 19.55501  22.30392  44.65493  1.000 40.71670  ? 80  CYS   B N     1 
ATOM   2017 C  CA    . CYS   B 1 81  ? 18.58810  21.52614  45.42577  1.000 46.81082  ? 80  CYS   B CA    1 
ATOM   2018 C  C     . CYS   B 1 81  ? 17.71452  22.52610  46.17758  1.000 43.20962  ? 80  CYS   B C     1 
ATOM   2019 O  O     . CYS   B 1 81  ? 18.15023  23.12544  47.16239  1.000 42.59869  ? 80  CYS   B O     1 
ATOM   2020 C  CB    . CYS   B 1 81  ? 19.29647  20.55282  46.36087  1.000 40.54581  ? 80  CYS   B CB    1 
ATOM   2021 S  SG    . CYS   B 1 81  ? 20.50316  19.47125  45.55233  1.000 46.50179  ? 80  CYS   B SG    1 
ATOM   2022 N  N     . VAL   B 1 82  ? 16.48790  22.72092  45.70023  1.000 37.90076  ? 81  VAL   B N     1 
ATOM   2023 C  CA    . VAL   B 1 82  ? 15.61318  23.79244  46.16657  1.000 41.14428  ? 81  VAL   B CA    1 
ATOM   2024 C  C     . VAL   B 1 82  ? 14.54319  23.22066  47.08375  1.000 49.52304  ? 81  VAL   B C     1 
ATOM   2025 O  O     . VAL   B 1 82  ? 13.94468  22.18140  46.78324  1.000 40.29842  ? 81  VAL   B O     1 
ATOM   2026 C  CB    . VAL   B 1 82  ? 14.95222  24.53021  44.98968  1.000 38.05867  ? 81  VAL   B CB    1 
ATOM   2027 C  CG1   . VAL   B 1 82  ? 14.20467  25.76268  45.48049  1.000 42.44096  ? 81  VAL   B CG1   1 
ATOM   2028 C  CG2   . VAL   B 1 82  ? 15.98847  24.90458  43.92888  1.000 37.20958  ? 81  VAL   B CG2   1 
ATOM   2029 N  N     . PHE   B 1 83  ? 14.29646  23.90228  48.19721  1.000 50.13573  ? 82  PHE   B N     1 
ATOM   2030 C  CA    . PHE   B 1 83  ? 13.09511  23.72194  48.99754  1.000 52.72250  ? 82  PHE   B CA    1 
ATOM   2031 C  C     . PHE   B 1 83  ? 12.44864  25.08554  49.20622  1.000 54.32412  ? 82  PHE   B C     1 
ATOM   2032 O  O     . PHE   B 1 83  ? 13.01110  26.12304  48.84580  1.000 53.15159  ? 82  PHE   B O     1 
ATOM   2033 C  CB    . PHE   B 1 83  ? 13.40929  23.04416  50.33576  1.000 55.26301  ? 82  PHE   B CB    1 
ATOM   2034 C  CG    . PHE   B 1 83  ? 14.21346  23.89730  51.27614  1.000 57.08363  ? 82  PHE   B CG    1 
ATOM   2035 C  CD1   . PHE   B 1 83  ? 15.58883  23.99802  51.13698  1.000 54.92489  ? 82  PHE   B CD1   1 
ATOM   2036 C  CD2   . PHE   B 1 83  ? 13.59328  24.59527  52.30134  1.000 61.27064  ? 82  PHE   B CD2   1 
ATOM   2037 C  CE1   . PHE   B 1 83  ? 16.33598  24.78118  52.00486  1.000 61.28792  ? 82  PHE   B CE1   1 
ATOM   2038 C  CE2   . PHE   B 1 83  ? 14.32970  25.37927  53.16878  1.000 63.37342  ? 82  PHE   B CE2   1 
ATOM   2039 C  CZ    . PHE   B 1 83  ? 15.70277  25.47271  53.02165  1.000 63.07797  ? 82  PHE   B CZ    1 
ATOM   2040 N  N     . ALA   B 1 84  ? 11.25303  25.07525  49.78256  1.000 52.71692  ? 83  ALA   B N     1 
ATOM   2041 C  CA    . ALA   B 1 84  ? 10.54510  26.29181  50.14642  1.000 56.81377  ? 83  ALA   B CA    1 
ATOM   2042 C  C     . ALA   B 1 84  ? 10.58795  26.45350  51.66283  1.000 63.10364  ? 83  ALA   B C     1 
ATOM   2043 O  O     . ALA   B 1 84  ? 10.55899  25.46416  52.40120  1.000 60.00867  ? 83  ALA   B O     1 
ATOM   2044 C  CB    . ALA   B 1 84  ? 9.10264   26.26054  49.63785  1.000 52.81307  ? 83  ALA   B CB    1 
ATOM   2045 N  N     . ILE   B 1 85  ? 10.68260  27.70333  52.12718  1.000 64.62356  ? 84  ILE   B N     1 
ATOM   2046 C  CA    . ILE   B 1 85  ? 10.86374  27.94323  53.55632  1.000 71.85668  ? 84  ILE   B CA    1 
ATOM   2047 C  C     . ILE   B 1 85  ? 9.57404   27.75478  54.34518  1.000 76.98192  ? 84  ILE   B C     1 
ATOM   2048 O  O     . ILE   B 1 85  ? 9.62426   27.59996  55.57199  1.000 81.22241  ? 84  ILE   B O     1 
ATOM   2049 C  CB    . ILE   B 1 85  ? 11.45058  29.34765  53.81074  1.000 73.13791  ? 84  ILE   B CB    1 
ATOM   2050 C  CG1   . ILE   B 1 85  ? 10.67259  30.42561  53.04725  1.000 69.44284  ? 84  ILE   B CG1   1 
ATOM   2051 C  CG2   . ILE   B 1 85  ? 12.93133  29.37893  53.45703  1.000 70.06168  ? 84  ILE   B CG2   1 
ATOM   2052 C  CD1   . ILE   B 1 85  ? 9.50113   31.02669  53.81126  1.000 76.05100  ? 84  ILE   B CD1   1 
ATOM   2053 N  N     . ASN   B 1 86  ? 8.41746   27.77212  53.68081  1.000 71.06520  ? 85  ASN   B N     1 
ATOM   2054 C  CA    . ASN   B 1 86  ? 7.13103   27.55945  54.33275  1.000 74.06879  ? 85  ASN   B CA    1 
ATOM   2055 C  C     . ASN   B 1 86  ? 6.55618   26.17462  54.03884  1.000 73.25478  ? 85  ASN   B C     1 
ATOM   2056 O  O     . ASN   B 1 86  ? 5.33504   25.98967  54.07899  1.000 73.35892  ? 85  ASN   B O     1 
ATOM   2057 C  CB    . ASN   B 1 86  ? 6.14014   28.64387  53.90982  1.000 73.60987  ? 85  ASN   B CB    1 
ATOM   2058 C  CG    . ASN   B 1 86  ? 5.78361   28.55549  52.44830  1.000 69.76134  ? 85  ASN   B CG    1 
ATOM   2059 O  OD1   . ASN   B 1 86  ? 6.58149   28.08915  51.64007  1.000 67.03750  ? 85  ASN   B OD1   1 
ATOM   2060 N  ND2   . ASN   B 1 86  ? 4.57812   28.98942  52.09881  1.000 70.39076  ? 85  ASN   B ND2   1 
ATOM   2061 N  N     . ASN   B 1 87  ? 7.41145   25.20000  53.73048  1.000 69.89014  ? 86  ASN   B N     1 
ATOM   2062 C  CA    . ASN   B 1 87  ? 6.97536   23.83546  53.42437  1.000 70.52601  ? 86  ASN   B CA    1 
ATOM   2063 C  C     . ASN   B 1 87  ? 8.02680   22.89295  53.99886  1.000 67.89131  ? 86  ASN   B C     1 
ATOM   2064 O  O     . ASN   B 1 87  ? 9.05422   22.63866  53.36158  1.000 63.86771  ? 86  ASN   B O     1 
ATOM   2065 C  CB    . ASN   B 1 87  ? 6.79755   23.62126  51.92449  1.000 64.77312  ? 86  ASN   B CB    1 
ATOM   2066 C  CG    . ASN   B 1 87  ? 6.17401   22.27489  51.59546  1.000 66.45682  ? 86  ASN   B CG    1 
ATOM   2067 O  OD1   . ASN   B 1 87  ? 6.75297   21.22374  51.87010  1.000 61.31409  ? 86  ASN   B OD1   1 
ATOM   2068 N  ND2   . ASN   B 1 87  ? 4.99612   22.30313  50.98543  1.000 70.13357  ? 86  ASN   B ND2   1 
ATOM   2069 N  N     . THR   B 1 88  ? 7.76517   22.37554  55.20107  1.000 68.11491  ? 87  THR   B N     1 
ATOM   2070 C  CA    . THR   B 1 88  ? 8.74361   21.51399  55.85474  1.000 71.79822  ? 87  THR   B CA    1 
ATOM   2071 C  C     . THR   B 1 88  ? 8.96172   20.22545  55.07578  1.000 65.84622  ? 87  THR   B C     1 
ATOM   2072 O  O     . THR   B 1 88  ? 10.08635  19.70824  55.04512  1.000 67.34407  ? 87  THR   B O     1 
ATOM   2073 C  CB    . THR   B 1 88  ? 8.30695   21.20854  57.29265  1.000 77.54684  ? 87  THR   B CB    1 
ATOM   2074 O  OG1   . THR   B 1 88  ? 8.15935   22.43413  58.02120  1.000 79.70866  ? 87  THR   B OG1   1 
ATOM   2075 C  CG2   . THR   B 1 88  ? 9.33696   20.33874  58.00735  1.000 76.55276  ? 87  THR   B CG2   1 
ATOM   2076 N  N     . LYS   B 1 89  ? 7.91388   19.70250  54.43260  1.000 63.91441  ? 88  LYS   B N     1 
ATOM   2077 C  CA    . LYS   B 1 89  ? 8.06444   18.46171  53.68096  1.000 60.86930  ? 88  LYS   B CA    1 
ATOM   2078 C  C     . LYS   B 1 89  ? 9.08112   18.62938  52.55804  1.000 56.78460  ? 88  LYS   B C     1 
ATOM   2079 O  O     . LYS   B 1 89  ? 9.94441   17.76867  52.34953  1.000 55.46076  ? 88  LYS   B O     1 
ATOM   2080 C  CB    . LYS   B 1 89  ? 6.71032   18.00804  53.13283  1.000 61.34263  ? 88  LYS   B CB    1 
ATOM   2081 C  CG    . LYS   B 1 89  ? 6.76572   16.70483  52.29329  1.000 59.07813  ? 88  LYS   B CG    1 
ATOM   2082 C  CD    . LYS   B 1 89  ? 7.71856   15.66369  52.90392  1.000 56.45984  ? 88  LYS   B CD    1 
ATOM   2083 C  CE    . LYS   B 1 89  ? 7.44270   14.23785  52.42501  1.000 48.31622  ? 88  LYS   B CE    1 
ATOM   2084 N  NZ    . LYS   B 1 89  ? 7.26182   14.17928  50.92339  1.000 54.99971  ? 88  LYS   B NZ    1 
ATOM   2085 N  N     . SER   B 1 90  ? 9.00570   19.74658  51.83252  1.000 55.63515  ? 89  SER   B N     1 
ATOM   2086 C  CA    . SER   B 1 90  ? 9.96225   19.98763  50.75633  1.000 55.63269  ? 89  SER   B CA    1 
ATOM   2087 C  C     . SER   B 1 90  ? 11.38178  20.02861  51.28934  1.000 59.61328  ? 89  SER   B C     1 
ATOM   2088 O  O     . SER   B 1 90  ? 12.32442  19.64588  50.58663  1.000 51.57076  ? 89  SER   B O     1 
ATOM   2089 C  CB    . SER   B 1 90  ? 9.63560   21.29411  50.03294  1.000 58.18687  ? 89  SER   B CB    1 
ATOM   2090 O  OG    . SER   B 1 90  ? 10.13077  22.40992  50.74794  1.000 55.67921  ? 89  SER   B OG    1 
ATOM   2091 N  N     . PHE   B 1 91  ? 11.55263  20.48727  52.52810  1.000 56.64248  ? 90  PHE   B N     1 
ATOM   2092 C  CA    . PHE   B 1 91  ? 12.87127  20.48083  53.14340  1.000 60.98723  ? 90  PHE   B CA    1 
ATOM   2093 C  C     . PHE   B 1 91  ? 13.30359  19.06327  53.50603  1.000 61.43076  ? 90  PHE   B C     1 
ATOM   2094 O  O     . PHE   B 1 91  ? 14.47136  18.70176  53.32593  1.000 58.97960  ? 90  PHE   B O     1 
ATOM   2095 C  CB    . PHE   B 1 91  ? 12.87571  21.39711  54.37095  1.000 66.58385  ? 90  PHE   B CB    1 
ATOM   2096 C  CG    . PHE   B 1 91  ? 14.20803  21.49146  55.04873  1.000 66.13572  ? 90  PHE   B CG    1 
ATOM   2097 C  CD1   . PHE   B 1 91  ? 15.26644  22.14240  54.43823  1.000 66.39330  ? 90  PHE   B CD1   1 
ATOM   2098 C  CD2   . PHE   B 1 91  ? 14.40379  20.92750  56.29554  1.000 70.79528  ? 90  PHE   B CD2   1 
ATOM   2099 C  CE1   . PHE   B 1 91  ? 16.49815  22.22779  55.05649  1.000 70.67946  ? 90  PHE   B CE1   1 
ATOM   2100 C  CE2   . PHE   B 1 91  ? 15.63210  21.01078  56.92196  1.000 76.01349  ? 90  PHE   B CE2   1 
ATOM   2101 C  CZ    . PHE   B 1 91  ? 16.68135  21.66148  56.30105  1.000 75.02067  ? 90  PHE   B CZ    1 
ATOM   2102 N  N     . GLU   B 1 92  ? 12.37746  18.24195  54.00722  1.000 64.92040  ? 91  GLU   B N     1 
ATOM   2103 C  CA    . GLU   B 1 92  ? 12.69441  16.83538  54.22775  1.000 65.74667  ? 91  GLU   B CA    1 
ATOM   2104 C  C     . GLU   B 1 92  ? 12.92545  16.10866  52.90891  1.000 63.51199  ? 91  GLU   B C     1 
ATOM   2105 O  O     . GLU   B 1 92  ? 13.75484  15.19205  52.84295  1.000 65.65985  ? 91  GLU   B O     1 
ATOM   2106 C  CB    . GLU   B 1 92  ? 11.57580  16.16373  55.02700  1.000 68.23786  ? 91  GLU   B CB    1 
ATOM   2107 C  CG    . GLU   B 1 92  ? 11.46770  16.64441  56.47202  1.000 70.86451  ? 91  GLU   B CG    1 
ATOM   2108 C  CD    . GLU   B 1 92  ? 10.05407  16.52854  57.02588  1.000 79.59975  ? 91  GLU   B CD    1 
ATOM   2109 O  OE1   . GLU   B 1 92  ? 9.16853   16.00518  56.31345  1.000 71.87514  ? 91  GLU   B OE1   1 
ATOM   2110 O  OE2   . GLU   B 1 92  ? 9.82619   16.97009  58.17268  1.000 83.27201  ? 91  GLU   B OE2   1 
ATOM   2111 N  N     . ASP   B 1 93  ? 12.21039  16.50847  51.85006  1.000 60.18707  ? 92  ASP   B N     1 
ATOM   2112 C  CA    . ASP   B 1 93  ? 12.41701  15.90462  50.53589  1.000 62.69549  ? 92  ASP   B CA    1 
ATOM   2113 C  C     . ASP   B 1 93  ? 13.81034  16.19551  49.99667  1.000 62.03760  ? 92  ASP   B C     1 
ATOM   2114 O  O     . ASP   B 1 93  ? 14.33545  15.41058  49.19637  1.000 57.41024  ? 92  ASP   B O     1 
ATOM   2115 C  CB    . ASP   B 1 93  ? 11.35736  16.39802  49.54767  1.000 54.75628  ? 92  ASP   B CB    1 
ATOM   2116 C  CG    . ASP   B 1 93  ? 9.97529   15.87243  49.86661  1.000 57.64786  ? 92  ASP   B CG    1 
ATOM   2117 O  OD1   . ASP   B 1 93  ? 9.88587   14.86590  50.59989  1.000 56.94592  ? 92  ASP   B OD1   1 
ATOM   2118 O  OD2   . ASP   B 1 93  ? 8.98128   16.45536  49.38393  1.000 56.35560  ? 92  ASP   B OD2   1 
ATOM   2119 N  N     . ILE   B 1 94  ? 14.41651  17.31174  50.42184  1.000 57.44459  ? 93  ILE   B N     1 
ATOM   2120 C  CA    . ILE   B 1 94  ? 15.76999  17.66360  49.99197  1.000 55.90107  ? 93  ILE   B CA    1 
ATOM   2121 C  C     . ILE   B 1 94  ? 16.70952  16.48071  50.16031  1.000 58.77822  ? 93  ILE   B C     1 
ATOM   2122 O  O     . ILE   B 1 94  ? 17.55310  16.20588  49.29759  1.000 51.14355  ? 93  ILE   B O     1 
ATOM   2123 C  CB    . ILE   B 1 94  ? 16.27603  18.89358  50.77300  1.000 54.22070  ? 93  ILE   B CB    1 
ATOM   2124 C  CG1   . ILE   B 1 94  ? 15.54048  20.16152  50.33777  1.000 54.39152  ? 93  ILE   B CG1   1 
ATOM   2125 C  CG2   . ILE   B 1 94  ? 17.78268  19.04896  50.62683  1.000 58.45829  ? 93  ILE   B CG2   1 
ATOM   2126 C  CD1   . ILE   B 1 94  ? 15.85075  20.59130  48.92573  1.000 51.64737  ? 93  ILE   B CD1   1 
ATOM   2127 N  N     . HIS   B 1 95  ? 16.56626  15.74991  51.26769  1.000 62.30486  ? 94  HIS   B N     1 
ATOM   2128 C  CA    . HIS   B 1 95  ? 17.47082  14.63941  51.54139  1.000 65.38026  ? 94  HIS   B CA    1 
ATOM   2129 C  C     . HIS   B 1 95  ? 17.35676  13.54882  50.47927  1.000 62.49708  ? 94  HIS   B C     1 
ATOM   2130 O  O     . HIS   B 1 95  ? 18.37080  12.99948  50.02877  1.000 61.33637  ? 94  HIS   B O     1 
ATOM   2131 C  CB    . HIS   B 1 95  ? 17.18703  14.07472  52.93283  1.000 69.96617  ? 94  HIS   B CB    1 
ATOM   2132 C  CG    . HIS   B 1 95  ? 18.03605  12.89770  53.28150  1.000 74.47360  ? 94  HIS   B CG    1 
ATOM   2133 N  ND1   . HIS   B 1 95  ? 19.40355  12.98744  53.42663  1.000 78.14163  ? 94  HIS   B ND1   1 
ATOM   2134 C  CD2   . HIS   B 1 95  ? 17.71744  11.59925  53.49235  1.000 77.27444  ? 94  HIS   B CD2   1 
ATOM   2135 C  CE1   . HIS   B 1 95  ? 19.89003  11.79584  53.72253  1.000 81.98480  ? 94  HIS   B CE1   1 
ATOM   2136 N  NE2   . HIS   B 1 95  ? 18.88829  10.93550  53.76635  1.000 83.27749  ? 94  HIS   B NE2   1 
ATOM   2137 N  N     . HIS   B 1 96  ? 16.12971  13.22137  50.06905  1.000 60.31259  ? 95  HIS   B N     1 
ATOM   2138 C  CA    . HIS   B 1 96  ? 15.93689  12.20879  49.03568  1.000 63.08185  ? 95  HIS   B CA    1 
ATOM   2139 C  C     . HIS   B 1 96  ? 16.63960  12.60240  47.73797  1.000 56.45722  ? 95  HIS   B C     1 
ATOM   2140 O  O     . HIS   B 1 96  ? 17.24031  11.75584  47.06287  1.000 53.77563  ? 95  HIS   B O     1 
ATOM   2141 C  CB    . HIS   B 1 96  ? 14.43888  11.98574  48.80743  1.000 59.20604  ? 95  HIS   B CB    1 
ATOM   2142 C  CG    . HIS   B 1 96  ? 13.70669  11.50757  50.02596  1.000 71.54919  ? 95  HIS   B CG    1 
ATOM   2143 N  ND1   . HIS   B 1 96  ? 13.63226  12.24400  51.18998  1.000 69.98319  ? 95  HIS   B ND1   1 
ATOM   2144 C  CD2   . HIS   B 1 96  ? 13.01985  10.36367  50.26222  1.000 71.97278  ? 95  HIS   B CD2   1 
ATOM   2145 C  CE1   . HIS   B 1 96  ? 12.93264  11.57492  52.08959  1.000 73.67582  ? 95  HIS   B CE1   1 
ATOM   2146 N  NE2   . HIS   B 1 96  ? 12.54952  10.43079  51.55210  1.000 77.01538  ? 95  HIS   B NE2   1 
ATOM   2147 N  N     . TYR   B 1 97  ? 16.59820  13.88871  47.38570  1.000 54.12563  ? 96  TYR   B N     1 
ATOM   2148 C  CA    . TYR   B 1 97  ? 17.27089  14.34202  46.17216  1.000 51.20242  ? 96  TYR   B CA    1 
ATOM   2149 C  C     . TYR   B 1 97  ? 18.78681  14.26559  46.32068  1.000 55.34241  ? 96  TYR   B C     1 
ATOM   2150 O  O     . TYR   B 1 97  ? 19.48482  13.78778  45.41811  1.000 49.56532  ? 96  TYR   B O     1 
ATOM   2151 C  CB    . TYR   B 1 97  ? 16.82768  15.76539  45.82445  1.000 50.86104  ? 96  TYR   B CB    1 
ATOM   2152 C  CG    . TYR   B 1 97  ? 15.48794  15.84785  45.12036  1.000 48.49728  ? 96  TYR   B CG    1 
ATOM   2153 C  CD1   . TYR   B 1 97  ? 15.38539  15.61450  43.75602  1.000 40.94323  ? 96  TYR   B CD1   1 
ATOM   2154 C  CD2   . TYR   B 1 97  ? 14.33138  16.17186  45.81601  1.000 45.17094  ? 96  TYR   B CD2   1 
ATOM   2155 C  CE1   . TYR   B 1 97  ? 14.16673  15.69032  43.10810  1.000 46.15175  ? 96  TYR   B CE1   1 
ATOM   2156 C  CE2   . TYR   B 1 97  ? 13.10705  16.24841  45.17873  1.000 42.89180  ? 96  TYR   B CE2   1 
ATOM   2157 C  CZ    . TYR   B 1 97  ? 13.02897  16.00505  43.82230  1.000 49.65580  ? 96  TYR   B CZ    1 
ATOM   2158 O  OH    . TYR   B 1 97  ? 11.81389  16.08309  43.17696  1.000 50.14696  ? 96  TYR   B OH    1 
ATOM   2159 N  N     . ARG   B 1 98  ? 19.31603  14.72816  47.45678  1.000 52.13141  ? 97  ARG   B N     1 
ATOM   2160 C  CA    . ARG   B 1 98  ? 20.75651  14.65762  47.68537  1.000 58.32709  ? 97  ARG   B CA    1 
ATOM   2161 C  C     . ARG   B 1 98  ? 21.26123  13.22530  47.56851  1.000 58.22667  ? 97  ARG   B C     1 
ATOM   2162 O  O     . ARG   B 1 98  ? 22.28318  12.96311  46.92382  1.000 59.34272  ? 97  ARG   B O     1 
ATOM   2163 C  CB    . ARG   B 1 98  ? 21.09875  15.23941  49.05903  1.000 67.48707  ? 97  ARG   B CB    1 
ATOM   2164 C  CG    . ARG   B 1 98  ? 22.45255  14.79599  49.61990  1.000 74.85449  ? 97  ARG   B CG    1 
ATOM   2165 C  CD    . ARG   B 1 98  ? 23.53433  15.84405  49.41632  1.000 74.69656  ? 97  ARG   B CD    1 
ATOM   2166 N  NE    . ARG   B 1 98  ? 24.83258  15.39026  49.90254  1.000 77.40228  ? 97  ARG   B NE    1 
ATOM   2167 C  CZ    . ARG   B 1 98  ? 25.98180  16.00730  49.65811  1.000 82.11852  ? 97  ARG   B CZ    1 
ATOM   2168 N  NH1   . ARG   B 1 98  ? 26.03141  17.11880  48.93970  1.000 77.00848  ? 97  ARG   B NH1   1 
ATOM   2169 N  NH2   . ARG   B 1 98  ? 27.11101  15.49319  50.14067  1.000 80.79392  ? 97  ARG   B NH2   1 
ATOM   2170 N  N     . GLU   B 1 99  ? 20.54276  12.27850  48.17133  1.000 58.92504  ? 98  GLU   B N     1 
ATOM   2171 C  CA    . GLU   B 1 99  ? 21.00323  10.89519  48.16090  1.000 62.23298  ? 98  GLU   B CA    1 
ATOM   2172 C  C     . GLU   B 1 99  ? 20.96940  10.30974  46.75687  1.000 61.37226  ? 98  GLU   B C     1 
ATOM   2173 O  O     . GLU   B 1 99  ? 21.91798  9.63550   46.33499  1.000 58.95183  ? 98  GLU   B O     1 
ATOM   2174 C  CB    . GLU   B 1 99  ? 20.15906  10.05955  49.12119  1.000 64.53306  ? 98  GLU   B CB    1 
ATOM   2175 C  CG    . GLU   B 1 99  ? 20.38470  10.42288  50.58285  1.000 74.31938  ? 98  GLU   B CG    1 
ATOM   2176 C  CD    . GLU   B 1 99  ? 21.84748  10.32076  50.98487  1.000 76.01066  ? 98  GLU   B CD    1 
ATOM   2177 O  OE1   . GLU   B 1 99  ? 22.50080  9.33072   50.59474  1.000 77.03963  ? 98  GLU   B OE1   1 
ATOM   2178 O  OE2   . GLU   B 1 99  ? 22.34774  11.23446  51.67667  1.000 78.93669  ? 98  GLU   B OE2   1 
ATOM   2179 N  N     . GLN   B 1 100 ? 19.88984  10.56520  46.01588  1.000 60.02525  ? 99  GLN   B N     1 
ATOM   2180 C  CA    . GLN   B 1 100 ? 19.78083  10.03171  44.66348  1.000 58.10780  ? 99  GLN   B CA    1 
ATOM   2181 C  C     . GLN   B 1 100 ? 20.91371  10.53778  43.77752  1.000 54.17384  ? 99  GLN   B C     1 
ATOM   2182 O  O     . GLN   B 1 100 ? 21.46440  9.78083   42.96961  1.000 58.26307  ? 99  GLN   B O     1 
ATOM   2183 C  CB    . GLN   B 1 100 ? 18.41629  10.39468  44.07527  1.000 57.04217  ? 99  GLN   B CB    1 
ATOM   2184 C  CG    . GLN   B 1 100 ? 18.13031  9.74442   42.73668  1.000 54.12712  ? 99  GLN   B CG    1 
ATOM   2185 C  CD    . GLN   B 1 100 ? 16.68939  9.92250   42.29794  1.000 52.68037  ? 99  GLN   B CD    1 
ATOM   2186 O  OE1   . GLN   B 1 100 ? 15.87907  10.52302  43.00398  1.000 51.69189  ? 99  GLN   B OE1   1 
ATOM   2187 N  NE2   . GLN   B 1 100 ? 16.36252  9.38897   41.12681  1.000 52.05610  ? 99  GLN   B NE2   1 
ATOM   2188 N  N     . ILE   B 1 101 ? 21.28493  11.81128  43.92436  1.000 53.00634  ? 100 ILE   B N     1 
ATOM   2189 C  CA    . ILE   B 1 101 ? 22.37746  12.36575  43.13134  1.000 54.94501  ? 100 ILE   B CA    1 
ATOM   2190 C  C     . ILE   B 1 101 ? 23.69053  11.67810  43.48184  1.000 59.52597  ? 100 ILE   B C     1 
ATOM   2191 O  O     . ILE   B 1 101 ? 24.44633  11.25982  42.59584  1.000 57.99264  ? 100 ILE   B O     1 
ATOM   2192 C  CB    . ILE   B 1 101 ? 22.47362  13.88738  43.33516  1.000 55.91417  ? 100 ILE   B CB    1 
ATOM   2193 C  CG1   . ILE   B 1 101 ? 21.17750  14.56555  42.90519  1.000 48.44409  ? 100 ILE   B CG1   1 
ATOM   2194 C  CG2   . ILE   B 1 101 ? 23.66527  14.44876  42.56238  1.000 52.53764  ? 100 ILE   B CG2   1 
ATOM   2195 C  CD1   . ILE   B 1 101 ? 20.99733  15.94546  43.48673  1.000 44.34412  ? 100 ILE   B CD1   1 
ATOM   2196 N  N     . LYS   B 1 102 ? 23.98875  11.56797  44.78134  1.000 64.61847  ? 101 LYS   B N     1 
ATOM   2197 C  CA    . LYS   B 1 102 ? 25.16528  10.81883  45.20954  1.000 66.70733  ? 101 LYS   B CA    1 
ATOM   2198 C  C     . LYS   B 1 102 ? 25.11836  9.39110   44.68733  1.000 67.18029  ? 101 LYS   B C     1 
ATOM   2199 O  O     . LYS   B 1 102 ? 26.12406  8.86788   44.19642  1.000 69.79189  ? 101 LYS   B O     1 
ATOM   2200 C  CB    . LYS   B 1 102 ? 25.27426  10.82625  46.73486  1.000 73.02018  ? 101 LYS   B CB    1 
ATOM   2201 C  CG    . LYS   B 1 102 ? 26.02128  12.02129  47.30243  1.000 79.82658  ? 101 LYS   B CG    1 
ATOM   2202 C  CD    . LYS   B 1 102 ? 26.25710  11.88560  48.80200  1.000 84.11069  ? 101 LYS   B CD    1 
ATOM   2203 C  CE    . LYS   B 1 102 ? 24.96284  11.99024  49.59365  1.000 84.11634  ? 101 LYS   B CE    1 
ATOM   2204 N  NZ    . LYS   B 1 102 ? 25.20936  12.02070  51.06548  1.000 82.69135  ? 101 LYS   B NZ    1 
ATOM   2205 N  N     . ARG   B 1 103 ? 23.94756  8.75689   44.76009  1.000 64.60840  ? 102 ARG   B N     1 
ATOM   2206 C  CA    . ARG   B 1 103 ? 23.81027  7.37828   44.30357  1.000 64.04465  ? 102 ARG   B CA    1 
ATOM   2207 C  C     . ARG   B 1 103 ? 24.03120  7.27039   42.79840  1.000 65.20543  ? 102 ARG   B C     1 
ATOM   2208 O  O     . ARG   B 1 103 ? 24.82521  6.44379   42.33419  1.000 63.72727  ? 102 ARG   B O     1 
ATOM   2209 C  CB    . ARG   B 1 103 ? 22.42710  6.84919   44.69284  1.000 66.68189  ? 102 ARG   B CB    1 
ATOM   2210 C  CG    . ARG   B 1 103 ? 22.28151  5.32927   44.72646  1.000 67.51354  ? 102 ARG   B CG    1 
ATOM   2211 C  CD    . ARG   B 1 103 ? 21.81472  4.73005   43.39211  1.000 70.00970  ? 102 ARG   B CD    1 
ATOM   2212 N  NE    . ARG   B 1 103 ? 20.69747  5.43967   42.77327  1.000 70.20369  ? 102 ARG   B NE    1 
ATOM   2213 C  CZ    . ARG   B 1 103 ? 19.44338  5.41928   43.20975  1.000 71.36382  ? 102 ARG   B CZ    1 
ATOM   2214 N  NH1   . ARG   B 1 103 ? 19.10994  4.80975   44.33675  1.000 72.73933  ? 102 ARG   B NH1   1 
ATOM   2215 N  NH2   . ARG   B 1 103 ? 18.49898  6.02924   42.49733  1.000 62.92286  ? 102 ARG   B NH2   1 
ATOM   2216 N  N     . VAL   B 1 104 ? 23.34761  8.11515   42.01884  1.000 65.70403  ? 103 VAL   B N     1 
ATOM   2217 C  CA    . VAL   B 1 104 ? 23.33223  7.94845   40.56630  1.000 64.64282  ? 103 VAL   B CA    1 
ATOM   2218 C  C     . VAL   B 1 104 ? 24.68075  8.32173   39.95845  1.000 62.89176  ? 103 VAL   B C     1 
ATOM   2219 O  O     . VAL   B 1 104 ? 25.17333  7.64469   39.04637  1.000 65.21219  ? 103 VAL   B O     1 
ATOM   2220 C  CB    . VAL   B 1 104 ? 22.17692  8.76106   39.94966  1.000 57.06128  ? 103 VAL   B CB    1 
ATOM   2221 C  CG1   . VAL   B 1 104 ? 22.35362  8.88602   38.45102  1.000 55.76852  ? 103 VAL   B CG1   1 
ATOM   2222 C  CG2   . VAL   B 1 104 ? 20.83827  8.10174   40.26207  1.000 51.91388  ? 103 VAL   B CG2   1 
ATOM   2223 N  N     . LYS   B 1 105 ? 25.29866  9.39832   40.44280  1.000 60.66053  ? 104 LYS   B N     1 
ATOM   2224 C  CA    . LYS   B 1 105 ? 26.62375  9.77280   39.96433  1.000 65.29800  ? 104 LYS   B CA    1 
ATOM   2225 C  C     . LYS   B 1 105 ? 27.73506  8.97604   40.63615  1.000 71.30747  ? 104 LYS   B C     1 
ATOM   2226 O  O     . LYS   B 1 105 ? 28.88551  9.05507   40.18846  1.000 75.53900  ? 104 LYS   B O     1 
ATOM   2227 C  CB    . LYS   B 1 105 ? 26.85396  11.27723  40.16651  1.000 63.62856  ? 104 LYS   B CB    1 
ATOM   2228 C  CG    . LYS   B 1 105 ? 25.79558  12.14459  39.48635  1.000 57.13348  ? 104 LYS   B CG    1 
ATOM   2229 C  CD    . LYS   B 1 105 ? 26.02385  13.64044  39.68815  1.000 51.64773  ? 104 LYS   B CD    1 
ATOM   2230 C  CE    . LYS   B 1 105 ? 27.13430  14.17277  38.79353  1.000 46.90710  ? 104 LYS   B CE    1 
ATOM   2231 N  NZ    . LYS   B 1 105 ? 26.86592  13.97654  37.34003  1.000 38.43006  ? 104 LYS   B NZ    1 
ATOM   2232 N  N     . ASP   B 1 106 ? 27.41108  8.20723   41.67793  1.000 73.89547  ? 105 ASP   B N     1 
ATOM   2233 C  CA    . ASP   B 1 106 ? 28.36921  7.39486   42.43216  1.000 75.99096  ? 105 ASP   B CA    1 
ATOM   2234 C  C     . ASP   B 1 106 ? 29.52901  8.24879   42.94751  1.000 74.31665  ? 105 ASP   B C     1 
ATOM   2235 O  O     . ASP   B 1 106 ? 30.69889  8.01292   42.64297  1.000 75.74496  ? 105 ASP   B O     1 
ATOM   2236 C  CB    . ASP   B 1 106 ? 28.87977  6.21706   41.59275  1.000 76.28591  ? 105 ASP   B CB    1 
ATOM   2237 C  CG    . ASP   B 1 106 ? 29.59448  5.16220   42.43342  1.000 82.02522  ? 105 ASP   B CG    1 
ATOM   2238 O  OD1   . ASP   B 1 106 ? 29.54692  5.25422   43.68076  1.000 73.85397  ? 105 ASP   B OD1   1 
ATOM   2239 O  OD2   . ASP   B 1 106 ? 30.20322  4.24103   41.84465  1.000 87.21267  ? 105 ASP   B OD2   1 
ATOM   2240 N  N     . SER   B 1 107 ? 29.17841  9.25472   43.74594  1.000 74.91046  ? 106 SER   B N     1 
ATOM   2241 C  CA    . SER   B 1 107 ? 30.16941  10.12417  44.36301  1.000 76.19540  ? 106 SER   B CA    1 
ATOM   2242 C  C     . SER   B 1 107 ? 29.49114  10.97569  45.42149  1.000 80.39984  ? 106 SER   B C     1 
ATOM   2243 O  O     . SER   B 1 107 ? 28.38103  11.46660  45.20860  1.000 80.69154  ? 106 SER   B O     1 
ATOM   2244 C  CB    . SER   B 1 107 ? 30.85156  11.02769  43.32714  1.000 80.22618  ? 106 SER   B CB    1 
ATOM   2245 O  OG    . SER   B 1 107 ? 31.73067  11.94342  43.95665  1.000 82.22137  ? 106 SER   B OG    1 
ATOM   2246 N  N     . GLU   B 1 108 ? 30.15952  11.13699  46.55939  1.000 86.54446  ? 107 GLU   B N     1 
ATOM   2247 C  CA    . GLU   B 1 108 ? 29.77349  12.13091  47.54882  1.000 88.13066  ? 107 GLU   B CA    1 
ATOM   2248 C  C     . GLU   B 1 108 ? 30.43245  13.47301  47.28229  1.000 85.77621  ? 107 GLU   B C     1 
ATOM   2249 O  O     . GLU   B 1 108 ? 30.37406  14.36598  48.13390  1.000 89.94704  ? 107 GLU   B O     1 
ATOM   2250 C  CB    . GLU   B 1 108 ? 30.12133  11.64480  48.95806  1.000 95.98788  ? 107 GLU   B CB    1 
ATOM   2251 C  CG    . GLU   B 1 108 ? 29.39833  10.36930  49.36733  1.000 95.54745  ? 107 GLU   B CG    1 
ATOM   2252 C  CD    . GLU   B 1 108 ? 29.75628  9.91891   50.76994  1.000 96.13647  ? 107 GLU   B CD    1 
ATOM   2253 O  OE1   . GLU   B 1 108 ? 30.76272  10.41903  51.31821  1.000 98.32379  ? 107 GLU   B OE1   1 
ATOM   2254 O  OE2   . GLU   B 1 108 ? 29.02901  9.06729   51.32495  1.000 95.51819  ? 107 GLU   B OE2   1 
ATOM   2255 N  N     . ASP   B 1 109 ? 31.05708  13.62650  46.11694  1.000 82.14611  ? 108 ASP   B N     1 
ATOM   2256 C  CA    . ASP   B 1 109 ? 31.75861  14.84778  45.75564  1.000 81.52001  ? 108 ASP   B CA    1 
ATOM   2257 C  C     . ASP   B 1 109 ? 31.09596  15.48492  44.53748  1.000 80.61968  ? 108 ASP   B C     1 
ATOM   2258 O  O     . ASP   B 1 109 ? 31.72445  15.63200  43.48308  1.000 81.65821  ? 108 ASP   B O     1 
ATOM   2259 C  CB    . ASP   B 1 109 ? 33.23292  14.53151  45.49021  1.000 86.89119  ? 108 ASP   B CB    1 
ATOM   2260 C  CG    . ASP   B 1 109 ? 34.11443  15.76250  45.52312  1.000 94.27715  ? 108 ASP   B CG    1 
ATOM   2261 O  OD1   . ASP   B 1 109 ? 33.91103  16.61751  46.41159  1.000 95.98637  ? 108 ASP   B OD1   1 
ATOM   2262 O  OD2   . ASP   B 1 109 ? 35.02460  15.86195  44.66946  1.000 98.41017  ? 108 ASP   B OD2   1 
ATOM   2263 N  N     . VAL   B 1 110 ? 29.82997  15.85859  44.66606  1.000 72.38224  ? 109 VAL   B N     1 
ATOM   2264 C  CA    . VAL   B 1 110 ? 29.04214  16.41084  43.56829  1.000 60.60751  ? 109 VAL   B CA    1 
ATOM   2265 C  C     . VAL   B 1 110 ? 28.72387  17.87296  43.88752  1.000 54.80328  ? 109 VAL   B C     1 
ATOM   2266 O  O     . VAL   B 1 110 ? 28.12342  18.13891  44.93389  1.000 52.76833  ? 109 VAL   B O     1 
ATOM   2267 C  CB    . VAL   B 1 110 ? 27.74359  15.62027  43.33082  1.000 60.29313  ? 109 VAL   B CB    1 
ATOM   2268 C  CG1   . VAL   B 1 110 ? 26.90175  16.29194  42.25449  1.000 54.82849  ? 109 VAL   B CG1   1 
ATOM   2269 C  CG2   . VAL   B 1 110 ? 28.06558  14.18809  42.94335  1.000 67.00121  ? 109 VAL   B CG2   1 
ATOM   2270 N  N     . PRO   B 1 111 ? 29.08778  18.81600  43.02370  1.000 51.64024  ? 110 PRO   B N     1 
ATOM   2271 C  CA    . PRO   B 1 111 ? 28.77727  20.23050  43.29427  1.000 49.80516  ? 110 PRO   B CA    1 
ATOM   2272 C  C     . PRO   B 1 111 ? 27.28523  20.43604  43.47620  1.000 50.88051  ? 110 PRO   B C     1 
ATOM   2273 O  O     . PRO   B 1 111 ? 26.48022  20.11127  42.59667  1.000 48.29872  ? 110 PRO   B O     1 
ATOM   2274 C  CB    . PRO   B 1 111 ? 29.30021  20.95325  42.04896  1.000 49.36751  ? 110 PRO   B CB    1 
ATOM   2275 C  CG    . PRO   B 1 111 ? 30.29506  20.01025  41.44571  1.000 55.21751  ? 110 PRO   B CG    1 
ATOM   2276 C  CD    . PRO   B 1 111 ? 29.77925  18.63996  41.73801  1.000 58.41403  ? 110 PRO   B CD    1 
ATOM   2277 N  N     . MET   B 1 112 ? 26.91703  20.95348  44.64411  1.000 50.00717  ? 111 MET   B N     1 
ATOM   2278 C  CA    . MET   B 1 112 ? 25.53119  21.24685  44.95989  1.000 46.28213  ? 111 MET   B CA    1 
ATOM   2279 C  C     . MET   B 1 112 ? 25.45188  22.56516  45.70101  1.000 49.11341  ? 111 MET   B C     1 
ATOM   2280 O  O     . MET   B 1 112 ? 26.42360  23.01227  46.31551  1.000 56.03134  ? 111 MET   B O     1 
ATOM   2281 C  CB    . MET   B 1 112 ? 24.88363  20.16164  45.81966  1.000 50.20983  ? 111 MET   B CB    1 
ATOM   2282 C  CG    . MET   B 1 112 ? 24.87023  18.79714  45.19314  1.000 53.17313  ? 111 MET   B CG    1 
ATOM   2283 S  SD    . MET   B 1 112 ? 23.80496  17.69246  46.12428  1.000 55.36338  ? 111 MET   B SD    1 
ATOM   2284 C  CE    . MET   B 1 112 ? 24.45369  16.11402  45.59502  1.000 56.32137  ? 111 MET   B CE    1 
ATOM   2285 N  N     . VAL   B 1 113 ? 24.27475  23.17229  45.64291  1.000 43.66987  ? 112 VAL   B N     1 
ATOM   2286 C  CA    . VAL   B 1 113 ? 23.95107  24.36319  46.41219  1.000 48.85179  ? 112 VAL   B CA    1 
ATOM   2287 C  C     . VAL   B 1 113 ? 22.55727  24.16270  46.98024  1.000 51.56713  ? 112 VAL   B C     1 
ATOM   2288 O  O     . VAL   B 1 113 ? 21.60947  23.91896  46.22652  1.000 47.45107  ? 112 VAL   B O     1 
ATOM   2289 C  CB    . VAL   B 1 113 ? 24.01450  25.64146  45.55955  1.000 53.09205  ? 112 VAL   B CB    1 
ATOM   2290 C  CG1   . VAL   B 1 113 ? 23.29430  26.78478  46.25129  1.000 50.21013  ? 112 VAL   B CG1   1 
ATOM   2291 C  CG2   . VAL   B 1 113 ? 25.46317  26.01601  45.27299  1.000 47.14811  ? 112 VAL   B CG2   1 
ATOM   2292 N  N     . LEU   B 1 114 ? 22.43313  24.23469  48.30551  1.000 51.69961  ? 113 LEU   B N     1 
ATOM   2293 C  CA    . LEU   B 1 114 ? 21.11834  24.20407  48.93558  1.000 51.31936  ? 113 LEU   B CA    1 
ATOM   2294 C  C     . LEU   B 1 114 ? 20.47492  25.58098  48.83166  1.000 49.82147  ? 113 LEU   B C     1 
ATOM   2295 O  O     . LEU   B 1 114 ? 21.09756  26.59199  49.16846  1.000 51.67873  ? 113 LEU   B O     1 
ATOM   2296 C  CB    . LEU   B 1 114 ? 21.22783  23.77017  50.39897  1.000 56.43695  ? 113 LEU   B CB    1 
ATOM   2297 C  CG    . LEU   B 1 114 ? 19.92321  23.72357  51.19799  1.000 59.28765  ? 113 LEU   B CG    1 
ATOM   2298 C  CD1   . LEU   B 1 114 ? 19.00493  22.61799  50.69675  1.000 53.44121  ? 113 LEU   B CD1   1 
ATOM   2299 C  CD2   . LEU   B 1 114 ? 20.21805  23.55389  52.68645  1.000 63.80022  ? 113 LEU   B CD2   1 
ATOM   2300 N  N     . VAL   B 1 115 ? 19.22975  25.62092  48.37020  1.000 47.65982  ? 114 VAL   B N     1 
ATOM   2301 C  CA    . VAL   B 1 115 ? 18.54036  26.86823  48.06889  1.000 49.35243  ? 114 VAL   B CA    1 
ATOM   2302 C  C     . VAL   B 1 115 ? 17.22078  26.87294  48.82045  1.000 50.23636  ? 114 VAL   B C     1 
ATOM   2303 O  O     . VAL   B 1 115 ? 16.29480  26.13671  48.46148  1.000 47.47822  ? 114 VAL   B O     1 
ATOM   2304 C  CB    . VAL   B 1 115 ? 18.30239  27.05465  46.56181  1.000 45.76436  ? 114 VAL   B CB    1 
ATOM   2305 C  CG1   . VAL   B 1 115 ? 17.33549  28.20618  46.30991  1.000 43.21982  ? 114 VAL   B CG1   1 
ATOM   2306 C  CG2   . VAL   B 1 115 ? 19.61779  27.29322  45.83380  1.000 49.15277  ? 114 VAL   B CG2   1 
ATOM   2307 N  N     . GLY   B 1 116 ? 17.12649  27.70431  49.85434  1.000 57.26331  ? 115 GLY   B N     1 
ATOM   2308 C  CA    . GLY   B 1 116 ? 15.85319  27.93243  50.50252  1.000 55.36864  ? 115 GLY   B CA    1 
ATOM   2309 C  C     . GLY   B 1 116 ? 15.11986  29.07832  49.84741  1.000 54.63435  ? 115 GLY   B C     1 
ATOM   2310 O  O     . GLY   B 1 116 ? 15.50509  30.23668  50.01994  1.000 58.94802  ? 115 GLY   B O     1 
ATOM   2311 N  N     . ASN   B 1 117 ? 14.07081  28.77472  49.09223  1.000 52.54858  ? 116 ASN   B N     1 
ATOM   2312 C  CA    . ASN   B 1 117 ? 13.35242  29.77037  48.30967  1.000 55.84116  ? 116 ASN   B CA    1 
ATOM   2313 C  C     . ASN   B 1 117 ? 12.12609  30.26278  49.06726  1.000 55.98654  ? 116 ASN   B C     1 
ATOM   2314 O  O     . ASN   B 1 117 ? 11.73706  29.70520  50.09542  1.000 58.61017  ? 116 ASN   B O     1 
ATOM   2315 C  CB    . ASN   B 1 117 ? 12.94596  29.19770  46.94287  1.000 54.42145  ? 116 ASN   B CB    1 
ATOM   2316 C  CG    . ASN   B 1 117 ? 12.38106  30.25468  46.00994  1.000 49.99267  ? 116 ASN   B CG    1 
ATOM   2317 O  OD1   . ASN   B 1 117 ? 12.95026  31.33910  45.86948  1.000 50.80875  ? 116 ASN   B OD1   1 
ATOM   2318 N  ND2   . ASN   B 1 117 ? 11.24942  29.95765  45.39466  1.000 44.19099  ? 116 ASN   B ND2   1 
ATOM   2319 N  N     . LYS   B 1 118 ? 11.52189  31.33245  48.53393  1.000 57.65560  ? 117 LYS   B N     1 
ATOM   2320 C  CA    . LYS   B 1 118 ? 10.31799  31.96884  49.07522  1.000 64.51984  ? 117 LYS   B CA    1 
ATOM   2321 C  C     . LYS   B 1 118 ? 10.58534  32.70339  50.38980  1.000 69.95936  ? 117 LYS   B C     1 
ATOM   2322 O  O     . LYS   B 1 118 ? 9.68276   32.83969  51.22048  1.000 71.66006  ? 117 LYS   B O     1 
ATOM   2323 C  CB    . LYS   B 1 118 ? 9.17416   30.96190  49.25670  1.000 60.81574  ? 117 LYS   B CB    1 
ATOM   2324 C  CG    . LYS   B 1 118 ? 8.86587   30.13229  48.02704  1.000 61.24415  ? 117 LYS   B CG    1 
ATOM   2325 C  CD    . LYS   B 1 118 ? 7.50890   29.45786  48.13098  1.000 55.00372  ? 117 LYS   B CD    1 
ATOM   2326 C  CE    . LYS   B 1 118 ? 7.25383   28.56305  46.93118  1.000 50.59409  ? 117 LYS   B CE    1 
ATOM   2327 N  NZ    . LYS   B 1 118 ? 5.82766   28.15687  46.84420  1.000 50.45753  ? 117 LYS   B NZ    1 
ATOM   2328 N  N     . CYS   B 1 119 ? 11.81312  33.20291  50.58489  1.000 65.34471  ? 118 CYS   B N     1 
ATOM   2329 C  CA    A CYS   B 1 119 ? 12.15885  33.88416  51.82515  0.500 70.84388  ? 118 CYS   B CA    1 
ATOM   2330 C  CA    B CYS   B 1 119 ? 12.17087  33.90252  51.81546  0.500 70.84291  ? 118 CYS   B CA    1 
ATOM   2331 C  C     . CYS   B 1 119 ? 11.44976  35.22953  51.98229  1.000 74.94727  ? 118 CYS   B C     1 
ATOM   2332 O  O     . CYS   B 1 119 ? 11.70121  35.93570  52.96328  1.000 78.31876  ? 118 CYS   B O     1 
ATOM   2333 C  CB    A CYS   B 1 119 ? 13.67939  34.06365  51.91631  0.500 73.12271  ? 118 CYS   B CB    1 
ATOM   2334 C  CB    B CYS   B 1 119 ? 13.67793  34.11285  51.87148  0.500 73.14891  ? 118 CYS   B CB    1 
ATOM   2335 S  SG    A CYS   B 1 119 ? 14.37478  35.26606  50.77250  0.500 79.35836  ? 118 CYS   B SG    1 
ATOM   2336 S  SG    B CYS   B 1 119 ? 14.59230  32.57283  52.17710  0.500 79.35836  ? 118 CYS   B SG    1 
ATOM   2337 N  N     . ASP   B 1 120 ? 10.57266  35.59830  51.05699  1.000 70.96023  ? 119 ASP   B N     1 
ATOM   2338 C  CA    . ASP   B 1 120 ? 9.75987   36.78735  51.24061  1.000 74.44461  ? 119 ASP   B CA    1 
ATOM   2339 C  C     . ASP   B 1 120 ? 8.56467   36.51984  52.13970  1.000 77.95030  ? 119 ASP   B C     1 
ATOM   2340 O  O     . ASP   B 1 120 ? 7.98213   37.46540  52.67939  1.000 82.63507  ? 119 ASP   B O     1 
ATOM   2341 C  CB    . ASP   B 1 120 ? 9.26163   37.28408  49.89253  1.000 72.20343  ? 119 ASP   B CB    1 
ATOM   2342 C  CG    . ASP   B 1 120 ? 8.48174   36.22841  49.15890  1.000 68.46442  ? 119 ASP   B CG    1 
ATOM   2343 O  OD1   . ASP   B 1 120 ? 9.08739   35.20986  48.75752  1.000 63.76439  ? 119 ASP   B OD1   1 
ATOM   2344 O  OD2   . ASP   B 1 120 ? 7.25819   36.40490  49.01571  1.000 71.91444  ? 119 ASP   B OD2   1 
ATOM   2345 N  N     . LEU   B 1 121 ? 8.19392   35.25409  52.30837  1.000 81.23525  ? 120 LEU   B N     1 
ATOM   2346 C  CA    . LEU   B 1 121 ? 6.97882   34.86539  53.00053  1.000 86.40765  ? 120 LEU   B CA    1 
ATOM   2347 C  C     . LEU   B 1 121 ? 7.15523   34.94506  54.51469  1.000 89.00204  ? 120 LEU   B C     1 
ATOM   2348 O  O     . LEU   B 1 121 ? 8.27423   34.86344  55.03120  1.000 85.06431  ? 120 LEU   B O     1 
ATOM   2349 C  CB    . LEU   B 1 121 ? 6.58145   33.45220  52.58266  1.000 81.20524  ? 120 LEU   B CB    1 
ATOM   2350 C  CG    . LEU   B 1 121 ? 6.10529   33.30396  51.13665  1.000 73.39788  ? 120 LEU   B CG    1 
ATOM   2351 C  CD1   . LEU   B 1 121 ? 5.81645   31.84857  50.81522  1.000 68.68092  ? 120 LEU   B CD1   1 
ATOM   2352 C  CD2   . LEU   B 1 121 ? 4.87835   34.16700  50.89454  1.000 73.28921  ? 120 LEU   B CD2   1 
ATOM   2353 N  N     . PRO   B 1 122 ? 6.05476   35.12411  55.25095  1.000 92.59950  ? 121 PRO   B N     1 
ATOM   2354 C  CA    . PRO   B 1 122 ? 6.13630   35.18566  56.71176  1.000 94.25488  ? 121 PRO   B CA    1 
ATOM   2355 C  C     . PRO   B 1 122 ? 5.97975   33.84468  57.40690  1.000 94.29700  ? 121 PRO   B C     1 
ATOM   2356 O  O     . PRO   B 1 122 ? 6.27337   33.75598  58.60628  1.000 98.70279  ? 121 PRO   B O     1 
ATOM   2357 C  CB    . PRO   B 1 122 ? 4.96591   36.11346  57.06211  1.000 99.17126  ? 121 PRO   B CB    1 
ATOM   2358 C  CG    . PRO   B 1 122 ? 3.93887   35.78579  56.02457  1.000 95.78928  ? 121 PRO   B CG    1 
ATOM   2359 C  CD    . PRO   B 1 122 ? 4.70147   35.45174  54.76106  1.000 94.19309  ? 121 PRO   B CD    1 
ATOM   2360 N  N     . SER   B 1 123 ? 5.53724   32.80531  56.69849  1.000 92.87922  ? 122 SER   B N     1 
ATOM   2361 C  CA    . SER   B 1 123 ? 5.19676   31.55164  57.35763  1.000 98.60816  ? 122 SER   B CA    1 
ATOM   2362 C  C     . SER   B 1 123 ? 6.41608   30.80416  57.87420  1.000 99.32391  ? 122 SER   B C     1 
ATOM   2363 O  O     . SER   B 1 123 ? 6.25643   29.93412  58.73575  1.000 93.14200  ? 122 SER   B O     1 
ATOM   2364 C  CB    . SER   B 1 123 ? 4.41369   30.65322  56.40132  1.000 96.16595  ? 122 SER   B CB    1 
ATOM   2365 O  OG    . SER   B 1 123 ? 3.22197   31.28601  55.97489  1.000 99.34492  ? 122 SER   B OG    1 
ATOM   2366 N  N     . ARG   B 1 124 ? 7.61358   31.15089  57.38555  1.000 97.71368  ? 123 ARG   B N     1 
ATOM   2367 C  CA    . ARG   B 1 124 ? 8.87219   30.42180  57.55919  1.000 92.53070  ? 123 ARG   B CA    1 
ATOM   2368 C  C     . ARG   B 1 124 ? 8.83129   29.29898  58.59071  1.000 95.11815  ? 123 ARG   B C     1 
ATOM   2369 O  O     . ARG   B 1 124 ? 8.90259   29.55033  59.79740  1.000 93.90747  ? 123 ARG   B O     1 
ATOM   2370 C  CB    . ARG   B 1 124 ? 9.99695   31.39222  57.92563  1.000 89.24376  ? 123 ARG   B CB    1 
ATOM   2371 C  CG    . ARG   B 1 124 ? 11.36304  30.73710  57.89117  1.000 89.67937  ? 123 ARG   B CG    1 
ATOM   2372 C  CD    . ARG   B 1 124 ? 12.41125  31.54566  58.62095  1.000 90.60182  ? 123 ARG   B CD    1 
ATOM   2373 N  NE    . ARG   B 1 124 ? 13.15818  32.41754  57.72460  1.000 88.69369  ? 123 ARG   B NE    1 
ATOM   2374 C  CZ    . ARG   B 1 124 ? 14.24673  32.05093  57.06405  1.000 90.39916  ? 123 ARG   B CZ    1 
ATOM   2375 N  NH1   . ARG   B 1 124 ? 14.72910  30.82227  57.15449  1.000 93.33602  ? 123 ARG   B NH1   1 
ATOM   2376 N  NH2   . ARG   B 1 124 ? 14.86611  32.93892  56.29351  1.000 88.23485  ? 123 ARG   B NH2   1 
ATOM   2377 N  N     . THR   B 1 125 ? 8.71053   28.05801  58.12424  1.000 88.75771  ? 124 THR   B N     1 
ATOM   2378 C  CA    . THR   B 1 125 ? 8.70635   26.89267  58.99660  1.000 88.34380  ? 124 THR   B CA    1 
ATOM   2379 C  C     . THR   B 1 125 ? 10.04469  26.17092  59.01502  1.000 89.52868  ? 124 THR   B C     1 
ATOM   2380 O  O     . THR   B 1 125 ? 10.20295  25.19875  59.76053  1.000 87.83425  ? 124 THR   B O     1 
ATOM   2381 C  CB    . THR   B 1 125 ? 7.60465   25.92173  58.57678  1.000 84.41160  ? 124 THR   B CB    1 
ATOM   2382 O  OG1   . THR   B 1 125 ? 7.87454   25.44801  57.25472  1.000 81.33230  ? 124 THR   B OG1   1 
ATOM   2383 C  CG2   . THR   B 1 125 ? 6.26491   26.62293  58.59183  1.000 86.30920  ? 124 THR   B CG2   1 
ATOM   2384 N  N     . VAL   B 1 126 ? 11.00341  26.61670  58.21015  1.000 86.80421  ? 125 VAL   B N     1 
ATOM   2385 C  CA    . VAL   B 1 126 ? 12.36518  26.10057  58.23026  1.000 87.79032  ? 125 VAL   B CA    1 
ATOM   2386 C  C     . VAL   B 1 126 ? 13.27961  27.24895  58.63067  1.000 90.20182  ? 125 VAL   B C     1 
ATOM   2387 O  O     . VAL   B 1 126 ? 13.32372  28.28232  57.95208  1.000 87.33836  ? 125 VAL   B O     1 
ATOM   2388 C  CB    . VAL   B 1 126 ? 12.77867  25.50946  56.87342  1.000 82.83170  ? 125 VAL   B CB    1 
ATOM   2389 C  CG1   . VAL   B 1 126 ? 14.10417  24.77038  57.00458  1.000 81.27718  ? 125 VAL   B CG1   1 
ATOM   2390 C  CG2   . VAL   B 1 126 ? 11.69103  24.58426  56.33693  1.000 78.14518  ? 125 VAL   B CG2   1 
ATOM   2391 N  N     . ASP   B 1 127 ? 13.99638  27.07592  59.73432  1.000 95.52637  ? 126 ASP   B N     1 
ATOM   2392 C  CA    . ASP   B 1 127 ? 14.83235  28.14925  60.24148  1.000 99.97216  ? 126 ASP   B CA    1 
ATOM   2393 C  C     . ASP   B 1 127 ? 16.09479  28.28980  59.40087  1.000 98.19496  ? 126 ASP   B C     1 
ATOM   2394 O  O     . ASP   B 1 127 ? 16.54891  27.34750  58.74753  1.000 94.69917  ? 126 ASP   B O     1 
ATOM   2395 C  CB    . ASP   B 1 127 ? 15.20990  27.89649  61.70063  1.000 105.02133 ? 126 ASP   B CB    1 
ATOM   2396 C  CG    . ASP   B 1 127 ? 14.00573  27.58574  62.56940  1.000 115.54300 ? 126 ASP   B CG    1 
ATOM   2397 O  OD1   . ASP   B 1 127 ? 12.91919  27.30345  62.01402  1.000 110.42639 ? 126 ASP   B OD1   1 
ATOM   2398 O  OD2   . ASP   B 1 127 ? 14.14799  27.62639  63.81006  1.000 125.26316 ? 126 ASP   B OD2   1 
ATOM   2399 N  N     . THR   B 1 128 ? 16.65886  29.49905  59.42137  1.000 99.92229  ? 127 THR   B N     1 
ATOM   2400 C  CA    . THR   B 1 128 ? 17.95521  29.72086  58.78939  1.000 101.96663 ? 127 THR   B CA    1 
ATOM   2401 C  C     . THR   B 1 128 ? 19.00633  28.77643  59.35960  1.000 101.12124 ? 127 THR   B C     1 
ATOM   2402 O  O     . THR   B 1 128 ? 19.83015  28.22678  58.61862  1.000 93.96607  ? 127 THR   B O     1 
ATOM   2403 C  CB    . THR   B 1 128 ? 18.38393  31.17833  58.97326  1.000 104.93784 ? 127 THR   B CB    1 
ATOM   2404 O  OG1   . THR   B 1 128 ? 17.42701  32.04475  58.34737  1.000 94.36837  ? 127 THR   B OG1   1 
ATOM   2405 C  CG2   . THR   B 1 128 ? 19.76188  31.41884  58.36745  1.000 98.84347  ? 127 THR   B CG2   1 
ATOM   2406 N  N     . LYS   B 1 129 ? 18.98444  28.57027  60.67823  1.000 102.64531 ? 128 LYS   B N     1 
ATOM   2407 C  CA    . LYS   B 1 129 ? 19.88631  27.60854  61.30213  1.000 102.13183 ? 128 LYS   B CA    1 
ATOM   2408 C  C     . LYS   B 1 129 ? 19.55588  26.18707  60.86932  1.000 98.77076  ? 128 LYS   B C     1 
ATOM   2409 O  O     . LYS   B 1 129 ? 20.45959  25.37727  60.62687  1.000 95.45598  ? 128 LYS   B O     1 
ATOM   2410 C  CB    . LYS   B 1 129 ? 19.80586  27.73991  62.82239  1.000 108.95786 ? 128 LYS   B CB    1 
ATOM   2411 C  CG    . LYS   B 1 129 ? 20.42790  26.58973  63.58869  1.000 112.36420 ? 128 LYS   B CG    1 
ATOM   2412 C  CD    . LYS   B 1 129 ? 20.01985  26.63979  65.05069  1.000 118.95192 ? 128 LYS   B CD    1 
ATOM   2413 C  CE    . LYS   B 1 129 ? 20.64064  25.50424  65.84050  1.000 122.89212 ? 128 LYS   B CE    1 
ATOM   2414 N  NZ    . LYS   B 1 129 ? 22.12592  25.57866  65.83436  1.000 124.43780 ? 128 LYS   B NZ    1 
ATOM   2415 N  N     . GLN   B 1 130 ? 18.26243  25.86989  60.77354  1.000 98.50019  ? 129 GLN   B N     1 
ATOM   2416 C  CA    . GLN   B 1 130 ? 17.84108  24.54313  60.33777  1.000 94.46522  ? 129 GLN   B CA    1 
ATOM   2417 C  C     . GLN   B 1 130 ? 18.43450  24.19973  58.97617  1.000 89.72681  ? 129 GLN   B C     1 
ATOM   2418 O  O     . GLN   B 1 130 ? 18.93741  23.08831  58.76606  1.000 84.33254  ? 129 GLN   B O     1 
ATOM   2419 C  CB    . GLN   B 1 130 ? 16.31309  24.48842  60.30220  1.000 93.45405  ? 129 GLN   B CB    1 
ATOM   2420 C  CG    . GLN   B 1 130 ? 15.71379  23.10183  60.39487  1.000 91.92305  ? 129 GLN   B CG    1 
ATOM   2421 C  CD    . GLN   B 1 130 ? 14.21318  23.13835  60.60885  1.000 90.56089  ? 129 GLN   B CD    1 
ATOM   2422 O  OE1   . GLN   B 1 130 ? 13.63063  24.19770  60.84278  1.000 93.60261  ? 129 GLN   B OE1   1 
ATOM   2423 N  NE2   . GLN   B 1 130 ? 13.57944  21.97786  60.52959  1.000 88.36764  ? 129 GLN   B NE2   1 
ATOM   2424 N  N     . ALA   B 1 131 ? 18.41412  25.15756  58.04913  1.000 91.12200  ? 130 ALA   B N     1 
ATOM   2425 C  CA    . ALA   B 1 131 ? 18.95460  24.92608  56.71575  1.000 85.04776  ? 130 ALA   B CA    1 
ATOM   2426 C  C     . ALA   B 1 131 ? 20.47912  24.95634  56.70839  1.000 88.59930  ? 130 ALA   B C     1 
ATOM   2427 O  O     . ALA   B 1 131 ? 21.11392  24.18179  55.98063  1.000 79.19699  ? 130 ALA   B O     1 
ATOM   2428 C  CB    . ALA   B 1 131 ? 18.39517  25.96458  55.74691  1.000 79.91517  ? 130 ALA   B CB    1 
ATOM   2429 N  N     . GLN   B 1 132 ? 21.08158  25.83431  57.51761  1.000 90.49439  ? 131 GLN   B N     1 
ATOM   2430 C  CA    . GLN   B 1 132 ? 22.53028  26.01279  57.46978  1.000 89.74332  ? 131 GLN   B CA    1 
ATOM   2431 C  C     . GLN   B 1 132 ? 23.26645  24.78549  57.98946  1.000 91.18240  ? 131 GLN   B C     1 
ATOM   2432 O  O     . GLN   B 1 132 ? 24.32692  24.42508  57.46511  1.000 88.05888  ? 131 GLN   B O     1 
ATOM   2433 C  CB    . GLN   B 1 132 ? 22.93675  27.25463  58.26135  1.000 95.52989  ? 131 GLN   B CB    1 
ATOM   2434 C  CG    . GLN   B 1 132 ? 22.81897  28.55160  57.47873  1.000 97.69166  ? 131 GLN   B CG    1 
ATOM   2435 C  CD    . GLN   B 1 132 ? 23.18180  29.76962  58.30420  1.000 104.68010 ? 131 GLN   B CD    1 
ATOM   2436 O  OE1   . GLN   B 1 132 ? 23.01814  29.78041  59.52470  1.000 106.70440 ? 131 GLN   B OE1   1 
ATOM   2437 N  NE2   . GLN   B 1 132 ? 23.67973  30.80512  57.63982  1.000 103.69815 ? 131 GLN   B NE2   1 
ATOM   2438 N  N     . ASP   B 1 133 ? 22.72563  24.13150  59.01838  1.000 92.08875  ? 132 ASP   B N     1 
ATOM   2439 C  CA    . ASP   B 1 133 ? 23.38139  22.94129  59.54689  1.000 93.36890  ? 132 ASP   B CA    1 
ATOM   2440 C  C     . ASP   B 1 133 ? 23.34077  21.79774  58.54114  1.000 89.02375  ? 132 ASP   B C     1 
ATOM   2441 O  O     . ASP   B 1 133 ? 24.30804  21.03650  58.41980  1.000 87.23007  ? 132 ASP   B O     1 
ATOM   2442 C  CB    . ASP   B 1 133 ? 22.73622  22.52961  60.86975  1.000 98.64938  ? 132 ASP   B CB    1 
ATOM   2443 C  CG    . ASP   B 1 133 ? 23.00121  23.52730  61.98118  1.000 103.98119 ? 132 ASP   B CG    1 
ATOM   2444 O  OD1   . ASP   B 1 133 ? 23.73078  24.51058  61.73782  1.000 103.29337 ? 132 ASP   B OD1   1 
ATOM   2445 O  OD2   . ASP   B 1 133 ? 22.48074  23.32886  63.09779  1.000 107.51447 ? 132 ASP   B OD2   1 
ATOM   2446 N  N     . LEU   B 1 134 ? 22.23506  21.66622  57.80511  1.000 87.63124  ? 133 LEU   B N     1 
ATOM   2447 C  CA    . LEU   B 1 134 ? 22.14026  20.61946  56.79204  1.000 84.46397  ? 133 LEU   B CA    1 
ATOM   2448 C  C     . LEU   B 1 134 ? 23.22110  20.78880  55.73377  1.000 80.59144  ? 133 LEU   B C     1 
ATOM   2449 O  O     . LEU   B 1 134 ? 23.88652  19.82137  55.34510  1.000 78.76622  ? 133 LEU   B O     1 
ATOM   2450 C  CB    . LEU   B 1 134 ? 20.75244  20.63434  56.15260  1.000 79.10956  ? 133 LEU   B CB    1 
ATOM   2451 C  CG    . LEU   B 1 134 ? 20.47992  19.50269  55.16002  1.000 79.37815  ? 133 LEU   B CG    1 
ATOM   2452 C  CD1   . LEU   B 1 134 ? 20.65932  18.14903  55.83012  1.000 79.98059  ? 133 LEU   B CD1   1 
ATOM   2453 C  CD2   . LEU   B 1 134 ? 19.08921  19.62915  54.55633  1.000 71.52635  ? 133 LEU   B CD2   1 
ATOM   2454 N  N     . ALA   B 1 135 ? 23.41557  22.02291  55.26401  1.000 79.39869  ? 134 ALA   B N     1 
ATOM   2455 C  CA    . ALA   B 1 135 ? 24.46800  22.29272  54.29167  1.000 77.21505  ? 134 ALA   B CA    1 
ATOM   2456 C  C     . ALA   B 1 135 ? 25.84144  21.92093  54.83379  1.000 81.25711  ? 134 ALA   B C     1 
ATOM   2457 O  O     . ALA   B 1 135 ? 26.70259  21.45722  54.07666  1.000 73.15499  ? 134 ALA   B O     1 
ATOM   2458 C  CB    . ALA   B 1 135 ? 24.43268  23.76515  53.88605  1.000 75.07408  ? 134 ALA   B CB    1 
ATOM   2459 N  N     . ARG   B 1 136 ? 26.06152  22.10519  56.14015  1.000 87.79699  ? 135 ARG   B N     1 
ATOM   2460 C  CA    . ARG   B 1 136 ? 27.35715  21.77338  56.72307  1.000 86.71043  ? 135 ARG   B CA    1 
ATOM   2461 C  C     . ARG   B 1 136 ? 27.58491  20.26615  56.73219  1.000 85.51816  ? 135 ARG   B C     1 
ATOM   2462 O  O     . ARG   B 1 136 ? 28.71195  19.80210  56.52040  1.000 85.86177  ? 135 ARG   B O     1 
ATOM   2463 C  CB    . ARG   B 1 136 ? 27.46161  22.35394  58.13473  1.000 93.31005  ? 135 ARG   B CB    1 
ATOM   2464 C  CG    . ARG   B 1 136 ? 28.82876  22.94126  58.46721  1.000 97.91731  ? 135 ARG   B CG    1 
ATOM   2465 C  CD    . ARG   B 1 136 ? 28.86324  23.59038  59.85302  1.000 103.22855 ? 135 ARG   B CD    1 
ATOM   2466 N  NE    . ARG   B 1 136 ? 28.00663  24.76827  59.95057  1.000 103.96118 ? 135 ARG   B NE    1 
ATOM   2467 C  CZ    . ARG   B 1 136 ? 26.87848  24.82328  60.64663  1.000 103.89842 ? 135 ARG   B CZ    1 
ATOM   2468 N  NH1   . ARG   B 1 136 ? 26.44138  23.78373  61.33806  1.000 105.40990 ? 135 ARG   B NH1   1 
ATOM   2469 N  NH2   . ARG   B 1 136 ? 26.17367  25.95169  60.65352  1.000 102.96976 ? 135 ARG   B NH2   1 
ATOM   2470 N  N     . SER   B 1 137 ? 26.52685  19.48390  56.96551  1.000 85.32893  ? 136 SER   B N     1 
ATOM   2471 C  CA    . SER   B 1 137 ? 26.65554  18.03328  56.89153  1.000 86.85264  ? 136 SER   B CA    1 
ATOM   2472 C  C     . SER   B 1 137 ? 26.90290  17.55505  55.46684  1.000 85.11444  ? 136 SER   B C     1 
ATOM   2473 O  O     . SER   B 1 137 ? 27.47652  16.47732  55.27685  1.000 82.08764  ? 136 SER   B O     1 
ATOM   2474 C  CB    . SER   B 1 137 ? 25.40711  17.35736  57.46246  1.000 86.60347  ? 136 SER   B CB    1 
ATOM   2475 O  OG    . SER   B 1 137 ? 24.29716  17.50986  56.59747  1.000 83.46538  ? 136 SER   B OG    1 
ATOM   2476 N  N     . TYR   B 1 138 ? 26.48796  18.33357  54.46703  1.000 85.00314  ? 137 TYR   B N     1 
ATOM   2477 C  CA    . TYR   B 1 138 ? 26.74145  18.00576  53.06941  1.000 81.96424  ? 137 TYR   B CA    1 
ATOM   2478 C  C     . TYR   B 1 138 ? 28.05126  18.59147  52.55889  1.000 79.44470  ? 137 TYR   B C     1 
ATOM   2479 O  O     . TYR   B 1 138 ? 28.65834  18.02668  51.64088  1.000 78.96927  ? 137 TYR   B O     1 
ATOM   2480 C  CB    . TYR   B 1 138 ? 25.59201  18.50834  52.18643  1.000 79.31194  ? 137 TYR   B CB    1 
ATOM   2481 C  CG    . TYR   B 1 138 ? 24.24839  17.83953  52.42079  1.000 81.46805  ? 137 TYR   B CG    1 
ATOM   2482 C  CD1   . TYR   B 1 138 ? 24.16252  16.53800  52.90163  1.000 81.19174  ? 137 TYR   B CD1   1 
ATOM   2483 C  CD2   . TYR   B 1 138 ? 23.06336  18.51389  52.14922  1.000 79.98547  ? 137 TYR   B CD2   1 
ATOM   2484 C  CE1   . TYR   B 1 138 ? 22.93341  15.93186  53.10823  1.000 76.84741  ? 137 TYR   B CE1   1 
ATOM   2485 C  CE2   . TYR   B 1 138 ? 21.83247  17.91540  52.35219  1.000 77.34561  ? 137 TYR   B CE2   1 
ATOM   2486 C  CZ    . TYR   B 1 138 ? 21.77327  16.62730  52.83254  1.000 76.12057  ? 137 TYR   B CZ    1 
ATOM   2487 O  OH    . TYR   B 1 138 ? 20.54780  16.03606  53.03321  1.000 71.81967  ? 137 TYR   B OH    1 
ATOM   2488 N  N     . GLY   B 1 139 ? 28.49880  19.70533  53.12959  1.000 78.65462  ? 138 GLY   B N     1 
ATOM   2489 C  CA    . GLY   B 1 139 ? 29.68771  20.37708  52.63848  1.000 78.87174  ? 138 GLY   B CA    1 
ATOM   2490 C  C     . GLY   B 1 139 ? 29.42419  21.28805  51.46357  1.000 75.28787  ? 138 GLY   B C     1 
ATOM   2491 O  O     . GLY   B 1 139 ? 30.23461  21.35044  50.52955  1.000 73.45229  ? 138 GLY   B O     1 
ATOM   2492 N  N     . ILE   B 1 140 ? 28.29429  22.00094  51.47564  1.000 71.53798  ? 139 ILE   B N     1 
ATOM   2493 C  CA    . ILE   B 1 140 ? 27.85764  22.81154  50.34528  1.000 70.50299  ? 139 ILE   B CA    1 
ATOM   2494 C  C     . ILE   B 1 140 ? 27.31541  24.13365  50.85363  1.000 66.61741  ? 139 ILE   B C     1 
ATOM   2495 O  O     . ILE   B 1 140 ? 26.90399  24.25257  52.02282  1.000 66.60683  ? 139 ILE   B O     1 
ATOM   2496 C  CB    . ILE   B 1 140 ? 26.77611  22.09773  49.50091  1.000 63.81552  ? 139 ILE   B CB    1 
ATOM   2497 C  CG1   . ILE   B 1 140 ? 25.48704  21.94178  50.31745  1.000 63.28778  ? 139 ILE   B CG1   1 
ATOM   2498 C  CG2   . ILE   B 1 140 ? 27.28260  20.75907  48.97120  1.000 63.07483  ? 139 ILE   B CG2   1 
ATOM   2499 C  CD1   . ILE   B 1 140 ? 24.35534  21.28070  49.57343  1.000 63.29911  ? 139 ILE   B CD1   1 
ATOM   2500 N  N     . PRO   B 1 141 ? 27.29464  25.15756  50.00655  1.000 65.32900  ? 140 PRO   B N     1 
ATOM   2501 C  CA    . PRO   B 1 141 ? 26.70670  26.44360  50.39450  1.000 63.83953  ? 140 PRO   B CA    1 
ATOM   2502 C  C     . PRO   B 1 141 ? 25.20344  26.34241  50.60923  1.000 60.11658  ? 140 PRO   B C     1 
ATOM   2503 O  O     . PRO   B 1 141 ? 24.54510  25.37576  50.22529  1.000 59.29586  ? 140 PRO   B O     1 
ATOM   2504 C  CB    . PRO   B 1 141 ? 27.03156  27.35813  49.20904  1.000 60.62773  ? 140 PRO   B CB    1 
ATOM   2505 C  CG    . PRO   B 1 141 ? 28.20302  26.71151  48.53669  1.000 61.84532  ? 140 PRO   B CG    1 
ATOM   2506 C  CD    . PRO   B 1 141 ? 28.00849  25.24201  48.71618  1.000 62.51819  ? 140 PRO   B CD    1 
ATOM   2507 N  N     . PHE   B 1 142 ? 24.66350  27.38116  51.24202  1.000 62.40896  ? 141 PHE   B N     1 
ATOM   2508 C  CA    . PHE   B 1 142 ? 23.22757  27.55977  51.40056  1.000 62.64057  ? 141 PHE   B CA    1 
ATOM   2509 C  C     . PHE   B 1 142 ? 22.89789  29.01027  51.09709  1.000 62.75111  ? 141 PHE   B C     1 
ATOM   2510 O  O     . PHE   B 1 142 ? 23.50742  29.91422  51.66907  1.000 64.88031  ? 141 PHE   B O     1 
ATOM   2511 C  CB    . PHE   B 1 142 ? 22.75063  27.20539  52.81386  1.000 70.18954  ? 141 PHE   B CB    1 
