data_9BGC
# 
_entry.id   9BGC 
# 
_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   9BGC         pdb_00009bgc 10.2210/pdb9bgc/pdb 
WWPDB D_1000283247 ?            ?                   
# 
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                        9BGC 
_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 ?                   
'Bar Ziv, T.'       3 0009-0008-1751-8507 
'Chen, A.'          4 0000-0002-3259-5868 
'Knox, J.E.'        5 ?                   
'Yano, J.K.'        6 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' 19458.979 2   3.6.5.2 G12R ? ? 
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 syn 'MAGNESIUM ION' 24.305    2   ?       ?    ? ? 
5 non-polymer nat 
;(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    418 ?       ?    ? ? 
# 
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 
;SMTEYKLVVVGARGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
;SMTEYKLVVVGARGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
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  ARG n 
1 14  GLY 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  ARG 13  12  12  ARG ARG A . n 
A 1 14  GLY 14  13  13  GLY GLY 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 ?   ?   ?   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  ARG 13  12  12  ARG ARG B . n 
B 1 14  GLY 14  13  13  GLY GLY 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 ?   ?   ?   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 166 165 165 GLU GLU 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 45   HOH   HOH A . 
K 6 HOH   2   302 247  HOH   HOH A . 
K 6 HOH   3   303 1    HOH   HOH A . 
K 6 HOH   4   304 307  HOH   HOH A . 
K 6 HOH   5   305 195  HOH   HOH A . 
K 6 HOH   6   306 184  HOH   HOH A . 
K 6 HOH   7   307 277  HOH   HOH A . 
K 6 HOH   8   308 33   HOH   HOH A . 
K 6 HOH   9   309 417  HOH   HOH A . 
K 6 HOH   10  310 85   HOH   HOH A . 
K 6 HOH   11  311 24   HOH   HOH A . 
K 6 HOH   12  312 101  HOH   HOH A . 
K 6 HOH   13  313 367  HOH   HOH A . 
K 6 HOH   14  314 30   HOH   HOH A . 
K 6 HOH   15  315 258  HOH   HOH A . 
K 6 HOH   16  316 103  HOH   HOH A . 
K 6 HOH   17  317 35   HOH   HOH A . 
K 6 HOH   18  318 111  HOH   HOH A . 
K 6 HOH   19  319 338  HOH   HOH A . 
K 6 HOH   20  320 438  HOH   HOH A . 
K 6 HOH   21  321 72   HOH   HOH A . 
K 6 HOH   22  322 200  HOH   HOH A . 
K 6 HOH   23  323 84   HOH   HOH A . 
K 6 HOH   24  324 62   HOH   HOH A . 
K 6 HOH   25  325 92   HOH   HOH A . 
K 6 HOH   26  326 444  HOH   HOH A . 
K 6 HOH   27  327 232  HOH   HOH A . 
K 6 HOH   28  328 296  HOH   HOH A . 
K 6 HOH   29  329 8    HOH   HOH A . 
K 6 HOH   30  330 179  HOH   HOH A . 
K 6 HOH   31  331 113  HOH   HOH A . 
K 6 HOH   32  332 90   HOH   HOH A . 
K 6 HOH   33  333 405  HOH   HOH A . 
K 6 HOH   34  334 288  HOH   HOH A . 
K 6 HOH   35  335 50   HOH   HOH A . 
K 6 HOH   36  336 230  HOH   HOH A . 
K 6 HOH   37  337 81   HOH   HOH A . 
K 6 HOH   38  338 142  HOH   HOH A . 
K 6 HOH   39  339 225  HOH   HOH A . 
K 6 HOH   40  340 220  HOH   HOH A . 
K 6 HOH   41  341 10   HOH   HOH A . 
K 6 HOH   42  342 132  HOH   HOH A . 
K 6 HOH   43  343 53   HOH   HOH A . 
K 6 HOH   44  344 383  HOH   HOH A . 
K 6 HOH   45  345 51   HOH   HOH A . 
K 6 HOH   46  346 375  HOH   HOH A . 
K 6 HOH   47  347 12   HOH   HOH A . 
K 6 HOH   48  348 340  HOH   HOH A . 
K 6 HOH   49  349 378  HOH   HOH A . 
K 6 HOH   50  350 2    HOH   HOH A . 
K 6 HOH   51  351 445  HOH   HOH A . 
K 6 HOH   52  352 396  HOH   HOH A . 
K 6 HOH   53  353 209  HOH   HOH A . 
K 6 HOH   54  354 207  HOH   HOH A . 
K 6 HOH   55  355 58   HOH   HOH A . 
K 6 HOH   56  356 318  HOH   HOH A . 
K 6 HOH   57  357 107  HOH   HOH A . 
K 6 HOH   58  358 18   HOH   HOH A . 
K 6 HOH   59  359 366  HOH   HOH A . 
K 6 HOH   60  360 320  HOH   HOH A . 
K 6 HOH   61  361 95   HOH   HOH A . 
K 6 HOH   62  362 239  HOH   HOH A . 
K 6 HOH   63  363 67   HOH   HOH A . 
K 6 HOH   64  364 119  HOH   HOH A . 
K 6 HOH   65  365 319  HOH   HOH A . 
K 6 HOH   66  366 20   HOH   HOH A . 
K 6 HOH   67  367 317  HOH   HOH A . 
K 6 HOH   68  368 161  HOH   HOH A . 
K 6 HOH   69  369 291  HOH   HOH A . 
K 6 HOH   70  370 100  HOH   HOH A . 
K 6 HOH   71  371 371  HOH   HOH A . 
K 6 HOH   72  372 175  HOH   HOH A . 
K 6 HOH   73  373 173  HOH   HOH A . 
K 6 HOH   74  374 41   HOH   HOH A . 
K 6 HOH   75  375 356  HOH   HOH A . 
K 6 HOH   76  376 348  HOH   HOH A . 
K 6 HOH   77  377 355  HOH   HOH A . 
K 6 HOH   78  378 224  HOH   HOH A . 
K 6 HOH   79  379 365  HOH   HOH A . 
K 6 HOH   80  380 261  HOH   HOH A . 
K 6 HOH   81  381 420  HOH   HOH A . 
K 6 HOH   82  382 158  HOH   HOH A . 
K 6 HOH   83  383 425  HOH   HOH A . 
K 6 HOH   84  384 271  HOH   HOH A . 
K 6 HOH   85  385 361  HOH   HOH A . 
K 6 HOH   86  386 214  HOH   HOH A . 
K 6 HOH   87  387 205  HOH   HOH A . 
K 6 HOH   88  388 294  HOH   HOH A . 
K 6 HOH   89  389 233  HOH   HOH A . 
K 6 HOH   90  390 104  HOH   HOH A . 
K 6 HOH   91  391 428  HOH   HOH A . 
K 6 HOH   92  392 193  HOH   HOH A . 
K 6 HOH   93  393 7    HOH   HOH A . 
K 6 HOH   94  394 223  HOH   HOH A . 
K 6 HOH   95  395 443  HOH   HOH A . 
K 6 HOH   96  396 185  HOH   HOH A . 
K 6 HOH   97  397 315  HOH   HOH A . 
K 6 HOH   98  398 197  HOH   HOH A . 
K 6 HOH   99  399 308  HOH   HOH A . 
K 6 HOH   100 400 324  HOH   HOH A . 
K 6 HOH   101 401 414  HOH   HOH A . 
K 6 HOH   102 402 170  HOH   HOH A . 
K 6 HOH   103 403 182  HOH   HOH A . 
K 6 HOH   104 404 429  HOH   HOH A . 
K 6 HOH   105 405 427  HOH   HOH A . 
K 6 HOH   106 406 382  HOH   HOH A . 
K 6 HOH   107 407 278  HOH   HOH A . 
K 6 HOH   108 408 165  HOH   HOH A . 
K 6 HOH   109 409 145  HOH   HOH A . 
K 6 HOH   110 410 221  HOH   HOH A . 
K 6 HOH   111 411 403  HOH   HOH A . 
L 6 HOH   1   301 149  HOH   HOH B . 
L 6 HOH   2   302 148  HOH   HOH B . 
L 6 HOH   3   303 38   HOH   HOH B . 
L 6 HOH   4   304 297  HOH   HOH B . 
L 6 HOH   5   305 264  HOH   HOH B . 
L 6 HOH   6   306 260  HOH   HOH B . 
L 6 HOH   7   307 188  HOH   HOH B . 
L 6 HOH   8   308 125  HOH   HOH B . 
L 6 HOH   9   309 3    HOH   HOH B . 
L 6 HOH   10  310 156  HOH   HOH B . 
L 6 HOH   11  311 26   HOH   HOH B . 
L 6 HOH   12  312 360  HOH   HOH B . 
L 6 HOH   13  313 346  HOH   HOH B . 
L 6 HOH   14  314 68   HOH   HOH B . 
L 6 HOH   15  315 143  HOH   HOH B . 
L 6 HOH   16  316 69   HOH   HOH B . 
L 6 HOH   17  317 4    HOH   HOH B . 
L 6 HOH   18  318 55   HOH   HOH B . 
L 6 HOH   19  319 59   HOH   HOH B . 
L 6 HOH   20  320 301  HOH   HOH B . 
L 6 HOH   21  321 146  HOH   HOH B . 
L 6 HOH   22  322 280  HOH   HOH B . 
L 6 HOH   23  323 153  HOH   HOH B . 
L 6 HOH   24  324 231  HOH   HOH B . 
L 6 HOH   25  325 282  HOH   HOH B . 
L 6 HOH   26  326 273  HOH   HOH B . 
L 6 HOH   27  327 54   HOH   HOH B . 
L 6 HOH   28  328 137  HOH   HOH B . 
L 6 HOH   29  329 431  HOH   HOH B . 
L 6 HOH   30  330 115  HOH   HOH B . 
L 6 HOH   31  331 65   HOH   HOH B . 
L 6 HOH   32  332 139  HOH   HOH B . 
L 6 HOH   33  333 380  HOH   HOH B . 
L 6 HOH   34  334 328  HOH   HOH B . 
L 6 HOH   35  335 66   HOH   HOH B . 
L 6 HOH   36  336 423  HOH   HOH B . 
L 6 HOH   37  337 163  HOH   HOH B . 
L 6 HOH   38  338 74   HOH   HOH B . 
L 6 HOH   39  339 452  HOH   HOH B . 
L 6 HOH   40  340 154  HOH   HOH B . 
L 6 HOH   41  341 216  HOH   HOH B . 
L 6 HOH   42  342 381  HOH   HOH B . 
L 6 HOH   43  343 364  HOH   HOH B . 
L 6 HOH   44  344 256  HOH   HOH B . 
L 6 HOH   45  345 334  HOH   HOH B . 
L 6 HOH   46  346 190  HOH   HOH B . 
L 6 HOH   47  347 305  HOH   HOH B . 
L 6 HOH   48  348 450  HOH   HOH B . 
L 6 HOH   49  349 286  HOH   HOH B . 
L 6 HOH   50  350 331  HOH   HOH B . 
L 6 HOH   51  351 56   HOH   HOH B . 
L 6 HOH   52  352 295  HOH   HOH B . 
L 6 HOH   53  353 79   HOH   HOH B . 
L 6 HOH   54  354 199  HOH   HOH B . 
L 6 HOH   55  355 250  HOH   HOH B . 
L 6 HOH   56  356 339  HOH   HOH B . 
L 6 HOH   57  357 141  HOH   HOH B . 
L 6 HOH   58  358 451  HOH   HOH B . 
L 6 HOH   59  359 402  HOH   HOH B . 
L 6 HOH   60  360 313  HOH   HOH B . 
L 6 HOH   61  361 293  HOH   HOH B . 
L 6 HOH   62  362 9    HOH   HOH B . 
L 6 HOH   63  363 186  HOH   HOH B . 
L 6 HOH   64  364 399  HOH   HOH B . 
L 6 HOH   65  365 404  HOH   HOH B . 
L 6 HOH   66  366 211  HOH   HOH B . 
L 6 HOH   67  367 162  HOH   HOH B . 
L 6 HOH   68  368 304  HOH   HOH B . 
L 6 HOH   69  369 323  HOH   HOH B . 
L 6 HOH   70  370 369  HOH   HOH B . 
L 6 HOH   71  371 133  HOH   HOH B . 
L 6 HOH   72  372 238  HOH   HOH B . 
L 6 HOH   73  373 412  HOH   HOH B . 
L 6 HOH   74  374 275  HOH   HOH B . 
L 6 HOH   75  375 347  HOH   HOH B . 
L 6 HOH   76  376 351  HOH   HOH B . 
L 6 HOH   77  377 302  HOH   HOH B . 
L 6 HOH   78  378 447  HOH   HOH B . 
L 6 HOH   79  379 192  HOH   HOH B . 
L 6 HOH   80  380 236  HOH   HOH B . 
M 6 HOH   1   301 377  HOH   HOH C . 
M 6 HOH   2   302 37   HOH   HOH C . 
M 6 HOH   3   303 353  HOH   HOH C . 
M 6 HOH   4   304 172  HOH   HOH C . 
M 6 HOH   5   305 110  HOH   HOH C . 
M 6 HOH   6   306 181  HOH   HOH C . 
M 6 HOH   7   307 13   HOH   HOH C . 
M 6 HOH   8   308 136  HOH   HOH C . 
M 6 HOH   9   309 180  HOH   HOH C . 
M 6 HOH   10  310 129  HOH   HOH C . 
M 6 HOH   11  311 298  HOH   HOH C . 
M 6 HOH   12  312 306  HOH   HOH C . 
M 6 HOH   13  313 166  HOH   HOH C . 
M 6 HOH   14  314 114  HOH   HOH C . 
M 6 HOH   15  315 171  HOH   HOH C . 
M 6 HOH   16  316 357  HOH   HOH C . 
M 6 HOH   17  317 164  HOH   HOH C . 
M 6 HOH   18  318 235  HOH   HOH C . 
M 6 HOH   19  319 40   HOH   HOH C . 
M 6 HOH   20  320 138  HOH   HOH C . 
M 6 HOH   21  321 219  HOH   HOH C . 
M 6 HOH   22  322 17   HOH   HOH C . 
M 6 HOH   23  323 265  HOH   HOH C . 
M 6 HOH   24  324 454  HOH   HOH C . 
M 6 HOH   25  325 135  HOH   HOH C . 
M 6 HOH   26  326 120  HOH   HOH C . 
M 6 HOH   27  327 326  HOH   HOH C . 
M 6 HOH   28  328 187  HOH   HOH C . 
M 6 HOH   29  329 322  HOH   HOH C . 
M 6 HOH   30  330 48   HOH   HOH C . 
M 6 HOH   31  331 358  HOH   HOH C . 
M 6 HOH   32  332 112  HOH   HOH C . 
M 6 HOH   33  333 82   HOH   HOH C . 
M 6 HOH   34  334 96   HOH   HOH C . 
M 6 HOH   35  335 176  HOH   HOH C . 
M 6 HOH   36  336 123  HOH   HOH C . 
M 6 HOH   37  337 433  HOH   HOH C . 
M 6 HOH   38  338 208  HOH   HOH C . 
M 6 HOH   39  339 202  HOH   HOH C . 
M 6 HOH   40  340 263  HOH   HOH C . 
M 6 HOH   41  341 453  HOH   HOH C . 
M 6 HOH   42  342 121  HOH   HOH C . 
M 6 HOH   43  343 47   HOH   HOH C . 
M 6 HOH   44  344 196  HOH   HOH C . 
M 6 HOH   45  345 83   HOH   HOH C . 
M 6 HOH   46  346 262  HOH   HOH C . 
M 6 HOH   47  347 64   HOH   HOH C . 
M 6 HOH   48  348 189  HOH   HOH C . 
M 6 HOH   49  349 76   HOH   HOH C . 
M 6 HOH   50  350 25   HOH   HOH C . 
M 6 HOH   51  351 394  HOH   HOH C . 
M 6 HOH   52  352 222  HOH   HOH C . 
M 6 HOH   53  353 14   HOH   HOH C . 
M 6 HOH   54  354 42   HOH   HOH C . 
M 6 HOH   55  355 78   HOH   HOH C . 
M 6 HOH   56  356 22   HOH   HOH C . 
M 6 HOH   57  357 266  HOH   HOH C . 
M 6 HOH   58  358 117  HOH   HOH C . 
M 6 HOH   59  359 71   HOH   HOH C . 
M 6 HOH   60  360 174  HOH   HOH C . 
M 6 HOH   61  361 248  HOH   HOH C . 
M 6 HOH   62  362 410  HOH   HOH C . 
M 6 HOH   63  363 244  HOH   HOH C . 
M 6 HOH   64  364 368  HOH   HOH C . 
M 6 HOH   65  365 401  HOH   HOH C . 
M 6 HOH   66  366 270  HOH   HOH C . 
M 6 HOH   67  367 379  HOH   HOH C . 
M 6 HOH   68  368 354  HOH   HOH C . 
M 6 HOH   69  369 341  HOH   HOH C . 
M 6 HOH   70  370 314  HOH   HOH C . 
M 6 HOH   71  371 39   HOH   HOH C . 
M 6 HOH   72  372 23   HOH   HOH C . 
M 6 HOH   73  373 432  HOH   HOH C . 
M 6 HOH   74  374 259  HOH   HOH C . 
M 6 HOH   75  375 362  HOH   HOH C . 
M 6 HOH   76  376 422  HOH   HOH C . 
M 6 HOH   77  377 274  HOH   HOH C . 
M 6 HOH   78  378 440  HOH   HOH C . 
M 6 HOH   79  379 285  HOH   HOH C . 
M 6 HOH   80  380 77   HOH   HOH C . 
M 6 HOH   81  381 419  HOH   HOH C . 
M 6 HOH   82  382 321  HOH   HOH C . 
M 6 HOH   83  383 335  HOH   HOH C . 
M 6 HOH   84  384 343  HOH   HOH C . 
M 6 HOH   85  385 229  HOH   HOH C . 
M 6 HOH   86  386 400  HOH   HOH C . 
M 6 HOH   87  387 167  HOH   HOH C . 
N 6 HOH   1   301 415  HOH   HOH D . 
N 6 HOH   2   302 28   HOH   HOH D . 
N 6 HOH   3   303 345  HOH   HOH D . 
N 6 HOH   4   304 212  HOH   HOH D . 
N 6 HOH   5   305 29   HOH   HOH D . 
N 6 HOH   6   306 437  HOH   HOH D . 
N 6 HOH   7   307 159  HOH   HOH D . 
N 6 HOH   8   308 269  HOH   HOH D . 
N 6 HOH   9   309 144  HOH   HOH D . 
N 6 HOH   10  310 210  HOH   HOH D . 
N 6 HOH   11  311 80   HOH   HOH D . 
N 6 HOH   12  312 183  HOH   HOH D . 
N 6 HOH   13  313 242  HOH   HOH D . 
N 6 HOH   14  314 206  HOH   HOH D . 
N 6 HOH   15  315 109  HOH   HOH D . 
N 6 HOH   16  316 201  HOH   HOH D . 
N 6 HOH   17  317 178  HOH   HOH D . 
N 6 HOH   18  318 281  HOH   HOH D . 
N 6 HOH   19  319 60   HOH   HOH D . 
N 6 HOH   20  320 5    HOH   HOH D . 
N 6 HOH   21  321 15   HOH   HOH D . 
N 6 HOH   22  322 243  HOH   HOH D . 
N 6 HOH   23  323 34   HOH   HOH D . 
N 6 HOH   24  324 87   HOH   HOH D . 
N 6 HOH   25  325 237  HOH   HOH D . 
N 6 HOH   26  326 127  HOH   HOH D . 
N 6 HOH   27  327 316  HOH   HOH D . 
N 6 HOH   28  328 49   HOH   HOH D . 
N 6 HOH   29  329 342  HOH   HOH D . 
N 6 HOH   30  330 124  HOH   HOH D . 
N 6 HOH   31  331 310  HOH   HOH D . 
N 6 HOH   32  332 446  HOH   HOH D . 
N 6 HOH   33  333 118  HOH   HOH D . 
N 6 HOH   34  334 97   HOH   HOH D . 
N 6 HOH   35  335 449  HOH   HOH D . 
N 6 HOH   36  336 134  HOH   HOH D . 
N 6 HOH   37  337 194  HOH   HOH D . 
N 6 HOH   38  338 11   HOH   HOH D . 
N 6 HOH   39  339 177  HOH   HOH D . 
N 6 HOH   40  340 131  HOH   HOH D . 
N 6 HOH   41  341 251  HOH   HOH D . 
N 6 HOH   42  342 70   HOH   HOH D . 
N 6 HOH   43  343 88   HOH   HOH D . 
N 6 HOH   44  344 46   HOH   HOH D . 
N 6 HOH   45  345 86   HOH   HOH D . 
N 6 HOH   46  346 108  HOH   HOH D . 
N 6 HOH   47  347 254  HOH   HOH D . 
N 6 HOH   48  348 213  HOH   HOH D . 
N 6 HOH   49  349 36   HOH   HOH D . 
N 6 HOH   50  350 16   HOH   HOH D . 
N 6 HOH   51  351 215  HOH   HOH D . 
N 6 HOH   52  352 290  HOH   HOH D . 
N 6 HOH   53  353 359  HOH   HOH D . 
N 6 HOH   54  354 19   HOH   HOH D . 
N 6 HOH   55  355 284  HOH   HOH D . 
N 6 HOH   56  356 21   HOH   HOH D . 
N 6 HOH   57  357 122  HOH   HOH D . 
N 6 HOH   58  358 61   HOH   HOH D . 
N 6 HOH   59  359 6    HOH   HOH D . 
N 6 HOH   60  360 73   HOH   HOH D . 
N 6 HOH   61  361 157  HOH   HOH D . 
N 6 HOH   62  362 299  HOH   HOH D . 
N 6 HOH   63  363 246  HOH   HOH D . 
N 6 HOH   64  364 130  HOH   HOH D . 
N 6 HOH   65  365 140  HOH   HOH D . 
N 6 HOH   66  366 309  HOH   HOH D . 
N 6 HOH   67  367 279  HOH   HOH D . 
N 6 HOH   68  368 31   HOH   HOH D . 
N 6 HOH   69  369 416  HOH   HOH D . 
N 6 HOH   70  370 234  HOH   HOH D . 
N 6 HOH   71  371 160  HOH   HOH D . 
N 6 HOH   72  372 98   HOH   HOH D . 
N 6 HOH   73  373 106  HOH   HOH D . 
N 6 HOH   74  374 203  HOH   HOH D . 
N 6 HOH   75  375 94   HOH   HOH D . 
N 6 HOH   76  376 441  HOH   HOH D . 
N 6 HOH   77  377 32   HOH   HOH D . 
N 6 HOH   78  378 93   HOH   HOH D . 
N 6 HOH   79  379 52   HOH   HOH D . 
N 6 HOH   80  380 63   HOH   HOH D . 
N 6 HOH   81  381 204  HOH   HOH D . 
N 6 HOH   82  382 89   HOH   HOH D . 
N 6 HOH   83  383 99   HOH   HOH D . 
N 6 HOH   84  384 439  HOH   HOH D . 
N 6 HOH   85  385 312  HOH   HOH D . 
N 6 HOH   86  386 147  HOH   HOH D . 
N 6 HOH   87  387 152  HOH   HOH D . 
N 6 HOH   88  388 43   HOH   HOH D . 
N 6 HOH   89  389 283  HOH   HOH D . 
N 6 HOH   90  390 91   HOH   HOH D . 
N 6 HOH   91  391 27   HOH   HOH D . 
N 6 HOH   92  392 168  HOH   HOH D . 
N 6 HOH   93  393 385  HOH   HOH D . 
N 6 HOH   94  394 337  HOH   HOH D . 
N 6 HOH   95  395 333  HOH   HOH D . 
N 6 HOH   96  396 434  HOH   HOH D . 
N 6 HOH   97  397 300  HOH   HOH D . 
N 6 HOH   98  398 128  HOH   HOH D . 
N 6 HOH   99  399 287  HOH   HOH D . 
N 6 HOH   100 400 268  HOH   HOH D . 
N 6 HOH   101 401 57   HOH   HOH D . 
N 6 HOH   102 402 407  HOH   HOH D . 
N 6 HOH   103 403 406  HOH   HOH D . 
N 6 HOH   104 404 150  HOH   HOH D . 
N 6 HOH   105 405 126  HOH   HOH D . 
N 6 HOH   106 406 389  HOH   HOH D . 
N 6 HOH   107 407 289  HOH   HOH D . 
N 6 HOH   108 408 392  HOH   HOH D . 
N 6 HOH   109 409 374  HOH   HOH D . 
N 6 HOH   110 410 249  HOH   HOH D . 
N 6 HOH   111 411 228  HOH   HOH D . 
N 6 HOH   112 412 303  HOH   HOH D . 
N 6 HOH   113 413 448  HOH   HOH D . 
N 6 HOH   114 414 455  HOH   HOH D . 
N 6 HOH   115 415 276  HOH   HOH D . 
N 6 HOH   116 416 411  HOH   HOH D . 
N 6 HOH   117 417 327  HOH   HOH D . 
N 6 HOH   118 418 397  HOH   HOH D . 
N 6 HOH   119 419 388  HOH   HOH D . 
N 6 HOH   120 420 370  HOH   HOH D . 
N 6 HOH   121 421 436  HOH   HOH D . 
N 6 HOH   122 422 116  HOH   HOH D . 
N 6 HOH   123 423 257  HOH   HOH D . 
N 6 HOH   124 424 226  HOH   HOH D . 
N 6 HOH   125 425 191  HOH   HOH D . 
N 6 HOH   126 426 252  HOH   HOH D . 
N 6 HOH   127 427 151  HOH   HOH D . 
N 6 HOH   128 428 245  HOH   HOH D . 
N 6 HOH   129 429 217  HOH   HOH D . 
N 6 HOH   130 430 155  HOH   HOH D . 
N 6 HOH   131 431 267  HOH   HOH D . 
N 6 HOH   132 432 325  HOH   HOH D . 
N 6 HOH   133 433 332  HOH   HOH D . 
N 6 HOH   134 434 311  HOH   HOH D . 
N 6 HOH   135 435 198  HOH   HOH D . 
N 6 HOH   136 436 329  HOH   HOH D . 
N 6 HOH   137 437 395  HOH   HOH D . 
N 6 HOH   138 438 44   HOH   HOH D . 
N 6 HOH   139 439 169  HOH   HOH D . 
N 6 HOH   140 440 387  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                     9BGC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.420 
_cell.length_a_esd                 ? 
_cell.length_b                     85.880 
_cell.length_b_esd                 ? 
_cell.length_c                     128.280 
_cell.length_c_esd                 ? 
_cell.volume                       731728.311 
_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                         9BGC 
_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                   9BGC 
_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             2.46 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.01 
_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              ? 
_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    '22% PEG2000 MME, 0.10 M Tris, pH 8' 
_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         2024-03-29 
_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                          19.47 
_reflns.entry_id                                       9BGC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.87 
_reflns.d_resolution_low                               58.98 
_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                                     60989 
_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                           98.52 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.77 
_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                                0.1267 
_reflns.pdbx_Rpim_I_all                                0.04687 
_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                              0.1175 
_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                                    1.87 
_reflns_shell.d_res_low                                     1.937 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.15 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5840 
_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                               1.815 
_reflns_shell.pdbx_Rpim_I_all                               0.6803 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.694 
_reflns_shell.pdbx_CC_star                                  0.905 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          95.02 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.68 
_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                               36.96 
_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                                 9BGC 
_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                            1.87 
_refine.ls_d_res_low                             58.98 
_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                     60803 
_refine.ls_number_reflns_R_free                  3012 
_refine.ls_number_reflns_R_work                  57791 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.53 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2401 
_refine.ls_R_factor_R_free                       0.2716 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2384 
_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                 35.2761 
_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                            0.3528 
_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                       1.87 
_refine_hist.d_res_low                        58.98 
_refine_hist.number_atoms_solvent             418 
_refine_hist.number_atoms_total               5814 
_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        5214 
_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' ? 0.0077  ? 5521 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9368  ? 7464 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0563  ? 795  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0084  ? 962  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.1831 ? 2097 ? 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' 1.87 1.90  . . 153 2562 98.62  . . . . 0.6729 . . . . . . . . . . . 0.7016 
'X-RAY DIFFRACTION' 1.90 1.93  . . 129 2351 90.71  . . . . 0.5649 . . . . . . . . . . . 0.5724 
'X-RAY DIFFRACTION' 1.93 1.96  . . 107 2351 87.85  . . . . 0.6152 . . . . . . . . . . . 0.6092 
'X-RAY DIFFRACTION' 1.96 2.00  . . 137 2533 97.45  . . . . 0.5773 . . . . . . . . . . . 0.6108 
'X-RAY DIFFRACTION' 2.00 2.03  . . 129 2673 99.79  . . . . 0.4027 . . . . . . . . . . . 0.4409 
'X-RAY DIFFRACTION' 2.03 2.08  . . 121 2635 99.93  . . . . 0.2747 . . . . . . . . . . . 0.3168 
'X-RAY DIFFRACTION' 2.08 2.12  . . 130 2641 100.00 . . . . 0.2571 . . . . . . . . . . . 0.3307 
'X-RAY DIFFRACTION' 2.12 2.17  . . 125 2655 100.00 . . . . 0.2664 . . . . . . . . . . . 0.3176 
'X-RAY DIFFRACTION' 2.17 2.22  . . 144 2585 98.20  . . . . 0.3218 . . . . . . . . . . . 0.3410 
'X-RAY DIFFRACTION' 2.22 2.28  . . 122 2569 96.52  . . . . 0.4204 . . . . . . . . . . . 0.4848 
'X-RAY DIFFRACTION' 2.28 2.35  . . 131 2606 99.24  . . . . 0.2750 . . . . . . . . . . . 0.3366 
'X-RAY DIFFRACTION' 2.35 2.43  . . 143 2652 100.00 . . . . 0.2268 . . . . . . . . . . . 0.2780 
'X-RAY DIFFRACTION' 2.43 2.51  . . 130 2674 99.96  . . . . 0.2192 . . . . . . . . . . . 0.2810 
'X-RAY DIFFRACTION' 2.51 2.61  . . 116 2682 99.93  . . . . 0.2326 . . . . . . . . . . . 0.2602 
'X-RAY DIFFRACTION' 2.61 2.73  . . 127 2663 100.00 . . . . 0.2385 . . . . . . . . . . . 0.3204 
'X-RAY DIFFRACTION' 2.73 2.88  . . 146 2655 99.93  . . . . 0.2117 . . . . . . . . . . . 0.2719 
'X-RAY DIFFRACTION' 2.88 3.06  . . 146 2674 100.00 . . . . 0.2107 . . . . . . . . . . . 0.2743 
'X-RAY DIFFRACTION' 3.06 3.29  . . 148 2696 99.96  . . . . 0.2075 . . . . . . . . . . . 0.2524 
'X-RAY DIFFRACTION' 3.29 3.63  . . 134 2673 99.82  . . . . 0.1886 . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 3.63 4.15  . . 160 2701 99.90  . . . . 0.1662 . . . . . . . . . . . 0.1938 
'X-RAY DIFFRACTION' 4.15 5.23  . . 163 2714 99.97  . . . . 0.1446 . . . . . . . . . . . 0.1594 
'X-RAY DIFFRACTION' 5.23 58.98 . . 171 2846 99.57  . . . . 0.1670 . . . . . . . . . . . 0.2086 
# 
_struct.entry_id                     9BGC 
_struct.title                        'Tri-complex of Daraxonrasib (RMC-6236), KRAS G12R, 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        9BGC 
_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 P01116-2 1 
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLV
REIRKHKEK
;
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 9BGC A 2 ? 170 ? P01116 1 ? 169 ? 1 169 
2 1 9BGC B 2 ? 170 ? P01116 1 ? 169 ? 1 169 
3 2 9BGC C 2 ? 166 ? P62937 1 ? 165 ? 1 165 
4 2 9BGC 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 9BGC SER A 1  ? UNP P01116 ?   ?  'expression tag'      0  1 
1 9BGC ARG A 13 ? UNP P01116 GLY 12 'engineered mutation' 12 2 
2 9BGC SER B 1  ? UNP P01116 ?   ?  'expression tag'      0  3 
2 9BGC ARG B 13 ? UNP P01116 GLY 12 'engineered mutation' 12 4 
3 9BGC SER C 1  ? UNP P62937 ?   ?  'expression tag'      0  5 
4 9BGC SER D 1  ? UNP P62937 ?   ?  'expression tag'      0  6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? 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 ? GLU B 169 ? GLY B 151 GLU B 168 1 ? 18 
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 ? ARG C 145 ? GLY C 135 ARG C 144 1 ? 10 
HELX_P HELX_P16 AB7 VAL D 30  ? GLY D 43  ? VAL D 29  GLY D 42  1 ? 14 
HELX_P HELX_P17 AB8 THR D 120 ? ASP D 124 ? THR D 119 ASP D 123 5 ? 5  
HELX_P HELX_P18 AB9 GLY D 136 ? ARG D 145 ? GLY D 135 ARG D 144 1 ? 10 
# 
_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 ? ? ? ? ? ? ? 2.178 ? ? 
metalc2  metalc ? ? A THR 36 OG1 ? ? ? 1_555 F MG  . MG ? ? A THR 35  A MG  202 1_555 ? ? ? ? ? ? ? 2.132 ? ? 
metalc3  metalc ? ? E GNP .  O1G ? ? ? 1_555 F MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc4  metalc ? ? E GNP .  O1B ? ? ? 1_555 F MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc5  metalc ? ? F MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 303 1_555 ? ? ? ? ? ? ? 2.190 ? ? 
metalc6  metalc ? ? F MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 350 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc7  metalc ? ? B SER 18 OG  ? ? ? 1_555 H MG  . MG ? ? B SER 17  B MG  202 1_555 ? ? ? ? ? ? ? 2.181 ? ? 
metalc8  metalc ? ? B THR 36 OG1 ? ? ? 1_555 H MG  . MG ? ? B THR 35  B MG  202 1_555 ? ? ? ? ? ? ? 2.191 ? ? 
metalc9  metalc ? ? G GNP .  O1G ? ? ? 1_555 H MG  . MG ? ? B GNP 201 B MG  202 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
metalc10 metalc ? ? G GNP .  O1B ? ? ? 1_555 H MG  . MG ? ? B GNP 201 B MG  202 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
metalc11 metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  202 B HOH 309 1_555 ? ? ? ? ? ? ? 2.202 ? ? 
metalc12 metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  202 B HOH 329 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
# 
_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 78.2  ? 
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_555 169.8 ? 
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 93.1  ? 
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 92.3  ? 
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_555 170.2 ? 
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 96.2  ? 
7  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 303 ? 1_555 92.4  ? 
8  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 303 ? 1_555 88.4  ? 
9  O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 303 ? 1_555 92.6  ? 
10 O1B ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 303 ? 1_555 94.3  ? 
11 OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 350 ? 1_555 89.8  ? 
12 OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 350 ? 1_555 93.1  ? 
13 O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 350 ? 1_555 85.4  ? 
14 O1B ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 350 ? 1_555 84.6  ? 
15 O   ? K HOH .  ? A HOH 303 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 350 ? 1_555 177.6 ? 
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 74.3  ? 
17 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O1G ? G GNP .  ? B GNP 201 ? 1_555 166.8 ? 
18 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O1G ? G GNP .  ? B GNP 201 ? 1_555 94.2  ? 
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_555 100.1 ? 
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_555 174.3 ? 
21 O1G ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O1B ? G GNP .  ? B GNP 201 ? 1_555 91.5  ? 
22 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 309 ? 1_555 90.6  ? 
23 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 309 ? 1_555 89.1  ? 
24 O1G ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 309 ? 1_555 95.7  ? 
25 O1B ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 309 ? 1_555 89.9  ? 
26 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 329 ? 1_555 87.6  ? 
27 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 329 ? 1_555 90.9  ? 
28 O1G ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 329 ? 1_555 86.1  ? 
29 O1B ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 329 ? 1_555 90.0  ? 
30 O   ? L HOH .  ? B HOH 309 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 329 ? 1_555 178.2 ? 
# 
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 ASP B 39  ? ILE B 47  ? ASP B 38  ILE B 46  
AA2 2 GLU B 50  ? ASP B 58  ? GLU B 49  ASP B 57  
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 ? GLU C 166 ? ILE C 156 GLU C 165 
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 ? VAL D 133 ? VAL D 128 VAL D 132 
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 ? LEU D 165 ? ILE D 156 LEU D 164 
# 
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 ASP A 55  ? O ASP A 54  N TYR A 5   ? N TYR A 4   
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 ASP B 55  ? O ASP B 54  N LEU B 7   ? N LEU B 6   
AA2 3 4 N VAL B 10  ? N VAL B 9   O LEU B 80  ? O LEU B 79  
AA2 4 5 N PHE B 83  ? N PHE B 82  O ASN B 117 ? O ASN B 116 
AA2 5 6 N GLY B 116 ? N GLY B 115 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 PHE C 114 ? O PHE C 113 N SER C 100 ? N SER C 99  
AA3 4 5 N LEU C 99  ? N LEU C 98  O PHE C 130 ? O PHE C 129 
AA3 5 6 O LYS C 134 ? O LYS C 133 N SER C 22  ? N SER C 21  
AA3 6 7 O GLY C 19  ? O GLY C 18  N ILE C 11  ? N ILE C 10  
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                   9BGC 
_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 GLU A 37  ? ? -170.85 131.10 
2 1 SER A 122 ? ? -81.85  38.39  
3 1 GLU B 37  ? ? -175.32 128.60 
4 1 LYS B 117 ? ? 76.95   35.75  
5 1 PHE C 60  ? ? -135.30 -69.07 
6 1 ASP D 13  ? ? 37.49   49.14  
7 1 PHE D 60  ? ? -130.62 -69.35 
8 1 ASN D 71  ? ? -144.20 15.46  
# 
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 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      D 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       440 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.03 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A LYS 169 ? A LYS 170 
2 1 Y 1 B LYS 169 ? B LYS 170 
3 1 Y 1 C SER 0   ? C SER 1   
4 1 Y 1 C MET 1   ? C MET 2   
5 1 Y 1 D SER 0   ? D SER 1   
6 1 Y 1 D MET 1   ? D MET 2   
7 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                    9BGC 
_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]   0.015056 
_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]   0.011644 
_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.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 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   ? -27.25594 1.54137   31.09138  1.000 58.15959  ?  0   SER   A N     1 
ATOM   2    C  CA    . SER   A 1 1   ? -27.96041 0.93572   29.96843  1.000 56.18220  ?  0   SER   A CA    1 
ATOM   3    C  C     . SER   A 1 1   ? -27.01817 0.68816   28.80201  1.000 59.04890  ?  0   SER   A C     1 
ATOM   4    O  O     . SER   A 1 1   ? -26.02099 -0.01432  28.97667  1.000 58.22099  ?  0   SER   A O     1 
ATOM   5    C  CB    . SER   A 1 1   ? -29.14393 1.80392   29.52921  1.000 55.41114  ?  0   SER   A CB    1 
ATOM   6    O  OG    . SER   A 1 1   ? -30.13166 1.86379   30.55280  1.000 62.56722  ?  0   SER   A OG    1 
ATOM   7    N  N     . MET   A 1 2   ? -27.31050 1.27841   27.63669  1.000 50.43913  ?  1   MET   A N     1 
ATOM   8    C  CA    . MET   A 1 2   ? -26.62673 0.87123   26.41500  1.000 42.66953  ?  1   MET   A CA    1 
ATOM   9    C  C     . MET   A 1 2   ? -25.15319 1.26875   26.40784  1.000 38.12708  ?  1   MET   A C     1 
ATOM   10   O  O     . MET   A 1 2   ? -24.76945 2.34379   26.86953  1.000 40.10377  ?  1   MET   A O     1 
ATOM   11   C  CB    . MET   A 1 2   ? -27.33061 1.45165   25.18911  1.000 49.01894  ?  1   MET   A CB    1 
ATOM   12   C  CG    . MET   A 1 2   ? -27.01369 2.92126   24.90756  1.000 47.69809  ?  1   MET   A CG    1 
ATOM   13   S  SD    . MET   A 1 2   ? -27.80827 3.49711   23.39471  1.000 36.19244  ?  1   MET   A SD    1 
ATOM   14   C  CE    . MET   A 1 2   ? -29.49584 3.55341   24.00588  1.000 31.79019  ?  1   MET   A CE    1 
ATOM   15   N  N     . THR   A 1 3   ? -24.33021 0.37057   25.88145  1.000 37.84674  ?  2   THR   A N     1 
ATOM   16   C  CA    . THR   A 1 3   ? -22.89259 0.56772   25.84035  1.000 40.52788  ?  2   THR   A CA    1 
ATOM   17   C  C     . THR   A 1 3   ? -22.52601 1.74258   24.93718  1.000 36.21726  ?  2   THR   A C     1 
ATOM   18   O  O     . THR   A 1 3   ? -23.07869 1.91411   23.85299  1.000 34.58144  ?  2   THR   A O     1 
ATOM   19   C  CB    . THR   A 1 3   ? -22.22917 -0.71669  25.35363  1.000 40.11601  ?  2   THR   A CB    1 
ATOM   20   O  OG1   . THR   A 1 3   ? -22.67097 -1.80817  26.18397  1.000 37.89312  ?  2   THR   A OG1   1 
ATOM   21   C  CG2   . THR   A 1 3   ? -20.71239 -0.60388  25.40023  1.000 38.34149  ?  2   THR   A CG2   1 
ATOM   22   N  N     . GLU   A 1 4   ? -21.59332 2.56391   25.39557  1.000 31.55769  ?  3   GLU   A N     1 
ATOM   23   C  CA    . GLU   A 1 4   ? -21.07410 3.67759   24.61166  1.000 34.97644  ?  3   GLU   A CA    1 
ATOM   24   C  C     . GLU   A 1 4   ? -19.70819 3.31330   24.03935  1.000 29.64114  ?  3   GLU   A C     1 
ATOM   25   O  O     . GLU   A 1 4   ? -18.85008 2.80005   24.75595  1.000 35.43838  ?  3   GLU   A O     1 
ATOM   26   C  CB    . GLU   A 1 4   ? -20.95157 4.94506   25.45567  1.000 40.84922  ?  3   GLU   A CB    1 
ATOM   27   C  CG    . GLU   A 1 4   ? -22.22399 5.34453   26.21933  1.000 46.08029  ?  3   GLU   A CG    1 
ATOM   28   C  CD    . GLU   A 1 4   ? -22.01096 6.58665   27.10022  1.000 50.04991  ?  3   GLU   A CD    1 
ATOM   29   O  OE1   . GLU   A 1 4   ? -21.07386 7.36736   26.80504  1.000 51.52072  ?  3   GLU   A OE1   1 
ATOM   30   O  OE2   . GLU   A 1 4   ? -22.76719 6.77996   28.08873  1.000 50.32010  -1 3   GLU   A OE2   1 
ATOM   31   N  N     . TYR   A 1 5   ? -19.50350 3.59043   22.75355  1.000 32.25602  ?  4   TYR   A N     1 
ATOM   32   C  CA    . TYR   A 1 5   ? -18.25494 3.28907   22.05866  1.000 30.85881  ?  4   TYR   A CA    1 
ATOM   33   C  C     . TYR   A 1 5   ? -17.58201 4.58615   21.63251  1.000 28.80964  ?  4   TYR   A C     1 
ATOM   34   O  O     . TYR   A 1 5   ? -18.22583 5.45139   21.02151  1.000 27.13543  ?  4   TYR   A O     1 
ATOM   35   C  CB    . TYR   A 1 5   ? -18.52642 2.39505   20.83557  1.000 29.75296  ?  4   TYR   A CB    1 
ATOM   36   C  CG    . TYR   A 1 5   ? -18.98622 1.02354   21.24674  1.000 32.02608  ?  4   TYR   A CG    1 
ATOM   37   C  CD1   . TYR   A 1 5   ? -18.07143 0.03659   21.56921  1.000 32.39428  ?  4   TYR   A CD1   1 
ATOM   38   C  CD2   . TYR   A 1 5   ? -20.33963 0.71983   21.33610  1.000 29.98782  ?  4   TYR   A CD2   1 
ATOM   39   C  CE1   . TYR   A 1 5   ? -18.48961 -1.22753  21.95669  1.000 37.07541  ?  4   TYR   A CE1   1 
ATOM   40   C  CE2   . TYR   A 1 5   ? -20.76168 -0.53096  21.72448  1.000 33.07287  ?  4   TYR   A CE2   1 
ATOM   41   C  CZ    . TYR   A 1 5   ? -19.83354 -1.49878  22.03476  1.000 32.25461  ?  4   TYR   A CZ    1 
ATOM   42   O  OH    . TYR   A 1 5   ? -20.25403 -2.74355  22.43665  1.000 38.25006  ?  4   TYR   A OH    1 
ATOM   43   N  N     . LYS   A 1 6   ? -16.28594 4.71756   21.93036  1.000 27.66251  ?  5   LYS   A N     1 
ATOM   44   C  CA    . LYS   A 1 6   ? -15.54660 5.95098   21.64745  1.000 25.22439  ?  5   LYS   A CA    1 
ATOM   45   C  C     . LYS   A 1 6   ? -14.74475 5.77134   20.35834  1.000 26.09703  ?  5   LYS   A C     1 
ATOM   46   O  O     . LYS   A 1 6   ? -13.62535 5.25055   20.37108  1.000 28.03445  ?  5   LYS   A O     1 
ATOM   47   C  CB    . LYS   A 1 6   ? -14.65928 6.33335   22.82945  1.000 29.51470  ?  5   LYS   A CB    1 
ATOM   48   C  CG    . LYS   A 1 6   ? -15.44184 6.85812   24.02604  1.000 26.41313  ?  5   LYS   A CG    1 
ATOM   49   C  CD    . LYS   A 1 6   ? -14.56041 6.97557   25.27430  1.000 29.38348  ?  5   LYS   A CD    1 
ATOM   50   C  CE    . LYS   A 1 6   ? -15.40388 7.25853   26.53593  1.000 41.06025  ?  5   LYS   A CE    1 
ATOM   51   N  NZ    . LYS   A 1 6   ? -16.58130 6.32560   26.67507  1.000 41.95005  ?  5   LYS   A NZ    1 
ATOM   52   N  N     . LEU   A 1 7   ? -15.32955 6.20661   19.24739  1.000 24.16858  ?  6   LEU   A N     1 
ATOM   53   C  CA    . LEU   A 1 7   ? -14.70602 6.12114   17.93704  1.000 26.88668  ?  6   LEU   A CA    1 
ATOM   54   C  C     . LEU   A 1 7   ? -13.97172 7.41838   17.62289  1.000 24.07423  ?  6   LEU   A C     1 
ATOM   55   O  O     . LEU   A 1 7   ? -14.44276 8.51215   17.95521  1.000 28.06418  ?  6   LEU   A O     1 
ATOM   56   C  CB    . LEU   A 1 7   ? -15.75708 5.84594   16.85891  1.000 27.18621  ?  6   LEU   A CB    1 
ATOM   57   C  CG    . LEU   A 1 7   ? -16.88204 4.85341   17.18298  1.000 30.16845  ?  6   LEU   A CG    1 
ATOM   58   C  CD1   . LEU   A 1 7   ? -17.73996 4.60909   15.92514  1.000 25.57409  ?  6   LEU   A CD1   1 
ATOM   59   C  CD2   . LEU   A 1 7   ? -16.33870 3.52944   17.73730  1.000 27.42296  ?  6   LEU   A CD2   1 
ATOM   60   N  N     . VAL   A 1 8   ? -12.80797 7.29378   17.00085  1.000 19.65538  ?  7   VAL   A N     1 
ATOM   61   C  CA    . VAL   A 1 8   ? -11.99383 8.44835   16.63254  1.000 24.01663  ?  7   VAL   A CA    1 
ATOM   62   C  C     . VAL   A 1 8   ? -11.67108 8.33431   15.14845  1.000 22.20266  ?  7   VAL   A C     1 
ATOM   63   O  O     . VAL   A 1 8   ? -11.18699 7.29335   14.69386  1.000 24.22467  ?  7   VAL   A O     1 
ATOM   64   C  CB    . VAL   A 1 8   ? -10.70619 8.54438   17.47883  1.000 21.69875  ?  7   VAL   A CB    1 
ATOM   65   C  CG1   . VAL   A 1 8   ? -9.89322  9.74750   17.06764  1.000 24.13976  ?  7   VAL   A CG1   1 
ATOM   66   C  CG2   . VAL   A 1 8   ? -11.05748 8.60455   18.97923  1.000 20.86546  ?  7   VAL   A CG2   1 
ATOM   67   N  N     . VAL   A 1 9   ? -11.95057 9.38714   14.39437  1.000 19.80101  ?  8   VAL   A N     1 
ATOM   68   C  CA    . VAL   A 1 9   ? -11.72136 9.38761   12.94903  1.000 25.29730  ?  8   VAL   A CA    1 
ATOM   69   C  C     . VAL   A 1 9   ? -10.44500 10.17790  12.69265  1.000 22.94125  ?  8   VAL   A C     1 
ATOM   70   O  O     . VAL   A 1 9   ? -10.37697 11.37110  13.02326  1.000 20.60734  ?  8   VAL   A O     1 
ATOM   71   C  CB    . VAL   A 1 9   ? -12.91371 9.99488   12.17734  1.000 21.56945  ?  8   VAL   A CB    1 
ATOM   72   C  CG1   . VAL   A 1 9   ? -12.68515 9.86469   10.63740  1.000 19.01459  ?  8   VAL   A CG1   1 
ATOM   73   C  CG2   . VAL   A 1 9   ? -14.22604 9.34635   12.59192  1.000 22.44495  ?  8   VAL   A CG2   1 
ATOM   74   N  N     . VAL   A 1 10  ? -9.43983  9.52510   12.08670  1.000 21.24418  ?  9   VAL   A N     1 
ATOM   75   C  CA    . VAL   A 1 10  ? -8.13821  10.13604  11.83763  1.000 19.07236  ?  9   VAL   A CA    1 
ATOM   76   C  C     . VAL   A 1 10  ? -7.73069  9.96339   10.37689  1.000 23.24866  ?  9   VAL   A C     1 
ATOM   77   O  O     . VAL   A 1 10  ? -8.21919  9.08623   9.66725   1.000 21.38792  ?  9   VAL   A O     1 
ATOM   78   C  CB    . VAL   A 1 10  ? -7.04492  9.54917   12.76177  1.000 20.68862  ?  9   VAL   A CB    1 
ATOM   79   C  CG1   . VAL   A 1 10  ? -7.45764  9.72335   14.22359  1.000 21.09466  ?  9   VAL   A CG1   1 
ATOM   80   C  CG2   . VAL   A 1 10  ? -6.77994  8.06908   12.41838  1.000 21.00729  ?  9   VAL   A CG2   1 
ATOM   81   N  N     . GLY   A 1 11  ? -6.81467  10.80710  9.93462   1.000 24.23520  ?  10  GLY   A N     1 
ATOM   82   C  CA    . GLY   A 1 11  ? -6.31051  10.70605  8.57172   1.000 28.33359  ?  10  GLY   A CA    1 
ATOM   83   C  C     . GLY   A 1 11  ? -5.89029  12.06357  8.05355   1.000 25.11212  ?  10  GLY   A C     1 
ATOM   84   O  O     . GLY   A 1 11  ? -6.10255  13.08909  8.69515   1.000 28.41761  ?  10  GLY   A O     1 
ATOM   85   N  N     . ALA   A 1 12  ? -5.29052  12.05282  6.85252   1.000 24.73143  ?  11  ALA   A N     1 
ATOM   86   C  CA    . ALA   A 1 12  ? -4.75534  13.26751  6.24266   1.000 28.70993  ?  11  ALA   A CA    1 
ATOM   87   C  C     . ALA   A 1 12  ? -5.86051  14.27530  5.93341   1.000 28.96786  ?  11  ALA   A C     1 
ATOM   88   O  O     . ALA   A 1 12  ? -7.04220  13.93768  5.81855   1.000 26.31510  ?  11  ALA   A O     1 
ATOM   89   C  CB    . ALA   A 1 12  ? -4.00218  12.94750  4.94389   1.000 27.23505  ?  11  ALA   A CB    1 
ATOM   90   N  N     . ARG   A 1 13  ? -5.44524  15.53384  5.80578   1.000 30.34677  ?  12  ARG   A N     1 
ATOM   91   C  CA    . ARG   A 1 13  ? -6.28598  16.62014  5.32237   1.000 33.81228  ?  12  ARG   A CA    1 
ATOM   92   C  C     . ARG   A 1 13  ? -7.06660  16.19639  4.08986   1.000 29.77630  ?  12  ARG   A C     1 
ATOM   93   O  O     . ARG   A 1 13  ? -6.50619  15.60101  3.17346   1.000 26.05603  ?  12  ARG   A O     1 
ATOM   94   C  CB    . ARG   A 1 13  ? -5.41356  17.82479  4.94839   1.000 37.29539  ?  12  ARG   A CB    1 
ATOM   95   C  CG    . ARG   A 1 13  ? -5.41306  18.98186  5.89723   1.000 42.65179  ?  12  ARG   A CG    1 
ATOM   96   C  CD    . ARG   A 1 13  ? -4.66740  20.18841  5.25724   1.000 37.09586  ?  12  ARG   A CD    1 
ATOM   97   N  NE    . ARG   A 1 13  ? -5.57157  21.08039  4.53872   1.000 41.04501  ?  12  ARG   A NE    1 
ATOM   98   C  CZ    . ARG   A 1 13  ? -5.68008  21.14062  3.21919   1.000 39.49057  ?  12  ARG   A CZ    1 
ATOM   99   N  NH1   . ARG   A 1 13  ? -4.90255  20.41939  2.42828   1.000 40.31884  ?  12  ARG   A NH1   1 
ATOM   100  N  NH2   . ARG   A 1 13  ? -6.59287  21.94524  2.67907   1.000 41.91992  ?  12  ARG   A NH2   1 
ATOM   101  N  N     . GLY   A 1 14  ? -8.36249  16.51089  4.08034   1.000 30.98056  ?  13  GLY   A N     1 
ATOM   102  C  CA    . GLY   A 1 14  ? -9.19892  16.44495  2.89012   1.000 28.47117  ?  13  GLY   A CA    1 
ATOM   103  C  C     . GLY   A 1 14  ? -9.59431  15.06445  2.41584   1.000 28.69443  ?  13  GLY   A C     1 
ATOM   104  O  O     . GLY   A 1 14  ? -10.13378 14.94214  1.30365   1.000 29.83012  ?  13  GLY   A O     1 
ATOM   105  N  N     . VAL   A 1 15  ? -9.31783  14.01398  3.19292   1.000 26.18570  ?  14  VAL   A N     1 
ATOM   106  C  CA    . VAL   A 1 15  ? -9.64503  12.66374  2.74025   1.000 25.97772  ?  14  VAL   A CA    1 
ATOM   107  C  C     . VAL   A 1 15  ? -11.11053 12.30807  2.91766   1.000 24.74692  ?  14  VAL   A C     1 
ATOM   108  O  O     . VAL   A 1 15  ? -11.54401 11.27105  2.40826   1.000 25.00816  ?  14  VAL   A O     1 
ATOM   109  C  CB    . VAL   A 1 15  ? -8.80223  11.59599  3.46189   1.000 26.27899  ?  14  VAL   A CB    1 
ATOM   110  C  CG1   . VAL   A 1 15  ? -7.29864  11.86024  3.27418   1.000 27.46381  ?  14  VAL   A CG1   1 
ATOM   111  C  CG2   . VAL   A 1 15  ? -9.17873  11.52426  4.96479   1.000 22.89682  ?  14  VAL   A CG2   1 
ATOM   112  N  N     . GLY   A 1 16  ? -11.87975 13.11974  3.63057   1.000 24.74956  ?  15  GLY   A N     1 
ATOM   113  C  CA    . GLY   A 1 16  ? -13.29645 12.88822  3.83584   1.000 23.68027  ?  15  GLY   A CA    1 
ATOM   114  C  C     . GLY   A 1 16  ? -13.71603 12.51135  5.27398   1.000 27.63122  ?  15  GLY   A C     1 
ATOM   115  O  O     . GLY   A 1 16  ? -14.81713 11.95483  5.45063   1.000 25.32809  ?  15  GLY   A O     1 
ATOM   116  N  N     . LYS   A 1 17  ? -12.88446 12.80062  6.28207   1.000 21.53513  ?  16  LYS   A N     1 
ATOM   117  C  CA    . LYS   A 1 17  ? -13.19241 12.38056  7.64308   1.000 24.96575  ?  16  LYS   A CA    1 
ATOM   118  C  C     . LYS   A 1 17  ? -14.51426 12.97514  8.09823   1.000 23.66791  ?  16  LYS   A C     1 
ATOM   119  O  O     . LYS   A 1 17  ? -15.38017 12.26164  8.60422   1.000 21.22749  ?  16  LYS   A O     1 
ATOM   120  C  CB    . LYS   A 1 17  ? -12.06515 12.77758  8.61482   1.000 21.08579  ?  16  LYS   A CB    1 
ATOM   121  C  CG    . LYS   A 1 17  ? -10.74663 12.04529  8.40639   1.000 23.60933  ?  16  LYS   A CG    1 
ATOM   122  C  CD    . LYS   A 1 17  ? -9.70749  12.44699  9.47610   1.000 20.60595  ?  16  LYS   A CD    1 
ATOM   123  C  CE    . LYS   A 1 17  ? -9.26138  13.91252  9.32771   1.000 23.87590  ?  16  LYS   A CE    1 
ATOM   124  N  NZ    . LYS   A 1 17  ? -8.62083  14.20270  8.01609   1.000 28.14465  ?  16  LYS   A NZ    1 
ATOM   125  N  N     . SER   A 1 18  ? -14.69312 14.28481  7.89658   1.000 23.80880  ?  17  SER   A N     1 
ATOM   126  C  CA    . SER   A 1 18  ? -15.91010 14.96199  8.32470   1.000 25.33475  ?  17  SER   A CA    1 
ATOM   127  C  C     . SER   A 1 18  ? -17.10218 14.60668  7.44987   1.000 27.01552  ?  17  SER   A C     1 
ATOM   128  O  O     . SER   A 1 18  ? -18.22902 14.50191  7.95706   1.000 26.84411  ?  17  SER   A O     1 
ATOM   129  C  CB    . SER   A 1 18  ? -15.69422 16.47973  8.32840   1.000 21.09341  ?  17  SER   A CB    1 
ATOM   130  O  OG    . SER   A 1 18  ? -14.68319 16.81633  9.28255   1.000 27.93563  ?  17  SER   A OG    1 
ATOM   131  N  N     . ALA   A 1 19  ? -16.87481 14.40095  6.14958   1.000 22.29494  ?  18  ALA   A N     1 
ATOM   132  C  CA    . ALA   A 1 19  ? -17.98708 14.06079  5.26556   1.000 27.31116  ?  18  ALA   A CA    1 
ATOM   133  C  C     . ALA   A 1 19  ? -18.54306 12.68400  5.59937   1.000 20.39575  ?  18  ALA   A C     1 
ATOM   134  O  O     . ALA   A 1 19  ? -19.76167 12.48961  5.60390   1.000 24.65347  ?  18  ALA   A O     1 
ATOM   135  C  CB    . ALA   A 1 19  ? -17.54093 14.15014  3.79517   1.000 21.06722  ?  18  ALA   A CB    1 
ATOM   136  N  N     . LEU   A 1 20  ? -17.66905 11.71826  5.90270   1.000 23.40436  ?  19  LEU   A N     1 
ATOM   137  C  CA    . LEU   A 1 20  ? -18.12377 10.41532  6.38258   1.000 23.57650  ?  19  LEU   A CA    1 
ATOM   138  C  C     . LEU   A 1 20  ? -18.94641 10.55599  7.66605   1.000 24.52769  ?  19  LEU   A C     1 
ATOM   139  O  O     . LEU   A 1 20  ? -20.02666 9.97002   7.79751   1.000 20.73755  ?  19  LEU   A O     1 
ATOM   140  C  CB    . LEU   A 1 20  ? -16.91638 9.50690   6.61852   1.000 23.15665  ?  19  LEU   A CB    1 
ATOM   141  C  CG    . LEU   A 1 20  ? -16.26456 8.99692   5.32634   1.000 25.47943  ?  19  LEU   A CG    1 
ATOM   142  C  CD1   . LEU   A 1 20  ? -14.92662 8.33857   5.60946   1.000 29.84852  ?  19  LEU   A CD1   1 
ATOM   143  C  CD2   . LEU   A 1 20  ? -17.21118 7.99477   4.69138   1.000 27.67402  ?  19  LEU   A CD2   1 
ATOM   144  N  N     . THR   A 1 21  ? -18.44303 11.33708  8.62192   1.000 23.61831  ?  20  THR   A N     1 
ATOM   145  C  CA    . THR   A 1 21  ? -19.12516 11.47976  9.90994   1.000 27.81015  ?  20  THR   A CA    1 
ATOM   146  C  C     . THR   A 1 21  ? -20.47584 12.18168  9.75098   1.000 24.03133  ?  20  THR   A C     1 
ATOM   147  O  O     . THR   A 1 21  ? -21.48570 11.72779  10.29140  1.000 24.25964  ?  20  THR   A O     1 
ATOM   148  C  CB    . THR   A 1 21  ? -18.22812 12.23642  10.88942  1.000 24.32731  ?  20  THR   A CB    1 
ATOM   149  O  OG1   . THR   A 1 21  ? -16.96254 11.56345  11.03573  1.000 25.16447  ?  20  THR   A OG1   1 
ATOM   150  C  CG2   . THR   A 1 21  ? -18.89575 12.34223  12.24922  1.000 20.48094  ?  20  THR   A CG2   1 
ATOM   151  N  N     . ILE   A 1 22  ? -20.51215 13.28773  9.00162   1.000 22.21616  ?  21  ILE   A N     1 
ATOM   152  C  CA    . ILE   A 1 22  ? -21.76945 14.00527  8.80427   1.000 26.80165  ?  21  ILE   A CA    1 
ATOM   153  C  C     . ILE   A 1 22  ? -22.77568 13.16091  8.01430   1.000 27.59635  ?  21  ILE   A C     1 
ATOM   154  O  O     . ILE   A 1 22  ? -23.98125 13.21354  8.28664   1.000 30.09997  ?  21  ILE   A O     1 
ATOM   155  C  CB    . ILE   A 1 22  ? -21.49788 15.37013  8.14903   1.000 28.64425  ?  21  ILE   A CB    1 
ATOM   156  C  CG1   . ILE   A 1 22  ? -20.65855 16.22360  9.11270   1.000 31.62325  ?  21  ILE   A CG1   1 
ATOM   157  C  CG2   . ILE   A 1 22  ? -22.81128 16.07778  7.77338   1.000 31.31461  ?  21  ILE   A CG2   1 
ATOM   158  C  CD1   . ILE   A 1 22  ? -20.09939 17.49273  8.50138   1.000 39.65019  ?  21  ILE   A CD1   1 
ATOM   159  N  N     . GLN   A 1 23  ? -22.31502 12.36302  7.04097   1.000 26.30212  ?  22  GLN   A N     1 
ATOM   160  C  CA    . GLN   A 1 23  ? -23.23531 11.40996  6.41657   1.000 25.61533  ?  22  GLN   A CA    1 
ATOM   161  C  C     . GLN   A 1 23  ? -23.83150 10.47258  7.45282   1.000 28.57197  ?  22  GLN   A C     1 
ATOM   162  O  O     . GLN   A 1 23  ? -25.03450 10.19468  7.42795   1.000 30.89853  ?  22  GLN   A O     1 
ATOM   163  C  CB    . GLN   A 1 23  ? -22.54661 10.57902  5.34056   1.000 28.18680  ?  22  GLN   A CB    1 
ATOM   164  C  CG    . GLN   A 1 23  ? -22.71873 11.06160  3.90298   1.000 31.32039  ?  22  GLN   A CG    1 
ATOM   165  C  CD    . GLN   A 1 23  ? -24.16897 11.17094  3.37661   1.000 32.44248  ?  22  GLN   A CD    1 
ATOM   166  O  OE1   . GLN   A 1 23  ? -25.15637 10.92568  4.07560   1.000 31.82280  ?  22  GLN   A OE1   1 
ATOM   167  N  NE2   . GLN   A 1 23  ? -24.27612 11.53461  2.10980   1.000 29.77891  ?  22  GLN   A NE2   1 
ATOM   168  N  N     . LEU   A 1 24  ? -22.99149 9.94556   8.35017   1.000 27.81197  ?  23  LEU   A N     1 
ATOM   169  C  CA    . LEU   A 1 24  ? -23.48237 9.05897   9.39414   1.000 29.67743  ?  23  LEU   A CA    1 
ATOM   170  C  C     . LEU   A 1 24  ? -24.51960 9.76133   10.26118  1.000 28.81367  ?  23  LEU   A C     1 
ATOM   171  O  O     . LEU   A 1 24  ? -25.58553 9.20724   10.52448  1.000 24.93369  ?  23  LEU   A O     1 
ATOM   172  C  CB    . LEU   A 1 24  ? -22.32265 8.55835   10.26422  1.000 29.72199  ?  23  LEU   A CB    1 
ATOM   173  C  CG    . LEU   A 1 24  ? -22.80908 7.56270   11.32805  1.000 27.65496  ?  23  LEU   A CG    1 
ATOM   174  C  CD1   . LEU   A 1 24  ? -23.12313 6.26076   10.64561  1.000 32.65115  ?  23  LEU   A CD1   1 
ATOM   175  C  CD2   . LEU   A 1 24  ? -21.82490 7.31972   12.45226  1.000 29.34322  ?  23  LEU   A CD2   1 
ATOM   176  N  N     . ILE   A 1 25  ? -24.23192 10.98989  10.68078  1.000 29.95145  ?  24  ILE   A N     1 
ATOM   177  C  CA    . ILE   A 1 25  ? -25.04433 11.71297  11.66151  1.000 31.81859  ?  24  ILE   A CA    1 
ATOM   178  C  C     . ILE   A 1 25  ? -26.24520 12.38812  11.01134  1.000 34.44556  ?  24  ILE   A C     1 
ATOM   179  O  O     . ILE   A 1 25  ? -27.36018 12.31404  11.53057  1.000 37.92994  ?  24  ILE   A O     1 
ATOM   180  C  CB    . ILE   A 1 25  ? -24.17512 12.75321  12.41857  1.000 29.04135  ?  24  ILE   A CB    1 
ATOM   181  C  CG1   . ILE   A 1 25  ? -22.99211 12.10400  13.15263  1.000 24.67551  ?  24  ILE   A CG1   1 
ATOM   182  C  CG2   . ILE   A 1 25  ? -25.01102 13.57321  13.39937  1.000 32.72097  ?  24  ILE   A CG2   1 
ATOM   183  C  CD1   . ILE   A 1 25  ? -23.38953 10.97136  14.01540  1.000 30.29640  ?  24  ILE   A CD1   1 
ATOM   184  N  N     . GLN   A 1 26  ? -26.05113 13.08221  9.88335   1.000 34.28548  ?  25  GLN   A N     1 
ATOM   185  C  CA    . GLN   A 1 26  ? -27.10075 13.92997  9.32260   1.000 36.23460  ?  25  GLN   A CA    1 
ATOM   186  C  C     . GLN   A 1 26  ? -27.62688 13.46542  7.96639   1.000 39.15039  ?  25  GLN   A C     1 
ATOM   187  O  O     . GLN   A 1 26  ? -28.54110 14.10294  7.42219   1.000 38.17661  ?  25  GLN   A O     1 
ATOM   188  C  CB    . GLN   A 1 26  ? -26.59216 15.37665  9.22340   1.000 38.08894  ?  25  GLN   A CB    1 
ATOM   189  C  CG    . GLN   A 1 26  ? -26.16856 15.94390  10.57483  1.000 44.21912  ?  25  GLN   A CG    1 
ATOM   190  C  CD    . GLN   A 1 26  ? -25.31233 17.19255  10.46257  1.000 46.17977  ?  25  GLN   A CD    1 
ATOM   191  O  OE1   . GLN   A 1 26  ? -25.09086 17.71529  9.37181   1.000 52.13754  ?  25  GLN   A OE1   1 
ATOM   192  N  NE2   . GLN   A 1 26  ? -24.82033 17.67765  11.60317  1.000 56.44937  ?  25  GLN   A NE2   1 
ATOM   193  N  N     . ASN   A 1 27  ? -27.09370 12.36939  7.41926   1.000 34.80332  ?  26  ASN   A N     1 
ATOM   194  C  CA    . ASN   A 1 27  ? -27.54270 11.76731  6.15320   1.000 30.80687  ?  26  ASN   A CA    1 
ATOM   195  C  C     . ASN   A 1 27  ? -27.46168 12.75299  4.98891   1.000 40.66046  ?  26  ASN   A C     1 
ATOM   196  O  O     . ASN   A 1 27  ? -28.33331 12.78901  4.11456   1.000 32.47134  ?  26  ASN   A O     1 
ATOM   197  C  CB    . ASN   A 1 27  ? -28.94894 11.17427  6.25092   1.000 29.33122  ?  26  ASN   A CB    1 
ATOM   198  C  CG    . ASN   A 1 27  ? -29.08929 9.86928   5.45124   1.000 38.98043  ?  26  ASN   A CG    1 
ATOM   199  O  OD1   . ASN   A 1 27  ? -28.93039 8.78956   6.01762   1.000 34.76839  ?  26  ASN   A OD1   1 
ATOM   200  N  ND2   . ASN   A 1 27  ? -29.37637 9.96569   4.11985   1.000 32.46087  ?  26  ASN   A ND2   1 
ATOM   201  N  N     . HIS   A 1 28  ? -26.39728 13.54636  4.94802   1.000 39.13647  ?  27  HIS   A N     1 
ATOM   202  C  CA    . HIS   A 1 28  ? -26.24064 14.39829  3.78438   1.000 39.74606  ?  27  HIS   A CA    1 
ATOM   203  C  C     . HIS   A 1 28  ? -24.76876 14.70061  3.56900   1.000 35.47061  ?  27  HIS   A C     1 
ATOM   204  O  O     . HIS   A 1 28  ? -23.93251 14.48809  4.45134   1.000 32.63612  ?  27  HIS   A O     1 
ATOM   205  C  CB    . HIS   A 1 28  ? -27.06592 15.67716  3.92896   1.000 42.13695  ?  27  HIS   A CB    1 
ATOM   206  C  CG    . HIS   A 1 28  ? -26.33482 16.80143  4.58378   1.000 40.83461  ?  27  HIS   A CG    1 
ATOM   207  N  ND1   . HIS   A 1 28  ? -25.69023 17.78576  3.86384   1.000 50.37660  ?  27  HIS   A ND1   1 
ATOM   208  C  CD2   . HIS   A 1 28  ? -26.17088 17.11706  5.88611   1.000 40.26467  ?  27  HIS   A CD2   1 
ATOM   209  C  CE1   . HIS   A 1 28  ? -25.14227 18.65083  4.69717   1.000 47.67857  ?  27  HIS   A CE1   1 
ATOM   210  N  NE2   . HIS   A 1 28  ? -25.41789 18.26691  5.93121   1.000 50.25371  ?  27  HIS   A NE2   1 
ATOM   211  N  N     . PHE   A 1 29  ? -24.47240 15.19994  2.37610   1.000 31.59151  ?  28  PHE   A N     1 
ATOM   212  C  CA    . PHE   A 1 29  ? -23.12215 15.44756  1.89895   1.000 31.70728  ?  28  PHE   A CA    1 
ATOM   213  C  C     . PHE   A 1 29  ? -23.07967 16.81092  1.22787   1.000 38.48852  ?  28  PHE   A C     1 
ATOM   214  O  O     . PHE   A 1 29  ? -23.97387 17.14929  0.45415   1.000 42.33310  ?  28  PHE   A O     1 
ATOM   215  C  CB    . PHE   A 1 29  ? -22.70099 14.35287  0.90005   1.000 34.80088  ?  28  PHE   A CB    1 
ATOM   216  C  CG    . PHE   A 1 29  ? -21.45940 14.67524  0.11430   1.000 35.06588  ?  28  PHE   A CG    1 
ATOM   217  C  CD1   . PHE   A 1 29  ? -20.20989 14.42050  0.64577   1.000 30.38186  ?  28  PHE   A CD1   1 
ATOM   218  C  CD2   . PHE   A 1 29  ? -21.54159 15.21533  -1.16029  1.000 30.58610  ?  28  PHE   A CD2   1 
ATOM   219  C  CE1   . PHE   A 1 29  ? -19.06516 14.70901  -0.05522  1.000 29.92214  ?  28  PHE   A CE1   1 
ATOM   220  C  CE2   . PHE   A 1 29  ? -20.40733 15.51104  -1.87481  1.000 33.53119  ?  28  PHE   A CE2   1 
ATOM   221  C  CZ    . PHE   A 1 29  ? -19.15343 15.26108  -1.31605  1.000 37.21540  ?  28  PHE   A CZ    1 
ATOM   222  N  N     . VAL   A 1 30  ? -22.03778 17.58159  1.49412   1.000 44.24265  ?  29  VAL   A N     1 
ATOM   223  C  CA    . VAL   A 1 30  ? -21.82703 18.83833  0.78684   1.000 44.48513  ?  29  VAL   A CA    1 
ATOM   224  C  C     . VAL   A 1 30  ? -20.42037 18.81183  0.21122   1.000 45.88613  ?  29  VAL   A C     1 
ATOM   225  O  O     . VAL   A 1 30  ? -19.50568 18.19715  0.77304   1.000 45.92237  ?  29  VAL   A O     1 
ATOM   226  C  CB    . VAL   A 1 30  ? -22.03177 20.09130  1.67658   1.000 50.63089  ?  29  VAL   A CB    1 
ATOM   227  C  CG1   . VAL   A 1 30  ? -20.83883 20.30446  2.60140   1.000 51.25700  ?  29  VAL   A CG1   1 
ATOM   228  C  CG2   . VAL   A 1 30  ? -22.27196 21.32630  0.80705   1.000 49.41003  ?  29  VAL   A CG2   1 
ATOM   229  N  N     . ASP   A 1 31  ? -20.24524 19.49359  -0.91650  1.000 41.84987  ?  30  ASP   A N     1 
ATOM   230  C  CA    . ASP   A 1 31  ? -18.96094 19.49688  -1.58489  1.000 38.45020  ?  30  ASP   A CA    1 
ATOM   231  C  C     . ASP   A 1 31  ? -18.00021 20.53522  -1.03212  1.000 43.08694  ?  30  ASP   A C     1 
ATOM   232  O  O     . ASP   A 1 31  ? -16.80077 20.46745  -1.33539  1.000 42.29883  ?  30  ASP   A O     1 
ATOM   233  C  CB    . ASP   A 1 31  ? -19.14600 19.71664  -3.08863  1.000 51.86699  ?  30  ASP   A CB    1 
ATOM   234  C  CG    . ASP   A 1 31  ? -18.57086 18.58139  -3.89223  1.000 56.82068  ?  30  ASP   A CG    1 
ATOM   235  O  OD1   . ASP   A 1 31  ? -17.47724 18.07325  -3.48027  1.000 52.92227  ?  30  ASP   A OD1   1 
ATOM   236  O  OD2   . ASP   A 1 31  ? -19.20634 18.16193  -4.89911  1.000 55.77969  ?  30  ASP   A OD2   1 
ATOM   237  N  N     . GLU   A 1 32  ? -18.48698 21.46624  -0.21567  1.000 40.63503  ?  31  GLU   A N     1 
ATOM   238  C  CA    . GLU   A 1 32  ? -17.63016 22.49429  0.34047   1.000 39.39095  ?  31  GLU   A CA    1 
ATOM   239  C  C     . GLU   A 1 32  ? -16.69675 21.88261  1.37740   1.000 40.73730  ?  31  GLU   A C     1 
ATOM   240  O  O     . GLU   A 1 32  ? -16.98646 20.84939  1.98692   1.000 35.20773  ?  31  GLU   A O     1 
ATOM   241  C  CB    . GLU   A 1 32  ? -18.47447 23.61138  0.95482   1.000 36.55860  ?  31  GLU   A CB    1 
ATOM   242  C  CG    . GLU   A 1 32  ? -19.26045 24.37380  -0.08373  1.000 46.86356  ?  31  GLU   A CG    1 
ATOM   243  C  CD    . GLU   A 1 32  ? -20.44130 25.12807  0.50530   1.000 51.16073  ?  31  GLU   A CD    1 
ATOM   244  O  OE1   . GLU   A 1 32  ? -20.75156 24.91630  1.70325   1.000 48.94001  ?  31  GLU   A OE1   1 
ATOM   245  O  OE2   . GLU   A 1 32  ? -21.05135 25.93819  -0.23352  1.000 49.23957  -1 31  GLU   A OE2   1 
ATOM   246  N  N     . TYR   A 1 33  ? -15.55656 22.51337  1.54634   1.000 34.89347  ?  32  TYR   A N     1 
ATOM   247  C  CA    . TYR   A 1 33  ? -14.50377 22.01736  2.41450   1.000 33.09804  ?  32  TYR   A CA    1 
ATOM   248  C  C     . TYR   A 1 33  ? -14.44077 22.95158  3.61248   1.000 30.45588  ?  32  TYR   A C     1 
ATOM   249  O  O     . TYR   A 1 33  ? -13.95130 24.08176  3.50286   1.000 33.11226  ?  32  TYR   A O     1 
ATOM   250  C  CB    . TYR   A 1 33  ? -13.17883 21.95193  1.66421   1.000 27.87816  ?  32  TYR   A CB    1 
ATOM   251  C  CG    . TYR   A 1 33  ? -12.00690 21.40207  2.43969   1.000 34.28325  ?  32  TYR   A CG    1 
ATOM   252  C  CD1   . TYR   A 1 33  ? -12.14426 20.92794  3.75412   1.000 29.89696  ?  32  TYR   A CD1   1 
ATOM   253  C  CD2   . TYR   A 1 33  ? -10.74201 21.37462  1.86967   1.000 34.17874  ?  32  TYR   A CD2   1 
ATOM   254  C  CE1   . TYR   A 1 33  ? -11.05744 20.43435  4.44709   1.000 28.61549  ?  32  TYR   A CE1   1 
ATOM   255  C  CE2   . TYR   A 1 33  ? -9.66263  20.87644  2.55970   1.000 36.78237  ?  32  TYR   A CE2   1 
ATOM   256  C  CZ    . TYR   A 1 33  ? -9.82338  20.41369  3.84508   1.000 32.20192  ?  32  TYR   A CZ    1 
ATOM   257  O  OH    . TYR   A 1 33  ? -8.72873  19.92687  4.51049   1.000 34.55237  ?  32  TYR   A OH    1 
ATOM   258  N  N     . ASP   A 1 34  ? -14.95506 22.47201  4.74485   1.000 30.07320  ?  33  ASP   A N     1 
ATOM   259  C  CA    . ASP   A 1 34  ? -14.89485 23.15138  6.03450   1.000 31.54278  ?  33  ASP   A CA    1 
ATOM   260  C  C     . ASP   A 1 34  ? -13.85353 22.38916  6.84623   1.000 28.14554  ?  33  ASP   A C     1 
ATOM   261  O  O     . ASP   A 1 34  ? -14.16448 21.33668  7.42435   1.000 30.74605  ?  33  ASP   A O     1 
ATOM   262  C  CB    . ASP   A 1 34  ? -16.26696 23.13219  6.71733   1.000 30.32486  ?  33  ASP   A CB    1 
ATOM   263  C  CG    . ASP   A 1 34  ? -16.33371 23.99929  7.96061   1.000 30.55829  ?  33  ASP   A CG    1 
ATOM   264  O  OD1   . ASP   A 1 34  ? -15.32514 24.65047  8.30657   1.000 33.07776  ?  33  ASP   A OD1   1 
ATOM   265  O  OD2   . ASP   A 1 34  ? -17.40940 24.02030  8.60556   1.000 32.83319  -1 33  ASP   A OD2   1 
ATOM   266  N  N     . PRO   A 1 35  ? -12.59537 22.83507  6.86312   1.000 28.47636  ?  34  PRO   A N     1 
ATOM   267  C  CA    . PRO   A 1 35  ? -11.55369 22.08317  7.57359   1.000 27.18667  ?  34  PRO   A CA    1 
ATOM   268  C  C     . PRO   A 1 35  ? -11.80001 22.09167  9.07474   1.000 28.33496  ?  34  PRO   A C     1 
ATOM   269  O  O     . PRO   A 1 35  ? -12.25049 23.08140  9.65606   1.000 28.35488  ?  34  PRO   A O     1 
ATOM   270  C  CB    . PRO   A 1 35  ? -10.26106 22.82497  7.20816   1.000 33.98576  ?  34  PRO   A CB    1 
ATOM   271  C  CG    . PRO   A 1 35  ? -10.71315 24.23025  6.94102   1.000 34.47416  ?  34  PRO   A CG    1 
ATOM   272  C  CD    . PRO   A 1 35  ? -12.08169 24.10155  6.30543   1.000 29.90018  ?  34  PRO   A CD    1 
ATOM   273  N  N     . THR   A 1 36  ? -11.50131 20.96590  9.69349   1.000 26.38633  ?  35  THR   A N     1 
ATOM   274  C  CA    . THR   A 1 36  ? -11.89504 20.69526  11.06765  1.000 26.33343  ?  35  THR   A CA    1 
ATOM   275  C  C     . THR   A 1 36  ? -10.85341 21.19916  12.05941  1.000 23.37894  ?  35  THR   A C     1 
ATOM   276  O  O     . THR   A 1 36  ? -9.66501  20.94262  11.88664  1.000 19.93259  ?  35  THR   A O     1 
ATOM   277  C  CB    . THR   A 1 36  ? -12.06577 19.19469  11.23576  1.000 26.03174  ?  35  THR   A CB    1 
ATOM   278  O  OG1   . THR   A 1 36  ? -13.12341 18.75369  10.37753  1.000 25.48008  ?  35  THR   A OG1   1 
ATOM   279  C  CG2   . THR   A 1 36  ? -12.35319 18.83835  12.73389  1.000 25.54967  ?  35  THR   A CG2   1 
ATOM   280  N  N     . ILE   A 1 37  ? -11.30457 21.91050  13.09266  1.000 25.41137  ?  36  ILE   A N     1 
ATOM   281  C  CA    . ILE   A 1 37  ? -10.51163 22.01768  14.31604  1.000 23.58032  ?  36  ILE   A CA    1 
ATOM   282  C  C     . ILE   A 1 37  ? -10.63826 20.73717  15.13563  1.000 20.49449  ?  36  ILE   A C     1 
ATOM   283  O  O     . ILE   A 1 37  ? -9.67225  19.98976  15.30559  1.000 20.63755  ?  36  ILE   A O     1 
ATOM   284  C  CB    . ILE   A 1 37  ? -10.91768 23.24839  15.14347  1.000 21.54176  ?  36  ILE   A CB    1 
ATOM   285  C  CG1   . ILE   A 1 37  ? -10.85240 24.53611  14.31919  1.000 25.20117  ?  36  ILE   A CG1   1 
ATOM   286  C  CG2   . ILE   A 1 37  ? -10.00676 23.34383  16.39529  1.000 24.45418  ?  36  ILE   A CG2   1 
ATOM   287  C  CD1   . ILE   A 1 37  ? -9.49698  24.78003  13.70835  1.000 28.85376  ?  36  ILE   A CD1   1 
ATOM   288  N  N     . GLU   A 1 38  ? -11.83977 20.46443  15.63886  1.000 21.18462  ?  37  GLU   A N     1 
ATOM   289  C  CA    . GLU   A 1 38  ? -12.15743 19.22623  16.33866  1.000 27.95180  ?  37  GLU   A CA    1 
ATOM   290  C  C     . GLU   A 1 38  ? -13.65924 19.19481  16.55175  1.000 23.53660  ?  37  GLU   A C     1 
ATOM   291  O  O     . GLU   A 1 38  ? -14.23636 20.18052  17.01652  1.000 23.90085  ?  37  GLU   A O     1 
ATOM   292  C  CB    . GLU   A 1 38  ? -11.41027 19.13666  17.68061  1.000 29.29299  ?  37  GLU   A CB    1 
ATOM   293  C  CG    . GLU   A 1 38  ? -11.51998 17.79449  18.37279  1.000 34.89373  ?  37  GLU   A CG    1 
ATOM   294  C  CD    . GLU   A 1 38  ? -10.62661 17.69104  19.61171  1.000 39.95188  ?  37  GLU   A CD    1 
ATOM   295  O  OE1   . GLU   A 1 38  ? -9.40649  17.43219  19.45473  1.000 48.66935  ?  37  GLU   A OE1   1 
ATOM   296  O  OE2   . GLU   A 1 38  ? -11.14724 17.85735  20.73228  1.000 38.98960  -1 37  GLU   A OE2   1 
ATOM   297  N  N     . ASP   A 1 39  ? -14.31527 18.09612  16.22170  1.000 21.62107  ?  38  ASP   A N     1 
ATOM   298  C  CA    . ASP   A 1 39  ? -15.74662 18.01049  16.43781  1.000 27.87545  ?  38  ASP   A CA    1 
ATOM   299  C  C     . ASP   A 1 39  ? -16.11155 16.67397  17.06836  1.000 25.56505  ?  38  ASP   A C     1 
ATOM   300  O  O     . ASP   A 1 39  ? -15.40245 15.67346  16.92304  1.000 26.59310  ?  38  ASP   A O     1 
ATOM   301  C  CB    . ASP   A 1 39  ? -16.51455 18.22144  15.11998  1.000 27.99020  ?  38  ASP   A CB    1 
ATOM   302  C  CG    . ASP   A 1 39  ? -16.55970 19.69423  14.71472  1.000 33.09979  ?  38  ASP   A CG    1 
ATOM   303  O  OD1   . ASP   A 1 39  ? -17.18959 20.50351  15.43898  1.000 36.31732  ?  38  ASP   A OD1   1 
ATOM   304  O  OD2   . ASP   A 1 39  ? -15.92240 20.04794  13.71077  1.000 34.07777  -1 38  ASP   A OD2   1 
ATOM   305  N  N     . SER   A 1 40  ? -17.25355 16.67241  17.74533  1.000 22.96335  ?  39  SER   A N     1 
ATOM   306  C  CA    . SER   A 1 40  ? -17.75237 15.51214  18.46334  1.000 23.90367  ?  39  SER   A CA    1 
ATOM   307  C  C     . SER   A 1 40  ? -19.23026 15.33140  18.18266  1.000 23.94043  ?  39  SER   A C     1 
ATOM   308  O  O     . SER   A 1 40  ? -19.98680 16.29969  18.08051  1.000 25.80177  ?  39  SER   A O     1 
ATOM   309  C  CB    . SER   A 1 40  ? -17.55658 15.63886  19.97701  1.000 27.09455  ?  39  SER   A CB    1 
ATOM   310  O  OG    . SER   A 1 40  ? -16.20205 15.46209  20.31827  1.000 40.30331  ?  39  SER   A OG    1 
ATOM   311  N  N     . TYR   A 1 41  ? -19.64057 14.07401  18.10820  1.000 25.48871  ?  40  TYR   A N     1 
ATOM   312  C  CA    . TYR   A 1 41  ? -21.00635 13.70930  17.78449  1.000 23.98186  ?  40  TYR   A CA    1 
ATOM   313  C  C     . TYR   A 1 41  ? -21.42182 12.50656  18.62471  1.000 25.76112  ?  40  TYR   A C     1 
ATOM   314  O  O     . TYR   A 1 41  ? -20.58694 11.74235  19.11081  1.000 26.61054  ?  40  TYR   A O     1 
ATOM   315  C  CB    . TYR   A 1 41  ? -21.15488 13.37378  16.29542  1.000 25.60959  ?  40  TYR   A CB    1 
ATOM   316  C  CG    . TYR   A 1 41  ? -20.66667 14.47583  15.39999  1.000 28.66783  ?  40  TYR   A CG    1 
ATOM   317  C  CD1   . TYR   A 1 41  ? -21.49354 15.54866  15.09371  1.000 26.99696  ?  40  TYR   A CD1   1 
ATOM   318  C  CD2   . TYR   A 1 41  ? -19.36238 14.47630  14.89539  1.000 22.94577  ?  40  TYR   A CD2   1 
ATOM   319  C  CE1   . TYR   A 1 41  ? -21.06186 16.57445  14.28992  1.000 30.35242  ?  40  TYR   A CE1   1 
ATOM   320  C  CE2   . TYR   A 1 41  ? -18.91577 15.50563  14.07082  1.000 29.24446  ?  40  TYR   A CE2   1 
ATOM   321  C  CZ    . TYR   A 1 41  ? -19.78132 16.54993  13.77103  1.000 30.28257  ?  40  TYR   A CZ    1 
ATOM   322  O  OH    . TYR   A 1 41  ? -19.37800 17.58914  12.97284  1.000 32.46579  ?  40  TYR   A OH    1 
ATOM   323  N  N     . ARG   A 1 42  ? -22.73185 12.34112  18.76602  1.000 24.62203  ?  41  ARG   A N     1 
ATOM   324  C  CA    . ARG   A 1 42  ? -23.33779 11.21328  19.45520  1.000 25.23916  ?  41  ARG   A CA    1 
ATOM   325  C  C     . ARG   A 1 42  ? -24.40423 10.63676  18.54251  1.000 23.11395  ?  41  ARG   A C     1 
ATOM   326  O  O     . ARG   A 1 42  ? -25.17108 11.39068  17.94073  1.000 22.17616  ?  41  ARG   A O     1 
ATOM   327  C  CB    . ARG   A 1 42  ? -23.97176 11.64640  20.79321  1.000 27.12464  ?  41  ARG   A CB    1 
ATOM   328  C  CG    . ARG   A 1 42  ? -22.99584 12.03026  21.90446  1.000 31.10390  ?  41  ARG   A CG    1 
ATOM   329  C  CD    . ARG   A 1 42  ? -22.31243 10.76854  22.39910  1.000 35.83454  ?  41  ARG   A CD    1 
ATOM   330  N  NE    . ARG   A 1 42  ? -21.29053 10.98835  23.41925  1.000 36.65348  ?  41  ARG   A NE    1 
ATOM   331  C  CZ    . ARG   A 1 42  ? -21.49746 10.82712  24.71848  1.000 41.72532  ?  41  ARG   A CZ    1 
ATOM   332  N  NH1   . ARG   A 1 42  ? -22.71007 10.59770  25.19488  1.000 30.94950  ?  41  ARG   A NH1   1 
ATOM   333  N  NH2   . ARG   A 1 42  ? -20.45824 10.88360  25.55641  1.000 38.25804  ?  41  ARG   A NH2   1 
ATOM   334  N  N     . LYS   A 1 43  ? -24.48304 9.31535   18.46115  1.000 28.31717  ?  42  LYS   A N     1 
ATOM   335  C  CA    . LYS   A 1 43  ? -25.58262 8.69402   17.73515  1.000 25.85167  ?  42  LYS   A CA    1 
ATOM   336  C  C     . LYS   A 1 43  ? -25.85410 7.30167   18.28652  1.000 24.47216  ?  42  LYS   A C     1 
ATOM   337  O  O     . LYS   A 1 43  ? -24.92368 6.53064   18.53080  1.000 26.31168  ?  42  LYS   A O     1 
ATOM   338  C  CB    . LYS   A 1 43  ? -25.29480 8.58881   16.22815  1.000 25.94607  ?  42  LYS   A CB    1 
ATOM   339  C  CG    . LYS   A 1 43  ? -26.46960 8.01030   15.45240  1.000 21.34439  ?  42  LYS   A CG    1 
ATOM   340  C  CD    . LYS   A 1 43  ? -26.14037 7.82767   13.95789  1.000 33.21136  ?  42  LYS   A CD    1 
ATOM   341  C  CE    . LYS   A 1 43  ? -27.41951 7.61666   13.15130  1.000 29.63863  ?  42  LYS   A CE    1 
ATOM   342  N  NZ    . LYS   A 1 43  ? -27.08556 7.14283   11.81154  1.000 47.39728  ?  42  LYS   A NZ    1 
ATOM   343  N  N     . GLN   A 1 44  ? -27.12467 6.96195   18.45797  1.000 25.84142  ?  43  GLN   A N     1 
ATOM   344  C  CA    . GLN   A 1 44  ? -27.45851 5.59545   18.82710  1.000 29.78043  ?  43  GLN   A CA    1 
ATOM   345  C  C     . GLN   A 1 44  ? -27.84114 4.82803   17.57327  1.000 27.45609  ?  43  GLN   A C     1 
ATOM   346  O  O     . GLN   A 1 44  ? -28.46652 5.37021   16.65131  1.000 31.01122  ?  43  GLN   A O     1 
ATOM   347  C  CB    . GLN   A 1 44  ? -28.57458 5.51634   19.88604  1.000 29.14023  ?  43  GLN   A CB    1 
ATOM   348  C  CG    . GLN   A 1 44  ? -29.99135 5.57953   19.36994  1.000 37.51781  ?  43  GLN   A CG    1 
ATOM   349  C  CD    . GLN   A 1 44  ? -31.03170 5.30826   20.45209  1.000 31.82665  ?  43  GLN   A CD    1 
ATOM   350  O  OE1   . GLN   A 1 44  ? -31.32066 4.16130   20.77927  1.000 33.89297  ?  43  GLN   A OE1   1 
ATOM   351  N  NE2   . GLN   A 1 44  ? -31.59908 6.36937   21.00263  1.000 27.47585  ?  43  GLN   A NE2   1 
ATOM   352  N  N     . VAL   A 1 45  ? -27.39826 3.58051   17.52543  1.000 28.10015  ?  44  VAL   A N     1 
ATOM   353  C  CA    . VAL   A 1 45  ? -27.55082 2.70588   16.37138  1.000 31.20354  ?  44  VAL   A CA    1 
ATOM   354  C  C     . VAL   A 1 45  ? -27.77303 1.30441   16.91477  1.000 35.74733  ?  44  VAL   A C     1 
ATOM   355  O  O     . VAL   A 1 45  ? -27.56695 1.04187   18.10263  1.000 33.67471  ?  44  VAL   A O     1 
ATOM   356  C  CB    . VAL   A 1 45  ? -26.31217 2.72095   15.43848  1.000 30.00421  ?  44  VAL   A CB    1 
ATOM   357  C  CG1   . VAL   A 1 45  ? -26.05866 4.11126   14.85983  1.000 28.93178  ?  44  VAL   A CG1   1 
ATOM   358  C  CG2   . VAL   A 1 45  ? -25.09725 2.22591   16.17495  1.000 27.80315  ?  44  VAL   A CG2   1 
ATOM   359  N  N     . VAL   A 1 46  ? -28.17823 0.39992   16.02564  1.000 35.21263  ?  45  VAL   A N     1 
ATOM   360  C  CA    . VAL   A 1 46  ? -28.28923 -1.02292  16.32993  1.000 37.59244  ?  45  VAL   A CA    1 
ATOM   361  C  C     . VAL   A 1 46  ? -27.27902 -1.76510  15.47677  1.000 34.79713  ?  45  VAL   A C     1 
ATOM   362  O  O     . VAL   A 1 46  ? -27.27329 -1.61773  14.25100  1.000 36.68773  ?  45  VAL   A O     1 
ATOM   363  C  CB    . VAL   A 1 46  ? -29.70957 -1.55079  16.07985  1.000 40.07290  ?  45  VAL   A CB    1 
ATOM   364  C  CG1   . VAL   A 1 46  ? -29.87823 -2.93905  16.69155  1.000 37.85792  ?  45  VAL   A CG1   1 
ATOM   365  C  CG2   . VAL   A 1 46  ? -30.72747 -0.57965  16.64874  1.000 45.19834  ?  45  VAL   A CG2   1 
ATOM   366  N  N     . ILE   A 1 47  ? -26.41285 -2.54594  16.12264  1.000 37.49465  ?  46  ILE   A N     1 
ATOM   367  C  CA    . ILE   A 1 47  ? -25.37546 -3.30905  15.43953  1.000 39.05237  ?  46  ILE   A CA    1 
ATOM   368  C  C     . ILE   A 1 47  ? -25.44955 -4.75004  15.91822  1.000 41.70687  ?  46  ILE   A C     1 
ATOM   369  O  O     . ILE   A 1 47  ? -25.25929 -5.02305  17.10987  1.000 41.24778  ?  46  ILE   A O     1 
ATOM   370  C  CB    . ILE   A 1 47  ? -23.97054 -2.73376  15.68036  1.000 40.06956  ?  46  ILE   A CB    1 
ATOM   371  C  CG1   . ILE   A 1 47  ? -23.87014 -1.30568  15.14306  1.000 33.09772  ?  46  ILE   A CG1   1 
ATOM   372  C  CG2   . ILE   A 1 47  ? -22.89200 -3.62792  15.04138  1.000 35.92417  ?  46  ILE   A CG2   1 
ATOM   373  C  CD1   . ILE   A 1 47  ? -22.68356 -0.57296  15.70812  1.000 37.93876  ?  46  ILE   A CD1   1 
ATOM   374  N  N     . ASP   A 1 48  ? -25.69661 -5.66849  14.98614  1.000 43.97795  ?  47  ASP   A N     1 
ATOM   375  C  CA    . ASP   A 1 48  ? -25.85991 -7.08276  15.29738  1.000 42.52441  ?  47  ASP   A CA    1 
ATOM   376  C  C     . ASP   A 1 48  ? -26.92996 -7.26060  16.36864  1.000 43.22445  ?  47  ASP   A C     1 
ATOM   377  O  O     . ASP   A 1 48  ? -26.76474 -8.00705  17.33072  1.000 52.34006  ?  47  ASP   A O     1 
ATOM   378  C  CB    . ASP   A 1 48  ? -24.53267 -7.71713  15.72336  1.000 41.31620  ?  47  ASP   A CB    1 
ATOM   379  C  CG    . ASP   A 1 48  ? -23.44908 -7.60780  14.65414  1.000 44.66741  ?  47  ASP   A CG    1 
ATOM   380  O  OD1   . ASP   A 1 48  ? -23.76756 -7.47109  13.45366  1.000 46.16137  ?  47  ASP   A OD1   1 
ATOM   381  O  OD2   . ASP   A 1 48  ? -22.25954 -7.66723  15.02119  1.000 51.15127  -1 47  ASP   A OD2   1 
ATOM   382  N  N     . GLY   A 1 49  ? -28.03848 -6.54025  16.19831  1.000 48.05123  ?  48  GLY   A N     1 
ATOM   383  C  CA    . GLY   A 1 49  ? -29.16063 -6.60647  17.11325  1.000 46.71112  ?  48  GLY   A CA    1 
ATOM   384  C  C     . GLY   A 1 49  ? -28.98819 -5.86861  18.42631  1.000 50.23419  ?  48  GLY   A C     1 
ATOM   385  O  O     . GLY   A 1 49  ? -29.96943 -5.70875  19.16304  1.000 47.81446  ?  48  GLY   A O     1 
ATOM   386  N  N     . GLU   A 1 50  ? -27.79004 -5.40274  18.75139  1.000 50.01042  ?  49  GLU   A N     1 
ATOM   387  C  CA    . GLU   A 1 50  ? -27.53189 -4.78112  20.04118  1.000 43.97139  ?  49  GLU   A CA    1 
ATOM   388  C  C     . GLU   A 1 50  ? -27.48533 -3.26623  19.87888  1.000 49.84270  ?  49  GLU   A C     1 
ATOM   389  O  O     . GLU   A 1 50  ? -26.68493 -2.74394  19.09238  1.000 48.13386  ?  49  GLU   A O     1 
ATOM   390  C  CB    . GLU   A 1 50  ? -26.23144 -5.30199  20.64204  1.000 46.17033  ?  49  GLU   A CB    1 
ATOM   391  C  CG    . GLU   A 1 50  ? -25.94399 -4.72045  22.00384  1.000 50.30459  ?  49  GLU   A CG    1 
ATOM   392  C  CD    . GLU   A 1 50  ? -25.02041 -5.58646  22.83106  1.000 58.45843  ?  49  GLU   A CD    1 
ATOM   393  O  OE1   . GLU   A 1 50  ? -24.18642 -6.30312  22.23856  1.000 59.87819  ?  49  GLU   A OE1   1 
ATOM   394  O  OE2   . GLU   A 1 50  ? -25.13184 -5.55148  24.07992  1.000 67.96372  -1 49  GLU   A OE2   1 
ATOM   395  N  N     . THR   A 1 51  ? -28.33873 -2.56903  20.62372  1.000 43.20023  ?  50  THR   A N     1 
ATOM   396  C  CA    . THR   A 1 51  ? -28.33821 -1.11214  20.61845  1.000 46.81200  ?  50  THR   A CA    1 
ATOM   397  C  C     . THR   A 1 51  ? -27.12438 -0.56825  21.37510  1.000 47.51712  ?  50  THR   A C     1 
ATOM   398  O  O     . THR   A 1 51  ? -26.75190 -1.07758  22.43482  1.000 45.42235  ?  50  THR   A O     1 
ATOM   399  C  CB    . THR   A 1 51  ? -29.64085 -0.60005  21.23364  1.000 48.83206  ?  50  THR   A CB    1 
ATOM   400  O  OG1   . THR   A 1 51  ? -30.74163 -1.11787  20.47762  1.000 54.37387  ?  50  THR   A OG1   1 
ATOM   401  C  CG2   . THR   A 1 51  ? -29.70885 0.91662   21.21469  1.000 47.45356  ?  50  THR   A CG2   1 
ATOM   402  N  N     . CYS   A 1 52  ? -26.48400 0.45478   20.80891  1.000 41.05902  ?  51  CYS   A N     1 
ATOM   403  C  CA    . CYS   A 1 52  ? -25.33413 1.07796   21.45567  1.000 37.92521  ?  51  CYS   A CA    1 
ATOM   404  C  C     . CYS   A 1 52  ? -25.22358 2.52829   21.01776  1.000 32.32807  ?  51  CYS   A C     1 
ATOM   405  O  O     . CYS   A 1 52  ? -25.81931 2.94561   20.02548  1.000 32.17094  ?  51  CYS   A O     1 
ATOM   406  C  CB    . CYS   A 1 52  ? -24.03350 0.34763   21.13648  1.000 40.31816  ?  51  CYS   A CB    1 
ATOM   407  S  SG    . CYS   A 1 52  ? -23.79370 0.07391   19.37391  1.000 39.92649  ?  51  CYS   A SG    1 
ATOM   408  N  N     . LEU   A 1 53  ? -24.44756 3.29081   21.78031  1.000 27.90349  ?  52  LEU   A N     1 
ATOM   409  C  CA    . LEU   A 1 53  ? -24.28309 4.72355   21.57085  1.000 30.53435  ?  52  LEU   A CA    1 
ATOM   410  C  C     . LEU   A 1 53  ? -22.87928 4.98814   21.03466  1.000 31.78351  ?  52  LEU   A C     1 
ATOM   411  O  O     . LEU   A 1 53  ? -21.88836 4.65148   21.69052  1.000 36.56556  ?  52  LEU   A O     1 
ATOM   412  C  CB    . LEU   A 1 53  ? -24.52600 5.48725   22.87282  1.000 30.81403  ?  52  LEU   A CB    1 
ATOM   413  C  CG    . LEU   A 1 53  ? -24.41294 7.01339   22.85043  1.000 38.05294  ?  52  LEU   A CG    1 
ATOM   414  C  CD1   . LEU   A 1 53  ? -25.35706 7.60867   21.80623  1.000 31.74997  ?  52  LEU   A CD1   1 
ATOM   415  C  CD2   . LEU   A 1 53  ? -24.71689 7.58447   24.24317  1.000 37.37754  ?  52  LEU   A CD2   1 
ATOM   416  N  N     . LEU   A 1 54  ? -22.79651 5.59960   19.85773  1.000 25.24953  ?  53  LEU   A N     1 
ATOM   417  C  CA    . LEU   A 1 54  ? -21.51569 5.96654   19.26785  1.000 26.94767  ?  53  LEU   A CA    1 
ATOM   418  C  C     . LEU   A 1 54  ? -21.13163 7.37098   19.70953  1.000 27.79809  ?  53  LEU   A C     1 
ATOM   419  O  O     . LEU   A 1 54  ? -21.91241 8.31111   19.56148  1.000 26.18719  ?  53  LEU   A O     1 
ATOM   420  C  CB    . LEU   A 1 54  ? -21.57588 5.89646   17.74058  1.000 24.81999  ?  53  LEU   A CB    1 
ATOM   421  C  CG    . LEU   A 1 54  ? -22.10582 4.61672   17.09991  1.000 30.02811  ?  53  LEU   A CG    1 
ATOM   422  C  CD1   . LEU   A 1 54  ? -21.87117 4.63554   15.60180  1.000 22.39369  ?  53  LEU   A CD1   1 
ATOM   423  C  CD2   . LEU   A 1 54  ? -21.50203 3.37238   17.73252  1.000 33.20610  ?  53  LEU   A CD2   1 
ATOM   424  N  N     . ASP   A 1 55  ? -19.94228 7.50177   20.28308  1.000 27.59624  ?  54  ASP   A N     1 
ATOM   425  C  CA    . ASP   A 1 55  ? -19.33583 8.78974   20.59043  1.000 27.20671  ?  54  ASP   A CA    1 
ATOM   426  C  C     . ASP   A 1 55  ? -18.20830 8.94834   19.57575  1.000 28.43865  ?  54  ASP   A C     1 
ATOM   427  O  O     . ASP   A 1 55  ? -17.26849 8.14494   19.55407  1.000 23.09461  ?  54  ASP   A O     1 
ATOM   428  C  CB    . ASP   A 1 55  ? -18.84389 8.80367   22.03524  1.000 30.26238  ?  54  ASP   A CB    1 
ATOM   429  C  CG    . ASP   A 1 55  ? -18.22331 10.13607  22.45902  1.000 33.76528  ?  54  ASP   A CG    1 
ATOM   430  O  OD1   . ASP   A 1 55  ? -17.36536 10.67873  21.73401  1.000 43.24268  ?  54  ASP   A OD1   1 
ATOM   431  O  OD2   . ASP   A 1 55  ? -18.56843 10.62255  23.56209  1.000 46.80851  -1 54  ASP   A OD2   1 
ATOM   432  N  N     . ILE   A 1 56  ? -18.33130 9.93000   18.68428  1.000 29.20834  ?  55  ILE   A N     1 
ATOM   433  C  CA    . ILE   A 1 56  ? -17.43947 10.02485  17.53979  1.000 23.57197  ?  55  ILE   A CA    1 
ATOM   434  C  C     . ILE   A 1 56  ? -16.66128 11.31639  17.66119  1.000 24.15529  ?  55  ILE   A C     1 
ATOM   435  O  O     . ILE   A 1 56  ? -17.25191 12.39605  17.76926  1.000 25.09434  ?  55  ILE   A O     1 
ATOM   436  C  CB    . ILE   A 1 56  ? -18.18929 9.94138   16.20303  1.000 23.51011  ?  55  ILE   A CB    1 
ATOM   437  C  CG1   . ILE   A 1 56  ? -18.89734 8.59077   16.12546  1.000 30.51319  ?  55  ILE   A CG1   1 
ATOM   438  C  CG2   . ILE   A 1 56  ? -17.19312 10.08240  15.01972  1.000 21.48930  ?  55  ILE   A CG2   1 
ATOM   439  C  CD1   . ILE   A 1 56  ? -19.94025 8.50074   15.07053  1.000 26.17738  ?  55  ILE   A CD1   1 
ATOM   440  N  N     . LEU   A 1 57  ? -15.33785 11.19921  17.65210  1.000 24.06843  ?  56  LEU   A N     1 
ATOM   441  C  CA    . LEU   A 1 57  ? -14.43816 12.33912  17.57665  1.000 24.75648  ?  56  LEU   A CA    1 
ATOM   442  C  C     . LEU   A 1 57  ? -13.94532 12.50402  16.14245  1.000 21.36672  ?  56  LEU   A C     1 
ATOM   443  O  O     . LEU   A 1 57  ? -13.24207 11.63090  15.61402  1.000 23.19224  ?  56  LEU   A O     1 
ATOM   444  C  CB    . LEU   A 1 57  ? -13.25159 12.17134  18.51784  1.000 21.83248  ?  56  LEU   A CB    1 
ATOM   445  C  CG    . LEU   A 1 57  ? -12.38196 13.42588  18.66726  1.000 23.59735  ?  56  LEU   A CG    1 
ATOM   446  C  CD1   . LEU   A 1 57  ? -13.17192 14.56269  19.29875  1.000 25.29331  ?  56  LEU   A CD1   1 
ATOM   447  C  CD2   . LEU   A 1 57  ? -11.14402 13.12348  19.48661  1.000 25.56737  ?  56  LEU   A CD2   1 
ATOM   448  N  N     . ASP   A 1 58  ? -14.25824 13.65155  15.54701  1.000 22.01269  ?  57  ASP   A N     1 
ATOM   449  C  CA    . ASP   A 1 58  ? -13.81362 14.02619  14.20139  1.000 25.14457  ?  57  ASP   A CA    1 
ATOM   450  C  C     . ASP   A 1 58  ? -12.61262 14.96092  14.36032  1.000 28.21599  ?  57  ASP   A C     1 
ATOM   451  O  O     . ASP   A 1 58  ? -12.75201 16.09527  14.84489  1.000 28.66380  ?  57  ASP   A O     1 
ATOM   452  C  CB    . ASP   A 1 58  ? -14.95737 14.68750  13.43486  1.000 24.56978  ?  57  ASP   A CB    1 
ATOM   453  C  CG    . ASP   A 1 58  ? -14.58377 15.09558  11.99675  1.000 26.70382  ?  57  ASP   A CG    1 
ATOM   454  O  OD1   . ASP   A 1 58  ? -13.57191 14.61070  11.45036  1.000 25.54173  ?  57  ASP   A OD1   1 
ATOM   455  O  OD2   . ASP   A 1 58  ? -15.33051 15.91064  11.39964  1.000 29.33681  -1 57  ASP   A OD2   1 
ATOM   456  N  N     . THR   A 1 59  ? -11.43453 14.47560  13.98721  1.000 23.24743  ?  58  THR   A N     1 
ATOM   457  C  CA    . THR   A 1 59  ? -10.16726 15.13666  14.28449  1.000 25.16885  ?  58  THR   A CA    1 
ATOM   458  C  C     . THR   A 1 59  ? -9.61145  15.89627  13.07436  1.000 27.55393  ?  58  THR   A C     1 
ATOM   459  O  O     . THR   A 1 59  ? -10.01458 15.66902  11.92966  1.000 25.63501  ?  58  THR   A O     1 