ATOM   2512 C  CG    . PHE   B 1 142 ? 21.40400  27.79748  53.16093  1.000 70.72135  ? 141 PHE   B CG    1 
ATOM   2513 C  CD1   . PHE   B 1 142 ? 20.25029  27.36994  52.51608  1.000 65.55494  ? 141 PHE   B CD1   1 
ATOM   2514 C  CD2   . PHE   B 1 142 ? 21.28925  28.77187  54.14003  1.000 77.71973  ? 141 PHE   B CD2   1 
ATOM   2515 C  CE1   . PHE   B 1 142 ? 19.01422  27.91265  52.83456  1.000 65.28157  ? 141 PHE   B CE1   1 
ATOM   2516 C  CE2   . PHE   B 1 142 ? 20.05341  29.31390  54.46486  1.000 75.84330  ? 141 PHE   B CE2   1 
ATOM   2517 C  CZ    . PHE   B 1 142 ? 18.91560  28.88322  53.80862  1.000 70.39597  ? 141 PHE   B CZ    1 
ATOM   2518 N  N     . ILE   B 1 143 ? 21.94255  29.23775  50.20269  1.000 60.92457  ? 142 ILE   B N     1 
ATOM   2519 C  CA    . ILE   B 1 143 ? 21.54838  30.57852  49.78294  1.000 61.80992  ? 142 ILE   B CA    1 
ATOM   2520 C  C     . ILE   B 1 143 ? 20.04383  30.72328  49.96907  1.000 57.71366  ? 142 ILE   B C     1 
ATOM   2521 O  O     . ILE   B 1 143 ? 19.27616  29.82285  49.61198  1.000 57.67207  ? 142 ILE   B O     1 
ATOM   2522 C  CB    . ILE   B 1 143 ? 21.93276  30.87142  48.31526  1.000 59.14040  ? 142 ILE   B CB    1 
ATOM   2523 C  CG1   . ILE   B 1 143 ? 23.43514  31.02284  48.14849  1.000 69.73648  ? 142 ILE   B CG1   1 
ATOM   2524 C  CG2   . ILE   B 1 143 ? 21.27768  32.14539  47.84978  1.000 59.46541  ? 142 ILE   B CG2   1 
ATOM   2525 C  CD1   . ILE   B 1 143 ? 24.19454  29.72512  48.07407  1.000 67.62520  ? 142 ILE   B CD1   1 
ATOM   2526 N  N     . GLU   B 1 144 ? 19.63029  31.84184  50.54920  1.000 60.89036  ? 143 GLU   B N     1 
ATOM   2527 C  CA    . GLU   B 1 144 ? 18.22765  32.21487  50.62586  1.000 64.17924  ? 143 GLU   B CA    1 
ATOM   2528 C  C     . GLU   B 1 144 ? 17.83809  32.98463  49.37639  1.000 62.95266  ? 143 GLU   B C     1 
ATOM   2529 O  O     . GLU   B 1 144 ? 18.60473  33.81769  48.88537  1.000 57.96106  ? 143 GLU   B O     1 
ATOM   2530 C  CB    . GLU   B 1 144 ? 17.96106  33.07370  51.86100  1.000 71.99406  ? 143 GLU   B CB    1 
ATOM   2531 C  CG    . GLU   B 1 144 ? 18.05256  32.31512  53.16486  1.000 75.94808  ? 143 GLU   B CG    1 
ATOM   2532 C  CD    . GLU   B 1 144 ? 17.85433  33.21648  54.35706  1.000 80.38952  ? 143 GLU   B CD    1 
ATOM   2533 O  OE1   . GLU   B 1 144 ? 18.03411  34.44800  54.20853  1.000 78.14292  ? 143 GLU   B OE1   1 
ATOM   2534 O  OE2   . GLU   B 1 144 ? 17.51967  32.69379  55.44005  1.000 85.08933  ? 143 GLU   B OE2   1 
ATOM   2535 N  N     . THR   B 1 145 ? 16.64328  32.70580  48.86338  1.000 58.33666  ? 144 THR   B N     1 
ATOM   2536 C  CA    . THR   B 1 145 ? 16.16913  33.36372  47.65825  1.000 63.42748  ? 144 THR   B CA    1 
ATOM   2537 C  C     . THR   B 1 145 ? 14.69098  33.66850  47.79514  1.000 54.73173  ? 144 THR   B C     1 
ATOM   2538 O  O     . THR   B 1 145 ? 13.97651  33.06309  48.59634  1.000 56.27138  ? 144 THR   B O     1 
ATOM   2539 C  CB    . THR   B 1 145 ? 16.39001  32.51402  46.38748  1.000 51.54430  ? 144 THR   B CB    1 
ATOM   2540 O  OG1   . THR   B 1 145 ? 15.75894  31.23605  46.53557  1.000 51.68503  ? 144 THR   B OG1   1 
ATOM   2541 C  CG2   . THR   B 1 145 ? 17.87236  32.31909  46.09154  1.000 52.87826  ? 144 THR   B CG2   1 
ATOM   2542 N  N     . SER   B 1 146 ? 14.25768  34.63966  47.00082  1.000 55.85568  ? 145 SER   B N     1 
ATOM   2543 C  CA    . SER   B 1 146 ? 12.85001  34.86208  46.70067  1.000 54.37116  ? 145 SER   B CA    1 
ATOM   2544 C  C     . SER   B 1 146 ? 12.76348  35.12262  45.20630  1.000 55.41749  ? 145 SER   B C     1 
ATOM   2545 O  O     . SER   B 1 146 ? 13.22629  36.16512  44.73585  1.000 56.09077  ? 145 SER   B O     1 
ATOM   2546 C  CB    . SER   B 1 146 ? 12.27199  36.03718  47.48540  1.000 60.77036  ? 145 SER   B CB    1 
ATOM   2547 O  OG    . SER   B 1 146 ? 11.09537  36.52050  46.85906  1.000 59.03224  ? 145 SER   B OG    1 
ATOM   2548 N  N     . ALA   B 1 147 ? 12.19721  34.17192  44.45928  1.000 53.57365  ? 146 ALA   B N     1 
ATOM   2549 C  CA    . ALA   B 1 147 ? 11.95070  34.39853  43.04043  1.000 52.27598  ? 146 ALA   B CA    1 
ATOM   2550 C  C     . ALA   B 1 147 ? 10.95606  35.52178  42.81029  1.000 54.68509  ? 146 ALA   B C     1 
ATOM   2551 O  O     . ALA   B 1 147 ? 10.88557  36.05745  41.70013  1.000 53.82615  ? 146 ALA   B O     1 
ATOM   2552 C  CB    . ALA   B 1 147 ? 11.44378  33.11787  42.37939  1.000 48.05648  ? 146 ALA   B CB    1 
ATOM   2553 N  N     . LYS   B 1 148 ? 10.18592  35.88570  43.83451  1.000 56.99318  ? 147 LYS   B N     1 
ATOM   2554 C  CA    . LYS   B 1 148 ? 9.17579   36.92879  43.68411  1.000 60.24219  ? 147 LYS   B CA    1 
ATOM   2555 C  C     . LYS   B 1 148 ? 9.81725   38.31147  43.60647  1.000 58.41376  ? 147 LYS   B C     1 
ATOM   2556 O  O     . LYS   B 1 148 ? 9.51765   39.10049  42.70150  1.000 58.45291  ? 147 LYS   B O     1 
ATOM   2557 C  CB    . LYS   B 1 148 ? 8.18913   36.85316  44.85251  1.000 66.03969  ? 147 LYS   B CB    1 
ATOM   2558 C  CG    . LYS   B 1 148 ? 7.02579   37.83464  44.77953  1.000 70.12672  ? 147 LYS   B CG    1 
ATOM   2559 C  CD    . LYS   B 1 148 ? 6.30824   37.93362  46.12164  1.000 69.82820  ? 147 LYS   B CD    1 
ATOM   2560 C  CE    . LYS   B 1 148 ? 5.05480   38.78500  46.01830  1.000 80.41812  ? 147 LYS   B CE    1 
ATOM   2561 N  NZ    . LYS   B 1 148 ? 4.10619   38.23371  45.01340  1.000 81.62706  ? 147 LYS   B NZ    1 
ATOM   2562 N  N     . THR   B 1 149 ? 10.69118  38.62682  44.56259  1.000 63.90312  ? 148 THR   B N     1 
ATOM   2563 C  CA    . THR   B 1 149 ? 11.39171  39.90282  44.58890  1.000 63.59001  ? 148 THR   B CA    1 
ATOM   2564 C  C     . THR   B 1 149 ? 12.67343  39.87853  43.76992  1.000 62.19160  ? 148 THR   B C     1 
ATOM   2565 O  O     . THR   B 1 149 ? 13.27946  40.93591  43.56550  1.000 58.53481  ? 148 THR   B O     1 
ATOM   2566 C  CB    . THR   B 1 149 ? 11.72679  40.28894  46.03360  1.000 64.81978  ? 148 THR   B CB    1 
ATOM   2567 O  OG1   . THR   B 1 149 ? 12.73640  39.40471  46.54510  1.000 64.97779  ? 148 THR   B OG1   1 
ATOM   2568 C  CG2   . THR   B 1 149 ? 10.48491  40.20328  46.91539  1.000 68.39389  ? 148 THR   B CG2   1 
ATOM   2569 N  N     . ARG   B 1 150 ? 13.08523  38.69750  43.30997  1.000 57.58276  ? 149 ARG   B N     1 
ATOM   2570 C  CA    . ARG   B 1 150 ? 14.35431  38.40806  42.64952  1.000 54.33199  ? 149 ARG   B CA    1 
ATOM   2571 C  C     . ARG   B 1 150 ? 15.53219  38.45771  43.61078  1.000 57.16094  ? 149 ARG   B C     1 
ATOM   2572 O  O     . ARG   B 1 150 ? 16.68304  38.47882  43.16786  1.000 54.57259  ? 149 ARG   B O     1 
ATOM   2573 C  CB    . ARG   B 1 150 ? 14.61817  39.33260  41.45620  1.000 54.26255  ? 149 ARG   B CB    1 
ATOM   2574 C  CG    . ARG   B 1 150 ? 15.24037  38.62402  40.26162  1.000 53.97701  ? 149 ARG   B CG    1 
ATOM   2575 C  CD    . ARG   B 1 150 ? 15.67929  39.62295  39.19495  1.000 51.84095  ? 149 ARG   B CD    1 
ATOM   2576 N  NE    . ARG   B 1 150 ? 16.13370  38.96184  37.97679  1.000 49.45768  ? 149 ARG   B NE    1 
ATOM   2577 C  CZ    . ARG   B 1 150 ? 17.38187  38.56931  37.76042  1.000 50.51543  ? 149 ARG   B CZ    1 
ATOM   2578 N  NH1   . ARG   B 1 150 ? 18.33195  38.75245  38.66423  1.000 49.67209  ? 149 ARG   B NH1   1 
ATOM   2579 N  NH2   . ARG   B 1 150 ? 17.68376  37.97005  36.61141  1.000 51.15648  ? 149 ARG   B NH2   1 
ATOM   2580 N  N     . GLN   B 1 151 ? 15.28335  38.46980  44.91737  1.000 56.37569  ? 150 GLN   B N     1 
ATOM   2581 C  CA    . GLN   B 1 151 ? 16.38194  38.41902  45.86732  1.000 57.84701  ? 150 GLN   B CA    1 
ATOM   2582 C  C     . GLN   B 1 151 ? 17.12452  37.09801  45.73578  1.000 55.03864  ? 150 GLN   B C     1 
ATOM   2583 O  O     . GLN   B 1 151 ? 16.52428  36.02415  45.81758  1.000 61.79427  ? 150 GLN   B O     1 
ATOM   2584 C  CB    . GLN   B 1 151 ? 15.86463  38.58707  47.29379  1.000 65.45341  ? 150 GLN   B CB    1 
ATOM   2585 C  CG    . GLN   B 1 151 ? 16.94878  38.41304  48.33672  1.000 71.43254  ? 150 GLN   B CG    1 
ATOM   2586 C  CD    . GLN   B 1 151 ? 16.40792  37.91779  49.65921  1.000 83.46412  ? 150 GLN   B CD    1 
ATOM   2587 O  OE1   . GLN   B 1 151 ? 15.25354  38.17321  50.00649  1.000 81.97447  ? 150 GLN   B OE1   1 
ATOM   2588 N  NE2   . GLN   B 1 151 ? 17.23797  37.19229  50.40237  1.000 86.92243  ? 150 GLN   B NE2   1 
ATOM   2589 N  N     . GLY   B 1 152 ? 18.43157  37.17945  45.51228  1.000 54.59842  ? 151 GLY   B N     1 
ATOM   2590 C  CA    . GLY   B 1 152 ? 19.28691  36.01135  45.51432  1.000 56.62338  ? 151 GLY   B CA    1 
ATOM   2591 C  C     . GLY   B 1 152 ? 19.20495  35.11656  44.29493  1.000 50.35245  ? 151 GLY   B C     1 
ATOM   2592 O  O     . GLY   B 1 152 ? 19.91113  34.10167  44.25763  1.000 51.04444  ? 151 GLY   B O     1 
ATOM   2593 N  N     . VAL   B 1 153 ? 18.36329  35.44159  43.30769  1.000 49.85745  ? 152 VAL   B N     1 
ATOM   2594 C  CA    . VAL   B 1 153 ? 18.29368  34.63955  42.08279  1.000 51.09402  ? 152 VAL   B CA    1 
ATOM   2595 C  C     . VAL   B 1 153 ? 19.68314  34.49311  41.46534  1.000 51.49425  ? 152 VAL   B C     1 
ATOM   2596 O  O     . VAL   B 1 153 ? 20.23403  33.38797  41.38200  1.000 45.19614  ? 152 VAL   B O     1 
ATOM   2597 C  CB    . VAL   B 1 153 ? 17.29253  35.25347  41.08656  1.000 51.46120  ? 152 VAL   B CB    1 
ATOM   2598 C  CG1   . VAL   B 1 153 ? 17.29773  34.48319  39.76583  1.000 43.62797  ? 152 VAL   B CG1   1 
ATOM   2599 C  CG2   . VAL   B 1 153 ? 15.89383  35.25619  41.66905  1.000 48.19077  ? 152 VAL   B CG2   1 
ATOM   2600 N  N     . ASP   B 1 154 ? 20.28811  35.61513  41.05651  1.000 53.47920  ? 153 ASP   B N     1 
ATOM   2601 C  CA    . ASP   B 1 154 ? 21.62441  35.54996  40.46991  1.000 49.50013  ? 153 ASP   B CA    1 
ATOM   2602 C  C     . ASP   B 1 154 ? 22.62013  34.93545  41.44112  1.000 49.00057  ? 153 ASP   B C     1 
ATOM   2603 O  O     . ASP   B 1 154 ? 23.50316  34.17225  41.03777  1.000 46.90238  ? 153 ASP   B O     1 
ATOM   2604 C  CB    . ASP   B 1 154 ? 22.09171  36.94231  40.03719  1.000 53.42542  ? 153 ASP   B CB    1 
ATOM   2605 C  CG    . ASP   B 1 154 ? 21.19808  37.55953  38.96844  1.000 54.53352  ? 153 ASP   B CG    1 
ATOM   2606 O  OD1   . ASP   B 1 154 ? 20.46328  36.81146  38.28962  1.000 58.10649  ? 153 ASP   B OD1   1 
ATOM   2607 O  OD2   . ASP   B 1 154 ? 21.23495  38.79805  38.79822  1.000 60.55520  ? 153 ASP   B OD2   1 
ATOM   2608 N  N     . ASP   B 1 155 ? 22.47810  35.23990  42.73297  1.000 55.63222  ? 154 ASP   B N     1 
ATOM   2609 C  CA    . ASP   B 1 155 ? 23.40828  34.71786  43.72597  1.000 50.26630  ? 154 ASP   B CA    1 
ATOM   2610 C  C     . ASP   B 1 155 ? 23.34099  33.19621  43.79925  1.000 46.82288  ? 154 ASP   B C     1 
ATOM   2611 O  O     . ASP   B 1 155 ? 24.37042  32.52579  43.94434  1.000 46.13859  ? 154 ASP   B O     1 
ATOM   2612 C  CB    . ASP   B 1 155 ? 23.10238  35.34631  45.08778  1.000 58.32845  ? 154 ASP   B CB    1 
ATOM   2613 C  CG    . ASP   B 1 155 ? 24.11907  34.97740  46.14597  1.000 57.72945  ? 154 ASP   B CG    1 
ATOM   2614 O  OD1   . ASP   B 1 155 ? 25.22263  34.51941  45.78831  1.000 62.64320  ? 154 ASP   B OD1   1 
ATOM   2615 O  OD2   . ASP   B 1 155 ? 23.80962  35.14081  47.34576  1.000 67.24493  ? 154 ASP   B OD2   1 
ATOM   2616 N  N     . ALA   B 1 156 ? 22.13455  32.63493  43.69269  1.000 48.55715  ? 155 ALA   B N     1 
ATOM   2617 C  CA    . ALA   B 1 156 ? 21.97148  31.18581  43.77279  1.000 45.66827  ? 155 ALA   B CA    1 
ATOM   2618 C  C     . ALA   B 1 156 ? 22.64699  30.48816  42.59863  1.000 40.28526  ? 155 ALA   B C     1 
ATOM   2619 O  O     . ALA   B 1 156 ? 23.45002  29.56635  42.78453  1.000 38.71928  ? 155 ALA   B O     1 
ATOM   2620 C  CB    . ALA   B 1 156 ? 20.48451  30.83326  43.82346  1.000 40.09313  ? 155 ALA   B CB    1 
ATOM   2621 N  N     . PHE   B 1 157 ? 22.33192  30.91570  41.37345  1.000 48.09466  ? 156 PHE   B N     1 
ATOM   2622 C  CA    . PHE   B 1 157 ? 22.93658  30.28124  40.20707  1.000 39.73156  ? 156 PHE   B CA    1 
ATOM   2623 C  C     . PHE   B 1 157 ? 24.44201  30.52312  40.16083  1.000 40.54839  ? 156 PHE   B C     1 
ATOM   2624 O  O     . PHE   B 1 157 ? 25.21607  29.58379  39.94145  1.000 42.72115  ? 156 PHE   B O     1 
ATOM   2625 C  CB    . PHE   B 1 157 ? 22.24581  30.77065  38.92757  1.000 36.96303  ? 156 PHE   B CB    1 
ATOM   2626 C  CG    . PHE   B 1 157 ? 20.86625  30.18585  38.72258  1.000 41.55368  ? 156 PHE   B CG    1 
ATOM   2627 C  CD1   . PHE   B 1 157 ? 20.70785  28.93532  38.13846  1.000 40.15169  ? 156 PHE   B CD1   1 
ATOM   2628 C  CD2   . PHE   B 1 157 ? 19.73029  30.87620  39.12065  1.000 38.53571  ? 156 PHE   B CD2   1 
ATOM   2629 C  CE1   . PHE   B 1 157 ? 19.43698  28.38459  37.96156  1.000 35.03922  ? 156 PHE   B CE1   1 
ATOM   2630 C  CE2   . PHE   B 1 157 ? 18.46129  30.33208  38.94649  1.000 39.28836  ? 156 PHE   B CE2   1 
ATOM   2631 C  CZ    . PHE   B 1 157 ? 18.31658  29.07911  38.35901  1.000 39.38850  ? 156 PHE   B CZ    1 
ATOM   2632 N  N     . TYR   B 1 158 ? 24.88603  31.76270  40.40705  1.000 44.81580  ? 157 TYR   B N     1 
ATOM   2633 C  CA    . TYR   B 1 158 ? 26.31895  32.04985  40.34370  1.000 42.29480  ? 157 TYR   B CA    1 
ATOM   2634 C  C     . TYR   B 1 158 ? 27.09650  31.24689  41.38158  1.000 40.48265  ? 157 TYR   B C     1 
ATOM   2635 O  O     . TYR   B 1 158 ? 28.21583  30.79345  41.11200  1.000 40.69327  ? 157 TYR   B O     1 
ATOM   2636 C  CB    . TYR   B 1 158 ? 26.58452  33.54733  40.52486  1.000 45.03063  ? 157 TYR   B CB    1 
ATOM   2637 C  CG    . TYR   B 1 158 ? 26.12952  34.42371  39.37507  1.000 51.27915  ? 157 TYR   B CG    1 
ATOM   2638 C  CD1   . TYR   B 1 158 ? 25.36276  33.90643  38.33570  1.000 46.15216  ? 157 TYR   B CD1   1 
ATOM   2639 C  CD2   . TYR   B 1 158 ? 26.47915  35.77045  39.32120  1.000 49.10649  ? 157 TYR   B CD2   1 
ATOM   2640 C  CE1   . TYR   B 1 158 ? 24.94508  34.70204  37.28910  1.000 42.95216  ? 157 TYR   B CE1   1 
ATOM   2641 C  CE2   . TYR   B 1 158 ? 26.06547  36.57685  38.27083  1.000 45.77271  ? 157 TYR   B CE2   1 
ATOM   2642 C  CZ    . TYR   B 1 158 ? 25.29939  36.03336  37.25526  1.000 47.13549  ? 157 TYR   B CZ    1 
ATOM   2643 O  OH    . TYR   B 1 158 ? 24.87994  36.81956  36.19928  1.000 51.44359  ? 157 TYR   B OH    1 
ATOM   2644 N  N     . THR   B 1 159 ? 26.51676  31.05070  42.57164  1.000 49.22644  ? 158 THR   B N     1 
ATOM   2645 C  CA    . THR   B 1 159 ? 27.19652  30.26792  43.60202  1.000 47.33305  ? 158 THR   B CA    1 
ATOM   2646 C  C     . THR   B 1 159 ? 27.41545  28.83099  43.15172  1.000 43.53565  ? 158 THR   B C     1 
ATOM   2647 O  O     . THR   B 1 159 ? 28.47958  28.24916  43.39562  1.000 44.69998  ? 158 THR   B O     1 
ATOM   2648 C  CB    . THR   B 1 159 ? 26.39922  30.29282  44.90397  1.000 51.79538  ? 158 THR   B CB    1 
ATOM   2649 O  OG1   . THR   B 1 159 ? 26.18058  31.64971  45.30612  1.000 55.81220  ? 158 THR   B OG1   1 
ATOM   2650 C  CG2   . THR   B 1 159 ? 27.16103  29.56121  45.99464  1.000 50.13117  ? 158 THR   B CG2   1 
ATOM   2651 N  N     . LEU   B 1 160 ? 26.41775  28.24168  42.48842  1.000 46.30995  ? 159 LEU   B N     1 
ATOM   2652 C  CA    . LEU   B 1 160 ? 26.57784  26.88403  41.98368  1.000 43.97196  ? 159 LEU   B CA    1 
ATOM   2653 C  C     . LEU   B 1 160 ? 27.74785  26.79026  41.01606  1.000 38.71859  ? 159 LEU   B C     1 
ATOM   2654 O  O     . LEU   B 1 160 ? 28.51370  25.82025  41.04710  1.000 42.99035  ? 159 LEU   B O     1 
ATOM   2655 C  CB    . LEU   B 1 160 ? 25.28347  26.41963  41.31473  1.000 40.12881  ? 159 LEU   B CB    1 
ATOM   2656 C  CG    . LEU   B 1 160 ? 25.32349  24.96915  40.84711  1.000 35.56722  ? 159 LEU   B CG    1 
ATOM   2657 C  CD1   . LEU   B 1 160 ? 25.68566  24.03809  42.00244  1.000 41.13784  ? 159 LEU   B CD1   1 
ATOM   2658 C  CD2   . LEU   B 1 160 ? 23.97480  24.58661  40.23819  1.000 37.72390  ? 159 LEU   B CD2   1 
ATOM   2659 N  N     . VAL   B 1 161 ? 27.89719  27.78700  40.14059  1.000 46.44719  ? 160 VAL   B N     1 
ATOM   2660 C  CA    . VAL   B 1 161 ? 29.03385  27.80938  39.22376  1.000 44.06359  ? 160 VAL   B CA    1 
ATOM   2661 C  C     . VAL   B 1 161 ? 30.34810  27.81113  39.99820  1.000 42.76450  ? 160 VAL   B C     1 
ATOM   2662 O  O     . VAL   B 1 161 ? 31.28040  27.06717  39.66636  1.000 46.76783  ? 160 VAL   B O     1 
ATOM   2663 C  CB    . VAL   B 1 161 ? 28.92173  29.01609  38.27164  1.000 43.74829  ? 160 VAL   B CB    1 
ATOM   2664 C  CG1   . VAL   B 1 161 ? 30.20098  29.19052  37.46756  1.000 41.94215  ? 160 VAL   B CG1   1 
ATOM   2665 C  CG2   . VAL   B 1 161 ? 27.71247  28.84428  37.33659  1.000 33.03020  ? 160 VAL   B CG2   1 
ATOM   2666 N  N     . ARG   B 1 162 ? 30.43926  28.62403  41.05566  1.000 49.38563  ? 161 ARG   B N     1 
ATOM   2667 C  CA    . ARG   B 1 162 ? 31.67849  28.66464  41.83218  1.000 51.31248  ? 161 ARG   B CA    1 
ATOM   2668 C  C     . ARG   B 1 162 ? 31.96933  27.32301  42.49576  1.000 53.07707  ? 161 ARG   B C     1 
ATOM   2669 O  O     . ARG   B 1 162 ? 33.13780  26.96688  42.68152  1.000 55.53603  ? 161 ARG   B O     1 
ATOM   2670 C  CB    . ARG   B 1 162 ? 31.62106  29.78788  42.86713  1.000 50.13644  ? 161 ARG   B CB    1 
ATOM   2671 C  CG    . ARG   B 1 162 ? 31.45290  31.17211  42.24163  1.000 53.64385  ? 161 ARG   B CG    1 
ATOM   2672 C  CD    . ARG   B 1 162 ? 31.55042  32.29535  43.26955  1.000 52.57032  ? 161 ARG   B CD    1 
ATOM   2673 N  NE    . ARG   B 1 162 ? 31.27293  33.60521  42.68812  1.000 50.57860  ? 161 ARG   B NE    1 
ATOM   2674 C  CZ    . ARG   B 1 162 ? 30.15464  34.29147  42.88274  1.000 49.73376  ? 161 ARG   B CZ    1 
ATOM   2675 N  NH1   . ARG   B 1 162 ? 29.18784  33.83141  43.65670  1.000 50.88772  ? 161 ARG   B NH1   1 
ATOM   2676 N  NH2   . ARG   B 1 162 ? 30.00226  35.47110  42.28696  1.000 49.41003  ? 161 ARG   B NH2   1 
ATOM   2677 N  N     . GLU   B 1 163 ? 30.92893  26.55155  42.82158  1.000 53.39355  ? 162 GLU   B N     1 
ATOM   2678 C  CA    . GLU   B 1 163 ? 31.14207  25.21648  43.37046  1.000 49.36182  ? 162 GLU   B CA    1 
ATOM   2679 C  C     . GLU   B 1 163 ? 31.67532  24.26091  42.31406  1.000 55.67199  ? 162 GLU   B C     1 
ATOM   2680 O  O     . GLU   B 1 163 ? 32.55696  23.44105  42.60030  1.000 53.02287  ? 162 GLU   B O     1 
ATOM   2681 C  CB    . GLU   B 1 163 ? 29.84116  24.67918  43.96520  1.000 51.88208  ? 162 GLU   B CB    1 
ATOM   2682 C  CG    . GLU   B 1 163 ? 29.44931  25.33449  45.26332  1.000 55.36359  ? 162 GLU   B CG    1 
ATOM   2683 C  CD    . GLU   B 1 163 ? 30.48244  25.09504  46.34849  1.000 63.08254  ? 162 GLU   B CD    1 
ATOM   2684 O  OE1   . GLU   B 1 163 ? 30.85791  23.92173  46.56610  1.000 54.87648  ? 162 GLU   B OE1   1 
ATOM   2685 O  OE2   . GLU   B 1 163 ? 30.93375  26.08375  46.96469  1.000 64.65634  ? 162 GLU   B OE2   1 
ATOM   2686 N  N     . ILE   B 1 164 ? 31.13673  24.32988  41.09125  1.000 48.33399  ? 163 ILE   B N     1 
ATOM   2687 C  CA    . ILE   B 1 164 ? 31.66475  23.49699  40.01591  1.000 52.83557  ? 163 ILE   B CA    1 
ATOM   2688 C  C     . ILE   B 1 164 ? 33.12458  23.84461  39.75509  1.000 54.24431  ? 163 ILE   B C     1 
ATOM   2689 O  O     . ILE   B 1 164 ? 33.95790  22.96142  39.51939  1.000 57.93211  ? 163 ILE   B O     1 
ATOM   2690 C  CB    . ILE   B 1 164 ? 30.80206  23.64428  38.74468  1.000 44.24225  ? 163 ILE   B CB    1 
ATOM   2691 C  CG1   . ILE   B 1 164 ? 29.34922  23.26091  39.03521  1.000 47.79633  ? 163 ILE   B CG1   1 
ATOM   2692 C  CG2   . ILE   B 1 164 ? 31.34288  22.77271  37.62909  1.000 50.36615  ? 163 ILE   B CG2   1 
ATOM   2693 C  CD1   . ILE   B 1 164 ? 28.42219  23.34677  37.80955  1.000 40.98248  ? 163 ILE   B CD1   1 
ATOM   2694 N  N     . ARG   B 1 165 ? 33.45817  25.13710  39.81624  1.000 54.84367  ? 164 ARG   B N     1 
ATOM   2695 C  CA    . ARG   B 1 165 ? 34.83418  25.57075  39.59420  1.000 62.57712  ? 164 ARG   B CA    1 
ATOM   2696 C  C     . ARG   B 1 165 ? 35.77292  24.98431  40.64220  1.000 63.19401  ? 164 ARG   B C     1 
ATOM   2697 O  O     . ARG   B 1 165 ? 36.86162  24.50128  40.30950  1.000 69.87628  ? 164 ARG   B O     1 
ATOM   2698 C  CB    . ARG   B 1 165 ? 34.90198  27.10311  39.58676  1.000 56.48052  ? 164 ARG   B CB    1 
ATOM   2699 C  CG    . ARG   B 1 165 ? 34.37180  27.73630  38.29215  1.000 55.63313  ? 164 ARG   B CG    1 
ATOM   2700 C  CD    . ARG   B 1 165 ? 34.19358  29.25756  38.36330  1.000 46.80349  ? 164 ARG   B CD    1 
ATOM   2701 N  NE    . ARG   B 1 165 ? 33.82835  29.78906  37.05251  1.000 50.49260  ? 164 ARG   B NE    1 
ATOM   2702 C  CZ    . ARG   B 1 165 ? 33.54689  31.05912  36.78306  1.000 48.53361  ? 164 ARG   B CZ    1 
ATOM   2703 N  NH1   . ARG   B 1 165 ? 33.56593  31.99229  37.72145  1.000 48.89457  ? 164 ARG   B NH1   1 
ATOM   2704 N  NH2   . ARG   B 1 165 ? 33.23482  31.40206  35.53628  1.000 45.28574  ? 164 ARG   B NH2   1 
ATOM   2705 N  N     . LYS   B 1 166 ? 35.35483  24.99289  41.91062  1.000 69.48169  ? 165 LYS   B N     1 
ATOM   2706 C  CA    . LYS   B 1 166 ? 36.18720  24.43620  42.97320  1.000 72.62538  ? 165 LYS   B CA    1 
ATOM   2707 C  C     . LYS   B 1 166 ? 36.36611  22.93097  42.81521  1.000 76.55679  ? 165 LYS   B C     1 
ATOM   2708 O  O     . LYS   B 1 166 ? 37.45452  22.39884  43.05846  1.000 85.80224  ? 165 LYS   B O     1 
ATOM   2709 C  CB    . LYS   B 1 166 ? 35.57743  24.75946  44.33373  1.000 72.76420  ? 165 LYS   B CB    1 
ATOM   2710 C  CG    . LYS   B 1 166 ? 35.51605  26.24045  44.64587  1.000 75.09725  ? 165 LYS   B CG    1 
ATOM   2711 C  CD    . LYS   B 1 166 ? 34.44199  26.53298  45.68281  1.000 73.12720  ? 165 LYS   B CD    1 
ATOM   2712 C  CE    . LYS   B 1 166 ? 34.62607  25.68260  46.92907  1.000 79.16150  ? 165 LYS   B CE    1 
ATOM   2713 N  NZ    . LYS   B 1 166 ? 33.53108  25.89470  47.91793  1.000 82.33601  ? 165 LYS   B NZ    1 
ATOM   2714 N  N     . HIS   B 1 167 ? 35.30897  22.22406  42.41753  1.000 71.59188  ? 166 HIS   B N     1 
ATOM   2715 C  CA    . HIS   B 1 167 ? 35.42215  20.78058  42.25236  1.000 77.06369  ? 166 HIS   B CA    1 
ATOM   2716 C  C     . HIS   B 1 167 ? 36.38951  20.41505  41.13204  1.000 83.29011  ? 166 HIS   B C     1 
ATOM   2717 O  O     . HIS   B 1 167 ? 36.95654  19.31592  41.13566  1.000 86.57414  ? 166 HIS   B O     1 
ATOM   2718 C  CB    . HIS   B 1 167 ? 34.04320  20.17660  41.98830  1.000 75.44219  ? 166 HIS   B CB    1 
ATOM   2719 C  CG    . HIS   B 1 167 ? 34.06648  18.69668  41.76845  1.000 82.10857  ? 166 HIS   B CG    1 
ATOM   2720 N  ND1   . HIS   B 1 167 ? 34.41465  18.12711  40.56215  1.000 86.25116  ? 166 HIS   B ND1   1 
ATOM   2721 C  CD2   . HIS   B 1 167 ? 33.78714  17.66794  42.60201  1.000 86.68316  ? 166 HIS   B CD2   1 
ATOM   2722 C  CE1   . HIS   B 1 167 ? 34.34891  16.81146  40.66182  1.000 89.76214  ? 166 HIS   B CE1   1 
ATOM   2723 N  NE2   . HIS   B 1 167 ? 33.97098  16.50668  41.89004  1.000 89.84214  ? 166 HIS   B NE2   1 
ATOM   2724 N  N     . LYS   B 1 168 ? 36.60223  21.32059  40.17365  1.000 82.12477  ? 167 LYS   B N     1 
ATOM   2725 C  CA    . LYS   B 1 168 ? 37.43346  20.99892  39.01812  1.000 83.59699  ? 167 LYS   B CA    1 
ATOM   2726 C  C     . LYS   B 1 168 ? 38.92398  21.11965  39.31536  1.000 91.77368  ? 167 LYS   B C     1 
ATOM   2727 O  O     . LYS   B 1 168 ? 39.72337  20.37068  38.74253  1.000 92.74488  ? 167 LYS   B O     1 
ATOM   2728 C  CB    . LYS   B 1 168 ? 37.05185  21.88998  37.83540  1.000 76.90407  ? 167 LYS   B CB    1 
ATOM   2729 C  CG    . LYS   B 1 168 ? 35.67933  21.56996  37.26403  1.000 73.75866  ? 167 LYS   B CG    1 
ATOM   2730 C  CD    . LYS   B 1 168 ? 35.21691  22.61390  36.25405  1.000 72.85687  ? 167 LYS   B CD    1 
ATOM   2731 C  CE    . LYS   B 1 168 ? 35.41188  22.15025  34.81415  1.000 65.29706  ? 167 LYS   B CE    1 
ATOM   2732 N  NZ    . LYS   B 1 168 ? 34.80548  23.12072  33.86013  1.000 52.83728  ? 167 LYS   B NZ    1 
ATOM   2733 N  N     . GLU   B 1 169 ? 39.32429  22.04529  40.19027  1.000 94.12632  ? 168 GLU   B N     1 
ATOM   2734 C  CA    . GLU   B 1 169 ? 40.72638  22.10898  40.58874  1.000 101.28883 ? 168 GLU   B CA    1 
ATOM   2735 C  C     . GLU   B 1 169 ? 41.11088  20.99004  41.54867  1.000 107.19583 ? 168 GLU   B C     1 
ATOM   2736 O  O     . GLU   B 1 169 ? 42.30180  20.82559  41.83691  1.000 107.30626 ? 168 GLU   B O     1 
ATOM   2737 C  CB    . GLU   B 1 169 ? 41.04712  23.47542  41.21265  1.000 104.20459 ? 168 GLU   B CB    1 
ATOM   2738 C  CG    . GLU   B 1 169 ? 40.01017  24.01139  42.20126  1.000 101.25148 ? 168 GLU   B CG    1 
ATOM   2739 C  CD    . GLU   B 1 169 ? 40.22341  23.53106  43.63276  1.000 105.34441 ? 168 GLU   B CD    1 
ATOM   2740 O  OE1   . GLU   B 1 169 ? 41.16134  22.74560  43.87903  1.000 110.65834 ? 168 GLU   B OE1   1 
ATOM   2741 O  OE2   . GLU   B 1 169 ? 39.44869  23.94825  44.51913  1.000 102.70323 ? 168 GLU   B OE2   1 
ATOM   2742 N  N     . LYS   B 1 170 ? 40.14269  20.22018  42.03623  1.000 102.05321 ? 169 LYS   B N     1 
ATOM   2743 C  CA    . LYS   B 1 170 ? 40.40050  19.15048  42.99068  1.000 105.19327 ? 169 LYS   B CA    1 
ATOM   2744 C  C     . LYS   B 1 170 ? 41.14556  17.98954  42.33962  1.000 106.61687 ? 169 LYS   B C     1 
ATOM   2745 O  O     . LYS   B 1 170 ? 42.37504  17.98718  42.26851  1.000 101.69186 ? 169 LYS   B O     1 
ATOM   2746 C  CB    . LYS   B 1 170 ? 39.08350  18.66032  43.59410  1.000 105.19412 ? 169 LYS   B CB    1 
ATOM   2747 C  CG    . LYS   B 1 170 ? 39.23973  17.78465  44.82206  1.000 111.70744 ? 169 LYS   B CG    1 
ATOM   2748 C  CD    . LYS   B 1 170 ? 37.88689  17.30196  45.31263  1.000 110.42193 ? 169 LYS   B CD    1 
ATOM   2749 C  CE    . LYS   B 1 170 ? 36.90605  18.45761  45.43817  1.000 104.77814 ? 169 LYS   B CE    1 
ATOM   2750 N  NZ    . LYS   B 1 170 ? 37.41460  19.52792  46.33985  1.000 107.01016 ? 169 LYS   B NZ    1 
ATOM   2751 N  N     . VAL   C 2 3   ? -28.76106 7.15803   27.88612  1.000 56.35938  ? 2   VAL   C N     1 
ATOM   2752 C  CA    . VAL   C 2 3   ? -27.80668 6.66793   26.89734  1.000 57.03604  ? 2   VAL   C CA    1 
ATOM   2753 C  C     . VAL   C 2 3   ? -26.63468 7.63535   26.77615  1.000 53.20736  ? 2   VAL   C C     1 
ATOM   2754 O  O     . VAL   C 2 3   ? -26.80372 8.85153   26.88564  1.000 53.80673  ? 2   VAL   C O     1 
ATOM   2755 C  CB    . VAL   C 2 3   ? -28.47554 6.44092   25.52966  1.000 56.93725  ? 2   VAL   C CB    1 
ATOM   2756 C  CG1   . VAL   C 2 3   ? -29.70563 5.55477   25.68517  1.000 60.11668  ? 2   VAL   C CG1   1 
ATOM   2757 C  CG2   . VAL   C 2 3   ? -28.84043 7.76333   24.87558  1.000 60.19332  ? 2   VAL   C CG2   1 
ATOM   2758 N  N     . ASN   C 2 4   ? -25.44870 7.08730   26.53894  1.000 50.21836  ? 3   ASN   C N     1 
ATOM   2759 C  CA    . ASN   C 2 4   ? -24.22625 7.88616   26.61355  1.000 45.12648  ? 3   ASN   C CA    1 
ATOM   2760 C  C     . ASN   C 2 4   ? -24.10977 8.83002   25.42055  1.000 47.44164  ? 3   ASN   C C     1 
ATOM   2761 O  O     . ASN   C 2 4   ? -24.22060 8.38872   24.26969  1.000 49.36529  ? 3   ASN   C O     1 
ATOM   2762 C  CB    . ASN   C 2 4   ? -23.00757 6.97352   26.68642  1.000 41.81563  ? 3   ASN   C CB    1 
ATOM   2763 C  CG    . ASN   C 2 4   ? -22.85843 6.33380   28.03324  1.000 41.31881  ? 3   ASN   C CG    1 
ATOM   2764 O  OD1   . ASN   C 2 4   ? -23.41762 6.81521   29.01598  1.000 43.88338  ? 3   ASN   C OD1   1 
ATOM   2765 N  ND2   . ASN   C 2 4   ? -22.09819 5.24930   28.09926  1.000 41.88945  ? 3   ASN   C ND2   1 
ATOM   2766 N  N     . PRO   C 2 5   ? -23.86085 10.11635  25.64760  1.000 43.71198  ? 4   PRO   C N     1 
ATOM   2767 C  CA    . PRO   C 2 5   ? -23.74635 11.05473  24.53072  1.000 40.91954  ? 4   PRO   C CA    1 
ATOM   2768 C  C     . PRO   C 2 5   ? -22.44585 10.85573  23.76883  1.000 42.03421  ? 4   PRO   C C     1 
ATOM   2769 O  O     . PRO   C 2 5   ? -21.49580 10.23320  24.24757  1.000 39.88521  ? 4   PRO   C O     1 
ATOM   2770 C  CB    . PRO   C 2 5   ? -23.78021 12.42286  25.21653  1.000 42.05652  ? 4   PRO   C CB    1 
ATOM   2771 C  CG    . PRO   C 2 5   ? -23.21328 12.17178  26.55499  1.000 44.13835  ? 4   PRO   C CG    1 
ATOM   2772 C  CD    . PRO   C 2 5   ? -23.56742 10.75564  26.94138  1.000 40.48791  ? 4   PRO   C CD    1 
ATOM   2773 N  N     . THR   C 2 6   ? -22.42462 11.40443  22.55913  1.000 45.32757  ? 5   THR   C N     1 
ATOM   2774 C  CA    . THR   C 2 6   ? -21.25853 11.39395  21.68596  1.000 41.01954  ? 5   THR   C CA    1 
ATOM   2775 C  C     . THR   C 2 6   ? -20.95993 12.82647  21.26759  1.000 44.04113  ? 5   THR   C C     1 
ATOM   2776 O  O     . THR   C 2 6   ? -21.86126 13.54470  20.82480  1.000 41.51444  ? 5   THR   C O     1 
ATOM   2777 C  CB    . THR   C 2 6   ? -21.49874 10.51227  20.45561  1.000 42.10653  ? 5   THR   C CB    1 
ATOM   2778 O  OG1   . THR   C 2 6   ? -21.52454 9.13609   20.84909  1.000 47.38926  ? 5   THR   C OG1   1 
ATOM   2779 C  CG2   . THR   C 2 6   ? -20.39829 10.71472  19.41811  1.000 47.41607  ? 5   THR   C CG2   1 
ATOM   2780 N  N     . VAL   C 2 7   ? -19.70274 13.24996  21.42199  1.000 35.35572  ? 6   VAL   C N     1 
ATOM   2781 C  CA    . VAL   C 2 7   ? -19.27903 14.57796  21.00396  1.000 33.87673  ? 6   VAL   C CA    1 
ATOM   2782 C  C     . VAL   C 2 7   ? -18.14696 14.42021  19.99347  1.000 35.06758  ? 6   VAL   C C     1 
ATOM   2783 O  O     . VAL   C 2 7   ? -17.59321 13.33461  19.80629  1.000 30.92624  ? 6   VAL   C O     1 
ATOM   2784 C  CB    . VAL   C 2 7   ? -18.84430 15.46848  22.18991  1.000 38.88160  ? 6   VAL   C CB    1 
ATOM   2785 C  CG1   . VAL   C 2 7   ? -20.02805 15.75246  23.10758  1.000 41.87385  ? 6   VAL   C CG1   1 
ATOM   2786 C  CG2   . VAL   C 2 7   ? -17.72007 14.81207  22.97013  1.000 32.61328  ? 6   VAL   C CG2   1 
ATOM   2787 N  N     . PHE   C 2 8   ? -17.82486 15.51817  19.31962  1.000 36.20560  ? 7   PHE   C N     1 
ATOM   2788 C  CA    . PHE   C 2 8   ? -16.82137 15.50041  18.26711  1.000 33.15170  ? 7   PHE   C CA    1 
ATOM   2789 C  C     . PHE   C 2 8   ? -15.91582 16.71783  18.38084  1.000 34.78226  ? 7   PHE   C C     1 
ATOM   2790 O  O     . PHE   C 2 8   ? -16.35021 17.79939  18.78290  1.000 34.64511  ? 7   PHE   C O     1 
ATOM   2791 C  CB    . PHE   C 2 8   ? -17.47274 15.46662  16.86257  1.000 38.89168  ? 7   PHE   C CB    1 
ATOM   2792 C  CG    . PHE   C 2 8   ? -18.10820 16.76754  16.45524  1.000 37.18225  ? 7   PHE   C CG    1 
ATOM   2793 C  CD1   . PHE   C 2 8   ? -19.43441 17.03226  16.77135  1.000 41.50903  ? 7   PHE   C CD1   1 
ATOM   2794 C  CD2   . PHE   C 2 8   ? -17.38453 17.72312  15.75039  1.000 38.49557  ? 7   PHE   C CD2   1 
ATOM   2795 C  CE1   . PHE   C 2 8   ? -20.02437 18.22875  16.39661  1.000 46.51778  ? 7   PHE   C CE1   1 
ATOM   2796 C  CE2   . PHE   C 2 8   ? -17.96302 18.92173  15.38206  1.000 43.15187  ? 7   PHE   C CE2   1 
ATOM   2797 C  CZ    . PHE   C 2 8   ? -19.28790 19.17769  15.70221  1.000 43.68772  ? 7   PHE   C CZ    1 
ATOM   2798 N  N     . PHE   C 2 9   ? -14.65035 16.52820  18.00743  1.000 35.83313  ? 8   PHE   C N     1 
ATOM   2799 C  CA    . PHE   C 2 9   ? -13.70920 17.61417  17.77847  1.000 33.73526  ? 8   PHE   C CA    1 
ATOM   2800 C  C     . PHE   C 2 9   ? -13.33170 17.61715  16.30983  1.000 30.37354  ? 8   PHE   C C     1 
ATOM   2801 O  O     . PHE   C 2 9   ? -13.01766 16.56148  15.75033  1.000 31.99204  ? 8   PHE   C O     1 
ATOM   2802 C  CB    . PHE   C 2 9   ? -12.41919 17.46610  18.58512  1.000 27.31239  ? 8   PHE   C CB    1 
ATOM   2803 C  CG    . PHE   C 2 9   ? -12.57250 17.69932  20.04812  1.000 35.21976  ? 8   PHE   C CG    1 
ATOM   2804 C  CD1   . PHE   C 2 9   ? -13.75750 18.18931  20.57576  1.000 31.19184  ? 8   PHE   C CD1   1 
ATOM   2805 C  CD2   . PHE   C 2 9   ? -11.50784 17.44825  20.89979  1.000 34.01842  ? 8   PHE   C CD2   1 
ATOM   2806 C  CE1   . PHE   C 2 9   ? -13.88233 18.41145  21.92755  1.000 30.17792  ? 8   PHE   C CE1   1 
ATOM   2807 C  CE2   . PHE   C 2 9   ? -11.62733 17.66246  22.25154  1.000 30.57229  ? 8   PHE   C CE2   1 
ATOM   2808 C  CZ    . PHE   C 2 9   ? -12.82637 18.14429  22.76817  1.000 34.43959  ? 8   PHE   C CZ    1 
ATOM   2809 N  N     . ASP   C 2 10  ? -13.34214 18.79263  15.69773  1.000 32.85012  ? 9   ASP   C N     1 
ATOM   2810 C  CA    . ASP   C 2 10  ? -12.74420 18.98150  14.37824  1.000 31.88951  ? 9   ASP   C CA    1 
ATOM   2811 C  C     . ASP   C 2 10  ? -11.37252 19.60790  14.59527  1.000 33.17388  ? 9   ASP   C C     1 
ATOM   2812 O  O     . ASP   C 2 10  ? -11.27193 20.75963  15.02675  1.000 36.93485  ? 9   ASP   C O     1 
ATOM   2813 C  CB    . ASP   C 2 10  ? -13.63663 19.83580  13.47696  1.000 33.15141  ? 9   ASP   C CB    1 
ATOM   2814 C  CG    . ASP   C 2 10  ? -14.78515 19.04035  12.88714  1.000 39.83587  ? 9   ASP   C CG    1 
ATOM   2815 O  OD1   . ASP   C 2 10  ? -14.57054 17.85445  12.55951  1.000 37.56425  ? 9   ASP   C OD1   1 
ATOM   2816 O  OD2   . ASP   C 2 10  ? -15.90642 19.58616  12.75540  1.000 42.30845  ? 9   ASP   C OD2   1 
ATOM   2817 N  N     . ILE   C 2 11  ? -10.31267 18.83201  14.32131  1.000 31.31909  ? 10  ILE   C N     1 
ATOM   2818 C  CA    . ILE   C 2 11  ? -8.94125  19.20779  14.65880  1.000 29.45269  ? 10  ILE   C CA    1 
ATOM   2819 C  C     . ILE   C 2 11  ? -8.30037  19.89319  13.46117  1.000 29.83137  ? 10  ILE   C C     1 
ATOM   2820 O  O     . ILE   C 2 11  ? -8.46639  19.45559  12.31717  1.000 33.02258  ? 10  ILE   C O     1 
ATOM   2821 C  CB    . ILE   C 2 11  ? -8.12649  17.97152  15.08065  1.000 30.83307  ? 10  ILE   C CB    1 
ATOM   2822 C  CG1   . ILE   C 2 11  ? -8.79144  17.27757  16.26968  1.000 28.29658  ? 10  ILE   C CG1   1 
ATOM   2823 C  CG2   . ILE   C 2 11  ? -6.69839  18.37010  15.43076  1.000 30.24874  ? 10  ILE   C CG2   1 
ATOM   2824 C  CD1   . ILE   C 2 11  ? -8.98704  18.20269  17.43810  1.000 29.28487  ? 10  ILE   C CD1   1 
ATOM   2825 N  N     . ALA   C 2 12  ? -7.55492  20.96542  13.71468  1.000 32.75318  ? 11  ALA   C N     1 
ATOM   2826 C  CA    . ALA   C 2 12  ? -6.85603  21.67320  12.64476  1.000 36.17537  ? 11  ALA   C CA    1 
ATOM   2827 C  C     . ALA   C 2 12  ? -5.39105  21.86963  13.01265  1.000 36.81762  ? 11  ALA   C C     1 
ATOM   2828 O  O     . ALA   C 2 12  ? -5.03928  21.99152  14.19133  1.000 32.68821  ? 11  ALA   C O     1 
ATOM   2829 C  CB    . ALA   C 2 12  ? -7.50126  23.03666  12.34959  1.000 34.13062  ? 11  ALA   C CB    1 
ATOM   2830 N  N     . VAL   C 2 13  ? -4.54084  21.91760  11.98777  1.000 30.98677  ? 12  VAL   C N     1 
ATOM   2831 C  CA    . VAL   C 2 13  ? -3.09899  22.08465  12.15262  1.000 32.93174  ? 12  VAL   C CA    1 
ATOM   2832 C  C     . VAL   C 2 13  ? -2.71534  23.38108  11.46379  1.000 39.55739  ? 12  VAL   C C     1 
ATOM   2833 O  O     . VAL   C 2 13  ? -2.78276  23.46915  10.23045  1.000 36.25486  ? 12  VAL   C O     1 
ATOM   2834 C  CB    . VAL   C 2 13  ? -2.30282  20.91279  11.56583  1.000 30.18141  ? 12  VAL   C CB    1 
ATOM   2835 C  CG1   . VAL   C 2 13  ? -0.80807  21.14643  11.75281  1.000 37.18120  ? 12  VAL   C CG1   1 
ATOM   2836 C  CG2   . VAL   C 2 13  ? -2.72760  19.60190  12.19083  1.000 40.70787  ? 12  VAL   C CG2   1 
ATOM   2837 N  N     . ASP   C 2 14  ? -2.30028  24.37865  12.25123  1.000 34.86619  ? 13  ASP   C N     1 
ATOM   2838 C  CA    . ASP   C 2 14  ? -1.98356  25.71203  11.73507  1.000 40.00028  ? 13  ASP   C CA    1 
ATOM   2839 C  C     . ASP   C 2 14  ? -3.12169  26.24564  10.86715  1.000 41.98835  ? 13  ASP   C C     1 
ATOM   2840 O  O     . ASP   C 2 14  ? -2.90058  26.86705  9.82802   1.000 43.25560  ? 13  ASP   C O     1 
ATOM   2841 C  CB    . ASP   C 2 14  ? -0.66403  25.71082  10.95142  1.000 40.59319  ? 13  ASP   C CB    1 
ATOM   2842 C  CG    . ASP   C 2 14  ? 0.56367   25.74642  11.85004  1.000 42.87812  ? 13  ASP   C CG    1 
ATOM   2843 O  OD1   . ASP   C 2 14  ? 0.44875   26.16329  13.02746  1.000 43.80709  ? 13  ASP   C OD1   1 
ATOM   2844 O  OD2   . ASP   C 2 14  ? 1.65475   25.38134  11.36509  1.000 42.25918  ? 13  ASP   C OD2   1 
ATOM   2845 N  N     . GLY   C 2 15  ? -4.35600  25.98585  11.29015  1.000 42.11722  ? 14  GLY   C N     1 
ATOM   2846 C  CA    . GLY   C 2 15  ? -5.52442  26.45555  10.58389  1.000 40.61144  ? 14  GLY   C CA    1 
ATOM   2847 C  C     . GLY   C 2 15  ? -6.04283  25.53432  9.50358   1.000 40.53230  ? 14  GLY   C C     1 
ATOM   2848 O  O     . GLY   C 2 15  ? -7.13263  25.78186  8.97868   1.000 44.76211  ? 14  GLY   C O     1 
ATOM   2849 N  N     . GLU   C 2 16  ? -5.30298  24.48275  9.14894   1.000 42.71198  ? 15  GLU   C N     1 
ATOM   2850 C  CA    . GLU   C 2 16  ? -5.75096  23.58720  8.08732   1.000 43.70935  ? 15  GLU   C CA    1 
ATOM   2851 C  C     . GLU   C 2 16  ? -6.42292  22.36540  8.68361   1.000 42.89614  ? 15  GLU   C C     1 
ATOM   2852 O  O     . GLU   C 2 16  ? -5.87104  21.75981  9.61183   1.000 38.00867  ? 15  GLU   C O     1 
ATOM   2853 C  CB    . GLU   C 2 16  ? -4.57727  23.15133  7.21431   1.000 48.62615  ? 15  GLU   C CB    1 
ATOM   2854 C  CG    . GLU   C 2 16  ? -3.83536  24.30367  6.55388   1.000 53.47721  ? 15  GLU   C CG    1 
ATOM   2855 C  CD    . GLU   C 2 16  ? -4.70253  25.07553  5.56952   1.000 56.81338  ? 15  GLU   C CD    1 
ATOM   2856 O  OE1   . GLU   C 2 16  ? -5.73529  24.53312  5.12048   1.000 61.38329  ? 15  GLU   C OE1   1 
ATOM   2857 O  OE2   . GLU   C 2 16  ? -4.35178  26.22981  5.24907   1.000 62.05102  ? 15  GLU   C OE2   1 
ATOM   2858 N  N     . PRO   C 2 17  ? -7.59791  21.97826  8.19228   1.000 37.65602  ? 16  PRO   C N     1 
ATOM   2859 C  CA    . PRO   C 2 17  ? -8.29729  20.83283  8.78025   1.000 37.61915  ? 16  PRO   C CA    1 
ATOM   2860 C  C     . PRO   C 2 17  ? -7.46110  19.56777  8.69777   1.000 41.59034  ? 16  PRO   C C     1 
ATOM   2861 O  O     . PRO   C 2 17  ? -6.83933  19.26721  7.67611   1.000 38.30081  ? 16  PRO   C O     1 
ATOM   2862 C  CB    . PRO   C 2 17  ? -9.57641  20.72417  7.93746   1.000 41.71772  ? 16  PRO   C CB    1 
ATOM   2863 C  CG    . PRO   C 2 17  ? -9.79861  22.11790  7.43045   1.000 42.32690  ? 16  PRO   C CG    1 
ATOM   2864 C  CD    . PRO   C 2 17  ? -8.41698  22.65854  7.16981   1.000 44.63903  ? 16  PRO   C CD    1 
ATOM   2865 N  N     . LEU   C 2 18  ? -7.43179  18.83703  9.80746   1.000 35.43994  ? 17  LEU   C N     1 
ATOM   2866 C  CA    . LEU   C 2 18  ? -6.81490  17.51983  9.85540   1.000 36.06408  ? 17  LEU   C CA    1 
ATOM   2867 C  C     . LEU   C 2 18  ? -7.85974  16.41346  9.83403   1.000 34.66879  ? 17  LEU   C C     1 
ATOM   2868 O  O     . LEU   C 2 18  ? -7.84840  15.56059  8.94416   1.000 34.88724  ? 17  LEU   C O     1 
ATOM   2869 C  CB    . LEU   C 2 18  ? -5.93894  17.39725  11.10931  1.000 34.24846  ? 17  LEU   C CB    1 
ATOM   2870 C  CG    . LEU   C 2 18  ? -5.18925  16.07469  11.29560  1.000 37.56474  ? 17  LEU   C CG    1 
ATOM   2871 C  CD1   . LEU   C 2 18  ? -4.11714  15.92475  10.23847  1.000 38.87432  ? 17  LEU   C CD1   1 
ATOM   2872 C  CD2   . LEU   C 2 18  ? -4.57443  15.99342  12.69260  1.000 31.62402  ? 17  LEU   C CD2   1 
ATOM   2873 N  N     . GLY   C 2 19  ? -8.77974  16.42328  10.79051  1.000 32.05269  ? 18  GLY   C N     1 
ATOM   2874 C  CA    . GLY   C 2 19  ? -9.83373  15.43231  10.80175  1.000 28.49437  ? 18  GLY   C CA    1 
ATOM   2875 C  C     . GLY   C 2 19  ? -10.72579 15.61662  12.00829  1.000 31.90004  ? 18  GLY   C C     1 
ATOM   2876 O  O     . GLY   C 2 19  ? -10.53043 16.51928  12.83251  1.000 33.56768  ? 18  GLY   C O     1 
ATOM   2877 N  N     . ARG   C 2 20  ? -11.71886 14.73901  12.08860  1.000 32.85905  ? 19  ARG   C N     1 
ATOM   2878 C  CA    . ARG   C 2 20  ? -12.69403 14.75147  13.16530  1.000 37.63640  ? 19  ARG   C CA    1 
ATOM   2879 C  C     . ARG   C 2 20  ? -12.43925 13.57860  14.09596  1.000 31.88951  ? 19  ARG   C C     1 
ATOM   2880 O  O     . ARG   C 2 20  ? -12.21420 12.45277  13.64250  1.000 29.55357  ? 19  ARG   C O     1 
ATOM   2881 C  CB    . ARG   C 2 20  ? -14.12382 14.68719  12.62835  1.000 38.03685  ? 19  ARG   C CB    1 
ATOM   2882 C  CG    . ARG   C 2 20  ? -15.17775 14.56440  13.72601  1.000 39.06881  ? 19  ARG   C CG    1 
ATOM   2883 C  CD    . ARG   C 2 20  ? -16.58709 14.81628  13.19106  1.000 37.26647  ? 19  ARG   C CD    1 
ATOM   2884 N  NE    . ARG   C 2 20  ? -16.77989 16.20869  12.80276  1.000 38.26922  ? 19  ARG   C NE    1 
ATOM   2885 C  CZ    . ARG   C 2 20  ? -17.96164 16.76502  12.56495  1.000 46.37759  ? 19  ARG   C CZ    1 
ATOM   2886 N  NH1   . ARG   C 2 20  ? -19.08930 16.07819  12.68527  1.000 40.51163  ? 19  ARG   C NH1   1 
ATOM   2887 N  NH2   . ARG   C 2 20  ? -18.01421 18.04250  12.19880  1.000 41.86702  ? 19  ARG   C NH2   1 
ATOM   2888 N  N     . VAL   C 2 21  ? -12.46190 13.85527  15.39431  1.000 31.86496  ? 20  VAL   C N     1 
ATOM   2889 C  CA    . VAL   C 2 21  ? -12.41203 12.83461  16.42730  1.000 34.97398  ? 20  VAL   C CA    1 
ATOM   2890 C  C     . VAL   C 2 21  ? -13.73904 12.87992  17.15941  1.000 28.51542  ? 20  VAL   C C     1 
ATOM   2891 O  O     . VAL   C 2 21  ? -14.20559 13.96344  17.52256  1.000 33.65815  ? 20  VAL   C O     1 
ATOM   2892 C  CB    . VAL   C 2 21  ? -11.25709 13.07137  17.41641  1.000 30.33293  ? 20  VAL   C CB    1 
ATOM   2893 C  CG1   . VAL   C 2 21  ? -11.20271 11.95420  18.43579  1.000 29.40032  ? 20  VAL   C CG1   1 
ATOM   2894 C  CG2   . VAL   C 2 21  ? -9.93603  13.22018  16.66714  1.000 31.41577  ? 20  VAL   C CG2   1 
ATOM   2895 N  N     . SER   C 2 22  ? -14.33814 11.71993  17.38012  1.000 29.23795  ? 21  SER   C N     1 
ATOM   2896 C  CA    . SER   C 2 22  ? -15.55299 11.65201  18.17604  1.000 30.75526  ? 21  SER   C CA    1 
ATOM   2897 C  C     . SER   C 2 22  ? -15.30803 10.81313  19.41945  1.000 31.02374  ? 21  SER   C C     1 
ATOM   2898 O  O     . SER   C 2 22  ? -14.49753 9.87843   19.41258  1.000 30.02604  ? 21  SER   C O     1 
ATOM   2899 C  CB    . SER   C 2 22  ? -16.72123 11.08337  17.35376  1.000 32.43168  ? 21  SER   C CB    1 
ATOM   2900 O  OG    . SER   C 2 22  ? -16.67585 9.66898   17.29750  1.000 37.35596  ? 21  SER   C OG    1 
ATOM   2901 N  N     . PHE   C 2 23  ? -16.01652 11.16714  20.49346  1.000 31.30260  ? 22  PHE   C N     1 
ATOM   2902 C  CA    . PHE   C 2 23  ? -15.86900 10.52475  21.78765  1.000 27.74970  ? 22  PHE   C CA    1 
ATOM   2903 C  C     . PHE   C 2 23  ? -17.21974 10.05239  22.29700  1.000 35.30938  ? 22  PHE   C C     1 
ATOM   2904 O  O     . PHE   C 2 23  ? -18.20986 10.78721  22.22534  1.000 34.65820  ? 22  PHE   C O     1 
ATOM   2905 C  CB    . PHE   C 2 23  ? -15.28751 11.47783  22.83708  1.000 26.83507  ? 22  PHE   C CB    1 
ATOM   2906 C  CG    . PHE   C 2 23  ? -14.08142 12.22915  22.37254  1.000 28.95314  ? 22  PHE   C CG    1 
ATOM   2907 C  CD1   . PHE   C 2 23  ? -12.81292 11.71348  22.57121  1.000 31.41782  ? 22  PHE   C CD1   1 
ATOM   2908 C  CD2   . PHE   C 2 23  ? -14.21629 13.46289  21.75887  1.000 27.59743  ? 22  PHE   C CD2   1 
ATOM   2909 C  CE1   . PHE   C 2 23  ? -11.69322 12.41809  22.14369  1.000 26.10236  ? 22  PHE   C CE1   1 
ATOM   2910 C  CE2   . PHE   C 2 23  ? -13.10668 14.17138  21.33076  1.000 28.66813  ? 22  PHE   C CE2   1 
ATOM   2911 C  CZ    . PHE   C 2 23  ? -11.84218 13.64794  21.52676  1.000 29.53313  ? 22  PHE   C CZ    1 
ATOM   2912 N  N     . GLU   C 2 24  ? -17.24156 8.84359   22.84571  1.000 33.29225  ? 23  GLU   C N     1 
ATOM   2913 C  CA    . GLU   C 2 24  ? -18.32956 8.42771   23.71238  1.000 33.47456  ? 23  GLU   C CA    1 
ATOM   2914 C  C     . GLU   C 2 24  ? -18.01481 8.89170   25.12802  1.000 35.91513  ? 23  GLU   C C     1 
ATOM   2915 O  O     . GLU   C 2 24  ? -16.89533 8.69752   25.61604  1.000 30.22859  ? 23  GLU   C O     1 
ATOM   2916 C  CB    . GLU   C 2 24  ? -18.51973 6.91292   23.68024  1.000 33.17713  ? 23  GLU   C CB    1 
ATOM   2917 C  CG    . GLU   C 2 24  ? -19.67177 6.46068   24.59056  1.000 40.10250  ? 23  GLU   C CG    1 
ATOM   2918 C  CD    . GLU   C 2 24  ? -19.80395 4.95178   24.70534  1.000 45.53022  ? 23  GLU   C CD    1 
ATOM   2919 O  OE1   . GLU   C 2 24  ? -19.01327 4.22273   24.06300  1.000 47.84841  ? 23  GLU   C OE1   1 
ATOM   2920 O  OE2   . GLU   C 2 24  ? -20.70196 4.49549   25.45349  1.000 47.95477  ? 23  GLU   C OE2   1 
ATOM   2921 N  N     . LEU   C 2 25  ? -18.99719 9.50657   25.78405  1.000 31.34314  ? 24  LEU   C N     1 
ATOM   2922 C  CA    . LEU   C 2 25  ? -18.84726 9.97908   27.15303  1.000 35.88129  ? 24  LEU   C CA    1 
ATOM   2923 C  C     . LEU   C 2 25  ? -19.65266 9.06812   28.07032  1.000 40.27437  ? 24  LEU   C C     1 
ATOM   2924 O  O     . LEU   C 2 25  ? -20.85560 8.88514   27.86579  1.000 39.11157  ? 24  LEU   C O     1 
ATOM   2925 C  CB    . LEU   C 2 25  ? -19.31663 11.42877  27.27862  1.000 32.90471  ? 24  LEU   C CB    1 
ATOM   2926 C  CG    . LEU   C 2 25  ? -18.75090 12.40042  26.24507  1.000 37.46254  ? 24  LEU   C CG    1 
ATOM   2927 C  CD1   . LEU   C 2 25  ? -19.31251 13.79875  26.46576  1.000 33.10808  ? 24  LEU   C CD1   1 
ATOM   2928 C  CD2   . LEU   C 2 25  ? -17.21220 12.41592  26.32464  1.000 29.77729  ? 24  LEU   C CD2   1 
ATOM   2929 N  N     . PHE   C 2 26  ? -18.99638 8.50887   29.07994  1.000 32.50610  ? 25  PHE   C N     1 
ATOM   2930 C  CA    . PHE   C 2 26  ? -19.60452 7.46723   29.89801  1.000 43.06273  ? 25  PHE   C CA    1 
ATOM   2931 C  C     . PHE   C 2 26  ? -20.41813 8.10963   31.02295  1.000 34.15557  ? 25  PHE   C C     1 
ATOM   2932 O  O     . PHE   C 2 26  ? -20.11901 7.98722   32.20707  1.000 33.39496  ? 25  PHE   C O     1 
ATOM   2933 C  CB    . PHE   C 2 26  ? -18.53280 6.52712   30.42922  1.000 38.77158  ? 25  PHE   C CB    1 
ATOM   2934 C  CG    . PHE   C 2 26  ? -17.73842 5.85233   29.34627  1.000 39.77013  ? 25  PHE   C CG    1 
ATOM   2935 C  CD1   . PHE   C 2 26  ? -18.37760 5.14234   28.34299  1.000 41.17310  ? 25  PHE   C CD1   1 
ATOM   2936 C  CD2   . PHE   C 2 26  ? -16.35331 5.94848   29.31898  1.000 38.78202  ? 25  PHE   C CD2   1 
ATOM   2937 C  CE1   . PHE   C 2 26  ? -17.64911 4.52532   27.34325  1.000 38.03458  ? 25  PHE   C CE1   1 
ATOM   2938 C  CE2   . PHE   C 2 26  ? -15.61478 5.32879   28.31403  1.000 35.05831  ? 25  PHE   C CE2   1 
ATOM   2939 C  CZ    . PHE   C 2 26  ? -16.26543 4.62122   27.32757  1.000 37.42344  ? 25  PHE   C CZ    1 
ATOM   2940 N  N     . ALA   C 2 27  ? -21.47437 8.81525   30.61227  1.000 34.79266  ? 26  ALA   C N     1 
ATOM   2941 C  CA    . ALA   C 2 27  ? -22.38455 9.41976   31.57988  1.000 38.69840  ? 26  ALA   C CA    1 
ATOM   2942 C  C     . ALA   C 2 27  ? -23.06710 8.36849   32.44340  1.000 40.34571  ? 26  ALA   C C     1 
ATOM   2943 O  O     . ALA   C 2 27  ? -23.52290 8.68930   33.54794  1.000 36.32586  ? 26  ALA   C O     1 
ATOM   2944 C  CB    . ALA   C 2 27  ? -23.43432 10.27317  30.86342  1.000 38.40253  ? 26  ALA   C CB    1 
ATOM   2945 N  N     . ASP   C 2 28  ? -23.13828 7.11838   31.97174  1.000 36.52722  ? 27  ASP   C N     1 
ATOM   2946 C  CA    . ASP   C 2 28  ? -23.70354 6.05195   32.79136  1.000 41.04913  ? 27  ASP   C CA    1 
ATOM   2947 C  C     . ASP   C 2 28  ? -22.83104 5.71659   33.99694  1.000 44.76611  ? 27  ASP   C C     1 
ATOM   2948 O  O     . ASP   C 2 28  ? -23.32014 5.08140   34.93579  1.000 45.49845  ? 27  ASP   C O     1 
ATOM   2949 C  CB    . ASP   C 2 28  ? -23.95245 4.79027   31.95065  1.000 41.69378  ? 27  ASP   C CB    1 
ATOM   2950 C  CG    . ASP   C 2 28  ? -22.69790 4.27591   31.25830  1.000 47.01140  ? 27  ASP   C CG    1 
ATOM   2951 O  OD1   . ASP   C 2 28  ? -21.66155 4.96335   31.29780  1.000 46.95291  ? 27  ASP   C OD1   1 
ATOM   2952 O  OD2   . ASP   C 2 28  ? -22.75196 3.17884   30.66734  1.000 52.54199  ? 27  ASP   C OD2   1 
ATOM   2953 N  N     . LYS   C 2 29  ? -21.56144 6.13776   34.01361  1.000 40.54988  ? 28  LYS   C N     1 
ATOM   2954 C  CA    . LYS   C 2 29  ? -20.68800 5.86685   35.14847  1.000 36.69839  ? 28  LYS   C CA    1 
ATOM   2955 C  C     . LYS   C 2 29  ? -20.11149 7.11525   35.79911  1.000 34.82652  ? 28  LYS   C C     1 
ATOM   2956 O  O     . LYS   C 2 29  ? -19.76796 7.07289   36.98453  1.000 38.01656  ? 28  LYS   C O     1 
ATOM   2957 C  CB    . LYS   C 2 29  ? -19.53205 4.94929   34.71913  1.000 40.45471  ? 28  LYS   C CB    1 
ATOM   2958 C  CG    . LYS   C 2 29  ? -19.94033 3.50711   34.50003  1.000 42.38118  ? 28  LYS   C CG    1 
ATOM   2959 C  CD    . LYS   C 2 29  ? -18.77061 2.70198   33.97759  1.000 47.42486  ? 28  LYS   C CD    1 
ATOM   2960 C  CE    . LYS   C 2 29  ? -19.14962 1.24376   33.78314  1.000 44.57280  ? 28  LYS   C CE    1 
ATOM   2961 N  NZ    . LYS   C 2 29  ? -20.38012 1.09015   32.95585  1.000 44.53792  ? 28  LYS   C NZ    1 
ATOM   2962 N  N     . VAL   C 2 30  ? -19.96613 8.20782   35.05102  1.000 35.51117  ? 29  VAL   C N     1 
ATOM   2963 C  CA    . VAL   C 2 30  ? -19.50467 9.49254   35.58000  1.000 31.97373  ? 29  VAL   C CA    1 
ATOM   2964 C  C     . VAL   C 2 30  ? -20.38534 10.58300  34.98114  1.000 41.59469  ? 29  VAL   C C     1 
ATOM   2965 O  O     . VAL   C 2 30  ? -19.94313 11.33075  34.09660  1.000 32.20707  ? 29  VAL   C O     1 
ATOM   2966 C  CB    . VAL   C 2 30  ? -18.01720 9.73616   35.27573  1.000 37.51778  ? 29  VAL   C CB    1 
ATOM   2967 C  CG1   . VAL   C 2 30  ? -17.15999 9.17644   36.38775  1.000 31.53329  ? 29  VAL   C CG1   1 
ATOM   2968 C  CG2   . VAL   C 2 30  ? -17.65892 9.09825   33.96275  1.000 33.03879  ? 29  VAL   C CG2   1 
ATOM   2969 N  N     . PRO   C 2 31  ? -21.64192 10.69853  35.42539  1.000 32.59223  ? 30  PRO   C N     1 
ATOM   2970 C  CA    . PRO   C 2 31  ? -22.55161 11.67185  34.79785  1.000 36.15055  ? 30  PRO   C CA    1 
ATOM   2971 C  C     . PRO   C 2 31  ? -22.11008 13.11432  34.96330  1.000 37.25331  ? 30  PRO   C C     1 
ATOM   2972 O  O     . PRO   C 2 31  ? -22.27321 13.91275  34.03246  1.000 36.80063  ? 30  PRO   C O     1 
ATOM   2973 C  CB    . PRO   C 2 31  ? -23.89197 11.39877  35.50926  1.000 36.72167  ? 30  PRO   C CB    1 
ATOM   2974 C  CG    . PRO   C 2 31  ? -23.50026 10.76279  36.82035  1.000 36.78484  ? 30  PRO   C CG    1 
ATOM   2975 C  CD    . PRO   C 2 31  ? -22.30053 9.92113   36.49351  1.000 40.35261  ? 30  PRO   C CD    1 
ATOM   2976 N  N     . LYS   C 2 32  ? -21.55706 13.47912  36.12123  1.000 34.83987  ? 31  LYS   C N     1 
ATOM   2977 C  CA    . LYS   C 2 32  ? -21.18655 14.87493  36.33093  1.000 32.57644  ? 31  LYS   C CA    1 
ATOM   2978 C  C     . LYS   C 2 32  ? -19.98792 15.25015  35.47125  1.000 40.14212  ? 31  LYS   C C     1 
ATOM   2979 O  O     . LYS   C 2 32  ? -19.99058 16.29620  34.80844  1.000 36.08031  ? 31  LYS   C O     1 
ATOM   2980 C  CB    . LYS   C 2 32  ? -20.88994 15.13070  37.80544  1.000 40.47465  ? 31  LYS   C CB    1 
ATOM   2981 C  CG    . LYS   C 2 32  ? -20.71512 16.60648  38.15465  1.000 47.00634  ? 31  LYS   C CG    1 
ATOM   2982 C  CD    . LYS   C 2 32  ? -20.59429 16.83402  39.66241  1.000 46.64138  ? 31  LYS   C CD    1 
ATOM   2983 C  CE    . LYS   C 2 32  ? -20.52723 18.32261  39.99387  1.000 50.31580  ? 31  LYS   C CE    1 
ATOM   2984 N  NZ    . LYS   C 2 32  ? -20.37159 18.57332  41.45433  1.000 56.74926  ? 31  LYS   C NZ    1 
ATOM   2985 N  N     . THR   C 2 33  ? -18.96485 14.39617  35.46737  1.000 32.60078  ? 32  THR   C N     1 
ATOM   2986 C  CA    . THR   C 2 33  ? -17.76692 14.66203  34.67177  1.000 34.62402  ? 32  THR   C CA    1 
ATOM   2987 C  C     . THR   C 2 33  ? -18.08380 14.62579  33.18135  1.000 31.41051  ? 32  THR   C C     1 
ATOM   2988 O  O     . THR   C 2 33  ? -17.60174 15.47111  32.41304  1.000 32.86579  ? 32  THR   C O     1 
ATOM   2989 C  CB    . THR   C 2 33  ? -16.68233 13.64784  35.03236  1.000 33.12634  ? 32  THR   C CB    1 
ATOM   2990 O  OG1   . THR   C 2 33  ? -16.55964 13.56313  36.45765  1.000 31.92909  ? 32  THR   C OG1   1 
ATOM   2991 C  CG2   . THR   C 2 33  ? -15.32557 14.05310  34.44449  1.000 30.56779  ? 32  THR   C CG2   1 
ATOM   2992 N  N     . ALA   C 2 34  ? -18.90096 13.66332  32.75509  1.000 32.05795  ? 33  ALA   C N     1 
ATOM   2993 C  CA    . ALA   C 2 34  ? -19.30207 13.58889  31.35604  1.000 32.57374  ? 33  ALA   C CA    1 
ATOM   2994 C  C     . ALA   C 2 34  ? -20.07715 14.83027  30.93740  1.000 38.82676  ? 33  ALA   C C     1 
ATOM   2995 O  O     . ALA   C 2 34  ? -19.87984 15.36106  29.83911  1.000 34.13189  ? 33  ALA   C O     1 
ATOM   2996 C  CB    . ALA   C 2 34  ? -20.14058 12.33269  31.11882  1.000 37.90245  ? 33  ALA   C CB    1 
ATOM   2997 N  N     . GLU   C 2 35  ? -20.98890 15.29510  31.79725  1.000 35.97459  ? 34  GLU   C N     1 
ATOM   2998 C  CA    . GLU   C 2 35  ? -21.80132 16.45724  31.45136  1.000 37.26767  ? 34  GLU   C CA    1 
ATOM   2999 C  C     . GLU   C 2 35  ? -20.94468 17.70068  31.25788  1.000 34.80302  ? 34  GLU   C C     1 
ATOM   3000 O  O     . GLU   C 2 35  ? -21.16882 18.47664  30.32089  1.000 40.83042  ? 34  GLU   C O     1 
ATOM   3001 C  CB    . GLU   C 2 35  ? -22.85799 16.69435  32.53508  1.000 35.34246  ? 34  GLU   C CB    1 
ATOM   3002 C  CG    . GLU   C 2 35  ? -23.64123 17.98619  32.37696  1.000 36.92412  ? 34  GLU   C CG    1 
ATOM   3003 C  CD    . GLU   C 2 35  ? -24.45589 18.04973  31.09509  1.000 41.22221  ? 34  GLU   C CD    1 
ATOM   3004 O  OE1   . GLU   C 2 35  ? -24.63920 17.01599  30.42124  1.000 42.65923  ? 34  GLU   C OE1   1 
ATOM   3005 O  OE2   . GLU   C 2 35  ? -24.92768 19.15260  30.76154  1.000 48.63528  ? 34  GLU   C OE2   1 
ATOM   3006 N  N     . ASN   C 2 36  ? -19.96964 17.91016  32.14332  1.000 38.25623  ? 35  ASN   C N     1 
ATOM   3007 C  CA    . ASN   C 2 36  ? -19.03271 19.02152  31.99797  1.000 38.49099  ? 35  ASN   C CA    1 
ATOM   3008 C  C     . ASN   C 2 36  ? -18.43684 19.03841  30.59927  1.000 35.69393  ? 35  ASN   C C     1 
ATOM   3009 O  O     . ASN   C 2 36  ? -18.52987 20.03659  29.87705  1.000 37.02652  ? 35  ASN   C O     1 
ATOM   3010 C  CB    . ASN   C 2 36  ? -17.92736 18.90640  33.05170  1.000 35.11693  ? 35  ASN   C CB    1 
ATOM   3011 C  CG    . ASN   C 2 36  ? -16.95596 20.06625  33.01732  1.000 39.18852  ? 35  ASN   C CG    1 
ATOM   3012 O  OD1   . ASN   C 2 36  ? -17.35205 21.23487  33.03364  1.000 36.84800  ? 35  ASN   C OD1   1 
ATOM   3013 N  ND2   . ASN   C 2 36  ? -15.66605 19.75058  32.95011  1.000 40.24802  ? 35  ASN   C ND2   1 
ATOM   3014 N  N     . PHE   C 2 37  ? -17.86420 17.90948  30.18506  1.000 38.80308  ? 36  PHE   C N     1 
ATOM   3015 C  CA    . PHE   C 2 37  ? -17.20238 17.84155  28.88728  1.000 34.44044  ? 36  PHE   C CA    1 
ATOM   3016 C  C     . PHE   C 2 37  ? -18.20433 17.97160  27.74253  1.000 41.48601  ? 36  PHE   C C     1 
ATOM   3017 O  O     . PHE   C 2 37  ? -17.90877 18.60940  26.72625  1.000 34.36456  ? 36  PHE   C O     1 
ATOM   3018 C  CB    . PHE   C 2 37  ? -16.41797 16.53389  28.79598  1.000 34.99574  ? 36  PHE   C CB    1 
ATOM   3019 C  CG    . PHE   C 2 37  ? -15.50449 16.44450  27.60949  1.000 28.90983  ? 36  PHE   C CG    1 
ATOM   3020 C  CD1   . PHE   C 2 37  ? -15.97313 15.98773  26.39024  1.000 29.77814  ? 36  PHE   C CD1   1 
ATOM   3021 C  CD2   . PHE   C 2 37  ? -14.17342 16.79248  27.72854  1.000 27.13108  ? 36  PHE   C CD2   1 
ATOM   3022 C  CE1   . PHE   C 2 37  ? -15.12545 15.89493  25.30460  1.000 33.36645  ? 36  PHE   C CE1   1 
ATOM   3023 C  CE2   . PHE   C 2 37  ? -13.32060 16.69724  26.63616  1.000 26.25376  ? 36  PHE   C CE2   1 
ATOM   3024 C  CZ    . PHE   C 2 37  ? -13.80219 16.24628  25.43678  1.000 29.37926  ? 36  PHE   C CZ    1 
ATOM   3025 N  N     . ARG   C 2 38  ? -19.40104 17.38671  27.89113  1.000 33.64665  ? 37  ARG   C N     1 
ATOM   3026 C  CA    . ARG   C 2 38  ? -20.42885 17.53312  26.86667  1.000 39.91439  ? 37  ARG   C CA    1 
ATOM   3027 C  C     . ARG   C 2 38  ? -20.83086 18.99242  26.71396  1.000 38.30607  ? 37  ARG   C C     1 
ATOM   3028 O  O     . ARG   C 2 38  ? -20.92905 19.51095  25.59599  1.000 37.49282  ? 37  ARG   C O     1 
ATOM   3029 C  CB    . ARG   C 2 38  ? -21.65187 16.67835  27.21376  1.000 38.28765  ? 37  ARG   C CB    1 
ATOM   3030 C  CG    . ARG   C 2 38  ? -22.72174 16.65556  26.12102  1.000 39.44272  ? 37  ARG   C CG    1 
ATOM   3031 C  CD    . ARG   C 2 38  ? -24.11297 16.31819  26.67028  1.000 43.90571  ? 37  ARG   C CD    1 
ATOM   3032 N  NE    . ARG   C 2 38  ? -24.57794 17.38782  27.54212  1.000 48.54917  ? 37  ARG   C NE    1 
ATOM   3033 C  CZ    . ARG   C 2 38  ? -25.05026 18.54836  27.11020  1.000 45.00410  ? 37  ARG   C CZ    1 
ATOM   3034 N  NH1   . ARG   C 2 38  ? -25.20951 18.79189  25.81852  1.000 43.09759  ? 37  ARG   C NH1   1 
ATOM   3035 N  NH2   . ARG   C 2 38  ? -25.35442 19.49400  27.99548  1.000 49.30084  ? 37  ARG   C NH2   1 
ATOM   3036 N  N     . ALA   C 2 39  ? -21.06670 19.67016  27.83708  1.000 39.04638  ? 38  ALA   C N     1 
ATOM   3037 C  CA    . ALA   C 2 39  ? -21.47665 21.07030  27.79758  1.000 45.14565  ? 38  ALA   C CA    1 
ATOM   3038 C  C     . ALA   C 2 39  ? -20.39037 21.95436  27.19518  1.000 43.31975  ? 38  ALA   C C     1 
ATOM   3039 O  O     . ALA   C 2 39  ? -20.68336 22.85257  26.39668  1.000 42.27760  ? 38  ALA   C O     1 
ATOM   3040 C  CB    . ALA   C 2 39  ? -21.83219 21.54667  29.20781  1.000 47.15763  ? 38  ALA   C CB    1 
ATOM   3041 N  N     . LEU   C 2 40  ? -19.12985 21.72676  27.58006  1.000 39.14718  ? 39  LEU   C N     1 
ATOM   3042 C  CA    . LEU   C 2 40  ? -18.03384 22.51219  27.02039  1.000 39.24719  ? 39  LEU   C CA    1 
ATOM   3043 C  C     . LEU   C 2 40  ? -17.84803 22.23713  25.53461  1.000 35.51507  ? 39  LEU   C C     1 
ATOM   3044 O  O     . LEU   C 2 40  ? -17.35909 23.10395  24.79930  1.000 40.04497  ? 39  LEU   C O     1 
ATOM   3045 C  CB    . LEU   C 2 40  ? -16.74393 22.22524  27.78661  1.000 32.20271  ? 39  LEU   C CB    1 
ATOM   3046 C  CG    . LEU   C 2 40  ? -16.73336 22.67016  29.25504  1.000 34.15028  ? 39  LEU   C CG    1 
ATOM   3047 C  CD1   . LEU   C 2 40  ? -15.56754 22.07322  29.99104  1.000 32.14757  ? 39  LEU   C CD1   1 
ATOM   3048 C  CD2   . LEU   C 2 40  ? -16.69813 24.18630  29.35212  1.000 41.34676  ? 39  LEU   C CD2   1 
ATOM   3049 N  N     . SER   C 2 41  ? -18.23698 21.04888  25.07303  1.000 35.66891  ? 40  SER   C N     1 
ATOM   3050 C  CA    . SER   C 2 41  ? -18.08463 20.71846  23.66274  1.000 32.71593  ? 40  SER   C CA    1 
ATOM   3051 C  C     . SER   C 2 41  ? -19.13654 21.41978  22.80497  1.000 44.10442  ? 40  SER   C C     1 
ATOM   3052 O  O     . SER   C 2 41  ? -18.85362 21.81204  21.66729  1.000 40.48791  ? 40  SER   C O     1 
ATOM   3053 C  CB    . SER   C 2 41  ? -18.15417 19.20341  23.47616  1.000 34.36907  ? 40  SER   C CB    1 
ATOM   3054 O  OG    . SER   C 2 41  ? -17.08194 18.57288  24.15785  1.000 38.80770  ? 40  SER   C OG    1 
ATOM   3055 N  N     . THR   C 2 42  ? -20.35531 21.59871  23.33327  1.000 43.57703  ? 41  THR   C N     1 
ATOM   3056 C  CA    . THR   C 2 42  ? -21.39734 22.28795  22.57387  1.000 43.34604  ? 41  THR   C CA    1 
ATOM   3057 C  C     . THR   C 2 42  ? -21.25137 23.80556  22.59674  1.000 42.83293  ? 41  THR   C C     1 
ATOM   3058 O  O     . THR   C 2 42  ? -21.74334 24.47425  21.68096  1.000 47.63786  ? 41  THR   C O     1 
ATOM   3059 C  CB    . THR   C 2 42  ? -22.78721 21.91759  23.10396  1.000 44.76474  ? 41  THR   C CB    1 
ATOM   3060 O  OG1   . THR   C 2 42  ? -22.87302 22.25021  24.49347  1.000 47.13608  ? 41  THR   C OG1   1 
ATOM   3061 C  CG2   . THR   C 2 42  ? -23.06574 20.43132  22.91216  1.000 42.91715  ? 41  THR   C CG2   1 
ATOM   3062 N  N     . GLY   C 2 43  ? -20.58740 24.35932  23.60669  1.000 41.76175  ? 42  GLY   C N     1 
ATOM   3063 C  CA    . GLY   C 2 43  ? -20.53687 25.79394  23.79628  1.000 45.02229  ? 42  GLY   C CA    1 
ATOM   3064 C  C     . GLY   C 2 43  ? -21.78259 26.39333  24.41204  1.000 49.88392  ? 42  GLY   C C     1 
ATOM   3065 O  O     . GLY   C 2 43  ? -21.88822 27.62185  24.49067  1.000 51.48584  ? 42  GLY   C O     1 
ATOM   3066 N  N     . GLU   C 2 44  ? -22.71456 25.56353  24.88070  1.000 48.57046  ? 43  GLU   C N     1 
ATOM   3067 C  CA    . GLU   C 2 44  ? -24.05732 26.02140  25.22153  1.000 55.72383  ? 43  GLU   C CA    1 
ATOM   3068 C  C     . GLU   C 2 44  ? -24.11324 26.86760  26.48591  1.000 54.56491  ? 43  GLU   C C     1 
ATOM   3069 O  O     . GLU   C 2 44  ? -25.15937 27.46548  26.75441  1.000 59.11206  ? 43  GLU   C O     1 
ATOM   3070 C  CB    . GLU   C 2 44  ? -24.98890 24.82093  25.37461  1.000 55.79948  ? 43  GLU   C CB    1 
ATOM   3071 C  CG    . GLU   C 2 44  ? -24.70229 23.97258  26.60361  1.000 54.74042  ? 43  GLU   C CG    1 
ATOM   3072 C  CD    . GLU   C 2 44  ? -25.45816 22.66174  26.58335  1.000 58.57406  ? 43  GLU   C CD    1 
ATOM   3073 O  OE1   . GLU   C 2 44  ? -25.35903 21.93323  25.57041  1.000 54.68668  ? 43  GLU   C OE1   1 
ATOM   3074 O  OE2   . GLU   C 2 44  ? -26.16311 22.36586  27.57313  1.000 61.92833  ? 43  GLU   C OE2   1 
ATOM   3075 N  N     . LYS   C 2 45  ? -23.04129 26.92846  27.26886  1.000 54.40578  ? 44  LYS   C N     1 
ATOM   3076 C  CA    . LYS   C 2 45  ? -23.00183 27.77588  28.45352  1.000 55.44760  ? 44  LYS   C CA    1 
ATOM   3077 C  C     . LYS   C 2 45  ? -22.34278 29.12451  28.19494  1.000 53.67498  ? 44  LYS   C C     1 
ATOM   3078 O  O     . LYS   C 2 45  ? -22.15246 29.89737  29.13912  1.000 59.91915  ? 44  LYS   C O     1 
ATOM   3079 C  CB    . LYS   C 2 45  ? -22.27074 27.06148  29.59428  1.000 54.37227  ? 44  LYS   C CB    1 
ATOM   3080 C  CG    . LYS   C 2 45  ? -22.97810 25.82137  30.11599  1.000 62.58497  ? 44  LYS   C CG    1 
ATOM   3081 C  CD    . LYS   C 2 45  ? -24.21277 26.17937  30.92194  1.000 61.88693  ? 44  LYS   C CD    1 
ATOM   3082 C  CE    . LYS   C 2 45  ? -24.76441 24.96653  31.66599  1.000 69.48876  ? 44  LYS   C CE    1 
ATOM   3083 N  NZ    . LYS   C 2 45  ? -25.29557 23.92313  30.74500  1.000 68.42635  ? 44  LYS   C NZ    1 
ATOM   3084 N  N     . GLY   C 2 46  ? -21.98957 29.42615  26.94967  1.000 56.90728  ? 45  GLY   C N     1 
ATOM   3085 C  CA    . GLY   C 2 46  ? -21.31875 30.66531  26.62116  1.000 57.70663  ? 45  GLY   C CA    1 
ATOM   3086 C  C     . GLY   C 2 46  ? -19.81098 30.57436  26.55018  1.000 59.10105  ? 45  GLY   C C     1 
ATOM   3087 O  O     . GLY   C 2 46  ? -19.15964 31.59042  26.27361  1.000 56.11376  ? 45  GLY   C O     1 
ATOM   3088 N  N     . PHE   C 2 47  ? -19.23870 29.39782  26.79909  1.000 49.70131  ? 46  PHE   C N     1 
ATOM   3089 C  CA    . PHE   C 2 47  ? -17.80507 29.17754  26.68133  1.000 46.58692  ? 46  PHE   C CA    1 
ATOM   3090 C  C     . PHE   C 2 47  ? -17.58932 27.70654  26.34720  1.000 44.78558  ? 46  PHE   C C     1 
ATOM   3091 O  O     . PHE   C 2 47  ? -18.54153 26.92565  26.26205  1.000 42.40810  ? 46  PHE   C O     1 
ATOM   3092 C  CB    . PHE   C 2 47  ? -17.07875 29.59914  27.96478  1.000 45.32949  ? 46  PHE   C CB    1 
ATOM   3093 C  CG    . PHE   C 2 47  ? -17.68845 29.03927  29.22709  1.000 53.18608  ? 46  PHE   C CG    1 
ATOM   3094 C  CD1   . PHE   C 2 47  ? -17.33302 27.77938  29.68906  1.000 50.86302  ? 46  PHE   C CD1   1 
ATOM   3095 C  CD2   . PHE   C 2 47  ? -18.60863 29.77748  29.95951  1.000 52.90207  ? 46  PHE   C CD2   1 
ATOM   3096 C  CE1   . PHE   C 2 47  ? -17.88892 27.26173  30.86156  1.000 48.06728  ? 46  PHE   C CE1   1 
ATOM   3097 C  CE2   . PHE   C 2 47  ? -19.16950 29.26380  31.12855  1.000 53.65619  ? 46  PHE   C CE2   1 
ATOM   3098 C  CZ    . PHE   C 2 47  ? -18.81116 28.00397  31.57512  1.000 52.30813  ? 46  PHE   C CZ    1 
ATOM   3099 N  N     . GLY   C 2 48  ? -16.33833 27.32101  26.14663  1.000 41.23086  ? 47  GLY   C N     1 
ATOM   3100 C  CA    . GLY   C 2 48  ? -16.06325 25.91979  25.91291  1.000 36.25630  ? 47  GLY   C CA    1 
ATOM   3101 C  C     . GLY   C 2 48  ? -14.82446 25.72120  25.05976  1.000 35.22013  ? 47  GLY   C C     1 
ATOM   3102 O  O     . GLY   C 2 48  ? -13.95700 26.58261  24.98125  1.000 37.20511  ? 47  GLY   C O     1 
ATOM   3103 N  N     . TYR   C 2 49  ? -14.79221 24.55163  24.42118  1.000 35.09345  ? 48  TYR   C N     1 
ATOM   3104 C  CA    . TYR   C 2 49  ? -13.56426 24.06135  23.80582  1.000 38.30289  ? 48  TYR   C CA    1 
ATOM   3105 C  C     . TYR   C 2 49  ? -13.31067 24.68253  22.44311  1.000 37.66117  ? 48  TYR   C C     1 
ATOM   3106 O  O     . TYR   C 2 49  ? -12.15180 24.74439  22.00930  1.000 36.07396  ? 48  TYR   C O     1 
ATOM   3107 C  CB    . TYR   C 2 49  ? -13.62383 22.53934  23.67504  1.000 30.95561  ? 48  TYR   C CB    1 
ATOM   3108 C  CG    . TYR   C 2 49  ? -13.50172 21.81020  24.99258  1.000 26.19528  ? 48  TYR   C CG    1 
ATOM   3109 C  CD1   . TYR   C 2 49  ? -12.55354 22.19461  25.92904  1.000 27.99790  ? 48  TYR   C CD1   1 
ATOM   3110 C  CD2   . TYR   C 2 49  ? -14.32876 20.73767  25.29351  1.000 31.31129  ? 48  TYR   C CD2   1 
ATOM   3111 C  CE1   . TYR   C 2 49  ? -12.42327 21.53072  27.12562  1.000 32.57373  ? 48  TYR   C CE1   1 
ATOM   3112 C  CE2   . TYR   C 2 49  ? -14.21316 20.06612  26.49978  1.000 29.03825  ? 48  TYR   C CE2   1 
ATOM   3113 C  CZ    . TYR   C 2 49  ? -13.25975 20.47437  27.40984  1.000 27.64163  ? 48  TYR   C CZ    1 
ATOM   3114 O  OH    . TYR   C 2 49  ? -13.11077 19.83656  28.60908  1.000 29.11614  ? 48  TYR   C OH    1 
ATOM   3115 N  N     . LYS   C 2 50  ? -14.35956 25.12315  21.74575  1.000 39.18301  ? 49  LYS   C N     1 
ATOM   3116 C  CA    . LYS   C 2 50  ? -14.17691 25.62522  20.38774  1.000 37.16580  ? 49  LYS   C CA    1 
ATOM   3117 C  C     . LYS   C 2 50  ? -13.12100 26.72135  20.37666  1.000 38.12404  ? 49  LYS   C C     1 
ATOM   3118 O  O     . LYS   C 2 50  ? -13.16055 27.64803  21.19200  1.000 38.45872  ? 49  LYS   C O     1 
ATOM   3119 C  CB    . LYS   C 2 50  ? -15.49655 26.14977  19.82062  1.000 42.01417  ? 49  LYS   C CB    1 
ATOM   3120 C  CG    . LYS   C 2 50  ? -15.38065 26.56288  18.35641  1.000 41.96827  ? 49  LYS   C CG    1 
ATOM   3121 C  CD    . LYS   C 2 50  ? -16.72057 26.96056  17.76256  1.000 38.39029  ? 49  LYS   C CD    1 
ATOM   3122 C  CE    . LYS   C 2 50  ? -16.54736 27.40786  16.31778  1.000 47.01500  ? 49  LYS   C CE    1 
ATOM   3123 N  NZ    . LYS   C 2 50  ? -17.81367 27.96236  15.75052  1.000 46.62939  ? 49  LYS   C NZ    1 
ATOM   3124 N  N     . GLY   C 2 51  ? -12.14510 26.58310  19.48213  1.000 33.14132  ? 50  GLY   C N     1 
ATOM   3125 C  CA    . GLY   C 2 51  ? -11.06385 27.53450  19.37153  1.000 37.65299  ? 50  GLY   C CA    1 
ATOM   3126 C  C     . GLY   C 2 51  ? -9.85627  27.26684  20.24783  1.000 42.51005  ? 50  GLY   C C     1 
ATOM   3127 O  O     . GLY   C 2 51  ? -8.82962  27.93869  20.07635  1.000 37.42073  ? 50  GLY   C O     1 
ATOM   3128 N  N     . SER   C 2 52  ? -9.93230  26.32513  21.18703  1.000 35.46820  ? 51  SER   C N     1 
ATOM   3129 C  CA    . SER   C 2 52  ? -8.78782  26.08407  22.05269  1.000 29.49449  ? 51  SER   C CA    1 
ATOM   3130 C  C     . SER   C 2 52  ? -7.79406  25.13034  21.38360  1.000 32.66329  ? 51  SER   C C     1 
ATOM   3131 O  O     . SER   C 2 52  ? -8.08299  24.49351  20.36480  1.000 32.11244  ? 51  SER   C O     1 
ATOM   3132 C  CB    . SER   C 2 52  ? -9.24223  25.53341  23.40841  1.000 36.47582  ? 51  SER   C CB    1 
ATOM   3133 O  OG    . SER   C 2 52  ? -9.91266  24.28774  23.25354  1.000 34.84267  ? 51  SER   C OG    1 
ATOM   3134 N  N     . CYS   C 2 53  ? -6.60960  25.02707  21.98588  1.000 27.96621  ? 52  CYS   C N     1 
ATOM   3135 C  CA    . CYS   C 2 53  ? -5.51115  24.25708  21.42777  1.000 34.39821  ? 52  CYS   C CA    1 
ATOM   3136 C  C     . CYS   C 2 53  ? -5.14930  23.06655  22.30943  1.000 29.52369  ? 52  CYS   C C     1 
ATOM   3137 O  O     . CYS   C 2 53  ? -5.52235  22.97555  23.48446  1.000 30.00239  ? 52  CYS   C O     1 
ATOM   3138 C  CB    . CYS   C 2 53  ? -4.26384  25.13380  21.21961  1.000 29.35500  ? 52  CYS   C CB    1 
ATOM   3139 S  SG    . CYS   C 2 53  ? -3.32054  25.56277  22.69774  1.000 42.61331  ? 52  CYS   C SG    1 
ATOM   3140 N  N     . PHE   C 2 54  ? -4.43649  22.13069  21.70558  1.000 30.82425  ? 53  PHE   C N     1 
ATOM   3141 C  CA    . PHE   C 2 54  ? -3.74081  21.09446  22.44734  1.000 29.41041  ? 53  PHE   C CA    1 
ATOM   3142 C  C     . PHE   C 2 54  ? -2.34666  21.62561  22.75710  1.000 28.83592  ? 53  PHE   C C     1 
ATOM   3143 O  O     . PHE   C 2 54  ? -1.49564  21.72819  21.86345  1.000 31.58093  ? 53  PHE   C O     1 
ATOM   3144 C  CB    . PHE   C 2 54  ? -3.70318  19.79936  21.64810  1.000 29.07227  ? 53  PHE   C CB    1 
ATOM   3145 C  CG    . PHE   C 2 54  ? -4.98883  19.04405  21.68091  1.000 27.14350  ? 53  PHE   C CG    1 
ATOM   3146 C  CD1   . PHE   C 2 54  ? -6.00300  19.33968  20.78670  1.000 29.70419  ? 53  PHE   C CD1   1 
ATOM   3147 C  CD2   . PHE   C 2 54  ? -5.20864  18.06056  22.64050  1.000 31.30976  ? 53  PHE   C CD2   1 
ATOM   3148 C  CE1   . PHE   C 2 54  ? -7.21347  18.66313  20.82217  1.000 31.40108  ? 53  PHE   C CE1   1 
ATOM   3149 C  CE2   . PHE   C 2 54  ? -6.42689  17.36446  22.67372  1.000 31.64566  ? 53  PHE   C CE2   1 
ATOM   3150 C  CZ    . PHE   C 2 54  ? -7.42548  17.67076  21.75988  1.000 28.54750  ? 53  PHE   C CZ    1 
ATOM   3151 N  N     . HIS   C 2 55  ? -2.12872  22.01226  24.00984  1.000 27.46458  ? 54  HIS   C N     1 
ATOM   3152 C  CA    . HIS   C 2 55  ? -0.88839  22.67029  24.38199  1.000 27.69026  ? 54  HIS   C CA    1 
ATOM   3153 C  C     . HIS   C 2 55  ? 0.22751   21.70051  24.72390  1.000 28.35283  ? 54  HIS   C C     1 
ATOM   3154 O  O     . HIS   C 2 55  ? 1.40003   22.09094  24.70179  1.000 27.98945  ? 54  HIS   C O     1 
ATOM   3155 C  CB    . HIS   C 2 55  ? -1.13419  23.61635  25.55446  1.000 28.09038  ? 54  HIS   C CB    1 
ATOM   3156 C  CG    . HIS   C 2 55  ? -1.60003  22.93444  26.79957  1.000 28.51038  ? 54  HIS   C CG    1 
ATOM   3157 N  ND1   . HIS   C 2 55  ? -2.91757  22.60114  27.01533  1.000 29.13046  ? 54  HIS   C ND1   1 
ATOM   3158 C  CD2   . HIS   C 2 55  ? -0.92577  22.54987  27.90970  1.000 31.04958  ? 54  HIS   C CD2   1 
ATOM   3159 C  CE1   . HIS   C 2 55  ? -3.03861  22.03240  28.20427  1.000 33.50255  ? 54  HIS   C CE1   1 
ATOM   3160 N  NE2   . HIS   C 2 55  ? -1.84520  21.99985  28.77188  1.000 29.30897  ? 54  HIS   C NE2   1 
ATOM   3161 N  N     . ARG   C 2 56  ? -0.08750  20.43907  24.99011  1.000 24.38455  ? 55  ARG   C N     1 
ATOM   3162 C  CA    . ARG   C 2 56  ? 0.93072   19.46600  25.35238  1.000 25.73128  ? 55  ARG   C CA    1 
ATOM   3163 C  C     . ARG   C 2 56  ? 0.62255   18.17542  24.61815  1.000 26.68688  ? 55  ARG   C C     1 
ATOM   3164 O  O     . ARG   C 2 56  ? -0.42746  17.56940  24.84210  1.000 25.97312  ? 55  ARG   C O     1 
ATOM   3165 C  CB    . ARG   C 2 56  ? 0.95559   19.25093  26.86666  1.000 22.36101  ? 55  ARG   C CB    1 
ATOM   3166 C  CG    . ARG   C 2 56  ? 2.01531   18.32119  27.37584  1.000 25.26143  ? 55  ARG   C CG    1 
ATOM   3167 C  CD    . ARG   C 2 56  ? 1.86378   18.18571  28.90556  1.000 24.93530  ? 55  ARG   C CD    1 
ATOM   3168 N  NE    . ARG   C 2 56  ? 2.30773   19.37861  29.62389  1.000 30.60056  ? 55  ARG   C NE    1 
ATOM   3169 C  CZ    . ARG   C 2 56  ? 1.96215   19.67181  30.87498  1.000 35.31722  ? 55  ARG   C CZ    1 
ATOM   3170 N  NH1   . ARG   C 2 56  ? 1.17699   18.87156  31.58612  1.000 28.85866  ? 55  ARG   C NH1   1 
ATOM   3171 N  NH2   . ARG   C 2 56  ? 2.41161   20.79740  31.42762  1.000 32.79369  ? 55  ARG   C NH2   1 
ATOM   3172 N  N     . ILE   C 2 57  ? 1.52184   17.76566  23.72908  1.000 21.14366  ? 56  ILE   C N     1 
ATOM   3173 C  CA    . ILE   C 2 57  ? 1.43091   16.48795  23.02780  1.000 19.65937  ? 56  ILE   C CA    1 
ATOM   3174 C  C     . ILE   C 2 57  ? 2.76318   15.77105  23.21330  1.000 26.91115  ? 56  ILE   C C     1 
ATOM   3175 O  O     . ILE   C 2 57  ? 3.80805   16.27501  22.77664  1.000 24.04009  ? 56  ILE   C O     1 
ATOM   3176 C  CB    . ILE   C 2 57  ? 1.11817   16.67266  21.53082  1.000 21.90775  ? 56  ILE   C CB    1 
ATOM   3177 C  CG1   . ILE   C 2 57  ? -0.25382  17.31538  21.34367  1.000 27.83538  ? 56  ILE   C CG1   1 
ATOM   3178 C  CG2   . ILE   C 2 57  ? 1.27060   15.34563  20.80012  1.000 23.71219  ? 56  ILE   C CG2   1 
ATOM   3179 C  CD1   . ILE   C 2 57  ? -0.52546  17.69508  19.88715  1.000 24.51924  ? 56  ILE   C CD1   1 
ATOM   3180 N  N     . ILE   C 2 58  ? 2.74144   14.62250  23.87716  1.000 24.05246  ? 57  ILE   C N     1 
ATOM   3181 C  CA    . ILE   C 2 58  ? 3.94439   13.84438  24.15325  1.000 23.16371  ? 57  ILE   C CA    1 
ATOM   3182 C  C     . ILE   C 2 58  ? 3.80204   12.48505  23.49077  1.000 23.07454  ? 57  ILE   C C     1 
ATOM   3183 O  O     . ILE   C 2 58  ? 3.08537   11.60989  23.99160  1.000 20.49743  ? 57  ILE   C O     1 
ATOM   3184 C  CB    . ILE   C 2 58  ? 4.19644   13.70145  25.66289  1.000 22.67369  ? 57  ILE   C CB    1 
ATOM   3185 C  CG1   . ILE   C 2 58  ? 4.25541   15.08703  26.31722  1.000 23.88621  ? 57  ILE   C CG1   1 
ATOM   3186 C  CG2   . ILE   C 2 58  ? 5.45199   12.87107  25.88273  1.000 22.93614  ? 57  ILE   C CG2   1 
ATOM   3187 C  CD1   . ILE   C 2 58  ? 4.82122   15.13084  27.73843  1.000 21.65894  ? 57  ILE   C CD1   1 
ATOM   3188 N  N     . PRO   C 2 59  ? 4.47908   12.24908  22.36448  1.000 22.46293  ? 58  PRO   C N     1 
ATOM   3189 C  CA    . PRO   C 2 59  ? 4.29611   10.99260  21.63389  1.000 21.71467  ? 58  PRO   C CA    1 
ATOM   3190 C  C     . PRO   C 2 59  ? 4.64391   9.78441   22.48304  1.000 21.32143  ? 58  PRO   C C     1 
ATOM   3191 O  O     . PRO   C 2 59  ? 5.62733   9.78945   23.23812  1.000 24.50512  ? 58  PRO   C O     1 
ATOM   3192 C  CB    . PRO   C 2 59  ? 5.25976   11.12321  20.44528  1.000 25.33648  ? 58  PRO   C CB    1 
ATOM   3193 C  CG    . PRO   C 2 59  ? 5.48208   12.60094  20.30065  1.000 24.84840  ? 58  PRO   C CG    1 
ATOM   3194 C  CD    . PRO   C 2 59  ? 5.42226   13.15679  21.68717  1.000 23.91783  ? 58  PRO   C CD    1 
ATOM   3195 N  N     . GLY   C 2 60  ? 3.85055   8.73205   22.31264  1.000 22.50211  ? 59  GLY   C N     1 
ATOM   3196 C  CA    . GLY   C 2 60  ? 3.91132   7.56004   23.15684  1.000 24.70727  ? 59  GLY   C CA    1 
ATOM   3197 C  C     . GLY   C 2 60  ? 3.06384   7.64525   24.40700  1.000 24.88048  ? 59  GLY   C C     1 
ATOM   3198 O  O     . GLY   C 2 60  ? 2.95656   6.64285   25.12838  1.000 26.20542  ? 59  GLY   C O     1 
ATOM   3199 N  N     . PHE   C 2 61  ? 2.47945   8.80897   24.70477  1.000 20.86152  ? 60  PHE   C N     1 
ATOM   3200 C  CA    . PHE   C 2 61  ? 1.71486   8.95875   25.94439  1.000 23.63143  ? 60  PHE   C CA    1 
ATOM   3201 C  C     . PHE   C 2 61  ? 0.34655   9.60917   25.76456  1.000 21.72982  ? 60  PHE   C C     1 
ATOM   3202 O  O     . PHE   C 2 61  ? -0.66701  8.92500   25.94888  1.000 26.65992  ? 60  PHE   C O     1 
ATOM   3203 C  CB    . PHE   C 2 61  ? 2.52470   9.74248   26.96815  1.000 23.19682  ? 60  PHE   C CB    1 
ATOM   3204 C  CG    . PHE   C 2 61  ? 3.75502   9.02549   27.42063  1.000 24.03855  ? 60  PHE   C CG    1 
ATOM   3205 C  CD1   . PHE   C 2 61  ? 3.69365   8.09609   28.45860  1.000 23.02238  ? 60  PHE   C CD1   1 
ATOM   3206 C  CD2   . PHE   C 2 61  ? 4.97255   9.25400   26.79832  1.000 27.16402  ? 60  PHE   C CD2   1 
ATOM   3207 C  CE1   . PHE   C 2 61  ? 4.83152   7.43249   28.88132  1.000 26.65802  ? 60  PHE   C CE1   1 
ATOM   3208 C  CE2   . PHE   C 2 61  ? 6.12399   8.60442   27.22501  1.000 28.65230  ? 60  PHE   C CE2   1 
ATOM   3209 C  CZ    . PHE   C 2 61  ? 6.04990   7.68407   28.26307  1.000 26.09871  ? 60  PHE   C CZ    1 
ATOM   3210 N  N     . MET   C 2 62  ? 0.27834   10.90755  25.46393  1.000 20.64234  ? 61  MET   C N     1 
ATOM   3211 C  CA    . MET   C 2 62  ? -1.04110  11.53355  25.39119  1.000 23.85795  ? 61  MET   C CA    1 
ATOM   3212 C  C     . MET   C 2 62  ? -1.01145  12.86665  24.64553  1.000 22.58561  ? 61  MET   C C     1 
ATOM   3213 O  O     . MET   C 2 62  ? 0.04161   13.48641  24.46300  1.000 24.37289  ? 61  MET   C O     1 
ATOM   3214 C  CB    . MET   C 2 62  ? -1.61549  11.74041  26.80747  1.000 19.74026  ? 61  MET   C CB    1 
ATOM   3215 C  CG    . MET   C 2 62  ? -1.22463  13.06423  27.45139  1.000 23.05622  ? 61  MET   C CG    1 
ATOM   3216 S  SD    . MET   C 2 62  ? 0.53874   13.20933  27.81514  1.000 26.92210  ? 61  MET   C SD    1 
ATOM   3217 C  CE    . MET   C 2 62  ? 0.66974   14.99414  27.76313  1.000 26.44340  ? 61  MET   C CE    1 
ATOM   3218 N  N     . CYS   C 2 63  ? -2.19721  13.29575  24.21982  1.000 22.85368  ? 62  CYS   C N     1 
ATOM   3219 C  CA    . CYS   C 2 63  ? -2.46156  14.66326  23.78503  1.000 21.96419  ? 62  CYS   C CA    1 
ATOM   3220 C  C     . CYS   C 2 63  ? -3.31283  15.36271  24.84287  1.000 24.71421  ? 62  CYS   C C     1 
ATOM   3221 O  O     . CYS   C 2 63  ? -4.40316  14.88374  25.16551  1.000 26.63125  ? 62  CYS   C O     1 
ATOM   3222 C  CB    . CYS   C 2 63  ? -3.21284  14.67874  22.44561  1.000 23.84965  ? 62  CYS   C CB    1 
ATOM   3223 S  SG    . CYS   C 2 63  ? -2.40750  13.76296  21.09036  1.000 28.47128  ? 62  CYS   C SG    1 
ATOM   3224 N  N     . GLN   C 2 64  ? -2.85963  16.51391  25.34479  1.000 23.69680  ? 63  GLN   C N     1 
ATOM   3225 C  CA    . GLN   C 2 64  ? -3.58026  17.20810  26.40427  1.000 24.31036  ? 63  GLN   C CA    1 
ATOM   3226 C  C     . GLN   C 2 64  ? -4.01956  18.58265  25.93171  1.000 27.75396  ? 63  GLN   C C     1 
ATOM   3227 O  O     . GLN   C 2 64  ? -3.23696  19.31480  25.31928  1.000 25.69290  ? 63  GLN   C O     1 
ATOM   3228 C  CB    . GLN   C 2 64  ? -2.71870  17.32881  27.67303  1.000 26.66090  ? 63  GLN   C CB    1 
ATOM   3229 C  CG    . GLN   C 2 64  ? -3.34920  18.15479  28.78406  1.000 20.24709  ? 63  GLN   C CG    1 
ATOM   3230 C  CD    . GLN   C 2 64  ? -2.46559  18.20488  29.99666  1.000 24.29605  ? 63  GLN   C CD    1 
ATOM   3231 O  OE1   . GLN   C 2 64  ? -1.54035  17.40319  30.13409  1.000 24.73889  ? 63  GLN   C OE1   1 
ATOM   3232 N  NE2   . GLN   C 2 64  ? -2.73768  19.14806  30.89144  1.000 26.33956  ? 63  GLN   C NE2   1 
ATOM   3233 N  N     . GLY   C 2 65  ? -5.27111  18.94413  26.24937  1.000 26.82610  ? 64  GLY   C N     1 
ATOM   3234 C  CA    . GLY   C 2 65  ? -5.80240  20.24086  25.85058  1.000 27.65557  ? 64  GLY   C CA    1 
ATOM   3235 C  C     . GLY   C 2 65  ? -6.84076  20.81118  26.80485  1.000 27.98768  ? 64  GLY   C C     1 
ATOM   3236 O  O     . GLY   C 2 65  ? -6.86143  20.45119  27.98609  1.000 33.45269  ? 64  GLY   C O     1 
ATOM   3237 N  N     . GLY   C 2 66  ? -7.67441  21.73785  26.31876  1.000 30.95017  ? 65  GLY   C N     1 
ATOM   3238 C  CA    . GLY   C 2 66  ? -8.83531  22.21267  27.05922  1.000 29.32818  ? 65  GLY   C CA    1 
ATOM   3239 C  C     . GLY   C 2 66  ? -8.66916  23.47445  27.89331  1.000 33.61634  ? 65  GLY   C C     1 
ATOM   3240 O  O     . GLY   C 2 66  ? -9.59920  23.82655  28.63937  1.000 35.57612  ? 65  GLY   C O     1 
ATOM   3241 N  N     . ASP   C 2 67  ? -7.53310  24.16682  27.80899  1.000 38.63555  ? 66  ASP   C N     1 
ATOM   3242 C  CA    . ASP   C 2 67  ? -7.37578  25.45921  28.47760  1.000 33.46726  ? 66  ASP   C CA    1 
ATOM   3243 C  C     . ASP   C 2 67  ? -7.88193  26.53310  27.52162  1.000 43.13185  ? 66  ASP   C C     1 
ATOM   3244 O  O     . ASP   C 2 67  ? -7.13336  27.06829  26.70375  1.000 43.37445  ? 66  ASP   C O     1 
ATOM   3245 C  CB    . ASP   C 2 67  ? -5.92861  25.70016  28.87874  1.000 32.91753  ? 66  ASP   C CB    1 
ATOM   3246 C  CG    . ASP   C 2 67  ? -5.70628  27.08255  29.48039  1.000 42.69651  ? 66  ASP   C CG    1 
ATOM   3247 O  OD1   . ASP   C 2 67  ? -6.68991  27.83029  29.69030  1.000 43.10455  ? 66  ASP   C OD1   1 
ATOM   3248 O  OD2   . ASP   C 2 67  ? -4.53789  27.42695  29.74765  1.000 40.30014  ? 66  ASP   C OD2   1 
ATOM   3249 N  N     . PHE   C 2 68  ? -9.16311  26.87023  27.63601  1.000 37.09038  ? 67  PHE   C N     1 
ATOM   3250 C  CA    . PHE   C 2 68  ? -9.75661  27.88540  26.77876  1.000 40.38107  ? 67  PHE   C CA    1 
ATOM   3251 C  C     . PHE   C 2 68  ? -9.84669  29.25200  27.43862  1.000 42.66697  ? 67  PHE   C C     1 
ATOM   3252 O  O     . PHE   C 2 68  ? -10.35674 30.18415  26.81368  1.000 44.20920  ? 67  PHE   C O     1 
ATOM   3253 C  CB    . PHE   C 2 68  ? -11.15007 27.45439  26.30718  1.000 40.78855  ? 67  PHE   C CB    1 
ATOM   3254 C  CG    . PHE   C 2 68  ? -12.12095 27.16286  27.42849  1.000 44.50778  ? 67  PHE   C CG    1 
ATOM   3255 C  CD1   . PHE   C 2 68  ? -12.76073 28.19238  28.11390  1.000 39.69211  ? 67  PHE   C CD1   1 
ATOM   3256 C  CD2   . PHE   C 2 68  ? -12.40707 25.85529  27.78249  1.000 40.06879  ? 67  PHE   C CD2   1 
ATOM   3257 C  CE1   . PHE   C 2 68  ? -13.65229 27.91528  29.13826  1.000 47.23129  ? 67  PHE   C CE1   1 
ATOM   3258 C  CE2   . PHE   C 2 68  ? -13.29714 25.57770  28.80372  1.000 44.07422  ? 67  PHE   C CE2   1 
ATOM   3259 C  CZ    . PHE   C 2 68  ? -13.92433 26.60821  29.48173  1.000 44.14919  ? 67  PHE   C CZ    1 
ATOM   3260 N  N     . THR   C 2 69  ? -9.38362  29.40145  28.67683  1.000 37.95866  ? 68  THR   C N     1 
ATOM   3261 C  CA    . THR   C 2 69  ? -9.38940  30.71067  29.32050  1.000 49.13885  ? 68  THR   C CA    1 
ATOM   3262 C  C     . THR   C 2 69  ? -8.03740  31.41193  29.25268  1.000 51.57612  ? 68  THR   C C     1 
ATOM   3263 O  O     . THR   C 2 69  ? -7.99030  32.63872  29.11754  1.000 58.43984  ? 68  THR   C O     1 
ATOM   3264 C  CB    . THR   C 2 69  ? -9.84638  30.60437  30.78808  1.000 49.04238  ? 68  THR   C CB    1 
ATOM   3265 O  OG1   . THR   C 2 69  ? -8.84255  29.95680  31.58440  1.000 43.30869  ? 68  THR   C OG1   1 
ATOM   3266 C  CG2   . THR   C 2 69  ? -11.15373 29.83153  30.88550  1.000 44.12851  ? 68  THR   C CG2   1 
ATOM   3267 N  N     . ARG   C 2 70  ? -6.92938  30.67515  29.32859  1.000 48.97874  ? 69  ARG   C N     1 
ATOM   3268 C  CA    . ARG   C 2 70  ? -5.61168  31.28669  29.23887  1.000 51.25116  ? 69  ARG   C CA    1 
ATOM   3269 C  C     . ARG   C 2 70  ? -4.79420  30.79545  28.05139  1.000 51.02209  ? 69  ARG   C C     1 
ATOM   3270 O  O     . ARG   C 2 70  ? -3.78937  31.43134  27.71383  1.000 57.65960  ? 69  ARG   C O     1 
ATOM   3271 C  CB    . ARG   C 2 70  ? -4.83318  31.06779  30.54733  1.000 52.04616  ? 69  ARG   C CB    1 
ATOM   3272 C  CG    . ARG   C 2 70  ? -5.63756  31.49007  31.77579  1.000 53.55550  ? 69  ARG   C CG    1 
ATOM   3273 C  CD    . ARG   C 2 70  ? -4.80733  32.25646  32.79285  1.000 61.41807  ? 69  ARG   C CD    1 
ATOM   3274 N  NE    . ARG   C 2 70  ? -4.14038  31.36699  33.73532  1.000 63.98716  ? 69  ARG   C NE    1 
ATOM   3275 C  CZ    . ARG   C 2 70  ? -4.67920  30.92929  34.86609  1.000 60.83955  ? 69  ARG   C CZ    1 
ATOM   3276 N  NH1   . ARG   C 2 70  ? -5.90111  31.28200  35.23317  1.000 63.77893  ? 69  ARG   C NH1   1 
ATOM   3277 N  NH2   . ARG   C 2 70  ? -3.97528  30.11430  35.64720  1.000 62.42908  ? 69  ARG   C NH2   1 
ATOM   3278 N  N     . HIS   C 2 71  ? -5.20599  29.70352  27.40155  1.000 47.71147  ? 70  HIS   C N     1 
ATOM   3279 C  CA    . HIS   C 2 71  ? -4.61576  29.22268  26.14571  1.000 48.06026  ? 70  HIS   C CA    1 
ATOM   3280 C  C     . HIS   C 2 71  ? -3.12021  28.95005  26.25886  1.000 52.94352  ? 70  HIS   C C     1 
ATOM   3281 O  O     . HIS   C 2 71  ? -2.40038  28.99621  25.25872  1.000 53.74732  ? 70  HIS   C O     1 
ATOM   3282 C  CB    . HIS   C 2 71  ? -4.88856  30.19828  24.99802  1.000 49.28872  ? 70  HIS   C CB    1 
ATOM   3283 C  CG    . HIS   C 2 71  ? -6.34324  30.40720  24.72947  1.000 44.61323  ? 70  HIS   C CG    1 
ATOM   3284 N  ND1   . HIS   C 2 71  ? -7.08618  29.54090  23.95831  1.000 47.51784  ? 70  HIS   C ND1   1 
ATOM   3285 C  CD2   . HIS   C 2 71  ? -7.19933  31.36878  25.14902  1.000 42.75397  ? 70  HIS   C CD2   1 
ATOM   3286 C  CE1   . HIS   C 2 71  ? -8.33575  29.96519  23.90224  1.000 44.96934  ? 70  HIS   C CE1   1 
ATOM   3287 N  NE2   . HIS   C 2 71  ? -8.43058  31.07328  24.61647  1.000 50.12510  ? 70  HIS   C NE2   1 
ATOM   3288 N  N     . ASN   C 2 72  ? -2.63041  28.65179  27.46667  1.000 52.74819  ? 71  ASN   C N     1 
ATOM   3289 C  CA    . ASN   C 2 72  ? -1.21047  28.36150  27.61973  1.000 50.51400  ? 71  ASN   C CA    1 
ATOM   3290 C  C     . ASN   C 2 72  ? -0.93503  27.17109  28.53234  1.000 49.61702  ? 71  ASN   C C     1 
ATOM   3291 O  O     . ASN   C 2 72  ? 0.22469   26.96017  28.91767  1.000 54.69711  ? 71  ASN   C O     1 
ATOM   3292 C  CB    . ASN   C 2 72  ? -0.46513  29.59943  28.13414  1.000 52.65585  ? 71  ASN   C CB    1 
ATOM   3293 C  CG    . ASN   C 2 72  ? -0.78375  29.92695  29.58381  1.000 53.81306  ? 71  ASN   C CG    1 
ATOM   3294 O  OD1   . ASN   C 2 72  ? -1.76956  29.44765  30.15505  1.000 53.09444  ? 71  ASN   C OD1   1 
ATOM   3295 N  ND2   . ASN   C 2 72  ? 0.05428   30.75912  30.18627  1.000 50.28645  ? 71  ASN   C ND2   1 
ATOM   3296 N  N     . GLY   C 2 73  ? -1.95008  26.39459  28.89815  1.000 46.08964  ? 72  GLY   C N     1 
ATOM   3297 C  CA    . GLY   C 2 73  ? -1.75618  25.21784  29.71540  1.000 39.82000  ? 72  GLY   C CA    1 
ATOM   3298 C  C     . GLY   C 2 73  ? -2.01328  25.40321  31.19716  1.000 44.16431  ? 72  GLY   C C     1 
ATOM   3299 O  O     . GLY   C 2 73  ? -1.91970  24.42326  31.94519  1.000 36.78472  ? 72  GLY   C O     1 
ATOM   3300 N  N     . THR   C 2 74  ? -2.33436  26.61830  31.64583  1.000 42.45007  ? 73  THR   C N     1 
ATOM   3301 C  CA    . THR   C 2 74  ? -2.49827  26.89249  33.06526  1.000 47.29052  ? 73  THR   C CA    1 
ATOM   3302 C  C     . THR   C 2 74  ? -3.92968  27.21905  33.45952  1.000 45.92276  ? 73  THR   C C     1 
ATOM   3303 O  O     . THR   C 2 74  ? -4.19665  27.39376  34.64916  1.000 51.96285  ? 73  THR   C O     1 
ATOM   3304 C  CB    . THR   C 2 74  ? -1.58852  28.04726  33.49704  1.000 50.87265  ? 73  THR   C CB    1 
ATOM   3305 O  OG1   . THR   C 2 74  ? -2.19171  29.29177  33.12853  1.000 53.50458  ? 73  THR   C OG1   1 
ATOM   3306 C  CG2   . THR   C 2 74  ? -0.22935  27.93274  32.82953  1.000 51.31076  ? 73  THR   C CG2   1 
ATOM   3307 N  N     . GLY   C 2 75  ? -4.85442  27.30238  32.50894  1.000 44.42897  ? 74  GLY   C N     1 
ATOM   3308 C  CA    . GLY   C 2 75  ? -6.20395  27.72308  32.82951  1.000 40.58266  ? 74  GLY   C CA    1 
ATOM   3309 C  C     . GLY   C 2 75  ? -7.28688  26.72781  32.46782  1.000 44.43074  ? 74  GLY   C C     1 
ATOM   3310 O  O     . GLY   C 2 75  ? -7.03826  25.52065  32.39059  1.000 38.86700  ? 74  GLY   C O     1 
ATOM   3311 N  N     . GLY   C 2 76  ? -8.49203  27.23121  32.23900  1.000 39.50354  ? 75  GLY   C N     1 
ATOM   3312 C  CA    . GLY   C 2 76  ? -9.67404  26.43181  32.02235  1.000 44.05501  ? 75  GLY   C CA    1 
ATOM   3313 C  C     . GLY   C 2 76  ? -10.58983 26.42424  33.24349  1.000 40.30990  ? 75  GLY   C C     1 
ATOM   3314 O  O     . GLY   C 2 76  ? -10.17390 26.71208  34.36863  1.000 41.08323  ? 75  GLY   C O     1 
ATOM   3315 N  N     . LYS   C 2 77  ? -11.85111 26.09191  33.00583  1.000 39.98370  ? 76  LYS   C N     1 
ATOM   3316 C  CA    . LYS   C 2 77  ? -12.80609 26.01554  34.10725  1.000 44.33845  ? 76  LYS   C CA    1 
ATOM   3317 C  C     . LYS   C 2 77  ? -13.96330 25.11630  33.70630  1.000 40.07355  ? 76  LYS   C C     1 
ATOM   3318 O  O     . LYS   C 2 77  ? -14.21816 24.89313  32.52149  1.000 40.93515  ? 76  LYS   C O     1 
ATOM   3319 C  CB    . LYS   C 2 77  ? -13.31865 27.40313  34.50988  1.000 43.75664  ? 76  LYS   C CB    1 
ATOM   3320 C  CG    . LYS   C 2 77  ? -14.02790 28.15939  33.39479  1.000 49.38182  ? 76  LYS   C CG    1 
ATOM   3321 C  CD    . LYS   C 2 77  ? -14.62973 29.46522  33.91309  1.000 53.01444  ? 76  LYS   C CD    1 
ATOM   3322 C  CE    . LYS   C 2 77  ? -15.02501 30.38091  32.77068  1.000 58.32938  ? 76  LYS   C CE    1 
ATOM   3323 N  NZ    . LYS   C 2 77  ? -15.78067 29.63930  31.72977  1.000 52.99290  ? 76  LYS   C NZ    1 
ATOM   3324 N  N     . SER   C 2 78  ? -14.67013 24.61143  34.71671  1.000 42.95682  ? 77  SER   C N     1 
ATOM   3325 C  CA    . SER   C 2 78  ? -15.81049 23.73559  34.49632  1.000 40.75882  ? 77  SER   C CA    1 
ATOM   3326 C  C     . SER   C 2 78  ? -17.11335 24.53083  34.42477  1.000 41.64806  ? 77  SER   C C     1 
ATOM   3327 O  O     . SER   C 2 78  ? -17.17221 25.71857  34.74630  1.000 42.95970  ? 77  SER   C O     1 
ATOM   3328 C  CB    . SER   C 2 78  ? -15.91244 22.69037  35.60633  1.000 46.05653  ? 77  SER   C CB    1 
ATOM   3329 O  OG    . SER   C 2 78  ? -16.49951 23.24532  36.77603  1.000 47.80967  ? 77  SER   C OG    1 
ATOM   3330 N  N     . ILE   C 2 79  ? -18.17552 23.84465  33.99469  1.000 44.02337  ? 78  ILE   C N     1 
ATOM   3331 C  CA    . ILE   C 2 79  ? -19.51022 24.43461  34.00350  1.000 43.40630  ? 78  ILE   C CA    1 
ATOM   3332 C  C     . ILE   C 2 79  ? -20.06597 24.58339  35.41047  1.000 47.28925  ? 78  ILE   C C     1 
ATOM   3333 O  O     . ILE   C 2 79  ? -21.08980 25.25201  35.59355  1.000 42.55847  ? 78  ILE   C O     1 
ATOM   3334 C  CB    . ILE   C 2 79  ? -20.50852 23.60434  33.17072  1.000 45.82428  ? 78  ILE   C CB    1 
ATOM   3335 C  CG1   . ILE   C 2 79  ? -20.80952 22.27751  33.87113  1.000 44.88525  ? 78  ILE   C CG1   1 
ATOM   3336 C  CG2   . ILE   C 2 79  ? -19.98721 23.38540  31.74890  1.000 38.01130  ? 78  ILE   C CG2   1 
ATOM   3337 C  CD1   . ILE   C 2 79  ? -21.90499 21.46321  33.20592  1.000 40.74288  ? 78  ILE   C CD1   1 
ATOM   3338 N  N     . TYR   C 2 80  ? -19.42059 23.97231  36.40402  1.000 43.23137  ? 79  TYR   C N     1 
ATOM   3339 C  CA    . TYR   C 2 80  ? -19.86524 24.00669  37.79248  1.000 46.09786  ? 79  TYR   C CA    1 
ATOM   3340 C  C     . TYR   C 2 80  ? -19.13549 25.05581  38.61440  1.000 49.26527  ? 79  TYR   C C     1 
ATOM   3341 O  O     . TYR   C 2 80  ? -19.39565 25.18313  39.81834  1.000 53.12860  ? 79  TYR   C O     1 
ATOM   3342 C  CB    . TYR   C 2 80  ? -19.67115 22.63008  38.43831  1.000 41.82723  ? 79  TYR   C CB    1 
ATOM   3343 C  CG    . TYR   C 2 80  ? -20.19748 21.49784  37.59504  1.000 44.87460  ? 79  TYR   C CG    1 
ATOM   3344 C  CD1   . TYR   C 2 80  ? -21.55042 21.40811  37.29940  1.000 41.96177  ? 79  TYR   C CD1   1 
ATOM   3345 C  CD2   . TYR   C 2 80  ? -19.34865 20.51655  37.09238  1.000 41.97634  ? 79  TYR   C CD2   1 
ATOM   3346 C  CE1   . TYR   C 2 80  ? -22.05025 20.38138  36.53437  1.000 47.11250  ? 79  TYR   C CE1   1 
ATOM   3347 C  CE2   . TYR   C 2 80  ? -19.84718 19.47748  36.31109  1.000 39.19565  ? 79  TYR   C CE2   1 
ATOM   3348 C  CZ    . TYR   C 2 80  ? -21.19853 19.41844  36.03721  1.000 40.67701  ? 79  TYR   C CZ    1 
ATOM   3349 O  OH    . TYR   C 2 80  ? -21.72714 18.40560  35.26955  1.000 38.94299  ? 79  TYR   C OH    1 
ATOM   3350 N  N     . GLY   C 2 81  ? -18.23881 25.80837  37.99285  1.000 47.07186  ? 80  GLY   C N     1 
ATOM   3351 C  CA    . GLY   C 2 81  ? -17.30978 26.66896  38.68137  1.000 49.06526  ? 80  GLY   C CA    1 
ATOM   3352 C  C     . GLY   C 2 81  ? -15.89206 26.37450  38.25296  1.000 47.45505  ? 80  GLY   C C     1 
ATOM   3353 O  O     . GLY   C 2 81  ? -15.63419 25.54934  37.37933  1.000 45.47518  ? 80  GLY   C O     1 
ATOM   3354 N  N     . GLU   C 2 82  ? -14.95734 27.07203  38.89728  1.000 48.50993  ? 81  GLU   C N     1 
ATOM   3355 C  CA    . GLU   C 2 82  ? -13.53994 26.92030  38.57986  1.000 55.49469  ? 81  GLU   C CA    1 
ATOM   3356 C  C     . GLU   C 2 82  ? -13.09856 25.46050  38.65305  1.000 52.48136  ? 81  GLU   C C     1 
ATOM   3357 O  O     . GLU   C 2 82  ? -12.58741 24.90260  37.67538  1.000 50.22106  ? 81  GLU   C O     1 
ATOM   3358 C  CB    . GLU   C 2 82  ? -12.70657 27.78473  39.52752  1.000 54.93934  ? 81  GLU   C CB    1 
ATOM   3359 C  CG    . GLU   C 2 82  ? -12.24984 29.10010  38.92302  1.000 65.37998  ? 81  GLU   C CG    1 
ATOM   3360 C  CD    . GLU   C 2 82  ? -10.85477 29.01284  38.33114  1.000 67.88615  ? 81  GLU   C CD    1 
ATOM   3361 O  OE1   . GLU   C 2 82  ? -9.97352  28.39417  38.97058  1.000 66.23915  ? 81  GLU   C OE1   1 
ATOM   3362 O  OE2   . GLU   C 2 82  ? -10.64052 29.56021  37.22641  1.000 69.07073  ? 81  GLU   C OE2   1 
ATOM   3363 N  N     . LYS   C 2 83  ? -13.28848 24.82720  39.81055  1.000 50.01389  ? 82  LYS   C N     1 
ATOM   3364 C  CA    . LYS   C 2 83  ? -12.88033 23.44878  40.03699  1.000 47.95577  ? 82  LYS   C CA    1 
ATOM   3365 C  C     . LYS   C 2 83  ? -14.06668 22.61532  40.50375  1.000 49.27772  ? 82  LYS   C C     1 
ATOM   3366 O  O     . LYS   C 2 83  ? -15.05736 23.14534  41.01666  1.000 46.81597  ? 82  LYS   C O     1 
ATOM   3367 C  CB    . LYS   C 2 83  ? -11.76510 23.35354  41.08594  1.000 42.01967  ? 82  LYS   C CB    1 
ATOM   3368 C  CG    . LYS   C 2 83  ? -10.59906 24.29246  40.87235  1.000 46.58597  ? 82  LYS   C CG    1 
ATOM   3369 C  CD    . LYS   C 2 83  ? -9.93356  24.07898  39.52459  1.000 52.29102  ? 82  LYS   C CD    1 
ATOM   3370 C  CE    . LYS   C 2 83  ? -8.82447  25.11318  39.30069  1.000 57.34341  ? 82  LYS   C CE    1 
ATOM   3371 N  NZ    . LYS   C 2 83  ? -8.44975  25.27753  37.86389  1.000 56.19868  ? 82  LYS   C NZ    1 
ATOM   3372 N  N     . PHE   C 2 84  ? -13.95696 21.29616  40.32538  1.000 43.75913  ? 83  PHE   C N     1 
ATOM   3373 C  CA    . PHE   C 2 84  ? -14.93227 20.38818  40.91452  1.000 37.89600  ? 83  PHE   C CA    1 
ATOM   3374 C  C     . PHE   C 2 84  ? -14.25868 19.06713  41.26524  1.000 43.64046  ? 83  PHE   C C     1 
ATOM   3375 O  O     . PHE   C 2 84  ? -13.13625 18.77365  40.84490  1.000 35.87851  ? 83  PHE   C O     1 
ATOM   3376 C  CB    . PHE   C 2 84  ? -16.17522 20.19069  40.02338  1.000 36.53217  ? 83  PHE   C CB    1 
ATOM   3377 C  CG    . PHE   C 2 84  ? -15.96199 19.36498  38.76492  1.000 41.50331  ? 83  PHE   C CG    1 
ATOM   3378 C  CD1   . PHE   C 2 84  ? -15.39567 19.92622  37.63064  1.000 39.85590  ? 83  PHE   C CD1   1 
ATOM   3379 C  CD2   . PHE   C 2 84  ? -16.42878 18.05653  38.69040  1.000 37.87061  ? 83  PHE   C CD2   1 
ATOM   3380 C  CE1   . PHE   C 2 84  ? -15.25033 19.18055  36.44800  1.000 36.16758  ? 83  PHE   C CE1   1 
ATOM   3381 C  CE2   . PHE   C 2 84  ? -16.28695 17.30138  37.52332  1.000 38.02071  ? 83  PHE   C CE2   1 
ATOM   3382 C  CZ    . PHE   C 2 84  ? -15.69106 17.86331  36.39703  1.000 37.37375  ? 83  PHE   C CZ    1 
ATOM   3383 N  N     . GLU   C 2 85  ? -14.95916 18.29127  42.08183  1.000 36.95432  ? 84  GLU   C N     1 
ATOM   3384 C  CA    . GLU   C 2 85  ? -14.38216 17.14248  42.74942  1.000 33.69733  ? 84  GLU   C CA    1 
ATOM   3385 C  C     . GLU   C 2 85  ? -14.16505 15.98072  41.77939  1.000 31.39735  ? 84  GLU   C C     1 
ATOM   3386 O  O     . GLU   C 2 85  ? -14.79365 15.88113  40.71685  1.000 32.34775  ? 84  GLU   C O     1 
ATOM   3387 C  CB    . GLU   C 2 85  ? -15.29755 16.69614  43.89549  1.000 36.25846  ? 84  GLU   C CB    1 
ATOM   3388 C  CG    . GLU   C 2 85  ? -16.61496 16.08158  43.42839  1.000 40.62195  ? 84  GLU   C CG    1 
ATOM   3389 C  CD    . GLU   C 2 85  ? -17.67593 17.10578  43.00186  1.000 45.74381  ? 84  GLU   C CD    1 
ATOM   3390 O  OE1   . GLU   C 2 85  ? -17.38360 18.32203  42.94667  1.000 44.06487  ? 84  GLU   C OE1   1 
ATOM   3391 O  OE2   . GLU   C 2 85  ? -18.81746 16.68086  42.72688  1.000 48.61931  ? 84  GLU   C OE2   1 
ATOM   3392 N  N     . ASP   C 2 86  ? -13.26150 15.08963  42.17689  1.000 34.23837  ? 85  ASP   C N     1 
ATOM   3393 C  CA    . ASP   C 2 86  ? -13.10616 13.79896  41.51480  1.000 33.74758  ? 85  ASP   C CA    1 
ATOM   3394 C  C     . ASP   C 2 86  ? -14.35294 12.95485  41.74780  1.000 38.89263  ? 85  ASP   C C     1 
ATOM   3395 O  O     . ASP   C 2 86  ? -14.59863 12.50346  42.87191  1.000 39.73688  ? 85  ASP   C O     1 
ATOM   3396 C  CB    . ASP   C 2 86  ? -11.86506 13.08551  42.04385  1.000 29.10497  ? 85  ASP   C CB    1 
ATOM   3397 C  CG    . ASP   C 2 86  ? -10.59064 13.81129  41.69922  1.000 33.33964  ? 85  ASP   C CG    1 
ATOM   3398 O  OD1   . ASP   C 2 86  ? -10.50274 14.32615  40.56517  1.000 35.12194  ? 85  ASP   C OD1   1 
ATOM   3399 O  OD2   . ASP   C 2 86  ? -9.67322  13.86177  42.54579  1.000 36.61775  ? 85  ASP   C OD2   1 
ATOM   3400 N  N     . GLU   C 2 87  ? -15.12888 12.73991  40.68312  1.000 30.63282  ? 86  GLU   C N     1 
ATOM   3401 C  CA    . GLU   C 2 87  ? -16.41858 12.06155  40.79196  1.000 37.34301  ? 86  GLU   C CA    1 
ATOM   3402 C  C     . GLU   C 2 87  ? -16.26712 10.61968  41.27924  1.000 41.38477  ? 86  GLU   C C     1 
ATOM   3403 O  O     . GLU   C 2 87  ? -16.96894 10.19311  42.20763  1.000 36.21894  ? 86  GLU   C O     1 
ATOM   3404 C  CB    . GLU   C 2 87  ? -17.13492 12.11086  39.44575  1.000 36.87916  ? 86  GLU   C CB    1 
ATOM   3405 C  CG    . GLU   C 2 87  ? -18.54870 11.56213  39.46614  1.000 34.88927  ? 86  GLU   C CG    1 
ATOM   3406 C  CD    . GLU   C 2 87  ? -19.34389 11.97249  38.24496  1.000 41.18181  ? 86  GLU   C CD    1 
ATOM   3407 O  OE1   . GLU   C 2 87  ? -18.73498 12.44089  37.25794  1.000 34.07662  ? 86  GLU   C OE1   1 
ATOM   3408 O  OE2   . GLU   C 2 87  ? -20.58636 11.83564  38.26519  1.000 35.03726  ? 86  GLU   C OE2   1 
ATOM   3409 N  N     . ASN   C 2 88  ? -15.38755 9.84765   40.64329  1.000 35.41716  ? 87  ASN   C N     1 
ATOM   3410 C  CA    . ASN   C 2 88  ? -15.04790 8.48391   41.04071  1.000 27.66532  ? 87  ASN   C CA    1 
ATOM   3411 C  C     . ASN   C 2 88  ? -13.93745 8.00083   40.11844  1.000 35.07093  ? 87  ASN   C C     1 
ATOM   3412 O  O     . ASN   C 2 88  ? -13.61301 8.64399   39.11715  1.000 30.97991  ? 87  ASN   C O     1 
ATOM   3413 C  CB    . ASN   C 2 88  ? -16.24086 7.52181   40.97285  1.000 30.58282  ? 87  ASN   C CB    1 
ATOM   3414 C  CG    . ASN   C 2 88  ? -16.81358 7.38873   39.56931  1.000 28.85757  ? 87  ASN   C CG    1 
ATOM   3415 O  OD1   . ASN   C 2 88  ? -16.12079 6.95968   38.62936  1.000 31.50335  ? 87  ASN   C OD1   1 
ATOM   3416 N  ND2   . ASN   C 2 88  ? -18.08613 7.73691   39.41629  1.000 30.45513  ? 87  ASN   C ND2   1 
ATOM   3417 N  N     . PHE   C 2 89  ? -13.39101 6.83785   40.44833  1.000 30.23421  ? 88  PHE   C N     1 
ATOM   3418 C  CA    . PHE   C 2 89  ? -12.33148 6.20221   39.67502  1.000 29.33452  ? 88  PHE   C CA    1 
ATOM   3419 C  C     . PHE   C 2 89  ? -12.75004 4.80620   39.22190  1.000 28.29698  ? 88  PHE   C C     1 
ATOM   3420 O  O     . PHE   C 2 89  ? -11.94889 3.86581   39.24791  1.000 31.77884  ? 88  PHE   C O     1 
ATOM   3421 C  CB    . PHE   C 2 89  ? -11.04364 6.15220   40.49047  1.000 27.55741  ? 88  PHE   C CB    1 
ATOM   3422 C  CG    . PHE   C 2 89  ? -10.54158 7.50753   40.91597  1.000 35.80614  ? 88  PHE   C CG    1 
ATOM   3423 C  CD1   . PHE   C 2 89  ? -9.91297  8.35012   40.00329  1.000 30.77689  ? 88  PHE   C CD1   1 
ATOM   3424 C  CD2   . PHE   C 2 89  ? -10.69679 7.94672   42.22694  1.000 38.29077  ? 88  PHE   C CD2   1 
ATOM   3425 C  CE1   . PHE   C 2 89  ? -9.44472  9.60287   40.39389  1.000 29.86113  ? 88  PHE   C CE1   1 
ATOM   3426 C  CE2   . PHE   C 2 89  ? -10.22704 9.20092   42.62574  1.000 38.00642  ? 88  PHE   C CE2   1 
ATOM   3427 C  CZ    . PHE   C 2 89  ? -9.59088  10.02872  41.70613  1.000 37.63826  ? 88  PHE   C CZ    1 
ATOM   3428 N  N     . ILE   C 2 90  ? -14.01924 4.65841   38.81256  1.000 30.11818  ? 89  ILE   C N     1 
ATOM   3429 C  CA    . ILE   C 2 90  ? -14.49743 3.38163   38.28049  1.000 27.07589  ? 89  ILE   C CA    1 
ATOM   3430 C  C     . ILE   C 2 90  ? -13.67080 2.97664   37.06745  1.000 30.78526  ? 89  ILE   C C     1 
ATOM   3431 O  O     . ILE   C 2 90  ? -13.18849 1.84278   36.97539  1.000 30.71841  ? 89  ILE   C O     1 
ATOM   3432 C  CB    . ILE   C 2 90  ? -15.99581 3.45331   37.92495  1.000 28.59175  ? 89  ILE   C CB    1 
ATOM   3433 C  CG1   . ILE   C 2 90  ? -16.85082 3.66547   39.18459  1.000 30.47882  ? 89  ILE   C CG1   1 
ATOM   3434 C  CG2   . ILE   C 2 90  ? -16.44176 2.19401   37.19682  1.000 29.78663  ? 89  ILE   C CG2   1 
ATOM   3435 C  CD1   . ILE   C 2 90  ? -18.30562 3.95212   38.87222  1.000 32.21060  ? 89  ILE   C CD1   1 
ATOM   3436 N  N     . LEU   C 2 91  ? -13.49220 3.90038   36.12648  1.000 32.01406  ? 90  LEU   C N     1 
ATOM   3437 C  CA    . LEU   C 2 91  ? -12.84185 3.59916   34.85409  1.000 29.65848  ? 90  LEU   C CA    1 
ATOM   3438 C  C     . LEU   C 2 91  ? -11.33286 3.80870   34.94531  1.000 33.38963  ? 90  LEU   C C     1 
ATOM   3439 O  O     . LEU   C 2 91  ? -10.85432 4.68575   35.66657  1.000 29.45089  ? 90  LEU   C O     1 
ATOM   3440 C  CB    . LEU   C 2 91  ? -13.42704 4.46688   33.74317  1.000 29.76547  ? 90  LEU   C CB    1 
ATOM   3441 C  CG    . LEU   C 2 91  ? -14.91915 4.20716   33.53392  1.000 32.17050  ? 90  LEU   C CG    1 
ATOM   3442 C  CD1   . LEU   C 2 91  ? -15.50513 5.17902   32.54149  1.000 32.90024  ? 90  LEU   C CD1   1 
ATOM   3443 C  CD2   . LEU   C 2 91  ? -15.15764 2.77371   33.07165  1.000 34.47011  ? 90  LEU   C CD2   1 
ATOM   3444 N  N     . LYS   C 2 92  ? -10.58386 3.00925   34.18888  1.000 33.18202  ? 91  LYS   C N     1 
ATOM   3445 C  CA    . LYS   C 2 92  ? -9.13412  3.01117   34.26686  1.000 31.11302  ? 91  LYS   C CA    1 
ATOM   3446 C  C     . LYS   C 2 92  ? -8.52321  3.45504   32.94163  1.000 25.08343  ? 91  LYS   C C     1 
ATOM   3447 O  O     . LYS   C 2 92  ? -9.18150  3.47177   31.89996  1.000 26.65354  ? 91  LYS   C O     1 
ATOM   3448 C  CB    . LYS   C 2 92  ? -8.60269  1.62232   34.62514  1.000 36.09462  ? 91  LYS   C CB    1 
ATOM   3449 C  CG    . LYS   C 2 92  ? -9.28075  0.99006   35.82154  1.000 35.21351  ? 91  LYS   C CG    1 
ATOM   3450 C  CD    . LYS   C 2 92  ? -9.07787  1.82910   37.06306  1.000 39.02871  ? 91  LYS   C CD    1 
ATOM   3451 C  CE    . LYS   C 2 92  ? -9.80707  1.21554   38.24823  1.000 45.43400  ? 91  LYS   C CE    1 
ATOM   3452 N  NZ    . LYS   C 2 92  ? -9.82198  2.13079   39.43458  1.000 45.11902  ? 91  LYS   C NZ    1 
ATOM   3453 N  N     . HIS   C 2 93  ? -7.22989  3.77848   33.00219  1.000 25.84265  ? 92  HIS   C N     1 
ATOM   3454 C  CA    . HIS   C 2 93  ? -6.45550  4.19425   31.82941  1.000 23.42503  ? 92  HIS   C CA    1 
ATOM   3455 C  C     . HIS   C 2 93  ? -5.92957  2.92664   31.15597  1.000 25.55814  ? 92  HIS   C C     1 
ATOM   3456 O  O     . HIS   C 2 93  ? -4.82037  2.45740   31.43967  1.000 29.14822  ? 92  HIS   C O     1 
ATOM   3457 C  CB    . HIS   C 2 93  ? -5.32839  5.13943   32.23885  1.000 26.55600  ? 92  HIS   C CB    1 
ATOM   3458 C  CG    . HIS   C 2 93  ? -5.79489  6.39606   32.91124  1.000 27.69268  ? 92  HIS   C CG    1 
ATOM   3459 N  ND1   . HIS   C 2 93  ? -6.02372  6.46874   34.27223  1.000 28.01150  ? 92  HIS   C ND1   1 
ATOM   3460 C  CD2   . HIS   C 2 93  ? -6.05556  7.63242   32.41904  1.000 27.34604  ? 92  HIS   C CD2   1 
ATOM   3461 C  CE1   . HIS   C 2 93  ? -6.42201  7.68976   34.58582  1.000 25.57048  ? 92  HIS   C CE1   1 
ATOM   3462 N  NE2   . HIS   C 2 93  ? -6.44688  8.41755   33.48426  1.000 25.68645  ? 92  HIS   C NE2   1 
ATOM   3463 N  N     . THR   C 2 94  ? -6.73343  2.36670   30.25068  1.000 28.33889  ? 93  THR   C N     1 
ATOM   3464 C  CA    . THR   C 2 94  ? -6.53367  1.00569   29.76198  1.000 28.61525  ? 93  THR   C CA    1 
ATOM   3465 C  C     . THR   C 2 94  ? -5.78111  0.93299   28.44153  1.000 27.79902  ? 93  THR   C C     1 
ATOM   3466 O  O     . THR   C 2 94  ? -5.25874  -0.13465  28.11128  1.000 29.33897  ? 93  THR   C O     1 
ATOM   3467 C  CB    . THR   C 2 94  ? -7.88002  0.28205   29.58412  1.000 28.83949  ? 93  THR   C CB    1 
ATOM   3468 O  OG1   . THR   C 2 94  ? -8.71522  1.01906   28.67854  1.000 32.30175  ? 93  THR   C OG1   1 
ATOM   3469 C  CG2   . THR   C 2 94  ? -8.58590  0.13482   30.90670  1.000 29.18806  ? 93  THR   C CG2   1 
ATOM   3470 N  N     . GLY   C 2 95  ? -5.72545  2.01807   27.67971  1.000 30.07036  ? 94  GLY   C N     1 
ATOM   3471 C  CA    . GLY   C 2 95  ? -5.07387  1.97842   26.39483  1.000 29.36878  ? 94  GLY   C CA    1 
ATOM   3472 C  C     . GLY   C 2 95  ? -5.32703  3.20810   25.55239  1.000 31.91778  ? 94  GLY   C C     1 
ATOM   3473 O  O     . GLY   C 2 95  ? -5.95435  4.17800   25.98959  1.000 29.60348  ? 94  GLY   C O     1 
ATOM   3474 N  N     . PRO   C 2 96  ? -4.79691  3.19691   24.32604  1.000 28.27692  ? 95  PRO   C N     1 
ATOM   3475 C  CA    . PRO   C 2 96  ? -5.05856  4.28728   23.37707  1.000 25.46550  ? 95  PRO   C CA    1 
ATOM   3476 C  C     . PRO   C 2 96  ? -6.54625  4.60396   23.28592  1.000 29.31212  ? 95  PRO   C C     1 
ATOM   3477 O  O     . PRO   C 2 96  ? -7.38522  3.70439   23.23076  1.000 33.99861  ? 95  PRO   C O     1 
ATOM   3478 C  CB    . PRO   C 2 96  ? -4.53026  3.73757   22.04372  1.000 27.46013  ? 95  PRO   C CB    1 
ATOM   3479 C  CG    . PRO   C 2 96  ? -3.53931  2.68162   22.43268  1.000 28.63833  ? 95  PRO   C CG    1 
ATOM   3480 C  CD    . PRO   C 2 96  ? -3.95405  2.13014   23.77164  1.000 26.98178  ? 95  PRO   C CD    1 
ATOM   3481 N  N     . GLY   C 2 97  ? -6.86450  5.89920   23.26182  1.000 25.59221  ? 96  GLY   C N     1 
ATOM   3482 C  CA    . GLY   C 2 97  ? -8.22460  6.37197   23.09762  1.000 30.19770  ? 96  GLY   C CA    1 
ATOM   3483 C  C     . GLY   C 2 97  ? -8.91354  6.78606   24.37952  1.000 22.24546  ? 96  GLY   C C     1 
ATOM   3484 O  O     . GLY   C 2 97  ? -9.97022  7.42493   24.31747  1.000 28.54653  ? 96  GLY   C O     1 
ATOM   3485 N  N     . ILE   C 2 98  ? -8.33702  6.47217   25.53333  1.000 24.93546  ? 97  ILE   C N     1 
ATOM   3486 C  CA    . ILE   C 2 98  ? -8.97688  6.83034   26.79756  1.000 24.37850  ? 97  ILE   C CA    1 
ATOM   3487 C  C     . ILE   C 2 98  ? -8.98490  8.34957   26.95772  1.000 27.59590  ? 97  ILE   C C     1 
ATOM   3488 O  O     . ILE   C 2 98  ? -7.98030  9.02753   26.68558  1.000 25.90446  ? 97  ILE   C O     1 
ATOM   3489 C  CB    . ILE   C 2 98  ? -8.26626  6.11643   27.95567  1.000 24.75089  ? 97  ILE   C CB    1 
ATOM   3490 C  CG1   . ILE   C 2 98  ? -8.62780  4.62513   27.94513  1.000 30.45084  ? 97  ILE   C CG1   1 
ATOM   3491 C  CG2   . ILE   C 2 98  ? -8.55103  6.76953   29.33329  1.000 27.28133  ? 97  ILE   C CG2   1 
ATOM   3492 C  CD1   . ILE   C 2 98  ? -10.08345 4.33151   28.35080  1.000 29.25547  ? 97  ILE   C CD1   1 
ATOM   3493 N  N     . LEU   C 2 99  ? -10.13245 8.89603   27.37988  1.000 23.85372  ? 98  LEU   C N     1 
ATOM   3494 C  CA    . LEU   C 2 99  ? -10.30694 10.32501  27.62864  1.000 24.17042  ? 98  LEU   C CA    1 
ATOM   3495 C  C     . LEU   C 2 99  ? -10.45642 10.56172  29.12217  1.000 27.26092  ? 98  LEU   C C     1 
ATOM   3496 O  O     . LEU   C 2 99  ? -11.31543 9.94867   29.76629  1.000 25.02343  ? 98  LEU   C O     1 
ATOM   3497 C  CB    . LEU   C 2 99  ? -11.53539 10.85539  26.89114  1.000 24.32642  ? 98  LEU   C CB    1 
ATOM   3498 C  CG    . LEU   C 2 99  ? -11.88138 12.33883  26.98558  1.000 25.02062  ? 98  LEU   C CG    1 
ATOM   3499 C  CD1   . LEU   C 2 99  ? -10.81032 13.17020  26.29024  1.000 25.45278  ? 98  LEU   C CD1   1 
ATOM   3500 C  CD2   . LEU   C 2 99  ? -13.26301 12.57857  26.35968  1.000 30.35416  ? 98  LEU   C CD2   1 
ATOM   3501 N  N     . SER   C 2 100 ? -9.64238  11.46186  29.66700  1.000 23.00270  ? 99  SER   C N     1 
ATOM   3502 C  CA    . SER   C 2 100 ? -9.53012  11.56247  31.10999  1.000 22.62553  ? 99  SER   C CA    1 