ATOM   460  C  CB    . THR   A 1 59  ? -9.15078  14.10211  14.73866  1.000 25.40884  ?  58  THR   A CB    1 
ATOM   461  O  OG1   . THR   A 1 59  ? -8.72481  13.33935  13.59975  1.000 25.24963  ?  58  THR   A OG1   1 
ATOM   462  C  CG2   . THR   A 1 59  ? -9.80591  13.17474  15.76219  1.000 25.29542  ?  58  THR   A CG2   1 
ATOM   463  N  N     . ALA   A 1 60  ? -8.66890  16.80367  13.35039  1.000 22.99577  ?  59  ALA   A N     1 
ATOM   464  C  CA    . ALA   A 1 60  ? -8.04121  17.60198  12.29872  1.000 25.25370  ?  59  ALA   A CA    1 
ATOM   465  C  C     . ALA   A 1 60  ? -7.02179  16.77937  11.52774  1.000 28.55768  ?  59  ALA   A C     1 
ATOM   466  O  O     . ALA   A 1 60  ? -6.24358  16.02186  12.11543  1.000 28.27751  ?  59  ALA   A O     1 
ATOM   467  C  CB    . ALA   A 1 60  ? -7.35728  18.84516  12.87741  1.000 24.20155  ?  59  ALA   A CB    1 
ATOM   468  N  N     . GLY   A 1 61  ? -7.05565  16.91423  10.19339  1.000 28.08790  ?  60  GLY   A N     1 
ATOM   469  C  CA    . GLY   A 1 61  ? -5.97386  16.42939  9.36190   1.000 31.72387  ?  60  GLY   A CA    1 
ATOM   470  C  C     . GLY   A 1 61  ? -4.76681  17.34856  9.27594   1.000 33.31420  ?  60  GLY   A C     1 
ATOM   471  O  O     . GLY   A 1 61  ? -3.77193  16.95379  8.65858   1.000 31.50604  ?  60  GLY   A O     1 
ATOM   472  N  N     . GLN   A 1 62  ? -4.83193  18.55754  9.85534   1.000 28.55256  ?  61  GLN   A N     1 
ATOM   473  C  CA    . GLN   A 1 62  ? -3.72805  19.51391  9.72822   1.000 38.30889  ?  61  GLN   A CA    1 
ATOM   474  C  C     . GLN   A 1 62  ? -2.44696  18.92692  10.28832  1.000 35.11882  ?  61  GLN   A C     1 
ATOM   475  O  O     . GLN   A 1 62  ? -2.36111  18.63955  11.48511  1.000 43.79047  ?  61  GLN   A O     1 
ATOM   476  C  CB    . GLN   A 1 62  ? -4.03158  20.82265  10.45471  1.000 37.45358  ?  61  GLN   A CB    1 
ATOM   477  C  CG    . GLN   A 1 62  ? -4.83529  21.81960  9.69685   1.000 35.40731  ?  61  GLN   A CG    1 
ATOM   478  C  CD    . GLN   A 1 62  ? -4.24185  22.23553  8.35286   1.000 33.60199  ?  61  GLN   A CD    1 
ATOM   479  O  OE1   . GLN   A 1 62  ? -4.98548  22.53096  7.43696   1.000 38.06151  ?  61  GLN   A OE1   1 
ATOM   480  N  NE2   . GLN   A 1 62  ? -2.91164  22.28726  8.24305   1.000 46.73841  ?  61  GLN   A NE2   1 
ATOM   481  N  N     . GLU   A 1 63  ? -1.44064  18.78096  9.42681   1.000 35.13827  ?  62  GLU   A N     1 
ATOM   482  C  CA    . GLU   A 1 63  ? -0.22552  18.08766  9.82453   1.000 39.11967  ?  62  GLU   A CA    1 
ATOM   483  C  C     . GLU   A 1 63  ? 0.58888   18.88126  10.84225  1.000 38.14775  ?  62  GLU   A C     1 
ATOM   484  O  O     . GLU   A 1 63  ? 1.31998   18.28046  11.63680  1.000 38.29287  ?  62  GLU   A O     1 
ATOM   485  C  CB    . GLU   A 1 63  ? 0.62128   17.76430  8.59223   1.000 43.01606  ?  62  GLU   A CB    1 
ATOM   486  C  CG    . GLU   A 1 63  ? 1.25585   16.38295  8.66922   1.000 52.25746  ?  62  GLU   A CG    1 
ATOM   487  C  CD    . GLU   A 1 63  ? 1.41502   15.71647  7.30995   1.000 63.64692  ?  62  GLU   A CD    1 
ATOM   488  O  OE1   . GLU   A 1 63  ? 2.37029   16.07686  6.57491   1.000 64.70870  ?  62  GLU   A OE1   1 
ATOM   489  O  OE2   . GLU   A 1 63  ? 0.57690   14.83504  6.97691   1.000 64.95304  -1 62  GLU   A OE2   1 
ATOM   490  N  N     . GLU   A 1 64  ? 0.46719   20.21353  10.86335  1.000 31.29272  ?  63  GLU   A N     1 
ATOM   491  C  CA    . GLU   A 1 64  ? 1.30681   21.00275  11.76526  1.000 39.55288  ?  63  GLU   A CA    1 
ATOM   492  C  C     . GLU   A 1 64  ? 1.03620   20.71666  13.23242  1.000 39.26032  ?  63  GLU   A C     1 
ATOM   493  O  O     . GLU   A 1 64  ? 1.83364   21.13026  14.08290  1.000 36.18926  ?  63  GLU   A O     1 
ATOM   494  C  CB    . GLU   A 1 64  ? 1.12083   22.50466  11.52369  1.000 36.20266  ?  63  GLU   A CB    1 
ATOM   495  C  CG    . GLU   A 1 64  ? 1.55433   22.97110  10.12970  1.000 43.22057  ?  63  GLU   A CG    1 
ATOM   496  C  CD    . GLU   A 1 64  ? 0.51120   22.65725  9.05265   1.000 47.13400  ?  63  GLU   A CD    1 
ATOM   497  O  OE1   . GLU   A 1 64  ? -0.53186  22.05686  9.40153   1.000 43.37872  ?  63  GLU   A OE1   1 
ATOM   498  O  OE2   . GLU   A 1 64  ? 0.74242   22.99958  7.86491   1.000 47.77615  -1 63  GLU   A OE2   1 
ATOM   499  N  N     . TYR   A 1 65  ? -0.06404  20.04188  13.56000  1.000 33.78889  ?  64  TYR   A N     1 
ATOM   500  C  CA    . TYR   A 1 65  ? -0.40833  19.77704  14.94743  1.000 34.75062  ?  64  TYR   A CA    1 
ATOM   501  C  C     . TYR   A 1 65  ? -0.27219  18.29279  15.28503  1.000 35.19501  ?  64  TYR   A C     1 
ATOM   502  O  O     . TYR   A 1 65  ? -0.91453  17.78515  16.20455  1.000 32.16663  ?  64  TYR   A O     1 
ATOM   503  C  CB    . TYR   A 1 65  ? -1.80140  20.33857  15.23464  1.000 33.99916  ?  64  TYR   A CB    1 
ATOM   504  C  CG    . TYR   A 1 65  ? -1.88405  21.79773  14.77916  1.000 32.59011  ?  64  TYR   A CG    1 
ATOM   505  C  CD1   . TYR   A 1 65  ? -1.19844  22.78964  15.46602  1.000 33.33489  ?  64  TYR   A CD1   1 
ATOM   506  C  CD2   . TYR   A 1 65  ? -2.59470  22.17253  13.62648  1.000 35.38279  ?  64  TYR   A CD2   1 
ATOM   507  C  CE1   . TYR   A 1 65  ? -1.23300  24.12645  15.04671  1.000 30.06235  ?  64  TYR   A CE1   1 
ATOM   508  C  CE2   . TYR   A 1 65  ? -2.63225  23.50888  13.19899  1.000 27.17516  ?  64  TYR   A CE2   1 
ATOM   509  C  CZ    . TYR   A 1 65  ? -1.94378  24.47939  13.92803  1.000 29.56492  ?  64  TYR   A CZ    1 
ATOM   510  O  OH    . TYR   A 1 65  ? -1.95144  25.79469  13.55032  1.000 31.77571  ?  64  TYR   A OH    1 
ATOM   511  N  N     . SER   A 1 66  ? 0.62744   17.60387  14.57952  1.000 38.98924  ?  65  SER   A N     1 
ATOM   512  C  CA    . SER   A 1 66  ? 0.78675   16.16604  14.77210  1.000 39.33199  ?  65  SER   A CA    1 
ATOM   513  C  C     . SER   A 1 66  ? 1.21564   15.83376  16.19739  1.000 33.07180  ?  65  SER   A C     1 
ATOM   514  O  O     . SER   A 1 66  ? 0.90448   14.75111  16.70473  1.000 37.35754  ?  65  SER   A O     1 
ATOM   515  C  CB    . SER   A 1 66  ? 1.77405   15.61134  13.73244  1.000 41.57937  ?  65  SER   A CB    1 
ATOM   516  O  OG    . SER   A 1 66  ? 2.98401   16.36294  13.67645  1.000 45.20054  ?  65  SER   A OG    1 
ATOM   517  N  N     . ALA   A 1 67  ? 1.87345   16.76559  16.88015  1.000 37.75666  ?  66  ALA   A N     1 
ATOM   518  C  CA    . ALA   A 1 67  ? 2.29353   16.52652  18.25662  1.000 42.10212  ?  66  ALA   A CA    1 
ATOM   519  C  C     . ALA   A 1 67  ? 1.15756   16.65390  19.26693  1.000 38.75096  ?  66  ALA   A C     1 
ATOM   520  O  O     . ALA   A 1 67  ? 1.40932   16.53839  20.47148  1.000 39.21288  ?  66  ALA   A O     1 
ATOM   521  C  CB    . ALA   A 1 67  ? 3.41242   17.50421  18.62426  1.000 47.85685  ?  66  ALA   A CB    1 
ATOM   522  N  N     . MET   A 1 68  ? -0.07558  16.90105  18.83153  1.000 32.03346  ?  67  MET   A N     1 
ATOM   523  C  CA    . MET   A 1 68  ? -1.17439  17.20710  19.74224  1.000 35.05350  ?  67  MET   A CA    1 
ATOM   524  C  C     . MET   A 1 68  ? -2.26122  16.14675  19.72533  1.000 34.72255  ?  67  MET   A C     1 
ATOM   525  O  O     . MET   A 1 68  ? -3.37498  16.39550  20.20487  1.000 32.56775  ?  67  MET   A O     1 
ATOM   526  C  CB    . MET   A 1 68  ? -1.77259  18.56610  19.40312  1.000 33.09004  ?  67  MET   A CB    1 
ATOM   527  C  CG    . MET   A 1 68  ? -0.79798  19.68345  19.64533  1.000 37.75246  ?  67  MET   A CG    1 
ATOM   528  S  SD    . MET   A 1 68  ? -1.61956  21.25024  19.43086  1.000 41.87373  ?  67  MET   A SD    1 
ATOM   529  C  CE    . MET   A 1 68  ? -2.84690  21.13609  20.73477  1.000 38.66137  ?  67  MET   A CE    1 
ATOM   530  N  N     . ARG   A 1 69  ? -1.94963  14.97073  19.19064  1.000 35.04984  ?  68  ARG   A N     1 
ATOM   531  C  CA    . ARG   A 1 69  ? -2.90178  13.88397  19.02514  1.000 34.74008  ?  68  ARG   A CA    1 
ATOM   532  C  C     . ARG   A 1 69  ? -2.89094  12.89765  20.17324  1.000 30.34747  ?  68  ARG   A C     1 
ATOM   533  O  O     . ARG   A 1 69  ? -3.77278  12.03411  20.23007  1.000 30.07560  ?  68  ARG   A O     1 
ATOM   534  C  CB    . ARG   A 1 69  ? -2.60635  13.11084  17.73977  1.000 28.17336  ?  68  ARG   A CB    1 
ATOM   535  C  CG    . ARG   A 1 69  ? -2.43342  13.97922  16.53944  1.000 32.78957  ?  68  ARG   A CG    1 
ATOM   536  C  CD    . ARG   A 1 69  ? -2.31933  13.13321  15.28173  1.000 31.67533  ?  68  ARG   A CD    1 
ATOM   537  N  NE    . ARG   A 1 69  ? -2.34734  13.96290  14.08694  1.000 33.56024  ?  68  ARG   A NE    1 
ATOM   538  C  CZ    . ARG   A 1 69  ? -1.43239  13.92818  13.12868  1.000 36.89084  ?  68  ARG   A CZ    1 
ATOM   539  N  NH1   . ARG   A 1 69  ? -0.44940  13.04075  13.14264  1.000 32.86673  ?  68  ARG   A NH1   1 
ATOM   540  N  NH2   . ARG   A 1 69  ? -1.50262  14.81071  12.13386  1.000 34.06823  ?  68  ARG   A NH2   1 
ATOM   541  N  N     . ASP   A 1 70  ? -1.92159  13.00652  21.08160  1.000 32.96524  ?  69  ASP   A N     1 
ATOM   542  C  CA    . ASP   A 1 70  ? -1.70377  11.94658  22.05339  1.000 33.92676  ?  69  ASP   A CA    1 
ATOM   543  C  C     . ASP   A 1 70  ? -2.89855  11.77341  22.97502  1.000 29.20435  ?  69  ASP   A C     1 
ATOM   544  O  O     . ASP   A 1 70  ? -3.28915  10.63838  23.27513  1.000 29.23593  ?  69  ASP   A O     1 
ATOM   545  C  CB    . ASP   A 1 70  ? -0.42844  12.21370  22.86391  1.000 36.37515  ?  69  ASP   A CB    1 
ATOM   546  C  CG    . ASP   A 1 70  ? 0.83896   11.87810  22.08649  1.000 47.46454  ?  69  ASP   A CG    1 
ATOM   547  O  OD1   . ASP   A 1 70  ? 0.74639   11.64431  20.85508  1.000 46.68572  ?  69  ASP   A OD1   1 
ATOM   548  O  OD2   . ASP   A 1 70  ? 1.92692   11.83121  22.71124  1.000 53.38574  -1 69  ASP   A OD2   1 
ATOM   549  N  N     . GLN   A 1 71  ? -3.49175  12.87234  23.44950  1.000 28.13537  ?  70  GLN   A N     1 
ATOM   550  C  CA    . GLN   A 1 71  ? -4.54468  12.69250  24.44329  1.000 32.73286  ?  70  GLN   A CA    1 
ATOM   551  C  C     . GLN   A 1 71  ? -5.78147  12.07104  23.81554  1.000 31.56022  ?  70  GLN   A C     1 
ATOM   552  O  O     . GLN   A 1 71  ? -6.37345  11.14824  24.38811  1.000 34.20828  ?  70  GLN   A O     1 
ATOM   553  C  CB    . GLN   A 1 71  ? -4.90332  13.99845  25.14004  1.000 32.31513  ?  70  GLN   A CB    1 
ATOM   554  C  CG    . GLN   A 1 71  ? -6.02383  13.80764  26.19826  1.000 38.22490  ?  70  GLN   A CG    1 
ATOM   555  C  CD    . GLN   A 1 71  ? -5.65067  12.85118  27.35591  1.000 48.26200  ?  70  GLN   A CD    1 
ATOM   556  O  OE1   . GLN   A 1 71  ? -4.49224  12.77747  27.78510  1.000 43.95620  ?  70  GLN   A OE1   1 
ATOM   557  N  NE2   . GLN   A 1 71  ? -6.64394  12.13102  27.86581  1.000 46.70544  ?  70  GLN   A NE2   1 
ATOM   558  N  N     . TYR   A 1 72  ? -6.17203  12.51999  22.61895  1.000 27.48391  ?  71  TYR   A N     1 
ATOM   559  C  CA    . TYR   A 1 72  ? -7.37246  11.91333  22.06847  1.000 26.72412  ?  71  TYR   A CA    1 
ATOM   560  C  C     . TYR   A 1 72  ? -7.11842  10.46619  21.67914  1.000 23.82323  ?  71  TYR   A C     1 
ATOM   561  O  O     . TYR   A 1 72  ? -8.03463  9.64451   21.74923  1.000 27.51834  ?  71  TYR   A O     1 
ATOM   562  C  CB    . TYR   A 1 72  ? -7.93899  12.77295  20.93825  1.000 25.84146  ?  71  TYR   A CB    1 
ATOM   563  C  CG    . TYR   A 1 72  ? -7.27302  12.77511  19.57630  1.000 22.88364  ?  71  TYR   A CG    1 
ATOM   564  C  CD1   . TYR   A 1 72  ? -7.09547  11.60798  18.85965  1.000 25.26779  ?  71  TYR   A CD1   1 
ATOM   565  C  CD2   . TYR   A 1 72  ? -6.94675  13.98015  18.95985  1.000 30.94686  ?  71  TYR   A CD2   1 
ATOM   566  C  CE1   . TYR   A 1 72  ? -6.51583  11.62121  17.58883  1.000 32.31348  ?  71  TYR   A CE1   1 
ATOM   567  C  CE2   . TYR   A 1 72  ? -6.38620  14.01806  17.68370  1.000 30.43284  ?  71  TYR   A CE2   1 
ATOM   568  C  CZ    . TYR   A 1 72  ? -6.18000  12.83462  17.00450  1.000 32.43908  ?  71  TYR   A CZ    1 
ATOM   569  O  OH    . TYR   A 1 72  ? -5.63749  12.82734  15.74937  1.000 34.00105  ?  71  TYR   A OH    1 
ATOM   570  N  N     . MET   A 1 73  ? -5.86619  10.10502  21.39267  1.000 25.54717  ?  72  MET   A N     1 
ATOM   571  C  CA    . MET   A 1 73  ? -5.57152  8.70670   21.10008  1.000 28.10184  ?  72  MET   A CA    1 
ATOM   572  C  C     . MET   A 1 73  ? -5.60751  7.85185   22.36393  1.000 25.36025  ?  72  MET   A C     1 
ATOM   573  O  O     . MET   A 1 73  ? -6.09260  6.71590   22.33531  1.000 28.53465  ?  72  MET   A O     1 
ATOM   574  C  CB    . MET   A 1 73  ? -4.21928  8.58760   20.40431  1.000 25.10861  ?  72  MET   A CB    1 
ATOM   575  C  CG    . MET   A 1 73  ? -4.23973  9.00932   18.96059  1.000 27.78228  ?  72  MET   A CG    1 
ATOM   576  S  SD    . MET   A 1 73  ? -2.61283  8.94157   18.16922  1.000 35.34939  ?  72  MET   A SD    1 
ATOM   577  C  CE    . MET   A 1 73  ? -3.05459  9.37076   16.47872  1.000 34.08494  ?  72  MET   A CE    1 
ATOM   578  N  N     . ARG   A 1 74  ? -5.11006  8.37936   23.48360  1.000 30.75146  ?  73  ARG   A N     1 
ATOM   579  C  CA    . ARG   A 1 74  ? -5.25728  7.66967   24.75265  1.000 34.03429  ?  73  ARG   A CA    1 
ATOM   580  C  C     . ARG   A 1 74  ? -6.72726  7.42510   25.07426  1.000 27.14532  ?  73  ARG   A C     1 
ATOM   581  O  O     . ARG   A 1 74  ? -7.10995  6.30641   25.42229  1.000 32.89535  ?  73  ARG   A O     1 
ATOM   582  C  CB    . ARG   A 1 74  ? -4.57475  8.44677   25.88876  1.000 40.14178  ?  73  ARG   A CB    1 
ATOM   583  C  CG    . ARG   A 1 74  ? -3.08253  8.15273   26.03581  1.000 41.34466  ?  73  ARG   A CG    1 
ATOM   584  C  CD    . ARG   A 1 74  ? -2.45964  8.84955   27.24794  1.000 39.70803  ?  73  ARG   A CD    1 
ATOM   585  N  NE    . ARG   A 1 74  ? -1.35944  9.70405   26.82542  1.000 43.49339  ?  73  ARG   A NE    1 
ATOM   586  C  CZ    . ARG   A 1 74  ? -1.43380  11.02215  26.70926  1.000 42.89430  ?  73  ARG   A CZ    1 
ATOM   587  N  NH1   . ARG   A 1 74  ? -2.50760  11.69408  27.10388  1.000 45.15072  ?  73  ARG   A NH1   1 
ATOM   588  N  NH2   . ARG   A 1 74  ? -0.40481  11.68453  26.18939  1.000 42.98758  ?  73  ARG   A NH2   1 
ATOM   589  N  N     . THR   A 1 75  ? -7.57318  8.45717   24.92589  1.000 26.16619  ?  74  THR   A N     1 
ATOM   590  C  CA    . THR   A 1 75  ? -8.99193  8.34605   25.28457  1.000 30.52194  ?  74  THR   A CA    1 
ATOM   591  C  C     . THR   A 1 75  ? -9.77025  7.41586   24.35205  1.000 31.02956  ?  74  THR   A C     1 
ATOM   592  O  O     . THR   A 1 75  ? -10.71482 6.74997   24.79163  1.000 29.73539  ?  74  THR   A O     1 
ATOM   593  C  CB    . THR   A 1 75  ? -9.66293  9.73540   25.28004  1.000 31.80209  ?  74  THR   A CB    1 
ATOM   594  O  OG1   . THR   A 1 75  ? -8.96375  10.63318  26.14870  1.000 38.08525  ?  74  THR   A OG1   1 
ATOM   595  C  CG2   . THR   A 1 75  ? -11.09833 9.65470   25.76530  1.000 28.27974  ?  74  THR   A CG2   1 
ATOM   596  N  N     . GLY   A 1 76  ? -9.43103  7.37566   23.06565  1.000 28.80467  ?  75  GLY   A N     1 
ATOM   597  C  CA    . GLY   A 1 76  ? -10.27799 6.67672   22.11446  1.000 27.60593  ?  75  GLY   A CA    1 
ATOM   598  C  C     . GLY   A 1 76  ? -10.19715 5.16989   22.27278  1.000 29.12348  ?  75  GLY   A C     1 
ATOM   599  O  O     . GLY   A 1 76  ? -9.17462  4.61994   22.66750  1.000 30.22395  ?  75  GLY   A O     1 
ATOM   600  N  N     . GLU   A 1 77  ? -11.29062 4.48400   21.94364  1.000 30.38760  ?  76  GLU   A N     1 
ATOM   601  C  CA    . GLU   A 1 77  ? -11.26827 3.02340   21.96499  1.000 33.12938  ?  76  GLU   A CA    1 
ATOM   602  C  C     . GLU   A 1 77  ? -11.01612 2.39267   20.60136  1.000 29.72552  ?  76  GLU   A C     1 
ATOM   603  O  O     . GLU   A 1 77  ? -10.39815 1.31990   20.53429  1.000 26.76565  ?  76  GLU   A O     1 
ATOM   604  C  CB    . GLU   A 1 77  ? -12.57245 2.48472   22.54519  1.000 26.40375  ?  76  GLU   A CB    1 
ATOM   605  C  CG    . GLU   A 1 77  ? -12.73917 2.89745   23.98904  1.000 33.62337  ?  76  GLU   A CG    1 
ATOM   606  C  CD    . GLU   A 1 77  ? -14.09588 2.51609   24.53393  1.000 38.45530  ?  76  GLU   A CD    1 
ATOM   607  O  OE1   . GLU   A 1 77  ? -15.10333 2.62947   23.79052  1.000 37.77248  ?  76  GLU   A OE1   1 
ATOM   608  O  OE2   . GLU   A 1 77  ? -14.15056 2.12099   25.71125  1.000 45.27002  -1 76  GLU   A OE2   1 
ATOM   609  N  N     . GLY   A 1 78  ? -11.44880 3.04087   19.52307  1.000 28.56595  ?  77  GLY   A N     1 
ATOM   610  C  CA    . GLY   A 1 78  ? -11.22740 2.53487   18.17856  1.000 26.54946  ?  77  GLY   A CA    1 
ATOM   611  C  C     . GLY   A 1 78  ? -11.08428 3.66767   17.17858  1.000 24.51519  ?  77  GLY   A C     1 
ATOM   612  O  O     . GLY   A 1 78  ? -11.60686 4.77570   17.37452  1.000 24.38772  ?  77  GLY   A O     1 
ATOM   613  N  N     . PHE   A 1 79  ? -10.38084 3.36905   16.08829  1.000 22.82586  ?  78  PHE   A N     1 
ATOM   614  C  CA    . PHE   A 1 79  ? -9.92128  4.38124   15.14320  1.000 26.11458  ?  78  PHE   A CA    1 
ATOM   615  C  C     . PHE   A 1 79  ? -10.30187 3.98635   13.72675  1.000 25.39132  ?  78  PHE   A C     1 
ATOM   616  O  O     . PHE   A 1 79  ? -10.00046 2.87481   13.29148  1.000 24.68417  ?  78  PHE   A O     1 
ATOM   617  C  CB    . PHE   A 1 79  ? -8.40214  4.58448   15.28500  1.000 26.67646  ?  78  PHE   A CB    1 
ATOM   618  C  CG    . PHE   A 1 79  ? -8.01135  4.98580   16.68187  1.000 26.26912  ?  78  PHE   A CG    1 
ATOM   619  C  CD1   . PHE   A 1 79  ? -7.91123  4.04328   17.68524  1.000 22.92815  ?  78  PHE   A CD1   1 
ATOM   620  C  CD2   . PHE   A 1 79  ? -7.81788  6.32569   17.00278  1.000 26.47191  ?  78  PHE   A CD2   1 
ATOM   621  C  CE1   . PHE   A 1 79  ? -7.61949  4.42656   18.98144  1.000 24.99595  ?  78  PHE   A CE1   1 
ATOM   622  C  CE2   . PHE   A 1 79  ? -7.49462  6.70387   18.28410  1.000 25.04209  ?  78  PHE   A CE2   1 
ATOM   623  C  CZ    . PHE   A 1 79  ? -7.41354  5.75888   19.28172  1.000 25.38006  ?  78  PHE   A CZ    1 
ATOM   624  N  N     . LEU   A 1 80  ? -11.01959 4.87516   13.04148  1.000 24.48362  ?  79  LEU   A N     1 
ATOM   625  C  CA    . LEU   A 1 80  ? -11.20287 4.80000   11.59354  1.000 27.36631  ?  79  LEU   A CA    1 
ATOM   626  C  C     . LEU   A 1 80  ? -10.02212 5.50566   10.95270  1.000 23.24541  ?  79  LEU   A C     1 
ATOM   627  O  O     . LEU   A 1 80  ? -9.85869  6.71895   11.11257  1.000 24.76194  ?  79  LEU   A O     1 
ATOM   628  C  CB    . LEU   A 1 80  ? -12.50363 5.46508   11.15551  1.000 23.64360  ?  79  LEU   A CB    1 
ATOM   629  C  CG    . LEU   A 1 80  ? -13.85640 4.77331   11.13194  1.000 31.22609  ?  79  LEU   A CG    1 
ATOM   630  C  CD1   . LEU   A 1 80  ? -14.77591 5.60218   10.21725  1.000 25.59343  ?  79  LEU   A CD1   1 
ATOM   631  C  CD2   . LEU   A 1 80  ? -13.78433 3.33336   10.67558  1.000 25.03986  ?  79  LEU   A CD2   1 
ATOM   632  N  N     . CYS   A 1 81  ? -9.18384  4.75456   10.27022  1.000 21.66268  ?  80  CYS   A N     1 
ATOM   633  C  CA    . CYS   A 1 81  ? -8.00663  5.30928   9.61559   1.000 23.07544  ?  80  CYS   A CA    1 
ATOM   634  C  C     . CYS   A 1 81  ? -8.39219  5.51713   8.15514   1.000 26.54418  ?  80  CYS   A C     1 
ATOM   635  O  O     . CYS   A 1 81  ? -8.49397  4.55976   7.38681   1.000 22.95474  ?  80  CYS   A O     1 
ATOM   636  C  CB    . CYS   A 1 81  ? -6.81208  4.37910   9.78884   1.000 22.29760  ?  80  CYS   A CB    1 
ATOM   637  S  SG    . CYS   A 1 81  ? -6.40073  4.12637   11.55308  1.000 30.47653  ?  80  CYS   A SG    1 
ATOM   638  N  N     . VAL   A 1 82  ? -8.66156  6.76973   7.80130   1.000 25.39773  ?  81  VAL   A N     1 
ATOM   639  C  CA    . VAL   A 1 82  ? -9.28015  7.12779   6.53087   1.000 25.01708  ?  81  VAL   A CA    1 
ATOM   640  C  C     . VAL   A 1 82  ? -8.20394  7.65719   5.59323   1.000 26.55318  ?  81  VAL   A C     1 
ATOM   641  O  O     . VAL   A 1 82  ? -7.39946  8.51545   5.97620   1.000 26.48847  ?  81  VAL   A O     1 
ATOM   642  C  CB    . VAL   A 1 82  ? -10.38744 8.18218   6.72323   1.000 22.96186  ?  81  VAL   A CB    1 
ATOM   643  C  CG1   . VAL   A 1 82  ? -11.07416 8.48170   5.40406   1.000 25.03461  ?  81  VAL   A CG1   1 
ATOM   644  C  CG2   . VAL   A 1 82  ? -11.44913 7.72356   7.76921   1.000 20.50456  ?  81  VAL   A CG2   1 
ATOM   645  N  N     . PHE   A 1 83  ? -8.19097  7.14535   4.37086   1.000 26.06964  ?  82  PHE   A N     1 
ATOM   646  C  CA    . PHE   A 1 83  ? -7.43530  7.71229   3.26414   1.000 28.46433  ?  82  PHE   A CA    1 
ATOM   647  C  C     . PHE   A 1 83  ? -8.39250  7.86114   2.08300   1.000 28.66657  ?  82  PHE   A C     1 
ATOM   648  O  O     . PHE   A 1 83  ? -9.51003  7.33028   2.10158   1.000 25.64604  ?  82  PHE   A O     1 
ATOM   649  C  CB    . PHE   A 1 83  ? -6.20652  6.84051   2.92725   1.000 24.68990  ?  82  PHE   A CB    1 
ATOM   650  C  CG    . PHE   A 1 83  ? -6.52473  5.55335   2.19424   1.000 25.00289  ?  82  PHE   A CG    1 
ATOM   651  C  CD1   . PHE   A 1 83  ? -6.81716  4.39084   2.88003   1.000 22.70242  ?  82  PHE   A CD1   1 
ATOM   652  C  CD2   . PHE   A 1 83  ? -6.47488  5.50698   0.78785   1.000 27.67946  ?  82  PHE   A CD2   1 
ATOM   653  C  CE1   . PHE   A 1 83  ? -7.09123  3.19928   2.19349   1.000 23.50211  ?  82  PHE   A CE1   1 
ATOM   654  C  CE2   . PHE   A 1 83  ? -6.76128  4.32914   0.08554   1.000 28.13575  ?  82  PHE   A CE2   1 
ATOM   655  C  CZ    . PHE   A 1 83  ? -7.07295  3.17290   0.77480   1.000 24.12063  ?  82  PHE   A CZ    1 
ATOM   656  N  N     . ALA   A 1 84  ? -7.97116  8.62309   1.06816   1.000 27.68200  ?  83  ALA   A N     1 
ATOM   657  C  CA    . ALA   A 1 84  ? -8.76186  8.85859   -0.13740  1.000 30.60730  ?  83  ALA   A CA    1 
ATOM   658  C  C     . ALA   A 1 84  ? -8.12420  8.10262   -1.29720  1.000 30.84120  ?  83  ALA   A C     1 
ATOM   659  O  O     . ALA   A 1 84  ? -6.91293  8.20398   -1.51534  1.000 30.28121  ?  83  ALA   A O     1 
ATOM   660  C  CB    . ALA   A 1 84  ? -8.87276  10.35152  -0.47217  1.000 24.80329  ?  83  ALA   A CB    1 
ATOM   661  N  N     . ILE   A 1 85  ? -8.94287  7.33173   -2.02017  1.000 30.14473  ?  84  ILE   A N     1 
ATOM   662  C  CA    . ILE   A 1 85  ? -8.44126  6.41649   -3.04369  1.000 34.00401  ?  84  ILE   A CA    1 
ATOM   663  C  C     . ILE   A 1 85  ? -7.80672  7.12345   -4.22842  1.000 31.90656  ?  84  ILE   A C     1 
ATOM   664  O  O     . ILE   A 1 85  ? -7.14139  6.46606   -5.03584  1.000 33.41914  ?  84  ILE   A O     1 
ATOM   665  C  CB    . ILE   A 1 85  ? -9.55400  5.50370   -3.59588  1.000 28.96409  ?  84  ILE   A CB    1 
ATOM   666  C  CG1   . ILE   A 1 85  ? -10.68231 6.36424   -4.15100  1.000 31.95918  ?  84  ILE   A CG1   1 
ATOM   667  C  CG2   . ILE   A 1 85  ? -10.04280 4.51016   -2.53786  1.000 30.61247  ?  84  ILE   A CG2   1 
ATOM   668  C  CD1   . ILE   A 1 85  ? -11.13604 5.95124   -5.51819  1.000 40.93893  ?  84  ILE   A CD1   1 
ATOM   669  N  N     . ASN   A 1 86  ? -8.02027  8.43190   -4.36473  1.000 32.42854  ?  85  ASN   A N     1 
ATOM   670  C  CA    . ASN   A 1 86  ? -7.38842  9.25284   -5.38696  1.000 31.91830  ?  85  ASN   A CA    1 
ATOM   671  C  C     . ASN   A 1 86  ? -6.21272  10.07225  -4.85139  1.000 36.98015  ?  85  ASN   A C     1 
ATOM   672  O  O     . ASN   A 1 86  ? -5.85661  11.08688  -5.45552  1.000 34.09234  ?  85  ASN   A O     1 
ATOM   673  C  CB    . ASN   A 1 86  ? -8.41983  10.19489  -6.00278  1.000 30.00881  ?  85  ASN   A CB    1 
ATOM   674  C  CG    . ASN   A 1 86  ? -8.84288  11.30184  -5.04454  1.000 41.52140  ?  85  ASN   A CG    1 
ATOM   675  O  OD1   . ASN   A 1 86  ? -8.73597  11.16760  -3.81121  1.000 35.52169  ?  85  ASN   A OD1   1 
ATOM   676  N  ND2   . ASN   A 1 86  ? -9.32465  12.40196  -5.59901  1.000 38.10876  ?  85  ASN   A ND2   1 
ATOM   677  N  N     . ASN   A 1 87  ? -5.61871  9.68025   -3.71301  1.000 34.47565  ?  86  ASN   A N     1 
ATOM   678  C  CA    . ASN   A 1 87  ? -4.61181  10.51604  -3.04298  1.000 34.51913  ?  86  ASN   A CA    1 
ATOM   679  C  C     . ASN   A 1 87  ? -3.58656  9.58077   -2.40347  1.000 37.07240  ?  86  ASN   A C     1 
ATOM   680  O  O     . ASN   A 1 87  ? -3.69991  9.21847   -1.22415  1.000 32.34780  ?  86  ASN   A O     1 
ATOM   681  C  CB    . ASN   A 1 87  ? -5.26527  11.44745  -2.02347  1.000 36.32996  ?  86  ASN   A CB    1 
ATOM   682  C  CG    . ASN   A 1 87  ? -4.25107  12.28827  -1.22899  1.000 40.28836  ?  86  ASN   A CG    1 
ATOM   683  O  OD1   . ASN   A 1 87  ? -3.05150  12.06889  -1.29334  1.000 36.57520  ?  86  ASN   A OD1   1 
ATOM   684  N  ND2   . ASN   A 1 87  ? -4.75667  13.24173  -0.45192  1.000 42.11931  ?  86  ASN   A ND2   1 
ATOM   685  N  N     . THR   A 1 88  ? -2.55709  9.24111   -3.18422  1.000 31.71855  ?  87  THR   A N     1 
ATOM   686  C  CA    . THR   A 1 88  ? -1.57294  8.25619   -2.75637  1.000 32.75595  ?  87  THR   A CA    1 
ATOM   687  C  C     . THR   A 1 88  ? -0.83925  8.70555   -1.49520  1.000 34.71817  ?  87  THR   A C     1 
ATOM   688  O  O     . THR   A 1 88  ? -0.43522  7.87582   -0.67675  1.000 29.97286  ?  87  THR   A O     1 
ATOM   689  C  CB    . THR   A 1 88  ? -0.58755  7.99548   -3.89906  1.000 33.48033  ?  87  THR   A CB    1 
ATOM   690  O  OG1   . THR   A 1 88  ? -1.31901  7.68418   -5.08514  1.000 37.09470  ?  87  THR   A OG1   1 
ATOM   691  C  CG2   . THR   A 1 88  ? 0.31241   6.81527   -3.57606  1.000 35.33813  ?  87  THR   A CG2   1 
ATOM   692  N  N     . LYS   A 1 89  ? -0.66924  10.01288  -1.31602  1.000 32.62318  ?  88  LYS   A N     1 
ATOM   693  C  CA    . LYS   A 1 89  ? 0.03342   10.50808  -0.13689  1.000 35.55774  ?  88  LYS   A CA    1 
ATOM   694  C  C     . LYS   A 1 89  ? -0.78517  10.28167  1.13745   1.000 37.51275  ?  88  LYS   A C     1 
ATOM   695  O  O     . LYS   A 1 89  ? -0.22629  9.99465   2.20644   1.000 36.15754  ?  88  LYS   A O     1 
ATOM   696  C  CB    . LYS   A 1 89  ? 0.37144   11.98910  -0.32511  1.000 39.80171  ?  88  LYS   A CB    1 
ATOM   697  C  CG    . LYS   A 1 89  ? 0.99495   12.67520  0.89521   1.000 37.77889  ?  88  LYS   A CG    1 
ATOM   698  C  CD    . LYS   A 1 89  ? 2.34441   12.07670  1.26893   1.000 44.38930  ?  88  LYS   A CD    1 
ATOM   699  C  CE    . LYS   A 1 89  ? 3.07689   12.93142  2.30825   1.000 52.15964  ?  88  LYS   A CE    1 
ATOM   700  N  NZ    . LYS   A 1 89  ? 2.21374   13.32417  3.46853   1.000 50.58596  ?  88  LYS   A NZ    1 
ATOM   701  N  N     . SER   A 1 90  ? -2.11051  10.38425  1.04180   1.000 35.28853  ?  89  SER   A N     1 
ATOM   702  C  CA    . SER   A 1 90  ? -2.94337  10.08130  2.19935   1.000 31.81517  ?  89  SER   A CA    1 
ATOM   703  C  C     . SER   A 1 90  ? -2.90267  8.59412   2.54169   1.000 32.47062  ?  89  SER   A C     1 
ATOM   704  O  O     . SER   A 1 90  ? -2.99659  8.23066   3.71984   1.000 33.30244  ?  89  SER   A O     1 
ATOM   705  C  CB    . SER   A 1 90  ? -4.36990  10.56201  1.95141   1.000 28.22812  ?  89  SER   A CB    1 
ATOM   706  O  OG    . SER   A 1 90  ? -5.12594  9.65221   1.16303   1.000 27.92002  ?  89  SER   A OG    1 
ATOM   707  N  N     . PHE   A 1 91  ? -2.70372  7.72574   1.54380   1.000 32.44232  ?  90  PHE   A N     1 
ATOM   708  C  CA    . PHE   A 1 91  ? -2.54891  6.30101   1.81951   1.000 29.60436  ?  90  PHE   A CA    1 
ATOM   709  C  C     . PHE   A 1 91  ? -1.22767  6.02675   2.52003   1.000 39.29938  ?  90  PHE   A C     1 
ATOM   710  O  O     . PHE   A 1 91  ? -1.15348  5.17362   3.41859   1.000 37.36708  ?  90  PHE   A O     1 
ATOM   711  C  CB    . PHE   A 1 91  ? -2.64745  5.50852   0.52107   1.000 34.03815  ?  90  PHE   A CB    1 
ATOM   712  C  CG    . PHE   A 1 91  ? -2.55235  4.02015   0.69768   1.000 33.97353  ?  90  PHE   A CG    1 
ATOM   713  C  CD1   . PHE   A 1 91  ? -3.55367  3.31243   1.34618   1.000 31.10705  ?  90  PHE   A CD1   1 
ATOM   714  C  CD2   . PHE   A 1 91  ? -1.47524  3.32152   0.17333   1.000 34.44283  ?  90  PHE   A CD2   1 
ATOM   715  C  CE1   . PHE   A 1 91  ? -3.46774  1.94201   1.49520   1.000 32.98888  ?  90  PHE   A CE1   1 
ATOM   716  C  CE2   . PHE   A 1 91  ? -1.38787  1.95825   0.30950   1.000 37.06178  ?  90  PHE   A CE2   1 
ATOM   717  C  CZ    . PHE   A 1 91  ? -2.38738  1.26087   0.97547   1.000 34.48170  ?  90  PHE   A CZ    1 
ATOM   718  N  N     . GLU   A 1 92  ? -0.17560  6.75513   2.13292   1.000 39.51710  ?  91  GLU   A N     1 
ATOM   719  C  CA    . GLU   A 1 92  ? 1.11427   6.62320   2.80106   1.000 32.90192  ?  91  GLU   A CA    1 
ATOM   720  C  C     . GLU   A 1 92  ? 1.06545   7.16621   4.22430   1.000 36.93359  ?  91  GLU   A C     1 
ATOM   721  O  O     . GLU   A 1 92  ? 1.78187   6.67206   5.10402   1.000 34.75432  ?  91  GLU   A O     1 
ATOM   722  C  CB    . GLU   A 1 92  ? 2.19056   7.35094   1.99001   1.000 39.62818  ?  91  GLU   A CB    1 
ATOM   723  C  CG    . GLU   A 1 92  ? 2.32396   6.85685   0.54175   1.000 42.59582  ?  91  GLU   A CG    1 
ATOM   724  C  CD    . GLU   A 1 92  ? 3.13080   7.80112   -0.34503  1.000 49.17460  ?  91  GLU   A CD    1 
ATOM   725  O  OE1   . GLU   A 1 92  ? 3.15719   9.02427   -0.07432  1.000 52.43383  ?  91  GLU   A OE1   1 
ATOM   726  O  OE2   . GLU   A 1 92  ? 3.74430   7.31548   -1.32075  1.000 53.17937  -1 91  GLU   A OE2   1 
ATOM   727  N  N     . ASP   A 1 93  ? 0.23990   8.18668   4.47019   1.000 36.40970  ?  92  ASP   A N     1 
ATOM   728  C  CA    . ASP   A 1 93  ? 0.17324   8.75335   5.81195   1.000 42.92435  ?  92  ASP   A CA    1 
ATOM   729  C  C     . ASP   A 1 93  ? -0.42791  7.77369   6.81188   1.000 37.44536  ?  92  ASP   A C     1 
ATOM   730  O  O     . ASP   A 1 93  ? -0.13560  7.86483   8.00708   1.000 35.56879  ?  92  ASP   A O     1 
ATOM   731  C  CB    . ASP   A 1 93  ? -0.60816  10.06332  5.78433   1.000 35.72028  ?  92  ASP   A CB    1 
ATOM   732  C  CG    . ASP   A 1 93  ? 0.08029   11.12929  4.93383   1.000 46.76251  ?  92  ASP   A CG    1 
ATOM   733  O  OD1   . ASP   A 1 93  ? 1.24273   10.91558  4.49598   1.000 42.95825  ?  92  ASP   A OD1   1 
ATOM   734  O  OD2   . ASP   A 1 93  ? -0.53272  12.19462  4.69582   1.000 52.15288  -1 92  ASP   A OD2   1 
ATOM   735  N  N     . ILE   A 1 94  ? -1.20097  6.79880   6.32884   1.000 35.60014  ?  93  ILE   A N     1 
ATOM   736  C  CA    . ILE   A 1 94  ? -1.92144  5.85857   7.19280   1.000 42.56276  ?  93  ILE   A CA    1 
ATOM   737  C  C     . ILE   A 1 94  ? -0.96778  5.15315   8.15301   1.000 40.72629  ?  93  ILE   A C     1 
ATOM   738  O  O     . ILE   A 1 94  ? -1.25977  4.97540   9.34125   1.000 37.87083  ?  93  ILE   A O     1 
ATOM   739  C  CB    . ILE   A 1 94  ? -2.68842  4.84283   6.32400   1.000 41.97472  ?  93  ILE   A CB    1 
ATOM   740  C  CG1   . ILE   A 1 94  ? -3.95887  5.48389   5.76446   1.000 34.63428  ?  93  ILE   A CG1   1 
ATOM   741  C  CG2   . ILE   A 1 94  ? -2.98272  3.55538   7.09373   1.000 33.14167  ?  93  ILE   A CG2   1 
ATOM   742  C  CD1   . ILE   A 1 94  ? -4.78853  6.17769   6.82491   1.000 27.48886  ?  93  ILE   A CD1   1 
ATOM   743  N  N     . HIS   A 1 95  ? 0.18305   4.72886   7.63841   1.000 40.10220  ?  94  HIS   A N     1 
ATOM   744  C  CA    . HIS   A 1 95  ? 1.15685   4.01081   8.45151   1.000 40.73266  ?  94  HIS   A CA    1 
ATOM   745  C  C     . HIS   A 1 95  ? 1.61873   4.85029   9.63748   1.000 41.22825  ?  94  HIS   A C     1 
ATOM   746  O  O     . HIS   A 1 95  ? 1.79268   4.33437   10.74862  1.000 40.45635  ?  94  HIS   A O     1 
ATOM   747  C  CB    . HIS   A 1 95  ? 2.33173   3.60023   7.55919   1.000 47.16922  ?  94  HIS   A CB    1 
ATOM   748  C  CG    . HIS   A 1 95  ? 3.58661   3.29290   8.30194   1.000 46.77591  ?  94  HIS   A CG    1 
ATOM   749  N  ND1   . HIS   A 1 95  ? 3.86430   2.03826   8.79999   1.000 49.21680  ?  94  HIS   A ND1   1 
ATOM   750  C  CD2   . HIS   A 1 95  ? 4.64941   4.07190   8.61786   1.000 47.52415  ?  94  HIS   A CD2   1 
ATOM   751  C  CE1   . HIS   A 1 95  ? 5.04083   2.05938   9.40223   1.000 49.45880  ?  94  HIS   A CE1   1 
ATOM   752  N  NE2   . HIS   A 1 95  ? 5.53746   3.28098   9.30564   1.000 53.52660  ?  94  HIS   A NE2   1 
ATOM   753  N  N     . HIS   A 1 96  ? 1.81387   6.14979   9.42295   1.000 41.58999  ?  95  HIS   A N     1 
ATOM   754  C  CA    . HIS   A 1 96  ? 2.27311   7.00404   10.50655  1.000 36.96726  ?  95  HIS   A CA    1 
ATOM   755  C  C     . HIS   A 1 96  ? 1.17621   7.20920   11.54477  1.000 37.09085  ?  95  HIS   A C     1 
ATOM   756  O  O     . HIS   A 1 96  ? 1.45656   7.27683   12.74565  1.000 35.45944  ?  95  HIS   A O     1 
ATOM   757  C  CB    . HIS   A 1 96  ? 2.76324   8.33527   9.93966   1.000 38.85469  ?  95  HIS   A CB    1 
ATOM   758  C  CG    . HIS   A 1 96  ? 3.86184   8.18582   8.92692   1.000 54.99922  ?  95  HIS   A CG    1 
ATOM   759  N  ND1   . HIS   A 1 96  ? 5.19416   8.09118   9.27772   1.000 55.81861  ?  95  HIS   A ND1   1 
ATOM   760  C  CD2   . HIS   A 1 96  ? 3.82409   8.09882   7.57379   1.000 44.21031  ?  95  HIS   A CD2   1 
ATOM   761  C  CE1   . HIS   A 1 96  ? 5.92847   7.96608   8.18591   1.000 48.49433  ?  95  HIS   A CE1   1 
ATOM   762  N  NE2   . HIS   A 1 96  ? 5.12118   7.96027   7.14049   1.000 50.89995  ?  95  HIS   A NE2   1 
ATOM   763  N  N     . TYR   A 1 97  ? -0.08233  7.31892   11.10986  1.000 39.58794  ?  96  TYR   A N     1 
ATOM   764  C  CA    . TYR   A 1 97  ? -1.17283  7.36427   12.08213  1.000 28.26740  ?  96  TYR   A CA    1 
ATOM   765  C  C     . TYR   A 1 97  ? -1.24786  6.07899   12.88543  1.000 29.79126  ?  96  TYR   A C     1 
ATOM   766  O  O     . TYR   A 1 97  ? -1.40804  6.12195   14.11137  1.000 32.78636  ?  96  TYR   A O     1 
ATOM   767  C  CB    . TYR   A 1 97  ? -2.50387  7.62675   11.38758  1.000 28.10678  ?  96  TYR   A CB    1 
ATOM   768  C  CG    . TYR   A 1 97  ? -2.79941  9.08608   11.20479  1.000 25.72492  ?  96  TYR   A CG    1 
ATOM   769  C  CD1   . TYR   A 1 97  ? -3.32392  9.83831   12.25323  1.000 28.43298  ?  96  TYR   A CD1   1 
ATOM   770  C  CD2   . TYR   A 1 97  ? -2.55362  9.72212   9.99006   1.000 31.35245  ?  96  TYR   A CD2   1 
ATOM   771  C  CE1   . TYR   A 1 97  ? -3.60009  11.17300  12.09209  1.000 26.90683  ?  96  TYR   A CE1   1 
ATOM   772  C  CE2   . TYR   A 1 97  ? -2.82219  11.06710  9.82841   1.000 29.51561  ?  96  TYR   A CE2   1 
ATOM   773  C  CZ    . TYR   A 1 97  ? -3.34889  11.77731  10.87758  1.000 32.29984  ?  96  TYR   A CZ    1 
ATOM   774  O  OH    . TYR   A 1 97  ? -3.62772  13.11498  10.73633  1.000 40.06320  ?  96  TYR   A OH    1 
ATOM   775  N  N     . ARG   A 1 98  ? -1.13473  4.92625   12.21802  1.000 28.05948  ?  97  ARG   A N     1 
ATOM   776  C  CA    . ARG   A 1 98  ? -1.21912  3.65827   12.93070  1.000 33.43840  ?  97  ARG   A CA    1 
ATOM   777  C  C     . ARG   A 1 98  ? -0.05329  3.48852   13.89809  1.000 37.05810  ?  97  ARG   A C     1 
ATOM   778  O  O     . ARG   A 1 98  ? -0.23286  2.99005   15.01537  1.000 33.75654  ?  97  ARG   A O     1 
ATOM   779  C  CB    . ARG   A 1 98  ? -1.27323  2.49258   11.94935  1.000 28.64956  ?  97  ARG   A CB    1 
ATOM   780  C  CG    . ARG   A 1 98  ? -1.29099  1.13704   12.64380  1.000 41.24169  ?  97  ARG   A CG    1 
ATOM   781  C  CD    . ARG   A 1 98  ? -1.45041  0.00097   11.66693  1.000 48.41647  ?  97  ARG   A CD    1 
ATOM   782  N  NE    . ARG   A 1 98  ? -1.65551  -1.25532  12.37009  1.000 43.73349  ?  97  ARG   A NE    1 
ATOM   783  C  CZ    . ARG   A 1 98  ? -0.69812  -2.14645  12.58771  1.000 50.88291  ?  97  ARG   A CZ    1 
ATOM   784  N  NH1   . ARG   A 1 98  ? 0.53544   -1.97690  12.10530  1.000 46.69158  ?  97  ARG   A NH1   1 
ATOM   785  N  NH2   . ARG   A 1 98  ? -0.97355  -3.22545  13.32926  1.000 58.21167  ?  97  ARG   A NH2   1 
ATOM   786  N  N     . GLU   A 1 99  ? 1.15266   3.89599   13.50144  1.000 36.27674  ?  98  GLU   A N     1 
ATOM   787  C  CA    . GLU   A 1 99  ? 2.26663   3.75445   14.43615  1.000 35.22968  ?  98  GLU   A CA    1 
ATOM   788  C  C     . GLU   A 1 99  ? 2.07824   4.66415   15.63962  1.000 38.46897  ?  98  GLU   A C     1 
ATOM   789  O  O     . GLU   A 1 99  ? 2.34489   4.26584   16.77845  1.000 34.67701  ?  98  GLU   A O     1 
ATOM   790  C  CB    . GLU   A 1 99  ? 3.59946   4.03374   13.73860  1.000 39.91000  ?  98  GLU   A CB    1 
ATOM   791  C  CG    . GLU   A 1 99  ? 4.04862   2.92542   12.79220  1.000 38.52652  ?  98  GLU   A CG    1 
ATOM   792  C  CD    . GLU   A 1 99  ? 4.12579   1.55527   13.45280  1.000 44.26668  ?  98  GLU   A CD    1 
ATOM   793  O  OE1   . GLU   A 1 99  ? 4.45760   1.47075   14.65528  1.000 57.58597  ?  98  GLU   A OE1   1 
ATOM   794  O  OE2   . GLU   A 1 99  ? 3.85505   0.54809   12.76921  1.000 46.64855  -1 98  GLU   A OE2   1 
ATOM   795  N  N     . GLN   A 1 100 ? 1.58576   5.87904   15.41023  1.000 34.29693  ?  99  GLN   A N     1 
ATOM   796  C  CA    . GLN   A 1 100 ? 1.34389   6.78648   16.51776  1.000 33.77187  ?  99  GLN   A CA    1 
ATOM   797  C  C     . GLN   A 1 100 ? 0.34313   6.19232   17.50308  1.000 34.75820  ?  99  GLN   A C     1 
ATOM   798  O  O     . GLN   A 1 100 ? 0.57770   6.19966   18.71738  1.000 35.43659  ?  99  GLN   A O     1 
ATOM   799  C  CB    . GLN   A 1 100 ? 0.87411   8.13401   15.96647  1.000 33.50929  ?  99  GLN   A CB    1 
ATOM   800  C  CG    . GLN   A 1 100 ? 0.77120   9.26103   16.97180  1.000 38.73534  ?  99  GLN   A CG    1 
ATOM   801  C  CD    . GLN   A 1 100 ? 0.79337   10.62941  16.31059  1.000 44.22929  ?  99  GLN   A CD    1 
ATOM   802  O  OE1   . GLN   A 1 100 ? 0.21322   10.83252  15.23110  1.000 36.75779  ?  99  GLN   A OE1   1 
ATOM   803  N  NE2   . GLN   A 1 100 ? 1.47937   11.57622  16.94771  1.000 39.15760  ?  99  GLN   A NE2   1 
ATOM   804  N  N     . ILE   A 1 101 ? -0.75722  5.62973   16.99702  1.000 36.38576  ?  100 ILE   A N     1 
ATOM   805  C  CA    . ILE   A 1 101 ? -1.79358  5.06539   17.86214  1.000 29.72055  ?  100 ILE   A CA    1 
ATOM   806  C  C     . ILE   A 1 101 ? -1.24051  3.89649   18.68309  1.000 35.30708  ?  100 ILE   A C     1 
ATOM   807  O  O     . ILE   A 1 101 ? -1.49907  3.78890   19.88828  1.000 36.79206  ?  100 ILE   A O     1 
ATOM   808  C  CB    . ILE   A 1 101 ? -3.01478  4.64309   17.02061  1.000 29.70445  ?  100 ILE   A CB    1 
ATOM   809  C  CG1   . ILE   A 1 101 ? -3.65949  5.86704   16.36990  1.000 29.80727  ?  100 ILE   A CG1   1 
ATOM   810  C  CG2   . ILE   A 1 101 ? -4.06422  3.90513   17.86003  1.000 25.98882  ?  100 ILE   A CG2   1 
ATOM   811  C  CD1   . ILE   A 1 101 ? -4.60020  5.50268   15.23606  1.000 29.74623  ?  100 ILE   A CD1   1 
ATOM   812  N  N     . LYS   A 1 102 ? -0.48228  2.99915   18.04388  1.000 32.60556  ?  101 LYS   A N     1 
ATOM   813  C  CA    . LYS   A 1 102 ? 0.11171   1.87940   18.77277  1.000 36.56471  ?  101 LYS   A CA    1 
ATOM   814  C  C     . LYS   A 1 102 ? 1.09910   2.37319   19.81824  1.000 36.01177  ?  101 LYS   A C     1 
ATOM   815  O  O     . LYS   A 1 102 ? 1.11902   1.88434   20.95759  1.000 31.19608  ?  101 LYS   A O     1 
ATOM   816  C  CB    . LYS   A 1 102 ? 0.81620   0.91862   17.80867  1.000 38.90566  ?  101 LYS   A CB    1 
ATOM   817  C  CG    . LYS   A 1 102 ? -0.09876  0.10456   16.91336  1.000 32.78933  ?  101 LYS   A CG    1 
ATOM   818  C  CD    . LYS   A 1 102 ? 0.64714   -1.05820  16.23949  1.000 42.49660  ?  101 LYS   A CD    1 
ATOM   819  C  CE    . LYS   A 1 102 ? 1.92232   -0.60795  15.53216  1.000 51.45145  ?  101 LYS   A CE    1 
ATOM   820  N  NZ    . LYS   A 1 102 ? 2.75450   -1.76243  15.01718  1.000 51.35291  ?  101 LYS   A NZ    1 
ATOM   821  N  N     . ARG   A 1 103 ? 1.92657   3.34601   19.44584  1.000 37.13318  ?  102 ARG   A N     1 
ATOM   822  C  CA    . ARG   A 1 103 ? 2.90348   3.88501   20.38387  1.000 41.03208  ?  102 ARG   A CA    1 
ATOM   823  C  C     . ARG   A 1 103 ? 2.22631   4.56718   21.56786  1.000 42.66470  ?  102 ARG   A C     1 
ATOM   824  O  O     . ARG   A 1 103 ? 2.60961   4.34540   22.72623  1.000 39.96160  ?  102 ARG   A O     1 
ATOM   825  C  CB    . ARG   A 1 103 ? 3.82599   4.85531   19.65314  1.000 40.15555  ?  102 ARG   A CB    1 
ATOM   826  C  CG    . ARG   A 1 103 ? 4.83714   5.50753   20.54250  1.000 48.49254  ?  102 ARG   A CG    1 
ATOM   827  C  CD    . ARG   A 1 103 ? 5.73078   6.43302   19.75232  1.000 54.66033  ?  102 ARG   A CD    1 
ATOM   828  N  NE    . ARG   A 1 103 ? 5.08464   7.70515   19.44948  1.000 59.00593  ?  102 ARG   A NE    1 
ATOM   829  C  CZ    . ARG   A 1 103 ? 4.89170   8.18431   18.22642  1.000 53.39926  ?  102 ARG   A CZ    1 
ATOM   830  N  NH1   . ARG   A 1 103 ? 5.31260   7.53195   17.15081  1.000 56.31744  ?  102 ARG   A NH1   1 
ATOM   831  N  NH2   . ARG   A 1 103 ? 4.26625   9.35030   18.07966  1.000 49.29951  ?  102 ARG   A NH2   1 
ATOM   832  N  N     . VAL   A 1 104 ? 1.22275   5.40390   21.29878  1.000 34.97062  ?  103 VAL   A N     1 
ATOM   833  C  CA    . VAL   A 1 104 ? 0.55318   6.12744   22.37183  1.000 36.72266  ?  103 VAL   A CA    1 
ATOM   834  C  C     . VAL   A 1 104 ? -0.20011  5.17312   23.29055  1.000 36.46815  ?  103 VAL   A C     1 
ATOM   835  O  O     . VAL   A 1 104 ? -0.19470  5.34941   24.51264  1.000 40.40851  ?  103 VAL   A O     1 
ATOM   836  C  CB    . VAL   A 1 104 ? -0.36966  7.21212   21.78809  1.000 39.26781  ?  103 VAL   A CB    1 
ATOM   837  C  CG1   . VAL   A 1 104 ? -1.33386  7.72370   22.84794  1.000 36.37232  ?  103 VAL   A CG1   1 
ATOM   838  C  CG2   . VAL   A 1 104 ? 0.47012   8.34851   21.22011  1.000 38.90811  ?  103 VAL   A CG2   1 
ATOM   839  N  N     . LYS   A 1 105 ? -0.85835  4.15119   22.73481  1.000 36.69905  ?  104 LYS   A N     1 
ATOM   840  C  CA    . LYS   A 1 105 ? -1.58362  3.19438   23.56852  1.000 33.05398  ?  104 LYS   A CA    1 
ATOM   841  C  C     . LYS   A 1 105 ? -0.71163  2.06135   24.09564  1.000 40.18074  ?  104 LYS   A C     1 
ATOM   842  O  O     . LYS   A 1 105 ? -1.22237  1.21484   24.84158  1.000 39.65034  ?  104 LYS   A O     1 
ATOM   843  C  CB    . LYS   A 1 105 ? -2.75004  2.57079   22.80240  1.000 39.22158  ?  104 LYS   A CB    1 
ATOM   844  C  CG    . LYS   A 1 105 ? -3.92011  3.48102   22.53329  1.000 43.23027  ?  104 LYS   A CG    1 
ATOM   845  C  CD    . LYS   A 1 105 ? -5.14005  2.62080   22.22697  1.000 41.60965  ?  104 LYS   A CD    1 
ATOM   846  C  CE    . LYS   A 1 105 ? -6.40948  3.37299   22.43878  1.000 31.47336  ?  104 LYS   A CE    1 
ATOM   847  N  NZ    . LYS   A 1 105 ? -6.43437  4.16874   23.69228  1.000 28.28468  ?  104 LYS   A NZ    1 
ATOM   848  N  N     . ASP   A 1 106 ? 0.56626   2.01325   23.71156  1.000 38.37862  ?  105 ASP   A N     1 
ATOM   849  C  CA    . ASP   A 1 106 ? 1.49298   0.96066   24.12985  1.000 42.31358  ?  105 ASP   A CA    1 
ATOM   850  C  C     . ASP   A 1 106 ? 0.87182   -0.42984  23.97113  1.000 42.26795  ?  105 ASP   A C     1 
ATOM   851  O  O     . ASP   A 1 106 ? 0.82901   -1.23975  24.90161  1.000 43.12932  ?  105 ASP   A O     1 
ATOM   852  C  CB    . ASP   A 1 106 ? 1.96460   1.19408   25.56554  1.000 40.34759  ?  105 ASP   A CB    1 
ATOM   853  C  CG    . ASP   A 1 106 ? 3.37186   0.65916   25.80820  1.000 51.42903  ?  105 ASP   A CG    1 
ATOM   854  O  OD1   . ASP   A 1 106 ? 4.15438   0.52809   24.83328  1.000 43.79821  ?  105 ASP   A OD1   1 
ATOM   855  O  OD2   . ASP   A 1 106 ? 3.68269   0.34956   26.97851  1.000 59.92657  -1 105 ASP   A OD2   1 
ATOM   856  N  N     . SER   A 1 107 ? 0.37759   -0.70463  22.77185  1.000 39.21608  ?  106 SER   A N     1 
ATOM   857  C  CA    . SER   A 1 107 ? -0.22304  -1.99670  22.48624  1.000 42.74282  ?  106 SER   A CA    1 
ATOM   858  C  C     . SER   A 1 107 ? -0.17068  -2.23723  20.98343  1.000 40.28885  ?  106 SER   A C     1 
ATOM   859  O  O     . SER   A 1 107 ? -0.27113  -1.29498  20.19266  1.000 33.92597  ?  106 SER   A O     1 
ATOM   860  C  CB    . SER   A 1 107 ? -1.66696  -2.06616  23.00701  1.000 41.79361  ?  106 SER   A CB    1 
ATOM   861  O  OG    . SER   A 1 107 ? -2.25452  -3.33903  22.78242  1.000 37.74181  ?  106 SER   A OG    1 
ATOM   862  N  N     . GLU   A 1 108 ? 0.01999   -3.49850  20.60498  1.000 39.41082  ?  107 GLU   A N     1 
ATOM   863  C  CA    . GLU   A 1 108 ? -0.07608  -3.94705  19.21961  1.000 44.97440  ?  107 GLU   A CA    1 
ATOM   864  C  C     . GLU   A 1 108 ? -1.49201  -4.34459  18.83934  1.000 45.17317  ?  107 GLU   A C     1 
ATOM   865  O  O     . GLU   A 1 108 ? -1.72043  -4.77328  17.70098  1.000 46.39809  ?  107 GLU   A O     1 
ATOM   866  C  CB    . GLU   A 1 108 ? 0.84846   -5.14778  18.97139  1.000 45.25648  ?  107 GLU   A CB    1 
ATOM   867  C  CG    . GLU   A 1 108 ? 2.34173   -4.87560  19.12298  1.000 49.72570  ?  107 GLU   A CG    1 
ATOM   868  C  CD    . GLU   A 1 108 ? 2.86635   -3.89125  18.09593  1.000 55.09239  ?  107 GLU   A CD    1 
ATOM   869  O  OE1   . GLU   A 1 108 ? 2.61851   -4.09254  16.88521  1.000 55.16793  ?  107 GLU   A OE1   1 
ATOM   870  O  OE2   . GLU   A 1 108 ? 3.52663   -2.90767  18.50442  1.000 61.97133  -1 107 GLU   A OE2   1 
ATOM   871  N  N     . ASP   A 1 109 ? -2.43837  -4.20400  19.75887  1.000 41.34791  ?  108 ASP   A N     1 
ATOM   872  C  CA    . ASP   A 1 109 ? -3.76576  -4.79336  19.64383  1.000 47.54806  ?  108 ASP   A CA    1 
ATOM   873  C  C     . ASP   A 1 109 ? -4.80787  -3.69197  19.89817  1.000 45.42291  ?  108 ASP   A C     1 
ATOM   874  O  O     . ASP   A 1 109 ? -5.54576  -3.71917  20.88994  1.000 44.19825  ?  108 ASP   A O     1 
ATOM   875  C  CB    . ASP   A 1 109 ? -3.90335  -5.96136  20.62945  1.000 48.74102  ?  108 ASP   A CB    1 
ATOM   876  C  CG    . ASP   A 1 109 ? -5.29348  -6.55599  20.65166  1.000 52.42370  ?  108 ASP   A CG    1 
ATOM   877  O  OD1   . ASP   A 1 109 ? -6.00359  -6.45140  19.63212  1.000 55.22659  ?  108 ASP   A OD1   1 
ATOM   878  O  OD2   . ASP   A 1 109 ? -5.67658  -7.11561  21.70209  1.000 61.48051  -1 108 ASP   A OD2   1 
ATOM   879  N  N     . VAL   A 1 110 ? -4.84679  -2.71207  19.01149  1.000 31.14237  ?  109 VAL   A N     1 
ATOM   880  C  CA    . VAL   A 1 110 ? -5.77619  -1.57677  19.11065  1.000 34.40381  ?  109 VAL   A CA    1 
ATOM   881  C  C     . VAL   A 1 110 ? -6.82963  -1.73354  18.05514  1.000 32.64884  ?  109 VAL   A C     1 
ATOM   882  O  O     . VAL   A 1 110 ? -6.51074  -1.97132  16.87975  1.000 33.27673  ?  109 VAL   A O     1 
ATOM   883  C  CB    . VAL   A 1 110 ? -5.04046  -0.23005  18.94042  1.000 27.31998  ?  109 VAL   A CB    1 
ATOM   884  C  CG1   . VAL   A 1 110 ? -6.04100  0.94798   19.06981  1.000 26.90668  ?  109 VAL   A CG1   1 
ATOM   885  C  CG2   . VAL   A 1 110 ? -3.88690  -0.11336  19.91636  1.000 34.86815  ?  109 VAL   A CG2   1 
ATOM   886  N  N     . PRO   A 1 111 ? -8.12671  -1.60597  18.38269  1.000 34.62197  ?  110 PRO   A N     1 
ATOM   887  C  CA    . PRO   A 1 111 ? -9.17784  -1.69356  17.35688  1.000 30.65255  ?  110 PRO   A CA    1 
ATOM   888  C  C     . PRO   A 1 111 ? -9.08225  -0.55477  16.34669  1.000 30.27883  ?  110 PRO   A C     1 
ATOM   889  O  O     . PRO   A 1 111 ? -9.07439  0.63120   16.71811  1.000 27.00730  ?  110 PRO   A O     1 
ATOM   890  C  CB    . PRO   A 1 111 ? -10.47389 -1.62656  18.17300  1.000 30.22791  ?  110 PRO   A CB    1 
ATOM   891  C  CG    . PRO   A 1 111 ? -10.06459 -2.11494  19.54750  1.000 32.62996  ?  110 PRO   A CG    1 
ATOM   892  C  CD    . PRO   A 1 111 ? -8.68059  -1.58553  19.75337  1.000 32.82760  ?  110 PRO   A CD    1 
ATOM   893  N  N     . MET   A 1 112 ? -8.98417  -0.92988  15.06204  1.000 29.69989  ?  111 MET   A N     1 
ATOM   894  C  CA    . MET   A 1 112 ? -8.85068  -0.00986  13.93342  1.000 24.68100  ?  111 MET   A CA    1 
ATOM   895  C  C     . MET   A 1 112 ? -9.55739  -0.58715  12.71992  1.000 24.20943  ?  111 MET   A C     1 
ATOM   896  O  O     . MET   A 1 112 ? -9.71257  -1.80554  12.60129  1.000 30.18914  ?  111 MET   A O     1 
ATOM   897  C  CB    . MET   A 1 112 ? -7.39840  0.24717   13.51142  1.000 28.97292  ?  111 MET   A CB    1 
ATOM   898  C  CG    . MET   A 1 112 ? -6.51013  0.86179   14.54191  1.000 35.95280  ?  111 MET   A CG    1 
ATOM   899  S  SD    . MET   A 1 112 ? -4.96039  1.32547   13.76792  1.000 38.38013  ?  111 MET   A SD    1 
ATOM   900  C  CE    . MET   A 1 112 ? -3.92255  1.37935   15.22026  1.000 33.26800  ?  111 MET   A CE    1 
ATOM   901  N  N     . VAL   A 1 113 ? -9.95753  0.29867   11.80584  1.000 24.86088  ?  112 VAL   A N     1 
ATOM   902  C  CA    . VAL   A 1 113 ? -10.47269 -0.07648  10.49050  1.000 25.71015  ?  112 VAL   A CA    1 
ATOM   903  C  C     . VAL   A 1 113 ? -9.82767  0.84376   9.46299   1.000 28.30386  ?  112 VAL   A C     1 
ATOM   904  O  O     . VAL   A 1 113 ? -9.76784  2.06260   9.67143   1.000 26.34970  ?  112 VAL   A O     1 
ATOM   905  C  CB    . VAL   A 1 113 ? -12.00981 0.02477   10.40894  1.000 27.30716  ?  112 VAL   A CB    1 
ATOM   906  C  CG1   . VAL   A 1 113 ? -12.49988 -0.29120  8.99898   1.000 29.72432  ?  112 VAL   A CG1   1 
ATOM   907  C  CG2   . VAL   A 1 113 ? -12.69352 -0.89515  11.42932  1.000 20.43965  ?  112 VAL   A CG2   1 
ATOM   908  N  N     . LEU   A 1 114 ? -9.31636  0.26499   8.37960   1.000 25.34841  ?  113 LEU   A N     1 
ATOM   909  C  CA    . LEU   A 1 114 ? -8.81826  1.05037   7.25325   1.000 26.50947  ?  113 LEU   A CA    1 
ATOM   910  C  C     . LEU   A 1 114 ? -9.98687  1.40557   6.33886   1.000 27.70824  ?  113 LEU   A C     1 
ATOM   911  O  O     . LEU   A 1 114 ? -10.77168 0.53203   5.95469   1.000 26.28018  ?  113 LEU   A O     1 
ATOM   912  C  CB    . LEU   A 1 114 ? -7.75146  0.28220   6.47353   1.000 26.60491  ?  113 LEU   A CB    1 
ATOM   913  C  CG    . LEU   A 1 114 ? -7.00067  1.05767   5.39358   1.000 26.24625  ?  113 LEU   A CG    1 
ATOM   914  C  CD1   . LEU   A 1 114 ? -6.24306  2.22754   5.99979   1.000 25.61057  ?  113 LEU   A CD1   1 
ATOM   915  C  CD2   . LEU   A 1 114 ? -6.04079  0.11709   4.66328   1.000 36.81914  ?  113 LEU   A CD2   1 
ATOM   916  N  N     . VAL   A 1 115 ? -10.10652 2.68570   6.01258   1.000 27.92540  ?  114 VAL   A N     1 
ATOM   917  C  CA    . VAL   A 1 115 ? -11.18910 3.20209   5.18282   1.000 27.41941  ?  114 VAL   A CA    1 
ATOM   918  C  C     . VAL   A 1 115 ? -10.56125 3.87733   3.96967   1.000 27.78643  ?  114 VAL   A C     1 
ATOM   919  O  O     . VAL   A 1 115 ? -9.80679  4.84739   4.11957   1.000 25.60701  ?  114 VAL   A O     1 
ATOM   920  C  CB    . VAL   A 1 115 ? -12.08642 4.18267   5.96237   1.000 23.66688  ?  114 VAL   A CB    1 
ATOM   921  C  CG1   . VAL   A 1 115 ? -13.18699 4.77938   5.06413   1.000 22.90686  ?  114 VAL   A CG1   1 
ATOM   922  C  CG2   . VAL   A 1 115 ? -12.69184 3.49810   7.18655   1.000 23.64654  ?  114 VAL   A CG2   1 
ATOM   923  N  N     . GLY   A 1 116 ? -10.86359 3.36008   2.77232   1.000 23.27924  ?  115 GLY   A N     1 
ATOM   924  C  CA    . GLY   A 1 116 ? -10.53618 4.06363   1.53908   1.000 27.80512  ?  115 GLY   A CA    1 
ATOM   925  C  C     . GLY   A 1 116 ? -11.74834 4.80867   0.98764   1.000 28.23622  ?  115 GLY   A C     1 
ATOM   926  O  O     . GLY   A 1 116 ? -12.66897 4.17147   0.47568   1.000 26.76474  ?  115 GLY   A O     1 
ATOM   927  N  N     . ASN   A 1 117 ? -11.76942 6.14216   1.10857   1.000 23.59048  ?  116 ASN   A N     1 
ATOM   928  C  CA    . ASN   A 1 117 ? -12.93772 6.97595   0.83713   1.000 25.37500  ?  116 ASN   A CA    1 
ATOM   929  C  C     . ASN   A 1 117 ? -12.85006 7.58529   -0.56304  1.000 24.84214  ?  116 ASN   A C     1 
ATOM   930  O  O     . ASN   A 1 117 ? -11.84711 7.44206   -1.26036  1.000 28.13778  ?  116 ASN   A O     1 
ATOM   931  C  CB    . ASN   A 1 117 ? -13.05914 8.07611   1.91590   1.000 23.52369  ?  116 ASN   A CB    1 
ATOM   932  C  CG    . ASN   A 1 117 ? -14.34209 8.89620   1.80076   1.000 23.19535  ?  116 ASN   A CG    1 
ATOM   933  O  OD1   . ASN   A 1 117 ? -15.44175 8.35263   1.62290   1.000 22.42143  ?  116 ASN   A OD1   1 
ATOM   934  N  ND2   . ASN   A 1 117 ? -14.20023 10.21205  1.88137   1.000 23.69228  ?  116 ASN   A ND2   1 
ATOM   935  N  N     . LYS   A 1 118 ? -13.93202 8.26231   -0.97533  1.000 25.03767  ?  117 LYS   A N     1 
ATOM   936  C  CA    . LYS   A 1 118 ? -14.06513 8.86768   -2.30614  1.000 26.61008  ?  117 LYS   A CA    1 
ATOM   937  C  C     . LYS   A 1 118 ? -14.06168 7.81429   -3.40797  1.000 31.44569  ?  117 LYS   A C     1 
ATOM   938  O  O     . LYS   A 1 118 ? -13.55493 8.05915   -4.51287  1.000 31.73606  ?  117 LYS   A O     1 
ATOM   939  C  CB    . LYS   A 1 118 ? -12.97884 9.92246   -2.58929  1.000 26.08547  ?  117 LYS   A CB    1 
ATOM   940  C  CG    . LYS   A 1 118 ? -12.71643 10.90616  -1.43356  1.000 28.06283  ?  117 LYS   A CG    1 
ATOM   941  C  CD    . LYS   A 1 118 ? -12.28501 12.29670  -1.92652  1.000 30.89944  ?  117 LYS   A CD    1 
ATOM   942  C  CE    . LYS   A 1 118 ? -11.95061 13.22462  -0.74568  1.000 27.86125  ?  117 LYS   A CE    1 
ATOM   943  N  NZ    . LYS   A 1 118 ? -11.35736 14.55618  -1.15430  1.000 30.10459  ?  117 LYS   A NZ    1 
ATOM   944  N  N     . CYS   A 1 119 ? -14.61241 6.63443   -3.12487  1.000 28.69188  ?  118 CYS   A N     1 
ATOM   945  C  CA    . CYS   A 1 119 ? -14.62514 5.58285   -4.13702  1.000 30.54842  ?  118 CYS   A CA    1 
ATOM   946  C  C     . CYS   A 1 119 ? -15.64934 5.84233   -5.24756  1.000 38.31702  ?  118 CYS   A C     1 
ATOM   947  O  O     . CYS   A 1 119 ? -15.74258 5.03612   -6.18552  1.000 32.72000  ?  118 CYS   A O     1 
ATOM   948  C  CB    . CYS   A 1 119 ? -14.86412 4.21791   -3.48078  1.000 29.12013  ?  118 CYS   A CB    1 
ATOM   949  S  SG    . CYS   A 1 119 ? -16.54891 3.89953   -2.93583  1.000 45.41727  ?  118 CYS   A SG    1 
ATOM   950  N  N     . ASP   A 1 120 ? -16.40576 6.94642   -5.16340  1.000 35.07701  ?  119 ASP   A N     1 
ATOM   951  C  CA    . ASP   A 1 120 ? -17.19389 7.43672   -6.28953  1.000 38.45913  ?  119 ASP   A CA    1 
ATOM   952  C  C     . ASP   A 1 120 ? -16.33832 8.07811   -7.37848  1.000 38.17433  ?  119 ASP   A C     1 
ATOM   953  O  O     . ASP   A 1 120 ? -16.84767 8.31760   -8.48063  1.000 39.78506  ?  119 ASP   A O     1 
ATOM   954  C  CB    . ASP   A 1 120 ? -18.22250 8.46442   -5.80524  1.000 34.27998  ?  119 ASP   A CB    1 
ATOM   955  C  CG    . ASP   A 1 120 ? -17.57529 9.61284   -5.03947  1.000 38.24720  ?  119 ASP   A CG    1 
ATOM   956  O  OD1   . ASP   A 1 120 ? -17.05546 9.36078   -3.91244  1.000 28.32205  ?  119 ASP   A OD1   1 
ATOM   957  O  OD2   . ASP   A 1 120 ? -17.56041 10.75575  -5.57593  1.000 30.59182  -1 119 ASP   A OD2   1 
ATOM   958  N  N     . LEU   A 1 121 ? -15.08639 8.39550   -7.09730  1.000 35.15701  ?  120 LEU   A N     1 
ATOM   959  C  CA    . LEU   A 1 121 ? -14.39082 9.20948   -8.08569  1.000 36.45109  ?  120 LEU   A CA    1 
ATOM   960  C  C     . LEU   A 1 121 ? -13.66957 8.32481   -9.09481  1.000 43.84040  ?  120 LEU   A C     1 
ATOM   961  O  O     . LEU   A 1 121 ? -13.27711 7.19814   -8.77720  1.000 42.14801  ?  120 LEU   A O     1 
ATOM   962  C  CB    . LEU   A 1 121 ? -13.37624 10.14592  -7.41482  1.000 33.46626  ?  120 LEU   A CB    1 
ATOM   963  C  CG    . LEU   A 1 121 ? -13.89983 11.27217  -6.52218  1.000 34.79097  ?  120 LEU   A CG    1 
ATOM   964  C  CD1   . LEU   A 1 121 ? -12.75333 11.97141  -5.77827  1.000 33.62168  ?  120 LEU   A CD1   1 
ATOM   965  C  CD2   . LEU   A 1 121 ? -14.76856 12.27580  -7.27796  1.000 31.21053  ?  120 LEU   A CD2   1 
ATOM   966  N  N     . PRO   A 1 122 ? -13.49012 8.82014   -10.32125 1.000 46.36790  ?  121 PRO   A N     1 
ATOM   967  C  CA    . PRO   A 1 122 ? -12.83169 7.99767   -11.35119 1.000 49.92124  ?  121 PRO   A CA    1 
ATOM   968  C  C     . PRO   A 1 122 ? -11.30667 8.00463   -11.28342 1.000 47.66972  ?  121 PRO   A C     1 
ATOM   969  O  O     . PRO   A 1 122 ? -10.67976 7.05612   -11.77568 1.000 50.29635  ?  121 PRO   A O     1 
ATOM   970  C  CB    . PRO   A 1 122 ? -13.34177 8.61238   -12.66314 1.000 49.95225  ?  121 PRO   A CB    1 
ATOM   971  C  CG    . PRO   A 1 122 ? -13.66961 10.03655  -12.31166 1.000 49.03640  ?  121 PRO   A CG    1 
ATOM   972  C  CD    . PRO   A 1 122 ? -14.12038 10.03256  -10.87503 1.000 38.11615  ?  121 PRO   A CD    1 
ATOM   973  N  N     . SER   A 1 123 ? -10.69349 9.00584   -10.65636 1.000 49.89274  ?  122 SER   A N     1 
ATOM   974  C  CA    . SER   A 1 123 ? -9.24131  9.18792   -10.69588 1.000 52.28080  ?  122 SER   A CA    1 
ATOM   975  C  C     . SER   A 1 123 ? -8.47943  8.31829   -9.69792  1.000 55.35222  ?  122 SER   A C     1 
ATOM   976  O  O     . SER   A 1 123 ? -7.47918  8.76743   -9.13361  1.000 49.81735  ?  122 SER   A O     1 
ATOM   977  C  CB    . SER   A 1 123 ? -8.92561  10.66444  -10.46767 1.000 56.35205  ?  122 SER   A CB    1 
ATOM   978  O  OG    . SER   A 1 123 ? -9.42404  11.11648  -9.21426  1.000 55.48016  ?  122 SER   A OG    1 
ATOM   979  N  N     . ARG   A 1 124 ? -8.90773  7.07242   -9.49168  1.000 48.51982  ?  123 ARG   A N     1 
ATOM   980  C  CA    . ARG   A 1 124 ? -8.31278  6.21098   -8.47593  1.000 41.41108  ?  123 ARG   A CA    1 
ATOM   981  C  C     . ARG   A 1 124 ? -6.81685  6.01899   -8.69027  1.000 46.59505  ?  123 ARG   A C     1 
ATOM   982  O  O     . ARG   A 1 124 ? -6.37311  5.62875   -9.77811  1.000 39.74385  ?  123 ARG   A O     1 
ATOM   983  C  CB    . ARG   A 1 124 ? -9.00914  4.85485   -8.48039  1.000 48.92977  ?  123 ARG   A CB    1 
ATOM   984  C  CG    . ARG   A 1 124 ? -8.26051  3.79665   -7.71766  1.000 46.88667  ?  123 ARG   A CG    1 
ATOM   985  C  CD    . ARG   A 1 124 ? -8.95574  2.46770   -7.84228  1.000 45.23828  ?  123 ARG   A CD    1 
ATOM   986  N  NE    . ARG   A 1 124 ? -10.23659 2.46956   -7.14828  1.000 51.46678  ?  123 ARG   A NE    1 
ATOM   987  C  CZ    . ARG   A 1 124 ? -10.41601 2.06512   -5.89569  1.000 45.31310  ?  123 ARG   A CZ    1 
ATOM   988  N  NH1   . ARG   A 1 124 ? -9.40024  1.69250   -5.13445  1.000 45.41206  ?  123 ARG   A NH1   1 
ATOM   989  N  NH2   . ARG   A 1 124 ? -11.64841 2.01583   -5.40201  1.000 42.58249  ?  123 ARG   A NH2   1 
ATOM   990  N  N     . THR   A 1 125 ? -6.03375  6.29336   -7.64092  1.000 38.42688  ?  124 THR   A N     1 
ATOM   991  C  CA    . THR   A 1 125 ? -4.59666  6.04921   -7.66361  1.000 40.25458  ?  124 THR   A CA    1 
ATOM   992  C  C     . THR   A 1 125 ? -4.12285  4.98158   -6.68900  1.000 45.80943  ?  124 THR   A C     1 
ATOM   993  O  O     . THR   A 1 125 ? -2.92333  4.67809   -6.68087  1.000 48.53228  ?  124 THR   A O     1 
ATOM   994  C  CB    . THR   A 1 125 ? -3.81246  7.33804   -7.36962  1.000 39.39896  ?  124 THR   A CB    1 
ATOM   995  O  OG1   . THR   A 1 125 ? -4.09303  7.78031   -6.03494  1.000 38.62484  ?  124 THR   A OG1   1 
ATOM   996  C  CG2   . THR   A 1 125 ? -4.18113  8.43632   -8.35385  1.000 41.30554  ?  124 THR   A CG2   1 
ATOM   997  N  N     . VAL   A 1 126 ? -5.00463  4.42273   -5.85989  1.000 43.78586  ?  125 VAL   A N     1 
ATOM   998  C  CA    . VAL   A 1 126 ? -4.65827  3.37244   -4.90595  1.000 38.79497  ?  125 VAL   A CA    1 
ATOM   999  C  C     . VAL   A 1 126 ? -5.52008  2.15455   -5.22403  1.000 44.15624  ?  125 VAL   A C     1 
ATOM   1000 O  O     . VAL   A 1 126 ? -6.74232  2.18674   -5.02507  1.000 36.02902  ?  125 VAL   A O     1 
ATOM   1001 C  CB    . VAL   A 1 126 ? -4.86469  3.82976   -3.45341  1.000 39.14864  ?  125 VAL   A CB    1 
ATOM   1002 C  CG1   . VAL   A 1 126 ? -4.38500  2.75691   -2.48100  1.000 34.84939  ?  125 VAL   A CG1   1 
ATOM   1003 C  CG2   . VAL   A 1 126 ? -4.15944  5.16114   -3.20232  1.000 34.13389  ?  125 VAL   A CG2   1 
ATOM   1004 N  N     . ASP   A 1 127 ? -4.88903  1.08330   -5.71668  1.000 45.57568  ?  126 ASP   A N     1 
ATOM   1005 C  CA    . ASP   A 1 127 ? -5.61009  -0.14512  -6.04308  1.000 49.53328  ?  126 ASP   A CA    1 
ATOM   1006 C  C     . ASP   A 1 127 ? -6.30058  -0.70502  -4.80888  1.000 46.69066  ?  126 ASP   A C     1 
ATOM   1007 O  O     . ASP   A 1 127 ? -5.78414  -0.62033  -3.69321  1.000 47.75999  ?  126 ASP   A O     1 
ATOM   1008 C  CB    . ASP   A 1 127 ? -4.66624  -1.23538  -6.57772  1.000 45.86233  ?  126 ASP   A CB    1 
ATOM   1009 C  CG    . ASP   A 1 127 ? -3.84547  -0.79230  -7.76756  1.000 64.55292  ?  126 ASP   A CG    1 
ATOM   1010 O  OD1   . ASP   A 1 127 ? -3.96207  0.38242   -8.19156  1.000 63.32117  -1 126 ASP   A OD1   1 
ATOM   1011 O  OD2   . ASP   A 1 127 ? -3.07494  -1.63906  -8.27942  1.000 68.81115  ?  126 ASP   A OD2   1 
ATOM   1012 N  N     . THR   A 1 128 ? -7.45734  -1.33149  -5.02468  1.000 45.32244  ?  127 THR   A N     1 
ATOM   1013 C  CA    . THR   A 1 128 ? -8.12066  -2.02907  -3.92660  1.000 47.82427  ?  127 THR   A CA    1 
ATOM   1014 C  C     . THR   A 1 128 ? -7.20556  -3.08149  -3.30998  1.000 46.90375  ?  127 THR   A C     1 
ATOM   1015 O  O     . THR   A 1 128 ? -7.08443  -3.17370  -2.07922  1.000 40.85744  ?  127 THR   A O     1 
ATOM   1016 C  CB    . THR   A 1 128 ? -9.41764  -2.66119  -4.42295  1.000 43.08598  ?  127 THR   A CB    1 
ATOM   1017 O  OG1   . THR   A 1 128 ? -10.36687 -1.62854  -4.70621  1.000 53.41980  ?  127 THR   A OG1   1 
ATOM   1018 C  CG2   . THR   A 1 128 ? -9.99979  -3.61588  -3.39164  1.000 40.62653  ?  127 THR   A CG2   1 
ATOM   1019 N  N     . LYS   A 1 129 ? -6.53092  -3.86528  -4.15418  1.000 44.87862  ?  128 LYS   A N     1 
ATOM   1020 C  CA    . LYS   A 1 129 ? -5.64041  -4.91022  -3.66388  1.000 44.39041  ?  128 LYS   A CA    1 
ATOM   1021 C  C     . LYS   A 1 129 ? -4.49574  -4.32980  -2.84608  1.000 45.28712  ?  128 LYS   A C     1 
ATOM   1022 O  O     . LYS   A 1 129 ? -4.03312  -4.95635  -1.87969  1.000 42.06379  ?  128 LYS   A O     1 
ATOM   1023 C  CB    . LYS   A 1 129 ? -5.10053  -5.71951  -4.84892  1.000 50.75040  ?  128 LYS   A CB    1 
ATOM   1024 C  CG    . LYS   A 1 129 ? -4.43693  -7.02627  -4.46098  1.000 55.92976  ?  128 LYS   A CG    1 
ATOM   1025 C  CD    . LYS   A 1 129 ? -3.05121  -7.14596  -5.07780  1.000 58.64783  ?  128 LYS   A CD    1 
ATOM   1026 C  CE    . LYS   A 1 129 ? -2.35627  -8.42857  -4.63362  1.000 58.03398  ?  128 LYS   A CE    1 
ATOM   1027 N  NZ    . LYS   A 1 129 ? -0.90266  -8.38140  -4.96849  1.000 62.14892  ?  128 LYS   A NZ    1 
ATOM   1028 N  N     . GLN   A 1 130 ? -4.03648  -3.13027  -3.20560  1.000 42.06017  ?  129 GLN   A N     1 
ATOM   1029 C  CA    . GLN   A 1 130 ? -2.96632  -2.49508  -2.44416  1.000 41.82345  ?  129 GLN   A CA    1 
ATOM   1030 C  C     . GLN   A 1 130 ? -3.42681  -2.14066  -1.03353  1.000 42.75391  ?  129 GLN   A C     1 
ATOM   1031 O  O     . GLN   A 1 130 ? -2.65590  -2.25283  -0.07179  1.000 39.51770  ?  129 GLN   A O     1 
ATOM   1032 C  CB    . GLN   A 1 130 ? -2.48077  -1.25270  -3.18343  1.000 42.74545  ?  129 GLN   A CB    1 
ATOM   1033 C  CG    . GLN   A 1 130 ? -1.16687  -0.70388  -2.68421  1.000 47.43682  ?  129 GLN   A CG    1 
ATOM   1034 C  CD    . GLN   A 1 130 ? -0.73235  0.51231   -3.47633  1.000 56.16064  ?  129 GLN   A CD    1 
ATOM   1035 O  OE1   . GLN   A 1 130 ? -1.31344  0.82765   -4.52525  1.000 58.06449  ?  129 GLN   A OE1   1 
ATOM   1036 N  NE2   . GLN   A 1 130 ? 0.28495   1.21186   -2.97784  1.000 55.22636  ?  129 GLN   A NE2   1 
ATOM   1037 N  N     . ALA   A 1 131 ? -4.68031  -1.71087  -0.89221  1.000 42.73508  ?  130 ALA   A N     1 
ATOM   1038 C  CA    . ALA   A 1 131 ? -5.21962  -1.39945  0.42619   1.000 39.10054  ?  130 ALA   A CA    1 
ATOM   1039 C  C     . ALA   A 1 131 ? -5.56864  -2.65595  1.20553   1.000 34.67080  ?  130 ALA   A C     1 
ATOM   1040 O  O     . ALA   A 1 131 ? -5.32421  -2.72284  2.41406   1.000 40.14883  ?  130 ALA   A O     1 
ATOM   1041 C  CB    . ALA   A 1 131 ? -6.44521  -0.50515  0.28728   1.000 40.08079  ?  130 ALA   A CB    1 
ATOM   1042 N  N     . GLN   A 1 132 ? -6.14407  -3.65995  0.53938   1.000 42.98200  ?  131 GLN   A N     1 
ATOM   1043 C  CA    . GLN   A 1 132 ? -6.48063  -4.90052  1.23049   1.000 40.92592  ?  131 GLN   A CA    1 
ATOM   1044 C  C     . GLN   A 1 132 ? -5.22799  -5.58854  1.75178   1.000 38.05854  ?  131 GLN   A C     1 
ATOM   1045 O  O     . GLN   A 1 132 ? -5.23556  -6.14978  2.85147   1.000 42.79447  ?  131 GLN   A O     1 
ATOM   1046 C  CB    . GLN   A 1 132 ? -7.26644  -5.83983  0.30827   1.000 44.41903  ?  131 GLN   A CB    1 
ATOM   1047 C  CG    . GLN   A 1 132 ? -8.67964  -5.37368  -0.01208  1.000 43.61347  ?  131 GLN   A CG    1 
ATOM   1048 C  CD    . GLN   A 1 132 ? -9.41026  -6.31326  -0.95927  1.000 54.10571  ?  131 GLN   A CD    1 
ATOM   1049 O  OE1   . GLN   A 1 132 ? -8.81066  -6.88663  -1.86981  1.000 50.92386  ?  131 GLN   A OE1   1 
ATOM   1050 N  NE2   . GLN   A 1 132 ? -10.71750 -6.47119  -0.74863  1.000 58.94518  ?  131 GLN   A NE2   1 
ATOM   1051 N  N     . ASP   A 1 133 ? -4.13868  -5.54704  0.98152   1.000 43.82685  ?  132 ASP   A N     1 
ATOM   1052 C  CA    . ASP   A 1 133 ? -2.88897  -6.15907  1.42493   1.000 41.71085  ?  132 ASP   A CA    1 
ATOM   1053 C  C     . ASP   A 1 133 ? -2.35553  -5.46908  2.66778   1.000 40.99015  ?  132 ASP   A C     1 
ATOM   1054 O  O     . ASP   A 1 133 ? -1.88778  -6.13041  3.60327   1.000 43.78996  ?  132 ASP   A O     1 
ATOM   1055 C  CB    . ASP   A 1 133 ? -1.83792  -6.10593  0.31182   1.000 47.92645  ?  132 ASP   A CB    1 
ATOM   1056 C  CG    . ASP   A 1 133 ? -2.08799  -7.12781  -0.80192  1.000 51.27005  ?  132 ASP   A CG    1 
ATOM   1057 O  OD1   . ASP   A 1 133 ? -2.94091  -8.02463  -0.63816  1.000 53.52313  -1 132 ASP   A OD1   1 
ATOM   1058 O  OD2   . ASP   A 1 133 ? -1.41632  -7.02515  -1.84795  1.000 51.70190  ?  132 ASP   A OD2   1 
ATOM   1059 N  N     . LEU   A 1 134 ? -2.39293  -4.13635  2.68344   1.000 37.74194  ?  133 LEU   A N     1 
ATOM   1060 C  CA    . LEU   A 1 134 ? -1.96820  -3.39715  3.86734   1.000 43.15141  ?  133 LEU   A CA    1 
ATOM   1061 C  C     . LEU   A 1 134 ? -2.81941  -3.77406  5.07110   1.000 39.29175  ?  133 LEU   A C     1 
ATOM   1062 O  O     . LEU   A 1 134 ? -2.29328  -4.09498  6.14314   1.000 36.09505  ?  133 LEU   A O     1 
ATOM   1063 C  CB    . LEU   A 1 134 ? -2.04956  -1.89570  3.60908   1.000 43.03437  ?  133 LEU   A CB    1 
ATOM   1064 C  CG    . LEU   A 1 134 ? -1.45854  -0.99968  4.68505   1.000 42.77834  ?  133 LEU   A CG    1 
ATOM   1065 C  CD1   . LEU   A 1 134 ? 0.06453   -1.11954  4.66940   1.000 44.49035  ?  133 LEU   A CD1   1 
ATOM   1066 C  CD2   . LEU   A 1 134 ? -1.88252  0.43279   4.44544   1.000 39.57480  ?  133 LEU   A CD2   1 
ATOM   1067 N  N     . ALA   A 1 135 ? -4.14287  -3.76075  4.90038   1.000 36.05935  ?  134 ALA   A N     1 
ATOM   1068 C  CA    . ALA   A 1 135 ? -5.03948  -4.12652  5.99019   1.000 38.91451  ?  134 ALA   A CA    1 
ATOM   1069 C  C     . ALA   A 1 135 ? -4.74964  -5.53674  6.49127   1.000 42.77332  ?  134 ALA   A C     1 
ATOM   1070 O  O     . ALA   A 1 135 ? -4.65942  -5.76880  7.70163   1.000 42.86474  ?  134 ALA   A O     1 
ATOM   1071 C  CB    . ALA   A 1 135 ? -6.49471  -4.00115  5.53930   1.000 33.64725  ?  134 ALA   A CB    1 
ATOM   1072 N  N     . ARG   A 1 136 ? -4.61104  -6.49580  5.57226   1.000 38.70243  ?  135 ARG   A N     1 
ATOM   1073 C  CA    . ARG   A 1 136 ? -4.25105  -7.85226  5.97741   1.000 47.61155  ?  135 ARG   A CA    1 
ATOM   1074 C  C     . ARG   A 1 136 ? -2.96999  -7.86083  6.80762   1.000 42.84396  ?  135 ARG   A C     1 
ATOM   1075 O  O     . ARG   A 1 136 ? -2.90177  -8.53541  7.83996   1.000 43.42185  ?  135 ARG   A O     1 
ATOM   1076 C  CB    . ARG   A 1 136 ? -4.10328  -8.75285  4.74801   1.000 45.73189  ?  135 ARG   A CB    1 
ATOM   1077 C  CG    . ARG   A 1 136 ? -3.90575  -10.23329 5.06248   1.000 48.57329  ?  135 ARG   A CG    1 
ATOM   1078 C  CD    . ARG   A 1 136 ? -3.72724  -11.05252 3.78323   1.000 50.25159  ?  135 ARG   A CD    1 
ATOM   1079 N  NE    . ARG   A 1 136 ? -4.71341  -10.68470 2.77202   1.000 55.91071  ?  135 ARG   A NE    1 
ATOM   1080 C  CZ    . ARG   A 1 136 ? -4.42351  -10.11987 1.60654   1.000 56.68897  ?  135 ARG   A CZ    1 
ATOM   1081 N  NH1   . ARG   A 1 136 ? -3.17123  -9.91109  1.23118   1.000 53.26715  ?  135 ARG   A NH1   1 
ATOM   1082 N  NH2   . ARG   A 1 136 ? -5.41610  -9.75127  0.79933   1.000 52.96610  ?  135 ARG   A NH2   1 
ATOM   1083 N  N     . SER   A 1 137 ? -1.95059  -7.09681  6.39133   1.000 42.70465  ?  136 SER   A N     1 
ATOM   1084 C  CA    . SER   A 1 137 ? -0.71748  -7.06322  7.17489   1.000 41.87296  ?  136 SER   A CA    1 
ATOM   1085 C  C     . SER   A 1 137 ? -0.94104  -6.44315  8.55296   1.000 47.86512  ?  136 SER   A C     1 
ATOM   1086 O  O     . SER   A 1 137 ? -0.27204  -6.82396  9.52213   1.000 51.41287  ?  136 SER   A O     1 
ATOM   1087 C  CB    . SER   A 1 137 ? 0.37999   -6.32135  6.40888   1.000 44.06540  ?  136 SER   A CB    1 
ATOM   1088 O  OG    . SER   A 1 137 ? 0.07628   -4.95185  6.20962   1.000 47.52007  ?  136 SER   A OG    1 
ATOM   1089 N  N     . TYR   A 1 138 ? -1.87894  -5.50587  8.67255   1.000 42.91283  ?  137 TYR   A N     1 
ATOM   1090 C  CA    . TYR   A 1 138 ? -2.19552  -4.92620  9.97018   1.000 39.92094  ?  137 TYR   A CA    1 
ATOM   1091 C  C     . TYR   A 1 138 ? -3.10357  -5.80801  10.81076  1.000 38.70174  ?  137 TYR   A C     1 
ATOM   1092 O  O     . TYR   A 1 138 ? -3.23965  -5.55503  12.01042  1.000 38.33473  ?  137 TYR   A O     1 
ATOM   1093 C  CB    . TYR   A 1 138 ? -2.87825  -3.57269  9.79864   1.000 41.67399  ?  137 TYR   A CB    1 
ATOM   1094 C  CG    . TYR   A 1 138 ? -2.01723  -2.44810  9.28216   1.000 40.06097  ?  137 TYR   A CG    1 
ATOM   1095 C  CD1   . TYR   A 1 138 ? -0.62773  -2.53594  9.26190   1.000 40.30429  ?  137 TYR   A CD1   1 
ATOM   1096 C  CD2   . TYR   A 1 138 ? -2.60561  -1.28116  8.82881   1.000 41.87286  ?  137 TYR   A CD2   1 
ATOM   1097 C  CE1   . TYR   A 1 138 ? 0.14552   -1.48238  8.79073   1.000 38.53415  ?  137 TYR   A CE1   1 
ATOM   1098 C  CE2   . TYR   A 1 138 ? -1.85261  -0.23302  8.36130   1.000 42.60254  ?  137 TYR   A CE2   1 
ATOM   1099 C  CZ    . TYR   A 1 138 ? -0.47852  -0.32864  8.34359   1.000 41.21236  ?  137 TYR   A CZ    1 
ATOM   1100 O  OH    . TYR   A 1 138 ? 0.23500   0.75532   7.87342   1.000 40.75280  ?  137 TYR   A OH    1 
ATOM   1101 N  N     . GLY   A 1 139 ? -3.75311  -6.80381  10.21301  1.000 38.16874  ?  138 GLY   A N     1 
ATOM   1102 C  CA    . GLY   A 1 139 ? -4.72582  -7.59526  10.93820  1.000 35.11295  ?  138 GLY   A CA    1 
ATOM   1103 C  C     . GLY   A 1 139 ? -6.04846  -6.90275  11.19821  1.000 36.30008  ?  138 GLY   A C     1 
ATOM   1104 O  O     . GLY   A 1 139 ? -6.77398  -7.29985  12.11648  1.000 35.74568  ?  138 GLY   A O     1 
ATOM   1105 N  N     . ILE   A 1 140 ? -6.39098  -5.88709  10.40297  1.000 38.12238  ?  139 ILE   A N     1 
ATOM   1106 C  CA    . ILE   A 1 140 ? -7.61615  -5.12247  10.59575  1.000 33.07026  ?  139 ILE   A CA    1 
ATOM   1107 C  C     . ILE   A 1 140 ? -8.44869  -5.18663  9.29083   1.000 30.27158  ?  139 ILE   A C     1 
ATOM   1108 O  O     . ILE   A 1 140 ? -7.90548  -5.41696  8.21612   1.000 34.42823  ?  139 ILE   A O     1 
ATOM   1109 C  CB    . ILE   A 1 140 ? -7.33429  -3.65314  10.97059  1.000 29.95707  ?  139 ILE   A CB    1 
ATOM   1110 C  CG1   . ILE   A 1 140 ? -6.71981  -2.89563  9.79099   1.000 30.13070  ?  139 ILE   A CG1   1 
ATOM   1111 C  CG2   . ILE   A 1 140 ? -6.42964  -3.57943  12.19784  1.000 27.81645  ?  139 ILE   A CG2   1 
ATOM   1112 C  CD1   . ILE   A 1 140 ? -6.49370  -1.42350  10.07103  1.000 28.14033  ?  139 ILE   A CD1   1 
ATOM   1113 N  N     . PRO   A 1 141 ? -9.75418  -4.97086  9.41495   1.000 35.39423  ?  140 PRO   A N     1 
ATOM   1114 C  CA    . PRO   A 1 141 ? -10.60461 -4.87574  8.21144   1.000 32.41617  ?  140 PRO   A CA    1 
ATOM   1115 C  C     . PRO   A 1 141 ? -10.29603 -3.66203  7.34261   1.000 30.82273  ?  140 PRO   A C     1 
ATOM   1116 O  O     . PRO   A 1 141 ? -9.79377  -2.63577  7.81353   1.000 29.35263  ?  140 PRO   A O     1 
ATOM   1117 C  CB    . PRO   A 1 141 ? -12.01728 -4.76183  8.80387   1.000 31.20137  ?  140 PRO   A CB    1 
ATOM   1118 C  CG    . PRO   A 1 141 ? -11.90289 -5.28554  10.19631  1.000 30.96922  ?  140 PRO   A CG    1 
ATOM   1119 C  CD    . PRO   A 1 141 ? -10.54003 -4.89905  10.65261  1.000 28.82281  ?  140 PRO   A CD    1 
ATOM   1120 N  N     . PHE   A 1 142 ? -10.61298 -3.79436  6.04644   1.000 32.19556  ?  141 PHE   A N     1 
ATOM   1121 C  CA    . PHE   A 1 142 ? -10.55781 -2.69950  5.08481   1.000 31.81460  ?  141 PHE   A CA    1 
ATOM   1122 C  C     . PHE   A 1 142 ? -11.92220 -2.55602  4.42331   1.000 32.09026  ?  141 PHE   A C     1 
ATOM   1123 O  O     . PHE   A 1 142 ? -12.48836 -3.53929  3.92655   1.000 35.96597  ?  141 PHE   A O     1 
ATOM   1124 C  CB    . PHE   A 1 142 ? -9.48432  -2.90811  4.01092   1.000 30.34433  ?  141 PHE   A CB    1 
ATOM   1125 C  CG    . PHE   A 1 142 ? -9.64464  -1.99714  2.80953   1.000 33.07481  ?  141 PHE   A CG    1 
ATOM   1126 C  CD1   . PHE   A 1 142 ? -9.51117  -0.61397  2.93822   1.000 27.19581  ?  141 PHE   A CD1   1 
ATOM   1127 C  CD2   . PHE   A 1 142 ? -9.94383  -2.52125  1.56125   1.000 35.35237  ?  141 PHE   A CD2   1 
ATOM   1128 C  CE1   . PHE   A 1 142 ? -9.66859  0.22520   1.84595   1.000 34.97176  ?  141 PHE   A CE1   1 
ATOM   1129 C  CE2   . PHE   A 1 142 ? -10.10834 -1.68758  0.46041   1.000 37.78507  ?  141 PHE   A CE2   1 
ATOM   1130 C  CZ    . PHE   A 1 142 ? -9.96492  -0.31042  0.59995   1.000 36.39246  ?  141 PHE   A CZ    1 
ATOM   1131 N  N     . ILE   A 1 143 ? -12.44400 -1.33496  4.40599   1.000 29.42938  ?  142 ILE   A N     1 
ATOM   1132 C  CA    . ILE   A 1 143 ? -13.76176 -1.04721  3.84467   1.000 31.05278  ?  142 ILE   A CA    1 
ATOM   1133 C  C     . ILE   A 1 143 ? -13.62435 0.14495   2.91623   1.000 30.11954  ?  142 ILE   A C     1 
ATOM   1134 O  O     . ILE   A 1 143 ? -12.97557 1.13078   3.27763   1.000 30.15313  ?  142 ILE   A O     1 
ATOM   1135 C  CB    . ILE   A 1 143 ? -14.79341 -0.77230  4.95816   1.000 40.45172  ?  142 ILE   A CB    1 
ATOM   1136 C  CG1   . ILE   A 1 143 ? -15.05550 -2.06149  5.74224   1.000 36.66429  ?  142 ILE   A CG1   1 
ATOM   1137 C  CG2   . ILE   A 1 143 ? -16.11975 -0.17998  4.39341   1.000 34.07775  ?  142 ILE   A CG2   1 
ATOM   1138 C  CD1   . ILE   A 1 143 ? -15.95301 -1.85569  6.88120   1.000 42.90856  ?  142 ILE   A CD1   1 
ATOM   1139 N  N     . GLU   A 1 144 ? -14.20021 0.04516   1.71003   1.000 28.10055  ?  143 GLU   A N     1 
ATOM   1140 C  CA    . GLU   A 1 144 ? -14.21413 1.15832   0.76563   1.000 28.73770  ?  143 GLU   A CA    1 
ATOM   1141 C  C     . GLU   A 1 144 ? -15.49284 1.95221   0.94448   1.000 27.38685  ?  143 GLU   A C     1 
ATOM   1142 O  O     . GLU   A 1 144 ? -16.55582 1.38187   1.17379   1.000 31.74077  ?  143 GLU   A O     1 
ATOM   1143 C  CB    . GLU   A 1 144 ? -14.12442 0.68869   -0.69075  1.000 32.67140  ?  143 GLU   A CB    1 
ATOM   1144 C  CG    . GLU   A 1 144 ? -12.83559 0.01347   -1.05035  1.000 36.17855  ?  143 GLU   A CG    1 
ATOM   1145 C  CD    . GLU   A 1 144 ? -12.55972 0.01984   -2.55027  1.000 51.59649  ?  143 GLU   A CD    1 
ATOM   1146 O  OE1   . GLU   A 1 144 ? -13.51973 -0.18467  -3.34195  1.000 52.60046  ?  143 GLU   A OE1   1 
ATOM   1147 O  OE2   . GLU   A 1 144 ? -11.38263 0.23949   -2.92793  1.000 47.79372  -1 143 GLU   A OE2   1 
ATOM   1148 N  N     . THR   A 1 145 ? -15.39163 3.27159   0.84896   1.000 25.51535  ?  144 THR   A N     1 
ATOM   1149 C  CA    . THR   A 1 145 ? -16.54110 4.12234   1.10819   1.000 31.31982  ?  144 THR   A CA    1 
ATOM   1150 C  C     . THR   A 1 145 ? -16.61462 5.26292   0.11212   1.000 22.79196  ?  144 THR   A C     1 
ATOM   1151 O  O     . THR   A 1 145 ? -15.63030 5.63539   -0.52310  1.000 25.90834  ?  144 THR   A O     1 
ATOM   1152 C  CB    . THR   A 1 145 ? -16.52419 4.73504   2.52587   1.000 24.92905  ?  144 THR   A CB    1 
ATOM   1153 O  OG1   . THR   A 1 145 ? -15.34857 5.54565   2.68989   1.000 22.79734  ?  144 THR   A OG1   1 
ATOM   1154 C  CG2   . THR   A 1 145 ? -16.55548 3.65901   3.57452   1.000 26.90684  ?  144 THR   A CG2   1 
ATOM   1155 N  N     . SER   A 1 146 ? -17.81039 5.82002   0.01071   1.000 25.15908  ?  145 SER   A N     1 
ATOM   1156 C  CA    . SER   A 1 146 ? -18.02919 7.13518   -0.57773  1.000 26.89658  ?  145 SER   A CA    1 
ATOM   1157 C  C     . SER   A 1 146 ? -18.95497 7.88226   0.36240   1.000 24.60899  ?  145 SER   A C     1 
ATOM   1158 O  O     . SER   A 1 146 ? -20.04803 7.39640   0.67418   1.000 26.05579  ?  145 SER   A O     1 
ATOM   1159 C  CB    . SER   A 1 146 ? -18.64233 7.04633   -1.98653  1.000 24.80635  ?  145 SER   A CB    1 
ATOM   1160 O  OG    . SER   A 1 146 ? -19.00936 8.32771   -2.47652  1.000 24.10354  ?  145 SER   A OG    1 
ATOM   1161 N  N     . ALA   A 1 147 ? -18.50899 9.04504   0.83687   1.000 28.03981  ?  146 ALA   A N     1 
ATOM   1162 C  CA    . ALA   A 1 147 ? -19.41840 9.91985   1.56113   1.000 26.74887  ?  146 ALA   A CA    1 
ATOM   1163 C  C     . ALA   A 1 147 ? -20.44975 10.53818  0.62531   1.000 28.63898  ?  146 ALA   A C     1 
ATOM   1164 O  O     . ALA   A 1 147 ? -21.55175 10.87080  1.06669   1.000 27.49670  ?  146 ALA   A O     1 
ATOM   1165 C  CB    . ALA   A 1 147 ? -18.64866 11.01578  2.28677   1.000 24.06606  ?  146 ALA   A CB    1 
ATOM   1166 N  N     . LYS   A 1 148 ? -20.12974 10.66268  -0.66343  1.000 30.32444  ?  147 LYS   A N     1 
ATOM   1167 C  CA    . LYS   A 1 148 ? -21.07455 11.28096  -1.58830  1.000 28.57770  ?  147 LYS   A CA    1 
ATOM   1168 C  C     . LYS   A 1 148 ? -22.25360 10.36533  -1.89368  1.000 28.37453  ?  147 LYS   A C     1 
ATOM   1169 O  O     . LYS   A 1 148 ? -23.41017 10.80991  -1.84866  1.000 31.31168  ?  147 LYS   A O     1 
ATOM   1170 C  CB    . LYS   A 1 148 ? -20.35860 11.69150  -2.86623  1.000 27.99326  ?  147 LYS   A CB    1 
ATOM   1171 C  CG    . LYS   A 1 148 ? -21.20839 12.54556  -3.76789  1.000 39.28888  ?  147 LYS   A CG    1 
ATOM   1172 C  CD    . LYS   A 1 148 ? -20.45031 12.84874  -5.03934  1.000 33.99342  ?  147 LYS   A CD    1 
ATOM   1173 C  CE    . LYS   A 1 148 ? -21.29230 13.64829  -6.00665  1.000 42.60255  ?  147 LYS   A CE    1 
ATOM   1174 N  NZ    . LYS   A 1 148 ? -20.42247 14.14103  -7.10274  1.000 41.35844  ?  147 LYS   A NZ    1 
ATOM   1175 N  N     . THR   A 1 149 ? -21.99833 9.08923   -2.18851  1.000 27.39789  ?  148 THR   A N     1 
ATOM   1176 C  CA    . THR   A 1 149 ? -23.08231 8.15596   -2.47910  1.000 28.00984  ?  148 THR   A CA    1 
ATOM   1177 C  C     . THR   A 1 149 ? -23.59397 7.42166   -1.24752  1.000 29.65509  ?  148 THR   A C     1 
ATOM   1178 O  O     . THR   A 1 149 ? -24.55767 6.65925   -1.36113  1.000 27.48454  ?  148 THR   A O     1 
ATOM   1179 C  CB    . THR   A 1 149 ? -22.64371 7.10060   -3.48914  1.000 25.34121  ?  148 THR   A CB    1 
ATOM   1180 O  OG1   . THR   A 1 149 ? -21.66799 6.25387   -2.86087  1.000 28.29561  ?  148 THR   A OG1   1 
ATOM   1181 C  CG2   . THR   A 1 149 ? -22.07496 7.72830   -4.77052  1.000 27.13163  ?  148 THR   A CG2   1 
ATOM   1182 N  N     . ARG   A 1 150 ? -22.95530 7.60028   -0.08650  1.000 27.66706  ?  149 ARG   A N     1 
ATOM   1183 C  CA    . ARG   A 1 150 ? -23.16463 6.85439   1.15959   1.000 27.90308  ?  149 ARG   A CA    1 
ATOM   1184 C  C     . ARG   A 1 150 ? -22.65126 5.41768   1.11488   1.000 28.57614  ?  149 ARG   A C     1 
ATOM   1185 O  O     . ARG   A 1 150 ? -22.77711 4.71277   2.11957   1.000 31.58007  ?  149 ARG   A O     1 
ATOM   1186 C  CB    . ARG   A 1 150 ? -24.63201 6.81106   1.62233   1.000 28.50768  ?  149 ARG   A CB    1 
ATOM   1187 C  CG    . ARG   A 1 150 ? -25.37659 8.12097   1.47871   1.000 36.18203  ?  149 ARG   A CG    1 
ATOM   1188 C  CD    . ARG   A 1 150 ? -26.66254 8.11443   2.27485   1.000 34.20134  ?  149 ARG   A CD    1 
ATOM   1189 N  NE    . ARG   A 1 150 ? -26.35698 8.33543   3.67229   1.000 39.06768  ?  149 ARG   A NE    1 
ATOM   1190 C  CZ    . ARG   A 1 150 ? -26.35386 7.39240   4.59833   1.000 40.41385  ?  149 ARG   A CZ    1 
ATOM   1191 N  NH1   . ARG   A 1 150 ? -26.75525 6.15951   4.32884   1.000 40.47959  ?  149 ARG   A NH1   1 
ATOM   1192 N  NH2   . ARG   A 1 150 ? -25.94080 7.69743   5.82322   1.000 39.02415  ?  149 ARG   A NH2   1 
ATOM   1193 N  N     . GLN   A 1 151 ? -22.05528 4.95791   0.01202   1.000 28.83211  ?  150 GLN   A N     1 
ATOM   1194 C  CA    . GLN   A 1 151 ? -21.54186 3.58950   -0.03022  1.000 26.03078  ?  150 GLN   A CA    1 
ATOM   1195 C  C     . GLN   A 1 151 ? -20.61905 3.30299   1.15712   1.000 29.52040  ?  150 GLN   A C     1 
ATOM   1196 O  O     . GLN   A 1 151 ? -19.66264 4.03040   1.39639   1.000 27.57959  ?  150 GLN   A O     1 
ATOM   1197 C  CB    . GLN   A 1 151 ? -20.78493 3.33307   -1.33207  1.000 31.40023  ?  150 GLN   A CB    1 
ATOM   1198 C  CG    . GLN   A 1 151 ? -20.18234 1.94337   -1.38637  1.000 30.24860  ?  150 GLN   A CG    1 
ATOM   1199 C  CD    . GLN   A 1 151 ? -19.37531 1.69855   -2.65278  1.000 40.78901  ?  150 GLN   A CD    1 
ATOM   1200 O  OE1   . GLN   A 1 151 ? -19.67365 2.25433   -3.71373  1.000 33.94046  ?  150 GLN   A OE1   1 
ATOM   1201 N  NE2   . GLN   A 1 151 ? -18.33960 0.86310   -2.54249  1.000 41.75127  ?  150 GLN   A NE2   1 
ATOM   1202 N  N     . GLY   A 1 152 ? -20.91386 2.23785   1.89381   1.000 28.71095  ?  151 GLY   A N     1 
ATOM   1203 C  CA    . GLY   A 1 152 ? -20.03759 1.76272   2.94984   1.000 29.19390  ?  151 GLY   A CA    1 
ATOM   1204 C  C     . GLY   A 1 152 ? -19.95182 2.61574   4.20624   1.000 28.71912  ?  151 GLY   A C     1 
ATOM   1205 O  O     . GLY   A 1 152 ? -19.16745 2.28473   5.09611   1.000 30.99021  ?  151 GLY   A O     1 
ATOM   1206 N  N     . VAL   A 1 153 ? -20.72958 3.69392   4.32453   1.000 27.61958  ?  152 VAL   A N     1 
ATOM   1207 C  CA    . VAL   A 1 153 ? -20.58158 4.58738   5.46839   1.000 29.20195  ?  152 VAL   A CA    1 
ATOM   1208 C  C     . VAL   A 1 153 ? -21.00198 3.88478   6.75982   1.000 30.96279  ?  152 VAL   A C     1 
ATOM   1209 O  O     . VAL   A 1 153 ? -20.22949 3.81776   7.72459   1.000 25.84440  ?  152 VAL   A O     1 
ATOM   1210 C  CB    . VAL   A 1 153 ? -21.37248 5.88615   5.25350   1.000 27.48976  ?  152 VAL   A CB    1 
ATOM   1211 C  CG1   . VAL   A 1 153 ? -21.35235 6.71294   6.53016   1.000 30.70413  ?  152 VAL   A CG1   1 
ATOM   1212 C  CG2   . VAL   A 1 153 ? -20.78838 6.67502   4.10000   1.000 28.68521  ?  152 VAL   A CG2   1 
ATOM   1213 N  N     . ASP   A 1 154 ? -22.22581 3.34811   6.79511   1.000 29.16227  ?  153 ASP   A N     1 
ATOM   1214 C  CA    . ASP   A 1 154 ? -22.65696 2.54036   7.93520   1.000 30.86988  ?  153 ASP   A CA    1 
ATOM   1215 C  C     . ASP   A 1 154 ? -21.67722 1.39744   8.20348   1.000 34.20388  ?  153 ASP   A C     1 
ATOM   1216 O  O     . ASP   A 1 154 ? -21.28048 1.14640   9.35101   1.000 34.59331  ?  153 ASP   A O     1 
ATOM   1217 C  CB    . ASP   A 1 154 ? -24.06874 1.98976   7.68691   1.000 33.01730  ?  153 ASP   A CB    1 
ATOM   1218 C  CG    . ASP   A 1 154 ? -25.17671 2.99384   8.01988   1.000 39.30948  ?  153 ASP   A CG    1 
ATOM   1219 O  OD1   . ASP   A 1 154 ? -24.88015 4.06870   8.59213   1.000 42.21312  ?  153 ASP   A OD1   1 
ATOM   1220 O  OD2   . ASP   A 1 154 ? -26.36232 2.70478   7.70946   1.000 42.10111  -1 153 ASP   A OD2   1 
ATOM   1221 N  N     . ASP   A 1 155 ? -21.25769 0.70314   7.14730   1.000 32.40599  ?  154 ASP   A N     1 
ATOM   1222 C  CA    . ASP   A 1 155 ? -20.44120 -0.49099  7.33399   1.000 35.04567  ?  154 ASP   A CA    1 
ATOM   1223 C  C     . ASP   A 1 155 ? -19.12053 -0.16018  8.03133   1.000 30.28100  ?  154 ASP   A C     1 
ATOM   1224 O  O     . ASP   A 1 155 ? -18.67313 -0.89756  8.91837   1.000 31.26743  ?  154 ASP   A O     1 
ATOM   1225 C  CB    . ASP   A 1 155 ? -20.20323 -1.15502  5.97632   1.000 36.77263  ?  154 ASP   A CB    1 
ATOM   1226 C  CG    . ASP   A 1 155 ? -19.66136 -2.56941  6.09736   1.000 44.72139  ?  154 ASP   A CG    1 
ATOM   1227 O  OD1   . ASP   A 1 155 ? -20.03918 -3.28144  7.05901   1.000 47.77950  ?  154 ASP   A OD1   1 
ATOM   1228 O  OD2   . ASP   A 1 155 ? -18.84409 -2.96824  5.23169   1.000 43.84673  -1 154 ASP   A OD2   1 
ATOM   1229 N  N     . ALA   A 1 156 ? -18.48758 0.95122   7.64284   1.000 30.72576  ?  155 ALA   A N     1 
ATOM   1230 C  CA    . ALA   A 1 156 ? -17.21254 1.35107   8.23198   1.000 28.98286  ?  155 ALA   A CA    1 
ATOM   1231 C  C     . ALA   A 1 156 ? -17.34884 1.61089   9.72920   1.000 26.84339  ?  155 ALA   A C     1 
ATOM   1232 O  O     . ALA   A 1 156 ? -16.59338 1.05784   10.53772  1.000 27.45248  ?  155 ALA   A O     1 
ATOM   1233 C  CB    . ALA   A 1 156 ? -16.67137 2.59708   7.51154   1.000 26.34993  ?  155 ALA   A CB    1 
ATOM   1234 N  N     . PHE   A 1 157 ? -18.29861 2.45928   10.12712  1.000 27.63546  ?  156 PHE   A N     1 
ATOM   1235 C  CA    . PHE   A 1 157 ? -18.44753 2.71154   11.55707  1.000 26.77983  ?  156 PHE   A CA    1 
ATOM   1236 C  C     . PHE   A 1 157 ? -18.87161 1.45368   12.30144  1.000 28.90513  ?  156 PHE   A C     1 
ATOM   1237 O  O     . PHE   A 1 157 ? -18.32033 1.15538   13.37177  1.000 29.40547  ?  156 PHE   A O     1 
ATOM   1238 C  CB    . PHE   A 1 157 ? -19.41730 3.85592   11.81543  1.000 25.93788  ?  156 PHE   A CB    1 
ATOM   1239 C  CG    . PHE   A 1 157 ? -18.87275 5.20021   11.42887  1.000 26.66023  ?  156 PHE   A CG    1 
ATOM   1240 C  CD1   . PHE   A 1 157 ? -18.12533 5.95066   12.32857  1.000 27.88613  ?  156 PHE   A CD1   1 
ATOM   1241 C  CD2   . PHE   A 1 157 ? -19.11790 5.72434   10.16183  1.000 23.28092  ?  156 PHE   A CD2   1 
ATOM   1242 C  CE1   . PHE   A 1 157 ? -17.61581 7.20268   11.97289  1.000 24.51133  ?  156 PHE   A CE1   1 
ATOM   1243 C  CE2   . PHE   A 1 157 ? -18.61725 6.96292   9.80440   1.000 20.39889  ?  156 PHE   A CE2   1 
ATOM   1244 C  CZ    . PHE   A 1 157 ? -17.85360 7.70253   10.71625  1.000 26.99476  ?  156 PHE   A CZ    1 
ATOM   1245 N  N     . TYR   A 1 158 ? -19.79682 0.66585   11.73936  1.000 26.34769  ?  157 TYR   A N     1 
ATOM   1246 C  CA    . TYR   A 1 158 ? -20.26852 -0.50323  12.48618  1.000 28.26017  ?  157 TYR   A CA    1 
ATOM   1247 C  C     . TYR   A 1 158 ? -19.16879 -1.55026  12.63529  1.000 27.72896  ?  157 TYR   A C     1 
ATOM   1248 O  O     . TYR   A 1 158 ? -19.04080 -2.17329  13.69372  1.000 29.04366  ?  157 TYR   A O     1 
ATOM   1249 C  CB    . TYR   A 1 158 ? -21.49120 -1.14727  11.82613  1.000 30.70600  ?  157 TYR   A CB    1 
ATOM   1250 C  CG    . TYR   A 1 158 ? -22.77488 -0.34381  11.80823  1.000 30.42821  ?  157 TYR   A CG    1 
ATOM   1251 C  CD1   . TYR   A 1 158 ? -22.82722 0.96620   12.26200  1.000 25.66777  ?  157 TYR   A CD1   1 
ATOM   1252 C  CD2   . TYR   A 1 158 ? -23.94210 -0.91716  11.32201  1.000 33.97418  ?  157 TYR   A CD2   1 
ATOM   1253 C  CE1   . TYR   A 1 158 ? -24.02209 1.68978   12.22213  1.000 41.28224  ?  157 TYR   A CE1   1 
ATOM   1254 C  CE2   . TYR   A 1 158 ? -25.13322 -0.21803  11.27253  1.000 37.17629  ?  157 TYR   A CE2   1 
ATOM   1255 C  CZ    . TYR   A 1 158 ? -25.17827 1.08551   11.71649  1.000 40.29432  ?  157 TYR   A CZ    1 
ATOM   1256 O  OH    . TYR   A 1 158 ? -26.37171 1.77211   11.65825  1.000 36.19596  ?  157 TYR   A OH    1 
ATOM   1257 N  N     . THR   A 1 159 ? -18.38549 -1.77361  11.57623  1.000 28.96875  ?  158 THR   A N     1 
ATOM   1258 C  CA    . THR   A 1 159 ? -17.27656 -2.72087  11.64116  1.000 28.56081  ?  158 THR   A CA    1 
ATOM   1259 C  C     . THR   A 1 159 ? -16.29688 -2.33976  12.75036  1.000 29.31410  ?  158 THR   A C     1 
ATOM   1260 O  O     . THR   A 1 159 ? -15.72756 -3.21418  13.41780  1.000 27.42113  ?  158 THR   A O     1 
ATOM   1261 C  CB    . THR   A 1 159 ? -16.56551 -2.79403  10.28688  1.000 29.15255  ?  158 THR   A CB    1 
ATOM   1262 O  OG1   . THR   A 1 159 ? -17.44510 -3.34713  9.29060   1.000 32.89612  ?  158 THR   A OG1   1 
ATOM   1263 C  CG2   . THR   A 1 159 ? -15.29658 -3.63518  10.35933  1.000 30.97891  ?  158 THR   A CG2   1 
ATOM   1264 N  N     . LEU   A 1 160 ? -16.10082 -1.03827  12.97117  1.000 26.79180  ?  159 LEU   A N     1 
ATOM   1265 C  CA    . LEU   A 1 160 ? -15.19782 -0.60982  14.03024  1.000 27.39433  ?  159 LEU   A CA    1 
ATOM   1266 C  C     . LEU   A 1 160 ? -15.76508 -0.94867  15.39689  1.000 28.66001  ?  159 LEU   A C     1 
ATOM   1267 O  O     . LEU   A 1 160 ? -15.02790 -1.35995  16.29488  1.000 28.04746  ?  159 LEU   A O     1 
ATOM   1268 C  CB    . LEU   A 1 160 ? -14.92974 0.88585   13.92258  1.000 22.76495  ?  159 LEU   A CB    1 
ATOM   1269 C  CG    . LEU   A 1 160 ? -13.95150 1.36629   14.99688  1.000 24.98751  ?  159 LEU   A CG    1 
ATOM   1270 C  CD1   . LEU   A 1 160 ? -12.58345 0.72352   14.81507  1.000 22.17665  ?  159 LEU   A CD1   1 
ATOM   1271 C  CD2   . LEU   A 1 160 ? -13.86537 2.90437   14.98977  1.000 21.86894  ?  159 LEU   A CD2   1 
ATOM   1272 N  N     . VAL   A 1 161 ? -17.07446 -0.79514  15.56579  1.000 28.10307  ?  160 VAL   A N     1 
ATOM   1273 C  CA    . VAL   A 1 161 ? -17.70417 -1.22132  16.80562  1.000 28.78370  ?  160 VAL   A CA    1 
ATOM   1274 C  C     . VAL   A 1 161 ? -17.49100 -2.71289  17.01835  1.000 30.10965  ?  160 VAL   A C     1 
ATOM   1275 O  O     . VAL   A 1 161 ? -17.15459 -3.14573  18.11780  1.000 30.49610  ?  160 VAL   A O     1 
ATOM   1276 C  CB    . VAL   A 1 161 ? -19.19261 -0.84888  16.80062  1.000 25.94019  ?  160 VAL   A CB    1 
ATOM   1277 C  CG1   . VAL   A 1 161 ? -19.89506 -1.47005  18.00707  1.000 31.10215  ?  160 VAL   A CG1   1 
ATOM   1278 C  CG2   . VAL   A 1 161 ? -19.34163 0.67086   16.79898  1.000 27.18853  ?  160 VAL   A CG2   1 
ATOM   1279 N  N     . ARG   A 1 162 ? -17.64235 -3.51705  15.96573  1.000 31.32118  ?  161 ARG   A N     1 
ATOM   1280 C  CA    . ARG   A 1 162 ? -17.40467 -4.95387  16.11390  1.000 37.16472  ?  161 ARG   A CA    1 
ATOM   1281 C  C     . ARG   A 1 162 ? -15.96760 -5.24311  16.51569  1.000 36.21970  ?  161 ARG   A C     1 
ATOM   1282 O  O     . ARG   A 1 162 ? -15.72181 -6.15161  17.31685  1.000 40.71955  ?  161 ARG   A O     1 
ATOM   1283 C  CB    . ARG   A 1 162 ? -17.75536 -5.70337  14.82584  1.000 29.81969  ?  161 ARG   A CB    1 
ATOM   1284 C  CG    . ARG   A 1 162 ? -19.22302 -5.54966  14.40653  1.000 37.92884  ?  161 ARG   A CG    1 
ATOM   1285 C  CD    . ARG   A 1 162 ? -19.58936 -6.41244  13.18365  1.000 40.36043  ?  161 ARG   A CD    1 
ATOM   1286 N  NE    . ARG   A 1 162 ? -20.96239 -6.17117  12.74147  1.000 42.45758  ?  161 ARG   A NE    1 
ATOM   1287 C  CZ    . ARG   A 1 162 ? -21.30880 -5.47830  11.66003  1.000 38.70929  ?  161 ARG   A CZ    1 
ATOM   1288 N  NH1   . ARG   A 1 162 ? -20.40116 -4.99982  10.81584  1.000 34.22232  ?  161 ARG   A NH1   1 
ATOM   1289 N  NH2   . ARG   A 1 162 ? -22.60082 -5.25836  11.41792  1.000 37.24405  ?  161 ARG   A NH2   1 
ATOM   1290 N  N     . GLU   A 1 163 ? -15.00581 -4.48558  15.97910  1.000 35.04467  ?  162 GLU   A N     1 
ATOM   1291 C  CA    . GLU   A 1 163 ? -13.61856 -4.67198  16.39017  1.000 33.34630  ?  162 GLU   A CA    1 
ATOM   1292 C  C     . GLU   A 1 163 ? -13.43148 -4.33441  17.86323  1.000 38.13471  ?  162 GLU   A C     1 
ATOM   1293 O  O     . GLU   A 1 163 ? -12.69282 -5.02514  18.57316  1.000 38.96243  ?  162 GLU   A O     1 
ATOM   1294 C  CB    . GLU   A 1 163 ? -12.69504 -3.82862  15.52007  1.000 34.71291  ?  162 GLU   A CB    1 
ATOM   1295 C  CG    . GLU   A 1 163 ? -12.69876 -4.27231  14.05182  1.000 35.14976  ?  162 GLU   A CG    1 
ATOM   1296 C  CD    . GLU   A 1 163 ? -12.07900 -5.66104  13.85817  1.000 38.95145  ?  162 GLU   A CD    1 
ATOM   1297 O  OE1   . GLU   A 1 163 ? -10.84470 -5.79349  13.99849  1.000 35.86335  ?  162 GLU   A OE1   1 
ATOM   1298 O  OE2   . GLU   A 1 163 ? -12.83019 -6.60883  13.55569  1.000 37.65525  -1 162 GLU   A OE2   1 
ATOM   1299 N  N     . ILE   A 1 164 ? -14.09267 -3.28129  18.34574  1.000 34.78520  ?  163 ILE   A N     1 
ATOM   1300 C  CA    . ILE   A 1 164 ? -13.94553 -2.92112  19.74417  1.000 32.15370  ?  163 ILE   A CA    1 
ATOM   1301 C  C     . ILE   A 1 164 ? -14.58410 -3.98159  20.63461  1.000 43.25181  ?  163 ILE   A C     1 
ATOM   1302 O  O     . ILE   A 1 164 ? -14.03516 -4.33909  21.68595  1.000 37.74178  ?  163 ILE   A O     1 
ATOM   1303 C  CB    . ILE   A 1 164 ? -14.54083 -1.53211  20.01567  1.000 32.62895  ?  163 ILE   A CB    1 
ATOM   1304 C  CG1   . ILE   A 1 164 ? -13.70561 -0.43000  19.35124  1.000 26.05964  ?  163 ILE   A CG1   1 
ATOM   1305 C  CG2   . ILE   A 1 164 ? -14.63559 -1.29041  21.51102  1.000 29.19097  ?  163 ILE   A CG2   1 
ATOM   1306 C  CD1   . ILE   A 1 164 ? -14.45345 0.87656   19.26490  1.000 25.72948  ?  163 ILE   A CD1   1 
ATOM   1307 N  N     . ARG   A 1 165 ? -15.74777 -4.49969  20.23142  1.000 34.38495  ?  164 ARG   A N     1 
ATOM   1308 C  CA    . ARG   A 1 165 ? -16.38845 -5.55646  21.00664  1.000 42.48465  ?  164 ARG   A CA    1 
ATOM   1309 C  C     . ARG   A 1 165 ? -15.47236 -6.76189  21.14075  1.000 47.41079  ?  164 ARG   A C     1 
ATOM   1310 O  O     . ARG   A 1 165 ? -15.30616 -7.30647  22.23914  1.000 52.79183  ?  164 ARG   A O     1 
ATOM   1311 C  CB    . ARG   A 1 165 ? -17.71350 -5.96597  20.35940  1.000 30.62640  ?  164 ARG   A CB    1 
ATOM   1312 C  CG    . ARG   A 1 165 ? -18.80702 -4.92770  20.50303  1.000 42.46268  ?  164 ARG   A CG    1 
ATOM   1313 C  CD    . ARG   A 1 165 ? -20.03485 -5.31372  19.69086  1.000 39.26635  ?  164 ARG   A CD    1 
ATOM   1314 N  NE    . ARG   A 1 165 ? -21.17282 -4.43150  19.92154  1.000 39.35812  ?  164 ARG   A NE    1 
ATOM   1315 C  CZ    . ARG   A 1 165 ? -22.34285 -4.55933  19.30884  1.000 41.43374  ?  164 ARG   A CZ    1 
ATOM   1316 N  NH1   . ARG   A 1 165 ? -22.54638 -5.50492  18.40922  1.000 46.44492  ?  164 ARG   A NH1   1 
ATOM   1317 N  NH2   . ARG   A 1 165 ? -23.33164 -3.71898  19.60567  1.000 40.70686  ?  164 ARG   A NH2   1 
ATOM   1318 N  N     . LYS   A 1 166 ? -14.86176 -7.18320  20.03141  1.000 45.36828  ?  165 LYS   A N     1 
ATOM   1319 C  CA    . LYS   A 1 166 ? -13.93132 -8.30852  20.06415  1.000 44.34662  ?  165 LYS   A CA    1 
ATOM   1320 C  C     . LYS   A 1 166 ? -12.77288 -8.04494  21.02003  1.000 53.89515  ?  165 LYS   A C     1 
ATOM   1321 O  O     . LYS   A 1 166 ? -12.38014 -8.92966  21.78918  1.000 60.57735  ?  165 LYS   A O     1 
ATOM   1322 C  CB    . LYS   A 1 166 ? -13.42891 -8.59788  18.64750  1.000 42.60505  ?  165 LYS   A CB    1 
ATOM   1323 C  CG    . LYS   A 1 166 ? -14.47445 -9.28227  17.77546  1.000 48.04629  ?  165 LYS   A CG    1 
ATOM   1324 C  CD    . LYS   A 1 166 ? -14.33210 -8.95217  16.28520  1.000 47.71233  ?  165 LYS   A CD    1 
ATOM   1325 C  CE    . LYS   A 1 166 ? -13.14889 -9.63793  15.63575  1.000 44.69714  ?  165 LYS   A CE    1 
ATOM   1326 N  NZ    . LYS   A 1 166 ? -13.27251 -9.55106  14.13824  1.000 38.76251  ?  165 LYS   A NZ    1 
ATOM   1327 N  N     . HIS   A 1 167 ? -12.23182 -6.82633  21.00386  1.000 47.43998  ?  166 HIS   A N     1 
ATOM   1328 C  CA    . HIS   A 1 167 ? -11.13189 -6.47897  21.89580  1.000 43.28735  ?  166 HIS   A CA    1 
ATOM   1329 C  C     . HIS   A 1 167 ? -11.54050 -6.61292  23.36296  1.000 52.96794  ?  166 HIS   A C     1 
ATOM   1330 O  O     . HIS   A 1 167 ? -10.79435 -7.17760  24.17097  1.000 58.27925  ?  166 HIS   A O     1 
ATOM   1331 C  CB    . HIS   A 1 167 ? -10.65856 -5.06086  21.57738  1.000 36.78947  ?  166 HIS   A CB    1 
ATOM   1332 C  CG    . HIS   A 1 167 ? -9.45546  -4.61989  22.35225  1.000 46.87949  ?  166 HIS   A CG    1 
ATOM   1333 N  ND1   . HIS   A 1 167 ? -9.54572  -3.85138  23.49378  1.000 45.32589  ?  166 HIS   A ND1   1 
ATOM   1334 C  CD2   . HIS   A 1 167 ? -8.13280  -4.81047  22.13076  1.000 45.38098  ?  166 HIS   A CD2   1 
ATOM   1335 C  CE1   . HIS   A 1 167 ? -8.33122  -3.60559  23.95159  1.000 46.68321  ?  166 HIS   A CE1   1 
ATOM   1336 N  NE2   . HIS   A 1 167 ? -7.45626  -4.17273  23.14118  1.000 44.55647  ?  166 HIS   A NE2   1 
ATOM   1337 N  N     . LYS   A 1 168 ? -12.72463 -6.11182  23.72506  1.000 47.98677  ?  167 LYS   A N     1 
ATOM   1338 C  CA    . LYS   A 1 168 ? -13.20844 -6.20292  25.09925  1.000 58.16267  ?  167 LYS   A CA    1 
ATOM   1339 C  C     . LYS   A 1 168 ? -13.83920 -7.55457  25.42266  1.000 65.43236  ?  167 LYS   A C     1 
ATOM   1340 O  O     . LYS   A 1 168 ? -14.04670 -7.85706  26.60529  1.000 65.39300  ?  167 LYS   A O     1 
ATOM   1341 C  CB    . LYS   A 1 168 ? -14.23345 -5.09782  25.37066  1.000 56.35746  ?  167 LYS   A CB    1 
ATOM   1342 C  CG    . LYS   A 1 168 ? -13.73111 -3.68335  25.11623  1.000 55.60289  ?  167 LYS   A CG    1 
ATOM   1343 C  CD    . LYS   A 1 168 ? -14.90112 -2.73737  24.82951  1.000 52.24501  ?  167 LYS   A CD    1 
ATOM   1344 C  CE    . LYS   A 1 168 ? -16.00741 -2.88475  25.87704  1.000 56.07770  ?  167 LYS   A CE    1 
ATOM   1345 N  NZ    . LYS   A 1 168 ? -17.26712 -2.16108  25.51683  1.000 43.93425  ?  167 LYS   A NZ    1 
ATOM   1346 N  N     . GLU   A 1 169 ? -14.13883 -8.36154  24.40307  1.000 67.88227  ?  168 GLU   A N     1 
ATOM   1347 C  CA    . GLU   A 1 169 ? -14.86362 -9.63488  24.52896  1.000 69.43422  ?  168 GLU   A CA    1 
ATOM   1348 C  C     . GLU   A 1 169 ? -16.23936 -9.45334  25.16161  1.000 72.98388  ?  168 GLU   A C     1 
ATOM   1349 O  O     . GLU   A 1 169 ? -17.26112 -9.58499  24.48321  1.000 69.68552  ?  168 GLU   A O     1 
ATOM   1350 C  CB    . GLU   A 1 169 ? -14.05189 -10.65788 25.32655  1.000 72.77012  ?  168 GLU   A CB    1 
ATOM   1351 C  CG    . GLU   A 1 169 ? -12.89477 -11.26106 24.55535  1.000 72.78508  ?  168 GLU   A CG    1 
ATOM   1352 C  CD    . GLU   A 1 169 ? -11.59171 -10.52483 24.79086  1.000 76.21525  ?  168 GLU   A CD    1 
ATOM   1353 O  OE1   . GLU   A 1 169 ? -11.50745 -9.77910  25.78871  1.000 75.75467  ?  168 GLU   A OE1   1 
ATOM   1354 O  OE2   . GLU   A 1 169 ? -10.65137 -10.69502 23.98252  1.000 77.06728  -1 168 GLU   A OE2   1 
ATOM   1355 N  N     . SER   B 1 1   ? 3.41813   29.11407  23.68713  1.000 39.93620  ?  0   SER   B N     1 
ATOM   1356 C  CA    . SER   B 1 1   ? 2.13010   29.73060  23.96213  1.000 36.96924  ?  0   SER   B CA    1 
ATOM   1357 C  C     . SER   B 1 1   ? 1.81297   29.73769  25.44706  1.000 41.40227  ?  0   SER   B C     1 
ATOM   1358 O  O     . SER   B 1 1   ? 2.42057   28.99337  26.22274  1.000 37.98239  ?  0   SER   B O     1 
ATOM   1359 C  CB    . SER   B 1 1   ? 1.02073   29.00242  23.20111  1.000 39.47190  ?  0   SER   B CB    1 
ATOM   1360 O  OG    . SER   B 1 1   ? 1.23625   29.10646  21.80730  1.000 48.08366  ?  0   SER   B OG    1 
ATOM   1361 N  N     . MET   B 1 2   ? 0.84566   30.57692  25.82037  1.000 31.70594  ?  1   MET   B N     1 
ATOM   1362 C  CA    . MET   B 1 2   ? 0.47440   30.73875  27.21513  1.000 41.13480  ?  1   MET   B CA    1 
ATOM   1363 C  C     . MET   B 1 2   ? 0.02728   29.39801  27.79416  1.000 33.89985  ?  1   MET   B C     1 
ATOM   1364 O  O     . MET   B 1 2   ? -0.48305  28.52808  27.08179  1.000 33.28304  ?  1   MET   B O     1 
ATOM   1365 C  CB    . MET   B 1 2   ? -0.62694  31.79911  27.34787  1.000 34.67580  ?  1   MET   B CB    1 
ATOM   1366 C  CG    . MET   B 1 2   ? -2.01405  31.35457  26.88637  1.000 31.13408  ?  1   MET   B CG    1 
ATOM   1367 S  SD    . MET   B 1 2   ? -3.29368  32.62843  27.07171  1.000 32.34804  ?  1   MET   B SD    1 
ATOM   1368 C  CE    . MET   B 1 2   ? -3.03392  33.62056  25.59687  1.000 29.63778  ?  1   MET   B CE    1 
ATOM   1369 N  N     . THR   B 1 3   ? 0.28396   29.21731  29.08896  1.000 31.43483  ?  2   THR   B N     1 
ATOM   1370 C  CA    . THR   B 1 3   ? -0.06498  27.97703  29.77697  1.000 29.30436  ?  2   THR   B CA    1 
ATOM   1371 C  C     . THR   B 1 3   ? -1.57884  27.86205  29.90854  1.000 31.12690  ?  2   THR   B C     1 
ATOM   1372 O  O     . THR   B 1 3   ? -2.26704  28.85019  30.17162  1.000 28.64810  ?  2   THR   B O     1 
ATOM   1373 C  CB    . THR   B 1 3   ? 0.57636   27.93320  31.17477  1.000 32.02030  ?  2   THR   B CB    1 
ATOM   1374 O  OG1   . THR   B 1 3   ? 1.97141   28.24378  31.07472  1.000 35.61732  ?  2   THR   B OG1   1 
ATOM   1375 C  CG2   . THR   B 1 3   ? 0.40485   26.56047  31.80936  1.000 30.84139  ?  2   THR   B CG2   1 
ATOM   1376 N  N     . GLU   B 1 4   ? -2.09748  26.65511  29.70272  1.000 29.05361  ?  3   GLU   B N     1 
ATOM   1377 C  CA    . GLU   B 1 4   ? -3.51790  26.39004  29.85746  1.000 32.58817  ?  3   GLU   B CA    1 
ATOM   1378 C  C     . GLU   B 1 4   ? -3.73392  25.67294  31.17973  1.000 29.85133  ?  3   GLU   B C     1 
ATOM   1379 O  O     . GLU   B 1 4   ? -2.95242  24.79512  31.54691  1.000 32.68611  ?  3   GLU   B O     1 
ATOM   1380 C  CB    . GLU   B 1 4   ? -4.05903  25.54211  28.70534  1.000 33.57550  ?  3   GLU   B CB    1 
ATOM   1381 C  CG    . GLU   B 1 4   ? -3.63715  26.05152  27.34179  1.000 39.47403  ?  3   GLU   B CG    1 
ATOM   1382 C  CD    . GLU   B 1 4   ? -4.34666  25.35530  26.19752  1.000 44.28473  ?  3   GLU   B CD    1 
ATOM   1383 O  OE1   . GLU   B 1 4   ? -4.99690  24.30673  26.42817  1.000 44.74940  ?  3   GLU   B OE1   1 
ATOM   1384 O  OE2   . GLU   B 1 4   ? -4.25332  25.87492  25.06730  1.000 46.06746  -1 3   GLU   B OE2   1 
ATOM   1385 N  N     . TYR   B 1 5   ? -4.79546  26.05122  31.88708  1.000 30.67758  ?  4   TYR   B N     1 
ATOM   1386 C  CA    . TYR   B 1 5   ? -5.16525  25.42525  33.15123  1.000 29.78952  ?  4   TYR   B CA    1 
ATOM   1387 C  C     . TYR   B 1 5   ? -6.56461  24.84522  33.02249  1.000 27.02618  ?  4   TYR   B C     1 
ATOM   1388 O  O     . TYR   B 1 5   ? -7.51593  25.58154  32.74721  1.000 31.39569  ?  4   TYR   B O     1 
ATOM   1389 C  CB    . TYR   B 1 5   ? -5.10829  26.43289  34.31261  1.000 31.19709  ?  4   TYR   B CB    1 
ATOM   1390 C  CG    . TYR   B 1 5   ? -3.73586  27.03582  34.54272  1.000 28.17526  ?  4   TYR   B CG    1 
ATOM   1391 C  CD1   . TYR   B 1 5   ? -2.74498  26.32901  35.22796  1.000 40.15281  ?  4   TYR   B CD1   1 
ATOM   1392 C  CD2   . TYR   B 1 5   ? -3.43645  28.30350  34.09374  1.000 33.64988  ?  4   TYR   B CD2   1 
ATOM   1393 C  CE1   . TYR   B 1 5   ? -1.48397  26.87272  35.43304  1.000 39.58570  ?  4   TYR   B CE1   1 
ATOM   1394 C  CE2   . TYR   B 1 5   ? -2.18359  28.85985  34.29361  1.000 33.94835  ?  4   TYR   B CE2   1 
ATOM   1395 C  CZ    . TYR   B 1 5   ? -1.21596  28.14791  34.96115  1.000 40.51847  ?  4   TYR   B CZ    1 
ATOM   1396 O  OH    . TYR   B 1 5   ? 0.01728   28.73041  35.14324  1.000 42.42495  ?  4   TYR   B OH    1 
ATOM   1397 N  N     . LYS   B 1 6   ? -6.68657  23.53642  33.24263  1.000 30.25223  ?  5   LYS   B N     1 
ATOM   1398 C  CA    . LYS   B 1 6   ? -7.97271  22.83370  33.28117  1.000 31.17163  ?  5   LYS   B CA    1 
ATOM   1399 C  C     . LYS   B 1 6   ? -8.57644  22.92094  34.68521  1.000 31.45344  ?  5   LYS   B C     1 
ATOM   1400 O  O     . LYS   B 1 6   ? -8.14567  22.22133  35.60150  1.000 27.50360  ?  5   LYS   B O     1 
ATOM   1401 C  CB    . LYS   B 1 6   ? -7.78266  21.38555  32.85566  1.000 31.17515  ?  5   LYS   B CB    1 
ATOM   1402 C  CG    . LYS   B 1 6   ? -7.10427  21.24478  31.50056  1.000 35.01435  ?  5   LYS   B CG    1 
ATOM   1403 C  CD    . LYS   B 1 6   ? -6.82072  19.78336  31.17661  1.000 37.13812  ?  5   LYS   B CD    1 
ATOM   1404 C  CE    . LYS   B 1 6   ? -5.97529  19.65158  29.92397  1.000 40.71744  ?  5   LYS   B CE    1 
ATOM   1405 N  NZ    . LYS   B 1 6   ? -6.37763  20.66569  28.92563  1.000 49.73738  ?  5   LYS   B NZ    1 
ATOM   1406 N  N     . LEU   B 1 7   ? -9.58819  23.77920  34.84124  1.000 28.56182  ?  6   LEU   B N     1 
ATOM   1407 C  CA    . LEU   B 1 7   ? -10.31590 23.97547  36.08254  1.000 25.48555  ?  6   LEU   B CA    1 
ATOM   1408 C  C     . LEU   B 1 7   ? -11.66709 23.26675  36.01041  1.000 31.24671  ?  6   LEU   B C     1 
ATOM   1409 O  O     . LEU   B 1 7   ? -12.33308 23.27263  34.96441  1.000 27.94124  ?  6   LEU   B O     1 
ATOM   1410 C  CB    . LEU   B 1 7   ? -10.51453 25.47676  36.35728  1.000 32.21272  ?  6   LEU   B CB    1 
ATOM   1411 C  CG    . LEU   B 1 7   ? -9.25825  26.37551  36.23386  1.000 24.33028  ?  6   LEU   B CG    1 
ATOM   1412 C  CD1   . LEU   B 1 7   ? -9.50987  27.78185  36.72557  1.000 28.22781  ?  6   LEU   B CD1   1 
ATOM   1413 C  CD2   . LEU   B 1 7   ? -8.11904  25.76340  36.98344  1.000 28.08244  ?  6   LEU   B CD2   1 
ATOM   1414 N  N     . VAL   B 1 8   ? -12.05187 22.62929  37.11302  1.000 27.40081  ?  7   VAL   B N     1 
ATOM   1415 C  CA    . VAL   B 1 8   ? -13.31716 21.90108  37.21986  1.000 25.72019  ?  7   VAL   B CA    1 
ATOM   1416 C  C     . VAL   B 1 8   ? -14.09035 22.45768  38.40851  1.000 28.21904  ?  7   VAL   B C     1 
ATOM   1417 O  O     . VAL   B 1 8   ? -13.59247 22.43975  39.53886  1.000 27.94180  ?  7   VAL   B O     1 
ATOM   1418 C  CB    . VAL   B 1 8   ? -13.10641 20.38702  37.38748  1.000 28.61285  ?  7   VAL   B CB    1 
ATOM   1419 C  CG1   . VAL   B 1 8   ? -14.45281 19.66581  37.41497  1.000 25.55961  ?  7   VAL   B CG1   1 
ATOM   1420 C  CG2   . VAL   B 1 8   ? -12.21047 19.82470  36.31229  1.000 29.07447  ?  7   VAL   B CG2   1 
ATOM   1421 N  N     . VAL   B 1 9   ? -15.30887 22.92144  38.16233  1.000 24.01104  ?  8   VAL   B N     1 
ATOM   1422 C  CA    . VAL   B 1 9   ? -16.17332 23.45687  39.20109  1.000 29.30853  ?  8   VAL   B CA    1 
ATOM   1423 C  C     . VAL   B 1 9   ? -17.14468 22.35716  39.62708  1.000 29.14581  ?  8   VAL   B C     1 
ATOM   1424 O  O     . VAL   B 1 9   ? -17.94080 21.86440  38.81503  1.000 25.92092  ?  8   VAL   B O     1 
ATOM   1425 C  CB    . VAL   B 1 9   ? -16.91611 24.70960  38.72456  1.000 29.97951  ?  8   VAL   B CB    1 
ATOM   1426 C  CG1   . VAL   B 1 9   ? -17.68789 25.30205  39.88265  1.000 29.64414  ?  8   VAL   B CG1   1 
ATOM   1427 C  CG2   . VAL   B 1 9   ? -15.91760 25.74845  38.13319  1.000 23.59670  ?  8   VAL   B CG2   1 
ATOM   1428 N  N     . VAL   B 1 10  ? -17.07155 21.96072  40.90508  1.000 28.72319  ?  9   VAL   B N     1 
ATOM   1429 C  CA    . VAL   B 1 10  ? -17.87650 20.85812  41.42414  1.000 35.17030  ?  9   VAL   B CA    1 
ATOM   1430 C  C     . VAL   B 1 10  ? -18.60566 21.27224  42.70052  1.000 39.50844  ?  9   VAL   B C     1 
ATOM   1431 O  O     . VAL   B 1 10  ? -18.24835 22.24236  43.38047  1.000 31.67826  ?  9   VAL   B O     1 
ATOM   1432 C  CB    . VAL   B 1 10  ? -17.03508 19.59827  41.70601  1.000 32.56458  ?  9   VAL   B CB    1 
ATOM   1433 C  CG1   . VAL   B 1 10  ? -16.37215 19.12019  40.44754  1.000 26.92809  ?  9   VAL   B CG1   1 
ATOM   1434 C  CG2   . VAL   B 1 10  ? -15.98976 19.89439  42.78759  1.000 35.51498  ?  9   VAL   B CG2   1 
ATOM   1435 N  N     . GLY   B 1 11  ? -19.65669 20.51425  43.00649  1.000 36.56886  ?  10  GLY   B N     1 
ATOM   1436 C  CA    . GLY   B 1 11  ? -20.42622 20.74321  44.20830  1.000 34.14712  ?  10  GLY   B CA    1 
ATOM   1437 C  C     . GLY   B 1 11  ? -21.87996 20.38778  44.00307  1.000 41.47009  ?  10  GLY   B C     1 
ATOM   1438 O  O     . GLY   B 1 11  ? -22.30377 20.08610  42.87868  1.000 32.57209  ?  10  GLY   B O     1 
ATOM   1439 N  N     . ALA   B 1 12  ? -22.64768 20.43989  45.08979  1.000 36.99611  ?  11  ALA   B N     1 
ATOM   1440 C  CA    . ALA   B 1 12  ? -24.01129 19.95296  45.10040  1.000 35.05768  ?  11  ALA   B CA    1 
ATOM   1441 C  C     . ALA   B 1 12  ? -24.91215 20.82435  44.23942  1.000 40.36524  ?  11  ALA   B C     1 
ATOM   1442 O  O     . ALA   B 1 12  ? -24.60326 21.97415  43.90982  1.000 40.86206  ?  11  ALA   B O     1 
ATOM   1443 C  CB    . ALA   B 1 12  ? -24.54282 19.89144  46.53853  1.000 43.46018  ?  11  ALA   B CB    1 
ATOM   1444 N  N     . ARG   B 1 13  ? -26.03161 20.23233  43.85049  1.000 37.50798  ?  12  ARG   B N     1 
ATOM   1445 C  CA    . ARG   B 1 13  ? -27.03993 20.89619  43.03849  1.000 40.16532  ?  12  ARG   B CA    1 
ATOM   1446 C  C     . ARG   B 1 13  ? -27.41387 22.26149  43.61467  1.000 48.47127  ?  12  ARG   B C     1 
ATOM   1447 O  O     . ARG   B 1 13  ? -27.57733 22.40976  44.83003  1.000 38.32387  ?  12  ARG   B O     1 
ATOM   1448 C  CB    . ARG   B 1 13  ? -28.26427 19.98415  42.98796  1.000 45.89218  ?  12  ARG   B CB    1 
ATOM   1449 C  CG    . ARG   B 1 13  ? -29.20773 20.20624  41.85341  1.000 48.82088  ?  12  ARG   B CG    1 
ATOM   1450 C  CD    . ARG   B 1 13  ? -30.37193 19.25066  41.97399  1.000 50.84724  ?  12  ARG   B CD    1 
ATOM   1451 N  NE    . ARG   B 1 13  ? -31.60785 19.88002  41.52924  1.000 58.32374  ?  12  ARG   B NE    1 
ATOM   1452 C  CZ    . ARG   B 1 13  ? -32.42820 20.56523  42.31503  1.000 58.19655  ?  12  ARG   B CZ    1 
ATOM   1453 N  NH1   . ARG   B 1 13  ? -32.16944 20.73931  43.60500  1.000 59.82091  ?  12  ARG   B NH1   1 
ATOM   1454 N  NH2   . ARG   B 1 13  ? -33.53949 21.08276  41.79657  1.000 52.11236  ?  12  ARG   B NH2   1 
ATOM   1455 N  N     . GLY   B 1 14  ? -27.53124 23.26536  42.73628  1.000 43.61427  ?  13  GLY   B N     1 
ATOM   1456 C  CA    . GLY   B 1 14  ? -28.12476 24.54668  43.09911  1.000 41.26695  ?  13  GLY   B CA    1 
ATOM   1457 C  C     . GLY   B 1 14  ? -27.25770 25.51210  43.88551  1.000 45.89579  ?  13  GLY   B C     1 
ATOM   1458 O  O     . GLY   B 1 14  ? -27.70568 26.63932  44.15604  1.000 40.65697  ?  13  GLY   B O     1 
ATOM   1459 N  N     . VAL   B 1 15  ? -26.03313 25.11503  44.25179  1.000 38.74760  ?  14  VAL   B N     1 
ATOM   1460 C  CA    . VAL   B 1 15  ? -25.13966 25.94274  45.05871  1.000 38.87920  ?  14  VAL   B CA    1 
ATOM   1461 C  C     . VAL   B 1 15  ? -24.58919 27.17121  44.34527  1.000 43.88247  ?  14  VAL   B C     1 
ATOM   1462 O  O     . VAL   B 1 15  ? -23.99778 28.03325  45.00499  1.000 38.20419  ?  14  VAL   B O     1 
ATOM   1463 C  CB    . VAL   B 1 15  ? -23.91237 25.14375  45.53259  1.000 43.63371  ?  14  VAL   B CB    1 
ATOM   1464 C  CG1   . VAL   B 1 15  ? -24.32653 23.90208  46.32152  1.000 41.70879  ?  14  VAL   B CG1   1 
ATOM   1465 C  CG2   . VAL   B 1 15  ? -23.05333 24.78706  44.34247  1.000 35.59855  ?  14  VAL   B CG2   1 
ATOM   1466 N  N     . GLY   B 1 16  ? -24.71450 27.25844  43.02606  1.000 43.55804  ?  15  GLY   B N     1 
ATOM   1467 C  CA    . GLY   B 1 16  ? -24.26256 28.40597  42.27149  1.000 41.71771  ?  15  GLY   B CA    1 
ATOM   1468 C  C     . GLY   B 1 16  ? -23.02008 28.20617  41.38142  1.000 42.30024  ?  15  GLY   B C     1 
ATOM   1469 O  O     . GLY   B 1 16  ? -22.43978 29.20391  40.94679  1.000 36.81468  ?  15  GLY   B O     1 
ATOM   1470 N  N     . LYS   B 1 17  ? -22.61892 26.95810  41.10758  1.000 38.53150  ?  16  LYS   B N     1 
ATOM   1471 C  CA    . LYS   B 1 17  ? -21.49431 26.66527  40.21330  1.000 33.12952  ?  16  LYS   B CA    1 
ATOM   1472 C  C     . LYS   B 1 17  ? -21.59907 27.38826  38.86660  1.000 32.46946  ?  16  LYS   B C     1 
ATOM   1473 O  O     . LYS   B 1 17  ? -20.61724 27.96245  38.37789  1.000 29.85906  ?  16  LYS   B O     1 
ATOM   1474 C  CB    . LYS   B 1 17  ? -21.41460 25.15237  39.97695  1.000 29.97567  ?  16  LYS   B CB    1 
ATOM   1475 C  CG    . LYS   B 1 17  ? -21.04688 24.31956  41.17921  1.000 29.87603  ?  16  LYS   B CG    1 
ATOM   1476 C  CD    . LYS   B 1 17  ? -20.82307 22.85710  40.79538  1.000 30.33284  ?  16  LYS   B CD    1 
ATOM   1477 C  CE    . LYS   B 1 17  ? -22.08404 22.20604  40.24813  1.000 30.21911  ?  16  LYS   B CE    1 
ATOM   1478 N  NZ    . LYS   B 1 17  ? -23.24669 22.26094  41.18303  1.000 37.77926  ?  16  LYS   B NZ    1 
ATOM   1479 N  N     . SER   B 1 18  ? -22.77596 27.33401  38.23229  1.000 33.77503  ?  17  SER   B N     1 
ATOM   1480 C  CA    . SER   B 1 18  ? -22.95420 27.95301  36.92357  1.000 36.17891  ?  17  SER   B CA    1 
ATOM   1481 C  C     . SER   B 1 18  ? -22.98882 29.46926  37.02037  1.000 33.88158  ?  17  SER   B C     1 
ATOM   1482 O  O     . SER   B 1 18  ? -22.47505 30.16909  36.14253  1.000 37.59915  ?  17  SER   B O     1 
ATOM   1483 C  CB    . SER   B 1 18  ? -24.24118 27.44863  36.27195  1.000 38.78505  ?  17  SER   B CB    1 
ATOM   1484 O  OG    . SER   B 1 18  ? -24.08046 26.14110  35.74611  1.000 37.60917  ?  17  SER   B OG    1 
ATOM   1485 N  N     . ALA   B 1 19  ? -23.61247 29.99490  38.06917  1.000 45.19040  ?  18  ALA   B N     1 
ATOM   1486 C  CA    . ALA   B 1 19  ? -23.71103 31.44107  38.20812  1.000 44.59294  ?  18  ALA   B CA    1 
ATOM   1487 C  C     . ALA   B 1 19  ? -22.33768 32.05927  38.42937  1.000 33.19082  ?  18  ALA   B C     1 
ATOM   1488 O  O     . ALA   B 1 19  ? -22.04893 33.13562  37.89595  1.000 37.50819  ?  18  ALA   B O     1 
ATOM   1489 C  CB    . ALA   B 1 19  ? -24.67174 31.79571  39.34425  1.000 41.75252  ?  18  ALA   B CB    1 
ATOM   1490 N  N     . LEU   B 1 20  ? -21.47516 31.38422  39.19646  1.000 29.73062  ?  19  LEU   B N     1 
ATOM   1491 C  CA    . LEU   B 1 20  ? -20.10057 31.84620  39.36062  1.000 29.49262  ?  19  LEU   B CA    1 
ATOM   1492 C  C     . LEU   B 1 20  ? -19.35116 31.82320  38.02944  1.000 34.16893  ?  19  LEU   B C     1 
ATOM   1493 O  O     . LEU   B 1 20  ? -18.76595 32.82943  37.61006  1.000 32.84242  ?  19  LEU   B O     1 
ATOM   1494 C  CB    . LEU   B 1 20  ? -19.37206 30.97491  40.38313  1.000 27.24622  ?  19  LEU   B CB    1 
ATOM   1495 C  CG    . LEU   B 1 20  ? -19.81988 31.08756  41.85041  1.000 38.99626  ?  19  LEU   B CG    1 
ATOM   1496 C  CD1   . LEU   B 1 20  ? -19.23940 29.97145  42.70247  1.000 33.66914  ?  19  LEU   B CD1   1 
ATOM   1497 C  CD2   . LEU   B 1 20  ? -19.43602 32.45030  42.41992  1.000 32.35736  ?  19  LEU   B CD2   1 
ATOM   1498 N  N     . THR   B 1 21  ? -19.33869 30.65887  37.37374  1.000 33.65666  ?  20  THR   B N     1 
ATOM   1499 C  CA    . THR   B 1 21  ? -18.67785 30.50074  36.07975  1.000 30.28723  ?  20  THR   B CA    1 
ATOM   1500 C  C     . THR   B 1 21  ? -19.18412 31.52202  35.07318  1.000 34.56256  ?  20  THR   B C     1 
ATOM   1501 O  O     . THR   B 1 21  ? -18.39332 32.10226  34.31260  1.000 34.66262  ?  20  THR   B O     1 
ATOM   1502 C  CB    . THR   B 1 21  ? -18.89827 29.07810  35.55309  1.000 27.11213  ?  20  THR   B CB    1 
ATOM   1503 O  OG1   . THR   B 1 21  ? -18.25016 28.12563  36.41130  1.000 26.71453  ?  20  THR   B OG1   1 
ATOM   1504 C  CG2   . THR   B 1 21  ? -18.32084 28.92125  34.13637  1.000 25.13367  ?  20  THR   B CG2   1 
ATOM   1505 N  N     . ILE   B 1 22  ? -20.50129 31.76819  35.05957  1.000 30.55685  ?  21  ILE   B N     1 
ATOM   1506 C  CA    . ILE   B 1 22  ? -21.05162 32.72033  34.10574  1.000 33.21646  ?  21  ILE   B CA    1 
ATOM   1507 C  C     . ILE   B 1 22  ? -20.68889 34.15439  34.49592  1.000 39.91083  ?  21  ILE   B C     1 
ATOM   1508 O  O     . ILE   B 1 22  ? -20.45656 34.99935  33.61823  1.000 39.45618  ?  21  ILE   B O     1 
ATOM   1509 C  CB    . ILE   B 1 22  ? -22.56721 32.49090  33.95053  1.000 42.12412  ?  21  ILE   B CB    1 
ATOM   1510 C  CG1   . ILE   B 1 22  ? -22.80335 31.33720  32.95937  1.000 37.42211  ?  21  ILE   B CG1   1 
ATOM   1511 C  CG2   . ILE   B 1 22  ? -23.29620 33.75541  33.47811  1.000 40.76680  ?  21  ILE   B CG2   1 
ATOM   1512 C  CD1   . ILE   B 1 22  ? -24.23713 30.85804  32.89235  1.000 37.52968  ?  21  ILE   B CD1   1 
ATOM   1513 N  N     . GLN   B 1 23  ? -20.56993 34.44498  35.79698  1.000 37.82010  ?  22  GLN   B N     1 
ATOM   1514 C  CA    . GLN   B 1 23  ? -20.01222 35.73230  36.20207  1.000 36.67948  ?  22  GLN   B CA    1 
ATOM   1515 C  C     . GLN   B 1 23  ? -18.59840 35.91661  35.65703  1.000 33.98715  ?  22  GLN   B C     1 
ATOM   1516 O  O     . GLN   B 1 23  ? -18.27864 36.95675  35.06831  1.000 34.59187  ?  22  GLN   B O     1 
ATOM   1517 C  CB    . GLN   B 1 23  ? -20.00978 35.86554  37.72573  1.000 38.81744  ?  22  GLN   B CB    1 
ATOM   1518 C  CG    . GLN   B 1 23  ? -21.27675 36.44750  38.31545  1.000 40.83197  ?  22  GLN   B CG    1 
ATOM   1519 C  CD    . GLN   B 1 23  ? -21.53301 37.89722  37.90594  1.000 48.73915  ?  22  GLN   B CD    1 
ATOM   1520 O  OE1   . GLN   B 1 23  ? -20.85969 38.44804  37.02561  1.000 41.95492  ?  22  GLN   B OE1   1 
ATOM   1521 N  NE2   . GLN   B 1 23  ? -22.51211 38.52623  38.55680  1.000 44.22508  ?  22  GLN   B NE2   1 
ATOM   1522 N  N     . LEU   B 1 24  ? -17.73012 34.92057  35.86284  1.000 31.81595  ?  23  LEU   B N     1 
ATOM   1523 C  CA    . LEU   B 1 24  ? -16.35114 35.02109  35.39102  1.000 28.96383  ?  23  LEU   B CA    1 
ATOM   1524 C  C     . LEU   B 1 24  ? -16.29190 35.26675  33.88187  1.000 32.98889  ?  23  LEU   B C     1 
ATOM   1525 O  O     . LEU   B 1 24  ? -15.57517 36.15980  33.41189  1.000 28.87732  ?  23  LEU   B O     1 
ATOM   1526 C  CB    . LEU   B 1 24  ? -15.57821 33.75193  35.75690  1.000 28.19647  ?  23  LEU   B CB    1 
ATOM   1527 C  CG    . LEU   B 1 24  ? -14.11220 33.77779  35.32121  1.000 34.72037  ?  23  LEU   B CG    1 
ATOM   1528 C  CD1   . LEU   B 1 24  ? -13.31532 34.77519  36.17210  1.000 38.35421  ?  23  LEU   B CD1   1 
ATOM   1529 C  CD2   . LEU   B 1 24  ? -13.50973 32.39853  35.40982  1.000 31.02250  ?  23  LEU   B CD2   1 
ATOM   1530 N  N     . ILE   B 1 25  ? -17.05543 34.49533  33.11128  1.000 30.35452  ?  24  ILE   B N     1 
ATOM   1531 C  CA    . ILE   B 1 25  ? -16.90679 34.47512  31.65713  1.000 30.06536  ?  24  ILE   B CA    1 
ATOM   1532 C  C     . ILE   B 1 25  ? -17.72233 35.57585  30.98865  1.000 32.46577  ?  24  ILE   B C     1 
ATOM   1533 O  O     . ILE   B 1 25  ? -17.24336 36.22216  30.05274  1.000 34.89784  ?  24  ILE   B O     1 
ATOM   1534 C  CB    . ILE   B 1 25  ? -17.30102 33.08712  31.10783  1.000 32.19144  ?  24  ILE   B CB    1 
ATOM   1535 C  CG1   . ILE   B 1 25  ? -16.40742 31.97348  31.67648  1.000 28.81086  ?  24  ILE   B CG1   1 
ATOM   1536 C  CG2   . ILE   B 1 25  ? -17.31783 33.09612  29.57308  1.000 34.99982  ?  24  ILE   B CG2   1 
ATOM   1537 C  CD1   . ILE   B 1 25  ? -14.92045 32.15756  31.43419  1.000 32.40801  ?  24  ILE   B CD1   1 
ATOM   1538 N  N     . GLN   B 1 26  ? -18.96440 35.79700  31.44307  1.000 35.15909  ?  25  GLN   B N     1 
ATOM   1539 C  CA    . GLN   B 1 26  ? -19.92511 36.65152  30.74855  1.000 39.03039  ?  25  GLN   B CA    1 
ATOM   1540 C  C     . GLN   B 1 26  ? -20.33719 37.90167  31.52025  1.000 43.92680  ?  25  GLN   B C     1 
ATOM   1541 O  O     . GLN   B 1 26  ? -21.07926 38.73071  30.96913  1.000 42.96694  ?  25  GLN   B O     1 
ATOM   1542 C  CB    . GLN   B 1 26  ? -21.17833 35.83800  30.40395  1.000 38.48570  ?  25  GLN   B CB    1 
ATOM   1543 C  CG    . GLN   B 1 26  ? -20.84209 34.59202  29.61011  1.000 35.47525  ?  25  GLN   B CG    1 
ATOM   1544 C  CD    . GLN   B 1 26  ? -22.06280 33.75454  29.28362  1.000 47.30914  ?  25  GLN   B CD    1 
ATOM   1545 O  OE1   . GLN   B 1 26  ? -23.19535 34.13493  29.59946  1.000 45.17687  ?  25  GLN   B OE1   1 
ATOM   1546 N  NE2   . GLN   B 1 26  ? -21.83960 32.60729  28.64583  1.000 43.55169  ?  25  GLN   B NE2   1 
ATOM   1547 N  N     . ASN   B 1 27  ? -19.90722 38.03989  32.77532  1.000 34.37174  ?  26  ASN   B N     1 
ATOM   1548 C  CA    . ASN   B 1 27  ? -20.00582 39.29092  33.53619  1.000 44.42471  ?  26  ASN   B CA    1 
ATOM   1549 C  C     . ASN   B 1 27  ? -21.45527 39.70335  33.79315  1.000 47.35676  ?  26  ASN   B C     1 
ATOM   1550 O  O     . ASN   B 1 27  ? -21.80901 40.88381  33.71453  1.000 42.61144  ?  26  ASN   B O     1 
ATOM   1551 C  CB    . ASN   B 1 27  ? -19.23774 40.42234  32.84450  1.000 41.34727  ?  26  ASN   B CB    1 
ATOM   1552 C  CG    . ASN   B 1 27  ? -18.87405 41.54516  33.80657  1.000 42.92959  ?  26  ASN   B CG    1 
ATOM   1553 O  OD1   . ASN   B 1 27  ? -18.36216 41.29739  34.89892  1.000 44.04432  ?  26  ASN   B OD1   1 
ATOM   1554 N  ND2   . ASN   B 1 27  ? -19.16044 42.78612  33.41049  1.000 44.27725  ?  26  ASN   B ND2   1 
ATOM   1555 N  N     . HIS   B 1 28  ? -22.29922 38.72925  34.12234  1.000 41.71560  ?  27  HIS   B N     1 
ATOM   1556 C  CA    . HIS   B 1 28  ? -23.68396 39.01562  34.44677  1.000 42.24663  ?  27  HIS   B CA    1 
ATOM   1557 C  C     . HIS   B 1 28  ? -24.20689 37.90550  35.34530  1.000 45.70026  ?  27  HIS   B C     1 
ATOM   1558 O  O     . HIS   B 1 28  ? -23.57615 36.85848  35.51774  1.000 45.65720  ?  27  HIS   B O     1 
ATOM   1559 C  CB    . HIS   B 1 28  ? -24.52944 39.17335  33.17745  1.000 45.84990  ?  27  HIS   B CB    1 
ATOM   1560 C  CG    . HIS   B 1 28  ? -24.79731 37.88567  32.46900  1.000 50.71275  ?  27  HIS   B CG    1 
ATOM   1561 N  ND1   . HIS   B 1 28  ? -25.68311 36.94455  32.94898  1.000 55.93779  ?  27  HIS   B ND1   1 
ATOM   1562 C  CD2   . HIS   B 1 28  ? -24.29533 37.37916  31.31734  1.000 48.88870  ?  27  HIS   B CD2   1 
ATOM   1563 C  CE1   . HIS   B 1 28  ? -25.71519 35.91366  32.12177  1.000 49.08342  ?  27  HIS   B CE1   1 
ATOM   1564 N  NE2   . HIS   B 1 28  ? -24.88264 36.15249  31.12486  1.000 48.31639  ?  27  HIS   B NE2   1 
ATOM   1565 N  N     . PHE   B 1 29  ? -25.35819 38.16238  35.94733  1.000 50.00131  ?  28  PHE   B N     1 
ATOM   1566 C  CA    . PHE   B 1 29  ? -25.99308 37.22772  36.85862  1.000 50.49503  ?  28  PHE   B CA    1 
ATOM   1567 C  C     . PHE   B 1 29  ? -27.35804 36.83836  36.30565  1.000 60.15581  ?  28  PHE   B C     1 
ATOM   1568 O  O     . PHE   B 1 29  ? -28.00611 37.61041  35.59005  1.000 55.06927  ?  28  PHE   B O     1 
ATOM   1569 C  CB    . PHE   B 1 29  ? -26.11621 37.84198  38.24852  1.000 55.18654  ?  28  PHE   B CB    1 
ATOM   1570 C  CG    . PHE   B 1 29  ? -26.83140 36.97923  39.23999  1.000 60.87100  ?  28  PHE   B CG    1 
ATOM   1571 C  CD1   . PHE   B 1 29  ? -26.33133 35.73354  39.59444  1.000 55.60924  ?  28  PHE   B CD1   1 
ATOM   1572 C  CD2   . PHE   B 1 29  ? -27.98907 37.43054  39.85131  1.000 56.98061  ?  28  PHE   B CD2   1 
ATOM   1573 C  CE1   . PHE   B 1 29  ? -26.99380 34.94747  40.52783  1.000 58.23081  ?  28  PHE   B CE1   1 
ATOM   1574 C  CE2   . PHE   B 1 29  ? -28.65226 36.64948  40.77473  1.000 52.85954  ?  28  PHE   B CE2   1 
ATOM   1575 C  CZ    . PHE   B 1 29  ? -28.15717 35.41232  41.11772  1.000 56.18185  ?  28  PHE   B CZ    1 
ATOM   1576 N  N     . VAL   B 1 30  ? -27.76957 35.61138  36.59835  1.000 71.17517  ?  29  VAL   B N     1 
ATOM   1577 C  CA    . VAL   B 1 30  ? -29.09167 35.12282  36.23514  1.000 69.87765  ?  29  VAL   B CA    1 
ATOM   1578 C  C     . VAL   B 1 30  ? -29.72388 34.58702  37.50173  1.000 69.90134  ?  29  VAL   B C     1 
ATOM   1579 O  O     . VAL   B 1 30  ? -29.15895 33.69325  38.14383  1.000 69.74605  ?  29  VAL   B O     1 
ATOM   1580 C  CB    . VAL   B 1 30  ? -29.03665 34.02686  35.15940  1.000 75.33620  ?  29  VAL   B CB    1 
ATOM   1581 C  CG1   . VAL   B 1 30  ? -30.44201 33.50907  34.86273  1.000 75.32304  ?  29  VAL   B CG1   1 
ATOM   1582 C  CG2   . VAL   B 1 30  ? -28.34581 34.53922  33.89035  1.000 76.73850  ?  29  VAL   B CG2   1 
ATOM   1583 N  N     . ASP   B 1 31  ? -30.87455 35.13774  37.88003  1.000 66.24324  ?  30  ASP   B N     1 
ATOM   1584 C  CA    . ASP   B 1 31  ? -31.54917 34.57167  39.03797  1.000 67.80190  ?  30  ASP   B CA    1 
ATOM   1585 C  C     . ASP   B 1 31  ? -32.38655 33.35380  38.67297  1.000 61.12904  ?  30  ASP   B C     1 
ATOM   1586 O  O     . ASP   B 1 31  ? -32.96952 32.73163  39.56208  1.000 59.78690  ?  30  ASP   B O     1 
ATOM   1587 C  CB    . ASP   B 1 31  ? -32.40474 35.62886  39.74848  1.000 72.58097  ?  30  ASP   B CB    1 
ATOM   1588 C  CG    . ASP   B 1 31  ? -32.28775 35.54251  41.27820  1.000 72.74963  ?  30  ASP   B CG    1 
ATOM   1589 O  OD1   . ASP   B 1 31  ? -32.07688 34.41719  41.79422  1.000 66.28473  ?  30  ASP   B OD1   1 
ATOM   1590 O  OD2   . ASP   B 1 31  ? -32.39111 36.59456  41.95968  1.000 66.83136  -1 30  ASP   B OD2   1 
ATOM   1591 N  N     . GLU   B 1 32  ? -32.43399 32.98508  37.39866  1.000 61.23520  ?  31  GLU   B N     1 
ATOM   1592 C  CA    . GLU   B 1 32  ? -33.13322 31.78515  36.97022  1.000 63.28452  ?  31  GLU   B CA    1 
ATOM   1593 C  C     . GLU   B 1 32  ? -32.22889 30.56822  37.09531  1.000 58.42578  ?  31  GLU   B C     1 
ATOM   1594 O  O     . GLU   B 1 32  ? -31.00987 30.65271  36.93201  1.000 57.62348  ?  31  GLU   B O     1 
ATOM   1595 C  CB    . GLU   B 1 32  ? -33.61245 31.91832  35.52759  1.000 55.14167  ?  31  GLU   B CB    1 
ATOM   1596 C  CG    . GLU   B 1 32  ? -34.44181 33.15175  35.28263  1.000 58.02352  ?  31  GLU   B CG    1 
ATOM   1597 C  CD    . GLU   B 1 32  ? -34.85790 33.27859  33.83889  1.000 60.18094  ?  31  GLU   B CD    1 
ATOM   1598 O  OE1   . GLU   B 1 32  ? -34.06308 32.89143  32.95301  1.000 64.41544  ?  31  GLU   B OE1   1 
ATOM   1599 O  OE2   . GLU   B 1 32  ? -35.98363 33.75761  33.58877  1.000 63.90601  -1 31  GLU   B OE2   1 
ATOM   1600 N  N     . TYR   B 1 33  ? -32.84627 29.42651  37.37460  1.000 56.90510  ?  32  TYR   B N     1 
ATOM   1601 C  CA    . TYR   B 1 33  ? -32.13761 28.16408  37.55536  1.000 55.19571  ?  32  TYR   B CA    1 
ATOM   1602 C  C     . TYR   B 1 33  ? -32.23529 27.36910  36.25592  1.000 48.13166  ?  32  TYR   B C     1 
ATOM   1603 O  O     . TYR   B 1 33  ? -33.32943 26.98125  35.83696  1.000 41.04125  ?  32  TYR   B O     1 
ATOM   1604 C  CB    . TYR   B 1 33  ? -32.72910 27.39705  38.73517  1.000 49.89685  ?  32  TYR   B CB    1 
ATOM   1605 C  CG    . TYR   B 1 33  ? -31.96950 26.16534  39.17717  1.000 52.68772  ?  32  TYR   B CG    1 
ATOM   1606 C  CD1   . TYR   B 1 33  ? -30.99640 25.57547  38.36706  1.000 48.54948  ?  32  TYR   B CD1   1 
ATOM   1607 C  CD2   . TYR   B 1 33  ? -32.23545 25.58013  40.41187  1.000 47.94970  ?  32  TYR   B CD2   1 
ATOM   1608 C  CE1   . TYR   B 1 33  ? -30.31604 24.44428  38.77855  1.000 49.38206  ?  32  TYR   B CE1   1 
ATOM   1609 C  CE2   . TYR   B 1 33  ? -31.55456 24.45407  40.83174  1.000 48.91676  ?  32  TYR   B CE2   1 
ATOM   1610 C  CZ    . TYR   B 1 33  ? -30.59949 23.88888  40.01009  1.000 46.59449  ?  32  TYR   B CZ    1 
ATOM   1611 O  OH    . TYR   B 1 33  ? -29.91756 22.76985  40.41119  1.000 37.51742  ?  32  TYR   B OH    1 
ATOM   1612 N  N     . ASP   B 1 34  ? -31.08915 27.13774  35.61831  1.000 44.58669  ?  33  ASP   B N     1 
ATOM   1613 C  CA    . ASP   B 1 34  ? -30.98820 26.30575  34.41925  1.000 43.84172  ?  33  ASP   B CA    1 
ATOM   1614 C  C     . ASP   B 1 34  ? -30.06191 25.15265  34.77941  1.000 45.43312  ?  33  ASP   B C     1 
ATOM   1615 O  O     . ASP   B 1 34  ? -28.82690 25.29178  34.71995  1.000 45.87837  ?  33  ASP   B O     1 
ATOM   1616 C  CB    . ASP   B 1 34  ? -30.45951 27.09915  33.22921  1.000 41.27097  ?  33  ASP   B CB    1 
ATOM   1617 C  CG    . ASP   B 1 34  ? -30.47455 26.29108  31.93894  1.000 53.62097  ?  33  ASP   B CG    1 
ATOM   1618 O  OD1   . ASP   B 1 34  ? -31.02241 25.16418  31.94980  1.000 51.11974  ?  33  ASP   B OD1   1 
ATOM   1619 O  OD2   . ASP   B 1 34  ? -29.94129 26.77503  30.90954  1.000 58.34873  -1 33  ASP   B OD2   1 
ATOM   1620 N  N     . PRO   B 1 35  ? -30.60193 24.00603  35.18336  1.000 42.33717  ?  34  PRO   B N     1 
ATOM   1621 C  CA    . PRO   B 1 35  ? -29.74207 22.96225  35.75184  1.000 40.20008  ?  34  PRO   B CA    1 
ATOM   1622 C  C     . PRO   B 1 35  ? -28.77514 22.43887  34.70062  1.000 33.64920  ?  34  PRO   B C     1 
ATOM   1623 O  O     . PRO   B 1 35  ? -29.15667 22.17255  33.56038  1.000 38.35701  ?  34  PRO   B O     1 
ATOM   1624 C  CB    . PRO   B 1 35  ? -30.73992 21.89213  36.21051  1.000 39.56687  ?  34  PRO   B CB    1 
ATOM   1625 C  CG    . PRO   B 1 35  ? -31.90478 22.05157  35.28366  1.000 35.94754  ?  34  PRO   B CG    1 
ATOM   1626 C  CD    . PRO   B 1 35  ? -31.98700 23.54024  34.98172  1.000 44.63810  ?  34  PRO   B CD    1 
ATOM   1627 N  N     . THR   B 1 36  ? -27.51074 22.31350  35.09305  1.000 37.50635  ?  35  THR   B N     1 
ATOM   1628 C  CA    . THR   B 1 36  ? -26.43422 21.98528  34.16236  1.000 33.66271  ?  35  THR   B CA    1 
ATOM   1629 C  C     . THR   B 1 36  ? -26.37580 20.49004  33.86939  1.000 32.88136  ?  35  THR   B C     1 
ATOM   1630 O  O     . THR   B 1 36  ? -26.52900 19.66705  34.77079  1.000 29.05852  ?  35  THR   B O     1 
ATOM   1631 C  CB    . THR   B 1 36  ? -25.09053 22.43056  34.75089  1.000 32.82881  ?  35  THR   B CB    1 
ATOM   1632 O  OG1   . THR   B 1 36  ? -25.05338 23.86034  34.84217  1.000 38.70604  ?  35  THR   B OG1   1 
ATOM   1633 C  CG2   . THR   B 1 36  ? -23.91972 21.93896  33.91383  1.000 35.77791  ?  35  THR   B CG2   1 
ATOM   1634 N  N     . ILE   B 1 37  ? -26.13934 20.14067  32.60080  1.000 30.87879  ?  36  ILE   B N     1 
ATOM   1635 C  CA    . ILE   B 1 37  ? -25.65740 18.80553  32.25339  1.000 30.07019  ?  36  ILE   B CA    1 
ATOM   1636 C  C     . ILE   B 1 37  ? -24.13823 18.83258  32.35973  1.000 36.46874  ?  36  ILE   B C     1 
ATOM   1637 O  O     . ILE   B 1 37  ? -23.55070 18.12317  33.18425  1.000 30.17479  ?  36  ILE   B O     1 
ATOM   1638 C  CB    . ILE   B 1 37  ? -26.09543 18.36656  30.83875  1.000 31.51720  ?  36  ILE   B CB    1 
ATOM   1639 C  CG1   . ILE   B 1 37  ? -27.60461 18.53854  30.64283  1.000 31.00998  ?  36  ILE   B CG1   1 
ATOM   1640 C  CG2   . ILE   B 1 37  ? -25.67359 16.91969  30.57369  1.000 26.67285  ?  36  ILE   B CG2   1 
ATOM   1641 C  CD1   . ILE   B 1 37  ? -28.43324 17.68920  31.61619  1.000 27.86998  ?  36  ILE   B CD1   1 
ATOM   1642 N  N     . GLU   B 1 38  ? -23.49882 19.66075  31.51711  1.000 28.87003  ?  37  GLU   B N     1 
ATOM   1643 C  CA    . GLU   B 1 38  ? -22.05122 19.85006  31.49909  1.000 29.16431  ?  37  GLU   B CA    1 
ATOM   1644 C  C     . GLU   B 1 38  ? -21.69258 20.94271  30.49916  1.000 30.52386  ?  37  GLU   B C     1 
ATOM   1645 O  O     . GLU   B 1 38  ? -22.10944 20.87791  29.34070  1.000 29.92016  ?  37  GLU   B O     1 
ATOM   1646 C  CB    . GLU   B 1 38  ? -21.31656 18.56327  31.11739  1.000 29.23002  ?  37  GLU   B CB    1 
ATOM   1647 C  CG    . GLU   B 1 38  ? -19.85871 18.58745  31.49211  1.000 28.18956  ?  37  GLU   B CG    1 
ATOM   1648 C  CD    . GLU   B 1 38  ? -19.00840 17.56402  30.73143  1.000 33.72706  ?  37  GLU   B CD    1 
ATOM   1649 O  OE1   . GLU   B 1 38  ? -18.53463 17.89909  29.63210  1.000 39.04922  ?  37  GLU   B OE1   1 
ATOM   1650 O  OE2   . GLU   B 1 38  ? -18.80855 16.43081  31.23060  1.000 39.55337  -1 37  GLU   B OE2   1 
ATOM   1651 N  N     . ASP   B 1 39  ? -20.91168 21.93160  30.91606  1.000 29.87799  ?  38  ASP   B N     1 
ATOM   1652 C  CA    . ASP   B 1 39  ? -20.52892 23.02292  30.03863  1.000 25.85674  ?  38  ASP   B CA    1 
ATOM   1653 C  C     . ASP   B 1 39  ? -19.03917 23.29649  30.18198  1.000 30.87101  ?  38  ASP   B C     1 
ATOM   1654 O  O     . ASP   B 1 39  ? -18.45510 23.07387  31.24871  1.000 30.95530  ?  38  ASP   B O     1 
ATOM   1655 C  CB    . ASP   B 1 39  ? -21.34160 24.29445  30.34600  1.000 31.28099  ?  38  ASP   B CB    1 
ATOM   1656 C  CG    . ASP   B 1 39  ? -22.82973 24.13010  30.07417  1.000 36.72015  ?  38  ASP   B CG    1 
ATOM   1657 O  OD1   . ASP   B 1 39  ? -23.21034 23.65251  28.99590  1.000 36.83409  ?  38  ASP   B OD1   1 
ATOM   1658 O  OD2   . ASP   B 1 39  ? -23.64235 24.49954  30.94384  1.000 42.87383  -1 38  ASP   B OD2   1 
ATOM   1659 N  N     . SER   B 1 40  ? -18.42237 23.76510  29.08517  1.000 26.71495  ?  39  SER   B N     1 
ATOM   1660 C  CA    . SER   B 1 40  ? -17.02183 24.15858  29.04771  1.000 25.80499  ?  39  SER   B CA    1 
ATOM   1661 C  C     . SER   B 1 40  ? -16.91158 25.59549  28.57432  1.000 26.61182  ?  39  SER   B C     1 
ATOM   1662 O  O     . SER   B 1 40  ? -17.68923 26.04836  27.73317  1.000 28.72830  ?  39  SER   B O     1 
ATOM   1663 C  CB    . SER   B 1 40  ? -16.17012 23.29476  28.10781  1.000 34.98946  ?  39  SER   B CB    1 
ATOM   1664 O  OG    . SER   B 1 40  ? -16.23209 21.93566  28.45265  1.000 38.90869  ?  39  SER   B OG    1 
ATOM   1665 N  N     . TYR   B 1 41  ? -15.91917 26.29436  29.10958  1.000 28.74228  ?  40  TYR   B N     1 
ATOM   1666 C  CA    . TYR   B 1 41  ? -15.67059 27.68541  28.78593  1.000 26.28303  ?  40  TYR   B CA    1 
ATOM   1667 C  C     . TYR   B 1 41  ? -14.17008 27.89602  28.70707  1.000 26.37859  ?  40  TYR   B C     1 
ATOM   1668 O  O     . TYR   B 1 41  ? -13.39794 27.14629  29.29239  1.000 26.85750  ?  40  TYR   B O     1 
ATOM   1669 C  CB    . TYR   B 1 41  ? -16.29911 28.63028  29.82773  1.000 27.76630  ?  40  TYR   B CB    1 
ATOM   1670 C  CG    . TYR   B 1 41  ? -17.79829 28.44549  30.00368  1.000 30.47404  ?  40  TYR   B CG    1 
ATOM   1671 C  CD1   . TYR   B 1 41  ? -18.70590 29.12217  29.20027  1.000 25.92536  ?  40  TYR   B CD1   1 
ATOM   1672 C  CD2   . TYR   B 1 41  ? -18.29852 27.60092  30.99136  1.000 24.75579  ?  40  TYR   B CD2   1 
ATOM   1673 C  CE1   . TYR   B 1 41  ? -20.08197 28.95969  29.37216  1.000 34.10717  ?  40  TYR   B CE1   1 
ATOM   1674 C  CE2   . TYR   B 1 41  ? -19.66113 27.43592  31.18478  1.000 27.95924  ?  40  TYR   B CE2   1 
ATOM   1675 C  CZ    . TYR   B 1 41  ? -20.55652 28.10652  30.37589  1.000 32.93610  ?  40  TYR   B CZ    1 
ATOM   1676 O  OH    . TYR   B 1 41  ? -21.91022 27.90419  30.57700  1.000 31.13540  ?  40  TYR   B OH    1 
ATOM   1677 N  N     . ARG   B 1 42  ? -13.76695 28.91549  27.94712  1.000 24.76985  ?  41  ARG   B N     1 
ATOM   1678 C  CA    . ARG   B 1 42  ? -12.37066 29.31633  27.80705  1.000 27.20567  ?  41  ARG   B CA    1 
ATOM   1679 C  C     . ARG   B 1 42  ? -12.26449 30.81888  27.94926  1.000 27.87143  ?  41  ARG   B C     1 
ATOM   1680 O  O     . ARG   B 1 42  ? -13.05082 31.56043  27.34850  1.000 25.01103  ?  41  ARG   B O     1 
ATOM   1681 C  CB    . ARG   B 1 42  ? -11.78025 28.93190  26.45648  1.000 34.22989  ?  41  ARG   B CB    1 
ATOM   1682 C  CG    . ARG   B 1 42  ? -11.53658 27.47708  26.28417  1.000 37.04881  ?  41  ARG   B CG    1 
ATOM   1683 C  CD    . ARG   B 1 42  ? -10.58875 27.26744  25.13123  1.000 43.52382  ?  41  ARG   B CD    1 
ATOM   1684 N  NE    . ARG   B 1 42  ? -9.84498  26.03960  25.36116  1.000 45.37086  ?  41  ARG   B NE    1 
ATOM   1685 C  CZ    . ARG   B 1 42  ? -8.67138  25.76781  24.81973  1.000 34.19899  ?  41  ARG   B CZ    1 
ATOM   1686 N  NH1   . ARG   B 1 42  ? -8.06107  26.63591  24.02261  1.000 41.51669  ?  41  ARG   B NH1   1 
ATOM   1687 N  NH2   . ARG   B 1 42  ? -8.09878  24.59813  25.08249  1.000 40.91326  ?  41  ARG   B NH2   1 
ATOM   1688 N  N     . LYS   B 1 43  ? -11.27261 31.26230  28.71395  1.000 27.14304  ?  42  LYS   B N     1 
ATOM   1689 C  CA    . LYS   B 1 43  ? -11.01368 32.68407  28.88843  1.000 31.71862  ?  42  LYS   B CA    1 
ATOM   1690 C  C     . LYS   B 1 43  ? -9.52094  32.86117  29.14092  1.000 31.29633  ?  42  LYS   B C     1 
ATOM   1691 O  O     . LYS   B 1 43  ? -8.95070  32.13493  29.96356  1.000 31.81989  ?  42  LYS   B O     1 
ATOM   1692 C  CB    . LYS   B 1 43  ? -11.83892 33.22945  30.05942  1.000 28.45687  ?  42  LYS   B CB    1 
ATOM   1693 C  CG    . LYS   B 1 43  ? -11.83614 34.73033  30.23506  1.000 32.44571  ?  42  LYS   B CG    1 
ATOM   1694 C  CD    . LYS   B 1 43  ? -12.53058 35.13005  31.52986  1.000 32.73719  ?  42  LYS   B CD    1 
ATOM   1695 C  CE    . LYS   B 1 43  ? -12.26402 36.59297  31.85906  1.000 36.04009  ?  42  LYS   B CE    1 
ATOM   1696 N  NZ    . LYS   B 1 43  ? -12.74971 37.47732  30.77593  1.000 42.61951  ?  42  LYS   B NZ    1 
ATOM   1697 N  N     . GLN   B 1 44  ? -8.88678  33.80185  28.44239  1.000 25.39225  ?  43  GLN   B N     1 
ATOM   1698 C  CA    . GLN   B 1 44  ? -7.50519  34.15055  28.76761  1.000 29.66306  ?  43  GLN   B CA    1 
ATOM   1699 C  C     . GLN   B 1 44  ? -7.48812  35.29912  29.77470  1.000 25.96015  ?  43  GLN   B C     1 
ATOM   1700 O  O     . GLN   B 1 44  ? -8.30157  36.22170  29.70412  1.000 29.78199  ?  43  GLN   B O     1 
ATOM   1701 C  CB    . GLN   B 1 44  ? -6.68360  34.50392  27.52241  1.000 29.19749  ?  43  GLN   B CB    1 
ATOM   1702 C  CG    . GLN   B 1 44  ? -7.06181  35.74895  26.75489  1.000 28.54815  ?  43  GLN   B CG    1 
ATOM   1703 C  CD    . GLN   B 1 44  ? -5.95039  36.15692  25.75717  1.000 34.80321  ?  43  GLN   B CD    1 
ATOM   1704 O  OE1   . GLN   B 1 44  ? -4.80923  36.41040  26.15402  1.000 30.40760  ?  43  GLN   B OE1   1 
ATOM   1705 N  NE2   . GLN   B 1 44  ? -6.28481  36.19524  24.46442  1.000 25.62497  ?  43  GLN   B NE2   1 
ATOM   1706 N  N     . VAL   B 1 45  ? -6.59317  35.20249  30.75255  1.000 27.19411  ?  44  VAL   B N     1 
ATOM   1707 C  CA    . VAL   B 1 45  ? -6.52677  36.14701  31.86410  1.000 29.76925  ?  44  VAL   B CA    1 
ATOM   1708 C  C     . VAL   B 1 45  ? -5.06456  36.43223  32.17575  1.000 31.59950  ?  44  VAL   B C     1 
ATOM   1709 O  O     . VAL   B 1 45  ? -4.15320  35.77043  31.67381  1.000 29.30384  ?  44  VAL   B O     1 
ATOM   1710 C  CB    . VAL   B 1 45  ? -7.24016  35.61511  33.12805  1.000 29.78497  ?  44  VAL   B CB    1 
ATOM   1711 C  CG1   . VAL   B 1 45  ? -8.75065  35.48635  32.89129  1.000 30.88731  ?  44  VAL   B CG1   1 
ATOM   1712 C  CG2   . VAL   B 1 45  ? -6.63362  34.27305  33.53949  1.000 25.40694  ?  44  VAL   B CG2   1 
ATOM   1713 N  N     . VAL   B 1 46  ? -4.84536  37.43533  33.02178  1.000 29.08686  ?  45  VAL   B N     1 
ATOM   1714 C  CA    . VAL   B 1 46  ? -3.51341  37.75120  33.52636  1.000 30.40186  ?  45  VAL   B CA    1 
ATOM   1715 C  C     . VAL   B 1 46  ? -3.55011  37.59412  35.04465  1.000 32.12312  ?  45  VAL   B C     1 
ATOM   1716 O  O     . VAL   B 1 46  ? -4.36380  38.23531  35.72517  1.000 32.19945  ?  45  VAL   B O     1 
ATOM   1717 C  CB    . VAL   B 1 46  ? -3.05755  39.16280  33.13085  1.000 32.14944  ?  45  VAL   B CB    1 
ATOM   1718 C  CG1   . VAL   B 1 46  ? -1.62423  39.37603  33.56704  1.000 34.33655  ?  45  VAL   B CG1   1 
ATOM   1719 C  CG2   . VAL   B 1 46  ? -3.20826  39.39213  31.61187  1.000 37.95239  ?  45  VAL   B CG2   1 
ATOM   1720 N  N     . ILE   B 1 47  ? -2.69029  36.73404  35.57071  1.000 31.98890  ?  46  ILE   B N     1 
ATOM   1721 C  CA    . ILE   B 1 47  ? -2.63071  36.47519  37.00513  1.000 33.36367  ?  46  ILE   B CA    1 
ATOM   1722 C  C     . ILE   B 1 47  ? -1.18734  36.64420  37.45285  1.000 35.33403  ?  46  ILE   B C     1 
ATOM   1723 O  O     . ILE   B 1 47  ? -0.29852  35.92992  36.97342  1.000 35.55774  ?  46  ILE   B O     1 
ATOM   1724 C  CB    . ILE   B 1 47  ? -3.15924  35.07594  37.35879  1.000 35.79733  ?  46  ILE   B CB    1 
ATOM   1725 C  CG1   . ILE   B 1 47  ? -4.65781  34.99858  37.06318  1.000 29.50702  ?  46  ILE   B CG1   1 
ATOM   1726 C  CG2   . ILE   B 1 47  ? -2.90627  34.74490  38.84630  1.000 34.55636  ?  46  ILE   B CG2   1 
ATOM   1727 C  CD1   . ILE   B 1 47  ? -5.17393  33.60160  36.95367  1.000 29.77265  ?  46  ILE   B CD1   1 
ATOM   1728 N  N     . ASP   B 1 48  ? -0.95604  37.59357  38.35770  1.000 37.45008  ?  47  ASP   B N     1 
ATOM   1729 C  CA    . ASP   B 1 48  ? 0.38317   37.87622  38.86691  1.000 40.24515  ?  47  ASP   B CA    1 
ATOM   1730 C  C     . ASP   B 1 48  ? 1.33817   38.17621  37.71833  1.000 40.73468  ?  47  ASP   B C     1 
ATOM   1731 O  O     . ASP   B 1 48  ? 2.48994   37.74267  37.71393  1.000 45.00751  ?  47  ASP   B O     1 
ATOM   1732 C  CB    . ASP   B 1 48  ? 0.91433   36.72142  39.72606  1.000 42.51384  ?  47  ASP   B CB    1 
ATOM   1733 C  CG    . ASP   B 1 48  ? 0.09176   36.48810  41.00067  1.000 41.34265  ?  47  ASP   B CG    1 
ATOM   1734 O  OD1   . ASP   B 1 48  ? -0.57282  37.43231  41.47753  1.000 42.09800  ?  47  ASP   B OD1   1 
ATOM   1735 O  OD2   . ASP   B 1 48  ? 0.11116   35.34936  41.52031  1.000 40.93997  -1 47  ASP   B OD2   1 
ATOM   1736 N  N     . GLY   B 1 49  ? 0.83945   38.90679  36.72015  1.000 39.57665  ?  48  GLY   B N     1 
ATOM   1737 C  CA    . GLY   B 1 49  ? 1.61635   39.29775  35.56272  1.000 40.84048  ?  48  GLY   B CA    1 
ATOM   1738 C  C     . GLY   B 1 49  ? 1.86242   38.22216  34.52466  1.000 41.58637  ?  48  GLY   B C     1 
ATOM   1739 O  O     . GLY   B 1 49  ? 2.61602   38.46912  33.57837  1.000 49.37794  ?  48  GLY   B O     1 
ATOM   1740 N  N     . GLU   B 1 50  ? 1.27151   37.03787  34.65198  1.000 37.27571  ?  49  GLU   B N     1 
ATOM   1741 C  CA    . GLU   B 1 50  ? 1.47878   35.97667  33.67650  1.000 36.20666  ?  49  GLU   B CA    1 
ATOM   1742 C  C     . GLU   B 1 50  ? 0.16753   35.65758  32.97373  1.000 42.00823  ?  49  GLU   B C     1 
ATOM   1743 O  O     . GLU   B 1 50  ? -0.80238  35.24082  33.62095  1.000 33.25467  ?  49  GLU   B O     1 
ATOM   1744 C  CB    . GLU   B 1 50  ? 2.06009   34.71616  34.31033  1.000 40.24372  ?  49  GLU   B CB    1 
ATOM   1745 C  CG    . GLU   B 1 50  ? 2.07093   33.53765  33.34082  1.000 48.27649  ?  49  GLU   B CG    1 
ATOM   1746 C  CD    . GLU   B 1 50  ? 3.24688   32.59286  33.54745  1.000 55.83414  ?  49  GLU   B CD    1 
ATOM   1747 O  OE1   . GLU   B 1 50  ? 4.18326   32.94507  34.29984  1.000 62.85221  ?  49  GLU   B OE1   1 
ATOM   1748 O  OE2   . GLU   B 1 50  ? 3.23964   31.49292  32.94848  1.000 60.07360  -1 49  GLU   B OE2   1 
ATOM   1749 N  N     . THR   B 1 51  ? 0.15840   35.85761  31.64759  1.000 34.48113  ?  50  THR   B N     1 
ATOM   1750 C  CA    . THR   B 1 51  ? -0.98486  35.53756  30.80356  1.000 33.27043  ?  50  THR   B CA    1 
ATOM   1751 C  C     . THR   B 1 51  ? -1.20509  34.03417  30.76596  1.000 34.74077  ?  50  THR   B C     1 
ATOM   1752 O  O     . THR   B 1 51  ? -0.25915  33.26164  30.58174  1.000 33.37746  ?  50  THR   B O     1 
ATOM   1753 C  CB    . THR   B 1 51  ? -0.75939  36.06033  29.37794  1.000 34.52048  ?  50  THR   B CB    1 
ATOM   1754 O  OG1   . THR   B 1 51  ? -0.61007  37.48321  29.40083  1.000 34.22985  ?  50  THR   B OG1   1 
ATOM   1755 C  CG2   . THR   B 1 51  ? -1.93436  35.67907  28.43563  1.000 32.53901  ?  50  THR   B CG2   1 
ATOM   1756 N  N     . CYS   B 1 52  ? -2.45464  33.61326  30.93823  1.000 27.28570  ?  51  CYS   B N     1 
ATOM   1757 C  CA    . CYS   B 1 52  ? -2.74400  32.19517  30.84006  1.000 27.49903  ?  51  CYS   B CA    1 
ATOM   1758 C  C     . CYS   B 1 52  ? -4.17457  31.99826  30.36429  1.000 26.05344  ?  51  CYS   B C     1 
ATOM   1759 O  O     . CYS   B 1 52  ? -4.99999  32.91250  30.41238  1.000 25.74052  ?  51  CYS   B O     1 
ATOM   1760 C  CB    . CYS   B 1 52  ? -2.51271  31.47202  32.17053  1.000 30.79713  ?  51  CYS   B CB    1 
ATOM   1761 S  SG    . CYS   B 1 52  ? -3.48280  32.14058  33.53335  1.000 35.22482  ?  51  CYS   B SG    1 
ATOM   1762 N  N     . LEU   B 1 53  ? -4.44392  30.77460  29.90685  1.000 27.70676  ?  52  LEU   B N     1 
ATOM   1763 C  CA    . LEU   B 1 53  ? -5.71206  30.37802  29.30630  1.000 30.55927  ?  52  LEU   B CA    1 
ATOM   1764 C  C     . LEU   B 1 53  ? -6.44377  29.46360  30.28129  1.000 25.70703  ?  52  LEU   B C     1 
ATOM   1765 O  O     . LEU   B 1 53  ? -5.95015  28.38091  30.60488  1.000 31.58565  ?  52  LEU   B O     1 
ATOM   1766 C  CB    . LEU   B 1 53  ? -5.47859  29.66295  27.96793  1.000 24.55583  ?  52  LEU   B CB    1 
ATOM   1767 C  CG    . LEU   B 1 53  ? -6.69813  29.35587  27.09331  1.000 30.89692  ?  52  LEU   B CG    1 
ATOM   1768 C  CD1   . LEU   B 1 53  ? -7.56160  30.60557  26.90047  1.000 28.00699  ?  52  LEU   B CD1   1 
ATOM   1769 C  CD2   . LEU   B 1 53  ? -6.25149  28.82380  25.71407  1.000 35.37133  ?  52  LEU   B CD2   1 
ATOM   1770 N  N     . LEU   B 1 54  ? -7.60365  29.90753  30.75705  1.000 27.30954  ?  53  LEU   B N     1 
ATOM   1771 C  CA    . LEU   B 1 54  ? -8.43852  29.11712  31.66160  1.000 31.67906  ?  53  LEU   B CA    1 
ATOM   1772 C  C     . LEU   B 1 54  ? -9.41067  28.26248  30.85371  1.000 30.03604  ?  53  LEU   B C     1 
ATOM   1773 O  O     . LEU   B 1 54  ? -10.23341 28.79026  30.10449  1.000 30.16245  ?  53  LEU   B O     1 
ATOM   1774 C  CB    . LEU   B 1 54  ? -9.22554  30.01500  32.61082  1.000 29.33649  ?  53  LEU   B CB    1 
ATOM   1775 C  CG    . LEU   B 1 54  ? -8.41842  31.03351  33.42319  1.000 35.31443  ?  53  LEU   B CG    1 
ATOM   1776 C  CD1   . LEU   B 1 54  ? -9.32339  31.82039  34.37956  1.000 34.60575  ?  53  LEU   B CD1   1 
ATOM   1777 C  CD2   . LEU   B 1 54  ? -7.27565  30.34631  34.15779  1.000 29.92276  ?  53  LEU   B CD2   1 
ATOM   1778 N  N     . ASP   B 1 55  ? -9.30212  26.95244  31.00487  1.000 31.94978  ?  54  ASP   B N     1 
ATOM   1779 C  CA    . ASP   B 1 55  ? -10.24361 25.98741  30.45992  1.000 28.03525  ?  54  ASP   B CA    1 
ATOM   1780 C  C     . ASP   B 1 55  ? -11.12618 25.52719  31.61678  1.000 27.56333  ?  54  ASP   B C     1 
ATOM   1781 O  O     . ASP   B 1 55  ? -10.63901 24.85727  32.53340  1.000 30.40939  ?  54  ASP   B O     1 
ATOM   1782 C  CB    . ASP   B 1 55  ? -9.47139  24.81893  29.86037  1.000 29.88833  ?  54  ASP   B CB    1 
ATOM   1783 C  CG    . ASP   B 1 55  ? -10.31118 23.98934  28.95566  1.000 39.32855  ?  54  ASP   B CG    1 
ATOM   1784 O  OD1   . ASP   B 1 55  ? -11.53894 24.20214  28.95616  1.000 49.30225  ?  54  ASP   B OD1   1 
ATOM   1785 O  OD2   . ASP   B 1 55  ? -9.75154  23.13445  28.24107  1.000 50.72318  -1 54  ASP   B OD2   1 
ATOM   1786 N  N     . ILE   B 1 56  ? -12.40306 25.89955  31.61516  1.000 26.82764  ?  55  ILE   B N     1 
ATOM   1787 C  CA    . ILE   B 1 56  ? -13.26179 25.66746  32.78075  1.000 27.21589  ?  55  ILE   B CA    1 
ATOM   1788 C  C     . ILE   B 1 56  ? -14.35867 24.67130  32.43681  1.000 27.16050  ?  55  ILE   B C     1 
ATOM   1789 O  O     . ILE   B 1 56  ? -15.13641 24.89206  31.49929  1.000 28.16573  ?  55  ILE   B O     1 
ATOM   1790 C  CB    . ILE   B 1 56  ? -13.86700 26.97944  33.31078  1.000 28.74134  ?  55  ILE   B CB    1 
ATOM   1791 C  CG1   . ILE   B 1 56  ? -12.76463 27.91206  33.80050  1.000 33.67677  ?  55  ILE   B CG1   1 
ATOM   1792 C  CG2   . ILE   B 1 56  ? -14.85718 26.71343  34.46648  1.000 29.51939  ?  55  ILE   B CG2   1 
ATOM   1793 C  CD1   . ILE   B 1 56  ? -13.21592 29.34752  33.85610  1.000 34.95900  ?  55  ILE   B CD1   1 
ATOM   1794 N  N     . LEU   B 1 57  ? -14.47128 23.61350  33.24144  1.000 25.33761  ?  56  LEU   B N     1 
ATOM   1795 C  CA    . LEU   B 1 57  ? -15.57123 22.65819  33.12936  1.000 29.54564  ?  56  LEU   B CA    1 
ATOM   1796 C  C     . LEU   B 1 57  ? -16.57276 22.90239  34.26049  1.000 29.98467  ?  56  LEU   B C     1 
ATOM   1797 O  O     . LEU   B 1 57  ? -16.23237 22.78193  35.44936  1.000 29.87905  ?  56  LEU   B O     1 
ATOM   1798 C  CB    . LEU   B 1 57  ? -15.05720 21.21732  33.15624  1.000 22.50290  ?  56  LEU   B CB    1 
ATOM   1799 C  CG    . LEU   B 1 57  ? -16.11302 20.14659  32.86586  1.000 27.15633  ?  56  LEU   B CG    1 
ATOM   1800 C  CD1   . LEU   B 1 57  ? -16.46569 20.11893  31.36306  1.000 27.19199  ?  56  LEU   B CD1   1 
ATOM   1801 C  CD2   . LEU   B 1 57  ? -15.58783 18.80264  33.26664  1.000 26.07298  ?  56  LEU   B CD2   1 
ATOM   1802 N  N     . ASP   B 1 58  ? -17.79614 23.24782  33.88207  1.000 25.97630  ?  57  ASP   B N     1 
ATOM   1803 C  CA    . ASP   B 1 58  ? -18.89520 23.51572  34.79987  1.000 28.93777  ?  57  ASP   B CA    1 
ATOM   1804 C  C     . ASP   B 1 58  ? -19.71753 22.23013  34.89658  1.000 28.52636  ?  57  ASP   B C     1 
ATOM   1805 O  O     . ASP   B 1 58  ? -20.40751 21.85943  33.94184  1.000 28.29024  ?  57  ASP   B O     1 
ATOM   1806 C  CB    . ASP   B 1 58  ? -19.70929 24.69814  34.27348  1.000 29.74204  ?  57  ASP   B CB    1 
ATOM   1807 C  CG    . ASP   B 1 58  ? -20.88179 25.07340  35.15926  1.000 33.02248  ?  57  ASP   B CG    1 
ATOM   1808 O  OD1   . ASP   B 1 58  ? -20.83297 24.80738  36.37383  1.000 36.16063  ?  57  ASP   B OD1   1 
ATOM   1809 O  OD2   . ASP   B 1 58  ? -21.85557 25.66127  34.62997  1.000 40.58815  -1 57  ASP   B OD2   1 
ATOM   1810 N  N     . THR   B 1 59  ? -19.59857 21.51547  36.01687  1.000 24.87977  ?  58  THR   B N     1 
ATOM   1811 C  CA    . THR   B 1 59  ? -20.19956 20.18880  36.11597  1.000 22.48210  ?  58  THR   B CA    1 
ATOM   1812 C  C     . THR   B 1 59  ? -21.59487 20.24760  36.72267  1.000 24.26628  ?  58  THR   B C     1 
ATOM   1813 O  O     . THR   B 1 59  ? -22.07066 21.29092  37.16702  1.000 29.03879  ?  58  THR   B O     1 
ATOM   1814 C  CB    . THR   B 1 59  ? -19.31607 19.25341  36.92751  1.000 30.27191  ?  58  THR   B CB    1 
ATOM   1815 O  OG1   . THR   B 1 59  ? -19.32361 19.67040  38.30503  1.000 27.96264  ?  58  THR   B OG1   1 
ATOM   1816 C  CG2   . THR   B 1 59  ? -17.90102 19.30107  36.36899  1.000 27.69673  ?  58  THR   B CG2   1 
ATOM   1817 N  N     . ALA   B 1 60  ? -22.26225 19.09766  36.72184  1.000 28.56753  ?  59  ALA   B N     1 
ATOM   1818 C  CA    . ALA   B 1 60  ? -23.62085 18.98792  37.22897  1.000 33.67576  ?  59  ALA   B CA    1 
ATOM   1819 C  C     . ALA   B 1 60  ? -23.59825 18.58173  38.70365  1.000 31.84044  ?  59  ALA   B C     1 
ATOM   1820 O  O     . ALA   B 1 60  ? -22.84203 17.69125  39.10120  1.000 31.64226  ?  59  ALA   B O     1 
ATOM   1821 C  CB    . ALA   B 1 60  ? -24.41951 17.97750  36.40042  1.000 31.00938  ?  59  ALA   B CB    1 
ATOM   1822 N  N     . GLY   B 1 61  ? -24.41497 19.25183  39.51422  1.000 35.77845  ?  60  GLY   B N     1 
ATOM   1823 C  CA    . GLY   B 1 61  ? -24.54482 18.89232  40.91619  1.000 37.59019  ?  60  GLY   B CA    1 
ATOM   1824 C  C     . GLY   B 1 61  ? -25.44414 17.70615  41.20190  1.000 41.61532  ?  60  GLY   B C     1 
ATOM   1825 O  O     . GLY   B 1 61  ? -25.66738 17.38320  42.37056  1.000 45.76862  ?  60  GLY   B O     1 
ATOM   1826 N  N     . GLN   B 1 62  ? -25.97659 17.05364  40.17826  1.000 40.08129  ?  61  GLN   B N     1 
ATOM   1827 C  CA    . GLN   B 1 62  ? -26.81797 15.88723  40.39580  1.000 46.10713  ?  61  GLN   B CA    1 
ATOM   1828 C  C     . GLN   B 1 62  ? -26.02256 14.74774  41.02932  1.000 50.14663  ?  61  GLN   B C     1 
ATOM   1829 O  O     . GLN   B 1 62  ? -24.85779 14.51508  40.68817  1.000 52.06098  ?  61  GLN   B O     1 
ATOM   1830 C  CB    . GLN   B 1 62  ? -27.42821 15.45975  39.07460  1.000 47.28719  ?  61  GLN   B CB    1 
ATOM   1831 C  CG    . GLN   B 1 62  ? -28.45492 16.44738  38.57432  1.000 44.16106  ?  61  GLN   B CG    1 
ATOM   1832 C  CD    . GLN   B 1 62  ? -29.85972 15.96370  38.85083  1.000 53.02188  ?  61  GLN   B CD    1 
ATOM   1833 O  OE1   . GLN   B 1 62  ? -30.68217 16.67104  39.45070  1.000 49.39294  ?  61  GLN   B OE1   1 
ATOM   1834 N  NE2   . GLN   B 1 62  ? -30.14190 14.73460  38.42027  1.000 45.73596  ?  61  GLN   B NE2   1 
ATOM   1835 N  N     . GLU   B 1 63  ? -26.65022 14.04820  41.98325  1.000 47.85922  ?  62  GLU   B N     1 
ATOM   1836 C  CA    . GLU   B 1 63  ? -25.96246 12.99268  42.72069  1.000 51.23307  ?  62  GLU   B CA    1 
ATOM   1837 C  C     . GLU   B 1 63  ? -26.26880 11.59527  42.20276  1.000 44.16151  ?  62  GLU   B C     1 
ATOM   1838 O  O     . GLU   B 1 63  ? -25.55572 10.65098  42.55615  1.000 43.13497  ?  62  GLU   B O     1 
ATOM   1839 C  CB    . GLU   B 1 63  ? -26.29590 13.07050  44.22527  1.000 50.68658  ?  62  GLU   B CB    1 
ATOM   1840 C  CG    . GLU   B 1 63  ? -27.72527 13.49902  44.55920  1.000 57.95867  ?  62  GLU   B CG    1 
ATOM   1841 C  CD    . GLU   B 1 63  ? -27.91434 13.87672  46.03806  1.000 67.49238  ?  62  GLU   B CD    1 
ATOM   1842 O  OE1   . GLU   B 1 63  ? -26.97247 14.42898  46.64823  1.000 69.01483  ?  62  GLU   B OE1   1 
ATOM   1843 O  OE2   . GLU   B 1 63  ? -29.00706 13.62000  46.59296  1.000 60.82003  -1 62  GLU   B OE2   1 
ATOM   1844 N  N     . GLU   B 1 64  ? -27.28834 11.44284  41.36326  1.000 42.39014  ?  63  GLU   B N     1 
ATOM   1845 C  CA    . GLU   B 1 64  ? -27.64995 10.12715  40.85276  1.000 44.07525  ?  63  GLU   B CA    1 
ATOM   1846 C  C     . GLU   B 1 64  ? -26.60109 9.51897   39.91908  1.000 44.60846  ?  63  GLU   B C     1 
ATOM   1847 O  O     . GLU   B 1 64  ? -26.69721 8.32440   39.61579  1.000 43.93243  ?  63  GLU   B O     1 
ATOM   1848 C  CB    . GLU   B 1 64  ? -28.98643 10.20714  40.11642  1.000 42.10028  ?  63  GLU   B CB    1 
ATOM   1849 C  CG    . GLU   B 1 64  ? -30.14352 10.76412  40.92983  1.000 44.43976  ?  63  GLU   B CG    1 
ATOM   1850 C  CD    . GLU   B 1 64  ? -30.47599 12.20808  40.58046  1.000 55.61071  ?  63  GLU   B CD    1 
ATOM   1851 O  OE1   . GLU   B 1 64  ? -29.53430 12.98484  40.28803  1.000 47.32115  ?  63  GLU   B OE1   1 
ATOM   1852 O  OE2   . GLU   B 1 64  ? -31.68415 12.55901  40.58270  1.000 61.33053  -1 63  GLU   B OE2   1 
ATOM   1853 N  N     . TYR   B 1 65  ? -25.61796 10.29009  39.44720  1.000 41.32159  ?  64  TYR   B N     1 
ATOM   1854 C  CA    . TYR   B 1 65  ? -24.64546 9.74698   38.50361  1.000 42.81651  ?  64  TYR   B CA    1 
ATOM   1855 C  C     . TYR   B 1 65  ? -23.20836 9.87888   39.01140  1.000 47.35611  ?  64  TYR   B C     1 
ATOM   1856 O  O     . TYR   B 1 65  ? -22.36094 10.46171  38.32755  1.000 39.63732  ?  64  TYR   B O     1 
ATOM   1857 C  CB    . TYR   B 1 65  ? -24.79130 10.44178  37.14270  1.000 40.31884  ?  64  TYR   B CB    1 
ATOM   1858 C  CG    . TYR   B 1 65  ? -26.23167 10.56027  36.66549  1.000 37.38674  ?  64  TYR   B CG    1 
ATOM   1859 C  CD1   . TYR   B 1 65  ? -26.94980 9.44401   36.26983  1.000 35.77619  ?  64  TYR   B CD1   1 
ATOM   1860 C  CD2   . TYR   B 1 65  ? -26.87611 11.79001  36.63943  1.000 34.67869  ?  64  TYR   B CD2   1 
ATOM   1861 C  CE1   . TYR   B 1 65  ? -28.26499 9.55244   35.85298  1.000 36.74736  ?  64  TYR   B CE1   1 
ATOM   1862 C  CE2   . TYR   B 1 65  ? -28.18306 11.90476  36.22768  1.000 34.15758  ?  64  TYR   B CE2   1 
ATOM   1863 C  CZ    . TYR   B 1 65  ? -28.87160 10.78439  35.82639  1.000 35.93674  ?  64  TYR   B CZ    1 
ATOM   1864 O  OH    . TYR   B 1 65  ? -30.17508 10.90606  35.42826  1.000 37.28953  ?  64  TYR   B OH    1 
ATOM   1865 N  N     . SER   B 1 66  ? -22.91259 9.32934   40.19472  1.000 41.60847  ?  65  SER   B N     1 
ATOM   1866 C  CA    . SER   B 1 66  ? -21.59178 9.52044   40.79726  1.000 45.64580  ?  65  SER   B CA    1 
ATOM   1867 C  C     . SER   B 1 66  ? -20.45900 9.03554   39.89311  1.000 46.15710  ?  65  SER   B C     1 
ATOM   1868 O  O     . SER   B 1 66  ? -19.45944 9.73961   39.71124  1.000 45.86278  ?  65  SER   B O     1 
ATOM   1869 C  CB    . SER   B 1 66  ? -21.51962 8.81223   42.15200  1.000 54.95064  ?  65  SER   B CB    1 
ATOM   1870 O  OG    . SER   B 1 66  ? -22.64592 9.14671   42.95717  1.000 53.15712  ?  65  SER   B OG    1 
ATOM   1871 N  N     . ALA   B 1 67  ? -20.58731 7.83125   39.32839  1.000 40.52832  ?  66  ALA   B N     1 
ATOM   1872 C  CA    . ALA   B 1 67  ? -19.49856 7.22379   38.56865  1.000 41.83309  ?  66  ALA   B CA    1 
ATOM   1873 C  C     . ALA   B 1 67  ? -19.19196 7.97207   37.28610  1.000 50.02214  ?  66  ALA   B C     1 
ATOM   1874 O  O     . ALA   B 1 67  ? -18.09124 7.81532   36.74471  1.000 50.16846  ?  66  ALA   B O     1 
ATOM   1875 C  CB    . ALA   B 1 67  ? -19.82459 5.76742   38.23055  1.000 45.16790  ?  66  ALA   B CB    1 
ATOM   1876 N  N     . MET   B 1 68  ? -20.13637 8.76632   36.78323  1.000 41.85919  ?  67  MET   B N     1 
ATOM   1877 C  CA    . MET   B 1 68  ? -19.87703 9.57474   35.60744  1.000 41.36735  ?  67  MET   B CA    1 
ATOM   1878 C  C     . MET   B 1 68  ? -18.86297 10.69103  35.87903  1.000 41.82789  ?  67  MET   B C     1 
ATOM   1879 O  O     . MET   B 1 68  ? -18.23915 11.19333  34.93568  1.000 38.88936  ?  67  MET   B O     1 
ATOM   1880 C  CB    . MET   B 1 68  ? -21.20167 10.13266  35.09497  1.000 41.45414  ?  67  MET   B CB    1 
ATOM   1881 C  CG    . MET   B 1 68  ? -22.20105 9.05524   34.66537  1.000 42.41267  ?  67  MET   B CG    1 
ATOM   1882 S  SD    . MET   B 1 68  ? -21.66834 8.19506   33.16443  1.000 46.22143  ?  67  MET   B SD    1 
ATOM   1883 C  CE    . MET   B 1 68  ? -21.35113 9.58115   32.06280  1.000 41.85486  ?  67  MET   B CE    1 
ATOM   1884 N  N     . ARG   B 1 69  ? -18.65846 11.06806  37.14363  1.000 41.23494  ?  68  ARG   B N     1 
ATOM   1885 C  CA    . ARG   B 1 69  ? -17.72729 12.14967  37.44958  1.000 42.81944  ?  68  ARG   B CA    1 
ATOM   1886 C  C     . ARG   B 1 69  ? -16.28283 11.73779  37.21594  1.000 41.71062  ?  68  ARG   B C     1 
ATOM   1887 O  O     . ARG   B 1 69  ? -15.42855 12.59765  36.96491  1.000 35.83603  ?  68  ARG   B O     1 
ATOM   1888 C  CB    . ARG   B 1 69  ? -17.88330 12.61327  38.90348  1.000 38.30269  ?  68  ARG   B CB    1 
ATOM   1889 C  CG    . ARG   B 1 69  ? -19.26906 13.08521  39.31874  1.000 42.10180  ?  68  ARG   B CG    1 
ATOM   1890 C  CD    . ARG   B 1 69  ? -19.20874 13.83961  40.65960  1.000 40.20746  ?  68  ARG   B CD    1 
ATOM   1891 N  NE    . ARG   B 1 69  ? -19.90769 13.14395  41.73161  1.000 48.48184  ?  68  ARG   B NE    1 
ATOM   1892 C  CZ    . ARG   B 1 69  ? -21.17133 13.36718  42.06437  1.000 50.38312  ?  68  ARG   B CZ    1 
ATOM   1893 N  NH1   . ARG   B 1 69  ? -21.89530 14.29531  41.45468  1.000 56.42941  ?  68  ARG   B NH1   1 
ATOM   1894 N  NH2   . ARG   B 1 69  ? -21.72677 12.63496  43.02257  1.000 51.93185  ?  68  ARG   B NH2   1 
ATOM   1895 N  N     . ASP   B 1 70  ? -15.99643 10.43576  37.29394  1.000 46.50435  ?  69  ASP   B N     1 
ATOM   1896 C  CA    . ASP   B 1 70  ? -14.61559 9.96212   37.35655  1.000 45.87579  ?  69  ASP   B CA    1 
ATOM   1897 C  C     . ASP   B 1 70  ? -13.77472 10.46522  36.18675  1.000 46.91918  ?  69  ASP   B C     1 
ATOM   1898 O  O     . ASP   B 1 70  ? -12.60120 10.81711  36.36789  1.000 42.32171  ?  69  ASP   B O     1 
ATOM   1899 C  CB    . ASP   B 1 70  ? -14.58984 8.42857   37.40908  1.000 48.31504  ?  69  ASP   B CB    1 
ATOM   1900 C  CG    . ASP   B 1 70  ? -15.14156 7.85895   38.73086  1.000 57.69169  ?  69  ASP   B CG    1 
ATOM   1901 O  OD1   . ASP   B 1 70  ? -15.72191 8.61602   39.55363  1.000 50.61578  ?  69  ASP   B OD1   1 
ATOM   1902 O  OD2   . ASP   B 1 70  ? -14.99416 6.63107   38.94119  1.000 60.59113  -1 69  ASP   B OD2   1 
ATOM   1903 N  N     . GLN   B 1 71  ? -14.35106 10.51296  34.97522  1.000 50.19067  ?  70  GLN   B N     1 
ATOM   1904 C  CA    . GLN   B 1 71  ? -13.53584 10.85741  33.80899  1.000 46.29446  ?  70  GLN   B CA    1 
ATOM   1905 C  C     . GLN   B 1 71  ? -13.14040 12.33017  33.80111  1.000 42.77451  ?  70  GLN   B C     1 
ATOM   1906 O  O     . GLN   B 1 71  ? -12.01895 12.67162  33.40757  1.000 41.85809  ?  70  GLN   B O     1 
ATOM   1907 C  CB    . GLN   B 1 71  ? -14.24884 10.50174  32.50771  1.000 47.88599  ?  70  GLN   B CB    1 
ATOM   1908 C  CG    . GLN   B 1 71  ? -13.40483 10.82882  31.26470  1.000 58.06234  ?  70  GLN   B CG    1 
ATOM   1909 C  CD    . GLN   B 1 71  ? -12.00193 10.18878  31.28347  1.000 59.02568  ?  70  GLN   B CD    1 
ATOM   1910 O  OE1   . GLN   B 1 71  ? -11.85356 8.99028   31.55124  1.000 54.48853  ?  70  GLN   B OE1   1 
ATOM   1911 N  NE2   . GLN   B 1 71  ? -10.97341 10.99278  31.00148  1.000 51.62283  ?  70  GLN   B NE2   1 
ATOM   1912 N  N     . TYR   B 1 72  ? -14.02819 13.22773  34.21773  1.000 38.98561  ?  71  TYR   B N     1 
ATOM   1913 C  CA    . TYR   B 1 72  ? -13.57491 14.60901  34.21800  1.000 42.97887  ?  71  TYR   B CA    1 
ATOM   1914 C  C     . TYR   B 1 72  ? -12.66426 14.91708  35.40331  1.000 36.43542  ?  71  TYR   B C     1 
ATOM   1915 O  O     . TYR   B 1 72  ? -11.81693 15.80917  35.29569  1.000 36.92608  ?  71  TYR   B O     1 
ATOM   1916 C  CB    . TYR   B 1 72  ? -14.75947 15.58345  34.12174  1.000 35.44410  ?  71  TYR   B CB    1 
ATOM   1917 C  CG    . TYR   B 1 72  ? -15.75927 15.66009  35.25583  1.000 31.52305  ?  71  TYR   B CG    1 
ATOM   1918 C  CD1   . TYR   B 1 72  ? -15.37722 16.06950  36.53090  1.000 35.21536  ?  71  TYR   B CD1   1 
ATOM   1919 C  CD2   . TYR   B 1 72  ? -17.11050 15.41394  35.02534  1.000 37.76688  ?  71  TYR   B CD2   1 
ATOM   1920 C  CE1   . TYR   B 1 72  ? -16.30247 16.17358  37.55837  1.000 34.94161  ?  71  TYR   B CE1   1 
ATOM   1921 C  CE2   . TYR   B 1 72  ? -18.04749 15.52054  36.04167  1.000 36.76653  ?  71  TYR   B CE2   1 
ATOM   1922 C  CZ    . TYR   B 1 72  ? -17.63306 15.89943  37.30852  1.000 30.20340  ?  71  TYR   B CZ    1 
ATOM   1923 O  OH    . TYR   B 1 72  ? -18.54886 16.00645  38.31929  1.000 39.17139  ?  71  TYR   B OH    1 
ATOM   1924 N  N     . MET   B 1 73  ? -12.77123 14.16622  36.50393  1.000 38.54203  ?  72  MET   B N     1 
ATOM   1925 C  CA    . MET   B 1 73  ? -11.82351 14.36339  37.59619  1.000 38.47482  ?  72  MET   B CA    1 
ATOM   1926 C  C     . MET   B 1 73  ? -10.41129 13.95398  37.19599  1.000 40.68746  ?  72  MET   B C     1 
ATOM   1927 O  O     . MET   B 1 73  ? -9.44322  14.56234  37.67355  1.000 39.82201  ?  72  MET   B O     1 
ATOM   1928 C  CB    . MET   B 1 73  ? -12.27580 13.59583  38.83729  1.000 39.25599  ?  72  MET   B CB    1 
ATOM   1929 C  CG    . MET   B 1 73  ? -13.48462 14.21149  39.51194  1.000 39.35903  ?  72  MET   B CG    1 
ATOM   1930 S  SD    . MET   B 1 73  ? -14.15473 13.19942  40.83624  1.000 43.04519  ?  72  MET   B SD    1 
ATOM   1931 C  CE    . MET   B 1 73  ? -15.39370 14.32535  41.46979  1.000 37.28690  ?  72  MET   B CE    1 
ATOM   1932 N  N     . ARG   B 1 74  ? -10.27821 12.94952  36.30998  1.000 39.23989  ?  73  ARG   B N     1 
ATOM   1933 C  CA    . ARG   B 1 74  ? -8.96209  12.53982  35.81559  1.000 41.02226  ?  73  ARG   B CA    1 
ATOM   1934 C  C     . ARG   B 1 74  ? -8.34630  13.59804  34.90637  1.000 36.79732  ?  73  ARG   B C     1 
ATOM   1935 O  O     . ARG   B 1 74  ? -7.12558  13.77855  34.88991  1.000 40.03877  ?  73  ARG   B O     1 
ATOM   1936 C  CB    . ARG   B 1 74  ? -9.05381  11.20593  35.05979  1.000 45.35479  ?  73  ARG   B CB    1 
ATOM   1937 C  CG    . ARG   B 1 74  ? -8.77370  9.93341   35.91101  1.000 52.67633  ?  73  ARG   B CG    1 
ATOM   1938 C  CD    . ARG   B 1 74  ? -8.65777  8.64553   35.06429  1.000 51.23228  ?  73  ARG   B CD    1 
ATOM   1939 N  NE    . ARG   B 1 74  ? -9.84198  8.40900   34.23482  1.000 49.21367  ?  73  ARG   B NE    1 
ATOM   1940 C  CZ    . ARG   B 1 74  ? -10.92302 7.73931   34.63492  1.000 60.26395  ?  73  ARG   B CZ    1 
ATOM   1941 N  NH1   . ARG   B 1 74  ? -11.00966 7.23701   35.85934  1.000 52.21677  ?  73  ARG   B NH1   1 
ATOM   1942 N  NH2   . ARG   B 1 74  ? -11.94244 7.56499   33.77650  1.000 49.37337  ?  73  ARG   B NH2   1 
ATOM   1943 N  N     . THR   B 1 75  ? -9.16094  14.29456  34.11837  1.000 37.85337  ?  74  THR   B N     1 
ATOM   1944 C  CA    . THR   B 1 75  ? -8.59585  15.28477  33.20976  1.000 39.53219  ?  74  THR   B CA    1 