ATOM   3503 C  C     . SER   C 2 100 ? -9.21910  13.00910  31.46914  1.000 28.74211  ? 99  SER   C C     1 
ATOM   3504 O  O     . SER   C 2 100 ? -8.82627  13.81002  30.61183  1.000 24.15177  ? 99  SER   C O     1 
ATOM   3505 C  CB    . SER   C 2 100 ? -8.48348  10.56267  31.60304  1.000 19.53885  ? 99  SER   C CB    1 
ATOM   3506 O  OG    . SER   C 2 100 ? -8.16006  10.69333  32.98287  1.000 25.84742  ? 99  SER   C OG    1 
ATOM   3507 N  N     . MET   C 2 101 ? -9.43271  13.35335  32.73785  1.000 22.48460  ? 100 MET   C N     1 
ATOM   3508 C  CA    . MET   C 2 101 ? -9.30850  14.73596  33.18781  1.000 22.95366  ? 100 MET   C CA    1 
ATOM   3509 C  C     . MET   C 2 101 ? -7.89711  15.02964  33.66354  1.000 23.90865  ? 100 MET   C C     1 
ATOM   3510 O  O     . MET   C 2 101 ? -7.33341  14.26821  34.45687  1.000 24.17774  ? 100 MET   C O     1 
ATOM   3511 C  CB    . MET   C 2 101 ? -10.29551 15.02268  34.33144  1.000 28.98643  ? 100 MET   C CB    1 
ATOM   3512 C  CG    . MET   C 2 101 ? -11.74759 14.98670  33.90831  1.000 26.57058  ? 100 MET   C CG    1 
ATOM   3513 S  SD    . MET   C 2 101 ? -12.14706 16.22393  32.66277  1.000 29.40746  ? 100 MET   C SD    1 
ATOM   3514 C  CE    . MET   C 2 101 ? -11.94523 17.75994  33.55893  1.000 28.57983  ? 100 MET   C CE    1 
ATOM   3515 N  N     . ALA   C 2 102 ? -7.33188  16.14208  33.18768  1.000 25.59804  ? 101 ALA   C N     1 
ATOM   3516 C  CA    . ALA   C 2 102 ? -6.12276  16.67813  33.78810  1.000 24.73614  ? 101 ALA   C CA    1 
ATOM   3517 C  C     . ALA   C 2 102 ? -6.49850  17.39528  35.08169  1.000 24.47464  ? 101 ALA   C C     1 
ATOM   3518 O  O     . ALA   C 2 102 ? -7.66807  17.72606  35.31261  1.000 27.89686  ? 101 ALA   C O     1 
ATOM   3519 C  CB    . ALA   C 2 102 ? -5.40654  17.62902  32.81941  1.000 26.82150  ? 101 ALA   C CB    1 
ATOM   3520 N  N     . ASN   C 2 103 ? -5.51393  17.59002  35.95210  1.000 27.39382  ? 102 ASN   C N     1 
ATOM   3521 C  CA    . ASN   C 2 103 ? -5.81080  18.19433  37.24481  1.000 29.35881  ? 102 ASN   C CA    1 
ATOM   3522 C  C     . ASN   C 2 103 ? -4.51756  18.61374  37.92251  1.000 35.20647  ? 102 ASN   C C     1 
ATOM   3523 O  O     . ASN   C 2 103 ? -3.41244  18.26387  37.49086  1.000 31.94642  ? 102 ASN   C O     1 
ATOM   3524 C  CB    . ASN   C 2 103 ? -6.61717  17.23639  38.13699  1.000 31.12295  ? 102 ASN   C CB    1 
ATOM   3525 C  CG    . ASN   C 2 103 ? -5.84170  15.99143  38.52132  1.000 25.74759  ? 102 ASN   C CG    1 
ATOM   3526 O  OD1   . ASN   C 2 103 ? -4.72179  16.06595  39.00481  1.000 26.24814  ? 102 ASN   C OD1   1 
ATOM   3527 N  ND2   . ASN   C 2 103 ? -6.44091  14.83611  38.29508  1.000 29.95141  ? 102 ASN   C ND2   1 
ATOM   3528 N  N     . ALA   C 2 104 ? -4.67742  19.35494  39.01733  1.000 35.09040  ? 103 ALA   C N     1 
ATOM   3529 C  CA    . ALA   C 2 104 ? -3.56596  19.83269  39.82596  1.000 32.76539  ? 103 ALA   C CA    1 
ATOM   3530 C  C     . ALA   C 2 104 ? -3.51500  19.13339  41.17864  1.000 39.83013  ? 103 ALA   C C     1 
ATOM   3531 O  O     . ALA   C 2 104 ? -3.05961  19.71504  42.16814  1.000 46.54618  ? 103 ALA   C O     1 
ATOM   3532 C  CB    . ALA   C 2 104 ? -3.66613  21.34357  40.02381  1.000 38.29817  ? 103 ALA   C CB    1 
ATOM   3533 N  N     . GLY   C 2 105 ? -3.99039  17.89264  41.23821  1.000 34.85210  ? 104 GLY   C N     1 
ATOM   3534 C  CA    . GLY   C 2 105 ? -4.16313  17.19565  42.49284  1.000 33.38409  ? 104 GLY   C CA    1 
ATOM   3535 C  C     . GLY   C 2 105 ? -5.62330  16.89950  42.77222  1.000 33.63788  ? 104 GLY   C C     1 
ATOM   3536 O  O     . GLY   C 2 105 ? -6.50985  17.22831  41.97773  1.000 33.03836  ? 104 GLY   C O     1 
ATOM   3537 N  N     . PRO   C 2 106 ? -5.89961  16.29631  43.93220  1.000 35.30045  ? 105 PRO   C N     1 
ATOM   3538 C  CA    . PRO   C 2 106 ? -7.26591  15.85065  44.23819  1.000 39.24368  ? 105 PRO   C CA    1 
ATOM   3539 C  C     . PRO   C 2 106 ? -8.30582  16.96019  44.11863  1.000 31.67896  ? 105 PRO   C C     1 
ATOM   3540 O  O     . PRO   C 2 106 ? -8.09771  18.09287  44.56445  1.000 37.51190  ? 105 PRO   C O     1 
ATOM   3541 C  CB    . PRO   C 2 106 ? -7.15121  15.34309  45.68088  1.000 36.06896  ? 105 PRO   C CB    1 
ATOM   3542 C  CG    . PRO   C 2 106 ? -5.74393  14.89351  45.80033  1.000 38.03762  ? 105 PRO   C CG    1 
ATOM   3543 C  CD    . PRO   C 2 106 ? -4.92601  15.84131  44.94102  1.000 39.36718  ? 105 PRO   C CD    1 
ATOM   3544 N  N     . ASN   C 2 107 ? -9.43494  16.61223  43.49931  1.000 30.62620  ? 106 ASN   C N     1 
ATOM   3545 C  CA    . ASN   C 2 107 ? -10.60737 17.48415  43.38924  1.000 35.73109  ? 106 ASN   C CA    1 
ATOM   3546 C  C     . ASN   C 2 107 ? -10.25781 18.85018  42.79751  1.000 44.69512  ? 106 ASN   C C     1 
ATOM   3547 O  O     . ASN   C 2 107 ? -10.60837 19.89969  43.34570  1.000 39.83248  ? 106 ASN   C O     1 
ATOM   3548 C  CB    . ASN   C 2 107 ? -11.29157 17.63571  44.75272  1.000 35.86200  ? 106 ASN   C CB    1 
ATOM   3549 C  CG    . ASN   C 2 107 ? -11.63281 16.30486  45.36569  1.000 35.91105  ? 106 ASN   C CG    1 
ATOM   3550 O  OD1   . ASN   C 2 107 ? -12.36840 15.51829  44.77956  1.000 37.54809  ? 106 ASN   C OD1   1 
ATOM   3551 N  ND2   . ASN   C 2 107 ? -11.07204 16.02707  46.53595  1.000 45.43548  ? 106 ASN   C ND2   1 
ATOM   3552 N  N     . THR   C 2 108 ? -9.55612  18.83903  41.66311  1.000 34.88897  ? 107 THR   C N     1 
ATOM   3553 C  CA    . THR   C 2 108 ? -9.22934  20.08685  40.97928  1.000 39.10986  ? 107 THR   C CA    1 
ATOM   3554 C  C     . THR   C 2 108 ? -9.53585  19.98387  39.49526  1.000 36.07659  ? 107 THR   C C     1 
ATOM   3555 O  O     . THR   C 2 108 ? -8.80868  20.51924  38.65594  1.000 34.40137  ? 107 THR   C O     1 
ATOM   3556 C  CB    . THR   C 2 108 ? -7.76714  20.48994  41.19082  1.000 36.64823  ? 107 THR   C CB    1 
ATOM   3557 O  OG1   . THR   C 2 108 ? -6.89780  19.45215  40.71931  1.000 36.97202  ? 107 THR   C OG1   1 
ATOM   3558 C  CG2   . THR   C 2 108 ? -7.47639  20.76923  42.66270  1.000 31.21575  ? 107 THR   C CG2   1 
ATOM   3559 N  N     . ASN   C 2 109 ? -10.61886 19.30233  39.14148  1.000 33.33862  ? 108 ASN   C N     1 
ATOM   3560 C  CA    . ASN   C 2 109 ? -11.00269 19.23046  37.74127  1.000 26.72707  ? 108 ASN   C CA    1 
ATOM   3561 C  C     . ASN   C 2 109 ? -11.58240 20.56050  37.28840  1.000 36.31337  ? 108 ASN   C C     1 
ATOM   3562 O  O     . ASN   C 2 109 ? -12.37749 21.18314  37.99633  1.000 34.01916  ? 108 ASN   C O     1 
ATOM   3563 C  CB    . ASN   C 2 109 ? -12.01567 18.11482  37.51810  1.000 29.20235  ? 108 ASN   C CB    1 
ATOM   3564 C  CG    . ASN   C 2 109 ? -11.52632 16.79462  38.04654  1.000 42.55420  ? 108 ASN   C CG    1 
ATOM   3565 O  OD1   . ASN   C 2 109 ? -10.68355 16.13995  37.41526  1.000 31.57019  ? 108 ASN   C OD1   1 
ATOM   3566 N  ND2   . ASN   C 2 109 ? -12.01557 16.40358  39.23639  1.000 34.86096  ? 108 ASN   C ND2   1 
ATOM   3567 N  N     . GLY   C 2 110 ? -11.15662 21.00282  36.10796  1.000 32.03171  ? 109 GLY   C N     1 
ATOM   3568 C  CA    . GLY   C 2 110 ? -11.74423 22.15221  35.44460  1.000 32.73187  ? 109 GLY   C CA    1 
ATOM   3569 C  C     . GLY   C 2 110 ? -12.21443 21.79044  34.05342  1.000 31.68791  ? 109 GLY   C C     1 
ATOM   3570 O  O     . GLY   C 2 110 ? -13.26001 21.16421  33.89081  1.000 31.13490  ? 109 GLY   C O     1 
ATOM   3571 N  N     . SER   C 2 111 ? -11.44828 22.16672  33.02854  1.000 30.85610  ? 110 SER   C N     1 
ATOM   3572 C  CA    . SER   C 2 111 ? -11.76501 21.77652  31.66460  1.000 30.70338  ? 110 SER   C CA    1 
ATOM   3573 C  C     . SER   C 2 111 ? -10.62806 21.04441  30.95830  1.000 26.72574  ? 110 SER   C C     1 
ATOM   3574 O  O     . SER   C 2 111 ? -10.88354 20.37053  29.95978  1.000 28.57096  ? 110 SER   C O     1 
ATOM   3575 C  CB    . SER   C 2 111 ? -12.15656 23.00584  30.82441  1.000 37.73686  ? 110 SER   C CB    1 
ATOM   3576 O  OG    . SER   C 2 111 ? -11.06815 23.91242  30.71520  1.000 31.93566  ? 110 SER   C OG    1 
ATOM   3577 N  N     . GLN   C 2 112 ? -9.40597  21.13141  31.46405  1.000 30.54166  ? 111 GLN   C N     1 
ATOM   3578 C  CA    . GLN   C 2 112 ? -8.28562  20.43570  30.84517  1.000 27.24337  ? 111 GLN   C CA    1 
ATOM   3579 C  C     . GLN   C 2 112 ? -8.47479  18.92282  30.89843  1.000 32.22764  ? 111 GLN   C C     1 
ATOM   3580 O  O     . GLN   C 2 112 ? -8.93144  18.36194  31.90151  1.000 29.40264  ? 111 GLN   C O     1 
ATOM   3581 C  CB    . GLN   C 2 112 ? -6.99320  20.84436  31.52345  1.000 35.16709  ? 111 GLN   C CB    1 
ATOM   3582 C  CG    . GLN   C 2 112 ? -6.55522  22.23369  31.09630  1.000 36.85415  ? 111 GLN   C CG    1 
ATOM   3583 C  CD    . GLN   C 2 112 ? -5.07953  22.43596  31.26747  1.000 34.75978  ? 111 GLN   C CD    1 
ATOM   3584 O  OE1   . GLN   C 2 112 ? -4.27616  21.55398  30.94639  1.000 32.41683  ? 111 GLN   C OE1   1 
ATOM   3585 N  NE2   . GLN   C 2 112 ? -4.69839  23.59552  31.78993  1.000 33.72676  ? 111 GLN   C NE2   1 
ATOM   3586 N  N     . PHE   C 2 113 ? -8.11745  18.26814  29.79801  1.000 24.52705  ? 112 PHE   C N     1 
ATOM   3587 C  CA    . PHE   C 2 113 ? -8.34867  16.84679  29.58441  1.000 24.15835  ? 112 PHE   C CA    1 
ATOM   3588 C  C     . PHE   C 2 113 ? -7.17161  16.30798  28.80058  1.000 26.59251  ? 112 PHE   C C     1 
ATOM   3589 O  O     . PHE   C 2 113 ? -6.37683  17.07344  28.23766  1.000 23.90315  ? 112 PHE   C O     1 
ATOM   3590 C  CB    . PHE   C 2 113 ? -9.63591  16.59896  28.79424  1.000 26.60277  ? 112 PHE   C CB    1 
ATOM   3591 C  CG    . PHE   C 2 113 ? -9.58716  17.18714  27.41329  1.000 23.20285  ? 112 PHE   C CG    1 
ATOM   3592 C  CD1   . PHE   C 2 113 ? -9.97988  18.49613  27.19797  1.000 25.37208  ? 112 PHE   C CD1   1 
ATOM   3593 C  CD2   . PHE   C 2 113 ? -9.06454  16.46099  26.34268  1.000 27.89010  ? 112 PHE   C CD2   1 
ATOM   3594 C  CE1   . PHE   C 2 113 ? -9.89495  19.05478  25.92120  1.000 30.01132  ? 112 PHE   C CE1   1 
ATOM   3595 C  CE2   . PHE   C 2 113 ? -8.97385  17.02067  25.07581  1.000 28.74909  ? 112 PHE   C CE2   1 
ATOM   3596 C  CZ    . PHE   C 2 113 ? -9.39040  18.31303  24.86486  1.000 34.53038  ? 112 PHE   C CZ    1 
ATOM   3597 N  N     . PHE   C 2 114 ? -7.06354  14.97902  28.74650  1.000 22.85571  ? 113 PHE   C N     1 
ATOM   3598 C  CA    . PHE   C 2 114 ? -6.06033  14.38548  27.87040  1.000 24.70981  ? 113 PHE   C CA    1 
ATOM   3599 C  C     . PHE   C 2 114 ? -6.64487  13.16166  27.18278  1.000 25.30043  ? 113 PHE   C C     1 
ATOM   3600 O  O     . PHE   C 2 114 ? -7.55379  12.49889  27.70665  1.000 22.90413  ? 113 PHE   C O     1 
ATOM   3601 C  CB    . PHE   C 2 114 ? -4.73921  14.05843  28.60895  1.000 23.01721  ? 113 PHE   C CB    1 
ATOM   3602 C  CG    . PHE   C 2 114 ? -4.86729  13.07435  29.75843  1.000 20.15249  ? 113 PHE   C CG    1 
ATOM   3603 C  CD1   . PHE   C 2 114 ? -5.44414  13.45378  30.97696  1.000 22.18636  ? 113 PHE   C CD1   1 
ATOM   3604 C  CD2   . PHE   C 2 114 ? -4.37976  11.78494  29.62473  1.000 20.77363  ? 113 PHE   C CD2   1 
ATOM   3605 C  CE1   . PHE   C 2 114 ? -5.54186  12.55191  32.03952  1.000 22.91962  ? 113 PHE   C CE1   1 
ATOM   3606 C  CE2   . PHE   C 2 114 ? -4.46225  10.86856  30.65168  1.000 24.21153  ? 113 PHE   C CE2   1 
ATOM   3607 C  CZ    . PHE   C 2 114 ? -5.05456  11.25240  31.90236  1.000 21.94355  ? 113 PHE   C CZ    1 
ATOM   3608 N  N     . ILE   C 2 115 ? -6.15774  12.91089  25.96551  1.000 22.59226  ? 114 ILE   C N     1 
ATOM   3609 C  CA    . ILE   C 2 115 ? -6.47601  11.71115  25.19823  1.000 22.22916  ? 114 ILE   C CA    1 
ATOM   3610 C  C     . ILE   C 2 115 ? -5.24072  10.82471  25.18610  1.000 21.99618  ? 114 ILE   C C     1 
ATOM   3611 O  O     . ILE   C 2 115 ? -4.18007  11.23442  24.68860  1.000 22.86918  ? 114 ILE   C O     1 
ATOM   3612 C  CB    . ILE   C 2 115 ? -6.88789  12.03860  23.75858  1.000 21.03856  ? 114 ILE   C CB    1 
ATOM   3613 C  CG1   . ILE   C 2 115 ? -7.92124  13.16955  23.70903  1.000 26.08895  ? 114 ILE   C CG1   1 
ATOM   3614 C  CG2   . ILE   C 2 115 ? -7.35575  10.77066  23.05960  1.000 24.94550  ? 114 ILE   C CG2   1 
ATOM   3615 C  CD1   . ILE   C 2 115 ? -8.16600  13.72219  22.29878  1.000 25.91781  ? 114 ILE   C CD1   1 
ATOM   3616 N  N     . CYS   C 2 116 ? -5.37907  9.59796   25.67510  1.000 20.07641  ? 115 CYS   C N     1 
ATOM   3617 C  CA    . CYS   C 2 116 ? -4.22755  8.71291   25.76733  1.000 23.91710  ? 115 CYS   C CA    1 
ATOM   3618 C  C     . CYS   C 2 116 ? -3.88917  8.16571   24.38949  1.000 23.93682  ? 115 CYS   C C     1 
ATOM   3619 O  O     . CYS   C 2 116 ? -4.78001  7.86702   23.59727  1.000 23.89509  ? 115 CYS   C O     1 
ATOM   3620 C  CB    . CYS   C 2 116 ? -4.51763  7.55628   26.71241  1.000 25.44498  ? 115 CYS   C CB    1 
ATOM   3621 S  SG    . CYS   C 2 116 ? -4.81764  8.04826   28.43775  1.000 25.93491  ? 115 CYS   C SG    1 
ATOM   3622 N  N     . THR   C 2 117 ? -2.59357  8.00061   24.11200  1.000 22.95674  ? 116 THR   C N     1 
ATOM   3623 C  CA    . THR   C 2 117 ? -2.17676  7.27040   22.91794  1.000 26.34786  ? 116 THR   C CA    1 
ATOM   3624 C  C     . THR   C 2 117 ? -1.53642  5.94022   23.26336  1.000 27.03461  ? 116 THR   C C     1 
ATOM   3625 O  O     . THR   C 2 117 ? -1.05328  5.22814   22.37140  1.000 27.76962  ? 116 THR   C O     1 
ATOM   3626 C  CB    . THR   C 2 117 ? -1.22375  8.11343   22.07583  1.000 23.92914  ? 116 THR   C CB    1 
ATOM   3627 O  OG1   . THR   C 2 117 ? -0.09990  8.51212   22.88189  1.000 24.92832  ? 116 THR   C OG1   1 
ATOM   3628 C  CG2   . THR   C 2 117 ? -1.94216  9.33046   21.57957  1.000 25.19865  ? 116 THR   C CG2   1 
ATOM   3629 N  N     . ALA   C 2 118 ? -1.54063  5.58703   24.53718  1.000 26.27541  ? 117 ALA   C N     1 
ATOM   3630 C  CA    . ALA   C 2 118 ? -0.99637  4.33859   25.04283  1.000 24.53771  ? 117 ALA   C CA    1 
ATOM   3631 C  C     . ALA   C 2 118 ? -1.65358  4.08678   26.38699  1.000 26.49553  ? 117 ALA   C C     1 
ATOM   3632 O  O     . ALA   C 2 118 ? -2.38874  4.93245   26.91364  1.000 26.88428  ? 117 ALA   C O     1 
ATOM   3633 C  CB    . ALA   C 2 118 ? 0.52515   4.38183   25.17870  1.000 26.98652  ? 117 ALA   C CB    1 
ATOM   3634 N  N     . LYS   C 2 119 ? -1.39609  2.91206   26.93384  1.000 27.72838  ? 118 LYS   C N     1 
ATOM   3635 C  CA    . LYS   C 2 119 ? -1.87763  2.61959   28.27321  1.000 32.43434  ? 118 LYS   C CA    1 
ATOM   3636 C  C     . LYS   C 2 119 ? -1.03530  3.37961   29.29549  1.000 26.46737  ? 118 LYS   C C     1 
ATOM   3637 O  O     . LYS   C 2 119 ? 0.19964   3.29681   29.29693  1.000 28.57733  ? 118 LYS   C O     1 
ATOM   3638 C  CB    . LYS   C 2 119 ? -1.84193  1.11118   28.52319  1.000 30.76695  ? 118 LYS   C CB    1 
ATOM   3639 C  CG    . LYS   C 2 119 ? -2.20851  0.69424   29.93382  1.000 35.91547  ? 118 LYS   C CG    1 
ATOM   3640 C  CD    . LYS   C 2 119 ? -2.20899  -0.82691  30.04113  1.000 39.78231  ? 118 LYS   C CD    1 
ATOM   3641 C  CE    . LYS   C 2 119 ? -1.96946  -1.29290  31.46020  1.000 51.07122  ? 118 LYS   C CE    1 
ATOM   3642 N  NZ    . LYS   C 2 119 ? -2.64806  -2.60974  31.65268  1.000 59.99878  ? 118 LYS   C NZ    1 
ATOM   3643 N  N     . THR   C 2 120 ? -1.70813  4.14639   30.15385  1.000 23.38279  ? 119 THR   C N     1 
ATOM   3644 C  CA    . THR   C 2 120 ? -1.04908  4.95912   31.18539  1.000 24.21097  ? 119 THR   C CA    1 
ATOM   3645 C  C     . THR   C 2 120 ? -1.61766  4.61320   32.57013  1.000 30.30452  ? 119 THR   C C     1 
ATOM   3646 O  O     . THR   C 2 120 ? -2.15178  5.46681   33.27904  1.000 27.54945  ? 119 THR   C O     1 
ATOM   3647 C  CB    . THR   C 2 120 ? -1.23240  6.45408   30.91280  1.000 26.99457  ? 119 THR   C CB    1 
ATOM   3648 O  OG1   . THR   C 2 120 ? -2.63654  6.76651   30.90530  1.000 24.80463  ? 119 THR   C OG1   1 
ATOM   3649 C  CG2   . THR   C 2 120 ? -0.63356  6.82972   29.54720  1.000 26.16860  ? 119 THR   C CG2   1 
ATOM   3650 N  N     . GLU   C 2 121 ? -1.42544  3.35780   32.98510  1.000 29.10123  ? 120 GLU   C N     1 
ATOM   3651 C  CA    . GLU   C 2 121 ? -2.11072  2.83513   34.16674  1.000 33.68231  ? 120 GLU   C CA    1 
ATOM   3652 C  C     . GLU   C 2 121 ? -1.69228  3.51721   35.46924  1.000 31.03915  ? 120 GLU   C C     1 
ATOM   3653 O  O     . GLU   C 2 121 ? -2.47417  3.49921   36.43149  1.000 29.44972  ? 120 GLU   C O     1 
ATOM   3654 C  CB    . GLU   C 2 121 ? -1.88164  1.31916   34.26178  1.000 31.24810  ? 120 GLU   C CB    1 
ATOM   3655 C  CG    . GLU   C 2 121 ? -0.47224  0.90587   34.69679  1.000 34.05867  ? 120 GLU   C CG    1 
ATOM   3656 C  CD    . GLU   C 2 121 ? 0.57683   0.96529   33.58665  1.000 32.98171  ? 120 GLU   C CD    1 
ATOM   3657 O  OE1   . GLU   C 2 121 ? 0.24113   1.29711   32.43848  1.000 33.47589  ? 120 GLU   C OE1   1 
ATOM   3658 O  OE2   . GLU   C 2 121 ? 1.75735   0.67644   33.88095  1.000 46.07501  ? 120 GLU   C OE2   1 
ATOM   3659 N  N     . TRP   C 2 122 ? -0.49898  4.12155   35.53467  1.000 30.77277  ? 121 TRP   C N     1 
ATOM   3660 C  CA    . TRP   C 2 122 ? -0.07757  4.81447   36.75230  1.000 31.67136  ? 121 TRP   C CA    1 
ATOM   3661 C  C     . TRP   C 2 122 ? -0.94798  6.02595   37.07613  1.000 29.51230  ? 121 TRP   C C     1 
ATOM   3662 O  O     . TRP   C 2 122 ? -0.88901  6.53933   38.20122  1.000 31.30529  ? 121 TRP   C O     1 
ATOM   3663 C  CB    . TRP   C 2 122 ? 1.39066   5.23230   36.64493  1.000 29.35325  ? 121 TRP   C CB    1 
ATOM   3664 C  CG    . TRP   C 2 122 ? 1.68100   6.20576   35.54661  1.000 31.41360  ? 121 TRP   C CG    1 
ATOM   3665 C  CD1   . TRP   C 2 122 ? 1.70728   7.56551   35.64441  1.000 28.20376  ? 121 TRP   C CD1   1 
ATOM   3666 C  CD2   . TRP   C 2 122 ? 1.99558   5.89123   34.17486  1.000 29.67283  ? 121 TRP   C CD2   1 
ATOM   3667 N  NE1   . TRP   C 2 122 ? 2.01128   8.11888   34.41735  1.000 31.17542  ? 121 TRP   C NE1   1 
ATOM   3668 C  CE2   . TRP   C 2 122 ? 2.19533   7.11225   33.50205  1.000 28.79316  ? 121 TRP   C CE2   1 
ATOM   3669 C  CE3   . TRP   C 2 122 ? 2.13015   4.69683   33.45948  1.000 28.87872  ? 121 TRP   C CE3   1 
ATOM   3670 C  CZ2   . TRP   C 2 122 ? 2.51901   7.17395   32.15206  1.000 29.13494  ? 121 TRP   C CZ2   1 
ATOM   3671 C  CZ3   . TRP   C 2 122 ? 2.45227   4.76231   32.10590  1.000 31.46754  ? 121 TRP   C CZ3   1 
ATOM   3672 C  CH2   . TRP   C 2 122 ? 2.63185   5.99156   31.46937  1.000 31.27839  ? 121 TRP   C CH2   1 
ATOM   3673 N  N     . LEU   C 2 123 ? -1.76019  6.48326   36.13763  1.000 28.27413  ? 122 LEU   C N     1 
ATOM   3674 C  CA    . LEU   C 2 123 ? -2.70310  7.55812   36.40493  1.000 28.81681  ? 122 LEU   C CA    1 
ATOM   3675 C  C     . LEU   C 2 123 ? -4.02408  7.05606   36.96910  1.000 31.18299  ? 122 LEU   C C     1 
ATOM   3676 O  O     . LEU   C 2 123 ? -4.90795  7.86800   37.25762  1.000 32.45822  ? 122 LEU   C O     1 
ATOM   3677 C  CB    . LEU   C 2 123 ? -2.96212  8.35241   35.11833  1.000 28.49990  ? 122 LEU   C CB    1 
ATOM   3678 C  CG    . LEU   C 2 123 ? -1.69944  8.85043   34.39103  1.000 27.54695  ? 122 LEU   C CG    1 
ATOM   3679 C  CD1   . LEU   C 2 123 ? -2.07591  9.49091   33.03556  1.000 28.50616  ? 122 LEU   C CD1   1 
ATOM   3680 C  CD2   . LEU   C 2 123 ? -0.87974  9.82428   35.25167  1.000 32.98964  ? 122 LEU   C CD2   1 
ATOM   3681 N  N     . ASP   C 2 124 ? -4.18819  5.74178   37.09866  1.000 31.14465  ? 123 ASP   C N     1 
ATOM   3682 C  CA    . ASP   C 2 124 ? -5.40911  5.18205   37.66359  1.000 31.00470  ? 123 ASP   C CA    1 
ATOM   3683 C  C     . ASP   C 2 124 ? -5.57047  5.63493   39.10873  1.000 28.56280  ? 123 ASP   C C     1 
ATOM   3684 O  O     . ASP   C 2 124 ? -4.60529  5.66443   39.87681  1.000 35.75217  ? 123 ASP   C O     1 
ATOM   3685 C  CB    . ASP   C 2 124 ? -5.36829  3.65075   37.60147  1.000 32.92069  ? 123 ASP   C CB    1 
ATOM   3686 C  CG    . ASP   C 2 124 ? -5.59878  3.10222   36.19482  1.000 37.02694  ? 123 ASP   C CG    1 
ATOM   3687 O  OD1   . ASP   C 2 124 ? -5.90474  3.88603   35.26832  1.000 31.83381  ? 123 ASP   C OD1   1 
ATOM   3688 O  OD2   . ASP   C 2 124 ? -5.47344  1.86630   36.02388  1.000 34.57427  ? 123 ASP   C OD2   1 
ATOM   3689 N  N     . GLY   C 2 125 ? -6.79514  5.99569   39.47354  1.000 36.32268  ? 124 GLY   C N     1 
ATOM   3690 C  CA    . GLY   C 2 125 ? -7.06468  6.48766   40.81094  1.000 37.58481  ? 124 GLY   C CA    1 
ATOM   3691 C  C     . GLY   C 2 125 ? -6.57374  7.89116   41.08481  1.000 40.30113  ? 124 GLY   C C     1 
ATOM   3692 O  O     . GLY   C 2 125 ? -6.73171  8.37620   42.21225  1.000 43.02841  ? 124 GLY   C O     1 
ATOM   3693 N  N     . LYS   C 2 126 ? -5.98879  8.56261   40.09706  1.000 39.91251  ? 125 LYS   C N     1 
ATOM   3694 C  CA    . LYS   C 2 126 ? -5.55840  9.95128   40.21460  1.000 37.24517  ? 125 LYS   C CA    1 
ATOM   3695 C  C     . LYS   C 2 126 ? -6.28064  10.86875  39.24664  1.000 34.33029  ? 125 LYS   C C     1 
ATOM   3696 O  O     . LYS   C 2 126 ? -6.63703  11.99055  39.60813  1.000 33.74460  ? 125 LYS   C O     1 
ATOM   3697 C  CB    . LYS   C 2 126 ? -4.04685  10.06012  39.99282  1.000 34.70370  ? 125 LYS   C CB    1 
ATOM   3698 C  CG    . LYS   C 2 126 ? -3.22804  9.41304   41.09190  1.000 41.00265  ? 125 LYS   C CG    1 
ATOM   3699 C  CD    . LYS   C 2 126 ? -1.81829  9.09602   40.62425  1.000 42.49078  ? 125 LYS   C CD    1 
ATOM   3700 C  CE    . LYS   C 2 126 ? -1.04287  8.43371   41.75624  1.000 63.24235  ? 125 LYS   C CE    1 
ATOM   3701 N  NZ    . LYS   C 2 126 ? -1.88122  7.39648   42.44318  1.000 54.39686  ? 125 LYS   C NZ    1 
ATOM   3702 N  N     . HIS   C 2 127 ? -6.53000  10.40503  38.03395  1.000 29.13843  ? 126 HIS   C N     1 
ATOM   3703 C  CA    . HIS   C 2 127 ? -7.24175  11.16123  37.02248  1.000 25.14113  ? 126 HIS   C CA    1 
ATOM   3704 C  C     . HIS   C 2 127 ? -8.54108  10.45341  36.71277  1.000 23.60604  ? 126 HIS   C C     1 
ATOM   3705 O  O     . HIS   C 2 127 ? -8.56103  9.23076   36.53972  1.000 29.65834  ? 126 HIS   C O     1 
ATOM   3706 C  CB    . HIS   C 2 127 ? -6.37760  11.29989  35.75515  1.000 24.89756  ? 126 HIS   C CB    1 
ATOM   3707 C  CG    . HIS   C 2 127 ? -5.11971  12.07400  35.99116  1.000 25.19332  ? 126 HIS   C CG    1 
ATOM   3708 N  ND1   . HIS   C 2 127 ? -5.01721  13.42089  35.71938  1.000 24.22878  ? 126 HIS   C ND1   1 
ATOM   3709 C  CD2   . HIS   C 2 127 ? -3.93799  11.70875  36.53716  1.000 23.06403  ? 126 HIS   C CD2   1 
ATOM   3710 C  CE1   . HIS   C 2 127 ? -3.82122  13.84793  36.07514  1.000 24.58563  ? 126 HIS   C CE1   1 
ATOM   3711 N  NE2   . HIS   C 2 127 ? -3.14440  12.82883  36.57235  1.000 25.91757  ? 126 HIS   C NE2   1 
ATOM   3712 N  N     . VAL   C 2 128 ? -9.62984  11.21499  36.65846  1.000 24.71523  ? 127 VAL   C N     1 
ATOM   3713 C  CA    . VAL   C 2 128 ? -10.94708 10.62863  36.42358  1.000 26.55771  ? 127 VAL   C CA    1 
ATOM   3714 C  C     . VAL   C 2 128 ? -11.09774 10.34429  34.93585  1.000 28.31463  ? 127 VAL   C C     1 
ATOM   3715 O  O     . VAL   C 2 128 ? -11.18400 11.27157  34.13122  1.000 24.65519  ? 127 VAL   C O     1 
ATOM   3716 C  CB    . VAL   C 2 128 ? -12.07273 11.53955  36.92228  1.000 27.07176  ? 127 VAL   C CB    1 
ATOM   3717 C  CG1   . VAL   C 2 128 ? -13.42721 10.96754  36.50673  1.000 28.79279  ? 127 VAL   C CG1   1 
ATOM   3718 C  CG2   . VAL   C 2 128 ? -11.96881 11.72330  38.44357  1.000 29.22845  ? 127 VAL   C CG2   1 
ATOM   3719 N  N     . VAL   C 2 129 ? -11.18585 9.06102   34.58220  1.000 25.84689  ? 128 VAL   C N     1 
ATOM   3720 C  CA    . VAL   C 2 129 ? -11.51722 8.63808   33.22494  1.000 26.20395  ? 128 VAL   C CA    1 
ATOM   3721 C  C     . VAL   C 2 129 ? -13.01565 8.75756   33.01221  1.000 32.07726  ? 128 VAL   C C     1 
ATOM   3722 O  O     . VAL   C 2 129 ? -13.80846 8.30971   33.85669  1.000 32.81384  ? 128 VAL   C O     1 
ATOM   3723 C  CB    . VAL   C 2 129 ? -11.05151 7.19663   32.97708  1.000 24.23632  ? 128 VAL   C CB    1 
ATOM   3724 C  CG1   . VAL   C 2 129 ? -11.51909 6.72695   31.61539  1.000 26.15171  ? 128 VAL   C CG1   1 
ATOM   3725 C  CG2   . VAL   C 2 129 ? -9.52935  7.10464   33.10382  1.000 22.79341  ? 128 VAL   C CG2   1 
ATOM   3726 N  N     . PHE   C 2 130 ? -13.41438 9.32245   31.86854  1.000 26.11184  ? 129 PHE   C N     1 
ATOM   3727 C  CA    . PHE   C 2 130 ? -14.82446 9.57348   31.62263  1.000 31.25010  ? 129 PHE   C CA    1 
ATOM   3728 C  C     . PHE   C 2 130 ? -15.25698 9.38390   30.17586  1.000 32.70943  ? 129 PHE   C C     1 
ATOM   3729 O  O     . PHE   C 2 130 ? -16.43404 9.61773   29.87072  1.000 34.55823  ? 129 PHE   C O     1 
ATOM   3730 C  CB    . PHE   C 2 130 ? -15.18820 10.99474  32.08658  1.000 28.12995  ? 129 PHE   C CB    1 
ATOM   3731 C  CG    . PHE   C 2 130 ? -14.52695 12.08532  31.28772  1.000 31.02926  ? 129 PHE   C CG    1 
ATOM   3732 C  CD1   . PHE   C 2 130 ? -13.24010 12.50790  31.59137  1.000 29.47873  ? 129 PHE   C CD1   1 
ATOM   3733 C  CD2   . PHE   C 2 130 ? -15.19551 12.68596  30.23406  1.000 27.77177  ? 129 PHE   C CD2   1 
ATOM   3734 C  CE1   . PHE   C 2 130 ? -12.63207 13.50832  30.84357  1.000 25.65211  ? 129 PHE   C CE1   1 
ATOM   3735 C  CE2   . PHE   C 2 130 ? -14.59483 13.68227  29.49017  1.000 27.74938  ? 129 PHE   C CE2   1 
ATOM   3736 C  CZ    . PHE   C 2 130 ? -13.30971 14.09456  29.80381  1.000 23.27916  ? 129 PHE   C CZ    1 
ATOM   3737 N  N     . GLY   C 2 131 ? -14.37105 8.95392   29.28249  1.000 26.66008  ? 130 GLY   C N     1 
ATOM   3738 C  CA    . GLY   C 2 131 ? -14.76999 8.80523   27.89646  1.000 27.04152  ? 130 GLY   C CA    1 
ATOM   3739 C  C     . GLY   C 2 131 ? -13.73554 8.01066   27.13095  1.000 28.06571  ? 130 GLY   C C     1 
ATOM   3740 O  O     . GLY   C 2 131 ? -12.72261 7.56170   27.68197  1.000 25.55732  ? 130 GLY   C O     1 
ATOM   3741 N  N     . LYS   C 2 132 ? -14.01267 7.84611   25.84398  1.000 27.97243  ? 131 LYS   C N     1 
ATOM   3742 C  CA    . LYS   C 2 132 ? -13.11966 7.10002   24.96909  1.000 31.78105  ? 131 LYS   C CA    1 
ATOM   3743 C  C     . LYS   C 2 132 ? -13.37648 7.52286   23.53262  1.000 34.66055  ? 131 LYS   C C     1 
ATOM   3744 O  O     . LYS   C 2 132 ? -14.50286 7.86966   23.15856  1.000 30.54755  ? 131 LYS   C O     1 
ATOM   3745 C  CB    . LYS   C 2 132 ? -13.30560 5.58819   25.14659  1.000 32.50932  ? 131 LYS   C CB    1 
ATOM   3746 C  CG    . LYS   C 2 132 ? -12.18935 4.73672   24.58488  1.000 36.14593  ? 131 LYS   C CG    1 
ATOM   3747 C  CD    . LYS   C 2 132 ? -12.38749 3.27228   24.96569  1.000 42.98360  ? 131 LYS   C CD    1 
ATOM   3748 C  CE    . LYS   C 2 132 ? -11.35542 2.38430   24.29567  1.000 52.33367  ? 131 LYS   C CE    1 
ATOM   3749 N  NZ    . LYS   C 2 132 ? -10.02487 3.05753   24.24224  1.000 43.00608  ? 131 LYS   C NZ    1 
ATOM   3750 N  N     . VAL   C 2 133 ? -12.30767 7.51992   22.73260  1.000 25.62845  ? 132 VAL   C N     1 
ATOM   3751 C  CA    . VAL   C 2 133 ? -12.44076 7.84030   21.32117  1.000 27.97406  ? 132 VAL   C CA    1 
ATOM   3752 C  C     . VAL   C 2 133 ? -13.31968 6.80416   20.64148  1.000 30.31509  ? 132 VAL   C C     1 
ATOM   3753 O  O     . VAL   C 2 133 ? -13.08634 5.59303   20.74547  1.000 32.97668  ? 132 VAL   C O     1 
ATOM   3754 C  CB    . VAL   C 2 133 ? -11.05435 7.91824   20.66529  1.000 29.64968  ? 132 VAL   C CB    1 
ATOM   3755 C  CG1   . VAL   C 2 133 ? -11.19866 7.96819   19.14530  1.000 26.51413  ? 132 VAL   C CG1   1 
ATOM   3756 C  CG2   . VAL   C 2 133 ? -10.32381 9.14476   21.18032  1.000 21.70146  ? 132 VAL   C CG2   1 
ATOM   3757 N  N     . LYS   C 2 134 ? -14.33889 7.28274   19.93648  1.000 32.11944  ? 133 LYS   C N     1 
ATOM   3758 C  CA    . LYS   C 2 134 ? -15.22120 6.43239   19.14262  1.000 42.37137  ? 133 LYS   C CA    1 
ATOM   3759 C  C     . LYS   C 2 134 ? -14.70963 6.31081   17.70988  1.000 36.27755  ? 133 LYS   C C     1 
ATOM   3760 O  O     . LYS   C 2 134 ? -14.35328 5.21999   17.25738  1.000 44.77428  ? 133 LYS   C O     1 
ATOM   3761 C  CB    . LYS   C 2 134 ? -16.64541 7.00434   19.17480  1.000 38.71591  ? 133 LYS   C CB    1 
ATOM   3762 C  CG    . LYS   C 2 134 ? -17.70592 6.12050   18.56103  1.000 48.06557  ? 133 LYS   C CG    1 
ATOM   3763 C  CD    . LYS   C 2 134 ? -19.08089 6.72492   18.78656  1.000 46.46006  ? 133 LYS   C CD    1 
ATOM   3764 C  CE    . LYS   C 2 134 ? -20.18030 5.80234   18.29820  1.000 55.27450  ? 133 LYS   C CE    1 
ATOM   3765 N  NZ    . LYS   C 2 134 ? -21.51852 6.42288   18.48339  1.000 60.94880  ? 133 LYS   C NZ    1 
ATOM   3766 N  N     . GLU   C 2 135 ? -14.66601 7.42475   16.99169  1.000 32.55275  ? 134 GLU   C N     1 
ATOM   3767 C  CA    . GLU   C 2 135 ? -14.16462 7.46319   15.62877  1.000 34.26514  ? 134 GLU   C CA    1 
ATOM   3768 C  C     . GLU   C 2 135 ? -13.03598 8.47802   15.51890  1.000 35.38628  ? 134 GLU   C C     1 
ATOM   3769 O  O     . GLU   C 2 135 ? -12.99092 9.46744   16.25894  1.000 32.50786  ? 134 GLU   C O     1 
ATOM   3770 C  CB    . GLU   C 2 135 ? -15.27498 7.81431   14.63840  1.000 41.99267  ? 134 GLU   C CB    1 
ATOM   3771 C  CG    . GLU   C 2 135 ? -16.27522 6.70107   14.41620  1.000 49.80063  ? 134 GLU   C CG    1 
ATOM   3772 C  CD    . GLU   C 2 135 ? -16.46272 6.37764   12.94942  1.000 58.89200  ? 134 GLU   C CD    1 
ATOM   3773 O  OE1   . GLU   C 2 135 ? -15.57331 5.72016   12.36442  1.000 61.88214  ? 134 GLU   C OE1   1 
ATOM   3774 O  OE2   . GLU   C 2 135 ? -17.49726 6.78975   12.38246  1.000 60.28165  ? 134 GLU   C OE2   1 
ATOM   3775 N  N     . GLY   C 2 136 ? -12.12150 8.21661   14.58869  1.000 33.46032  ? 135 GLY   C N     1 
ATOM   3776 C  CA    . GLY   C 2 136 ? -11.04243 9.14208   14.31415  1.000 35.94645  ? 135 GLY   C CA    1 
ATOM   3777 C  C     . GLY   C 2 136 ? -9.81370  8.99682   15.18418  1.000 29.76365  ? 135 GLY   C C     1 
ATOM   3778 O  O     . GLY   C 2 136 ? -9.09693  9.98393   15.38261  1.000 27.34949  ? 135 GLY   C O     1 
ATOM   3779 N  N     . MET   C 2 137 ? -9.54277  7.79860   15.70336  1.000 26.78419  ? 136 MET   C N     1 
ATOM   3780 C  CA    . MET   C 2 137 ? -8.29008  7.57507   16.41337  1.000 29.68766  ? 136 MET   C CA    1 
ATOM   3781 C  C     . MET   C 2 137 ? -7.09307  7.83936   15.50522  1.000 29.34053  ? 136 MET   C C     1 
ATOM   3782 O  O     . MET   C 2 137 ? -6.03397  8.27592   15.97396  1.000 27.15795  ? 136 MET   C O     1 
ATOM   3783 C  CB    . MET   C 2 137 ? -8.25960  6.14823   16.97126  1.000 30.02547  ? 136 MET   C CB    1 
ATOM   3784 C  CG    . MET   C 2 137 ? -7.11776  5.87663   17.93134  1.000 30.96497  ? 136 MET   C CG    1 
ATOM   3785 S  SD    . MET   C 2 137 ? -7.23296  6.87672   19.43552  1.000 28.97195  ? 136 MET   C SD    1 
ATOM   3786 C  CE    . MET   C 2 137 ? -5.51557  6.87165   19.94175  1.000 30.86431  ? 136 MET   C CE    1 
ATOM   3787 N  N     . ASN   C 2 138 ? -7.24276  7.62218   14.19397  1.000 26.78876  ? 137 ASN   C N     1 
ATOM   3788 C  CA    . ASN   C 2 138 ? -6.13137  7.92593   13.29890  1.000 27.96577  ? 137 ASN   C CA    1 
ATOM   3789 C  C     . ASN   C 2 138 ? -5.77951  9.40447   13.33805  1.000 26.07566  ? 137 ASN   C C     1 
ATOM   3790 O  O     . ASN   C 2 138 ? -4.62807  9.77424   13.08458  1.000 27.76682  ? 137 ASN   C O     1 
ATOM   3791 C  CB    . ASN   C 2 138 ? -6.44952  7.49986   11.85493  1.000 30.96349  ? 137 ASN   C CB    1 
ATOM   3792 C  CG    . ASN   C 2 138 ? -7.53919  8.35650   11.20854  1.000 31.73411  ? 137 ASN   C CG    1 
ATOM   3793 O  OD1   . ASN   C 2 138 ? -8.62541  8.51527   11.76121  1.000 31.64978  ? 137 ASN   C OD1   1 
ATOM   3794 N  ND2   . ASN   C 2 138 ? -7.24534  8.91391   10.02804  1.000 30.08871  ? 137 ASN   C ND2   1 
ATOM   3795 N  N     . ILE   C 2 139 ? -6.75308  10.26601  13.63669  1.000 23.52742  ? 138 ILE   C N     1 
ATOM   3796 C  CA    . ILE   C 2 139 ? -6.46348  11.68797  13.74569  1.000 24.46494  ? 138 ILE   C CA    1 
ATOM   3797 C  C     . ILE   C 2 139 ? -5.64938  11.95643  15.00879  1.000 25.11764  ? 138 ILE   C C     1 
ATOM   3798 O  O     . ILE   C 2 139 ? -4.68161  12.72581  14.98752  1.000 26.58074  ? 138 ILE   C O     1 
ATOM   3799 C  CB    . ILE   C 2 139 ? -7.77002  12.50509  13.72569  1.000 29.09444  ? 138 ILE   C CB    1 
ATOM   3800 C  CG1   . ILE   C 2 139 ? -8.52080  12.27174  12.41089  1.000 33.77992  ? 138 ILE   C CG1   1 
ATOM   3801 C  CG2   . ILE   C 2 139 ? -7.48973  13.97857  13.93978  1.000 26.24147  ? 138 ILE   C CG2   1 
ATOM   3802 C  CD1   . ILE   C 2 139 ? -7.67723  12.50014  11.15780  1.000 30.60778  ? 138 ILE   C CD1   1 
ATOM   3803 N  N     . VAL   C 2 140 ? -6.01675  11.30799  16.11745  1.000 24.22561  ? 139 VAL   C N     1 
ATOM   3804 C  CA    . VAL   C 2 140 ? -5.23361  11.44682  17.34014  1.000 21.88042  ? 139 VAL   C CA    1 
ATOM   3805 C  C     . VAL   C 2 140 ? -3.81504  10.93470  17.11470  1.000 25.06626  ? 139 VAL   C C     1 
ATOM   3806 O  O     . VAL   C 2 140 ? -2.83751  11.53954  17.57785  1.000 27.07712  ? 139 VAL   C O     1 
ATOM   3807 C  CB    . VAL   C 2 140 ? -5.91746  10.71230  18.50940  1.000 22.55789  ? 139 VAL   C CB    1 
ATOM   3808 C  CG1   . VAL   C 2 140 ? -5.01612  10.73140  19.72063  1.000 22.60034  ? 139 VAL   C CG1   1 
ATOM   3809 C  CG2   . VAL   C 2 140 ? -7.26047  11.34547  18.83244  1.000 27.17130  ? 139 VAL   C CG2   1 
ATOM   3810 N  N     . GLU   C 2 141 ? -3.68022  9.79579   16.43357  1.000 25.78146  ? 140 GLU   C N     1 
ATOM   3811 C  CA    . GLU   C 2 141 ? -2.34568  9.29741   16.10872  1.000 31.76379  ? 140 GLU   C CA    1 
ATOM   3812 C  C     . GLU   C 2 141 ? -1.56438  10.32310  15.30548  1.000 25.54328  ? 140 GLU   C C     1 
ATOM   3813 O  O     . GLU   C 2 141 ? -0.37365  10.54973  15.56153  1.000 28.36857  ? 140 GLU   C O     1 
ATOM   3814 C  CB    . GLU   C 2 141 ? -2.43626  7.97336   15.35153  1.000 28.40130  ? 140 GLU   C CB    1 
ATOM   3815 C  CG    . GLU   C 2 141 ? -3.01905  6.86684   16.16797  1.000 28.51445  ? 140 GLU   C CG    1 
ATOM   3816 C  CD    . GLU   C 2 141 ? -3.37976  5.65224   15.34958  1.000 35.89354  ? 140 GLU   C CD    1 
ATOM   3817 O  OE1   . GLU   C 2 141 ? -3.34005  5.71857   14.09639  1.000 35.55808  ? 140 GLU   C OE1   1 
ATOM   3818 O  OE2   . GLU   C 2 141 ? -3.70393  4.62068   15.96353  1.000 36.80407  ? 140 GLU   C OE2   1 
ATOM   3819 N  N     . ALA   C 2 142 ? -2.22354  10.97622  14.34526  1.000 26.04890  ? 141 ALA   C N     1 
ATOM   3820 C  CA    . ALA   C 2 142 ? -1.52203  11.96089  13.53149  1.000 26.04736  ? 141 ALA   C CA    1 
ATOM   3821 C  C     . ALA   C 2 142 ? -1.11783  13.17366  14.35241  1.000 25.98747  ? 141 ALA   C C     1 
ATOM   3822 O  O     . ALA   C 2 142 ? -0.08288  13.78908  14.08050  1.000 31.01648  ? 141 ALA   C O     1 
ATOM   3823 C  CB    . ALA   C 2 142 ? -2.39293  12.37755  12.34465  1.000 29.84016  ? 141 ALA   C CB    1 
ATOM   3824 N  N     . MET   C 2 143 ? -1.89594  13.51320  15.37837  1.000 27.96096  ? 142 MET   C N     1 
ATOM   3825 C  CA    . MET   C 2 143 ? -1.53170  14.63337  16.23902  1.000 27.92325  ? 142 MET   C CA    1 
ATOM   3826 C  C     . MET   C 2 143 ? -0.16197  14.43073  16.88445  1.000 27.44161  ? 142 MET   C C     1 
ATOM   3827 O  O     . MET   C 2 143 ? 0.51684   15.41444  17.19244  1.000 25.27560  ? 142 MET   C O     1 
ATOM   3828 C  CB    . MET   C 2 143 ? -2.62725  14.85191  17.29083  1.000 25.91880  ? 142 MET   C CB    1 
ATOM   3829 C  CG    . MET   C 2 143 ? -3.88454  15.46505  16.67511  1.000 28.85802  ? 142 MET   C CG    1 
ATOM   3830 S  SD    . MET   C 2 143 ? -5.36176  15.36381  17.69241  1.000 31.71753  ? 142 MET   C SD    1 
ATOM   3831 C  CE    . MET   C 2 143 ? -4.89027  16.43852  19.04052  1.000 31.28331  ? 142 MET   C CE    1 
ATOM   3832 N  N     . GLU   C 2 144 ? 0.28181   13.17321  17.03263  1.000 30.29328  ? 143 GLU   C N     1 
ATOM   3833 C  CA    . GLU   C 2 144 ? 1.56229   12.89078  17.68456  1.000 27.69586  ? 143 GLU   C CA    1 
ATOM   3834 C  C     . GLU   C 2 144 ? 2.74893   13.36506  16.86181  1.000 35.70975  ? 143 GLU   C C     1 
ATOM   3835 O  O     . GLU   C 2 144 ? 3.82400   13.61675  17.42085  1.000 37.06135  ? 143 GLU   C O     1 
ATOM   3836 C  CB    . GLU   C 2 144 ? 1.71569   11.39106  17.95635  1.000 28.76969  ? 143 GLU   C CB    1 
ATOM   3837 C  CG    . GLU   C 2 144 ? 0.86864   10.86945  19.12724  1.000 28.18531  ? 143 GLU   C CG    1 
ATOM   3838 C  CD    . GLU   C 2 144 ? 1.34492   9.52216   19.66053  1.000 29.90533  ? 143 GLU   C CD    1 
ATOM   3839 O  OE1   . GLU   C 2 144 ? 1.57302   8.60967   18.84492  1.000 35.05712  ? 143 GLU   C OE1   1 
ATOM   3840 O  OE2   . GLU   C 2 144 ? 1.47189   9.36613   20.90134  1.000 30.56862  ? 143 GLU   C OE2   1 
ATOM   3841 N  N     . ARG   C 2 145 ? 2.59336   13.45587  15.54000  1.000 27.60936  ? 144 ARG   C N     1 
ATOM   3842 C  CA    . ARG   C 2 145 ? 3.65218   14.01014  14.70499  1.000 35.91229  ? 144 ARG   C CA    1 
ATOM   3843 C  C     . ARG   C 2 145 ? 4.05146   15.40421  15.15039  1.000 32.39437  ? 144 ARG   C C     1 
ATOM   3844 O  O     . ARG   C 2 145 ? 5.15415   15.85543  14.83064  1.000 38.91571  ? 144 ARG   C O     1 
ATOM   3845 C  CB    . ARG   C 2 145 ? 3.20419   14.06621  13.23620  1.000 36.82590  ? 144 ARG   C CB    1 
ATOM   3846 C  CG    . ARG   C 2 145 ? 2.73379   12.75052  12.63459  1.000 42.57250  ? 144 ARG   C CG    1 
ATOM   3847 C  CD    . ARG   C 2 145 ? 2.34773   12.94462  11.16269  1.000 43.76115  ? 144 ARG   C CD    1 
ATOM   3848 N  NE    . ARG   C 2 145 ? 2.44999   11.70081  10.40635  1.000 49.20306  ? 144 ARG   C NE    1 
ATOM   3849 C  CZ    . ARG   C 2 145 ? 1.45567   11.14769  9.72439   1.000 56.53068  ? 144 ARG   C CZ    1 
ATOM   3850 N  NH1   . ARG   C 2 145 ? 0.27388   11.73891  9.62227   1.000 53.49396  ? 144 ARG   C NH1   1 
ATOM   3851 N  NH2   . ARG   C 2 145 ? 1.65324   9.97441   9.12390   1.000 57.80315  ? 144 ARG   C NH2   1 
ATOM   3852 N  N     . PHE   C 2 146 ? 3.17991   16.10781  15.86989  1.000 30.09072  ? 145 PHE   C N     1 
ATOM   3853 C  CA    . PHE   C 2 146 ? 3.42684   17.49835  16.19511  1.000 24.29343  ? 145 PHE   C CA    1 
ATOM   3854 C  C     . PHE   C 2 146 ? 3.81613   17.70777  17.64250  1.000 25.96154  ? 145 PHE   C C     1 
ATOM   3855 O  O     . PHE   C 2 146 ? 3.94523   18.85961  18.06503  1.000 29.24965  ? 145 PHE   C O     1 
ATOM   3856 C  CB    . PHE   C 2 146 ? 2.19905   18.33255  15.83855  1.000 28.54467  ? 145 PHE   C CB    1 
ATOM   3857 C  CG    . PHE   C 2 146 ? 1.72976   18.07938  14.45000  1.000 26.15198  ? 145 PHE   C CG    1 
ATOM   3858 C  CD1   . PHE   C 2 146 ? 2.50179   18.47985  13.36789  1.000 30.04490  ? 145 PHE   C CD1   1 
ATOM   3859 C  CD2   . PHE   C 2 146 ? 0.56140   17.37436  14.21529  1.000 28.67888  ? 145 PHE   C CD2   1 
ATOM   3860 C  CE1   . PHE   C 2 146 ? 2.08397   18.22523  12.07395  1.000 34.26875  ? 145 PHE   C CE1   1 
ATOM   3861 C  CE2   . PHE   C 2 146 ? 0.15175   17.11275  12.92195  1.000 34.16782  ? 145 PHE   C CE2   1 
ATOM   3862 C  CZ    . PHE   C 2 146 ? 0.91813   17.53541  11.85954  1.000 33.86200  ? 145 PHE   C CZ    1 
ATOM   3863 N  N     . GLY   C 2 147 ? 4.02194   16.62935  18.40121  1.000 27.29355  ? 146 GLY   C N     1 
ATOM   3864 C  CA    . GLY   C 2 147 ? 4.45775   16.71784  19.77769  1.000 25.31080  ? 146 GLY   C CA    1 
ATOM   3865 C  C     . GLY   C 2 147 ? 5.95622   16.54441  19.92969  1.000 27.10983  ? 146 GLY   C C     1 
ATOM   3866 O  O     . GLY   C 2 147 ? 6.72145   16.52079  18.96238  1.000 28.45805  ? 146 GLY   C O     1 
ATOM   3867 N  N     . SER   C 2 148 ? 6.38278   16.41815  21.17900  1.000 25.32812  ? 147 SER   C N     1 
ATOM   3868 C  CA    . SER   C 2 148 ? 7.80569   16.35824  21.47861  1.000 23.29714  ? 147 SER   C CA    1 
ATOM   3869 C  C     . SER   C 2 148 ? 7.97683   15.73664  22.86063  1.000 26.19332  ? 147 SER   C C     1 
ATOM   3870 O  O     . SER   C 2 148 ? 7.00037   15.43306  23.55093  1.000 26.56623  ? 147 SER   C O     1 
ATOM   3871 C  CB    . SER   C 2 148 ? 8.42421   17.75306  21.41377  1.000 26.67632  ? 147 SER   C CB    1 
ATOM   3872 O  OG    . SER   C 2 148 ? 7.88768   18.57519  22.44208  1.000 28.01697  ? 147 SER   C OG    1 
ATOM   3873 N  N     . ARG   C 2 149 ? 9.23237   15.59441  23.28002  1.000 26.07078  ? 148 ARG   C N     1 
ATOM   3874 C  CA    . ARG   C 2 149 ? 9.51312   14.92529  24.55303  1.000 26.53302  ? 148 ARG   C CA    1 
ATOM   3875 C  C     . ARG   C 2 149 ? 8.91255   15.66819  25.74447  1.000 27.76146  ? 148 ARG   C C     1 
ATOM   3876 O  O     . ARG   C 2 149 ? 8.39350   15.03812  26.67877  1.000 28.48918  ? 148 ARG   C O     1 
ATOM   3877 C  CB    . ARG   C 2 149 ? 11.02760  14.75307  24.71621  1.000 25.89523  ? 148 ARG   C CB    1 
ATOM   3878 C  CG    . ARG   C 2 149 ? 11.41338  14.02154  25.99043  1.000 28.79205  ? 148 ARG   C CG    1 
ATOM   3879 C  CD    . ARG   C 2 149 ? 12.86750  13.60372  25.96591  1.000 27.13710  ? 148 ARG   C CD    1 
ATOM   3880 N  NE    . ARG   C 2 149 ? 13.29078  13.07227  27.25691  1.000 28.48741  ? 148 ARG   C NE    1 
ATOM   3881 C  CZ    . ARG   C 2 149 ? 13.64950  13.83690  28.27676  1.000 28.00863  ? 148 ARG   C CZ    1 
ATOM   3882 N  NH1   . ARG   C 2 149 ? 13.60547  15.15512  28.19303  1.000 28.27521  ? 148 ARG   C NH1   1 
ATOM   3883 N  NH2   . ARG   C 2 149 ? 14.05721  13.26329  29.40957  1.000 31.69090  ? 148 ARG   C NH2   1 
ATOM   3884 N  N     . ASN   C 2 150 ? 8.97868   16.99614  25.75936  1.000 24.48375  ? 149 ASN   C N     1 
ATOM   3885 C  CA    . ASN   C 2 150 ? 8.39815   17.74402  26.86642  1.000 26.19047  ? 149 ASN   C CA    1 
ATOM   3886 C  C     . ASN   C 2 150 ? 7.00457   18.28297  26.56481  1.000 28.60937  ? 149 ASN   C C     1 
ATOM   3887 O  O     . ASN   C 2 150 ? 6.45917   19.04708  27.37140  1.000 27.60995  ? 149 ASN   C O     1 
ATOM   3888 C  CB    . ASN   C 2 150 ? 9.32929   18.88631  27.28577  1.000 32.76904  ? 149 ASN   C CB    1 
ATOM   3889 C  CG    . ASN   C 2 150 ? 9.27041   20.08592  26.34641  1.000 31.39857  ? 149 ASN   C CG    1 
ATOM   3890 O  OD1   . ASN   C 2 150 ? 8.71628   20.02193  25.24484  1.000 31.76822  ? 149 ASN   C OD1   1 
ATOM   3891 N  ND2   . ASN   C 2 150 ? 9.86642   21.19171  26.78470  1.000 33.23041  ? 149 ASN   C ND2   1 
ATOM   3892 N  N     . GLY   C 2 151 ? 6.42545   17.91516  25.42072  1.000 26.66441  ? 150 GLY   C N     1 
ATOM   3893 C  CA    . GLY   C 2 151 ? 5.05919   18.25227  25.07909  1.000 22.46935  ? 150 GLY   C CA    1 
ATOM   3894 C  C     . GLY   C 2 151 ? 4.89091   19.45119  24.17138  1.000 27.10354  ? 150 GLY   C C     1 
ATOM   3895 O  O     . GLY   C 2 151 ? 3.81904   19.61220  23.58507  1.000 26.01283  ? 150 GLY   C O     1 
ATOM   3896 N  N     . LYS   C 2 152 ? 5.91863   20.28626  24.02512  1.000 30.01496  ? 151 LYS   C N     1 
ATOM   3897 C  CA    . LYS   C 2 152 ? 5.78431   21.47139  23.19376  1.000 30.71703  ? 151 LYS   C CA    1 
ATOM   3898 C  C     . LYS   C 2 152 ? 5.48913   21.04339  21.76797  1.000 23.81130  ? 151 LYS   C C     1 
ATOM   3899 O  O     . LYS   C 2 152 ? 6.13757   20.13522  21.23495  1.000 26.83512  ? 151 LYS   C O     1 
ATOM   3900 C  CB    . LYS   C 2 152 ? 7.06429   22.31803  23.24535  1.000 30.69563  ? 151 LYS   C CB    1 
ATOM   3901 C  CG    . LYS   C 2 152 ? 7.40079   22.90951  24.62112  1.000 40.22476  ? 151 LYS   C CG    1 
ATOM   3902 C  CD    . LYS   C 2 152 ? 6.20079   23.58639  25.31039  1.000 44.32871  ? 151 LYS   C CD    1 
ATOM   3903 C  CE    . LYS   C 2 152 ? 6.63316   24.56336  26.41975  1.000 48.61900  ? 151 LYS   C CE    1 
ATOM   3904 N  NZ    . LYS   C 2 152 ? 7.32552   23.95082  27.61676  1.000 51.76523  ? 151 LYS   C NZ    1 
ATOM   3905 N  N     . THR   C 2 153 ? 4.49198   21.67829  21.16184  1.000 23.13681  ? 152 THR   C N     1 
ATOM   3906 C  CA    . THR   C 2 153 ? 4.04607   21.30421  19.83033  1.000 23.80696  ? 152 THR   C CA    1 
ATOM   3907 C  C     . THR   C 2 153 ? 4.74220   22.16253  18.78109  1.000 29.41027  ? 152 THR   C C     1 
ATOM   3908 O  O     . THR   C 2 153 ? 5.05555   23.33316  19.01068  1.000 31.95157  ? 152 THR   C O     1 
ATOM   3909 C  CB    . THR   C 2 153 ? 2.52596   21.43376  19.65108  1.000 29.36382  ? 152 THR   C CB    1 
ATOM   3910 O  OG1   . THR   C 2 153 ? 2.13208   22.81078  19.68870  1.000 29.28624  ? 152 THR   C OG1   1 
ATOM   3911 C  CG2   . THR   C 2 153 ? 1.79036   20.65880  20.74119  1.000 27.11277  ? 152 THR   C CG2   1 
ATOM   3912 N  N     . SER   C 2 154 ? 4.95726   21.56317  17.62296  1.000 29.66229  ? 153 SER   C N     1 
ATOM   3913 C  CA    . SER   C 2 154 ? 5.72893   22.17757  16.55153  1.000 34.32564  ? 153 SER   C CA    1 
ATOM   3914 C  C     . SER   C 2 154 ? 4.84073   22.86280  15.52751  1.000 38.24491  ? 153 SER   C C     1 
ATOM   3915 O  O     . SER   C 2 154 ? 5.35039   23.56599  14.64726  1.000 36.12133  ? 153 SER   C O     1 
ATOM   3916 C  CB    . SER   C 2 154 ? 6.58090   21.11665  15.86714  1.000 33.11071  ? 153 SER   C CB    1 
ATOM   3917 O  OG    . SER   C 2 154 ? 5.73353   20.12847  15.31114  1.000 33.83182  ? 153 SER   C OG    1 
ATOM   3918 N  N     . LYS   C 2 155 ? 3.53375   22.63720  15.60883  1.000 29.71030  ? 154 LYS   C N     1 
ATOM   3919 C  CA    . LYS   C 2 155 ? 2.52970   23.42844  14.91995  1.000 33.55275  ? 154 LYS   C CA    1 
ATOM   3920 C  C     . LYS   C 2 155 ? 1.36550   23.58024  15.87973  1.000 39.28716  ? 154 LYS   C C     1 
ATOM   3921 O  O     . LYS   C 2 155 ? 1.21467   22.78716  16.81183  1.000 36.97793  ? 154 LYS   C O     1 
ATOM   3922 C  CB    . LYS   C 2 155 ? 2.07863   22.77598  13.60450  1.000 37.22047  ? 154 LYS   C CB    1 
ATOM   3923 C  CG    . LYS   C 2 155 ? 3.20925   22.63016  12.59253  1.000 35.12784  ? 154 LYS   C CG    1 
ATOM   3924 C  CD    . LYS   C 2 155 ? 2.76313   21.99331  11.29003  1.000 41.10130  ? 154 LYS   C CD    1 
ATOM   3925 C  CE    . LYS   C 2 155 ? 3.91706   21.99408  10.28835  1.000 42.67292  ? 154 LYS   C CE    1 
ATOM   3926 N  NZ    . LYS   C 2 155 ? 3.49821   21.41750  8.98232   1.000 49.87850  ? 154 LYS   C NZ    1 
ATOM   3927 N  N     . LYS   C 2 156 ? 0.56666   24.62475  15.67296  1.000 36.70444  ? 155 LYS   C N     1 
ATOM   3928 C  CA    . LYS   C 2 156 ? -0.57635  24.87900  16.54128  1.000 39.64894  ? 155 LYS   C CA    1 
ATOM   3929 C  C     . LYS   C 2 156 ? -1.68517  23.89066  16.19598  1.000 41.36156  ? 155 LYS   C C     1 
ATOM   3930 O  O     . LYS   C 2 156 ? -2.16555  23.86123  15.05868  1.000 34.55909  ? 155 LYS   C O     1 
ATOM   3931 C  CB    . LYS   C 2 156 ? -1.06391  26.31829  16.38716  1.000 37.68032  ? 155 LYS   C CB    1 
ATOM   3932 C  CG    . LYS   C 2 156 ? 0.02729   27.36995  16.52732  1.000 45.79225  ? 155 LYS   C CG    1 
ATOM   3933 C  CD    . LYS   C 2 156 ? -0.53158  28.78275  16.35452  1.000 55.36166  ? 155 LYS   C CD    1 
ATOM   3934 C  CE    . LYS   C 2 156 ? 0.16787   29.54500  15.22193  1.000 53.75769  ? 155 LYS   C CE    1 
ATOM   3935 N  NZ    . LYS   C 2 156 ? -0.15195  28.99076  13.86239  1.000 50.45567  ? 155 LYS   C NZ    1 
ATOM   3936 N  N     . ILE   C 2 157 ? -2.09313  23.08404  17.17641  1.000 32.26124  ? 156 ILE   C N     1 
ATOM   3937 C  CA    . ILE   C 2 157 ? -3.12618  22.07311  16.98742  1.000 32.60605  ? 156 ILE   C CA    1 
ATOM   3938 C  C     . ILE   C 2 157 ? -4.35380  22.57340  17.74044  1.000 28.45442  ? 156 ILE   C C     1 
ATOM   3939 O  O     . ILE   C 2 157 ? -4.30874  22.73359  18.96783  1.000 32.13235  ? 156 ILE   C O     1 
ATOM   3940 C  CB    . ILE   C 2 157 ? -2.66894  20.69575  17.49100  1.000 33.80131  ? 156 ILE   C CB    1 
ATOM   3941 C  CG1   . ILE   C 2 157 ? -1.23450  20.39803  17.00817  1.000 35.09599  ? 156 ILE   C CG1   1 
ATOM   3942 C  CG2   . ILE   C 2 157 ? -3.63826  19.61062  17.04296  1.000 34.64059  ? 156 ILE   C CG2   1 
ATOM   3943 C  CD1   . ILE   C 2 157 ? -1.08209  20.30790  15.48485  1.000 33.74534  ? 156 ILE   C CD1   1 
ATOM   3944 N  N     . THR   C 2 158 ? -5.42961  22.86627  17.01361  1.000 29.31177  ? 157 THR   C N     1 
ATOM   3945 C  CA    . THR   C 2 158 ? -6.58595  23.53954  17.59029  1.000 33.48672  ? 157 THR   C CA    1 
ATOM   3946 C  C     . THR   C 2 158 ? -7.85416  22.72212  17.39550  1.000 30.94751  ? 157 THR   C C     1 
ATOM   3947 O  O     . THR   C 2 158 ? -7.94391  21.84464  16.53080  1.000 31.09468  ? 157 THR   C O     1 
ATOM   3948 C  CB    . THR   C 2 158 ? -6.80717  24.93185  16.97920  1.000 33.93150  ? 157 THR   C CB    1 
ATOM   3949 O  OG1   . THR   C 2 158 ? -6.93371  24.80842  15.54975  1.000 30.94484  ? 157 THR   C OG1   1 
ATOM   3950 C  CG2   . THR   C 2 158 ? -5.65915  25.86943  17.34557  1.000 37.84726  ? 157 THR   C CG2   1 
ATOM   3951 N  N     . ILE   C 2 159 ? -8.84640  23.03963  18.22334  1.000 33.06256  ? 158 ILE   C N     1 
ATOM   3952 C  CA    . ILE   C 2 159 ? -10.18899 22.48580  18.07631  1.000 32.99931  ? 158 ILE   C CA    1 
ATOM   3953 C  C     . ILE   C 2 159 ? -10.94856 23.50209  17.23246  1.000 39.98832  ? 158 ILE   C C     1 
ATOM   3954 O  O     . ILE   C 2 159 ? -11.54829 24.45033  17.74550  1.000 32.65050  ? 158 ILE   C O     1 
ATOM   3955 C  CB    . ILE   C 2 159 ? -10.84968 22.22654  19.42290  1.000 29.39475  ? 158 ILE   C CB    1 
ATOM   3956 C  CG1   . ILE   C 2 159 ? -10.06052 21.16123  20.17332  1.000 29.73927  ? 158 ILE   C CG1   1 
ATOM   3957 C  CG2   . ILE   C 2 159 ? -12.28339 21.77249  19.23801  1.000 31.30467  ? 158 ILE   C CG2   1 
ATOM   3958 C  CD1   . ILE   C 2 159 ? -10.53211 20.95422  21.63325  1.000 30.06776  ? 158 ILE   C CD1   1 
ATOM   3959 N  N     . ALA   C 2 160 ? -10.87768 23.32186  15.90847  1.000 35.97142  ? 159 ALA   C N     1 
ATOM   3960 C  CA    . ALA   C 2 160 ? -11.50486 24.27877  15.00799  1.000 35.13653  ? 159 ALA   C CA    1 
ATOM   3961 C  C     . ALA   C 2 160 ? -13.00926 24.32971  15.22577  1.000 41.34077  ? 159 ALA   C C     1 
ATOM   3962 O  O     . ALA   C 2 160 ? -13.61735 25.40083  15.10907  1.000 43.96085  ? 159 ALA   C O     1 
ATOM   3963 C  CB    . ALA   C 2 160 ? -11.17137 23.92992  13.56018  1.000 35.97158  ? 159 ALA   C CB    1 
ATOM   3964 N  N     . ASP   C 2 161 ? -13.61418 23.19455  15.57252  1.000 35.01620  ? 160 ASP   C N     1 
ATOM   3965 C  CA    . ASP   C 2 161 ? -15.04829 23.10573  15.81516  1.000 39.98359  ? 160 ASP   C CA    1 
ATOM   3966 C  C     . ASP   C 2 161 ? -15.30696 21.93848  16.76107  1.000 39.24799  ? 160 ASP   C C     1 
ATOM   3967 O  O     . ASP   C 2 161 ? -14.53320 20.97807  16.80490  1.000 35.70613  ? 160 ASP   C O     1 
ATOM   3968 C  CB    . ASP   C 2 161 ? -15.81379 22.91316  14.50507  1.000 40.18908  ? 160 ASP   C CB    1 
ATOM   3969 C  CG    . ASP   C 2 161 ? -17.24871 23.40299  14.58482  1.000 44.51762  ? 160 ASP   C CG    1 
ATOM   3970 O  OD1   . ASP   C 2 161 ? -17.60586 24.08788  15.56951  1.000 43.56986  ? 160 ASP   C OD1   1 
ATOM   3971 O  OD2   . ASP   C 2 161 ? -18.01195 23.09397  13.64924  1.000 42.41709  ? 160 ASP   C OD2   1 
ATOM   3972 N  N     . CYS   C 2 162 ? -16.40111 22.02653  17.51593  1.000 33.60214  ? 161 CYS   C N     1 
ATOM   3973 C  CA    . CYS   C 2 162 ? -16.80321 20.90152  18.34195  1.000 36.80852  ? 161 CYS   C CA    1 
ATOM   3974 C  C     . CYS   C 2 162 ? -18.30612 20.96968  18.57269  1.000 36.29377  ? 161 CYS   C C     1 
ATOM   3975 O  O     . CYS   C 2 162 ? -18.94054 21.99694  18.33204  1.000 40.16919  ? 161 CYS   C O     1 
ATOM   3976 C  CB    . CYS   C 2 162 ? -16.03836 20.87841  19.67105  1.000 29.24183  ? 161 CYS   C CB    1 
ATOM   3977 S  SG    . CYS   C 2 162 ? -15.88630 22.47209  20.49560  1.000 37.61317  ? 161 CYS   C SG    1 
ATOM   3978 N  N     . GLY   C 2 163 ? -18.86535 19.85557  19.02761  1.000 40.17904  ? 162 GLY   C N     1 
ATOM   3979 C  CA    . GLY   C 2 163 ? -20.27543 19.81265  19.36288  1.000 39.56817  ? 162 GLY   C CA    1 
ATOM   3980 C  C     . GLY   C 2 163 ? -20.70919 18.39971  19.70697  1.000 45.19658  ? 162 GLY   C C     1 
ATOM   3981 O  O     . GLY   C 2 163 ? -19.88437 17.51776  19.94443  1.000 38.69559  ? 162 GLY   C O     1 
ATOM   3982 N  N     . GLN   C 2 164 ? -22.02717 18.20071  19.73097  1.000 44.33599  ? 163 GLN   C N     1 
ATOM   3983 C  CA    . GLN   C 2 164 ? -22.61224 16.91762  20.10023  1.000 41.51220  ? 163 GLN   C CA    1 
ATOM   3984 C  C     . GLN   C 2 164 ? -23.25983 16.26257  18.88945  1.000 45.11157  ? 163 GLN   C C     1 
ATOM   3985 O  O     . GLN   C 2 164 ? -23.91814 16.93172  18.09025  1.000 43.05138  ? 163 GLN   C O     1 
ATOM   3986 C  CB    . GLN   C 2 164 ? -23.64530 17.08262  21.22014  1.000 45.79712  ? 163 GLN   C CB    1 
ATOM   3987 C  CG    . GLN   C 2 164 ? -24.32016 15.78617  21.62242  1.000 42.34588  ? 163 GLN   C CG    1 
ATOM   3988 C  CD    . GLN   C 2 164 ? -25.03620 15.88069  22.95872  1.000 45.43324  ? 163 GLN   C CD    1 
ATOM   3989 O  OE1   . GLN   C 2 164 ? -25.13714 16.95685  23.55440  1.000 41.65647  ? 163 GLN   C OE1   1 
ATOM   3990 N  NE2   . GLN   C 2 164 ? -25.52861 14.74381  23.44153  1.000 43.55933  ? 163 GLN   C NE2   1 
ATOM   3991 N  N     . LEU   C 2 165 ? -23.07267 14.95198  18.76090  1.000 42.31971  ? 164 LEU   C N     1 
ATOM   3992 C  CA    . LEU   C 2 165 ? -23.62564 14.20701  17.63297  1.000 48.40562  ? 164 LEU   C CA    1 
ATOM   3993 C  C     . LEU   C 2 165 ? -24.96902 13.54699  17.96465  1.000 50.88390  ? 164 LEU   C C     1 
ATOM   3994 O  O     . LEU   C 2 165 ? -25.06381 12.68360  18.84399  1.000 54.12902  ? 164 LEU   C O     1 
ATOM   3995 C  CB    . LEU   C 2 165 ? -22.62342 13.14961  17.16261  1.000 42.75661  ? 164 LEU   C CB    1 
ATOM   3996 C  CG    . LEU   C 2 165 ? -21.32706 13.67202  16.52922  1.000 47.31160  ? 164 LEU   C CG    1 
ATOM   3997 C  CD1   . LEU   C 2 165 ? -20.38683 12.51384  16.23048  1.000 46.00195  ? 164 LEU   C CD1   1 
ATOM   3998 C  CD2   . LEU   C 2 165 ? -21.63108 14.46149  15.26815  1.000 44.71210  ? 164 LEU   C CD2   1 
ATOM   3999 N  N     . VAL   D 2 3   ? 34.83156  56.19186  2.50670   1.000 51.21824  ? 2   VAL   D N     1 
ATOM   4000 C  CA    . VAL   D 2 3   ? 34.32911  55.88349  3.84866   1.000 56.02558  ? 2   VAL   D CA    1 
ATOM   4001 C  C     . VAL   D 2 3   ? 33.41639  54.65103  3.80629   1.000 53.27612  ? 2   VAL   D C     1 
ATOM   4002 O  O     . VAL   D 2 3   ? 32.72737  54.39851  2.80818   1.000 53.43926  ? 2   VAL   D O     1 
ATOM   4003 C  CB    . VAL   D 2 3   ? 33.58855  57.09442  4.47384   1.000 49.02933  ? 2   VAL   D CB    1 
ATOM   4004 C  CG1   . VAL   D 2 3   ? 32.20428  57.26576  3.85598   1.000 53.54350  ? 2   VAL   D CG1   1 
ATOM   4005 C  CG2   . VAL   D 2 3   ? 33.49737  56.95602  5.99149   1.000 51.73491  ? 2   VAL   D CG2   1 
ATOM   4006 N  N     . ASN   D 2 4   ? 33.43075  53.88610  4.89674   1.000 48.25584  ? 3   ASN   D N     1 
ATOM   4007 C  CA    . ASN   D 2 4   ? 32.65608  52.64898  4.96748   1.000 42.40682  ? 3   ASN   D CA    1 
ATOM   4008 C  C     . ASN   D 2 4   ? 31.17808  52.95878  5.17789   1.000 35.79874  ? 3   ASN   D C     1 
ATOM   4009 O  O     . ASN   D 2 4   ? 30.83854  53.78952  6.02353   1.000 41.51169  ? 3   ASN   D O     1 
ATOM   4010 C  CB    . ASN   D 2 4   ? 33.17980  51.76924  6.09637   1.000 36.45674  ? 3   ASN   D CB    1 
ATOM   4011 C  CG    . ASN   D 2 4   ? 34.40198  50.97388  5.68760   1.000 39.76897  ? 3   ASN   D CG    1 
ATOM   4012 O  OD1   . ASN   D 2 4   ? 34.66363  50.79144  4.49312   1.000 41.24223  ? 3   ASN   D OD1   1 
ATOM   4013 N  ND2   . ASN   D 2 4   ? 35.14118  50.47390  6.66708   1.000 31.39114  ? 3   ASN   D ND2   1 
ATOM   4014 N  N     . PRO   D 2 5   ? 30.27672  52.32529  4.43624   1.000 35.11622  ? 4   PRO   D N     1 
ATOM   4015 C  CA    . PRO   D 2 5   ? 28.85002  52.60136  4.62782   1.000 34.96883  ? 4   PRO   D CA    1 
ATOM   4016 C  C     . PRO   D 2 5   ? 28.33572  52.00323  5.92769   1.000 40.95034  ? 4   PRO   D C     1 
ATOM   4017 O  O     . PRO   D 2 5   ? 28.91504  51.07104  6.49026   1.000 33.99850  ? 4   PRO   D O     1 
ATOM   4018 C  CB    . PRO   D 2 5   ? 28.18723  51.94527  3.41191   1.000 35.20482  ? 4   PRO   D CB    1 
ATOM   4019 C  CG    . PRO   D 2 5   ? 29.15897  50.90224  2.95693   1.000 35.42043  ? 4   PRO   D CG    1 
ATOM   4020 C  CD    . PRO   D 2 5   ? 30.53147  51.35059  3.36397   1.000 36.58920  ? 4   PRO   D CD    1 
ATOM   4021 N  N     . THR   D 2 6   ? 27.22495  52.57167  6.40119   1.000 41.74480  ? 5   THR   D N     1 
ATOM   4022 C  CA    A THR   D 2 6   ? 26.52061  52.11125  7.58864   0.500 37.32589  ? 5   THR   D CA    1 
ATOM   4023 C  CA    B THR   D 2 6   ? 26.53296  52.09346  7.58534   0.500 37.32011  ? 5   THR   D CA    1 
ATOM   4024 C  C     . THR   D 2 6   ? 25.09148  51.74551  7.21393   1.000 36.86267  ? 5   THR   D C     1 
ATOM   4025 O  O     . THR   D 2 6   ? 24.45305  52.44983  6.42252   1.000 35.06148  ? 5   THR   D O     1 
ATOM   4026 C  CB    A THR   D 2 6   ? 26.53561  53.18724  8.68873   0.500 35.10836  ? 5   THR   D CB    1 
ATOM   4027 C  CB    B THR   D 2 6   ? 26.55679  53.13474  8.70912   0.500 35.10049  ? 5   THR   D CB    1 
ATOM   4028 O  OG1   A THR   D 2 6   ? 27.88740  53.41703  9.11552   0.500 39.02195  ? 5   THR   D OG1   1 
ATOM   4029 O  OG1   B THR   D 2 6   ? 25.86864  54.30945  8.27353   0.500 39.02195  ? 5   THR   D OG1   1 
ATOM   4030 C  CG2   A THR   D 2 6   ? 25.70122  52.76879  9.88732   0.500 36.85503  ? 5   THR   D CG2   1 
ATOM   4031 C  CG2   B THR   D 2 6   ? 27.97611  53.50207  9.09715   0.500 38.88150  ? 5   THR   D CG2   1 
ATOM   4032 N  N     . VAL   D 2 7   ? 24.59490  50.62917  7.76372   1.000 35.54570  ? 6   VAL   D N     1 
ATOM   4033 C  CA    . VAL   D 2 7   ? 23.22043  50.18492  7.56808   1.000 32.30888  ? 6   VAL   D CA    1 
ATOM   4034 C  C     . VAL   D 2 7   ? 22.60178  49.90769  8.93371   1.000 28.88389  ? 6   VAL   D C     1 
ATOM   4035 O  O     . VAL   D 2 7   ? 23.29992  49.68834  9.92292   1.000 28.93546  ? 6   VAL   D O     1 
ATOM   4036 C  CB    . VAL   D 2 7   ? 23.12231  48.93145  6.67294   1.000 32.21516  ? 6   VAL   D CB    1 
ATOM   4037 C  CG1   . VAL   D 2 7   ? 23.52394  49.26391  5.23816   1.000 32.68420  ? 6   VAL   D CG1   1 
ATOM   4038 C  CG2   . VAL   D 2 7   ? 23.99477  47.81611  7.21949   1.000 31.06798  ? 6   VAL   D CG2   1 
ATOM   4039 N  N     . PHE   D 2 8   ? 21.27374  49.90461  8.97870   1.000 32.01831  ? 7   PHE   D N     1 
ATOM   4040 C  CA    . PHE   D 2 8   ? 20.56078  49.66901  10.22798  1.000 32.97157  ? 7   PHE   D CA    1 
ATOM   4041 C  C     . PHE   D 2 8   ? 19.52119  48.57576  10.05239  1.000 29.20498  ? 7   PHE   D C     1 
ATOM   4042 O  O     . PHE   D 2 8   ? 18.96528  48.38914  8.96609   1.000 29.88162  ? 7   PHE   D O     1 
ATOM   4043 C  CB    . PHE   D 2 8   ? 19.86516  50.94218  10.75362  1.000 34.61051  ? 7   PHE   D CB    1 
ATOM   4044 C  CG    . PHE   D 2 8   ? 18.71203  51.40318  9.90726   1.000 40.88350  ? 7   PHE   D CG    1 
ATOM   4045 C  CD1   . PHE   D 2 8   ? 18.91695  52.29155  8.86387   1.000 42.53355  ? 7   PHE   D CD1   1 
ATOM   4046 C  CD2   . PHE   D 2 8   ? 17.42128  50.96200  10.16551  1.000 33.58475  ? 7   PHE   D CD2   1 
ATOM   4047 C  CE1   . PHE   D 2 8   ? 17.85366  52.72868  8.08525   1.000 40.24506  ? 7   PHE   D CE1   1 
ATOM   4048 C  CE2   . PHE   D 2 8   ? 16.36557  51.38458  9.39486   1.000 40.62483  ? 7   PHE   D CE2   1 
ATOM   4049 C  CZ    . PHE   D 2 8   ? 16.58060  52.27298  8.35103   1.000 38.61197  ? 7   PHE   D CZ    1 
ATOM   4050 N  N     . PHE   D 2 9   ? 19.25743  47.86582  11.15116  1.000 34.23409  ? 8   PHE   D N     1 
ATOM   4051 C  CA    . PHE   D 2 9   ? 18.12764  46.95320  11.28456  1.000 28.61665  ? 8   PHE   D CA    1 
ATOM   4052 C  C     . PHE   D 2 9   ? 17.26311  47.45282  12.43049  1.000 27.78639  ? 8   PHE   D C     1 
ATOM   4053 O  O     . PHE   D 2 9   ? 17.77865  47.69597  13.52655  1.000 29.33438  ? 8   PHE   D O     1 
ATOM   4054 C  CB    . PHE   D 2 9   ? 18.55369  45.51994  11.62741  1.000 28.07132  ? 8   PHE   D CB    1 
ATOM   4055 C  CG    . PHE   D 2 9   ? 19.22412  44.76798  10.51447  1.000 28.63317  ? 8   PHE   D CG    1 
ATOM   4056 C  CD1   . PHE   D 2 9   ? 19.28251  45.26631  9.22077   1.000 28.53165  ? 8   PHE   D CD1   1 
ATOM   4057 C  CD2   . PHE   D 2 9   ? 19.75605  43.50893  10.77138  1.000 33.33305  ? 8   PHE   D CD2   1 
ATOM   4058 C  CE1   . PHE   D 2 9   ? 19.90134  44.53254  8.21028   1.000 31.06848  ? 8   PHE   D CE1   1 
ATOM   4059 C  CE2   . PHE   D 2 9   ? 20.36407  42.77210  9.77350   1.000 23.87990  ? 8   PHE   D CE2   1 
ATOM   4060 C  CZ    . PHE   D 2 9   ? 20.43349  43.27764  8.48131   1.000 25.43524  ? 8   PHE   D CZ    1 
ATOM   4061 N  N     . ASP   D 2 10  ? 15.95922  47.57773  12.19176  1.000 29.38483  ? 9   ASP   D N     1 
ATOM   4062 C  CA    . ASP   D 2 10  ? 14.99088  47.78629  13.26907  1.000 35.81810  ? 9   ASP   D CA    1 
ATOM   4063 C  C     . ASP   D 2 10  ? 14.39800  46.42724  13.62151  1.000 31.06310  ? 9   ASP   D C     1 
ATOM   4064 O  O     . ASP   D 2 10  ? 13.68489  45.83026  12.81093  1.000 31.57105  ? 9   ASP   D O     1 
ATOM   4065 C  CB    . ASP   D 2 10  ? 13.90422  48.77867  12.85692  1.000 32.23020  ? 9   ASP   D CB    1 
ATOM   4066 C  CG    . ASP   D 2 10  ? 14.39292  50.21995  12.84407  1.000 35.13990  ? 9   ASP   D CG    1 
ATOM   4067 O  OD1   . ASP   D 2 10  ? 15.03673  50.66692  13.81881  1.000 36.15318  ? 9   ASP   D OD1   1 
ATOM   4068 O  OD2   . ASP   D 2 10  ? 14.11979  50.91443  11.84439  1.000 40.27076  ? 9   ASP   D OD2   1 
ATOM   4069 N  N     . ILE   D 2 11  ? 14.70810  45.92982  14.82417  1.000 26.77311  ? 10  ILE   D N     1 
ATOM   4070 C  CA    . ILE   D 2 11  ? 14.38020  44.56400  15.22709  1.000 22.36995  ? 10  ILE   D CA    1 
ATOM   4071 C  C     . ILE   D 2 11  ? 13.05622  44.55887  15.98078  1.000 29.59307  ? 10  ILE   D C     1 
ATOM   4072 O  O     . ILE   D 2 11  ? 12.82824  45.40183  16.85588  1.000 30.96064  ? 10  ILE   D O     1 
ATOM   4073 C  CB    . ILE   D 2 11  ? 15.48665  43.95308  16.10812  1.000 26.29913  ? 10  ILE   D CB    1 
ATOM   4074 C  CG1   . ILE   D 2 11  ? 16.81827  43.91820  15.35565  1.000 26.67601  ? 10  ILE   D CG1   1 
ATOM   4075 C  CG2   . ILE   D 2 11  ? 15.11244  42.54190  16.52308  1.000 23.10368  ? 10  ILE   D CG2   1 
ATOM   4076 C  CD1   . ILE   D 2 11  ? 16.77589  43.00797  14.14232  1.000 25.50775  ? 10  ILE   D CD1   1 
ATOM   4077 N  N     . ALA   D 2 12  ? 12.19642  43.59190  15.65311  1.000 26.79383  ? 11  ALA   D N     1 
ATOM   4078 C  CA    . ALA   D 2 12  ? 10.93269  43.37915  16.34499  1.000 26.23519  ? 11  ALA   D CA    1 
ATOM   4079 C  C     . ALA   D 2 12  ? 10.86828  41.94847  16.86907  1.000 31.21361  ? 11  ALA   D C     1 
ATOM   4080 O  O     . ALA   D 2 12  ? 11.49042  41.02742  16.32192  1.000 27.24135  ? 11  ALA   D O     1 
ATOM   4081 C  CB    . ALA   D 2 12  ? 9.72738   43.65941  15.42580  1.000 29.63205  ? 11  ALA   D CB    1 
ATOM   4082 N  N     . VAL   D 2 13  ? 10.09430  41.77368  17.94580  1.000 27.59689  ? 12  VAL   D N     1 
ATOM   4083 C  CA    . VAL   D 2 13  ? 9.87634   40.47948  18.58790  1.000 26.96524  ? 12  VAL   D CA    1 
ATOM   4084 C  C     . VAL   D 2 13  ? 8.37376   40.24447  18.61988  1.000 34.60087  ? 12  VAL   D C     1 
ATOM   4085 O  O     . VAL   D 2 13  ? 7.64563   40.98175  19.29781  1.000 34.84129  ? 12  VAL   D O     1 
ATOM   4086 C  CB    . VAL   D 2 13  ? 10.46239  40.43212  20.00346  1.000 26.10987  ? 12  VAL   D CB    1 
ATOM   4087 C  CG1   . VAL   D 2 13  ? 10.20785  39.07845  20.63312  1.000 26.40728  ? 12  VAL   D CG1   1 
ATOM   4088 C  CG2   . VAL   D 2 13  ? 11.96243  40.76770  19.97026  1.000 30.45613  ? 12  VAL   D CG2   1 
ATOM   4089 N  N     . ASP   D 2 14  ? 7.90791   39.23604  17.88591  1.000 28.94179  ? 13  ASP   D N     1 
ATOM   4090 C  CA    . ASP   D 2 14  ? 6.47103   39.02508  17.65901  1.000 32.85283  ? 13  ASP   D CA    1 
ATOM   4091 C  C     . ASP   D 2 14  ? 5.76801   40.34125  17.32467  1.000 39.55639  ? 13  ASP   D C     1 
ATOM   4092 O  O     . ASP   D 2 14  ? 4.73588   40.69668  17.90462  1.000 39.98017  ? 13  ASP   D O     1 
ATOM   4093 C  CB    . ASP   D 2 14  ? 5.81661   38.34780  18.86533  1.000 36.67827  ? 13  ASP   D CB    1 
ATOM   4094 C  CG    . ASP   D 2 14  ? 6.09240   36.86600  18.90996  1.000 40.88474  ? 13  ASP   D CG    1 
ATOM   4095 O  OD1   . ASP   D 2 14  ? 6.47970   36.31316  17.85888  1.000 33.68442  ? 13  ASP   D OD1   1 
ATOM   4096 O  OD2   . ASP   D 2 14  ? 5.92183   36.25720  19.98571  1.000 42.11647  ? 13  ASP   D OD2   1 
ATOM   4097 N  N     . GLY   D 2 15  ? 6.35990   41.09045  16.39067  1.000 36.92119  ? 14  GLY   D N     1 
ATOM   4098 C  CA    . GLY   D 2 15  ? 5.79082   42.34437  15.92868  1.000 37.37953  ? 14  GLY   D CA    1 
ATOM   4099 C  C     . GLY   D 2 15  ? 5.97189   43.52894  16.85314  1.000 36.83484  ? 14  GLY   D C     1 
ATOM   4100 O  O     . GLY   D 2 15  ? 5.64673   44.65815  16.45887  1.000 48.95792  ? 14  GLY   D O     1 
ATOM   4101 N  N     . GLU   D 2 16  ? 6.46606   43.32693  18.03917  1.000 34.90830  ? 15  GLU   D N     1 
ATOM   4102 C  CA    . GLU   D 2 16  ? 6.66773   44.41688  18.98592  1.000 37.76973  ? 15  GLU   D CA    1 
ATOM   4103 C  C     . GLU   D 2 16  ? 8.08174   44.95935  18.85547  1.000 38.52983  ? 15  GLU   D C     1 
ATOM   4104 O  O     . GLU   D 2 16  ? 9.03415   44.17263  18.81754  1.000 35.18620  ? 15  GLU   D O     1 
ATOM   4105 C  CB    . GLU   D 2 16  ? 6.42959   43.94434  20.40903  1.000 41.30782  ? 15  GLU   D CB    1 
ATOM   4106 C  CG    . GLU   D 2 16  ? 5.00295   43.39882  20.63943  1.000 49.36899  ? 15  GLU   D CG    1 
ATOM   4107 C  CD    . GLU   D 2 16  ? 3.90591   44.19810  19.95354  1.000 60.11874  ? 15  GLU   D CD    1 
ATOM   4108 O  OE1   . GLU   D 2 16  ? 3.84432   45.46035  20.10580  1.000 60.74952  ? 15  GLU   D OE1   1 
ATOM   4109 O  OE2   . GLU   D 2 16  ? 3.07521   43.56989  19.21440  1.000 72.65676  ? 15  GLU   D OE2   1 
ATOM   4110 N  N     . PRO   D 2 17  ? 8.25748   46.27621  18.80701  1.000 44.92263  ? 16  PRO   D N     1 
ATOM   4111 C  CA    . PRO   D 2 17  ? 9.59564   46.83497  18.59262  1.000 36.68992  ? 16  PRO   D CA    1 
ATOM   4112 C  C     . PRO   D 2 17  ? 10.54040  46.47149  19.72860  1.000 39.96599  ? 16  PRO   D C     1 
ATOM   4113 O  O     . PRO   D 2 17  ? 10.17652  46.51656  20.90453  1.000 37.18145  ? 16  PRO   D O     1 
ATOM   4114 C  CB    . PRO   D 2 17  ? 9.34525   48.34590  18.54031  1.000 43.36263  ? 16  PRO   D CB    1 
ATOM   4115 C  CG    . PRO   D 2 17  ? 8.08956   48.53818  19.36171  1.000 42.77340  ? 16  PRO   D CG    1 
ATOM   4116 C  CD    . PRO   D 2 17  ? 7.25350   47.32393  19.07264  1.000 41.26986  ? 16  PRO   D CD    1 
ATOM   4117 N  N     . LEU   D 2 18  ? 11.77118  46.10900  19.36411  1.000 30.52453  ? 17  LEU   D N     1 
ATOM   4118 C  CA    . LEU   D 2 18  ? 12.83757  45.92270  20.33716  1.000 28.14169  ? 17  LEU   D CA    1 
ATOM   4119 C  C     . LEU   D 2 18  ? 13.85068  47.05950  20.27079  1.000 34.72939  ? 17  LEU   D C     1 
ATOM   4120 O  O     . LEU   D 2 18  ? 14.12315  47.69356  21.29599  1.000 28.99443  ? 17  LEU   D O     1 
ATOM   4121 C  CB    . LEU   D 2 18  ? 13.51507  44.55749  20.12558  1.000 30.27835  ? 17  LEU   D CB    1 
ATOM   4122 C  CG    . LEU   D 2 18  ? 14.70531  44.18886  21.00950  1.000 31.50708  ? 17  LEU   D CG    1 
ATOM   4123 C  CD1   . LEU   D 2 18  ? 14.34695  44.04792  22.50468  1.000 27.02925  ? 17  LEU   D CD1   1 
ATOM   4124 C  CD2   . LEU   D 2 18  ? 15.36916  42.91436  20.50244  1.000 32.96638  ? 17  LEU   D CD2   1 
ATOM   4125 N  N     . GLY   D 2 19  ? 14.38745  47.35957  19.09102  1.000 29.93762  ? 18  GLY   D N     1 
ATOM   4126 C  CA    . GLY   D 2 19  ? 15.35723  48.43049  18.97493  1.000 28.89287  ? 18  GLY   D CA    1 
ATOM   4127 C  C     . GLY   D 2 19  ? 16.17466  48.30580  17.70473  1.000 30.21081  ? 18  GLY   D C     1 
ATOM   4128 O  O     . GLY   D 2 19  ? 16.00809  47.37490  16.91201  1.000 29.07992  ? 18  GLY   D O     1 
ATOM   4129 N  N     . ARG   D 2 20  ? 17.06399  49.28109  17.52792  1.000 30.37414  ? 19  ARG   D N     1 
ATOM   4130 C  CA    . ARG   D 2 20  ? 17.84114  49.42515  16.30107  1.000 32.64042  ? 19  ARG   D CA    1 
ATOM   4131 C  C     . ARG   D 2 20  ? 19.27557  48.94977  16.49569  1.000 32.43199  ? 19  ARG   D C     1 
ATOM   4132 O  O     . ARG   D 2 20  ? 19.95485  49.36500  17.44968  1.000 31.60909  ? 19  ARG   D O     1 
ATOM   4133 C  CB    . ARG   D 2 20  ? 17.83528  50.88153  15.82848  1.000 36.63791  ? 19  ARG   D CB    1 
ATOM   4134 C  CG    . ARG   D 2 20  ? 18.72441  51.13286  14.60132  1.000 41.72098  ? 19  ARG   D CG    1 
ATOM   4135 C  CD    . ARG   D 2 20  ? 18.44714  52.49073  13.96024  1.000 29.17340  ? 19  ARG   D CD    1 
ATOM   4136 N  NE    . ARG   D 2 20  ? 17.17811  52.49287  13.24397  1.000 33.27652  ? 19  ARG   D NE    1 
ATOM   4137 C  CZ    . ARG   D 2 20  ? 16.77980  53.47234  12.44804  1.000 37.17047  ? 19  ARG   D CZ    1 
ATOM   4138 N  NH1   . ARG   D 2 20  ? 17.52966  54.54276  12.25190  1.000 41.30108  ? 19  ARG   D NH1   1 
ATOM   4139 N  NH2   . ARG   D 2 20  ? 15.60739  53.36910  11.82486  1.000 38.34715  ? 19  ARG   D NH2   1 
ATOM   4140 N  N     . VAL   D 2 21  ? 19.74008  48.10228  15.57371  1.000 28.43571  ? 20  VAL   D N     1 
ATOM   4141 C  CA    . VAL   D 2 21  ? 21.15948  47.77230  15.43635  1.000 28.44813  ? 20  VAL   D CA    1 
ATOM   4142 C  C     . VAL   D 2 21  ? 21.64924  48.38424  14.13552  1.000 26.12830  ? 20  VAL   D C     1 
ATOM   4143 O  O     . VAL   D 2 21  ? 20.97133  48.30797  13.10569  1.000 27.02279  ? 20  VAL   D O     1 
ATOM   4144 C  CB    . VAL   D 2 21  ? 21.42549  46.25440  15.44624  1.000 28.29522  ? 20  VAL   D CB    1 
ATOM   4145 C  CG1   . VAL   D 2 21  ? 22.92551  45.96238  15.66641  1.000 28.55538  ? 20  VAL   D CG1   1 
ATOM   4146 C  CG2   . VAL   D 2 21  ? 20.63061  45.58852  16.50553  1.000 36.68183  ? 20  VAL   D CG2   1 
ATOM   4147 N  N     . SER   D 2 22  ? 22.81585  49.00218  14.19417  1.000 31.83748  ? 21  SER   D N     1 
ATOM   4148 C  CA    . SER   D 2 22  ? 23.49812  49.53073  13.02340  1.000 36.61294  ? 21  SER   D CA    1 
ATOM   4149 C  C     . SER   D 2 22  ? 24.83426  48.81610  12.86011  1.000 27.46602  ? 21  SER   D C     1 
ATOM   4150 O  O     . SER   D 2 22  ? 25.42644  48.34919  13.83655  1.000 29.01680  ? 21  SER   D O     1 
ATOM   4151 C  CB    . SER   D 2 22  ? 23.72262  51.03307  13.15635  1.000 34.47901  ? 21  SER   D CB    1 
ATOM   4152 O  OG    . SER   D 2 22  ? 24.63220  51.29836  14.20440  1.000 35.87596  ? 21  SER   D OG    1 
ATOM   4153 N  N     . PHE   D 2 23  ? 25.30498  48.72842  11.61553  1.000 29.15975  ? 22  PHE   D N     1 
ATOM   4154 C  CA    . PHE   D 2 23  ? 26.53977  48.02028  11.31007  1.000 27.91979  ? 22  PHE   D CA    1 
ATOM   4155 C  C     . PHE   D 2 23  ? 27.43181  48.89303  10.45082  1.000 24.69824  ? 22  PHE   D C     1 
ATOM   4156 O  O     . PHE   D 2 23  ? 26.95657  49.54863  9.52113   1.000 29.64322  ? 22  PHE   D O     1 
ATOM   4157 C  CB    . PHE   D 2 23  ? 26.30009  46.70616  10.54554  1.000 29.00275  ? 22  PHE   D CB    1 
ATOM   4158 C  CG    . PHE   D 2 23  ? 25.22942  45.82424  11.13506  1.000 26.65071  ? 22  PHE   D CG    1 
ATOM   4159 C  CD1   . PHE   D 2 23  ? 23.91221  45.96437  10.74183  1.000 30.49846  ? 22  PHE   D CD1   1 
ATOM   4160 C  CD2   . PHE   D 2 23  ? 25.54829  44.82675  12.04544  1.000 26.37756  ? 22  PHE   D CD2   1 
ATOM   4161 C  CE1   . PHE   D 2 23  ? 22.91142  45.14983  11.26744  1.000 27.53082  ? 22  PHE   D CE1   1 
ATOM   4162 C  CE2   . PHE   D 2 23  ? 24.54491  44.01315  12.57947  1.000 29.55978  ? 22  PHE   D CE2   1 
ATOM   4163 C  CZ    . PHE   D 2 23  ? 23.23251  44.17384  12.17907  1.000 28.03330  ? 22  PHE   D CZ    1 
ATOM   4164 N  N     . GLU   D 2 24  ? 28.72186  48.86882  10.74138  1.000 27.39605  ? 23  GLU   D N     1 
ATOM   4165 C  CA    . GLU   D 2 24  ? 29.71201  49.35003  9.78425   1.000 27.84744  ? 23  GLU   D CA    1 
ATOM   4166 C  C     . GLU   D 2 24  ? 30.02409  48.22226  8.80615   1.000 29.18972  ? 23  GLU   D C     1 
ATOM   4167 O  O     . GLU   D 2 24  ? 30.27070  47.09137  9.22731   1.000 27.53283  ? 23  GLU   D O     1 
ATOM   4168 C  CB    . GLU   D 2 24  ? 30.98636  49.81131  10.48646  1.000 30.57655  ? 23  GLU   D CB    1 
ATOM   4169 C  CG    . GLU   D 2 24  ? 32.10315  50.13723  9.48498   1.000 34.04671  ? 23  GLU   D CG    1 
ATOM   4170 C  CD    . GLU   D 2 24  ? 33.38800  50.61949  10.12890  1.000 40.62817  ? 23  GLU   D CD    1 
ATOM   4171 O  OE1   . GLU   D 2 24  ? 33.50138  50.56932  11.36778  1.000 33.35285  ? 23  GLU   D OE1   1 
ATOM   4172 O  OE2   . GLU   D 2 24  ? 34.30727  51.03801  9.38082   1.000 40.47009  ? 23  GLU   D OE2   1 
ATOM   4173 N  N     . LEU   D 2 25  ? 30.02075  48.52823  7.50796   1.000 29.17428  ? 24  LEU   D N     1 
ATOM   4174 C  CA    . LEU   D 2 25  ? 30.34866  47.55555  6.46699   1.000 28.51239  ? 24  LEU   D CA    1 
ATOM   4175 C  C     . LEU   D 2 25  ? 31.73874  47.85507  5.92968   1.000 30.76272  ? 24  LEU   D C     1 
ATOM   4176 O  O     . LEU   D 2 25  ? 32.01043  48.98713  5.51658   1.000 33.12213  ? 24  LEU   D O     1 
ATOM   4177 C  CB    . LEU   D 2 25  ? 29.34873  47.60468  5.31684   1.000 26.96082  ? 24  LEU   D CB    1 
ATOM   4178 C  CG    . LEU   D 2 25  ? 27.87299  47.47140  5.70036   1.000 27.82901  ? 24  LEU   D CG    1 
ATOM   4179 C  CD1   . LEU   D 2 25  ? 26.98024  47.37993  4.45635   1.000 28.35638  ? 24  LEU   D CD1   1 
ATOM   4180 C  CD2   . LEU   D 2 25  ? 27.70109  46.26083  6.62646   1.000 25.29328  ? 24  LEU   D CD2   1 
ATOM   4181 N  N     . PHE   D 2 26  ? 32.60073  46.84077  5.90928   1.000 27.19696  ? 25  PHE   D N     1 
ATOM   4182 C  CA    . PHE   D 2 26  ? 34.01342  47.03879  5.57936   1.000 27.41714  ? 25  PHE   D CA    1 
ATOM   4183 C  C     . PHE   D 2 26  ? 34.23015  47.02628  4.06426   1.000 30.77892  ? 25  PHE   D C     1 
ATOM   4184 O  O     . PHE   D 2 26  ? 34.91665  46.16701  3.50568   1.000 32.82205  ? 25  PHE   D O     1 
ATOM   4185 C  CB    . PHE   D 2 26  ? 34.86188  45.97818  6.26481   1.000 28.60631  ? 25  PHE   D CB    1 
ATOM   4186 C  CG    . PHE   D 2 26  ? 34.77265  46.00616  7.75564   1.000 26.86588  ? 25  PHE   D CG    1 
ATOM   4187 C  CD1   . PHE   D 2 26  ? 34.72540  47.20356  8.43663   1.000 32.28702  ? 25  PHE   D CD1   1 
ATOM   4188 C  CD2   . PHE   D 2 26  ? 34.71453  44.82750  8.47409   1.000 31.57822  ? 25  PHE   D CD2   1 
ATOM   4189 C  CE1   . PHE   D 2 26  ? 34.64300  47.23026  9.82482   1.000 32.86711  ? 25  PHE   D CE1   1 
ATOM   4190 C  CE2   . PHE   D 2 26  ? 34.63609  44.84120  9.86371   1.000 29.77485  ? 25  PHE   D CE2   1 
ATOM   4191 C  CZ    . PHE   D 2 26  ? 34.59884  46.04493  10.53310  1.000 28.81477  ? 25  PHE   D CZ    1 
ATOM   4192 N  N     . ALA   D 2 27  ? 33.62320  48.01332  3.39904   1.000 30.49610  ? 26  ALA   D N     1 
ATOM   4193 C  CA    . ALA   D 2 27  ? 33.80444  48.14883  1.95645   1.000 35.45063  ? 26  ALA   D CA    1 
ATOM   4194 C  C     . ALA   D 2 27  ? 35.26877  48.33893  1.59334   1.000 31.49189  ? 26  ALA   D C     1 
ATOM   4195 O  O     . ALA   D 2 27  ? 35.67198  47.99882  0.47637   1.000 31.71982  ? 26  ALA   D O     1 
ATOM   4196 C  CB    . ALA   D 2 27  ? 32.97390  49.31508  1.41687   1.000 32.11962  ? 26  ALA   D CB    1 
ATOM   4197 N  N     . ASP   D 2 28  ? 36.08056  48.85175  2.52346   1.000 32.81665  ? 27  ASP   D N     1 
ATOM   4198 C  CA    . ASP   D 2 28  ? 37.49149  49.07839  2.23100   1.000 35.17352  ? 27  ASP   D CA    1 
ATOM   4199 C  C     . ASP   D 2 28  ? 38.28892  47.78271  2.14202   1.000 43.73599  ? 27  ASP   D C     1 
ATOM   4200 O  O     . ASP   D 2 28  ? 39.35184  47.77227  1.50715   1.000 44.72292  ? 27  ASP   D O     1 
ATOM   4201 C  CB    . ASP   D 2 28  ? 38.11192  50.01366  3.27409   1.000 39.80719  ? 27  ASP   D CB    1 
ATOM   4202 C  CG    . ASP   D 2 28  ? 37.98594  49.49028  4.69259   1.000 41.82325  ? 27  ASP   D CG    1 
ATOM   4203 O  OD1   . ASP   D 2 28  ? 37.01629  48.75621  4.97919   1.000 39.28672  ? 27  ASP   D OD1   1 
ATOM   4204 O  OD2   . ASP   D 2 28  ? 38.84939  49.83037  5.52503   1.000 47.59207  ? 27  ASP   D OD2   1 
ATOM   4205 N  N     . LYS   D 2 29  ? 37.80689  46.69484  2.74248   1.000 34.40367  ? 28  LYS   D N     1 
ATOM   4206 C  CA    . LYS   D 2 29  ? 38.48643  45.40311  2.70763   1.000 30.71183  ? 28  LYS   D CA    1 
ATOM   4207 C  C     . LYS   D 2 29  ? 37.76150  44.36152  1.87230   1.000 34.57980  ? 28  LYS   D C     1 
ATOM   4208 O  O     . LYS   D 2 29  ? 38.40926  43.52501  1.24386   1.000 32.31156  ? 28  LYS   D O     1 
ATOM   4209 C  CB    . LYS   D 2 29  ? 38.64914  44.84887  4.12246   1.000 37.49954  ? 28  LYS   D CB    1 
ATOM   4210 C  CG    . LYS   D 2 29  ? 39.42613  45.74125  5.05966   1.000 42.10323  ? 28  LYS   D CG    1 
ATOM   4211 C  CD    . LYS   D 2 29  ? 40.89471  45.75751  4.70441   1.000 43.60924  ? 28  LYS   D CD    1 
ATOM   4212 C  CE    . LYS   D 2 29  ? 41.74703  45.83214  5.97238   1.000 50.95872  ? 28  LYS   D CE    1 
ATOM   4213 N  NZ    . LYS   D 2 29  ? 41.27561  46.91329  6.87324   1.000 50.43101  ? 28  LYS   D NZ    1 
ATOM   4214 N  N     . VAL   D 2 30  ? 36.43231  44.36158  1.89657   1.000 28.46357  ? 29  VAL   D N     1 
ATOM   4215 C  CA    . VAL   D 2 30  ? 35.61830  43.37512  1.18845   1.000 28.18402  ? 29  VAL   D CA    1 
ATOM   4216 C  C     . VAL   D 2 30  ? 34.52124  44.13739  0.46185   1.000 30.66805  ? 29  VAL   D C     1 
ATOM   4217 O  O     . VAL   D 2 30  ? 33.34692  44.07289  0.86259   1.000 28.87505  ? 29  VAL   D O     1 
ATOM   4218 C  CB    . VAL   D 2 30  ? 35.03245  42.31863  2.14694   1.000 29.11411  ? 29  VAL   D CB    1 
ATOM   4219 C  CG1   . VAL   D 2 30  ? 35.98933  41.16298  2.31788   1.000 28.61204  ? 29  VAL   D CG1   1 
ATOM   4220 C  CG2   . VAL   D 2 30  ? 34.74077  42.94445  3.49219   1.000 32.73038  ? 29  VAL   D CG2   1 
ATOM   4221 N  N     . PRO   D 2 31  ? 34.85826  44.88996  -0.59135  1.000 31.58272  ? 30  PRO   D N     1 
ATOM   4222 C  CA    . PRO   D 2 31  ? 33.84994  45.75378  -1.22243  1.000 28.52357  ? 30  PRO   D CA    1 
ATOM   4223 C  C     . PRO   D 2 31  ? 32.68576  44.99497  -1.83272  1.000 28.71808  ? 30  PRO   D C     1 
ATOM   4224 O  O     . PRO   D 2 31  ? 31.55608  45.48792  -1.78290  1.000 36.56645  ? 30  PRO   D O     1 
ATOM   4225 C  CB    . PRO   D 2 31  ? 34.65956  46.51314  -2.29482  1.000 36.62898  ? 30  PRO   D CB    1 
ATOM   4226 C  CG    . PRO   D 2 31  ? 35.91233  45.68629  -2.50383  1.000 30.13636  ? 30  PRO   D CG    1 
ATOM   4227 C  CD    . PRO   D 2 31  ? 36.20345  45.07881  -1.16503  1.000 29.73196  ? 30  PRO   D CD    1 
ATOM   4228 N  N     . LYS   D 2 32  ? 32.91315  43.81906  -2.41870  1.000 29.81821  ? 31  LYS   D N     1 
ATOM   4229 C  CA    . LYS   D 2 32  ? 31.81760  43.14772  -3.11786  1.000 25.80194  ? 31  LYS   D CA    1 
ATOM   4230 C  C     . LYS   D 2 32  ? 30.83268  42.53959  -2.13046  1.000 27.70283  ? 31  LYS   D C     1 
ATOM   4231 O  O     . LYS   D 2 32  ? 29.61681  42.54867  -2.36569  1.000 30.32626  ? 31  LYS   D O     1 
ATOM   4232 C  CB    . LYS   D 2 32  ? 32.35934  42.07069  -4.05327  1.000 29.59187  ? 31  LYS   D CB    1 
ATOM   4233 C  CG    . LYS   D 2 32  ? 31.28630  41.37326  -4.86813  1.000 33.25684  ? 31  LYS   D CG    1 
ATOM   4234 C  CD    . LYS   D 2 32  ? 31.89510  40.41877  -5.87903  1.000 37.14804  ? 31  LYS   D CD    1 
ATOM   4235 C  CE    . LYS   D 2 32  ? 30.81416  39.68291  -6.65300  1.000 35.22064  ? 31  LYS   D CE    1 
ATOM   4236 N  NZ    . LYS   D 2 32  ? 31.42097  38.80578  -7.68122  1.000 42.56185  ? 31  LYS   D NZ    1 
ATOM   4237 N  N     . THR   D 2 33  ? 31.34980  42.00512  -1.02437  1.000 25.56495  ? 32  THR   D N     1 
ATOM   4238 C  CA    . THR   D 2 33  ? 30.48530  41.43388  0.00661   1.000 23.05064  ? 32  THR   D CA    1 
ATOM   4239 C  C     . THR   D 2 33  ? 29.75975  42.53125  0.77714   1.000 26.86904  ? 32  THR   D C     1 
ATOM   4240 O  O     . THR   D 2 33  ? 28.56563  42.40275  1.07735   1.000 25.67252  ? 32  THR   D O     1 
ATOM   4241 C  CB    . THR   D 2 33  ? 31.32548  40.56374  0.93722   1.000 25.80166  ? 32  THR   D CB    1 
ATOM   4242 O  OG1   . THR   D 2 33  ? 32.13704  39.66085  0.15180   1.000 25.74949  ? 32  THR   D OG1   1 
ATOM   4243 C  CG2   . THR   D 2 33  ? 30.45458  39.76414  1.91512   1.000 23.57600  ? 32  THR   D CG2   1 
ATOM   4244 N  N     . ALA   D 2 34  ? 30.46161  43.61591  1.11381   1.000 26.90030  ? 33  ALA   D N     1 
ATOM   4245 C  CA    . ALA   D 2 34  ? 29.79599  44.73860  1.76375   1.000 27.11717  ? 33  ALA   D CA    1 
ATOM   4246 C  C     . ALA   D 2 34  ? 28.67473  45.28506  0.88962   1.000 30.76678  ? 33  ALA   D C     1 
ATOM   4247 O  O     . ALA   D 2 34  ? 27.58811  45.60489  1.37965   1.000 27.07647  ? 33  ALA   D O     1 
ATOM   4248 C  CB    . ALA   D 2 34  ? 30.81021  45.83342  2.09224   1.000 31.34502  ? 33  ALA   D CB    1 
ATOM   4249 N  N     . GLU   D 2 35  ? 28.91071  45.37191  -0.41961  1.000 30.19354  ? 34  GLU   D N     1 
ATOM   4250 C  CA    . GLU   D 2 35  ? 27.89675  45.93893  -1.29795  1.000 28.51571  ? 34  GLU   D CA    1 
ATOM   4251 C  C     . GLU   D 2 35  ? 26.66011  45.04662  -1.37640  1.000 26.25031  ? 34  GLU   D C     1 
ATOM   4252 O  O     . GLU   D 2 35  ? 25.53366  45.54856  -1.42868  1.000 25.75823  ? 34  GLU   D O     1 
ATOM   4253 C  CB    . GLU   D 2 35  ? 28.50794  46.17524  -2.68489  1.000 29.32939  ? 34  GLU   D CB    1 
ATOM   4254 C  CG    . GLU   D 2 35  ? 27.51630  46.58943  -3.75724  1.000 36.08489  ? 34  GLU   D CG    1 
ATOM   4255 C  CD    . GLU   D 2 35  ? 26.98294  47.99260  -3.56305  1.000 37.40596  ? 34  GLU   D CD    1 
ATOM   4256 O  OE1   . GLU   D 2 35  ? 27.48376  48.72354  -2.67466  1.000 35.58244  ? 34  GLU   D OE1   1 
ATOM   4257 O  OE2   . GLU   D 2 35  ? 26.05603  48.36336  -4.30782  1.000 41.33275  ? 34  GLU   D OE2   1 
ATOM   4258 N  N     . ASN   D 2 36  ? 26.85165  43.72374  -1.40834  1.000 26.32048  ? 35  ASN   D N     1 
ATOM   4259 C  CA    . ASN   D 2 36  ? 25.72652  42.79766  -1.35992  1.000 28.07176  ? 35  ASN   D CA    1 
ATOM   4260 C  C     . ASN   D 2 36  ? 24.85105  43.06233  -0.14010  1.000 25.87827  ? 35  ASN   D C     1 
ATOM   4261 O  O     . ASN   D 2 36  ? 23.62961  43.18352  -0.25037  1.000 26.60656  ? 35  ASN   D O     1 
ATOM   4262 C  CB    . ASN   D 2 36  ? 26.24180  41.35614  -1.34720  1.000 30.32554  ? 35  ASN   D CB    1 
ATOM   4263 C  CG    . ASN   D 2 36  ? 25.11644  40.33417  -1.34322  1.000 29.59327  ? 35  ASN   D CG    1 
ATOM   4264 O  OD1   . ASN   D 2 36  ? 24.29703  40.29622  -2.25858  1.000 26.54799  ? 35  ASN   D OD1   1 
ATOM   4265 N  ND2   . ASN   D 2 36  ? 25.06578  39.50868  -0.30381  1.000 27.40077  ? 35  ASN   D ND2   1 
ATOM   4266 N  N     . PHE   D 2 37  ? 25.46870  43.18061  1.03151   1.000 26.66198  ? 36  PHE   D N     1 
ATOM   4267 C  CA    . PHE   D 2 37  ? 24.69977  43.41404  2.25354   1.000 26.57605  ? 36  PHE   D CA    1 
ATOM   4268 C  C     . PHE   D 2 37  ? 24.04204  44.78888  2.23689   1.000 29.49494  ? 36  PHE   D C     1 
ATOM   4269 O  O     . PHE   D 2 37  ? 22.87808  44.93078  2.63024   1.000 30.76961  ? 36  PHE   D O     1 
ATOM   4270 C  CB    . PHE   D 2 37  ? 25.61786  43.26100  3.46864   1.000 22.00648  ? 36  PHE   D CB    1 
ATOM   4271 C  CG    . PHE   D 2 37  ? 24.89292  43.19539  4.79974   1.000 23.35146  ? 36  PHE   D CG    1 
ATOM   4272 C  CD1   . PHE   D 2 37  ? 24.42045  41.98752  5.28495   1.000 23.51494  ? 36  PHE   D CD1   1 
ATOM   4273 C  CD2   . PHE   D 2 37  ? 24.75184  44.32911  5.57751   1.000 25.62454  ? 36  PHE   D CD2   1 
ATOM   4274 C  CE1   . PHE   D 2 37  ? 23.76807  41.91741  6.52268   1.000 26.05094  ? 36  PHE   D CE1   1 
ATOM   4275 C  CE2   . PHE   D 2 37  ? 24.11278  44.27478  6.83087   1.000 31.38114  ? 36  PHE   D CE2   1 
ATOM   4276 C  CZ    . PHE   D 2 37  ? 23.62754  43.07212  7.29734   1.000 25.80353  ? 36  PHE   D CZ    1 
ATOM   4277 N  N     . ARG   D 2 38  ? 24.76908  45.81255  1.77922   1.000 25.97089  ? 37  ARG   D N     1 
ATOM   4278 C  CA    . ARG   D 2 38  ? 24.21040  47.15992  1.72406   1.000 28.26835  ? 37  ARG   D CA    1 
ATOM   4279 C  C     . ARG   D 2 38  ? 22.96157  47.19088  0.85415   1.000 30.68410  ? 37  ARG   D C     1 
ATOM   4280 O  O     . ARG   D 2 38  ? 21.90174  47.66598  1.27721   1.000 28.09695  ? 37  ARG   D O     1 
ATOM   4281 C  CB    . ARG   D 2 38  ? 25.25244  48.14469  1.18194   1.000 29.83994  ? 37  ARG   D CB    1 
ATOM   4282 C  CG    . ARG   D 2 38  ? 24.85991  49.61657  1.33465   1.000 32.83015  ? 37  ARG   D CG    1 
ATOM   4283 C  CD    . ARG   D 2 38  ? 25.62825  50.53112  0.37794   1.000 32.34086  ? 37  ARG   D CD    1 
ATOM   4284 N  NE    . ARG   D 2 38  ? 25.38080  50.14932  -1.01109  1.000 35.62943  ? 37  ARG   D NE    1 
ATOM   4285 C  CZ    . ARG   D 2 38  ? 24.25751  50.40075  -1.67150  1.000 36.56902  ? 37  ARG   D CZ    1 
ATOM   4286 N  NH1   . ARG   D 2 38  ? 23.25812  51.06483  -1.11197  1.000 35.56627  ? 37  ARG   D NH1   1 
ATOM   4287 N  NH2   . ARG   D 2 38  ? 24.13337  49.97510  -2.92703  1.000 36.92696  ? 37  ARG   D NH2   1 
ATOM   4288 N  N     . ALA   D 2 39  ? 23.07182  46.66941  -0.36690  1.000 30.44787  ? 38  ALA   D N     1 
ATOM   4289 C  CA    . ALA   D 2 39  ? 21.95406  46.70275  -1.29849  1.000 30.44475  ? 38  ALA   D CA    1 
ATOM   4290 C  C     . ALA   D 2 39  ? 20.77327  45.90402  -0.77542  1.000 35.87130  ? 38  ALA   D C     1 
ATOM   4291 O  O     . ALA   D 2 39  ? 19.61848  46.28781  -0.98420  1.000 33.26679  ? 38  ALA   D O     1 
ATOM   4292 C  CB    . ALA   D 2 39  ? 22.38700  46.17147  -2.66533  1.000 30.97361  ? 38  ALA   D CB    1 
ATOM   4293 N  N     . LEU   D 2 40  ? 21.03712  44.77775  -0.11022  1.000 31.41960  ? 39  LEU   D N     1 
ATOM   4294 C  CA    . LEU   D 2 40  ? 19.93035  43.99385  0.42008   1.000 29.06457  ? 39  LEU   D CA    1 
ATOM   4295 C  C     . LEU   D 2 40  ? 19.26275  44.70599  1.58483   1.000 28.06011  ? 39  LEU   D C     1 
ATOM   4296 O  O     . LEU   D 2 40  ? 18.06237  44.50927  1.81963   1.000 31.23637  ? 39  LEU   D O     1 
ATOM   4297 C  CB    . LEU   D 2 40  ? 20.40941  42.60424  0.83510   1.000 28.32031  ? 39  LEU   D CB    1 
ATOM   4298 C  CG    . LEU   D 2 40  ? 20.81294  41.66226  -0.28817  1.000 26.57186  ? 39  LEU   D CG    1 
ATOM   4299 C  CD1   . LEU   D 2 40  ? 21.47339  40.38266  0.23147   1.000 23.41842  ? 39  LEU   D CD1   1 
ATOM   4300 C  CD2   . LEU   D 2 40  ? 19.59502  41.34686  -1.17877  1.000 32.34975  ? 39  LEU   D CD2   1 
ATOM   4301 N  N     . SER   D 2 41  ? 20.01448  45.53985  2.31125   1.000 28.58122  ? 40  SER   D N     1 
ATOM   4302 C  CA    . SER   D 2 41  ? 19.44054  46.30027  3.41552   1.000 29.50500  ? 40  SER   D CA    1 
ATOM   4303 C  C     . SER   D 2 41  ? 18.61510  47.48380  2.93018   1.000 35.37666  ? 40  SER   D C     1 
ATOM   4304 O  O     . SER   D 2 41  ? 17.73599  47.95355  3.65923   1.000 32.42379  ? 40  SER   D O     1 
ATOM   4305 C  CB    . SER   D 2 41  ? 20.53777  46.80455  4.35132   1.000 30.47675  ? 40  SER   D CB    1 
ATOM   4306 O  OG    . SER   D 2 41  ? 21.30285  45.74259  4.89163   1.000 30.94036  ? 40  SER   D OG    1 
ATOM   4307 N  N     . THR   D 2 42  ? 18.88402  47.99048  1.71863   1.000 33.63887  ? 41  THR   D N     1 
ATOM   4308 C  CA    . THR   D 2 42  ? 18.05387  49.05532  1.16004   1.000 34.12453  ? 41  THR   D CA    1 
ATOM   4309 C  C     . THR   D 2 42  ? 16.88994  48.52459  0.33828   1.000 38.21179  ? 41  THR   D C     1 
ATOM   4310 O  O     . THR   D 2 42  ? 15.94796  49.27729  0.06434   1.000 37.22214  ? 41  THR   D O     1 
ATOM   4311 C  CB    . THR   D 2 42  ? 18.89224  49.99755  0.27791   1.000 37.99814  ? 41  THR   D CB    1 
ATOM   4312 O  OG1   . THR   D 2 42  ? 19.29827  49.30844  -0.91270  1.000 35.99264  ? 41  THR   D OG1   1 
ATOM   4313 C  CG2   . THR   D 2 42  ? 20.13758  50.50279  1.03001   1.000 32.20008  ? 41  THR   D CG2   1 
ATOM   4314 N  N     . GLY   D 2 43  ? 16.93721  47.25565  -0.06330  1.000 33.56953  ? 42  GLY   D N     1 
ATOM   4315 C  CA    . GLY   D 2 43  ? 15.93423  46.70422  -0.94859  1.000 37.09431  ? 42  GLY   D CA    1 
ATOM   4316 C  C     . GLY   D 2 43  ? 15.96034  47.27013  -2.35093  1.000 39.29699  ? 42  GLY   D C     1 
ATOM   4317 O  O     . GLY   D 2 43  ? 14.99630  47.08915  -3.09982  1.000 41.39669  ? 42  GLY   D O     1 
ATOM   4318 N  N     . GLU   D 2 44  ? 17.06000  47.91805  -2.74231  1.000 39.69330  ? 43  GLU   D N     1 
ATOM   4319 C  CA    . GLU   D 2 44  ? 17.08648  48.67151  -3.99011  1.000 43.64229  ? 43  GLU   D CA    1 
ATOM   4320 C  C     . GLU   D 2 44  ? 16.98157  47.78748  -5.23327  1.000 46.41667  ? 43  GLU   D C     1 
ATOM   4321 O  O     . GLU   D 2 44  ? 16.63022  48.29522  -6.30300  1.000 43.07859  ? 43  GLU   D O     1 
ATOM   4322 C  CB    . GLU   D 2 44  ? 18.35516  49.51664  -4.04139  1.000 45.07193  ? 43  GLU   D CB    1 
ATOM   4323 C  CG    . GLU   D 2 44  ? 19.61539  48.68671  -4.14212  1.000 45.93888  ? 43  GLU   D CG    1 
ATOM   4324 C  CD    . GLU   D 2 44  ? 20.86437  49.49257  -3.87656  1.000 44.86212  ? 43  GLU   D CD    1 
ATOM   4325 O  OE1   . GLU   D 2 44  ? 20.86369  50.29785  -2.91889  1.000 41.08272  ? 43  GLU   D OE1   1 
ATOM   4326 O  OE2   . GLU   D 2 44  ? 21.84674  49.31373  -4.62651  1.000 45.35137  ? 43  GLU   D OE2   1 
ATOM   4327 N  N     . LYS   D 2 45  ? 17.25979  46.48801  -5.13212  1.000 36.20845  ? 44  LYS   D N     1 
ATOM   4328 C  CA    . LYS   D 2 45  ? 17.10848  45.59631  -6.27748  1.000 41.79805  ? 44  LYS   D CA    1 
ATOM   4329 C  C     . LYS   D 2 45  ? 15.71572  44.98445  -6.37762  1.000 39.49569  ? 44  LYS   D C     1 
ATOM   4330 O  O     . LYS   D 2 45  ? 15.49043  44.14290  -7.25388  1.000 41.33275  ? 44  LYS   D O     1 
ATOM   4331 C  CB    . LYS   D 2 45  ? 18.15283  44.47136  -6.23272  1.000 41.39169  ? 44  LYS   D CB    1 
ATOM   4332 C  CG    . LYS   D 2 45  ? 19.59644  44.95469  -6.20931  1.000 46.33677  ? 44  LYS   D CG    1 
ATOM   4333 C  CD    . LYS   D 2 45  ? 19.89372  45.81679  -7.42771  1.000 49.65609  ? 44  LYS   D CD    1 
ATOM   4334 C  CE    . LYS   D 2 45  ? 21.38441  45.99529  -7.64148  1.000 48.31061  ? 44  LYS   D CE    1 
ATOM   4335 N  NZ    . LYS   D 2 45  ? 21.74825  45.78367  -9.07524  1.000 60.08075  ? 44  LYS   D NZ    1 
ATOM   4336 N  N     . GLY   D 2 46  ? 14.78039  45.38164  -5.51230  1.000 37.37964  ? 45  GLY   D N     1 
ATOM   4337 C  CA    . GLY   D 2 46  ? 13.45011  44.80598  -5.48720  1.000 35.26360  ? 45  GLY   D CA    1 
ATOM   4338 C  C     . GLY   D 2 46  ? 13.25572  43.68711  -4.48673  1.000 39.97381  ? 45  GLY   D C     1 
ATOM   4339 O  O     . GLY   D 2 46  ? 12.15199  43.13079  -4.40905  1.000 33.98190  ? 45  GLY   D O     1 
ATOM   4340 N  N     . PHE   D 2 47  ? 14.29350  43.34325  -3.72126  1.000 38.02287  ? 46  PHE   D N     1 
ATOM   4341 C  CA    . PHE   D 2 47  ? 14.22809  42.27897  -2.73317  1.000 31.33201  ? 46  PHE   D CA    1 
ATOM   4342 C  C     . PHE   D 2 47  ? 15.28388  42.56845  -1.67755  1.000 29.47904  ? 46  PHE   D C     1 
ATOM   4343 O  O     . PHE   D 2 47  ? 16.18364  43.38046  -1.89293  1.000 31.85530  ? 46  PHE   D O     1 
ATOM   4344 C  CB    . PHE   D 2 47  ? 14.43671  40.89871  -3.37654  1.000 32.29746  ? 46  PHE   D CB    1 
ATOM   4345 C  CG    . PHE   D 2 47  ? 15.68355  40.79809  -4.23922  1.000 38.19646  ? 46  PHE   D CG    1 
ATOM   4346 C  CD1   . PHE   D 2 47  ? 16.94017  40.66123  -3.66071  1.000 35.53645  ? 46  PHE   D CD1   1 
ATOM   4347 C  CD2   . PHE   D 2 47  ? 15.59188  40.81835  -5.62974  1.000 38.98929  ? 46  PHE   D CD2   1 
ATOM   4348 C  CE1   . PHE   D 2 47  ? 18.08286  40.55926  -4.44271  1.000 33.74770  ? 46  PHE   D CE1   1 
ATOM   4349 C  CE2   . PHE   D 2 47  ? 16.73435  40.71507  -6.42281  1.000 39.39726  ? 46  PHE   D CE2   1 
ATOM   4350 C  CZ    . PHE   D 2 47  ? 17.98709  40.58708  -5.82242  1.000 40.44407  ? 46  PHE   D CZ    1 
ATOM   4351 N  N     . GLY   D 2 48  ? 15.16247  41.91912  -0.52551  1.000 33.69906  ? 47  GLY   D N     1 
ATOM   4352 C  CA    . GLY   D 2 48  ? 16.17748  42.11755  0.49438   1.000 32.95814  ? 47  GLY   D CA    1 
ATOM   4353 C  C     . GLY   D 2 48  ? 15.67888  41.70860  1.87218   1.000 26.15878  ? 47  GLY   D C     1 
ATOM   4354 O  O     . GLY   D 2 48  ? 14.73650  40.93180  2.00508   1.000 28.53608  ? 47  GLY   D O     1 
ATOM   4355 N  N     . TYR   D 2 49  ? 16.33181  42.28116  2.88215   1.000 28.84039  ? 48  TYR   D N     1 
ATOM   4356 C  CA    . TYR   D 2 49  ? 16.19278  41.79206  4.25340   1.000 32.61683  ? 48  TYR   D CA    1 
ATOM   4357 C  C     . TYR   D 2 49  ? 14.89144  42.23147  4.92032   1.000 31.71437  ? 48  TYR   D C     1 
ATOM   4358 O  O     . TYR   D 2 49  ? 14.40384  41.53458  5.82014   1.000 31.43317  ? 48  TYR   D O     1 
ATOM   4359 C  CB    . TYR   D 2 49  ? 17.38081  42.26406  5.08673   1.000 27.97500  ? 48  TYR   D CB    1 
ATOM   4360 C  CG    . TYR   D 2 49  ? 18.70623  41.61773  4.71869   1.000 22.10055  ? 48  TYR   D CG    1 
ATOM   4361 C  CD1   . TYR   D 2 49  ? 18.79968  40.24934  4.49974   1.000 25.42744  ? 48  TYR   D CD1   1 
ATOM   4362 C  CD2   . TYR   D 2 49  ? 19.85083  42.38018  4.59408   1.000 23.64308  ? 48  TYR   D CD2   1 
ATOM   4363 C  CE1   . TYR   D 2 49  ? 20.01583  39.65989  4.16880   1.000 22.90559  ? 48  TYR   D CE1   1 
ATOM   4364 C  CE2   . TYR   D 2 49  ? 21.06911  41.80247  4.26781   1.000 25.10838  ? 48  TYR   D CE2   1 
ATOM   4365 C  CZ    . TYR   D 2 49  ? 21.13957  40.44425  4.05198   1.000 24.97217  ? 48  TYR   D CZ    1 
ATOM   4366 O  OH    . TYR   D 2 49  ? 22.34407  39.85989  3.73495   1.000 23.09189  ? 48  TYR   D OH    1 
ATOM   4367 N  N     . LYS   D 2 50  ? 14.32806  43.37492  4.52087   1.000 31.18130  ? 49  LYS   D N     1 
ATOM   4368 C  CA    . LYS   D 2 50  ? 13.13345  43.89995  5.18438   1.000 29.89454  ? 49  LYS   D CA    1 
ATOM   4369 C  C     . LYS   D 2 50  ? 12.05000  42.83636  5.29282   1.000 30.91045  ? 49  LYS   D C     1 
ATOM   4370 O  O     . LYS   D 2 50  ? 11.69635  42.18261  4.30722   1.000 32.41326  ? 49  LYS   D O     1 
ATOM   4371 C  CB    . LYS   D 2 50  ? 12.59419  45.11785  4.42924   1.000 33.42574  ? 49  LYS   D CB    1 
ATOM   4372 C  CG    . LYS   D 2 50  ? 11.52041  45.85354  5.21244   1.000 38.98526  ? 49  LYS   D CG    1 
ATOM   4373 C  CD    . LYS   D 2 50  ? 11.23540  47.24098  4.64524   1.000 43.36694  ? 49  LYS   D CD    1 
ATOM   4374 C  CE    . LYS   D 2 50  ? 10.09029  47.87613  5.40374   1.000 45.84381  ? 49  LYS   D CE    1 
ATOM   4375 N  NZ    . LYS   D 2 50  ? 8.87443   47.04253  5.24084   1.000 50.52416  ? 49  LYS   D NZ    1 
ATOM   4376 N  N     . GLY   D 2 51  ? 11.54729  42.64605  6.51085   1.000 32.69698  ? 50  GLY   D N     1 
ATOM   4377 C  CA    . GLY   D 2 51  ? 10.50534  41.67849  6.77059   1.000 27.88593  ? 50  GLY   D CA    1 
ATOM   4378 C  C     . GLY   D 2 51  ? 10.97681  40.27169  7.07496   1.000 32.89672  ? 50  GLY   D C     1 
ATOM   4379 O  O     . GLY   D 2 51  ? 10.15974  39.44701  7.49667   1.000 30.99910  ? 50  GLY   D O     1 
ATOM   4380 N  N     . SER   D 2 52  ? 12.25940  39.96361  6.87261   1.000 30.73535  ? 51  SER   D N     1 
ATOM   4381 C  CA    . SER   D 2 52  ? 12.76815  38.62260  7.13654   1.000 29.43550  ? 51  SER   D CA    1 
ATOM   4382 C  C     . SER   D 2 52  ? 13.11613  38.45977  8.62135   1.000 27.09147  ? 51  SER   D C     1 
ATOM   4383 O  O     . SER   D 2 52  ? 13.06647  39.40492  9.41251   1.000 28.02216  ? 51  SER   D O     1 
ATOM   4384 C  CB    . SER   D 2 52  ? 13.99004  38.32240  6.25807   1.000 27.39470  ? 51  SER   D CB    1 
ATOM   4385 O  OG    . SER   D 2 52  ? 15.08824  39.14474  6.60323   1.000 28.76431  ? 51  SER   D OG    1 
ATOM   4386 N  N     . CYS   D 2 53  ? 13.46247  37.23537  9.00454   1.000 25.39527  ? 52  CYS   D N     1 
ATOM   4387 C  CA    . CYS   D 2 53  ? 13.61658  36.91683  10.41864  1.000 22.26903  ? 52  CYS   D CA    1 
ATOM   4388 C  C     . CYS   D 2 53  ? 15.01293  36.38513  10.72684  1.000 25.66263  ? 52  CYS   D C     1 
ATOM   4389 O  O     . CYS   D 2 53  ? 15.77787  36.02012  9.84191   1.000 26.24046  ? 52  CYS   D O     1 
ATOM   4390 C  CB    . CYS   D 2 53  ? 12.56551  35.89119  10.86924  1.000 24.99395  ? 52  CYS   D CB    1 
ATOM   4391 S  SG    . CYS   D 2 53  ? 12.85833  34.20757  10.32033  1.000 32.88806  ? 52  CYS   D SG    1 
ATOM   4392 N  N     . PHE   D 2 54  ? 15.33148  36.32104  12.01642  1.000 24.71733  ? 53  PHE   D N     1 
ATOM   4393 C  CA    . PHE   D 2 54  ? 16.51627  35.58508  12.47572  1.000 22.70318  ? 53  PHE   D CA    1 
ATOM   4394 C  C     . PHE   D 2 54  ? 16.06820  34.17567  12.82896  1.000 24.01858  ? 53  PHE   D C     1 
ATOM   4395 O  O     . PHE   D 2 54  ? 15.42023  33.96274  13.86260  1.000 26.42305  ? 53  PHE   D O     1 
ATOM   4396 C  CB    . PHE   D 2 54  ? 17.15268  36.27755  13.67176  1.000 21.19487  ? 53  PHE   D CB    1 
ATOM   4397 C  CG    . PHE   D 2 54  ? 17.98488  37.47180  13.31656  1.000 22.42569  ? 53  PHE   D CG    1 
ATOM   4398 C  CD1   . PHE   D 2 54  ? 17.39420  38.70311  13.09026  1.000 25.04561  ? 53  PHE   D CD1   1 
ATOM   4399 C  CD2   . PHE   D 2 54  ? 19.37773  37.35791  13.20305  1.000 21.62243  ? 53  PHE   D CD2   1 
ATOM   4400 C  CE1   . PHE   D 2 54  ? 18.17115  39.81453  12.75819  1.000 27.96514  ? 53  PHE   D CE1   1 
ATOM   4401 C  CE2   . PHE   D 2 54  ? 20.15475  38.45456  12.89946  1.000 23.55149  ? 53  PHE   D CE2   1 
ATOM   4402 C  CZ    . PHE   D 2 54  ? 19.55436  39.69874  12.66839  1.000 25.92066  ? 53  PHE   D CZ    1 
ATOM   4403 N  N     . HIS   D 2 55  ? 16.35792  33.21561  11.96265  1.000 18.78954  ? 54  HIS   D N     1 
ATOM   4404 C  CA    . HIS   D 2 55  ? 15.82828  31.87153  12.11399  1.000 23.40209  ? 54  HIS   D CA    1 
ATOM   4405 C  C     . HIS   D 2 55  ? 16.65321  30.99721  13.03469  1.000 24.16704  ? 54  HIS   D C     1 
ATOM   4406 O  O     . HIS   D 2 55  ? 16.15579  29.95856  13.49904  1.000 23.50920  ? 54  HIS   D O     1 
ATOM   4407 C  CB    . HIS   D 2 55  ? 15.70544  31.19183  10.75913  1.000 22.64691  ? 54  HIS   D CB    1 
ATOM   4408 C  CG    . HIS   D 2 55  ? 17.00875  31.04433  10.05116  1.000 22.77382  ? 54  HIS   D CG    1 
ATOM   4409 N  ND1   . HIS   D 2 55  ? 17.63114  32.10108  9.42334   1.000 26.59096  ? 54  HIS   D ND1   1 
ATOM   4410 C  CD2   . HIS   D 2 55  ? 17.80871  29.96875  9.87598   1.000 23.64947  ? 54  HIS   D CD2   1 
ATOM   4411 C  CE1   . HIS   D 2 55  ? 18.75943  31.67600  8.88070   1.000 25.72702  ? 54  HIS   D CE1   1 
ATOM   4412 N  NE2   . HIS   D 2 55  ? 18.88974  30.38800  9.14066   1.000 23.12970  ? 54  HIS   D NE2   1 
ATOM   4413 N  N     . ARG   D 2 56  ? 17.88521  31.40253  13.33929  1.000 21.27198  ? 55  ARG   D N     1 
ATOM   4414 C  CA    . ARG   D 2 56  ? 18.78589  30.58149  14.14115  1.000 23.57309  ? 55  ARG   D CA    1 
ATOM   4415 C  C     . ARG   D 2 56  ? 19.50336  31.47736  15.13916  1.000 22.20654  ? 55  ARG   D C     1 
ATOM   4416 O  O     . ARG   D 2 56  ? 20.33581  32.30408  14.75353  1.000 23.46423  ? 55  ARG   D O     1 
ATOM   4417 C  CB    . ARG   D 2 56  ? 19.78324  29.84198  13.24660  1.000 25.09116  ? 55  ARG   D CB    1 
ATOM   4418 C  CG    . ARG   D 2 56  ? 20.80478  29.06926  14.03840  1.000 25.72299  ? 55  ARG   D CG    1 
ATOM   4419 C  CD    . ARG   D 2 56  ? 21.75383  28.32648  13.12088  1.000 20.82941  ? 55  ARG   D CD    1 
ATOM   4420 N  NE    . ARG   D 2 56  ? 21.06174  27.29411  12.36444  1.000 24.07030  ? 55  ARG   D NE    1 
ATOM   4421 C  CZ    . ARG   D 2 56  ? 21.57426  26.67435  11.31176  1.000 29.35161  ? 55  ARG   D CZ    1 
ATOM   4422 N  NH1   . ARG   D 2 56  ? 22.77706  26.98954  10.84215  1.000 27.46685  ? 55  ARG   D NH1   1 
ATOM   4423 N  NH2   . ARG   D 2 56  ? 20.86959  25.70912  10.72517  1.000 29.77243  ? 55  ARG   D NH2   1 
ATOM   4424 N  N     . ILE   D 2 57  ? 19.21361  31.30504  16.43114  1.000 18.87135  ? 56  ILE   D N     1 
ATOM   4425 C  CA    . ILE   D 2 57  ? 19.86270  32.07322  17.48521  1.000 19.42264  ? 56  ILE   D CA    1 
ATOM   4426 C  C     . ILE   D 2 57  ? 20.37053  31.10726  18.55213  1.000 22.30905  ? 56  ILE   D C     1 
ATOM   4427 O  O     . ILE   D 2 57  ? 19.57364  30.40586  19.19309  1.000 19.53289  ? 56  ILE   D O     1 
ATOM   4428 C  CB    . ILE   D 2 57  ? 18.90756  33.09650  18.12528  1.000 22.69039  ? 56  ILE   D CB    1 
ATOM   4429 C  CG1   . ILE   D 2 57  ? 18.43031  34.12271  17.08902  1.000 26.25268  ? 56  ILE   D CG1   1 
ATOM   4430 C  CG2   . ILE   D 2 57  ? 19.58084  33.76645  19.34495  1.000 19.63807  ? 56  ILE   D CG2   1 
ATOM   4431 C  CD1   . ILE   D 2 57  ? 17.35171  35.07829  17.66235  1.000 22.06919  ? 56  ILE   D CD1   1 
ATOM   4432 N  N     . ILE   D 2 58  ? 21.67706  31.09677  18.76982  1.000 21.35849  ? 57  ILE   D N     1 
ATOM   4433 C  CA    . ILE   D 2 58  ? 22.26983  30.15605  19.71503  1.000 23.13722  ? 57  ILE   D CA    1 
ATOM   4434 C  C     . ILE   D 2 58  ? 23.00628  30.95123  20.78643  1.000 21.56742  ? 57  ILE   D C     1 
ATOM   4435 O  O     . ILE   D 2 58  ? 24.09694  31.49003  20.52228  1.000 20.54544  ? 57  ILE   D O     1 
ATOM   4436 C  CB    . ILE   D 2 58  ? 23.19728  29.16226  18.99717  1.000 24.23760  ? 57  ILE   D CB    1 
ATOM   4437 C  CG1   . ILE   D 2 58  ? 22.38070  28.30125  18.04971  1.000 21.65090  ? 57  ILE   D CG1   1 
ATOM   4438 C  CG2   . ILE   D 2 58  ? 23.92249  28.26330  20.01356  1.000 22.63520  ? 57  ILE   D CG2   1 
ATOM   4439 C  CD1   . ILE   D 2 58  ? 23.22571  27.33555  17.19410  1.000 22.85003  ? 57  ILE   D CD1   1 
ATOM   4440 N  N     . PRO   D 2 59  ? 22.44771  31.05529  21.99998  1.000 21.80781  ? 58  PRO   D N     1 
ATOM   4441 C  CA    . PRO   D 2 59  ? 23.10532  31.82814  23.06026  1.000 21.17478  ? 58  PRO   D CA    1 
ATOM   4442 C  C     . PRO   D 2 59  ? 24.53513  31.35728  23.29680  1.000 22.56598  ? 58  PRO   D C     1 
ATOM   4443 O  O     . PRO   D 2 59  ? 24.81836  30.16197  23.35656  1.000 21.86873  ? 58  PRO   D O     1 
ATOM   4444 C  CB    . PRO   D 2 59  ? 22.21735  31.56846  24.28773  1.000 23.92627  ? 58  PRO   D CB    1 
ATOM   4445 C  CG    . PRO   D 2 59  ? 20.86140  31.30653  23.69763  1.000 23.19627  ? 58  PRO   D CG    1 
ATOM   4446 C  CD    . PRO   D 2 59  ? 21.13367  30.53614  22.42628  1.000 22.96770  ? 58  PRO   D CD    1 
ATOM   4447 N  N     . GLY   D 2 60  ? 25.43620  32.31933  23.41597  1.000 23.52219  ? 59  GLY   D N     1 
ATOM   4448 C  CA    . GLY   D 2 60  ? 26.84741  32.05579  23.56392  1.000 24.37633  ? 59  GLY   D CA    1 
ATOM   4449 C  C     . GLY   D 2 60  ? 27.62435  32.04592  22.26240  1.000 23.49936  ? 59  GLY   D C     1 
ATOM   4450 O  O     . GLY   D 2 60  ? 28.85894  31.94979  22.29678  1.000 25.01732  ? 59  GLY   D O     1 
ATOM   4451 N  N     . PHE   D 2 61  ? 26.94536  32.14040  21.11603  1.000 21.64002  ? 60  PHE   D N     1 
ATOM   4452 C  CA    . PHE   D 2 61  ? 27.62950  31.99144  19.83993  1.000 20.07612  ? 60  PHE   D CA    1 
ATOM   4453 C  C     . PHE   D 2 61  ? 27.18790  33.03803  18.81195  1.000 21.09048  ? 60  PHE   D C     1 
ATOM   4454 O  O     . PHE   D 2 61  ? 27.99467  33.89851  18.43631  1.000 20.43263  ? 60  PHE   D O     1 
ATOM   4455 C  CB    . PHE   D 2 61  ? 27.41935  30.56965  19.29040  1.000 16.67235  ? 60  PHE   D CB    1 
ATOM   4456 C  CG    . PHE   D 2 61  ? 28.13096  29.50585  20.09080  1.000 24.36971  ? 60  PHE   D CG    1 
ATOM   4457 C  CD1   . PHE   D 2 61  ? 29.46024  29.21247  19.84794  1.000 21.12665  ? 60  PHE   D CD1   1 
ATOM   4458 C  CD2   . PHE   D 2 61  ? 27.47121  28.81327  21.09925  1.000 23.70431  ? 60  PHE   D CD2   1 
ATOM   4459 C  CE1   . PHE   D 2 61  ? 30.11960  28.25527  20.58952  1.000 24.80511  ? 60  PHE   D CE1   1 
ATOM   4460 C  CE2   . PHE   D 2 61  ? 28.13316  27.85178  21.84707  1.000 26.33228  ? 60  PHE   D CE2   1 
ATOM   4461 C  CZ    . PHE   D 2 61  ? 29.45720  27.56823  21.58118  1.000 23.63679  ? 60  PHE   D CZ    1 
ATOM   4462 N  N     . MET   D 2 62  ? 25.94312  32.98734  18.32975  1.000 20.39740  ? 61  MET   D N     1 
ATOM   4463 C  CA    . MET   D 2 62  ? 25.62600  33.90851  17.23489  1.000 19.42537  ? 61  MET   D CA    1 
ATOM   4464 C  C     . MET   D 2 62  ? 24.12438  33.98717  16.98550  1.000 23.31304  ? 61  MET   D C     1 
ATOM   4465 O  O     . MET   D 2 62  ? 23.35176  33.13934  17.43890  1.000 23.55625  ? 61  MET   D O     1 
ATOM   4466 C  CB    . MET   D 2 62  ? 26.34342  33.49729  15.93289  1.000 20.48822  ? 61  MET   D CB    1 
ATOM   4467 C  CG    . MET   D 2 62  ? 25.51577  32.57023  15.06287  1.000 23.50620  ? 61  MET   D CG    1 
ATOM   4468 S  SD    . MET   D 2 62  ? 25.37805  30.91195  15.73983  1.000 23.84439  ? 61  MET   D SD    1 
ATOM   4469 C  CE    . MET   D 2 62  ? 23.98810  30.37173  14.77530  1.000 25.69197  ? 61  MET   D CE    1 
ATOM   4470 N  N     . CYS   D 2 63  ? 23.73043  35.03660  16.25633  1.000 21.34565  ? 62  CYS   D N     1 
ATOM   4471 C  CA    . CYS   D 2 63  ? 22.38297  35.21741  15.71536  1.000 18.66360  ? 62  CYS   D CA    1 
ATOM   4472 C  C     . CYS   D 2 63  ? 22.47530  35.21870  14.20303  1.000 19.76282  ? 62  CYS   D C     1 
ATOM   4473 O  O     . CYS   D 2 63  ? 23.21730  36.02600  13.63544  1.000 22.86079  ? 62  CYS   D O     1 
ATOM   4474 C  CB    . CYS   D 2 63  ? 21.75200  36.54657  16.15319  1.000 20.60444  ? 62  CYS   D CB    1 
ATOM   4475 S  SG    . CYS   D 2 63  ? 21.65339  36.81606  17.96877  1.000 26.72453  ? 62  CYS   D SG    1 
ATOM   4476 N  N     . GLN   D 2 64  ? 21.69159  34.37255  13.55293  1.000 19.39575  ? 63  GLN   D N     1 
ATOM   4477 C  CA    . GLN   D 2 64  ? 21.78843  34.20950  12.10377  1.000 18.37118  ? 63  GLN   D CA    1 
ATOM   4478 C  C     . GLN   D 2 64  ? 20.44888  34.49641  11.45331  1.000 21.36975  ? 63  GLN   D C     1 
ATOM   4479 O  O     . GLN   D 2 64  ? 19.40599  34.05091  11.94568  1.000 21.11038  ? 63  GLN   D O     1 
ATOM   4480 C  CB    . GLN   D 2 64  ? 22.25236  32.79972  11.77408  1.000 20.99946  ? 63  GLN   D CB    1 
ATOM   4481 C  CG    . GLN   D 2 64  ? 22.35459  32.45121  10.26490  1.000 18.19461  ? 63  GLN   D CG    1 
ATOM   4482 C  CD    . GLN   D 2 64  ? 22.87016  31.04678  10.06263  1.000 18.07592  ? 63  GLN   D CD    1 
ATOM   4483 O  OE1   . GLN   D 2 64  ? 23.49400  30.49933  10.96219  1.000 20.15992  ? 63  GLN   D OE1   1 
ATOM   4484 N  NE2   . GLN   D 2 64  ? 22.62289  30.45391  8.88334   1.000 18.66588  ? 63  GLN   D NE2   1 
ATOM   4485 N  N     . GLY   D 2 65  ? 20.48891  35.22410  10.33554  1.000 18.52758  ? 64  GLY   D N     1 
ATOM   4486 C  CA    . GLY   D 2 65  ? 19.27856  35.50189  9.58012   1.000 21.62498  ? 64  GLY   D CA    1 
ATOM   4487 C  C     . GLY   D 2 65  ? 19.59134  35.67143  8.11049   1.000 23.33928  ? 64  GLY   D C     1 
ATOM   4488 O  O     . GLY   D 2 65  ? 20.59843  35.13961  7.61725   1.000 21.15433  ? 64  GLY   D O     1 
ATOM   4489 N  N     . GLY   D 2 66  ? 18.69940  36.36868  7.39985   1.000 21.06829  ? 65  GLY   D N     1 
ATOM   4490 C  CA    . GLY   D 2 66  ? 18.93630  36.75256  6.02355   1.000 21.07811  ? 65  GLY   D CA    1 
ATOM   4491 C  C     . GLY   D 2 66  ? 18.24876  35.90728  4.98065   1.000 24.17153  ? 65  GLY   D C     1 
ATOM   4492 O  O     . GLY   D 2 66  ? 18.46027  36.14926  3.78616   1.000 25.75160  ? 65  GLY   D O     1 
ATOM   4493 N  N     . ASP   D 2 67  ? 17.43622  34.92388  5.36918   1.000 22.39329  ? 66  ASP   D N     1 