ATOM   1945 C  C     . THR   B 1 75  ? -8.44749  16.65431  33.85812  1.000 41.18604  ?  74  THR   B C     1 
ATOM   1946 O  O     . THR   B 1 75  ? -7.64934  17.46482  33.37490  1.000 37.97003  ?  74  THR   B O     1 
ATOM   1947 C  CB    . THR   B 1 75  ? -9.43813  15.41687  31.93741  1.000 40.50134  ?  74  THR   B CB    1 
ATOM   1948 O  OG1   . THR   B 1 75  ? -10.74989 15.89943  32.27347  1.000 50.53183  ?  74  THR   B OG1   1 
ATOM   1949 C  CG2   . THR   B 1 75  ? -9.56813  14.06922  31.22629  1.000 39.33098  ?  74  THR   B CG2   1 
ATOM   1950 N  N     . GLY   B 1 76  ? -9.15783  16.91445  34.95743  1.000 37.80075  ?  75  GLY   B N     1 
ATOM   1951 C  CA    . GLY   B 1 76  ? -9.05836  18.20284  35.61284  1.000 34.89109  ?  75  GLY   B CA    1 
ATOM   1952 C  C     . GLY   B 1 76  ? -7.74948  18.34146  36.37042  1.000 34.86473  ?  75  GLY   B C     1 
ATOM   1953 O  O     . GLY   B 1 76  ? -7.24023  17.38931  36.95529  1.000 34.85224  ?  75  GLY   B O     1 
ATOM   1954 N  N     . GLU   B 1 77  ? -7.19441  19.55194  36.33482  1.000 40.81028  ?  76  GLU   B N     1 
ATOM   1955 C  CA    . GLU   B 1 77  ? -5.97790  19.85799  37.09007  1.000 39.60609  ?  76  GLU   B CA    1 
ATOM   1956 C  C     . GLU   B 1 77  ? -6.27200  20.47348  38.45525  1.000 40.69734  ?  76  GLU   B C     1 
ATOM   1957 O  O     . GLU   B 1 77  ? -5.50971  20.26541  39.41376  1.000 39.47356  ?  76  GLU   B O     1 
ATOM   1958 C  CB    . GLU   B 1 77  ? -5.08709  20.81961  36.29686  1.000 34.51288  ?  76  GLU   B CB    1 
ATOM   1959 C  CG    . GLU   B 1 77  ? -4.52526  20.24681  35.02378  1.000 41.17183  ?  76  GLU   B CG    1 
ATOM   1960 C  CD    . GLU   B 1 77  ? -3.79094  21.29694  34.19928  1.000 45.45289  ?  76  GLU   B CD    1 
ATOM   1961 O  OE1   . GLU   B 1 77  ? -4.46666  22.14060  33.56898  1.000 38.77412  ?  76  GLU   B OE1   1 
ATOM   1962 O  OE2   . GLU   B 1 77  ? -2.53819  21.29091  34.20893  1.000 48.31165  -1 76  GLU   B OE2   1 
ATOM   1963 N  N     . GLY   B 1 78  ? -7.34554  21.23377  38.55953  1.000 31.59072  ?  77  GLY   B N     1 
ATOM   1964 C  CA    . GLY   B 1 78  ? -7.68730  21.87508  39.81464  1.000 35.07127  ?  77  GLY   B CA    1 
ATOM   1965 C  C     . GLY   B 1 78  ? -9.18333  22.03123  39.90253  1.000 36.90505  ?  77  GLY   B C     1 
ATOM   1966 O  O     . GLY   B 1 78  ? -9.87565  22.13346  38.88024  1.000 32.89362  ?  77  GLY   B O     1 
ATOM   1967 N  N     . PHE   B 1 79  ? -9.68782  22.06933  41.13654  1.000 32.31774  ?  78  PHE   B N     1 
ATOM   1968 C  CA    . PHE   B 1 79  ? -11.11089 21.93723  41.39642  1.000 27.21990  ?  78  PHE   B CA    1 
ATOM   1969 C  C     . PHE   B 1 79  ? -11.58430 23.04079  42.32374  1.000 31.60905  ?  78  PHE   B C     1 
ATOM   1970 O  O     . PHE   B 1 79  ? -10.99958 23.25454  43.39006  1.000 34.44611  ?  78  PHE   B O     1 
ATOM   1971 C  CB    . PHE   B 1 79  ? -11.41250 20.56520  41.98729  1.000 33.63907  ?  78  PHE   B CB    1 
ATOM   1972 C  CG    . PHE   B 1 79  ? -10.97942 19.42964  41.10872  1.000 35.16967  ?  78  PHE   B CG    1 
ATOM   1973 C  CD1   . PHE   B 1 79  ? -9.64955  19.02455  41.07585  1.000 29.66493  ?  78  PHE   B CD1   1 
ATOM   1974 C  CD2   . PHE   B 1 79  ? -11.89913 18.78101  40.29146  1.000 29.32805  ?  78  PHE   B CD2   1 
ATOM   1975 C  CE1   . PHE   B 1 79  ? -9.25036  17.99096  40.25621  1.000 36.58199  ?  78  PHE   B CE1   1 
ATOM   1976 C  CE2   . PHE   B 1 79  ? -11.50781 17.74963  39.48197  1.000 29.42737  ?  78  PHE   B CE2   1 
ATOM   1977 C  CZ    . PHE   B 1 79  ? -10.17849 17.35111  39.45349  1.000 34.84778  ?  78  PHE   B CZ    1 
ATOM   1978 N  N     . LEU   B 1 80  ? -12.63330 23.74259  41.91219  1.000 28.63591  ?  79  LEU   B N     1 
ATOM   1979 C  CA    . LEU   B 1 80  ? -13.39217 24.60242  42.81001  1.000 33.28358  ?  79  LEU   B CA    1 
ATOM   1980 C  C     . LEU   B 1 80  ? -14.48202 23.76215  43.46564  1.000 37.41061  ?  79  LEU   B C     1 
ATOM   1981 O  O     . LEU   B 1 80  ? -15.41114 23.31066  42.78654  1.000 35.07782  ?  79  LEU   B O     1 
ATOM   1982 C  CB    . LEU   B 1 80  ? -14.02768 25.76213  42.06106  1.000 26.71983  ?  79  LEU   B CB    1 
ATOM   1983 C  CG    . LEU   B 1 80  ? -13.33856 27.06437  41.68182  1.000 34.39798  ?  79  LEU   B CG    1 
ATOM   1984 C  CD1   . LEU   B 1 80  ? -14.47233 28.06617  41.36183  1.000 29.21225  ?  79  LEU   B CD1   1 
ATOM   1985 C  CD2   . LEU   B 1 80  ? -12.44380 27.55914  42.79142  1.000 35.56402  ?  79  LEU   B CD2   1 
ATOM   1986 N  N     . CYS   B 1 81  ? -14.38098 23.54447  44.77666  1.000 33.12582  ?  80  CYS   B N     1 
ATOM   1987 C  CA    . CYS   B 1 81  ? -15.39509 22.79712  45.51196  1.000 31.93099  ?  80  CYS   B CA    1 
ATOM   1988 C  C     . CYS   B 1 81  ? -16.34833 23.79402  46.15270  1.000 32.93111  ?  80  CYS   B C     1 
ATOM   1989 O  O     . CYS   B 1 81  ? -15.98746 24.48532  47.10498  1.000 35.80302  ?  80  CYS   B O     1 
ATOM   1990 C  CB    . CYS   B 1 81  ? -14.74933 21.87931  46.53802  1.000 34.31286  ?  80  CYS   B CB    1 
ATOM   1991 S  SG    . CYS   B 1 81  ? -13.62584 20.68064  45.78642  1.000 38.24228  ?  80  CYS   B SG    1 
ATOM   1992 N  N     . VAL   B 1 82  ? -17.56154 23.86990  45.62734  1.000 33.97448  ?  81  VAL   B N     1 
ATOM   1993 C  CA    . VAL   B 1 82  ? -18.49170 24.94711  45.93645  1.000 37.32535  ?  81  VAL   B CA    1 
ATOM   1994 C  C     . VAL   B 1 82  ? -19.61673 24.40546  46.80926  1.000 42.25517  ?  81  VAL   B C     1 
ATOM   1995 O  O     . VAL   B 1 82  ? -20.21383 23.36603  46.49738  1.000 39.05489  ?  81  VAL   B O     1 
ATOM   1996 C  CB    . VAL   B 1 82  ? -19.06322 25.56621  44.64931  1.000 36.25538  ?  81  VAL   B CB    1 
ATOM   1997 C  CG1   . VAL   B 1 82  ? -19.95235 26.76429  44.97967  1.000 38.30801  ?  81  VAL   B CG1   1 
ATOM   1998 C  CG2   . VAL   B 1 82  ? -17.94522 25.93391  43.66247  1.000 36.10447  ?  81  VAL   B CG2   1 
ATOM   1999 N  N     . PHE   B 1 83  ? -19.91813 25.11386  47.89580  1.000 44.60212  ?  82  PHE   B N     1 
ATOM   2000 C  CA    . PHE   B 1 83  ? -21.14474 24.90448  48.64860  1.000 46.39143  ?  82  PHE   B CA    1 
ATOM   2001 C  C     . PHE   B 1 83  ? -21.83795 26.24737  48.79907  1.000 47.21155  ?  82  PHE   B C     1 
ATOM   2002 O  O     . PHE   B 1 83  ? -21.27151 27.29483  48.48841  1.000 49.15203  ?  82  PHE   B O     1 
ATOM   2003 C  CB    . PHE   B 1 83  ? -20.86988 24.28382  50.02074  1.000 45.82121  ?  82  PHE   B CB    1 
ATOM   2004 C  CG    . PHE   B 1 83  ? -20.21480 25.22240  50.98371  1.000 50.00775  ?  82  PHE   B CG    1 
ATOM   2005 C  CD1   . PHE   B 1 83  ? -18.84149 25.39475  50.97739  1.000 44.15665  ?  82  PHE   B CD1   1 
ATOM   2006 C  CD2   . PHE   B 1 83  ? -20.97851 25.93439  51.90362  1.000 52.76805  ?  82  PHE   B CD2   1 
ATOM   2007 C  CE1   . PHE   B 1 83  ? -18.23380 26.26379  51.86955  1.000 52.80016  ?  82  PHE   B CE1   1 
ATOM   2008 C  CE2   . PHE   B 1 83  ? -20.38406 26.80386  52.79220  1.000 53.33156  ?  82  PHE   B CE2   1 
ATOM   2009 C  CZ    . PHE   B 1 83  ? -19.00610 26.96799  52.77874  1.000 48.56983  ?  82  PHE   B CZ    1 
ATOM   2010 N  N     . ALA   B 1 84  ? -23.07282 26.22406  49.27737  1.000 43.72118  ?  83  ALA   B N     1 
ATOM   2011 C  CA    . ALA   B 1 84  ? -23.80388 27.44837  49.55935  1.000 46.82369  ?  83  ALA   B CA    1 
ATOM   2012 C  C     . ALA   B 1 84  ? -23.93085 27.61778  51.07132  1.000 52.72732  ?  83  ALA   B C     1 
ATOM   2013 O  O     . ALA   B 1 84  ? -24.03396 26.63221  51.81005  1.000 52.71832  ?  83  ALA   B O     1 
ATOM   2014 C  CB    . ALA   B 1 84  ? -25.17911 27.44001  48.88737  1.000 51.68752  ?  83  ALA   B CB    1 
ATOM   2015 N  N     . ILE   B 1 85  ? -23.90029 28.87200  51.53010  1.000 49.91210  ?  84  ILE   B N     1 
ATOM   2016 C  CA    . ILE   B 1 85  ? -23.86945 29.15422  52.96242  1.000 61.29568  ?  84  ILE   B CA    1 
ATOM   2017 C  C     . ILE   B 1 85  ? -25.22339 28.97105  53.63089  1.000 59.25493  ?  84  ILE   B C     1 
ATOM   2018 O  O     . ILE   B 1 85  ? -25.28859 28.87974  54.86004  1.000 60.18701  ?  84  ILE   B O     1 
ATOM   2019 C  CB    . ILE   B 1 85  ? -23.36118 30.58623  53.22596  1.000 54.86269  ?  84  ILE   B CB    1 
ATOM   2020 C  CG1   . ILE   B 1 85  ? -24.26256 31.60090  52.51709  1.000 58.41125  ?  84  ILE   B CG1   1 
ATOM   2021 C  CG2   . ILE   B 1 85  ? -21.90074 30.71730  52.81000  1.000 54.72063  ?  84  ILE   B CG2   1 
ATOM   2022 C  CD1   . ILE   B 1 85  ? -24.24997 32.97734  53.15140  1.000 66.33480  ?  84  ILE   B CD1   1 
ATOM   2023 N  N     . ASN   B 1 86  ? -26.30409 28.92466  52.85234  1.000 55.86807  ?  85  ASN   B N     1 
ATOM   2024 C  CA    . ASN   B 1 86  ? -27.64195 28.65353  53.35981  1.000 66.01914  ?  85  ASN   B CA    1 
ATOM   2025 C  C     . ASN   B 1 86  ? -28.07744 27.20500  53.12304  1.000 61.95844  ?  85  ASN   B C     1 
ATOM   2026 O  O     . ASN   B 1 86  ? -29.28007 26.91578  53.13623  1.000 59.92382  ?  85  ASN   B O     1 
ATOM   2027 C  CB    . ASN   B 1 86  ? -28.64521 29.61287  52.71810  1.000 62.09145  ?  85  ASN   B CB    1 
ATOM   2028 C  CG    . ASN   B 1 86  ? -28.71161 29.45396  51.21524  1.000 59.35671  ?  85  ASN   B CG    1 
ATOM   2029 O  OD1   . ASN   B 1 86  ? -27.80158 28.89352  50.61124  1.000 56.79683  ?  85  ASN   B OD1   1 
ATOM   2030 N  ND2   . ASN   B 1 86  ? -29.78758 29.93873  50.60304  1.000 56.62080  ?  85  ASN   B ND2   1 
ATOM   2031 N  N     . ASN   B 1 87  ? -27.12393 26.28980  52.91018  1.000 58.22022  ?  86  ASN   B N     1 
ATOM   2032 C  CA    . ASN   B 1 87  ? -27.41440 24.90751  52.50567  1.000 58.41255  ?  86  ASN   B CA    1 
ATOM   2033 C  C     . ASN   B 1 87  ? -26.40886 23.99304  53.21145  1.000 57.64697  ?  86  ASN   B C     1 
ATOM   2034 O  O     . ASN   B 1 87  ? -25.32740 23.71482  52.68726  1.000 51.99129  ?  86  ASN   B O     1 
ATOM   2035 C  CB    . ASN   B 1 87  ? -27.36152 24.76417  50.98216  1.000 58.90684  ?  86  ASN   B CB    1 
ATOM   2036 C  CG    . ASN   B 1 87  ? -27.86290 23.40810  50.49175  1.000 59.02191  ?  86  ASN   B CG    1 
ATOM   2037 O  OD1   . ASN   B 1 87  ? -27.66893 22.38245  51.14799  1.000 54.56300  ?  86  ASN   B OD1   1 
ATOM   2038 N  ND2   . ASN   B 1 87  ? -28.50095 23.40098  49.32232  1.000 59.38943  ?  86  ASN   B ND2   1 
ATOM   2039 N  N     . THR   B 1 88  ? -26.79115 23.50940  54.39733  1.000 58.09729  ?  87  THR   B N     1 
ATOM   2040 C  CA    . THR   B 1 88  ? -25.88726 22.70261  55.21629  1.000 61.13216  ?  87  THR   B CA    1 
ATOM   2041 C  C     . THR   B 1 88  ? -25.56072 21.36955  54.55417  1.000 57.04453  ?  87  THR   B C     1 
ATOM   2042 O  O     . THR   B 1 88  ? -24.44941 20.84483  54.70251  1.000 56.51026  ?  87  THR   B O     1 
ATOM   2043 C  CB    . THR   B 1 88  ? -26.51117 22.46038  56.58943  1.000 63.81640  ?  87  THR   B CB    1 
ATOM   2044 O  OG1   . THR   B 1 88  ? -26.95096 23.70830  57.13708  1.000 66.11930  ?  87  THR   B OG1   1 
ATOM   2045 C  CG2   . THR   B 1 88  ? -25.49530 21.81883  57.52071  1.000 65.47186  ?  87  THR   B CG2   1 
ATOM   2046 N  N     . LYS   B 1 89  ? -26.53335 20.78269  53.86011  1.000 57.01571  ?  88  LYS   B N     1 
ATOM   2047 C  CA    . LYS   B 1 89  ? -26.26035 19.56681  53.10919  1.000 58.89848  ?  88  LYS   B CA    1 
ATOM   2048 C  C     . LYS   B 1 89  ? -25.15363 19.80930  52.08827  1.000 55.17394  ?  88  LYS   B C     1 
ATOM   2049 O  O     . LYS   B 1 89  ? -24.21709 19.00827  51.97101  1.000 50.62512  ?  88  LYS   B O     1 
ATOM   2050 C  CB    . LYS   B 1 89  ? -27.54943 19.08830  52.43974  1.000 56.24200  ?  88  LYS   B CB    1 
ATOM   2051 C  CG    . LYS   B 1 89  ? -27.45067 17.79691  51.64084  1.000 56.93826  ?  88  LYS   B CG    1 
ATOM   2052 C  CD    . LYS   B 1 89  ? -26.99194 16.61873  52.48627  1.000 58.64017  ?  88  LYS   B CD    1 
ATOM   2053 C  CE    . LYS   B 1 89  ? -27.26715 15.29993  51.75975  1.000 65.69103  ?  88  LYS   B CE    1 
ATOM   2054 N  NZ    . LYS   B 1 89  ? -26.80329 15.31867  50.32945  1.000 60.46423  ?  88  LYS   B NZ    1 
ATOM   2055 N  N     . SER   B 1 90  ? -25.21728 20.94111  51.37894  1.000 51.32522  ?  89  SER   B N     1 
ATOM   2056 C  CA    . SER   B 1 90  ? -24.19745 21.22088  50.37389  1.000 57.38971  ?  89  SER   B CA    1 
ATOM   2057 C  C     . SER   B 1 90  ? -22.81679 21.35329  51.01100  1.000 50.72908  ?  89  SER   B C     1 
ATOM   2058 O  O     . SER   B 1 90  ? -21.81407 20.99094  50.38582  1.000 44.82077  ?  89  SER   B O     1 
ATOM   2059 C  CB    . SER   B 1 90  ? -24.57448 22.46942  49.56909  1.000 53.33318  ?  89  SER   B CB    1 
ATOM   2060 O  OG    . SER   B 1 90  ? -24.33966 23.66672  50.29091  1.000 52.75121  ?  89  SER   B OG    1 
ATOM   2061 N  N     . PHE   B 1 91  ? -22.74963 21.80603  52.26882  1.000 48.73564  ?  90  PHE   B N     1 
ATOM   2062 C  CA    . PHE   B 1 91  ? -21.47032 21.82530  52.97464  1.000 51.79031  ?  90  PHE   B CA    1 
ATOM   2063 C  C     . PHE   B 1 91  ? -21.04320 20.41985  53.38105  1.000 50.72009  ?  90  PHE   B C     1 
ATOM   2064 O  O     . PHE   B 1 91  ? -19.85319 20.08503  53.32376  1.000 49.96737  ?  90  PHE   B O     1 
ATOM   2065 C  CB    . PHE   B 1 91  ? -21.54769 22.74334  54.20366  1.000 55.76919  ?  90  PHE   B CB    1 
ATOM   2066 C  CG    . PHE   B 1 91  ? -20.24327 22.87536  54.94843  1.000 54.77105  ?  90  PHE   B CG    1 
ATOM   2067 C  CD1   . PHE   B 1 91  ? -19.13629 23.43468  54.33281  1.000 55.13632  ?  90  PHE   B CD1   1 
ATOM   2068 C  CD2   . PHE   B 1 91  ? -20.12515 22.44647  56.26352  1.000 62.28199  ?  90  PHE   B CD2   1 
ATOM   2069 C  CE1   . PHE   B 1 91  ? -17.92950 23.55828  55.00691  1.000 61.47603  ?  90  PHE   B CE1   1 
ATOM   2070 C  CE2   . PHE   B 1 91  ? -18.92418 22.56338  56.94714  1.000 59.68169  ?  90  PHE   B CE2   1 
ATOM   2071 C  CZ    . PHE   B 1 91  ? -17.82291 23.12083  56.32226  1.000 64.78479  ?  90  PHE   B CZ    1 
ATOM   2072 N  N     . GLU   B 1 92  ? -21.99628 19.58415  53.80848  1.000 53.92939  ?  91  GLU   B N     1 
ATOM   2073 C  CA    . GLU   B 1 92  ? -21.65268 18.20570  54.14406  1.000 57.39454  ?  91  GLU   B CA    1 
ATOM   2074 C  C     . GLU   B 1 92  ? -21.19039 17.44140  52.91212  1.000 54.88599  ?  91  GLU   B C     1 
ATOM   2075 O  O     . GLU   B 1 92  ? -20.26302 16.62640  52.99983  1.000 58.46243  ?  91  GLU   B O     1 
ATOM   2076 C  CB    . GLU   B 1 92  ? -22.84551 17.50916  54.80532  1.000 60.94981  ?  91  GLU   B CB    1 
ATOM   2077 C  CG    . GLU   B 1 92  ? -23.27437 18.15537  56.12780  1.000 64.78559  ?  91  GLU   B CG    1 
ATOM   2078 C  CD    . GLU   B 1 92  ? -24.62516 17.65363  56.64811  1.000 71.87305  ?  91  GLU   B CD    1 
ATOM   2079 O  OE1   . GLU   B 1 92  ? -25.33232 16.93127  55.90562  1.000 66.94799  ?  91  GLU   B OE1   1 
ATOM   2080 O  OE2   . GLU   B 1 92  ? -24.97767 17.99105  57.80332  1.000 67.33080  -1 91  GLU   B OE2   1 
ATOM   2081 N  N     . ASP   B 1 93  ? -21.78940 17.72657  51.75130  1.000 49.09742  ?  92  ASP   B N     1 
ATOM   2082 C  CA    . ASP   B 1 93  ? -21.42612 17.02645  50.52241  1.000 55.23009  ?  92  ASP   B CA    1 
ATOM   2083 C  C     . ASP   B 1 93  ? -19.97686 17.26545  50.10720  1.000 51.55651  ?  92  ASP   B C     1 
ATOM   2084 O  O     . ASP   B 1 93  ? -19.40429 16.41592  49.41719  1.000 51.47514  ?  92  ASP   B O     1 
ATOM   2085 C  CB    . ASP   B 1 93  ? -22.37600 17.42931  49.38861  1.000 47.41383  ?  92  ASP   B CB    1 
ATOM   2086 C  CG    . ASP   B 1 93  ? -23.77767 16.86321  49.57209  1.000 48.15662  ?  92  ASP   B CG    1 
ATOM   2087 O  OD1   . ASP   B 1 93  ? -23.89906 15.77200  50.17107  1.000 51.21264  ?  92  ASP   B OD1   1 
ATOM   2088 O  OD2   . ASP   B 1 93  ? -24.75476 17.50376  49.12190  1.000 44.14825  -1 92  ASP   B OD2   1 
ATOM   2089 N  N     . ILE   B 1 94  ? -19.36669 18.38293  50.52004  1.000 50.12791  ?  93  ILE   B N     1 
ATOM   2090 C  CA    . ILE   B 1 94  ? -18.00673 18.70609  50.07932  1.000 48.91847  ?  93  ILE   B CA    1 
ATOM   2091 C  C     . ILE   B 1 94  ? -17.04651 17.56165  50.38004  1.000 48.54878  ?  93  ILE   B C     1 
ATOM   2092 O  O     . ILE   B 1 94  ? -16.13527 17.27618  49.59419  1.000 45.02204  ?  93  ILE   B O     1 
ATOM   2093 C  CB    . ILE   B 1 94  ? -17.52834 20.02302  50.72131  1.000 51.31251  ?  93  ILE   B CB    1 
ATOM   2094 C  CG1   . ILE   B 1 94  ? -18.38347 21.20166  50.24595  1.000 49.94624  ?  93  ILE   B CG1   1 
ATOM   2095 C  CG2   . ILE   B 1 94  ? -16.05852 20.28022  50.39594  1.000 46.44063  ?  93  ILE   B CG2   1 
ATOM   2096 C  CD1   . ILE   B 1 94  ? -18.05998 21.65383  48.83114  1.000 38.72391  ?  93  ILE   B CD1   1 
ATOM   2097 N  N     . HIS   B 1 95  ? -17.24503 16.88048  51.51099  1.000 52.59182  ?  94  HIS   B N     1 
ATOM   2098 C  CA    . HIS   B 1 95  ? -16.33267 15.81645  51.92757  1.000 55.54322  ?  94  HIS   B CA    1 
ATOM   2099 C  C     . HIS   B 1 95  ? -16.24257 14.71619  50.87537  1.000 51.73863  ?  94  HIS   B C     1 
ATOM   2100 O  O     . HIS   B 1 95  ? -15.14828 14.25573  50.52269  1.000 49.59472  ?  94  HIS   B O     1 
ATOM   2101 C  CB    . HIS   B 1 95  ? -16.79174 15.24154  53.27499  1.000 55.37093  ?  94  HIS   B CB    1 
ATOM   2102 C  CG    . HIS   B 1 95  ? -16.16740 13.92308  53.61663  1.000 55.26274  ?  94  HIS   B CG    1 
ATOM   2103 N  ND1   . HIS   B 1 95  ? -14.82132 13.78008  53.87713  1.000 56.88719  ?  94  HIS   B ND1   1 
ATOM   2104 C  CD2   . HIS   B 1 95  ? -16.70514 12.68577  53.73050  1.000 56.65415  ?  94  HIS   B CD2   1 
ATOM   2105 C  CE1   . HIS   B 1 95  ? -14.55663 12.51227  54.13799  1.000 60.98624  ?  94  HIS   B CE1   1 
ATOM   2106 N  NE2   . HIS   B 1 95  ? -15.68311 11.82749  54.05804  1.000 59.82644  ?  94  HIS   B NE2   1 
ATOM   2107 N  N     . HIS   B 1 96  ? -17.39023 14.28733  50.35775  1.000 51.34217  ?  95  HIS   B N     1 
ATOM   2108 C  CA    . HIS   B 1 96  ? -17.40777 13.18466  49.40438  1.000 51.46846  ?  95  HIS   B CA    1 
ATOM   2109 C  C     . HIS   B 1 96  ? -16.79203 13.59482  48.07059  1.000 47.63437  ?  95  HIS   B C     1 
ATOM   2110 O  O     . HIS   B 1 96  ? -16.10602 12.79171  47.42686  1.000 43.65345  ?  95  HIS   B O     1 
ATOM   2111 C  CB    . HIS   B 1 96  ? -18.84562 12.69089  49.24739  1.000 48.52688  ?  95  HIS   B CB    1 
ATOM   2112 C  CG    . HIS   B 1 96  ? -19.52391 12.45617  50.56409  1.000 62.34947  ?  95  HIS   B CG    1 
ATOM   2113 N  ND1   . HIS   B 1 96  ? -19.24225 11.36425  51.36049  1.000 60.65180  ?  95  HIS   B ND1   1 
ATOM   2114 C  CD2   . HIS   B 1 96  ? -20.42650 13.19856  51.25062  1.000 63.42012  ?  95  HIS   B CD2   1 
ATOM   2115 C  CE1   . HIS   B 1 96  ? -19.96100 11.43082  52.46713  1.000 63.02698  ?  95  HIS   B CE1   1 
ATOM   2116 N  NE2   . HIS   B 1 96  ? -20.68774 12.53385  52.42627  1.000 65.16805  ?  95  HIS   B NE2   1 
ATOM   2117 N  N     . TYR   B 1 97  ? -17.00985 14.84315  47.64700  1.000 44.09782  ?  96  TYR   B N     1 
ATOM   2118 C  CA    . TYR   B 1 97  ? -16.33168 15.33880  46.45095  1.000 49.13653  ?  96  TYR   B CA    1 
ATOM   2119 C  C     . TYR   B 1 97  ? -14.82109 15.25447  46.60749  1.000 44.80056  ?  96  TYR   B C     1 
ATOM   2120 O  O     . TYR   B 1 97  ? -14.13304 14.67154  45.76272  1.000 42.69105  ?  96  TYR   B O     1 
ATOM   2121 C  CB    . TYR   B 1 97  ? -16.76293 16.77338  46.14291  1.000 39.44093  ?  96  TYR   B CB    1 
ATOM   2122 C  CG    . TYR   B 1 97  ? -18.08117 16.83334  45.43170  1.000 40.99078  ?  96  TYR   B CG    1 
ATOM   2123 C  CD1   . TYR   B 1 97  ? -18.19241 16.42696  44.10530  1.000 39.85883  ?  96  TYR   B CD1   1 
ATOM   2124 C  CD2   . TYR   B 1 97  ? -19.21641 17.28812  46.07155  1.000 40.73049  ?  96  TYR   B CD2   1 
ATOM   2125 C  CE1   . TYR   B 1 97  ? -19.40198 16.46806  43.44938  1.000 38.58170  ?  96  TYR   B CE1   1 
ATOM   2126 C  CE2   . TYR   B 1 97  ? -20.42813 17.33877  45.41611  1.000 41.06256  ?  96  TYR   B CE2   1 
ATOM   2127 C  CZ    . TYR   B 1 97  ? -20.51348 16.92408  44.10967  1.000 39.67666  ?  96  TYR   B CZ    1 
ATOM   2128 O  OH    . TYR   B 1 97  ? -21.72263 16.96822  43.46683  1.000 46.89331  ?  96  TYR   B OH    1 
ATOM   2129 N  N     . ARG   B 1 98  ? -14.28413 15.81613  47.69582  1.000 43.25432  ?  97  ARG   B N     1 
ATOM   2130 C  CA    . ARG   B 1 98  ? -12.83757 15.79367  47.87570  1.000 41.39529  ?  97  ARG   B CA    1 
ATOM   2131 C  C     . ARG   B 1 98  ? -12.31590 14.36553  47.90012  1.000 47.55522  ?  97  ARG   B C     1 
ATOM   2132 O  O     . ARG   B 1 98  ? -11.24836 14.07663  47.34777  1.000 46.89331  ?  97  ARG   B O     1 
ATOM   2133 C  CB    . ARG   B 1 98  ? -12.44039 16.53893  49.14986  1.000 50.60225  ?  97  ARG   B CB    1 
ATOM   2134 C  CG    . ARG   B 1 98  ? -10.94275 16.49967  49.41998  1.000 56.34457  ?  97  ARG   B CG    1 
ATOM   2135 C  CD    . ARG   B 1 98  ? -10.50382 17.51881  50.46377  1.000 57.92858  ?  97  ARG   B CD    1 
ATOM   2136 N  NE    . ARG   B 1 98  ? -9.19372  17.19072  51.01583  1.000 58.82250  ?  97  ARG   B NE    1 
ATOM   2137 C  CZ    . ARG   B 1 98  ? -8.04052  17.61493  50.51948  1.000 59.76189  ?  97  ARG   B CZ    1 
ATOM   2138 N  NH1   . ARG   B 1 98  ? -7.99374  18.42290  49.47347  1.000 63.67258  ?  97  ARG   B NH1   1 
ATOM   2139 N  NH2   . ARG   B 1 98  ? -6.90556  17.21131  51.08143  1.000 66.61302  ?  97  ARG   B NH2   1 
ATOM   2140 N  N     . GLU   B 1 99  ? -13.08115 13.44923  48.49613  1.000 49.17536  ?  98  GLU   B N     1 
ATOM   2141 C  CA    . GLU   B 1 99  ? -12.66699 12.05277  48.53154  1.000 50.54167  ?  98  GLU   B CA    1 
ATOM   2142 C  C     . GLU   B 1 99  ? -12.68527 11.43908  47.14164  1.000 51.32328  ?  98  GLU   B C     1 
ATOM   2143 O  O     . GLU   B 1 99  ? -11.73662 10.74366  46.75118  1.000 46.33535  ?  98  GLU   B O     1 
ATOM   2144 C  CB    . GLU   B 1 99  ? -13.56645 11.26177  49.48011  1.000 50.89244  ?  98  GLU   B CB    1 
ATOM   2145 C  CG    . GLU   B 1 99  ? -13.29484 11.53811  50.96145  1.000 60.73079  ?  98  GLU   B CG    1 
ATOM   2146 C  CD    . GLU   B 1 99  ? -11.88998 11.12122  51.38493  1.000 59.92382  ?  98  GLU   B CD    1 
ATOM   2147 O  OE1   . GLU   B 1 99  ? -11.43112 10.04319  50.94979  1.000 61.61854  ?  98  GLU   B OE1   1 
ATOM   2148 O  OE2   . GLU   B 1 99  ? -11.23647 11.87748  52.13445  1.000 63.62770  -1 98  GLU   B OE2   1 
ATOM   2149 N  N     . GLN   B 1 100 ? -13.75800 11.67735  46.38196  1.000 49.04996  ?  99  GLN   B N     1 
ATOM   2150 C  CA    . GLN   B 1 100 ? -13.80872 11.15553  45.01998  1.000 47.30604  ?  99  GLN   B CA    1 
ATOM   2151 C  C     . GLN   B 1 100 ? -12.61862 11.64573  44.20989  1.000 47.97217  ?  99  GLN   B C     1 
ATOM   2152 O  O     . GLN   B 1 100 ? -11.93022 10.84933  43.56384  1.000 50.74722  ?  99  GLN   B O     1 
ATOM   2153 C  CB    . GLN   B 1 100 ? -15.12084 11.54815  44.34564  1.000 47.21271  ?  99  GLN   B CB    1 
ATOM   2154 C  CG    . GLN   B 1 100 ? -15.43514 10.67445  43.15910  1.000 54.00597  ?  99  GLN   B CG    1 
ATOM   2155 C  CD    . GLN   B 1 100 ? -16.83669 10.86418  42.63139  1.000 54.79672  ?  99  GLN   B CD    1 
ATOM   2156 O  OE1   . GLN   B 1 100 ? -17.61483 11.66806  43.15021  1.000 48.55930  ?  99  GLN   B OE1   1 
ATOM   2157 N  NE2   . GLN   B 1 100 ? -17.16919 10.11535  41.58467  1.000 50.04367  ?  99  GLN   B NE2   1 
ATOM   2158 N  N     . ILE   B 1 101 ? -12.32731 12.94751  44.28592  1.000 47.93323  ?  100 ILE   B N     1 
ATOM   2159 C  CA    . ILE   B 1 101 ? -11.21953 13.52577  43.52778  1.000 47.71823  ?  100 ILE   B CA    1 
ATOM   2160 C  C     . ILE   B 1 101 ? -9.90321  12.86865  43.92020  1.000 51.88378  ?  100 ILE   B C     1 
ATOM   2161 O  O     . ILE   B 1 101 ? -9.11369  12.45548  43.05964  1.000 47.75658  ?  100 ILE   B O     1 
ATOM   2162 C  CB    . ILE   B 1 101 ? -11.16972 15.05114  43.73824  1.000 43.31551  ?  100 ILE   B CB    1 
ATOM   2163 C  CG1   . ILE   B 1 101 ? -12.41628 15.70868  43.15356  1.000 37.03161  ?  100 ILE   B CG1   1 
ATOM   2164 C  CG2   . ILE   B 1 101 ? -9.90174  15.63254  43.15487  1.000 39.82796  ?  100 ILE   B CG2   1 
ATOM   2165 C  CD1   . ILE   B 1 101 ? -12.67060 17.09214  43.67443  1.000 41.41944  ?  100 ILE   B CD1   1 
ATOM   2166 N  N     . LYS   B 1 102 ? -9.64712  12.77227  45.23080  1.000 45.67738  ?  101 LYS   B N     1 
ATOM   2167 C  CA    . LYS   B 1 102 ? -8.40554  12.17982  45.71722  1.000 54.58111  ?  101 LYS   B CA    1 
ATOM   2168 C  C     . LYS   B 1 102 ? -8.26546  10.72829  45.28456  1.000 53.72308  ?  101 LYS   B C     1 
ATOM   2169 O  O     . LYS   B 1 102 ? -7.15268  10.27473  45.00368  1.000 58.02096  ?  101 LYS   B O     1 
ATOM   2170 C  CB    . LYS   B 1 102 ? -8.32771  12.27763  47.24420  1.000 54.99740  ?  101 LYS   B CB    1 
ATOM   2171 C  CG    . LYS   B 1 102 ? -8.11686  13.68441  47.78917  1.000 57.21885  ?  101 LYS   B CG    1 
ATOM   2172 C  CD    . LYS   B 1 102 ? -7.89474  13.66397  49.30196  1.000 67.17660  ?  101 LYS   B CD    1 
ATOM   2173 C  CE    . LYS   B 1 102 ? -9.09727  13.08449  50.03962  1.000 61.53650  ?  101 LYS   B CE    1 
ATOM   2174 N  NZ    . LYS   B 1 102 ? -8.73781  12.53234  51.38018  1.000 60.89498  ?  101 LYS   B NZ    1 
ATOM   2175 N  N     . ARG   B 1 103 ? -9.37169  9.98458   45.23129  1.000 51.99393  ?  102 ARG   B N     1 
ATOM   2176 C  CA    . ARG   B 1 103 ? -9.30641  8.58512   44.82202  1.000 54.93843  ?  102 ARG   B CA    1 
ATOM   2177 C  C     . ARG   B 1 103 ? -9.08477  8.45056   43.32330  1.000 59.36937  ?  102 ARG   B C     1 
ATOM   2178 O  O     . ARG   B 1 103 ? -8.23817  7.66625   42.87935  1.000 58.04948  ?  102 ARG   B O     1 
ATOM   2179 C  CB    . ARG   B 1 103 ? -10.58605 7.85028   45.21535  1.000 54.40318  ?  102 ARG   B CB    1 
ATOM   2180 C  CG    . ARG   B 1 103 ? -10.65253 6.46755   44.59380  1.000 61.10835  ?  102 ARG   B CG    1 
ATOM   2181 C  CD    . ARG   B 1 103 ? -11.96199 5.76737   44.86421  1.000 66.68135  ?  102 ARG   B CD    1 
ATOM   2182 N  NE    . ARG   B 1 103 ? -13.04582 6.27341   44.03280  1.000 57.31874  ?  102 ARG   B NE    1 
ATOM   2183 C  CZ    . ARG   B 1 103 ? -14.05090 7.00501   44.48729  1.000 62.02726  ?  102 ARG   B CZ    1 
ATOM   2184 N  NH1   . ARG   B 1 103 ? -14.11569 7.37416   45.75822  1.000 63.44526  ?  102 ARG   B NH1   1 
ATOM   2185 N  NH2   . ARG   B 1 103 ? -15.02257 7.36265   43.65018  1.000 62.77729  ?  102 ARG   B NH2   1 
ATOM   2186 N  N     . VAL   B 1 104 ? -9.85654  9.19929   42.53253  1.000 57.50035  ?  103 VAL   B N     1 
ATOM   2187 C  CA    . VAL   B 1 104 ? -9.77328  9.09021   41.08134  1.000 58.79355  ?  103 VAL   B CA    1 
ATOM   2188 C  C     . VAL   B 1 104 ? -8.41322  9.56202   40.58643  1.000 57.97302  ?  103 VAL   B C     1 
ATOM   2189 O  O     . VAL   B 1 104 ? -7.82438  8.95818   39.68041  1.000 57.83217  ?  103 VAL   B O     1 
ATOM   2190 C  CB    . VAL   B 1 104 ? -10.92953 9.86956   40.42960  1.000 55.88336  ?  103 VAL   B CB    1 
ATOM   2191 C  CG1   . VAL   B 1 104 ? -10.79397 9.86083   38.92170  1.000 54.85265  ?  103 VAL   B CG1   1 
ATOM   2192 C  CG2   . VAL   B 1 104 ? -12.26137 9.26748   40.84645  1.000 55.50450  ?  103 VAL   B CG2   1 
ATOM   2193 N  N     . LYS   B 1 105 ? -7.87871  10.62549  41.18582  1.000 56.50747  ?  104 LYS   B N     1 
ATOM   2194 C  CA    . LYS   B 1 105 ? -6.55863  11.12223  40.82016  1.000 59.02873  ?  104 LYS   B CA    1 
ATOM   2195 C  C     . LYS   B 1 105 ? -5.43316  10.46602  41.60843  1.000 60.98287  ?  104 LYS   B C     1 
ATOM   2196 O  O     . LYS   B 1 105 ? -4.26471  10.63115  41.23758  1.000 62.25282  ?  104 LYS   B O     1 
ATOM   2197 C  CB    . LYS   B 1 105 ? -6.49206  12.64375  41.00596  1.000 52.78221  ?  104 LYS   B CB    1 
ATOM   2198 C  CG    . LYS   B 1 105 ? -7.60294  13.39216  40.28020  1.000 48.97203  ?  104 LYS   B CG    1 
ATOM   2199 C  CD    . LYS   B 1 105 ? -7.31496  14.87665  40.20213  1.000 51.84127  ?  104 LYS   B CD    1 
ATOM   2200 C  CE    . LYS   B 1 105 ? -6.08131  15.14007  39.33438  1.000 43.03087  ?  104 LYS   B CE    1 
ATOM   2201 N  NZ    . LYS   B 1 105 ? -6.28697  14.74751  37.90810  1.000 38.59852  ?  104 LYS   B NZ    1 
ATOM   2202 N  N     . ASP   B 1 106 ? -5.75719  9.73773   42.67952  1.000 67.17287  ?  105 ASP   B N     1 
ATOM   2203 C  CA    . ASP   B 1 106 ? -4.77943  8.99347   43.47617  1.000 69.40583  ?  105 ASP   B CA    1 
ATOM   2204 C  C     . ASP   B 1 106 ? -3.68301  9.91911   44.00912  1.000 66.92384  ?  105 ASP   B C     1 
ATOM   2205 O  O     . ASP   B 1 106 ? -2.50971  9.81787   43.64431  1.000 65.29289  ?  105 ASP   B O     1 
ATOM   2206 C  CB    . ASP   B 1 106 ? -4.18550  7.83613   42.66588  1.000 69.89067  ?  105 ASP   B CB    1 
ATOM   2207 C  CG    . ASP   B 1 106 ? -3.36769  6.88816   43.52047  1.000 81.38637  ?  105 ASP   B CG    1 
ATOM   2208 O  OD1   . ASP   B 1 106 ? -3.95869  6.23316   44.40579  1.000 80.24636  ?  105 ASP   B OD1   1 
ATOM   2209 O  OD2   . ASP   B 1 106 ? -2.13960  6.79995   43.30744  1.000 81.94567  -1 105 ASP   B OD2   1 
ATOM   2210 N  N     . SER   B 1 107 ? -4.09505  10.83735  44.88153  1.000 63.74270  ?  106 SER   B N     1 
ATOM   2211 C  CA    . SER   B 1 107 ? -3.17068  11.76688  45.51338  1.000 68.25296  ?  106 SER   B CA    1 
ATOM   2212 C  C     . SER   B 1 107 ? -3.89538  12.49413  46.63328  1.000 72.31059  ?  106 SER   B C     1 
ATOM   2213 O  O     . SER   B 1 107 ? -5.09457  12.76204  46.53063  1.000 69.84316  ?  106 SER   B O     1 
ATOM   2214 C  CB    . SER   B 1 107 ? -2.60763  12.78135  44.50417  1.000 73.72961  ?  106 SER   B CB    1 
ATOM   2215 O  OG    . SER   B 1 107 ? -1.67732  13.66305  45.11902  1.000 74.82220  ?  106 SER   B OG    1 
ATOM   2216 N  N     . GLU   B 1 108 ? -3.16063  12.79830  47.70001  1.000 72.49211  ?  107 GLU   B N     1 
ATOM   2217 C  CA    . GLU   B 1 108 ? -3.63781  13.66709  48.76767  1.000 75.74642  ?  107 GLU   B CA    1 
ATOM   2218 C  C     . GLU   B 1 108 ? -3.38325  15.13488  48.46601  1.000 76.59085  ?  107 GLU   B C     1 
ATOM   2219 O  O     . GLU   B 1 108 ? -3.70480  15.99361  49.29538  1.000 74.69402  ?  107 GLU   B O     1 
ATOM   2220 C  CB    . GLU   B 1 108 ? -2.95480  13.29382  50.08681  1.000 75.76374  ?  107 GLU   B CB    1 
ATOM   2221 C  CG    . GLU   B 1 108 ? -3.04310  11.82012  50.43523  1.000 79.12547  ?  107 GLU   B CG    1 
ATOM   2222 C  CD    . GLU   B 1 108 ? -4.43624  11.40998  50.87425  1.000 85.06311  ?  107 GLU   B CD    1 
ATOM   2223 O  OE1   . GLU   B 1 108 ? -4.79157  11.66972  52.04844  1.000 88.64489  ?  107 GLU   B OE1   1 
ATOM   2224 O  OE2   . GLU   B 1 108 ? -5.17961  10.84008  50.04288  1.000 79.54544  -1 107 GLU   B OE2   1 
ATOM   2225 N  N     . ASP   B 1 109 ? -2.84028  15.43007  47.28677  1.000 74.52263  ?  108 ASP   B N     1 
ATOM   2226 C  CA    . ASP   B 1 109 ? -2.17378  16.69032  46.99460  1.000 75.08508  ?  108 ASP   B CA    1 
ATOM   2227 C  C     . ASP   B 1 109 ? -2.70826  17.26187  45.67659  1.000 72.32005  ?  108 ASP   B C     1 
ATOM   2228 O  O     . ASP   B 1 109 ? -1.96406  17.51853  44.73119  1.000 75.40463  ?  108 ASP   B O     1 
ATOM   2229 C  CB    . ASP   B 1 109 ? -0.66694  16.43511  46.94825  1.000 79.07410  ?  108 ASP   B CB    1 
ATOM   2230 C  CG    . ASP   B 1 109 ? 0.14828   17.69999  47.04414  1.000 85.24598  ?  108 ASP   B CG    1 
ATOM   2231 O  OD1   . ASP   B 1 109 ? 0.28125   18.24278  48.16121  1.000 89.24507  ?  108 ASP   B OD1   1 
ATOM   2232 O  OD2   . ASP   B 1 109 ? 0.66859   18.14461  46.00162  1.000 87.35694  -1 108 ASP   B OD2   1 
ATOM   2233 N  N     . VAL   B 1 110 ? -4.01400  17.45670  45.61580  1.000 63.75040  ?  109 VAL   B N     1 
ATOM   2234 C  CA    . VAL   B 1 110 ? -4.70070  17.90528  44.39372  1.000 58.53057  ?  109 VAL   B CA    1 
ATOM   2235 C  C     . VAL   B 1 110 ? -5.09839  19.33615  44.57141  1.000 47.56274  ?  109 VAL   B C     1 
ATOM   2236 O  O     . VAL   B 1 110 ? -5.73892  19.69898  45.56887  1.000 45.59276  ?  109 VAL   B O     1 
ATOM   2237 C  CB    . VAL   B 1 110 ? -5.93120  17.02239  44.08795  1.000 53.33413  ?  109 VAL   B CB    1 
ATOM   2238 C  CG1   . VAL   B 1 110 ? -6.68726  17.57050  42.86111  1.000 49.21108  ?  109 VAL   B CG1   1 
ATOM   2239 C  CG2   . VAL   B 1 110 ? -5.50148  15.57622  43.87257  1.000 55.16762  ?  109 VAL   B CG2   1 
ATOM   2240 N  N     . PRO   B 1 111 ? -4.75327  20.24173  43.63123  1.000 48.20039  ?  110 PRO   B N     1 
ATOM   2241 C  CA    . PRO   B 1 111 ? -5.14356  21.65300  43.73583  1.000 39.92143  ?  110 PRO   B CA    1 
ATOM   2242 C  C     . PRO   B 1 111 ? -6.64736  21.84286  43.88602  1.000 42.44797  ?  110 PRO   B C     1 
ATOM   2243 O  O     . PRO   B 1 111 ? -7.44089  21.46167  43.01380  1.000 39.18260  ?  110 PRO   B O     1 
ATOM   2244 C  CB    . PRO   B 1 111 ? -4.62804  22.24914  42.42390  1.000 38.30544  ?  110 PRO   B CB    1 
ATOM   2245 C  CG    . PRO   B 1 111 ? -3.48329  21.39578  42.06621  1.000 45.47514  ?  110 PRO   B CG    1 
ATOM   2246 C  CD    . PRO   B 1 111 ? -3.84740  20.00099  42.49554  1.000 49.72496  ?  110 PRO   B CD    1 
ATOM   2247 N  N     . MET   B 1 112 ? -7.04221  22.44887  45.00150  1.000 41.73065  ?  111 MET   B N     1 
ATOM   2248 C  CA    . MET   B 1 112 ? -8.44705  22.71571  45.26274  1.000 34.82871  ?  111 MET   B CA    1 
ATOM   2249 C  C     . MET   B 1 112 ? -8.60254  24.04838  45.96418  1.000 35.62354  ?  111 MET   B C     1 
ATOM   2250 O  O     . MET   B 1 112 ? -7.67336  24.55206  46.59981  1.000 37.81468  ?  111 MET   B O     1 
ATOM   2251 C  CB    . MET   B 1 112 ? -9.10105  21.65409  46.14258  1.000 37.30310  ?  111 MET   B CB    1 
ATOM   2252 C  CG    . MET   B 1 112 ? -8.93265  20.23416  45.68634  1.000 45.59093  ?  111 MET   B CG    1 
ATOM   2253 S  SD    . MET   B 1 112 ? -9.98406  19.19471  46.71398  1.000 48.75933  ?  111 MET   B SD    1 
ATOM   2254 C  CE    . MET   B 1 112 ? -9.54180  17.57128  46.09869  1.000 45.25407  ?  111 MET   B CE    1 
ATOM   2255 N  N     . VAL   B 1 113 ? -9.80313  24.59557  45.86675  1.000 34.26548  ?  112 VAL   B N     1 
ATOM   2256 C  CA    . VAL   B 1 113 ? -10.19789 25.77249  46.62215  1.000 38.60760  ?  112 VAL   B CA    1 
ATOM   2257 C  C     . VAL   B 1 113 ? -11.62135 25.54824  47.10551  1.000 42.65504  ?  112 VAL   B C     1 
ATOM   2258 O  O     . VAL   B 1 113 ? -12.49600 25.19437  46.30843  1.000 33.77332  ?  112 VAL   B O     1 
ATOM   2259 C  CB    . VAL   B 1 113 ? -10.09386 27.05625  45.77676  1.000 38.33270  ?  112 VAL   B CB    1 
ATOM   2260 C  CG1   . VAL   B 1 113 ? -10.89229 28.18757  46.41150  1.000 41.69006  ?  112 VAL   B CG1   1 
ATOM   2261 C  CG2   . VAL   B 1 113 ? -8.63194  27.45238  45.60875  1.000 34.74186  ?  112 VAL   B CG2   1 
ATOM   2262 N  N     . LEU   B 1 114 ? -11.84785 25.71713  48.41444  1.000 38.26070  ?  113 LEU   B N     1 
ATOM   2263 C  CA    . LEU   B 1 114 ? -13.19674 25.63745  48.95931  1.000 38.97131  ?  113 LEU   B CA    1 
ATOM   2264 C  C     . LEU   B 1 114 ? -13.89197 26.97410  48.76906  1.000 38.60811  ?  113 LEU   B C     1 
ATOM   2265 O  O     . LEU   B 1 114 ? -13.29592 28.02393  49.01244  1.000 46.43537  ?  113 LEU   B O     1 
ATOM   2266 C  CB    . LEU   B 1 114 ? -13.15510 25.26517  50.44269  1.000 43.45606  ?  113 LEU   B CB    1 
ATOM   2267 C  CG    . LEU   B 1 114 ? -14.50216 25.22673  51.15508  1.000 43.71399  ?  113 LEU   B CG    1 
ATOM   2268 C  CD1   . LEU   B 1 114 ? -15.37381 24.14257  50.56061  1.000 44.96150  ?  113 LEU   B CD1   1 
ATOM   2269 C  CD2   . LEU   B 1 114 ? -14.30608 25.01158  52.65519  1.000 49.63744  ?  113 LEU   B CD2   1 
ATOM   2270 N  N     . VAL   B 1 115 ? -15.15211 26.94836  48.34996  1.000 37.41323  ?  114 VAL   B N     1 
ATOM   2271 C  CA    . VAL   B 1 115 ? -15.85618 28.17071  47.97853  1.000 37.09146  ?  114 VAL   B CA    1 
ATOM   2272 C  C     . VAL   B 1 115 ? -17.24092 28.18309  48.62005  1.000 46.63036  ?  114 VAL   B C     1 
ATOM   2273 O  O     . VAL   B 1 115 ? -18.05963 27.29008  48.36210  1.000 38.74760  ?  114 VAL   B O     1 
ATOM   2274 C  CB    . VAL   B 1 115 ? -15.96174 28.32214  46.44797  1.000 40.70409  ?  114 VAL   B CB    1 
ATOM   2275 C  CG1   . VAL   B 1 115 ? -16.82252 29.52427  46.09706  1.000 40.24914  ?  114 VAL   B CG1   1 
ATOM   2276 C  CG2   . VAL   B 1 115 ? -14.56149 28.43669  45.81014  1.000 32.70477  ?  114 VAL   B CG2   1 
ATOM   2277 N  N     . GLY   B 1 116 ? -17.50563 29.20169  49.44761  1.000 40.95313  ?  115 GLY   B N     1 
ATOM   2278 C  CA    . GLY   B 1 116 ? -18.82966 29.40230  49.99846  1.000 42.86915  ?  115 GLY   B CA    1 
ATOM   2279 C  C     . GLY   B 1 116 ? -19.60632 30.49298  49.28926  1.000 43.95086  ?  115 GLY   B C     1 
ATOM   2280 O  O     . GLY   B 1 116 ? -19.27769 31.67707  49.39902  1.000 46.16428  ?  115 GLY   B O     1 
ATOM   2281 N  N     . ASN   B 1 117 ? -20.64163 30.11359  48.56280  1.000 43.23235  ?  116 ASN   B N     1 
ATOM   2282 C  CA    . ASN   B 1 117 ? -21.35715 31.03778  47.69558  1.000 49.45098  ?  116 ASN   B CA    1 
ATOM   2283 C  C     . ASN   B 1 117 ? -22.68210 31.47627  48.32005  1.000 48.32475  ?  116 ASN   B C     1 
ATOM   2284 O  O     . ASN   B 1 117 ? -23.17887 30.88446  49.28157  1.000 45.34050  ?  116 ASN   B O     1 
ATOM   2285 C  CB    . ASN   B 1 117 ? -21.60849 30.40507  46.31613  1.000 37.55798  ?  116 ASN   B CB    1 
ATOM   2286 C  CG    . ASN   B 1 117 ? -22.04229 31.42048  45.29461  1.000 40.63218  ?  116 ASN   B CG    1 
ATOM   2287 O  OD1   . ASN   B 1 117 ? -21.49611 32.51352  45.24900  1.000 45.49494  ?  116 ASN   B OD1   1 
ATOM   2288 N  ND2   . ASN   B 1 117 ? -23.05518 31.08800  44.49179  1.000 45.68983  ?  116 ASN   B ND2   1 
ATOM   2289 N  N     . LYS   B 1 118 ? -23.25445 32.52953  47.72873  1.000 47.95392  ?  117 LYS   B N     1 
ATOM   2290 C  CA    . LYS   B 1 118 ? -24.54076 33.11892  48.09175  1.000 56.55223  ?  117 LYS   B CA    1 
ATOM   2291 C  C     . LYS   B 1 118 ? -24.43017 33.97387  49.35384  1.000 59.70565  ?  117 LYS   B C     1 
ATOM   2292 O  O     . LYS   B 1 118 ? -25.37432 34.02206  50.15283  1.000 57.53399  ?  117 LYS   B O     1 
ATOM   2293 C  CB    . LYS   B 1 118 ? -25.62131 32.04106  48.27102  1.000 51.88554  ?  117 LYS   B CB    1 
ATOM   2294 C  CG    . LYS   B 1 118 ? -25.86264 31.15639  47.04711  1.000 52.88392  ?  117 LYS   B CG    1 
ATOM   2295 C  CD    . LYS   B 1 118 ? -27.23190 30.47577  47.12135  1.000 47.50701  ?  117 LYS   B CD    1 
ATOM   2296 C  CE    . LYS   B 1 118 ? -27.39758 29.44163  46.02377  1.000 50.58707  ?  117 LYS   B CE    1 
ATOM   2297 N  NZ    . LYS   B 1 118 ? -28.74776 28.80749  46.02420  1.000 49.47755  ?  117 LYS   B NZ    1 
ATOM   2298 N  N     . CYS   B 1 119 ? -23.29864 34.67023  49.53000  1.000 53.27880  ?  118 CYS   B N     1 
ATOM   2299 C  CA    . CYS   B 1 119 ? -23.08740 35.48961  50.72296  1.000 57.40122  ?  118 CYS   B CA    1 
ATOM   2300 C  C     . CYS   B 1 119 ? -23.90641 36.77616  50.72653  1.000 59.96365  ?  118 CYS   B C     1 
ATOM   2301 O  O     . CYS   B 1 119 ? -23.96130 37.45261  51.75929  1.000 59.93698  ?  118 CYS   B O     1 
ATOM   2302 C  CB    . CYS   B 1 119 ? -21.60807 35.82374  50.87723  1.000 54.79953  ?  118 CYS   B CB    1 
ATOM   2303 S  SG    . CYS   B 1 119 ? -20.61754 34.40142  51.31154  1.000 59.82118  ?  118 CYS   B SG    1 
ATOM   2304 N  N     . ASP   B 1 120 ? -24.53909 37.12782  49.60674  1.000 55.96809  ?  119 ASP   B N     1 
ATOM   2305 C  CA    . ASP   B 1 120 ? -25.50171 38.22114  49.59742  1.000 62.20416  ?  119 ASP   B CA    1 
ATOM   2306 C  C     . ASP   B 1 120 ? -26.79257 37.86830  50.32671  1.000 66.76888  ?  119 ASP   B C     1 
ATOM   2307 O  O     . ASP   B 1 120 ? -27.58615 38.76796  50.63075  1.000 64.63491  ?  119 ASP   B O     1 
ATOM   2308 C  CB    . ASP   B 1 120 ? -25.84817 38.58115  48.16764  1.000 57.03783  ?  119 ASP   B CB    1 
ATOM   2309 C  CG    . ASP   B 1 120 ? -26.43800 37.41362  47.43704  1.000 60.01100  ?  119 ASP   B CG    1 
ATOM   2310 O  OD1   . ASP   B 1 120 ? -25.71948 36.39700  47.29703  1.000 58.58718  ?  119 ASP   B OD1   1 
ATOM   2311 O  OD2   . ASP   B 1 120 ? -27.62875 37.48767  47.06272  1.000 60.14718  -1 119 ASP   B OD2   1 
ATOM   2312 N  N     . LEU   B 1 121 ? -27.03742 36.57513  50.57686  1.000 67.01875  ?  120 LEU   B N     1 
ATOM   2313 C  CA    . LEU   B 1 121 ? -28.25575 36.10692  51.21550  1.000 72.34983  ?  120 LEU   B CA    1 
ATOM   2314 C  C     . LEU   B 1 121 ? -28.14709 36.22782  52.73811  1.000 77.98646  ?  120 LEU   B C     1 
ATOM   2315 O  O     . LEU   B 1 121 ? -27.06637 36.04924  53.31011  1.000 76.60000  ?  120 LEU   B O     1 
ATOM   2316 C  CB    . LEU   B 1 121 ? -28.54098 34.66030  50.81773  1.000 64.81503  ?  120 LEU   B CB    1 
ATOM   2317 C  CG    . LEU   B 1 121 ? -29.01462 34.45151  49.37630  1.000 66.84993  ?  120 LEU   B CG    1 
ATOM   2318 C  CD1   . LEU   B 1 121 ? -29.32670 32.98687  49.09593  1.000 61.36525  ?  120 LEU   B CD1   1 
ATOM   2319 C  CD2   . LEU   B 1 121 ? -30.23178 35.32210  49.07312  1.000 69.01267  ?  120 LEU   B CD2   1 
ATOM   2320 N  N     . PRO   B 1 122 ? -29.26049 36.53952  53.41584  1.000 81.15813  ?  121 PRO   B N     1 
ATOM   2321 C  CA    . PRO   B 1 122 ? -29.19185 36.84689  54.85184  1.000 88.14680  ?  121 PRO   B CA    1 
ATOM   2322 C  C     . PRO   B 1 122 ? -29.24119 35.63751  55.77792  1.000 93.06180  ?  121 PRO   B C     1 
ATOM   2323 O  O     . PRO   B 1 122 ? -28.79183 35.73312  56.92468  1.000 87.59556  ?  121 PRO   B O     1 
ATOM   2324 C  CB    . PRO   B 1 122 ? -30.41614 37.74421  55.06073  1.000 87.17670  ?  121 PRO   B CB    1 
ATOM   2325 C  CG    . PRO   B 1 122 ? -31.39629 37.25619  54.04149  1.000 86.92920  ?  121 PRO   B CG    1 
ATOM   2326 C  CD    . PRO   B 1 122 ? -30.59239 36.82210  52.84911  1.000 79.48272  ?  121 PRO   B CD    1 
ATOM   2327 N  N     . SER   B 1 123 ? -29.77285 34.50573  55.31253  1.000 97.60729  ?  122 SER   B N     1 
ATOM   2328 C  CA    . SER   B 1 123 ? -30.05993 33.36917  56.19430  1.000 98.61834  ?  122 SER   B CA    1 
ATOM   2329 C  C     . SER   B 1 123 ? -28.93005 32.33848  56.13916  1.000 96.33082  ?  122 SER   B C     1 
ATOM   2330 O  O     . SER   B 1 123 ? -29.08535 31.21477  55.65956  1.000 91.66184  ?  122 SER   B O     1 
ATOM   2331 C  CB    . SER   B 1 123 ? -31.40000 32.73997  55.82496  1.000 104.21292 ?  122 SER   B CB    1 
ATOM   2332 O  OG    . SER   B 1 123 ? -31.24225 31.79454  54.78118  1.000 105.89445 ?  122 SER   B OG    1 
ATOM   2333 N  N     . ARG   B 1 124 ? -27.77943 32.73352  56.67631  1.000 83.53215  ?  123 ARG   B N     1 
ATOM   2334 C  CA    . ARG   B 1 124 ? -26.64456 31.82448  56.75322  1.000 75.29700  ?  123 ARG   B CA    1 
ATOM   2335 C  C     . ARG   B 1 124 ? -26.91459 30.70382  57.75488  1.000 77.33245  ?  123 ARG   B C     1 
ATOM   2336 O  O     . ARG   B 1 124 ? -27.31824 30.95992  58.89239  1.000 76.44159  ?  123 ARG   B O     1 
ATOM   2337 C  CB    . ARG   B 1 124 ? -25.38736 32.59202  57.14641  1.000 73.16261  ?  123 ARG   B CB    1 
ATOM   2338 C  CG    . ARG   B 1 124 ? -24.26618 31.70934  57.64879  1.000 71.85834  ?  123 ARG   B CG    1 
ATOM   2339 C  CD    . ARG   B 1 124 ? -23.08451 32.52757  58.14194  1.000 70.75407  ?  123 ARG   B CD    1 
ATOM   2340 N  NE    . ARG   B 1 124 ? -22.45804 33.29090  57.07045  1.000 69.42084  ?  123 ARG   B NE    1 
ATOM   2341 C  CZ    . ARG   B 1 124 ? -21.59100 32.78767  56.20209  1.000 68.30433  ?  123 ARG   B CZ    1 
ATOM   2342 N  NH1   . ARG   B 1 124 ? -21.24263 31.51315  56.23440  1.000 66.05983  ?  123 ARG   B NH1   1 
ATOM   2343 N  NH2   . ARG   B 1 124 ? -21.05988 33.58346  55.27951  1.000 62.34170  ?  123 ARG   B NH2   1 
ATOM   2344 N  N     . THR   B 1 125 ? -26.69340 29.45532  57.32243  1.000 77.66322  ?  124 THR   B N     1 
ATOM   2345 C  CA    . THR   B 1 125 ? -26.78937 28.27818  58.18047  1.000 73.03864  ?  124 THR   B CA    1 
ATOM   2346 C  C     . THR   B 1 125 ? -25.49729 27.47577  58.24471  1.000 69.46971  ?  124 THR   B C     1 
ATOM   2347 O  O     . THR   B 1 125 ? -25.46988 26.42801  58.89577  1.000 71.05674  ?  124 THR   B O     1 
ATOM   2348 C  CB    . THR   B 1 125 ? -27.92302 27.34945  57.71597  1.000 72.73169  ?  124 THR   B CB    1 
ATOM   2349 O  OG1   . THR   B 1 125 ? -27.65081 26.87552  56.39229  1.000 66.21943  ?  124 THR   B OG1   1 
ATOM   2350 C  CG2   . THR   B 1 125 ? -29.25783 28.07409  57.72636  1.000 73.39912  ?  124 THR   B CG2   1 
ATOM   2351 N  N     . VAL   B 1 126 ? -24.44105 27.91690  57.57388  1.000 66.44829  ?  125 VAL   B N     1 
ATOM   2352 C  CA    . VAL   B 1 126 ? -23.12575 27.29151  57.65204  1.000 72.07362  ?  125 VAL   B CA    1 
ATOM   2353 C  C     . VAL   B 1 126 ? -22.19954 28.32609  58.26306  1.000 69.92401  ?  125 VAL   B C     1 
ATOM   2354 O  O     . VAL   B 1 126 ? -21.94685 29.37493  57.65622  1.000 72.06377  ?  125 VAL   B O     1 
ATOM   2355 C  CB    . VAL   B 1 126 ? -22.60663 26.82769  56.28039  1.000 63.85526  ?  125 VAL   B CB    1 
ATOM   2356 C  CG1   . VAL   B 1 126 ? -21.18076 26.29676  56.40547  1.000 59.26848  ?  125 VAL   B CG1   1 
ATOM   2357 C  CG2   . VAL   B 1 126 ? -23.52859 25.76860  55.68656  1.000 59.54835  ?  125 VAL   B CG2   1 
ATOM   2358 N  N     . ASP   B 1 127 ? -21.71744 28.05443  59.47002  1.000 75.61590  ?  126 ASP   B N     1 
ATOM   2359 C  CA    . ASP   B 1 127 ? -20.81670 28.98949  60.12798  1.000 78.73702  ?  126 ASP   B CA    1 
ATOM   2360 C  C     . ASP   B 1 127 ? -19.61173 29.27049  59.23995  1.000 74.68767  ?  126 ASP   B C     1 
ATOM   2361 O  O     . ASP   B 1 127 ? -18.98595 28.34654  58.71271  1.000 69.61618  ?  126 ASP   B O     1 
ATOM   2362 C  CB    . ASP   B 1 127 ? -20.36453 28.43280  61.48228  1.000 78.74665  ?  126 ASP   B CB    1 
ATOM   2363 C  CG    . ASP   B 1 127 ? -21.37865 28.68434  62.59342  1.000 85.18658  ?  126 ASP   B CG    1 
ATOM   2364 O  OD1   . ASP   B 1 127 ? -21.69576 29.86642  62.86259  1.000 87.23762  -1 126 ASP   B OD1   1 
ATOM   2365 O  OD2   . ASP   B 1 127 ? -21.85646 27.69581  63.19502  1.000 83.18451  ?  126 ASP   B OD2   1 
ATOM   2366 N  N     . THR   B 1 128 ? -19.32906 30.56213  59.03927  1.000 69.77117  ?  127 THR   B N     1 
ATOM   2367 C  CA    . THR   B 1 128 ? -18.07466 30.97164  58.41662  1.000 69.46356  ?  127 THR   B CA    1 
ATOM   2368 C  C     . THR   B 1 128 ? -16.88694 30.27466  59.06975  1.000 69.13074  ?  127 THR   B C     1 
ATOM   2369 O  O     . THR   B 1 128 ? -16.00123 29.75629  58.37967  1.000 65.18761  ?  127 THR   B O     1 
ATOM   2370 C  CB    . THR   B 1 128 ? -17.91775 32.49307  58.50865  1.000 68.29588  ?  127 THR   B CB    1 
ATOM   2371 O  OG1   . THR   B 1 128 ? -18.81068 33.13783  57.58999  1.000 66.21932  ?  127 THR   B OG1   1 
ATOM   2372 C  CG2   . THR   B 1 128 ? -16.48967 32.91117  58.20418  1.000 67.37472  ?  127 THR   B CG2   1 
ATOM   2373 N  N     . LYS   B 1 129 ? -16.86883 30.23142  60.40467  1.000 72.39111  ?  128 LYS   B N     1 
ATOM   2374 C  CA    . LYS   B 1 129 ? -15.76192 29.60774  61.12291  1.000 78.66149  ?  128 LYS   B CA    1 
ATOM   2375 C  C     . LYS   B 1 129 ? -15.66393 28.11940  60.81501  1.000 73.50423  ?  128 LYS   B C     1 
ATOM   2376 O  O     . LYS   B 1 129 ? -14.56191 27.55632  60.79240  1.000 72.29373  ?  128 LYS   B O     1 
ATOM   2377 C  CB    . LYS   B 1 129 ? -15.93205 29.83868  62.62659  1.000 79.80252  ?  128 LYS   B CB    1 
ATOM   2378 C  CG    . LYS   B 1 129 ? -14.63641 30.10170  63.37797  1.000 85.20665  ?  128 LYS   B CG    1 
ATOM   2379 C  CD    . LYS   B 1 129 ? -13.91552 28.80800  63.71959  1.000 86.84985  ?  128 LYS   B CD    1 
ATOM   2380 C  CE    . LYS   B 1 129 ? -12.93065 29.00582  64.86101  1.000 90.88803  ?  128 LYS   B CE    1 
ATOM   2381 N  NZ    . LYS   B 1 129 ? -12.43589 27.69748  65.37260  1.000 93.36707  ?  128 LYS   B NZ    1 
ATOM   2382 N  N     . GLN   B 1 130 ? -16.80449 27.47339  60.57406  1.000 71.48310  ?  129 GLN   B N     1 
ATOM   2383 C  CA    . GLN   B 1 130 ? -16.81149 26.05729  60.22946  1.000 70.91901  ?  129 GLN   B CA    1 
ATOM   2384 C  C     . GLN   B 1 130 ? -16.07298 25.81343  58.91778  1.000 67.67450  ?  129 GLN   B C     1 
ATOM   2385 O  O     . GLN   B 1 130 ? -15.13476 25.00905  58.85684  1.000 64.96917  ?  129 GLN   B O     1 
ATOM   2386 C  CB    . GLN   B 1 130 ? -18.25895 25.57473  60.14460  1.000 72.44973  ?  129 GLN   B CB    1 
ATOM   2387 C  CG    . GLN   B 1 130 ? -18.49421 24.14261  60.54918  1.000 71.92698  ?  129 GLN   B CG    1 
ATOM   2388 C  CD    . GLN   B 1 130 ? -19.96966 23.83284  60.68730  1.000 75.98012  ?  129 GLN   B CD    1 
ATOM   2389 O  OE1   . GLN   B 1 130 ? -20.76585 24.68439  61.09721  1.000 78.91557  ?  129 GLN   B OE1   1 
ATOM   2390 N  NE2   . GLN   B 1 130 ? -20.34624 22.61202  60.33526  1.000 71.34696  ?  129 GLN   B NE2   1 
ATOM   2391 N  N     . ALA   B 1 131 ? -16.47613 26.52273  57.85777  1.000 67.12813  ?  130 ALA   B N     1 
ATOM   2392 C  CA    . ALA   B 1 131 ? -15.82948 26.36237  56.55738  1.000 64.22428  ?  130 ALA   B CA    1 
ATOM   2393 C  C     . ALA   B 1 131 ? -14.34645 26.71551  56.62635  1.000 63.94774  ?  130 ALA   B C     1 
ATOM   2394 O  O     . ALA   B 1 131 ? -13.50586 26.01345  56.04811  1.000 56.80766  ?  130 ALA   B O     1 
ATOM   2395 C  CB    . ALA   B 1 131 ? -16.54677 27.21675  55.51494  1.000 55.46013  ?  130 ALA   B CB    1 
ATOM   2396 N  N     . GLN   B 1 132 ? -14.00595 27.79032  57.34844  1.000 64.18697  ?  131 GLN   B N     1 
ATOM   2397 C  CA    . GLN   B 1 132 ? -12.60431 28.16647  57.51590  1.000 64.70367  ?  131 GLN   B CA    1 
ATOM   2398 C  C     . GLN   B 1 132 ? -11.79596 27.04239  58.15627  1.000 67.19456  ?  131 GLN   B C     1 
ATOM   2399 O  O     . GLN   B 1 132 ? -10.65357 26.78468  57.75672  1.000 63.37424  ?  131 GLN   B O     1 
ATOM   2400 C  CB    . GLN   B 1 132 ? -12.49959 29.44143  58.35307  1.000 65.89662  ?  131 GLN   B CB    1 
ATOM   2401 C  CG    . GLN   B 1 132 ? -13.08292 30.67624  57.69262  1.000 66.66889  ?  131 GLN   B CG    1 
ATOM   2402 C  CD    . GLN   B 1 132 ? -13.08390 31.88052  58.61088  1.000 67.69581  ?  131 GLN   B CD    1 
ATOM   2403 O  OE1   . GLN   B 1 132 ? -13.05973 31.74405  59.83240  1.000 71.63049  ?  131 GLN   B OE1   1 
ATOM   2404 N  NE2   . GLN   B 1 132 ? -13.10645 33.06657  58.02644  1.000 66.78780  ?  131 GLN   B NE2   1 
ATOM   2405 N  N     . ASP   B 1 133 ? -12.36845 26.36735  59.15844  1.000 70.92525  ?  132 ASP   B N     1 
ATOM   2406 C  CA    . ASP   B 1 133 ? -11.65862 25.27623  59.82035  1.000 71.46692  ?  132 ASP   B CA    1 
ATOM   2407 C  C     . ASP   B 1 133 ? -11.50892 24.07858  58.89271  1.000 66.63515  ?  132 ASP   B C     1 
ATOM   2408 O  O     . ASP   B 1 133 ? -10.43161 23.47761  58.80339  1.000 67.01941  ?  132 ASP   B O     1 
ATOM   2409 C  CB    . ASP   B 1 133 ? -12.39448 24.87125  61.09747  1.000 74.06660  ?  132 ASP   B CB    1 
ATOM   2410 C  CG    . ASP   B 1 133 ? -12.21979 25.87569  62.21622  1.000 82.93214  ?  132 ASP   B CG    1 
ATOM   2411 O  OD1   . ASP   B 1 133 ? -11.50332 26.88173  62.01127  1.000 77.59700  -1 132 ASP   B OD1   1 
ATOM   2412 O  OD2   . ASP   B 1 133 ? -12.80001 25.65275  63.30316  1.000 86.72360  ?  132 ASP   B OD2   1 
ATOM   2413 N  N     . LEU   B 1 134 ? -12.59333 23.71334  58.20714  1.000 64.04274  ?  133 LEU   B N     1 
ATOM   2414 C  CA    . LEU   B 1 134 ? -12.57111 22.57721  57.29224  1.000 65.32992  ?  133 LEU   B CA    1 
ATOM   2415 C  C     . LEU   B 1 134 ? -11.49840 22.73964  56.22310  1.000 61.10020  ?  133 LEU   B C     1 
ATOM   2416 O  O     . LEU   B 1 134 ? -10.71967 21.81515  55.95904  1.000 58.66841  ?  133 LEU   B O     1 
ATOM   2417 C  CB    . LEU   B 1 134 ? -13.94291 22.41579  56.64537  1.000 60.14260  ?  133 LEU   B CB    1 
ATOM   2418 C  CG    . LEU   B 1 134 ? -14.02626 21.26988  55.64105  1.000 63.10166  ?  133 LEU   B CG    1 
ATOM   2419 C  CD1   . LEU   B 1 134 ? -14.01443 19.92122  56.35873  1.000 60.06353  ?  133 LEU   B CD1   1 
ATOM   2420 C  CD2   . LEU   B 1 134 ? -15.25331 21.42824  54.76406  1.000 58.94906  ?  133 LEU   B CD2   1 
ATOM   2421 N  N     . ALA   B 1 135 ? -11.44460 23.91742  55.59593  1.000 57.30977  ?  134 ALA   B N     1 
ATOM   2422 C  CA    . ALA   B 1 135 ? -10.42713 24.15997  54.57814  1.000 64.01643  ?  134 ALA   B CA    1 
ATOM   2423 C  C     . ALA   B 1 135 ? -9.02567  24.05415  55.16637  1.000 65.50492  ?  134 ALA   B C     1 
ATOM   2424 O  O     . ALA   B 1 135 ? -8.11196  23.52255  54.52037  1.000 58.16835  ?  134 ALA   B O     1 
ATOM   2425 C  CB    . ALA   B 1 135 ? -10.64214 25.52956  53.93340  1.000 54.83805  ?  134 ALA   B CB    1 
ATOM   2426 N  N     . ARG   B 1 136 ? -8.84324  24.54432  56.40079  1.000 63.96125  ?  135 ARG   B N     1 
ATOM   2427 C  CA    . ARG   B 1 136 ? -7.54139  24.46430  57.05705  1.000 66.30025  ?  135 ARG   B CA    1 
ATOM   2428 C  C     . ARG   B 1 136 ? -7.10038  23.01522  57.24148  1.000 65.17445  ?  135 ARG   B C     1 
ATOM   2429 O  O     . ARG   B 1 136 ? -5.92809  22.68111  57.02258  1.000 65.88506  ?  135 ARG   B O     1 
ATOM   2430 C  CB    . ARG   B 1 136 ? -7.59508  25.19344  58.40228  1.000 72.90673  ?  135 ARG   B CB    1 
ATOM   2431 C  CG    . ARG   B 1 136 ? -6.29443  25.15384  59.20436  1.000 74.18335  ?  135 ARG   B CG    1 
ATOM   2432 C  CD    . ARG   B 1 136 ? -6.41865  25.87591  60.54496  1.000 76.12050  ?  135 ARG   B CD    1 
ATOM   2433 N  NE    . ARG   B 1 136 ? -6.87126  27.25642  60.39863  1.000 76.19166  ?  135 ARG   B NE    1 
ATOM   2434 C  CZ    . ARG   B 1 136 ? -8.07265  27.69344  60.75593  1.000 77.98850  ?  135 ARG   B CZ    1 
ATOM   2435 N  NH1   . ARG   B 1 136 ? -8.96236  26.88951  61.31799  1.000 77.53611  ?  135 ARG   B NH1   1 
ATOM   2436 N  NH2   . ARG   B 1 136 ? -8.38807  28.96975  60.54951  1.000 76.08413  ?  135 ARG   B NH2   1 
ATOM   2437 N  N     . SER   B 1 137 ? -8.02667  22.13973  57.64563  1.000 65.86138  ?  136 SER   B N     1 
ATOM   2438 C  CA    . SER   B 1 137 ? -7.70629  20.72281  57.76586  1.000 67.19575  ?  136 SER   B CA    1 
ATOM   2439 C  C     . SER   B 1 137 ? -7.39588  20.09273  56.41454  1.000 67.91301  ?  136 SER   B C     1 
ATOM   2440 O  O     . SER   B 1 137 ? -6.67948  19.08544  56.36090  1.000 65.03496  ?  136 SER   B O     1 
ATOM   2441 C  CB    . SER   B 1 137 ? -8.85737  19.97965  58.44070  1.000 68.63539  ?  136 SER   B CB    1 
ATOM   2442 O  OG    . SER   B 1 137 ? -9.97916  19.88352  57.58394  1.000 65.04812  ?  136 SER   B OG    1 
ATOM   2443 N  N     . TYR   B 1 138 ? -7.92312  20.66333  55.32485  1.000 61.98660  ?  137 TYR   B N     1 
ATOM   2444 C  CA    . TYR   B 1 138 ? -7.56695  20.22783  53.98039  1.000 62.17981  ?  137 TYR   B CA    1 
ATOM   2445 C  C     . TYR   B 1 138 ? -6.25019  20.82016  53.49964  1.000 57.58432  ?  137 TYR   B C     1 
ATOM   2446 O  O     . TYR   B 1 138 ? -5.60757  20.23347  52.62117  1.000 57.85779  ?  137 TYR   B O     1 
ATOM   2447 C  CB    . TYR   B 1 138 ? -8.66372  20.60705  52.98451  1.000 62.93718  ?  137 TYR   B CB    1 
ATOM   2448 C  CG    . TYR   B 1 138 ? -9.97770  19.86983  53.13750  1.000 61.07957  ?  137 TYR   B CG    1 
ATOM   2449 C  CD1   . TYR   B 1 138 ? -10.08476 18.73321  53.92721  1.000 60.62304  ?  137 TYR   B CD1   1 
ATOM   2450 C  CD2   . TYR   B 1 138 ? -11.11230 20.30913  52.46752  1.000 57.49542  ?  137 TYR   B CD2   1 
ATOM   2451 C  CE1   . TYR   B 1 138 ? -11.29322 18.06577  54.04875  1.000 61.57915  ?  137 TYR   B CE1   1 
ATOM   2452 C  CE2   . TYR   B 1 138 ? -12.31758 19.65116  52.58484  1.000 57.38570  ?  137 TYR   B CE2   1 
ATOM   2453 C  CZ    . TYR   B 1 138 ? -12.40632 18.53293  53.37547  1.000 56.85825  ?  137 TYR   B CZ    1 
ATOM   2454 O  OH    . TYR   B 1 138 ? -13.61878 17.89258  53.48248  1.000 54.96369  ?  137 TYR   B OH    1 
ATOM   2455 N  N     . GLY   B 1 139 ? -5.83639  21.95864  54.04763  1.000 57.99728  ?  138 GLY   B N     1 
ATOM   2456 C  CA    . GLY   B 1 139 ? -4.65719  22.64181  53.54306  1.000 60.05021  ?  138 GLY   B CA    1 
ATOM   2457 C  C     . GLY   B 1 139 ? -4.90680  23.38638  52.24597  1.000 55.27760  ?  138 GLY   B C     1 
ATOM   2458 O  O     . GLY   B 1 139 ? -4.05343  23.37229  51.35138  1.000 52.50451  ?  138 GLY   B O     1 
ATOM   2459 N  N     . ILE   B 1 140 ? -6.06703  24.02435  52.11977  1.000 51.70442  ?  139 ILE   B N     1 
ATOM   2460 C  CA    . ILE   B 1 140 ? -6.49267  24.66598  50.87812  1.000 56.14771  ?  139 ILE   B CA    1 
ATOM   2461 C  C     . ILE   B 1 140 ? -7.22130  25.95510  51.21552  1.000 54.75857  ?  139 ILE   B C     1 
ATOM   2462 O  O     . ILE   B 1 140 ? -7.80182  26.10375  52.30455  1.000 52.18696  ?  139 ILE   B O     1 
ATOM   2463 C  CB    . ILE   B 1 140 ? -7.40421  23.74938  50.02366  1.000 49.61469  ?  139 ILE   B CB    1 
ATOM   2464 C  CG1   . ILE   B 1 140 ? -8.75795  23.54454  50.70553  1.000 53.83074  ?  139 ILE   B CG1   1 
ATOM   2465 C  CG2   . ILE   B 1 140 ? -6.72735  22.41696  49.69897  1.000 46.74066  ?  139 ILE   B CG2   1 
ATOM   2466 C  CD1   . ILE   B 1 140 ? -9.79361  22.87980  49.81999  1.000 46.78270  ?  139 ILE   B CD1   1 
ATOM   2467 N  N     . PRO   B 1 141 ? -7.20335  26.91619  50.30297  1.000 46.56696  ?  140 PRO   B N     1 
ATOM   2468 C  CA    . PRO   B 1 141 ? -7.82786  28.21054  50.57925  1.000 48.29875  ?  140 PRO   B CA    1 
ATOM   2469 C  C     . PRO   B 1 141 ? -9.34106  28.11036  50.67294  1.000 49.73548  ?  140 PRO   B C     1 
ATOM   2470 O  O     . PRO   B 1 141 ? -9.97645  27.19503  50.14603  1.000 52.06928  ?  140 PRO   B O     1 
ATOM   2471 C  CB    . PRO   B 1 141 ? -7.40918  29.06860  49.38324  1.000 48.01852  ?  140 PRO   B CB    1 
ATOM   2472 C  CG    . PRO   B 1 141 ? -6.14948  28.39862  48.85818  1.000 44.29300  ?  140 PRO   B CG    1 
ATOM   2473 C  CD    . PRO   B 1 141 ? -6.36589  26.94140  49.08701  1.000 46.71664  ?  140 PRO   B CD    1 
ATOM   2474 N  N     . PHE   B 1 142 ? -9.92150  29.09031  51.35382  1.000 47.18282  ?  141 PHE   B N     1 
ATOM   2475 C  CA    . PHE   B 1 142 ? -11.36673 29.22528  51.45174  1.000 48.72107  ?  141 PHE   B CA    1 
ATOM   2476 C  C     . PHE   B 1 142 ? -11.74562 30.64378  51.05580  1.000 47.25606  ?  141 PHE   B C     1 
ATOM   2477 O  O     . PHE   B 1 142 ? -11.13596 31.60898  51.52591  1.000 47.77237  ?  141 PHE   B O     1 
ATOM   2478 C  CB    . PHE   B 1 142 ? -11.87419 28.89869  52.86579  1.000 49.48836  ?  141 PHE   B CB    1 
ATOM   2479 C  CG    . PHE   B 1 142 ? -13.29140 29.33664  53.11583  1.000 49.91473  ?  141 PHE   B CG    1 
ATOM   2480 C  CD1   . PHE   B 1 142 ? -14.32293 28.88866  52.31193  1.000 49.61171  ?  141 PHE   B CD1   1 
ATOM   2481 C  CD2   . PHE   B 1 142 ? -13.59189 30.20243  54.14935  1.000 53.15459  ?  141 PHE   B CD2   1 
ATOM   2482 C  CE1   . PHE   B 1 142 ? -15.62842 29.30041  52.52425  1.000 48.15399  ?  141 PHE   B CE1   1 
ATOM   2483 C  CE2   . PHE   B 1 142 ? -14.89853 30.61538  54.37311  1.000 55.10391  ?  141 PHE   B CE2   1 
ATOM   2484 C  CZ    . PHE   B 1 142 ? -15.91519 30.16412  53.56241  1.000 54.60694  ?  141 PHE   B CZ    1 
ATOM   2485 N  N     . ILE   B 1 143 ? -12.73705 30.76873  50.17843  1.000 46.68114  ?  142 ILE   B N     1 
ATOM   2486 C  CA    . ILE   B 1 143 ? -13.15162 32.05631  49.64353  1.000 45.16942  ?  142 ILE   B CA    1 
ATOM   2487 C  C     . ILE   B 1 143 ? -14.66557 32.12633  49.69990  1.000 49.35360  ?  142 ILE   B C     1 
ATOM   2488 O  O     . ILE   B 1 143 ? -15.34587 31.15794  49.34738  1.000 48.06706  ?  142 ILE   B O     1 
ATOM   2489 C  CB    . ILE   B 1 143 ? -12.65007 32.26007  48.20072  1.000 44.63515  ?  142 ILE   B CB    1 
ATOM   2490 C  CG1   . ILE   B 1 143 ? -11.13844 32.06483  48.14590  1.000 45.16416  ?  142 ILE   B CG1   1 
ATOM   2491 C  CG2   . ILE   B 1 143 ? -13.01558 33.64628  47.70211  1.000 45.63380  ?  142 ILE   B CG2   1 
ATOM   2492 C  CD1   . ILE   B 1 143 ? -10.58613 31.96855  46.77974  1.000 46.40707  ?  142 ILE   B CD1   1 
ATOM   2493 N  N     . GLU   B 1 144 ? -15.19005 33.25615  50.16171  1.000 47.79869  ?  143 GLU   B N     1 
ATOM   2494 C  CA    . GLU   B 1 144 ? -16.62107 33.50598  50.14347  1.000 47.66709  ?  143 GLU   B CA    1 
ATOM   2495 C  C     . GLU   B 1 144 ? -16.95671 34.29645  48.89514  1.000 45.21941  ?  143 GLU   B C     1 
ATOM   2496 O  O     . GLU   B 1 144 ? -16.20977 35.18783  48.49125  1.000 46.14605  ?  143 GLU   B O     1 
ATOM   2497 C  CB    . GLU   B 1 144 ? -17.07290 34.27624  51.38460  1.000 53.82043  ?  143 GLU   B CB    1 
ATOM   2498 C  CG    . GLU   B 1 144 ? -17.34378 33.41292  52.61133  1.000 57.47238  ?  143 GLU   B CG    1 
ATOM   2499 C  CD    . GLU   B 1 144 ? -17.87927 34.23064  53.77893  1.000 62.42202  ?  143 GLU   B CD    1 
ATOM   2500 O  OE1   . GLU   B 1 144 ? -17.70398 35.47231  53.75963  1.000 57.17876  ?  143 GLU   B OE1   1 
ATOM   2501 O  OE2   . GLU   B 1 144 ? -18.48347 33.63185  54.70093  1.000 59.82415  -1 143 GLU   B OE2   1 
ATOM   2502 N  N     . THR   B 1 145 ? -18.06453 33.94846  48.26414  1.000 46.52748  ?  144 THR   B N     1 
ATOM   2503 C  CA    . THR   B 1 145 ? -18.38448 34.55381  46.98863  1.000 44.10614  ?  144 THR   B CA    1 
ATOM   2504 C  C     . THR   B 1 145 ? -19.85884 34.90855  46.95444  1.000 47.88817  ?  144 THR   B C     1 
ATOM   2505 O  O     . THR   B 1 145 ? -20.66409 34.42107  47.74964  1.000 44.08771  ?  144 THR   B O     1 
ATOM   2506 C  CB    . THR   B 1 145 ? -18.03834 33.62339  45.81279  1.000 42.67741  ?  144 THR   B CB    1 
ATOM   2507 O  OG1   . THR   B 1 145 ? -18.86154 32.44528  45.84775  1.000 42.17394  ?  144 THR   B OG1   1 
ATOM   2508 C  CG2   . THR   B 1 145 ? -16.56102 33.21670  45.85320  1.000 46.72570  ?  144 THR   B CG2   1 
ATOM   2509 N  N     . SER   B 1 146 ? -20.20534 35.77395  46.01696  1.000 44.69568  ?  145 SER   B N     1 
ATOM   2510 C  CA    . SER   B 1 146 ? -21.59353 35.94210  45.63110  1.000 46.85661  ?  145 SER   B CA    1 
ATOM   2511 C  C     . SER   B 1 146 ? -21.63628 36.14163  44.12939  1.000 51.06339  ?  145 SER   B C     1 
ATOM   2512 O  O     . SER   B 1 146 ? -21.17017 37.16576  43.62246  1.000 49.66789  ?  145 SER   B O     1 
ATOM   2513 C  CB    . SER   B 1 146 ? -22.24773 37.11866  46.34471  1.000 47.41706  ?  145 SER   B CB    1 
ATOM   2514 O  OG    . SER   B 1 146 ? -23.54545 37.31217  45.81521  1.000 48.21979  ?  145 SER   B OG    1 
ATOM   2515 N  N     . ALA   B 1 147 ? -22.18579 35.16284  43.42006  1.000 45.88606  ?  146 ALA   B N     1 
ATOM   2516 C  CA    . ALA   B 1 147 ? -22.38062 35.33161  41.99066  1.000 51.46894  ?  146 ALA   B CA    1 
ATOM   2517 C  C     . ALA   B 1 147 ? -23.36917 36.44422  41.68258  1.000 50.46534  ?  146 ALA   B C     1 
ATOM   2518 O  O     . ALA   B 1 147 ? -23.38070 36.95349  40.55570  1.000 43.67451  ?  146 ALA   B O     1 
ATOM   2519 C  CB    . ALA   B 1 147 ? -22.85468 34.02119  41.36667  1.000 45.57931  ?  146 ALA   B CB    1 
ATOM   2520 N  N     . LYS   B 1 148 ? -24.19458 36.83729  42.65413  1.000 47.00638  ?  147 LYS   B N     1 
ATOM   2521 C  CA    . LYS   B 1 148 ? -25.16136 37.90288  42.40103  1.000 53.62879  ?  147 LYS   B CA    1 
ATOM   2522 C  C     . LYS   B 1 148 ? -24.47265 39.26368  42.34716  1.000 46.09059  ?  147 LYS   B C     1 
ATOM   2523 O  O     . LYS   B 1 148 ? -24.74754 40.07281  41.45376  1.000 47.97765  ?  147 LYS   B O     1 
ATOM   2524 C  CB    . LYS   B 1 148 ? -26.25722 37.88197  43.46933  1.000 56.99450  ?  147 LYS   B CB    1 
ATOM   2525 C  CG    . LYS   B 1 148 ? -27.44862 38.78040  43.17486  1.000 55.82948  ?  147 LYS   B CG    1 
ATOM   2526 C  CD    . LYS   B 1 148 ? -28.51410 38.60667  44.24588  1.000 62.59743  ?  147 LYS   B CD    1 
ATOM   2527 C  CE    . LYS   B 1 148 ? -29.69819 39.54007  44.02606  1.000 66.76500  ?  147 LYS   B CE    1 
ATOM   2528 N  NZ    . LYS   B 1 148 ? -30.57786 39.56390  45.22261  1.000 64.42487  ?  147 LYS   B NZ    1 
ATOM   2529 N  N     . THR   B 1 149 ? -23.54759 39.51561  43.27407  1.000 45.45630  ?  148 THR   B N     1 
ATOM   2530 C  CA    . THR   B 1 149 ? -22.85172 40.79195  43.37802  1.000 48.96172  ?  148 THR   B CA    1 
ATOM   2531 C  C     . THR   B 1 149 ? -21.43020 40.75434  42.82506  1.000 54.56580  ?  148 THR   B C     1 
ATOM   2532 O  O     . THR   B 1 149 ? -20.75993 41.79333  42.83016  1.000 56.61385  ?  148 THR   B O     1 
ATOM   2533 C  CB    . THR   B 1 149 ? -22.80557 41.26497  44.84478  1.000 50.55356  ?  148 THR   B CB    1 
ATOM   2534 O  OG1   . THR   B 1 149 ? -21.84964 40.49152  45.58703  1.000 49.10674  ?  148 THR   B OG1   1 
ATOM   2535 C  CG2   . THR   B 1 149 ? -24.17660 41.14588  45.50186  1.000 53.13617  ?  148 THR   B CG2   1 
ATOM   2536 N  N     . ARG   B 1 150 ? -20.95310 39.59227  42.36306  1.000 47.75842  ?  149 ARG   B N     1 
ATOM   2537 C  CA    . ARG   B 1 150 ? -19.59450 39.35316  41.86498  1.000 43.15415  ?  149 ARG   B CA    1 
ATOM   2538 C  C     . ARG   B 1 150 ? -18.53728 39.32447  42.95603  1.000 43.12444  ?  149 ARG   B C     1 
ATOM   2539 O  O     . ARG   B 1 150 ? -17.34514 39.26384  42.63724  1.000 43.92651  ?  149 ARG   B O     1 
ATOM   2540 C  CB    . ARG   B 1 150 ? -19.14647 40.37500  40.81183  1.000 45.64884  ?  149 ARG   B CB    1 
ATOM   2541 C  CG    . ARG   B 1 150 ? -19.59232 40.08414  39.40433  1.000 51.56224  ?  149 ARG   B CG    1 
ATOM   2542 C  CD    . ARG   B 1 150 ? -18.71516 40.78780  38.37730  1.000 50.12362  ?  149 ARG   B CD    1 
ATOM   2543 N  NE    . ARG   B 1 150 ? -18.00504 39.83803  37.52602  1.000 46.40959  ?  149 ARG   B NE    1 
ATOM   2544 C  CZ    . ARG   B 1 150 ? -16.70354 39.59544  37.58735  1.000 45.11994  ?  149 ARG   B CZ    1 
ATOM   2545 N  NH1   . ARG   B 1 150 ? -15.92164 40.22590  38.44261  1.000 53.27953  ?  149 ARG   B NH1   1 
ATOM   2546 N  NH2   . ARG   B 1 150 ? -16.16970 38.70689  36.75813  1.000 47.48838  ?  149 ARG   B NH2   1 
ATOM   2547 N  N     . GLN   B 1 151 ? -18.92276 39.39028  44.22682  1.000 45.12093  ?  150 GLN   B N     1 
ATOM   2548 C  CA    . GLN   B 1 151 ? -17.94358 39.37244  45.31053  1.000 46.69702  ?  150 GLN   B CA    1 
ATOM   2549 C  C     . GLN   B 1 151 ? -17.10891 38.09519  45.25512  1.000 42.36399  ?  150 GLN   B C     1 
ATOM   2550 O  O     . GLN   B 1 151 ? -17.66149 36.99736  45.22251  1.000 45.90820  ?  150 GLN   B O     1 
ATOM   2551 C  CB    . GLN   B 1 151 ? -18.66979 39.49619  46.65593  1.000 50.53541  ?  150 GLN   B CB    1 
ATOM   2552 C  CG    . GLN   B 1 151 ? -17.85042 39.15664  47.90873  1.000 51.27575  ?  150 GLN   B CG    1 
ATOM   2553 C  CD    . GLN   B 1 151 ? -18.74070 38.91082  49.13554  1.000 59.63055  ?  150 GLN   B CD    1 
ATOM   2554 O  OE1   . GLN   B 1 151 ? -18.68284 37.85273  49.76973  1.000 58.68420  ?  150 GLN   B OE1   1 
ATOM   2555 N  NE2   . GLN   B 1 151 ? -19.56851 39.88972  49.46330  1.000 61.70750  ?  150 GLN   B NE2   1 
ATOM   2556 N  N     . GLY   B 1 152 ? -15.78164 38.23893  45.21190  1.000 40.62677  ?  151 GLY   B N     1 
ATOM   2557 C  CA    . GLY   B 1 152 ? -14.86957 37.10483  45.27510  1.000 40.13056  ?  151 GLY   B CA    1 
ATOM   2558 C  C     . GLY   B 1 152 ? -14.77693 36.21411  44.03982  1.000 38.89762  ?  151 GLY   B C     1 
ATOM   2559 O  O     . GLY   B 1 152 ? -14.00413 35.24516  44.05403  1.000 35.21560  ?  151 GLY   B O     1 
ATOM   2560 N  N     . VAL   B 1 153 ? -15.53076 36.50669  42.97702  1.000 36.78158  ?  152 VAL   B N     1 
ATOM   2561 C  CA    . VAL   B 1 153 ? -15.59165 35.61223  41.81771  1.000 40.11187  ?  152 VAL   B CA    1 
ATOM   2562 C  C     . VAL   B 1 153 ? -14.20742 35.42111  41.19789  1.000 39.72427  ?  152 VAL   B C     1 
ATOM   2563 O  O     . VAL   B 1 153 ? -13.72174 34.28918  41.06466  1.000 35.42228  ?  152 VAL   B O     1 
ATOM   2564 C  CB    . VAL   B 1 153 ? -16.60298 36.13870  40.78112  1.000 44.66424  ?  152 VAL   B CB    1 
ATOM   2565 C  CG1   . VAL   B 1 153 ? -16.54623 35.29552  39.50678  1.000 37.44113  ?  152 VAL   B CG1   1 
ATOM   2566 C  CG2   . VAL   B 1 153 ? -18.02834 36.14675  41.35707  1.000 39.04096  ?  152 VAL   B CG2   1 
ATOM   2567 N  N     . ASP   B 1 154 ? -13.55781 36.52361  40.79849  1.000 37.51610  ?  153 ASP   B N     1 
ATOM   2568 C  CA    . ASP   B 1 154 ? -12.21758 36.43602  40.22024  1.000 39.52189  ?  153 ASP   B CA    1 
ATOM   2569 C  C     . ASP   B 1 154 ? -11.23561 35.82310  41.20504  1.000 35.02140  ?  153 ASP   B C     1 
ATOM   2570 O  O     . ASP   B 1 154 ? -10.40156 34.98714  40.83997  1.000 33.62671  ?  153 ASP   B O     1 
ATOM   2571 C  CB    . ASP   B 1 154 ? -11.70628 37.82128  39.80685  1.000 43.01327  ?  153 ASP   B CB    1 
ATOM   2572 C  CG    . ASP   B 1 154 ? -12.46225 38.42860  38.64284  1.000 46.20156  ?  153 ASP   B CG    1 
ATOM   2573 O  OD1   . ASP   B 1 154 ? -12.91614 37.70662  37.72201  1.000 46.43832  ?  153 ASP   B OD1   1 
ATOM   2574 O  OD2   . ASP   B 1 154 ? -12.57035 39.67132  38.63667  1.000 54.04401  -1 153 ASP   B OD2   1 
ATOM   2575 N  N     . ASP   B 1 155 ? -11.28499 36.27417  42.45768  1.000 40.35996  ?  154 ASP   B N     1 
ATOM   2576 C  CA    . ASP   B 1 155 ? -10.37603 35.75703  43.47402  1.000 36.63711  ?  154 ASP   B CA    1 
ATOM   2577 C  C     . ASP   B 1 155 ? -10.46692 34.23724  43.56817  1.000 34.93925  ?  154 ASP   B C     1 
ATOM   2578 O  O     . ASP   B 1 155 ? -9.44160  33.55548  43.69427  1.000 35.39670  ?  154 ASP   B O     1 
ATOM   2579 C  CB    . ASP   B 1 155 ? -10.69688 36.42683  44.81413  1.000 37.90513  ?  154 ASP   B CB    1 
ATOM   2580 C  CG    . ASP   B 1 155 ? -9.74098  36.03131  45.92600  1.000 44.76574  ?  154 ASP   B CG    1 
ATOM   2581 O  OD1   . ASP   B 1 155 ? -8.59390  35.60947  45.64649  1.000 49.11463  ?  154 ASP   B OD1   1 
ATOM   2582 O  OD2   . ASP   B 1 155 ? -10.15376 36.14871  47.10338  1.000 48.25552  -1 154 ASP   B OD2   1 
ATOM   2583 N  N     . ALA   B 1 156 ? -11.68642 33.68783  43.45174  1.000 35.56383  ?  155 ALA   B N     1 
ATOM   2584 C  CA    . ALA   B 1 156 ? -11.88671 32.23957  43.55401  1.000 36.17910  ?  155 ALA   B CA    1 
ATOM   2585 C  C     . ALA   B 1 156 ? -11.13568 31.47598  42.46263  1.000 33.09994  ?  155 ALA   B C     1 
ATOM   2586 O  O     . ALA   B 1 156 ? -10.34011 30.57036  42.75089  1.000 29.72547  ?  155 ALA   B O     1 
ATOM   2587 C  CB    . ALA   B 1 156 ? -13.37832 31.92015  43.49377  1.000 31.09932  ?  155 ALA   B CB    1 
ATOM   2588 N  N     . PHE   B 1 157 ? -11.39877 31.80957  41.19727  1.000 33.40279  ?  156 PHE   B N     1 
ATOM   2589 C  CA    . PHE   B 1 157 ? -10.73357 31.11933  40.09798  1.000 28.51839  ?  156 PHE   B CA    1 
ATOM   2590 C  C     . PHE   B 1 157 ? -9.23731  31.43161  40.05906  1.000 29.73305  ?  156 PHE   B C     1 
ATOM   2591 O  O     . PHE   B 1 157 ? -8.41449  30.53304  39.84225  1.000 30.24746  ?  156 PHE   B O     1 
ATOM   2592 C  CB    . PHE   B 1 157 ? -11.40689 31.49088  38.77501  1.000 30.61419  ?  156 PHE   B CB    1 
ATOM   2593 C  CG    . PHE   B 1 157 ? -12.77696 30.87352  38.58894  1.000 33.22609  ?  156 PHE   B CG    1 
ATOM   2594 C  CD1   . PHE   B 1 157 ? -12.90986 29.59023  38.08325  1.000 31.03694  ?  156 PHE   B CD1   1 
ATOM   2595 C  CD2   . PHE   B 1 157 ? -13.93455 31.58073  38.90764  1.000 29.21910  ?  156 PHE   B CD2   1 
ATOM   2596 C  CE1   . PHE   B 1 157 ? -14.17604 29.01113  37.89730  1.000 26.93728  ?  156 PHE   B CE1   1 
ATOM   2597 C  CE2   . PHE   B 1 157 ? -15.19236 30.99968  38.74421  1.000 35.60538  ?  156 PHE   B CE2   1 
ATOM   2598 C  CZ    . PHE   B 1 157 ? -15.30721 29.71226  38.22039  1.000 27.92714  ?  156 PHE   B CZ    1 
ATOM   2599 N  N     . TYR   B 1 158 ? -8.85516  32.69613  40.26513  1.000 31.79195  ?  157 TYR   B N     1 
ATOM   2600 C  CA    . TYR   B 1 158 ? -7.42689  33.01761  40.24697  1.000 32.38694  ?  157 TYR   B CA    1 
ATOM   2601 C  C     . TYR   B 1 158 ? -6.67074  32.30177  41.35995  1.000 31.06510  ?  157 TYR   B C     1 
ATOM   2602 O  O     . TYR   B 1 158 ? -5.53937  31.84946  41.14272  1.000 35.22246  ?  157 TYR   B O     1 
ATOM   2603 C  CB    . TYR   B 1 158 ? -7.19549  34.52745  40.35271  1.000 33.87627  ?  157 TYR   B CB    1 
ATOM   2604 C  CG    . TYR   B 1 158 ? -7.66733  35.34789  39.17036  1.000 39.36724  ?  157 TYR   B CG    1 
ATOM   2605 C  CD1   . TYR   B 1 158 ? -8.30102  34.75127  38.08529  1.000 39.01446  ?  157 TYR   B CD1   1 
ATOM   2606 C  CD2   . TYR   B 1 158 ? -7.45260  36.72556  39.12646  1.000 46.13019  ?  157 TYR   B CD2   1 
ATOM   2607 C  CE1   . TYR   B 1 158 ? -8.73011  35.49786  37.00182  1.000 40.76738  ?  157 TYR   B CE1   1 
ATOM   2608 C  CE2   . TYR   B 1 158 ? -7.87601  37.48205  38.03878  1.000 44.95090  ?  157 TYR   B CE2   1 
ATOM   2609 C  CZ    . TYR   B 1 158 ? -8.52012  36.86003  36.98485  1.000 43.07259  ?  157 TYR   B CZ    1 
ATOM   2610 O  OH    . TYR   B 1 158 ? -8.94748  37.59810  35.90081  1.000 50.81661  ?  157 TYR   B OH    1 
ATOM   2611 N  N     . THR   B 1 159 ? -7.27108  32.17988  42.54738  1.000 32.19945  ?  158 THR   B N     1 
ATOM   2612 C  CA    . THR   B 1 159 ? -6.60352  31.45394  43.62644  1.000 34.09967  ?  158 THR   B CA    1 
ATOM   2613 C  C     . THR   B 1 159 ? -6.36112  29.99746  43.24235  1.000 33.11798  ?  158 THR   B C     1 
ATOM   2614 O  O     . THR   B 1 159 ? -5.26616  29.46068  43.46435  1.000 34.86556  ?  158 THR   B O     1 
ATOM   2615 C  CB    . THR   B 1 159 ? -7.42199  31.54418  44.91585  1.000 36.68901  ?  158 THR   B CB    1 
ATOM   2616 O  OG1   . THR   B 1 159 ? -7.65582  32.92301  45.24045  1.000 41.59642  ?  158 THR   B OG1   1 
ATOM   2617 C  CG2   . THR   B 1 159 ? -6.69044  30.85945  46.06543  1.000 37.99488  ?  158 THR   B CG2   1 
ATOM   2618 N  N     . LEU   B 1 160 ? -7.36723  29.34389  42.64667  1.000 31.55617  ?  159 LEU   B N     1 
ATOM   2619 C  CA    . LEU   B 1 160 ? -7.16149  27.98281  42.16767  1.000 31.89647  ?  159 LEU   B CA    1 
ATOM   2620 C  C     . LEU   B 1 160 ? -6.00334  27.91941  41.18015  1.000 32.73648  ?  159 LEU   B C     1 
ATOM   2621 O  O     . LEU   B 1 160 ? -5.17752  27.00835  41.25007  1.000 33.43410  ?  159 LEU   B O     1 
ATOM   2622 C  CB    . LEU   B 1 160 ? -8.44386  27.44151  41.53495  1.000 31.40527  ?  159 LEU   B CB    1 
ATOM   2623 C  CG    . LEU   B 1 160 ? -8.34797  26.02474  40.96909  1.000 31.29245  ?  159 LEU   B CG    1 
ATOM   2624 C  CD1   . LEU   B 1 160 ? -7.73183  25.05911  41.95619  1.000 32.59359  ?  159 LEU   B CD1   1 
ATOM   2625 C  CD2   . LEU   B 1 160 ? -9.74610  25.52299  40.49474  1.000 28.39939  ?  159 LEU   B CD2   1 
ATOM   2626 N  N     . VAL   B 1 161 ? -5.91901  28.88595  40.25849  1.000 29.40137  ?  160 VAL   B N     1 
ATOM   2627 C  CA    . VAL   B 1 161 ? -4.77220  28.94561  39.34750  1.000 29.14382  ?  160 VAL   B CA    1 
ATOM   2628 C  C     . VAL   B 1 161 ? -3.46541  28.99578  40.13253  1.000 33.96110  ?  160 VAL   B C     1 
ATOM   2629 O  O     . VAL   B 1 161 ? -2.52760  28.23844  39.85683  1.000 34.01552  ?  160 VAL   B O     1 
ATOM   2630 C  CB    . VAL   B 1 161 ? -4.89188  30.15451  38.40486  1.000 32.38384  ?  160 VAL   B CB    1 
ATOM   2631 C  CG1   . VAL   B 1 161 ? -3.58290  30.35148  37.63490  1.000 29.03328  ?  160 VAL   B CG1   1 
ATOM   2632 C  CG2   . VAL   B 1 161 ? -6.08436  29.98614  37.47089  1.000 28.66922  ?  160 VAL   B CG2   1 
ATOM   2633 N  N     . ARG   B 1 162 ? -3.38448  29.90675  41.11683  1.000 38.58814  ?  161 ARG   B N     1 
ATOM   2634 C  CA    . ARG   B 1 162 ? -2.18697  29.99796  41.95185  1.000 37.21559  ?  161 ARG   B CA    1 
ATOM   2635 C  C     . ARG   B 1 162 ? -1.91820  28.68362  42.66841  1.000 40.44988  ?  161 ARG   B C     1 
ATOM   2636 O  O     . ARG   B 1 162 ? -0.75707  28.26995  42.79319  1.000 46.31892  ?  161 ARG   B O     1 
ATOM   2637 C  CB    . ARG   B 1 162 ? -2.32019  31.14102  42.96615  1.000 37.75274  ?  161 ARG   B CB    1 
ATOM   2638 C  CG    . ARG   B 1 162 ? -2.27704  32.54938  42.36762  1.000 45.89661  ?  161 ARG   B CG    1 
ATOM   2639 C  CD    . ARG   B 1 162 ? -2.46162  33.66764  43.42220  1.000 39.83785  ?  161 ARG   B CD    1 
ATOM   2640 N  NE    . ARG   B 1 162 ? -2.57480  34.98507  42.79844  1.000 39.93458  ?  161 ARG   B NE    1 
ATOM   2641 C  CZ    . ARG   B 1 162 ? -3.68665  35.70728  42.75256  1.000 42.05900  ?  161 ARG   B CZ    1 
ATOM   2642 N  NH1   . ARG   B 1 162 ? -4.79915  35.30188  43.34279  1.000 38.49767  ?  161 ARG   B NH1   1 
ATOM   2643 N  NH2   . ARG   B 1 162 ? -3.67904  36.87483  42.11302  1.000 38.69320  ?  161 ARG   B NH2   1 
ATOM   2644 N  N     . GLU   B 1 163 ? -2.97392  28.00571  43.13011  1.000 36.42101  ?  162 GLU   B N     1 
ATOM   2645 C  CA    . GLU   B 1 163 ? -2.78050  26.71648  43.78668  1.000 38.79425  ?  162 GLU   B CA    1 
ATOM   2646 C  C     . GLU   B 1 163 ? -2.17000  25.70593  42.82937  1.000 39.12375  ?  162 GLU   B C     1 
ATOM   2647 O  O     . GLU   B 1 163 ? -1.33242  24.89092  43.22991  1.000 40.65437  ?  162 GLU   B O     1 
ATOM   2648 C  CB    . GLU   B 1 163 ? -4.10430  26.19803  44.35153  1.000 37.15004  ?  162 GLU   B CB    1 
ATOM   2649 C  CG    . GLU   B 1 163 ? -4.56567  26.91795  45.61924  1.000 40.27432  ?  162 GLU   B CG    1 
ATOM   2650 C  CD    . GLU   B 1 163 ? -3.58400  26.74853  46.77736  1.000 49.94141  ?  162 GLU   B CD    1 
ATOM   2651 O  OE1   . GLU   B 1 163 ? -3.35178  25.59601  47.21103  1.000 46.97005  ?  162 GLU   B OE1   1 
ATOM   2652 O  OE2   . GLU   B 1 163 ? -3.03013  27.77112  47.23573  1.000 48.79091  -1 162 GLU   B OE2   1 
ATOM   2653 N  N     . ILE   B 1 164 ? -2.57469  25.74728  41.55582  1.000 41.81334  ?  163 ILE   B N     1 
ATOM   2654 C  CA    . ILE   B 1 164 ? -1.99738  24.84616  40.56209  1.000 40.14516  ?  163 ILE   B CA    1 
ATOM   2655 C  C     . ILE   B 1 164 ? -0.54020  25.20457  40.29256  1.000 44.42007  ?  163 ILE   B C     1 
ATOM   2656 O  O     . ILE   B 1 164 ? 0.30799   24.32375  40.10241  1.000 45.16153  ?  163 ILE   B O     1 
ATOM   2657 C  CB    . ILE   B 1 164 ? -2.82725  24.87779  39.26897  1.000 38.92118  ?  163 ILE   B CB    1 
ATOM   2658 C  CG1   . ILE   B 1 164 ? -4.28415  24.48581  39.53841  1.000 34.67836  ?  163 ILE   B CG1   1 
ATOM   2659 C  CG2   . ILE   B 1 164 ? -2.20810  23.96353  38.21234  1.000 36.47628  ?  163 ILE   B CG2   1 
ATOM   2660 C  CD1   . ILE   B 1 164 ? -5.13311  24.49215  38.28142  1.000 29.40587  ?  163 ILE   B CD1   1 
ATOM   2661 N  N     . ARG   B 1 165 ? -0.22651  26.49955  40.25026  1.000 39.06095  ?  164 ARG   B N     1 
ATOM   2662 C  CA    . ARG   B 1 165 ? 1.16056   26.90385  40.04902  1.000 47.12921  ?  164 ARG   B CA    1 
ATOM   2663 C  C     . ARG   B 1 165 ? 2.04018   26.41022  41.19267  1.000 51.23263  ?  164 ARG   B C     1 
ATOM   2664 O  O     . ARG   B 1 165 ? 3.08844   25.79623  40.96259  1.000 53.03879  ?  164 ARG   B O     1 
ATOM   2665 C  CB    . ARG   B 1 165 ? 1.24626   28.42073  39.89373  1.000 39.22736  ?  164 ARG   B CB    1 
ATOM   2666 C  CG    . ARG   B 1 165 ? 0.65023   28.92226  38.59019  1.000 40.44969  ?  164 ARG   B CG    1 
ATOM   2667 C  CD    . ARG   B 1 165 ? 0.71148   30.44166  38.47650  1.000 40.89838  ?  164 ARG   B CD    1 
ATOM   2668 N  NE    . ARG   B 1 165 ? 0.18491   30.92161  37.19976  1.000 47.13913  ?  164 ARG   B NE    1 
ATOM   2669 C  CZ    . ARG   B 1 165 ? 0.00135   32.20149  36.89898  1.000 42.13332  ?  164 ARG   B CZ    1 
ATOM   2670 N  NH1   . ARG   B 1 165 ? 0.28478   33.16352  37.76284  1.000 41.36260  ?  164 ARG   B NH1   1 
ATOM   2671 N  NH2   . ARG   B 1 165 ? -0.47720  32.52549  35.70238  1.000 42.07033  ?  164 ARG   B NH2   1 
ATOM   2672 N  N     . LYS   B 1 166 ? 1.60443   26.64094  42.43641  1.000 48.51014  ?  165 LYS   B N     1 
ATOM   2673 C  CA    . LYS   B 1 166 ? 2.32759   26.12412  43.59587  1.000 50.50008  ?  165 LYS   B CA    1 
ATOM   2674 C  C     . LYS   B 1 166 ? 2.51810   24.61434  43.51045  1.000 57.69228  ?  165 LYS   B C     1 
ATOM   2675 O  O     . LYS   B 1 166 ? 3.60834   24.10300  43.79041  1.000 61.14518  ?  165 LYS   B O     1 
ATOM   2676 C  CB    . LYS   B 1 166 ? 1.58245   26.48509  44.87914  1.000 53.82727  ?  165 LYS   B CB    1 
ATOM   2677 C  CG    . LYS   B 1 166 ? 1.59385   27.96409  45.22437  1.000 56.84984  ?  165 LYS   B CG    1 
ATOM   2678 C  CD    . LYS   B 1 166 ? 0.56211   28.26403  46.30059  1.000 63.02414  ?  165 LYS   B CD    1 
ATOM   2679 C  CE    . LYS   B 1 166 ? 0.66899   27.27410  47.46765  1.000 64.96037  ?  165 LYS   B CE    1 
ATOM   2680 N  NZ    . LYS   B 1 166 ? -0.36722  27.51854  48.51674  1.000 60.43613  ?  165 LYS   B NZ    1 
ATOM   2681 N  N     . HIS   B 1 167 ? 1.46693   23.88367  43.12692  1.000 56.43576  ?  166 HIS   B N     1 
ATOM   2682 C  CA    . HIS   B 1 167 ? 1.56826   22.43254  43.03679  1.000 56.61531  ?  166 HIS   B CA    1 
ATOM   2683 C  C     . HIS   B 1 167 ? 2.62264   21.99958  42.02599  1.000 62.32966  ?  166 HIS   B C     1 
ATOM   2684 O  O     . HIS   B 1 167 ? 3.25536   20.95338  42.20336  1.000 66.39872  ?  166 HIS   B O     1 
ATOM   2685 C  CB    . HIS   B 1 167 ? 0.21135   21.83136  42.67619  1.000 53.17281  ?  166 HIS   B CB    1 
ATOM   2686 C  CG    . HIS   B 1 167 ? 0.20939   20.33491  42.65190  1.000 67.00649  ?  166 HIS   B CG    1 
ATOM   2687 N  ND1   . HIS   B 1 167 ? 0.41618   19.60546  41.50031  1.000 69.01652  ?  166 HIS   B ND1   1 
ATOM   2688 C  CD2   . HIS   B 1 167 ? 0.03564   19.42948  43.64294  1.000 72.16232  ?  166 HIS   B CD2   1 
ATOM   2689 C  CE1   . HIS   B 1 167 ? 0.36359   18.31585  41.78177  1.000 67.61896  ?  166 HIS   B CE1   1 
ATOM   2690 N  NE2   . HIS   B 1 167 ? 0.13443   18.18186  43.07544  1.000 75.14312  ?  166 HIS   B NE2   1 
ATOM   2691 N  N     . LYS   B 1 168 ? 2.83362   22.78903  40.96906  1.000 63.14134  ?  167 LYS   B N     1 
ATOM   2692 C  CA    . LYS   B 1 168 ? 3.83618   22.43268  39.96744  1.000 69.81142  ?  167 LYS   B CA    1 
ATOM   2693 C  C     . LYS   B 1 168 ? 5.25439   22.57314  40.51876  1.000 75.68670  ?  167 LYS   B C     1 
ATOM   2694 O  O     . LYS   B 1 168 ? 6.13062   21.75682  40.20725  1.000 78.91343  ?  167 LYS   B O     1 
ATOM   2695 C  CB    . LYS   B 1 168 ? 3.66231   23.29587  38.71532  1.000 67.91337  ?  167 LYS   B CB    1 
ATOM   2696 C  CG    . LYS   B 1 168 ? 2.38844   23.03670  37.91776  1.000 61.68861  ?  167 LYS   B CG    1 
ATOM   2697 C  CD    . LYS   B 1 168 ? 2.36588   23.89620  36.65049  1.000 66.33081  ?  167 LYS   B CD    1 
ATOM   2698 C  CE    . LYS   B 1 168 ? 1.25830   23.48555  35.68332  1.000 60.96396  ?  167 LYS   B CE    1 
ATOM   2699 N  NZ    . LYS   B 1 168 ? 1.25988   24.31646  34.43429  1.000 48.33296  ?  167 LYS   B NZ    1 
ATOM   2700 N  N     . GLU   B 1 169 ? 5.49968   23.59608  41.33551  1.000 74.28125  ?  168 GLU   B N     1 
ATOM   2701 C  CA    . GLU   B 1 169 ? 6.82720   23.83749  41.90229  1.000 78.50245  ?  168 GLU   B CA    1 
ATOM   2702 C  C     . GLU   B 1 169 ? 7.01985   23.08787  43.22450  1.000 75.18687  ?  168 GLU   B C     1 
ATOM   2703 O  O     . GLU   B 1 169 ? 6.76498   21.88574  43.31930  1.000 71.77261  ?  168 GLU   B O     1 
ATOM   2704 C  CB    . GLU   B 1 169 ? 7.05830   25.34019  42.11814  1.000 79.99058  ?  168 GLU   B CB    1 
ATOM   2705 C  CG    . GLU   B 1 169 ? 6.31246   26.25930  41.14482  1.000 75.86087  ?  168 GLU   B CG    1 
ATOM   2706 C  CD    . GLU   B 1 169 ? 6.64524   25.99033  39.68486  1.000 83.67068  ?  168 GLU   B CD    1 
ATOM   2707 O  OE1   . GLU   B 1 169 ? 7.81172   25.65225  39.38502  1.000 90.16241  ?  168 GLU   B OE1   1 
ATOM   2708 O  OE2   . GLU   B 1 169 ? 5.73410   26.11033  38.83454  1.000 82.55027  -1 168 GLU   B OE2   1 
ATOM   2709 N  N     . VAL   C 2 3   ? -61.79089 6.88222   28.39300  1.000 43.10681  ?  2   VAL   C N     1 
ATOM   2710 C  CA    . VAL   C 2 3   ? -60.98871 6.58413   27.20437  1.000 51.72474  ?  2   VAL   C CA    1 
ATOM   2711 C  C     . VAL   C 2 3   ? -59.77672 7.51310   27.14492  1.000 46.60764  ?  2   VAL   C C     1 
ATOM   2712 O  O     . VAL   C 2 3   ? -59.90492 8.73915   27.25215  1.000 48.92090  ?  2   VAL   C O     1 
ATOM   2713 C  CB    . VAL   C 2 3   ? -61.82176 6.69169   25.91683  1.000 49.42930  ?  2   VAL   C CB    1 
ATOM   2714 C  CG1   . VAL   C 2 3   ? -62.44593 8.07364   25.80364  1.000 57.75102  ?  2   VAL   C CG1   1 
ATOM   2715 C  CG2   . VAL   C 2 3   ? -60.96765 6.38059   24.68704  1.000 46.37714  ?  2   VAL   C CG2   1 
ATOM   2716 N  N     . ASN   C 2 4   ? -58.60249 6.91676   26.98361  1.000 38.40160  ?  3   ASN   C N     1 
ATOM   2717 C  CA    . ASN   C 2 4   ? -57.36454 7.68276   27.01569  1.000 41.15894  ?  3   ASN   C CA    1 
ATOM   2718 C  C     . ASN   C 2 4   ? -57.31179 8.64517   25.83430  1.000 41.04297  ?  3   ASN   C C     1 
ATOM   2719 O  O     . ASN   C 2 4   ? -57.49184 8.22134   24.68552  1.000 40.48728  ?  3   ASN   C O     1 
ATOM   2720 C  CB    . ASN   C 2 4   ? -56.16268 6.74969   26.97606  1.000 33.70489  ?  3   ASN   C CB    1 
ATOM   2721 C  CG    . ASN   C 2 4   ? -55.92554 6.03482   28.29052  1.000 38.87988  ?  3   ASN   C CG    1 
ATOM   2722 O  OD1   . ASN   C 2 4   ? -56.39946 6.45363   29.35539  1.000 39.59466  ?  3   ASN   C OD1   1 
ATOM   2723 N  ND2   . ASN   C 2 4   ? -55.17233 4.95211   28.22497  1.000 32.23587  ?  3   ASN   C ND2   1 
ATOM   2724 N  N     . PRO   C 2 5   ? -57.05669 9.92771   26.06263  1.000 41.99269  ?  4   PRO   C N     1 
ATOM   2725 C  CA    . PRO   C 2 5   ? -56.96068 10.86349  24.94021  1.000 39.67511  ?  4   PRO   C CA    1 
ATOM   2726 C  C     . PRO   C 2 5   ? -55.69362 10.63875  24.12371  1.000 38.26352  ?  4   PRO   C C     1 
ATOM   2727 O  O     . PRO   C 2 5   ? -54.72563 10.02302  24.57127  1.000 39.11596  ?  4   PRO   C O     1 
ATOM   2728 C  CB    . PRO   C 2 5   ? -56.95303 12.23585  25.62028  1.000 38.03041  ?  4   PRO   C CB    1 
ATOM   2729 C  CG    . PRO   C 2 5   ? -56.44558 11.98243  26.99182  1.000 42.62088  ?  4   PRO   C CG    1 
ATOM   2730 C  CD    . PRO   C 2 5   ? -56.84872 10.58107  27.36815  1.000 41.80291  ?  4   PRO   C CD    1 
ATOM   2731 N  N     . THR   C 2 6   ? -55.73424 11.13387  22.89313  1.000 37.02115  ?  5   THR   C N     1 
ATOM   2732 C  CA    . THR   C 2 6   ? -54.61065 11.14754  21.96373  1.000 43.69174  ?  5   THR   C CA    1 
ATOM   2733 C  C     . THR   C 2 6   ? -54.33695 12.59331  21.57469  1.000 40.82828  ?  5   THR   C C     1 
ATOM   2734 O  O     . THR   C 2 6   ? -55.25776 13.30110  21.15179  1.000 41.30144  ?  5   THR   C O     1 
ATOM   2735 C  CB    . THR   C 2 6   ? -54.91694 10.31919  20.69362  1.000 39.96001  ?  5   THR   C CB    1 
ATOM   2736 O  OG1   . THR   C 2 6   ? -54.99747 8.92727   21.02571  1.000 43.58533  ?  5   THR   C OG1   1 
ATOM   2737 C  CG2   . THR   C 2 6   ? -53.84500 10.51122  19.64857  1.000 42.28160  ?  5   THR   C CG2   1 
ATOM   2738 N  N     . VAL   C 2 7   ? -53.08063 13.03346  21.70518  1.000 39.57202  ?  6   VAL   C N     1 
ATOM   2739 C  CA    . VAL   C 2 7   ? -52.68366 14.37470  21.28553  1.000 33.33115  ?  6   VAL   C CA    1 
ATOM   2740 C  C     . VAL   C 2 7   ? -51.53888 14.27130  20.28821  1.000 32.59469  ?  6   VAL   C C     1 
ATOM   2741 O  O     . VAL   C 2 7   ? -50.90710 13.22540  20.13821  1.000 32.12118  ?  6   VAL   C O     1 
ATOM   2742 C  CB    . VAL   C 2 7   ? -52.26955 15.27564  22.46716  1.000 32.02222  ?  6   VAL   C CB    1 
ATOM   2743 C  CG1   . VAL   C 2 7   ? -53.42789 15.42396  23.46268  1.000 30.27988  ?  6   VAL   C CG1   1 
ATOM   2744 C  CG2   . VAL   C 2 7   ? -51.02432 14.73545  23.13866  1.000 29.05502  ?  6   VAL   C CG2   1 
ATOM   2745 N  N     . PHE   C 2 8   ? -51.25481 15.38848  19.62409  1.000 31.53068  ?  7   PHE   C N     1 
ATOM   2746 C  CA    . PHE   C 2 8   ? -50.27042 15.39261  18.55091  1.000 30.35131  ?  7   PHE   C CA    1 
ATOM   2747 C  C     . PHE   C 2 8   ? -49.41386 16.64579  18.60522  1.000 28.49259  ?  7   PHE   C C     1 
ATOM   2748 O  O     . PHE   C 2 8   ? -49.88060 17.71981  18.98546  1.000 33.66600  ?  7   PHE   C O     1 
ATOM   2749 C  CB    . PHE   C 2 8   ? -50.92427 15.30846  17.15766  1.000 34.39035  ?  7   PHE   C CB    1 
ATOM   2750 C  CG    . PHE   C 2 8   ? -51.49533 16.61709  16.67971  1.000 38.89006  ?  7   PHE   C CG    1 
ATOM   2751 C  CD1   . PHE   C 2 8   ? -50.71079 17.53650  15.99666  1.000 36.82631  ?  7   PHE   C CD1   1 
ATOM   2752 C  CD2   . PHE   C 2 8   ? -52.82737 16.92802  16.91406  1.000 40.75581  ?  7   PHE   C CD2   1 
ATOM   2753 C  CE1   . PHE   C 2 8   ? -51.24610 18.74293  15.57947  1.000 36.59524  ?  7   PHE   C CE1   1 
ATOM   2754 C  CE2   . PHE   C 2 8   ? -53.36358 18.11917  16.48389  1.000 36.92560  ?  7   PHE   C CE2   1 
ATOM   2755 C  CZ    . PHE   C 2 8   ? -52.57108 19.02755  15.81809  1.000 39.54861  ?  7   PHE   C CZ    1 
ATOM   2756 N  N     . PHE   C 2 9   ? -48.16755 16.49492  18.15095  1.000 34.91499  ?  8   PHE   C N     1 
ATOM   2757 C  CA    . PHE   C 2 9   ? -47.20977 17.57443  17.92715  1.000 31.71792  ?  8   PHE   C CA    1 
ATOM   2758 C  C     . PHE   C 2 9   ? -46.82425 17.56644  16.44599  1.000 33.26675  ?  8   PHE   C C     1 
ATOM   2759 O  O     . PHE   C 2 9   ? -46.46767 16.51223  15.90586  1.000 30.45220  ?  8   PHE   C O     1 
ATOM   2760 C  CB    . PHE   C 2 9   ? -45.91728 17.37480  18.73812  1.000 33.91234  ?  8   PHE   C CB    1 
ATOM   2761 C  CG    . PHE   C 2 9   ? -46.02097 17.63685  20.22997  1.000 30.82863  ?  8   PHE   C CG    1 
ATOM   2762 C  CD1   . PHE   C 2 9   ? -47.11587 18.26164  20.80435  1.000 30.43793  ?  8   PHE   C CD1   1 
ATOM   2763 C  CD2   . PHE   C 2 9   ? -44.96502 17.26940  21.04461  1.000 28.18706  ?  8   PHE   C CD2   1 
ATOM   2764 C  CE1   . PHE   C 2 9   ? -47.15935 18.49579  22.18302  1.000 34.42240  ?  8   PHE   C CE1   1 
ATOM   2765 C  CE2   . PHE   C 2 9   ? -44.98312 17.49513  22.42328  1.000 31.84821  ?  8   PHE   C CE2   1 
ATOM   2766 C  CZ    . PHE   C 2 9   ? -46.09059 18.10966  22.99334  1.000 33.85763  ?  8   PHE   C CZ    1 
ATOM   2767 N  N     . ASP   C 2 10  ? -46.85849 18.72703  15.79324  1.000 30.10449  ?  9   ASP   C N     1 
ATOM   2768 C  CA    . ASP   C 2 10  ? -46.20645 18.88909  14.49555  1.000 35.77089  ?  9   ASP   C CA    1 
ATOM   2769 C  C     . ASP   C 2 10  ? -44.85519 19.55772  14.74440  1.000 30.70042  ?  9   ASP   C C     1 
ATOM   2770 O  O     . ASP   C 2 10  ? -44.79858 20.68345  15.25216  1.000 33.53985  ?  9   ASP   C O     1 
ATOM   2771 C  CB    . ASP   C 2 10  ? -47.07027 19.69538  13.51647  1.000 31.68682  ?  9   ASP   C CB    1 
ATOM   2772 C  CG    . ASP   C 2 10  ? -48.31896 18.92755  13.05639  1.000 35.23968  ?  9   ASP   C CG    1 
ATOM   2773 O  OD1   . ASP   C 2 10  ? -48.21712 17.71355  12.77203  1.000 36.81803  ?  9   ASP   C OD1   1 
ATOM   2774 O  OD2   . ASP   C 2 10  ? -49.41503 19.52538  12.99138  1.000 41.03250  -1 9   ASP   C OD2   1 
ATOM   2775 N  N     . ILE   C 2 11  ? -43.77001 18.85019  14.41969  1.000 29.40179  ?  10  ILE   C N     1 
ATOM   2776 C  CA    . ILE   C 2 11  ? -42.41226 19.27640  14.75024  1.000 28.44104  ?  10  ILE   C CA    1 
ATOM   2777 C  C     . ILE   C 2 11  ? -41.79528 19.96776  13.53717  1.000 30.98264  ?  10  ILE   C C     1 
ATOM   2778 O  O     . ILE   C 2 11  ? -42.01587 19.55860  12.38953  1.000 32.85782  ?  10  ILE   C O     1 
ATOM   2779 C  CB    . ILE   C 2 11  ? -41.56449 18.07441  15.21561  1.000 27.85316  ?  10  ILE   C CB    1 
ATOM   2780 C  CG1   . ILE   C 2 11  ? -42.20434 17.42189  16.45119  1.000 24.27947  ?  10  ILE   C CG1   1 
ATOM   2781 C  CG2   . ILE   C 2 11  ? -40.14218 18.48888  15.55937  1.000 23.10295  ?  10  ILE   C CG2   1 
ATOM   2782 C  CD1   . ILE   C 2 11  ? -42.12851 18.30652  17.65709  1.000 25.12221  ?  10  ILE   C CD1   1 
ATOM   2783 N  N     . ALA   C 2 12  ? -41.04443 21.03731  13.78672  1.000 31.82820  ?  11  ALA   C N     1 
ATOM   2784 C  CA    . ALA   C 2 12  ? -40.37417 21.77285  12.72394  1.000 39.59412  ?  11  ALA   C CA    1 
ATOM   2785 C  C     . ALA   C 2 12  ? -38.91596 21.96613  13.09756  1.000 38.02732  ?  11  ALA   C C     1 
ATOM   2786 O  O     . ALA   C 2 12  ? -38.55829 22.04282  14.27833  1.000 36.79773  ?  11  ALA   C O     1 
ATOM   2787 C  CB    . ALA   C 2 12  ? -41.02825 23.14493  12.45507  1.000 35.33753  ?  11  ALA   C CB    1 
ATOM   2788 N  N     . VAL   C 2 13  ? -38.07481 22.04860  12.07755  1.000 34.78486  ?  12  VAL   C N     1 
ATOM   2789 C  CA    . VAL   C 2 13  ? -36.64711 22.19556  12.26275  1.000 32.34231  ?  12  VAL   C CA    1 
ATOM   2790 C  C     . VAL   C 2 13  ? -36.26636 23.46931  11.54088  1.000 42.94234  ?  12  VAL   C C     1 
ATOM   2791 O  O     . VAL   C 2 13  ? -36.37000 23.53467  10.30643  1.000 37.28224  ?  12  VAL   C O     1 
ATOM   2792 C  CB    . VAL   C 2 13  ? -35.86436 20.99816  11.71837  1.000 30.46503  ?  12  VAL   C CB    1 
ATOM   2793 C  CG1   . VAL   C 2 13  ? -34.39369 21.19508  11.96102  1.000 37.12898  ?  12  VAL   C CG1   1 
ATOM   2794 C  CG2   . VAL   C 2 13  ? -36.36869 19.69756  12.33701  1.000 34.13388  ?  12  VAL   C CG2   1 
ATOM   2795 N  N     . ASP   C 2 14  ? -35.85028 24.48663  12.30209  1.000 33.66848  ?  13  ASP   C N     1 
ATOM   2796 C  CA    . ASP   C 2 14  ? -35.49062 25.78621  11.72623  1.000 39.34474  ?  13  ASP   C CA    1 
ATOM   2797 C  C     . ASP   C 2 14  ? -36.62536 26.31730  10.86112  1.000 40.29328  ?  13  ASP   C C     1 
ATOM   2798 O  O     . ASP   C 2 14  ? -36.40146 26.84283  9.76913   1.000 39.04488  ?  13  ASP   C O     1 
ATOM   2799 C  CB    . ASP   C 2 14  ? -34.19082 25.70543  10.91476  1.000 33.89858  ?  13  ASP   C CB    1 
ATOM   2800 C  CG    . ASP   C 2 14  ? -32.95734 25.71134  11.78679  1.000 42.37532  ?  13  ASP   C CG    1 
ATOM   2801 O  OD1   . ASP   C 2 14  ? -33.09183 25.97738  13.00713  1.000 43.45256  ?  13  ASP   C OD1   1 
ATOM   2802 O  OD2   . ASP   C 2 14  ? -31.84628 25.45479  11.25700  1.000 39.36839  -1 13  ASP   C OD2   1 
ATOM   2803 N  N     . GLY   C 2 15  ? -37.86137 26.12413  11.32562  1.000 41.20342  ?  14  GLY   C N     1 
ATOM   2804 C  CA    . GLY   C 2 15  ? -39.02436 26.57599  10.60475  1.000 38.39756  ?  14  GLY   C CA    1 
ATOM   2805 C  C     . GLY   C 2 15  ? -39.53103 25.62664  9.54592   1.000 36.88948  ?  14  GLY   C C     1 
ATOM   2806 O  O     . GLY   C 2 15  ? -40.62569 25.84663  9.02179   1.000 43.09812  ?  14  GLY   C O     1 
ATOM   2807 N  N     . GLU   C 2 16  ? -38.79405 24.58147  9.22919   1.000 36.94766  ?  15  GLU   C N     1 
ATOM   2808 C  CA    . GLU   C 2 16  ? -39.20208 23.67588  8.15593   1.000 41.67259  ?  15  GLU   C CA    1 
ATOM   2809 C  C     . GLU   C 2 16  ? -39.88048 22.44679  8.73245   1.000 44.25633  ?  15  GLU   C C     1 
ATOM   2810 O  O     . GLU   C 2 16  ? -39.30589 21.78919  9.61446   1.000 43.43088  ?  15  GLU   C O     1 
ATOM   2811 C  CB    . GLU   C 2 16  ? -37.99694 23.25230  7.31714   1.000 42.50903  ?  15  GLU   C CB    1 
ATOM   2812 C  CG    . GLU   C 2 16  ? -37.59192 24.29766  6.29246   1.000 51.05823  ?  15  GLU   C CG    1 
ATOM   2813 C  CD    . GLU   C 2 16  ? -38.77680 24.74080  5.45181   1.000 54.30473  ?  15  GLU   C CD    1 
ATOM   2814 O  OE1   . GLU   C 2 16  ? -39.25250 23.93341  4.62177   1.000 56.03488  ?  15  GLU   C OE1   1 
ATOM   2815 O  OE2   . GLU   C 2 16  ? -39.25142 25.88083  5.65254   1.000 54.60476  -1 15  GLU   C OE2   1 
ATOM   2816 N  N     . PRO   C 2 17  ? -41.07792 22.10480  8.26373   1.000 35.39264  ?  16  PRO   C N     1 
ATOM   2817 C  CA    . PRO   C 2 17  ? -41.80449 20.97107  8.84649   1.000 36.74775  ?  16  PRO   C CA    1 
ATOM   2818 C  C     . PRO   C 2 17  ? -41.00816 19.68051  8.77087   1.000 38.36118  ?  16  PRO   C C     1 
ATOM   2819 O  O     . PRO   C 2 17  ? -40.37379 19.37283  7.76068   1.000 35.66059  ?  16  PRO   C O     1 
ATOM   2820 C  CB    . PRO   C 2 17  ? -43.08215 20.90164  8.00222   1.000 37.53765  ?  16  PRO   C CB    1 
ATOM   2821 C  CG    . PRO   C 2 17  ? -43.27195 22.31807  7.53720   1.000 39.56769  ?  16  PRO   C CG    1 
ATOM   2822 C  CD    . PRO   C 2 17  ? -41.89351 22.83996  7.28407   1.000 38.17646  ?  16  PRO   C CD    1 
ATOM   2823 N  N     . LEU   C 2 18  ? -41.02774 18.93291  9.87642   1.000 38.44959  ?  17  LEU   C N     1 
ATOM   2824 C  CA    . LEU   C 2 18  ? -40.35519 17.64422  9.97046   1.000 33.26553  ?  17  LEU   C CA    1 
ATOM   2825 C  C     . LEU   C 2 18  ? -41.34695 16.49314  9.99679   1.000 36.44682  ?  17  LEU   C C     1 
ATOM   2826 O  O     . LEU   C 2 18  ? -41.25055 15.57674  9.17784   1.000 35.59289  ?  17  LEU   C O     1 
ATOM   2827 C  CB    . LEU   C 2 18  ? -39.45438 17.60801  11.21181  1.000 35.65759  ?  17  LEU   C CB    1 
ATOM   2828 C  CG    . LEU   C 2 18  ? -38.67198 16.32153  11.49092  1.000 39.80510  ?  17  LEU   C CG    1 
ATOM   2829 C  CD1   . LEU   C 2 18  ? -37.52698 16.14703  10.50481  1.000 34.76558  ?  17  LEU   C CD1   1 
ATOM   2830 C  CD2   . LEU   C 2 18  ? -38.16270 16.30960  12.94807  1.000 33.31752  ?  17  LEU   C CD2   1 
ATOM   2831 N  N     . GLY   C 2 19  ? -42.30680 16.50840  10.91643  1.000 35.12558  ?  18  GLY   C N     1 
ATOM   2832 C  CA    . GLY   C 2 19  ? -43.31348 15.46473  10.93220  1.000 30.89036  ?  18  GLY   C CA    1 
ATOM   2833 C  C     . GLY   C 2 19  ? -44.23915 15.62757  12.11783  1.000 29.57673  ?  18  GLY   C C     1 
ATOM   2834 O  O     . GLY   C 2 19  ? -44.13377 16.58141  12.88965  1.000 33.90387  ?  18  GLY   C O     1 
ATOM   2835 N  N     . ARG   C 2 20  ? -45.13860 14.66690  12.26529  1.000 33.04400  ?  19  ARG   C N     1 
ATOM   2836 C  CA    . ARG   C 2 20  ? -46.12974 14.67784  13.33124  1.000 29.07174  ?  19  ARG   C CA    1 
ATOM   2837 C  C     . ARG   C 2 20  ? -45.87404 13.52537  14.29395  1.000 27.72870  ?  19  ARG   C C     1 
ATOM   2838 O  O     . ARG   C 2 20  ? -45.66170 12.38668  13.86716  1.000 28.22755  ?  19  ARG   C O     1 
ATOM   2839 C  CB    . ARG   C 2 20  ? -47.54383 14.58544  12.76302  1.000 34.37163  ?  19  ARG   C CB    1 
ATOM   2840 C  CG    . ARG   C 2 20  ? -48.61930 14.31614  13.80550  1.000 34.04842  ?  19  ARG   C CG    1 
ATOM   2841 C  CD    . ARG   C 2 20  ? -50.02558 14.52019  13.23683  1.000 29.13509  ?  19  ARG   C CD    1 
ATOM   2842 N  NE    . ARG   C 2 20  ? -50.27497 15.93047  12.98777  1.000 37.16754  ?  19  ARG   C NE    1 
ATOM   2843 C  CZ    . ARG   C 2 20  ? -51.46097 16.46042  12.72347  1.000 38.22363  ?  19  ARG   C CZ    1 
ATOM   2844 N  NH1   . ARG   C 2 20  ? -52.56080 15.72225  12.70256  1.000 42.15527  ?  19  ARG   C NH1   1 
ATOM   2845 N  NH2   . ARG   C 2 20  ? -51.54690 17.76708  12.49792  1.000 32.07914  ?  19  ARG   C NH2   1 
ATOM   2846 N  N     . VAL   C 2 21  ? -45.90174 13.82189  15.59192  1.000 31.35115  ?  20  VAL   C N     1 
ATOM   2847 C  CA    . VAL   C 2 21  ? -45.83365 12.80269  16.62759  1.000 30.06020  ?  20  VAL   C CA    1 
ATOM   2848 C  C     . VAL   C 2 21  ? -47.16159 12.81604  17.35656  1.000 29.82521  ?  20  VAL   C C     1 
ATOM   2849 O  O     . VAL   C 2 21  ? -47.67221 13.88609  17.70409  1.000 34.60914  ?  20  VAL   C O     1 
ATOM   2850 C  CB    . VAL   C 2 21  ? -44.67778 13.03750  17.61550  1.000 32.08506  ?  20  VAL   C CB    1 
ATOM   2851 C  CG1   . VAL   C 2 21  ? -44.51675 11.80162  18.54418  1.000 29.76381  ?  20  VAL   C CG1   1 
ATOM   2852 C  CG2   . VAL   C 2 21  ? -43.40845 13.32100  16.88300  1.000 32.59164  ?  20  VAL   C CG2   1 
ATOM   2853 N  N     . SER   C 2 22  ? -47.72381 11.64261  17.58520  1.000 30.89467  ?  21  SER   C N     1 
ATOM   2854 C  CA    . SER   C 2 22  ? -48.93549 11.55219  18.37729  1.000 33.18791  ?  21  SER   C CA    1 
ATOM   2855 C  C     . SER   C 2 22  ? -48.67362 10.68268  19.59548  1.000 31.79253  ?  21  SER   C C     1 
ATOM   2856 O  O     . SER   C 2 22  ? -47.86348 9.74974   19.55815  1.000 31.56771  ?  21  SER   C O     1 
ATOM   2857 C  CB    . SER   C 2 22  ? -50.09673 11.00018  17.57002  1.000 28.27167  ?  21  SER   C CB    1 
ATOM   2858 O  OG    . SER   C 2 22  ? -49.86191 9.63825   17.31689  1.000 33.58769  ?  21  SER   C OG    1 
ATOM   2859 N  N     . PHE   C 2 23  ? -49.38953 10.99896  20.67293  1.000 32.98486  ?  22  PHE   C N     1 
ATOM   2860 C  CA    . PHE   C 2 23  ? -49.14278 10.45422  21.99743  1.000 28.69308  ?  22  PHE   C CA    1 
ATOM   2861 C  C     . PHE   C 2 23  ? -50.46140 9.96497   22.57411  1.000 28.41508  ?  22  PHE   C C     1 
ATOM   2862 O  O     . PHE   C 2 23  ? -51.44394 10.70955  22.57855  1.000 31.14942  ?  22  PHE   C O     1 
ATOM   2863 C  CB    . PHE   C 2 23  ? -48.57335 11.51913  22.94905  1.000 28.98057  ?  22  PHE   C CB    1 
ATOM   2864 C  CG    . PHE   C 2 23  ? -47.31519 12.17850  22.48619  1.000 30.96618  ?  22  PHE   C CG    1 
ATOM   2865 C  CD1   . PHE   C 2 23  ? -46.08297 11.58086  22.70205  1.000 32.43860  ?  22  PHE   C CD1   1 
ATOM   2866 C  CD2   . PHE   C 2 23  ? -47.35655 13.43564  21.90519  1.000 34.10212  ?  22  PHE   C CD2   1 
ATOM   2867 C  CE1   . PHE   C 2 23  ? -44.90476 12.21644  22.29022  1.000 32.26996  ?  22  PHE   C CE1   1 
ATOM   2868 C  CE2   . PHE   C 2 23  ? -46.19545 14.07895  21.51498  1.000 33.58110  ?  22  PHE   C CE2   1 
ATOM   2869 C  CZ    . PHE   C 2 23  ? -44.96770 13.46912  21.71156  1.000 32.14645  ?  22  PHE   C CZ    1 
ATOM   2870 N  N     . GLU   C 2 24  ? -50.48014 8.73171   23.06774  1.000 31.57494  ?  23  GLU   C N     1 
ATOM   2871 C  CA    . GLU   C 2 24  ? -51.53346 8.30328   23.97387  1.000 32.27687  ?  23  GLU   C CA    1 
ATOM   2872 C  C     . GLU   C 2 24  ? -51.19266 8.76485   25.38652  1.000 32.70930  ?  23  GLU   C C     1 
ATOM   2873 O  O     . GLU   C 2 24  ? -50.04309 8.67216   25.81903  1.000 32.12574  ?  23  GLU   C O     1 
ATOM   2874 C  CB    . GLU   C 2 24  ? -51.70291 6.78573   23.93975  1.000 34.37565  ?  23  GLU   C CB    1 
ATOM   2875 C  CG    . GLU   C 2 24  ? -52.71365 6.29837   24.96848  1.000 41.67727  ?  23  GLU   C CG    1 
ATOM   2876 C  CD    . GLU   C 2 24  ? -52.88551 4.79040   24.97945  1.000 43.94847  ?  23  GLU   C CD    1 
ATOM   2877 O  OE1   . GLU   C 2 24  ? -52.04916 4.07678   24.39149  1.000 36.92781  ?  23  GLU   C OE1   1 
ATOM   2878 O  OE2   . GLU   C 2 24  ? -53.86723 4.32564   25.58603  1.000 52.73322  -1 23  GLU   C OE2   1 
ATOM   2879 N  N     . LEU   C 2 25  ? -52.18591 9.30803   26.08817  1.000 30.99713  ?  24  LEU   C N     1 
ATOM   2880 C  CA    . LEU   C 2 25  ? -52.02976 9.77837   27.46146  1.000 34.54952  ?  24  LEU   C CA    1 
ATOM   2881 C  C     . LEU   C 2 25  ? -52.78302 8.82199   28.37593  1.000 27.89897  ?  24  LEU   C C     1 
ATOM   2882 O  O     . LEU   C 2 25  ? -53.96868 8.57108   28.17171  1.000 32.83046  ?  24  LEU   C O     1 
ATOM   2883 C  CB    . LEU   C 2 25  ? -52.54116 11.21604  27.61190  1.000 36.23038  ?  24  LEU   C CB    1 
ATOM   2884 C  CG    . LEU   C 2 25  ? -52.02047 12.20265  26.54995  1.000 33.90511  ?  24  LEU   C CG    1 
ATOM   2885 C  CD1   . LEU   C 2 25  ? -52.48703 13.65497  26.78327  1.000 32.40470  ?  24  LEU   C CD1   1 
ATOM   2886 C  CD2   . LEU   C 2 25  ? -50.48176 12.15509  26.42609  1.000 32.69199  ?  24  LEU   C CD2   1 
ATOM   2887 N  N     . PHE   C 2 26  ? -52.09466 8.27034   29.36513  1.000 31.49310  ?  25  PHE   C N     1 
ATOM   2888 C  CA    . PHE   C 2 26  ? -52.69499 7.24317   30.22462  1.000 35.45906  ?  25  PHE   C CA    1 
ATOM   2889 C  C     . PHE   C 2 26  ? -53.50324 7.90810   31.34615  1.000 32.04822  ?  25  PHE   C C     1 
ATOM   2890 O  O     . PHE   C 2 26  ? -53.15708 7.88854   32.52585  1.000 33.83584  ?  25  PHE   C O     1 
ATOM   2891 C  CB    . PHE   C 2 26  ? -51.61547 6.30538   30.74499  1.000 30.70383  ?  25  PHE   C CB    1 
ATOM   2892 C  CG    . PHE   C 2 26  ? -50.79691 5.67901   29.64768  1.000 34.87450  ?  25  PHE   C CG    1 
ATOM   2893 C  CD1   . PHE   C 2 26  ? -51.41537 4.91017   28.65623  1.000 40.29276  ?  25  PHE   C CD1   1 
ATOM   2894 C  CD2   . PHE   C 2 26  ? -49.41837 5.87135   29.58124  1.000 32.20546  ?  25  PHE   C CD2   1 
ATOM   2895 C  CE1   . PHE   C 2 26  ? -50.67117 4.33440   27.62840  1.000 32.73764  ?  25  PHE   C CE1   1 
ATOM   2896 C  CE2   . PHE   C 2 26  ? -48.66553 5.29147   28.54899  1.000 31.50953  ?  25  PHE   C CE2   1 
ATOM   2897 C  CZ    . PHE   C 2 26  ? -49.30129 4.52056   27.57485  1.000 30.41561  ?  25  PHE   C CZ    1 
ATOM   2898 N  N     . ALA   C 2 27  ? -54.61198 8.52711   30.93344  1.000 38.54046  ?  26  ALA   C N     1 
ATOM   2899 C  CA    . ALA   C 2 27  ? -55.53499 9.13698   31.88230  1.000 37.81063  ?  26  ALA   C CA    1 
ATOM   2900 C  C     . ALA   C 2 27  ? -56.13246 8.10540   32.82979  1.000 37.92710  ?  26  ALA   C C     1 
ATOM   2901 O  O     . ALA   C 2 27  ? -56.49497 8.44350   33.96064  1.000 32.49655  ?  26  ALA   C O     1 
ATOM   2902 C  CB    . ALA   C 2 27  ? -56.64796 9.85734   31.13370  1.000 33.68236  ?  26  ALA   C CB    1 
ATOM   2903 N  N     . ASP   C 2 28  ? -56.26349 6.85443   32.38044  1.000 33.46199  ?  27  ASP   C N     1 
ATOM   2904 C  CA    . ASP   C 2 28  ? -56.78274 5.81384   33.25630  1.000 36.06087  ?  27  ASP   C CA    1 
ATOM   2905 C  C     . ASP   C 2 28  ? -55.84736 5.50192   34.41312  1.000 38.11619  ?  27  ASP   C C     1 
ATOM   2906 O  O     . ASP   C 2 28  ? -56.30431 4.92833   35.40525  1.000 36.59380  ?  27  ASP   C O     1 
ATOM   2907 C  CB    . ASP   C 2 28  ? -57.07985 4.53258   32.46615  1.000 42.25569  ?  27  ASP   C CB    1 
ATOM   2908 C  CG    . ASP   C 2 28  ? -55.96175 4.15155   31.47843  1.000 39.35928  ?  27  ASP   C CG    1 
ATOM   2909 O  OD1   . ASP   C 2 28  ? -54.81553 4.64395   31.58739  1.000 36.74681  ?  27  ASP   C OD1   1 
ATOM   2910 O  OD2   . ASP   C 2 28  ? -56.23880 3.33834   30.57415  1.000 51.03595  -1 27  ASP   C OD2   1 
ATOM   2911 N  N     . LYS   C 2 29  ? -54.56272 5.86423   34.32616  1.000 32.07317  ?  28  LYS   C N     1 
ATOM   2912 C  CA    . LYS   C 2 29  ? -53.61971 5.65416   35.42252  1.000 34.96504  ?  28  LYS   C CA    1 
ATOM   2913 C  C     . LYS   C 2 29  ? -53.15178 6.93853   36.08836  1.000 33.48169  ?  28  LYS   C C     1 
ATOM   2914 O  O     . LYS   C 2 29  ? -52.96885 6.96673   37.30660  1.000 33.82835  ?  28  LYS   C O     1 
ATOM   2915 C  CB    . LYS   C 2 29  ? -52.39724 4.88718   34.92228  1.000 35.82435  ?  28  LYS   C CB    1 
ATOM   2916 C  CG    . LYS   C 2 29  ? -52.73390 3.64358   34.15403  1.000 37.65089  ?  28  LYS   C CG    1 
ATOM   2917 C  CD    . LYS   C 2 29  ? -52.41470 2.43573   34.96462  1.000 37.91008  ?  28  LYS   C CD    1 
ATOM   2918 C  CE    . LYS   C 2 29  ? -52.01092 1.28416   34.07871  1.000 34.46288  ?  28  LYS   C CE    1 
ATOM   2919 N  NZ    . LYS   C 2 29  ? -53.07228 0.89281   33.10413  1.000 33.04692  ?  28  LYS   C NZ    1 
ATOM   2920 N  N     . VAL   C 2 30  ? -52.93429 8.00245   35.32031  1.000 32.48580  ?  29  VAL   C N     1 
ATOM   2921 C  CA    . VAL   C 2 30  ? -52.51243 9.28152   35.88169  1.000 29.08792  ?  29  VAL   C CA    1 
ATOM   2922 C  C     . VAL   C 2 30  ? -53.42662 10.35874  35.31517  1.000 34.11254  ?  29  VAL   C C     1 
ATOM   2923 O  O     . VAL   C 2 30  ? -53.02693 11.09874  34.39857  1.000 30.56132  ?  29  VAL   C O     1 
ATOM   2924 C  CB    . VAL   C 2 30  ? -51.04079 9.57122   35.56962  1.000 34.18938  ?  29  VAL   C CB    1 
ATOM   2925 C  CG1   . VAL   C 2 30  ? -50.15983 8.98426   36.63322  1.000 33.90064  ?  29  VAL   C CG1   1 
ATOM   2926 C  CG2   . VAL   C 2 30  ? -50.69603 8.98276   34.22855  1.000 36.36410  ?  29  VAL   C CG2   1 
ATOM   2927 N  N     . PRO   C 2 31  ? -54.66762 10.46246  35.80076  1.000 36.00655  ?  30  PRO   C N     1 
ATOM   2928 C  CA    . PRO   C 2 31  ? -55.60903 11.38750  35.15653  1.000 37.18129  ?  30  PRO   C CA    1 
ATOM   2929 C  C     . PRO   C 2 31  ? -55.20768 12.84010  35.30801  1.000 34.63885  ?  30  PRO   C C     1 
ATOM   2930 O  O     . PRO   C 2 31  ? -55.41909 13.63200  34.37975  1.000 34.11612  ?  30  PRO   C O     1 
ATOM   2931 C  CB    . PRO   C 2 31  ? -56.94703 11.07173  35.85503  1.000 37.44492  ?  30  PRO   C CB    1 
ATOM   2932 C  CG    . PRO   C 2 31  ? -56.56177 10.43773  37.15339  1.000 30.93127  ?  30  PRO   C CG    1 
ATOM   2933 C  CD    . PRO   C 2 31  ? -55.30264 9.67644   36.87810  1.000 32.29146  ?  30  PRO   C CD    1 
ATOM   2934 N  N     . LYS   C 2 32  ? -54.61154 13.21085  36.44361  1.000 32.45029  ?  31  LYS   C N     1 
ATOM   2935 C  CA    . LYS   C 2 32  ? -54.30443 14.61909  36.67006  1.000 34.50992  ?  31  LYS   C CA    1 
ATOM   2936 C  C     . LYS   C 2 32  ? -53.10934 15.06340  35.83516  1.000 33.48721  ?  31  LYS   C C     1 
ATOM   2937 O  O     . LYS   C 2 32  ? -53.07424 16.19656  35.34611  1.000 32.14773  ?  31  LYS   C O     1 
ATOM   2938 C  CB    . LYS   C 2 32  ? -54.04363 14.87158  38.15258  1.000 37.54572  ?  31  LYS   C CB    1 
ATOM   2939 C  CG    . LYS   C 2 32  ? -54.07269 16.34505  38.53332  1.000 40.23723  ?  31  LYS   C CG    1 
ATOM   2940 C  CD    . LYS   C 2 32  ? -53.88515 16.57349  40.04530  1.000 38.86658  ?  31  LYS   C CD    1 
ATOM   2941 C  CE    . LYS   C 2 32  ? -54.05336 18.06060  40.39308  1.000 40.63467  ?  31  LYS   C CE    1 
ATOM   2942 N  NZ    . LYS   C 2 32  ? -53.10575 18.51918  41.43508  1.000 41.83744  ?  31  LYS   C NZ    1 
ATOM   2943 N  N     . THR   C 2 33  ? -52.12461 14.18465  35.66858  1.000 30.61168  ?  32  THR   C N     1 
ATOM   2944 C  CA    . THR   C 2 33  ? -50.94428 14.52626  34.87891  1.000 35.20916  ?  32  THR   C CA    1 
ATOM   2945 C  C     . THR   C 2 33  ? -51.26379 14.49142  33.39162  1.000 30.95811  ?  32  THR   C C     1 
ATOM   2946 O  O     . THR   C 2 33  ? -50.82067 15.36249  32.63694  1.000 31.62811  ?  32  THR   C O     1 
ATOM   2947 C  CB    . THR   C 2 33  ? -49.80778 13.56481  35.22274  1.000 34.43636  ?  32  THR   C CB    1 
ATOM   2948 O  OG1   . THR   C 2 33  ? -49.60958 13.57025  36.63686  1.000 32.73017  ?  32  THR   C OG1   1 
ATOM   2949 C  CG2   . THR   C 2 33  ? -48.50656 13.96989  34.54331  1.000 26.78817  ?  32  THR   C CG2   1 
ATOM   2950 N  N     . ALA   C 2 34  ? -52.06071 13.50722  32.96527  1.000 29.79282  ?  33  ALA   C N     1 
ATOM   2951 C  CA    . ALA   C 2 34  ? -52.46649 13.40991  31.56825  1.000 28.47551  ?  33  ALA   C CA    1 
ATOM   2952 C  C     . ALA   C 2 34  ? -53.27055 14.63023  31.14303  1.000 35.74069  ?  33  ALA   C C     1 
ATOM   2953 O  O     . ALA   C 2 34  ? -53.01748 15.21670  30.08564  1.000 34.69571  ?  33  ALA   C O     1 
ATOM   2954 C  CB    . ALA   C 2 34  ? -53.27420 12.13329  31.34787  1.000 29.07850  ?  33  ALA   C CB    1 
ATOM   2955 N  N     . GLU   C 2 35  ? -54.24579 15.03048  31.96345  1.000 36.61160  ?  34  GLU   C N     1 
ATOM   2956 C  CA    . GLU   C 2 35  ? -55.08287 16.17481  31.62572  1.000 35.36580  ?  34  GLU   C CA    1 
ATOM   2957 C  C     . GLU   C 2 35  ? -54.27546 17.46185  31.54735  1.000 33.56857  ?  34  GLU   C C     1 
ATOM   2958 O  O     . GLU   C 2 35  ? -54.58712 18.33928  30.73680  1.000 36.18906  ?  34  GLU   C O     1 
ATOM   2959 C  CB    . GLU   C 2 35  ? -56.22053 16.30744  32.64713  1.000 37.57886  ?  34  GLU   C CB    1 
ATOM   2960 C  CG    . GLU   C 2 35  ? -57.01531 17.60409  32.57006  1.000 37.30575  ?  34  GLU   C CG    1 
ATOM   2961 C  CD    . GLU   C 2 35  ? -57.81200 17.77236  31.28804  1.000 34.73189  ?  34  GLU   C CD    1 
ATOM   2962 O  OE1   . GLU   C 2 35  ? -58.05199 16.78938  30.54860  1.000 39.52530  ?  34  GLU   C OE1   1 
ATOM   2963 O  OE2   . GLU   C 2 35  ? -58.21694 18.91748  31.00783  1.000 43.32816  -1 34  GLU   C OE2   1 
ATOM   2964 N  N     . ASN   C 2 36  ? -53.23576 17.59640  32.36390  1.000 34.24854  ?  35  ASN   C N     1 
ATOM   2965 C  CA    . ASN   C 2 36  ? -52.37292 18.76535  32.24657  1.000 36.21970  ?  35  ASN   C CA    1 
ATOM   2966 C  C     . ASN   C 2 36  ? -51.74606 18.83000  30.85915  1.000 32.91996  ?  35  ASN   C C     1 
ATOM   2967 O  O     . ASN   C 2 36  ? -51.87563 19.83189  30.14830  1.000 30.41369  ?  35  ASN   C O     1 
ATOM   2968 C  CB    . ASN   C 2 36  ? -51.29422 18.73989  33.32826  1.000 34.24890  ?  35  ASN   C CB    1 
ATOM   2969 C  CG    . ASN   C 2 36  ? -50.28774 19.85290  33.16051  1.000 32.62776  ?  35  ASN   C CG    1 
ATOM   2970 O  OD1   . ASN   C 2 36  ? -50.62764 21.02422  33.25459  1.000 35.82344  ?  35  ASN   C OD1   1 
ATOM   2971 N  ND2   . ASN   C 2 36  ? -49.03429 19.48931  32.90069  1.000 35.88208  ?  35  ASN   C ND2   1 
ATOM   2972 N  N     . PHE   C 2 37  ? -51.09266 17.74261  30.44532  1.000 31.56608  ?  36  PHE   C N     1 
ATOM   2973 C  CA    . PHE   C 2 37  ? -50.48810 17.69838  29.11904  1.000 30.58624  ?  36  PHE   C CA    1 
ATOM   2974 C  C     . PHE   C 2 37  ? -51.53150 17.90736  28.03130  1.000 34.47548  ?  36  PHE   C C     1 
ATOM   2975 O  O     . PHE   C 2 37  ? -51.26839 18.59334  27.03621  1.000 32.64140  ?  36  PHE   C O     1 
ATOM   2976 C  CB    . PHE   C 2 37  ? -49.77402 16.36011  28.92483  1.000 34.76186  ?  36  PHE   C CB    1 
ATOM   2977 C  CG    . PHE   C 2 37  ? -48.86647 16.30250  27.70878  1.000 28.24435  ?  36  PHE   C CG    1 
ATOM   2978 C  CD1   . PHE   C 2 37  ? -47.54281 16.67212  27.80217  1.000 31.91253  ?  36  PHE   C CD1   1 
ATOM   2979 C  CD2   . PHE   C 2 37  ? -49.34082 15.84763  26.49642  1.000 26.97724  ?  36  PHE   C CD2   1 
ATOM   2980 C  CE1   . PHE   C 2 37  ? -46.69826 16.59782  26.69058  1.000 34.04619  ?  36  PHE   C CE1   1 
ATOM   2981 C  CE2   . PHE   C 2 37  ? -48.51273 15.77506  25.38754  1.000 31.95487  ?  36  PHE   C CE2   1 
ATOM   2982 C  CZ    . PHE   C 2 37  ? -47.19229 16.14670  25.48623  1.000 33.18518  ?  36  PHE   C CZ    1 
ATOM   2983 N  N     . ARG   C 2 38  ? -52.72363 17.31756  28.20438  1.000 36.00982  ?  37  ARG   C N     1 
ATOM   2984 C  CA    . ARG   C 2 38  ? -53.75930 17.39846  27.18192  1.000 32.95919  ?  37  ARG   C CA    1 
ATOM   2985 C  C     . ARG   C 2 38  ? -54.18294 18.84215  26.95053  1.000 35.32838  ?  37  ARG   C C     1 
ATOM   2986 O  O     . ARG   C 2 38  ? -54.23753 19.30843  25.80863  1.000 33.34051  ?  37  ARG   C O     1 
ATOM   2987 C  CB    . ARG   C 2 38  ? -54.96813 16.54578  27.57272  1.000 29.68483  ?  37  ARG   C CB    1 
ATOM   2988 C  CG    . ARG   C 2 38  ? -55.99590 16.38897  26.44715  1.000 36.32897  ?  37  ARG   C CG    1 
ATOM   2989 C  CD    . ARG   C 2 38  ? -57.39393 16.07670  26.97291  1.000 34.62237  ?  37  ARG   C CD    1 
ATOM   2990 N  NE    . ARG   C 2 38  ? -57.89015 17.19068  27.76994  1.000 38.17547  ?  37  ARG   C NE    1 
ATOM   2991 C  CZ    . ARG   C 2 38  ? -58.41884 18.29669  27.26636  1.000 37.75393  ?  37  ARG   C CZ    1 
ATOM   2992 N  NH1   . ARG   C 2 38  ? -58.61292 18.44231  25.96319  1.000 36.19009  ?  37  ARG   C NH1   1 
ATOM   2993 N  NH2   . ARG   C 2 38  ? -58.75256 19.28590  28.09021  1.000 40.79301  ?  37  ARG   C NH2   1 
ATOM   2994 N  N     . ALA   C 2 39  ? -54.48649 19.56436  28.02789  1.000 33.45349  ?  38  ALA   C N     1 
ATOM   2995 C  CA    . ALA   C 2 39  ? -54.92732 20.94817  27.89348  1.000 38.15256  ?  38  ALA   C CA    1 
ATOM   2996 C  C     . ALA   C 2 39  ? -53.80418 21.83467  27.36648  1.000 39.34406  ?  38  ALA   C C     1 
ATOM   2997 O  O     . ALA   C 2 39  ? -54.03698 22.70196  26.51238  1.000 42.61400  ?  38  ALA   C O     1 
ATOM   2998 C  CB    . ALA   C 2 39  ? -55.43866 21.46055  29.24020  1.000 36.66062  ?  38  ALA   C CB    1 
ATOM   2999 N  N     . LEU   C 2 40  ? -52.57821 21.62786  27.86537  1.000 36.33532  ?  39  LEU   C N     1 
ATOM   3000 C  CA    . LEU   C 2 40  ? -51.42481 22.33418  27.32039  1.000 34.35708  ?  39  LEU   C CA    1 
ATOM   3001 C  C     . LEU   C 2 40  ? -51.23755 22.05396  25.82650  1.000 35.31119  ?  39  LEU   C C     1 
ATOM   3002 O  O     . LEU   C 2 40  ? -50.79815 22.94067  25.08876  1.000 36.68418  ?  39  LEU   C O     1 
ATOM   3003 C  CB    . LEU   C 2 40  ? -50.17226 21.96614  28.10584  1.000 30.26450  ?  39  LEU   C CB    1 
ATOM   3004 C  CG    . LEU   C 2 40  ? -50.13872 22.51453  29.53502  1.000 33.18889  ?  39  LEU   C CG    1 
ATOM   3005 C  CD1   . LEU   C 2 40  ? -48.85247 22.16252  30.24224  1.000 29.64478  ?  39  LEU   C CD1   1 
ATOM   3006 C  CD2   . LEU   C 2 40  ? -50.35028 24.02410  29.52931  1.000 34.22659  ?  39  LEU   C CD2   1 
ATOM   3007 N  N     . SER   C 2 41  ? -51.58580 20.84798  25.35742  1.000 32.25467  ?  40  SER   C N     1 
ATOM   3008 C  CA    . SER   C 2 41  ? -51.44325 20.53130  23.93769  1.000 32.76779  ?  40  SER   C CA    1 
ATOM   3009 C  C     . SER   C 2 41  ? -52.50707 21.21244  23.06850  1.000 37.52687  ?  40  SER   C C     1 
ATOM   3010 O  O     . SER   C 2 41  ? -52.23708 21.53114  21.90177  1.000 34.12071  ?  40  SER   C O     1 
ATOM   3011 C  CB    . SER   C 2 41  ? -51.49201 19.01618  23.72984  1.000 29.55825  ?  40  SER   C CB    1 
ATOM   3012 O  OG    . SER   C 2 41  ? -50.34106 18.38744  24.27303  1.000 36.41943  ?  40  SER   C OG    1 
ATOM   3013 N  N     . THR   C 2 42  ? -53.72356 21.42417  23.59294  1.000 37.54272  ?  41  THR   C N     1 
ATOM   3014 C  CA    . THR   C 2 42  ? -54.74901 22.13765  22.82739  1.000 33.05048  ?  41  THR   C CA    1 
ATOM   3015 C  C     . THR   C 2 42  ? -54.62069 23.65239  22.94747  1.000 35.72902  ?  41  THR   C C     1 
ATOM   3016 O  O     . THR   C 2 42  ? -55.06805 24.37508  22.05037  1.000 39.92652  ?  41  THR   C O     1 
ATOM   3017 C  CB    . THR   C 2 42  ? -56.16071 21.72939  23.27272  1.000 34.64448  ?  41  THR   C CB    1 
ATOM   3018 O  OG1   . THR   C 2 42  ? -56.33033 22.02740  24.66517  1.000 41.37749  ?  41  THR   C OG1   1 
ATOM   3019 C  CG2   . THR   C 2 42  ? -56.41355 20.24391  23.05273  1.000 29.32542  ?  41  THR   C CG2   1 
ATOM   3020 N  N     . GLY   C 2 43  ? -54.01957 24.14820  24.02513  1.000 36.69507  ?  42  GLY   C N     1 
ATOM   3021 C  CA    . GLY   C 2 43  ? -53.98386 25.57993  24.25485  1.000 48.67038  ?  42  GLY   C CA    1 
ATOM   3022 C  C     . GLY   C 2 43  ? -55.29193 26.16631  24.74143  1.000 45.80423  ?  42  GLY   C C     1 
ATOM   3023 O  O     . GLY   C 2 43  ? -55.48773 27.38436  24.67154  1.000 45.85461  ?  42  GLY   C O     1 
ATOM   3024 N  N     . GLU   C 2 44  ? -56.19399 25.32775  25.25103  1.000 45.28121  ?  43  GLU   C N     1 
ATOM   3025 C  CA    . GLU   C 2 44  ? -57.54896 25.77226  25.54843  1.000 47.59342  ?  43  GLU   C CA    1 
ATOM   3026 C  C     . GLU   C 2 44  ? -57.63473 26.67221  26.77582  1.000 44.39476  ?  43  GLU   C C     1 
ATOM   3027 O  O     . GLU   C 2 44  ? -58.68917 27.27766  27.00062  1.000 52.11263  ?  43  GLU   C O     1 
ATOM   3028 C  CB    . GLU   C 2 44  ? -58.45689 24.55350  25.71189  1.000 47.78061  ?  43  GLU   C CB    1 
ATOM   3029 C  CG    . GLU   C 2 44  ? -58.11830 23.63569  26.88574  1.000 44.83738  ?  43  GLU   C CG    1 
ATOM   3030 C  CD    . GLU   C 2 44  ? -58.83195 22.30530  26.74961  1.000 48.54501  ?  43  GLU   C CD    1 
ATOM   3031 O  OE1   . GLU   C 2 44  ? -58.66520 21.65661  25.69589  1.000 47.52262  ?  43  GLU   C OE1   1 
ATOM   3032 O  OE2   . GLU   C 2 44  ? -59.58735 21.92195  27.66564  1.000 52.87661  -1 43  GLU   C OE2   1 
ATOM   3033 N  N     . LYS   C 2 45  ? -56.56571 26.78657  27.56213  1.000 44.39184  ?  44  LYS   C N     1 
ATOM   3034 C  CA    . LYS   C 2 45  ? -56.52789 27.67170  28.71734  1.000 45.17782  ?  44  LYS   C CA    1 
ATOM   3035 C  C     . LYS   C 2 45  ? -55.84448 29.00322  28.42335  1.000 46.76059  ?  44  LYS   C C     1 
ATOM   3036 O  O     . LYS   C 2 45  ? -55.59735 29.77811  29.35328  1.000 49.20776  ?  44  LYS   C O     1 
ATOM   3037 C  CB    . LYS   C 2 45  ? -55.81867 26.98101  29.88571  1.000 48.01694  ?  44  LYS   C CB    1 
ATOM   3038 C  CG    . LYS   C 2 45  ? -56.34362 25.58962  30.20972  1.000 48.80802  ?  44  LYS   C CG    1 
ATOM   3039 C  CD    . LYS   C 2 45  ? -57.66293 25.61723  30.97187  1.000 48.82305  ?  44  LYS   C CD    1 
ATOM   3040 C  CE    . LYS   C 2 45  ? -58.26225 24.20927  31.03253  1.000 51.25486  ?  44  LYS   C CE    1 
ATOM   3041 N  NZ    . LYS   C 2 45  ? -59.55262 24.13623  31.76411  1.000 53.88099  ?  44  LYS   C NZ    1 
ATOM   3042 N  N     . GLY   C 2 46  ? -55.52043 29.28267  27.16182  1.000 49.24019  ?  45  GLY   C N     1 
ATOM   3043 C  CA    . GLY   C 2 46  ? -54.85513 30.51565  26.79482  1.000 43.57289  ?  45  GLY   C CA    1 
ATOM   3044 C  C     . GLY   C 2 46  ? -53.35073 30.43323  26.73036  1.000 45.51355  ?  45  GLY   C C     1 
ATOM   3045 O  O     . GLY   C 2 46  ? -52.71336 31.41805  26.34509  1.000 49.17009  ?  45  GLY   C O     1 
ATOM   3046 N  N     . PHE   C 2 47  ? -52.76314 29.30328  27.11664  1.000 44.48090  ?  46  PHE   C N     1 
ATOM   3047 C  CA    . PHE   C 2 47  ? -51.33729 29.06977  26.95273  1.000 43.04177  ?  46  PHE   C CA    1 
ATOM   3048 C  C     . PHE   C 2 47  ? -51.12833 27.59356  26.62788  1.000 42.30083  ?  46  PHE   C C     1 
ATOM   3049 O  O     . PHE   C 2 47  ? -52.08775 26.81980  26.52176  1.000 42.04900  ?  46  PHE   C O     1 
ATOM   3050 C  CB    . PHE   C 2 47  ? -50.55203 29.49561  28.19832  1.000 38.20280  ?  46  PHE   C CB    1 
ATOM   3051 C  CG    . PHE   C 2 47  ? -51.14021 28.99325  29.49689  1.000 49.88030  ?  46  PHE   C CG    1 
ATOM   3052 C  CD1   . PHE   C 2 47  ? -50.73432 27.78346  30.04146  1.000 44.81400  ?  46  PHE   C CD1   1 
ATOM   3053 C  CD2   . PHE   C 2 47  ? -52.08325 29.74127  30.17983  1.000 41.45228  ?  46  PHE   C CD2   1 
ATOM   3054 C  CE1   . PHE   C 2 47  ? -51.26536 27.32905  31.23273  1.000 39.18011  ?  46  PHE   C CE1   1 
ATOM   3055 C  CE2   . PHE   C 2 47  ? -52.62415 29.28493  31.36898  1.000 42.53576  ?  46  PHE   C CE2   1 
ATOM   3056 C  CZ    . PHE   C 2 47  ? -52.21557 28.07714  31.89623  1.000 40.82641  ?  46  PHE   C CZ    1 
ATOM   3057 N  N     . GLY   C 2 48  ? -49.86897 27.20842  26.44881  1.000 34.51468  ?  47  GLY   C N     1 
ATOM   3058 C  CA    . GLY   C 2 48  ? -49.55534 25.81459  26.18906  1.000 38.65190  ?  47  GLY   C CA    1 
ATOM   3059 C  C     . GLY   C 2 48  ? -48.34872 25.66450  25.27419  1.000 35.71237  ?  47  GLY   C C     1 
ATOM   3060 O  O     . GLY   C 2 48  ? -47.56350 26.58482  25.10053  1.000 31.62004  ?  47  GLY   C O     1 
ATOM   3061 N  N     . TYR   C 2 49  ? -48.24703 24.47031  24.68115  1.000 34.94337  ?  48  TYR   C N     1 
ATOM   3062 C  CA    . TYR   C 2 49  ? -47.01373 24.01727  24.03768  1.000 31.20902  ?  48  TYR   C CA    1 
ATOM   3063 C  C     . TYR   C 2 49  ? -46.78780 24.61169  22.64965  1.000 36.16515  ?  48  TYR   C C     1 
ATOM   3064 O  O     . TYR   C 2 49  ? -45.63288 24.68474  22.20981  1.000 36.84585  ?  48  TYR   C O     1 
ATOM   3065 C  CB    . TYR   C 2 49  ? -47.01287 22.49132  23.91909  1.000 29.86667  ?  48  TYR   C CB    1 
ATOM   3066 C  CG    . TYR   C 2 49  ? -46.86242 21.76829  25.23373  1.000 27.09161  ?  48  TYR   C CG    1 
ATOM   3067 C  CD1   . TYR   C 2 49  ? -45.93618 22.17928  26.16375  1.000 27.56831  ?  48  TYR   C CD1   1 
ATOM   3068 C  CD2   . TYR   C 2 49  ? -47.66190 20.68094  25.53550  1.000 28.88308  ?  48  TYR   C CD2   1 
ATOM   3069 C  CE1   . TYR   C 2 49  ? -45.79592 21.52438  27.37178  1.000 30.64315  ?  48  TYR   C CE1   1 
ATOM   3070 C  CE2   . TYR   C 2 49  ? -47.53808 20.01120  26.74262  1.000 32.76298  ?  48  TYR   C CE2   1 
ATOM   3071 C  CZ    . TYR   C 2 49  ? -46.60331 20.43567  27.65348  1.000 24.43311  ?  48  TYR   C CZ    1 
ATOM   3072 O  OH    . TYR   C 2 49  ? -46.48112 19.77972  28.84299  1.000 25.51964  ?  48  TYR   C OH    1 
ATOM   3073 N  N     . LYS   C 2 50  ? -47.85046 24.99168  21.93122  1.000 33.29580  ?  49  LYS   C N     1 
ATOM   3074 C  CA    . LYS   C 2 50  ? -47.67644 25.47620  20.56436  1.000 39.38388  ?  49  LYS   C CA    1 
ATOM   3075 C  C     . LYS   C 2 50  ? -46.66550 26.61150  20.54188  1.000 37.60588  ?  49  LYS   C C     1 
ATOM   3076 O  O     . LYS   C 2 50  ? -46.73863 27.54209  21.35721  1.000 33.23319  ?  49  LYS   C O     1 
ATOM   3077 C  CB    . LYS   C 2 50  ? -49.00714 25.94275  19.98148  1.000 42.76517  ?  49  LYS   C CB    1 
ATOM   3078 C  CG    . LYS   C 2 50  ? -48.95876 26.31730  18.48773  1.000 39.95145  ?  49  LYS   C CG    1 
ATOM   3079 C  CD    . LYS   C 2 50  ? -50.32092 26.81993  18.04952  1.000 40.29664  ?  49  LYS   C CD    1 
ATOM   3080 C  CE    . LYS   C 2 50  ? -50.39579 27.08670  16.57482  1.000 50.14619  ?  49  LYS   C CE    1 
ATOM   3081 N  NZ    . LYS   C 2 50  ? -51.72445 27.66597  16.22369  1.000 53.60662  ?  49  LYS   C NZ    1 
ATOM   3082 N  N     . GLY   C 2 51  ? -45.68956 26.50216  19.63699  1.000 34.97765  ?  50  GLY   C N     1 
ATOM   3083 C  CA    . GLY   C 2 51  ? -44.64093 27.48856  19.52054  1.000 29.17528  ?  50  GLY   C CA    1 
ATOM   3084 C  C     . GLY   C 2 51  ? -43.40321 27.25364  20.36445  1.000 38.91382  ?  50  GLY   C C     1 
ATOM   3085 O  O     . GLY   C 2 51  ? -42.39113 27.93650  20.14516  1.000 40.29792  ?  50  GLY   C O     1 
ATOM   3086 N  N     . SER   C 2 52  ? -43.42737 26.32078  21.31582  1.000 33.36974  ?  51  SER   C N     1 
ATOM   3087 C  CA    . SER   C 2 52  ? -42.26724 26.14250  22.17445  1.000 32.73554  ?  51  SER   C CA    1 
ATOM   3088 C  C     . SER   C 2 52  ? -41.26685 25.16510  21.55362  1.000 32.14277  ?  51  SER   C C     1 
ATOM   3089 O  O     . SER   C 2 52  ? -41.55692 24.45873  20.58988  1.000 32.51218  ?  51  SER   C O     1 
ATOM   3090 C  CB    . SER   C 2 52  ? -42.68732 25.66166  23.56382  1.000 39.66129  ?  51  SER   C CB    1 
ATOM   3091 O  OG    . SER   C 2 52  ? -43.47569 24.48272  23.47871  1.000 33.01706  ?  51  SER   C OG    1 
ATOM   3092 N  N     A CYS   C 2 53  ? -40.07079 25.12201  22.12925  0.500 33.53497  ?  52  CYS   C N     1 
ATOM   3093 N  N     B CYS   C 2 53  ? -40.07663 25.12379  22.14305  0.500 34.03523  ?  52  CYS   C N     1 
ATOM   3094 C  CA    A CYS   C 2 53  ? -38.97674 24.36384  21.54793  0.500 35.57280  ?  52  CYS   C CA    1 
ATOM   3095 C  CA    B CYS   C 2 53  ? -38.95154 24.38016  21.60563  0.500 36.53222  ?  52  CYS   C CA    1 
ATOM   3096 C  C     A CYS   C 2 53  ? -38.57583 23.19262  22.43173  0.500 35.08199  ?  52  CYS   C C     1 
ATOM   3097 C  C     B CYS   C 2 53  ? -38.66784 23.13122  22.42635  0.500 36.52458  ?  52  CYS   C C     1 
ATOM   3098 O  O     A CYS   C 2 53  ? -38.81268 23.17502  23.64656  0.500 33.97985  ?  52  CYS   C O     1 
ATOM   3099 O  O     B CYS   C 2 53  ? -39.07736 23.00089  23.58736  0.500 33.81702  ?  52  CYS   C O     1 
ATOM   3100 C  CB    A CYS   C 2 53  ? -37.75362 25.25803  21.31497  0.500 36.77216  ?  52  CYS   C CB    1 
ATOM   3101 C  CB    B CYS   C 2 53  ? -37.68782 25.25084  21.57196  0.500 36.59911  ?  52  CYS   C CB    1 
ATOM   3102 S  SG    A CYS   C 2 53  ? -36.52264 25.15776  22.63076  0.500 43.41909  ?  52  CYS   C SG    1 
ATOM   3103 S  SG    B CYS   C 2 53  ? -37.78306 26.73505  20.54874  0.500 43.39091  ?  52  CYS   C SG    1 
ATOM   3104 N  N     . PHE   C 2 54  ? -37.95194 22.20762  21.79717  1.000 32.31212  ?  53  PHE   C N     1 
ATOM   3105 C  CA    . PHE   C 2 54  ? -37.24108 21.16084  22.50875  1.000 28.17625  ?  53  PHE   C CA    1 
ATOM   3106 C  C     . PHE   C 2 54  ? -35.84279 21.69759  22.77985  1.000 33.86690  ?  53  PHE   C C     1 
ATOM   3107 O  O     . PHE   C 2 54  ? -35.01694 21.78744  21.86233  1.000 34.98699  ?  53  PHE   C O     1 
ATOM   3108 C  CB    . PHE   C 2 54  ? -37.18968 19.87322  21.70378  1.000 31.06891  ?  53  PHE   C CB    1 
ATOM   3109 C  CG    . PHE   C 2 54  ? -38.45457 19.08184  21.76560  1.000 29.81396  ?  53  PHE   C CG    1 
ATOM   3110 C  CD1   . PHE   C 2 54  ? -39.49408 19.36221  20.89854  1.000 31.67858  ?  53  PHE   C CD1   1 
ATOM   3111 C  CD2   . PHE   C 2 54  ? -38.60485 18.05710  22.69755  1.000 27.57627  ?  53  PHE   C CD2   1 
ATOM   3112 C  CE1   . PHE   C 2 54  ? -40.67309 18.63672  20.95080  1.000 26.84445  ?  53  PHE   C CE1   1 
ATOM   3113 C  CE2   . PHE   C 2 54  ? -39.77663 17.33115  22.75346  1.000 27.83543  ?  53  PHE   C CE2   1 
ATOM   3114 C  CZ    . PHE   C 2 54  ? -40.80808 17.61646  21.86460  1.000 29.45739  ?  53  PHE   C CZ    1 
ATOM   3115 N  N     . HIS   C 2 55  ? -35.58158 22.08441  24.03082  1.000 27.30634  ?  54  HIS   C N     1 
ATOM   3116 C  CA    . HIS   C 2 55  ? -34.34758 22.78014  24.35477  1.000 27.99949  ?  54  HIS   C CA    1 
ATOM   3117 C  C     . HIS   C 2 55  ? -33.19712 21.83649  24.66467  1.000 29.76778  ?  54  HIS   C C     1 
ATOM   3118 O  O     . HIS   C 2 55  ? -32.02867 22.25631  24.63698  1.000 28.98635  ?  54  HIS   C O     1 
ATOM   3119 C  CB    . HIS   C 2 55  ? -34.57878 23.71264  25.53368  1.000 26.34000  ?  54  HIS   C CB    1 
ATOM   3120 C  CG    . HIS   C 2 55  ? -34.98449 23.00320  26.78540  1.000 31.27227  ?  54  HIS   C CG    1 
ATOM   3121 N  ND1   . HIS   C 2 55  ? -36.28963 22.64410  27.04908  1.000 32.35574  ?  54  HIS   C ND1   1 
ATOM   3122 C  CD2   . HIS   C 2 55  ? -34.25707 22.58715  27.84638  1.000 28.02626  ?  54  HIS   C CD2   1 
ATOM   3123 C  CE1   . HIS   C 2 55  ? -36.35002 22.03492  28.22091  1.000 29.68544  ?  54  HIS   C CE1   1 
ATOM   3124 N  NE2   . HIS   C 2 55  ? -35.13281 22.00037  28.73119  1.000 33.29250  ?  54  HIS   C NE2   1 
ATOM   3125 N  N     . ARG   C 2 56  ? -33.49380 20.57275  24.93718  1.000 25.65044  ?  55  ARG   C N     1 
ATOM   3126 C  CA    . ARG   C 2 56  ? -32.48365 19.62646  25.36234  1.000 26.70111  ?  55  ARG   C CA    1 
ATOM   3127 C  C     . ARG   C 2 56  ? -32.74311 18.29364  24.68121  1.000 27.42128  ?  55  ARG   C C     1 
ATOM   3128 O  O     . ARG   C 2 56  ? -33.82092 17.70150  24.83426  1.000 25.97271  ?  55  ARG   C O     1 
ATOM   3129 C  CB    . ARG   C 2 56  ? -32.48656 19.48615  26.88854  1.000 23.66334  ?  55  ARG   C CB    1 
ATOM   3130 C  CG    . ARG   C 2 56  ? -31.49864 18.46330  27.39187  1.000 30.75839  ?  55  ARG   C CG    1 
ATOM   3131 C  CD    . ARG   C 2 56  ? -31.50992 18.38651  28.91122  1.000 28.80557  ?  55  ARG   C CD    1 
ATOM   3132 N  NE    . ARG   C 2 56  ? -31.05426 19.61652  29.54921  1.000 31.75021  ?  55  ARG   C NE    1 
ATOM   3133 C  CZ    . ARG   C 2 56  ? -31.32471 19.94065  30.80725  1.000 36.91449  ?  55  ARG   C CZ    1 
ATOM   3134 N  NH1   . ARG   C 2 56  ? -32.10307 19.18084  31.56508  1.000 31.94670  ?  55  ARG   C NH1   1 
ATOM   3135 N  NH2   . ARG   C 2 56  ? -30.81088 21.05749  31.31617  1.000 35.49173  ?  55  ARG   C NH2   1 
ATOM   3136 N  N     . ILE   C 2 57  ? -31.76024 17.83730  23.90526  1.000 23.97610  ?  56  ILE   C N     1 
ATOM   3137 C  CA    . ILE   C 2 57  ? -31.83728 16.58320  23.16800  1.000 21.70447  ?  56  ILE   C CA    1 
ATOM   3138 C  C     . ILE   C 2 57  ? -30.49034 15.88363  23.30749  1.000 21.53813  ?  56  ILE   C C     1 
ATOM   3139 O  O     . ILE   C 2 57  ? -29.46037 16.41217  22.86929  1.000 23.95865  ?  56  ILE   C O     1 
ATOM   3140 C  CB    . ILE   C 2 57  ? -32.19548 16.82515  21.68626  1.000 25.81380  ?  56  ILE   C CB    1 
ATOM   3141 C  CG1   . ILE   C 2 57  ? -33.55649 17.52202  21.57376  1.000 26.80767  ?  56  ILE   C CG1   1 
ATOM   3142 C  CG2   . ILE   C 2 57  ? -32.16824 15.51218  20.84199  1.000 23.56076  ?  56  ILE   C CG2   1 
ATOM   3143 C  CD1   . ILE   C 2 57  ? -34.00037 17.77187  20.10275  1.000 28.63361  ?  56  ILE   C CD1   1 
ATOM   3144 N  N     . ILE   C 2 58  ? -30.48954 14.70642  23.92338  1.000 23.29245  ?  57  ILE   C N     1 
ATOM   3145 C  CA    . ILE   C 2 58  ? -29.25840 13.97286  24.17297  1.000 22.00266  ?  57  ILE   C CA    1 
ATOM   3146 C  C     . ILE   C 2 58  ? -29.40899 12.60744  23.52560  1.000 25.34003  ?  57  ILE   C C     1 
ATOM   3147 O  O     . ILE   C 2 58  ? -30.16192 11.76510  24.03836  1.000 24.23054  ?  57  ILE   C O     1 
ATOM   3148 C  CB    . ILE   C 2 58  ? -28.94585 13.85860  25.67853  1.000 26.35795  ?  57  ILE   C CB    1 
ATOM   3149 C  CG1   . ILE   C 2 58  ? -28.74657 15.24714  26.29119  1.000 23.13587  ?  57  ILE   C CG1   1 
ATOM   3150 C  CG2   . ILE   C 2 58  ? -27.71943 12.98746  25.90433  1.000 20.77532  ?  57  ILE   C CG2   1 
ATOM   3151 C  CD1   . ILE   C 2 58  ? -28.36639 15.23486  27.78593  1.000 24.52516  ?  57  ILE   C CD1   1 
ATOM   3152 N  N     . PRO   C 2 59  ? -28.71883 12.36391  22.40232  1.000 26.33046  ?  58  PRO   C N     1 
ATOM   3153 C  CA    . PRO   C 2 59  ? -28.87081 11.09597  21.67700  1.000 26.75386  ?  58  PRO   C CA    1 
ATOM   3154 C  C     . PRO   C 2 59  ? -28.54860 9.89813   22.54648  1.000 23.86260  ?  58  PRO   C C     1 
ATOM   3155 O  O     . PRO   C 2 59  ? -27.59599 9.90571   23.33220  1.000 29.79949  ?  58  PRO   C O     1 
ATOM   3156 C  CB    . PRO   C 2 59  ? -27.87371 11.22377  20.51427  1.000 27.64394  ?  58  PRO   C CB    1 
ATOM   3157 C  CG    . PRO   C 2 59  ? -27.76259 12.69891  20.26984  1.000 26.21414  ?  58  PRO   C CG    1 
ATOM   3158 C  CD    . PRO   C 2 59  ? -27.92719 13.35554  21.65209  1.000 25.57596  ?  58  PRO   C CD    1 
ATOM   3159 N  N     . GLY   C 2 60  ? -29.36197 8.86481   22.39688  1.000 22.79322  ?  59  GLY   C N     1 
ATOM   3160 C  CA    . GLY   C 2 60  ? -29.32689 7.71966   23.27026  1.000 26.68883  ?  59  GLY   C CA    1 
ATOM   3161 C  C     . GLY   C 2 60  ? -30.06810 7.88809   24.58350  1.000 25.99587  ?  59  GLY   C C     1 
ATOM   3162 O  O     . GLY   C 2 60  ? -30.02905 6.96239   25.41260  1.000 28.64261  ?  59  GLY   C O     1 
ATOM   3163 N  N     . PHE   C 2 61  ? -30.73053 9.02737   24.81569  1.000 22.39161  ?  60  PHE   C N     1 
ATOM   3164 C  CA    . PHE   C 2 61  ? -31.48197 9.16838   26.06986  1.000 26.54914  ?  60  PHE   C CA    1 
ATOM   3165 C  C     . PHE   C 2 61  ? -32.87361 9.76727   25.87323  1.000 25.52141  ?  60  PHE   C C     1 
ATOM   3166 O  O     . PHE   C 2 61  ? -33.86291 9.04292   26.04535  1.000 25.53219  ?  60  PHE   C O     1 
ATOM   3167 C  CB    . PHE   C 2 61  ? -30.67403 9.98360   27.10073  1.000 22.82336  ?  60  PHE   C CB    1 
ATOM   3168 C  CG    . PHE   C 2 61  ? -29.38345 9.31886   27.50632  1.000 24.55381  ?  60  PHE   C CG    1 
ATOM   3169 C  CD1   . PHE   C 2 61  ? -29.35187 8.40992   28.56013  1.000 28.71468  ?  60  PHE   C CD1   1 
ATOM   3170 C  CD2   . PHE   C 2 61  ? -28.20863 9.57976   26.80892  1.000 27.68092  ?  60  PHE   C CD2   1 
ATOM   3171 C  CE1   . PHE   C 2 61  ? -28.16120 7.78668   28.92666  1.000 33.83974  ?  60  PHE   C CE1   1 
ATOM   3172 C  CE2   . PHE   C 2 61  ? -27.01889 8.96067   27.15591  1.000 31.51163  ?  60  PHE   C CE2   1 
ATOM   3173 C  CZ    . PHE   C 2 61  ? -26.99005 8.06317   28.22088  1.000 31.76465  ?  60  PHE   C CZ    1 
ATOM   3174 N  N     . MET   C 2 62  ? -32.99303 11.04969  25.51300  1.000 22.35786  ?  61  MET   C N     1 
ATOM   3175 C  CA    . MET   C 2 62  ? -34.33411 11.63409  25.48455  1.000 26.94576  ?  61  MET   C CA    1 
ATOM   3176 C  C     . MET   C 2 62  ? -34.31940 12.95891  24.73423  1.000 22.44543  ?  61  MET   C C     1 
ATOM   3177 O  O     . MET   C 2 62  ? -33.27450 13.58135  24.56362  1.000 24.02560  ?  61  MET   C O     1 
ATOM   3178 C  CB    . MET   C 2 62  ? -34.87945 11.85826  26.90855  1.000 25.59924  ?  61  MET   C CB    1 
ATOM   3179 C  CG    . MET   C 2 62  ? -34.47701 13.21809  27.50121  1.000 26.33975  ?  61  MET   C CG    1 
ATOM   3180 S  SD    . MET   C 2 62  ? -32.70740 13.39309  27.86537  1.000 33.46071  ?  61  MET   C SD    1 
ATOM   3181 C  CE    . MET   C 2 62  ? -32.59449 15.16919  27.81342  1.000 26.96002  ?  61  MET   C CE    1 
ATOM   3182 N  N     . CYS   C 2 63  ? -35.50052 13.39088  24.30356  1.000 24.56409  ?  62  CYS   C N     1 
ATOM   3183 C  CA    . CYS   C 2 63  ? -35.71840 14.76094  23.86612  1.000 28.53087  ?  62  CYS   C CA    1 
ATOM   3184 C  C     . CYS   C 2 63  ? -36.58481 15.44206  24.91578  1.000 27.92763  ?  62  CYS   C C     1 
ATOM   3185 O  O     . CYS   C 2 63  ? -37.63888 14.91783  25.27153  1.000 26.03582  ?  62  CYS   C O     1 
ATOM   3186 C  CB    . CYS   C 2 63  ? -36.40208 14.82263  22.49047  1.000 25.32934  ?  62  CYS   C CB    1 
ATOM   3187 S  SG    . CYS   C 2 63  ? -35.68103 13.75329  21.21116  1.000 35.50086  ?  62  CYS   C SG    1 
ATOM   3188 N  N     . GLN   C 2 64  ? -36.15786 16.60844  25.39771  1.000 27.07917  ?  63  GLN   C N     1 
ATOM   3189 C  CA    . GLN   C 2 64  ? -36.85227 17.28428  26.49142  1.000 29.03966  ?  63  GLN   C CA    1 
ATOM   3190 C  C     . GLN   C 2 64  ? -37.32170 18.66325  26.03853  1.000 26.17859  ?  63  GLN   C C     1 
ATOM   3191 O  O     . GLN   C 2 64  ? -36.56907 19.41349  25.41048  1.000 29.58705  ?  63  GLN   C O     1 
ATOM   3192 C  CB    . GLN   C 2 64  ? -35.94189 17.38025  27.73174  1.000 24.25887  ?  63  GLN   C CB    1 
ATOM   3193 C  CG    . GLN   C 2 64  ? -36.46943 18.30702  28.85216  1.000 23.05572  ?  63  GLN   C CG    1 
ATOM   3194 C  CD    . GLN   C 2 64  ? -35.64256 18.24400  30.12864  1.000 23.92759  ?  63  GLN   C CD    1 
ATOM   3195 O  OE1   . GLN   C 2 64  ? -34.70156 17.45553  30.24396  1.000 25.31611  ?  63  GLN   C OE1   1 
ATOM   3196 N  NE2   . GLN   C 2 64  ? -35.97240 19.09885  31.08449  1.000 27.70026  ?  63  GLN   C NE2   1 
ATOM   3197 N  N     . GLY   C 2 65  ? -38.57726 18.98426  26.31881  1.000 26.28248  ?  64  GLY   C N     1 
ATOM   3198 C  CA    . GLY   C 2 65  ? -39.11314 20.27416  25.90620  1.000 32.05752  ?  64  GLY   C CA    1 
ATOM   3199 C  C     . GLY   C 2 65  ? -40.14271 20.82190  26.86578  1.000 31.14400  ?  64  GLY   C C     1 
ATOM   3200 O  O     . GLY   C 2 65  ? -40.17900 20.39826  28.01984  1.000 28.68438  ?  64  GLY   C O     1 
ATOM   3201 N  N     . GLY   C 2 66  ? -40.95663 21.78131  26.43128  1.000 30.33795  ?  65  GLY   C N     1 
ATOM   3202 C  CA    . GLY   C 2 66  ? -42.15322 22.16599  27.16224  1.000 34.59148  ?  65  GLY   C CA    1 
ATOM   3203 C  C     . GLY   C 2 66  ? -42.10675 23.47866  27.92195  1.000 37.46517  ?  65  GLY   C C     1 
ATOM   3204 O  O     . GLY   C 2 66  ? -43.10906 23.83275  28.56589  1.000 33.77423  ?  65  GLY   C O     1 
ATOM   3205 N  N     . ASP   C 2 67  ? -41.00417 24.21806  27.87943  1.000 32.42574  ?  66  ASP   C N     1 
ATOM   3206 C  CA    . ASP   C 2 67  ? -40.95289 25.52892  28.52834  1.000 38.88559  ?  66  ASP   C CA    1 
ATOM   3207 C  C     . ASP   C 2 67  ? -41.53658 26.55702  27.56414  1.000 43.63116  ?  66  ASP   C C     1 
ATOM   3208 O  O     . ASP   C 2 67  ? -40.88391 26.95368  26.59420  1.000 42.59755  ?  66  ASP   C O     1 
ATOM   3209 C  CB    . ASP   C 2 67  ? -39.52795 25.87600  28.94456  1.000 32.63613  ?  66  ASP   C CB    1 
ATOM   3210 C  CG    . ASP   C 2 67  ? -39.38122 27.32731  29.42425  1.000 43.88268  ?  66  ASP   C CG    1 
ATOM   3211 O  OD1   . ASP   C 2 67  ? -40.40486 28.04300  29.56485  1.000 42.72389  ?  66  ASP   C OD1   1 
ATOM   3212 O  OD2   . ASP   C 2 67  ? -38.21984 27.75238  29.66577  1.000 40.72094  -1 66  ASP   C OD2   1 
ATOM   3213 N  N     . PHE   C 2 68  ? -42.76333 27.00949  27.84578  1.000 38.09234  ?  67  PHE   C N     1 
ATOM   3214 C  CA    . PHE   C 2 68  ? -43.45880 27.97373  26.99637  1.000 43.14947  ?  67  PHE   C CA    1 
ATOM   3215 C  C     . PHE   C 2 68  ? -43.63936 29.32602  27.67591  1.000 44.04625  ?  67  PHE   C C     1 
ATOM   3216 O  O     . PHE   C 2 68  ? -44.35410 30.18352  27.14682  1.000 49.83334  ?  67  PHE   C O     1 
ATOM   3217 C  CB    . PHE   C 2 68  ? -44.82676 27.42989  26.54968  1.000 38.45087  ?  67  PHE   C CB    1 
ATOM   3218 C  CG    . PHE   C 2 68  ? -45.73655 27.04064  27.68977  1.000 39.19649  ?  67  PHE   C CG    1 
ATOM   3219 C  CD1   . PHE   C 2 68  ? -46.38730 28.00828  28.45212  1.000 45.87321  ?  67  PHE   C CD1   1 
ATOM   3220 C  CD2   . PHE   C 2 68  ? -45.95805 25.70585  27.98769  1.000 40.38774  ?  67  PHE   C CD2   1 
ATOM   3221 C  CE1   . PHE   C 2 68  ? -47.21178 27.64567  29.50779  1.000 41.77533  ?  67  PHE   C CE1   1 
ATOM   3222 C  CE2   . PHE   C 2 68  ? -46.79458 25.34553  29.02696  1.000 41.38906  ?  67  PHE   C CE2   1 
ATOM   3223 C  CZ    . PHE   C 2 68  ? -47.41421 26.31847  29.78994  1.000 38.62043  ?  67  PHE   C CZ    1 
ATOM   3224 N  N     . THR   C 2 69  ? -43.03128 29.52729  28.83980  1.000 43.59054  ?  68  THR   C N     1 
ATOM   3225 C  CA    . THR   C 2 69  ? -43.12161 30.79260  29.55772  1.000 47.10490  ?  68  THR   C CA    1 
ATOM   3226 C  C     . THR   C 2 69  ? -41.83068 31.59840  29.50604  1.000 46.92291  ?  68  THR   C C     1 
ATOM   3227 O  O     . THR   C 2 69  ? -41.88605 32.83181  29.50714  1.000 49.24148  ?  68  THR   C O     1 
ATOM   3228 C  CB    . THR   C 2 69  ? -43.49595 30.55704  31.02865  1.000 41.93459  ?  68  THR   C CB    1 
ATOM   3229 O  OG1   . THR   C 2 69  ? -42.39388 29.95496  31.72713  1.000 40.16093  ?  68  THR   C OG1   1 
ATOM   3230 C  CG2   . THR   C 2 69  ? -44.72488 29.65616  31.13452  1.000 40.77581  ?  68  THR   C CG2   1 
ATOM   3231 N  N     . ARG   C 2 70  ? -40.67610 30.93044  29.48003  1.000 42.20687  ?  69  ARG   C N     1 
ATOM   3232 C  CA    . ARG   C 2 70  ? -39.39091 31.59608  29.34431  1.000 43.78382  ?  69  ARG   C CA    1 
ATOM   3233 C  C     . ARG   C 2 70  ? -38.59792 31.15589  28.12656  1.000 43.65840  ?  69  ARG   C C     1 
ATOM   3234 O  O     . ARG   C 2 70  ? -37.62893 31.83633  27.77314  1.000 46.97050  ?  69  ARG   C O     1 
ATOM   3235 C  CB    . ARG   C 2 70  ? -38.52102 31.36300  30.58391  1.000 41.94051  ?  69  ARG   C CB    1 
ATOM   3236 C  CG    . ARG   C 2 70  ? -39.12374 31.86242  31.87612  1.000 48.56530  ?  69  ARG   C CG    1 
ATOM   3237 C  CD    . ARG   C 2 70  ? -38.11956 31.68604  32.99406  1.000 53.55838  ?  69  ARG   C CD    1 
ATOM   3238 N  NE    . ARG   C 2 70  ? -38.73483 31.73156  34.31247  1.000 60.45886  ?  69  ARG   C NE    1 
ATOM   3239 C  CZ    . ARG   C 2 70  ? -38.22706 31.15381  35.39169  1.000 58.91755  ?  69  ARG   C CZ    1 
ATOM   3240 N  NH1   . ARG   C 2 70  ? -37.08939 30.48310  35.34481  1.000 54.23412  ?  69  ARG   C NH1   1 
ATOM   3241 N  NH2   . ARG   C 2 70  ? -38.88601 31.23983  36.54368  1.000 63.22254  ?  69  ARG   C NH2   1 
ATOM   3242 N  N     . HIS   C 2 71  ? -38.95658 30.03165  27.50227  1.000 43.99053  ?  70  HIS   C N     1 
ATOM   3243 C  CA    . HIS   C 2 71  ? -38.37114 29.59331  26.23522  1.000 46.97826  ?  70  HIS   C CA    1 
ATOM   3244 C  C     . HIS   C 2 71  ? -36.86093 29.39752  26.32759  1.000 43.98389  ?  70  HIS   C C     1 
ATOM   3245 O  O     . HIS   C 2 71  ? -36.16217 29.46995  25.31639  1.000 45.78002  ?  70  HIS   C O     1 
ATOM   3246 C  CB    . HIS   C 2 71  ? -38.71695 30.57241  25.11011  1.000 39.95311  ?  70  HIS   C CB    1 
ATOM   3247 C  CG    . HIS   C 2 71  ? -40.18358 30.70085  24.85936  1.000 43.81270  ?  70  HIS   C CG    1 
ATOM   3248 N  ND1   . HIS   C 2 71  ? -40.87723 29.83670  24.03532  1.000 46.97403  ?  70  HIS   C ND1   1 
ATOM   3249 C  CD2   . HIS   C 2 71  ? -41.09474 31.58305  25.33282  1.000 41.80497  ?  70  HIS   C CD2   1 
ATOM   3250 C  CE1   . HIS   C 2 71  ? -42.15107 30.18615  24.00646  1.000 46.55843  ?  70  HIS   C CE1   1 
ATOM   3251 N  NE2   . HIS   C 2 71  ? -42.30916 31.24343  24.78465  1.000 46.20562  ?  70  HIS   C NE2   1 
ATOM   3252 N  N     . ASN   C 2 72  ? -36.33886 29.15121  27.53888  1.000 38.37124  ?  71  ASN   C N     1 
ATOM   3253 C  CA    . ASN   C 2 72  ? -34.90179 28.96361  27.69857  1.000 41.78725  ?  71  ASN   C CA    1 
ATOM   3254 C  C     . ASN   C 2 72  ? -34.55200 27.72532  28.52249  1.000 42.83613  ?  71  ASN   C C     1 
ATOM   3255 O  O     . ASN   C 2 72  ? -33.42857 27.63074  29.02885  1.000 43.54068  ?  71  ASN   C O     1 
ATOM   3256 C  CB    . ASN   C 2 72  ? -34.25419 30.20036  28.34623  1.000 41.65367  ?  71  ASN   C CB    1 
ATOM   3257 C  CG    . ASN   C 2 72  ? -34.72645 30.43930  29.77700  1.000 51.25481  ?  71  ASN   C CG    1 
ATOM   3258 O  OD1   . ASN   C 2 72  ? -35.57376 29.70941  30.30673  1.000 45.68491  ?  71  ASN   C OD1   1 
ATOM   3259 N  ND2   . ASN   C 2 72  ? -34.16879 31.47024  30.41718  1.000 54.94208  ?  71  ASN   C ND2   1 
ATOM   3260 N  N     . GLY   C 2 73  ? -35.47829 26.78919  28.70299  1.000 41.84848  ?  72  GLY   C N     1 
ATOM   3261 C  CA    . GLY   C 2 73  ? -35.19318 25.60103  29.47966  1.000 38.66943  ?  72  GLY   C CA    1 
ATOM   3262 C  C     . GLY   C 2 73  ? -35.44898 25.69351  30.97417  1.000 40.53461  ?  72  GLY   C C     1 
ATOM   3263 O  O     . GLY   C 2 73  ? -35.37829 24.66024  31.65450  1.000 37.32949  ?  72  GLY   C O     1 
ATOM   3264 N  N     . THR   C 2 74  ? -35.75013 26.88092  31.51626  1.000 36.85485  ?  73  THR   C N     1 
ATOM   3265 C  CA    . THR   C 2 74  ? -35.90440 27.03675  32.95987  1.000 41.98151  ?  73  THR   C CA    1 
ATOM   3266 C  C     . THR   C 2 74  ? -37.35248 27.20345  33.40423  1.000 39.48190  ?  73  THR   C C     1 
ATOM   3267 O  O     . THR   C 2 74  ? -37.61782 27.13791  34.60500  1.000 43.85804  ?  73  THR   C O     1 
ATOM   3268 C  CB    . THR   C 2 74  ? -35.09140 28.24323  33.47727  1.000 46.38213  ?  73  THR   C CB    1 
ATOM   3269 O  OG1   . THR   C 2 74  ? -35.82075 29.45536  33.24956  1.000 50.14930  ?  73  THR   C OG1   1 
ATOM   3270 C  CG2   . THR   C 2 74  ? -33.74344 28.34086  32.76749  1.000 45.73291  ?  73  THR   C CG2   1 
ATOM   3271 N  N     . GLY   C 2 75  ? -38.29083 27.40552  32.48388  1.000 40.17383  ?  74  GLY   C N     1 
ATOM   3272 C  CA    . GLY   C 2 75  ? -39.63533 27.78058  32.88135  1.000 40.81114  ?  74  GLY   C CA    1 
ATOM   3273 C  C     . GLY   C 2 75  ? -40.72640 26.75882  32.61931  1.000 40.80448  ?  74  GLY   C C     1 
ATOM   3274 O  O     . GLY   C 2 75  ? -40.50214 25.54102  32.68900  1.000 34.19248  ?  74  GLY   C O     1 
ATOM   3275 N  N     . GLY   C 2 76  ? -41.91985 27.25990  32.33005  1.000 42.21640  ?  75  GLY   C N     1 
ATOM   3276 C  CA    . GLY   C 2 76  ? -43.12714 26.47999  32.17327  1.000 37.80914  ?  75  GLY   C CA    1 
ATOM   3277 C  C     . GLY   C 2 76  ? -43.99015 26.48952  33.43682  1.000 39.35774  ?  75  GLY   C C     1 
ATOM   3278 O  O     . GLY   C 2 76  ? -43.53080 26.79848  34.54175  1.000 32.90782  ?  75  GLY   C O     1 
ATOM   3279 N  N     . LYS   C 2 77  ? -45.26110 26.13534  33.24950  1.000 41.54744  ?  76  LYS   C N     1 
ATOM   3280 C  CA    . LYS   C 2 77  ? -46.25149 26.09539  34.32254  1.000 38.71220  ?  76  LYS   C CA    1 
ATOM   3281 C  C     . LYS   C 2 77  ? -47.35789 25.12654  33.92363  1.000 33.52608  ?  76  LYS   C C     1 
ATOM   3282 O  O     . LYS   C 2 77  ? -47.60287 24.89565  32.73888  1.000 37.60805  ?  76  LYS   C O     1 
ATOM   3283 C  CB    . LYS   C 2 77  ? -46.83508 27.49326  34.60956  1.000 33.57883  ?  76  LYS   C CB    1 
ATOM   3284 C  CG    . LYS   C 2 77  ? -47.64990 28.07479  33.46813  1.000 38.27495  ?  76  LYS   C CG    1 
ATOM   3285 C  CD    . LYS   C 2 77  ? -48.19757 29.46965  33.76442  1.000 43.37796  ?  76  LYS   C CD    1 
ATOM   3286 C  CE    . LYS   C 2 77  ? -48.98869 29.99794  32.55500  1.000 43.74922  ?  76  LYS   C CE    1 
ATOM   3287 N  NZ    . LYS   C 2 77  ? -49.42200 31.41737  32.71299  1.000 50.69979  ?  76  LYS   C NZ    1 
ATOM   3288 N  N     . SER   C 2 78  ? -48.03736 24.57394  34.92772  1.000 35.87316  ?  77  SER   C N     1 
ATOM   3289 C  CA    . SER   C 2 78  ? -49.12373 23.63134  34.70725  1.000 40.27668  ?  77  SER   C CA    1 
ATOM   3290 C  C     . SER   C 2 78  ? -50.45882 24.36808  34.59981  1.000 37.39536  ?  77  SER   C C     1 
ATOM   3291 O  O     . SER   C 2 78  ? -50.54394 25.58307  34.79812  1.000 35.64518  ?  77  SER   C O     1 
ATOM   3292 C  CB    . SER   C 2 78  ? -49.16956 22.60455  35.83543  1.000 38.18535  ?  77  SER   C CB    1 
ATOM   3293 O  OG    . SER   C 2 78  ? -49.86137 23.13205  36.95199  1.000 40.99105  ?  77  SER   C OG    1 
ATOM   3294 N  N     . ILE   C 2 79  ? -51.52145 23.61965  34.27597  1.000 37.50433  ?  78  ILE   C N     1 
ATOM   3295 C  CA    . ILE   C 2 79  ? -52.85973 24.21458  34.30237  1.000 39.40682  ?  78  ILE   C CA    1 
ATOM   3296 C  C     . ILE   C 2 79  ? -53.42645 24.32245  35.71227  1.000 40.55089  ?  78  ILE   C C     1 
ATOM   3297 O  O     . ILE   C 2 79  ? -54.48964 24.92912  35.89382  1.000 42.80610  ?  78  ILE   C O     1 
ATOM   3298 C  CB    . ILE   C 2 79  ? -53.88080 23.44128  33.44476  1.000 40.39361  ?  78  ILE   C CB    1 
ATOM   3299 C  CG1   . ILE   C 2 79  ? -54.18816 22.07587  34.07577  1.000 36.21835  ?  78  ILE   C CG1   1 
ATOM   3300 C  CG2   . ILE   C 2 79  ? -53.41947 23.35254  31.95914  1.000 39.73455  ?  78  ILE   C CG2   1 
ATOM   3301 C  CD1   . ILE   C 2 79  ? -55.36715 21.35628  33.44181  1.000 39.16818  ?  78  ILE   C CD1   1 
ATOM   3302 N  N     . TYR   C 2 80  ? -52.74576 23.76177  36.71622  1.000 40.96933  ?  79  TYR   C N     1 
ATOM   3303 C  CA    . TYR   C 2 80  ? -53.16946 23.81637  38.11180  1.000 40.68741  ?  79  TYR   C CA    1 
ATOM   3304 C  C     . TYR   C 2 80  ? -52.45850 24.90075  38.90154  1.000 47.04974  ?  79  TYR   C C     1 
ATOM   3305 O  O     . TYR   C 2 80  ? -52.83286 25.15442  40.05001  1.000 50.07297  ?  79  TYR   C O     1 
ATOM   3306 C  CB    . TYR   C 2 80  ? -52.92354 22.47163  38.80819  1.000 38.24317  ?  79  TYR   C CB    1 
ATOM   3307 C  CG    . TYR   C 2 80  ? -53.39684 21.29888  37.99923  1.000 40.03787  ?  79  TYR   C CG    1 
ATOM   3308 C  CD1   . TYR   C 2 80  ? -54.74196 21.11960  37.73650  1.000 40.41821  ?  79  TYR   C CD1   1 
ATOM   3309 C  CD2   . TYR   C 2 80  ? -52.50143 20.37470  37.49168  1.000 38.01479  ?  79  TYR   C CD2   1 
ATOM   3310 C  CE1   . TYR   C 2 80  ? -55.18929 20.04224  36.99632  1.000 43.35248  ?  79  TYR   C CE1   1 
ATOM   3311 C  CE2   . TYR   C 2 80  ? -52.93541 19.29484  36.74374  1.000 32.38105  ?  79  TYR   C CE2   1 
ATOM   3312 C  CZ    . TYR   C 2 80  ? -54.27533 19.13442  36.50059  1.000 37.39885  ?  79  TYR   C CZ    1 
ATOM   3313 O  OH    . TYR   C 2 80  ? -54.72509 18.08222  35.75699  1.000 35.22149  ?  79  TYR   C OH    1 
ATOM   3314 N  N     . GLY   C 2 81  ? -51.46015 25.54229  38.31454  1.000 43.68563  ?  80  GLY   C N     1 
ATOM   3315 C  CA    . GLY   C 2 81  ? -50.57508 26.45328  38.99608  1.000 43.45869  ?  80  GLY   C CA    1 
ATOM   3316 C  C     . GLY   C 2 81  ? -49.16166 26.26532  38.49546  1.000 44.40800  ?  80  GLY   C C     1 
ATOM   3317 O  O     . GLY   C 2 81  ? -48.91310 25.52618  37.54002  1.000 46.14070  ?  80  GLY   C O     1 
ATOM   3318 N  N     . GLU   C 2 82  ? -48.23030 26.94535  39.16677  1.000 40.48823  ?  81  GLU   C N     1 
ATOM   3319 C  CA    . GLU   C 2 82  ? -46.82155 26.85771  38.79605  1.000 43.74470  ?  81  GLU   C CA    1 
ATOM   3320 C  C     . GLU   C 2 82  ? -46.30485 25.42710  38.87582  1.000 46.84567  ?  81  GLU   C C     1 
ATOM   3321 O  O     . GLU   C 2 82  ? -45.72054 24.91657  37.91447  1.000 43.58578  ?  81  GLU   C O     1 
ATOM   3322 C  CB    . GLU   C 2 82  ? -45.98769 27.77386  39.68062  1.000 38.74845  ?  81  GLU   C CB    1 
ATOM   3323 C  CG    . GLU   C 2 82  ? -46.27818 29.27881  39.40896  1.000 56.45961  ?  81  GLU   C CG    1 
ATOM   3324 C  CD    . GLU   C 2 82  ? -45.99617 29.71695  37.96910  1.000 61.77562  ?  81  GLU   C CD    1 
ATOM   3325 O  OE1   . GLU   C 2 82  ? -44.81580 29.56757  37.50963  1.000 65.62317  ?  81  GLU   C OE1   1 
ATOM   3326 O  OE2   . GLU   C 2 82  ? -46.95503 30.18337  37.25809  1.000 56.40763  ?  81  GLU   C OE2   1 
ATOM   3327 N  N     . LYS   C 2 83  ? -46.50050 24.75909  40.01022  1.000 44.72150  ?  82  LYS   C N     1 
ATOM   3328 C  CA    . LYS   C 2 83  ? -46.11250 23.36233  40.12271  1.000 41.07656  ?  82  LYS   C CA    1 
ATOM   3329 C  C     . LYS   C 2 83  ? -47.26333 22.52456  40.67966  1.000 47.65533  ?  82  LYS   C C     1 
ATOM   3330 O  O     . LYS   C 2 83  ? -48.20674 23.05560  41.27891  1.000 43.34441  ?  82  LYS   C O     1 
ATOM   3331 C  CB    . LYS   C 2 83  ? -44.84483 23.21625  40.97235  1.000 35.33877  ?  82  LYS   C CB    1 
ATOM   3332 C  CG    . LYS   C 2 83  ? -44.87247 23.93211  42.30844  1.000 51.27969  ?  82  LYS   C CG    1 
ATOM   3333 C  CD    . LYS   C 2 83  ? -44.36984 23.01606  43.42170  1.000 50.68230  ?  82  LYS   C CD    1 
ATOM   3334 C  CE    . LYS   C 2 83  ? -43.78362 23.79098  44.60199  1.000 54.26517  ?  82  LYS   C CE    1 
ATOM   3335 N  NZ    . LYS   C 2 83  ? -44.79389 24.64385  45.30235  1.000 57.50637  ?  82  LYS   C NZ    1 
ATOM   3336 N  N     . PHE   C 2 84  ? -47.20597 21.20784  40.43603  1.000 38.78797  ?  83  PHE   C N     1 
ATOM   3337 C  CA    . PHE   C 2 84  ? -48.13586 20.27760  41.05743  1.000 33.99177  ?  83  PHE   C CA    1 
ATOM   3338 C  C     . PHE   C 2 84  ? -47.39507 19.00876  41.44377  1.000 34.68334  ?  83  PHE   C C     1 
ATOM   3339 O  O     . PHE   C 2 84  ? -46.22353 18.81736  41.12096  1.000 34.36815  ?  83  PHE   C O     1 
ATOM   3340 C  CB    . PHE   C 2 84  ? -49.36676 19.98160  40.17921  1.000 35.97739  ?  83  PHE   C CB    1 
ATOM   3341 C  CG    . PHE   C 2 84  ? -49.08803 19.22052  38.89753  1.000 39.08358  ?  83  PHE   C CG    1 
ATOM   3342 C  CD1   . PHE   C 2 84  ? -48.58301 19.87043  37.78008  1.000 36.20167  ?  83  PHE   C CD1   1 
ATOM   3343 C  CD2   . PHE   C 2 84  ? -49.41046 17.87675  38.78890  1.000 33.05840  ?  83  PHE   C CD2   1 
ATOM   3344 C  CE1   . PHE   C 2 84  ? -48.36117 19.17814  36.57311  1.000 36.84554  ?  83  PHE   C CE1   1 
ATOM   3345 C  CE2   . PHE   C 2 84  ? -49.20750 17.17723  37.59831  1.000 36.04180  ?  83  PHE   C CE2   1 
ATOM   3346 C  CZ    . PHE   C 2 84  ? -48.68090 17.82580  36.48254  1.000 36.27853  ?  83  PHE   C CZ    1 
ATOM   3347 N  N     . GLU   C 2 85  ? -48.08997 18.15137  42.17851  1.000 35.20803  ?  84  GLU   C N     1 
ATOM   3348 C  CA    . GLU   C 2 85  ? -47.45359 17.03758  42.85737  1.000 35.28473  ?  84  GLU   C CA    1 
ATOM   3349 C  C     . GLU   C 2 85  ? -47.29479 15.83540  41.92444  1.000 34.47457  ?  84  GLU   C C     1 
ATOM   3350 O  O     . GLU   C 2 85  ? -47.97926 15.70316  40.90722  1.000 32.86829  ?  84  GLU   C O     1 
ATOM   3351 C  CB    . GLU   C 2 85  ? -48.26303 16.63900  44.09665  1.000 34.21487  ?  84  GLU   C CB    1 
ATOM   3352 C  CG    . GLU   C 2 85  ? -49.61769 16.00328  43.78719  1.000 37.22752  ?  84  GLU   C CG    1 
ATOM   3353 C  CD    . GLU   C 2 85  ? -50.71888 17.00164  43.36929  1.000 47.88181  ?  84  GLU   C CD    1 
ATOM   3354 O  OE1   . GLU   C 2 85  ? -50.56759 18.23416  43.56416  1.000 45.15935  ?  84  GLU   C OE1   1 
ATOM   3355 O  OE2   . GLU   C 2 85  ? -51.75762 16.53320  42.84965  1.000 49.71734  -1 84  GLU   C OE2   1 
ATOM   3356 N  N     . ASP   C 2 86  ? -46.35769 14.96298  42.29082  1.000 31.17261  ?  85  ASP   C N     1 
ATOM   3357 C  CA    . ASP   C 2 86  ? -46.17225 13.66883  41.64570  1.000 29.77827  ?  85  ASP   C CA    1 
ATOM   3358 C  C     . ASP   C 2 86  ? -47.39894 12.80554  41.90697  1.000 38.15509  ?  85  ASP   C C     1 
ATOM   3359 O  O     . ASP   C 2 86  ? -47.56630 12.27381  43.01416  1.000 37.94090  ?  85  ASP   C O     1 
ATOM   3360 C  CB    . ASP   C 2 86  ? -44.90364 13.00629  42.17851  1.000 29.00823  ?  85  ASP   C CB    1 
ATOM   3361 C  CG    . ASP   C 2 86  ? -43.66553 13.87152  41.98083  1.000 35.02580  ?  85  ASP   C CG    1 
ATOM   3362 O  OD1   . ASP   C 2 86  ? -43.56858 14.52914  40.90907  1.000 33.46568  ?  85  ASP   C OD1   1 
ATOM   3363 O  OD2   . ASP   C 2 86  ? -42.78995 13.89395  42.88417  1.000 33.66940  -1 85  ASP   C OD2   1 
ATOM   3364 N  N     . GLU   C 2 87  ? -48.26712 12.69173  40.89426  1.000 33.52556  ?  86  GLU   C N     1 
ATOM   3365 C  CA    . GLU   C 2 87  ? -49.50843 11.93417  41.02848  1.000 31.00952  ?  86  GLU   C CA    1 
ATOM   3366 C  C     . GLU   C 2 87  ? -49.24378 10.52928  41.56961  1.000 41.37529  ?  86  GLU   C C     1 
ATOM   3367 O  O     . GLU   C 2 87  ? -49.81468 10.12751  42.59662  1.000 36.17787  ?  86  GLU   C O     1 
ATOM   3368 C  CB    . GLU   C 2 87  ? -50.22532 11.87830  39.67463  1.000 31.68463  ?  86  GLU   C CB    1 
ATOM   3369 C  CG    . GLU   C 2 87  ? -51.71943 11.55082  39.77564  1.000 31.97777  ?  86  GLU   C CG    1 
ATOM   3370 C  CD    . GLU   C 2 87  ? -52.45921 11.87096  38.50629  1.000 37.34904  ?  86  GLU   C CD    1 
ATOM   3371 O  OE1   . GLU   C 2 87  ? -51.80451 12.21857  37.49426  1.000 35.34302  ?  86  GLU   C OE1   1 
ATOM   3372 O  OE2   . GLU   C 2 87  ? -53.70580 11.78417  38.49712  1.000 40.77838  -1 86  GLU   C OE2   1 
ATOM   3373 N  N     . ASN   C 2 88  ? -48.35607 9.77829   40.91055  1.000 29.66872  ?  87  ASN   C N     1 
ATOM   3374 C  CA    . ASN   C 2 88  ? -48.00870 8.42272   41.33268  1.000 35.14678  ?  87  ASN   C CA    1 
ATOM   3375 C  C     . ASN   C 2 88  ? -46.85632 7.92269   40.46715  1.000 32.36319  ?  87  ASN   C C     1 
ATOM   3376 O  O     . ASN   C 2 88  ? -46.42586 8.58921   39.52004  1.000 31.54603  ?  87  ASN   C O     1 
ATOM   3377 C  CB    . ASN   C 2 88  ? -49.21090 7.46438   41.24604  1.000 30.90488  ?  87  ASN   C CB    1 
ATOM   3378 C  CG    . ASN   C 2 88  ? -49.71009 7.26782   39.82311  1.000 29.69603  ?  87  ASN   C CG    1 
ATOM   3379 O  OD1   . ASN   C 2 88  ? -48.95620 6.86045   38.93834  1.000 30.41859  ?  87  ASN   C OD1   1 
ATOM   3380 N  ND2   . ASN   C 2 88  ? -50.99143 7.53624   39.60000  1.000 33.31731  ?  87  ASN   C ND2   1 
ATOM   3381 N  N     . PHE   C 2 89  ? -46.36625 6.73132   40.78937  1.000 29.44703  ?  88  PHE   C N     1 
ATOM   3382 C  CA    . PHE   C 2 89  ? -45.31045 6.12661   39.99179  1.000 27.07553  ?  88  PHE   C CA    1 
ATOM   3383 C  C     . PHE   C 2 89  ? -45.70984 4.74925   39.48202  1.000 25.01437  ?  88  PHE   C C     1 
ATOM   3384 O  O     . PHE   C 2 89  ? -44.90310 3.82482   39.45339  1.000 29.09389  ?  88  PHE   C O     1 
ATOM   3385 C  CB    . PHE   C 2 89  ? -44.00165 6.09388   40.77763  1.000 28.26213  ?  88  PHE   C CB    1 
ATOM   3386 C  CG    . PHE   C 2 89  ? -43.48792 7.46769   41.10617  1.000 32.92599  ?  88  PHE   C CG    1 
ATOM   3387 C  CD1   . PHE   C 2 89  ? -43.07115 8.32324   40.08840  1.000 26.29401  ?  88  PHE   C CD1   1 
ATOM   3388 C  CD2   . PHE   C 2 89  ? -43.47462 7.93387   42.42594  1.000 32.52542  ?  88  PHE   C CD2   1 
ATOM   3389 C  CE1   . PHE   C 2 89  ? -42.61684 9.60952   40.37593  1.000 26.13292  ?  88  PHE   C CE1   1 
ATOM   3390 C  CE2   . PHE   C 2 89  ? -43.02411 9.20970   42.71481  1.000 33.46013  ?  88  PHE   C CE2   1 
ATOM   3391 C  CZ    . PHE   C 2 89  ? -42.59043 10.04684  41.69138  1.000 31.32021  ?  88  PHE   C CZ    1 
ATOM   3392 N  N     . ILE   C 2 90  ? -46.95480 4.62084   39.01818  1.000 25.53669  ?  89  ILE   C N     1 
ATOM   3393 C  CA    . ILE   C 2 90  ? -47.42115 3.34240   38.48742  1.000 25.10221  ?  89  ILE   C CA    1 
ATOM   3394 C  C     . ILE   C 2 90  ? -46.63067 2.95898   37.23628  1.000 29.31768  ?  89  ILE   C C     1 
ATOM   3395 O  O     . ILE   C 2 90  ? -46.18659 1.81234   37.08169  1.000 29.96130  ?  89  ILE   C O     1 
ATOM   3396 C  CB    . ILE   C 2 90  ? -48.93229 3.40099   38.20010  1.000 25.54626  ?  89  ILE   C CB    1 
ATOM   3397 C  CG1   . ILE   C 2 90  ? -49.74166 3.56230   39.49572  1.000 26.81144  ?  89  ILE   C CG1   1 
ATOM   3398 C  CG2   . ILE   C 2 90  ? -49.38109 2.16712   37.41615  1.000 26.96626  ?  89  ILE   C CG2   1 
ATOM   3399 C  CD1   . ILE   C 2 90  ? -51.20911 3.91453   39.24628  1.000 29.61738  ?  89  ILE   C CD1   1 
ATOM   3400 N  N     . LEU   C 2 91  ? -46.45362 3.90240   36.32082  1.000 25.98233  ?  90  LEU   C N     1 
ATOM   3401 C  CA    . LEU   C 2 91  ? -45.80295 3.58295   35.05286  1.000 24.49379  ?  90  LEU   C CA    1 
ATOM   3402 C  C     . LEU   C 2 91  ? -44.30630 3.85809   35.10608  1.000 26.29292  ?  90  LEU   C C     1 
ATOM   3403 O  O     . LEU   C 2 91  ? -43.84495 4.80734   35.74380  1.000 26.45816  ?  90  LEU   C O     1 
ATOM   3404 C  CB    . LEU   C 2 91  ? -46.44115 4.38069   33.93130  1.000 27.52687  ?  90  LEU   C CB    1 
ATOM   3405 C  CG    . LEU   C 2 91  ? -47.90578 4.03525   33.79086  1.000 28.78829  ?  90  LEU   C CG    1 
ATOM   3406 C  CD1   . LEU   C 2 91  ? -48.54511 5.03483   32.85515  1.000 25.75934  ?  90  LEU   C CD1   1 
ATOM   3407 C  CD2   . LEU   C 2 91  ? -48.06632 2.59722   33.28242  1.000 29.61128  ?  90  LEU   C CD2   1 
ATOM   3408 N  N     . LYS   C 2 92  ? -43.54599 3.01558   34.41443  1.000 30.05739  ?  91  LYS   C N     1 
ATOM   3409 C  CA    . LYS   C 2 92  ? -42.09104 3.04623   34.43927  1.000 26.86242  ?  91  LYS   C CA    1 
ATOM   3410 C  C     . LYS   C 2 92  ? -41.53572 3.48940   33.08358  1.000 28.40263  ?  91  LYS   C C     1 
ATOM   3411 O  O     . LYS   C 2 92  ? -42.25367 3.57960   32.07877  1.000 28.59483  ?  91  LYS   C O     1 
ATOM   3412 C  CB    . LYS   C 2 92  ? -41.51534 1.67362   34.82827  1.000 34.65893  ?  91  LYS   C CB    1 
ATOM   3413 C  CG    . LYS   C 2 92  ? -42.08657 1.06785   36.12600  1.000 35.53093  ?  91  LYS   C CG    1 
ATOM   3414 C  CD    . LYS   C 2 92  ? -42.02885 2.02021   37.29358  1.000 40.85911  ?  91  LYS   C CD    1 
ATOM   3415 C  CE    . LYS   C 2 92  ? -42.44425 1.28805   38.57758  1.000 45.01203  ?  91  LYS   C CE    1 
ATOM   3416 N  NZ    . LYS   C 2 92  ? -41.65440 -0.00546  38.58502  1.000 45.10817  ?  91  LYS   C NZ    1 
ATOM   3417 N  N     . HIS   C 2 93  ? -40.23545 3.79361   33.07722  1.000 24.51907  ?  92  HIS   C N     1 
ATOM   3418 C  CA    . HIS   C 2 93  ? -39.49858 4.18163   31.86294  1.000 28.66663  ?  92  HIS   C CA    1 
ATOM   3419 C  C     . HIS   C 2 93  ? -38.99859 2.88899   31.23174  1.000 25.14315  ?  92  HIS   C C     1 
ATOM   3420 O  O     . HIS   C 2 93  ? -37.90320 2.40165   31.51390  1.000 29.31598  ?  92  HIS   C O     1 
ATOM   3421 C  CB    . HIS   C 2 93  ? -38.35327 5.14223   32.17721  1.000 28.56855  ?  92  HIS   C CB    1 
ATOM   3422 C  CG    . HIS   C 2 93  ? -38.78536 6.38599   32.89526  1.000 28.51805  ?  92  HIS   C CG    1 
ATOM   3423 N  ND1   . HIS   C 2 93  ? -38.86649 6.46215   34.27043  1.000 24.59903  ?  92  HIS   C ND1   1 
ATOM   3424 C  CD2   . HIS   C 2 93  ? -39.13959 7.60764   32.42805  1.000 29.32817  ?  92  HIS   C CD2   1 
ATOM   3425 C  CE1   . HIS   C 2 93  ? -39.28792 7.66585   34.61641  1.000 26.59625  ?  92  HIS   C CE1   1 
ATOM   3426 N  NE2   . HIS   C 2 93  ? -39.44571 8.38661   33.51988  1.000 24.62042  ?  92  HIS   C NE2   1 
ATOM   3427 N  N     . THR   C 2 94  ? -39.82116 2.31223   30.37603  1.000 29.43227  ?  93  THR   C N     1 
ATOM   3428 C  CA    . THR   C 2 94  ? -39.56827 0.96068   29.91390  1.000 29.61760  ?  93  THR   C CA    1 
ATOM   3429 C  C     . THR   C 2 94  ? -38.95436 0.90751   28.52789  1.000 33.59663  ?  93  THR   C C     1 