ATOM   4494 C  CA    . ASP   D 2 67  ? 16.71735  34.13317  4.36224   1.000 25.98192  ? 66  ASP   D CA    1 
ATOM   4495 C  C     . ASP   D 2 67  ? 15.40104  34.83059  4.05123   1.000 31.56957  ? 66  ASP   D C     1 
ATOM   4496 O  O     . ASP   D 2 67  ? 14.36848  34.55861  4.66779   1.000 31.15276  ? 66  ASP   D O     1 
ATOM   4497 C  CB    . ASP   D 2 67  ? 16.49708  32.70304  4.83281   1.000 22.60203  ? 66  ASP   D CB    1 
ATOM   4498 C  CG    . ASP   D 2 67  ? 15.68706  31.87452  3.84748   1.000 32.10511  ? 66  ASP   D CG    1 
ATOM   4499 O  OD1   . ASP   D 2 67  ? 15.33738  32.37989  2.75546   1.000 31.08361  ? 66  ASP   D OD1   1 
ATOM   4500 O  OD2   . ASP   D 2 67  ? 15.40829  30.70129  4.16287   1.000 32.14668  ? 66  ASP   D OD2   1 
ATOM   4501 N  N     . PHE   D 2 68  ? 15.42094  35.72416  3.06015   1.000 27.41120  ? 67  PHE   D N     1 
ATOM   4502 C  CA    . PHE   D 2 68  ? 14.20369  36.41610  2.65310   1.000 30.27885  ? 67  PHE   D CA    1 
ATOM   4503 C  C     . PHE   D 2 68  ? 13.48934  35.75229  1.48435   1.000 32.25903  ? 67  PHE   D C     1 
ATOM   4504 O  O     . PHE   D 2 68  ? 12.50837  36.31256  0.98947   1.000 35.89614  ? 67  PHE   D O     1 
ATOM   4505 C  CB    . PHE   D 2 68  ? 14.50511  37.87501  2.29778   1.000 31.81709  ? 67  PHE   D CB    1 
ATOM   4506 C  CG    . PHE   D 2 68  ? 15.51537  38.04082  1.18529   1.000 27.32138  ? 67  PHE   D CG    1 
ATOM   4507 C  CD1   . PHE   D 2 68  ? 15.12761  37.94115  -0.15044  1.000 30.52490  ? 67  PHE   D CD1   1 
ATOM   4508 C  CD2   . PHE   D 2 68  ? 16.84497  38.31177  1.46710   1.000 31.35833  ? 67  PHE   D CD2   1 
ATOM   4509 C  CE1   . PHE   D 2 68  ? 16.05221  38.09710  -1.16839  1.000 32.68059  ? 67  PHE   D CE1   1 
ATOM   4510 C  CE2   . PHE   D 2 68  ? 17.77548  38.47215  0.43695   1.000 29.29804  ? 67  PHE   D CE2   1 
ATOM   4511 C  CZ    . PHE   D 2 68  ? 17.37356  38.36044  -0.88254  1.000 30.17990  ? 67  PHE   D CZ    1 
ATOM   4512 N  N     . THR   D 2 69  ? 13.94444  34.59440  1.01386   1.000 30.42998  ? 68  THR   D N     1 
ATOM   4513 C  CA    . THR   D 2 69  ? 13.21351  33.94179  -0.06607  1.000 35.81030  ? 68  THR   D CA    1 
ATOM   4514 C  C     . THR   D 2 69  ? 12.36051  32.77538  0.41286   1.000 42.52273  ? 68  THR   D C     1 
ATOM   4515 O  O     . THR   D 2 69  ? 11.28110  32.54413  -0.14343  1.000 42.21564  ? 68  THR   D O     1 
ATOM   4516 C  CB    . THR   D 2 69  ? 14.16984  33.48076  -1.18221  1.000 37.19605  ? 68  THR   D CB    1 
ATOM   4517 O  OG1   . THR   D 2 69  ? 14.95232  32.35939  -0.75609  1.000 37.11096  ? 68  THR   D OG1   1 
ATOM   4518 C  CG2   . THR   D 2 69  ? 15.11030  34.61616  -1.58867  1.000 34.60036  ? 68  THR   D CG2   1 
ATOM   4519 N  N     . ARG   D 2 70  ? 12.78730  32.05425  1.44903   1.000 38.62838  ? 69  ARG   D N     1 
ATOM   4520 C  CA    . ARG   D 2 70  ? 11.98126  30.97994  2.00790   1.000 41.27103  ? 69  ARG   D CA    1 
ATOM   4521 C  C     . ARG   D 2 70  ? 11.63691  31.17531  3.47353   1.000 40.44966  ? 69  ARG   D C     1 
ATOM   4522 O  O     . ARG   D 2 70  ? 10.73921  30.48382  3.96927   1.000 47.45944  ? 69  ARG   D O     1 
ATOM   4523 C  CB    . ARG   D 2 70  ? 12.68921  29.62826  1.82346   1.000 39.40884  ? 69  ARG   D CB    1 
ATOM   4524 C  CG    . ARG   D 2 70  ? 13.49693  29.56607  0.55058   1.000 46.04699  ? 69  ARG   D CG    1 
ATOM   4525 C  CD    . ARG   D 2 70  ? 13.28371  28.29823  -0.24765  1.000 53.41578  ? 69  ARG   D CD    1 
ATOM   4526 N  NE    . ARG   D 2 70  ? 14.15597  28.28520  -1.41849  1.000 58.50849  ? 69  ARG   D NE    1 
ATOM   4527 C  CZ    . ARG   D 2 70  ? 15.28050  27.58610  -1.51851  1.000 58.89259  ? 69  ARG   D CZ    1 
ATOM   4528 N  NH1   . ARG   D 2 70  ? 15.66697  26.75187  -0.56501  1.000 59.00659  ? 69  ARG   D NH1   1 
ATOM   4529 N  NH2   . ARG   D 2 70  ? 16.03925  27.72851  -2.60332  1.000 64.58742  ? 69  ARG   D NH2   1 
ATOM   4530 N  N     . HIS   D 2 71  ? 12.31688  32.09130  4.17335   1.000 34.76795  ? 70  HIS   D N     1 
ATOM   4531 C  CA    . HIS   D 2 71  ? 12.00503  32.48434  5.55137   1.000 41.15485  ? 70  HIS   D CA    1 
ATOM   4532 C  C     . HIS   D 2 71  ? 12.14537  31.33192  6.53888   1.000 46.47979  ? 70  HIS   D C     1 
ATOM   4533 O  O     . HIS   D 2 71  ? 11.54242  31.35036  7.61549   1.000 44.26468  ? 70  HIS   D O     1 
ATOM   4534 C  CB    . HIS   D 2 71  ? 10.60640  33.10064  5.65246   1.000 41.03778  ? 70  HIS   D CB    1 
ATOM   4535 C  CG    . HIS   D 2 71  ? 10.44210  34.33081  4.82371   1.000 38.29219  ? 70  HIS   D CG    1 
ATOM   4536 N  ND1   . HIS   D 2 71  ? 10.77907  35.58495  5.28504   1.000 38.88917  ? 70  HIS   D ND1   1 
ATOM   4537 C  CD2   . HIS   D 2 71  ? 10.00792  34.49945  3.55172   1.000 34.74962  ? 70  HIS   D CD2   1 
ATOM   4538 C  CE1   . HIS   D 2 71  ? 10.54981  36.47482  4.33581   1.000 38.76201  ? 70  HIS   D CE1   1 
ATOM   4539 N  NE2   . HIS   D 2 71  ? 10.08255  35.84155  3.27475   1.000 37.17172  ? 70  HIS   D NE2   1 
ATOM   4540 N  N     . ASN   D 2 72  ? 12.96131  30.33228  6.20404   1.000 38.75739  ? 71  ASN   D N     1 
ATOM   4541 C  CA    . ASN   D 2 72  ? 13.11855  29.18767  7.09147   1.000 46.95813  ? 71  ASN   D CA    1 
ATOM   4542 C  C     . ASN   D 2 72  ? 14.56194  28.70876  7.20810   1.000 37.35987  ? 71  ASN   D C     1 
ATOM   4543 O  O     . ASN   D 2 72  ? 14.79574  27.62147  7.75038   1.000 35.63878  ? 71  ASN   D O     1 
ATOM   4544 C  CB    . ASN   D 2 72  ? 12.22514  28.03325  6.62621   1.000 42.50991  ? 71  ASN   D CB    1 
ATOM   4545 C  CG    . ASN   D 2 72  ? 12.55821  27.55150  5.22585   1.000 44.05799  ? 71  ASN   D CG    1 
ATOM   4546 O  OD1   . ASN   D 2 72  ? 13.58938  27.91454  4.64078   1.000 39.80962  ? 71  ASN   D OD1   1 
ATOM   4547 N  ND2   . ASN   D 2 72  ? 11.68670  26.70701  4.68055   1.000 45.84865  ? 71  ASN   D ND2   1 
ATOM   4548 N  N     . GLY   D 2 73  ? 15.52835  29.45724  6.68880   1.000 32.86724  ? 72  GLY   D N     1 
ATOM   4549 C  CA    . GLY   D 2 73  ? 16.90765  29.06111  6.80186   1.000 30.38767  ? 72  GLY   D CA    1 
ATOM   4550 C  C     . GLY   D 2 73  ? 17.46105  28.28771  5.62823   1.000 34.90574  ? 72  GLY   D C     1 
ATOM   4551 O  O     . GLY   D 2 73  ? 18.65080  27.96777  5.63770   1.000 34.51127  ? 72  GLY   D O     1 
ATOM   4552 N  N     . THR   D 2 74  ? 16.63994  27.95943  4.62751   1.000 32.19627  ? 73  THR   D N     1 
ATOM   4553 C  CA    . THR   D 2 74  ? 17.10536  27.21109  3.46532   1.000 41.31068  ? 73  THR   D CA    1 
ATOM   4554 C  C     . THR   D 2 74  ? 17.27315  28.06971  2.22042   1.000 44.02190  ? 73  THR   D C     1 
ATOM   4555 O  O     . THR   D 2 74  ? 17.65098  27.53595  1.17196   1.000 47.69188  ? 73  THR   D O     1 
ATOM   4556 C  CB    . THR   D 2 74  ? 16.14375  26.07297  3.12277   1.000 43.58532  ? 73  THR   D CB    1 
ATOM   4557 O  OG1   . THR   D 2 74  ? 14.92040  26.62476  2.61635   1.000 45.72657  ? 73  THR   D OG1   1 
ATOM   4558 C  CG2   . THR   D 2 74  ? 15.84800  25.22278  4.34437   1.000 40.56910  ? 73  THR   D CG2   1 
ATOM   4559 N  N     . GLY   D 2 75  ? 16.99442  29.36781  2.29408   1.000 33.49691  ? 74  GLY   D N     1 
ATOM   4560 C  CA    . GLY   D 2 75  ? 16.97932  30.19779  1.11130   1.000 35.30920  ? 74  GLY   D CA    1 
ATOM   4561 C  C     . GLY   D 2 75  ? 17.93575  31.36979  1.21621   1.000 33.42267  ? 74  GLY   D C     1 
ATOM   4562 O  O     . GLY   D 2 75  ? 18.95860  31.32134  1.91372   1.000 28.64250  ? 74  GLY   D O     1 
ATOM   4563 N  N     . GLY   D 2 76  ? 17.57424  32.43725  0.51196   1.000 35.49432  ? 75  GLY   D N     1 
ATOM   4564 C  CA    . GLY   D 2 76  ? 18.39992  33.61018  0.34113   1.000 30.84614  ? 75  GLY   D CA    1 
ATOM   4565 C  C     . GLY   D 2 76  ? 19.04674  33.66708  -1.03930  1.000 28.01273  ? 75  GLY   D C     1 
ATOM   4566 O  O     . GLY   D 2 76  ? 19.19833  32.66183  -1.73547  1.000 29.79871  ? 75  GLY   D O     1 
ATOM   4567 N  N     . LYS   D 2 77  ? 19.43553  34.87632  -1.43427  1.000 30.30037  ? 76  LYS   D N     1 
ATOM   4568 C  CA    . LYS   D 2 77  ? 20.14651  35.07057  -2.69475  1.000 30.64463  ? 76  LYS   D CA    1 
ATOM   4569 C  C     . LYS   D 2 77  ? 20.90012  36.38955  -2.64000  1.000 27.58373  ? 76  LYS   D C     1 
ATOM   4570 O  O     . LYS   D 2 77  ? 20.51279  37.31059  -1.91650  1.000 27.33300  ? 76  LYS   D O     1 
ATOM   4571 C  CB    . LYS   D 2 77  ? 19.19012  35.05190  -3.89561  1.000 29.59735  ? 76  LYS   D CB    1 
ATOM   4572 C  CG    . LYS   D 2 77  ? 18.15383  36.17105  -3.90421  1.000 27.80481  ? 76  LYS   D CG    1 
ATOM   4573 C  CD    . LYS   D 2 77  ? 17.23561  36.02333  -5.11370  1.000 34.80828  ? 76  LYS   D CD    1 
ATOM   4574 C  CE    . LYS   D 2 77  ? 16.10933  37.04281  -5.09423  1.000 39.09806  ? 76  LYS   D CE    1 
ATOM   4575 N  NZ    . LYS   D 2 77  ? 15.25830  36.90943  -6.32505  1.000 40.23259  ? 76  LYS   D NZ    1 
ATOM   4576 N  N     . SER   D 2 78  ? 21.97233  36.47318  -3.42158  1.000 28.84704  ? 77  SER   D N     1 
ATOM   4577 C  CA    . SER   D 2 78  ? 22.76617  37.68696  -3.48440  1.000 27.34686  ? 77  SER   D CA    1 
ATOM   4578 C  C     . SER   D 2 78  ? 22.26346  38.59306  -4.60726  1.000 30.91087  ? 77  SER   D C     1 
ATOM   4579 O  O     . SER   D 2 78  ? 21.42854  38.20477  -5.43125  1.000 33.87161  ? 77  SER   D O     1 
ATOM   4580 C  CB    . SER   D 2 78  ? 24.24016  37.35721  -3.71557  1.000 30.83573  ? 77  SER   D CB    1 
ATOM   4581 O  OG    . SER   D 2 78  ? 24.52653  37.26777  -5.10899  1.000 34.80095  ? 77  SER   D OG    1 
ATOM   4582 N  N     . ILE   D 2 79  ? 22.79650  39.82005  -4.63629  1.000 32.15739  ? 78  ILE   D N     1 
ATOM   4583 C  CA    . ILE   D 2 79  ? 22.55383  40.70760  -5.77423  1.000 34.11109  ? 78  ILE   D CA    1 
ATOM   4584 C  C     . ILE   D 2 79  ? 23.34078  40.30960  -7.01193  1.000 33.69377  ? 78  ILE   D C     1 
ATOM   4585 O  O     . ILE   D 2 79  ? 23.18477  40.95535  -8.05555  1.000 31.95008  ? 78  ILE   D O     1 
ATOM   4586 C  CB    . ILE   D 2 79  ? 22.89133  42.17470  -5.44108  1.000 30.23931  ? 78  ILE   D CB    1 
ATOM   4587 C  CG1   . ILE   D 2 79  ? 24.39962  42.34783  -5.24616  1.000 29.12936  ? 78  ILE   D CG1   1 
ATOM   4588 C  CG2   . ILE   D 2 79  ? 22.12995  42.62987  -4.22042  1.000 32.43164  ? 78  ILE   D CG2   1 
ATOM   4589 C  CD1   . ILE   D 2 79  ? 24.80849  43.77934  -5.00504  1.000 32.34220  ? 78  ILE   D CD1   1 
ATOM   4590 N  N     . TYR   D 2 80  ? 24.16445  39.26145  -6.94372  1.000 30.03238  ? 79  TYR   D N     1 
ATOM   4591 C  CA    . TYR   D 2 80  ? 25.00388  38.84978  -8.06429  1.000 32.50917  ? 79  TYR   D CA    1 
ATOM   4592 C  C     . TYR   D 2 80  ? 24.55756  37.54148  -8.70868  1.000 36.83985  ? 79  TYR   D C     1 
ATOM   4593 O  O     . TYR   D 2 80  ? 25.28712  36.99063  -9.55283  1.000 35.36573  ? 79  TYR   D O     1 
ATOM   4594 C  CB    . TYR   D 2 80  ? 26.45189  38.70200  -7.60893  1.000 27.77060  ? 79  TYR   D CB    1 
ATOM   4595 C  CG    . TYR   D 2 80  ? 26.98869  39.86997  -6.83361  1.000 32.59231  ? 79  TYR   D CG    1 
ATOM   4596 C  CD1   . TYR   D 2 80  ? 27.23574  41.08679  -7.45473  1.000 32.47906  ? 79  TYR   D CD1   1 
ATOM   4597 C  CD2   . TYR   D 2 80  ? 27.29701  39.74603  -5.47676  1.000 29.40500  ? 79  TYR   D CD2   1 
ATOM   4598 C  CE1   . TYR   D 2 80  ? 27.74356  42.15207  -6.75291  1.000 32.08954  ? 79  TYR   D CE1   1 
ATOM   4599 C  CE2   . TYR   D 2 80  ? 27.81200  40.81049  -4.76541  1.000 26.53098  ? 79  TYR   D CE2   1 
ATOM   4600 C  CZ    . TYR   D 2 80  ? 28.02694  42.01215  -5.40421  1.000 30.11706  ? 79  TYR   D CZ    1 
ATOM   4601 O  OH    . TYR   D 2 80  ? 28.53549  43.07890  -4.71959  1.000 27.08631  ? 79  TYR   D OH    1 
ATOM   4602 N  N     . GLY   D 2 81  ? 23.39150  37.03385  -8.33560  1.000 32.19970  ? 80  GLY   D N     1 
ATOM   4603 C  CA    . GLY   D 2 81  ? 22.98124  35.67779  -8.61200  1.000 32.36062  ? 80  GLY   D CA    1 
ATOM   4604 C  C     . GLY   D 2 81  ? 22.65797  34.95481  -7.32495  1.000 31.50709  ? 80  GLY   D C     1 
ATOM   4605 O  O     . GLY   D 2 81  ? 22.72994  35.51542  -6.23145  1.000 30.45250  ? 80  GLY   D O     1 
ATOM   4606 N  N     . GLU   D 2 82  ? 22.29678  33.67296  -7.46559  1.000 31.95701  ? 81  GLU   D N     1 
ATOM   4607 C  CA    . GLU   D 2 82  ? 21.95659  32.90075  -6.27304  1.000 33.27054  ? 81  GLU   D CA    1 
ATOM   4608 C  C     . GLU   D 2 82  ? 23.08777  32.95014  -5.25184  1.000 32.76859  ? 81  GLU   D C     1 
ATOM   4609 O  O     . GLU   D 2 82  ? 22.85712  33.21856  -4.06680  1.000 32.29634  ? 81  GLU   D O     1 
ATOM   4610 C  CB    . GLU   D 2 82  ? 21.63021  31.44816  -6.61952  1.000 34.65618  ? 81  GLU   D CB    1 
ATOM   4611 C  CG    . GLU   D 2 82  ? 21.42330  30.61282  -5.35054  1.000 38.80868  ? 81  GLU   D CG    1 
ATOM   4612 C  CD    . GLU   D 2 82  ? 20.80741  29.24774  -5.58525  1.000 49.20957  ? 81  GLU   D CD    1 
ATOM   4613 O  OE1   . GLU   D 2 82  ? 21.39680  28.44315  -6.34493  1.000 53.43702  ? 81  GLU   D OE1   1 
ATOM   4614 O  OE2   . GLU   D 2 82  ? 19.73433  28.98043  -4.99128  1.000 47.61147  ? 81  GLU   D OE2   1 
ATOM   4615 N  N     . LYS   D 2 83  ? 24.31926  32.73242  -5.69685  1.000 26.28884  ? 82  LYS   D N     1 
ATOM   4616 C  CA    . LYS   D 2 83  ? 25.46683  32.69647  -4.80618  1.000 24.84528  ? 82  LYS   D CA    1 
ATOM   4617 C  C     . LYS   D 2 83  ? 26.63062  33.44781  -5.44728  1.000 35.09730  ? 82  LYS   D C     1 
ATOM   4618 O  O     . LYS   D 2 83  ? 26.62501  33.72828  -6.65240  1.000 32.60473  ? 82  LYS   D O     1 
ATOM   4619 C  CB    . LYS   D 2 83  ? 25.86648  31.24897  -4.49489  1.000 28.36183  ? 82  LYS   D CB    1 
ATOM   4620 C  CG    . LYS   D 2 83  ? 24.78631  30.45274  -3.74601  1.000 38.00155  ? 82  LYS   D CG    1 
ATOM   4621 C  CD    . LYS   D 2 83  ? 25.07862  28.96930  -3.67203  1.000 37.37622  ? 82  LYS   D CD    1 
ATOM   4622 C  CE    . LYS   D 2 83  ? 24.04462  28.27324  -2.76590  1.000 53.03906  ? 82  LYS   D CE    1 
ATOM   4623 N  NZ    . LYS   D 2 83  ? 24.51243  26.89524  -2.34104  1.000 59.70793  ? 82  LYS   D NZ    1 
ATOM   4624 N  N     . PHE   D 2 84  ? 27.62356  33.79513  -4.62994  1.000 29.43293  ? 83  PHE   D N     1 
ATOM   4625 C  CA    . PHE   D 2 84  ? 28.85974  34.38115  -5.14064  1.000 25.44045  ? 83  PHE   D CA    1 
ATOM   4626 C  C     . PHE   D 2 84  ? 30.05428  33.88791  -4.32355  1.000 30.53026  ? 83  PHE   D C     1 
ATOM   4627 O  O     . PHE   D 2 84  ? 29.92113  33.28587  -3.25519  1.000 24.60209  ? 83  PHE   D O     1 
ATOM   4628 C  CB    . PHE   D 2 84  ? 28.79408  35.92711  -5.20096  1.000 26.68489  ? 83  PHE   D CB    1 
ATOM   4629 C  CG    . PHE   D 2 84  ? 28.69478  36.62383  -3.86320  1.000 24.88830  ? 83  PHE   D CG    1 
ATOM   4630 C  CD1   . PHE   D 2 84  ? 27.49914  36.62868  -3.16089  1.000 25.29098  ? 83  PHE   D CD1   1 
ATOM   4631 C  CD2   . PHE   D 2 84  ? 29.77297  37.34525  -3.34545  1.000 27.90324  ? 83  PHE   D CD2   1 
ATOM   4632 C  CE1   . PHE   D 2 84  ? 27.38467  37.29495  -1.94050  1.000 25.10185  ? 83  PHE   D CE1   1 
ATOM   4633 C  CE2   . PHE   D 2 84  ? 29.67172  38.01254  -2.10586  1.000 26.20348  ? 83  PHE   D CE2   1 
ATOM   4634 C  CZ    . PHE   D 2 84  ? 28.45699  37.98532  -1.41158  1.000 23.72582  ? 83  PHE   D CZ    1 
ATOM   4635 N  N     . GLU   D 2 85  ? 31.24582  34.13316  -4.85722  1.000 24.44209  ? 84  GLU   D N     1 
ATOM   4636 C  CA    . GLU   D 2 85  ? 32.45498  33.54208  -4.31533  1.000 24.00962  ? 84  GLU   D CA    1 
ATOM   4637 C  C     . GLU   D 2 85  ? 32.87411  34.19772  -2.99128  1.000 24.87341  ? 84  GLU   D C     1 
ATOM   4638 O  O     . GLU   D 2 85  ? 32.44731  35.29973  -2.64180  1.000 25.83446  ? 84  GLU   D O     1 
ATOM   4639 C  CB    . GLU   D 2 85  ? 33.58652  33.67067  -5.34220  1.000 28.63656  ? 84  GLU   D CB    1 
ATOM   4640 C  CG    . GLU   D 2 85  ? 33.95642  35.11673  -5.66035  1.000 34.64247  ? 84  GLU   D CG    1 
ATOM   4641 C  CD    . GLU   D 2 85  ? 32.88505  35.87750  -6.45260  1.000 38.47188  ? 84  GLU   D CD    1 
ATOM   4642 O  OE1   . GLU   D 2 85  ? 32.09017  35.24654  -7.19763  1.000 39.43047  ? 84  GLU   D OE1   1 
ATOM   4643 O  OE2   . GLU   D 2 85  ? 32.83600  37.12047  -6.32172  1.000 41.05920  ? 84  GLU   D OE2   1 
ATOM   4644 N  N     . ASP   D 2 86  ? 33.74156  33.50238  -2.26296  1.000 23.49144  ? 85  ASP   D N     1 
ATOM   4645 C  CA    . ASP   D 2 86  ? 34.39988  34.07834  -1.09106  1.000 23.99476  ? 85  ASP   D CA    1 
ATOM   4646 C  C     . ASP   D 2 86  ? 35.37953  35.16462  -1.51928  1.000 31.68423  ? 85  ASP   D C     1 
ATOM   4647 O  O     . ASP   D 2 86  ? 36.35000  34.88965  -2.23469  1.000 30.83846  ? 85  ASP   D O     1 
ATOM   4648 C  CB    . ASP   D 2 86  ? 35.12041  32.98864  -0.31270  1.000 22.91945  ? 85  ASP   D CB    1 
ATOM   4649 C  CG    . ASP   D 2 86  ? 34.16628  31.96211  0.25247   1.000 24.92478  ? 85  ASP   D CG    1 
ATOM   4650 O  OD1   . ASP   D 2 86  ? 33.11647  32.38492  0.78138   1.000 26.27109  ? 85  ASP   D OD1   1 
ATOM   4651 O  OD2   . ASP   D 2 86  ? 34.47275  30.75052  0.18511   1.000 23.95938  ? 85  ASP   D OD2   1 
ATOM   4652 N  N     . GLU   D 2 87  ? 35.12800  36.39936  -1.09306  1.000 24.33471  ? 86  GLU   D N     1 
ATOM   4653 C  CA    . GLU   D 2 87  ? 35.91353  37.51757  -1.60569  1.000 27.15985  ? 86  GLU   D CA    1 
ATOM   4654 C  C     . GLU   D 2 87  ? 37.33345  37.50615  -1.05510  1.000 30.85733  ? 86  GLU   D C     1 
ATOM   4655 O  O     . GLU   D 2 87  ? 38.30900  37.54964  -1.81883  1.000 31.02401  ? 86  GLU   D O     1 
ATOM   4656 C  CB    . GLU   D 2 87  ? 35.20460  38.82512  -1.28271  1.000 25.00435  ? 86  GLU   D CB    1 
ATOM   4657 C  CG    . GLU   D 2 87  ? 35.87485  40.05604  -1.83729  1.000 26.34441  ? 86  GLU   D CG    1 
ATOM   4658 C  CD    . GLU   D 2 87  ? 34.97160  41.25950  -1.74647  1.000 25.71699  ? 86  GLU   D CD    1 
ATOM   4659 O  OE1   . GLU   D 2 87  ? 33.96042  41.19147  -1.01937  1.000 26.41869  ? 86  GLU   D OE1   1 
ATOM   4660 O  OE2   . GLU   D 2 87  ? 35.26072  42.28233  -2.38553  1.000 33.48994  ? 86  GLU   D OE2   1 
ATOM   4661 N  N     . ASN   D 2 88  ? 37.46905  37.48173  0.26296   1.000 23.63348  ? 87  ASN   D N     1 
ATOM   4662 C  CA    . ASN   D 2 88  ? 38.72618  37.17551  0.92890   1.000 23.12057  ? 87  ASN   D CA    1 
ATOM   4663 C  C     . ASN   D 2 88  ? 38.41483  36.77410  2.36197   1.000 26.34979  ? 87  ASN   D C     1 
ATOM   4664 O  O     . ASN   D 2 88  ? 37.26610  36.82217  2.80714   1.000 26.60262  ? 87  ASN   D O     1 
ATOM   4665 C  CB    . ASN   D 2 88  ? 39.72115  38.34970  0.88157   1.000 27.49704  ? 87  ASN   D CB    1 
ATOM   4666 C  CG    . ASN   D 2 88  ? 39.20482  39.59320  1.56897   1.000 26.31303  ? 87  ASN   D CG    1 
ATOM   4667 O  OD1   . ASN   D 2 88  ? 38.95363  39.58831  2.77251   1.000 27.93595  ? 87  ASN   D OD1   1 
ATOM   4668 N  ND2   . ASN   D 2 88  ? 39.03760  40.67007  0.80786   1.000 26.88485  ? 87  ASN   D ND2   1 
ATOM   4669 N  N     . PHE   D 2 89  ? 39.44836  36.34818  3.06826   1.000 24.92900  ? 88  PHE   D N     1 
ATOM   4670 C  CA    . PHE   D 2 89  ? 39.35478  35.98774  4.46933   1.000 23.56333  ? 88  PHE   D CA    1 
ATOM   4671 C  C     . PHE   D 2 89  ? 40.33550  36.80667  5.29932   1.000 20.24864  ? 88  PHE   D C     1 
ATOM   4672 O  O     . PHE   D 2 89  ? 40.92508  36.31144  6.24340   1.000 22.81474  ? 88  PHE   D O     1 
ATOM   4673 C  CB    . PHE   D 2 89  ? 39.60982  34.50371  4.66509   1.000 20.78869  ? 88  PHE   D CB    1 
ATOM   4674 C  CG    . PHE   D 2 89  ? 38.61738  33.63689  3.98735   1.000 25.09297  ? 88  PHE   D CG    1 
ATOM   4675 C  CD1   . PHE   D 2 89  ? 37.32537  33.51133  4.49598   1.000 24.08190  ? 88  PHE   D CD1   1 
ATOM   4676 C  CD2   . PHE   D 2 89  ? 38.95130  32.94898  2.84086   1.000 30.43625  ? 88  PHE   D CD2   1 
ATOM   4677 C  CE1   . PHE   D 2 89  ? 36.40660  32.71327  3.85984   1.000 22.83242  ? 88  PHE   D CE1   1 
ATOM   4678 C  CE2   . PHE   D 2 89  ? 38.04259  32.14022  2.20869   1.000 26.84086  ? 88  PHE   D CE2   1 
ATOM   4679 C  CZ    . PHE   D 2 89  ? 36.75155  32.02241  2.72259   1.000 28.53934  ? 88  PHE   D CZ    1 
ATOM   4680 N  N     . ILE   D 2 90  ? 40.52582  38.06911  4.91234   1.000 24.72326  ? 89  ILE   D N     1 
ATOM   4681 C  CA    . ILE   D 2 90  ? 41.45989  38.94702  5.61287   1.000 25.78438  ? 89  ILE   D CA    1 
ATOM   4682 C  C     . ILE   D 2 90  ? 41.03024  39.13540  7.05590   1.000 28.35127  ? 89  ILE   D C     1 
ATOM   4683 O  O     . ILE   D 2 90  ? 41.85099  39.06869  7.97738   1.000 27.70872  ? 89  ILE   D O     1 
ATOM   4684 C  CB    . ILE   D 2 90  ? 41.56716  40.30192  4.88761   1.000 26.09364  ? 89  ILE   D CB    1 
ATOM   4685 C  CG1   . ILE   D 2 90  ? 42.26605  40.13558  3.52916   1.000 27.21118  ? 89  ILE   D CG1   1 
ATOM   4686 C  CG2   . ILE   D 2 90  ? 42.28615  41.33251  5.76722   1.000 26.37833  ? 89  ILE   D CG2   1 
ATOM   4687 C  CD1   . ILE   D 2 90  ? 42.12603  41.34705  2.65064   1.000 29.03391  ? 89  ILE   D CD1   1 
ATOM   4688 N  N     . LEU   D 2 91  ? 39.73320  39.36106  7.26971   1.000 24.68983  ? 90  LEU   D N     1 
ATOM   4689 C  CA    . LEU   D 2 91  ? 39.20482  39.70125  8.58624   1.000 26.39776  ? 90  LEU   D CA    1 
ATOM   4690 C  C     . LEU   D 2 91  ? 38.77297  38.45174  9.35154   1.000 22.82838  ? 90  LEU   D C     1 
ATOM   4691 O  O     . LEU   D 2 91  ? 38.31392  37.46581  8.77232   1.000 24.77325  ? 90  LEU   D O     1 
ATOM   4692 C  CB    . LEU   D 2 91  ? 38.03720  40.66812  8.43494   1.000 22.87196  ? 90  LEU   D CB    1 
ATOM   4693 C  CG    . LEU   D 2 91  ? 38.45022  41.99776  7.81554   1.000 27.54924  ? 90  LEU   D CG    1 
ATOM   4694 C  CD1   . LEU   D 2 91  ? 37.25920  42.89710  7.62911   1.000 30.87466  ? 90  LEU   D CD1   1 
ATOM   4695 C  CD2   . LEU   D 2 91  ? 39.50671  42.68877  8.64552   1.000 33.00414  ? 90  LEU   D CD2   1 
ATOM   4696 N  N     . LYS   D 2 92  ? 38.93826  38.50243  10.66946  1.000 24.62976  ? 91  LYS   D N     1 
ATOM   4697 C  CA    . LYS   D 2 92  ? 38.74957  37.34653  11.52569  1.000 24.57841  ? 91  LYS   D CA    1 
ATOM   4698 C  C     . LYS   D 2 92  ? 37.53237  37.53282  12.41911  1.000 23.36930  ? 91  LYS   D C     1 
ATOM   4699 O  O     . LYS   D 2 92  ? 37.04842  38.64603  12.62634  1.000 21.11252  ? 91  LYS   D O     1 
ATOM   4700 C  CB    . LYS   D 2 92  ? 39.97823  37.10234  12.40653  1.000 25.28281  ? 91  LYS   D CB    1 
ATOM   4701 C  CG    . LYS   D 2 92  ? 41.29644  36.99267  11.64884  1.000 30.61506  ? 91  LYS   D CG    1 
ATOM   4702 C  CD    . LYS   D 2 92  ? 41.27661  35.88750  10.61494  1.000 35.26293  ? 91  LYS   D CD    1 
ATOM   4703 C  CE    . LYS   D 2 92  ? 42.67371  35.74652  9.95657   1.000 37.03494  ? 91  LYS   D CE    1 
ATOM   4704 N  NZ    . LYS   D 2 92  ? 42.61942  34.97235  8.66928   1.000 43.63652  ? 91  LYS   D NZ    1 
ATOM   4705 N  N     . HIS   D 2 93  ? 37.05734  36.41560  12.96028  1.000 23.40809  ? 92  HIS   D N     1 
ATOM   4706 C  CA    . HIS   D 2 93  ? 35.93738  36.43176  13.90950  1.000 23.25327  ? 92  HIS   D CA    1 
ATOM   4707 C  C     . HIS   D 2 93  ? 36.50361  36.67856  15.30325  1.000 23.10954  ? 92  HIS   D C     1 
ATOM   4708 O  O     . HIS   D 2 93  ? 36.74054  35.75990  16.08489  1.000 26.74326  ? 92  HIS   D O     1 
ATOM   4709 C  CB    . HIS   D 2 93  ? 35.16567  35.12798  13.84117  1.000 22.49311  ? 92  HIS   D CB    1 
ATOM   4710 C  CG    . HIS   D 2 93  ? 34.60773  34.83215  12.47944  1.000 19.79262  ? 92  HIS   D CG    1 
ATOM   4711 N  ND1   . HIS   D 2 93  ? 35.38327  34.31322  11.46546  1.000 20.85946  ? 92  HIS   D ND1   1 
ATOM   4712 C  CD2   . HIS   D 2 93  ? 33.36388  34.98783  11.96410  1.000 18.48947  ? 92  HIS   D CD2   1 
ATOM   4713 C  CE1   . HIS   D 2 93  ? 34.63899  34.16722  10.37996  1.000 19.83624  ? 92  HIS   D CE1   1 
ATOM   4714 N  NE2   . HIS   D 2 93  ? 33.40904  34.57103  10.65739  1.000 19.96466  ? 92  HIS   D NE2   1 
ATOM   4715 N  N     . THR   D 2 94  ? 36.70803  37.95261  15.61879  1.000 23.80598  ? 93  THR   D N     1 
ATOM   4716 C  CA    . THR   D 2 94  ? 37.49655  38.30811  16.79372  1.000 26.35406  ? 93  THR   D CA    1 
ATOM   4717 C  C     . THR   D 2 94  ? 36.68062  38.38355  18.09034  1.000 30.47950  ? 93  THR   D C     1 
ATOM   4718 O  O     . THR   D 2 94  ? 37.26930  38.35248  19.18080  1.000 27.48821  ? 93  THR   D O     1 
ATOM   4719 C  CB    . THR   D 2 94  ? 38.19229  39.65007  16.54634  1.000 29.56392  ? 93  THR   D CB    1 
ATOM   4720 O  OG1   . THR   D 2 94  ? 37.21080  40.60525  16.14193  1.000 25.64314  ? 93  THR   D OG1   1 
ATOM   4721 C  CG2   . THR   D 2 94  ? 39.26210  39.52215  15.44949  1.000 31.03052  ? 93  THR   D CG2   1 
ATOM   4722 N  N     . GLY   D 2 95  ? 35.35324  38.48219  18.01594  1.000 22.60951  ? 94  GLY   D N     1 
ATOM   4723 C  CA    . GLY   D 2 95  ? 34.56916  38.66589  19.22123  1.000 23.91978  ? 94  GLY   D CA    1 
ATOM   4724 C  C     . GLY   D 2 95  ? 33.15281  39.10423  18.92061  1.000 23.62235  ? 94  GLY   D C     1 
ATOM   4725 O  O     . GLY   D 2 95  ? 32.71618  39.11537  17.76379  1.000 22.70300  ? 94  GLY   D O     1 
ATOM   4726 N  N     . PRO   D 2 96  ? 32.40270  39.47523  19.96425  1.000 23.30262  ? 95  PRO   D N     1 
ATOM   4727 C  CA    . PRO   D 2 96  ? 31.00125  39.86164  19.77870  1.000 24.34481  ? 95  PRO   D CA    1 
ATOM   4728 C  C     . PRO   D 2 96  ? 30.86193  41.04260  18.84015  1.000 22.33110  ? 95  PRO   D C     1 
ATOM   4729 O  O     . PRO   D 2 96  ? 31.63719  41.99760  18.88691  1.000 27.23588  ? 95  PRO   D O     1 
ATOM   4730 C  CB    . PRO   D 2 96  ? 30.53710  40.23317  21.20180  1.000 25.26633  ? 95  PRO   D CB    1 
ATOM   4731 C  CG    . PRO   D 2 96  ? 31.43728  39.49822  22.09300  1.000 22.76378  ? 95  PRO   D CG    1 
ATOM   4732 C  CD    . PRO   D 2 96  ? 32.78851  39.43958  21.38763  1.000 23.12821  ? 95  PRO   D CD    1 
ATOM   4733 N  N     . GLY   D 2 97  ? 29.85638  40.97339  17.99034  1.000 19.72334  ? 96  GLY   D N     1 
ATOM   4734 C  CA    . GLY   D 2 97  ? 29.51665  42.05252  17.09428  1.000 22.39438  ? 96  GLY   D CA    1 
ATOM   4735 C  C     . GLY   D 2 97  ? 30.02466  41.85477  15.68856  1.000 23.98999  ? 96  GLY   D C     1 
ATOM   4736 O  O     . GLY   D 2 97  ? 29.58740  42.56467  14.78464  1.000 21.68925  ? 96  GLY   D O     1 
ATOM   4737 N  N     . ILE   D 2 98  ? 30.88826  40.87121  15.46999  1.000 20.39327  ? 97  ILE   D N     1 
ATOM   4738 C  CA    . ILE   D 2 98  ? 31.37590  40.62747  14.11313  1.000 19.32676  ? 97  ILE   D CA    1 
ATOM   4739 C  C     . ILE   D 2 98  ? 30.22355  40.20040  13.21628  1.000 21.21003  ? 97  ILE   D C     1 
ATOM   4740 O  O     . ILE   D 2 98  ? 29.39323  39.36074  13.59895  1.000 19.42337  ? 97  ILE   D O     1 
ATOM   4741 C  CB    . ILE   D 2 98  ? 32.48717  39.57059  14.14086  1.000 23.00629  ? 97  ILE   D CB    1 
ATOM   4742 C  CG1   . ILE   D 2 98  ? 33.73439  40.11581  14.83236  1.000 26.64037  ? 97  ILE   D CG1   1 
ATOM   4743 C  CG2   . ILE   D 2 98  ? 32.80630  39.12608  12.73750  1.000 24.07258  ? 97  ILE   D CG2   1 
ATOM   4744 C  CD1   . ILE   D 2 98  ? 34.40505  41.23625  14.04471  1.000 30.08203  ? 97  ILE   D CD1   1 
ATOM   4745 N  N     . LEU   D 2 99  ? 30.17107  40.76950  12.00353  1.000 21.57981  ? 98  LEU   D N     1 
ATOM   4746 C  CA    . LEU   D 2 99  ? 29.16603  40.43511  11.00167  1.000 21.59058  ? 98  LEU   D CA    1 
ATOM   4747 C  C     . LEU   D 2 99  ? 29.83924  39.65771  9.88331   1.000 24.31728  ? 98  LEU   D C     1 
ATOM   4748 O  O     . LEU   D 2 99  ? 30.82798  40.13701  9.31391   1.000 22.20793  ? 98  LEU   D O     1 
ATOM   4749 C  CB    . LEU   D 2 99  ? 28.50621  41.69128  10.43060  1.000 20.67527  ? 98  LEU   D CB    1 
ATOM   4750 C  CG    . LEU   D 2 99  ? 27.45865  41.55354  9.32560   1.000 20.55305  ? 98  LEU   D CG    1 
ATOM   4751 C  CD1   . LEU   D 2 99  ? 26.19030  40.80533  9.80213   1.000 21.22119  ? 98  LEU   D CD1   1 
ATOM   4752 C  CD2   . LEU   D 2 99  ? 27.10093  42.95152  8.86210   1.000 20.54323  ? 98  LEU   D CD2   1 
ATOM   4753 N  N     . SER   D 2 100 ? 29.28951  38.49006  9.54802   1.000 21.46396  ? 99  SER   D N     1 
ATOM   4754 C  CA    . SER   D 2 100 ? 29.99042  37.54503  8.67759   1.000 23.21641  ? 99  SER   D CA    1 
ATOM   4755 C  C     . SER   D 2 100 ? 28.96053  36.76133  7.86141   1.000 20.84537  ? 99  SER   D C     1 
ATOM   4756 O  O     . SER   D 2 100 ? 27.79287  36.66302  8.23773   1.000 20.57157  ? 99  SER   D O     1 
ATOM   4757 C  CB    . SER   D 2 100 ? 30.89229  36.64362  9.54434   1.000 21.09213  ? 99  SER   D CB    1 
ATOM   4758 O  OG    . SER   D 2 100 ? 31.52010  35.61952  8.79422   1.000 22.76321  ? 99  SER   D OG    1 
ATOM   4759 N  N     . MET   D 2 101 ? 29.39027  36.22855  6.71719   1.000 18.57710  ? 100 MET   D N     1 
ATOM   4760 C  CA    . MET   D 2 101 ? 28.48344  35.55386  5.79247   1.000 20.99521  ? 100 MET   D CA    1 
ATOM   4761 C  C     . MET   D 2 101 ? 28.28621  34.09408  6.18357   1.000 20.95935  ? 100 MET   D C     1 
ATOM   4762 O  O     . MET   D 2 101 ? 29.24806  33.38198  6.46422   1.000 20.25463  ? 100 MET   D O     1 
ATOM   4763 C  CB    . MET   D 2 101 ? 29.03526  35.63188  4.36452   1.000 18.82872  ? 100 MET   D CB    1 
ATOM   4764 C  CG    . MET   D 2 101 ? 28.96999  37.03407  3.79790   1.000 22.41581  ? 100 MET   D CG    1 
ATOM   4765 S  SD    . MET   D 2 101 ? 27.27278  37.69230  3.70178   1.000 25.27402  ? 100 MET   D SD    1 
ATOM   4766 C  CE    . MET   D 2 101 ? 26.51599  36.58112  2.52545   1.000 22.10033  ? 100 MET   D CE    1 
ATOM   4767 N  N     . ALA   D 2 102 ? 27.04226  33.64663  6.19531   1.000 18.61674  ? 101 ALA   D N     1 
ATOM   4768 C  CA    . ALA   D 2 102 ? 26.75171  32.22542  6.27155   1.000 18.66155  ? 101 ALA   D CA    1 
ATOM   4769 C  C     . ALA   D 2 102 ? 27.00223  31.58109  4.90694   1.000 21.38991  ? 101 ALA   D C     1 
ATOM   4770 O  O     . ALA   D 2 102 ? 26.95365  32.24025  3.86936   1.000 24.97812  ? 101 ALA   D O     1 
ATOM   4771 C  CB    . ALA   D 2 102 ? 25.28741  32.01566  6.69354   1.000 22.70469  ? 101 ALA   D CB    1 
ATOM   4772 N  N     . ASN   D 2 103 ? 27.24033  30.27820  4.89198   1.000 20.55963  ? 102 ASN   D N     1 
ATOM   4773 C  CA    . ASN   D 2 103 ? 27.43205  29.64844  3.59002   1.000 24.68552  ? 102 ASN   D CA    1 
ATOM   4774 C  C     . ASN   D 2 103 ? 27.18573  28.15333  3.70453   1.000 25.27065  ? 102 ASN   D C     1 
ATOM   4775 O  O     . ASN   D 2 103 ? 26.96748  27.61807  4.79154   1.000 26.25722  ? 102 ASN   D O     1 
ATOM   4776 C  CB    . ASN   D 2 103 ? 28.82568  29.95623  3.00344   1.000 24.27080  ? 102 ASN   D CB    1 
ATOM   4777 C  CG    . ASN   D 2 103 ? 29.96249  29.39490  3.81463   1.000 23.34262  ? 102 ASN   D CG    1 
ATOM   4778 O  OD1   . ASN   D 2 103 ? 29.98985  28.21258  4.14948   1.000 23.09808  ? 102 ASN   D OD1   1 
ATOM   4779 N  ND2   . ASN   D 2 103 ? 30.94211  30.24423  4.11180   1.000 25.23877  ? 102 ASN   D ND2   1 
ATOM   4780 N  N     . ALA   D 2 104 ? 27.21904  27.48940  2.55112   1.000 27.39579  ? 103 ALA   D N     1 
ATOM   4781 C  CA    . ALA   D 2 104 ? 27.09392  26.04142  2.45219   1.000 24.93195  ? 103 ALA   D CA    1 
ATOM   4782 C  C     . ALA   D 2 104 ? 28.38637  25.41204  1.93823   1.000 28.67136  ? 103 ALA   D C     1 
ATOM   4783 O  O     . ALA   D 2 104 ? 28.35387  24.40397  1.22868   1.000 32.31846  ? 103 ALA   D O     1 
ATOM   4784 C  CB    . ALA   D 2 104 ? 25.92506  25.67078  1.54336   1.000 31.76604  ? 103 ALA   D CB    1 
ATOM   4785 N  N     . GLY   D 2 105 ? 29.53031  25.98657  2.30100   1.000 26.59611  ? 104 GLY   D N     1 
ATOM   4786 C  CA    . GLY   D 2 105 ? 30.79150  25.54677  1.76076   1.000 24.22922  ? 104 GLY   D CA    1 
ATOM   4787 C  C     . GLY   D 2 105 ? 31.45407  26.62803  0.93523   1.000 26.61210  ? 104 GLY   D C     1 
ATOM   4788 O  O     . GLY   D 2 105 ? 30.95288  27.74986  0.80313   1.000 25.98114  ? 104 GLY   D O     1 
ATOM   4789 N  N     . PRO   D 2 106 ? 32.60902  26.30104  0.36326   1.000 29.01884  ? 105 PRO   D N     1 
ATOM   4790 C  CA    . PRO   D 2 106 ? 33.37420  27.30368  -0.38874  1.000 24.67597  ? 105 PRO   D CA    1 
ATOM   4791 C  C     . PRO   D 2 106 ? 32.53784  27.94976  -1.48301  1.000 22.66789  ? 105 PRO   D C     1 
ATOM   4792 O  O     . PRO   D 2 106 ? 31.82031  27.27496  -2.22080  1.000 26.90213  ? 105 PRO   D O     1 
ATOM   4793 C  CB    . PRO   D 2 106 ? 34.54116  26.49015  -0.96174  1.000 30.75313  ? 105 PRO   D CB    1 
ATOM   4794 C  CG    . PRO   D 2 106 ? 34.71267  25.35334  0.01629   1.000 29.98072  ? 105 PRO   D CG    1 
ATOM   4795 C  CD    . PRO   D 2 106 ? 33.29004  24.99910  0.42134   1.000 29.51245  ? 105 PRO   D CD    1 
ATOM   4796 N  N     . ASN   D 2 107 ? 32.61468  29.27832  -1.56158  1.000 23.87431  ? 106 ASN   D N     1 
ATOM   4797 C  CA    . ASN   D 2 107 ? 32.02452  30.06068  -2.64637  1.000 23.21798  ? 106 ASN   D CA    1 
ATOM   4798 C  C     . ASN   D 2 107 ? 30.51922  29.83840  -2.77125  1.000 25.63357  ? 106 ASN   D C     1 
ATOM   4799 O  O     . ASN   D 2 107 ? 29.98325  29.61647  -3.86211  1.000 27.41694  ? 106 ASN   D O     1 
ATOM   4800 C  CB    . ASN   D 2 107 ? 32.73224  29.76191  -3.97089  1.000 23.57637  ? 106 ASN   D CB    1 
ATOM   4801 C  CG    . ASN   D 2 107 ? 34.21525  29.97883  -3.86712  1.000 23.97539  ? 106 ASN   D CG    1 
ATOM   4802 O  OD1   . ASN   D 2 107 ? 34.65356  30.98989  -3.32261  1.000 24.50820  ? 106 ASN   D OD1   1 
ATOM   4803 N  ND2   . ASN   D 2 107 ? 34.99956  29.02033  -4.35382  1.000 27.05493  ? 106 ASN   D ND2   1 
ATOM   4804 N  N     . THR   D 2 108 ? 29.82487  29.90598  -1.63886  1.000 21.72631  ? 107 THR   D N     1 
ATOM   4805 C  CA    . THR   D 2 108 ? 28.37108  29.77637  -1.66468  1.000 23.55763  ? 107 THR   D CA    1 
ATOM   4806 C  C     . THR   D 2 108 ? 27.70619  30.87018  -0.84729  1.000 26.28273  ? 107 THR   D C     1 
ATOM   4807 O  O     . THR   D 2 108 ? 26.68963  30.63565  -0.18964  1.000 25.11572  ? 107 THR   D O     1 
ATOM   4808 C  CB    . THR   D 2 108 ? 27.91021  28.40397  -1.17053  1.000 26.49291  ? 107 THR   D CB    1 
ATOM   4809 O  OG1   . THR   D 2 108 ? 28.42793  28.16457  0.14096   1.000 24.96789  ? 107 THR   D OG1   1 
ATOM   4810 C  CG2   . THR   D 2 108 ? 28.35016  27.28787  -2.07529  1.000 23.23651  ? 107 THR   D CG2   1 
ATOM   4811 N  N     . ASN   D 2 109 ? 28.22656  32.09024  -0.90938  1.000 24.59996  ? 108 ASN   D N     1 
ATOM   4812 C  CA    . ASN   D 2 109 ? 27.58958  33.20855  -0.22597  1.000 23.71564  ? 108 ASN   D CA    1 
ATOM   4813 C  C     . ASN   D 2 109 ? 26.29696  33.59561  -0.91813  1.000 28.17013  ? 108 ASN   D C     1 
ATOM   4814 O  O     . ASN   D 2 109 ? 26.26344  33.73437  -2.14174  1.000 27.69159  ? 108 ASN   D O     1 
ATOM   4815 C  CB    . ASN   D 2 109 ? 28.50400  34.41671  -0.19514  1.000 24.98395  ? 108 ASN   D CB    1 
ATOM   4816 C  CG    . ASN   D 2 109 ? 29.79751  34.11801  0.46141   1.000 29.28427  ? 108 ASN   D CG    1 
ATOM   4817 O  OD1   . ASN   D 2 109 ? 29.85252  34.04630  1.66745   1.000 25.15051  ? 108 ASN   D OD1   1 
ATOM   4818 N  ND2   . ASN   D 2 109 ? 30.85315  33.89996  -0.33187  1.000 23.26924  ? 108 ASN   D ND2   1 
ATOM   4819 N  N     . GLY   D 2 110 ? 25.23164  33.78208  -0.12676  1.000 22.57379  ? 109 GLY   D N     1 
ATOM   4820 C  CA    . GLY   D 2 110 ? 23.97327  34.25058  -0.67351  1.000 22.86211  ? 109 GLY   D CA    1 
ATOM   4821 C  C     . GLY   D 2 110 ? 23.54156  35.55721  -0.04718  1.000 22.72364  ? 109 GLY   D C     1 
ATOM   4822 O  O     . GLY   D 2 110 ? 24.09533  36.61987  -0.32899  1.000 24.90114  ? 109 GLY   D O     1 
ATOM   4823 N  N     . SER   D 2 111 ? 22.54016  35.49018  0.81757   1.000 24.14464  ? 110 SER   D N     1 
ATOM   4824 C  CA    . SER   D 2 111 ? 22.18205  36.61710  1.65910   1.000 22.02319  ? 110 SER   D CA    1 
ATOM   4825 C  C     . SER   D 2 111 ? 22.26927  36.30872  3.14052   1.000 21.22614  ? 110 SER   D C     1 
ATOM   4826 O  O     . SER   D 2 111 ? 22.25859  37.24818  3.94043   1.000 19.24776  ? 110 SER   D O     1 
ATOM   4827 C  CB    . SER   D 2 111 ? 20.74835  37.08499  1.36790   1.000 23.02577  ? 110 SER   D CB    1 
ATOM   4828 O  OG    . SER   D 2 111 ? 19.87410  35.98553  1.46670   1.000 24.66838  ? 110 SER   D OG    1 
ATOM   4829 N  N     . GLN   D 2 112 ? 22.32295  35.03912  3.52709   1.000 20.18360  ? 111 GLN   D N     1 
ATOM   4830 C  CA    . GLN   D 2 112 ? 22.31204  34.74832  4.96219   1.000 21.92785  ? 111 GLN   D CA    1 
ATOM   4831 C  C     . GLN   D 2 112 ? 23.61889  35.19925  5.60388   1.000 23.86589  ? 111 GLN   D C     1 
ATOM   4832 O  O     . GLN   D 2 112 ? 24.70331  35.14359  5.00493   1.000 22.86404  ? 111 GLN   D O     1 
ATOM   4833 C  CB    . GLN   D 2 112 ? 22.06370  33.26222  5.22565   1.000 17.59259  ? 111 GLN   D CB    1 
ATOM   4834 C  CG    . GLN   D 2 112 ? 20.60818  32.78150  4.97810   1.000 22.47284  ? 111 GLN   D CG    1 
ATOM   4835 C  CD    . GLN   D 2 112 ? 20.41075  31.34760  5.43873   1.000 23.09567  ? 111 GLN   D CD    1 
ATOM   4836 O  OE1   . GLN   D 2 112 ? 20.82738  30.98154  6.53685   1.000 21.39828  ? 111 GLN   D OE1   1 
ATOM   4837 N  NE2   . GLN   D 2 112 ? 19.80686  30.52337  4.59997   1.000 22.06228  ? 111 GLN   D NE2   1 
ATOM   4838 N  N     . PHE   D 2 113 ? 23.50202  35.63914  6.84860   1.000 18.23059  ? 112 PHE   D N     1 
ATOM   4839 C  CA    . PHE   D 2 113 ? 24.60264  36.26285  7.55931   1.000 17.32660  ? 112 PHE   D CA    1 
ATOM   4840 C  C     . PHE   D 2 113 ? 24.45815  35.89045  9.02287   1.000 19.08300  ? 112 PHE   D C     1 
ATOM   4841 O  O     . PHE   D 2 113 ? 23.39791  35.43304  9.46371   1.000 21.35486  ? 112 PHE   D O     1 
ATOM   4842 C  CB    . PHE   D 2 113 ? 24.56608  37.77554  7.40548   1.000 18.44343  ? 112 PHE   D CB    1 
ATOM   4843 C  CG    . PHE   D 2 113 ? 23.30418  38.38771  7.96621   1.000 21.60783  ? 112 PHE   D CG    1 
ATOM   4844 C  CD1   . PHE   D 2 113 ? 22.15904  38.48921  7.19362   1.000 21.92669  ? 112 PHE   D CD1   1 
ATOM   4845 C  CD2   . PHE   D 2 113 ? 23.25732  38.81443  9.28990   1.000 21.78456  ? 112 PHE   D CD2   1 
ATOM   4846 C  CE1   . PHE   D 2 113 ? 20.98750  39.02218  7.71508   1.000 19.80273  ? 112 PHE   D CE1   1 
ATOM   4847 C  CE2   . PHE   D 2 113 ? 22.09607  39.34424  9.81806   1.000 22.27550  ? 112 PHE   D CE2   1 
ATOM   4848 C  CZ    . PHE   D 2 113 ? 20.95336  39.45536  9.02202   1.000 20.73014  ? 112 PHE   D CZ    1 
ATOM   4849 N  N     . PHE   D 2 114 ? 25.50818  36.14388  9.79535   1.000 18.16512  ? 113 PHE   D N     1 
ATOM   4850 C  CA    . PHE   D 2 114 ? 25.38257  35.95880  11.23211  1.000 18.85656  ? 113 PHE   D CA    1 
ATOM   4851 C  C     . PHE   D 2 114 ? 26.12775  37.06754  11.94337  1.000 20.82041  ? 113 PHE   D C     1 
ATOM   4852 O  O     . PHE   D 2 114 ? 27.08589  37.63783  11.40327  1.000 21.79124  ? 113 PHE   D O     1 
ATOM   4853 C  CB    . PHE   D 2 114 ? 25.86021  34.57116  11.71839  1.000 17.26684  ? 113 PHE   D CB    1 
ATOM   4854 C  CG    . PHE   D 2 114 ? 27.31404  34.25116  11.42264  1.000 18.01577  ? 113 PHE   D CG    1 
ATOM   4855 C  CD1   . PHE   D 2 114 ? 27.71514  33.95276  10.12849  1.000 22.81063  ? 113 PHE   D CD1   1 
ATOM   4856 C  CD2   . PHE   D 2 114 ? 28.25892  34.23813  12.44207  1.000 18.21482  ? 113 PHE   D CD2   1 
ATOM   4857 C  CE1   . PHE   D 2 114 ? 29.07153  33.64908  9.84713   1.000 19.99247  ? 113 PHE   D CE1   1 
ATOM   4858 C  CE2   . PHE   D 2 114 ? 29.62300  33.93637  12.19105  1.000 19.19401  ? 113 PHE   D CE2   1 
ATOM   4859 C  CZ    . PHE   D 2 114 ? 30.01450  33.62948  10.88699  1.000 21.59346  ? 113 PHE   D CZ    1 
ATOM   4860 N  N     . ILE   D 2 115 ? 25.63827  37.39412  13.14412  1.000 18.88815  ? 114 ILE   D N     1 
ATOM   4861 C  CA    . ILE   D 2 115 ? 26.25142  38.35855  14.05409  1.000 20.60802  ? 114 ILE   D CA    1 
ATOM   4862 C  C     . ILE   D 2 115 ? 26.79032  37.57883  15.23978  1.000 21.53436  ? 114 ILE   D C     1 
ATOM   4863 O  O     . ILE   D 2 115 ? 26.03199  36.85640  15.90421  1.000 21.29650  ? 114 ILE   D O     1 
ATOM   4864 C  CB    . ILE   D 2 115 ? 25.24474  39.42348  14.52557  1.000 20.36930  ? 114 ILE   D CB    1 
ATOM   4865 C  CG1   . ILE   D 2 115 ? 24.46132  40.02651  13.35138  1.000 23.94284  ? 114 ILE   D CG1   1 
ATOM   4866 C  CG2   . ILE   D 2 115 ? 25.95416  40.51255  15.31188  1.000 22.66521  ? 114 ILE   D CG2   1 
ATOM   4867 C  CD1   . ILE   D 2 115 ? 23.17653  40.72248  13.80044  1.000 24.75423  ? 114 ILE   D CD1   1 
ATOM   4868 N  N     . CYS   D 2 116 ? 28.08576  37.71437  15.51249  1.000 18.95021  ? 115 CYS   D N     1 
ATOM   4869 C  CA    . CYS   D 2 116 ? 28.69304  36.95507  16.58885  1.000 20.24897  ? 115 CYS   D CA    1 
ATOM   4870 C  C     . CYS   D 2 116 ? 28.31802  37.56470  17.92999  1.000 23.29441  ? 115 CYS   D C     1 
ATOM   4871 O  O     . CYS   D 2 116 ? 28.28194  38.78633  18.07858  1.000 24.13050  ? 115 CYS   D O     1 
ATOM   4872 C  CB    . CYS   D 2 116 ? 30.20162  36.95091  16.45011  1.000 20.60954  ? 115 CYS   D CB    1 
ATOM   4873 S  SG    . CYS   D 2 116 ? 30.76917  36.08007  14.97726  1.000 24.43313  ? 115 CYS   D SG    1 
ATOM   4874 N  N     . THR   D 2 117 ? 28.06499  36.71273  18.91443  1.000 21.20026  ? 116 THR   D N     1 
ATOM   4875 C  CA    . THR   D 2 117 ? 27.94500  37.19588  20.28057  1.000 20.26572  ? 116 THR   D CA    1 
ATOM   4876 C  C     . THR   D 2 117 ? 29.11023  36.73247  21.13938  1.000 27.92890  ? 116 THR   D C     1 
ATOM   4877 O  O     . THR   D 2 117 ? 29.09330  36.91195  22.36986  1.000 26.61494  ? 116 THR   D O     1 
ATOM   4878 C  CB    . THR   D 2 117 ? 26.60592  36.77060  20.88074  1.000 21.77440  ? 116 THR   D CB    1 
ATOM   4879 O  OG1   . THR   D 2 117 ? 26.49288  35.34272  20.83632  1.000 22.68773  ? 116 THR   D OG1   1 
ATOM   4880 C  CG2   . THR   D 2 117 ? 25.45907  37.42100  20.11311  1.000 23.05045  ? 116 THR   D CG2   1 
ATOM   4881 N  N     . ALA   D 2 118 ? 30.13566  36.16529  20.51036  1.000 23.05329  ? 117 ALA   D N     1 
ATOM   4882 C  CA    . ALA   D 2 118 ? 31.36757  35.74043  21.16134  1.000 23.73644  ? 117 ALA   D CA    1 
ATOM   4883 C  C     . ALA   D 2 118 ? 32.40856  35.55540  20.07207  1.000 23.76588  ? 117 ALA   D C     1 
ATOM   4884 O  O     . ALA   D 2 118 ? 32.10089  35.63400  18.88570  1.000 23.57005  ? 117 ALA   D O     1 
ATOM   4885 C  CB    . ALA   D 2 118 ? 31.18684  34.43655  21.94503  1.000 25.33577  ? 117 ALA   D CB    1 
ATOM   4886 N  N     . LYS   D 2 119 ? 33.64083  35.28493  20.48834  1.000 25.29866  ? 118 LYS   D N     1 
ATOM   4887 C  CA    . LYS   D 2 119 ? 34.69878  34.95700  19.53639  1.000 26.14538  ? 118 LYS   D CA    1 
ATOM   4888 C  C     . LYS   D 2 119 ? 34.48045  33.55391  18.97448  1.000 23.68570  ? 118 LYS   D C     1 
ATOM   4889 O  O     . LYS   D 2 119 ? 34.29630  32.59248  19.73053  1.000 23.04598  ? 118 LYS   D O     1 
ATOM   4890 C  CB    . LYS   D 2 119 ? 36.06021  35.06673  20.23755  1.000 23.69736  ? 118 LYS   D CB    1 
ATOM   4891 C  CG    . LYS   D 2 119 ? 37.28634  34.76203  19.35600  1.000 27.11117  ? 118 LYS   D CG    1 
ATOM   4892 C  CD    . LYS   D 2 119 ? 38.57647  34.93151  20.17317  1.000 33.38281  ? 118 LYS   D CD    1 
ATOM   4893 C  CE    . LYS   D 2 119 ? 39.75154  34.29896  19.45361  1.000 41.29132  ? 118 LYS   D CE    1 
ATOM   4894 N  NZ    . LYS   D 2 119 ? 40.98092  34.27708  20.29196  1.000 51.33750  ? 118 LYS   D NZ    1 
ATOM   4895 N  N     . THR   D 2 120 ? 34.48243  33.43045  17.62704  1.000 23.66798  ? 119 THR   D N     1 
ATOM   4896 C  CA    . THR   D 2 120 ? 34.25866  32.15235  16.94595  1.000 24.30843  ? 119 THR   D CA    1 
ATOM   4897 C  C     . THR   D 2 120 ? 35.40326  31.91402  15.94646  1.000 23.78869  ? 119 THR   D C     1 
ATOM   4898 O  O     . THR   D 2 120 ? 35.19870  31.88737  14.73294  1.000 21.32951  ? 119 THR   D O     1 
ATOM   4899 C  CB    . THR   D 2 120 ? 32.89582  32.12739  16.25160  1.000 22.84363  ? 119 THR   D CB    1 
ATOM   4900 O  OG1   . THR   D 2 120 ? 32.82654  33.18166  15.27845  1.000 23.81946  ? 119 THR   D OG1   1 
ATOM   4901 C  CG2   . THR   D 2 120 ? 31.78123  32.31577  17.28492  1.000 25.59059  ? 119 THR   D CG2   1 
ATOM   4902 N  N     . GLU   D 2 121 ? 36.61590  31.72450  16.47721  1.000 24.33422  ? 120 GLU   D N     1 
ATOM   4903 C  CA    . GLU   D 2 121 ? 37.81490  31.70684  15.62957  1.000 24.31239  ? 120 GLU   D CA    1 
ATOM   4904 C  C     . GLU   D 2 121 ? 37.91329  30.48589  14.72318  1.000 25.11573  ? 120 GLU   D C     1 
ATOM   4905 O  O     . GLU   D 2 121 ? 38.63063  30.54826  13.71418  1.000 23.44110  ? 120 GLU   D O     1 
ATOM   4906 C  CB    . GLU   D 2 121 ? 39.07969  31.79983  16.49707  1.000 26.22883  ? 120 GLU   D CB    1 
ATOM   4907 C  CG    . GLU   D 2 121 ? 39.42291  30.53089  17.27467  1.000 25.56790  ? 120 GLU   D CG    1 
ATOM   4908 C  CD    . GLU   D 2 121 ? 38.55658  30.29988  18.51098  1.000 37.58030  ? 120 GLU   D CD    1 
ATOM   4909 O  OE1   . GLU   D 2 121 ? 37.79041  31.20946  18.93260  1.000 29.53635  ? 120 GLU   D OE1   1 
ATOM   4910 O  OE2   . GLU   D 2 121 ? 38.64955  29.18166  19.07501  1.000 49.44478  ? 120 GLU   D OE2   1 
ATOM   4911 N  N     . TRP   D 2 122 ? 37.23795  29.37709  15.04493  1.000 25.23535  ? 121 TRP   D N     1 
ATOM   4912 C  CA    . TRP   D 2 122 ? 37.24985  28.22847  14.13556  1.000 24.39623  ? 121 TRP   D CA    1 
ATOM   4913 C  C     . TRP   D 2 122 ? 36.54179  28.50024  12.80794  1.000 26.02563  ? 121 TRP   D C     1 
ATOM   4914 O  O     . TRP   D 2 122 ? 36.70162  27.71290  11.86325  1.000 25.80882  ? 121 TRP   D O     1 
ATOM   4915 C  CB    . TRP   D 2 122 ? 36.62434  27.00097  14.80832  1.000 25.25793  ? 121 TRP   D CB    1 
ATOM   4916 C  CG    . TRP   D 2 122 ? 35.17193  27.17350  15.16912  1.000 27.91577  ? 121 TRP   D CG    1 
ATOM   4917 C  CD1   . TRP   D 2 122 ? 34.07790  26.79126  14.43084  1.000 30.01531  ? 121 TRP   D CD1   1 
ATOM   4918 C  CD2   . TRP   D 2 122 ? 34.65545  27.78903  16.36345  1.000 23.59456  ? 121 TRP   D CD2   1 
ATOM   4919 N  NE1   . TRP   D 2 122 ? 32.91875  27.11987  15.10671  1.000 23.83000  ? 121 TRP   D NE1   1 
ATOM   4920 C  CE2   . TRP   D 2 122 ? 33.24516  27.73613  16.28732  1.000 23.63670  ? 121 TRP   D CE2   1 
ATOM   4921 C  CE3   . TRP   D 2 122 ? 35.24743  28.38533  17.47895  1.000 26.67795  ? 121 TRP   D CE3   1 
ATOM   4922 C  CZ2   . TRP   D 2 122 ? 32.42313  28.25149  17.29030  1.000 22.11269  ? 121 TRP   D CZ2   1 
ATOM   4923 C  CZ3   . TRP   D 2 122 ? 34.42928  28.89485  18.48191  1.000 29.29860  ? 121 TRP   D CZ3   1 
ATOM   4924 C  CH2   . TRP   D 2 122 ? 33.02815  28.82942  18.37344  1.000 26.42383  ? 121 TRP   D CH2   1 
ATOM   4925 N  N     . LEU   D 2 123 ? 35.77770  29.58330  12.70655  1.000 23.94791  ? 122 LEU   D N     1 
ATOM   4926 C  CA    . LEU   D 2 123 ? 35.15949  29.99348  11.45677  1.000 21.38184  ? 122 LEU   D CA    1 
ATOM   4927 C  C     . LEU   D 2 123 ? 36.08575  30.84772  10.59087  1.000 22.72241  ? 122 LEU   D C     1 
ATOM   4928 O  O     . LEU   D 2 123 ? 35.76280  31.09702  9.42449   1.000 22.88634  ? 122 LEU   D O     1 
ATOM   4929 C  CB    . LEU   D 2 123 ? 33.85133  30.75460  11.75523  1.000 21.30162  ? 122 LEU   D CB    1 
ATOM   4930 C  CG    . LEU   D 2 123 ? 32.84687  30.00934  12.63956  1.000 23.12384  ? 122 LEU   D CG    1 
ATOM   4931 C  CD1   . LEU   D 2 123 ? 31.63531  30.90397  12.91106  1.000 20.60957  ? 122 LEU   D CD1   1 
ATOM   4932 C  CD2   . LEU   D 2 123 ? 32.41963  28.69719  11.99853  1.000 25.10681  ? 122 LEU   D CD2   1 
ATOM   4933 N  N     . ASP   D 2 124 ? 37.21906  31.29545  11.13838  1.000 22.28936  ? 123 ASP   D N     1 
ATOM   4934 C  CA    . ASP   D 2 124 ? 38.19343  32.06117  10.36606  1.000 22.94914  ? 123 ASP   D CA    1 
ATOM   4935 C  C     . ASP   D 2 124 ? 38.61398  31.28350  9.12696   1.000 19.99769  ? 123 ASP   D C     1 
ATOM   4936 O  O     . ASP   D 2 124 ? 38.86831  30.08346  9.19322   1.000 24.44061  ? 123 ASP   D O     1 
ATOM   4937 C  CB    . ASP   D 2 124 ? 39.43606  32.36119  11.21392  1.000 24.43654  ? 123 ASP   D CB    1 
ATOM   4938 C  CG    . ASP   D 2 124 ? 39.16104  33.36097  12.33918  1.000 28.50448  ? 123 ASP   D CG    1 
ATOM   4939 O  OD1   . ASP   D 2 124 ? 38.06273  33.94691  12.37596  1.000 25.91738  ? 123 ASP   D OD1   1 
ATOM   4940 O  OD2   . ASP   D 2 124 ? 40.04540  33.56934  13.19476  1.000 25.54597  ? 123 ASP   D OD2   1 
ATOM   4941 N  N     . GLY   D 2 125 ? 38.69599  31.97914  8.00079   1.000 22.94233  ? 124 GLY   D N     1 
ATOM   4942 C  CA    . GLY   D 2 125 ? 39.08193  31.37644  6.73857   1.000 26.21536  ? 124 GLY   D CA    1 
ATOM   4943 C  C     . GLY   D 2 125 ? 38.02726  30.50563  6.09904   1.000 28.91626  ? 124 GLY   D C     1 
ATOM   4944 O  O     . GLY   D 2 125 ? 38.28412  29.93885  5.02662   1.000 27.52246  ? 124 GLY   D O     1 
ATOM   4945 N  N     . LYS   D 2 126 ? 36.84039  30.37616  6.71833   1.000 24.16513  ? 125 LYS   D N     1 
ATOM   4946 C  CA    . LYS   D 2 126 ? 35.72122  29.67592  6.10742   1.000 23.68113  ? 125 LYS   D CA    1 
ATOM   4947 C  C     . LYS   D 2 126 ? 34.51980  30.56738  5.85585   1.000 23.57388  ? 125 LYS   D C     1 
ATOM   4948 O  O     . LYS   D 2 126 ? 33.79902  30.35383  4.87525   1.000 24.48828  ? 125 LYS   D O     1 
ATOM   4949 C  CB    . LYS   D 2 126 ? 35.27669  28.49218  6.97941   1.000 28.26980  ? 125 LYS   D CB    1 
ATOM   4950 C  CG    . LYS   D 2 126 ? 36.41477  27.55838  7.36059   1.000 32.70496  ? 125 LYS   D CG    1 
ATOM   4951 C  CD    . LYS   D 2 126 ? 35.90091  26.27514  7.99610   1.000 38.90019  ? 125 LYS   D CD    1 
ATOM   4952 C  CE    . LYS   D 2 126 ? 37.02446  25.54911  8.74750   1.000 43.65063  ? 125 LYS   D CE    1 
ATOM   4953 N  NZ    . LYS   D 2 126 ? 38.28009  25.53345  7.94619   1.000 45.43587  ? 125 LYS   D NZ    1 
ATOM   4954 N  N     . HIS   D 2 127 ? 34.29525  31.56111  6.70687   1.000 20.81268  ? 126 HIS   D N     1 
ATOM   4955 C  CA    . HIS   D 2 127 ? 33.24778  32.54381  6.51859   1.000 20.55443  ? 126 HIS   D CA    1 
ATOM   4956 C  C     . HIS   D 2 127 ? 33.86507  33.91173  6.33317   1.000 18.86834  ? 126 HIS   D C     1 
ATOM   4957 O  O     . HIS   D 2 127 ? 34.78116  34.27794  7.06586   1.000 21.46340  ? 126 HIS   D O     1 
ATOM   4958 C  CB    . HIS   D 2 127 ? 32.31928  32.53890  7.73191   1.000 19.51957  ? 126 HIS   D CB    1 
ATOM   4959 C  CG    . HIS   D 2 127 ? 31.65105  31.22162  7.93073   1.000 20.32889  ? 126 HIS   D CG    1 
ATOM   4960 N  ND1   . HIS   D 2 127 ? 30.38352  30.96738  7.46299   1.000 20.90705  ? 126 HIS   D ND1   1 
ATOM   4961 C  CD2   . HIS   D 2 127 ? 32.10367  30.05797  8.45204   1.000 20.12026  ? 126 HIS   D CD2   1 
ATOM   4962 C  CE1   . HIS   D 2 127 ? 30.06802  29.71137  7.72404   1.000 21.45821  ? 126 HIS   D CE1   1 
ATOM   4963 N  NE2   . HIS   D 2 127 ? 31.09535  29.13696  8.31750   1.000 19.57657  ? 126 HIS   D NE2   1 
ATOM   4964 N  N     . VAL   D 2 128 ? 33.34775  34.66370  5.36586   1.000 21.07243  ? 127 VAL   D N     1 
ATOM   4965 C  CA    . VAL   D 2 128 ? 33.85994  35.99412  5.04913   1.000 19.76845  ? 127 VAL   D CA    1 
ATOM   4966 C  C     . VAL   D 2 128 ? 33.29205  36.99717  6.04778   1.000 23.80235  ? 127 VAL   D C     1 
ATOM   4967 O  O     . VAL   D 2 128 ? 32.08624  37.26418  6.04623   1.000 21.27829  ? 127 VAL   D O     1 
ATOM   4968 C  CB    . VAL   D 2 128 ? 33.50594  36.39931  3.61216   1.000 22.47060  ? 127 VAL   D CB    1 
ATOM   4969 C  CG1   . VAL   D 2 128 ? 33.93566  37.83847  3.35111   1.000 24.26407  ? 127 VAL   D CG1   1 
ATOM   4970 C  CG2   . VAL   D 2 128 ? 34.17513  35.47418  2.60528   1.000 23.86053  ? 127 VAL   D CG2   1 
ATOM   4971 N  N     . VAL   D 2 129 ? 34.15962  37.57017  6.87328   1.000 20.08162  ? 128 VAL   D N     1 
ATOM   4972 C  CA    . VAL   D 2 129 ? 33.81894  38.68836  7.73957   1.000 23.13093  ? 128 VAL   D CA    1 
ATOM   4973 C  C     . VAL   D 2 129 ? 33.80365  39.96150  6.91843   1.000 25.37313  ? 128 VAL   D C     1 
ATOM   4974 O  O     . VAL   D 2 129 ? 34.74450  40.23517  6.15232   1.000 23.72068  ? 128 VAL   D O     1 
ATOM   4975 C  CB    . VAL   D 2 129 ? 34.83339  38.81138  8.88398   1.000 20.79361  ? 128 VAL   D CB    1 
ATOM   4976 C  CG1   . VAL   D 2 129 ? 34.55421  40.06630  9.67445   1.000 22.14159  ? 128 VAL   D CG1   1 
ATOM   4977 C  CG2   . VAL   D 2 129 ? 34.80836  37.56718  9.74305   1.000 19.65956  ? 128 VAL   D CG2   1 
ATOM   4978 N  N     . PHE   D 2 130 ? 32.76351  40.76038  7.09386   1.000 21.27258  ? 129 PHE   D N     1 
ATOM   4979 C  CA    . PHE   D 2 130 ? 32.63577  41.94701  6.25817   1.000 22.89225  ? 129 PHE   D CA    1 
ATOM   4980 C  C     . PHE   D 2 130 ? 32.05822  43.13826  7.00616   1.000 23.17450  ? 129 PHE   D C     1 
ATOM   4981 O  O     . PHE   D 2 130 ? 31.80214  44.17027  6.37401   1.000 25.03648  ? 129 PHE   D O     1 
ATOM   4982 C  CB    . PHE   D 2 130 ? 31.78459  41.63749  5.01772   1.000 24.69769  ? 129 PHE   D CB    1 
ATOM   4983 C  CG    . PHE   D 2 130 ? 30.33838  41.33732  5.33297   1.000 24.18374  ? 129 PHE   D CG    1 
ATOM   4984 C  CD1   . PHE   D 2 130 ? 29.94077  40.04763  5.62638   1.000 21.44388  ? 129 PHE   D CD1   1 
ATOM   4985 C  CD2   . PHE   D 2 130 ? 29.38778  42.35699  5.34182   1.000 22.94961  ? 129 PHE   D CD2   1 
ATOM   4986 C  CE1   . PHE   D 2 130 ? 28.61435  39.77108  5.93337   1.000 20.75824  ? 129 PHE   D CE1   1 
ATOM   4987 C  CE2   . PHE   D 2 130 ? 28.05632  42.09493  5.64066   1.000 23.72109  ? 129 PHE   D CE2   1 
ATOM   4988 C  CZ    . PHE   D 2 130 ? 27.66194  40.79606  5.92424   1.000 24.83489  ? 129 PHE   D CZ    1 
ATOM   4989 N  N     . GLY   D 2 131 ? 31.85922  43.05523  8.31780   1.000 23.97857  ? 130 GLY   D N     1 