ATOM   3430 O  O     . THR   C 2 94  ? -38.56168 -0.17983  28.09851  1.000 36.98608  ?  93  THR   C O     1 
ATOM   3431 C  CB    . THR   C 2 94  ? -40.86268 0.16444   29.90019  1.000 37.30034  ?  93  THR   C CB    1 
ATOM   3432 O  OG1   . THR   C 2 94  ? -41.70606 0.70044   28.88481  1.000 28.58165  ?  93  THR   C OG1   1 
ATOM   3433 C  CG2   . THR   C 2 94  ? -41.55302 0.26527   31.25449  1.000 33.12513  ?  93  THR   C CG2   1 
ATOM   3434 N  N     . GLY   C 2 95  ? -38.87105 2.03322   27.81756  1.000 26.82980  ?  94  GLY   C N     1 
ATOM   3435 C  CA    . GLY   C 2 95  ? -38.16337 2.06164   26.56400  1.000 27.89866  ?  94  GLY   C CA    1 
ATOM   3436 C  C     . GLY   C 2 95  ? -38.44427 3.28081   25.71129  1.000 32.18114  ?  94  GLY   C C     1 
ATOM   3437 O  O     . GLY   C 2 95  ? -38.96076 4.30490   26.16994  1.000 31.97508  ?  94  GLY   C O     1 
ATOM   3438 N  N     . PRO   C 2 96  ? -38.08782 3.19455   24.43532  1.000 29.87821  ?  95  PRO   C N     1 
ATOM   3439 C  CA    . PRO   C 2 96  ? -38.29004 4.33982   23.53943  1.000 31.36007  ?  95  PRO   C CA    1 
ATOM   3440 C  C     . PRO   C 2 96  ? -39.77154 4.67544   23.38776  1.000 26.21713  ?  95  PRO   C C     1 
ATOM   3441 O  O     . PRO   C 2 96  ? -40.62784 3.78942   23.32880  1.000 26.87884  ?  95  PRO   C O     1 
ATOM   3442 C  CB    . PRO   C 2 96  ? -37.68838 3.86770   22.20496  1.000 28.39822  ?  95  PRO   C CB    1 
ATOM   3443 C  CG    . PRO   C 2 96  ? -36.82079 2.69088   22.56692  1.000 32.64416  ?  95  PRO   C CG    1 
ATOM   3444 C  CD    . PRO   C 2 96  ? -37.42835 2.05900   23.78045  1.000 26.65783  ?  95  PRO   C CD    1 
ATOM   3445 N  N     . GLY   C 2 97  ? -40.07066 5.97034   23.32592  1.000 21.53020  ?  96  GLY   C N     1 
ATOM   3446 C  CA    . GLY   C 2 97  ? -41.43228 6.42421   23.13971  1.000 27.63875  ?  96  GLY   C CA    1 
ATOM   3447 C  C     . GLY   C 2 97  ? -42.13789 6.83079   24.41924  1.000 26.12647  ?  96  GLY   C C     1 
ATOM   3448 O  O     . GLY   C 2 97  ? -43.22423 7.41088   24.34814  1.000 26.71017  ?  96  GLY   C O     1 
ATOM   3449 N  N     . ILE   C 2 98  ? -41.53476 6.57912   25.57850  1.000 27.68173  ?  97  ILE   C N     1 
ATOM   3450 C  CA    . ILE   C 2 98  ? -42.17516 6.89767   26.85719  1.000 24.64270  ?  97  ILE   C CA    1 
ATOM   3451 C  C     . ILE   C 2 98  ? -42.22625 8.41289   27.05008  1.000 24.84435  ?  97  ILE   C C     1 
ATOM   3452 O  O     . ILE   C 2 98  ? -41.22094 9.11229   26.86318  1.000 24.01097  ?  97  ILE   C O     1 
ATOM   3453 C  CB    . ILE   C 2 98  ? -41.41446 6.20023   27.98883  1.000 28.31949  ?  97  ILE   C CB    1 
ATOM   3454 C  CG1   . ILE   C 2 98  ? -41.74388 4.68524   28.00301  1.000 31.91116  ?  97  ILE   C CG1   1 
ATOM   3455 C  CG2   . ILE   C 2 98  ? -41.58738 6.92680   29.34599  1.000 31.58871  ?  97  ILE   C CG2   1 
ATOM   3456 C  CD1   . ILE   C 2 98  ? -43.22070 4.35928   28.34431  1.000 33.94509  ?  97  ILE   C CD1   1 
ATOM   3457 N  N     . LEU   C 2 99  ? -43.39075 8.92606   27.45415  1.000 23.97516  ?  98  LEU   C N     1 
ATOM   3458 C  CA    . LEU   C 2 99  ? -43.58414 10.34341  27.75375  1.000 24.56503  ?  98  LEU   C CA    1 
ATOM   3459 C  C     . LEU   C 2 99  ? -43.69984 10.54629  29.26389  1.000 28.78407  ?  98  LEU   C C     1 
ATOM   3460 O  O     . LEU   C 2 99  ? -44.53212 9.90272   29.91283  1.000 24.27907  ?  98  LEU   C O     1 
ATOM   3461 C  CB    . LEU   C 2 99  ? -44.83671 10.84496  27.03908  1.000 27.18591  ?  98  LEU   C CB    1 
ATOM   3462 C  CG    . LEU   C 2 99  ? -45.29667 12.30403  27.06050  1.000 30.92121  ?  98  LEU   C CG    1 
ATOM   3463 C  CD1   . LEU   C 2 99  ? -44.25138 13.23508  26.45701  1.000 30.17755  ?  98  LEU   C CD1   1 
ATOM   3464 C  CD2   . LEU   C 2 99  ? -46.60287 12.39568  26.29566  1.000 31.43638  ?  98  LEU   C CD2   1 
ATOM   3465 N  N     . SER   C 2 100 ? -42.88704 11.44997  29.81705  1.000 22.70587  ?  99  SER   C N     1 
ATOM   3466 C  CA    . SER   C 2 100 ? -42.71364 11.54716  31.26287  1.000 22.74876  ?  99  SER   C CA    1 
ATOM   3467 C  C     . SER   C 2 100 ? -42.42385 13.00340  31.61226  1.000 29.03865  ?  99  SER   C C     1 
ATOM   3468 O  O     . SER   C 2 100 ? -41.99924 13.78604  30.75164  1.000 25.79814  ?  99  SER   C O     1 
ATOM   3469 C  CB    . SER   C 2 100 ? -41.59410 10.58930  31.71926  1.000 21.62611  ?  99  SER   C CB    1 
ATOM   3470 O  OG    . SER   C 2 100 ? -41.34475 10.59545  33.12423  1.000 24.08914  ?  99  SER   C OG    1 
ATOM   3471 N  N     . MET   C 2 101 ? -42.63350 13.35967  32.88947  1.000 28.34669  ?  100 MET   C N     1 
ATOM   3472 C  CA    . MET   C 2 101 ? -42.51127 14.74007  33.36424  1.000 26.98662  ?  100 MET   C CA    1 
ATOM   3473 C  C     . MET   C 2 101 ? -41.09821 15.06254  33.85114  1.000 24.70522  ?  100 MET   C C     1 
ATOM   3474 O  O     . MET   C 2 101 ? -40.55196 14.37493  34.71679  1.000 27.55882  ?  100 MET   C O     1 
ATOM   3475 C  CB    . MET   C 2 101 ? -43.49858 15.01163  34.50706  1.000 29.07561  ?  100 MET   C CB    1 
ATOM   3476 C  CG    . MET   C 2 101 ? -44.96570 14.98960  34.10045  1.000 26.78146  ?  100 MET   C CG    1 
ATOM   3477 S  SD    . MET   C 2 101 ? -45.40470 16.23293  32.87182  1.000 33.83039  ?  100 MET   C SD    1 
ATOM   3478 C  CE    . MET   C 2 101 ? -45.19558 17.74745  33.80074  1.000 32.03107  ?  100 MET   C CE    1 
ATOM   3479 N  N     . ALA   C 2 102 ? -40.51995 16.12181  33.30207  1.000 26.60937  ?  101 ALA   C N     1 
ATOM   3480 C  CA    . ALA   C 2 102 ? -39.33035 16.72206  33.87283  1.000 22.86409  ?  101 ALA   C CA    1 
ATOM   3481 C  C     . ALA   C 2 102 ? -39.71744 17.45797  35.15970  1.000 26.68199  ?  101 ALA   C C     1 
ATOM   3482 O  O     . ALA   C 2 102 ? -40.86271 17.87274  35.33271  1.000 28.12454  ?  101 ALA   C O     1 
ATOM   3483 C  CB    . ALA   C 2 102 ? -38.69983 17.69045  32.87642  1.000 24.31973  ?  101 ALA   C CB    1 
ATOM   3484 N  N     . ASN   C 2 103 ? -38.74971 17.63702  36.04861  1.000 29.11184  ?  102 ASN   C N     1 
ATOM   3485 C  CA    . ASN   C 2 103 ? -39.01513 18.27310  37.33786  1.000 26.36922  ?  102 ASN   C CA    1 
ATOM   3486 C  C     . ASN   C 2 103 ? -37.69762 18.71521  37.96297  1.000 28.03245  ?  102 ASN   C C     1 
ATOM   3487 O  O     . ASN   C 2 103 ? -36.61382 18.29786  37.54504  1.000 26.50260  ?  102 ASN   C O     1 
ATOM   3488 C  CB    . ASN   C 2 103 ? -39.76983 17.32259  38.27370  1.000 28.66086  ?  102 ASN   C CB    1 
ATOM   3489 C  CG    . ASN   C 2 103 ? -38.96663 16.07676  38.62736  1.000 25.71266  ?  102 ASN   C CG    1 
ATOM   3490 O  OD1   . ASN   C 2 103 ? -37.81514 16.14994  39.06617  1.000 26.42148  ?  102 ASN   C OD1   1 
ATOM   3491 N  ND2   . ASN   C 2 103 ? -39.58028 14.91994  38.44069  1.000 24.65411  ?  102 ASN   C ND2   1 
ATOM   3492 N  N     . ALA   C 2 104 ? -37.80622 19.57315  38.98113  1.000 31.53688  ?  103 ALA   C N     1 
ATOM   3493 C  CA    . ALA   C 2 104 ? -36.66534 19.97762  39.79399  1.000 33.91351  ?  103 ALA   C CA    1 
ATOM   3494 C  C     . ALA   C 2 104 ? -36.65797 19.28102  41.15501  1.000 39.42794  ?  103 ALA   C C     1 
ATOM   3495 O  O     . ALA   C 2 104 ? -36.20293 19.85155  42.14886  1.000 41.77527  ?  103 ALA   C O     1 
ATOM   3496 C  CB    . ALA   C 2 104 ? -36.65396 21.49173  39.98029  1.000 33.74164  ?  103 ALA   C CB    1 
ATOM   3497 N  N     . GLY   C 2 105 ? -37.15558 18.04787  41.21744  1.000 32.35882  ?  104 GLY   C N     1 
ATOM   3498 C  CA    . GLY   C 2 105 ? -37.27252 17.34080  42.46400  1.000 29.36180  ?  104 GLY   C CA    1 
ATOM   3499 C  C     . GLY   C 2 105 ? -38.71159 16.97087  42.74670  1.000 27.15411  ?  104 GLY   C C     1 
ATOM   3500 O  O     . GLY   C 2 105 ? -39.60996 17.24463  41.94682  1.000 27.19162  ?  104 GLY   C O     1 
ATOM   3501 N  N     . PRO   C 2 106 ? -38.95435 16.36367  43.91218  1.000 32.17806  ?  105 PRO   C N     1 
ATOM   3502 C  CA    . PRO   C 2 106 ? -40.30768 15.87990  44.25115  1.000 32.69662  ?  105 PRO   C CA    1 
ATOM   3503 C  C     . PRO   C 2 106 ? -41.37765 16.96671  44.20017  1.000 31.18059  ?  105 PRO   C C     1 
ATOM   3504 O  O     . PRO   C 2 106 ? -41.19165 18.07629  44.69945  1.000 33.93753  ?  105 PRO   C O     1 
ATOM   3505 C  CB    . PRO   C 2 106 ? -40.13782 15.33578  45.67414  1.000 33.55397  ?  105 PRO   C CB    1 
ATOM   3506 C  CG    . PRO   C 2 106 ? -38.67949 14.95360  45.77107  1.000 35.84709  ?  105 PRO   C CG    1 
ATOM   3507 C  CD    . PRO   C 2 106 ? -37.92979 15.91142  44.87337  1.000 29.60440  ?  105 PRO   C CD    1 
ATOM   3508 N  N     . ASN   C 2 107 ? -42.51595 16.62313  43.59374  1.000 30.71288  ?  106 ASN   C N     1 
ATOM   3509 C  CA    . ASN   C 2 107 ? -43.70125 17.48475  43.51650  1.000 33.39559  ?  106 ASN   C CA    1 
ATOM   3510 C  C     . ASN   C 2 107 ? -43.37331 18.88175  42.98874  1.000 38.32360  ?  106 ASN   C C     1 
ATOM   3511 O  O     . ASN   C 2 107 ? -43.75530 19.89702  43.58126  1.000 35.47460  ?  106 ASN   C O     1 
ATOM   3512 C  CB    . ASN   C 2 107 ? -44.40908 17.55935  44.87641  1.000 34.57920  ?  106 ASN   C CB    1 
ATOM   3513 C  CG    . ASN   C 2 107 ? -44.43783 16.22298  45.57185  1.000 31.27590  ?  106 ASN   C CG    1 
ATOM   3514 O  OD1   . ASN   C 2 107 ? -45.03077 15.26922  45.06936  1.000 37.07460  ?  106 ASN   C OD1   1 
ATOM   3515 N  ND2   . ASN   C 2 107 ? -43.77504 16.13276  46.72334  1.000 42.79524  ?  106 ASN   C ND2   1 
ATOM   3516 N  N     . THR   C 2 108 ? -42.65582 18.92571  41.84963  1.000 32.63322  ?  107 THR   C N     1 
ATOM   3517 C  CA    . THR   C 2 108 ? -42.33888 20.16859  41.14859  1.000 33.78746  ?  107 THR   C CA    1 
ATOM   3518 C  C     . THR   C 2 108 ? -42.68501 20.08224  39.66534  1.000 36.65307  ?  107 THR   C C     1 
ATOM   3519 O  O     . THR   C 2 108 ? -41.99642 20.68491  38.83277  1.000 36.85288  ?  107 THR   C O     1 
ATOM   3520 C  CB    . THR   C 2 108 ? -40.86057 20.53914  41.28731  1.000 33.79140  ?  107 THR   C CB    1 
ATOM   3521 O  OG1   . THR   C 2 108 ? -40.04661 19.48483  40.74661  1.000 34.84468  ?  107 THR   C OG1   1 
ATOM   3522 C  CG2   . THR   C 2 108 ? -40.47335 20.80871  42.73763  1.000 31.28133  ?  107 THR   C CG2   1 
ATOM   3523 N  N     . ASN   C 2 109 ? -43.75014 19.36438  39.31263  1.000 32.41101  ?  108 ASN   C N     1 
ATOM   3524 C  CA    . ASN   C 2 109 ? -44.14093 19.26678  37.91337  1.000 28.78420  ?  108 ASN   C CA    1 
ATOM   3525 C  C     . ASN   C 2 109 ? -44.78292 20.55972  37.42454  1.000 35.91027  ?  108 ASN   C C     1 
ATOM   3526 O  O     . ASN   C 2 109 ? -45.52195 21.22158  38.15703  1.000 33.70171  ?  108 ASN   C O     1 
ATOM   3527 C  CB    . ASN   C 2 109 ? -45.09265 18.10082  37.71187  1.000 31.31398  ?  108 ASN   C CB    1 
ATOM   3528 C  CG    . ASN   C 2 109 ? -44.52357 16.79976  38.24760  1.000 35.13164  ?  108 ASN   C CG    1 
ATOM   3529 O  OD1   . ASN   C 2 109 ? -43.58206 16.24512  37.67905  1.000 30.60515  ?  108 ASN   C OD1   1 
ATOM   3530 N  ND2   . ASN   C 2 109 ? -45.08814 16.30934  39.34670  1.000 30.20636  ?  108 ASN   C ND2   1 
ATOM   3531 N  N     . GLY   C 2 110 ? -44.50076 20.91437  36.16722  1.000 29.33641  ?  109 GLY   C N     1 
ATOM   3532 C  CA    . GLY   C 2 110 ? -45.11814 22.06618  35.55454  1.000 33.25358  ?  109 GLY   C CA    1 
ATOM   3533 C  C     . GLY   C 2 110 ? -45.61681 21.76242  34.16291  1.000 33.71429  ?  109 GLY   C C     1 
ATOM   3534 O  O     . GLY   C 2 110 ? -46.74423 21.29493  33.97290  1.000 29.92913  ?  109 GLY   C O     1 
ATOM   3535 N  N     . SER   C 2 111 ? -44.77816 22.03621  33.17268  1.000 30.16623  ?  110 SER   C N     1 
ATOM   3536 C  CA    . SER   C 2 111 ? -45.11228 21.73575  31.79358  1.000 31.43341  ?  110 SER   C CA    1 
ATOM   3537 C  C     . SER   C 2 111 ? -43.99919 21.01934  31.05469  1.000 25.39670  ?  110 SER   C C     1 
ATOM   3538 O  O     . SER   C 2 111 ? -44.28016 20.37542  30.03721  1.000 29.26627  ?  110 SER   C O     1 
ATOM   3539 C  CB    . SER   C 2 111 ? -45.47530 23.02010  31.02855  1.000 34.19257  ?  110 SER   C CB    1 
ATOM   3540 O  OG    . SER   C 2 111 ? -44.37726 23.93563  30.98347  1.000 34.63402  ?  110 SER   C OG    1 
ATOM   3541 N  N     . GLN   C 2 112 ? -42.76624 21.08350  31.54206  1.000 25.56146  ?  111 GLN   C N     1 
ATOM   3542 C  CA    . GLN   C 2 112 ? -41.66189 20.42222  30.87490  1.000 28.20673  ?  111 GLN   C CA    1 
ATOM   3543 C  C     . GLN   C 2 112 ? -41.82007 18.91238  30.97033  1.000 31.91851  ?  111 GLN   C C     1 
ATOM   3544 O  O     . GLN   C 2 112 ? -42.33784 18.37609  31.95959  1.000 27.68147  ?  111 GLN   C O     1 
ATOM   3545 C  CB    . GLN   C 2 112 ? -40.34276 20.87305  31.47495  1.000 30.20690  ?  111 GLN   C CB    1 
ATOM   3546 C  CG    . GLN   C 2 112 ? -39.91515 22.26873  31.01607  1.000 26.93914  ?  111 GLN   C CG    1 
ATOM   3547 C  CD    . GLN   C 2 112 ? -38.47675 22.52637  31.34237  1.000 28.55387  ?  111 GLN   C CD    1 
ATOM   3548 O  OE1   . GLN   C 2 112 ? -37.63229 21.66266  31.12577  1.000 27.55216  ?  111 GLN   C OE1   1 
ATOM   3549 N  NE2   . GLN   C 2 112 ? -38.18202 23.70034  31.90860  1.000 30.01473  ?  111 GLN   C NE2   1 
ATOM   3550 N  N     . PHE   C 2 113 ? -41.39040 18.23539  29.91267  1.000 25.22552  ?  112 PHE   C N     1 
ATOM   3551 C  CA    . PHE   C 2 113 ? -41.62904 16.81924  29.69903  1.000 24.35464  ?  112 PHE   C CA    1 
ATOM   3552 C  C     . PHE   C 2 113 ? -40.44898 16.31083  28.88748  1.000 29.20623  ?  112 PHE   C C     1 
ATOM   3553 O  O     . PHE   C 2 113 ? -39.70388 17.10261  28.28820  1.000 28.74868  ?  112 PHE   C O     1 
ATOM   3554 C  CB    . PHE   C 2 113 ? -42.93908 16.59482  28.94123  1.000 27.12098  ?  112 PHE   C CB    1 
ATOM   3555 C  CG    . PHE   C 2 113 ? -42.90392 17.17675  27.56090  1.000 30.01511  ?  112 PHE   C CG    1 
ATOM   3556 C  CD1   . PHE   C 2 113 ? -42.36134 16.45542  26.50216  1.000 30.70426  ?  112 PHE   C CD1   1 
ATOM   3557 C  CD2   . PHE   C 2 113 ? -43.32721 18.47905  27.33234  1.000 29.56326  ?  112 PHE   C CD2   1 
ATOM   3558 C  CE1   . PHE   C 2 113 ? -42.27194 17.01153  25.22892  1.000 28.63003  ?  112 PHE   C CE1   1 
ATOM   3559 C  CE2   . PHE   C 2 113 ? -43.24403 19.04105  26.05587  1.000 34.77362  ?  112 PHE   C CE2   1 
ATOM   3560 C  CZ    . PHE   C 2 113 ? -42.71090 18.30132  25.00513  1.000 28.87074  ?  112 PHE   C CZ    1 
ATOM   3561 N  N     . PHE   C 2 114 ? -40.28903 14.98817  28.83553  1.000 22.89224  ?  113 PHE   C N     1 
ATOM   3562 C  CA    . PHE   C 2 114 ? -39.28406 14.41807  27.95105  1.000 23.01345  ?  113 PHE   C CA    1 
ATOM   3563 C  C     . PHE   C 2 114 ? -39.86634 13.18202  27.28789  1.000 29.59137  ?  113 PHE   C C     1 
ATOM   3564 O  O     . PHE   C 2 114 ? -40.70342 12.47999  27.87215  1.000 25.91288  ?  113 PHE   C O     1 
ATOM   3565 C  CB    . PHE   C 2 114 ? -37.94629 14.09699  28.67796  1.000 22.82670  ?  113 PHE   C CB    1 
ATOM   3566 C  CG    . PHE   C 2 114 ? -38.07694 13.13505  29.86083  1.000 25.28212  ?  113 PHE   C CG    1 
ATOM   3567 C  CD1   . PHE   C 2 114 ? -38.66638 13.56064  31.05523  1.000 21.22268  ?  113 PHE   C CD1   1 
ATOM   3568 C  CD2   . PHE   C 2 114 ? -37.58886 11.83133  29.77881  1.000 24.91362  ?  113 PHE   C CD2   1 
ATOM   3569 C  CE1   . PHE   C 2 114 ? -38.78185 12.69802  32.14599  1.000 29.07605  ?  113 PHE   C CE1   1 
ATOM   3570 C  CE2   . PHE   C 2 114 ? -37.69483 10.96512  30.86420  1.000 28.66411  ?  113 PHE   C CE2   1 
ATOM   3571 C  CZ    . PHE   C 2 114 ? -38.29299 11.39625  32.04995  1.000 25.54346  ?  113 PHE   C CZ    1 
ATOM   3572 N  N     . ILE   C 2 115 ? -39.45897 12.96147  26.03224  1.000 24.28798  ?  114 ILE   C N     1 
ATOM   3573 C  CA    . ILE   C 2 115 ? -39.74455 11.73700  25.28808  1.000 22.72144  ?  114 ILE   C CA    1 
ATOM   3574 C  C     . ILE   C 2 115 ? -38.47685 10.89662  25.29999  1.000 22.81087  ?  114 ILE   C C     1 
ATOM   3575 O  O     . ILE   C 2 115 ? -37.42102 11.35389  24.85268  1.000 25.10182  ?  114 ILE   C O     1 
ATOM   3576 C  CB    . ILE   C 2 115 ? -40.17254 12.02236  23.84457  1.000 23.72065  ?  114 ILE   C CB    1 
ATOM   3577 C  CG1   . ILE   C 2 115 ? -41.22048 13.14011  23.78942  1.000 27.58391  ?  114 ILE   C CG1   1 
ATOM   3578 C  CG2   . ILE   C 2 115 ? -40.64995 10.72642  23.19644  1.000 23.80304  ?  114 ILE   C CG2   1 
ATOM   3579 C  CD1   . ILE   C 2 115 ? -41.44912 13.72709  22.36731  1.000 26.54504  ?  114 ILE   C CD1   1 
ATOM   3580 N  N     . CYS   C 2 116 ? -38.56738 9.67682   25.80663  1.000 22.75953  ?  115 CYS   C N     1 
ATOM   3581 C  CA    . CYS   C 2 116 ? -37.39667 8.80906   25.84861  1.000 22.68060  ?  115 CYS   C CA    1 
ATOM   3582 C  C     . CYS   C 2 116 ? -37.10055 8.26983   24.45399  1.000 30.38333  ?  115 CYS   C C     1 
ATOM   3583 O  O     . CYS   C 2 116 ? -38.00887 7.99796   23.66820  1.000 27.49804  ?  115 CYS   C O     1 
ATOM   3584 C  CB    . CYS   C 2 116 ? -37.61652 7.62245   26.77664  1.000 25.45530  ?  115 CYS   C CB    1 
ATOM   3585 S  SG    . CYS   C 2 116 ? -37.93927 8.05147   28.51020  1.000 27.28218  ?  115 CYS   C SG    1 
ATOM   3586 N  N     . THR   C 2 117 ? -35.81512 8.06012   24.17545  1.000 28.13283  ?  116 THR   C N     1 
ATOM   3587 C  CA    . THR   C 2 117 ? -35.38952 7.35525   22.97128  1.000 28.11083  ?  116 THR   C CA    1 
ATOM   3588 C  C     . THR   C 2 117 ? -34.76127 6.01619   23.31405  1.000 32.42756  ?  116 THR   C C     1 
ATOM   3589 O  O     . THR   C 2 117 ? -34.19877 5.34809   22.43160  1.000 30.28453  ?  116 THR   C O     1 
ATOM   3590 C  CB    . THR   C 2 117 ? -34.43074 8.22812   22.17646  1.000 24.81286  ?  116 THR   C CB    1 
ATOM   3591 O  OG1   . THR   C 2 117 ? -33.26282 8.49807   22.98101  1.000 25.28165  ?  116 THR   C OG1   1 
ATOM   3592 C  CG2   . THR   C 2 117 ? -35.12987 9.52303   21.84376  1.000 26.88813  ?  116 THR   C CG2   1 
ATOM   3593 N  N     . ALA   C 2 118 ? -34.86942 5.60840   24.57778  1.000 26.50223  ?  117 ALA   C N     1 
ATOM   3594 C  CA    . ALA   C 2 118 ? -34.31707 4.35838   25.08601  1.000 28.26024  ?  117 ALA   C CA    1 
ATOM   3595 C  C     . ALA   C 2 118 ? -34.90118 4.11805   26.46854  1.000 29.07450  ?  117 ALA   C C     1 
ATOM   3596 O  O     . ALA   C 2 118 ? -35.63953 4.94819   27.00388  1.000 28.30749  ?  117 ALA   C O     1 
ATOM   3597 C  CB    . ALA   C 2 118 ? -32.79428 4.39584   25.14912  1.000 32.79554  ?  117 ALA   C CB    1 
ATOM   3598 N  N     . LYS   C 2 119 ? -34.56549 2.96534   27.03680  1.000 31.42967  ?  118 LYS   C N     1 
ATOM   3599 C  CA    . LYS   C 2 119 ? -34.94460 2.66484   28.40784  1.000 32.70348  ?  118 LYS   C CA    1 
ATOM   3600 C  C     . LYS   C 2 119 ? -34.08204 3.47730   29.36867  1.000 30.52622  ?  118 LYS   C C     1 
ATOM   3601 O  O     . LYS   C 2 119 ? -32.84809 3.45008   29.28591  1.000 38.26488  ?  118 LYS   C O     1 
ATOM   3602 C  CB    . LYS   C 2 119 ? -34.78345 1.16299   28.68125  1.000 37.68044  ?  118 LYS   C CB    1 
ATOM   3603 C  CG    . LYS   C 2 119 ? -35.64672 0.61104   29.81362  1.000 36.80896  ?  118 LYS   C CG    1 
ATOM   3604 C  CD    . LYS   C 2 119 ? -35.52897 -0.91336  29.90858  1.000 39.28059  ?  118 LYS   C CD    1 
ATOM   3605 C  CE    . LYS   C 2 119 ? -34.38180 -1.33801  30.80030  1.000 43.89072  ?  118 LYS   C CE    1 
ATOM   3606 N  NZ    . LYS   C 2 119 ? -34.51088 -2.78521  31.16851  1.000 55.52923  ?  118 LYS   C NZ    1 
ATOM   3607 N  N     . THR   C 2 120 ? -34.73789 4.21026   30.27579  1.000 30.56454  ?  119 THR   C N     1 
ATOM   3608 C  CA    . THR   C 2 120 ? -34.08149 5.05943   31.27051  1.000 31.57594  ?  119 THR   C CA    1 
ATOM   3609 C  C     . THR   C 2 120 ? -34.62800 4.69260   32.66493  1.000 31.86123  ?  119 THR   C C     1 
ATOM   3610 O  O     . THR   C 2 120 ? -35.22027 5.50055   33.37831  1.000 28.60713  ?  119 THR   C O     1 
ATOM   3611 C  CB    . THR   C 2 120 ? -34.28710 6.55266   30.95655  1.000 28.17323  ?  119 THR   C CB    1 
ATOM   3612 O  OG1   . THR   C 2 120 ? -35.68326 6.84878   30.97263  1.000 25.03686  ?  119 THR   C OG1   1 
ATOM   3613 C  CG2   . THR   C 2 120 ? -33.75159 6.91351   29.56054  1.000 28.43493  ?  119 THR   C CG2   1 
ATOM   3614 N  N     . GLU   C 2 121 ? -34.41269 3.43498   33.04889  1.000 28.63506  ?  120 GLU   C N     1 
ATOM   3615 C  CA    . GLU   C 2 121 ? -35.01719 2.89776   34.26701  1.000 29.92608  ?  120 GLU   C CA    1 
ATOM   3616 C  C     . GLU   C 2 121 ? -34.54412 3.58707   35.54174  1.000 27.79080  ?  120 GLU   C C     1 
ATOM   3617 O  O     . GLU   C 2 121 ? -35.26429 3.55379   36.54591  1.000 32.20790  ?  120 GLU   C O     1 
ATOM   3618 C  CB    . GLU   C 2 121 ? -34.74854 1.39078   34.35539  1.000 34.18180  ?  120 GLU   C CB    1 
ATOM   3619 C  CG    . GLU   C 2 121 ? -33.31809 1.02293   34.71952  1.000 34.81358  ?  120 GLU   C CG    1 
ATOM   3620 C  CD    . GLU   C 2 121 ? -32.34452 1.04114   33.53937  1.000 41.11183  ?  120 GLU   C CD    1 
ATOM   3621 O  OE1   . GLU   C 2 121 ? -32.65320 1.63041   32.47417  1.000 38.26060  ?  120 GLU   C OE1   1 
ATOM   3622 O  OE2   . GLU   C 2 121 ? -31.24335 0.46235   33.68537  1.000 45.96419  -1 120 GLU   C OE2   1 
ATOM   3623 N  N     . TRP   C 2 122 ? -33.35528 4.19449   35.55809  1.000 31.99358  ?  121 TRP   C N     1 
ATOM   3624 C  CA    . TRP   C 2 122 ? -32.93837 4.89684   36.77283  1.000 29.09893  ?  121 TRP   C CA    1 
ATOM   3625 C  C     . TRP   C 2 122 ? -33.80218 6.11742   37.05927  1.000 28.57396  ?  121 TRP   C C     1 
ATOM   3626 O  O     . TRP   C 2 122 ? -33.70646 6.69406   38.15112  1.000 31.13606  ?  121 TRP   C O     1 
ATOM   3627 C  CB    . TRP   C 2 122 ? -31.47255 5.32176   36.67088  1.000 30.95730  ?  121 TRP   C CB    1 
ATOM   3628 C  CG    . TRP   C 2 122 ? -31.22494 6.27009   35.53741  1.000 32.21120  ?  121 TRP   C CG    1 
ATOM   3629 C  CD1   . TRP   C 2 122 ? -31.22658 7.63862   35.58864  1.000 30.13404  ?  121 TRP   C CD1   1 
ATOM   3630 C  CD2   . TRP   C 2 122 ? -30.96014 5.91790   34.17234  1.000 30.19312  ?  121 TRP   C CD2   1 
ATOM   3631 N  NE1   . TRP   C 2 122 ? -30.97306 8.15349   34.34148  1.000 33.30076  ?  121 TRP   C NE1   1 
ATOM   3632 C  CE2   . TRP   C 2 122 ? -30.80224 7.12072   33.45432  1.000 31.80111  ?  121 TRP   C CE2   1 
ATOM   3633 C  CE3   . TRP   C 2 122 ? -30.82696 4.70400   33.49533  1.000 32.72534  ?  121 TRP   C CE3   1 
ATOM   3634 C  CZ2   . TRP   C 2 122 ? -30.51986 7.14652   32.08383  1.000 28.49318  ?  121 TRP   C CZ2   1 
ATOM   3635 C  CZ3   . TRP   C 2 122 ? -30.55160 4.72770   32.14301  1.000 31.98656  ?  121 TRP   C CZ3   1 
ATOM   3636 C  CH2   . TRP   C 2 122 ? -30.40282 5.94273   31.44863  1.000 35.12165  ?  121 TRP   C CH2   1 
ATOM   3637 N  N     . LEU   C 2 123 ? -34.63091 6.53398   36.10921  1.000 27.47788  ?  122 LEU   C N     1 
ATOM   3638 C  CA    . LEU   C 2 123 ? -35.56828 7.62167   36.34904  1.000 29.81916  ?  122 LEU   C CA    1 
ATOM   3639 C  C     . LEU   C 2 123 ? -36.84689 7.15079   37.02766  1.000 28.11505  ?  122 LEU   C C     1 
ATOM   3640 O  O     . LEU   C 2 123 ? -37.67089 7.98845   37.41131  1.000 27.51071  ?  122 LEU   C O     1 
ATOM   3641 C  CB    . LEU   C 2 123 ? -35.91025 8.32245   35.02861  1.000 26.63299  ?  122 LEU   C CB    1 
ATOM   3642 C  CG    . LEU   C 2 123 ? -34.74251 8.95496   34.25461  1.000 29.16867  ?  122 LEU   C CG    1 
ATOM   3643 C  CD1   . LEU   C 2 123 ? -35.24572 9.58241   32.95944  1.000 26.06364  ?  122 LEU   C CD1   1 
ATOM   3644 C  CD2   . LEU   C 2 123 ? -34.02185 9.99449   35.09791  1.000 28.43268  ?  122 LEU   C CD2   1 
ATOM   3645 N  N     . ASP   C 2 124 ? -37.03012 5.83960   37.16598  1.000 27.19143  ?  123 ASP   C N     1 
ATOM   3646 C  CA    . ASP   C 2 124 ? -38.21827 5.29513   37.80845  1.000 28.38131  ?  123 ASP   C CA    1 
ATOM   3647 C  C     . ASP   C 2 124 ? -38.30630 5.80332   39.23636  1.000 30.99969  ?  123 ASP   C C     1 
ATOM   3648 O  O     . ASP   C 2 124 ? -37.31604 5.79408   39.97300  1.000 31.23841  ?  123 ASP   C O     1 
ATOM   3649 C  CB    . ASP   C 2 124 ? -38.18557 3.76002   37.78370  1.000 27.17950  ?  123 ASP   C CB    1 
ATOM   3650 C  CG    . ASP   C 2 124 ? -38.53775 3.19002   36.40383  1.000 28.77220  ?  123 ASP   C CG    1 
ATOM   3651 O  OD1   . ASP   C 2 124 ? -38.92295 3.97358   35.51031  1.000 30.26595  ?  123 ASP   C OD1   1 
ATOM   3652 O  OD2   . ASP   C 2 124 ? -38.43596 1.96186   36.20149  1.000 30.28471  -1 123 ASP   C OD2   1 
ATOM   3653 N  N     . GLY   C 2 125 ? -39.48605 6.28505   39.60866  1.000 31.80363  ?  124 GLY   C N     1 
ATOM   3654 C  CA    . GLY   C 2 125 ? -39.72379 6.80636   40.93711  1.000 32.88929  ?  124 GLY   C CA    1 
ATOM   3655 C  C     . GLY   C 2 125 ? -39.24420 8.22282   41.15999  1.000 37.03433  ?  124 GLY   C C     1 
ATOM   3656 O  O     . GLY   C 2 125 ? -39.41827 8.75494   42.26286  1.000 35.05403  ?  124 GLY   C O     1 
ATOM   3657 N  N     . LYS   C 2 126 ? -38.63853 8.84999   40.15499  1.000 35.90470  ?  125 LYS   C N     1 
ATOM   3658 C  CA    . LYS   C 2 126 ? -38.29291 10.25829  40.21537  1.000 33.74543  ?  125 LYS   C CA    1 
ATOM   3659 C  C     . LYS   C 2 126 ? -39.05569 11.10718  39.21532  1.000 30.98561  ?  125 LYS   C C     1 
ATOM   3660 O  O     . LYS   C 2 126 ? -39.13477 12.32940  39.40053  1.000 32.55479  ?  125 LYS   C O     1 
ATOM   3661 C  CB    . LYS   C 2 126 ? -36.78458 10.44050  39.99804  1.000 31.87648  ?  125 LYS   C CB    1 
ATOM   3662 C  CG    . LYS   C 2 126 ? -35.97526 9.71249   41.04296  1.000 38.98758  ?  125 LYS   C CG    1 
ATOM   3663 C  CD    . LYS   C 2 126 ? -34.56425 9.43079   40.55552  1.000 44.91949  ?  125 LYS   C CD    1 
ATOM   3664 C  CE    . LYS   C 2 126 ? -33.70003 8.93592   41.70910  1.000 55.91910  ?  125 LYS   C CE    1 
ATOM   3665 N  NZ    . LYS   C 2 126 ? -34.50415 8.09189   42.63877  1.000 58.18098  ?  125 LYS   C NZ    1 
ATOM   3666 N  N     . HIS   C 2 127 ? -39.65268 10.49664  38.19548  1.000 27.93908  ?  126 HIS   C N     1 
ATOM   3667 C  CA    . HIS   C 2 127 ? -40.35999 11.21128  37.14753  1.000 26.63832  ?  126 HIS   C CA    1 
ATOM   3668 C  C     . HIS   C 2 127 ? -41.65714 10.49626  36.85366  1.000 24.28086  ?  126 HIS   C C     1 
ATOM   3669 O  O     . HIS   C 2 127 ? -41.66867 9.27650   36.67918  1.000 33.28220  ?  126 HIS   C O     1 
ATOM   3670 C  CB    . HIS   C 2 127 ? -39.50628 11.29756  35.87376  1.000 25.79565  ?  126 HIS   C CB    1 
ATOM   3671 C  CG    . HIS   C 2 127 ? -38.27297 12.10334  36.06558  1.000 24.37622  ?  126 HIS   C CG    1 
ATOM   3672 N  ND1   . HIS   C 2 127 ? -38.23529 13.46295  35.82652  1.000 23.88782  ?  126 HIS   C ND1   1 
ATOM   3673 C  CD2   . HIS   C 2 127 ? -37.05320 11.76403  36.53417  1.000 22.42446  ?  126 HIS   C CD2   1 
ATOM   3674 C  CE1   . HIS   C 2 127 ? -37.03049 13.91734  36.11616  1.000 23.61563  ?  126 HIS   C CE1   1 
ATOM   3675 N  NE2   . HIS   C 2 127 ? -36.29472 12.90940  36.54616  1.000 26.45923  ?  126 HIS   C NE2   1 
ATOM   3676 N  N     . VAL   C 2 128 ? -42.74201 11.24971  36.77123  1.000 26.45762  ?  127 VAL   C N     1 
ATOM   3677 C  CA    . VAL   C 2 128 ? -44.04629 10.63903  36.54868  1.000 29.60432  ?  127 VAL   C CA    1 
ATOM   3678 C  C     . VAL   C 2 128 ? -44.22886 10.37064  35.05744  1.000 31.07007  ?  127 VAL   C C     1 
ATOM   3679 O  O     . VAL   C 2 128 ? -44.34597 11.30306  34.25658  1.000 25.24001  ?  127 VAL   C O     1 
ATOM   3680 C  CB    . VAL   C 2 128 ? -45.17632 11.51100  37.10012  1.000 28.96272  ?  127 VAL   C CB    1 
ATOM   3681 C  CG1   . VAL   C 2 128 ? -46.51688 10.87712  36.75871  1.000 27.64317  ?  127 VAL   C CG1   1 
ATOM   3682 C  CG2   . VAL   C 2 128 ? -44.99003 11.68990  38.61506  1.000 27.14775  ?  127 VAL   C CG2   1 
ATOM   3683 N  N     . VAL   C 2 129 ? -44.25350 9.08298   34.68663  1.000 26.38603  ?  128 VAL   C N     1 
ATOM   3684 C  CA    . VAL   C 2 129 ? -44.58952 8.66011   33.33188  1.000 29.42247  ?  128 VAL   C CA    1 
ATOM   3685 C  C     . VAL   C 2 129 ? -46.09119 8.75370   33.15462  1.000 30.45787  ?  128 VAL   C C     1 
ATOM   3686 O  O     . VAL   C 2 129 ? -46.85790 8.36393   34.05144  1.000 28.54285  ?  128 VAL   C O     1 
ATOM   3687 C  CB    . VAL   C 2 129 ? -44.09843 7.22074   33.07547  1.000 28.24229  ?  128 VAL   C CB    1 
ATOM   3688 C  CG1   . VAL   C 2 129 ? -44.64229 6.69147   31.73032  1.000 25.81087  ?  128 VAL   C CG1   1 
ATOM   3689 C  CG2   . VAL   C 2 129 ? -42.58173 7.14839   33.16156  1.000 24.43011  ?  128 VAL   C CG2   1 
ATOM   3690 N  N     . PHE   C 2 130 ? -46.52417 9.26980   31.99582  1.000 26.51222  ?  129 PHE   C N     1 
ATOM   3691 C  CA    . PHE   C 2 130 ? -47.95191 9.43572   31.77165  1.000 30.22767  ?  129 PHE   C CA    1 
ATOM   3692 C  C     . PHE   C 2 130 ? -48.38525 9.20629   30.33548  1.000 31.28442  ?  129 PHE   C C     1 
ATOM   3693 O  O     . PHE   C 2 130 ? -49.57051 9.38658   30.04912  1.000 30.57469  ?  129 PHE   C O     1 
ATOM   3694 C  CB    . PHE   C 2 130 ? -48.40567 10.83978  32.22709  1.000 24.11122  ?  129 PHE   C CB    1 
ATOM   3695 C  CG    . PHE   C 2 130 ? -47.77311 11.96514  31.44958  1.000 26.50931  ?  129 PHE   C CG    1 
ATOM   3696 C  CD1   . PHE   C 2 130 ? -46.49592 12.40823  31.76160  1.000 25.84022  ?  129 PHE   C CD1   1 
ATOM   3697 C  CD2   . PHE   C 2 130 ? -48.43884 12.55390  30.39073  1.000 26.78114  ?  129 PHE   C CD2   1 
ATOM   3698 C  CE1   . PHE   C 2 130 ? -45.90115 13.44675  31.02975  1.000 28.72868  ?  129 PHE   C CE1   1 
ATOM   3699 C  CE2   . PHE   C 2 130 ? -47.85597 13.57974  29.65564  1.000 30.88287  ?  129 PHE   C CE2   1 
ATOM   3700 C  CZ    . PHE   C 2 130 ? -46.58473 14.03582  29.98171  1.000 27.99498  ?  129 PHE   C CZ    1 
ATOM   3701 N  N     . GLY   C 2 131 ? -47.49614 8.83113   29.42181  1.000 29.50829  ?  130 GLY   C N     1 
ATOM   3702 C  CA    . GLY   C 2 131 ? -47.93057 8.63218   28.05053  1.000 28.36670  ?  130 GLY   C CA    1 
ATOM   3703 C  C     . GLY   C 2 131 ? -46.89198 7.83977   27.27943  1.000 29.22539  ?  130 GLY   C C     1 
ATOM   3704 O  O     . GLY   C 2 131 ? -45.87873 7.40650   27.82944  1.000 29.56354  ?  130 GLY   C O     1 
ATOM   3705 N  N     . LYS   C 2 132 ? -47.15102 7.65576   25.98567  1.000 27.33028  ?  131 LYS   C N     1 
ATOM   3706 C  CA    . LYS   C 2 132 ? -46.25970 6.89177   25.11902  1.000 30.35704  ?  131 LYS   C CA    1 
ATOM   3707 C  C     . LYS   C 2 132 ? -46.49209 7.32285   23.67779  1.000 31.04959  ?  131 LYS   C C     1 
ATOM   3708 O  O     . LYS   C 2 132 ? -47.61235 7.67447   23.29768  1.000 26.51953  ?  131 LYS   C O     1 
ATOM   3709 C  CB    . LYS   C 2 132 ? -46.48102 5.38196   25.25032  1.000 31.10076  ?  131 LYS   C CB    1 
ATOM   3710 C  CG    . LYS   C 2 132 ? -45.29553 4.58026   24.73508  1.000 42.21493  ?  131 LYS   C CG    1 
ATOM   3711 C  CD    . LYS   C 2 132 ? -45.40753 3.05047   24.78909  1.000 41.32132  ?  131 LYS   C CD    1 
ATOM   3712 C  CE    . LYS   C 2 132 ? -44.49625 2.45327   23.69025  1.000 52.48430  ?  131 LYS   C CE    1 
ATOM   3713 N  NZ    . LYS   C 2 132 ? -44.63297 0.98574   23.36762  1.000 53.54897  ?  131 LYS   C NZ    1 
ATOM   3714 N  N     . VAL   C 2 133 ? -45.41994 7.34175   22.88197  1.000 28.31223  ?  132 VAL   C N     1 
ATOM   3715 C  CA    . VAL   C 2 133 ? -45.59007 7.71344   21.48528  1.000 25.00484  ?  132 VAL   C CA    1 
ATOM   3716 C  C     . VAL   C 2 133 ? -46.48540 6.68334   20.80644  1.000 27.57897  ?  132 VAL   C C     1 
ATOM   3717 O  O     . VAL   C 2 133 ? -46.25005 5.46673   20.87902  1.000 30.26787  ?  132 VAL   C O     1 
ATOM   3718 C  CB    . VAL   C 2 133 ? -44.23040 7.85618   20.78363  1.000 27.47509  ?  132 VAL   C CB    1 
ATOM   3719 C  CG1   . VAL   C 2 133 ? -44.43949 7.94520   19.25190  1.000 28.56470  ?  132 VAL   C CG1   1 
ATOM   3720 C  CG2   . VAL   C 2 133 ? -43.50176 9.11544   21.28781  1.000 19.93041  ?  132 VAL   C CG2   1 
ATOM   3721 N  N     . LYS   C 2 134 ? -47.54963 7.16626   20.18140  1.000 26.81127  ?  133 LYS   C N     1 
ATOM   3722 C  CA    . LYS   C 2 134 ? -48.43517 6.30305   19.40676  1.000 35.41052  ?  133 LYS   C CA    1 
ATOM   3723 C  C     . LYS   C 2 134 ? -47.91390 6.17061   17.97528  1.000 33.08339  ?  133 LYS   C C     1 
ATOM   3724 O  O     . LYS   C 2 134 ? -47.56928 5.07269   17.53007  1.000 40.08897  ?  133 LYS   C O     1 
ATOM   3725 C  CB    . LYS   C 2 134 ? -49.85974 6.87412   19.46219  1.000 32.62126  ?  133 LYS   C CB    1 
ATOM   3726 C  CG    . LYS   C 2 134 ? -50.97406 5.98688   18.96584  1.000 44.74930  ?  133 LYS   C CG    1 
ATOM   3727 C  CD    . LYS   C 2 134 ? -52.32330 6.68877   19.19582  1.000 46.73643  ?  133 LYS   C CD    1 
ATOM   3728 C  CE    . LYS   C 2 134 ? -53.51034 5.72890   19.14475  1.000 47.42913  ?  133 LYS   C CE    1 
ATOM   3729 N  NZ    . LYS   C 2 134 ? -54.43034 5.97171   20.30531  1.000 54.36311  ?  133 LYS   C NZ    1 
ATOM   3730 N  N     . GLU   C 2 135 ? -47.80988 7.28574   17.25760  1.000 36.66086  ?  134 GLU   C N     1 
ATOM   3731 C  CA    . GLU   C 2 135 ? -47.32969 7.29187   15.87924  1.000 37.75531  ?  134 GLU   C CA    1 
ATOM   3732 C  C     . GLU   C 2 135 ? -46.28982 8.38499   15.70558  1.000 33.56092  ?  134 GLU   C C     1 
ATOM   3733 O  O     . GLU   C 2 135 ? -46.30689 9.39453   16.41301  1.000 34.29541  ?  134 GLU   C O     1 
ATOM   3734 C  CB    . GLU   C 2 135 ? -48.47256 7.50638   14.87167  1.000 39.28582  ?  134 GLU   C CB    1 
ATOM   3735 C  CG    . GLU   C 2 135 ? -48.98552 6.22019   14.24901  1.000 47.33749  ?  134 GLU   C CG    1 
ATOM   3736 C  CD    . GLU   C 2 135 ? -50.25035 6.44258   13.44532  1.000 59.84331  ?  134 GLU   C CD    1 
ATOM   3737 O  OE1   . GLU   C 2 135 ? -50.77317 7.57823   13.48252  1.000 55.84353  ?  134 GLU   C OE1   1 
ATOM   3738 O  OE2   . GLU   C 2 135 ? -50.71867 5.48965   12.78111  1.000 68.28071  -1 134 GLU   C OE2   1 
ATOM   3739 N  N     . GLY   C 2 136 ? -45.39077 8.17980   14.74658  1.000 35.63092  ?  135 GLY   C N     1 
ATOM   3740 C  CA    . GLY   C 2 136 ? -44.33370 9.13304   14.49368  1.000 32.51640  ?  135 GLY   C CA    1 
ATOM   3741 C  C     . GLY   C 2 136 ? -43.09039 8.95003   15.33107  1.000 26.30588  ?  135 GLY   C C     1 
ATOM   3742 O  O     . GLY   C 2 136 ? -42.33052 9.90386   15.49678  1.000 24.85098  ?  135 GLY   C O     1 
ATOM   3743 N  N     . MET   C 2 137 ? -42.87315 7.76166   15.89443  1.000 26.00391  ?  136 MET   C N     1 
ATOM   3744 C  CA    . MET   C 2 137 ? -41.60770 7.49626   16.56597  1.000 24.63662  ?  136 MET   C CA    1 
ATOM   3745 C  C     . MET   C 2 137 ? -40.42912 7.78923   15.64953  1.000 29.29689  ?  136 MET   C C     1 
ATOM   3746 O  O     . MET   C 2 137 ? -39.35511 8.18026   16.11597  1.000 25.20440  ?  136 MET   C O     1 
ATOM   3747 C  CB    . MET   C 2 137 ? -41.57006 6.05184   17.05045  1.000 25.43070  ?  136 MET   C CB    1 
ATOM   3748 C  CG    . MET   C 2 137 ? -40.49745 5.77368   18.10036  1.000 31.62716  ?  136 MET   C CG    1 
ATOM   3749 S  SD    . MET   C 2 137 ? -40.50228 6.91304   19.53249  1.000 29.23342  ?  136 MET   C SD    1 
ATOM   3750 C  CE    . MET   C 2 137 ? -38.82337 6.65787   20.13526  1.000 25.44840  ?  136 MET   C CE    1 
ATOM   3751 N  N     . ASN   C 2 138 ? -40.60823 7.62058   14.33994  1.000 25.52900  ?  137 ASN   C N     1 
ATOM   3752 C  CA    . ASN   C 2 138 ? -39.51778 7.94980   13.42769  1.000 28.68498  ?  137 ASN   C CA    1 
ATOM   3753 C  C     . ASN   C 2 138 ? -39.19604 9.43658   13.47385  1.000 25.96694  ?  137 ASN   C C     1 
ATOM   3754 O  O     . ASN   C 2 138 ? -38.04719 9.83133   13.23821  1.000 25.96511  ?  137 ASN   C O     1 
ATOM   3755 C  CB    . ASN   C 2 138 ? -39.87178 7.52066   12.00085  1.000 31.84806  ?  137 ASN   C CB    1 
ATOM   3756 C  CG    . ASN   C 2 138 ? -40.79291 8.50382   11.31597  1.000 32.96289  ?  137 ASN   C CG    1 
ATOM   3757 O  OD1   . ASN   C 2 138 ? -41.95601 8.63955   11.68068  1.000 36.01220  ?  137 ASN   C OD1   1 
ATOM   3758 N  ND2   . ASN   C 2 138 ? -40.26903 9.21266   10.32586  1.000 36.87527  ?  137 ASN   C ND2   1 
ATOM   3759 N  N     . ILE   C 2 139 ? -40.19090 10.26972  13.77864  1.000 24.23057  ?  138 ILE   C N     1 
ATOM   3760 C  CA    . ILE   C 2 139 ? -39.94180 11.69827  13.91187  1.000 27.85077  ?  138 ILE   C CA    1 
ATOM   3761 C  C     . ILE   C 2 139 ? -39.14997 11.98505  15.19374  1.000 30.79208  ?  138 ILE   C C     1 
ATOM   3762 O  O     . ILE   C 2 139 ? -38.26843 12.84986  15.21603  1.000 25.95054  ?  138 ILE   C O     1 
ATOM   3763 C  CB    . ILE   C 2 139 ? -41.26561 12.48583  13.87756  1.000 25.17500  ?  138 ILE   C CB    1 
ATOM   3764 C  CG1   . ILE   C 2 139 ? -42.04033 12.25535  12.56901  1.000 32.97173  ?  138 ILE   C CG1   1 
ATOM   3765 C  CG2   . ILE   C 2 139 ? -41.00671 13.97919  14.15139  1.000 27.07796  ?  138 ILE   C CG2   1 
ATOM   3766 C  CD1   . ILE   C 2 139 ? -41.23170 12.58175  11.26979  1.000 30.85363  ?  138 ILE   C CD1   1 
ATOM   3767 N  N     . VAL   C 2 140 ? -39.44787 11.27074  16.27931  1.000 26.84235  ?  139 VAL   C N     1 
ATOM   3768 C  CA    . VAL   C 2 140 ? -38.64555 11.44873  17.48666  1.000 27.85000  ?  139 VAL   C CA    1 
ATOM   3769 C  C     . VAL   C 2 140 ? -37.20894 11.00220  17.24033  1.000 28.93376  ?  139 VAL   C C     1 
ATOM   3770 O  O     . VAL   C 2 140 ? -36.25794 11.66005  17.68088  1.000 30.30898  ?  139 VAL   C O     1 
ATOM   3771 C  CB    . VAL   C 2 140 ? -39.28779 10.70932  18.67374  1.000 29.27224  ?  139 VAL   C CB    1 
ATOM   3772 C  CG1   . VAL   C 2 140 ? -38.31481 10.64744  19.84509  1.000 24.79826  ?  139 VAL   C CG1   1 
ATOM   3773 C  CG2   . VAL   C 2 140 ? -40.55233 11.41091  19.07663  1.000 29.19651  ?  139 VAL   C CG2   1 
ATOM   3774 N  N     . GLU   C 2 141 ? -37.02151 9.89163   16.51544  1.000 28.74290  ?  140 GLU   C N     1 
ATOM   3775 C  CA    . GLU   C 2 141 ? -35.66673 9.45652   16.17813  1.000 32.67330  ?  140 GLU   C CA    1 
ATOM   3776 C  C     . GLU   C 2 141 ? -34.93340 10.51353  15.35632  1.000 33.13952  ?  140 GLU   C C     1 
ATOM   3777 O  O     . GLU   C 2 141 ? -33.75393 10.79826  15.60683  1.000 33.40657  ?  140 GLU   C O     1 
ATOM   3778 C  CB    . GLU   C 2 141 ? -35.70951 8.11629   15.43667  1.000 30.85069  ?  140 GLU   C CB    1 
ATOM   3779 C  CG    . GLU   C 2 141 ? -36.01581 6.92080   16.33324  1.000 27.98981  ?  140 GLU   C CG    1 
ATOM   3780 C  CD    . GLU   C 2 141 ? -36.50239 5.67973   15.54607  1.000 37.58950  ?  140 GLU   C CD    1 
ATOM   3781 O  OE1   . GLU   C 2 141 ? -36.27811 5.56720   14.31731  1.000 37.07964  ?  140 GLU   C OE1   1 
ATOM   3782 O  OE2   . GLU   C 2 141 ? -37.13162 4.80830   16.15897  1.000 41.02303  -1 140 GLU   C OE2   1 
ATOM   3783 N  N     . ALA   C 2 142 ? -35.62067 11.12835  14.38821  1.000 30.36362  ?  141 ALA   C N     1 
ATOM   3784 C  CA    . ALA   C 2 142 ? -34.97468 12.15596  13.57448  1.000 35.23539  ?  141 ALA   C CA    1 
ATOM   3785 C  C     . ALA   C 2 142 ? -34.60650 13.37812  14.40844  1.000 31.65315  ?  141 ALA   C C     1 
ATOM   3786 O  O     . ALA   C 2 142 ? -33.57148 14.00978  14.15784  1.000 32.07461  ?  141 ALA   C O     1 
ATOM   3787 C  CB    . ALA   C 2 142 ? -35.87438 12.55075  12.39311  1.000 28.24443  ?  141 ALA   C CB    1 
ATOM   3788 N  N     . MET   C 2 143 ? -35.43337 13.72398  15.39950  1.000 32.55082  ?  142 MET   C N     1 
ATOM   3789 C  CA    . MET   C 2 143 ? -35.08673 14.81932  16.29971  1.000 30.80104  ?  142 MET   C CA    1 
ATOM   3790 C  C     . MET   C 2 143 ? -33.76031 14.54853  16.98623  1.000 28.84513  ?  142 MET   C C     1 
ATOM   3791 O  O     . MET   C 2 143 ? -32.93704 15.45846  17.14422  1.000 27.72157  ?  142 MET   C O     1 
ATOM   3792 C  CB    . MET   C 2 143 ? -36.19410 15.02183  17.33997  1.000 25.66746  ?  142 MET   C CB    1 
ATOM   3793 C  CG    . MET   C 2 143 ? -37.46213 15.57844  16.76566  1.000 33.29418  ?  142 MET   C CG    1 
ATOM   3794 S  SD    . MET   C 2 143 ? -38.80787 15.64538  17.96355  1.000 37.87399  ?  142 MET   C SD    1 
ATOM   3795 C  CE    . MET   C 2 143 ? -37.97214 16.42776  19.32425  1.000 30.89790  ?  142 MET   C CE    1 
ATOM   3796 N  N     . GLU   C 2 144 ? -33.52771 13.28415  17.36111  1.000 35.14907  ?  143 GLU   C N     1 
ATOM   3797 C  CA    . GLU   C 2 144 ? -32.33968 12.89263  18.11601  1.000 37.94639  ?  143 GLU   C CA    1 
ATOM   3798 C  C     . GLU   C 2 144 ? -31.06734 13.27165  17.38556  1.000 38.01645  ?  143 GLU   C C     1 
ATOM   3799 O  O     . GLU   C 2 144 ? -30.03254 13.50709  18.01492  1.000 41.04409  ?  143 GLU   C O     1 
ATOM   3800 C  CB    . GLU   C 2 144 ? -32.36128 11.37340  18.37389  1.000 35.03934  ?  143 GLU   C CB    1 
ATOM   3801 C  CG    . GLU   C 2 144 ? -32.18861 10.96094  19.81931  1.000 34.11819  ?  143 GLU   C CG    1 
ATOM   3802 C  CD    . GLU   C 2 144 ? -31.78146 9.49924   19.97796  1.000 36.51582  ?  143 GLU   C CD    1 
ATOM   3803 O  OE1   . GLU   C 2 144 ? -31.52468 8.82097   18.95758  1.000 33.39957  ?  143 GLU   C OE1   1 
ATOM   3804 O  OE2   . GLU   C 2 144 ? -31.70809 9.03119   21.13590  1.000 36.48213  -1 143 GLU   C OE2   1 
ATOM   3805 N  N     . ARG   C 2 145 ? -31.13053 13.36513  16.05780  1.000 37.70736  ?  144 ARG   C N     1 
ATOM   3806 C  CA    . ARG   C 2 145 ? -29.95370 13.65326  15.25360  1.000 35.46850  ?  144 ARG   C CA    1 
ATOM   3807 C  C     . ARG   C 2 145 ? -29.51124 15.10418  15.35105  1.000 31.97967  ?  144 ARG   C C     1 
ATOM   3808 O  O     . ARG   C 2 145 ? -28.40495 15.42073  14.90109  1.000 32.00278  ?  144 ARG   C O     1 
ATOM   3809 C  CB    . ARG   C 2 145 ? -30.23447 13.25524  13.79415  1.000 45.21357  ?  144 ARG   C CB    1 
ATOM   3810 C  CG    . ARG   C 2 145 ? -31.00549 11.92534  13.70086  1.000 44.26006  ?  144 ARG   C CG    1 
ATOM   3811 C  CD    . ARG   C 2 145 ? -30.85185 11.21171  12.36501  1.000 48.75809  ?  144 ARG   C CD    1 
ATOM   3812 N  NE    . ARG   C 2 145 ? -31.50165 9.90420   12.41086  1.000 60.13850  ?  144 ARG   C NE    1 
ATOM   3813 C  CZ    . ARG   C 2 145 ? -32.67489 9.61924   11.85465  1.000 56.14932  ?  144 ARG   C CZ    1 
ATOM   3814 N  NH1   . ARG   C 2 145 ? -33.32664 10.51007  11.11975  1.000 53.30575  ?  144 ARG   C NH1   1 
ATOM   3815 N  NH2   . ARG   C 2 145 ? -33.20300 8.40674   12.03403  1.000 45.81269  ?  144 ARG   C NH2   1 
ATOM   3816 N  N     . PHE   C 2 146 ? -30.31659 15.98157  15.94496  1.000 28.50488  ?  145 PHE   C N     1 
ATOM   3817 C  CA    . PHE   C 2 146 ? -29.92689 17.36523  16.16465  1.000 26.29874  ?  145 PHE   C CA    1 
ATOM   3818 C  C     . PHE   C 2 146 ? -29.50560 17.63526  17.60563  1.000 30.56428  ?  145 PHE   C C     1 
ATOM   3819 O  O     . PHE   C 2 146 ? -29.41771 18.80389  18.00640  1.000 31.96234  ?  145 PHE   C O     1 
ATOM   3820 C  CB    . PHE   C 2 146 ? -31.06794 18.30451  15.77794  1.000 30.67732  ?  145 PHE   C CB    1 
ATOM   3821 C  CG    . PHE   C 2 146 ? -31.54699 18.12480  14.36203  1.000 33.62027  ?  145 PHE   C CG    1 
ATOM   3822 C  CD1   . PHE   C 2 146 ? -30.86340 18.70638  13.30834  1.000 32.49942  ?  145 PHE   C CD1   1 
ATOM   3823 C  CD2   . PHE   C 2 146 ? -32.67291 17.36105  14.08512  1.000 35.40260  ?  145 PHE   C CD2   1 
ATOM   3824 C  CE1   . PHE   C 2 146 ? -31.29795 18.53482  12.00567  1.000 33.98947  ?  145 PHE   C CE1   1 
ATOM   3825 C  CE2   . PHE   C 2 146 ? -33.11410 17.18627  12.78085  1.000 37.59114  ?  145 PHE   C CE2   1 
ATOM   3826 C  CZ    . PHE   C 2 146 ? -32.41815 17.77312  11.74142  1.000 36.42819  ?  145 PHE   C CZ    1 
ATOM   3827 N  N     . GLY   C 2 147 ? -29.26293 16.58472  18.39715  1.000 34.15525  ?  146 GLY   C N     1 
ATOM   3828 C  CA    . GLY   C 2 147 ? -28.84255 16.73227  19.77805  1.000 24.46001  ?  146 GLY   C CA    1 
ATOM   3829 C  C     . GLY   C 2 147 ? -27.33497 16.69871  19.93289  1.000 29.43224  ?  146 GLY   C C     1 
ATOM   3830 O  O     . GLY   C 2 147 ? -26.57479 16.82101  18.96931  1.000 33.44430  ?  146 GLY   C O     1 
ATOM   3831 N  N     . SER   C 2 148 ? -26.89532 16.54998  21.18429  1.000 29.44806  ?  147 SER   C N     1 
ATOM   3832 C  CA    . SER   C 2 148 ? -25.47445 16.51746  21.49956  1.000 32.78538  ?  147 SER   C CA    1 
ATOM   3833 C  C     . SER   C 2 148 ? -25.29194 15.93735  22.89847  1.000 31.91540  ?  147 SER   C C     1 
ATOM   3834 O  O     . SER   C 2 148 ? -26.25946 15.70858  23.63555  1.000 28.91944  ?  147 SER   C O     1 
ATOM   3835 C  CB    . SER   C 2 148 ? -24.84868 17.91424  21.40496  1.000 31.76119  ?  147 SER   C CB    1 
ATOM   3836 O  OG    . SER   C 2 148 ? -25.40402 18.78684  22.37515  1.000 30.58592  ?  147 SER   C OG    1 
ATOM   3837 N  N     . ARG   C 2 149 ? -24.02465 15.75816  23.27711  1.000 29.02222  ?  148 ARG   C N     1 
ATOM   3838 C  CA    . ARG   C 2 149 ? -23.69346 15.12259  24.55267  1.000 32.93677  ?  148 ARG   C CA    1 
ATOM   3839 C  C     . ARG   C 2 149 ? -24.29993 15.87758  25.73901  1.000 31.45166  ?  148 ARG   C C     1 
ATOM   3840 O  O     . ARG   C 2 149 ? -24.85509 15.26478  26.65998  1.000 30.17772  ?  148 ARG   C O     1 
ATOM   3841 C  CB    . ARG   C 2 149 ? -22.17672 15.02456  24.68509  1.000 33.34002  ?  148 ARG   C CB    1 
ATOM   3842 C  CG    . ARG   C 2 149 ? -21.70113 14.38482  25.94069  1.000 30.93009  ?  148 ARG   C CG    1 
ATOM   3843 C  CD    . ARG   C 2 149 ? -20.21201 14.27086  25.91480  1.000 37.86167  ?  148 ARG   C CD    1 
ATOM   3844 N  NE    . ARG   C 2 149 ? -19.71819 13.75498  27.17789  1.000 32.67128  ?  148 ARG   C NE    1 
ATOM   3845 C  CZ    . ARG   C 2 149 ? -19.41556 14.52985  28.20232  1.000 33.93249  ?  148 ARG   C CZ    1 
ATOM   3846 N  NH1   . ARG   C 2 149 ? -19.42793 15.84608  28.09120  1.000 31.22830  ?  148 ARG   C NH1   1 
ATOM   3847 N  NH2   . ARG   C 2 149 ? -19.10171 13.97085  29.36112  1.000 32.11153  ?  148 ARG   C NH2   1 
ATOM   3848 N  N     . ASN   C 2 150 ? -24.22596 17.20393  25.73036  1.000 27.93923  ?  149 ASN   C N     1 
ATOM   3849 C  CA    . ASN   C 2 150 ? -24.78596 17.99539  26.82290  1.000 27.18086  ?  149 ASN   C CA    1 
ATOM   3850 C  C     . ASN   C 2 150 ? -26.19715 18.52478  26.54848  1.000 29.96500  ?  149 ASN   C C     1 
ATOM   3851 O  O     . ASN   C 2 150 ? -26.72081 19.28965  27.36647  1.000 30.06109  ?  149 ASN   C O     1 
ATOM   3852 C  CB    . ASN   C 2 150 ? -23.84423 19.16553  27.17975  1.000 28.14597  ?  149 ASN   C CB    1 
ATOM   3853 C  CG    . ASN   C 2 150 ? -23.93665 20.33003  26.21154  1.000 36.82642  ?  149 ASN   C CG    1 
ATOM   3854 O  OD1   . ASN   C 2 150 ? -24.35207 20.16815  25.06059  1.000 39.51719  ?  149 ASN   C OD1   1 
ATOM   3855 N  ND2   . ASN   C 2 150 ? -23.54327 21.52191  26.67491  1.000 36.73421  ?  149 ASN   C ND2   1 
ATOM   3856 N  N     . GLY   C 2 151 ? -26.83038 18.14802  25.42424  1.000 29.89468  ?  150 GLY   C N     1 
ATOM   3857 C  CA    . GLY   C 2 151 ? -28.21166 18.48802  25.15571  1.000 27.39241  ?  150 GLY   C CA    1 
ATOM   3858 C  C     . GLY   C 2 151 ? -28.42646 19.66059  24.21708  1.000 31.64358  ?  150 GLY   C C     1 
ATOM   3859 O  O     . GLY   C 2 151 ? -29.49804 19.74760  23.60774  1.000 29.32277  ?  150 GLY   C O     1 
ATOM   3860 N  N     . LYS   C 2 152 ? -27.44287 20.55731  24.08200  1.000 35.43320  ?  151 LYS   C N     1 
ATOM   3861 C  CA    . LYS   C 2 152 ? -27.55723 21.67963  23.15517  1.000 35.11372  ?  151 LYS   C CA    1 
ATOM   3862 C  C     . LYS   C 2 152 ? -27.90029 21.18745  21.75390  1.000 29.11335  ?  151 LYS   C C     1 
ATOM   3863 O  O     . LYS   C 2 152 ? -27.28653 20.24579  21.25135  1.000 32.01589  ?  151 LYS   C O     1 
ATOM   3864 C  CB    . LYS   C 2 152 ? -26.25137 22.47559  23.13887  1.000 36.26382  ?  151 LYS   C CB    1 
ATOM   3865 C  CG    . LYS   C 2 152 ? -25.97132 23.22072  24.44409  1.000 44.48665  ?  151 LYS   C CG    1 
ATOM   3866 C  CD    . LYS   C 2 152 ? -27.25364 23.85542  24.99084  1.000 48.33865  ?  151 LYS   C CD    1 
ATOM   3867 C  CE    . LYS   C 2 152 ? -27.02500 24.72961  26.23119  1.000 49.12850  ?  151 LYS   C CE    1 
ATOM   3868 N  NZ    . LYS   C 2 152 ? -26.34828 24.02787  27.37663  1.000 53.15476  ?  151 LYS   C NZ    1 
ATOM   3869 N  N     . THR   C 2 153 ? -28.90511 21.80325  21.13775  1.000 27.47111  ?  152 THR   C N     1 
ATOM   3870 C  CA    . THR   C 2 153 ? -29.34816 21.41043  19.81117  1.000 33.39638  ?  152 THR   C CA    1 
ATOM   3871 C  C     . THR   C 2 153 ? -28.64504 22.22713  18.72846  1.000 35.78919  ?  152 THR   C C     1 
ATOM   3872 O  O     . THR   C 2 153 ? -28.35561 23.41733  18.89452  1.000 34.19106  ?  152 THR   C O     1 
ATOM   3873 C  CB    . THR   C 2 153 ? -30.86613 21.56021  19.63691  1.000 31.73840  ?  152 THR   C CB    1 
ATOM   3874 O  OG1   . THR   C 2 153 ? -31.25148 22.92843  19.80336  1.000 29.36618  ?  152 THR   C OG1   1 
ATOM   3875 C  CG2   . THR   C 2 153 ? -31.61151 20.67141  20.61760  1.000 29.14775  ?  152 THR   C CG2   1 
ATOM   3876 N  N     . SER   C 2 154 ? -28.39755 21.56828  17.60389  1.000 31.58025  ?  153 SER   C N     1 
ATOM   3877 C  CA    . SER   C 2 154 ? -27.70765 22.17532  16.47274  1.000 36.25157  ?  153 SER   C CA    1 
ATOM   3878 C  C     . SER   C 2 154 ? -28.62905 22.98727  15.57201  1.000 37.98823  ?  153 SER   C C     1 
ATOM   3879 O  O     . SER   C 2 154 ? -28.15494 23.89985  14.88809  1.000 41.62098  ?  153 SER   C O     1 
ATOM   3880 C  CB    . SER   C 2 154 ? -27.02079 21.08427  15.64931  1.000 27.53573  ?  153 SER   C CB    1 
ATOM   3881 O  OG    . SER   C 2 154 ? -27.99825 20.18344  15.15488  1.000 34.47478  ?  153 SER   C OG    1 
ATOM   3882 N  N     . LYS   C 2 155 ? -29.91872 22.66378  15.52909  1.000 36.48875  ?  154 LYS   C N     1 
ATOM   3883 C  CA    . LYS   C 2 155 ? -30.92499 23.48555  14.87255  1.000 34.11283  ?  154 LYS   C CA    1 
ATOM   3884 C  C     . LYS   C 2 155 ? -32.09725 23.64936  15.82664  1.000 39.42468  ?  154 LYS   C C     1 
ATOM   3885 O  O     . LYS   C 2 155 ? -32.21082 22.91934  16.81271  1.000 31.94744  ?  154 LYS   C O     1 
ATOM   3886 C  CB    . LYS   C 2 155 ? -31.41037 22.86802  13.54869  1.000 41.43025  ?  154 LYS   C CB    1 
ATOM   3887 C  CG    . LYS   C 2 155 ? -30.32290 22.67248  12.51430  1.000 33.15504  ?  154 LYS   C CG    1 
ATOM   3888 C  CD    . LYS   C 2 155 ? -30.87372 22.31919  11.14256  1.000 41.16760  ?  154 LYS   C CD    1 
ATOM   3889 C  CE    . LYS   C 2 155 ? -29.73642 22.20645  10.10236  1.000 36.51031  ?  154 LYS   C CE    1 
ATOM   3890 N  NZ    . LYS   C 2 155 ? -30.28989 22.15967  8.72888   1.000 49.63877  ?  154 LYS   C NZ    1 
ATOM   3891 N  N     . LYS   C 2 156 ? -32.97980 24.60250  15.52056  1.000 36.09674  ?  155 LYS   C N     1 
ATOM   3892 C  CA    . LYS   C 2 156 ? -34.07764 24.94001  16.42242  1.000 43.09367  ?  155 LYS   C CA    1 
ATOM   3893 C  C     . LYS   C 2 156 ? -35.26167 24.01791  16.16296  1.000 39.26369  ?  155 LYS   C C     1 
ATOM   3894 O  O     . LYS   C 2 156 ? -35.95786 24.13978  15.14699  1.000 37.86587  ?  155 LYS   C O     1 
ATOM   3895 C  CB    . LYS   C 2 156 ? -34.48970 26.40129  16.28316  1.000 37.80708  ?  155 LYS   C CB    1 
ATOM   3896 C  CG    . LYS   C 2 156 ? -35.12240 26.91638  17.57245  1.000 51.41647  ?  155 LYS   C CG    1 
ATOM   3897 C  CD    . LYS   C 2 156 ? -35.39399 28.41593  17.55747  1.000 52.68668  ?  155 LYS   C CD    1 
ATOM   3898 C  CE    . LYS   C 2 156 ? -36.78496 28.72235  17.03941  1.000 44.93213  ?  155 LYS   C CE    1 
ATOM   3899 N  NZ    . LYS   C 2 156 ? -37.22730 30.07499  17.44109  1.000 44.01911  ?  155 LYS   C NZ    1 
ATOM   3900 N  N     . ILE   C 2 157 ? -35.50902 23.12493  17.11136  1.000 32.29234  ?  156 ILE   C N     1 
ATOM   3901 C  CA    . ILE   C 2 157 ? -36.54064 22.10189  17.02152  1.000 27.91177  ?  156 ILE   C CA    1 
ATOM   3902 C  C     . ILE   C 2 157 ? -37.73951 22.61569  17.80174  1.000 31.21013  ?  156 ILE   C C     1 
ATOM   3903 O  O     . ILE   C 2 157 ? -37.67150 22.73307  19.02472  1.000 35.14868  ?  156 ILE   C O     1 
ATOM   3904 C  CB    . ILE   C 2 157 ? -36.03612 20.76953  17.59210  1.000 33.15674  ?  156 ILE   C CB    1 
ATOM   3905 C  CG1   . ILE   C 2 157 ? -34.64435 20.44644  17.03031  1.000 30.08486  ?  156 ILE   C CG1   1 
ATOM   3906 C  CG2   . ILE   C 2 157 ? -37.03995 19.64472  17.34628  1.000 27.70588  ?  156 ILE   C CG2   1 
ATOM   3907 C  CD1   . ILE   C 2 157 ? -34.59405 20.40651  15.48522  1.000 37.67700  ?  156 ILE   C CD1   1 
ATOM   3908 N  N     . THR   C 2 158 ? -38.84210 22.90189  17.11741  1.000 29.43758  ?  157 THR   C N     1 
ATOM   3909 C  CA    . THR   C 2 158 ? -39.98578 23.56189  17.72609  1.000 37.24936  ?  157 THR   C CA    1 
ATOM   3910 C  C     . THR   C 2 158 ? -41.25728 22.73413  17.57262  1.000 35.37805  ?  157 THR   C C     1 
ATOM   3911 O  O     . THR   C 2 158 ? -41.37429 21.87476  16.69185  1.000 34.94294  ?  157 THR   C O     1 
ATOM   3912 C  CB    . THR   C 2 158 ? -40.22356 24.94955  17.10571  1.000 36.85463  ?  157 THR   C CB    1 
ATOM   3913 O  OG1   . THR   C 2 158 ? -40.47391 24.79769  15.70328  1.000 39.06565  ?  157 THR   C OG1   1 
ATOM   3914 C  CG2   . THR   C 2 158 ? -39.01475 25.83951  17.30048  1.000 38.85048  ?  157 THR   C CG2   1 
ATOM   3915 N  N     . ILE   C 2 159 ? -42.21980 23.01299  18.44933  1.000 33.35274  ?  158 ILE   C N     1 
ATOM   3916 C  CA    . ILE   C 2 159 ? -43.57499 22.49095  18.31162  1.000 31.05727  ?  158 ILE   C CA    1 
ATOM   3917 C  C     . ILE   C 2 159 ? -44.34501 23.53080  17.50537  1.000 35.00627  ?  158 ILE   C C     1 
ATOM   3918 O  O     . ILE   C 2 159 ? -44.84023 24.52100  18.04953  1.000 35.18564  ?  158 ILE   C O     1 
ATOM   3919 C  CB    . ILE   C 2 159 ? -44.22398 22.21723  19.66850  1.000 28.01213  ?  158 ILE   C CB    1 
ATOM   3920 C  CG1   . ILE   C 2 159 ? -43.49609 21.07487  20.38267  1.000 24.57334  ?  158 ILE   C CG1   1 
ATOM   3921 C  CG2   . ILE   C 2 159 ? -45.71408 21.89660  19.48860  1.000 34.00147  ?  158 ILE   C CG2   1 
ATOM   3922 C  CD1   . ILE   C 2 159 ? -43.93105 20.86766  21.85997  1.000 25.41817  ?  158 ILE   C CD1   1 
ATOM   3923 N  N     . ALA   C 2 160 ? -44.41558 23.31769  16.19257  1.000 35.07558  ?  159 ALA   C N     1 
ATOM   3924 C  CA    . ALA   C 2 160 ? -45.05238 24.29788  15.32046  1.000 44.24526  ?  159 ALA   C CA    1 
ATOM   3925 C  C     . ALA   C 2 160 ? -46.55344 24.31908  15.53972  1.000 42.97867  ?  159 ALA   C C     1 
ATOM   3926 O  O     . ALA   C 2 160 ? -47.16797 25.39083  15.57472  1.000 46.03170  ?  159 ALA   C O     1 
ATOM   3927 C  CB    . ALA   C 2 160 ? -44.72962 23.99654  13.86136  1.000 33.20089  ?  159 ALA   C CB    1 
ATOM   3928 N  N     . ASP   C 2 161 ? -47.15672 23.14665  15.69786  1.000 44.30079  ?  160 ASP   C N     1 
ATOM   3929 C  CA    . ASP   C 2 161 ? -48.58044 23.04926  15.96452  1.000 41.28547  ?  160 ASP   C CA    1 
ATOM   3930 C  C     . ASP   C 2 161 ? -48.80629 21.86029  16.88865  1.000 42.82812  ?  160 ASP   C C     1 
ATOM   3931 O  O     . ASP   C 2 161 ? -48.02360 20.90498  16.89159  1.000 39.41374  ?  160 ASP   C O     1 
ATOM   3932 C  CB    . ASP   C 2 161 ? -49.38182 22.89645  14.66520  1.000 40.46219  ?  160 ASP   C CB    1 
ATOM   3933 C  CG    . ASP   C 2 161 ? -50.88507 23.16432  14.84729  1.000 41.06487  ?  160 ASP   C CG    1 
ATOM   3934 O  OD1   . ASP   C 2 161 ? -51.29399 23.69588  15.90567  1.000 37.99131  ?  160 ASP   C OD1   1 
ATOM   3935 O  OD2   . ASP   C 2 161 ? -51.65111 22.84426  13.91251  1.000 42.71191  -1 160 ASP   C OD2   1 
ATOM   3936 N  N     . CYS   C 2 162 ? -49.87087 21.93325  17.68543  1.000 34.65560  ?  161 CYS   C N     1 
ATOM   3937 C  CA    . CYS   C 2 162 ? -50.24516 20.80607  18.52289  1.000 38.36132  ?  161 CYS   C CA    1 
ATOM   3938 C  C     . CYS   C 2 162 ? -51.73780 20.86595  18.82245  1.000 34.86671  ?  161 CYS   C C     1 
ATOM   3939 O  O     . CYS   C 2 162 ? -52.37431 21.91643  18.71583  1.000 41.34262  ?  161 CYS   C O     1 
ATOM   3940 C  CB    . CYS   C 2 162 ? -49.42805 20.77415  19.82144  1.000 34.08985  ?  161 CYS   C CB    1 
ATOM   3941 S  SG    . CYS   C 2 162 ? -49.36062 22.35370  20.69443  1.000 37.84632  ?  161 CYS   C SG    1 
ATOM   3942 N  N     . GLY   C 2 163 ? -52.28582 19.71261  19.17754  1.000 36.11093  ?  162 GLY   C N     1 
ATOM   3943 C  CA    . GLY   C 2 163 ? -53.65935 19.63826  19.63105  1.000 35.57644  ?  162 GLY   C CA    1 
ATOM   3944 C  C     . GLY   C 2 163 ? -54.03072 18.20932  19.96584  1.000 40.77101  ?  162 GLY   C C     1 
ATOM   3945 O  O     . GLY   C 2 163 ? -53.16009 17.35762  20.17431  1.000 39.01722  ?  162 GLY   C O     1 
ATOM   3946 N  N     . GLN   C 2 164 ? -55.33967 17.95100  19.98858  1.000 38.71550  ?  163 GLN   C N     1 
ATOM   3947 C  CA    . GLN   C 2 164 ? -55.91362 16.66715  20.37534  1.000 37.43316  ?  163 GLN   C CA    1 
ATOM   3948 C  C     . GLN   C 2 164 ? -56.56479 16.00930  19.16988  1.000 36.39208  ?  163 GLN   C C     1 
ATOM   3949 O  O     . GLN   C 2 164 ? -57.28564 16.66601  18.41858  1.000 40.64906  ?  163 GLN   C O     1 
ATOM   3950 C  CB    . GLN   C 2 164 ? -56.94496 16.85559  21.49782  1.000 45.12807  ?  163 GLN   C CB    1 
ATOM   3951 C  CG    . GLN   C 2 164 ? -57.72247 15.60349  21.90256  1.000 38.16709  ?  163 GLN   C CG    1 
ATOM   3952 C  CD    . GLN   C 2 164 ? -58.31976 15.71792  23.31210  1.000 39.55878  ?  163 GLN   C CD    1 
ATOM   3953 O  OE1   . GLN   C 2 164 ? -58.46829 16.81678  23.85701  1.000 40.03068  ?  163 GLN   C OE1   1 
ATOM   3954 N  NE2   . GLN   C 2 164 ? -58.65041 14.57908  23.90486  1.000 43.81296  ?  163 GLN   C NE2   1 
ATOM   3955 N  N     . LEU   C 2 165 ? -56.30837 14.71712  18.99228  1.000 37.58941  ?  164 LEU   C N     1 
ATOM   3956 C  CA    . LEU   C 2 165 ? -56.89452 13.89456  17.94184  1.000 42.71675  ?  164 LEU   C CA    1 
ATOM   3957 C  C     . LEU   C 2 165 ? -58.03765 13.01713  18.44007  1.000 47.04490  ?  164 LEU   C C     1 
ATOM   3958 O  O     . LEU   C 2 165 ? -59.02983 12.82776  17.73083  1.000 52.26057  ?  164 LEU   C O     1 
ATOM   3959 C  CB    . LEU   C 2 165 ? -55.81816 12.99472  17.32039  1.000 42.50206  ?  164 LEU   C CB    1 
ATOM   3960 C  CG    . LEU   C 2 165 ? -54.55278 13.65717  16.77954  1.000 44.21542  ?  164 LEU   C CG    1 
ATOM   3961 C  CD1   . LEU   C 2 165 ? -53.55356 12.59697  16.30190  1.000 44.14041  ?  164 LEU   C CD1   1 
ATOM   3962 C  CD2   . LEU   C 2 165 ? -54.90426 14.62176  15.65409  1.000 35.23347  ?  164 LEU   C CD2   1 
ATOM   3963 N  N     . GLU   C 2 166 ? -57.90545 12.45162  19.63245  1.000 46.60161  ?  165 GLU   C N     1 
ATOM   3964 C  CA    . GLU   C 2 166 ? -58.90312 11.54421  20.19030  1.000 54.91844  ?  165 GLU   C CA    1 
ATOM   3965 C  C     . GLU   C 2 166 ? -59.06559 11.78255  21.69793  1.000 53.23514  ?  165 GLU   C C     1 
ATOM   3966 O  O     . GLU   C 2 166 ? -58.33183 12.58117  22.30958  1.000 43.52481  ?  165 GLU   C O     1 
ATOM   3967 C  CB    . GLU   C 2 166 ? -58.51546 10.08212  19.93209  1.000 53.85812  ?  165 GLU   C CB    1 
ATOM   3968 C  CG    . GLU   C 2 166 ? -58.24651 9.73751   18.47311  1.000 53.37131  ?  165 GLU   C CG    1 
ATOM   3969 C  CD    . GLU   C 2 166 ? -57.53819 8.39624   18.29571  1.000 57.14326  ?  165 GLU   C CD    1 
ATOM   3970 O  OE1   . GLU   C 2 166 ? -58.13552 7.35397   18.62239  1.000 52.42924  ?  165 GLU   C OE1   1 
ATOM   3971 O  OE2   . GLU   C 2 166 ? -56.37299 8.38656   17.82994  1.000 66.44458  ?  165 GLU   C OE2   1 
ATOM   3972 O  OXT   . GLU   C 2 166 ? -59.94014 11.17671  22.34375  1.000 53.79203  ?  165 GLU   C OXT   1 
ATOM   3973 N  N     . VAL   D 2 3   ? 1.69453   56.37115  2.37390   1.000 47.41760  ?  2   VAL   D N     1 
ATOM   3974 C  CA    . VAL   D 2 3   ? 1.12625   56.23127  3.71633   1.000 52.76376  ?  2   VAL   D CA    1 
ATOM   3975 C  C     . VAL   D 2 3   ? 0.13392   55.06111  3.74228   1.000 47.00901  ?  2   VAL   D C     1 
ATOM   3976 O  O     . VAL   D 2 3   ? -0.71842  54.92213  2.85411   1.000 46.70626  ?  2   VAL   D O     1 
ATOM   3977 C  CB    . VAL   D 2 3   ? 0.45469   57.54779  4.19671   1.000 47.93966  ?  2   VAL   D CB    1 
ATOM   3978 C  CG1   . VAL   D 2 3   ? -0.61525  58.00181  3.21593   1.000 53.81379  ?  2   VAL   D CG1   1 
ATOM   3979 C  CG2   . VAL   D 2 3   ? -0.13493  57.38378  5.60209   1.000 45.58669  ?  2   VAL   D CG2   1 
ATOM   3980 N  N     . ASN   D 2 4   ? 0.25602   54.22737  4.77425   1.000 42.09261  ?  3   ASN   D N     1 
ATOM   3981 C  CA    . ASN   D 2 4   ? -0.52187  53.00248  4.83851   1.000 35.11808  ?  3   ASN   D CA    1 
ATOM   3982 C  C     . ASN   D 2 4   ? -2.00065  53.32814  5.00209   1.000 34.93126  ?  3   ASN   D C     1 
ATOM   3983 O  O     . ASN   D 2 4   ? -2.35891  54.18473  5.81156   1.000 38.15332  ?  3   ASN   D O     1 
ATOM   3984 C  CB    . ASN   D 2 4   ? -0.03415  52.13366  5.99120   1.000 29.77547  ?  3   ASN   D CB    1 
ATOM   3985 C  CG    . ASN   D 2 4   ? 1.28522   51.46286  5.67773   1.000 31.80729  ?  3   ASN   D CG    1 
ATOM   3986 O  OD1   . ASN   D 2 4   ? 1.60073   51.21345  4.50848   1.000 33.60164  ?  3   ASN   D OD1   1 
ATOM   3987 N  ND2   . ASN   D 2 4   ? 2.06557   51.17825  6.70349   1.000 27.23012  ?  3   ASN   D ND2   1 
ATOM   3988 N  N     . PRO   D 2 5   ? -2.88046  52.68552  4.23910   1.000 31.24176  ?  4   PRO   D N     1 
ATOM   3989 C  CA    . PRO   D 2 5   ? -4.31532  52.91821  4.43320   1.000 32.74644  ?  4   PRO   D CA    1 
ATOM   3990 C  C     . PRO   D 2 5   ? -4.76608  52.46364  5.81408   1.000 35.17084  ?  4   PRO   D C     1 
ATOM   3991 O  O     . PRO   D 2 5   ? -4.10058  51.67709  6.49165   1.000 31.91870  ?  4   PRO   D O     1 
ATOM   3992 C  CB    . PRO   D 2 5   ? -4.98095  52.08334  3.33218   1.000 36.93548  ?  4   PRO   D CB    1 
ATOM   3993 C  CG    . PRO   D 2 5   ? -3.94467  51.09616  2.87670   1.000 31.46097  ?  4   PRO   D CG    1 
ATOM   3994 C  CD    . PRO   D 2 5   ? -2.59597  51.71429  3.16592   1.000 35.25406  ?  4   PRO   D CD    1 
ATOM   3995 N  N     . THR   D 2 6   ? -5.92151  52.98152  6.21695   1.000 34.06388  ?  5   THR   D N     1 
ATOM   3996 C  CA    . THR   D 2 6   ? -6.61878  52.56906  7.42457   1.000 32.40453  ?  5   THR   D CA    1 
ATOM   3997 C  C     . THR   D 2 6   ? -8.06262  52.22502  7.08360   1.000 34.22353  ?  5   THR   D C     1 
ATOM   3998 O  O     . THR   D 2 6   ? -8.72917  52.98131  6.36622   1.000 37.64946  ?  5   THR   D O     1 
ATOM   3999 C  CB    . THR   D 2 6   ? -6.58634  53.67678  8.48150   1.000 32.22513  ?  5   THR   D CB    1 
ATOM   4000 O  OG1   . THR   D 2 6   ? -5.26752  53.77794  9.02795   1.000 42.37114  ?  5   THR   D OG1   1 
ATOM   4001 C  CG2   . THR   D 2 6   ? -7.53986  53.35424  9.58298   1.000 35.87380  ?  5   THR   D CG2   1 
ATOM   4002 N  N     . VAL   D 2 7   ? -8.54541  51.08774  7.59995   1.000 28.00793  ?  6   VAL   D N     1 
ATOM   4003 C  CA    . VAL   D 2 7   ? -9.92425  50.66021  7.43750   1.000 25.90145  ?  6   VAL   D CA    1 
ATOM   4004 C  C     . VAL   D 2 7   ? -10.49017 50.36244  8.82652   1.000 25.70656  ?  6   VAL   D C     1 
ATOM   4005 O  O     . VAL   D 2 7   ? -9.74986  50.17789  9.78841   1.000 28.11335  ?  6   VAL   D O     1 
ATOM   4006 C  CB    . VAL   D 2 7   ? -10.03544 49.42790  6.53029   1.000 27.89376  ?  6   VAL   D CB    1 
ATOM   4007 C  CG1   . VAL   D 2 7   ? -9.67384  49.78722  5.07064   1.000 32.41887  ?  6   VAL   D CG1   1 
ATOM   4008 C  CG2   . VAL   D 2 7   ? -9.11420  48.33851  7.04813   1.000 29.43535  ?  6   VAL   D CG2   1 
ATOM   4009 N  N     . PHE   D 2 8   ? -11.81108 50.29632  8.90751   1.000 24.64249  ?  7   PHE   D N     1 
ATOM   4010 C  CA    . PHE   D 2 8   ? -12.53896 50.04148  10.14403  1.000 28.16940  ?  7   PHE   D CA    1 
ATOM   4011 C  C     . PHE   D 2 8   ? -13.59209 48.96914  9.92932   1.000 28.90359  ?  7   PHE   D C     1 
ATOM   4012 O  O     . PHE   D 2 8   ? -14.12638 48.81173  8.83012   1.000 29.99051  ?  7   PHE   D O     1 
ATOM   4013 C  CB    . PHE   D 2 8   ? -13.24228 51.31654  10.69401  1.000 32.12361  ?  7   PHE   D CB    1 
ATOM   4014 C  CG    . PHE   D 2 8   ? -14.40745 51.77600  9.85918   1.000 33.26817  ?  7   PHE   D CG    1 
ATOM   4015 C  CD1   . PHE   D 2 8   ? -14.20696 52.60286  8.77004   1.000 31.63970  ?  7   PHE   D CD1   1 
ATOM   4016 C  CD2   . PHE   D 2 8   ? -15.70270 51.37260  10.15786  1.000 33.71595  ?  7   PHE   D CD2   1 
ATOM   4017 C  CE1   . PHE   D 2 8   ? -15.27765 53.01915  7.98721   1.000 32.50579  ?  7   PHE   D CE1   1 
ATOM   4018 C  CE2   . PHE   D 2 8   ? -16.76774 51.79303  9.38344   1.000 33.48562  ?  7   PHE   D CE2   1 
ATOM   4019 C  CZ    . PHE   D 2 8   ? -16.55001 52.61541  8.29326   1.000 30.34211  ?  7   PHE   D CZ    1 
ATOM   4020 N  N     . PHE   D 2 9   ? -13.89239 48.24453  11.00846  1.000 30.66375  ?  8   PHE   D N     1 
ATOM   4021 C  CA    . PHE   D 2 9   ? -15.02892 47.33780  11.09512  1.000 28.29179  ?  8   PHE   D CA    1 
ATOM   4022 C  C     . PHE   D 2 9   ? -15.91421 47.83852  12.23316  1.000 28.13851  ?  8   PHE   D C     1 
ATOM   4023 O  O     . PHE   D 2 9   ? -15.41816 48.08829  13.33564  1.000 30.17533  ?  8   PHE   D O     1 
ATOM   4024 C  CB    . PHE   D 2 9   ? -14.60568 45.88722  11.40795  1.000 28.94849  ?  8   PHE   D CB    1 
ATOM   4025 C  CG    . PHE   D 2 9   ? -13.93325 45.12536  10.27266  1.000 30.55996  ?  8   PHE   D CG    1 
ATOM   4026 C  CD1   . PHE   D 2 9   ? -13.88605 45.61061  8.96564   1.000 32.37693  ?  8   PHE   D CD1   1 
ATOM   4027 C  CD2   . PHE   D 2 9   ? -13.40075 43.85914  10.53168  1.000 27.84794  ?  8   PHE   D CD2   1 
ATOM   4028 C  CE1   . PHE   D 2 9   ? -13.27449 44.85514  7.94694   1.000 31.20032  ?  8   PHE   D CE1   1 
ATOM   4029 C  CE2   . PHE   D 2 9   ? -12.79840 43.10486  9.54188   1.000 29.21194  ?  8   PHE   D CE2   1 
ATOM   4030 C  CZ    . PHE   D 2 9   ? -12.73647 43.60507  8.23281   1.000 26.65543  ?  8   PHE   D CZ    1 
ATOM   4031 N  N     . ASP   D 2 10  ? -17.21525 47.97230  11.98607  1.000 31.16548  ?  9   ASP   D N     1 
ATOM   4032 C  CA    . ASP   D 2 10  ? -18.18103 48.15975  13.06969  1.000 36.94798  ?  9   ASP   D CA    1 
ATOM   4033 C  C     . ASP   D 2 10  ? -18.74274 46.79359  13.45428  1.000 31.24164  ?  9   ASP   D C     1 
ATOM   4034 O  O     . ASP   D 2 10  ? -19.49707 46.18891  12.68981  1.000 28.01468  ?  9   ASP   D O     1 
ATOM   4035 C  CB    . ASP   D 2 10  ? -19.29090 49.12494  12.65704  1.000 35.40512  ?  9   ASP   D CB    1 
ATOM   4036 C  CG    . ASP   D 2 10  ? -18.80929 50.56096  12.57564  1.000 35.96276  ?  9   ASP   D CG    1 
ATOM   4037 O  OD1   . ASP   D 2 10  ? -18.10405 51.01950  13.50908  1.000 37.10396  ?  9   ASP   D OD1   1 
ATOM   4038 O  OD2   . ASP   D 2 10  ? -19.10170 51.22075  11.55798  1.000 36.84914  -1 9   ASP   D OD2   1 
ATOM   4039 N  N     . ILE   D 2 11  ? -18.37388 46.30217  14.63464  1.000 29.05530  ?  10  ILE   D N     1 
ATOM   4040 C  CA    . ILE   D 2 11  ? -18.73997 44.95180  15.04145  1.000 25.26016  ?  10  ILE   D CA    1 
ATOM   4041 C  C     . ILE   D 2 11  ? -20.08596 44.98196  15.76845  1.000 31.25676  ?  10  ILE   D C     1 
ATOM   4042 O  O     . ILE   D 2 11  ? -20.37065 45.88854  16.56752  1.000 27.86902  ?  10  ILE   D O     1 
ATOM   4043 C  CB    . ILE   D 2 11  ? -17.63183 44.33768  15.91411  1.000 25.24898  ?  10  ILE   D CB    1 
ATOM   4044 C  CG1   . ILE   D 2 11  ? -16.29204 44.29351  15.15300  1.000 27.18029  ?  10  ILE   D CG1   1 
ATOM   4045 C  CG2   . ILE   D 2 11  ? -18.04630 42.96278  16.43163  1.000 28.09970  ?  10  ILE   D CG2   1 
ATOM   4046 C  CD1   . ILE   D 2 11  ? -16.32959 43.44804  13.87711  1.000 28.01711  ?  10  ILE   D CD1   1 
ATOM   4047 N  N     . ALA   D 2 12  ? -20.92613 43.98717  15.48458  1.000 28.68821  ?  11  ALA   D N     1 
ATOM   4048 C  CA    . ALA   D 2 12  ? -22.20577 43.81651  16.15382  1.000 28.95596  ?  11  ALA   D CA    1 
ATOM   4049 C  C     . ALA   D 2 12  ? -22.30041 42.39548  16.67979  1.000 32.61128  ?  11  ALA   D C     1 
ATOM   4050 O  O     . ALA   D 2 12  ? -21.59380 41.50212  16.20984  1.000 27.47790  ?  11  ALA   D O     1 
ATOM   4051 C  CB    . ALA   D 2 12  ? -23.37219 44.10518  15.22381  1.000 36.59261  ?  11  ALA   D CB    1 
ATOM   4052 N  N     . VAL   D 2 13  ? -23.16861 42.19950  17.67739  1.000 33.24082  ?  12  VAL   D N     1 
ATOM   4053 C  CA    . VAL   D 2 13  ? -23.36656 40.91648  18.34761  1.000 29.96677  ?  12  VAL   D CA    1 
ATOM   4054 C  C     . VAL   D 2 13  ? -24.86084 40.64849  18.42032  1.000 33.63797  ?  12  VAL   D C     1 
ATOM   4055 O  O     . VAL   D 2 13  ? -25.59422 41.41830  19.04991  1.000 32.90849  ?  12  VAL   D O     1 
ATOM   4056 C  CB    . VAL   D 2 13  ? -22.76829 40.90914  19.76078  1.000 30.16182  ?  12  VAL   D CB    1 
ATOM   4057 C  CG1   . VAL   D 2 13  ? -23.04112 39.57437  20.42392  1.000 24.54704  ?  12  VAL   D CG1   1 
ATOM   4058 C  CG2   . VAL   D 2 13  ? -21.27849 41.21133  19.71078  1.000 30.88213  ?  12  VAL   D CG2   1 
ATOM   4059 N  N     . ASP   D 2 14  ? -25.30748 39.55534  17.79920  1.000 35.55770  ?  13  ASP   D N     1 
ATOM   4060 C  CA    . ASP   D 2 14  ? -26.72165 39.36584  17.47297  1.000 37.15504  ?  13  ASP   D CA    1 
ATOM   4061 C  C     . ASP   D 2 14  ? -27.36160 40.68683  17.04747  1.000 35.76263  ?  13  ASP   D C     1 
ATOM   4062 O  O     . ASP   D 2 14  ? -28.41541 41.07043  17.56330  1.000 42.38384  ?  13  ASP   D O     1 
ATOM   4063 C  CB    . ASP   D 2 14  ? -27.49043 38.75738  18.65071  1.000 38.59212  ?  13  ASP   D CB    1 
ATOM   4064 C  CG    . ASP   D 2 14  ? -27.11188 37.29893  18.91708  1.000 41.45334  ?  13  ASP   D CG    1 
ATOM   4065 O  OD1   . ASP   D 2 14  ? -26.84922 36.54078  17.94684  1.000 34.69065  ?  13  ASP   D OD1   1 
ATOM   4066 O  OD2   . ASP   D 2 14  ? -27.07647 36.90789  20.10683  1.000 39.07567  -1 13  ASP   D OD2   1 
ATOM   4067 N  N     . GLY   D 2 15  ? -26.72077 41.40716  16.12888  1.000 38.93295  ?  14  GLY   D N     1 
ATOM   4068 C  CA    . GLY   D 2 15  ? -27.26691 42.63545  15.59125  1.000 35.07564  ?  14  GLY   D CA    1 
ATOM   4069 C  C     . GLY   D 2 15  ? -27.11586 43.86345  16.46961  1.000 42.85027  ?  14  GLY   D C     1 
ATOM   4070 O  O     . GLY   D 2 15  ? -27.32832 44.97880  15.97789  1.000 48.97439  ?  14  GLY   D O     1 
ATOM   4071 N  N     . GLU   D 2 16  ? -26.76074 43.70723  17.74524  1.000 35.11523  ?  15  GLU   D N     1 
ATOM   4072 C  CA    . GLU   D 2 16  ? -26.56130 44.88337  18.58975  1.000 38.41360  ?  15  GLU   D CA    1 
ATOM   4073 C  C     . GLU   D 2 16  ? -25.11277 45.36215  18.49667  1.000 40.45048  ?  15  GLU   D C     1 
ATOM   4074 O  O     . GLU   D 2 16  ? -24.18758 44.55090  18.63910  1.000 35.33667  ?  15  GLU   D O     1 
ATOM   4075 C  CB    . GLU   D 2 16  ? -26.90752 44.58359  20.05006  1.000 42.16888  ?  15  GLU   D CB    1 
ATOM   4076 C  CG    . GLU   D 2 16  ? -28.38243 44.19608  20.31368  1.000 51.02920  ?  15  GLU   D CG    1 
ATOM   4077 C  CD    . GLU   D 2 16  ? -29.40119 45.23816  19.79543  1.000 57.39063  ?  15  GLU   D CD    1 
ATOM   4078 O  OE1   . GLU   D 2 16  ? -29.16556 46.46271  19.95201  1.000 51.56464  ?  15  GLU   D OE1   1 
ATOM   4079 O  OE2   . GLU   D 2 16  ? -30.43766 44.82251  19.21499  1.000 59.01943  -1 15  GLU   D OE2   1 
ATOM   4080 N  N     . PRO   D 2 17  ? -24.89092 46.65614  18.26818  1.000 36.83145  ?  16  PRO   D N     1 
ATOM   4081 C  CA    . PRO   D 2 17  ? -23.52431 47.17951  18.17435  1.000 35.40615  ?  16  PRO   D CA    1 
ATOM   4082 C  C     . PRO   D 2 17  ? -22.67579 46.86861  19.39798  1.000 41.09750  ?  16  PRO   D C     1 
ATOM   4083 O  O     . PRO   D 2 17  ? -23.14491 46.89835  20.54069  1.000 35.99279  ?  16  PRO   D O     1 
ATOM   4084 C  CB    . PRO   D 2 17  ? -23.73666 48.68794  18.02425  1.000 37.14745  ?  16  PRO   D CB    1 
ATOM   4085 C  CG    . PRO   D 2 17  ? -25.05811 48.81004  17.32971  1.000 44.58443  ?  16  PRO   D CG    1 
ATOM   4086 C  CD    . PRO   D 2 17  ? -25.89471 47.62618  17.78674  1.000 44.08208  ?  16  PRO   D CD    1 
ATOM   4087 N  N     . LEU   D 2 18  ? -21.40151 46.58409  19.13109  1.000 29.85028  ?  17  LEU   D N     1 
ATOM   4088 C  CA    . LEU   D 2 18  ? -20.36836 46.42468  20.14076  1.000 30.24112  ?  17  LEU   D CA    1 
ATOM   4089 C  C     . LEU   D 2 18  ? -19.34406 47.54704  20.09475  1.000 32.24327  ?  17  LEU   D C     1 
ATOM   4090 O  O     . LEU   D 2 18  ? -18.99385 48.09421  21.14425  1.000 33.05023  ?  17  LEU   D O     1 
ATOM   4091 C  CB    . LEU   D 2 18  ? -19.67917 45.06235  19.96982  1.000 24.46843  ?  17  LEU   D CB    1 
ATOM   4092 C  CG    . LEU   D 2 18  ? -18.62245 44.65582  20.98600  1.000 31.20196  ?  17  LEU   D CG    1 
ATOM   4093 C  CD1   . LEU   D 2 18  ? -19.23064 44.46911  22.39902  1.000 29.97995  ?  17  LEU   D CD1   1 
ATOM   4094 C  CD2   . LEU   D 2 18  ? -17.92255 43.38935  20.50922  1.000 29.09934  ?  17  LEU   D CD2   1 
ATOM   4095 N  N     . GLY   D 2 19  ? -18.86547 47.91468  18.91228  1.000 28.74524  ?  18  GLY   D N     1 
ATOM   4096 C  CA    . GLY   D 2 19  ? -17.85863 48.95041  18.79691  1.000 27.30060  ?  18  GLY   D CA    1 
ATOM   4097 C  C     . GLY   D 2 19  ? -17.03842 48.77908  17.53270  1.000 32.89452  ?  18  GLY   D C     1 
ATOM   4098 O  O     . GLY   D 2 19  ? -17.19891 47.82347  16.76833  1.000 30.58760  ?  18  GLY   D O     1 
ATOM   4099 N  N     . ARG   D 2 20  ? -16.13700 49.72536  17.33217  1.000 32.17453  ?  19  ARG   D N     1 
ATOM   4100 C  CA    . ARG   D 2 20  ? -15.39061 49.82480  16.08925  1.000 31.93131  ?  19  ARG   D CA    1 
ATOM   4101 C  C     . ARG   D 2 20  ? -13.95556 49.34327  16.28863  1.000 28.25144  ?  19  ARG   D C     1 
ATOM   4102 O  O     . ARG   D 2 20  ? -13.29600 49.72399  17.25608  1.000 30.07912  ?  19  ARG   D O     1 
ATOM   4103 C  CB    . ARG   D 2 20  ? -15.41384 51.26298  15.58169  1.000 31.57188  ?  19  ARG   D CB    1 
ATOM   4104 C  CG    . ARG   D 2 20  ? -14.48188 51.53762  14.40305  1.000 34.95175  ?  19  ARG   D CG    1 
ATOM   4105 C  CD    . ARG   D 2 20  ? -14.78128 52.91120  13.78282  1.000 32.21138  ?  19  ARG   D CD    1 
ATOM   4106 N  NE    . ARG   D 2 20  ? -16.07260 52.92988  13.10684  1.000 35.21282  ?  19  ARG   D NE    1 
ATOM   4107 C  CZ    . ARG   D 2 20  ? -16.49479 53.90536  12.30886  1.000 39.48845  ?  19  ARG   D CZ    1 
ATOM   4108 N  NH1   . ARG   D 2 20  ? -15.73819 54.95474  12.03831  1.000 35.60687  ?  19  ARG   D NH1   1 
ATOM   4109 N  NH2   . ARG   D 2 20  ? -17.70397 53.81807  11.75966  1.000 41.85922  ?  19  ARG   D NH2   1 
ATOM   4110 N  N     . VAL   D 2 21  ? -13.48388 48.49606  15.37797  1.000 28.49306  ?  20  VAL   D N     1 
ATOM   4111 C  CA    . VAL   D 2 21  ? -12.07257 48.14137  15.27826  1.000 28.06757  ?  20  VAL   D CA    1 
ATOM   4112 C  C     . VAL   D 2 21  ? -11.54126 48.77345  14.00255  1.000 25.68058  ?  20  VAL   D C     1 
ATOM   4113 O  O     . VAL   D 2 21  ? -12.18823 48.69574  12.95279  1.000 29.05961  ?  20  VAL   D O     1 
ATOM   4114 C  CB    . VAL   D 2 21  ? -11.84074 46.61996  15.25045  1.000 29.21333  ?  20  VAL   D CB    1 
ATOM   4115 C  CG1   . VAL   D 2 21  ? -10.36701 46.33556  15.44593  1.000 26.81391  ?  20  VAL   D CG1   1 
ATOM   4116 C  CG2   . VAL   D 2 21  ? -12.68399 45.91152  16.29125  1.000 30.30148  ?  20  VAL   D CG2   1 
ATOM   4117 N  N     . SER   D 2 22  ? -10.37848 49.39789  14.09544  1.000 26.97893  ?  21  SER   D N     1 
ATOM   4118 C  CA    . SER   D 2 22  ? -9.70337  49.96628  12.94589  1.000 30.34015  ?  21  SER   D CA    1 
ATOM   4119 C  C     . SER   D 2 22  ? -8.36197  49.26579  12.75898  1.000 28.22415  ?  21  SER   D C     1 
ATOM   4120 O  O     . SER   D 2 22  ? -7.80693  48.69429  13.69646  1.000 29.26817  ?  21  SER   D O     1 
ATOM   4121 C  CB    . SER   D 2 22  ? -9.51631  51.47410  13.13010  1.000 29.13809  ?  21  SER   D CB    1 
ATOM   4122 O  OG    . SER   D 2 22  ? -8.51891  51.70063  14.08507  1.000 30.56821  ?  21  SER   D OG    1 
ATOM   4123 N  N     . PHE   D 2 23  ? -7.85511  49.28282  11.52055  1.000 29.48143  ?  22  PHE   D N     1 
ATOM   4124 C  CA    . PHE   D 2 23  ? -6.63960  48.55454  11.17816  1.000 28.28624  ?  22  PHE   D CA    1 
ATOM   4125 C  C     . PHE   D 2 23  ? -5.72713  49.41009  10.31952  1.000 26.87819  ?  22  PHE   D C     1 
ATOM   4126 O  O     . PHE   D 2 23  ? -6.18872  50.06871  9.38668   1.000 29.34997  ?  22  PHE   D O     1 
ATOM   4127 C  CB    . PHE   D 2 23  ? -6.92667  47.27930  10.37055  1.000 28.51846  ?  22  PHE   D CB    1 
ATOM   4128 C  CG    . PHE   D 2 23  ? -7.94673  46.36552  10.98321  1.000 29.13752  ?  22  PHE   D CG    1 
ATOM   4129 C  CD1   . PHE   D 2 23  ? -7.58021  45.44536  11.95817  1.000 25.50522  ?  22  PHE   D CD1   1 
ATOM   4130 C  CD2   . PHE   D 2 23  ? -9.25677  46.38377  10.53997  1.000 26.06996  ?  22  PHE   D CD2   1 
ATOM   4131 C  CE1   . PHE   D 2 23  ? -8.51452  44.58447  12.49902  1.000 24.95466  ?  22  PHE   D CE1   1 
ATOM   4132 C  CE2   . PHE   D 2 23  ? -10.19831 45.52813  11.08711  1.000 28.35483  ?  22  PHE   D CE2   1 
ATOM   4133 C  CZ    . PHE   D 2 23  ? -9.81966  44.62554  12.06705  1.000 27.78098  ?  22  PHE   D CZ    1 
ATOM   4134 N  N     . GLU   D 2 24  ? -4.42888  49.34548  10.59197  1.000 27.35418  ?  23  GLU   D N     1 
ATOM   4135 C  CA    . GLU   D 2 24  ? -3.42753  49.79684  9.63468   1.000 29.62465  ?  23  GLU   D CA    1 
ATOM   4136 C  C     . GLU   D 2 24  ? -3.08573  48.64319  8.70193   1.000 29.38141  ?  23  GLU   D C     1 
ATOM   4137 O  O     . GLU   D 2 24  ? -2.77242  47.54239  9.16542   1.000 30.90936  ?  23  GLU   D O     1 
ATOM   4138 C  CB    . GLU   D 2 24  ? -2.15902  50.30049  10.33921  1.000 28.57779  ?  23  GLU   D CB    1 
ATOM   4139 C  CG    . GLU   D 2 24  ? -1.08465  50.77055  9.33962   1.000 31.59427  ?  23  GLU   D CG    1 
ATOM   4140 C  CD    . GLU   D 2 24  ? 0.23334   51.11830  9.99209   1.000 41.27035  ?  23  GLU   D CD    1 
ATOM   4141 O  OE1   . GLU   D 2 24  ? 0.30003   51.12071  11.24607  1.000 37.77699  ?  23  GLU   D OE1   1 
ATOM   4142 O  OE2   . GLU   D 2 24  ? 1.21085   51.38570  9.24572   1.000 37.29324  -1 23  GLU   D OE2   1 
ATOM   4143 N  N     . LEU   D 2 25  ? -3.14566  48.89518  7.39455   1.000 29.20748  ?  24  LEU   D N     1 
ATOM   4144 C  CA    . LEU   D 2 25  ? -2.80238  47.89998  6.37889   1.000 31.34517  ?  24  LEU   D CA    1 
ATOM   4145 C  C     . LEU   D 2 25  ? -1.42206  48.21851  5.82646   1.000 30.13572  ?  24  LEU   D C     1 
ATOM   4146 O  O     . LEU   D 2 25  ? -1.19995  49.31522  5.30527   1.000 29.16863  ?  24  LEU   D O     1 
ATOM   4147 C  CB    . LEU   D 2 25  ? -3.82292  47.87278  5.24680   1.000 28.30351  ?  24  LEU   D CB    1 
ATOM   4148 C  CG    . LEU   D 2 25  ? -5.29497  47.76972  5.64885   1.000 31.63547  ?  24  LEU   D CG    1 
ATOM   4149 C  CD1   . LEU   D 2 25  ? -6.16625  47.68970  4.39169   1.000 24.36674  ?  24  LEU   D CD1   1 
ATOM   4150 C  CD2   . LEU   D 2 25  ? -5.56126  46.58145  6.59979   1.000 25.73288  ?  24  LEU   D CD2   1 
ATOM   4151 N  N     . PHE   D 2 26  ? -0.50337  47.26164  5.94175   1.000 26.02739  ?  25  PHE   D N     1 
ATOM   4152 C  CA    . PHE   D 2 26  ? 0.90411   47.48130  5.61689   1.000 27.67287  ?  25  PHE   D CA    1 
ATOM   4153 C  C     . PHE   D 2 26  ? 1.11946   47.45892  4.09568   1.000 27.48862  ?  25  PHE   D C     1 
ATOM   4154 O  O     . PHE   D 2 26  ? 1.77730   46.58468  3.52394   1.000 30.68732  ?  25  PHE   D O     1 
ATOM   4155 C  CB    . PHE   D 2 26  ? 1.75128   46.43265  6.32185   1.000 27.64475  ?  25  PHE   D CB    1 
ATOM   4156 C  CG    . PHE   D 2 26  ? 1.63955   46.46778  7.82519   1.000 30.84241  ?  25  PHE   D CG    1 
ATOM   4157 C  CD1   . PHE   D 2 26  ? 1.52055   47.67826  8.49770   1.000 29.43152  ?  25  PHE   D CD1   1 
ATOM   4158 C  CD2   . PHE   D 2 26  ? 1.65724   45.28987  8.56637   1.000 33.32651  ?  25  PHE   D CD2   1 
ATOM   4159 C  CE1   . PHE   D 2 26  ? 1.43179   47.71415  9.87697   1.000 34.00765  ?  25  PHE   D CE1   1 
ATOM   4160 C  CE2   . PHE   D 2 26  ? 1.57453   45.31396  9.95158   1.000 30.71229  ?  25  PHE   D CE2   1 
ATOM   4161 C  CZ    . PHE   D 2 26  ? 1.46364   46.52707  10.60717  1.000 30.96624  ?  25  PHE   D CZ    1 
ATOM   4162 N  N     . ALA   D 2 27  ? 0.57451   48.47154  3.42916   1.000 27.56240  ?  26  ALA   D N     1 
ATOM   4163 C  CA    . ALA   D 2 27  ? 0.77164   48.57265  1.98737   1.000 32.19388  ?  26  ALA   D CA    1 
ATOM   4164 C  C     . ALA   D 2 27  ? 2.24323   48.71389  1.61684   1.000 33.51947  ?  26  ALA   D C     1 
ATOM   4165 O  O     . ALA   D 2 27  ? 2.60998   48.40928  0.47989   1.000 29.73185  ?  26  ALA   D O     1 
ATOM   4166 C  CB    . ALA   D 2 27  ? -0.02282  49.75135  1.40706   1.000 28.30725  ?  26  ALA   D CB    1 
ATOM   4167 N  N     . ASP   D 2 28  ? 3.09815   49.14978  2.54892   1.000 31.50375  ?  27  ASP   D N     1 
ATOM   4168 C  CA    . ASP   D 2 28  ? 4.50038   49.37718  2.22253   1.000 36.08293  ?  27  ASP   D CA    1 
ATOM   4169 C  C     . ASP   D 2 28  ? 5.29776   48.08161  2.11349   1.000 38.94704  ?  27  ASP   D C     1 
ATOM   4170 O  O     . ASP   D 2 28  ? 6.35856   48.07359  1.47137   1.000 43.71172  ?  27  ASP   D O     1 
ATOM   4171 C  CB    . ASP   D 2 28  ? 5.13666   50.32051  3.25704   1.000 34.42889  ?  27  ASP   D CB    1 
ATOM   4172 C  CG    . ASP   D 2 28  ? 4.97446   49.83629  4.69899   1.000 39.74717  ?  27  ASP   D CG    1 