ATOM   4990 C  CA    . GLY   D 2 131 ? 31.34785  44.21528  9.01594   1.000 25.46579  ? 130 GLY   D CA    1 
ATOM   4991 C  C     . GLY   D 2 131 ? 31.32988  43.97561  10.50667  1.000 22.62543  ? 130 GLY   D C     1 
ATOM   4992 O  O     . GLY   D 2 131 ? 31.78280  42.93972  10.99992  1.000 23.84976  ? 130 GLY   D O     1 
ATOM   4993 N  N     . LYS   D 2 132 ? 30.79660  44.96055  11.22572  1.000 24.36112  ? 131 LYS   D N     1 
ATOM   4994 C  CA    . LYS   D 2 132 ? 30.73418  44.89105  12.67953  1.000 23.24132  ? 131 LYS   D CA    1 
ATOM   4995 C  C     . LYS   D 2 132 ? 29.59595  45.77451  13.16418  1.000 26.64210  ? 131 LYS   D C     1 
ATOM   4996 O  O     . LYS   D 2 132 ? 29.25663  46.77670  12.53010  1.000 27.40696  ? 131 LYS   D O     1 
ATOM   4997 C  CB    . LYS   D 2 132 ? 32.06026  45.32292  13.31678  1.000 24.21532  ? 131 LYS   D CB    1 
ATOM   4998 C  CG    . LYS   D 2 132 ? 32.28174  44.80584  14.72680  1.000 37.66779  ? 131 LYS   D CG    1 
ATOM   4999 C  CD    . LYS   D 2 132 ? 33.72898  45.01340  15.23157  1.000 43.21866  ? 131 LYS   D CD    1 
ATOM   5000 C  CE    . LYS   D 2 132 ? 33.84536  44.64005  16.71425  1.000 51.08841  ? 131 LYS   D CE    1 
ATOM   5001 N  NZ    . LYS   D 2 132 ? 32.77978  43.63747  17.02109  1.000 46.51502  ? 131 LYS   D NZ    1 
ATOM   5002 N  N     . VAL   D 2 133 ? 28.96604  45.34149  14.26221  1.000 28.28980  ? 132 VAL   D N     1 
ATOM   5003 C  CA    . VAL   D 2 133 ? 27.96183  46.16635  14.92551  1.000 26.18644  ? 132 VAL   D CA    1 
ATOM   5004 C  C     . VAL   D 2 133 ? 28.60646  47.46039  15.40594  1.000 25.05711  ? 132 VAL   D C     1 
ATOM   5005 O  O     . VAL   D 2 133 ? 29.63639  47.44725  16.08885  1.000 29.59312  ? 132 VAL   D O     1 
ATOM   5006 C  CB    . VAL   D 2 133 ? 27.33195  45.39536  16.09559  1.000 25.15831  ? 132 VAL   D CB    1 
ATOM   5007 C  CG1   . VAL   D 2 133 ? 26.41177  46.29972  16.91725  1.000 30.20273  ? 132 VAL   D CG1   1 
ATOM   5008 C  CG2   . VAL   D 2 133 ? 26.58587  44.15066  15.58257  1.000 21.32912  ? 132 VAL   D CG2   1 
ATOM   5009 N  N     . LYS   D 2 134 ? 27.98102  48.58638  15.07375  1.000 27.17265  ? 133 LYS   D N     1 
ATOM   5010 C  CA    . LYS   D 2 134 ? 28.42916  49.90857  15.49488  1.000 26.79182  ? 133 LYS   D CA    1 
ATOM   5011 C  C     . LYS   D 2 134 ? 27.62365  50.41298  16.68490  1.000 32.63330  ? 133 LYS   D C     1 
ATOM   5012 O  O     . LYS   D 2 134 ? 28.18412  50.76525  17.72665  1.000 37.52789  ? 133 LYS   D O     1 
ATOM   5013 C  CB    . LYS   D 2 134 ? 28.30447  50.87833  14.30890  1.000 33.94295  ? 133 LYS   D CB    1 
ATOM   5014 C  CG    . LYS   D 2 134 ? 28.65561  52.32972  14.58605  1.000 40.40261  ? 133 LYS   D CG    1 
ATOM   5015 C  CD    . LYS   D 2 134 ? 28.45380  53.12131  13.29800  1.000 46.45922  ? 133 LYS   D CD    1 
ATOM   5016 C  CE    . LYS   D 2 134 ? 28.85194  54.57418  13.43558  1.000 48.98180  ? 133 LYS   D CE    1 
ATOM   5017 N  NZ    . LYS   D 2 134 ? 28.68900  55.25459  12.11455  1.000 52.50562  ? 133 LYS   D NZ    1 
ATOM   5018 N  N     . GLU   D 2 135 ? 26.30731  50.43991  16.55272  1.000 30.48042  ? 134 GLU   D N     1 
ATOM   5019 C  CA    . GLU   D 2 135 ? 25.44706  50.82719  17.65540  1.000 40.08842  ? 134 GLU   D CA    1 
ATOM   5020 C  C     . GLU   D 2 135 ? 24.39901  49.75342  17.88676  1.000 31.30711  ? 134 GLU   D C     1 
ATOM   5021 O  O     . GLU   D 2 135 ? 23.96154  49.06987  16.95452  1.000 29.80854  ? 134 GLU   D O     1 
ATOM   5022 C  CB    . GLU   D 2 135 ? 24.77577  52.17751  17.39133  1.000 35.68431  ? 134 GLU   D CB    1 
ATOM   5023 C  CG    . GLU   D 2 135 ? 25.70914  53.34740  17.63158  1.000 45.56346  ? 134 GLU   D CG    1 
ATOM   5024 C  CD    . GLU   D 2 135 ? 24.98773  54.66971  17.66000  1.000 60.58606  ? 134 GLU   D CD    1 
ATOM   5025 O  OE1   . GLU   D 2 135 ? 24.29541  54.98632  16.66617  1.000 64.90890  ? 134 GLU   D OE1   1 
ATOM   5026 O  OE2   . GLU   D 2 135 ? 25.10278  55.38455  18.68228  1.000 66.84896  ? 134 GLU   D OE2   1 
ATOM   5027 N  N     . GLY   D 2 136 ? 23.99464  49.61779  19.14963  1.000 32.69422  ? 135 GLY   D N     1 
ATOM   5028 C  CA    . GLY   D 2 136 ? 22.92389  48.69864  19.46808  1.000 30.76486  ? 135 GLY   D CA    1 
ATOM   5029 C  C     . GLY   D 2 136 ? 23.35060  47.26440  19.65785  1.000 26.22235  ? 135 GLY   D C     1 
ATOM   5030 O  O     . GLY   D 2 136 ? 22.56665  46.35518  19.39156  1.000 25.90777  ? 135 GLY   D O     1 
ATOM   5031 N  N     . MET   D 2 137 ? 24.58588  47.02441  20.09364  1.000 24.26484  ? 136 MET   D N     1 
ATOM   5032 C  CA    . MET   D 2 137 ? 24.94400  45.66352  20.47164  1.000 26.70295  ? 136 MET   D CA    1 
ATOM   5033 C  C     . MET   D 2 137 ? 24.04682  45.14039  21.59773  1.000 27.68385  ? 136 MET   D C     1 
ATOM   5034 O  O     . MET   D 2 137 ? 23.82958  43.92697  21.70588  1.000 22.96839  ? 136 MET   D O     1 
ATOM   5035 C  CB    . MET   D 2 137 ? 26.40730  45.59108  20.89203  1.000 30.03614  ? 136 MET   D CB    1 
ATOM   5036 C  CG    . MET   D 2 137 ? 26.90358  44.16441  21.13415  1.000 26.99933  ? 136 MET   D CG    1 
ATOM   5037 S  SD    . MET   D 2 137 ? 26.90450  43.18962  19.58100  1.000 27.19820  ? 136 MET   D SD    1 
ATOM   5038 C  CE    . MET   D 2 137 ? 27.01729  41.53003  20.23133  1.000 25.68770  ? 136 MET   D CE    1 
ATOM   5039 N  N     . ASN   D 2 138 ? 23.51124  46.02449  22.44666  1.000 26.78659  ? 137 ASN   D N     1 
ATOM   5040 C  CA    . ASN   D 2 138 ? 22.62546  45.51187  23.48986  1.000 25.95140  ? 137 ASN   D CA    1 
ATOM   5041 C  C     . ASN   D 2 138 ? 21.33459  44.93813  22.90773  1.000 25.46080  ? 137 ASN   D C     1 
ATOM   5042 O  O     . ASN   D 2 138 ? 20.71672  44.05725  23.52340  1.000 26.74207  ? 137 ASN   D O     1 
ATOM   5043 C  CB    . ASN   D 2 138 ? 22.32668  46.59583  24.54080  1.000 26.45021  ? 137 ASN   D CB    1 
ATOM   5044 C  CG    . ASN   D 2 138 ? 21.85341  47.90317  23.93452  1.000 27.36532  ? 137 ASN   D CG    1 
ATOM   5045 O  OD1   . ASN   D 2 138 ? 21.61658  47.99795  22.73689  1.000 30.35512  ? 137 ASN   D OD1   1 
ATOM   5046 N  ND2   . ASN   D 2 138 ? 21.70003  48.92873  24.77942  1.000 36.43897  ? 137 ASN   D ND2   1 
ATOM   5047 N  N     . ILE   D 2 139 ? 20.92312  45.40127  21.72661  1.000 23.48871  ? 138 ILE   D N     1 
ATOM   5048 C  CA    . ILE   D 2 139 ? 19.79809  44.78501  21.02779  1.000 24.69998  ? 138 ILE   D CA    1 
ATOM   5049 C  C     . ILE   D 2 139 ? 20.12617  43.33696  20.66939  1.000 28.31097  ? 138 ILE   D C     1 
ATOM   5050 O  O     . ILE   D 2 139 ? 19.29987  42.43077  20.84234  1.000 25.97804  ? 138 ILE   D O     1 
ATOM   5051 C  CB    . ILE   D 2 139 ? 19.42322  45.60557  19.77744  1.000 25.26416  ? 138 ILE   D CB    1 
ATOM   5052 C  CG1   . ILE   D 2 139 ? 19.11172  47.06529  20.12932  1.000 27.96639  ? 138 ILE   D CG1   1 
ATOM   5053 C  CG2   . ILE   D 2 139 ? 18.24363  44.96916  19.03511  1.000 25.77690  ? 138 ILE   D CG2   1 
ATOM   5054 C  CD1   . ILE   D 2 139 ? 17.89592  47.19975  21.06019  1.000 28.72885  ? 138 ILE   D CD1   1 
ATOM   5055 N  N     . VAL   D 2 140 ? 21.33642  43.09622  20.15212  1.000 24.63443  ? 139 VAL   D N     1 
ATOM   5056 C  CA    . VAL   D 2 140 ? 21.72363  41.73728  19.79418  1.000 24.60011  ? 139 VAL   D CA    1 
ATOM   5057 C  C     . VAL   D 2 140 ? 21.80169  40.86926  21.03668  1.000 24.97981  ? 139 VAL   D C     1 
ATOM   5058 O  O     . VAL   D 2 140 ? 21.33824  39.72444  21.03866  1.000 24.31360  ? 139 VAL   D O     1 
ATOM   5059 C  CB    . VAL   D 2 140 ? 23.05498  41.75823  19.01256  1.000 24.10069  ? 139 VAL   D CB    1 
ATOM   5060 C  CG1   . VAL   D 2 140 ? 23.49223  40.32961  18.68275  1.000 20.12040  ? 139 VAL   D CG1   1 
ATOM   5061 C  CG2   . VAL   D 2 140 ? 22.86690  42.57867  17.74441  1.000 23.34053  ? 139 VAL   D CG2   1 
ATOM   5062 N  N     . GLU   D 2 141 ? 22.39677  41.38904  22.11062  1.000 22.89870  ? 140 GLU   D N     1 
ATOM   5063 C  CA    . GLU   D 2 141 ? 22.42182  40.64390  23.36046  1.000 24.36687  ? 140 GLU   D CA    1 
ATOM   5064 C  C     . GLU   D 2 141 ? 21.00436  40.28856  23.79906  1.000 26.68446  ? 140 GLU   D C     1 
ATOM   5065 O  O     . GLU   D 2 141 ? 20.74907  39.17066  24.26053  1.000 26.25346  ? 140 GLU   D O     1 
ATOM   5066 C  CB    . GLU   D 2 141 ? 23.14568  41.45897  24.43198  1.000 27.31794  ? 140 GLU   D CB    1 
ATOM   5067 C  CG    . GLU   D 2 141 ? 24.61158  41.71857  24.05702  1.000 28.98355  ? 140 GLU   D CG    1 
ATOM   5068 C  CD    . GLU   D 2 141 ? 25.28612  42.77497  24.91925  1.000 35.09870  ? 140 GLU   D CD    1 
ATOM   5069 O  OE1   . GLU   D 2 141 ? 24.58014  43.56738  25.56991  1.000 34.94416  ? 140 GLU   D OE1   1 
ATOM   5070 O  OE2   . GLU   D 2 141 ? 26.53147  42.81686  24.92609  1.000 41.17603  ? 140 GLU   D OE2   1 
ATOM   5071 N  N     . ALA   D 2 142 ? 20.06341  41.21109  23.60473  1.000 25.04680  ? 141 ALA   D N     1 
ATOM   5072 C  CA    . ALA   D 2 142 ? 18.68539  40.96137  24.02809  1.000 24.24550  ? 141 ALA   D CA    1 
ATOM   5073 C  C     . ALA   D 2 142 ? 18.00508  39.89776  23.17027  1.000 27.32536  ? 141 ALA   D C     1 
ATOM   5074 O  O     . ALA   D 2 142 ? 17.11867  39.19231  23.65081  1.000 26.96772  ? 141 ALA   D O     1 
ATOM   5075 C  CB    . ALA   D 2 142 ? 17.88050  42.26264  23.98617  1.000 26.72738  ? 141 ALA   D CB    1 
ATOM   5076 N  N     . MET   D 2 143 ? 18.39982  39.76516  21.90031  1.000 25.25444  ? 142 MET   D N     1 
ATOM   5077 C  CA    . MET   D 2 143 ? 17.83236  38.73593  21.04514  1.000 24.30438  ? 142 MET   D CA    1 
ATOM   5078 C  C     . MET   D 2 143 ? 18.21656  37.33142  21.49776  1.000 27.46800  ? 142 MET   D C     1 
ATOM   5079 O  O     . MET   D 2 143 ? 17.48585  36.37786  21.20428  1.000 25.83838  ? 142 MET   D O     1 
ATOM   5080 C  CB    . MET   D 2 143 ? 18.27049  38.97032  19.58685  1.000 23.06306  ? 142 MET   D CB    1 
ATOM   5081 C  CG    . MET   D 2 143 ? 17.79575  40.29905  18.96419  1.000 24.52472  ? 142 MET   D CG    1 
ATOM   5082 S  SD    . MET   D 2 143 ? 18.70148  40.80995  17.46370  1.000 29.04133  ? 142 MET   D SD    1 
ATOM   5083 C  CE    . MET   D 2 143 ? 18.64291  39.28387  16.55957  1.000 23.93066  ? 142 MET   D CE    1 
ATOM   5084 N  N     . GLU   D 2 144 ? 19.32769  37.18327  22.22378  1.000 27.91471  ? 143 GLU   D N     1 
ATOM   5085 C  CA    . GLU   D 2 144 ? 19.84712  35.85244  22.52345  1.000 24.80198  ? 143 GLU   D CA    1 
ATOM   5086 C  C     . GLU   D 2 144 ? 18.86213  35.01536  23.32122  1.000 28.06096  ? 143 GLU   D C     1 
ATOM   5087 O  O     . GLU   D 2 144 ? 18.78288  33.79874  23.12404  1.000 30.57590  ? 143 GLU   D O     1 
ATOM   5088 C  CB    . GLU   D 2 144 ? 21.16292  35.94519  23.29258  1.000 26.98763  ? 143 GLU   D CB    1 
ATOM   5089 C  CG    . GLU   D 2 144 ? 22.37557  36.07340  22.39625  1.000 26.32548  ? 143 GLU   D CG    1 
ATOM   5090 C  CD    . GLU   D 2 144 ? 23.65227  35.67176  23.11528  1.000 27.36412  ? 143 GLU   D CD    1 
ATOM   5091 O  OE1   . GLU   D 2 144 ? 23.84371  36.08624  24.26710  1.000 29.63080  ? 143 GLU   D OE1   1 
ATOM   5092 O  OE2   . GLU   D 2 144 ? 24.45945  34.91613  22.54344  1.000 29.07723  ? 143 GLU   D OE2   1 
ATOM   5093 N  N     . ARG   D 2 145 ? 18.12573  35.63042  24.25162  1.000 26.73108  ? 144 ARG   D N     1 
ATOM   5094 C  CA    . ARG   D 2 145 ? 17.24660  34.82276  25.08724  1.000 30.13653  ? 144 ARG   D CA    1 
ATOM   5095 C  C     . ARG   D 2 145 ? 16.08520  34.22255  24.31411  1.000 28.24022  ? 144 ARG   D C     1 
ATOM   5096 O  O     . ARG   D 2 145 ? 15.41850  33.32455  24.83315  1.000 32.90509  ? 144 ARG   D O     1 
ATOM   5097 C  CB    . ARG   D 2 145 ? 16.72450  35.63247  26.27888  1.000 34.28892  ? 144 ARG   D CB    1 
ATOM   5098 C  CG    . ARG   D 2 145 ? 15.60484  36.61624  25.98053  1.000 37.48578  ? 144 ARG   D CG    1 
ATOM   5099 C  CD    . ARG   D 2 145 ? 15.07455  37.13669  27.30773  1.000 38.00607  ? 144 ARG   D CD    1 
ATOM   5100 N  NE    . ARG   D 2 145 ? 14.14536  38.25180  27.18930  1.000 37.18704  ? 144 ARG   D NE    1 
ATOM   5101 C  CZ    . ARG   D 2 145 ? 12.82846  38.13492  27.30306  1.000 44.82662  ? 144 ARG   D CZ    1 
ATOM   5102 N  NH1   . ARG   D 2 145 ? 12.24675  36.94888  27.39920  1.000 37.57177  ? 144 ARG   D NH1   1 
ATOM   5103 N  NH2   . ARG   D 2 145 ? 12.07885  39.23549  27.34650  1.000 38.88577  ? 144 ARG   D NH2   1 
ATOM   5104 N  N     . PHE   D 2 146 ? 15.85451  34.63694  23.07753  1.000 23.18865  ? 145 PHE   D N     1 
ATOM   5105 C  CA    . PHE   D 2 146 ? 14.82153  33.97519  22.30649  1.000 22.47004  ? 145 PHE   D CA    1 
ATOM   5106 C  C     . PHE   D 2 146 ? 15.35941  32.78779  21.52552  1.000 21.10387  ? 145 PHE   D C     1 
ATOM   5107 O  O     . PHE   D 2 146 ? 14.60318  32.15497  20.79660  1.000 23.78215  ? 145 PHE   D O     1 
ATOM   5108 C  CB    . PHE   D 2 146 ? 14.13129  34.99439  21.39499  1.000 25.20816  ? 145 PHE   D CB    1 
ATOM   5109 C  CG    . PHE   D 2 146 ? 13.63222  36.20007  22.14136  1.000 25.36234  ? 145 PHE   D CG    1 
ATOM   5110 C  CD1   . PHE   D 2 146 ? 12.43765  36.14858  22.86157  1.000 29.00318  ? 145 PHE   D CD1   1 
ATOM   5111 C  CD2   . PHE   D 2 146 ? 14.36867  37.37245  22.16173  1.000 25.59947  ? 145 PHE   D CD2   1 
ATOM   5112 C  CE1   . PHE   D 2 146 ? 12.00641  37.25341  23.56440  1.000 28.99180  ? 145 PHE   D CE1   1 
ATOM   5113 C  CE2   . PHE   D 2 146 ? 13.93733  38.47254  22.84708  1.000 26.91399  ? 145 PHE   D CE2   1 
ATOM   5114 C  CZ    . PHE   D 2 146 ? 12.74834  38.41415  23.56762  1.000 28.74177  ? 145 PHE   D CZ    1 
ATOM   5115 N  N     . GLY   D 2 147 ? 16.64023  32.45412  21.68522  1.000 23.09604  ? 146 GLY   D N     1 
ATOM   5116 C  CA    . GLY   D 2 147 ? 17.22597  31.30052  21.05586  1.000 24.61761  ? 146 GLY   D CA    1 
ATOM   5117 C  C     . GLY   D 2 147 ? 17.31142  30.09314  21.97048  1.000 28.85014  ? 146 GLY   D C     1 
ATOM   5118 O  O     . GLY   D 2 147 ? 16.67903  30.03223  23.03387  1.000 28.22724  ? 146 GLY   D O     1 
ATOM   5119 N  N     . SER   D 2 148 ? 18.08314  29.09948  21.52322  1.000 23.00402  ? 147 SER   D N     1 
ATOM   5120 C  CA    . SER   D 2 148 ? 18.19984  27.81506  22.20700  1.000 27.21532  ? 147 SER   D CA    1 
ATOM   5121 C  C     . SER   D 2 148 ? 19.46932  27.10251  21.74771  1.000 27.06836  ? 147 SER   D C     1 
ATOM   5122 O  O     . SER   D 2 148 ? 20.19869  27.58077  20.87497  1.000 21.98700  ? 147 SER   D O     1 
ATOM   5123 C  CB    . SER   D 2 148 ? 16.97190  26.94640  21.94256  1.000 27.27809  ? 147 SER   D CB    1 
ATOM   5124 O  OG    . SER   D 2 148 ? 16.86274  26.65387  20.56916  1.000 24.74595  ? 147 SER   D OG    1 
ATOM   5125 N  N     . ARG   D 2 149 ? 19.70307  25.91622  22.32338  1.000 25.10764  ? 148 ARG   D N     1 
ATOM   5126 C  CA    . ARG   D 2 149 ? 20.91704  25.16139  22.03060  1.000 26.22820  ? 148 ARG   D CA    1 
ATOM   5127 C  C     . ARG   D 2 149 ? 21.04312  24.83516  20.53612  1.000 25.85555  ? 148 ARG   D C     1 
ATOM   5128 O  O     . ARG   D 2 149 ? 22.12519  24.97729  19.96374  1.000 21.27604  ? 148 ARG   D O     1 
ATOM   5129 C  CB    . ARG   D 2 149 ? 20.93884  23.89393  22.88494  1.000 30.87640  ? 148 ARG   D CB    1 
ATOM   5130 C  CG    . ARG   D 2 149 ? 22.10667  22.98594  22.63310  1.000 31.87028  ? 148 ARG   D CG    1 
ATOM   5131 C  CD    . ARG   D 2 149 ? 22.11248  21.83523  23.61488  1.000 37.40628  ? 148 ARG   D CD    1 
ATOM   5132 N  NE    . ARG   D 2 149 ? 23.27637  20.98515  23.41270  1.000 34.60176  ? 148 ARG   D NE    1 
ATOM   5133 C  CZ    . ARG   D 2 149 ? 23.27511  19.92188  22.62338  1.000 36.96348  ? 148 ARG   D CZ    1 
ATOM   5134 N  NH1   . ARG   D 2 149 ? 22.18265  19.55066  21.97352  1.000 38.13735  ? 148 ARG   D NH1   1 
ATOM   5135 N  NH2   . ARG   D 2 149 ? 24.39681  19.21759  22.48068  1.000 35.87854  ? 148 ARG   D NH2   1 
ATOM   5136 N  N     . ASN   D 2 150 ? 19.95999  24.40929  19.88636  1.000 25.42990  ? 149 ASN   D N     1 
ATOM   5137 C  CA    . ASN   D 2 150 ? 20.01933  24.13015  18.45566  1.000 26.46829  ? 149 ASN   D CA    1 
ATOM   5138 C  C     . ASN   D 2 150 ? 19.59262  25.31313  17.59126  1.000 22.95686  ? 149 ASN   D C     1 
ATOM   5139 O  O     . ASN   D 2 150 ? 19.56345  25.18344  16.36473  1.000 23.87310  ? 149 ASN   D O     1 
ATOM   5140 C  CB    . ASN   D 2 150 ? 19.20467  22.87934  18.09542  1.000 27.72019  ? 149 ASN   D CB    1 
ATOM   5141 C  CG    . ASN   D 2 150 ? 17.71042  23.12706  18.04509  1.000 26.14711  ? 149 ASN   D CG    1 
ATOM   5142 O  OD1   . ASN   D 2 150 ? 17.22322  24.17317  18.44182  1.000 28.97492  ? 149 ASN   D OD1   1 
ATOM   5143 N  ND2   . ASN   D 2 150 ? 16.97907  22.14689  17.54252  1.000 31.46258  ? 149 ASN   D ND2   1 
ATOM   5144 N  N     . GLY   D 2 151 ? 19.31063  26.46727  18.18538  1.000 18.91517  ? 150 GLY   D N     1 
ATOM   5145 C  CA    . GLY   D 2 151 ? 19.03468  27.67095  17.43830  1.000 20.31429  ? 150 GLY   D CA    1 
ATOM   5146 C  C     . GLY   D 2 151 ? 17.57751  27.97941  17.16298  1.000 23.65603  ? 150 GLY   D C     1 
ATOM   5147 O  O     . GLY   D 2 151 ? 17.28126  29.12110  16.78249  1.000 22.95099  ? 150 GLY   D O     1 
ATOM   5148 N  N     . LYS   D 2 152 ? 16.65890  27.02560  17.36551  1.000 23.35627  ? 151 LYS   D N     1 
ATOM   5149 C  CA    . LYS   D 2 152 ? 15.23641  27.34865  17.22453  1.000 25.05230  ? 151 LYS   D CA    1 
ATOM   5150 C  C     . LYS   D 2 152 ? 14.85357  28.50697  18.14296  1.000 21.47003  ? 151 LYS   D C     1 
ATOM   5151 O  O     . LYS   D 2 152 ? 15.26806  28.56776  19.30345  1.000 25.05915  ? 151 LYS   D O     1 
ATOM   5152 C  CB    . LYS   D 2 152 ? 14.33919  26.13725  17.52406  1.000 27.81727  ? 151 LYS   D CB    1 
ATOM   5153 C  CG    . LYS   D 2 152 ? 14.58695  24.84942  16.72346  1.000 45.94441  ? 151 LYS   D CG    1 
ATOM   5154 C  CD    . LYS   D 2 152 ? 14.92988  25.06104  15.23914  1.000 47.36607  ? 151 LYS   D CD    1 
ATOM   5155 C  CE    . LYS   D 2 152 ? 14.45544  23.87139  14.33099  1.000 47.48529  ? 151 LYS   D CE    1 
ATOM   5156 N  NZ    . LYS   D 2 152 ? 15.55682  22.87331  13.95682  1.000 41.51179  ? 151 LYS   D NZ    1 
ATOM   5157 N  N     . THR   D 2 153 ? 14.04533  29.43407  17.62715  1.000 22.83989  ? 152 THR   D N     1 
ATOM   5158 C  CA    . THR   D 2 153 ? 13.67236  30.60646  18.40367  1.000 21.26117  ? 152 THR   D CA    1 
ATOM   5159 C  C     . THR   D 2 153 ? 12.28485  30.39657  18.99761  1.000 21.76198  ? 152 THR   D C     1 
ATOM   5160 O  O     . THR   D 2 153 ? 11.43141  29.73068  18.40950  1.000 25.95839  ? 152 THR   D O     1 
ATOM   5161 C  CB    . THR   D 2 153 ? 13.70318  31.89650  17.57183  1.000 20.23467  ? 152 THR   D CB    1 
ATOM   5162 O  OG1   . THR   D 2 153 ? 12.75972  31.81735  16.49076  1.000 26.16822  ? 152 THR   D OG1   1 
ATOM   5163 C  CG2   . THR   D 2 153 ? 15.12683  32.11581  16.98230  1.000 21.50389  ? 152 THR   D CG2   1 
ATOM   5164 N  N     . SER   D 2 154 ? 12.07238  30.98019  20.16554  1.000 22.81200  ? 153 SER   D N     1 
ATOM   5165 C  CA    . SER   D 2 154 ? 10.80873  30.84224  20.88120  1.000 23.18998  ? 153 SER   D CA    1 
ATOM   5166 C  C     . SER   D 2 154 ? 9.83970   31.97728  20.58550  1.000 33.16289  ? 153 SER   D C     1 
ATOM   5167 O  O     . SER   D 2 154 ? 8.66452   31.89852  20.98102  1.000 28.89293  ? 153 SER   D O     1 
ATOM   5168 C  CB    . SER   D 2 154 ? 11.07308  30.75503  22.38657  1.000 26.61783  ? 153 SER   D CB    1 
ATOM   5169 O  OG    . SER   D 2 154 ? 11.83563  31.85960  22.83960  1.000 26.24722  ? 153 SER   D OG    1 
ATOM   5170 N  N     . LYS   D 2 155 ? 10.31013  33.04137  19.93928  1.000 27.15623  ? 154 LYS   D N     1 
ATOM   5171 C  CA    . LYS   D 2 155 ? 9.45012   34.07338  19.37618  1.000 30.27771  ? 154 LYS   D CA    1 
ATOM   5172 C  C     . LYS   D 2 155 ? 9.99743   34.43057  17.99830  1.000 30.26844  ? 154 LYS   D C     1 
ATOM   5173 O  O     . LYS   D 2 155 ? 11.12335  34.06706  17.64952  1.000 25.50899  ? 154 LYS   D O     1 
ATOM   5174 C  CB    . LYS   D 2 155 ? 9.36762   35.29956  20.29602  1.000 30.21082  ? 154 LYS   D CB    1 
ATOM   5175 C  CG    . LYS   D 2 155 ? 8.75925   34.98679  21.67013  1.000 33.00683  ? 154 LYS   D CG    1 
ATOM   5176 C  CD    . LYS   D 2 155 ? 8.65017   36.23076  22.52465  1.000 35.23227  ? 154 LYS   D CD    1 
ATOM   5177 C  CE    . LYS   D 2 155 ? 7.93178   35.94772  23.84029  1.000 35.86875  ? 154 LYS   D CE    1 
ATOM   5178 N  NZ    . LYS   D 2 155 ? 7.65945   37.23284  24.52542  1.000 44.34183  ? 154 LYS   D NZ    1 
ATOM   5179 N  N     . LYS   D 2 156 ? 9.18441   35.10178  17.18897  1.000 26.90318  ? 155 LYS   D N     1 
ATOM   5180 C  CA    . LYS   D 2 156 ? 9.61321   35.49229  15.84454  1.000 28.20548  ? 155 LYS   D CA    1 
ATOM   5181 C  C     . LYS   D 2 156 ? 10.39044  36.79875  15.94176  1.000 26.13875  ? 155 LYS   D C     1 
ATOM   5182 O  O     . LYS   D 2 156 ? 9.82825   37.83652  16.29725  1.000 27.62379  ? 155 LYS   D O     1 
ATOM   5183 C  CB    . LYS   D 2 156 ? 8.41788   35.62560  14.90365  1.000 29.82557  ? 155 LYS   D CB    1 
ATOM   5184 C  CG    . LYS   D 2 156 ? 7.64120   34.33025  14.70628  1.000 35.06239  ? 155 LYS   D CG    1 
ATOM   5185 C  CD    . LYS   D 2 156 ? 6.50487   34.49985  13.69687  1.000 46.85331  ? 155 LYS   D CD    1 
ATOM   5186 C  CE    . LYS   D 2 156 ? 5.14273   34.22879  14.34190  1.000 48.83831  ? 155 LYS   D CE    1 
ATOM   5187 N  NZ    . LYS   D 2 156 ? 4.85351   35.17965  15.45987  1.000 45.10330  ? 155 LYS   D NZ    1 
ATOM   5188 N  N     . ILE   D 2 157 ? 11.69072  36.74715  15.62401  1.000 25.75232  ? 156 ILE   D N     1 
ATOM   5189 C  CA    . ILE   D 2 157 ? 12.58206  37.90330  15.69883  1.000 25.82554  ? 156 ILE   D CA    1 
ATOM   5190 C  C     . ILE   D 2 157 ? 12.76168  38.40986  14.27688  1.000 23.47592  ? 156 ILE   D C     1 
ATOM   5191 O  O     . ILE   D 2 157 ? 13.34331  37.70435  13.44639  1.000 29.47080  ? 156 ILE   D O     1 
ATOM   5192 C  CB    . ILE   D 2 157 ? 13.93593  37.51886  16.31330  1.000 29.97066  ? 156 ILE   D CB    1 
ATOM   5193 C  CG1   . ILE   D 2 157 ? 13.72045  36.69556  17.58939  1.000 27.96229  ? 156 ILE   D CG1   1 
ATOM   5194 C  CG2   . ILE   D 2 157 ? 14.83271  38.75766  16.50979  1.000 25.65683  ? 156 ILE   D CG2   1 
ATOM   5195 C  CD1   . ILE   D 2 157 ? 12.91709  37.42872  18.66764  1.000 27.51637  ? 156 ILE   D CD1   1 
ATOM   5196 N  N     . THR   D 2 158 ? 12.27159  39.61452  13.96883  1.000 26.07902  ? 157 THR   D N     1 
ATOM   5197 C  CA    . THR   D 2 158 ? 12.20652  40.05423  12.58131  1.000 27.13993  ? 157 THR   D CA    1 
ATOM   5198 C  C     . THR   D 2 158 ? 12.93549  41.37300  12.36546  1.000 28.93390  ? 157 THR   D C     1 
ATOM   5199 O  O     . THR   D 2 158 ? 13.12900  42.17514  13.28182  1.000 28.50782  ? 157 THR   D O     1 
ATOM   5200 C  CB    . THR   D 2 158 ? 10.74978  40.20707  12.09468  1.000 32.57952  ? 157 THR   D CB    1 
ATOM   5201 O  OG1   . THR   D 2 158 ? 10.04510  41.10671  12.95611  1.000 31.21122  ? 157 THR   D OG1   1 
ATOM   5202 C  CG2   . THR   D 2 158 ? 10.04382  38.85809  12.05821  1.000 32.68285  ? 157 THR   D CG2   1 
ATOM   5203 N  N     . ILE   D 2 159 ? 13.34085  41.57492  11.11107  1.000 28.89661  ? 158 ILE   D N     1 
ATOM   5204 C  CA    . ILE   D 2 159 ? 13.86388  42.85483  10.65123  1.000 25.18035  ? 158 ILE   D CA    1 
ATOM   5205 C  C     . ILE   D 2 159 ? 12.65260  43.63841  10.16064  1.000 28.08906  ? 158 ILE   D C     1 
ATOM   5206 O  O     . ILE   D 2 159 ? 12.23747  43.53171  9.00861   1.000 28.85557  ? 158 ILE   D O     1 
ATOM   5207 C  CB    . ILE   D 2 159 ? 14.91808  42.66848  9.56846   1.000 27.83968  ? 158 ILE   D CB    1 
ATOM   5208 C  CG1   . ILE   D 2 159 ? 16.13877  41.97993  10.18485  1.000 26.84121  ? 158 ILE   D CG1   1 
ATOM   5209 C  CG2   . ILE   D 2 159 ? 15.27498  44.00441  8.90360   1.000 28.16984  ? 158 ILE   D CG2   1 
ATOM   5210 C  CD1   . ILE   D 2 159 ? 17.09401  41.42716  9.10084   1.000 26.78233  ? 158 ILE   D CD1   1 
ATOM   5211 N  N     . ALA   D 2 160 ? 12.05446  44.41638  11.06433  1.000 31.71055  ? 159 ALA   D N     1 
ATOM   5212 C  CA    . ALA   D 2 160 ? 10.84622  45.15459  10.70355  1.000 36.44534  ? 159 ALA   D CA    1 
ATOM   5213 C  C     . ALA   D 2 160 ? 11.14041  46.25077  9.68645   1.000 33.78406  ? 159 ALA   D C     1 
ATOM   5214 O  O     . ALA   D 2 160 ? 10.28026  46.57892  8.85952   1.000 34.62462  ? 159 ALA   D O     1 
ATOM   5215 C  CB    . ALA   D 2 160 ? 10.19573  45.74445  11.95717  1.000 31.11274  ? 159 ALA   D CB    1 
ATOM   5216 N  N     . ASP   D 2 161 ? 12.33171  46.83612  9.74280   1.000 31.89323  ? 160 ASP   D N     1 
ATOM   5217 C  CA    . ASP   D 2 161 ? 12.75145  47.83507  8.76877   1.000 39.04229  ? 160 ASP   D CA    1 
ATOM   5218 C  C     . ASP   D 2 161 ? 14.27125  47.80327  8.68544   1.000 32.92648  ? 160 ASP   D C     1 
ATOM   5219 O  O     . ASP   D 2 161 ? 14.94667  47.41462  9.64292   1.000 32.97134  ? 160 ASP   D O     1 
ATOM   5220 C  CB    . ASP   D 2 161 ? 12.26151  49.23602  9.15828   1.000 36.59732  ? 160 ASP   D CB    1 
ATOM   5221 C  CG    . ASP   D 2 161 ? 12.28761  50.21704  7.99728   1.000 39.15982  ? 160 ASP   D CG    1 
ATOM   5222 O  OD1   . ASP   D 2 161 ? 12.33879  49.77160  6.83236   1.000 37.40151  ? 160 ASP   D OD1   1 
ATOM   5223 O  OD2   . ASP   D 2 161 ? 12.27108  51.43693  8.26363   1.000 36.77431  ? 160 ASP   D OD2   1 
ATOM   5224 N  N     . CYS   D 2 162 ? 14.80125  48.22028  7.53712   1.000 32.33167  ? 161 CYS   D N     1 
ATOM   5225 C  CA    . CYS   D 2 162 ? 16.24593  48.29201  7.36431   1.000 36.64589  ? 161 CYS   D CA    1 
ATOM   5226 C  C     . CYS   D 2 162 ? 16.55248  49.26899  6.24075   1.000 35.52991  ? 161 CYS   D C     1 
ATOM   5227 O  O     . CYS   D 2 162 ? 15.72506  49.50772  5.35499   1.000 34.29663  ? 161 CYS   D O     1 
ATOM   5228 C  CB    . CYS   D 2 162 ? 16.85948  46.91357  7.06936   1.000 28.55227  ? 161 CYS   D CB    1 
ATOM   5229 S  SG    . CYS   D 2 162 ? 16.04352  45.94296  5.78306   1.000 31.38838  ? 161 CYS   D SG    1 
ATOM   5230 N  N     . GLY   D 2 163 ? 17.74763  49.83689  6.29535   1.000 37.60783  ? 162 GLY   D N     1 
ATOM   5231 C  CA    . GLY   D 2 163 ? 18.19174  50.70508  5.22016   1.000 36.19387  ? 162 GLY   D CA    1 
ATOM   5232 C  C     . GLY   D 2 163 ? 19.60460  51.17737  5.47037   1.000 37.77760  ? 162 GLY   D C     1 
ATOM   5233 O  O     . GLY   D 2 163 ? 20.30720  50.68299  6.35718   1.000 33.21780  ? 162 GLY   D O     1 
ATOM   5234 N  N     . GLN   D 2 164 ? 20.01561  52.15090  4.66486   1.000 37.46453  ? 163 GLN   D N     1 
ATOM   5235 C  CA    . GLN   D 2 164 ? 21.33198  52.75504  4.79150   1.000 38.00847  ? 163 GLN   D CA    1 
ATOM   5236 C  C     . GLN   D 2 164 ? 21.21573  54.08762  5.51662   1.000 38.88752  ? 163 GLN   D C     1 
ATOM   5237 O  O     . GLN   D 2 164 ? 20.24045  54.82052  5.33070   1.000 42.84138  ? 163 GLN   D O     1 
ATOM   5238 C  CB    . GLN   D 2 164 ? 21.97332  52.95112  3.41566   1.000 35.54104  ? 163 GLN   D CB    1 
ATOM   5239 C  CG    . GLN   D 2 164 ? 23.37365  53.49212  3.48710   1.000 38.71658  ? 163 GLN   D CG    1 
ATOM   5240 C  CD    . GLN   D 2 164 ? 24.09635  53.39219  2.16246   1.000 37.57704  ? 163 GLN   D CD    1 
ATOM   5241 O  OE1   . GLN   D 2 164 ? 23.53679  52.92475  1.16554   1.000 38.92193  ? 163 GLN   D OE1   1 
ATOM   5242 N  NE2   . GLN   D 2 164 ? 25.35474  53.81369  2.14904   1.000 43.29020  ? 163 GLN   D NE2   1 
ATOM   5243 N  N     . LEU   D 2 165 ? 22.20232  54.38413  6.35585   1.000 41.00414  ? 164 LEU   D N     1 
ATOM   5244 C  CA    . LEU   D 2 165 ? 22.24564  55.63366  7.11585   1.000 43.18884  ? 164 LEU   D CA    1 
ATOM   5245 C  C     . LEU   D 2 165 ? 23.09012  56.69014  6.40933   1.000 41.64904  ? 164 LEU   D C     1 
ATOM   5246 O  O     . LEU   D 2 165 ? 24.21501  56.41189  5.99893   1.000 46.10151  ? 164 LEU   D O     1 
ATOM   5247 C  CB    . LEU   D 2 165 ? 22.80090  55.38504  8.51938   1.000 35.83954  ? 164 LEU   D CB    1 
ATOM   5248 C  CG    . LEU   D 2 165 ? 21.87352  54.56558  9.42016   1.000 38.22805  ? 164 LEU   D CG    1 
ATOM   5249 C  CD1   . LEU   D 2 165 ? 22.52351  54.28072  10.76303  1.000 36.80276  ? 164 LEU   D CD1   1 
ATOM   5250 C  CD2   . LEU   D 2 165 ? 20.55674  55.28834  9.60855   1.000 41.51983  ? 164 LEU   D CD2   1 
HETATM 5251 P  PG    . GNP   E 3 .   ? 23.33765  17.57397  7.40487   1.000 26.99047  ? 201 GNP   A PG    1 
HETATM 5252 O  O1G   . GNP   E 3 .   ? 22.22270  17.81769  8.37893   1.000 23.62480  ? 201 GNP   A O1G   1 
HETATM 5253 O  O2G   . GNP   E 3 .   ? 24.29099  16.56663  8.04746   1.000 29.23901  ? 201 GNP   A O2G   1 
HETATM 5254 O  O3G   . GNP   E 3 .   ? 23.99984  18.92528  7.03742   1.000 25.67513  ? 201 GNP   A O3G   1 
HETATM 5255 N  N3B   . GNP   E 3 .   ? 22.72643  16.91308  5.94557   1.000 23.40624  ? 201 GNP   A N3B   1 
HETATM 5256 P  PB    . GNP   E 3 .   ? 21.67921  15.65981  5.98297   1.000 26.19972  ? 201 GNP   A PB    1 
HETATM 5257 O  O1B   . GNP   E 3 .   ? 20.63982  15.75906  7.08173   1.000 24.70591  ? 201 GNP   A O1B   1 
HETATM 5258 O  O2B   . GNP   E 3 .   ? 22.35786  14.33918  5.99632   1.000 19.70267  ? 201 GNP   A O2B   1 
HETATM 5259 O  O3A   . GNP   E 3 .   ? 20.94888  15.73177  4.50002   1.000 22.61936  ? 201 GNP   A O3A   1 
HETATM 5260 P  PA    . GNP   E 3 .   ? 19.48253  16.26534  4.20066   1.000 25.15988  ? 201 GNP   A PA    1 
HETATM 5261 O  O1A   . GNP   E 3 .   ? 19.29813  17.67320  4.56959   1.000 23.09365  ? 201 GNP   A O1A   1 
HETATM 5262 O  O2A   . GNP   E 3 .   ? 18.52074  15.20322  4.71133   1.000 21.63911  ? 201 GNP   A O2A   1 
HETATM 5263 O  "O5'" . GNP   E 3 .   ? 19.49150  16.10912  2.61319   1.000 23.76465  ? 201 GNP   A "O5'" 1 
HETATM 5264 C  "C5'" . GNP   E 3 .   ? 20.49985  16.74770  1.79957   1.000 25.28683  ? 201 GNP   A "C5'" 1 
HETATM 5265 C  "C4'" . GNP   E 3 .   ? 19.90411  16.97428  0.42594   1.000 27.27843  ? 201 GNP   A "C4'" 1 
HETATM 5266 O  "O4'" . GNP   E 3 .   ? 19.65467  15.70490  -0.21504  1.000 27.78619  ? 201 GNP   A "O4'" 1 
HETATM 5267 C  "C3'" . GNP   E 3 .   ? 18.56959  17.71882  0.39976   1.000 31.50970  ? 201 GNP   A "C3'" 1 
HETATM 5268 O  "O3'" . GNP   E 3 .   ? 18.48771  18.50788  -0.78233  1.000 37.87915  ? 201 GNP   A "O3'" 1 
HETATM 5269 C  "C2'" . GNP   E 3 .   ? 17.54671  16.57950  0.37832   1.000 31.94814  ? 201 GNP   A "C2'" 1 
HETATM 5270 O  "O2'" . GNP   E 3 .   ? 16.32044  16.94445  -0.24243  1.000 36.38446  ? 201 GNP   A "O2'" 1 
HETATM 5271 C  "C1'" . GNP   E 3 .   ? 18.26847  15.56024  -0.49779  1.000 25.18721  ? 201 GNP   A "C1'" 1 
HETATM 5272 N  N9    . GNP   E 3 .   ? 17.89247  14.16911  -0.22303  1.000 27.94363  ? 201 GNP   A N9    1 
HETATM 5273 C  C8    . GNP   E 3 .   ? 17.88053  13.53329  1.00561   1.000 20.56244  ? 201 GNP   A C8    1 
HETATM 5274 N  N7    . GNP   E 3 .   ? 17.53779  12.26881  0.92419   1.000 24.64055  ? 201 GNP   A N7    1 
HETATM 5275 C  C5    . GNP   E 3 .   ? 17.28226  12.06702  -0.43949  1.000 24.47404  ? 201 GNP   A C5    1 
HETATM 5276 C  C6    . GNP   E 3 .   ? 16.85447  10.90004  -1.16698  1.000 23.46920  ? 201 GNP   A C6    1 
HETATM 5277 O  O6    . GNP   E 3 .   ? 16.61586  9.78248   -0.72822  1.000 25.33876  ? 201 GNP   A O6    1 
HETATM 5278 N  N1    . GNP   E 3 .   ? 16.72926  11.14855  -2.52417  1.000 27.97743  ? 201 GNP   A N1    1 
HETATM 5279 C  C2    . GNP   E 3 .   ? 16.98103  12.34899  -3.12783  1.000 30.48131  ? 201 GNP   A C2    1 
HETATM 5280 N  N2    . GNP   E 3 .   ? 16.81199  12.40533  -4.45704  1.000 30.98483  ? 201 GNP   A N2    1 
HETATM 5281 N  N3    . GNP   E 3 .   ? 17.37233  13.43641  -2.47251  1.000 27.36773  ? 201 GNP   A N3    1 
HETATM 5282 C  C4    . GNP   E 3 .   ? 17.49771  13.23342  -1.13932  1.000 26.05839  ? 201 GNP   A C4    1 
HETATM 5283 MG MG    . MG    F 4 .   ? 20.43926  17.10389  8.58244   1.000 23.50754  ? 202 MG    A MG    1 
HETATM 5284 P  PG    . GNP   G 3 .   ? 7.12196   22.00889  39.43302  1.000 35.41184  ? 201 GNP   B PG    1 
HETATM 5285 O  O1G   . GNP   G 3 .   ? 8.05931   21.07399  40.13876  1.000 35.88999  ? 201 GNP   B O1G   1 
HETATM 5286 O  O2G   . GNP   G 3 .   ? 7.68383   22.39989  38.06617  1.000 36.77215  ? 201 GNP   B O2G   1 
HETATM 5287 O  O3G   . GNP   G 3 .   ? 5.73639   21.36347  39.19471  1.000 33.04917  ? 201 GNP   B O3G   1 
HETATM 5288 N  N3B   . GNP   G 3 .   ? 6.94795   23.39166  40.44825  1.000 33.49683  ? 201 GNP   B N3B   1 
HETATM 5289 P  PB    . GNP   G 3 .   ? 8.18649   24.43597  40.73315  1.000 33.98450  ? 201 GNP   B PB    1 
HETATM 5290 O  O1B   . GNP   G 3 .   ? 8.82864   24.78997  39.40700  1.000 35.31229  ? 201 GNP   B O1B   1 
HETATM 5291 O  O2B   . GNP   G 3 .   ? 9.21002   23.86081  41.66353  1.000 33.20020  ? 201 GNP   B O2B   1 
HETATM 5292 O  O3A   . GNP   G 3 .   ? 7.55060   25.79804  41.37542  1.000 38.97194  ? 201 GNP   B O3A   1 
HETATM 5293 P  PA    . GNP   G 3 .   ? 7.08604   27.09599  40.59192  1.000 42.45575  ? 201 GNP   B PA    1 
HETATM 5294 O  O1A   . GNP   G 3 .   ? 6.10319   26.89312  39.51173  1.000 33.24494  ? 201 GNP   B O1A   1 
HETATM 5295 O  O2A   . GNP   G 3 .   ? 8.35319   27.87468  40.24734  1.000 37.08750  ? 201 GNP   B O2A   1 
HETATM 5296 O  "O5'" . GNP   G 3 .   ? 6.40883   27.88770  41.77461  1.000 43.74368  ? 201 GNP   B "O5'" 1 
HETATM 5297 C  "C5'" . GNP   G 3 .   ? 5.27824   27.34461  42.48718  1.000 47.43705  ? 201 GNP   B "C5'" 1 
HETATM 5298 C  "C4'" . GNP   G 3 .   ? 4.43807   28.48313  43.01453  1.000 53.82848  ? 201 GNP   B "C4'" 1 
HETATM 5299 O  "O4'" . GNP   G 3 .   ? 5.18008   29.22781  44.00824  1.000 50.23119  ? 201 GNP   B "O4'" 1 
HETATM 5300 C  "C3'" . GNP   G 3 .   ? 3.97269   29.50521  41.97997  1.000 52.33933  ? 201 GNP   B "C3'" 1 
HETATM 5301 O  "O3'" . GNP   G 3 .   ? 2.67274   29.96111  42.32560  1.000 58.60849  ? 201 GNP   B "O3'" 1 
HETATM 5302 C  "C2'" . GNP   G 3 .   ? 5.01392   30.61934  42.11073  1.000 50.11405  ? 201 GNP   B "C2'" 1 
HETATM 5303 O  "O2'" . GNP   G 3 .   ? 4.48657   31.89131  41.76147  1.000 61.49843  ? 201 GNP   B "O2'" 1 
HETATM 5304 C  "C1'" . GNP   G 3 .   ? 5.30716   30.58124  43.60888  1.000 54.50692  ? 201 GNP   B "C1'" 1 
HETATM 5305 N  N9    . GNP   G 3 .   ? 6.66171   31.03385  43.96034  1.000 56.37399  ? 201 GNP   B N9    1 
HETATM 5306 C  C8    . GNP   G 3 .   ? 7.84012   30.61964  43.39749  1.000 52.54142  ? 201 GNP   B C8    1 
HETATM 5307 N  N7    . GNP   G 3 .   ? 8.89911   31.18438  43.93380  1.000 49.90541  ? 201 GNP   B N7    1 
HETATM 5308 C  C5    . GNP   G 3 .   ? 8.37934   32.02214  44.90756  1.000 55.73784  ? 201 GNP   B C5    1 
HETATM 5309 C  C6    . GNP   G 3 .   ? 9.03142   32.91289  45.84099  1.000 55.78362  ? 201 GNP   B C6    1 
HETATM 5310 O  O6    . GNP   G 3 .   ? 10.23240  33.11280  45.95566  1.000 54.93175  ? 201 GNP   B O6    1 
HETATM 5311 N  N1    . GNP   G 3 .   ? 8.12738   33.56150  46.65536  1.000 59.62424  ? 201 GNP   B N1    1 
HETATM 5312 C  C2    . GNP   G 3 .   ? 6.76805   33.40747  46.60620  1.000 59.43561  ? 201 GNP   B C2    1 
HETATM 5313 N  N2    . GNP   G 3 .   ? 6.04910   34.12277  47.47372  1.000 63.16307  ? 201 GNP   B N2    1 
HETATM 5314 N  N3    . GNP   G 3 .   ? 6.15058   32.59126  45.74939  1.000 54.15008  ? 201 GNP   B N3    1 
HETATM 5315 C  C4    . GNP   G 3 .   ? 7.00540   31.93568  44.94257  1.000 58.36492  ? 201 GNP   B C4    1 
HETATM 5316 MG MG    . MG    H 4 .   ? 8.58487   23.96075  37.51734  1.000 32.03995  ? 202 MG    B MG    1 
HETATM 5317 C  C1    . A1AHB I 5 .   ? 9.57768   12.65555  34.53187  1.000 27.89918  ? 201 A1AHB C C1    1 
HETATM 5318 C  C10   . A1AHB I 5 .   ? 3.60583   17.66176  35.45582  1.000 29.72777  ? 201 A1AHB C C10   1 
HETATM 5319 C  C11   . A1AHB I 5 .   ? 1.39671   16.68774  35.49222  1.000 26.71029  ? 201 A1AHB C C11   1 
HETATM 5320 C  C12   . A1AHB I 5 .   ? -0.05496  16.41087  35.64668  1.000 25.22124  ? 201 A1AHB C C12   1 
HETATM 5321 C  C13   . A1AHB I 5 .   ? -0.85437  17.27411  34.65965  1.000 27.21750  ? 201 A1AHB C C13   1 
HETATM 5322 C  C14   . A1AHB I 5 .   ? -1.51071  19.62660  34.54498  1.000 35.04598  ? 201 A1AHB C C14   1 
HETATM 5323 C  C15   . A1AHB I 5 .   ? -2.27814  20.67743  35.22740  1.000 30.47224  ? 201 A1AHB C C15   1 
HETATM 5324 C  C16   . A1AHB I 5 .   ? -2.08444  22.10091  34.77371  1.000 32.78632  ? 201 A1AHB C C16   1 
HETATM 5325 C  C17   . A1AHB I 5 .   ? -3.34267  21.39391  34.41366  1.000 30.32347  ? 201 A1AHB C C17   1 
HETATM 5326 C  C18   . A1AHB I 5 .   ? -4.66818  21.76944  35.02902  1.000 35.64733  ? 201 A1AHB C C18   1 
HETATM 5327 C  C19   . A1AHB I 5 .   ? -2.00423  16.45587  34.11730  1.000 28.93659  ? 201 A1AHB C C19   1 
HETATM 5328 C  C2    . A1AHB I 5 .   ? 9.11312   13.21655  33.21041  1.000 25.50822  ? 201 A1AHB C C2    1 
HETATM 5329 C  C20   . A1AHB I 5 .   ? -2.75938  14.80894  32.35987  1.000 23.80686  ? 201 A1AHB C C20   1 
HETATM 5330 C  C21   . A1AHB I 5 .   ? -2.19705  13.40272  32.38209  1.000 24.61630  ? 201 A1AHB C C21   1 
HETATM 5331 C  C22   . A1AHB I 5 .   ? -0.81192  13.39128  31.75071  1.000 21.10389  ? 201 A1AHB C C22   1 
HETATM 5332 C  C23   . A1AHB I 5 .   ? 0.12260   14.41033  32.41541  1.000 21.49909  ? 201 A1AHB C C23   1 
HETATM 5333 C  C24   . A1AHB I 5 .   ? 1.38462   14.51770  31.60788  1.000 20.50173  ? 201 A1AHB C C24   1 
HETATM 5334 C  C25   . A1AHB I 5 .   ? 3.25796   13.26788  30.82221  1.000 21.87850  ? 201 A1AHB C C25   1 
HETATM 5335 C  C26   . A1AHB I 5 .   ? 3.77273   11.83206  30.89833  1.000 20.02388  ? 201 A1AHB C C26   1 
HETATM 5336 C  C27   . A1AHB I 5 .   ? 2.60351   10.87038  30.66231  1.000 20.46643  ? 201 A1AHB C C27   1 
HETATM 5337 C  C28   . A1AHB I 5 .   ? 4.79390   11.60906  29.77633  1.000 24.86059  ? 201 A1AHB C C28   1 
HETATM 5338 C  C29   . A1AHB I 5 .   ? 4.40545   11.50806  32.27250  1.000 20.56182  ? 201 A1AHB C C29   1 
HETATM 5339 C  C3    . A1AHB I 5 .   ? 6.78531   14.03033  33.66570  1.000 25.09608  ? 201 A1AHB C C3    1 
HETATM 5340 C  C30   . A1AHB I 5 .   ? 5.56272   12.35568  32.71650  1.000 23.04822  ? 201 A1AHB C C30   1 
HETATM 5341 C  C31   . A1AHB I 5 .   ? 6.91664   12.09360  32.51975  1.000 23.10845  ? 201 A1AHB C C31   1 
HETATM 5342 C  C32   . A1AHB I 5 .   ? 7.46402   10.89027  31.88115  1.000 24.49235  ? 201 A1AHB C C32   1 
HETATM 5343 C  C33   . A1AHB I 5 .   ? 8.24479   10.92508  30.69677  1.000 25.22060  ? 201 A1AHB C C33   1 
HETATM 5344 C  C34   . A1AHB I 5 .   ? 8.42675   8.60950   30.69965  1.000 27.12153  ? 201 A1AHB C C34   1 
HETATM 5345 C  C35   . A1AHB I 5 .   ? 7.66033   8.49290   31.84975  1.000 29.40132  ? 201 A1AHB C C35   1 
HETATM 5346 C  C36   . A1AHB I 5 .   ? 7.17608   9.65060   32.44261  1.000 22.90743  ? 201 A1AHB C C36   1 
HETATM 5347 C  C37   . A1AHB I 5 .   ? 6.20253   7.09317   33.24594  1.000 32.57439  ? 201 A1AHB C C37   1 
HETATM 5348 C  C38   . A1AHB I 5 .   ? 6.06091   5.73137   33.88409  1.000 37.38044  ? 201 A1AHB C C38   1 
HETATM 5349 C  C39   . A1AHB I 5 .   ? 6.07194   3.36838   33.51537  1.000 39.02066  ? 201 A1AHB C C39   1 
HETATM 5350 C  C4    . A1AHB I 5 .   ? 5.46981   13.58777  33.43473  1.000 21.16761  ? 201 A1AHB C C4    1 
HETATM 5351 C  C40   . A1AHB I 5 .   ? 7.77018   4.78395   32.60835  1.000 38.94739  ? 201 A1AHB C C40   1 
HETATM 5352 C  C41   . A1AHB I 5 .   ? 8.06063   6.05320   31.84489  1.000 30.75798  ? 201 A1AHB C C41   1 
HETATM 5353 C  C42   . A1AHB I 5 .   ? 8.59697   12.21379  29.98231  1.000 22.38122  ? 201 A1AHB C C42   1 
HETATM 5354 C  C43   . A1AHB I 5 .   ? 8.25828   12.14467  28.50535  1.000 24.42069  ? 201 A1AHB C C43   1 
HETATM 5355 C  C44   . A1AHB I 5 .   ? 10.35648  13.80570  29.96059  1.000 27.96561  ? 201 A1AHB C C44   1 
HETATM 5356 C  C5    . A1AHB I 5 .   ? 4.39452   14.34499  33.90243  1.000 23.57355  ? 201 A1AHB C C5    1 
HETATM 5357 C  C6    . A1AHB I 5 .   ? 4.64951   15.53116  34.58605  1.000 26.06086  ? 201 A1AHB C C6    1 
HETATM 5358 C  C7    . A1AHB I 5 .   ? 5.96421   15.94441  34.79185  1.000 28.86583  ? 201 A1AHB C C7    1 
HETATM 5359 C  C8    . A1AHB I 5 .   ? 7.04787   15.21407  34.34758  1.000 33.34995  ? 201 A1AHB C C8    1 
HETATM 5360 C  C9    . A1AHB I 5 .   ? 3.54074   16.36908  35.05666  1.000 28.55240  ? 201 A1AHB C C9    1 
HETATM 5361 N  N1    . A1AHB I 5 .   ? 7.65861   13.11243  33.10559  1.000 23.60255  ? 201 A1AHB C N1    1 
HETATM 5362 N  N2    . A1AHB I 5 .   ? -1.32340  18.51129  35.26292  1.000 28.47148  ? 201 A1AHB C N2    1 
HETATM 5363 N  N3    . A1AHB I 5 .   ? -1.76976  15.69139  32.98479  1.000 26.76597  ? 201 A1AHB C N3    1 
HETATM 5364 N  N4    . A1AHB I 5 .   ? -0.48597  15.73755  32.39574  1.000 23.31768  ? 201 A1AHB C N4    1 
HETATM 5365 N  N5    . A1AHB I 5 .   ? 8.70651   9.79635   30.14069  1.000 24.93568  ? 201 A1AHB C N5    1 
HETATM 5366 N  N6    . A1AHB I 5 .   ? 7.35728   7.24423   32.34511  1.000 26.33395  ? 201 A1AHB C N6    1 
HETATM 5367 N  N7    . A1AHB I 5 .   ? 6.35370   4.67523   32.92544  1.000 37.31352  ? 201 A1AHB C N7    1 
HETATM 5368 N  N8    . A1AHB I 5 .   ? 2.27236   15.79347  35.12106  1.000 23.67206  ? 201 A1AHB C N8    1 
HETATM 5369 O  O1    . A1AHB I 5 .   ? -1.11054  19.75618  33.38691  1.000 31.64253  ? 201 A1AHB C O1    1 
HETATM 5370 O  O2    . A1AHB I 5 .   ? -3.10565  16.45625  34.65093  1.000 25.58161  ? 201 A1AHB C O2    1 
HETATM 5371 O  O3    . A1AHB I 5 .   ? 1.64794   15.46700  30.91616  1.000 23.16195  ? 201 A1AHB C O3    1 
HETATM 5372 O  O4    . A1AHB I 5 .   ? 2.12043   13.41243  31.72544  1.000 22.73049  ? 201 A1AHB C O4    1 
HETATM 5373 O  O5    . A1AHB I 5 .   ? 10.00161  12.43383  30.08991  1.000 25.73883  ? 201 A1AHB C O5    1 
HETATM 5374 S  S1    . A1AHB I 5 .   ? 2.04027   18.26266  35.78622  1.000 30.33125  ? 201 A1AHB C S1    1 
HETATM 5375 C  C1    . A1AHB J 5 .   ? 28.34452  20.20790  16.95137  1.000 26.85218  ? 201 A1AHB D C1    1 
HETATM 5376 C  C10   . A1AHB J 5 .   ? 25.55583  23.21022  10.32895  1.000 24.59352  ? 201 A1AHB D C10   1 
HETATM 5377 C  C11   . A1AHB J 5 .   ? 26.62294  25.24674  9.56304   1.000 21.56415  ? 201 A1AHB D C11   1 
HETATM 5378 C  C12   . A1AHB J 5 .   ? 27.10832  26.45013  8.81598   1.000 21.44022  ? 201 A1AHB D C12   1 
HETATM 5379 C  C13   . A1AHB J 5 .   ? 25.95125  27.41281  8.50762   1.000 20.31306  ? 201 A1AHB D C13   1 
HETATM 5380 C  C14   . A1AHB J 5 .   ? 24.05186  27.45650  6.97524   1.000 21.04110  ? 201 A1AHB D C14   1 
HETATM 5381 C  C15   . A1AHB J 5 .   ? 23.66602  27.52515  5.55237   1.000 21.23158  ? 201 A1AHB D C15   1 
HETATM 5382 C  C16   . A1AHB J 5 .   ? 22.19510  27.49546  5.24296   1.000 23.20883  ? 201 A1AHB D C16   1 
HETATM 5383 C  C17   . A1AHB J 5 .   ? 22.93497  28.76905  5.06583   1.000 24.25082  ? 201 A1AHB D C17   1 
HETATM 5384 C  C18   . A1AHB J 5 .   ? 23.18978  29.33420  3.68510   1.000 27.48107  ? 201 A1AHB D C18   1 
HETATM 5385 C  C19   . A1AHB J 5 .   ? 26.45086  28.84360  8.61048   1.000 19.39489  ? 201 A1AHB D C19   1 
HETATM 5386 C  C2    . A1AHB J 5 .   ? 27.25274  21.18815  17.27197  1.000 24.35528  ? 201 A1AHB D C2    1 
HETATM 5387 C  C20   . A1AHB J 5 .   ? 27.05838  30.73895  10.14152  1.000 19.54104  ? 201 A1AHB D C20   1 
HETATM 5388 C  C21   . A1AHB J 5 .   ? 28.19454  30.49026  11.11310  1.000 19.98137  ? 201 A1AHB D C21   1 
HETATM 5389 C  C22   . A1AHB J 5 .   ? 27.64541  29.77071  12.34125  1.000 20.64058  ? 201 A1AHB D C22   1 
HETATM 5390 C  C23   . A1AHB J 5 .   ? 26.88909  28.48786  11.95916  1.000 17.29578  ? 201 A1AHB D C23   1 
HETATM 5391 C  C24   . A1AHB J 5 .   ? 26.22623  27.89103  13.17512  1.000 19.71132  ? 201 A1AHB D C24   1 
HETATM 5392 C  C25   . A1AHB J 5 .   ? 26.55019  27.08478  15.36498  1.000 19.57561  ? 201 A1AHB D C25   1 
HETATM 5393 C  C26   . A1AHB J 5 .   ? 27.71312  27.01560  16.35030  1.000 18.72148  ? 201 A1AHB D C26   1 
HETATM 5394 C  C27   . A1AHB J 5 .   ? 28.50009  28.32705  16.31712  1.000 20.14294  ? 201 A1AHB D C27   1 
HETATM 5395 C  C28   . A1AHB J 5 .   ? 27.16328  26.81183  17.76514  1.000 20.50322  ? 201 A1AHB D C28   1 
HETATM 5396 C  C29   . A1AHB J 5 .   ? 28.69625  25.89766  15.97214  1.000 19.12933  ? 201 A1AHB D C29   1 
HETATM 5397 C  C3    . A1AHB J 5 .   ? 27.15579  22.57677  15.19822  1.000 23.16339  ? 201 A1AHB D C3    1 
HETATM 5398 C  C30   . A1AHB J 5 .   ? 28.11111  24.51401  15.93762  1.000 21.78515  ? 201 A1AHB D C30   1 
HETATM 5399 C  C31   . A1AHB J 5 .   ? 28.05486  23.60023  16.98895  1.000 20.90872  ? 201 A1AHB D C31   1 
HETATM 5400 C  C32   . A1AHB J 5 .   ? 28.59328  23.77729  18.34095  1.000 23.77830  ? 201 A1AHB D C32   1 
HETATM 5401 C  C33   . A1AHB J 5 .   ? 27.77871  23.79097  19.49720  1.000 21.87444  ? 201 A1AHB D C33   1 
HETATM 5402 C  C34   . A1AHB J 5 .   ? 29.63985  24.14097  20.83697  1.000 26.25502  ? 201 A1AHB D C34   1 
HETATM 5403 C  C35   . A1AHB J 5 .   ? 30.49948  24.15182  19.74867  1.000 23.48700  ? 201 A1AHB D C35   1 
HETATM 5404 C  C36   . A1AHB J 5 .   ? 29.96736  23.95341  18.48453  1.000 24.75013  ? 201 A1AHB D C36   1 
HETATM 5405 C  C37   . A1AHB J 5 .   ? 32.76105  24.46732  18.77552  1.000 26.19263  ? 201 A1AHB D C37   1 
HETATM 5406 C  C38   . A1AHB J 5 .   ? 33.96588  25.32540  19.08096  1.000 28.06230  ? 201 A1AHB D C38   1 
HETATM 5407 C  C39   . A1AHB J 5 .   ? 35.89767  25.56398  20.48350  1.000 37.61133  ? 201 A1AHB D C39   1 
HETATM 5408 C  C4    . A1AHB J 5 .   ? 27.53520  23.87199  14.79910  1.000 19.03847  ? 201 A1AHB D C4    1 
HETATM 5409 C  C40   . A1AHB J 5 .   ? 33.74187  24.99894  21.40260  1.000 28.26230  ? 201 A1AHB D C40   1 
HETATM 5410 C  C41   . A1AHB J 5 .   ? 32.50389  24.14478  21.23925  1.000 29.15714  ? 201 A1AHB D C41   1 
HETATM 5411 C  C42   . A1AHB J 5 .   ? 26.26958  23.61956  19.45165  1.000 21.07803  ? 201 A1AHB D C42   1 
HETATM 5412 C  C43   . A1AHB J 5 .   ? 25.61838  24.68767  20.30332  1.000 20.76069  ? 201 A1AHB D C43   1 
HETATM 5413 C  C44   . A1AHB J 5 .   ? 24.59583  21.97598  19.86965  1.000 25.90967  ? 201 A1AHB D C44   1 
HETATM 5414 C  C5    . A1AHB J 5 .   ? 27.28983  24.27440  13.48057  1.000 18.54347  ? 201 A1AHB D C5    1 
HETATM 5415 C  C6    . A1AHB J 5 .   ? 26.68430  23.38258  12.60226  1.000 22.33608  ? 201 A1AHB D C6    1 
HETATM 5416 C  C7    . A1AHB J 5 .   ? 26.31545  22.11208  13.04080  1.000 20.10509  ? 201 A1AHB D C7    1 
HETATM 5417 C  C8    . A1AHB J 5 .   ? 26.52991  21.68512  14.33314  1.000 24.01542  ? 201 A1AHB D C8    1 
HETATM 5418 C  C9    . A1AHB J 5 .   ? 26.39810  23.79354  11.21435  1.000 23.09897  ? 201 A1AHB D C9    1 
HETATM 5419 N  N1    . A1AHB J 5 .   ? 27.46648  22.43166  16.53633  1.000 24.35597  ? 201 A1AHB D N1    1 
HETATM 5420 N  N2    . A1AHB J 5 .   ? 25.32904  27.12723  7.22679   1.000 21.03217  ? 201 A1AHB D N2    1 
HETATM 5421 N  N3    . A1AHB J 5 .   ? 26.44881  29.43183  9.84793   1.000 21.11019  ? 201 A1AHB D N3    1 
HETATM 5422 N  N4    . A1AHB J 5 .   ? 25.86050  28.74920  10.93773  1.000 19.46519  ? 201 A1AHB D N4    1 
HETATM 5423 N  N5    . A1AHB J 5 .   ? 28.31166  23.96935  20.71317  1.000 24.91854  ? 201 A1AHB D N5    1 
HETATM 5424 N  N6    . A1AHB J 5 .   ? 31.86328  24.30785  19.92518  1.000 27.91357  ? 201 A1AHB D N6    1 
HETATM 5425 N  N7    . A1AHB J 5 .   ? 34.64903  24.83098  20.27139  1.000 29.67522  ? 201 A1AHB D N7    1 
HETATM 5426 N  N8    . A1AHB J 5 .   ? 27.06577  24.91903  10.74207  1.000 19.69310  ? 201 A1AHB D N8    1 
HETATM 5427 O  O1    . A1AHB J 5 .   ? 23.26016  27.76151  7.86233   1.000 21.50997  ? 201 A1AHB D O1    1 
HETATM 5428 O  O2    . A1AHB J 5 .   ? 26.89704  29.44771  7.64211   1.000 21.45568  ? 201 A1AHB D O2    1 
HETATM 5429 O  O3    . A1AHB J 5 .   ? 25.03339  27.74738  13.29956  1.000 20.59634  ? 201 A1AHB D O3    1 
HETATM 5430 O  O4    . A1AHB J 5 .   ? 27.12215  27.54939  14.10783  1.000 19.99596  ? 201 A1AHB D O4    1 
HETATM 5431 O  O5    . A1AHB J 5 .   ? 25.95873  22.34458  20.01378  1.000 24.98003  ? 201 A1AHB D O5    1 
HETATM 5432 S  S1    . A1AHB J 5 .   ? 25.39556  24.19803  8.94251   1.000 25.39622  ? 201 A1AHB D S1    1 
HETATM 5433 O  O     A HOH   K 6 .   ? 16.97558  12.15363  20.80413  0.500 30.63230  ? 301 HOH   A O     1 
HETATM 5434 O  O     B HOH   K 6 .   ? 17.75593  13.37675  22.25074  0.500 32.58807  ? 301 HOH   A O     1 
HETATM 5435 O  O     . HOH   K 6 .   ? 10.32829  9.22716   27.91552  1.000 33.07778  ? 302 HOH   A O     1 
HETATM 5436 O  O     . HOH   K 6 .   ? 16.07923  11.41799  24.82311  1.000 41.97747  ? 303 HOH   A O     1 
HETATM 5437 O  O     . HOH   K 6 .   ? 11.05769  -7.83194  21.87683  1.000 48.69230  ? 304 HOH   A O     1 
HETATM 5438 O  O     . HOH   K 6 .   ? 32.90616  25.20355  6.78392   1.000 45.57230  ? 305 HOH   A O     1 
HETATM 5439 O  O     . HOH   K 6 .   ? 25.51947  16.80636  20.81550  1.000 45.64650  ? 306 HOH   A O     1 
HETATM 5440 O  O     . HOH   K 6 .   ? 15.84044  17.45477  11.53691  1.000 29.50391  ? 307 HOH   A O     1 
HETATM 5441 O  O     . HOH   K 6 .   ? 28.15636  -3.56840  15.52270  1.000 45.73981  ? 308 HOH   A O     1 
HETATM 5442 O  O     . HOH   K 6 .   ? 37.48419  2.03613   16.72063  1.000 47.21394  ? 309 HOH   A O     1 
HETATM 5443 O  O     . HOH   K 6 .   ? 7.81489   -2.01842  24.42163  1.000 39.02129  ? 310 HOH   A O     1 
HETATM 5444 O  O     . HOH   K 6 .   ? 28.31525  14.80059  21.52928  1.000 33.21887  ? 311 HOH   A O     1 
HETATM 5445 O  O     . HOH   K 6 .   ? 19.54368  18.59675  7.21466   1.000 25.62578  ? 312 HOH   A O     1 
HETATM 5446 O  O     . HOH   K 6 .   ? 27.65463  17.42683  19.57365  1.000 40.30175  ? 313 HOH   A O     1 
HETATM 5447 O  O     . HOH   K 6 .   ? 11.39052  -4.35754  25.30030  1.000 52.97687  ? 314 HOH   A O     1 
HETATM 5448 O  O     . HOH   K 6 .   ? 27.89554  14.65020  14.62446  1.000 33.30640  ? 315 HOH   A O     1 
HETATM 5449 O  O     . HOH   K 6 .   ? 21.45389  6.05833   26.96563  1.000 49.78454  ? 316 HOH   A O     1 
HETATM 5450 O  O     . HOH   K 6 .   ? 27.54606  13.76646  1.14213   1.000 43.70335  ? 317 HOH   A O     1 
HETATM 5451 O  O     . HOH   K 6 .   ? 15.08709  -0.92483  0.19349   1.000 41.27454  ? 318 HOH   A O     1 
HETATM 5452 O  O     . HOH   K 6 .   ? 14.16564  7.60218   25.55642  1.000 38.22469  ? 319 HOH   A O     1 
HETATM 5453 O  O     . HOH   K 6 .   ? 33.38158  14.90781  22.04761  1.000 41.70102  ? 320 HOH   A O     1 
HETATM 5454 O  O     . HOH   K 6 .   ? 7.00563   3.84484   11.09670  1.000 37.22503  ? 321 HOH   A O     1 
HETATM 5455 O  O     . HOH   K 6 .   ? 12.29091  19.47577  12.16018  1.000 45.63082  ? 322 HOH   A O     1 
HETATM 5456 O  O     . HOH   K 6 .   ? 33.91534  13.40057  19.09591  1.000 35.66330  ? 323 HOH   A O     1 
HETATM 5457 O  O     . HOH   K 6 .   ? 21.15223  15.75704  10.05517  1.000 19.71005  ? 324 HOH   A O     1 
HETATM 5458 O  O     . HOH   K 6 .   ? 38.00820  2.73543   22.99890  1.000 46.69586  ? 325 HOH   A O     1 
HETATM 5459 O  O     . HOH   K 6 .   ? 35.07219  0.24405   10.67987  1.000 49.16299  ? 326 HOH   A O     1 
HETATM 5460 O  O     . HOH   K 6 .   ? 30.63229  14.26984  9.00627   1.000 35.46769  ? 327 HOH   A O     1 
HETATM 5461 O  O     . HOH   K 6 .   ? 14.10095  10.81523  -7.92257  1.000 44.53285  ? 328 HOH   A O     1 
HETATM 5462 O  O     . HOH   K 6 .   ? 4.67677   3.78183   8.43956   1.000 41.72208  ? 329 HOH   A O     1 
HETATM 5463 O  O     . HOH   K 6 .   ? 12.01970  14.04627  4.28428   1.000 27.29392  ? 330 HOH   A O     1 
HETATM 5464 O  O     . HOH   K 6 .   ? 16.20663  -13.44847 23.36342  1.000 61.13894  ? 331 HOH   A O     1 
HETATM 5465 O  O     . HOH   K 6 .   ? 12.69905  4.26160   -4.72339  1.000 33.49498  ? 332 HOH   A O     1 
HETATM 5466 O  O     . HOH   K 6 .   ? 33.13536  -2.55992  -0.05044  1.000 48.33282  ? 333 HOH   A O     1 
HETATM 5467 O  O     . HOH   K 6 .   ? 29.59036  26.17203  11.44671  1.000 21.48784  ? 334 HOH   A O     1 
HETATM 5468 O  O     . HOH   K 6 .   ? 19.33576  10.34076  27.21786  1.000 48.32998  ? 335 HOH   A O     1 
HETATM 5469 O  O     . HOH   K 6 .   ? 28.80085  -5.70574  14.50193  1.000 47.56437  ? 336 HOH   A O     1 
HETATM 5470 O  O     . HOH   K 6 .   ? 22.98880  19.72982  4.39514   1.000 40.97765  ? 337 HOH   A O     1 
HETATM 5471 O  O     . HOH   K 6 .   ? 29.80979  16.21909  12.31758  1.000 29.84934  ? 338 HOH   A O     1 
HETATM 5472 O  O     . HOH   K 6 .   ? 15.19688  16.96843  2.76249   1.000 38.04087  ? 339 HOH   A O     1 
HETATM 5473 O  O     . HOH   K 6 .   ? 35.96149  19.28009  15.72377  1.000 33.34928  ? 340 HOH   A O     1 
HETATM 5474 O  O     . HOH   K 6 .   ? 10.66089  16.72299  18.67046  1.000 34.48882  ? 341 HOH   A O     1 
HETATM 5475 O  O     . HOH   K 6 .   ? 9.52709   2.37519   29.08777  1.000 46.32230  ? 342 HOH   A O     1 
HETATM 5476 O  O     A HOH   K 6 .   ? 13.99440  19.48561  16.95193  0.500 35.13230  ? 343 HOH   A O     1 
HETATM 5477 O  O     B HOH   K 6 .   ? 15.09747  18.91702  18.74482  0.500 35.13230  ? 343 HOH   A O     1 
HETATM 5478 O  O     . HOH   K 6 .   ? 13.63957  22.06221  6.34354   1.000 46.52230  ? 344 HOH   A O     1 
HETATM 5479 O  O     . HOH   K 6 .   ? 22.27594  13.93925  -5.06625  1.000 42.85602  ? 345 HOH   A O     1 
HETATM 5480 O  O     . HOH   K 6 .   ? 14.36527  -4.36116  24.00697  1.000 45.29256  ? 346 HOH   A O     1 
HETATM 5481 O  O     . HOH   K 6 .   ? 6.18998   -0.17077  7.52627   1.000 51.17099  ? 347 HOH   A O     1 
HETATM 5482 O  O     . HOH   K 6 .   ? 4.45751   1.03090   13.39372  1.000 34.84472  ? 348 HOH   A O     1 
HETATM 5483 O  O     . HOH   K 6 .   ? 26.51131  19.65392  6.26538   1.000 38.60502  ? 349 HOH   A O     1 
HETATM 5484 O  O     . HOH   K 6 .   ? 37.51675  5.47644   5.14205   1.000 54.15212  ? 350 HOH   A O     1 