ATOM   4173 O  OD1   . ASP   D 2 28  ? 4.09522   48.98383  4.95391   1.000 38.28269  ?  27  ASP   D OD1   1 
ATOM   4174 O  OD2   . ASP   D 2 28  ? 5.71706   50.32868  5.59082   1.000 38.64071  -1 27  ASP   D OD2   1 
ATOM   4175 N  N     . LYS   D 2 29  ? 4.81099   46.99278  2.71304   1.000 31.73635  ?  28  LYS   D N     1 
ATOM   4176 C  CA    . LYS   D 2 29  ? 5.46012   45.68896  2.68350   1.000 29.17235  ?  28  LYS   D CA    1 
ATOM   4177 C  C     . LYS   D 2 29  ? 4.71809   44.66381  1.83831   1.000 32.06077  ?  28  LYS   D C     1 
ATOM   4178 O  O     . LYS   D 2 29  ? 5.34787   43.84931  1.15123   1.000 28.91188  ?  28  LYS   D O     1 
ATOM   4179 C  CB    . LYS   D 2 29  ? 5.59650   45.14120  4.10557   1.000 36.35308  ?  28  LYS   D CB    1 
ATOM   4180 C  CG    . LYS   D 2 29  ? 6.43009   46.01387  5.04612   1.000 46.14950  ?  28  LYS   D CG    1 
ATOM   4181 C  CD    . LYS   D 2 29  ? 7.84054   46.13787  4.52016   1.000 45.79114  ?  28  LYS   D CD    1 
ATOM   4182 C  CE    . LYS   D 2 29  ? 8.86930   46.17625  5.64063   1.000 52.98289  ?  28  LYS   D CE    1 
ATOM   4183 N  NZ    . LYS   D 2 29  ? 10.24633  46.03121  5.07249   1.000 57.28506  ?  28  LYS   D NZ    1 
ATOM   4184 N  N     . VAL   D 2 30  ? 3.39262   44.66574  1.91263   1.000 28.33345  ?  29  VAL   D N     1 
ATOM   4185 C  CA    . VAL   D 2 30  ? 2.54600   43.72420  1.18868   1.000 30.74692  ?  29  VAL   D CA    1 
ATOM   4186 C  C     . VAL   D 2 30  ? 1.47059   44.52261  0.46117   1.000 28.90554  ?  29  VAL   D C     1 
ATOM   4187 O  O     . VAL   D 2 30  ? 0.30270   44.49520  0.86117   1.000 29.91927  ?  29  VAL   D O     1 
ATOM   4188 C  CB    . VAL   D 2 30  ? 1.93603   42.66863  2.12629   1.000 29.82945  ?  29  VAL   D CB    1 
ATOM   4189 C  CG1   . VAL   D 2 30  ? 2.83908   41.45898  2.20713   1.000 33.23088  ?  29  VAL   D CG1   1 
ATOM   4190 C  CG2   . VAL   D 2 30  ? 1.71281   43.24132  3.51038   1.000 27.44760  ?  29  VAL   D CG2   1 
ATOM   4191 N  N     . PRO   D 2 31  ? 1.81917   45.25258  -0.60772  1.000 30.86825  ?  30  PRO   D N     1 
ATOM   4192 C  CA    . PRO   D 2 31  ? 0.81029   46.07781  -1.29286  1.000 27.19247  ?  30  PRO   D CA    1 
ATOM   4193 C  C     . PRO   D 2 31  ? -0.33340  45.28061  -1.88424  1.000 29.73361  ?  30  PRO   D C     1 
ATOM   4194 O  O     . PRO   D 2 31  ? -1.48795  45.71291  -1.78461  1.000 30.01740  ?  30  PRO   D O     1 
ATOM   4195 C  CB    . PRO   D 2 31  ? 1.63055   46.79534  -2.38450  1.000 30.73039  ?  30  PRO   D CB    1 
ATOM   4196 C  CG    . PRO   D 2 31  ? 2.80881   45.90621  -2.62791  1.000 30.17230  ?  30  PRO   D CG    1 
ATOM   4197 C  CD    . PRO   D 2 31  ? 3.13786   45.35441  -1.25003  1.000 32.30305  ?  30  PRO   D CD    1 
ATOM   4198 N  N     . LYS   D 2 32  ? -0.06566  44.13251  -2.51792  1.000 28.40584  ?  31  LYS   D N     1 
ATOM   4199 C  CA    . LYS   D 2 32  ? -1.16994  43.41865  -3.16310  1.000 29.15555  ?  31  LYS   D CA    1 
ATOM   4200 C  C     . LYS   D 2 32  ? -2.15901  42.89612  -2.12587  1.000 24.76317  ?  31  LYS   D C     1 
ATOM   4201 O  O     . LYS   D 2 32  ? -3.37525  43.00067  -2.30830  1.000 24.98392  ?  31  LYS   D O     1 
ATOM   4202 C  CB    . LYS   D 2 32  ? -0.64456  42.28034  -4.03266  1.000 26.40829  ?  31  LYS   D CB    1 
ATOM   4203 C  CG    . LYS   D 2 32  ? -1.67932  41.67962  -4.96255  1.000 38.04764  ?  31  LYS   D CG    1 
ATOM   4204 C  CD    . LYS   D 2 32  ? -1.06859  40.61562  -5.90250  1.000 36.93633  ?  31  LYS   D CD    1 
ATOM   4205 C  CE    . LYS   D 2 32  ? -2.12025  40.03258  -6.86680  1.000 40.50315  ?  31  LYS   D CE    1 
ATOM   4206 N  NZ    . LYS   D 2 32  ? -1.60895  38.82019  -7.59773  1.000 41.84818  ?  31  LYS   D NZ    1 
ATOM   4207 N  N     . THR   D 2 33  ? -1.65151  42.35531  -1.01426  1.000 27.20262  ?  32  THR   D N     1 
ATOM   4208 C  CA    . THR   D 2 33  ? -2.53831  41.82060  0.01860   1.000 24.01849  ?  32  THR   D CA    1 
ATOM   4209 C  C     . THR   D 2 33  ? -3.30527  42.93791  0.71805   1.000 23.63595  ?  32  THR   D C     1 
ATOM   4210 O  O     . THR   D 2 33  ? -4.51684  42.82982  0.92086   1.000 23.63435  ?  32  THR   D O     1 
ATOM   4211 C  CB    . THR   D 2 33  ? -1.70971  40.98409  0.98958   1.000 26.39019  ?  32  THR   D CB    1 
ATOM   4212 O  OG1   . THR   D 2 33  ? -0.97016  40.00794  0.22355   1.000 25.69545  ?  32  THR   D OG1   1 
ATOM   4213 C  CG2   . THR   D 2 33  ? -2.59128  40.28664  2.03870   1.000 25.15092  ?  32  THR   D CG2   1 
ATOM   4214 N  N     . ALA   D 2 34  ? -2.62696  44.03767  1.06153   1.000 30.90185  ?  33  ALA   D N     1 
ATOM   4215 C  CA    . ALA   D 2 34  ? -3.30586  45.15208  1.72487   1.000 25.11667  ?  33  ALA   D CA    1 
ATOM   4216 C  C     . ALA   D 2 34  ? -4.41976  45.71645  0.85108   1.000 27.93436  ?  33  ALA   D C     1 
ATOM   4217 O  O     . ALA   D 2 34  ? -5.52428  45.99464  1.33143   1.000 25.27670  ?  33  ALA   D O     1 
ATOM   4218 C  CB    . ALA   D 2 34  ? -2.28520  46.23550  2.09568   1.000 27.03698  ?  33  ALA   D CB    1 
ATOM   4219 N  N     . GLU   D 2 35  ? -4.16590  45.83518  -0.45525  1.000 27.64932  ?  34  GLU   D N     1 
ATOM   4220 C  CA    . GLU   D 2 35  ? -5.14876  46.40293  -1.36424  1.000 26.40936  ?  34  GLU   D CA    1 
ATOM   4221 C  C     . GLU   D 2 35  ? -6.39053  45.52289  -1.48039  1.000 26.79600  ?  34  GLU   D C     1 
ATOM   4222 O  O     . GLU   D 2 35  ? -7.51186  46.03072  -1.59692  1.000 23.67763  ?  34  GLU   D O     1 
ATOM   4223 C  CB    . GLU   D 2 35  ? -4.49668  46.60658  -2.74422  1.000 29.20871  ?  34  GLU   D CB    1 
ATOM   4224 C  CG    . GLU   D 2 35  ? -5.46924  46.93441  -3.85261  1.000 34.17380  ?  34  GLU   D CG    1 
ATOM   4225 C  CD    . GLU   D 2 35  ? -6.04653  48.33714  -3.71158  1.000 37.12235  ?  34  GLU   D CD    1 
ATOM   4226 O  OE1   . GLU   D 2 35  ? -5.49910  49.12150  -2.89547  1.000 36.60918  ?  34  GLU   D OE1   1 
ATOM   4227 O  OE2   . GLU   D 2 35  ? -7.03950  48.64477  -4.40939  1.000 37.84486  -1 34  GLU   D OE2   1 
ATOM   4228 N  N     . ASN   D 2 36  ? -6.20891  44.20194  -1.49065  1.000 23.92996  ?  35  ASN   D N     1 
ATOM   4229 C  CA    . ASN   D 2 36  ? -7.34893  43.28948  -1.44660  1.000 25.82333  ?  35  ASN   D CA    1 
ATOM   4230 C  C     . ASN   D 2 36  ? -8.21798  43.56829  -0.22157  1.000 22.57780  ?  35  ASN   D C     1 
ATOM   4231 O  O     . ASN   D 2 36  ? -9.43150  43.78008  -0.32902  1.000 24.55437  ?  35  ASN   D O     1 
ATOM   4232 C  CB    . ASN   D 2 36  ? -6.83281  41.84882  -1.44761  1.000 22.61021  ?  35  ASN   D CB    1 
ATOM   4233 C  CG    . ASN   D 2 36  ? -7.95168  40.80552  -1.45320  1.000 31.32696  ?  35  ASN   D CG    1 
ATOM   4234 O  OD1   . ASN   D 2 36  ? -8.80837  40.78560  -2.34398  1.000 28.50345  ?  35  ASN   D OD1   1 
ATOM   4235 N  ND2   . ASN   D 2 36  ? -7.92340  39.90706  -0.47218  1.000 27.40221  ?  35  ASN   D ND2   1 
ATOM   4236 N  N     . PHE   D 2 37  ? -7.59623  43.60869  0.95494   1.000 25.50308  ?  36  PHE   D N     1 
ATOM   4237 C  CA    . PHE   D 2 37  ? -8.35528  43.84468  2.17766   1.000 28.71715  ?  36  PHE   D CA    1 
ATOM   4238 C  C     . PHE   D 2 37  ? -8.98417  45.23730  2.18023   1.000 23.27083  ?  36  PHE   D C     1 
ATOM   4239 O  O     . PHE   D 2 37  ? -10.14036 45.39060  2.57577   1.000 27.73512  ?  36  PHE   D O     1 
ATOM   4240 C  CB    . PHE   D 2 37  ? -7.43921  43.64185  3.38072   1.000 28.06710  ?  36  PHE   D CB    1 
ATOM   4241 C  CG    . PHE   D 2 37  ? -8.16105  43.52081  4.69745   1.000 28.07355  ?  36  PHE   D CG    1 
ATOM   4242 C  CD1   . PHE   D 2 37  ? -8.66073  42.29495  5.12977   1.000 27.67789  ?  36  PHE   D CD1   1 
ATOM   4243 C  CD2   . PHE   D 2 37  ? -8.29035  44.62634  5.53095   1.000 31.10686  ?  36  PHE   D CD2   1 
ATOM   4244 C  CE1   . PHE   D 2 37  ? -9.30369  42.18490  6.40722   1.000 26.72465  ?  36  PHE   D CE1   1 
ATOM   4245 C  CE2   . PHE   D 2 37  ? -8.92619  44.52337  6.79510   1.000 28.23426  ?  36  PHE   D CE2   1 
ATOM   4246 C  CZ    . PHE   D 2 37  ? -9.43277  43.30589  7.20890   1.000 26.36433  ?  36  PHE   D CZ    1 
ATOM   4247 N  N     . ARG   D 2 38  ? -8.24941  46.25401  1.71126   1.000 25.99593  ?  37  ARG   D N     1 
ATOM   4248 C  CA    . ARG   D 2 38  ? -8.81060  47.60055  1.60114   1.000 27.04421  ?  37  ARG   D CA    1 
ATOM   4249 C  C     . ARG   D 2 38  ? -10.05902 47.60809  0.72936   1.000 28.23881  ?  37  ARG   D C     1 
ATOM   4250 O  O     . ARG   D 2 38  ? -11.10234 48.14264  1.12272   1.000 27.86506  ?  37  ARG   D O     1 
ATOM   4251 C  CB    . ARG   D 2 38  ? -7.77613  48.57496  1.02424   1.000 28.97039  ?  37  ARG   D CB    1 
ATOM   4252 C  CG    . ARG   D 2 38  ? -8.14991  50.06769  1.23037   1.000 36.12994  ?  37  ARG   D CG    1 
ATOM   4253 C  CD    . ARG   D 2 38  ? -7.43272  51.01756  0.24040   1.000 33.35867  ?  37  ARG   D CD    1 
ATOM   4254 N  NE    . ARG   D 2 38  ? -7.61141  50.59636  -1.14663  1.000 34.70595  ?  37  ARG   D NE    1 
ATOM   4255 C  CZ    . ARG   D 2 38  ? -8.73474  50.72975  -1.84257  1.000 32.99954  ?  37  ARG   D CZ    1 
ATOM   4256 N  NH1   . ARG   D 2 38  ? -9.81021  51.31056  -1.33002  1.000 32.95552  ?  37  ARG   D NH1   1 
ATOM   4257 N  NH2   . ARG   D 2 38  ? -8.78266  50.26981  -3.08594  1.000 37.83284  ?  37  ARG   D NH2   1 
ATOM   4258 N  N     . ALA   D 2 39  ? -9.95953  47.04579  -0.47882  1.000 28.14612  ?  38  ALA   D N     1 
ATOM   4259 C  CA    . ALA   D 2 39  ? -11.08311 47.08670  -1.40565  1.000 27.45692  ?  38  ALA   D CA    1 
ATOM   4260 C  C     . ALA   D 2 39  ? -12.25359 46.25592  -0.90091  1.000 32.11263  ?  38  ALA   D C     1 
ATOM   4261 O  O     . ALA   D 2 39  ? -13.41150 46.63746  -1.09635  1.000 31.49899  ?  38  ALA   D O     1 
ATOM   4262 C  CB    . ALA   D 2 39  ? -10.65053 46.60872  -2.80140  1.000 28.21409  ?  38  ALA   D CB    1 
ATOM   4263 N  N     . LEU   D 2 40  ? -11.97980 45.10637  -0.26614  1.000 28.09823  ?  39  LEU   D N     1 
ATOM   4264 C  CA    . LEU   D 2 40  ? -13.07430 44.32840  0.31437   1.000 32.60428  ?  39  LEU   D CA    1 
ATOM   4265 C  C     . LEU   D 2 40  ? -13.73602 45.07408  1.46629   1.000 31.39428  ?  39  LEU   D C     1 
ATOM   4266 O  O     . LEU   D 2 40  ? -14.93667 44.91045  1.69777   1.000 34.25852  ?  39  LEU   D O     1 
ATOM   4267 C  CB    . LEU   D 2 40  ? -12.57924 42.95309  0.78864   1.000 28.57276  ?  39  LEU   D CB    1 
ATOM   4268 C  CG    . LEU   D 2 40  ? -12.09286 42.00704  -0.31626  1.000 30.63334  ?  39  LEU   D CG    1 
ATOM   4269 C  CD1   . LEU   D 2 40  ? -11.49397 40.71927  0.26388   1.000 20.32309  ?  39  LEU   D CD1   1 
ATOM   4270 C  CD2   . LEU   D 2 40  ? -13.20830 41.70756  -1.36822  1.000 27.65043  ?  39  LEU   D CD2   1 
ATOM   4271 N  N     . SER   D 2 41  ? -12.97420 45.89122  2.19778   1.000 29.65750  ?  40  SER   D N     1 
ATOM   4272 C  CA    . SER   D 2 41  ? -13.55743 46.65760  3.29317   1.000 26.08471  ?  40  SER   D CA    1 
ATOM   4273 C  C     . SER   D 2 41  ? -14.45193 47.77468  2.77271   1.000 33.71627  ?  40  SER   D C     1 
ATOM   4274 O  O     . SER   D 2 41  ? -15.48224 48.07686  3.38807   1.000 30.62798  ?  40  SER   D O     1 
ATOM   4275 C  CB    . SER   D 2 41  ? -12.46432 47.24906  4.18512   1.000 26.87749  ?  40  SER   D CB    1 
ATOM   4276 O  OG    . SER   D 2 41  ? -11.74371 46.25320  4.87743   1.000 30.59861  ?  40  SER   D OG    1 
ATOM   4277 N  N     . THR   D 2 42  ? -14.06627 48.42022  1.64848   1.000 33.11086  ?  41  THR   D N     1 
ATOM   4278 C  CA    . THR   D 2 42  ? -14.90904 49.48079  1.09361   1.000 31.94785  ?  41  THR   D CA    1 
ATOM   4279 C  C     . THR   D 2 42  ? -16.11216 48.93898  0.35145   1.000 32.68905  ?  41  THR   D C     1 
ATOM   4280 O  O     . THR   D 2 42  ? -17.10377 49.66192  0.20515   1.000 33.29431  ?  41  THR   D O     1 
ATOM   4281 C  CB    . THR   D 2 42  ? -14.12924 50.40400  0.13752   1.000 35.53095  ?  41  THR   D CB    1 
ATOM   4282 O  OG1   . THR   D 2 42  ? -13.77548 49.69776  -1.05912  1.000 33.36974  ?  41  THR   D OG1   1 
ATOM   4283 C  CG2   . THR   D 2 42  ? -12.87402 50.98103  0.79853   1.000 30.28869  ?  41  THR   D CG2   1 
ATOM   4284 N  N     . GLY   D 2 43  ? -16.05297 47.69340  -0.11941  1.000 32.01731  ?  42  GLY   D N     1 
ATOM   4285 C  CA    . GLY   D 2 43  ? -17.10584 47.16276  -0.96143  1.000 32.16934  ?  42  GLY   D CA    1 
ATOM   4286 C  C     . GLY   D 2 43  ? -17.08833 47.66642  -2.39606  1.000 34.02188  ?  42  GLY   D C     1 
ATOM   4287 O  O     . GLY   D 2 43  ? -18.07772 47.48737  -3.11339  1.000 38.52572  ?  42  GLY   D O     1 
ATOM   4288 N  N     . GLU   D 2 44  ? -15.97437 48.24454  -2.85505  1.000 36.97256  ?  43  GLU   D N     1 
ATOM   4289 C  CA    . GLU   D 2 44  ? -15.98891 49.01943  -4.09389  1.000 40.85671  ?  43  GLU   D CA    1 
ATOM   4290 C  C     . GLU   D 2 44  ? -16.09159 48.15784  -5.35353  1.000 44.73642  ?  43  GLU   D C     1 
ATOM   4291 O  O     . GLU   D 2 44  ? -16.47986 48.67077  -6.40496  1.000 37.52342  ?  43  GLU   D O     1 
ATOM   4292 C  CB    . GLU   D 2 44  ? -14.75277 49.91611  -4.15962  1.000 38.59261  ?  43  GLU   D CB    1 
ATOM   4293 C  CG    . GLU   D 2 44  ? -13.42991 49.18924  -4.22170  1.000 36.47364  ?  43  GLU   D CG    1 
ATOM   4294 C  CD    . GLU   D 2 44  ? -12.26615 50.10287  -3.90424  1.000 39.91879  ?  43  GLU   D CD    1 
ATOM   4295 O  OE1   . GLU   D 2 44  ? -12.34545 50.83319  -2.88997  1.000 35.99633  ?  43  GLU   D OE1   1 
ATOM   4296 O  OE2   . GLU   D 2 44  ? -11.26771 50.09057  -4.65971  1.000 42.97003  -1 43  GLU   D OE2   1 
ATOM   4297 N  N     . LYS   D 2 45  ? -15.75892 46.87276  -5.27421  1.000 35.28580  ?  44  LYS   D N     1 
ATOM   4298 C  CA    . LYS   D 2 45  ? -15.98628 45.94297  -6.36742  1.000 38.91495  ?  44  LYS   D CA    1 
ATOM   4299 C  C     . LYS   D 2 45  ? -17.41243 45.41711  -6.40586  1.000 35.75250  ?  44  LYS   D C     1 
ATOM   4300 O  O     . LYS   D 2 45  ? -17.70164 44.53780  -7.21787  1.000 37.62691  ?  44  LYS   D O     1 
ATOM   4301 C  CB    . LYS   D 2 45  ? -15.01815 44.75431  -6.27090  1.000 35.20329  ?  44  LYS   D CB    1 
ATOM   4302 C  CG    . LYS   D 2 45  ? -13.53649 45.12690  -6.22658  1.000 35.04855  ?  44  LYS   D CG    1 
ATOM   4303 C  CD    . LYS   D 2 45  ? -13.10753 45.88768  -7.48613  1.000 37.07920  ?  44  LYS   D CD    1 
ATOM   4304 C  CE    . LYS   D 2 45  ? -11.59602 46.09697  -7.53230  1.000 39.49731  ?  44  LYS   D CE    1 
ATOM   4305 N  NZ    . LYS   D 2 45  ? -11.19007 47.37596  -8.19494  1.000 48.99305  ?  44  LYS   D NZ    1 
ATOM   4306 N  N     . GLY   D 2 46  ? -18.29953 45.90881  -5.54655  1.000 31.99319  ?  45  GLY   D N     1 
ATOM   4307 C  CA    . GLY   D 2 46  ? -19.63673 45.36726  -5.45193  1.000 33.33379  ?  45  GLY   D CA    1 
ATOM   4308 C  C     . GLY   D 2 46  ? -19.76011 44.13707  -4.58366  1.000 37.08828  ?  45  GLY   D C     1 
ATOM   4309 O  O     . GLY   D 2 46  ? -20.78028 43.43833  -4.65730  1.000 36.05780  ?  45  GLY   D O     1 
ATOM   4310 N  N     . PHE   D 2 47  ? -18.75302 43.84835  -3.76459  1.000 32.15064  ?  46  PHE   D N     1 
ATOM   4311 C  CA    . PHE   D 2 47  ? -18.80936 42.74166  -2.82622  1.000 32.40590  ?  46  PHE   D CA    1 
ATOM   4312 C  C     . PHE   D 2 47  ? -17.70698 42.96663  -1.80175  1.000 30.67299  ?  46  PHE   D C     1 
ATOM   4313 O  O     . PHE   D 2 47  ? -16.74863 43.70220  -2.05575  1.000 35.36222  ?  46  PHE   D O     1 
ATOM   4314 C  CB    . PHE   D 2 47  ? -18.67148 41.39300  -3.54559  1.000 30.54885  ?  46  PHE   D CB    1 
ATOM   4315 C  CG    . PHE   D 2 47  ? -17.42030 41.26674  -4.39965  1.000 39.09073  ?  46  PHE   D CG    1 
ATOM   4316 C  CD1   . PHE   D 2 47  ? -16.17705 41.06962  -3.80962  1.000 29.61292  ?  46  PHE   D CD1   1 
ATOM   4317 C  CD2   . PHE   D 2 47  ? -17.50065 41.29997  -5.79162  1.000 34.72194  ?  46  PHE   D CD2   1 
ATOM   4318 C  CE1   . PHE   D 2 47  ? -15.04945 40.93365  -4.56076  1.000 30.20889  ?  46  PHE   D CE1   1 
ATOM   4319 C  CE2   . PHE   D 2 47  ? -16.36876 41.16052  -6.56491  1.000 33.20746  ?  46  PHE   D CE2   1 
ATOM   4320 C  CZ    . PHE   D 2 47  ? -15.13723 40.97322  -5.95337  1.000 41.80611  ?  46  PHE   D CZ    1 
ATOM   4321 N  N     . GLY   D 2 48  ? -17.85205 42.34771  -0.63727  1.000 30.36109  ?  47  GLY   D N     1 
ATOM   4322 C  CA    . GLY   D 2 48  ? -16.83441 42.52830  0.39125   1.000 27.95757  ?  47  GLY   D CA    1 
ATOM   4323 C  C     . GLY   D 2 48  ? -17.35996 42.14827  1.76622   1.000 27.76542  ?  47  GLY   D C     1 
ATOM   4324 O  O     . GLY   D 2 48  ? -18.36159 41.44463  1.89044   1.000 28.52296  ?  47  GLY   D O     1 
ATOM   4325 N  N     . TYR   D 2 49  ? -16.66123 42.65960  2.78693   1.000 27.94899  ?  48  TYR   D N     1 
ATOM   4326 C  CA    . TYR   D 2 49  ? -16.81249 42.18102  4.16321   1.000 27.47584  ?  48  TYR   D CA    1 
ATOM   4327 C  C     . TYR   D 2 49  ? -18.12553 42.59539  4.82251   1.000 35.36988  ?  48  TYR   D C     1 
ATOM   4328 O  O     . TYR   D 2 49  ? -18.55772 41.92650  5.77433   1.000 30.48986  ?  48  TYR   D O     1 
ATOM   4329 C  CB    . TYR   D 2 49  ? -15.64029 42.68388  5.01633   1.000 26.45744  ?  48  TYR   D CB    1 
ATOM   4330 C  CG    . TYR   D 2 49  ? -14.31302 42.03352  4.68665   1.000 26.36795  ?  48  TYR   D CG    1 
ATOM   4331 C  CD1   . TYR   D 2 49  ? -14.21836 40.66043  4.50341   1.000 27.21222  ?  48  TYR   D CD1   1 
ATOM   4332 C  CD2   . TYR   D 2 49  ? -13.15911 42.79894  4.52698   1.000 25.52153  ?  48  TYR   D CD2   1 
ATOM   4333 C  CE1   . TYR   D 2 49  ? -13.01393 40.06061  4.19726   1.000 19.87998  ?  48  TYR   D CE1   1 
ATOM   4334 C  CE2   . TYR   D 2 49  ? -11.95279 42.20183  4.21897   1.000 26.59366  ?  48  TYR   D CE2   1 
ATOM   4335 C  CZ    . TYR   D 2 49  ? -11.89264 40.83347  4.06356   1.000 23.61125  ?  48  TYR   D CZ    1 
ATOM   4336 O  OH    . TYR   D 2 49  ? -10.68731 40.24375  3.75767   1.000 23.30818  ?  48  TYR   D OH    1 
ATOM   4337 N  N     . LYS   D 2 50  ? -18.74998 43.68830  4.37733   1.000 32.09798  ?  49  LYS   D N     1 
ATOM   4338 C  CA    . LYS   D 2 50  ? -19.96175 44.15457  5.03412   1.000 32.61244  ?  49  LYS   D CA    1 
ATOM   4339 C  C     . LYS   D 2 50  ? -21.00946 43.05951  5.06870   1.000 30.15532  ?  49  LYS   D C     1 
ATOM   4340 O  O     . LYS   D 2 50  ? -21.26416 42.39534  4.06165   1.000 31.55241  ?  49  LYS   D O     1 
ATOM   4341 C  CB    . LYS   D 2 50  ? -20.54232 45.38052  4.33250   1.000 29.56082  ?  49  LYS   D CB    1 
ATOM   4342 C  CG    . LYS   D 2 50  ? -21.82688 45.85127  4.99323   1.000 33.48597  ?  49  LYS   D CG    1 
ATOM   4343 C  CD    . LYS   D 2 50  ? -22.23235 47.23123  4.49613   1.000 37.59221  ?  49  LYS   D CD    1 
ATOM   4344 C  CE    . LYS   D 2 50  ? -23.45377 47.75392  5.24036   1.000 40.11155  ?  49  LYS   D CE    1 
ATOM   4345 N  NZ    . LYS   D 2 50  ? -24.04753 48.90197  4.48580   1.000 46.28004  ?  49  LYS   D NZ    1 
ATOM   4346 N  N     . GLY   D 2 51  ? -21.62217 42.88309  6.23780   1.000 27.20575  ?  50  GLY   D N     1 
ATOM   4347 C  CA    . GLY   D 2 51  ? -22.65579 41.89591  6.43807   1.000 27.76061  ?  50  GLY   D CA    1 
ATOM   4348 C  C     . GLY   D 2 51  ? -22.15289 40.52565  6.83595   1.000 32.95406  ?  50  GLY   D C     1 
ATOM   4349 O  O     . GLY   D 2 51  ? -22.95510 39.68853  7.27153   1.000 36.61469  ?  50  GLY   D O     1 
ATOM   4350 N  N     . SER   D 2 52  ? -20.86078 40.26137  6.70341   1.000 30.25252  ?  51  SER   D N     1 
ATOM   4351 C  CA    . SER   D 2 52  ? -20.34348 38.93393  6.98986   1.000 31.85327  ?  51  SER   D CA    1 
ATOM   4352 C  C     . SER   D 2 52  ? -19.99452 38.78902  8.47262   1.000 32.09842  ?  51  SER   D C     1 
ATOM   4353 O  O     . SER   D 2 52  ? -19.98155 39.75444  9.23765   1.000 26.46521  ?  51  SER   D O     1 
ATOM   4354 C  CB    . SER   D 2 52  ? -19.13330 38.63749  6.11358   1.000 28.37112  ?  51  SER   D CB    1 
ATOM   4355 O  OG    . SER   D 2 52  ? -18.04293 39.45466  6.46547   1.000 26.56840  ?  51  SER   D OG    1 
ATOM   4356 N  N     . CYS   D 2 53  ? -19.67729 37.55500  8.86236   1.000 30.32502  ?  52  CYS   D N     1 
ATOM   4357 C  CA    A CYS   D 2 53  ? -19.51631 37.13518  10.25215  0.500 30.37380  ?  52  CYS   D CA    1 
ATOM   4358 C  CA    B CYS   D 2 53  ? -19.51245 37.19827  10.26392  0.500 30.82933  ?  52  CYS   D CA    1 
ATOM   4359 C  C     . CYS   D 2 53  ? -18.06917 36.81930  10.58509  1.000 30.32256  ?  52  CYS   D C     1 
ATOM   4360 O  O     . CYS   D 2 53  ? -17.23195 36.59981  9.70298   1.000 29.74625  ?  52  CYS   D O     1 
ATOM   4361 C  CB    A CYS   D 2 53  ? -20.35963 35.87530  10.52787  0.500 34.73863  ?  52  CYS   D CB    1 
ATOM   4362 C  CB    B CYS   D 2 53  ? -20.46091 36.05278  10.66066  0.500 34.76601  ?  52  CYS   D CB    1 
ATOM   4363 S  SG    A CYS   D 2 53  ? -22.13086 36.06708  10.46512  0.500 43.05338  ?  52  CYS   D SG    1 
ATOM   4364 S  SG    B CYS   D 2 53  ? -20.11132 34.46261  9.89869   0.500 43.05338  ?  52  CYS   D SG    1 
ATOM   4365 N  N     . PHE   D 2 54  ? -17.77846 36.76216  11.89034  1.000 32.80989  ?  53  PHE   D N     1 
ATOM   4366 C  CA    . PHE   D 2 54  ? -16.57421 36.11388  12.40800  1.000 27.60412  ?  53  PHE   D CA    1 
ATOM   4367 C  C     . PHE   D 2 54  ? -16.98590 34.69382  12.77135  1.000 27.76624  ?  53  PHE   D C     1 
ATOM   4368 O  O     . PHE   D 2 54  ? -17.59088 34.46072  13.81978  1.000 32.12752  ?  53  PHE   D O     1 
ATOM   4369 C  CB    . PHE   D 2 54  ? -16.00248 36.85056  13.61505  1.000 27.05009  ?  53  PHE   D CB    1 
ATOM   4370 C  CG    . PHE   D 2 54  ? -15.07971 37.98043  13.26028  1.000 26.47003  ?  53  PHE   D CG    1 
ATOM   4371 C  CD1   . PHE   D 2 54  ? -15.59070 39.24133  12.99027  1.000 25.47238  ?  53  PHE   D CD1   1 
ATOM   4372 C  CD2   . PHE   D 2 54  ? -13.69195 37.77955  13.18364  1.000 20.84371  ?  53  PHE   D CD2   1 
ATOM   4373 C  CE1   . PHE   D 2 54  ? -14.74526 40.29901  12.64666  1.000 25.77493  ?  53  PHE   D CE1   1 
ATOM   4374 C  CE2   . PHE   D 2 54  ? -12.85005 38.82174  12.86803  1.000 25.97854  ?  53  PHE   D CE2   1 
ATOM   4375 C  CZ    . PHE   D 2 54  ? -13.37912 40.10168  12.59653  1.000 26.14627  ?  53  PHE   D CZ    1 
ATOM   4376 N  N     . HIS   D 2 55  ? -16.66593 33.73503  11.91516  1.000 23.03955  ?  54  HIS   D N     1 
ATOM   4377 C  CA    . HIS   D 2 55  ? -17.22791 32.39973  12.06425  1.000 23.57525  ?  54  HIS   D CA    1 
ATOM   4378 C  C     . HIS   D 2 55  ? -16.43779 31.50665  13.00777  1.000 22.84282  ?  54  HIS   D C     1 
ATOM   4379 O  O     . HIS   D 2 55  ? -16.96162 30.46940  13.44471  1.000 27.34621  ?  54  HIS   D O     1 
ATOM   4380 C  CB    . HIS   D 2 55  ? -17.34916 31.71212  10.70500  1.000 26.08068  ?  54  HIS   D CB    1 
ATOM   4381 C  CG    . HIS   D 2 55  ? -16.03913 31.45985  10.03199  1.000 23.94790  ?  54  HIS   D CG    1 
ATOM   4382 N  ND1   . HIS   D 2 55  ? -15.33432 32.44928  9.37585   1.000 22.69537  ?  54  HIS   D ND1   1 
ATOM   4383 C  CD2   . HIS   D 2 55  ? -15.31061 30.32550  9.90520   1.000 23.48079  ?  54  HIS   D CD2   1 
ATOM   4384 C  CE1   . HIS   D 2 55  ? -14.22570 31.93173  8.87456   1.000 22.97953  ?  54  HIS   D CE1   1 
ATOM   4385 N  NE2   . HIS   D 2 55  ? -14.18704 30.64624  9.18358   1.000 25.17407  ?  54  HIS   D NE2   1 
ATOM   4386 N  N     . ARG   D 2 56  ? -15.21427 31.88575  13.35444  1.000 25.80608  ?  55  ARG   D N     1 
ATOM   4387 C  CA    . ARG   D 2 56  ? -14.33632 31.04383  14.16570  1.000 26.58401  ?  55  ARG   D CA    1 
ATOM   4388 C  C     . ARG   D 2 56  ? -13.60272 31.92755  15.16226  1.000 28.36430  ?  55  ARG   D C     1 
ATOM   4389 O  O     . ARG   D 2 56  ? -12.76485 32.74905  14.78098  1.000 22.81107  ?  55  ARG   D O     1 
ATOM   4390 C  CB    . ARG   D 2 56  ? -13.34818 30.25937  13.29621  1.000 22.64102  ?  55  ARG   D CB    1 
ATOM   4391 C  CG    . ARG   D 2 56  ? -12.41077 29.39871  14.13516  1.000 29.43388  ?  55  ARG   D CG    1 
ATOM   4392 C  CD    . ARG   D 2 56  ? -11.46607 28.57000  13.30132  1.000 28.13891  ?  55  ARG   D CD    1 
ATOM   4393 N  NE    . ARG   D 2 56  ? -12.14268 27.59030  12.45229  1.000 29.34014  ?  55  ARG   D NE    1 
ATOM   4394 C  CZ    . ARG   D 2 56  ? -11.64936 27.14364  11.31008  1.000 27.84570  ?  55  ARG   D CZ    1 
ATOM   4395 N  NH1   . ARG   D 2 56  ? -10.53028 27.64369  10.79344  1.000 29.64281  ?  55  ARG   D NH1   1 
ATOM   4396 N  NH2   . ARG   D 2 56  ? -12.28733 26.17341  10.66724  1.000 38.52329  ?  55  ARG   D NH2   1 
ATOM   4397 N  N     . ILE   D 2 57  ? -13.89768 31.74623  16.44836  1.000 25.85589  ?  56  ILE   D N     1 
ATOM   4398 C  CA    . ILE   D 2 57  ? -13.28430 32.51881  17.51438  1.000 24.99464  ?  56  ILE   D CA    1 
ATOM   4399 C  C     . ILE   D 2 57  ? -12.79262 31.52610  18.56462  1.000 26.33961  ?  56  ILE   D C     1 
ATOM   4400 O  O     . ILE   D 2 57  ? -13.57731 30.71880  19.08420  1.000 22.89025  ?  56  ILE   D O     1 
ATOM   4401 C  CB    . ILE   D 2 57  ? -14.26721 33.53772  18.12525  1.000 27.49329  ?  56  ILE   D CB    1 
ATOM   4402 C  CG1   . ILE   D 2 57  ? -14.64199 34.60853  17.10280  1.000 26.52437  ?  56  ILE   D CG1   1 
ATOM   4403 C  CG2   . ILE   D 2 57  ? -13.66838 34.18713  19.40831  1.000 22.03213  ?  56  ILE   D CG2   1 
ATOM   4404 C  CD1   . ILE   D 2 57  ? -15.78904 35.52280  17.55264  1.000 28.63966  ?  56  ILE   D CD1   1 
ATOM   4405 N  N     . ILE   D 2 58  ? -11.50001 31.56867  18.85519  1.000 26.94506  ?  57  ILE   D N     1 
ATOM   4406 C  CA    . ILE   D 2 58  ? -10.88090 30.62980  19.78747  1.000 30.54915  ?  57  ILE   D CA    1 
ATOM   4407 C  C     . ILE   D 2 58  ? -10.11654 31.45194  20.81363  1.000 25.07517  ?  57  ILE   D C     1 
ATOM   4408 O  O     . ILE   D 2 58  ? -9.02494  31.96377  20.51937  1.000 26.41804  ?  57  ILE   D O     1 
ATOM   4409 C  CB    . ILE   D 2 58  ? -9.97081  29.62451  19.07504  1.000 25.85752  ?  57  ILE   D CB    1 
ATOM   4410 C  CG1   . ILE   D 2 58  ? -10.77773 28.85235  18.03960  1.000 28.75221  ?  57  ILE   D CG1   1 
ATOM   4411 C  CG2   . ILE   D 2 58  ? -9.33228  28.66372  20.08078  1.000 20.71058  ?  57  ILE   D CG2   1 
ATOM   4412 C  CD1   . ILE   D 2 58  ? -10.04095 27.71278  17.36395  1.000 25.39576  ?  57  ILE   D CD1   1 
ATOM   4413 N  N     . PRO   D 2 59  ? -10.66627 31.60635  22.01587  1.000 26.99454  ?  58  PRO   D N     1 
ATOM   4414 C  CA    . PRO   D 2 59  ? -10.01185 32.42409  23.04777  1.000 25.62416  ?  58  PRO   D CA    1 
ATOM   4415 C  C     . PRO   D 2 59  ? -8.57958  31.97324  23.30859  1.000 21.98771  ?  58  PRO   D C     1 
ATOM   4416 O  O     . PRO   D 2 59  ? -8.26901  30.77508  23.35369  1.000 23.96913  ?  58  PRO   D O     1 
ATOM   4417 C  CB    . PRO   D 2 59  ? -10.90999 32.22147  24.27848  1.000 26.65414  ?  58  PRO   D CB    1 
ATOM   4418 C  CG    . PRO   D 2 59  ? -12.23174 31.78748  23.73925  1.000 25.65838  ?  58  PRO   D CG    1 
ATOM   4419 C  CD    . PRO   D 2 59  ? -11.95669 31.05179  22.45473  1.000 26.47023  ?  58  PRO   D CD    1 
ATOM   4420 N  N     . GLY   D 2 60  ? -7.69231  32.94965  23.45737  1.000 22.53620  ?  59  GLY   D N     1 
ATOM   4421 C  CA    . GLY   D 2 60  ? -6.27809  32.68076  23.57717  1.000 23.34531  ?  59  GLY   D CA    1 
ATOM   4422 C  C     . GLY   D 2 60  ? -5.52836  32.57344  22.26661  1.000 26.07204  ?  59  GLY   D C     1 
ATOM   4423 O  O     . GLY   D 2 60  ? -4.28677  32.48590  22.28792  1.000 25.84574  ?  59  GLY   D O     1 
ATOM   4424 N  N     . PHE   D 2 61  ? -6.22870  32.58709  21.12391  1.000 24.04071  ?  60  PHE   D N     1 
ATOM   4425 C  CA    . PHE   D 2 61  ? -5.56164  32.42290  19.82654  1.000 22.47489  ?  60  PHE   D CA    1 
ATOM   4426 C  C     . PHE   D 2 61  ? -5.95820  33.48090  18.79210  1.000 23.07362  ?  60  PHE   D C     1 
ATOM   4427 O  O     . PHE   D 2 61  ? -5.12889  34.32447  18.44579  1.000 24.04481  ?  60  PHE   D O     1 
ATOM   4428 C  CB    . PHE   D 2 61  ? -5.81782  31.01565  19.28799  1.000 20.55480  ?  60  PHE   D CB    1 
ATOM   4429 C  CG    . PHE   D 2 61  ? -5.15504  29.95136  20.09996  1.000 24.40577  ?  60  PHE   D CG    1 
ATOM   4430 C  CD1   . PHE   D 2 61  ? -3.80642  29.68590  19.94121  1.000 24.99954  ?  60  PHE   D CD1   1 
ATOM   4431 C  CD2   . PHE   D 2 61  ? -5.85948  29.26077  21.07595  1.000 23.93087  ?  60  PHE   D CD2   1 
ATOM   4432 C  CE1   . PHE   D 2 61  ? -3.17823  28.72657  20.71573  1.000 25.78112  ?  60  PHE   D CE1   1 
ATOM   4433 C  CE2   . PHE   D 2 61  ? -5.24234  28.30750  21.84899  1.000 31.16328  ?  60  PHE   D CE2   1 
ATOM   4434 C  CZ    . PHE   D 2 61  ? -3.88938  28.03321  21.66687  1.000 29.55308  ?  60  PHE   D CZ    1 
ATOM   4435 N  N     . MET   D 2 62  ? -7.19264  33.47387  18.28334  1.000 24.93106  ?  61  MET   D N     1 
ATOM   4436 C  CA    . MET   D 2 62  ? -7.49192  34.40176  17.19660  1.000 22.50703  ?  61  MET   D CA    1 
ATOM   4437 C  C     . MET   D 2 62  ? -8.99201  34.46275  16.94421  1.000 23.69218  ?  61  MET   D C     1 
ATOM   4438 O  O     . MET   D 2 62  ? -9.74249  33.58108  17.36785  1.000 27.11997  ?  61  MET   D O     1 
ATOM   4439 C  CB    . MET   D 2 62  ? -6.75601  33.99970  15.89358  1.000 23.71118  ?  61  MET   D CB    1 
ATOM   4440 C  CG    . MET   D 2 62  ? -7.50639  33.03267  15.00124  1.000 26.58661  ?  61  MET   D CG    1 
ATOM   4441 S  SD    . MET   D 2 62  ? -7.72570  31.38640  15.69361  1.000 29.47757  ?  61  MET   D SD    1 
ATOM   4442 C  CE    . MET   D 2 62  ? -9.32752  31.09539  14.94611  1.000 23.89423  ?  61  MET   D CE    1 
ATOM   4443 N  N     . CYS   D 2 63  ? -9.41684  35.52647  16.25335  1.000 20.64308  ?  62  CYS   D N     1 
ATOM   4444 C  CA    . CYS   D 2 63  ? -10.74977 35.64188  15.66919  1.000 22.26487  ?  62  CYS   D CA    1 
ATOM   4445 C  C     . CYS   D 2 63  ? -10.64119 35.66403  14.14532  1.000 22.07097  ?  62  CYS   D C     1 
ATOM   4446 O  O     . CYS   D 2 63  ? -9.94208  36.51584  13.58103  1.000 21.00311  ?  62  CYS   D O     1 
ATOM   4447 C  CB    . CYS   D 2 63  ? -11.47306 36.91563  16.12593  1.000 23.45716  ?  62  CYS   D CB    1 
ATOM   4448 S  SG    . CYS   D 2 63  ? -11.47002 37.18620  17.92574  1.000 29.79630  ?  62  CYS   D SG    1 
ATOM   4449 N  N     . GLN   D 2 64  ? -11.40002 34.79707  13.48338  1.000 21.97164  ?  63  GLN   D N     1 
ATOM   4450 C  CA    . GLN   D 2 64  ? -11.29935 34.61214  12.03663  1.000 21.29972  ?  63  GLN   D CA    1 
ATOM   4451 C  C     . GLN   D 2 64  ? -12.64671 34.87241  11.37562  1.000 20.06631  ?  63  GLN   D C     1 
ATOM   4452 O  O     . GLN   D 2 64  ? -13.70468 34.49988  11.91243  1.000 23.59845  ?  63  GLN   D O     1 
ATOM   4453 C  CB    . GLN   D 2 64  ? -10.78724 33.19614  11.72517  1.000 20.10078  ?  63  GLN   D CB    1 
ATOM   4454 C  CG    . GLN   D 2 64  ? -10.71647 32.80656  10.20581  1.000 22.44172  ?  63  GLN   D CG    1 
ATOM   4455 C  CD    . GLN   D 2 64  ? -10.22550 31.37364  9.97867   1.000 24.10949  ?  63  GLN   D CD    1 
ATOM   4456 O  OE1   . GLN   D 2 64  ? -9.62076  30.75987  10.87435  1.000 24.33294  ?  63  GLN   D OE1   1 
ATOM   4457 N  NE2   . GLN   D 2 64  ? -10.48272 30.83172  8.77905   1.000 25.27000  ?  63  GLN   D NE2   1 
ATOM   4458 N  N     . GLY   D 2 65  ? -12.60819 35.54678  10.22362  1.000 22.22295  ?  64  GLY   D N     1 
ATOM   4459 C  CA    . GLY   D 2 65  ? -13.81432 35.88602  9.49969   1.000 21.84649  ?  64  GLY   D CA    1 
ATOM   4460 C  C     . GLY   D 2 65  ? -13.56599 36.09965  8.02281   1.000 24.83683  ?  64  GLY   D C     1 
ATOM   4461 O  O     . GLY   D 2 65  ? -12.56029 35.62762  7.46921   1.000 24.14028  ?  64  GLY   D O     1 
ATOM   4462 N  N     . GLY   D 2 66  ? -14.49703 36.76735  7.36082   1.000 25.84398  ?  65  GLY   D N     1 
ATOM   4463 C  CA    . GLY   D 2 66  ? -14.28519 37.19904  6.00346   1.000 24.01059  ?  65  GLY   D CA    1 
ATOM   4464 C  C     . GLY   D 2 66  ? -14.92944 36.37832  4.91034   1.000 26.81582  ?  65  GLY   D C     1 
ATOM   4465 O  O     . GLY   D 2 66  ? -14.66586 36.65867  3.73311   1.000 29.30402  ?  65  GLY   D O     1 
ATOM   4466 N  N     . ASP   D 2 67  ? -15.74797 35.37576  5.24006   1.000 21.98555  ?  66  ASP   D N     1 
ATOM   4467 C  CA    . ASP   D 2 67  ? -16.42749 34.57689  4.21236   1.000 27.74706  ?  66  ASP   D CA    1 
ATOM   4468 C  C     . ASP   D 2 67  ? -17.73824 35.26567  3.85168   1.000 30.12297  ?  66  ASP   D C     1 
ATOM   4469 O  O     . ASP   D 2 67  ? -18.78837 34.97754  4.41382   1.000 30.15291  ?  66  ASP   D O     1 
ATOM   4470 C  CB    . ASP   D 2 67  ? -16.67740 33.14492  4.67623   1.000 28.42680  ?  66  ASP   D CB    1 
ATOM   4471 C  CG    . ASP   D 2 67  ? -17.52755 32.33690  3.68268   1.000 31.83771  ?  66  ASP   D CG    1 
ATOM   4472 O  OD1   . ASP   D 2 67  ? -17.79210 32.84317  2.56513   1.000 28.90991  ?  66  ASP   D OD1   1 
ATOM   4473 O  OD2   . ASP   D 2 67  ? -17.89968 31.17725  4.01449   1.000 32.01724  -1 66  ASP   D OD2   1 
ATOM   4474 N  N     . PHE   D 2 68  ? -17.68583 36.15807  2.87052   1.000 28.40819  ?  67  PHE   D N     1 
ATOM   4475 C  CA    . PHE   D 2 68  ? -18.88632 36.85248  2.42817   1.000 31.09835  ?  67  PHE   D CA    1 
ATOM   4476 C  C     . PHE   D 2 68  ? -19.57382 36.18457  1.23954   1.000 31.14076  ?  67  PHE   D C     1 
ATOM   4477 O  O     . PHE   D 2 68  ? -20.58387 36.70858  0.77026   1.000 31.72498  ?  67  PHE   D O     1 
ATOM   4478 C  CB    . PHE   D 2 68  ? -18.56725 38.31101  2.07496   1.000 27.26788  ?  67  PHE   D CB    1 
ATOM   4479 C  CG    . PHE   D 2 68  ? -17.53135 38.47410  1.00019   1.000 31.55514  ?  67  PHE   D CG    1 
ATOM   4480 C  CD1   . PHE   D 2 68  ? -17.88960 38.44187  -0.34778  1.000 30.46818  ?  67  PHE   D CD1   1 
ATOM   4481 C  CD2   . PHE   D 2 68  ? -16.20349 38.70393  1.32761   1.000 28.93510  ?  67  PHE   D CD2   1 
ATOM   4482 C  CE1   . PHE   D 2 68  ? -16.93359 38.59453  -1.32545  1.000 32.23471  ?  67  PHE   D CE1   1 
ATOM   4483 C  CE2   . PHE   D 2 68  ? -15.25035 38.86123  0.35285   1.000 30.82184  ?  67  PHE   D CE2   1 
ATOM   4484 C  CZ    . PHE   D 2 68  ? -15.60956 38.80614  -0.98161  1.000 30.47448  ?  67  PHE   D CZ    1 
ATOM   4485 N  N     . THR   D 2 69  ? -19.05123 35.07191  0.71330   1.000 31.34166  ?  68  THR   D N     1 
ATOM   4486 C  CA    . THR   D 2 69  ? -19.70125 34.43894  -0.43252  1.000 30.01834  ?  68  THR   D CA    1 
ATOM   4487 C  C     . THR   D 2 69  ? -20.59086 33.27099  -0.03862  1.000 34.75472  ?  68  THR   D C     1 
ATOM   4488 O  O     . THR   D 2 69  ? -21.64547 33.07100  -0.65116  1.000 31.53589  ?  68  THR   D O     1 
ATOM   4489 C  CB    . THR   D 2 69  ? -18.67160 33.95793  -1.46961  1.000 33.15896  ?  68  THR   D CB    1 
ATOM   4490 O  OG1   . THR   D 2 69  ? -17.86839 32.91482  -0.90784  1.000 30.09376  ?  68  THR   D OG1   1 
ATOM   4491 C  CG2   . THR   D 2 69  ? -17.76922 35.09471  -1.90993  1.000 33.30641  ?  68  THR   D CG2   1 
ATOM   4492 N  N     . ARG   D 2 70  ? -20.18929 32.47992  0.95573   1.000 31.66404  ?  69  ARG   D N     1 
ATOM   4493 C  CA    . ARG   D 2 70  ? -21.02042 31.38898  1.43101   1.000 31.65905  ?  69  ARG   D CA    1 
ATOM   4494 C  C     . ARG   D 2 70  ? -21.48553 31.54665  2.87379   1.000 32.19837  ?  69  ARG   D C     1 
ATOM   4495 O  O     . ARG   D 2 70  ? -22.40362 30.83377  3.28145   1.000 33.54489  ?  69  ARG   D O     1 
ATOM   4496 C  CB    . ARG   D 2 70  ? -20.27983 30.05120  1.29817   1.000 31.10525  ?  69  ARG   D CB    1 
ATOM   4497 C  CG    . ARG   D 2 70  ? -19.56351 29.86259  -0.02227  1.000 36.83659  ?  69  ARG   D CG    1 
ATOM   4498 C  CD    . ARG   D 2 70  ? -19.48843 28.40069  -0.38111  1.000 41.16452  ?  69  ARG   D CD    1 
ATOM   4499 N  NE    . ARG   D 2 70  ? -18.74192 28.19094  -1.60996  1.000 40.34779  ?  69  ARG   D NE    1 
ATOM   4500 C  CZ    . ARG   D 2 70  ? -17.57885 27.56087  -1.69104  1.000 46.85072  ?  69  ARG   D CZ    1 
ATOM   4501 N  NH1   . ARG   D 2 70  ? -17.02963 26.97725  -0.63243  1.000 39.04607  ?  69  ARG   D NH1   1 
ATOM   4502 N  NH2   . ARG   D 2 70  ? -16.95203 27.50777  -2.86773  1.000 56.82561  ?  69  ARG   D NH2   1 
ATOM   4503 N  N     . HIS   D 2 71  ? -20.88032 32.44454  3.65276   1.000 33.09516  ?  70  HIS   D N     1 
ATOM   4504 C  CA    . HIS   D 2 71  ? -21.30283 32.72968  5.03488   1.000 34.73601  ?  70  HIS   D CA    1 
ATOM   4505 C  C     . HIS   D 2 71  ? -21.31887 31.47346  5.90346   1.000 32.15649  ?  70  HIS   D C     1 
ATOM   4506 O  O     . HIS   D 2 71  ? -22.18656 31.31383  6.76451   1.000 33.46472  ?  70  HIS   D O     1 
ATOM   4507 C  CB    . HIS   D 2 71  ? -22.67887 33.40635  5.07327   1.000 29.37263  ?  70  HIS   D CB    1 
ATOM   4508 C  CG    . HIS   D 2 71  ? -22.74891 34.69477  4.31625   1.000 33.93775  ?  70  HIS   D CG    1 
ATOM   4509 N  ND1   . HIS   D 2 71  ? -22.31855 35.89385  4.84279   1.000 37.49824  ?  70  HIS   D ND1   1 
ATOM   4510 C  CD2   . HIS   D 2 71  ? -23.20185 34.97399  3.07046   1.000 37.85197  ?  70  HIS   D CD2   1 
ATOM   4511 C  CE1   . HIS   D 2 71  ? -22.49669 36.85584  3.95530   1.000 33.86396  ?  70  HIS   D CE1   1 
ATOM   4512 N  NE2   . HIS   D 2 71  ? -23.02759 36.32398  2.86937   1.000 35.60793  ?  70  HIS   D NE2   1 
ATOM   4513 N  N     . ASN   D 2 72  ? -20.35055 30.57350  5.69095   1.000 31.40639  ?  71  ASN   D N     1 
ATOM   4514 C  CA    . ASN   D 2 72  ? -20.30409 29.35954  6.50176   1.000 35.11010  ?  71  ASN   D CA    1 
ATOM   4515 C  C     . ASN   D 2 72  ? -18.87106 28.90720  6.81230   1.000 31.45136  ?  71  ASN   D C     1 
ATOM   4516 O  O     . ASN   D 2 72  ? -18.66293 27.75528  7.22936   1.000 29.15875  ?  71  ASN   D O     1 
ATOM   4517 C  CB    . ASN   D 2 72  ? -21.10712 28.22267  5.82595   1.000 27.28022  ?  71  ASN   D CB    1 
ATOM   4518 C  CG    . ASN   D 2 72  ? -20.51212 27.75676  4.48317   1.000 34.72442  ?  71  ASN   D CG    1 
ATOM   4519 O  OD1   . ASN   D 2 72  ? -19.36743 28.06407  4.11793   1.000 29.17539  ?  71  ASN   D OD1   1 
ATOM   4520 N  ND2   . ASN   D 2 72  ? -21.30085 26.96403  3.75453   1.000 38.28933  ?  71  ASN   D ND2   1 
ATOM   4521 N  N     . GLY   D 2 73  ? -17.87810 29.77347  6.61572   1.000 28.79884  ?  72  GLY   D N     1 
ATOM   4522 C  CA    . GLY   D 2 73  ? -16.50296 29.42907  6.91517   1.000 26.72889  ?  72  GLY   D CA    1 
ATOM   4523 C  C     . GLY   D 2 73  ? -15.74286 28.75708  5.79615   1.000 26.80258  ?  72  GLY   D C     1 
ATOM   4524 O  O     . GLY   D 2 73  ? -14.52843 28.56914  5.92476   1.000 28.39100  ?  72  GLY   D O     1 
ATOM   4525 N  N     . THR   D 2 74  ? -16.40395 28.39479  4.69094   1.000 25.27908  ?  73  THR   D N     1 
ATOM   4526 C  CA    . THR   D 2 74  ? -15.71822 27.70753  3.59958   1.000 26.29025  ?  73  THR   D CA    1 
ATOM   4527 C  C     . THR   D 2 74  ? -15.41918 28.60309  2.40580   1.000 30.12291  ?  73  THR   D C     1 
ATOM   4528 O  O     . THR   D 2 74  ? -14.64349 28.19217  1.53212   1.000 32.06782  ?  73  THR   D O     1 
ATOM   4529 C  CB    . THR   D 2 74  ? -16.53613 26.49749  3.10691   1.000 29.21555  ?  73  THR   D CB    1 
ATOM   4530 O  OG1   . THR   D 2 74  ? -17.67480 26.94563  2.35488   1.000 29.98763  ?  73  THR   D OG1   1 
ATOM   4531 C  CG2   . THR   D 2 74  ? -16.98279 25.63895  4.28544   1.000 26.75242  ?  73  THR   D CG2   1 
ATOM   4532 N  N     . GLY   D 2 75  ? -16.00118 29.80328  2.35159   1.000 30.55910  ?  74  GLY   D N     1 
ATOM   4533 C  CA    . GLY   D 2 75  ? -15.96779 30.62692  1.15539   1.000 32.15621  ?  74  GLY   D CA    1 
ATOM   4534 C  C     . GLY   D 2 75  ? -15.05192 31.83265  1.19644   1.000 32.79191  ?  74  GLY   D C     1 
ATOM   4535 O  O     . GLY   D 2 75  ? -14.02206 31.82287  1.88644   1.000 29.56591  ?  74  GLY   D O     1 
ATOM   4536 N  N     . GLY   D 2 76  ? -15.41833 32.86565  0.44299   1.000 31.26730  ?  75  GLY   D N     1 
ATOM   4537 C  CA    . GLY   D 2 76  ? -14.65149 34.07204  0.23288   1.000 28.34046  ?  75  GLY   D CA    1 
ATOM   4538 C  C     . GLY   D 2 76  ? -13.96005 34.09097  -1.13409  1.000 28.32145  ?  75  GLY   D C     1 
ATOM   4539 O  O     . GLY   D 2 76  ? -13.82019 33.06432  -1.80686  1.000 30.44661  ?  75  GLY   D O     1 
ATOM   4540 N  N     . LYS   D 2 77  ? -13.52683 35.28902  -1.54111  1.000 27.14418  ?  76  LYS   D N     1 
ATOM   4541 C  CA    . LYS   D 2 77  ? -12.84218 35.47133  -2.82302  1.000 27.79233  ?  76  LYS   D CA    1 
ATOM   4542 C  C     . LYS   D 2 77  ? -12.10051 36.79595  -2.78632  1.000 28.86479  ?  76  LYS   D C     1 
ATOM   4543 O  O     . LYS   D 2 77  ? -12.54095 37.73373  -2.12321  1.000 30.32299  ?  76  LYS   D O     1 
ATOM   4544 C  CB    . LYS   D 2 77  ? -13.82066 35.44195  -4.02079  1.000 26.21810  ?  76  LYS   D CB    1 
ATOM   4545 C  CG    . LYS   D 2 77  ? -14.70695 36.67108  -4.18583  1.000 29.29899  ?  76  LYS   D CG    1 
ATOM   4546 C  CD    . LYS   D 2 77  ? -15.78328 36.42066  -5.25178  1.000 36.19607  ?  76  LYS   D CD    1 
ATOM   4547 C  CE    . LYS   D 2 77  ? -16.70164 37.62957  -5.45636  1.000 35.97637  ?  76  LYS   D CE    1 
ATOM   4548 N  NZ    . LYS   D 2 77  ? -17.79588 37.31933  -6.42724  1.000 36.02957  ?  76  LYS   D NZ    1 
ATOM   4549 N  N     . SER   D 2 78  ? -10.97577 36.86777  -3.50603  1.000 25.12418  ?  77  SER   D N     1 
ATOM   4550 C  CA    . SER   D 2 78  ? -10.21025 38.10346  -3.56015  1.000 25.75713  ?  77  SER   D CA    1 
ATOM   4551 C  C     . SER   D 2 78  ? -10.71305 38.99353  -4.69790  1.000 29.14910  ?  77  SER   D C     1 
ATOM   4552 O  O     . SER   D 2 78  ? -11.53897 38.58900  -5.52619  1.000 29.79924  ?  77  SER   D O     1 
ATOM   4553 C  CB    . SER   D 2 78  ? -8.71906  37.82240  -3.73592  1.000 29.47116  ?  77  SER   D CB    1 
ATOM   4554 O  OG    . SER   D 2 78  ? -8.36842  37.58825  -5.10903  1.000 29.07988  ?  77  SER   D OG    1 
ATOM   4555 N  N     . ILE   D 2 79  ? -10.20615 40.22982  -4.72464  1.000 30.26134  ?  78  ILE   D N     1 
ATOM   4556 C  CA    . ILE   D 2 79  ? -10.48799 41.12485  -5.84521  1.000 31.97094  ?  78  ILE   D CA    1 
ATOM   4557 C  C     . ILE   D 2 79  ? -9.71266  40.75180  -7.09699  1.000 33.07855  ?  78  ILE   D C     1 
ATOM   4558 O  O     . ILE   D 2 79  ? -9.89939  41.39718  -8.13167  1.000 29.87495  ?  78  ILE   D O     1 
ATOM   4559 C  CB    . ILE   D 2 79  ? -10.15171 42.59607  -5.54136  1.000 26.97028  ?  78  ILE   D CB    1 
ATOM   4560 C  CG1   . ILE   D 2 79  ? -8.64000  42.74891  -5.33702  1.000 28.59943  ?  78  ILE   D CG1   1 
ATOM   4561 C  CG2   . ILE   D 2 79  ? -10.99070 43.12674  -4.37815  1.000 30.42341  ?  78  ILE   D CG2   1 
ATOM   4562 C  CD1   . ILE   D 2 79  ? -8.13159  44.19556  -5.33817  1.000 29.69813  ?  78  ILE   D CD1   1 
ATOM   4563 N  N     . TYR   D 2 80  ? -8.82542  39.75647  -7.03133  1.000 30.10035  ?  79  TYR   D N     1 
ATOM   4564 C  CA    . TYR   D 2 80  ? -8.05066  39.33801  -8.19469  1.000 32.86163  ?  79  TYR   D CA    1 
ATOM   4565 C  C     . TYR   D 2 80  ? -8.54210  38.03449  -8.81023  1.000 31.48065  ?  79  TYR   D C     1 
ATOM   4566 O  O     . TYR   D 2 80  ? -7.88008  37.49998  -9.70872  1.000 31.48895  ?  79  TYR   D O     1 
ATOM   4567 C  CB    . TYR   D 2 80  ? -6.57799  39.17089  -7.83094  1.000 28.89205  ?  79  TYR   D CB    1 
ATOM   4568 C  CG    . TYR   D 2 80  ? -6.01717  40.28286  -7.01098  1.000 32.52095  ?  79  TYR   D CG    1 
ATOM   4569 C  CD1   . TYR   D 2 80  ? -5.80103  41.53507  -7.56663  1.000 25.26440  ?  79  TYR   D CD1   1 
ATOM   4570 C  CD2   . TYR   D 2 80  ? -5.69117  40.08079  -5.65736  1.000 28.43450  ?  79  TYR   D CD2   1 
ATOM   4571 C  CE1   . TYR   D 2 80  ? -5.28295  42.55573  -6.81912  1.000 30.98553  ?  79  TYR   D CE1   1 
ATOM   4572 C  CE2   . TYR   D 2 80  ? -5.16439  41.10335  -4.89488  1.000 27.69690  ?  79  TYR   D CE2   1 
ATOM   4573 C  CZ    . TYR   D 2 80  ? -4.96600  42.33592  -5.48078  1.000 28.55238  ?  79  TYR   D CZ    1 
ATOM   4574 O  OH    . TYR   D 2 80  ? -4.44815  43.36066  -4.75021  1.000 27.00101  ?  79  TYR   D OH    1 
ATOM   4575 N  N     . GLY   D 2 81  ? -9.67892  37.52380  -8.36303  1.000 28.65972  ?  80  GLY   D N     1 
ATOM   4576 C  CA    . GLY   D 2 81  ? -10.10258 36.16634  -8.63795  1.000 32.88631  ?  80  GLY   D CA    1 
ATOM   4577 C  C     . GLY   D 2 81  ? -10.35150 35.41880  -7.34583  1.000 33.69342  ?  80  GLY   D C     1 
ATOM   4578 O  O     . GLY   D 2 81  ? -10.18219 35.95057  -6.24934  1.000 31.73499  ?  80  GLY   D O     1 
ATOM   4579 N  N     . GLU   D 2 82  ? -10.73444 34.14210  -7.48539  1.000 29.96584  ?  81  GLU   D N     1 
ATOM   4580 C  CA    . GLU   D 2 82  ? -11.08479 33.37394  -6.29339  1.000 34.99593  ?  81  GLU   D CA    1 
ATOM   4581 C  C     . GLU   D 2 82  ? -9.93768  33.37273  -5.28470  1.000 31.53427  ?  81  GLU   D C     1 
ATOM   4582 O  O     . GLU   D 2 82  ? -10.13492 33.64538  -4.09142  1.000 33.63279  ?  81  GLU   D O     1 
ATOM   4583 C  CB    . GLU   D 2 82  ? -11.46934 31.93891  -6.65704  1.000 32.22398  ?  81  GLU   D CB    1 
ATOM   4584 C  CG    . GLU   D 2 82  ? -11.75487 31.10665  -5.37761  1.000 42.01664  ?  81  GLU   D CG    1 
ATOM   4585 C  CD    . GLU   D 2 82  ? -12.24470 29.66923  -5.62281  1.000 47.25339  ?  81  GLU   D CD    1 
ATOM   4586 O  OE1   . GLU   D 2 82  ? -11.67669 28.94571  -6.47928  1.000 45.46647  ?  81  GLU   D OE1   1 
ATOM   4587 O  OE2   . GLU   D 2 82  ? -13.21041 29.26464  -4.93324  1.000 49.21383  -1 81  GLU   D OE2   1 
ATOM   4588 N  N     . LYS   D 2 83  ? -8.73048  33.07373  -5.75324  1.000 25.90996  ?  82  LYS   D N     1 
ATOM   4589 C  CA    . LYS   D 2 83  ? -7.55068  32.92970  -4.92499  1.000 29.22158  ?  82  LYS   D CA    1 
ATOM   4590 C  C     . LYS   D 2 83  ? -6.40089  33.71439  -5.54342  1.000 30.75871  ?  82  LYS   D C     1 
ATOM   4591 O  O     . LYS   D 2 83  ? -6.42187  34.03419  -6.72985  1.000 33.05242  ?  82  LYS   D O     1 
ATOM   4592 C  CB    . LYS   D 2 83  ? -7.19567  31.44776  -4.76743  1.000 30.84105  ?  82  LYS   D CB    1 
ATOM   4593 C  CG    . LYS   D 2 83  ? -8.20050  30.70816  -3.88543  1.000 34.63830  ?  82  LYS   D CG    1 
ATOM   4594 C  CD    . LYS   D 2 83  ? -8.17613  29.20916  -4.04734  1.000 45.35029  ?  82  LYS   D CD    1 
ATOM   4595 C  CE    . LYS   D 2 83  ? -9.21168  28.57156  -3.10844  1.000 46.61443  ?  82  LYS   D CE    1 
ATOM   4596 N  NZ    . LYS   D 2 83  ? -9.89046  27.38092  -3.71704  1.000 53.11720  ?  82  LYS   D NZ    1 
ATOM   4597 N  N     . PHE   D 2 84  ? -5.40136  34.04719  -4.72344  1.000 29.45391  ?  83  PHE   D N     1 
ATOM   4598 C  CA    . PHE   D 2 84  ? -4.18170  34.68270  -5.20803  1.000 29.13016  ?  83  PHE   D CA    1 
ATOM   4599 C  C     . PHE   D 2 84  ? -3.01860  34.22302  -4.34568  1.000 32.89046  ?  83  PHE   D C     1 
ATOM   4600 O  O     . PHE   D 2 84  ? -3.20990  33.65846  -3.26681  1.000 26.68351  ?  83  PHE   D O     1 
ATOM   4601 C  CB    . PHE   D 2 84  ? -4.26385  36.23145  -5.24697  1.000 30.07407  ?  83  PHE   D CB    1 
ATOM   4602 C  CG    . PHE   D 2 84  ? -4.37521  36.92391  -3.88889  1.000 28.22909  ?  83  PHE   D CG    1 
ATOM   4603 C  CD1   . PHE   D 2 84  ? -5.57760  36.96524  -3.20226  1.000 25.13312  ?  83  PHE   D CD1   1 
ATOM   4604 C  CD2   . PHE   D 2 84  ? -3.29904  37.61764  -3.36566  1.000 26.33140  ?  83  PHE   D CD2   1 
ATOM   4605 C  CE1   . PHE   D 2 84  ? -5.70302  37.65162  -1.99649  1.000 29.21052  ?  83  PHE   D CE1   1 
ATOM   4606 C  CE2   . PHE   D 2 84  ? -3.40405  38.30143  -2.13806  1.000 25.39584  ?  83  PHE   D CE2   1 
ATOM   4607 C  CZ    . PHE   D 2 84  ? -4.60126  38.31835  -1.46442  1.000 28.32715  ?  83  PHE   D CZ    1 
ATOM   4608 N  N     . GLU   D 2 85  ? -1.81013  34.46947  -4.84361  1.000 25.83422  ?  84  GLU   D N     1 
ATOM   4609 C  CA    . GLU   D 2 85  ? -0.61780  33.84607  -4.30501  1.000 26.88743  ?  84  GLU   D CA    1 
ATOM   4610 C  C     . GLU   D 2 85  ? -0.17240  34.50375  -2.98520  1.000 26.44725  ?  84  GLU   D C     1 
ATOM   4611 O  O     . GLU   D 2 85  ? -0.58426  35.60809  -2.63164  1.000 25.31803  ?  84  GLU   D O     1 
ATOM   4612 C  CB    . GLU   D 2 85  ? 0.50540   33.90591  -5.35008  1.000 25.95193  ?  84  GLU   D CB    1 
ATOM   4613 C  CG    . GLU   D 2 85  ? 0.92292   35.31861  -5.74448  1.000 29.88426  ?  84  GLU   D CG    1 
ATOM   4614 C  CD    . GLU   D 2 85  ? -0.10016  36.05699  -6.64025  1.000 40.74237  ?  84  GLU   D CD    1 
ATOM   4615 O  OE1   . GLU   D 2 85  ? -0.98366  35.41172  -7.27297  1.000 35.61105  ?  84  GLU   D OE1   1 
ATOM   4616 O  OE2   . GLU   D 2 85  ? -0.01248  37.30336  -6.70126  1.000 43.28356  -1 84  GLU   D OE2   1 
ATOM   4617 N  N     . ASP   D 2 86  ? 0.69330   33.79924  -2.26112  1.000 27.17304  ?  85  ASP   D N     1 
ATOM   4618 C  CA    . ASP   D 2 86  ? 1.32120   34.35354  -1.06180  1.000 27.18205  ?  85  ASP   D CA    1 
ATOM   4619 C  C     . ASP   D 2 86  ? 2.32667   35.42995  -1.46851  1.000 32.44013  ?  85  ASP   D C     1 
ATOM   4620 O  O     . ASP   D 2 86  ? 3.34554   35.12433  -2.11020  1.000 30.90868  ?  85  ASP   D O     1 
ATOM   4621 C  CB    . ASP   D 2 86  ? 2.00467   33.24270  -0.26979  1.000 25.64026  ?  85  ASP   D CB    1 
ATOM   4622 C  CG    . ASP   D 2 86  ? 1.02974   32.19550  0.24652   1.000 28.25803  ?  85  ASP   D CG    1 
ATOM   4623 O  OD1   . ASP   D 2 86  ? -0.00710  32.57570  0.84251   1.000 25.32980  ?  85  ASP   D OD1   1 
ATOM   4624 O  OD2   . ASP   D 2 86  ? 1.29719   30.97839  0.06481   1.000 28.41503  -1 85  ASP   D OD2   1 
ATOM   4625 N  N     . GLU   D 2 87  ? 2.04640   36.68876  -1.09323  1.000 25.81746  ?  86  GLU   D N     1 
ATOM   4626 C  CA    . GLU   D 2 87  ? 2.83622   37.81574  -1.58945  1.000 26.55473  ?  86  GLU   D CA    1 
ATOM   4627 C  C     . GLU   D 2 87  ? 4.26039   37.77837  -1.04663  1.000 33.21574  ?  86  GLU   D C     1 
ATOM   4628 O  O     . GLU   D 2 87  ? 5.22603   37.86007  -1.81790  1.000 30.47298  ?  86  GLU   D O     1 
ATOM   4629 C  CB    . GLU   D 2 87  ? 2.14125   39.12965  -1.23340  1.000 27.23354  ?  86  GLU   D CB    1 
ATOM   4630 C  CG    . GLU   D 2 87  ? 2.73668   40.36927  -1.86704  1.000 25.95366  ?  86  GLU   D CG    1 
ATOM   4631 C  CD    . GLU   D 2 87  ? 1.85428   41.61152  -1.72253  1.000 29.22896  ?  86  GLU   D CD    1 
ATOM   4632 O  OE1   . GLU   D 2 87  ? 0.79702   41.56448  -1.04337  1.000 29.19676  ?  86  GLU   D OE1   1 
ATOM   4633 O  OE2   . GLU   D 2 87  ? 2.21130   42.66159  -2.30443  1.000 33.43121  -1 86  GLU   D OE2   1 
ATOM   4634 N  N     . ASN   D 2 88  ? 4.41088   37.68258  0.27761   1.000 23.97833  ?  87  ASN   D N     1 
ATOM   4635 C  CA    . ASN   D 2 88  ? 5.67791   37.43109  0.95019   1.000 22.07336  ?  87  ASN   D CA    1 
ATOM   4636 C  C     . ASN   D 2 88  ? 5.40212   37.07402  2.40762   1.000 25.70781  ?  87  ASN   D C     1 
ATOM   4637 O  O     . ASN   D 2 88  ? 4.28005   37.20718  2.90484   1.000 20.88429  ?  87  ASN   D O     1 
ATOM   4638 C  CB    . ASN   D 2 88  ? 6.64306   38.62057  0.86204   1.000 24.68738  ?  87  ASN   D CB    1 
ATOM   4639 C  CG    . ASN   D 2 88  ? 6.15033   39.83871  1.58240   1.000 23.67974  ?  87  ASN   D CG    1 
ATOM   4640 O  OD1   . ASN   D 2 88  ? 6.00946   39.84377  2.81391   1.000 27.24241  ?  87  ASN   D OD1   1 
ATOM   4641 N  ND2   . ASN   D 2 88  ? 5.91963   40.90505  0.83313   1.000 25.16872  ?  87  ASN   D ND2   1 
ATOM   4642 N  N     . PHE   D 2 89  ? 6.43512   36.59833  3.08912   1.000 24.10340  ?  88  PHE   D N     1 
ATOM   4643 C  CA    . PHE   D 2 89  ? 6.28947   36.25683  4.49248   1.000 24.52015  ?  88  PHE   D CA    1 
ATOM   4644 C  C     . PHE   D 2 89  ? 7.23942   37.08907  5.34279   1.000 23.86584  ?  88  PHE   D C     1 
ATOM   4645 O  O     . PHE   D 2 89  ? 7.81730   36.58608  6.30034   1.000 27.30031  ?  88  PHE   D O     1 
ATOM   4646 C  CB    . PHE   D 2 89  ? 6.51275   34.76071  4.72260   1.000 23.86336  ?  88  PHE   D CB    1 
ATOM   4647 C  CG    . PHE   D 2 89  ? 5.50555   33.88448  4.03776   1.000 31.56867  ?  88  PHE   D CG    1 
ATOM   4648 C  CD1   . PHE   D 2 89  ? 4.19196   33.79780  4.50538   1.000 24.88178  ?  88  PHE   D CD1   1 
ATOM   4649 C  CD2   . PHE   D 2 89  ? 5.87041   33.13366  2.92223   1.000 28.78102  ?  88  PHE   D CD2   1 
ATOM   4650 C  CE1   . PHE   D 2 89  ? 3.28063   32.99461  3.85985   1.000 27.84070  ?  88  PHE   D CE1   1 
ATOM   4651 C  CE2   . PHE   D 2 89  ? 4.96576   32.31440  2.29144   1.000 30.13824  ?  88  PHE   D CE2   1 
ATOM   4652 C  CZ    . PHE   D 2 89  ? 3.66939   32.24222  2.75013   1.000 32.62351  ?  88  PHE   D CZ    1 
ATOM   4653 N  N     . ILE   D 2 90  ? 7.44544   38.34920  4.94545   1.000 27.05345  ?  89  ILE   D N     1 
ATOM   4654 C  CA    . ILE   D 2 90  ? 8.39143   39.22061  5.63803   1.000 26.11195  ?  89  ILE   D CA    1 
ATOM   4655 C  C     . ILE   D 2 90  ? 7.97213   39.39718  7.09031   1.000 27.33817  ?  89  ILE   D C     1 
ATOM   4656 O  O     . ILE   D 2 90  ? 8.75990   39.16509  8.01274   1.000 28.95747  ?  89  ILE   D O     1 
ATOM   4657 C  CB    . ILE   D 2 90  ? 8.50807   40.57767  4.91737   1.000 24.93199  ?  89  ILE   D CB    1 
ATOM   4658 C  CG1   . ILE   D 2 90  ? 9.23178   40.42694  3.56459   1.000 24.44358  ?  89  ILE   D CG1   1 
ATOM   4659 C  CG2   . ILE   D 2 90  ? 9.26268   41.59879  5.79179   1.000 33.16325  ?  89  ILE   D CG2   1 
ATOM   4660 C  CD1   . ILE   D 2 90  ? 9.13830   41.65297  2.74288   1.000 29.06790  ?  89  ILE   D CD1   1 
ATOM   4661 N  N     . LEU   D 2 91  ? 6.71224   39.76626  7.30456   1.000 28.67787  ?  90  LEU   D N     1 
ATOM   4662 C  CA    . LEU   D 2 91  ? 6.17738   40.11541  8.61780   1.000 26.88702  ?  90  LEU   D CA    1 
ATOM   4663 C  C     . LEU   D 2 91  ? 5.71368   38.87241  9.36760   1.000 28.57279  ?  90  LEU   D C     1 
ATOM   4664 O  O     . LEU   D 2 91  ? 5.27602   37.88143  8.76871   1.000 25.45341  ?  90  LEU   D O     1 
ATOM   4665 C  CB    . LEU   D 2 91  ? 5.02008   41.10268  8.46105   1.000 26.05876  ?  90  LEU   D CB    1 
ATOM   4666 C  CG    . LEU   D 2 91  ? 5.42376   42.42934  7.80986   1.000 30.52362  ?  90  LEU   D CG    1 
ATOM   4667 C  CD1   . LEU   D 2 91  ? 4.21753   43.27672  7.57540   1.000 31.90168  ?  90  LEU   D CD1   1 
ATOM   4668 C  CD2   . LEU   D 2 91  ? 6.43278   43.18321  8.64119   1.000 35.61406  ?  90  LEU   D CD2   1 
ATOM   4669 N  N     . LYS   D 2 92  ? 5.80906   38.93338  10.69514  1.000 26.58039  ?  91  LYS   D N     1 
ATOM   4670 C  CA    . LYS   D 2 92  ? 5.64916   37.75924  11.52734  1.000 27.98449  ?  91  LYS   D CA    1 
ATOM   4671 C  C     . LYS   D 2 92  ? 4.47874   37.94852  12.48947  1.000 27.58743  ?  91  LYS   D C     1 
ATOM   4672 O  O     . LYS   D 2 92  ? 3.98086   39.05949  12.68515  1.000 24.48486  ?  91  LYS   D O     1 
ATOM   4673 C  CB    . LYS   D 2 92  ? 6.93292   37.46325  12.30814  1.000 30.54167  ?  91  LYS   D CB    1 
ATOM   4674 C  CG    . LYS   D 2 92  ? 8.21179   37.41256  11.47769  1.000 34.64788  ?  91  LYS   D CG    1 
ATOM   4675 C  CD    . LYS   D 2 92  ? 8.24862   36.19319  10.58722  1.000 30.48372  ?  91  LYS   D CD    1 
ATOM   4676 C  CE    . LYS   D 2 92  ? 9.66665   35.93880  10.07410  1.000 35.22554  ?  91  LYS   D CE    1 
ATOM   4677 N  NZ    . LYS   D 2 92  ? 9.67723   35.64315  8.60603   1.000 38.21745  ?  91  LYS   D NZ    1 
ATOM   4678 N  N     . HIS   D 2 93  ? 4.02442   36.83326  13.06722  1.000 22.91879  ?  92  HIS   D N     1 
ATOM   4679 C  CA    . HIS   D 2 93  ? 2.86918   36.83782  13.96751  1.000 22.65465  ?  92  HIS   D CA    1 
ATOM   4680 C  C     . HIS   D 2 93  ? 3.40767   37.08882  15.37579  1.000 23.19787  ?  92  HIS   D C     1 
ATOM   4681 O  O     . HIS   D 2 93  ? 3.61931   36.16945  16.16930  1.000 28.60464  ?  92  HIS   D O     1 
ATOM   4682 C  CB    . HIS   D 2 93  ? 2.09612   35.52490  13.87509  1.000 20.97557  ?  92  HIS   D CB    1 
ATOM   4683 C  CG    . HIS   D 2 93  ? 1.52358   35.22825  12.50843  1.000 20.50251  ?  92  HIS   D CG    1 
ATOM   4684 N  ND1   . HIS   D 2 93  ? 2.26548   34.65731  11.49365  1.000 23.11855  ?  92  HIS   D ND1   1 
ATOM   4685 C  CD2   . HIS   D 2 93  ? 0.26823   35.37476  12.01694  1.000 22.01965  ?  92  HIS   D CD2   1 
ATOM   4686 C  CE1   . HIS   D 2 93  ? 1.50036   34.49321  10.42975  1.000 22.65740  ?  92  HIS   D CE1   1 
ATOM   4687 N  NE2   . HIS   D 2 93  ? 0.28300   34.91708  10.72089  1.000 21.88329  ?  92  HIS   D NE2   1 
ATOM   4688 N  N     . THR   D 2 94  ? 3.63509   38.37252  15.67703  1.000 25.46451  ?  93  THR   D N     1 
ATOM   4689 C  CA    . THR   D 2 94  ? 4.41855   38.77326  16.84558  1.000 26.40751  ?  93  THR   D CA    1 
ATOM   4690 C  C     . THR   D 2 94  ? 3.60570   38.92851  18.12809  1.000 35.63269  ?  93  THR   D C     1 
ATOM   4691 O  O     . THR   D 2 94  ? 4.20702   39.06565  19.20369  1.000 29.86722  ?  93  THR   D O     1 
ATOM   4692 C  CB    . THR   D 2 94  ? 5.11865   40.10481  16.57228  1.000 23.79571  ?  93  THR   D CB    1 
ATOM   4693 O  OG1   . THR   D 2 94  ? 4.14561   41.05875  16.14659  1.000 28.10943  ?  93  THR   D OG1   1 
ATOM   4694 C  CG2   . THR   D 2 94  ? 6.20045   39.96589  15.51423  1.000 29.89415  ?  93  THR   D CG2   1 
ATOM   4695 N  N     . GLY   D 2 95  ? 2.27192   38.93213  18.05986  1.000 27.51590  ?  94  GLY   D N     1 
ATOM   4696 C  CA    . GLY   D 2 95  ? 1.46628   39.13308  19.24321  1.000 29.34551  ?  94  GLY   D CA    1 
ATOM   4697 C  C     . GLY   D 2 95  ? 0.02521   39.52559  18.95279  1.000 29.09163  ?  94  GLY   D C     1 
ATOM   4698 O  O     . GLY   D 2 95  ? -0.44699  39.45145  17.81017  1.000 26.06114  ?  94  GLY   D O     1 
ATOM   4699 N  N     . PRO   D 2 96  ? -0.69398  39.97216  19.99413  1.000 29.80624  ?  95  PRO   D N     1 
ATOM   4700 C  CA    . PRO   D 2 96  ? -2.09278  40.37873  19.81409  1.000 26.82891  ?  95  PRO   D CA    1 
ATOM   4701 C  C     . PRO   D 2 96  ? -2.21500  41.52345  18.82046  1.000 27.34191  ?  95  PRO   D C     1 
ATOM   4702 O  O     . PRO   D 2 96  ? -1.36623  42.41890  18.76709  1.000 27.50200  ?  95  PRO   D O     1 
ATOM   4703 C  CB    . PRO   D 2 96  ? -2.51958  40.82520  21.22293  1.000 28.38089  ?  95  PRO   D CB    1 
ATOM   4704 C  CG    . PRO   D 2 96  ? -1.60298  40.12092  22.14661  1.000 27.14326  ?  95  PRO   D CG    1 
ATOM   4705 C  CD    . PRO   D 2 96  ? -0.27312  40.06611  21.41064  1.000 25.11803  ?  95  PRO   D CD    1 
ATOM   4706 N  N     . GLY   D 2 97  ? -3.27818  41.47708  18.02128  1.000 22.40997  ?  96  GLY   D N     1 
ATOM   4707 C  CA    . GLY   D 2 97  ? -3.61432  42.54310  17.10489  1.000 25.73108  ?  96  GLY   D CA    1 
ATOM   4708 C  C     . GLY   D 2 97  ? -3.11829  42.35581  15.68172  1.000 23.84294  ?  96  GLY   D C     1 
ATOM   4709 O  O     . GLY   D 2 97  ? -3.62161  43.02916  14.78081  1.000 25.92127  ?  96  GLY   D O     1 
ATOM   4710 N  N     . ILE   D 2 98  ? -2.14866  41.46567  15.45819  1.000 21.09808  ?  97  ILE   D N     1 
ATOM   4711 C  CA    . ILE   D 2 98  ? -1.70430  41.15325  14.09784  1.000 24.66799  ?  97  ILE   D CA    1 
ATOM   4712 C  C     . ILE   D 2 98  ? -2.88569  40.71950  13.23566  1.000 24.56817  ?  97  ILE   D C     1 
ATOM   4713 O  O     . ILE   D 2 98  ? -3.73194  39.92527  13.66590  1.000 22.76445  ?  97  ILE   D O     1 
ATOM   4714 C  CB    . ILE   D 2 98  ? -0.64001  40.04584  14.12994  1.000 24.60484  ?  97  ILE   D CB    1 
ATOM   4715 C  CG1   . ILE   D 2 98  ? 0.68999   40.54078  14.73976  1.000 22.51571  ?  97  ILE   D CG1   1 
ATOM   4716 C  CG2   . ILE   D 2 98  ? -0.48485  39.40551  12.73803  1.000 28.21352  ?  97  ILE   D CG2   1 
ATOM   4717 C  CD1   . ILE   D 2 98  ? 1.28597   41.76095  14.08819  1.000 33.03613  ?  97  ILE   D CD1   1 
ATOM   4718 N  N     . LEU   D 2 99  ? -2.95134  41.25199  12.01306  1.000 24.99893  ?  98  LEU   D N     1 
ATOM   4719 C  CA    . LEU   D 2 99  ? -3.94379  40.87752  11.00433  1.000 23.26054  ?  98  LEU   D CA    1 
ATOM   4720 C  C     . LEU   D 2 99  ? -3.27727  40.06109  9.89632   1.000 23.31393  ?  98  LEU   D C     1 
ATOM   4721 O  O     . LEU   D 2 99  ? -2.25356  40.48578  9.33923   1.000 22.97332  ?  98  LEU   D O     1 
ATOM   4722 C  CB    . LEU   D 2 99  ? -4.59654  42.13063  10.42366  1.000 22.32346  ?  98  LEU   D CB    1 
ATOM   4723 C  CG    . LEU   D 2 99  ? -5.63253  42.06478  9.29763   1.000 25.29701  ?  98  LEU   D CG    1 
ATOM   4724 C  CD1   . LEU   D 2 99  ? -6.89179  41.28083  9.74187   1.000 24.66923  ?  98  LEU   D CD1   1 
ATOM   4725 C  CD2   . LEU   D 2 99  ? -5.97616  43.48784  8.80459   1.000 20.49762  ?  98  LEU   D CD2   1 
ATOM   4726 N  N     . SER   D 2 100 ? -3.86242  38.90994  9.55379   1.000 20.41094  ?  99  SER   D N     1 
ATOM   4727 C  CA    . SER   D 2 100 ? -3.16304  37.97313  8.67049   1.000 26.68808  ?  99  SER   D CA    1 
ATOM   4728 C  C     . SER   D 2 100 ? -4.18049  37.17336  7.85763   1.000 21.48602  ?  99  SER   D C     1 
ATOM   4729 O  O     . SER   D 2 100 ? -5.32315  36.98895  8.28400   1.000 21.90722  ?  99  SER   D O     1 
ATOM   4730 C  CB    . SER   D 2 100 ? -2.26592  37.06004  9.50381   1.000 21.12067  ?  99  SER   D CB    1 
ATOM   4731 O  OG    . SER   D 2 100 ? -1.52175  36.14428  8.73652   1.000 22.12143  ?  99  SER   D OG    1 
ATOM   4732 N  N     . MET   D 2 101 ? -3.73861  36.65434  6.70142   1.000 24.05407  ?  100 MET   D N     1 
ATOM   4733 C  CA    . MET   D 2 101 ? -4.63803  35.95374  5.78757   1.000 22.05066  ?  100 MET   D CA    1 
ATOM   4734 C  C     . MET   D 2 101 ? -4.82871  34.49173  6.17382   1.000 20.14606  ?  100 MET   D C     1 
ATOM   4735 O  O     . MET   D 2 101 ? -3.86347  33.76487  6.45099   1.000 20.79649  ?  100 MET   D O     1 
ATOM   4736 C  CB    . MET   D 2 101 ? -4.12434  36.03403  4.33735   1.000 22.74318  ?  100 MET   D CB    1 
ATOM   4737 C  CG    . MET   D 2 101 ? -4.20542  37.41979  3.72033   1.000 23.06208  ?  100 MET   D CG    1 
ATOM   4738 S  SD    . MET   D 2 101 ? -5.85571  38.11318  3.66953   1.000 27.63888  ?  100 MET   D SD    1 
ATOM   4739 C  CE    . MET   D 2 101 ? -6.73294  37.06781  2.51021   1.000 28.04156  ?  100 MET   D CE    1 
ATOM   4740 N  N     . ALA   D 2 102 ? -6.08099  34.06250  6.20418   1.000 19.25054  ?  101 ALA   D N     1 
ATOM   4741 C  CA    . ALA   D 2 102 ? -6.38043  32.63451  6.28259   1.000 20.75047  ?  101 ALA   D CA    1 
ATOM   4742 C  C     . ALA   D 2 102 ? -6.14899  31.98063  4.91211   1.000 24.95726  ?  101 ALA   D C     1 
ATOM   4743 O  O     . ALA   D 2 102 ? -6.17859  32.65030  3.88034   1.000 23.95612  ?  101 ALA   D O     1 
ATOM   4744 C  CB    . ALA   D 2 102 ? -7.83653  32.43001  6.70727   1.000 22.62111  ?  101 ALA   D CB    1 
ATOM   4745 N  N     . ASN   D 2 103 ? -5.92241  30.66622  4.90248   1.000 23.22656  ?  102 ASN   D N     1 
ATOM   4746 C  CA    . ASN   D 2 103 ? -5.80982  29.95666  3.62793   1.000 26.82694  ?  102 ASN   D CA    1 
ATOM   4747 C  C     . ASN   D 2 103 ? -5.98210  28.45969  3.84173   1.000 28.04285  ?  102 ASN   D C     1 
ATOM   4748 O  O     . ASN   D 2 103 ? -6.08003  27.97387  4.97103   1.000 25.19284  ?  102 ASN   D O     1 
ATOM   4749 C  CB    . ASN   D 2 103 ? -4.46818  30.22022  2.94072   1.000 25.06329  ?  102 ASN   D CB    1 
ATOM   4750 C  CG    . ASN   D 2 103 ? -3.27375  29.81290  3.79385   1.000 23.43305  ?  102 ASN   D CG    1 
ATOM   4751 O  OD1   . ASN   D 2 103 ? -3.09055  28.64190  4.12688   1.000 23.87253  ?  102 ASN   D OD1   1 
ATOM   4752 N  ND2   . ASN   D 2 103 ? -2.43523  30.77622  4.11082   1.000 23.03125  ?  102 ASN   D ND2   1 
ATOM   4753 N  N     . ALA   D 2 104 ? -5.94810  27.72649  2.72223   1.000 27.44802  ?  103 ALA   D N     1 
ATOM   4754 C  CA    . ALA   D 2 104 ? -6.04620  26.27892  2.67821   1.000 27.24246  ?  103 ALA   D CA    1 
ATOM   4755 C  C     . ALA   D 2 104 ? -4.76974  25.67638  2.10371   1.000 28.81767  ?  103 ALA   D C     1 
ATOM   4756 O  O     . ALA   D 2 104 ? -4.80706  24.71381  1.34633   1.000 35.96636  ?  103 ALA   D O     1 
ATOM   4757 C  CB    . ALA   D 2 104 ? -7.26764  25.84963  1.86650   1.000 25.51096  ?  103 ALA   D CB    1 
ATOM   4758 N  N     . GLY   D 2 105 ? -3.62245  26.23414  2.45996   1.000 25.50494  ?  104 GLY   D N     1 
ATOM   4759 C  CA    . GLY   D 2 105 ? -2.37377  25.82832  1.87414   1.000 26.92951  ?  104 GLY   D CA    1 
ATOM   4760 C  C     . GLY   D 2 105 ? -1.77664  26.91680  1.00173   1.000 26.48015  ?  104 GLY   D C     1 
ATOM   4761 O  O     . GLY   D 2 105 ? -2.34608  27.99953  0.83352   1.000 26.40924  ?  104 GLY   D O     1 
ATOM   4762 N  N     . PRO   D 2 106 ? -0.60417  26.63618  0.43180   1.000 24.04600  ?  105 PRO   D N     1 
ATOM   4763 C  CA    . PRO   D 2 106 ? 0.14293   27.66645  -0.29793  1.000 29.60975  ?  105 PRO   D CA    1 
ATOM   4764 C  C     . PRO   D 2 106 ? -0.66186  28.28569  -1.43126  1.000 26.13766  ?  105 PRO   D C     1 
ATOM   4765 O  O     . PRO   D 2 106 ? -1.37188  27.59722  -2.16087  1.000 24.51019  ?  105 PRO   D O     1 
ATOM   4766 C  CB    . PRO   D 2 106 ? 1.35830   26.89378  -0.82906  1.000 31.86409  ?  105 PRO   D CB    1 
ATOM   4767 C  CG    . PRO   D 2 106 ? 1.57782   25.82936  0.20826   1.000 32.28856  ?  105 PRO   D CG    1 
ATOM   4768 C  CD    . PRO   D 2 106 ? 0.19540   25.41637  0.64157   1.000 26.89795  ?  105 PRO   D CD    1 
ATOM   4769 N  N     . ASN   D 2 107 ? -0.55513  29.60851  -1.55561  1.000 24.99653  ?  106 ASN   D N     1 
ATOM   4770 C  CA    . ASN   D 2 107 ? -1.11223  30.35157  -2.68581  1.000 26.69318  ?  106 ASN   D CA    1 
ATOM   4771 C  C     . ASN   D 2 107 ? -2.62625  30.17717  -2.81132  1.000 27.56580  ?  106 ASN   D C     1 
ATOM   4772 O  O     . ASN   D 2 107 ? -3.17024  30.04528  -3.90942  1.000 27.50252  ?  106 ASN   D O     1 
ATOM   4773 C  CB    . ASN   D 2 107 ? -0.39237  29.96494  -3.97977  1.000 28.72547  ?  106 ASN   D CB    1 
ATOM   4774 C  CG    . ASN   D 2 107 ? 1.10318   30.23927  -3.89510  1.000 27.75723  ?  106 ASN   D CG    1 
ATOM   4775 O  OD1   . ASN   D 2 107 ? 1.51269   31.28531  -3.40610  1.000 30.19484  ?  106 ASN   D OD1   1 
ATOM   4776 N  ND2   . ASN   D 2 107 ? 1.91889   29.28849  -4.32433  1.000 29.46986  ?  106 ASN   D ND2   1 
ATOM   4777 N  N     . THR   D 2 108 ? -3.32380  30.20968  -1.67690  1.000 25.55879  ?  107 THR   D N     1 
ATOM   4778 C  CA    . THR   D 2 108 ? -4.77635  30.12466  -1.67112  1.000 27.18151  ?  107 THR   D CA    1 
ATOM   4779 C  C     . THR   D 2 108 ? -5.39393  31.28534  -0.90173  1.000 26.25792  ?  107 THR   D C     1 
ATOM   4780 O  O     . THR   D 2 108 ? -6.41234  31.12886  -0.23076  1.000 28.13475  ?  107 THR   D O     1 
ATOM   4781 C  CB    . THR   D 2 108 ? -5.26163  28.78322  -1.10825  1.000 28.13550  ?  107 THR   D CB    1 
ATOM   4782 O  OG1   . THR   D 2 108 ? -4.76921  28.59140  0.22727   1.000 26.93044  ?  107 THR   D OG1   1 
ATOM   4783 C  CG2   . THR   D 2 108 ? -4.77725  27.61794  -1.99620  1.000 26.32273  ?  107 THR   D CG2   1 
ATOM   4784 N  N     . ASN   D 2 109 ? -4.83724  32.48563  -1.01757  1.000 27.85709  ?  108 ASN   D N     1 
ATOM   4785 C  CA    . ASN   D 2 109 ? -5.44821  33.61547  -0.32783  1.000 26.80435  ?  108 ASN   D CA    1 
ATOM   4786 C  C     . ASN   D 2 109 ? -6.73173  34.01659  -1.02172  1.000 31.35605  ?  108 ASN   D C     1 
ATOM   4787 O  O     . ASN   D 2 109 ? -6.76264  34.13948  -2.25118  1.000 30.18002  ?  108 ASN   D O     1 
ATOM   4788 C  CB    . ASN   D 2 109 ? -4.51119  34.80347  -0.28164  1.000 26.03992  ?  108 ASN   D CB    1 
ATOM   4789 C  CG    . ASN   D 2 109 ? -3.26378  34.51074  0.48397   1.000 30.89177  ?  108 ASN   D CG    1 
ATOM   4790 O  OD1   . ASN   D 2 109 ? -3.29599  34.45700  1.69942   1.000 27.20673  ?  108 ASN   D OD1   1 
ATOM   4791 N  ND2   . ASN   D 2 109 ? -2.15099  34.30840  -0.21647  1.000 23.91266  ?  108 ASN   D ND2   1 
ATOM   4792 N  N     . GLY   D 2 110 ? -7.79233  34.21844  -0.23734  1.000 22.68248  ?  109 GLY   D N     1 
ATOM   4793 C  CA    . GLY   D 2 110 ? -9.03529  34.72106  -0.79366  1.000 28.01308  ?  109 GLY   D CA    1 
ATOM   4794 C  C     . GLY   D 2 110 ? -9.50497  36.00105  -0.12969  1.000 25.07374  ?  109 GLY   D C     1 
ATOM   4795 O  O     . GLY   D 2 110 ? -8.98562  37.09245  -0.39122  1.000 24.66505  ?  109 GLY   D O     1 
ATOM   4796 N  N     . SER   D 2 111 ? -10.49255 35.87946  0.74511   1.000 22.88852  ?  110 SER   D N     1 
ATOM   4797 C  CA    . SER   D 2 111 ? -10.87407 36.98833  1.60041   1.000 25.98186  ?  110 SER   D CA    1 
ATOM   4798 C  C     . SER   D 2 111 ? -10.83131 36.66331  3.09099   1.000 23.28434  ?  110 SER   D C     1 
ATOM   4799 O  O     . SER   D 2 111 ? -10.80214 37.59939  3.89756   1.000 23.89164  ?  110 SER   D O     1 
ATOM   4800 C  CB    . SER   D 2 111 ? -12.27693 37.48735  1.24212   1.000 19.81534  ?  110 SER   D CB    1 
ATOM   4801 O  OG    . SER   D 2 111 ? -13.19903 36.43428  1.28991   1.000 22.89943  ?  110 SER   D OG    1 
ATOM   4802 N  N     . GLN   D 2 112 ? -10.80695 35.39049  3.48396   1.000 22.41905  ?  111 GLN   D N     1 
ATOM   4803 C  CA    . GLN   D 2 112 ? -10.79875 35.09580  4.91339   1.000 23.70700  ?  111 GLN   D CA    1 
ATOM   4804 C  C     . GLN   D 2 112 ? -9.48667  35.56127  5.53914   1.000 25.87594  ?  111 GLN   D C     1 
ATOM   4805 O  O     . GLN   D 2 112 ? -8.41626  35.53321  4.90857   1.000 21.94177  ?  111 GLN   D O     1 
ATOM   4806 C  CB    . GLN   D 2 112 ? -11.03607 33.60848  5.17563   1.000 23.47266  ?  111 GLN   D CB    1 
ATOM   4807 C  CG    . GLN   D 2 112 ? -12.46028 33.12440  4.90470   1.000 24.89388  ?  111 GLN   D CG    1 
ATOM   4808 C  CD    . GLN   D 2 112 ? -12.68226 31.71110  5.43291   1.000 28.80781  ?  111 GLN   D CD    1 
ATOM   4809 O  OE1   . GLN   D 2 112 ? -12.25299 31.37612  6.53041   1.000 27.02628  ?  111 GLN   D OE1   1 
ATOM   4810 N  NE2   . GLN   D 2 112 ? -13.31157 30.87552  4.64011   1.000 23.26930  ?  111 GLN   D NE2   1 
ATOM   4811 N  N     . PHE   D 2 113 ? -9.59208  36.04481  6.77119   1.000 20.51644  ?  112 PHE   D N     1 
ATOM   4812 C  CA    . PHE   D 2 113 ? -8.49921  36.65008  7.50080   1.000 22.46829  ?  112 PHE   D CA    1 
ATOM   4813 C  C     . PHE   D 2 113 ? -8.65531  36.27924  8.97379   1.000 20.32702  ?  112 PHE   D C     1 
ATOM   4814 O  O     . PHE   D 2 113 ? -9.68633  35.74762  9.38607   1.000 20.27071  ?  112 PHE   D O     1 
ATOM   4815 C  CB    . PHE   D 2 113 ? -8.52656  38.16847  7.34512   1.000 25.02853  ?  112 PHE   D CB    1 
ATOM   4816 C  CG    . PHE   D 2 113 ? -9.75684  38.77633  7.92621   1.000 23.63264  ?  112 PHE   D CG    1 
ATOM   4817 C  CD1   . PHE   D 2 113 ? -10.90179 38.91473  7.16120   1.000 27.35620  ?  112 PHE   D CD1   1 
ATOM   4818 C  CD2   . PHE   D 2 113 ? -9.79902  39.14639  9.26649   1.000 26.28437  ?  112 PHE   D CD2   1 
ATOM   4819 C  CE1   . PHE   D 2 113 ? -12.06305 39.42968  7.71387   1.000 26.10054  ?  112 PHE   D CE1   1 
ATOM   4820 C  CE2   . PHE   D 2 113 ? -10.95104 39.66552  9.81545   1.000 27.63658  ?  112 PHE   D CE2   1 
ATOM   4821 C  CZ    . PHE   D 2 113 ? -12.07971 39.80061  9.05140   1.000 29.01996  ?  112 PHE   D CZ    1 
ATOM   4822 N  N     . PHE   D 2 114 ? -7.65443  36.61631  9.78455   1.000 20.58758  ?  113 PHE   D N     1 
ATOM   4823 C  CA    . PHE   D 2 114 ? -7.77430  36.38282  11.21629  1.000 23.25760  ?  113 PHE   D CA    1 
ATOM   4824 C  C     . PHE   D 2 114 ? -7.01410  37.46955  11.97664  1.000 23.91685  ?  113 PHE   D C     1 
ATOM   4825 O  O     . PHE   D 2 114 ? -5.98934  37.98730  11.51362  1.000 23.72750  ?  113 PHE   D O     1 
ATOM   4826 C  CB    . PHE   D 2 114 ? -7.31725  34.94479  11.61672  1.000 21.50775  ?  113 PHE   D CB    1 
ATOM   4827 C  CG    . PHE   D 2 114 ? -5.85235  34.64016  11.34917  1.000 21.15425  ?  113 PHE   D CG    1 
ATOM   4828 C  CD1   . PHE   D 2 114 ? -5.39785  34.36681  10.05960  1.000 21.98124  ?  113 PHE   D CD1   1 
ATOM   4829 C  CD2   . PHE   D 2 114 ? -4.93654  34.58886  12.40256  1.000 24.93936  ?  113 PHE   D CD2   1 
ATOM   4830 C  CE1   . PHE   D 2 114 ? -4.02896  34.06601  9.81238   1.000 20.12115  ?  113 PHE   D CE1   1 
ATOM   4831 C  CE2   . PHE   D 2 114 ? -3.55790  34.30884  12.18123  1.000 20.54862  ?  113 PHE   D CE2   1 
ATOM   4832 C  CZ    . PHE   D 2 114 ? -3.11099  34.03534  10.89145  1.000 24.56086  ?  113 PHE   D CZ    1 
ATOM   4833 N  N     . ILE   D 2 115 ? -7.57347  37.85347  13.12666  1.000 21.47242  ?  114 ILE   D N     1 
ATOM   4834 C  CA    . ILE   D 2 115 ? -6.95510  38.78694  14.06581  1.000 23.08230  ?  114 ILE   D CA    1 
ATOM   4835 C  C     . ILE   D 2 115 ? -6.42749  37.98184  15.24559  1.000 24.39838  ?  114 ILE   D C     1 
ATOM   4836 O  O     . ILE   D 2 115 ? -7.19500  37.26426  15.90430  1.000 23.62355  ?  114 ILE   D O     1 
ATOM   4837 C  CB    . ILE   D 2 115 ? -7.94256  39.85416  14.55705  1.000 22.55493  ?  114 ILE   D CB    1 
ATOM   4838 C  CG1   . ILE   D 2 115 ? -8.71323  40.49901  13.39538  1.000 23.48370  ?  114 ILE   D CG1   1 
ATOM   4839 C  CG2   . ILE   D 2 115 ? -7.20619  40.91220  15.37666  1.000 24.28043  ?  114 ILE   D CG2   1 
ATOM   4840 C  CD1   . ILE   D 2 115 ? -9.96089  41.25804  13.87151  1.000 24.98162  ?  114 ILE   D CD1   1 
ATOM   4841 N  N     . CYS   D 2 116 ? -5.13082  38.10383  15.50880  1.000 20.07742  ?  115 CYS   D N     1 
ATOM   4842 C  CA    . CYS   D 2 116 ? -4.49933  37.37550  16.59823  1.000 23.50426  ?  115 CYS   D CA    1 
ATOM   4843 C  C     . CYS   D 2 116 ? -4.83477  38.02334  17.93634  1.000 22.54978  ?  115 CYS   D C     1 
ATOM   4844 O  O     . CYS   D 2 116 ? -4.84815  39.24857  18.06957  1.000 27.10053  ?  115 CYS   D O     1 
ATOM   4845 C  CB    . CYS   D 2 116 ? -2.98074  37.35648  16.42919  1.000 21.89360  ?  115 CYS   D CB    1 
ATOM   4846 S  SG    . CYS   D 2 116 ? -2.30650  36.45353  15.01262  1.000 25.82794  ?  115 CYS   D SG    1 
ATOM   4847 N  N     . THR   D 2 117 ? -5.09136  37.20196  18.93327  1.000 22.86624  ?  116 THR   D N     1 
ATOM   4848 C  CA    . THR   D 2 117 ? -5.24876  37.70338  20.29435  1.000 25.20217  ?  116 THR   D CA    1 
ATOM   4849 C  C     . THR   D 2 117 ? -4.09407  37.27342  21.18176  1.000 26.74548  ?  116 THR   D C     1 
ATOM   4850 O  O     . THR   D 2 117 ? -4.14505  37.48404  22.40826  1.000 29.02317  ?  116 THR   D O     1 
ATOM   4851 C  CB    . THR   D 2 117 ? -6.57042  37.22859  20.88066  1.000 21.26823  ?  116 THR   D CB    1 
ATOM   4852 O  OG1   . THR   D 2 117 ? -6.59320  35.80186  20.87776  1.000 27.40286  ?  116 THR   D OG1   1 
ATOM   4853 C  CG2   . THR   D 2 117 ? -7.74774  37.75676  20.07828  1.000 25.13989  ?  116 THR   D CG2   1 
ATOM   4854 N  N     . ALA   D 2 118 ? -3.07225  36.65949  20.58367  1.000 27.14885  ?  117 ALA   D N     1 
ATOM   4855 C  CA    . ALA   D 2 118 ? -1.84796  36.20774  21.22524  1.000 26.97785  ?  117 ALA   D CA    1 
ATOM   4856 C  C     . ALA   D 2 118 ? -0.81294  36.00278  20.12589  1.000 28.90466  ?  117 ALA   D C     1 
ATOM   4857 O  O     . ALA   D 2 118 ? -1.13723  36.00636  18.94066  1.000 28.16503  ?  117 ALA   D O     1 
ATOM   4858 C  CB    . ALA   D 2 118 ? -2.07088  34.91138  22.01389  1.000 29.86727  ?  117 ALA   D CB    1 
ATOM   4859 N  N     . LYS   D 2 119 ? 0.43402   35.79867  20.53062  1.000 30.54208  ?  118 LYS   D N     1 
ATOM   4860 C  CA    . LYS   D 2 119 ? 1.47681   35.43897  19.57814  1.000 33.69109  ?  118 LYS   D CA    1 
ATOM   4861 C  C     . LYS   D 2 119 ? 1.22241   34.03201  19.02791  1.000 25.58945  ?  118 LYS   D C     1 
ATOM   4862 O  O     . LYS   D 2 119 ? 0.96798   33.09927  19.79381  1.000 29.47154  ?  118 LYS   D O     1 
ATOM   4863 C  CB    . LYS   D 2 119 ? 2.83310   35.52396  20.28042  1.000 29.27315  ?  118 LYS   D CB    1 
ATOM   4864 C  CG    . LYS   D 2 119 ? 4.06343   35.26665  19.43929  1.000 30.91676  ?  118 LYS   D CG    1 
ATOM   4865 C  CD    . LYS   D 2 119 ? 5.34954   35.63044  20.23495  1.000 37.05366  ?  118 LYS   D CD    1 
ATOM   4866 C  CE    . LYS   D 2 119 ? 6.35640   34.48161  20.22135  1.000 42.71376  ?  118 LYS   D CE    1 
ATOM   4867 N  NZ    . LYS   D 2 119 ? 7.73570   34.92260  20.57421  1.000 47.55619  ?  118 LYS   D NZ    1 
ATOM   4868 N  N     . THR   D 2 120 ? 1.25999   33.88384  17.68550  1.000 23.60501  ?  119 THR   D N     1 
ATOM   4869 C  CA    . THR   D 2 120 ? 1.04329   32.59568  17.00571  1.000 29.72175  ?  119 THR   D CA    1 
ATOM   4870 C  C     . THR   D 2 120 ? 2.20690   32.36157  16.02882  1.000 29.28340  ?  119 THR   D C     1 
ATOM   4871 O  O     . THR   D 2 120 ? 2.03959   32.31895  14.79634  1.000 22.41771  ?  119 THR   D O     1 
ATOM   4872 C  CB    . THR   D 2 120 ? -0.30702  32.55164  16.27793  1.000 26.16827  ?  119 THR   D CB    1 
ATOM   4873 O  OG1   . THR   D 2 120 ? -0.35473  33.59663  15.29083  1.000 24.30147  ?  119 THR   D OG1   1 
ATOM   4874 C  CG2   . THR   D 2 120 ? -1.44990  32.71610  17.26107  1.000 25.96059  ?  119 THR   D CG2   1 
ATOM   4875 N  N     . GLU   D 2 121 ? 3.39846   32.19143  16.59954  1.000 29.45066  ?  120 GLU   D N     1 
ATOM   4876 C  CA    . GLU   D 2 121 ? 4.60850   32.19609  15.78869  1.000 23.23865  ?  120 GLU   D CA    1 
ATOM   4877 C  C     . GLU   D 2 121 ? 4.70987   30.98350  14.87641  1.000 26.43983  ?  120 GLU   D C     1 
ATOM   4878 O  O     . GLU   D 2 121 ? 5.35267   31.08987  13.82651  1.000 25.63961  ?  120 GLU   D O     1 
ATOM   4879 C  CB    . GLU   D 2 121 ? 5.85197   32.29491  16.68161  1.000 26.49913  ?  120 GLU   D CB    1 
ATOM   4880 C  CG    . GLU   D 2 121 ? 6.19660   31.02229  17.42915  1.000 32.81202  ?  120 GLU   D CG    1 
ATOM   4881 C  CD    . GLU   D 2 121 ? 5.34496   30.79584  18.66954  1.000 37.28901  ?  120 GLU   D CD    1 
ATOM   4882 O  OE1   . GLU   D 2 121 ? 4.56942   31.69999  19.08522  1.000 35.40205  ?  120 GLU   D OE1   1 
ATOM   4883 O  OE2   . GLU   D 2 121 ? 5.46307   29.69275  19.25068  1.000 56.21942  -1 120 GLU   D OE2   1 
ATOM   4884 N  N     . TRP   D 2 122 ? 4.06948   29.85129  15.21932  1.000 22.33522  ?  121 TRP   D N     1 
ATOM   4885 C  CA    . TRP   D 2 122 ? 4.12275   28.69720  14.32517  1.000 26.89277  ?  121 TRP   D CA    1 
ATOM   4886 C  C     . TRP   D 2 122 ? 3.43211   28.93513  12.97872  1.000 25.34779  ?  121 TRP   D C     1 
ATOM   4887 O  O     . TRP   D 2 122 ? 3.62540   28.12810  12.06021  1.000 26.94525  ?  121 TRP   D O     1 
ATOM   4888 C  CB    . TRP   D 2 122 ? 3.51011   27.45035  14.98678  1.000 24.67986  ?  121 TRP   D CB    1 
ATOM   4889 C  CG    . TRP   D 2 122 ? 2.06114   27.59093  15.29976  1.000 24.43425  ?  121 TRP   D CG    1 
ATOM   4890 C  CD1   . TRP   D 2 122 ? 0.99947   27.17429  14.53013  1.000 26.66977  ?  121 TRP   D CD1   1 
ATOM   4891 C  CD2   . TRP   D 2 122 ? 1.50185   28.21536  16.45870  1.000 27.64489  ?  121 TRP   D CD2   1 
ATOM   4892 N  NE1   . TRP   D 2 122 ? -0.18852  27.49141  15.16349  1.000 31.34508  ?  121 TRP   D NE1   1 
ATOM   4893 C  CE2   . TRP   D 2 122 ? 0.09419   28.12609  16.34772  1.000 30.10012  ?  121 TRP   D CE2   1 
ATOM   4894 C  CE3   . TRP   D 2 122 ? 2.05577   28.81718  17.59963  1.000 27.29533  ?  121 TRP   D CE3   1 
ATOM   4895 C  CZ2   . TRP   D 2 122 ? -0.76887  28.63278  17.32910  1.000 27.03955  ?  121 TRP   D CZ2   1 
ATOM   4896 C  CZ3   . TRP   D 2 122 ? 1.20309   29.32644  18.56888  1.000 28.91654  ?  121 TRP   D CZ3   1 
ATOM   4897 C  CH2   . TRP   D 2 122 ? -0.20321  29.22596  18.42552  1.000 28.91683  ?  121 TRP   D CH2   1 
ATOM   4898 N  N     . LEU   D 2 123 ? 2.65083   30.00733  12.82759  1.000 25.87011  ?  122 LEU   D N     1 
ATOM   4899 C  CA    . LEU   D 2 123 ? 2.04274   30.34689  11.53732  1.000 25.18828  ?  122 LEU   D CA    1 
ATOM   4900 C  C     . LEU   D 2 123 ? 2.93560   31.22407  10.66473  1.000 26.00574  ?  122 LEU   D C     1 
ATOM   4901 O  O     . LEU   D 2 123 ? 2.56009   31.51732  9.50791   1.000 22.82081  ?  122 LEU   D O     1 
ATOM   4902 C  CB    . LEU   D 2 123 ? 0.70914   31.06113  11.74493  1.000 21.75633  ?  122 LEU   D CB    1 
ATOM   4903 C  CG    . LEU   D 2 123 ? -0.26660  30.39184  12.72092  1.000 24.16765  ?  122 LEU   D CG    1 
ATOM   4904 C  CD1   . LEU   D 2 123 ? -1.45558  31.33200  12.98980  1.000 23.76788  ?  122 LEU   D CD1   1 
ATOM   4905 C  CD2   . LEU   D 2 123 ? -0.72183  29.05624  12.16735  1.000 22.22663  ?  122 LEU   D CD2   1 
ATOM   4906 N  N     . ASP   D 2 124 ? 4.08776   31.64861  11.19941  1.000 24.03869  ?  123 ASP   D N     1 
ATOM   4907 C  CA    . ASP   D 2 124 ? 5.08410   32.38221  10.42763  1.000 24.72798  ?  123 ASP   D CA    1 
ATOM   4908 C  C     . ASP   D 2 124 ? 5.52475   31.54996  9.23047   1.000 27.61401  ?  123 ASP   D C     1 
ATOM   4909 O  O     . ASP   D 2 124 ? 5.78133   30.35013  9.35175   1.000 26.62337  ?  123 ASP   D O     1 
ATOM   4910 C  CB    . ASP   D 2 124 ? 6.30697   32.72183  11.29758  1.000 23.82489  ?  123 ASP   D CB    1 
ATOM   4911 C  CG    . ASP   D 2 124 ? 6.00222   33.75112  12.39118  1.000 25.14314  ?  123 ASP   D CG    1 
ATOM   4912 O  OD1   . ASP   D 2 124 ? 4.94340   34.40458  12.36293  1.000 26.94594  ?  123 ASP   D OD1   1 
ATOM   4913 O  OD2   . ASP   D 2 124 ? 6.81873   33.88048  13.32893  1.000 31.93582  -1 123 ASP   D OD2   1 
ATOM   4914 N  N     . GLY   D 2 125 ? 5.61804   32.19515  8.07070   1.000 24.14443  ?  124 GLY   D N     1 
ATOM   4915 C  CA    . GLY   D 2 125 ? 6.01305   31.51647  6.84697   1.000 27.29235  ?  124 GLY   D CA    1 