HETATM 5485 O  O     . HOH   K 6 .   ? 0.10832   2.55364   22.06574  1.000 34.28976  ? 351 HOH   A O     1 
HETATM 5486 O  O     . HOH   K 6 .   ? 25.64048  -8.20266  6.89058   1.000 45.37202  ? 352 HOH   A O     1 
HETATM 5487 O  O     . HOH   K 6 .   ? 6.91273   14.64350  0.01855   1.000 48.59987  ? 353 HOH   A O     1 
HETATM 5488 O  O     . HOH   K 6 .   ? 17.96439  20.22441  10.11066  1.000 36.11554  ? 354 HOH   A O     1 
HETATM 5489 O  O     . HOH   K 6 .   ? 7.22389   6.31697   8.01602   1.000 44.25264  ? 355 HOH   A O     1 
HETATM 5490 O  O     . HOH   K 6 .   ? 28.35001  9.19094   5.45005   1.000 28.79950  ? 356 HOH   A O     1 
HETATM 5491 O  O     . HOH   K 6 .   ? 24.41419  12.95644  -2.54448  1.000 34.87099  ? 357 HOH   A O     1 
HETATM 5492 O  O     . HOH   K 6 .   ? 9.96658   -3.21305  22.14069  1.000 41.04937  ? 358 HOH   A O     1 
HETATM 5493 O  O     . HOH   K 6 .   ? 30.76783  9.72819   -5.94706  1.000 42.45894  ? 359 HOH   A O     1 
HETATM 5494 O  O     . HOH   K 6 .   ? 20.71992  19.96697  3.92720   1.000 34.28968  ? 360 HOH   A O     1 
HETATM 5495 O  O     . HOH   K 6 .   ? 19.10930  21.78465  14.09113  1.000 27.42420  ? 361 HOH   A O     1 
HETATM 5496 O  O     . HOH   K 6 .   ? 24.48381  17.15759  16.13727  1.000 24.84870  ? 362 HOH   A O     1 
HETATM 5497 O  O     . HOH   K 6 .   ? 26.50273  12.72892  11.71182  1.000 23.19141  ? 363 HOH   A O     1 
HETATM 5498 O  O     . HOH   K 6 .   ? 29.48316  17.01545  15.32332  1.000 33.43230  ? 364 HOH   A O     1 
HETATM 5499 O  O     . HOH   K 6 .   ? 9.08488   2.86257   4.20110   1.000 30.06343  ? 365 HOH   A O     1 
HETATM 5500 O  O     . HOH   K 6 .   ? 15.13580  -6.72773  10.23855  1.000 45.31445  ? 366 HOH   A O     1 
HETATM 5501 O  O     . HOH   K 6 .   ? 24.03989  -4.17873  14.40050  1.000 30.97107  ? 367 HOH   A O     1 
HETATM 5502 O  O     . HOH   K 6 .   ? 15.77271  -5.75217  7.28686   1.000 45.83326  ? 368 HOH   A O     1 
HETATM 5503 O  O     . HOH   K 6 .   ? 24.36742  -5.93527  18.38924  1.000 52.40612  ? 369 HOH   A O     1 
HETATM 5504 O  O     . HOH   K 6 .   ? 23.87922  -0.02502  22.80725  1.000 38.70223  ? 370 HOH   A O     1 
HETATM 5505 O  O     . HOH   K 6 .   ? 26.76317  14.27059  -3.68164  1.000 52.71709  ? 371 HOH   A O     1 
HETATM 5506 O  O     . HOH   K 6 .   ? 25.16570  19.61335  9.53683   1.000 25.21156  ? 372 HOH   A O     1 
HETATM 5507 O  O     . HOH   K 6 .   ? 11.09323  -4.17609  8.61814   1.000 48.60820  ? 373 HOH   A O     1 
HETATM 5508 O  O     . HOH   K 6 .   ? 6.29323   3.02149   4.00699   1.000 40.05736  ? 374 HOH   A O     1 
HETATM 5509 O  O     . HOH   K 6 .   ? 3.19129   7.11393   15.17909  1.000 38.24981  ? 375 HOH   A O     1 
HETATM 5510 O  O     . HOH   K 6 .   ? 34.428    -2.403    27.406    1.000 42.54230  ? 376 HOH   A O     1 
HETATM 5511 O  O     . HOH   K 6 .   ? 18.27408  9.14208   20.53365  1.000 26.56944  ? 377 HOH   A O     1 
HETATM 5512 O  O     . HOH   K 6 .   ? 28.54310  19.22603  4.98271   1.000 36.97230  ? 378 HOH   A O     1 
HETATM 5513 O  O     . HOH   K 6 .   ? 3.49511   5.67576   7.05475   1.000 49.20246  ? 379 HOH   A O     1 
HETATM 5514 O  O     . HOH   K 6 .   ? 24.46904  2.25071   24.91006  1.000 46.96713  ? 380 HOH   A O     1 
HETATM 5515 O  O     . HOH   K 6 .   ? 4.22385   -5.80516  13.61994  1.000 50.02636  ? 381 HOH   A O     1 
HETATM 5516 O  O     . HOH   K 6 .   ? 16.80396  19.16134  4.54026   1.000 43.27326  ? 382 HOH   A O     1 
HETATM 5517 O  O     A HOH   K 6 .   ? 7.72267   11.98984  -0.39879  0.500 33.02230  ? 383 HOH   A O     1 
HETATM 5518 O  O     B HOH   K 6 .   ? 6.23316   11.21092  0.92171   0.500 33.02230  ? 383 HOH   A O     1 
HETATM 5519 O  O     . HOH   K 6 .   ? 11.11504  18.88925  -3.32119  1.000 50.53275  ? 384 HOH   A O     1 
HETATM 5520 O  O     . HOH   K 6 .   ? 32.94845  -8.82958  3.70883   1.000 47.97650  ? 385 HOH   A O     1 
HETATM 5521 O  O     . HOH   K 6 .   ? 25.64509  -7.79808  4.04395   1.000 55.09068  ? 386 HOH   A O     1 
HETATM 5522 O  O     . HOH   K 6 .   ? 12.52830  -7.82614  17.16080  1.000 48.79561  ? 387 HOH   A O     1 
HETATM 5523 O  O     . HOH   K 6 .   ? 5.25026   10.41333  13.96594  1.000 42.44308  ? 388 HOH   A O     1 
HETATM 5524 O  O     . HOH   K 6 .   ? 33.90976  3.19324   4.87171   1.000 44.16260  ? 389 HOH   A O     1 
HETATM 5525 O  O     . HOH   K 6 .   ? 30.86079  15.21182  23.36931  1.000 43.25851  ? 390 HOH   A O     1 
HETATM 5526 O  O     . HOH   K 6 .   ? 27.04135  24.26767  5.75497   1.000 31.76246  ? 391 HOH   A O     1 
HETATM 5527 O  O     . HOH   K 6 .   ? 37.25003  7.87200   13.45619  1.000 38.28123  ? 392 HOH   A O     1 
HETATM 5528 O  O     . HOH   K 6 .   ? 22.49841  10.43661  22.11684  1.000 28.96804  ? 393 HOH   A O     1 
HETATM 5529 O  O     . HOH   K 6 .   ? 5.40705   11.13505  16.30802  1.000 38.84862  ? 394 HOH   A O     1 
HETATM 5530 O  O     . HOH   K 6 .   ? 28.62032  3.86198   25.70228  1.000 40.55259  ? 395 HOH   A O     1 
HETATM 5531 O  O     . HOH   K 6 .   ? 12.42197  2.20450   27.99158  1.000 38.53473  ? 396 HOH   A O     1 
HETATM 5532 O  O     . HOH   K 6 .   ? 17.63314  -7.53710  12.04476  1.000 50.22820  ? 397 HOH   A O     1 
HETATM 5533 O  O     . HOH   K 6 .   ? 15.45339  3.33579   -8.10632  1.000 46.74736  ? 398 HOH   A O     1 
HETATM 5534 O  O     . HOH   K 6 .   ? 34.65964  0.08459   -1.46920  1.000 57.83573  ? 399 HOH   A O     1 
HETATM 5535 O  O     . HOH   K 6 .   ? 9.16176   14.71386  18.18120  1.000 32.51738  ? 400 HOH   A O     1 
HETATM 5536 O  O     . HOH   K 6 .   ? 17.75044  -2.98293  1.02454   1.000 39.27230  ? 401 HOH   A O     1 
HETATM 5537 O  O     . HOH   K 6 .   ? 17.30226  14.88251  -6.03143  1.000 43.59248  ? 402 HOH   A O     1 
HETATM 5538 O  O     . HOH   K 6 .   ? 8.67110   -4.50439  9.21428   1.000 51.44944  ? 403 HOH   A O     1 
HETATM 5539 O  O     . HOH   K 6 .   ? 16.13795  0.03121   24.79702  1.000 39.13166  ? 404 HOH   A O     1 
HETATM 5540 O  O     . HOH   K 6 .   ? 13.90081  20.93280  9.29847   1.000 47.81978  ? 405 HOH   A O     1 
HETATM 5541 O  O     . HOH   K 6 .   ? 21.90263  -7.02877  5.21876   1.000 46.55020  ? 406 HOH   A O     1 
HETATM 5542 O  O     . HOH   K 6 .   ? 9.53627   0.44477   1.17614   1.000 37.04412  ? 407 HOH   A O     1 
HETATM 5543 O  O     . HOH   K 6 .   ? 12.74928  16.28982  3.55424   1.000 46.50616  ? 408 HOH   A O     1 
HETATM 5544 O  O     . HOH   K 6 .   ? 19.95635  14.81842  -3.25434  1.000 31.43763  ? 409 HOH   A O     1 
HETATM 5545 O  O     . HOH   K 6 .   ? 16.28634  3.46009   26.32820  1.000 39.82137  ? 410 HOH   A O     1 
HETATM 5546 O  O     . HOH   K 6 .   ? 18.11889  19.55781  19.82625  1.000 37.94409  ? 411 HOH   A O     1 
HETATM 5547 O  O     . HOH   K 6 .   ? 20.67894  20.58376  -1.19538  1.000 51.78621  ? 412 HOH   A O     1 
HETATM 5548 O  O     . HOH   K 6 .   ? 10.35988  0.91907   4.40443   1.000 29.78930  ? 413 HOH   A O     1 
HETATM 5549 O  O     . HOH   K 6 .   ? 34.93920  -5.12852  11.49640  1.000 55.86728  ? 414 HOH   A O     1 
HETATM 5550 O  O     . HOH   K 6 .   ? 22.91532  15.51289  22.49867  1.000 41.04940  ? 415 HOH   A O     1 
HETATM 5551 O  O     . HOH   K 6 .   ? 4.92698   1.80779   5.40005   1.000 47.94870  ? 416 HOH   A O     1 
HETATM 5552 O  O     . HOH   K 6 .   ? 25.89952  13.41241  -0.37347  1.000 41.46496  ? 417 HOH   A O     1 
HETATM 5553 O  O     . HOH   K 6 .   ? 19.89874  17.23992  -3.25105  1.000 36.42644  ? 418 HOH   A O     1 
HETATM 5554 O  O     . HOH   K 6 .   ? 20.58540  3.67229   27.35732  1.000 45.07211  ? 419 HOH   A O     1 
HETATM 5555 O  O     . HOH   K 6 .   ? 18.24428  23.61067  11.02422  1.000 44.76728  ? 420 HOH   A O     1 
HETATM 5556 O  O     . HOH   K 6 .   ? 27.80459  13.16844  30.67174  1.000 47.54038  ? 421 HOH   A O     1 
HETATM 5557 O  O     . HOH   K 6 .   ? 1.16357   -1.97103  23.21744  1.000 54.80023  ? 422 HOH   A O     1 
HETATM 5558 O  O     . HOH   K 6 .   ? 32.63882  11.74888  -3.91952  1.000 45.13408  ? 423 HOH   A O     1 
HETATM 5559 O  O     . HOH   K 6 .   ? 15.55332  0.82452   27.18341  1.000 50.60719  ? 424 HOH   A O     1 
HETATM 5560 O  O     . HOH   K 6 .   ? 15.60104  -6.60868  24.29203  1.000 52.56260  ? 425 HOH   A O     1 
HETATM 5561 O  O     . HOH   K 6 .   ? 13.23181  13.29041  21.73730  1.000 37.41830  ? 426 HOH   A O     1 
HETATM 5562 O  O     . HOH   K 6 .   ? 10.14674  -2.63792  6.53170   1.000 51.44764  ? 427 HOH   A O     1 
HETATM 5563 O  O     . HOH   K 6 .   ? 32.22286  12.98561  7.70567   1.000 42.69756  ? 428 HOH   A O     1 
HETATM 5564 O  O     . HOH   K 6 .   ? 33.81332  11.13113  8.49443   1.000 41.56761  ? 429 HOH   A O     1 
HETATM 5565 O  O     . HOH   K 6 .   ? 15.40664  6.10278   27.00210  1.000 43.89850  ? 430 HOH   A O     1 
HETATM 5566 O  O     . HOH   K 6 .   ? 26.23273  -5.42144  15.52298  1.000 44.94962  ? 431 HOH   A O     1 
HETATM 5567 O  O     . HOH   K 6 .   ? 36.22692  23.97059  13.45716  1.000 44.25536  ? 432 HOH   A O     1 
HETATM 5568 O  O     . HOH   K 6 .   ? 21.98426  -1.38662  23.12478  1.000 49.03229  ? 433 HOH   A O     1 
HETATM 5569 O  O     . HOH   K 6 .   ? 15.62542  18.78185  9.34080   1.000 34.93790  ? 434 HOH   A O     1 
HETATM 5570 O  O     . HOH   K 6 .   ? 34.73482  21.32696  17.13184  1.000 34.82320  ? 435 HOH   A O     1 
HETATM 5571 O  O     . HOH   K 6 .   ? 30.20269  17.87560  23.16938  1.000 44.83806  ? 436 HOH   A O     1 
HETATM 5572 O  O     . HOH   K 6 .   ? 13.43041  18.07504  4.74184   1.000 47.90659  ? 437 HOH   A O     1 
HETATM 5573 O  O     . HOH   K 6 .   ? 26.67763  -0.57565  22.70187  1.000 43.81372  ? 438 HOH   A O     1 
HETATM 5574 O  O     . HOH   K 6 .   ? 18.57603  10.20577  24.58183  1.000 38.74840  ? 439 HOH   A O     1 
HETATM 5575 O  O     . HOH   K 6 .   ? 23.99395  6.06038   28.77896  1.000 47.90503  ? 440 HOH   A O     1 
HETATM 5576 O  O     . HOH   K 6 .   ? 20.34278  9.12235   22.25340  1.000 25.37746  ? 441 HOH   A O     1 
HETATM 5577 O  O     . HOH   K 6 .   ? 35.33809  23.48243  16.36392  1.000 36.96914  ? 442 HOH   A O     1 
HETATM 5578 O  O     . HOH   K 6 .   ? 5.140     17.289    0.597     1.000 42.20314  ? 443 HOH   A O     1 
HETATM 5579 O  O     . HOH   K 6 .   ? 22.35640  12.86207  23.39231  1.000 34.42881  ? 444 HOH   A O     1 
HETATM 5580 O  O     . HOH   K 6 .   ? 22.53398  -8.93634  7.43056   1.000 53.48363  ? 445 HOH   A O     1 
HETATM 5581 O  O     . HOH   K 6 .   ? 38.52661  18.82758  15.86023  1.000 44.69990  ? 446 HOH   A O     1 
HETATM 5582 O  O     . HOH   K 6 .   ? 27.13646  17.32343  16.57193  1.000 44.19357  ? 447 HOH   A O     1 
HETATM 5583 O  O     . HOH   K 6 .   ? 18.52538  -8.06286  9.42729   1.000 53.64320  ? 448 HOH   A O     1 
HETATM 5584 O  O     . HOH   K 6 .   ? 16.09490  -2.45593  25.10512  1.000 52.74344  ? 449 HOH   A O     1 
HETATM 5585 O  O     . HOH   K 6 .   ? 13.10746  4.65253   -7.41208  1.000 38.98287  ? 450 HOH   A O     1 
HETATM 5586 O  O     . HOH   K 6 .   ? 7.668     -1.163    5.201     1.000 50.67826  ? 451 HOH   A O     1 
HETATM 5587 O  O     . HOH   K 6 .   ? 11.07517  19.83613  16.26072  1.000 48.84876  ? 452 HOH   A O     1 
HETATM 5588 O  O     . HOH   K 6 .   ? 19.86099  12.93655  23.69643  1.000 41.63370  ? 453 HOH   A O     1 
HETATM 5589 O  O     . HOH   L 6 .   ? 27.52879  35.51064  43.55006  1.000 54.78491  ? 301 HOH   B O     1 
HETATM 5590 O  O     . HOH   L 6 .   ? 10.07565  33.63998  37.76145  1.000 39.84899  ? 302 HOH   B O     1 
HETATM 5591 O  O     . HOH   L 6 .   ? 23.07375  20.66568  27.28279  1.000 46.10755  ? 303 HOH   B O     1 
HETATM 5592 O  O     . HOH   L 6 .   ? 5.78960   26.49030  50.00423  1.000 57.47310  ? 304 HOH   B O     1 
HETATM 5593 O  O     . HOH   L 6 .   ? 26.53941  22.65366  27.76209  1.000 40.26426  ? 305 HOH   B O     1 
HETATM 5594 O  O     . HOH   L 6 .   ? 22.62245  36.48413  35.35552  1.000 51.07041  ? 306 HOH   B O     1 
HETATM 5595 O  O     . HOH   L 6 .   ? 9.23223   6.81262   39.89240  1.000 54.17439  ? 307 HOH   B O     1 
HETATM 5596 O  O     . HOH   L 6 .   ? 18.66492  32.76442  27.73069  1.000 35.45514  ? 308 HOH   B O     1 
HETATM 5597 O  O     . HOH   L 6 .   ? 3.71173   29.12873  49.79956  1.000 54.06130  ? 309 HOH   B O     1 
HETATM 5598 O  O     . HOH   L 6 .   ? 13.06968  40.42887  37.53938  1.000 52.20992  ? 310 HOH   B O     1 
HETATM 5599 O  O     . HOH   L 6 .   ? 11.96194  15.43843  37.79733  1.000 41.46070  ? 311 HOH   B O     1 
HETATM 5600 O  O     . HOH   L 6 .   ? 10.30309  23.06958  37.43336  1.000 28.29017  ? 312 HOH   B O     1 
HETATM 5601 O  O     . HOH   L 6 .   ? 34.71592  30.73558  30.69205  1.000 39.24143  ? 313 HOH   B O     1 
HETATM 5602 O  O     . HOH   L 6 .   ? 7.15062   24.75319  33.64255  1.000 40.78806  ? 314 HOH   B O     1 
HETATM 5603 O  O     . HOH   L 6 .   ? 4.19647   26.34967  56.29401  1.000 63.20248  ? 315 HOH   B O     1 
HETATM 5604 O  O     . HOH   L 6 .   ? 27.63365  15.93236  31.57161  1.000 49.65249  ? 316 HOH   B O     1 
HETATM 5605 O  O     . HOH   L 6 .   ? 21.19473  16.64978  33.02596  1.000 40.88827  ? 317 HOH   B O     1 
HETATM 5606 O  O     . HOH   L 6 .   ? 12.46341  20.32329  47.74345  1.000 39.50372  ? 318 HOH   B O     1 
HETATM 5607 O  O     . HOH   L 6 .   ? 27.32579  24.02369  23.29697  1.000 31.50176  ? 319 HOH   B O     1 
HETATM 5608 O  O     . HOH   L 6 .   ? 20.02549  21.61351  29.80408  1.000 41.64066  ? 320 HOH   B O     1 
HETATM 5609 O  O     . HOH   L 6 .   ? 36.62276  27.53870  32.96234  1.000 42.19705  ? 321 HOH   B O     1 
HETATM 5610 O  O     . HOH   L 6 .   ? 31.36281  25.62663  24.01871  1.000 39.02315  ? 322 HOH   B O     1 
HETATM 5611 O  O     . HOH   L 6 .   ? 3.44980   25.23123  52.45012  1.000 63.81680  ? 323 HOH   B O     1 
HETATM 5612 O  O     . HOH   L 6 .   ? 13.53552  31.71817  27.75511  1.000 38.97249  ? 324 HOH   B O     1 
HETATM 5613 O  O     . HOH   L 6 .   ? 4.47564   30.39021  46.79392  1.000 44.92715  ? 325 HOH   B O     1 
HETATM 5614 O  O     . HOH   L 6 .   ? 32.12403  22.72644  32.98860  1.000 39.86230  ? 326 HOH   B O     1 
HETATM 5615 O  O     . HOH   L 6 .   ? 34.23342  29.81939  33.45347  1.000 40.75040  ? 327 HOH   B O     1 
HETATM 5616 O  O     . HOH   L 6 .   ? 4.79779   19.70241  40.99851  1.000 40.16350  ? 328 HOH   B O     1 
HETATM 5617 O  O     . HOH   L 6 .   ? 5.95269   23.30953  56.86534  1.000 64.08173  ? 329 HOH   B O     1 
HETATM 5618 O  O     . HOH   L 6 .   ? 11.82900  11.38676  45.75985  1.000 58.45439  ? 330 HOH   B O     1 
HETATM 5619 O  O     . HOH   L 6 .   ? 19.29116  6.68736   46.21544  1.000 60.26899  ? 331 HOH   B O     1 
HETATM 5620 O  O     . HOH   L 6 .   ? 13.03619  18.06566  40.59601  1.000 31.52932  ? 332 HOH   B O     1 
HETATM 5621 O  O     . HOH   L 6 .   ? 6.11967   19.14339  37.70801  1.000 29.96773  ? 333 HOH   B O     1 
HETATM 5622 O  O     . HOH   L 6 .   ? 33.67289  25.73306  25.84691  1.000 40.77053  ? 334 HOH   B O     1 
HETATM 5623 O  O     . HOH   L 6 .   ? 18.48271  35.22794  29.33698  1.000 31.41503  ? 335 HOH   B O     1 
HETATM 5624 O  O     . HOH   L 6 .   ? 28.32224  39.40067  37.55426  1.000 46.03280  ? 336 HOH   B O     1 
HETATM 5625 O  O     . HOH   L 6 .   ? 10.50260  26.20126  32.87570  1.000 32.47395  ? 337 HOH   B O     1 
HETATM 5626 O  O     . HOH   L 6 .   ? 16.23890  26.99412  25.44764  1.000 36.93225  ? 338 HOH   B O     1 
HETATM 5627 O  O     . HOH   L 6 .   ? 34.74892  38.28215  31.00215  1.000 44.35489  ? 339 HOH   B O     1 
HETATM 5628 O  O     . HOH   L 6 .   ? 37.02260  27.77153  28.54768  1.000 40.60933  ? 340 HOH   B O     1 
HETATM 5629 O  O     . HOH   L 6 .   ? 17.17093  15.47097  29.98091  1.000 39.40490  ? 341 HOH   B O     1 
HETATM 5630 O  O     . HOH   L 6 .   ? 31.23668  28.10761  24.60888  1.000 31.31861  ? 342 HOH   B O     1 
HETATM 5631 O  O     . HOH   L 6 .   ? 6.95516   25.24881  37.30682  1.000 35.82900  ? 343 HOH   B O     1 
HETATM 5632 O  O     . HOH   L 6 .   ? 20.54472  13.53868  30.01348  1.000 39.13079  ? 344 HOH   B O     1 
HETATM 5633 O  O     . HOH   L 6 .   ? 30.00231  21.41986  30.58233  1.000 39.45849  ? 345 HOH   B O     1 
HETATM 5634 O  O     . HOH   L 6 .   ? 11.91444  16.56748  34.54400  1.000 29.47411  ? 346 HOH   B O     1 
HETATM 5635 O  O     . HOH   L 6 .   ? 31.32552  38.89508  28.22529  1.000 36.65072  ? 347 HOH   B O     1 
HETATM 5636 O  O     . HOH   L 6 .   ? 35.28029  25.69401  35.21580  1.000 51.50684  ? 348 HOH   B O     1 
HETATM 5637 O  O     . HOH   L 6 .   ? 7.88992   21.40208  30.62317  1.000 31.32234  ? 349 HOH   B O     1 
HETATM 5638 O  O     . HOH   L 6 .   ? 30.21666  38.04043  39.52359  1.000 39.54215  ? 350 HOH   B O     1 
HETATM 5639 O  O     . HOH   L 6 .   ? 33.29181  32.20973  23.97183  1.000 33.58217  ? 351 HOH   B O     1 
HETATM 5640 O  O     . HOH   L 6 .   ? 10.73345  40.50324  31.01553  1.000 44.90217  ? 352 HOH   B O     1 
HETATM 5641 O  O     . HOH   L 6 .   ? 21.78208  21.38542  32.41457  1.000 28.74037  ? 353 HOH   B O     1 
HETATM 5642 O  O     . HOH   L 6 .   ? 38.11559  30.70968  25.05603  1.000 42.94398  ? 354 HOH   B O     1 
HETATM 5643 O  O     . HOH   L 6 .   ? 10.81117  13.07303  38.07449  1.000 43.26172  ? 355 HOH   B O     1 
HETATM 5644 O  O     . HOH   L 6 .   ? 12.69039  19.90521  27.24259  1.000 39.10714  ? 356 HOH   B O     1 
HETATM 5645 O  O     . HOH   L 6 .   ? 18.02651  5.83287   33.74678  1.000 55.09810  ? 357 HOH   B O     1 
HETATM 5646 O  O     . HOH   L 6 .   ? 28.61367  24.86322  54.33238  1.000 60.89460  ? 358 HOH   B O     1 
HETATM 5647 O  O     . HOH   L 6 .   ? 26.57239  38.92335  33.46258  1.000 45.90493  ? 359 HOH   B O     1 
HETATM 5648 O  O     . HOH   L 6 .   ? 32.53926  23.83511  28.21688  1.000 37.43654  ? 360 HOH   B O     1 
HETATM 5649 O  O     . HOH   L 6 .   ? 16.36810  7.87964   34.27050  1.000 44.39419  ? 361 HOH   B O     1 
HETATM 5650 O  O     . HOH   L 6 .   ? 19.97755  37.92478  42.88883  1.000 51.77800  ? 362 HOH   B O     1 
HETATM 5651 O  O     . HOH   L 6 .   ? 36.25339  35.32620  30.47432  1.000 43.32287  ? 363 HOH   B O     1 
HETATM 5652 O  O     . HOH   L 6 .   ? 28.32642  37.76859  28.78160  1.000 41.68290  ? 364 HOH   B O     1 
HETATM 5653 O  O     . HOH   L 6 .   ? 15.07208  19.13572  28.16158  1.000 43.93593  ? 365 HOH   B O     1 
HETATM 5654 O  O     . HOH   L 6 .   ? 20.05593  24.17403  26.93127  1.000 38.46874  ? 366 HOH   B O     1 
HETATM 5655 O  O     . HOH   L 6 .   ? 35.79595  33.13852  29.22912  1.000 48.08812  ? 367 HOH   B O     1 
HETATM 5656 O  O     . HOH   L 6 .   ? 24.01903  38.43181  30.60110  1.000 48.40837  ? 368 HOH   B O     1 
HETATM 5657 O  O     . HOH   L 6 .   ? 16.25975  38.64752  30.63557  1.000 38.62366  ? 369 HOH   B O     1 
HETATM 5658 O  O     . HOH   L 6 .   ? 22.53823  37.08429  28.45718  1.000 36.33961  ? 370 HOH   B O     1 
HETATM 5659 O  O     A HOH   L 6 .   ? 12.41072  24.04479  26.97461  0.500 31.59230  ? 371 HOH   B O     1 
HETATM 5660 O  O     B HOH   L 6 .   ? 13.58077  22.47751  26.59745  0.500 31.59230  ? 371 HOH   B O     1 
HETATM 5661 O  O     . HOH   L 6 .   ? 10.47495  41.05822  38.89722  1.000 46.59573  ? 372 HOH   B O     1 
HETATM 5662 O  O     . HOH   L 6 .   ? 2.24542   30.48066  45.51527  1.000 45.77721  ? 373 HOH   B O     1 
HETATM 5663 O  O     . HOH   L 6 .   ? 5.12259   5.91197   37.24987  1.000 43.46918  ? 374 HOH   B O     1 
HETATM 5664 O  O     . HOH   L 6 .   ? 17.17981  38.64296  32.77327  1.000 47.67415  ? 375 HOH   B O     1 
HETATM 5665 O  O     . HOH   L 6 .   ? 30.08871  22.24910  23.93490  1.000 42.49524  ? 376 HOH   B O     1 
HETATM 5666 O  O     . HOH   L 6 .   ? 5.812     28.320    61.902    1.000 61.85532  ? 377 HOH   B O     1 
HETATM 5667 O  O     . HOH   L 6 .   ? 37.35412  32.68107  23.39981  1.000 47.80616  ? 378 HOH   B O     1 
HETATM 5668 O  O     . HOH   L 6 .   ? 31.30134  21.73142  27.32294  1.000 50.49267  ? 379 HOH   B O     1 
HETATM 5669 O  O     . HOH   L 6 .   ? 22.65208  18.91313  32.25891  1.000 35.31486  ? 380 HOH   B O     1 
HETATM 5670 O  O     . HOH   L 6 .   ? 31.43996  38.73467  25.68660  1.000 40.54904  ? 381 HOH   B O     1 
HETATM 5671 O  O     . HOH   L 6 .   ? 15.78281  41.29740  30.07118  1.000 37.02756  ? 382 HOH   B O     1 
HETATM 5672 O  O     . HOH   L 6 .   ? 19.64067  16.24700  30.62654  1.000 36.01335  ? 383 HOH   B O     1 
HETATM 5673 O  O     . HOH   L 6 .   ? 23.22379  18.77288  29.37451  1.000 40.46450  ? 384 HOH   B O     1 
HETATM 5674 O  O     . HOH   L 6 .   ? 18.76737  38.39769  28.41775  1.000 45.44719  ? 385 HOH   B O     1 
HETATM 5675 O  O     . HOH   L 6 .   ? 8.15685   40.04883  29.84300  1.000 47.47628  ? 386 HOH   B O     1 
HETATM 5676 O  O     . HOH   L 6 .   ? 28.128    4.421     52.326    1.000 52.71158  ? 387 HOH   B O     1 
HETATM 5677 O  O     A HOH   L 6 .   ? 20.36137  18.03057  29.04948  0.500 36.42230  ? 388 HOH   B O     1 
HETATM 5678 O  O     B HOH   L 6 .   ? 19.28904  19.58132  28.26710  0.500 36.42230  ? 388 HOH   B O     1 
HETATM 5679 O  O     . HOH   M 6 .   ? 3.95814   0.83844   32.90351  1.000 48.73713  ? 301 HOH   C O     1 
HETATM 5680 O  O     . HOH   M 6 .   ? -3.76287  4.04716   18.39670  1.000 35.55735  ? 302 HOH   C O     1 
HETATM 5681 O  O     . HOH   M 6 .   ? -6.80674  20.00339  5.28153   1.000 44.06230  ? 303 HOH   C O     1 
HETATM 5682 O  O     . HOH   M 6 .   ? -1.38300  11.33815  7.78363   1.000 45.78916  ? 304 HOH   C O     1 
HETATM 5683 O  O     . HOH   M 6 .   ? -2.35843  29.01983  37.23088  1.000 61.29101  ? 305 HOH   C O     1 
HETATM 5684 O  O     . HOH   M 6 .   ? -11.03288 4.23854   21.40996  1.000 36.46211  ? 306 HOH   C O     1 
HETATM 5685 O  O     . HOH   M 6 .   ? -8.07115  22.37243  23.87378  1.000 33.13662  ? 307 HOH   C O     1 
HETATM 5686 O  O     . HOH   M 6 .   ? -5.21091  0.66842   33.74634  1.000 32.25487  ? 308 HOH   C O     1 
HETATM 5687 O  O     . HOH   M 6 .   ? -8.63531  28.55885  35.32886  1.000 53.80748  ? 309 HOH   C O     1 
HETATM 5688 O  O     A HOH   M 6 .   ? -24.14314 14.45548  30.52437  0.500 39.13230  ? 310 HOH   C O     1 
HETATM 5689 O  O     B HOH   M 6 .   ? -24.21375 13.17530  32.31630  0.500 39.13230  ? 310 HOH   C O     1 
HETATM 5690 O  O     . HOH   M 6 .   ? -9.26829  13.94791  37.76698  1.000 29.58583  ? 311 HOH   C O     1 
HETATM 5691 O  O     . HOH   M 6 .   ? -11.55021 2.63827   31.09379  1.000 32.97356  ? 312 HOH   C O     1 
HETATM 5692 O  O     . HOH   M 6 .   ? 7.98151   20.58409  19.39969  1.000 34.19421  ? 313 HOH   C O     1 
HETATM 5693 O  O     . HOH   M 6 .   ? -24.12568 17.69577  36.11402  1.000 44.67230  ? 314 HOH   C O     1 
HETATM 5694 O  O     . HOH   M 6 .   ? -20.62099 25.31156  27.35917  1.000 45.03633  ? 315 HOH   C O     1 
HETATM 5695 O  O     . HOH   M 6 .   ? 6.27040   19.83685  12.72088  1.000 39.02230  ? 316 HOH   C O     1 
HETATM 5696 O  O     . HOH   M 6 .   ? -12.29019 11.25325  11.26340  1.000 36.97515  ? 317 HOH   C O     1 
HETATM 5697 O  O     . HOH   M 6 .   ? -4.72149  25.22475  14.11933  1.000 34.99588  ? 318 HOH   C O     1 
HETATM 5698 O  O     . HOH   M 6 .   ? -0.86992  23.39567  8.36581   1.000 48.98300  ? 319 HOH   C O     1 
HETATM 5699 O  O     . HOH   M 6 .   ? -15.05963 28.75115  22.74015  1.000 44.17291  ? 320 HOH   C O     1 
HETATM 5700 O  O     . HOH   M 6 .   ? -6.22437  26.84226  24.18328  1.000 41.56033  ? 321 HOH   C O     1 
HETATM 5701 O  O     . HOH   M 6 .   ? -0.95757  21.92654  31.31174  1.000 29.84101  ? 322 HOH   C O     1 
HETATM 5702 O  O     . HOH   M 6 .   ? 4.22843   4.74710   26.56072  1.000 39.24037  ? 323 HOH   C O     1 
HETATM 5703 O  O     . HOH   M 6 .   ? -11.61616 7.07869   36.67009  1.000 30.57195  ? 324 HOH   C O     1 
HETATM 5704 O  O     . HOH   M 6 .   ? 2.64700   23.51915  22.75376  1.000 29.66629  ? 325 HOH   C O     1 
HETATM 5705 O  O     . HOH   M 6 .   ? -15.29652 16.92000  32.38569  1.000 30.92857  ? 326 HOH   C O     1 
HETATM 5706 O  O     . HOH   M 6 .   ? -16.89797 21.77772  11.47792  1.000 46.97014  ? 327 HOH   C O     1 
HETATM 5707 O  O     . HOH   M 6 .   ? -8.69883  16.54300  40.47339  1.000 32.90648  ? 328 HOH   C O     1 
HETATM 5708 O  O     . HOH   M 6 .   ? -9.28503  19.74060  34.43688  1.000 31.58634  ? 329 HOH   C O     1 
HETATM 5709 O  O     . HOH   M 6 .   ? -18.74666 8.67921   15.80535  1.000 45.27596  ? 330 HOH   C O     1 
HETATM 5710 O  O     . HOH   M 6 .   ? -12.28124 30.38553  24.87328  1.000 46.46153  ? 331 HOH   C O     1 
HETATM 5711 O  O     . HOH   M 6 .   ? 7.01370   17.91381  16.62015  1.000 31.75931  ? 332 HOH   C O     1 
HETATM 5712 O  O     . HOH   M 6 .   ? -5.08281  24.02109  26.11103  1.000 28.31750  ? 333 HOH   C O     1 
HETATM 5713 O  O     . HOH   M 6 .   ? -9.66552  13.66900  8.13421   1.000 37.59604  ? 334 HOH   C O     1 
HETATM 5714 O  O     . HOH   M 6 .   ? -25.07417 4.36085   26.61330  1.000 54.14275  ? 335 HOH   C O     1 
HETATM 5715 O  O     . HOH   M 6 .   ? -10.09631 12.63009  44.97225  1.000 33.94230  ? 336 HOH   C O     1 
HETATM 5716 O  O     . HOH   M 6 .   ? -6.46786  0.04083   37.83196  1.000 44.86529  ? 337 HOH   C O     1 
HETATM 5717 O  O     . HOH   M 6 .   ? -14.52575 14.11369  38.23605  1.000 34.47513  ? 338 HOH   C O     1 
HETATM 5718 O  O     . HOH   M 6 .   ? -11.33246 0.30420   28.13811  1.000 41.20807  ? 339 HOH   C O     1 
HETATM 5719 O  O     . HOH   M 6 .   ? 4.00702   8.82259   17.53725  1.000 27.35761  ? 340 HOH   C O     1 
HETATM 5720 O  O     . HOH   M 6 .   ? 1.81336   1.08659   30.16387  1.000 42.93009  ? 341 HOH   C O     1 
HETATM 5721 O  O     . HOH   M 6 .   ? 3.46583   22.43720  26.51911  1.000 35.90164  ? 342 HOH   C O     1 
HETATM 5722 O  O     . HOH   M 6 .   ? -16.76859 9.49015   44.88270  1.000 37.05531  ? 343 HOH   C O     1 
HETATM 5723 O  O     . HOH   M 6 .   ? -0.62882  23.27681  19.73182  1.000 28.80664  ? 344 HOH   C O     1 
HETATM 5724 O  O     . HOH   M 6 .   ? -6.93007  13.38419  41.99251  1.000 33.15402  ? 345 HOH   C O     1 
HETATM 5725 O  O     . HOH   M 6 .   ? 1.42842   13.17659  35.53291  1.000 27.18415  ? 346 HOH   C O     1 
HETATM 5726 O  O     . HOH   M 6 .   ? 1.70766   24.93125  8.62049   1.000 53.85952  ? 347 HOH   C O     1 
HETATM 5727 O  O     . HOH   M 6 .   ? 12.00902  11.01110  31.39185  1.000 45.43425  ? 348 HOH   C O     1 
HETATM 5728 O  O     . HOH   M 6 .   ? -13.42270 -0.36519  38.65609  1.000 35.83406  ? 349 HOH   C O     1 
HETATM 5729 O  O     . HOH   M 6 .   ? -25.01034 12.46238  21.90358  1.000 38.21533  ? 350 HOH   C O     1 
HETATM 5730 O  O     . HOH   M 6 .   ? -19.83143 21.31083  41.71071  1.000 51.43171  ? 351 HOH   C O     1 
HETATM 5731 O  O     . HOH   M 6 .   ? 2.24870   25.56200  19.09986  1.000 42.51762  ? 352 HOH   C O     1 
HETATM 5732 O  O     . HOH   M 6 .   ? -14.39222 6.78609   36.40888  1.000 30.64238  ? 353 HOH   C O     1 
HETATM 5733 O  O     . HOH   M 6 .   ? 4.31869   20.74174  28.17818  1.000 40.45362  ? 354 HOH   C O     1 
HETATM 5734 O  O     . HOH   M 6 .   ? -21.81554 12.95392  40.56588  1.000 54.73106  ? 355 HOH   C O     1 
HETATM 5735 O  O     . HOH   M 6 .   ? -6.00761  28.11763  20.32960  1.000 44.43835  ? 356 HOH   C O     1 
HETATM 5736 O  O     . HOH   M 6 .   ? -13.54850 -0.27208  35.10523  1.000 43.41794  ? 357 HOH   C O     1 
HETATM 5737 O  O     . HOH   M 6 .   ? -0.44590  13.18373  37.40576  1.000 29.23341  ? 358 HOH   C O     1 
HETATM 5738 O  O     . HOH   M 6 .   ? -9.78744  21.62550  45.46726  1.000 46.31818  ? 359 HOH   C O     1 
HETATM 5739 O  O     . HOH   M 6 .   ? -14.06408 10.02330  44.20052  1.000 42.96909  ? 360 HOH   C O     1 
HETATM 5740 O  O     . HOH   M 6 .   ? -18.57512 12.18315  43.50466  1.000 42.84808  ? 361 HOH   C O     1 
HETATM 5741 O  O     . HOH   M 6 .   ? 10.51213  20.39520  23.03977  1.000 40.65051  ? 362 HOH   C O     1 
HETATM 5742 O  O     . HOH   M 6 .   ? -14.40627 26.03796  42.16379  1.000 50.42905  ? 363 HOH   C O     1 
HETATM 5743 O  O     . HOH   M 6 .   ? -11.03654 19.58618  11.03520  1.000 39.61157  ? 364 HOH   C O     1 
HETATM 5744 O  O     . HOH   M 6 .   ? -5.82295  19.33075  45.82700  1.000 43.63503  ? 365 HOH   C O     1 
HETATM 5745 O  O     . HOH   M 6 .   ? -5.50206  -2.72248  29.37001  1.000 48.39245  ? 366 HOH   C O     1 
HETATM 5746 O  O     . HOH   M 6 .   ? 11.34705  15.37603  21.32451  1.000 28.44607  ? 367 HOH   C O     1 
HETATM 5747 O  O     . HOH   M 6 .   ? -1.91098  5.43536   19.61777  1.000 34.06782  ? 368 HOH   C O     1 
HETATM 5748 O  O     . HOH   M 6 .   ? -8.54266  6.40565   37.18993  1.000 25.60396  ? 369 HOH   C O     1 
HETATM 5749 O  O     . HOH   M 6 .   ? -11.33862 5.52264   15.65879  1.000 38.60505  ? 370 HOH   C O     1 
HETATM 5750 O  O     . HOH   M 6 .   ? -10.812   9.664     10.223    1.000 29.84589  ? 371 HOH   C O     1 
HETATM 5751 O  O     . HOH   M 6 .   ? -19.42934 13.97172  41.83991  1.000 49.19003  ? 372 HOH   C O     1 
HETATM 5752 O  O     . HOH   M 6 .   ? -12.00019 6.56902   12.17850  1.000 43.38766  ? 373 HOH   C O     1 
HETATM 5753 O  O     . HOH   M 6 .   ? -8.72105  23.01966  33.65912  1.000 34.56726  ? 374 HOH   C O     1 
HETATM 5754 O  O     . HOH   M 6 .   ? -21.296   9.928     40.383    1.000 41.79859  ? 375 HOH   C O     1 
HETATM 5755 O  O     . HOH   M 6 .   ? -17.84941 22.92483  41.90348  1.000 48.59873  ? 376 HOH   C O     1 
HETATM 5756 O  O     . HOH   M 6 .   ? -11.70039 12.91734  9.78348   1.000 38.91945  ? 377 HOH   C O     1 
HETATM 5757 O  O     . HOH   M 6 .   ? 2.53924   2.65087   27.63878  1.000 42.51706  ? 378 HOH   C O     1 
HETATM 5758 O  O     . HOH   M 6 .   ? -19.51744 13.16938  12.79462  1.000 44.52062  ? 379 HOH   C O     1 
HETATM 5759 O  O     . HOH   M 6 .   ? -14.45767 13.48488  45.64531  1.000 44.76219  ? 380 HOH   C O     1 
HETATM 5760 O  O     . HOH   M 6 .   ? -13.37047 20.79690  43.91090  1.000 44.36330  ? 381 HOH   C O     1 
HETATM 5761 O  O     . HOH   M 6 .   ? -2.62148  2.55980   14.12982  1.000 49.72106  ? 382 HOH   C O     1 
HETATM 5762 O  O     . HOH   M 6 .   ? -4.63459  4.77466   28.85595  1.000 26.97253  ? 383 HOH   C O     1 
HETATM 5763 O  O     . HOH   M 6 .   ? -17.24066 24.99218  22.47991  1.000 37.45942  ? 384 HOH   C O     1 
HETATM 5764 O  O     . HOH   M 6 .   ? -7.08403  2.21541   40.60302  1.000 43.16044  ? 385 HOH   C O     1 
HETATM 5765 O  O     . HOH   M 6 .   ? -9.34814  5.75916   12.64784  1.000 37.70715  ? 386 HOH   C O     1 
HETATM 5766 O  O     . HOH   M 6 .   ? -1.31456  16.73454  38.96440  1.000 39.51368  ? 387 HOH   C O     1 
HETATM 5767 O  O     . HOH   M 6 .   ? 10.39668  23.76443  25.30950  1.000 49.12037  ? 388 HOH   C O     1 
HETATM 5768 O  O     . HOH   M 6 .   ? -2.967    0.887     37.850    1.000 45.60029  ? 389 HOH   C O     1 
HETATM 5769 O  O     . HOH   M 6 .   ? -3.26462  19.68716  45.21684  1.000 48.07094  ? 390 HOH   C O     1 
HETATM 5770 O  O     . HOH   M 6 .   ? -12.142   0.695     32.811    1.000 41.50983  ? 391 HOH   C O     1 
HETATM 5771 O  O     . HOH   M 6 .   ? -11.06845 29.34386  22.75859  1.000 41.08230  ? 392 HOH   C O     1 
HETATM 5772 O  O     . HOH   M 6 .   ? -27.24410 14.60549  26.09086  1.000 43.45284  ? 393 HOH   C O     1 
HETATM 5773 O  O     . HOH   M 6 .   ? -21.84452 17.71855  12.47694  1.000 54.02283  ? 394 HOH   C O     1 
HETATM 5774 O  O     . HOH   M 6 .   ? -18.78469 24.81070  20.44386  1.000 43.44023  ? 395 HOH   C O     1 
HETATM 5775 O  O     . HOH   M 6 .   ? -0.08015  6.04646   17.66615  1.000 36.68282  ? 396 HOH   C O     1 
HETATM 5776 O  O     . HOH   M 6 .   ? -14.63595 30.08785  25.63465  1.000 46.30174  ? 397 HOH   C O     1 
HETATM 5777 O  O     . HOH   M 6 .   ? -24.648   7.639     18.699    1.000 53.56230  ? 398 HOH   C O     1 
HETATM 5778 O  O     . HOH   M 6 .   ? -11.336   -0.645    40.749    1.000 33.20882  ? 399 HOH   C O     1 
HETATM 5779 O  O     . HOH   M 6 .   ? -1.32396  15.75653  41.57453  1.000 44.89746  ? 400 HOH   C O     1 
HETATM 5780 O  O     . HOH   M 6 .   ? -4.16146  27.87852  14.15049  1.000 44.04161  ? 401 HOH   C O     1 
HETATM 5781 O  O     . HOH   M 6 .   ? 16.47279  11.61984  27.51986  1.000 40.68866  ? 402 HOH   C O     1 
HETATM 5782 O  O     . HOH   M 6 .   ? 5.06828   22.69366  29.98119  1.000 48.12820  ? 403 HOH   C O     1 
HETATM 5783 O  O     . HOH   M 6 .   ? -17.67253 27.39889  22.88165  1.000 40.35708  ? 404 HOH   C O     1 
HETATM 5784 O  O     . HOH   M 6 .   ? -11.85101 17.83021  9.77505   1.000 42.40230  ? 405 HOH   C O     1 
HETATM 5785 O  O     . HOH   M 6 .   ? 8.62778   23.07742  18.59355  1.000 45.25721  ? 406 HOH   C O     1 
HETATM 5786 O  O     . HOH   M 6 .   ? -15.22608 15.60733  47.09207  1.000 52.61495  ? 407 HOH   C O     1 
HETATM 5787 O  O     . HOH   M 6 .   ? -9.25485  3.46831   20.03619  1.000 42.44137  ? 408 HOH   C O     1 
HETATM 5788 O  O     A HOH   M 6 .   ? 1.38547   0.76163   25.73338  0.500 41.11230  ? 409 HOH   C O     1 
HETATM 5789 O  O     B HOH   M 6 .   ? -0.59617  0.91425   25.13803  0.500 41.11230  ? 409 HOH   C O     1 
HETATM 5790 O  O     . HOH   M 6 .   ? -28.79173 5.53106   31.25604  1.000 56.33612  ? 410 HOH   C O     1 
HETATM 5791 O  O     . HOH   M 6 .   ? -17.91549 11.02949  14.00368  1.000 48.59505  ? 411 HOH   C O     1 
HETATM 5792 O  O     . HOH   M 6 .   ? -12.97541 8.28794   10.87522  1.000 41.02982  ? 412 HOH   C O     1 
HETATM 5793 O  O     . HOH   M 6 .   ? 9.48881   18.96895  17.98899  1.000 39.57768  ? 413 HOH   C O     1 
HETATM 5794 O  O     . HOH   M 6 .   ? -4.20484  21.13652  4.20208   1.000 53.82309  ? 414 HOH   C O     1 
HETATM 5795 O  O     . HOH   M 6 .   ? 17.37820  14.45543  27.59426  1.000 37.57392  ? 415 HOH   C O     1 
HETATM 5796 O  O     . HOH   M 6 .   ? -0.05711  25.94414  20.47483  1.000 44.49170  ? 416 HOH   C O     1 
HETATM 5797 O  O     . HOH   M 6 .   ? -13.33654 19.97898  46.57436  1.000 50.08684  ? 417 HOH   C O     1 
HETATM 5798 O  O     . HOH   M 6 .   ? -31.45609 5.11204   30.49315  1.000 56.58151  ? 418 HOH   C O     1 
HETATM 5799 O  O     . HOH   M 6 .   ? -4.38567  0.85392   13.75407  1.000 52.35230  ? 419 HOH   C O     1 
HETATM 5800 O  O     . HOH   M 6 .   ? -2.00223  20.95161  6.54392   1.000 51.43173  ? 420 HOH   C O     1 
HETATM 5801 O  O     . HOH   M 6 .   ? -10.09586 3.40682   17.35634  1.000 53.96194  ? 421 HOH   C O     1 
HETATM 5802 O  O     . HOH   M 6 .   ? -11.70684 22.29893  10.34013  1.000 42.48230  ? 422 HOH   C O     1 
HETATM 5803 O  O     . HOH   M 6 .   ? -0.81814  28.65692  20.17461  1.000 60.44956  ? 423 HOH   C O     1 
HETATM 5804 O  O     . HOH   N 6 .   ? 16.55062  27.57302  13.49630  1.000 31.70284  ? 301 HOH   D O     1 
HETATM 5805 O  O     . HOH   N 6 .   ? 11.86052  52.01777  10.60587  1.000 47.08692  ? 302 HOH   D O     1 
HETATM 5806 O  O     . HOH   N 6 .   ? 39.96463  28.16710  8.11354   1.000 40.97828  ? 303 HOH   D O     1 
HETATM 5807 O  O     . HOH   N 6 .   ? 28.98401  49.13062  -0.74972  1.000 35.63115  ? 304 HOH   D O     1 
HETATM 5808 O  O     . HOH   N 6 .   ? 25.11660  33.44223  2.68961   1.000 25.38344  ? 305 HOH   D O     1 
HETATM 5809 O  O     . HOH   N 6 .   ? 42.06118  32.13921  13.60048  1.000 35.55108  ? 306 HOH   D O     1 
HETATM 5810 O  O     . HOH   N 6 .   ? 37.26073  48.84375  -1.29729  1.000 41.78446  ? 307 HOH   D O     1 
HETATM 5811 O  O     . HOH   N 6 .   ? 42.75168  40.31264  10.01186  1.000 41.66386  ? 308 HOH   D O     1 
HETATM 5812 O  O     . HOH   N 6 .   ? 15.60647  30.72355  -2.61537  1.000 41.73400  ? 309 HOH   D O     1 
HETATM 5813 O  O     . HOH   N 6 .   ? 10.61978  33.26478  24.62045  1.000 35.67638  ? 310 HOH   D O     1 
HETATM 5814 O  O     . HOH   N 6 .   ? 33.07198  30.71961  21.00993  1.000 39.45622  ? 311 HOH   D O     1 
HETATM 5815 O  O     . HOH   N 6 .   ? 30.80968  45.63893  17.50682  1.000 36.52238  ? 312 HOH   D O     1 
HETATM 5816 O  O     . HOH   N 6 .   ? 8.26815   42.66873  11.90877  1.000 50.71451  ? 313 HOH   D O     1 
HETATM 5817 O  O     . HOH   N 6 .   ? 23.11931  38.03481  25.81411  1.000 33.61001  ? 314 HOH   D O     1 
HETATM 5818 O  O     . HOH   N 6 .   ? 19.05660  26.08848  13.97589  1.000 30.61298  ? 315 HOH   D O     1 
HETATM 5819 O  O     . HOH   N 6 .   ? 36.42967  41.92831  18.25384  1.000 34.94833  ? 316 HOH   D O     1 
HETATM 5820 O  O     . HOH   N 6 .   ? 37.58173  42.40227  -3.58052  1.000 42.34951  ? 317 HOH   D O     1 
HETATM 5821 O  O     . HOH   N 6 .   ? 14.49263  51.58244  4.34597   1.000 41.22899  ? 318 HOH   D O     1 
HETATM 5822 O  O     . HOH   N 6 .   ? 31.04175  30.37016  0.86147   1.000 24.00568  ? 319 HOH   D O     1 
HETATM 5823 O  O     . HOH   N 6 .   ? 39.39154  35.04568  15.26703  1.000 30.06793  ? 320 HOH   D O     1 
HETATM 5824 O  O     . HOH   N 6 .   ? 19.49213  50.72424  19.65021  1.000 42.53919  ? 321 HOH   D O     1 
HETATM 5825 O  O     . HOH   N 6 .   ? 8.66393   39.83915  14.81198  1.000 31.94457  ? 322 HOH   D O     1 
HETATM 5826 O  O     . HOH   N 6 .   ? 28.54979  41.64262  23.67664  1.000 32.51431  ? 323 HOH   D O     1 
HETATM 5827 O  O     . HOH   N 6 .   ? 35.42415  54.12472  6.63385   1.000 40.17748  ? 324 HOH   D O     1 
HETATM 5828 O  O     . HOH   N 6 .   ? 36.76201  38.60153  21.78293  1.000 42.77662  ? 325 HOH   D O     1 
HETATM 5829 O  O     . HOH   N 6 .   ? 31.11846  30.66773  22.88755  1.000 29.42912  ? 326 HOH   D O     1 
HETATM 5830 O  O     . HOH   N 6 .   ? 36.60785  31.31785  21.31832  1.000 38.99120  ? 327 HOH   D O     1 
HETATM 5831 O  O     . HOH   N 6 .   ? 26.22576  54.66659  4.52311   1.000 35.42606  ? 328 HOH   D O     1 
HETATM 5832 O  O     . HOH   N 6 .   ? 18.09657  44.81336  -3.09503  1.000 35.20489  ? 329 HOH   D O     1 
HETATM 5833 O  O     . HOH   N 6 .   ? 31.59398  33.04037  3.44333   1.000 23.28840  ? 330 HOH   D O     1 
HETATM 5834 O  O     . HOH   N 6 .   ? 7.19801   40.93047  21.94603  1.000 40.89125  ? 331 HOH   D O     1 
HETATM 5835 O  O     . HOH   N 6 .   ? 13.22290  53.71872  7.19697   1.000 44.79383  ? 332 HOH   D O     1 
HETATM 5836 O  O     . HOH   N 6 .   ? 31.45821  48.16112  -1.42423  1.000 39.64567  ? 333 HOH   D O     1 
HETATM 5837 O  O     . HOH   N 6 .   ? 14.16909  52.94736  14.97636  1.000 44.41573  ? 334 HOH   D O     1 
HETATM 5838 O  O     . HOH   N 6 .   ? 32.43896  36.98682  -0.08023  1.000 21.81216  ? 335 HOH   D O     1 
HETATM 5839 O  O     . HOH   N 6 .   ? 8.52488   44.86458  7.71444   1.000 40.33473  ? 336 HOH   D O     1 
HETATM 5840 O  O     . HOH   N 6 .   ? 13.68428  29.72002  14.58277  1.000 28.90155  ? 337 HOH   D O     1 
HETATM 5841 O  O     . HOH   N 6 .   ? 27.06412  40.22927  1.67844   1.000 28.04896  ? 338 HOH   D O     1 
HETATM 5842 O  O     . HOH   N 6 .   ? 34.22917  29.19218  2.46293   1.000 29.55594  ? 339 HOH   D O     1 
HETATM 5843 O  O     . HOH   N 6 .   ? 31.86362  54.02996  8.52294   1.000 47.18521  ? 340 HOH   D O     1 
HETATM 5844 O  O     . HOH   N 6 .   ? 41.98948  48.44419  1.59673   1.000 46.33440  ? 341 HOH   D O     1 
HETATM 5845 O  O     . HOH   N 6 .   ? 16.08994  31.55514  26.79255  1.000 33.91661  ? 342 HOH   D O     1 
HETATM 5846 O  O     . HOH   N 6 .   ? 28.29611  34.10016  -8.77895  1.000 34.42882  ? 343 HOH   D O     1 
HETATM 5847 O  O     . HOH   N 6 .   ? 20.21741  37.00454  -7.56345  1.000 37.03240  ? 344 HOH   D O     1 
HETATM 5848 O  O     . HOH   N 6 .   ? 37.44630  39.66525  5.05133   1.000 25.60850  ? 345 HOH   D O     1 
HETATM 5849 O  O     . HOH   N 6 .   ? 30.54071  36.61243  24.66968  1.000 34.92878  ? 346 HOH   D O     1 
HETATM 5850 O  O     . HOH   N 6 .   ? 14.12769  30.51695  23.89971  1.000 30.08735  ? 347 HOH   D O     1 
HETATM 5851 O  O     . HOH   N 6 .   ? 24.52796  51.51188  21.05408  1.000 42.78705  ? 348 HOH   D O     1 
HETATM 5852 O  O     . HOH   N 6 .   ? 19.08895  37.80266  25.97721  1.000 30.80870  ? 349 HOH   D O     1 
HETATM 5853 O  O     . HOH   N 6 .   ? 7.74860   40.49114  8.32474   1.000 44.01407  ? 350 HOH   D O     1 
HETATM 5854 O  O     . HOH   N 6 .   ? 13.10184  35.10203  7.05426   1.000 32.48604  ? 351 HOH   D O     1 
HETATM 5855 O  O     . HOH   N 6 .   ? 29.79995  44.90059  -6.35656  1.000 40.00256  ? 352 HOH   D O     1 
HETATM 5856 O  O     . HOH   N 6 .   ? 16.89443  38.15886  8.46694   1.000 27.00691  ? 353 HOH   D O     1 
HETATM 5857 O  O     . HOH   N 6 .   ? 23.57865  47.66390  -6.02315  1.000 51.14501  ? 354 HOH   D O     1 
HETATM 5858 O  O     . HOH   N 6 .   ? 13.50237  28.11215  21.39359  1.000 25.81834  ? 355 HOH   D O     1 
HETATM 5859 O  O     . HOH   N 6 .   ? 36.78632  30.01092  -1.16465  1.000 29.04288  ? 356 HOH   D O     1 
HETATM 5860 O  O     . HOH   N 6 .   ? 29.52484  30.88568  -6.29221  1.000 37.24409  ? 357 HOH   D O     1 
HETATM 5861 O  O     . HOH   N 6 .   ? 12.88573  45.78610  -1.84131  1.000 43.64260  ? 358 HOH   D O     1 
HETATM 5862 O  O     . HOH   N 6 .   ? 35.42776  22.18264  19.90292  1.000 34.74364  ? 359 HOH   D O     1 
HETATM 5863 O  O     . HOH   N 6 .   ? 27.67732  39.08088  23.39411  1.000 35.15960  ? 360 HOH   D O     1 
HETATM 5864 O  O     . HOH   N 6 .   ? 11.30685  38.82524  1.12232   1.000 31.69931  ? 361 HOH   D O     1 
HETATM 5865 O  O     . HOH   N 6 .   ? 12.25370  48.09322  16.40304  1.000 40.84301  ? 362 HOH   D O     1 
HETATM 5866 O  O     . HOH   N 6 .   ? 15.37173  23.80724  20.51794  1.000 34.60934  ? 363 HOH   D O     1 
HETATM 5867 O  O     . HOH   N 6 .   ? 41.05927  43.51835  0.30960   1.000 36.08682  ? 364 HOH   D O     1 
HETATM 5868 O  O     . HOH   N 6 .   ? 34.29879  42.29462  19.74200  1.000 35.14500  ? 365 HOH   D O     1 
HETATM 5869 O  O     . HOH   N 6 .   ? 15.59537  40.22700  25.80953  1.000 29.21989  ? 366 HOH   D O     1 
HETATM 5870 O  O     . HOH   N 6 .   ? 16.21049  34.01892  7.91101   1.000 24.28937  ? 367 HOH   D O     1 
HETATM 5871 O  O     . HOH   N 6 .   ? 11.03259  39.51954  3.67193   1.000 36.22533  ? 368 HOH   D O     1 
HETATM 5872 O  O     . HOH   N 6 .   ? 22.78335  34.56476  26.38902  1.000 27.50437  ? 369 HOH   D O     1 
HETATM 5873 O  O     . HOH   N 6 .   ? 36.89421  37.17239  6.31825   1.000 22.51247  ? 370 HOH   D O     1 
HETATM 5874 O  O     . HOH   N 6 .   ? 40.90462  30.22822  4.02247   1.000 33.43049  ? 371 HOH   D O     1 
HETATM 5875 O  O     . HOH   N 6 .   ? 32.20333  26.95133  5.36304   1.000 38.70697  ? 372 HOH   D O     1 
HETATM 5876 O  O     . HOH   N 6 .   ? 18.30030  56.16311  6.88828   1.000 48.30357  ? 373 HOH   D O     1 
HETATM 5877 O  O     . HOH   N 6 .   ? 12.75863  34.13314  14.80488  1.000 24.85991  ? 374 HOH   D O     1 
HETATM 5878 O  O     . HOH   N 6 .   ? 19.87877  50.21364  22.35915  1.000 38.13389  ? 375 HOH   D O     1 
HETATM 5879 O  O     . HOH   N 6 .   ? 11.92585  42.58832  1.50439   1.000 36.10958  ? 376 HOH   D O     1 
HETATM 5880 O  O     . HOH   N 6 .   ? 34.05607  26.59186  -5.49185  1.000 40.09894  ? 377 HOH   D O     1 
HETATM 5881 O  O     . HOH   N 6 .   ? 37.47973  34.54848  8.16631   1.000 23.05792  ? 378 HOH   D O     1 
HETATM 5882 O  O     . HOH   N 6 .   ? 9.99772   31.46156  15.89614  1.000 32.78906  ? 379 HOH   D O     1 
HETATM 5883 O  O     . HOH   N 6 .   ? 34.36114  35.77285  23.20979  1.000 37.15122  ? 380 HOH   D O     1 
HETATM 5884 O  O     . HOH   N 6 .   ? 20.61443  42.19626  -8.22601  1.000 48.65463  ? 381 HOH   D O     1 
HETATM 5885 O  O     . HOH   N 6 .   ? 2.33634   42.06416  16.89762  1.000 49.64164  ? 382 HOH   D O     1 
HETATM 5886 O  O     . HOH   N 6 .   ? 33.73578  48.51952  13.34909  1.000 53.16880  ? 383 HOH   D O     1 
HETATM 5887 O  O     . HOH   N 6 .   ? 42.14382  32.19422  9.15893   1.000 40.54099  ? 384 HOH   D O     1 
HETATM 5888 O  O     . HOH   N 6 .   ? 37.16784  28.41162  2.87854   1.000 35.30695  ? 385 HOH   D O     1 
HETATM 5889 O  O     . HOH   N 6 .   ? 18.03691  53.01210  2.78410   1.000 32.60050  ? 386 HOH   D O     1 
HETATM 5890 O  O     . HOH   N 6 .   ? 14.04892  50.17361  16.47479  1.000 39.03972  ? 387 HOH   D O     1 
HETATM 5891 O  O     . HOH   N 6 .   ? 38.37557  48.55455  8.06239   1.000 48.87050  ? 388 HOH   D O     1 
HETATM 5892 O  O     . HOH   N 6 .   ? 25.00650  48.41360  23.08491  1.000 37.83115  ? 389 HOH   D O     1 
HETATM 5893 O  O     . HOH   N 6 .   ? 20.53051  43.67780  26.38251  1.000 28.73446  ? 390 HOH   D O     1 
HETATM 5894 O  O     . HOH   N 6 .   ? 10.74469  41.32022  -2.64799  1.000 41.56872  ? 391 HOH   D O     1 
HETATM 5895 O  O     . HOH   N 6 .   ? 22.01558  31.22347  -2.14894  1.000 36.54125  ? 392 HOH   D O     1 
HETATM 5896 O  O     . HOH   N 6 .   ? 27.54580  20.46893  21.56565  1.000 39.24514  ? 393 HOH   D O     1 
HETATM 5897 O  O     . HOH   N 6 .   ? 45.46886  35.33632  8.22162   1.000 34.04906  ? 394 HOH   D O     1 
HETATM 5898 O  O     . HOH   N 6 .   ? 30.77779  26.34951  9.10575   1.000 29.03570  ? 395 HOH   D O     1 
HETATM 5899 O  O     . HOH   N 6 .   ? 40.14826  38.16437  19.61180  1.000 41.19159  ? 396 HOH   D O     1 
HETATM 5900 O  O     . HOH   N 6 .   ? 10.14477  43.73997  21.80207  1.000 36.93131  ? 397 HOH   D O     1 
HETATM 5901 O  O     . HOH   N 6 .   ? 20.38488  27.95864  8.32119   1.000 26.43834  ? 398 HOH   D O     1 
HETATM 5902 O  O     . HOH   N 6 .   ? 39.80397  28.65871  11.56887  1.000 40.81834  ? 399 HOH   D O     1 
HETATM 5903 O  O     . HOH   N 6 .   ? 40.55274  40.61353  11.89172  1.000 31.60713  ? 400 HOH   D O     1 
HETATM 5904 O  O     . HOH   N 6 .   ? 12.57308  40.55732  -0.57538  1.000 30.79386  ? 401 HOH   D O     1 
HETATM 5905 O  O     . HOH   N 6 .   ? 39.89367  40.90148  -1.98554  1.000 35.74121  ? 402 HOH   D O     1 
HETATM 5906 O  O     . HOH   N 6 .   ? 31.30916  24.39435  -2.41109  1.000 40.76084  ? 403 HOH   D O     1 
HETATM 5907 O  O     . HOH   N 6 .   ? 24.99344  31.15716  -8.09133  1.000 30.78932  ? 404 HOH   D O     1 
HETATM 5908 O  O     . HOH   N 6 .   ? 18.39166  25.32673  24.89657  1.000 31.18980  ? 405 HOH   D O     1 
HETATM 5909 O  O     . HOH   N 6 .   ? 15.29357  45.41561  2.42808   1.000 31.63131  ? 406 HOH   D O     1 
HETATM 5910 O  O     . HOH   N 6 .   ? 26.77371  49.01596  20.53790  1.000 34.33739  ? 407 HOH   D O     1 
HETATM 5911 O  O     . HOH   N 6 .   ? 37.78464  41.52087  12.24309  1.000 36.82126  ? 408 HOH   D O     1 
HETATM 5912 O  O     . HOH   N 6 .   ? 20.06312  55.39860  13.59491  1.000 45.43046  ? 409 HOH   D O     1 
HETATM 5913 O  O     . HOH   N 6 .   ? 35.44889  38.19592  -5.30015  1.000 34.28230  ? 410 HOH   D O     1 
HETATM 5914 O  O     . HOH   N 6 .   ? 29.49860  36.89221  -9.04004  1.000 41.71690  ? 411 HOH   D O     1 
HETATM 5915 O  O     . HOH   N 6 .   ? 39.10652  26.74216  17.33039  1.000 46.69521  ? 412 HOH   D O     1 
HETATM 5916 O  O     . HOH   N 6 .   ? 33.64898  36.43494  16.40254  1.000 25.95503  ? 413 HOH   D O     1 
HETATM 5917 O  O     . HOH   N 6 .   ? 17.42240  29.02269  25.79891  1.000 34.06026  ? 414 HOH   D O     1 
HETATM 5918 O  O     . HOH   N 6 .   ? 17.71828  23.21277  21.55673  1.000 32.83362  ? 415 HOH   D O     1 
HETATM 5919 O  O     . HOH   N 6 .   ? 24.59309  54.30653  13.70708  1.000 51.32067  ? 416 HOH   D O     1 
HETATM 5920 O  O     . HOH   N 6 .   ? 21.91167  32.60250  1.73847   1.000 27.36227  ? 417 HOH   D O     1 
HETATM 5921 O  O     . HOH   N 6 .   ? 12.84068  34.08110  26.54021  1.000 40.39388  ? 418 HOH   D O     1 
HETATM 5922 O  O     . HOH   N 6 .   ? 29.26638  25.88946  6.05066   1.000 34.88665  ? 419 HOH   D O     1 
HETATM 5923 O  O     . HOH   N 6 .   ? 41.56756  29.51914  13.87863  1.000 47.51321  ? 420 HOH   D O     1 
HETATM 5924 O  O     . HOH   N 6 .   ? 13.08858  27.99464  10.40240  1.000 49.57550  ? 421 HOH   D O     1 
HETATM 5925 O  O     . HOH   N 6 .   ? 33.65219  26.82578  3.34010   1.000 37.88313  ? 422 HOH   D O     1 
HETATM 5926 O  O     . HOH   N 6 .   ? 7.94936   43.96734  5.20467   1.000 41.15681  ? 423 HOH   D O     1 
HETATM 5927 O  O     . HOH   N 6 .   ? 27.33426  53.79547  -0.40751  1.000 40.70877  ? 424 HOH   D O     1 
HETATM 5928 O  O     . HOH   N 6 .   ? 13.35338  44.40334  0.52905   1.000 34.76409  ? 425 HOH   D O     1 
HETATM 5929 O  O     . HOH   N 6 .   ? 11.99090  30.40462  10.71229  1.000 47.99249  ? 426 HOH   D O     1 
HETATM 5930 O  O     . HOH   N 6 .   ? 14.36369  54.82623  9.16515   1.000 50.85121  ? 427 HOH   D O     1 
HETATM 5931 O  O     . HOH   N 6 .   ? 14.44273  47.82922  2.80997   1.000 39.80207  ? 428 HOH   D O     1 
HETATM 5932 O  O     . HOH   N 6 .   ? 16.85182  56.07877  9.38131   1.000 45.83126  ? 429 HOH   D O     1 
HETATM 5933 O  O     . HOH   N 6 .   ? 23.90684  51.34135  23.86592  1.000 42.51149  ? 430 HOH   D O     1 
HETATM 5934 O  O     . HOH   N 6 .   ? 19.09092  34.67912  -8.12005  1.000 40.81785  ? 431 HOH   D O     1 
HETATM 5935 O  O     . HOH   N 6 .   ? 9.14665   40.25899  23.84343  1.000 45.71771  ? 432 HOH   D O     1 
HETATM 5936 O  O     . HOH   N 6 .   ? 7.83132   46.91855  14.92008  1.000 43.94505  ? 433 HOH   D O     1 
HETATM 5937 O  O     . HOH   N 6 .   ? 44.92885  32.71859  7.29965   1.000 39.65745  ? 434 HOH   D O     1 
HETATM 5938 O  O     . HOH   N 6 .   ? 20.04784  41.07412  27.23771  1.000 37.15207  ? 435 HOH   D O     1 
HETATM 5939 O  O     . HOH   N 6 .   ? 21.73872  53.79231  14.41087  1.000 43.40879  ? 436 HOH   D O     1 
HETATM 5940 O  O     . HOH   N 6 .   ? 39.60677  46.25474  -1.78436  1.000 46.73139  ? 437 HOH   D O     1 
HETATM 5941 O  O     . HOH   N 6 .   ? 10.92778  27.16827  20.99263  1.000 36.53490  ? 438 HOH   D O     1 
HETATM 5942 O  O     . HOH   N 6 .   ? 6.99923   44.63113  13.03665  1.000 41.50917  ? 439 HOH   D O     1 
HETATM 5943 O  O     . HOH   N 6 .   ? 22.24398  30.60036  0.24771   1.000 44.39088  ? 440 HOH   D O     1 
HETATM 5944 O  O     . HOH   N 6 .   ? 42.56046  29.89398  8.45036   1.000 47.81265  ? 441 HOH   D O     1 
HETATM 5945 O  O     . HOH   N 6 .   ? 6.44865   38.73363  13.43708  1.000 37.35805  ? 442 HOH   D O     1 
HETATM 5946 O  O     . HOH   N 6 .   ? 26.08278  15.86028  22.93748  1.000 42.14256  ? 443 HOH   D O     1 
HETATM 5947 O  O     . HOH   N 6 .   ? 40.53142  27.50524  15.25701  1.000 41.60434  ? 444 HOH   D O     1 
HETATM 5948 O  O     . HOH   N 6 .   ? 42.49457  31.86701  6.47300   1.000 40.15498  ? 445 HOH   D O     1 
HETATM 5949 O  O     . HOH   N 6 .   ? 43.34008  32.12705  11.09366  1.000 48.14638  ? 446 HOH   D O     1 
HETATM 5950 O  O     . HOH   N 6 .   ? 27.50084  30.17782  -7.79958  1.000 40.08283  ? 447 HOH   D O     1 
HETATM 5951 O  O     . HOH   N 6 .   ? 12.81529  29.44749  25.66081  1.000 35.70235  ? 448 HOH   D O     1 
HETATM 5952 O  O     . HOH   N 6 .   ? 29.72449  40.73236  25.49589  1.000 37.78724  ? 449 HOH   D O     1 
HETATM 5953 O  O     . HOH   N 6 .   ? 38.33862  46.65167  9.38987   1.000 48.53821  ? 450 HOH   D O     1 
HETATM 5954 O  O     . HOH   N 6 .   ? 29.15879  51.79319  -0.97128  1.000 44.24957  ? 451 HOH   D O     1 
HETATM 5955 O  O     . HOH   N 6 .   ? 22.25128  16.96860  24.91992  1.000 43.88089  ? 452 HOH   D O     1 
HETATM 5956 O  O     . HOH   N 6 .   ? 12.57290  49.23384  2.11926   1.000 48.39440  ? 453 HOH   D O     1 
HETATM 5957 O  O     . HOH   N 6 .   ? 4.18747   43.72049  23.67582  1.000 47.54417  ? 454 HOH   D O     1 
HETATM 5958 O  O     . HOH   N 6 .   ? 9.60813   43.82664  1.26605   1.000 42.37949  ? 455 HOH   D O     1 
HETATM 5959 O  O     . HOH   N 6 .   ? 16.043    53.809    16.908    1.000 44.14178  ? 456 HOH   D O     1 
HETATM 5960 O  O     . HOH   N 6 .   ? 7.00231   41.38764  5.81118   1.000 48.25849  ? 457 HOH   D O     1 
HETATM 5961 O  O     . HOH   N 6 .   ? 17.47858  40.60259  27.59977  1.000 42.80087  ? 458 HOH   D O     1 
HETATM 5962 O  O     A HOH   N 6 .   ? 41.49691  36.15550  16.61504  0.500 38.37230  ? 459 HOH   D O     1 
HETATM 5963 O  O     B HOH   N 6 .   ? 42.39417  37.52114  15.23305  0.500 38.37230  ? 459 HOH   D O     1 
HETATM 5964 O  O     . HOH   N 6 .   ? 10.12828  49.72737  11.77643  1.000 55.61889  ? 460 HOH   D O     1 
HETATM 5965 O  O     . HOH   N 6 .   ? 39.89755  25.71663  13.81733  1.000 46.16923  ? 461 HOH   D O     1 
HETATM 5966 O  O     . HOH   N 6 .   ? 37.60967  27.88516  0.42646   1.000 40.96853  ? 462 HOH   D O     1 
HETATM 5967 O  O     . HOH   N 6 .   ? 17.42594  23.01295  24.45642  1.000 52.19679  ? 463 HOH   D O     1 
HETATM 5968 O  O     . HOH   N 6 .   ? 8.89268   38.48647  0.07422   1.000 49.31645  ? 464 HOH   D O     1 
HETATM 5969 O  O     . HOH   N 6 .   ? 39.59074  44.16931  -2.90446  1.000 41.72072  ? 465 HOH   D O     1 
HETATM 5970 O  O     . HOH   N 6 .   ? 13.78069  26.84772  23.77946  1.000 39.11125  ? 466 HOH   D O     1 
HETATM 5971 O  O     A HOH   N 6 .   ? 25.13789  39.28770  27.18264  0.500 38.65230  ? 467 HOH   D O     1 
HETATM 5972 O  O     B HOH   N 6 .   ? 25.86144  38.50259  25.38630  0.500 38.65230  ? 467 HOH   D O     1 
HETATM 5973 O  O     . HOH   N 6 .   ? 7.61505   42.84388  9.07541   1.000 45.55736  ? 468 HOH   D O     1 
HETATM 5974 O  O     . HOH   N 6 .   ? 11.92653  28.10259  13.25400  1.000 42.32658  ? 469 HOH   D O     1 
HETATM 5975 O  O     . HOH   N 6 .   ? 36.89931  34.95393  23.80075  1.000 45.40234  ? 470 HOH   D O     1 
HETATM 5976 O  O     . HOH   N 6 .   ? 9.97383   48.59395  14.97970  1.000 41.81421  ? 471 HOH   D O     1 
HETATM 5977 O  O     . HOH   N 6 .   ? 42.43718  39.47338  13.74664  1.000 35.67737  ? 472 HOH   D O     1 
HETATM 5978 O  O     . HOH   N 6 .   ? 35.57572  49.21458  -4.13835  1.000 46.50598  ? 473 HOH   D O     1 
HETATM 5979 O  O     . HOH   N 6 .   ? 33.05124  21.79804  23.81216  1.000 44.69777  ? 474 HOH   D O     1 
HETATM 5980 O  O     . HOH   N 6 .   ? 9.29083   27.33704  23.27312  1.000 53.02022  ? 475 HOH   D O     1 
# 