ATOM   4916 C  C     . GLY   D 2 125 ? 4.90940   30.71592  6.18614   1.000 30.14923  ?  124 GLY   D C     1 
ATOM   4917 O  O     . GLY   D 2 125 ? 5.12515   30.16894  5.09383   1.000 25.78659  ?  124 GLY   D O     1 
ATOM   4918 N  N     . LYS   D 2 126 ? 3.73544   30.62547  6.81127   1.000 26.19230  ?  125 LYS   D N     1 
ATOM   4919 C  CA    . LYS   D 2 126 ? 2.58981   29.94276  6.23115   1.000 28.82205  ?  125 LYS   D CA    1 
ATOM   4920 C  C     . LYS   D 2 126 ? 1.40230   30.85602  5.95702   1.000 28.23521  ?  125 LYS   D C     1 
ATOM   4921 O  O     . LYS   D 2 126 ? 0.60607   30.55943  5.05409   1.000 27.79610  ?  125 LYS   D O     1 
ATOM   4922 C  CB    . LYS   D 2 126 ? 2.13778   28.79477  7.14206   1.000 30.35135  ?  125 LYS   D CB    1 
ATOM   4923 C  CG    . LYS   D 2 126 ? 3.22068   27.76859  7.40441   1.000 34.12797  ?  125 LYS   D CG    1 
ATOM   4924 C  CD    . LYS   D 2 126 ? 2.69750   26.62228  8.26649   1.000 41.02826  ?  125 LYS   D CD    1 
ATOM   4925 C  CE    . LYS   D 2 126 ? 3.85304   25.79916  8.83432   1.000 48.67873  ?  125 LYS   D CE    1 
ATOM   4926 N  NZ    . LYS   D 2 126 ? 4.64105   25.19084  7.72928   1.000 56.80855  ?  125 LYS   D NZ    1 
ATOM   4927 N  N     . HIS   D 2 127 ? 1.25948   31.94805  6.70089   1.000 21.06218  ?  126 HIS   D N     1 
ATOM   4928 C  CA    . HIS   D 2 127 ? 0.19940   32.91812  6.50109   1.000 19.53400  ?  126 HIS   D CA    1 
ATOM   4929 C  C     . HIS   D 2 127 ? 0.80054   34.29940  6.33205   1.000 19.95555  ?  126 HIS   D C     1 
ATOM   4930 O  O     . HIS   D 2 127 ? 1.65483   34.71539  7.12659   1.000 23.01328  ?  126 HIS   D O     1 
ATOM   4931 C  CB    . HIS   D 2 127 ? -0.78191  32.94292  7.69289   1.000 20.82437  ?  126 HIS   D CB    1 
ATOM   4932 C  CG    . HIS   D 2 127 ? -1.48276  31.64503  7.90645   1.000 20.92454  ?  126 HIS   D CG    1 
ATOM   4933 N  ND1   . HIS   D 2 127 ? -2.74896  31.41192  7.43353   1.000 17.51389  ?  126 HIS   D ND1   1 
ATOM   4934 C  CD2   . HIS   D 2 127 ? -1.08433  30.49599  8.51108   1.000 18.61992  ?  126 HIS   D CD2   1 
ATOM   4935 C  CE1   . HIS   D 2 127 ? -3.10385  30.17198  7.72549   1.000 19.36494  ?  126 HIS   D CE1   1 
ATOM   4936 N  NE2   . HIS   D 2 127 ? -2.11687  29.59697  8.39011   1.000 22.94735  ?  126 HIS   D NE2   1 
ATOM   4937 N  N     . VAL   D 2 128 ? 0.26423   35.03703  5.36492   1.000 20.01658  ?  127 VAL   D N     1 
ATOM   4938 C  CA    . VAL   D 2 128 ? 0.76446   36.36026  5.01438   1.000 23.02717  ?  127 VAL   D CA    1 
ATOM   4939 C  C     . VAL   D 2 128 ? 0.22057   37.38821  6.00465   1.000 21.62093  ?  127 VAL   D C     1 
ATOM   4940 O  O     . VAL   D 2 128 ? -0.99088  37.63344  6.05900   1.000 24.27658  ?  127 VAL   D O     1 
ATOM   4941 C  CB    . VAL   D 2 128 ? 0.37534   36.70863  3.56706   1.000 23.78709  ?  127 VAL   D CB    1 
ATOM   4942 C  CG1   . VAL   D 2 128 ? 0.79061   38.13615  3.21156   1.000 22.12141  ?  127 VAL   D CG1   1 
ATOM   4943 C  CG2   . VAL   D 2 128 ? 0.97461   35.67423  2.57739   1.000 20.08786  ?  127 VAL   D CG2   1 
ATOM   4944 N  N     . VAL   D 2 129 ? 1.11368   37.97405  6.80499   1.000 25.15181  ?  128 VAL   D N     1 
ATOM   4945 C  CA    . VAL   D 2 129 ? 0.76007   39.07808  7.69463   1.000 24.45071  ?  128 VAL   D CA    1 
ATOM   4946 C  C     . VAL   D 2 129 ? 0.70622   40.36428  6.87425   1.000 25.73706  ?  128 VAL   D C     1 
ATOM   4947 O  O     . VAL   D 2 129 ? 1.64048   40.67001  6.12432   1.000 25.55617  ?  128 VAL   D O     1 
ATOM   4948 C  CB    . VAL   D 2 129 ? 1.78161   39.18982  8.84510   1.000 23.36239  ?  128 VAL   D CB    1 
ATOM   4949 C  CG1   . VAL   D 2 129 ? 1.57335   40.47637  9.66616   1.000 23.18159  ?  128 VAL   D CG1   1 
ATOM   4950 C  CG2   . VAL   D 2 129 ? 1.73638   37.94247  9.72853   1.000 23.73409  ?  128 VAL   D CG2   1 
ATOM   4951 N  N     . PHE   D 2 130 ? -0.37085  41.13981  7.02678   1.000 21.26541  ?  129 PHE   D N     1 
ATOM   4952 C  CA    . PHE   D 2 130 ? -0.52400  42.33612  6.20139   1.000 25.74804  ?  129 PHE   D CA    1 
ATOM   4953 C  C     . PHE   D 2 130 ? -1.07090  43.55714  6.93339   1.000 26.28840  ?  129 PHE   D C     1 
ATOM   4954 O  O     . PHE   D 2 130 ? -1.24012  44.60433  6.29494   1.000 24.72596  ?  129 PHE   D O     1 
ATOM   4955 C  CB    . PHE   D 2 130 ? -1.41644  42.03620  4.97823   1.000 21.56754  ?  129 PHE   D CB    1 
ATOM   4956 C  CG    . PHE   D 2 130 ? -2.86131  41.73404  5.31428   1.000 22.20883  ?  129 PHE   D CG    1 
ATOM   4957 C  CD1   . PHE   D 2 130 ? -3.26693  40.44330  5.60755   1.000 22.30059  ?  129 PHE   D CD1   1 
ATOM   4958 C  CD2   . PHE   D 2 130 ? -3.80639  42.73627  5.32028   1.000 23.14037  ?  129 PHE   D CD2   1 
ATOM   4959 C  CE1   . PHE   D 2 130 ? -4.59458  40.15380  5.92643   1.000 21.15456  ?  129 PHE   D CE1   1 
ATOM   4960 C  CE2   . PHE   D 2 130 ? -5.13042  42.46956  5.62561   1.000 24.98289  ?  129 PHE   D CE2   1 
ATOM   4961 C  CZ    . PHE   D 2 130 ? -5.53733  41.16432  5.91784   1.000 25.51975  ?  129 PHE   D CZ    1 
ATOM   4962 N  N     . GLY   D 2 131 ? -1.36182  43.46627  8.22855   1.000 29.11450  ?  130 GLY   D N     1 
ATOM   4963 C  CA    . GLY   D 2 131 ? -1.83445  44.62775  8.96263   1.000 27.17954  ?  130 GLY   D CA    1 
ATOM   4964 C  C     . GLY   D 2 131 ? -1.82899  44.38611  10.46273  1.000 25.77872  ?  130 GLY   D C     1 
ATOM   4965 O  O     . GLY   D 2 131 ? -1.28042  43.39787  10.94902  1.000 25.79396  ?  130 GLY   D O     1 
ATOM   4966 N  N     . LYS   D 2 132 ? -2.44885  45.31189  11.19435  1.000 24.33975  ?  131 LYS   D N     1 
ATOM   4967 C  CA    . LYS   D 2 132 ? -2.60389  45.15422  12.64178  1.000 28.16871  ?  131 LYS   D CA    1 
ATOM   4968 C  C     . LYS   D 2 132 ? -3.68108  46.10387  13.14447  1.000 28.97911  ?  131 LYS   D C     1 
ATOM   4969 O  O     . LYS   D 2 132 ? -3.95031  47.14613  12.53206  1.000 25.91936  ?  131 LYS   D O     1 
ATOM   4970 C  CB    . LYS   D 2 132 ? -1.29777  45.41736  13.41019  1.000 28.23571  ?  131 LYS   D CB    1 
ATOM   4971 C  CG    . LYS   D 2 132 ? -0.92648  46.87681  13.44379  1.000 35.21188  ?  131 LYS   D CG    1 
ATOM   4972 C  CD    . LYS   D 2 132 ? 0.46266   47.10317  14.02120  1.000 45.11053  ?  131 LYS   D CD    1 
ATOM   4973 C  CE    . LYS   D 2 132 ? 0.92739   48.54970  13.80259  1.000 45.11814  ?  131 LYS   D CE    1 
ATOM   4974 N  NZ    . LYS   D 2 132 ? 2.37690   48.70227  14.13380  1.000 51.09949  ?  131 LYS   D NZ    1 
ATOM   4975 N  N     . VAL   D 2 133 ? -4.28282  45.72593  14.27838  1.000 25.42916  ?  132 VAL   D N     1 
ATOM   4976 C  CA    . VAL   D 2 133 ? -5.27238  46.57422  14.92829  1.000 26.63307  ?  132 VAL   D CA    1 
ATOM   4977 C  C     . VAL   D 2 133 ? -4.63660  47.90875  15.27896  1.000 26.79967  ?  132 VAL   D C     1 
ATOM   4978 O  O     . VAL   D 2 133 ? -3.53150  47.96834  15.83316  1.000 26.06530  ?  132 VAL   D O     1 
ATOM   4979 C  CB    . VAL   D 2 133 ? -5.82236  45.89036  16.18526  1.000 28.71565  ?  132 VAL   D CB    1 
ATOM   4980 C  CG1   . VAL   D 2 133 ? -6.58557  46.90214  17.05393  1.000 22.59796  ?  132 VAL   D CG1   1 
ATOM   4981 C  CG2   . VAL   D 2 133 ? -6.68413  44.70599  15.79908  1.000 22.67049  ?  132 VAL   D CG2   1 
ATOM   4982 N  N     . LYS   D 2 134 ? -5.32472  48.98785  14.93693  1.000 24.79256  ?  133 LYS   D N     1 
ATOM   4983 C  CA    . LYS   D 2 134 ? -4.86948  50.31093  15.32764  1.000 28.84962  ?  133 LYS   D CA    1 
ATOM   4984 C  C     . LYS   D 2 134 ? -5.63039  50.78804  16.55215  1.000 30.81411  ?  133 LYS   D C     1 
ATOM   4985 O  O     . LYS   D 2 134 ? -5.03359  51.04385  17.60075  1.000 36.47267  ?  133 LYS   D O     1 
ATOM   4986 C  CB    . LYS   D 2 134 ? -5.04611  51.29019  14.15710  1.000 28.84636  ?  133 LYS   D CB    1 
ATOM   4987 C  CG    . LYS   D 2 134 ? -4.38474  52.63675  14.35247  1.000 38.36085  ?  133 LYS   D CG    1 
ATOM   4988 C  CD    . LYS   D 2 134 ? -4.61396  53.52565  13.14171  1.000 40.45238  ?  133 LYS   D CD    1 
ATOM   4989 C  CE    . LYS   D 2 134 ? -3.91959  54.86159  13.29843  1.000 41.42836  ?  133 LYS   D CE    1 
ATOM   4990 N  NZ    . LYS   D 2 134 ? -4.41192  55.82916  12.28448  1.000 48.70881  ?  133 LYS   D NZ    1 
ATOM   4991 N  N     . GLU   D 2 135 ? -6.95187  50.86223  16.44594  1.000 32.75957  ?  134 GLU   D N     1 
ATOM   4992 C  CA    . GLU   D 2 135 ? -7.79804  51.20910  17.57209  1.000 40.35554  ?  134 GLU   D CA    1 
ATOM   4993 C  C     . GLU   D 2 135 ? -8.89480  50.17127  17.73915  1.000 33.59213  ?  134 GLU   D C     1 
ATOM   4994 O  O     . GLU   D 2 135 ? -9.35208  49.55137  16.77325  1.000 29.14005  ?  134 GLU   D O     1 
ATOM   4995 C  CB    . GLU   D 2 135 ? -8.39310  52.60638  17.39679  1.000 37.57580  ?  134 GLU   D CB    1 
ATOM   4996 C  CG    . GLU   D 2 135 ? -7.41270  53.66529  17.88699  1.000 46.16015  ?  134 GLU   D CG    1 
ATOM   4997 C  CD    . GLU   D 2 135 ? -7.76085  55.04716  17.41807  1.000 59.23548  ?  134 GLU   D CD    1 
ATOM   4998 O  OE1   . GLU   D 2 135 ? -8.31828  55.17816  16.30895  1.000 68.61888  ?  134 GLU   D OE1   1 
ATOM   4999 O  OE2   . GLU   D 2 135 ? -7.48088  56.00341  18.16941  1.000 77.17980  -1 134 GLU   D OE2   1 
ATOM   5000 N  N     . GLY   D 2 136 ? -9.28928  49.96745  18.98977  1.000 27.98509  ?  135 GLY   D N     1 
ATOM   5001 C  CA    . GLY   D 2 136 ? -10.35183 49.05152  19.27788  1.000 24.26527  ?  135 GLY   D CA    1 
ATOM   5002 C  C     . GLY   D 2 136 ? -9.90682  47.64675  19.55602  1.000 22.32543  ?  135 GLY   D C     1 
ATOM   5003 O  O     . GLY   D 2 136 ? -10.68269 46.71811  19.32065  1.000 25.59311  ?  135 GLY   D O     1 
ATOM   5004 N  N     . MET   D 2 137 ? -8.67196  47.45106  20.02475  1.000 27.15572  ?  136 MET   D N     1 
ATOM   5005 C  CA    . MET   D 2 137 ? -8.28740  46.13047  20.50244  1.000 23.75938  ?  136 MET   D CA    1 
ATOM   5006 C  C     . MET   D 2 137 ? -9.19715  45.65338  21.63264  1.000 30.64138  ?  136 MET   D C     1 
ATOM   5007 O  O     . MET   D 2 137 ? -9.35052  44.44187  21.82875  1.000 28.90255  ?  136 MET   D O     1 
ATOM   5008 C  CB    . MET   D 2 137 ? -6.82887  46.12499  20.95654  1.000 24.02208  ?  136 MET   D CB    1 
ATOM   5009 C  CG    . MET   D 2 137 ? -6.22046  44.71708  21.09812  1.000 25.35986  ?  136 MET   D CG    1 
ATOM   5010 S  SD    . MET   D 2 137 ? -6.31964  43.75601  19.53476  1.000 31.49616  ?  136 MET   D SD    1 
ATOM   5011 C  CE    . MET   D 2 137 ? -6.53889  42.09647  20.16195  1.000 28.76517  ?  136 MET   D CE    1 
ATOM   5012 N  N     . ASN   D 2 138 ? -9.84434  46.56551  22.36084  1.000 28.60776  ?  137 ASN   D N     1 
ATOM   5013 C  CA    . ASN   D 2 138 ? -10.72181 46.07381  23.41850  1.000 31.93806  ?  137 ASN   D CA    1 
ATOM   5014 C  C     . ASN   D 2 138 ? -11.98359 45.46448  22.84426  1.000 25.28526  ?  137 ASN   D C     1 
ATOM   5015 O  O     . ASN   D 2 138 ? -12.58272 44.58265  23.47184  1.000 26.86853  ?  137 ASN   D O     1 
ATOM   5016 C  CB    . ASN   D 2 138 ? -11.04757 47.16752  24.44782  1.000 25.57945  ?  137 ASN   D CB    1 
ATOM   5017 C  CG    . ASN   D 2 138 ? -11.43235 48.49753  23.83698  1.000 29.63700  ?  137 ASN   D CG    1 
ATOM   5018 O  OD1   . ASN   D 2 138 ? -11.60550 48.65048  22.63335  1.000 32.36021  ?  137 ASN   D OD1   1 
ATOM   5019 N  ND2   . ASN   D 2 138 ? -11.57341 49.48991  24.70233  1.000 40.81611  ?  137 ASN   D ND2   1 
ATOM   5020 N  N     . ILE   D 2 139 ? -12.37219 45.87832  21.63824  1.000 25.71503  ?  138 ILE   D N     1 
ATOM   5021 C  CA    . ILE   D 2 139 ? -13.49546 45.23831  20.96321  1.000 29.07066  ?  138 ILE   D CA    1 
ATOM   5022 C  C     . ILE   D 2 139 ? -13.13457 43.81102  20.58278  1.000 28.78476  ?  138 ILE   D C     1 
ATOM   5023 O  O     . ILE   D 2 139 ? -13.94228 42.88677  20.73614  1.000 23.63915  ?  138 ILE   D O     1 
ATOM   5024 C  CB    . ILE   D 2 139 ? -13.91744 46.05606  19.72701  1.000 27.59063  ?  138 ILE   D CB    1 
ATOM   5025 C  CG1   . ILE   D 2 139 ? -14.05657 47.54935  20.06694  1.000 26.58074  ?  138 ILE   D CG1   1 
ATOM   5026 C  CG2   . ILE   D 2 139 ? -15.21559 45.51151  19.17528  1.000 25.45517  ?  138 ILE   D CG2   1 
ATOM   5027 C  CD1   . ILE   D 2 139 ? -15.19171 47.81582  21.07053  1.000 28.58976  ?  138 ILE   D CD1   1 
ATOM   5028 N  N     . VAL   D 2 140 ? -11.91905 43.60695  20.06557  1.000 31.17982  ?  139 VAL   D N     1 
ATOM   5029 C  CA    . VAL   D 2 140 ? -11.51475 42.25984  19.67054  1.000 28.15607  ?  139 VAL   D CA    1 
ATOM   5030 C  C     . VAL   D 2 140 ? -11.45401 41.35885  20.89154  1.000 25.51957  ?  139 VAL   D C     1 
ATOM   5031 O  O     . VAL   D 2 140 ? -11.85431 40.19468  20.83890  1.000 25.54587  ?  139 VAL   D O     1 
ATOM   5032 C  CB    . VAL   D 2 140 ? -10.17086 42.28690  18.91188  1.000 29.00116  ?  139 VAL   D CB    1 
ATOM   5033 C  CG1   . VAL   D 2 140 ? -9.64772  40.85049  18.74168  1.000 25.78722  ?  139 VAL   D CG1   1 
ATOM   5034 C  CG2   . VAL   D 2 140 ? -10.34290 42.95315  17.52386  1.000 26.30370  ?  139 VAL   D CG2   1 
ATOM   5035 N  N     . GLU   D 2 141 ? -10.96117 41.88390  22.01182  1.000 26.22013  ?  140 GLU   D N     1 
ATOM   5036 C  CA    . GLU   D 2 141 ? -10.97441 41.11819  23.25877  1.000 31.09775  ?  140 GLU   D CA    1 
ATOM   5037 C  C     . GLU   D 2 141 ? -12.39654 40.81493  23.72345  1.000 26.29727  ?  140 GLU   D C     1 
ATOM   5038 O  O     . GLU   D 2 141 ? -12.67522 39.71000  24.19974  1.000 27.22298  ?  140 GLU   D O     1 
ATOM   5039 C  CB    . GLU   D 2 141 ? -10.21280 41.88159  24.33972  1.000 31.15748  ?  140 GLU   D CB    1 
ATOM   5040 C  CG    . GLU   D 2 141 ? -8.75488  42.14220  23.99785  1.000 30.02208  ?  140 GLU   D CG    1 
ATOM   5041 C  CD    . GLU   D 2 141 ? -8.15321  43.21090  24.90158  1.000 41.63867  ?  140 GLU   D CD    1 
ATOM   5042 O  OE1   . GLU   D 2 141 ? -8.92911  43.93866  25.55866  1.000 37.98255  ?  140 GLU   D OE1   1 
ATOM   5043 O  OE2   . GLU   D 2 141 ? -6.91385  43.32676  24.94769  1.000 42.80355  -1 140 GLU   D OE2   1 
ATOM   5044 N  N     . ALA   D 2 142 ? -13.30586 41.79043  23.61769  1.000 24.36883  ?  141 ALA   D N     1 
ATOM   5045 C  CA    . ALA   D 2 142 ? -14.69888 41.53735  23.97145  1.000 26.78048  ?  141 ALA   D CA    1 
ATOM   5046 C  C     . ALA   D 2 142 ? -15.29142 40.41161  23.13515  1.000 25.93572  ?  141 ALA   D C     1 
ATOM   5047 O  O     . ALA   D 2 142 ? -16.16650 39.68413  23.60973  1.000 27.76538  ?  141 ALA   D O     1 
ATOM   5048 C  CB    . ALA   D 2 142 ? -15.53566 42.80955  23.79598  1.000 28.23534  ?  141 ALA   D CB    1 
ATOM   5049 N  N     . MET   D 2 143 ? -14.81511 40.24466  21.90243  1.000 25.21016  ?  142 MET   D N     1 
ATOM   5050 C  CA    . MET   D 2 143 ? -15.34757 39.22959  21.00369  1.000 26.36829  ?  142 MET   D CA    1 
ATOM   5051 C  C     . MET   D 2 143 ? -14.97838 37.82852  21.45513  1.000 27.24041  ?  142 MET   D C     1 
ATOM   5052 O  O     . MET   D 2 143 ? -15.71751 36.88332  21.17400  1.000 25.65692  ?  142 MET   D O     1 
ATOM   5053 C  CB    . MET   D 2 143 ? -14.82372 39.47244  19.58435  1.000 25.82050  ?  142 MET   D CB    1 
ATOM   5054 C  CG    . MET   D 2 143 ? -15.33363 40.77077  18.93883  1.000 29.31609  ?  142 MET   D CG    1 
ATOM   5055 S  SD    . MET   D 2 143 ? -14.49453 41.24446  17.39663  1.000 33.37010  ?  142 MET   D SD    1 
ATOM   5056 C  CE    . MET   D 2 143 ? -14.71802 39.74826  16.41644  1.000 28.62220  ?  142 MET   D CE    1 
ATOM   5057 N  N     . GLU   D 2 144 ? -13.85536 37.68523  22.16934  1.000 27.52714  ?  143 GLU   D N     1 
ATOM   5058 C  CA    . GLU   D 2 144 ? -13.31039 36.36807  22.49063  1.000 28.12250  ?  143 GLU   D CA    1 
ATOM   5059 C  C     . GLU   D 2 144 ? -14.28267 35.52295  23.31246  1.000 36.73915  ?  143 GLU   D C     1 
ATOM   5060 O  O     . GLU   D 2 144 ? -14.34566 34.30086  23.13447  1.000 35.62881  ?  143 GLU   D O     1 
ATOM   5061 C  CB    . GLU   D 2 144 ? -11.97946 36.52145  23.24268  1.000 31.30477  ?  143 GLU   D CB    1 
ATOM   5062 C  CG    . GLU   D 2 144 ? -10.72574 36.53679  22.36910  1.000 32.05833  ?  143 GLU   D CG    1 
ATOM   5063 C  CD    . GLU   D 2 144 ? -9.45843  36.15934  23.15229  1.000 33.29282  ?  143 GLU   D CD    1 
ATOM   5064 O  OE1   . GLU   D 2 144 ? -9.22539  36.74669  24.22502  1.000 32.59409  ?  143 GLU   D OE1   1 
ATOM   5065 O  OE2   . GLU   D 2 144 ? -8.68596  35.27238  22.69508  1.000 36.79289  -1 143 GLU   D OE2   1 
ATOM   5066 N  N     . ARG   D 2 145 ? -15.03130 36.13839  24.23576  1.000 28.42642  ?  144 ARG   D N     1 
ATOM   5067 C  CA    . ARG   D 2 145 ? -15.93829 35.34492  25.06280  1.000 31.96734  ?  144 ARG   D CA    1 
ATOM   5068 C  C     . ARG   D 2 145 ? -17.10618 34.75513  24.29126  1.000 36.07905  ?  144 ARG   D C     1 
ATOM   5069 O  O     . ARG   D 2 145 ? -17.83328 33.92036  24.84484  1.000 42.13557  ?  144 ARG   D O     1 
ATOM   5070 C  CB    . ARG   D 2 145 ? -16.49271 36.17120  26.21048  1.000 36.86297  ?  144 ARG   D CB    1 
ATOM   5071 C  CG    . ARG   D 2 145 ? -17.66717 37.04916  25.81732  1.000 38.43905  ?  144 ARG   D CG    1 
ATOM   5072 C  CD    . ARG   D 2 145 ? -18.27948 37.69477  27.04912  1.000 41.27640  ?  144 ARG   D CD    1 
ATOM   5073 N  NE    . ARG   D 2 145 ? -19.18475 38.79342  26.72944  1.000 39.04057  ?  144 ARG   D NE    1 
ATOM   5074 C  CZ    . ARG   D 2 145 ? -20.49701 38.77392  26.92502  1.000 43.92253  ?  144 ARG   D CZ    1 
ATOM   5075 N  NH1   . ARG   D 2 145 ? -21.12146 37.67683  27.32177  1.000 43.64124  ?  144 ARG   D NH1   1 
ATOM   5076 N  NH2   . ARG   D 2 145 ? -21.19768 39.89270  26.74074  1.000 49.13876  ?  144 ARG   D NH2   1 
ATOM   5077 N  N     . PHE   D 2 146 ? -17.32456 35.16110  23.05039  1.000 29.85548  ?  145 PHE   D N     1 
ATOM   5078 C  CA    . PHE   D 2 146 ? -18.32450 34.49048  22.23806  1.000 30.93275  ?  145 PHE   D CA    1 
ATOM   5079 C  C     . PHE   D 2 146 ? -17.76540 33.27148  21.51393  1.000 30.23041  ?  145 PHE   D C     1 
ATOM   5080 O  O     . PHE   D 2 146 ? -18.53867 32.54451  20.89265  1.000 28.06934  ?  145 PHE   D O     1 
ATOM   5081 C  CB    . PHE   D 2 146 ? -18.95268 35.49928  21.27227  1.000 28.93748  ?  145 PHE   D CB    1 
ATOM   5082 C  CG    . PHE   D 2 146 ? -19.53760 36.70175  21.99177  1.000 29.64306  ?  145 PHE   D CG    1 
ATOM   5083 C  CD1   . PHE   D 2 146 ? -20.67890 36.57110  22.76312  1.000 36.69000  ?  145 PHE   D CD1   1 
ATOM   5084 C  CD2   . PHE   D 2 146 ? -18.91805 37.93888  21.94248  1.000 31.13861  ?  145 PHE   D CD2   1 
ATOM   5085 C  CE1   . PHE   D 2 146 ? -21.21382 37.66558  23.45461  1.000 33.50083  ?  145 PHE   D CE1   1 
ATOM   5086 C  CE2   . PHE   D 2 146 ? -19.44096 39.03233  22.63300  1.000 32.25803  ?  145 PHE   D CE2   1 
ATOM   5087 C  CZ    . PHE   D 2 146 ? -20.60177 38.88678  23.39328  1.000 28.38951  ?  145 PHE   D CZ    1 
ATOM   5088 N  N     . GLY   D 2 147 ? -16.46760 32.98485  21.66058  1.000 25.48086  ?  146 GLY   D N     1 
ATOM   5089 C  CA    . GLY   D 2 147 ? -15.84474 31.82677  21.05247  1.000 27.24760  ?  146 GLY   D CA    1 
ATOM   5090 C  C     . GLY   D 2 147 ? -15.87688 30.60290  21.94534  1.000 31.51760  ?  146 GLY   D C     1 
ATOM   5091 O  O     . GLY   D 2 147 ? -16.62819 30.53425  22.92123  1.000 29.15419  ?  146 GLY   D O     1 
ATOM   5092 N  N     . SER   D 2 148 ? -15.01595 29.64317  21.62334  1.000 24.35222  ?  147 SER   D N     1 
ATOM   5093 C  CA    . SER   D 2 148 ? -14.98278 28.34062  22.28300  1.000 28.17379  ?  147 SER   D CA    1 
ATOM   5094 C  C     . SER   D 2 148 ? -13.74816 27.57063  21.81002  1.000 32.34363  ?  147 SER   D C     1 
ATOM   5095 O  O     . SER   D 2 148 ? -13.00240 28.01092  20.92408  1.000 24.63915  ?  147 SER   D O     1 
ATOM   5096 C  CB    . SER   D 2 148 ? -16.24911 27.53776  21.98737  1.000 24.60240  ?  147 SER   D CB    1 
ATOM   5097 O  OG    . SER   D 2 148 ? -16.32914 27.25256  20.58313  1.000 24.47380  ?  147 SER   D OG    1 
ATOM   5098 N  N     . ARG   D 2 149 ? -13.57327 26.37102  22.37049  1.000 27.09835  ?  148 ARG   D N     1 
ATOM   5099 C  CA    . ARG   D 2 149 ? -12.35745 25.60804  22.10285  1.000 29.49965  ?  148 ARG   D CA    1 
ATOM   5100 C  C     . ARG   D 2 149 ? -12.18622 25.29329  20.61817  1.000 28.56154  ?  148 ARG   D C     1 
ATOM   5101 O  O     . ARG   D 2 149 ? -11.07651 25.41636  20.08412  1.000 25.67644  ?  148 ARG   D O     1 
ATOM   5102 C  CB    . ARG   D 2 149 ? -12.36342 24.32651  22.91070  1.000 32.17070  ?  148 ARG   D CB    1 
ATOM   5103 C  CG    . ARG   D 2 149 ? -11.19969 23.42042  22.60951  1.000 29.47846  ?  148 ARG   D CG    1 
ATOM   5104 C  CD    . ARG   D 2 149 ? -11.17761 22.30645  23.60900  1.000 31.16567  ?  148 ARG   D CD    1 
ATOM   5105 N  NE    . ARG   D 2 149 ? -10.03723 21.42819  23.40987  1.000 29.70490  ?  148 ARG   D NE    1 
ATOM   5106 C  CZ    . ARG   D 2 149 ? -10.08017 20.32681  22.68224  1.000 32.57082  ?  148 ARG   D CZ    1 
ATOM   5107 N  NH1   . ARG   D 2 149 ? -11.19474 19.94429  22.08265  1.000 33.60161  ?  148 ARG   D NH1   1 
ATOM   5108 N  NH2   . ARG   D 2 149 ? -8.97688  19.58912  22.55568  1.000 33.52757  ?  148 ARG   D NH2   1 
ATOM   5109 N  N     . ASN   D 2 150 ? -13.26246 24.89589  19.93051  1.000 30.37510  ?  149 ASN   D N     1 
ATOM   5110 C  CA    . ASN   D 2 150 ? -13.18866 24.53755  18.51213  1.000 30.74494  ?  149 ASN   D CA    1 
ATOM   5111 C  C     . ASN   D 2 150 ? -13.57306 25.68383  17.57071  1.000 29.43151  ?  149 ASN   D C     1 
ATOM   5112 O  O     . ASN   D 2 150 ? -13.60884 25.49071  16.34971  1.000 28.86778  ?  149 ASN   D O     1 
ATOM   5113 C  CB    . ASN   D 2 150 ? -14.05285 23.28898  18.23894  1.000 28.36154  ?  149 ASN   D CB    1 
ATOM   5114 C  CG    . ASN   D 2 150 ? -15.52188 23.59954  18.06910  1.000 31.48263  ?  149 ASN   D CG    1 
ATOM   5115 O  OD1   . ASN   D 2 150 ? -16.02668 24.61630  18.55319  1.000 31.54785  ?  149 ASN   D OD1   1 
ATOM   5116 N  ND2   . ASN   D 2 150 ? -16.23094 22.71143  17.36522  1.000 33.70671  ?  149 ASN   D ND2   1 
ATOM   5117 N  N     . GLY   D 2 151 ? -13.86091 26.86082  18.10140  1.000 24.86191  ?  150 GLY   D N     1 
ATOM   5118 C  CA    . GLY   D 2 151 ? -14.13208 28.03064  17.30933  1.000 26.64841  ?  150 GLY   D CA    1 
ATOM   5119 C  C     . GLY   D 2 151 ? -15.59550 28.41345  17.17935  1.000 27.64664  ?  150 GLY   D C     1 
ATOM   5120 O  O     . GLY   D 2 151 ? -15.88074 29.57077  16.84605  1.000 25.30917  ?  150 GLY   D O     1 
ATOM   5121 N  N     . LYS   D 2 152 ? -16.52656 27.48408  17.39543  1.000 26.02247  ?  151 LYS   D N     1 
ATOM   5122 C  CA    . LYS   D 2 152 ? -17.93674 27.82166  17.23651  1.000 25.61079  ?  151 LYS   D CA    1 
ATOM   5123 C  C     . LYS   D 2 152 ? -18.30258 28.96682  18.16424  1.000 29.06196  ?  151 LYS   D C     1 
ATOM   5124 O  O     . LYS   D 2 152 ? -17.92560 28.98763  19.34188  1.000 30.61173  ?  151 LYS   D O     1 
ATOM   5125 C  CB    . LYS   D 2 152 ? -18.84190 26.61236  17.52238  1.000 29.34594  ?  151 LYS   D CB    1 
ATOM   5126 C  CG    . LYS   D 2 152 ? -18.54251 25.36205  16.69516  1.000 39.41144  ?  151 LYS   D CG    1 
ATOM   5127 C  CD    . LYS   D 2 152 ? -18.58965 25.59598  15.17028  1.000 47.77763  ?  151 LYS   D CD    1 
ATOM   5128 C  CE    . LYS   D 2 152 ? -17.94391 24.42064  14.40554  1.000 43.07663  ?  151 LYS   D CE    1 
ATOM   5129 N  NZ    . LYS   D 2 152 ? -18.92122 23.69891  13.52814  1.000 44.38747  ?  151 LYS   D NZ    1 
ATOM   5130 N  N     . THR   D 2 153 ? -19.01702 29.93773  17.62461  1.000 28.40255  ?  152 THR   D N     1 
ATOM   5131 C  CA    . THR   D 2 153 ? -19.41036 31.09488  18.39705  1.000 29.48217  ?  152 THR   D CA    1 
ATOM   5132 C  C     . THR   D 2 153 ? -20.80448 30.86212  18.97367  1.000 30.98848  ?  152 THR   D C     1 
ATOM   5133 O  O     . THR   D 2 153 ? -21.63531 30.17752  18.37138  1.000 27.95040  ?  152 THR   D O     1 
ATOM   5134 C  CB    . THR   D 2 153 ? -19.35111 32.37379  17.55499  1.000 32.80775  ?  152 THR   D CB    1 
ATOM   5135 O  OG1   . THR   D 2 153 ? -20.32634 32.34480  16.49983  1.000 29.62705  ?  152 THR   D OG1   1 
ATOM   5136 C  CG2   . THR   D 2 153 ? -17.96564 32.51907  16.92240  1.000 29.24276  ?  152 THR   D CG2   1 
ATOM   5137 N  N     . SER   D 2 154 ? -21.02460 31.37933  20.17486  1.000 31.44015  ?  153 SER   D N     1 
ATOM   5138 C  CA    . SER   D 2 154 ? -22.30589 31.25699  20.85581  1.000 33.29607  ?  153 SER   D CA    1 
ATOM   5139 C  C     . SER   D 2 154 ? -23.26343 32.38481  20.51442  1.000 37.31365  ?  153 SER   D C     1 
ATOM   5140 O  O     . SER   D 2 154 ? -24.42893 32.33090  20.91892  1.000 30.02635  ?  153 SER   D O     1 
ATOM   5141 C  CB    . SER   D 2 154 ? -22.10120 31.23226  22.36328  1.000 33.09761  ?  153 SER   D CB    1 
ATOM   5142 O  OG    . SER   D 2 154 ? -21.34499 32.36274  22.75451  1.000 31.14905  ?  153 SER   D OG    1 
ATOM   5143 N  N     . LYS   D 2 155 ? -22.78613 33.41929  19.82823  1.000 33.13231  ?  154 LYS   D N     1 
ATOM   5144 C  CA    . LYS   D 2 155 ? -23.63264 34.48632  19.32806  1.000 32.64595  ?  154 LYS   D CA    1 
ATOM   5145 C  C     . LYS   D 2 155 ? -23.13097 34.86372  17.94491  1.000 32.08706  ?  154 LYS   D C     1 
ATOM   5146 O  O     . LYS   D 2 155 ? -21.98599 34.58829  17.58905  1.000 26.99749  ?  154 LYS   D O     1 
ATOM   5147 C  CB    . LYS   D 2 155 ? -23.63127 35.69374  20.25944  1.000 28.65296  ?  154 LYS   D CB    1 
ATOM   5148 C  CG    . LYS   D 2 155 ? -24.51328 35.48834  21.47074  1.000 37.76052  ?  154 LYS   D CG    1 
ATOM   5149 C  CD    . LYS   D 2 155 ? -24.58358 36.74338  22.33639  1.000 33.42601  ?  154 LYS   D CD    1 
ATOM   5150 C  CE    . LYS   D 2 155 ? -25.39330 36.44934  23.60059  1.000 36.22468  ?  154 LYS   D CE    1 
ATOM   5151 N  NZ    . LYS   D 2 155 ? -25.22083 37.53701  24.57910  1.000 44.72667  ?  154 LYS   D NZ    1 
ATOM   5152 N  N     . LYS   D 2 156 ? -24.00302 35.47484  17.15822  1.000 30.83383  ?  155 LYS   D N     1 
ATOM   5153 C  CA    . LYS   D 2 156 ? -23.64018 35.88510  15.80617  1.000 35.00339  ?  155 LYS   D CA    1 
ATOM   5154 C  C     . LYS   D 2 156 ? -22.79375 37.14711  15.87756  1.000 32.80476  ?  155 LYS   D C     1 
ATOM   5155 O  O     . LYS   D 2 156 ? -23.29711 38.21561  16.24760  1.000 32.19967  ?  155 LYS   D O     1 
ATOM   5156 C  CB    . LYS   D 2 156 ? -24.89006 36.11667  14.96989  1.000 35.88532  ?  155 LYS   D CB    1 
ATOM   5157 C  CG    . LYS   D 2 156 ? -24.71695 35.75158  13.53296  1.000 39.71467  ?  155 LYS   D CG    1 
ATOM   5158 C  CD    . LYS   D 2 156 ? -26.05996 35.68729  12.83191  1.000 50.79882  ?  155 LYS   D CD    1 
ATOM   5159 C  CE    . LYS   D 2 156 ? -25.89292 35.21961  11.39643  1.000 54.80286  ?  155 LYS   D CE    1 
ATOM   5160 N  NZ    . LYS   D 2 156 ? -24.91552 36.08420  10.68163  1.000 56.84026  ?  155 LYS   D NZ    1 
ATOM   5161 N  N     . ILE   D 2 157 ? -21.51676 37.03641  15.50284  1.000 28.84449  ?  156 ILE   D N     1 
ATOM   5162 C  CA    . ILE   D 2 157 ? -20.58949 38.16574  15.51149  1.000 28.51920  ?  156 ILE   D CA    1 
ATOM   5163 C  C     . ILE   D 2 157 ? -20.44124 38.65276  14.07617  1.000 31.52169  ?  156 ILE   D C     1 
ATOM   5164 O  O     . ILE   D 2 157 ? -19.87872 37.93664  13.24174  1.000 30.85626  ?  156 ILE   D O     1 
ATOM   5165 C  CB    . ILE   D 2 157 ? -19.22162 37.77571  16.08758  1.000 32.00068  ?  156 ILE   D CB    1 
ATOM   5166 C  CG1   . ILE   D 2 157 ? -19.37759 36.99210  17.39684  1.000 27.89319  ?  156 ILE   D CG1   1 
ATOM   5167 C  CG2   . ILE   D 2 157 ? -18.35407 39.02372  16.26175  1.000 26.29780  ?  156 ILE   D CG2   1 
ATOM   5168 C  CD1   . ILE   D 2 157 ? -20.18593 37.71549  18.41829  1.000 27.58606  ?  156 ILE   D CD1   1 
ATOM   5169 N  N     . THR   D 2 158 ? -20.89125 39.87765  13.77747  1.000 27.33005  ?  157 THR   D N     1 
ATOM   5170 C  CA    . THR   D 2 158 ? -20.96300 40.32442  12.38789  1.000 32.17064  ?  157 THR   D CA    1 
ATOM   5171 C  C     . THR   D 2 158 ? -20.22699 41.63974  12.16657  1.000 27.06872  ?  157 THR   D C     1 
ATOM   5172 O  O     . THR   D 2 158 ? -20.10227 42.47820  13.06627  1.000 29.21357  ?  157 THR   D O     1 
ATOM   5173 C  CB    . THR   D 2 158 ? -22.42607 40.49915  11.90417  1.000 34.89521  ?  157 THR   D CB    1 
ATOM   5174 O  OG1   . THR   D 2 158 ? -23.10166 41.43697  12.75223  1.000 35.72405  ?  157 THR   D OG1   1 
ATOM   5175 C  CG2   . THR   D 2 158 ? -23.17236 39.17667  11.92131  1.000 31.98240  ?  157 THR   D CG2   1 
ATOM   5176 N  N     . ILE   D 2 159 ? -19.75082 41.81942  10.93832  1.000 28.08369  ?  158 ILE   D N     1 
ATOM   5177 C  CA    . ILE   D 2 159 ? -19.23576 43.10723  10.49871  1.000 24.88728  ?  158 ILE   D CA    1 
ATOM   5178 C  C     . ILE   D 2 159 ? -20.44536 43.87101  9.97440   1.000 28.52080  ?  158 ILE   D C     1 
ATOM   5179 O  O     . ILE   D 2 159 ? -20.82025 43.76404  8.80569   1.000 34.24904  ?  158 ILE   D O     1 
ATOM   5180 C  CB    . ILE   D 2 159 ? -18.14147 42.95641  9.45066   1.000 28.74162  ?  158 ILE   D CB    1 
ATOM   5181 C  CG1   . ILE   D 2 159 ? -17.00899 42.07556  9.98515   1.000 25.68735  ?  158 ILE   D CG1   1 
ATOM   5182 C  CG2   . ILE   D 2 159 ? -17.63000 44.31150  9.00250   1.000 26.09819  ?  158 ILE   D CG2   1 
ATOM   5183 C  CD1   . ILE   D 2 159 ? -16.04902 41.66024  8.85302   1.000 25.54054  ?  158 ILE   D CD1   1 
ATOM   5184 N  N     . ALA   D 2 160 ? -21.06670 44.66318  10.85317  1.000 35.42473  ?  159 ALA   D N     1 
ATOM   5185 C  CA    . ALA   D 2 160 ? -22.24599 45.42187  10.44374  1.000 31.20795  ?  159 ALA   D CA    1 
ATOM   5186 C  C     . ALA   D 2 160 ? -21.88507 46.52663  9.45608   1.000 30.80532  ?  159 ALA   D C     1 
ATOM   5187 O  O     . ALA   D 2 160 ? -22.65957 46.82144  8.53875   1.000 34.48484  ?  159 ALA   D O     1 
ATOM   5188 C  CB    . ALA   D 2 160 ? -22.96192 45.99578  11.67261  1.000 24.75851  ?  159 ALA   D CB    1 
ATOM   5189 N  N     . ASP   D 2 161 ? -20.72412 47.14490  9.61030   1.000 34.14026  ?  160 ASP   D N     1 
ATOM   5190 C  CA    . ASP   D 2 161 ? -20.31241 48.12639  8.61412   1.000 37.32681  ?  160 ASP   D CA    1 
ATOM   5191 C  C     . ASP   D 2 161 ? -18.79143 48.16886  8.56272   1.000 33.79101  ?  160 ASP   D C     1 
ATOM   5192 O  O     . ASP   D 2 161 ? -18.10633 47.81241  9.52737   1.000 31.41087  ?  160 ASP   D O     1 
ATOM   5193 C  CB    . ASP   D 2 161 ? -20.90105 49.51111  8.91677   1.000 33.13600  ?  160 ASP   D CB    1 
ATOM   5194 C  CG    . ASP   D 2 161 ? -20.84356 50.46666  7.71715   1.000 34.86869  ?  160 ASP   D CG    1 
ATOM   5195 O  OD1   . ASP   D 2 161 ? -20.59707 50.02304  6.57579   1.000 39.08902  ?  160 ASP   D OD1   1 
ATOM   5196 O  OD2   . ASP   D 2 161 ? -21.02561 51.67759  7.93365   1.000 38.07750  -1 160 ASP   D OD2   1 
ATOM   5197 N  N     . CYS   D 2 162 ? -18.27604 48.61324  7.41838   1.000 27.23079  ?  161 CYS   D N     1 
ATOM   5198 C  CA    . CYS   D 2 162 ? -16.83696 48.69788  7.20302   1.000 34.00193  ?  161 CYS   D CA    1 
ATOM   5199 C  C     . CYS   D 2 162 ? -16.55451 49.66463  6.06110   1.000 36.41100  ?  161 CYS   D C     1 
ATOM   5200 O  O     . CYS   D 2 162 ? -17.41806 49.94874  5.22636   1.000 35.47586  ?  161 CYS   D O     1 
ATOM   5201 C  CB    . CYS   D 2 162 ? -16.20638 47.32224  6.90913   1.000 32.42663  ?  161 CYS   D CB    1 
ATOM   5202 S  SG    . CYS   D 2 162 ? -17.04580 46.29280  5.67351   1.000 33.67642  ?  161 CYS   D SG    1 
ATOM   5203 N  N     . GLY   D 2 163 ? -15.32652 50.16426  6.04288   1.000 32.23698  ?  162 GLY   D N     1 
ATOM   5204 C  CA    . GLY   D 2 163 ? -14.92629 51.13298  5.04917   1.000 32.47100  ?  162 GLY   D CA    1 
ATOM   5205 C  C     . GLY   D 2 163 ? -13.51473 51.58823  5.33788   1.000 33.31863  ?  162 GLY   D C     1 
ATOM   5206 O  O     . GLY   D 2 163 ? -12.82543 51.01597  6.18346   1.000 34.97584  ?  162 GLY   D O     1 
ATOM   5207 N  N     . GLN   D 2 164 ? -13.10815 52.64385  4.63902   1.000 35.65863  ?  163 GLN   D N     1 
ATOM   5208 C  CA    . GLN   D 2 164 ? -11.76458 53.19472  4.75132   1.000 33.84588  ?  163 GLN   D CA    1 
ATOM   5209 C  C     . GLN   D 2 164 ? -11.82587 54.54020  5.46434   1.000 34.68618  ?  163 GLN   D C     1 
ATOM   5210 O  O     . GLN   D 2 164 ? -12.78954 55.28982  5.30493   1.000 38.98492  ?  163 GLN   D O     1 
ATOM   5211 C  CB    . GLN   D 2 164 ? -11.12619 53.33676  3.36635   1.000 33.76806  ?  163 GLN   D CB    1 
ATOM   5212 C  CG    . GLN   D 2 164 ? -9.66002  53.74630  3.37147   1.000 38.56996  ?  163 GLN   D CG    1 
ATOM   5213 C  CD    . GLN   D 2 164 ? -9.01078  53.63676  2.00222   1.000 35.56301  ?  163 GLN   D CD    1 
ATOM   5214 O  OE1   . GLN   D 2 164 ? -9.65413  53.25079  1.02370   1.000 38.12014  ?  163 GLN   D OE1   1 
ATOM   5215 N  NE2   . GLN   D 2 164 ? -7.73503  53.97446  1.92781   1.000 32.00205  ?  163 GLN   D NE2   1 
ATOM   5216 N  N     . LEU   D 2 165 ? -10.82795 54.81882  6.29235   1.000 35.75317  ?  164 LEU   D N     1 
ATOM   5217 C  CA    . LEU   D 2 165 ? -10.78765 56.06321  7.05143   1.000 39.18327  ?  164 LEU   D CA    1 
ATOM   5218 C  C     . LEU   D 2 165 ? -9.84802  57.03334  6.35234   1.000 34.02665  ?  164 LEU   D C     1 
ATOM   5219 O  O     . LEU   D 2 165 ? -8.98034  56.58694  5.59785   1.000 37.93906  ?  164 LEU   D O     1 
ATOM   5220 C  CB    . LEU   D 2 165 ? -10.32230 55.82326  8.49822   1.000 37.50843  ?  164 LEU   D CB    1 
ATOM   5221 C  CG    . LEU   D 2 165 ? -11.21585 55.10236  9.51792   1.000 40.55527  ?  164 LEU   D CG    1 
ATOM   5222 C  CD1   . LEU   D 2 165 ? -10.45983 54.82861  10.80659  1.000 36.90751  ?  164 LEU   D CD1   1 
ATOM   5223 C  CD2   . LEU   D 2 165 ? -12.47433 55.89232  9.83585   1.000 40.13797  ?  164 LEU   D CD2   1 
HETATM 5224 P  PG    . GNP   E 3 .   ? -9.75196  18.04111  7.46892   1.000 27.49074  ?  201 GNP   A PG    1 
HETATM 5225 O  O1G   . GNP   E 3 .   ? -10.79155 18.22031  8.51218   1.000 23.01621  ?  201 GNP   A O1G   1 
HETATM 5226 O  O2G   . GNP   E 3 .   ? -8.75699  17.02156  7.99242   1.000 31.95651  ?  201 GNP   A O2G   1 
HETATM 5227 O  O3G   . GNP   E 3 .   ? -9.08383  19.39218  7.10284   1.000 24.76301  ?  201 GNP   A O3G   1 
HETATM 5228 N  N3B   . GNP   E 3 .   ? -10.56065 17.41510  6.09352   1.000 23.09911  ?  201 GNP   A N3B   1 
HETATM 5229 P  PB    . GNP   E 3 .   ? -11.52484 16.08336  6.11399   1.000 23.68122  ?  201 GNP   A PB    1 
HETATM 5230 O  O1B   . GNP   E 3 .   ? -12.56762 16.12864  7.21588   1.000 21.45624  ?  201 GNP   A O1B   1 
HETATM 5231 O  O2B   . GNP   E 3 .   ? -10.74657 14.81990  6.13668   1.000 21.76595  ?  201 GNP   A O2B   1 
HETATM 5232 O  O3A   . GNP   E 3 .   ? -12.27491 16.10808  4.67252   1.000 24.20267  ?  201 GNP   A O3A   1 
HETATM 5233 P  PA    . GNP   E 3 .   ? -13.66372 16.77014  4.37232   1.000 26.20591  ?  201 GNP   A PA    1 
HETATM 5234 O  O1A   . GNP   E 3 .   ? -13.74079 18.18951  4.71071   1.000 25.99676  ?  201 GNP   A O1A   1 
HETATM 5235 O  O2A   . GNP   E 3 .   ? -14.73667 15.81038  4.86479   1.000 25.90612  -1 201 GNP   A O2A   1 
HETATM 5236 O  "O5'" . GNP   E 3 .   ? -13.71105 16.60940  2.76793   1.000 30.03660  ?  201 GNP   A "O5'" 1 
HETATM 5237 C  "C5'" . GNP   E 3 .   ? -12.75912 17.29464  1.92688   1.000 29.34020  ?  201 GNP   A "C5'" 1 
HETATM 5238 C  "C4'" . GNP   E 3 .   ? -13.36018 17.53606  0.55920   1.000 28.63693  ?  201 GNP   A "C4'" 1 
HETATM 5239 O  "O4'" . GNP   E 3 .   ? -13.54447 16.27653  -0.12216  1.000 28.94813  ?  201 GNP   A "O4'" 1 
HETATM 5240 C  "C3'" . GNP   E 3 .   ? -14.72402 18.22267  0.55825   1.000 31.43737  ?  201 GNP   A "C3'" 1 
HETATM 5241 O  "O3'" . GNP   E 3 .   ? -14.85858 19.13658  -0.52283  1.000 36.58936  ?  201 GNP   A "O3'" 1 
HETATM 5242 C  "C2'" . GNP   E 3 .   ? -15.69246 17.04792  0.43255   1.000 31.80294  ?  201 GNP   A "C2'" 1 
HETATM 5243 O  "O2'" . GNP   E 3 .   ? -16.91434 17.42131  -0.18074  1.000 34.75565  ?  201 GNP   A "O2'" 1 
HETATM 5244 C  "C1'" . GNP   E 3 .   ? -14.90181 16.09086  -0.45423  1.000 23.35628  ?  201 GNP   A "C1'" 1 
HETATM 5245 N  N9    . GNP   E 3 .   ? -15.24604 14.68079  -0.21902  1.000 29.71169  ?  201 GNP   A N9    1 
HETATM 5246 C  C8    . GNP   E 3 .   ? -15.27249 14.01785  0.98890   1.000 29.83574  ?  201 GNP   A C8    1 
HETATM 5247 N  N7    . GNP   E 3 .   ? -15.63151 12.75974  0.87641   1.000 29.21243  ?  201 GNP   A N7    1 
HETATM 5248 C  C5    . GNP   E 3 .   ? -15.87469 12.59028  -0.47932  1.000 30.54884  ?  201 GNP   A C5    1 
HETATM 5249 C  C6    . GNP   E 3 .   ? -16.30673 11.43761  -1.23133  1.000 28.99806  ?  201 GNP   A C6    1 
HETATM 5250 O  O6    . GNP   E 3 .   ? -16.55876 10.31450  -0.80004  1.000 28.87438  ?  201 GNP   A O6    1 
HETATM 5251 N  N1    . GNP   E 3 .   ? -16.42092 11.71682  -2.58433  1.000 30.02777  ?  201 GNP   A N1    1 
HETATM 5252 C  C2    . GNP   E 3 .   ? -16.16616 12.93227  -3.16142  1.000 31.53723  ?  201 GNP   A C2    1 
HETATM 5253 N  N2    . GNP   E 3 .   ? -16.32749 13.02203  -4.48728  1.000 33.18652  ?  201 GNP   A N2    1 
HETATM 5254 N  N3    . GNP   E 3 .   ? -15.76219 13.99994  -2.47866  1.000 31.49190  ?  201 GNP   A N3    1 
HETATM 5255 C  C4    . GNP   E 3 .   ? -15.64387 13.76693  -1.15872  1.000 29.15395  ?  201 GNP   A C4    1 
HETATM 5256 MG MG    . MG    F 4 .   ? -12.69957 17.50419  8.70282   1.000 26.11108  ?  202 MG    A MG    1 
HETATM 5257 P  PG    . GNP   G 3 .   ? -26.63196 22.57037  39.02346  1.000 35.21906  ?  201 GNP   B PG    1 
HETATM 5258 O  O1G   . GNP   G 3 .   ? -26.18148 22.95852  37.63933  1.000 39.38638  ?  201 GNP   B O1G   1 
HETATM 5259 O  O2G   . GNP   G 3 .   ? -25.61819 21.71813  39.76346  1.000 32.11796  ?  201 GNP   B O2G   1 
HETATM 5260 O  O3G   . GNP   G 3 .   ? -27.98147 21.82271  38.87425  1.000 39.20682  ?  201 GNP   B O3G   1 
HETATM 5261 N  N3B   . GNP   G 3 .   ? -26.83799 24.04717  39.88673  1.000 44.44033  ?  201 GNP   B N3B   1 
HETATM 5262 P  PB    . GNP   G 3 .   ? -25.62266 25.14777  40.13067  1.000 38.38520  ?  201 GNP   B PB    1 
HETATM 5263 O  O1B   . GNP   G 3 .   ? -24.86446 25.38967  38.85100  1.000 37.38000  ?  201 GNP   B O1B   1 
HETATM 5264 O  O2B   . GNP   G 3 .   ? -24.66885 24.71206  41.21178  1.000 32.24178  ?  201 GNP   B O2B   1 
HETATM 5265 O  O3A   . GNP   G 3 .   ? -26.41588 26.51184  40.55221  1.000 40.77863  ?  201 GNP   B O3A   1 
HETATM 5266 P  PA    . GNP   G 3 .   ? -26.85122 27.71098  39.60914  1.000 37.95508  ?  201 GNP   B PA    1 
HETATM 5267 O  O1A   . GNP   G 3 .   ? -27.69445 27.40113  38.41610  1.000 37.26303  ?  201 GNP   B O1A   1 
HETATM 5268 O  O2A   . GNP   G 3 .   ? -25.59459 28.56402  39.45420  1.000 44.31245  -1 201 GNP   B O2A   1 
HETATM 5269 O  "O5'" . GNP   G 3 .   ? -27.73726 28.59255  40.57503  1.000 54.26042  ?  201 GNP   B "O5'" 1 
HETATM 5270 C  "C5'" . GNP   G 3 .   ? -28.92235 28.06203  41.20607  1.000 48.40327  ?  201 GNP   B "C5'" 1 
HETATM 5271 C  "C4'" . GNP   G 3 .   ? -29.87886 29.19386  41.50046  1.000 47.63480  ?  201 GNP   B "C4'" 1 
HETATM 5272 O  "O4'" . GNP   G 3 .   ? -29.36996 29.99665  42.58986  1.000 39.81049  ?  201 GNP   B "O4'" 1 
HETATM 5273 C  "C3'" . GNP   G 3 .   ? -30.14166 30.16341  40.34915  1.000 53.51918  ?  201 GNP   B "C3'" 1 
HETATM 5274 O  "O3'" . GNP   G 3 .   ? -31.48195 30.64879  40.35628  1.000 52.85919  ?  201 GNP   B "O3'" 1 
HETATM 5275 C  "C2'" . GNP   G 3 .   ? -29.14856 31.29243  40.62720  1.000 50.21296  ?  201 GNP   B "C2'" 1 
HETATM 5276 O  "O2'" . GNP   G 3 .   ? -29.61816 32.52613  40.10459  1.000 51.74123  ?  201 GNP   B "O2'" 1 
HETATM 5277 C  "C1'" . GNP   G 3 .   ? -29.14348 31.32611  42.15663  1.000 42.51815  ?  201 GNP   B "C1'" 1 
HETATM 5278 N  N9    . GNP   G 3 .   ? -27.86282 31.77161  42.71269  1.000 41.13245  ?  201 GNP   B N9    1 
HETATM 5279 C  C8    . GNP   G 3 .   ? -26.62460 31.26648  42.41228  1.000 51.64682  ?  201 GNP   B C8    1 
HETATM 5280 N  N7    . GNP   G 3 .   ? -25.64705 31.85209  43.06605  1.000 46.91658  ?  201 GNP   B N7    1 
HETATM 5281 C  C5    . GNP   G 3 .   ? -26.28248 32.79554  43.85094  1.000 52.70936  ?  201 GNP   B C5    1 
HETATM 5282 C  C6    . GNP   G 3 .   ? -25.75695 33.75536  44.79152  1.000 53.45233  ?  201 GNP   B C6    1 
HETATM 5283 O  O6    . GNP   G 3 .   ? -24.57609 33.93279  45.09416  1.000 48.42994  ?  201 GNP   B O6    1 
HETATM 5284 N  N1    . GNP   G 3 .   ? -26.76079 34.51349  45.36757  1.000 55.47871  ?  201 GNP   B N1    1 
HETATM 5285 C  C2    . GNP   G 3 .   ? -28.09921 34.39690  45.08884  1.000 54.29302  ?  201 GNP   B C2    1 
HETATM 5286 N  N2    . GNP   G 3 .   ? -28.92474 35.22401  45.73317  1.000 52.44725  ?  201 GNP   B N2    1 
HETATM 5287 N  N3    . GNP   G 3 .   ? -28.59859 33.51701  44.22186  1.000 51.26271  ?  201 GNP   B N3    1 
HETATM 5288 C  C4    . GNP   G 3 .   ? -27.65010 32.75529  43.64490  1.000 53.25792  ?  201 GNP   B C4    1 
HETATM 5289 MG MG    . MG    H 4 .   ? -25.02296 24.56160  36.91747  1.000 37.27619  ?  202 MG    B MG    1 
HETATM 5290 C  C1    . A1AHB I 5 .   ? -23.52032 13.02011  34.51623  1.000 32.33459  ?  201 A1AHB C C1    1 
HETATM 5291 C  C10   . A1AHB I 5 .   ? -29.63384 17.89555  35.50149  1.000 32.10326  ?  201 A1AHB C C10   1 
HETATM 5292 C  C11   . A1AHB I 5 .   ? -31.82149 16.87056  35.49195  1.000 32.68621  ?  201 A1AHB C C11   1 
HETATM 5293 C  C12   . A1AHB I 5 .   ? -33.26737 16.55743  35.64610  1.000 26.47802  ?  201 A1AHB C C12   1 
HETATM 5294 C  C13   . A1AHB I 5 .   ? -34.07538 17.41177  34.66073  1.000 27.75325  ?  201 A1AHB C C13   1 
HETATM 5295 C  C14   . A1AHB I 5 .   ? -34.83463 19.74616  34.56423  1.000 29.19330  ?  201 A1AHB C C14   1 
HETATM 5296 C  C15   . A1AHB I 5 .   ? -35.62408 20.76978  35.27747  1.000 30.78635  ?  201 A1AHB C C15   1 
HETATM 5297 C  C16   . A1AHB I 5 .   ? -35.38287 22.20765  34.89735  1.000 33.29476  ?  201 A1AHB C C16   1 
HETATM 5298 C  C17   . A1AHB I 5 .   ? -36.67711 21.57816  34.53120  1.000 32.70843  ?  201 A1AHB C C17   1 
HETATM 5299 C  C18   . A1AHB I 5 .   ? -37.96505 21.98585  35.20096  1.000 34.93061  ?  201 A1AHB C C18   1 
HETATM 5300 C  C19   . A1AHB I 5 .   ? -35.22214 16.57709  34.11562  1.000 29.12102  ?  201 A1AHB C C19   1 
HETATM 5301 C  C2    . A1AHB I 5 .   ? -24.04445 13.54410  33.20923  1.000 22.95672  ?  201 A1AHB C C2    1 
HETATM 5302 C  C20   . A1AHB I 5 .   ? -35.92827 14.84341  32.38681  1.000 21.84201  ?  201 A1AHB C C20   1 
HETATM 5303 C  C21   . A1AHB I 5 .   ? -35.34770 13.44826  32.50867  1.000 23.12464  ?  201 A1AHB C C21   1 
HETATM 5304 C  C22   . A1AHB I 5 .   ? -33.92809 13.40070  31.95793  1.000 22.83945  ?  201 A1AHB C C22   1 
HETATM 5305 C  C23   . A1AHB I 5 .   ? -33.02678 14.51366  32.51646  1.000 22.62099  ?  201 A1AHB C C23   1 
HETATM 5306 C  C24   . A1AHB I 5 .   ? -31.79649 14.63885  31.64997  1.000 25.43760  ?  201 A1AHB C C24   1 
HETATM 5307 C  C25   . A1AHB I 5 .   ? -29.84300 13.50980  30.88833  1.000 21.71928  ?  201 A1AHB C C25   1 
HETATM 5308 C  C26   . A1AHB I 5 .   ? -29.33184 12.07037  30.94527  1.000 25.77682  ?  201 A1AHB C C26   1 
HETATM 5309 C  C27   . A1AHB I 5 .   ? -28.26294 11.85548  29.86682  1.000 23.56137  ?  201 A1AHB C C27   1 
HETATM 5310 C  C28   . A1AHB I 5 .   ? -30.49290 11.11456  30.64893  1.000 22.03351  ?  201 A1AHB C C28   1 
HETATM 5311 C  C29   . A1AHB I 5 .   ? -28.76318 11.73953  32.34689  1.000 24.39855  ?  201 A1AHB C C29   1 
HETATM 5312 C  C3    . A1AHB I 5 .   ? -26.38503 14.31111  33.68215  1.000 28.37715  ?  201 A1AHB C C3    1 
HETATM 5313 C  C30   . A1AHB I 5 .   ? -27.60387 12.59825  32.76886  1.000 25.46923  ?  201 A1AHB C C30   1 
HETATM 5314 C  C31   . A1AHB I 5 .   ? -26.24511 12.35269  32.55919  1.000 24.73441  ?  201 A1AHB C C31   1 
HETATM 5315 C  C32   . A1AHB I 5 .   ? -25.66345 11.17029  31.90853  1.000 25.83419  ?  201 A1AHB C C32   1 
HETATM 5316 C  C33   . A1AHB I 5 .   ? -24.86398 11.23655  30.72622  1.000 25.56132  ?  201 A1AHB C C33   1 
HETATM 5317 C  C34   . A1AHB I 5 .   ? -24.61032 8.92306   30.72369  1.000 29.36608  ?  201 A1AHB C C34   1 
HETATM 5318 C  C35   . A1AHB I 5 .   ? -25.38863 8.77589   31.86991  1.000 33.21218  ?  201 A1AHB C C35   1 
HETATM 5319 C  C36   . A1AHB I 5 .   ? -25.91627 9.91720   32.46257  1.000 26.62110  ?  201 A1AHB C C36   1 
HETATM 5320 C  C37   . A1AHB I 5 .   ? -26.76706 7.31671   33.31715  1.000 37.07867  ?  201 A1AHB C C37   1 
HETATM 5321 C  C38   . A1AHB I 5 .   ? -26.87484 5.93863   33.92543  1.000 39.36042  ?  201 A1AHB C C38   1 
HETATM 5322 C  C39   . A1AHB I 5 .   ? -26.92045 3.58820   33.46422  1.000 43.09512  ?  201 A1AHB C C39   1 
HETATM 5323 C  C4    . A1AHB I 5 .   ? -27.69802 13.83796  33.47696  1.000 21.02615  ?  201 A1AHB C C4    1 
HETATM 5324 C  C40   . A1AHB I 5 .   ? -25.21761 5.02893   32.57323  1.000 40.31314  ?  201 A1AHB C C40   1 
HETATM 5325 C  C41   . A1AHB I 5 .   ? -24.94768 6.32254   31.83842  1.000 37.95537  ?  201 A1AHB C C41   1 
HETATM 5326 C  C42   . A1AHB I 5 .   ? -24.53010 12.54096  30.03230  1.000 28.91895  ?  201 A1AHB C C42   1 
HETATM 5327 C  C43   . A1AHB I 5 .   ? -24.86335 12.47091  28.55493  1.000 29.72279  ?  201 A1AHB C C43   1 
HETATM 5328 C  C44   . A1AHB I 5 .   ? -22.81919 14.20433  29.96471  1.000 26.26039  ?  201 A1AHB C C44   1 
HETATM 5329 C  C5    . A1AHB I 5 .   ? -28.76905 14.59898  33.94113  1.000 27.01203  ?  201 A1AHB C C5    1 
HETATM 5330 C  C6    . A1AHB I 5 .   ? -28.53045 15.79313  34.62020  1.000 29.41755  ?  201 A1AHB C C6    1 
HETATM 5331 C  C7    . A1AHB I 5 .   ? -27.21921 16.22953  34.80980  1.000 28.16512  ?  201 A1AHB C C7    1 
HETATM 5332 C  C8    . A1AHB I 5 .   ? -26.13580 15.50463  34.35717  1.000 27.10057  ?  201 A1AHB C C8    1 
HETATM 5333 C  C9    . A1AHB I 5 .   ? -29.65684 16.59976  35.10886  1.000 28.19690  ?  201 A1AHB C C9    1 
HETATM 5334 N  N1    . A1AHB I 5 .   ? -25.50050 13.40200  33.12809  1.000 22.80009  ?  201 A1AHB C N1    1 
HETATM 5335 N  N2    . A1AHB I 5 .   ? -34.53655 18.64799  35.27344  1.000 30.57676  ?  201 A1AHB C N2    1 
HETATM 5336 N  N3    . A1AHB I 5 .   ? -34.97003 15.76819  33.00417  1.000 26.41558  ?  201 A1AHB C N3    1 
HETATM 5337 N  N4    . A1AHB I 5 .   ? -33.68882 15.81527  32.42904  1.000 21.14504  ?  201 A1AHB C N4    1 
HETATM 5338 N  N5    . A1AHB I 5 .   ? -24.35016 10.12414  30.17474  1.000 30.17099  ?  201 A1AHB C N5    1 
HETATM 5339 N  N6    . A1AHB I 5 .   ? -25.65816 7.50012   32.37011  1.000 32.89752  ?  201 A1AHB C N6    1 
HETATM 5340 N  N7    . A1AHB I 5 .   ? -26.62535 4.91353   32.92317  1.000 38.50181  ?  201 A1AHB C N7    1 
HETATM 5341 N  N8    . A1AHB I 5 .   ? -30.91598 15.99847  35.14378  1.000 30.23792  ?  201 A1AHB C N8    1 
HETATM 5342 O  O1    . A1AHB I 5 .   ? -34.52292 19.87988  33.38299  1.000 28.80412  ?  201 A1AHB C O1    1 
HETATM 5343 O  O2    . A1AHB I 5 .   ? -36.32835 16.59414  34.63367  1.000 26.54799  ?  201 A1AHB C O2    1 
HETATM 5344 O  O3    . A1AHB I 5 .   ? -31.59189 15.55508  30.91016  1.000 20.52016  ?  201 A1AHB C O3    1 
HETATM 5345 O  O4    . A1AHB I 5 .   ? -30.98639 13.59028  31.78131  1.000 26.31153  ?  201 A1AHB C O4    1 
HETATM 5346 O  O5    . A1AHB I 5 .   ? -23.13626 12.83243  30.16544  1.000 29.38648  ?  201 A1AHB C O5    1 
HETATM 5347 S  S1    . A1AHB I 5 .   ? -31.22635 18.47513  35.72728  1.000 36.19700  ?  201 A1AHB C S1    1 
HETATM 5348 C  C1    . A1AHB J 5 .   ? -4.88694  20.55647  17.16032  1.000 29.19616  ?  201 A1AHB D C1    1 
HETATM 5349 C  C10   . A1AHB J 5 .   ? -7.62874  23.70910  10.44799  1.000 31.33098  ?  201 A1AHB D C10   1 
HETATM 5350 C  C11   . A1AHB J 5 .   ? -6.49186  25.67621  9.59035   1.000 29.03094  ?  201 A1AHB D C11   1 
HETATM 5351 C  C12   . A1AHB J 5 .   ? -6.06098  26.87263  8.79374   1.000 25.91521  ?  201 A1AHB D C12   1 
HETATM 5352 C  C13   . A1AHB J 5 .   ? -7.27768  27.78790  8.56754   1.000 24.69984  ?  201 A1AHB D C13   1 
HETATM 5353 C  C14   . A1AHB J 5 .   ? -9.18349  27.81879  7.00129   1.000 23.37986  ?  201 A1AHB D C14   1 
HETATM 5354 C  C15   . A1AHB J 5 .   ? -9.53927  27.83004  5.55682   1.000 21.90208  ?  201 A1AHB D C15   1 
HETATM 5355 C  C16   . A1AHB J 5 .   ? -11.00436 27.75815  5.20671   1.000 22.21094  ?  201 A1AHB D C16   1 
HETATM 5356 C  C17   . A1AHB J 5 .   ? -10.28253 29.04182  5.00815   1.000 25.85914  ?  201 A1AHB D C17   1 
HETATM 5357 C  C18   . A1AHB J 5 .   ? -9.98022  29.59353  3.63243   1.000 30.08090  ?  201 A1AHB D C18   1 
HETATM 5358 C  C19   . A1AHB J 5 .   ? -6.79583  29.22691  8.65619   1.000 23.70486  ?  201 A1AHB D C19   1 
HETATM 5359 C  C2    . A1AHB J 5 .   ? -5.97301  21.57419  17.36118  1.000 25.59275  ?  201 A1AHB D C2    1 
HETATM 5360 C  C20   . A1AHB J 5 .   ? -6.15277  31.13416  10.17655  1.000 18.64951  ?  201 A1AHB D C20   1 
HETATM 5361 C  C21   . A1AHB J 5 .   ? -5.03790  30.92269  11.18024  1.000 21.13642  ?  201 A1AHB D C21   1 
HETATM 5362 C  C22   . A1AHB J 5 .   ? -5.58242  30.17392  12.38894  1.000 20.60973  ?  201 A1AHB D C22   1 
HETATM 5363 C  C23   . A1AHB J 5 .   ? -6.29895  28.87492  11.98852  1.000 21.33125  ?  201 A1AHB D C23   1 
HETATM 5364 C  C24   . A1AHB J 5 .   ? -6.97463  28.28286  13.19608  1.000 23.82229  ?  201 A1AHB D C24   1 
HETATM 5365 C  C25   . A1AHB J 5 .   ? -6.61249  27.49977  15.41389  1.000 19.43870  ?  201 A1AHB D C25   1 
HETATM 5366 C  C26   . A1AHB J 5 .   ? -5.46055  27.42414  16.41214  1.000 22.47931  ?  201 A1AHB D C26   1 
HETATM 5367 C  C27   . A1AHB J 5 .   ? -6.01266  27.19489  17.82813  1.000 25.28438  ?  201 A1AHB D C27   1 
HETATM 5368 C  C28   . A1AHB J 5 .   ? -4.70993  28.76012  16.37977  1.000 23.27027  ?  201 A1AHB D C28   1 
HETATM 5369 C  C29   . A1AHB J 5 .   ? -4.46810  26.30169  16.06917  1.000 20.36673  ?  201 A1AHB D C29   1 
HETATM 5370 C  C3    . A1AHB J 5 .   ? -6.02776  22.98896  15.26512  1.000 25.32843  ?  201 A1AHB D C3    1 
HETATM 5371 C  C30   . A1AHB J 5 .   ? -5.05685  24.91981  16.03457  1.000 23.59494  ?  201 A1AHB D C30   1 
HETATM 5372 C  C31   . A1AHB J 5 .   ? -5.13751  23.99258  17.08613  1.000 26.36863  ?  201 A1AHB D C31   1 
HETATM 5373 C  C32   . A1AHB J 5 .   ? -4.60673  24.15570  18.44882  1.000 25.61429  ?  201 A1AHB D C32   1 
HETATM 5374 C  C33   . A1AHB J 5 .   ? -5.40169  24.13049  19.62514  1.000 26.91298  ?  201 A1AHB D C33   1 
HETATM 5375 C  C34   . A1AHB J 5 .   ? -3.53056  24.47384  20.95526  1.000 26.56892  ?  201 A1AHB D C34   1 
HETATM 5376 C  C35   . A1AHB J 5 .   ? -2.68472  24.50919  19.85438  1.000 29.71951  ?  201 A1AHB D C35   1 
HETATM 5377 C  C36   . A1AHB J 5 .   ? -3.23521  24.33814  18.59290  1.000 24.63692  ?  201 A1AHB D C36   1 
HETATM 5378 C  C37   . A1AHB J 5 .   ? -0.50598  25.13747  18.87415  1.000 26.96634  ?  201 A1AHB D C37   1 
HETATM 5379 C  C38   . A1AHB J 5 .   ? 0.98450   25.17620  19.12459  1.000 38.17280  ?  201 A1AHB D C38   1 
HETATM 5380 C  C39   . A1AHB J 5 .   ? 2.73814   25.82044  20.64178  1.000 35.58096  ?  201 A1AHB D C39   1 
HETATM 5381 C  C4    . A1AHB J 5 .   ? -5.63247  24.28972  14.88311  1.000 26.25138  ?  201 A1AHB D C4    1 
HETATM 5382 C  C40   . A1AHB J 5 .   ? 0.76790   24.68445  21.39698  1.000 36.68893  ?  201 A1AHB D C40   1 
HETATM 5383 C  C41   . A1AHB J 5 .   ? -0.73979  24.68981  21.37474  1.000 34.48810  ?  201 A1AHB D C41   1 
HETATM 5384 C  C42   . A1AHB J 5 .   ? -6.90196  23.94884  19.59319  1.000 25.03020  ?  201 A1AHB D C42   1 
HETATM 5385 C  C43   . A1AHB J 5 .   ? -7.55530  25.00720  20.45685  1.000 22.64997  ?  201 A1AHB D C43   1 
HETATM 5386 C  C44   . A1AHB J 5 .   ? -8.63372  22.37219  19.92181  1.000 29.73532  ?  201 A1AHB D C44   1 
HETATM 5387 C  C5    . A1AHB J 5 .   ? -5.84948  24.70833  13.57019  1.000 22.43712  ?  201 A1AHB D C5    1 
HETATM 5388 C  C6    . A1AHB J 5 .   ? -6.44435  23.83769  12.66365  1.000 25.62942  ?  201 A1AHB D C6    1 
HETATM 5389 C  C7    . A1AHB J 5 .   ? -6.83969  22.56588  13.08092  1.000 27.99532  ?  201 A1AHB D C7    1 
HETATM 5390 C  C8    . A1AHB J 5 .   ? -6.64055  22.12159  14.36715  1.000 23.47880  ?  201 A1AHB D C8    1 
HETATM 5391 C  C9    . A1AHB J 5 .   ? -6.71588  24.25637  11.28304  1.000 26.72958  ?  201 A1AHB D C9    1 
HETATM 5392 N  N1    . A1AHB J 5 .   ? -5.72436  22.81393  16.60500  1.000 24.77700  ?  201 A1AHB D N1    1 
HETATM 5393 N  N2    . A1AHB J 5 .   ? -7.90057  27.53158  7.27867   1.000 25.40691  ?  201 A1AHB D N2    1 
HETATM 5394 N  N3    . A1AHB J 5 .   ? -6.76907  29.82564  9.89549   1.000 23.34127  ?  201 A1AHB D N3    1 
HETATM 5395 N  N4    . A1AHB J 5 .   ? -7.32630  29.13092  10.98600  1.000 20.33377  ?  201 A1AHB D N4    1 
HETATM 5396 N  N5    . A1AHB J 5 .   ? -4.85266  24.28004  20.84099  1.000 26.03600  ?  201 A1AHB D N5    1 
HETATM 5397 N  N6    . A1AHB J 5 .   ? -1.32861  24.73046  20.02567  1.000 29.10640  ?  201 A1AHB D N6    1 
HETATM 5398 N  N7    . A1AHB J 5 .   ? 1.29474   25.66547  20.46190  1.000 37.47392  ?  201 A1AHB D N7    1 
HETATM 5399 N  N8    . A1AHB J 5 .   ? -6.02260  25.35386  10.76366  1.000 25.56460  ?  201 A1AHB D N8    1 
HETATM 5400 O  O1    . A1AHB J 5 .   ? -10.00080 28.11295  7.87022   1.000 20.54307  ?  201 A1AHB D O1    1 
HETATM 5401 O  O2    . A1AHB J 5 .   ? -6.36707  29.82967  7.68589   1.000 23.59063  ?  201 A1AHB D O2    1 
HETATM 5402 O  O3    . A1AHB J 5 .   ? -8.16963  28.25375  13.35612  1.000 21.92454  ?  201 A1AHB D O3    1 
HETATM 5403 O  O4    . A1AHB J 5 .   ? -6.08136  27.86833  14.09451  1.000 21.22353  ?  201 A1AHB D O4    1 
HETATM 5404 O  O5    . A1AHB J 5 .   ? -7.25223  22.64716  20.07071  1.000 22.85805  ?  201 A1AHB D O5    1 
HETATM 5405 S  S1    . A1AHB J 5 .   ? -7.72903  24.62223  9.00951   1.000 30.33413  ?  201 A1AHB D S1    1 
HETATM 5406 O  O     . HOH   K 6 .   ? -2.55631  14.38765  9.19805   1.000 36.77990  ?  301 HOH   A O     1 
HETATM 5407 O  O     . HOH   K 6 .   ? -0.52008  14.11557  3.41647   1.000 48.65745  ?  302 HOH   A O     1 
HETATM 5408 O  O     . HOH   K 6 .   ? -13.52055 19.06773  7.40840   1.000 28.06625  ?  303 HOH   A O     1 
HETATM 5409 O  O     . HOH   K 6 .   ? 0.18184   15.17229  21.98585  1.000 42.69879  ?  304 HOH   A O     1 
HETATM 5410 O  O     . HOH   K 6 .   ? 4.62486   2.34673   16.87314  1.000 41.00343  ?  305 HOH   A O     1 
HETATM 5411 O  O     . HOH   K 6 .   ? -5.05292  -3.06440  15.29544  1.000 40.31626  ?  306 HOH   A O     1 
HETATM 5412 O  O     . HOH   K 6 .   ? -26.87752 3.72454   4.05994   1.000 38.68888  ?  307 HOH   A O     1 
HETATM 5413 O  O     . HOH   K 6 .   ? -5.47381  15.05484  14.69312  1.000 29.29917  ?  308 HOH   A O     1 
HETATM 5414 O  O     . HOH   K 6 .   ? -4.24231  -3.78219  24.19276  1.000 42.44529  ?  309 HOH   A O     1 
HETATM 5415 O  O     . HOH   K 6 .   ? -7.19063  21.48862  6.94459   1.000 36.47361  ?  310 HOH   A O     1 
HETATM 5416 O  O     . HOH   K 6 .   ? -17.21286 17.71392  11.70749  1.000 33.02574  ?  311 HOH   A O     1 
HETATM 5417 O  O     . HOH   K 6 .   ? -7.36258  21.92958  0.28528   1.000 36.89426  ?  312 HOH   A O     1 
HETATM 5418 O  O     . HOH   K 6 .   ? -7.15901  -7.31807  3.99772   1.000 45.52214  ?  313 HOH   A O     1 
HETATM 5419 O  O     . HOH   K 6 .   ? -25.00581 11.25177  24.30722  1.000 34.54355  ?  314 HOH   A O     1 
HETATM 5420 O  O     . HOH   K 6 .   ? -15.12279 -6.75339  12.45564  1.000 43.44075  ?  315 HOH   A O     1 
HETATM 5421 O  O     . HOH   K 6 .   ? -16.15187 12.84007  21.12394  1.000 37.89942  ?  316 HOH   A O     1 
HETATM 5422 O  O     . HOH   K 6 .   ? -18.75627 7.63999   25.76931  1.000 42.02067  ?  317 HOH   A O     1 
HETATM 5423 O  O     . HOH   K 6 .   ? -25.29208 -1.64614  24.46832  1.000 45.98092  ?  318 HOH   A O     1 
HETATM 5424 O  O     . HOH   K 6 .   ? -11.82208 6.13263   27.02928  1.000 41.29540  ?  319 HOH   A O     1 
HETATM 5425 O  O     . HOH   K 6 .   ? -15.23128 27.13694  9.02569   1.000 34.16003  ?  320 HOH   A O     1 
HETATM 5426 O  O     . HOH   K 6 .   ? -16.88319 3.70901   26.19576  1.000 36.60163  ?  321 HOH   A O     1 
HETATM 5427 O  O     . HOH   K 6 .   ? -20.28413 23.67092  3.93978   1.000 35.27718  ?  322 HOH   A O     1 
HETATM 5428 O  O     . HOH   K 6 .   ? -20.21941 4.64845   -4.59982  1.000 29.87410  ?  323 HOH   A O     1 
HETATM 5429 O  O     . HOH   K 6 .   ? -28.90145 1.15267   13.62880  1.000 35.94127  ?  324 HOH   A O     1 
HETATM 5430 O  O     . HOH   K 6 .   ? -9.07985  -3.89122  14.43058  1.000 32.32647  ?  325 HOH   A O     1 
HETATM 5431 O  O     . HOH   K 6 .   ? -18.88952 19.72013  17.30296  1.000 40.79916  ?  326 HOH   A O     1 
HETATM 5432 O  O     . HOH   K 6 .   ? -33.19021 2.86262   22.13019  1.000 37.13846  ?  327 HOH   A O     1 
HETATM 5433 O  O     . HOH   K 6 .   ? -5.11313  15.08332  21.74119  1.000 35.59106  ?  328 HOH   A O     1 
HETATM 5434 O  O     . HOH   K 6 .   ? -3.56245  26.51628  11.55241  1.000 21.69963  ?  329 HOH   A O     1 
HETATM 5435 O  O     . HOH   K 6 .   ? -20.32239 17.31535  3.52458   1.000 45.36548  ?  330 HOH   A O     1 
HETATM 5436 O  O     . HOH   K 6 .   ? -18.02429 -6.21942  10.60181  1.000 41.53587  ?  331 HOH   A O     1 
HETATM 5437 O  O     . HOH   K 6 .   ? -10.48958 10.61374  22.22595  1.000 30.20026  ?  332 HOH   A O     1 
HETATM 5438 O  O     . HOH   K 6 .   ? 0.01807   -2.45958  0.07397   1.000 44.76094  ?  333 HOH   A O     1 
HETATM 5439 O  O     . HOH   K 6 .   ? -8.86881  13.51333  -2.50948  1.000 34.14086  ?  334 HOH   A O     1 
HETATM 5440 O  O     . HOH   K 6 .   ? -13.17864 25.85718  1.63529   1.000 32.55932  ?  335 HOH   A O     1 
HETATM 5441 O  O     . HOH   K 6 .   ? 4.81648   10.06631  1.77402   1.000 45.12175  ?  336 HOH   A O     1 
HETATM 5442 O  O     . HOH   K 6 .   ? -17.88265 -0.85625  0.47362   1.000 32.69288  ?  337 HOH   A O     1 
HETATM 5443 O  O     . HOH   K 6 .   ? -25.35731 12.22294  -0.63520  1.000 37.47006  ?  338 HOH   A O     1 
HETATM 5444 O  O     . HOH   K 6 .   ? -16.90388 0.41429   24.80115  1.000 34.61057  ?  339 HOH   A O     1 
HETATM 5445 O  O     . HOH   K 6 .   ? -2.57990  10.00506  -5.82300  1.000 36.54434  ?  340 HOH   A O     1 
HETATM 5446 O  O     . HOH   K 6 .   ? -15.90862 19.79726  4.77294   1.000 32.38468  ?  341 HOH   A O     1 
HETATM 5447 O  O     . HOH   K 6 .   ? -26.33118 4.45666   11.36987  1.000 36.23128  ?  342 HOH   A O     1 
HETATM 5448 O  O     . HOH   K 6 .   ? -21.03963 14.51809  4.35618   1.000 31.79270  ?  343 HOH   A O     1 
HETATM 5449 O  O     . HOH   K 6 .   ? -27.30766 12.24289  16.50521  1.000 34.08598  ?  344 HOH   A O     1 
HETATM 5450 O  O     . HOH   K 6 .   ? -8.05491  20.12661  9.50547   1.000 27.21190  ?  345 HOH   A O     1 
HETATM 5451 O  O     . HOH   K 6 .   ? -7.41355  13.65918  -0.02246  1.000 35.70836  ?  346 HOH   A O     1 
HETATM 5452 O  O     . HOH   K 6 .   ? -4.67722  9.49397   5.45840   1.000 27.32203  ?  347 HOH   A O     1 
HETATM 5453 O  O     . HOH   K 6 .   ? 2.63451   19.54646  16.15544  1.000 36.81324  ?  348 HOH   A O     1 
HETATM 5454 O  O     . HOH   K 6 .   ? -5.56999  24.41976  5.54685   1.000 33.98741  ?  349 HOH   A O     1 
HETATM 5455 O  O     . HOH   K 6 .   ? -11.85995 16.04306  9.86665   1.000 25.88204  ?  350 HOH   A O     1 
HETATM 5456 O  O     . HOH   K 6 .   ? -18.51307 -4.13504  24.06351  1.000 41.83064  ?  351 HOH   A O     1 
HETATM 5457 O  O     . HOH   K 6 .   ? -17.45869 18.26604  2.82809   1.000 41.39097  ?  352 HOH   A O     1 
HETATM 5458 O  O     . HOH   K 6 .   ? -11.38753 -6.40236  5.54367   1.000 37.25030  ?  353 HOH   A O     1 
HETATM 5459 O  O     . HOH   K 6 .   ? -22.66521 16.85803  18.50579  1.000 36.12658  ?  354 HOH   A O     1 
HETATM 5460 O  O     . HOH   K 6 .   ? -22.78815 9.54578   27.93469  1.000 32.23585  ?  355 HOH   A O     1 
HETATM 5461 O  O     . HOH   K 6 .   ? -7.99777  -7.70850  6.65908   1.000 43.13489  ?  356 HOH   A O     1 
HETATM 5462 O  O     . HOH   K 6 .   ? -24.03315 14.63737  17.89690  1.000 29.58909  ?  357 HOH   A O     1 
HETATM 5463 O  O     . HOH   K 6 .   ? -6.58176  12.96488  11.86303  1.000 26.01478  ?  358 HOH   A O     1 
HETATM 5464 O  O     . HOH   K 6 .   ? -5.16660  2.74413   -9.04443  1.000 43.81385  ?  359 HOH   A O     1 
HETATM 5465 O  O     . HOH   K 6 .   ? -22.14277 -3.58192  9.14717   1.000 47.15351  ?  360 HOH   A O     1 
HETATM 5466 O  O     . HOH   K 6 .   ? -13.08823 15.45869  -3.16099  1.000 33.60598  ?  361 HOH   A O     1 
HETATM 5467 O  O     . HOH   K 6 .   ? 1.48532   -2.04247  27.50864  1.000 38.31383  ?  362 HOH   A O     1 
HETATM 5468 O  O     . HOH   K 6 .   ? -1.95170  19.06285  6.66947   1.000 31.06598  ?  363 HOH   A O     1 
HETATM 5469 O  O     . HOH   K 6 .   ? -23.94197 3.34736   4.29427   1.000 32.80857  ?  364 HOH   A O     1 
HETATM 5470 O  O     . HOH   K 6 .   ? 4.30449   9.72374   21.26042  1.000 48.66537  ?  365 HOH   A O     1 
HETATM 5471 O  O     . HOH   K 6 .   ? -8.61334  17.54850  16.24815  1.000 26.26401  ?  366 HOH   A O     1 
HETATM 5472 O  O     . HOH   K 6 .   ? -8.90154  -1.01989  -7.43165  1.000 47.20594  ?  367 HOH   A O     1 
HETATM 5473 O  O     . HOH   K 6 .   ? -21.69064 -7.61030  21.97834  1.000 46.43088  ?  368 HOH   A O     1 
HETATM 5474 O  O     . HOH   K 6 .   ? -25.74108 -5.11727  12.20028  1.000 49.65743  ?  369 HOH   A O     1 
HETATM 5475 O  O     . HOH   K 6 .   ? -14.65046 9.31895   20.67213  1.000 26.02422  ?  370 HOH   A O     1 
HETATM 5476 O  O     . HOH   K 6 .   ? -17.55677 -5.14009  7.07760   1.000 49.58581  ?  371 HOH   A O     1 
HETATM 5477 O  O     . HOH   K 6 .   ? 4.98301   2.84079   23.20765  1.000 47.74114  ?  372 HOH   A O     1 
HETATM 5478 O  O     . HOH   K 6 .   ? -5.95324  17.56179  19.72281  1.000 38.44044  ?  373 HOH   A O     1 
HETATM 5479 O  O     . HOH   K 6 .   ? -14.24791 22.37184  13.97248  1.000 28.66172  ?  374 HOH   A O     1 
HETATM 5480 O  O     . HOH   K 6 .   ? -26.70682 -0.15021  7.48806   1.000 49.66562  ?  375 HOH   A O     1 
HETATM 5481 O  O     . HOH   K 6 .   ? -12.65217 3.87059   27.47059  1.000 44.81165  ?  376 HOH   A O     1 
HETATM 5482 O  O     . HOH   K 6 .   ? 1.66904   0.90223   10.89509  1.000 40.02732  ?  377 HOH   A O     1 
HETATM 5483 O  O     . HOH   K 6 .   ? -10.90840 14.62271  -4.60053  1.000 38.65048  ?  378 HOH   A O     1 
HETATM 5484 O  O     . HOH   K 6 .   ? -16.07807 -9.33412  13.40909  1.000 46.91087  ?  379 HOH   A O     1 
HETATM 5485 O  O     . HOH   K 6 .   ? -15.41264 20.57114  10.27817  1.000 39.60731  ?  380 HOH   A O     1 
HETATM 5486 O  O     . HOH   K 6 .   ? 0.74530   3.49034   4.87842   1.000 46.57776  ?  381 HOH   A O     1 
HETATM 5487 O  O     . HOH   K 6 .   ? -14.97495 24.61650  -0.42630  1.000 36.59210  ?  382 HOH   A O     1 
HETATM 5488 O  O     . HOH   K 6 .   ? 1.07332   13.03408  10.62576  1.000 45.93739  ?  383 HOH   A O     1 
HETATM 5489 O  O     . HOH   K 6 .   ? -23.280   0.643     1.152     1.000 30.99574  ?  384 HOH   A O     1 
HETATM 5490 O  O     . HOH   K 6 .   ? 0.80989   7.99827   25.45768  1.000 41.97689  ?  385 HOH   A O     1 
HETATM 5491 O  O     . HOH   K 6 .   ? -19.85868 -1.80810  2.64701   1.000 42.48997  ?  386 HOH   A O     1 
HETATM 5492 O  O     . HOH   K 6 .   ? -15.50045 -2.55233  0.92352   1.000 38.90315  ?  387 HOH   A O     1 
HETATM 5493 O  O     . HOH   K 6 .   ? -20.46210 2.42878   28.20394  1.000 39.50824  ?  388 HOH   A O     1 
HETATM 5494 O  O     . HOH   K 6 .   ? -9.02723  0.07877   22.94301  1.000 37.76800  ?  389 HOH   A O     1 
HETATM 5495 O  O     . HOH   K 6 .   ? -23.28660 -2.88011  22.63113  1.000 38.16955  ?  390 HOH   A O     1 
HETATM 5496 O  O     . HOH   K 6 .   ? -8.59988  -5.54152  18.33306  1.000 41.96923  ?  391 HOH   A O     1 
HETATM 5497 O  O     . HOH   K 6 .   ? -13.73238 17.84979  -3.08158  1.000 43.02290  ?  392 HOH   A O     1 
HETATM 5498 O  O     . HOH   K 6 .   ? -22.81019 1.08702   4.45814   1.000 28.97414  ?  393 HOH   A O     1 
HETATM 5499 O  O     . HOH   K 6 .   ? 0.76556   16.10677  3.43694   1.000 54.55207  ?  394 HOH   A O     1 
HETATM 5500 O  O     . HOH   K 6 .   ? -27.29477 4.29170   29.53590  1.000 48.10069  ?  395 HOH   A O     1 
HETATM 5501 O  O     . HOH   K 6 .   ? -27.30277 11.62168  1.19349   1.000 38.84674  ?  396 HOH   A O     1 
HETATM 5502 O  O     . HOH   K 6 .   ? -7.09477  -4.78448  15.55085  1.000 38.24051  ?  397 HOH   A O     1 
HETATM 5503 O  O     . HOH   K 6 .   ? -10.29830 15.51826  22.72053  1.000 41.06264  ?  398 HOH   A O     1 
HETATM 5504 O  O     . HOH   K 6 .   ? -28.21590 -2.31558  29.16521  1.000 58.22733  ?  399 HOH   A O     1 
HETATM 5505 O  O     . HOH   K 6 .   ? -26.33114 14.51086  -0.12860  1.000 40.02799  ?  400 HOH   A O     1 
HETATM 5506 O  O     . HOH   K 6 .   ? -2.29748  16.22104  5.73066   1.000 39.89847  ?  401 HOH   A O     1 
HETATM 5507 O  O     . HOH   K 6 .   ? -8.58777  2.08686   24.93034  1.000 32.66070  ?  402 HOH   A O     1 
HETATM 5508 O  O     . HOH   K 6 .   ? -0.25041  20.66298  5.81034   1.000 41.20835  ?  403 HOH   A O     1 
HETATM 5509 O  O     . HOH   K 6 .   ? -9.41271  17.63750  -0.40305  1.000 43.96874  ?  404 HOH   A O     1 
HETATM 5510 O  O     . HOH   K 6 .   ? -19.63648 -7.85219  17.39488  1.000 42.82438  ?  405 HOH   A O     1 
HETATM 5511 O  O     . HOH   K 6 .   ? 1.31845   -4.08555  2.39959   1.000 42.71002  ?  406 HOH   A O     1 
HETATM 5512 O  O     . HOH   K 6 .   ? -17.56603 19.31485  9.63195   1.000 37.12483  ?  407 HOH   A O     1 
HETATM 5513 O  O     . HOH   K 6 .   ? -12.69147 9.35662   22.49128  1.000 35.90771  ?  408 HOH   A O     1 
HETATM 5514 O  O     . HOH   K 6 .   ? -17.42743 19.32337  6.75637   1.000 36.58967  ?  409 HOH   A O     1 
HETATM 5515 O  O     . HOH   K 6 .   ? -10.77136 13.24597  23.43970  1.000 35.62813  ?  410 HOH   A O     1 
HETATM 5516 O  O     . HOH   K 6 .   ? 2.17515   2.26329   3.30787   1.000 53.06431  ?  411 HOH   A O     1 
HETATM 5517 O  O     . HOH   L 6 .   ? -11.82536 17.46441  33.38301  1.000 36.60975  ?  301 HOH   B O     1 
HETATM 5518 O  O     . HOH   L 6 .   ? -3.51002  19.11593  39.20462  1.000 47.21391  ?  302 HOH   B O     1 
HETATM 5519 O  O     . HOH   L 6 .   ? 0.72149   30.65831  33.91445  1.000 38.37942  ?  303 HOH   B O     1 
HETATM 5520 O  O     . HOH   L 6 .   ? -1.93613  26.12198  24.34107  1.000 38.74940  ?  304 HOH   B O     1 
HETATM 5521 O  O     . HOH   L 6 .   ? -9.58525  15.47685  52.73495  1.000 50.79180  ?  305 HOH   B O     1 
HETATM 5522 O  O     . HOH   L 6 .   ? -26.27121 25.10260  33.09545  1.000 42.03461  ?  306 HOH   B O     1 
HETATM 5523 O  O     . HOH   L 6 .   ? -5.40456  23.70130  47.06713  1.000 38.50508  ?  307 HOH   B O     1 
HETATM 5524 O  O     . HOH   L 6 .   ? -22.95010 26.60558  32.60997  1.000 37.41949  ?  308 HOH   B O     1 
HETATM 5525 O  O     . HOH   L 6 .   ? -23.07668 23.56704  37.18885  1.000 26.26303  ?  309 HOH   B O     1 
HETATM 5526 O  O     . HOH   L 6 .   ? 1.88219   20.16246  47.92176  1.000 61.84626  ?  310 HOH   B O     1 
HETATM 5527 O  O     . HOH   L 6 .   ? -5.74250  24.87754  23.30811  1.000 30.34453  ?  311 HOH   B O     1 
HETATM 5528 O  O     . HOH   L 6 .   ? -13.05018 24.42934  26.95340  1.000 43.33077  ?  312 HOH   B O     1 
HETATM 5529 O  O     . HOH   L 6 .   ? -10.36708 9.26616   48.79717  1.000 48.55867  ?  313 HOH   B O     1 
HETATM 5530 O  O     . HOH   L 6 .   ? -6.72136  22.98418  27.96942  1.000 42.04930  ?  314 HOH   B O     1 
HETATM 5531 O  O     . HOH   L 6 .   ? -0.24039  31.07473  21.17213  1.000 40.87077  ?  315 HOH   B O     1 
HETATM 5532 O  O     . HOH   L 6 .   ? 0.81654   33.02618  40.29005  1.000 41.60375  ?  316 HOH   B O     1 
HETATM 5533 O  O     . HOH   L 6 .   ? -31.47890 13.13464  35.74805  1.000 26.08078  ?  317 HOH   B O     1 
HETATM 5534 O  O     . HOH   L 6 .   ? -27.42737 19.71465  37.44723  1.000 31.92705  ?  318 HOH   B O     1 
HETATM 5535 O  O     . HOH   L 6 .   ? -24.13000 34.43438  36.99452  1.000 45.39021  ?  319 HOH   B O     1 
HETATM 5536 O  O     . HOH   L 6 .   ? 1.39559   31.23755  30.58075  1.000 40.95535  ?  320 HOH   B O     1 
HETATM 5537 O  O     . HOH   L 6 .   ? 3.30540   28.50523  28.82437  1.000 37.44595  ?  321 HOH   B O     1 
HETATM 5538 O  O     . HOH   L 6 .   ? -1.32912  23.46382  33.34939  1.000 44.20988  ?  322 HOH   B O     1 
HETATM 5539 O  O     . HOH   L 6 .   ? -10.33104 20.83522  27.08243  1.000 46.02179  ?  323 HOH   B O     1 
HETATM 5540 O  O     . HOH   L 6 .   ? -10.20413 40.87290  38.69939  1.000 48.89126  ?  324 HOH   B O     1 
HETATM 5541 O  O     . HOH   L 6 .   ? -28.92193 27.65756  48.43464  1.000 46.19571  ?  325 HOH   B O     1 
HETATM 5542 O  O     . HOH   L 6 .   ? -16.54550 8.60847   34.70754  1.000 43.85115  ?  326 HOH   B O     1 
HETATM 5543 O  O     . HOH   L 6 .   ? -14.73101 35.93364  29.12978  1.000 36.00531  ?  327 HOH   B O     1 
HETATM 5544 O  O     . HOH   L 6 .   ? -9.42494  23.07351  61.27226  1.000 62.59506  ?  328 HOH   B O     1 
HETATM 5545 O  O     . HOH   L 6 .   ? -26.79297 25.53454  36.64657  1.000 34.31754  ?  329 HOH   B O     1 
HETATM 5546 O  O     . HOH   L 6 .   ? -1.90424  28.81668  24.77099  1.000 35.49332  ?  330 HOH   B O     1 
HETATM 5547 O  O     . HOH   L 6 .   ? -20.42927 18.63389  40.57425  1.000 25.41999  ?  331 HOH   B O     1 
HETATM 5548 O  O     . HOH   L 6 .   ? -13.84372 35.27977  51.40527  1.000 43.72123  ?  332 HOH   B O     1 
HETATM 5549 O  O     . HOH   L 6 .   ? -19.58658 32.31258  27.09891  1.000 43.39818  ?  333 HOH   B O     1 
HETATM 5550 O  O     . HOH   L 6 .   ? -6.69214  39.46178  33.27548  1.000 39.24642  ?  334 HOH   B O     1 
HETATM 5551 O  O     . HOH   L 6 .   ? -21.23182 21.05032  47.59399  1.000 39.64246  ?  335 HOH   B O     1 
HETATM 5552 O  O     . HOH   L 6 .   ? 5.18942   30.35478  25.41698  1.000 52.44295  ?  336 HOH   B O     1 
HETATM 5553 O  O     . HOH   L 6 .   ? 2.54210   36.55033  30.41325  1.000 37.85740  ?  337 HOH   B O     1 
HETATM 5554 O  O     . HOH   L 6 .   ? -21.45684 17.06066  34.68832  1.000 32.71114  ?  338 HOH   B O     1 
HETATM 5555 O  O     . HOH   L 6 .   ? -6.13742  8.05936   37.63829  1.000 49.71953  ?  339 HOH   B O     1 
HETATM 5556 O  O     . HOH   L 6 .   ? -35.62091 29.27461  37.70803  1.000 50.39171  ?  340 HOH   B O     1 
HETATM 5557 O  O     . HOH   L 6 .   ? -11.48719 22.06995  32.57825  1.000 33.46969  ?  341 HOH   B O     1 
HETATM 5558 O  O     . HOH   L 6 .   ? -5.71187  16.45794  31.61368  1.000 43.82102  ?  342 HOH   B O     1 
HETATM 5559 O  O     . HOH   L 6 .   ? -14.88089 40.91682  45.15263  1.000 50.75612  ?  343 HOH   B O     1 
HETATM 5560 O  O     . HOH   L 6 .   ? 4.80675   36.96447  36.29432  1.000 39.12426  ?  344 HOH   B O     1 
HETATM 5561 O  O     . HOH   L 6 .   ? -23.16366 27.87286  65.70192  1.000 57.74261  ?  345 HOH   B O     1 
HETATM 5562 O  O     . HOH   L 6 .   ? -14.70526 39.23543  41.60608  1.000 39.90261  ?  346 HOH   B O     1 
HETATM 5563 O  O     . HOH   L 6 .   ? 1.40339   38.76352  30.96067  1.000 40.60262  ?  347 HOH   B O     1 
HETATM 5564 O  O     . HOH   L 6 .   ? -17.25312 6.60255   40.87372  1.000 60.19097  ?  348 HOH   B O     1 
HETATM 5565 O  O     . HOH   L 6 .   ? -10.50309 37.59716  28.51389  1.000 35.67779  ?  349 HOH   B O     1 
HETATM 5566 O  O     . HOH   L 6 .   ? -9.07997  40.42769  36.29755  1.000 53.15500  ?  350 HOH   B O     1 
HETATM 5567 O  O     . HOH   L 6 .   ? -25.51493 21.82895  30.32000  1.000 33.27501  ?  351 HOH   B O     1 
HETATM 5568 O  O     . HOH   L 6 .   ? -23.37449 13.46484  38.42039  1.000 52.57748  ?  352 HOH   B O     1 
HETATM 5569 O  O     . HOH   L 6 .   ? -12.81428 38.58111  43.37513  1.000 37.49679  ?  353 HOH   B O     1 
HETATM 5570 O  O     . HOH   L 6 .   ? -19.49232 30.67785  64.59371  1.000 47.51756  ?  354 HOH   B O     1 
HETATM 5571 O  O     . HOH   L 6 .   ? 3.89046   28.02137  33.30218  1.000 40.64471  ?  355 HOH   B O     1 
HETATM 5572 O  O     . HOH   L 6 .   ? -30.84105 26.88529  45.17916  1.000 47.29390  ?  356 HOH   B O     1 
HETATM 5573 O  O     . HOH   L 6 .   ? -0.56417  24.37494  28.57655  1.000 38.38094  ?  357 HOH   B O     1 
HETATM 5574 O  O     . HOH   L 6 .   ? -29.45965 21.36035  53.48552  1.000 47.94015  ?  358 HOH   B O     1 
HETATM 5575 O  O     . HOH   L 6 .   ? 0.42582   25.91385  25.89306  1.000 48.14003  ?  359 HOH   B O     1 
HETATM 5576 O  O     . HOH   L 6 .   ? -20.34063 24.30147  26.80734  1.000 36.09730  ?  360 HOH   B O     1 
HETATM 5577 O  O     . HOH   L 6 .   ? -6.99013  27.20636  55.00483  1.000 47.83872  ?  361 HOH   B O     1 
HETATM 5578 O  O     . HOH   L 6 .   ? -15.98411 29.77714  26.01895  1.000 28.91003  ?  362 HOH   B O     1 
HETATM 5579 O  O     . HOH   L 6 .   ? 0.56028   32.71884  23.65028  1.000 35.17762  ?  363 HOH   B O     1 
HETATM 5580 O  O     . HOH   L 6 .   ? -6.92128  39.89686  36.40707  1.000 51.02495  ?  364 HOH   B O     1 
HETATM 5581 O  O     . HOH   L 6 .   ? -29.68822 24.68675  55.29808  1.000 54.48931  ?  365 HOH   B O     1 
HETATM 5582 O  O     . HOH   L 6 .   ? -13.42823 16.62699  30.80749  1.000 38.97290  ?  366 HOH   B O     1 
HETATM 5583 O  O     . HOH   L 6 .   ? -22.90291 41.29981  30.45488  1.000 45.56433  ?  367 HOH   B O     1 
HETATM 5584 O  O     . HOH   L 6 .   ? -6.24630  36.40713  47.67612  1.000 55.29384  ?  368 HOH   B O     1 
HETATM 5585 O  O     . HOH   L 6 .   ? -33.60583 15.28412  39.34018  1.000 44.40153  ?  369 HOH   B O     1 
HETATM 5586 O  O     . HOH   L 6 .   ? -3.67013  16.72385  37.82962  1.000 43.89903  ?  370 HOH   B O     1 
HETATM 5587 O  O     . HOH   L 6 .   ? -15.69049 15.87150  30.34126  1.000 40.39414  ?  371 HOH   B O     1 
HETATM 5588 O  O     . HOH   L 6 .   ? -17.17522 39.53603  30.46308  1.000 41.77268  ?  372 HOH   B O     1 
HETATM 5589 O  O     . HOH   L 6 .   ? -16.34073 44.67236  33.86008  1.000 37.53969  ?  373 HOH   B O     1 
HETATM 5590 O  O     . HOH   L 6 .   ? -15.87403 13.19967  31.30265  1.000 43.37386  ?  374 HOH   B O     1 
HETATM 5591 O  O     . HOH   L 6 .   ? -3.81218  21.71833  47.68439  1.000 48.03763  ?  375 HOH   B O     1 
HETATM 5592 O  O     . HOH   L 6 .   ? -1.77529  20.89402  46.31708  1.000 52.69123  ?  376 HOH   B O     1 
HETATM 5593 O  O     . HOH   L 6 .   ? -25.70809 27.46871  32.67688  1.000 44.74140  ?  377 HOH   B O     1 
HETATM 5594 O  O     . HOH   L 6 .   ? -14.86335 39.12516  28.16196  1.000 44.61243  ?  378 HOH   B O     1 
HETATM 5595 O  O     . HOH   L 6 .   ? -17.54931 41.97745  29.54922  1.000 37.67451  ?  379 HOH   B O     1 
HETATM 5596 O  O     . HOH   L 6 .   ? -26.487   40.987    30.470    1.000 41.58437  ?  380 HOH   B O     1 
HETATM 5597 O  O     . HOH   M 6 .   ? -29.15291 1.12074   33.35449  1.000 47.25751  ?  301 HOH   C O     1 
HETATM 5598 O  O     . HOH   M 6 .   ? -42.16355 19.76114  34.59684  1.000 30.67206  ?  302 HOH   C O     1 
HETATM 5599 O  O     . HOH   M 6 .   ? -42.21140 26.03495  14.57668  1.000 45.02795  ?  303 HOH   C O     1 
HETATM 5600 O  O     . HOH   M 6 .   ? -39.78868 26.97872  24.35560  1.000 42.70455  ?  304 HOH   C O     1 
HETATM 5601 O  O     . HOH   M 6 .   ? -58.48406 4.43471   26.55005  1.000 42.87621  ?  305 HOH   C O     1 
HETATM 5602 O  O     . HOH   M 6 .   ? -34.35910 22.34724  31.37327  1.000 35.08730  ?  306 HOH   C O     1 
HETATM 5603 O  O     . HOH   M 6 .   ? -42.37104 14.00292  37.81131  1.000 26.30544  ?  307 HOH   C O     1 
HETATM 5604 O  O     . HOH   M 6 .   ? -41.53331 22.32753  23.98006  1.000 34.72552  ?  308 HOH   C O     1 
HETATM 5605 O  O     . HOH   M 6 .   ? -57.33964 12.77955  32.87523  1.000 38.81435  ?  309 HOH   C O     1 
HETATM 5606 O  O     . HOH   M 6 .   ? -48.63360 28.56552  22.78733  1.000 36.90835  ?  310 HOH   C O     1 
HETATM 5607 O  O     . HOH   M 6 .   ? -60.68243 11.41001  24.80983  1.000 49.86640  ?  311 HOH   C O     1 
HETATM 5608 O  O     . HOH   M 6 .   ? -35.90776 26.53502  36.45874  1.000 39.43722  ?  312 HOH   C O     1 
HETATM 5609 O  O     . HOH   M 6 .   ? -26.24148 18.12488  16.75006  1.000 35.19535  ?  313 HOH   C O     1 
HETATM 5610 O  O     . HOH   M 6 .   ? -40.48091 19.93724  5.21737   1.000 38.78721  ?  314 HOH   C O     1 
HETATM 5611 O  O     . HOH   M 6 .   ? -28.98414 20.50691  27.81402  1.000 39.42933  ?  315 HOH   C O     1 
HETATM 5612 O  O     . HOH   M 6 .   ? -29.20565 5.03837   26.97649  1.000 41.58541  ?  316 HOH   C O     1 
HETATM 5613 O  O     . HOH   M 6 .   ? -46.44384 -0.23897  35.47956  1.000 38.69316  ?  317 HOH   C O     1 
HETATM 5614 O  O     . HOH   M 6 .   ? -31.28672 28.84448  29.91712  1.000 48.88436  ?  318 HOH   C O     1 
HETATM 5615 O  O     . HOH   M 6 .   ? -43.91962 9.69324   10.29784  1.000 29.81244  ?  319 HOH   C O     1 
HETATM 5616 O  O     . HOH   M 6 .   ? -50.33306 9.12148   44.96589  1.000 34.87295  ?  320 HOH   C O     1 
HETATM 5617 O  O     . HOH   M 6 .   ? -42.12036 30.71095  34.23076  1.000 50.13132  ?  321 HOH   C O     1 
HETATM 5618 O  O     . HOH   M 6 .   ? -41.74822 16.42124  40.63492  1.000 30.04602  ?  322 HOH   C O     1 
HETATM 5619 O  O     . HOH   M 6 .   ? -44.34567 19.74825  11.14968  1.000 38.35658  ?  323 HOH   C O     1 
HETATM 5620 O  O     . HOH   M 6 .   ? -46.83598 13.49145  45.84293  1.000 46.23066  ?  324 HOH   C O     1 
HETATM 5621 O  O     . HOH   M 6 .   ? -37.08114 3.79398   18.60898  1.000 41.60528  ?  325 HOH   C O     1 
HETATM 5622 O  O     . HOH   M 6 .   ? -48.52682 16.69624  32.73463  1.000 29.96680  ?  326 HOH   C O     1 
HETATM 5623 O  O     . HOH   M 6 .   ? -59.10619 20.65165  32.84026  1.000 36.41123  ?  327 HOH   C O     1 
HETATM 5624 O  O     . HOH   M 6 .   ? -33.18251 14.15797  11.51335  1.000 42.33006  ?  328 HOH   C O     1 
HETATM 5625 O  O     . HOH   M 6 .   ? -50.04325 21.52868  11.32846  1.000 46.87741  ?  329 HOH   C O     1 
HETATM 5626 O  O     . HOH   M 6 .   ? -44.65622 7.09702   36.92639  1.000 28.76313  ?  330 HOH   C O     1 
HETATM 5627 O  O     . HOH   M 6 .   ? -38.37809 -2.54551  29.39385  1.000 45.73796  ?  331 HOH   C O     1 
HETATM 5628 O  O     . HOH   M 6 .   ? -30.97849 25.45828  18.88373  1.000 36.03565  ?  332 HOH   C O     1 
HETATM 5629 O  O     . HOH   M 6 .   ? -54.21930 25.23166  27.47667  1.000 41.99442  ?  333 HOH   C O     1 
HETATM 5630 O  O     . HOH   M 6 .   ? -43.01829 12.24098  45.02463  1.000 37.61548  ?  334 HOH   C O     1 
HETATM 5631 O  O     . HOH   M 6 .   ? -44.65201 2.78881   31.02160  1.000 32.62005  ?  335 HOH   C O     1 
HETATM 5632 O  O     . HOH   M 6 .   ? -38.53655 24.23766  26.16800  1.000 33.25187  ?  336 HOH   C O     1 
HETATM 5633 O  O     . HOH   M 6 .   ? -34.53333 23.61460  8.24929   1.000 46.34854  ?  337 HOH   C O     1 
HETATM 5634 O  O     . HOH   M 6 .   ? -44.52702 5.53237   15.92000  1.000 36.26030  ?  338 HOH   C O     1 
HETATM 5635 O  O     . HOH   M 6 .   ? -46.54713 10.02446  44.28914  1.000 39.70380  ?  339 HOH   C O     1 
HETATM 5636 O  O     . HOH   M 6 .   ? -38.30596 0.68104   33.67943  1.000 32.22757  ?  340 HOH   C O     1 
HETATM 5637 O  O     . HOH   M 6 .   ? -57.26139 14.10356  30.49556  1.000 42.65499  ?  341 HOH   C O     1 
HETATM 5638 O  O     . HOH   M 6 .   ? -44.99086 12.63592  10.34059  1.000 34.81926  ?  342 HOH   C O     1 
HETATM 5639 O  O     . HOH   M 6 .   ? -34.24724 23.39608  19.69702  1.000 30.12094  ?  343 HOH   C O     1 
HETATM 5640 O  O     . HOH   M 6 .   ? -21.97845 16.04654  21.37678  1.000 31.03053  ?  344 HOH   C O     1 
HETATM 5641 O  O     . HOH   M 6 .   ? -38.22042 25.41375  14.02263  1.000 39.74333  ?  345 HOH   C O     1 
HETATM 5642 O  O     . HOH   M 6 .   ? -57.18462 19.99568  19.39289  1.000 42.13364  ?  346 HOH   C O     1 
HETATM 5643 O  O     . HOH   M 6 .   ? -29.10530 8.95518   17.51646  1.000 24.89227  ?  347 HOH   C O     1 
HETATM 5644 O  O     . HOH   M 6 .   ? -29.69893 22.43515  26.21455  1.000 40.05036  ?  348 HOH   C O     1 
HETATM 5645 O  O     . HOH   M 6 .   ? -42.61262 6.13045   13.01832  1.000 37.20496  ?  349 HOH   C O     1 
HETATM 5646 O  O     . HOH   M 6 .   ? -47.52784 14.12880  38.50061  1.000 32.29944  ?  350 HOH   C O     1 
HETATM 5647 O  O     . HOH   M 6 .   ? -42.32454 17.75515  48.56424  1.000 38.06555  ?  351 HOH   C O     1 
HETATM 5648 O  O     . HOH   M 6 .   ? -33.60352 13.22037  37.46449  1.000 35.84634  ?  352 HOH   C O     1 
HETATM 5649 O  O     . HOH   M 6 .   ? -37.82361 4.93309   28.88837  1.000 25.75852  ?  353 HOH   C O     1 
HETATM 5650 O  O     . HOH   M 6 .   ? -38.78356 19.07587  45.94051  1.000 35.59947  ?  354 HOH   C O     1 
HETATM 5651 O  O     . HOH   M 6 .   ? -47.30926 6.79324   36.45115  1.000 25.46585  ?  355 HOH   C O     1 
HETATM 5652 O  O     . HOH   M 6 .   ? -41.45288 6.40296   37.13751  1.000 26.61269  ?  356 HOH   C O     1 
HETATM 5653 O  O     . HOH   M 6 .   ? -22.11414 18.71260  23.87669  1.000 36.20806  ?  357 HOH   C O     1 
HETATM 5654 O  O     . HOH   M 6 .   ? -30.65495 23.77867  22.55377  1.000 36.50352  ?  358 HOH   C O     1 
HETATM 5655 O  O     . HOH   M 6 .   ? -42.18020 23.23393  33.83433  1.000 33.13709  ?  359 HOH   C O     1 
HETATM 5656 O  O     . HOH   M 6 .   ? -50.82836 24.83704  22.80178  1.000 35.55348  ?  360 HOH   C O     1 
HETATM 5657 O  O     . HOH   M 6 .   ? -45.33228 6.32987   12.40798  1.000 40.95344  ?  361 HOH   C O     1 
HETATM 5658 O  O     . HOH   M 6 .   ? -64.15414 8.58193   29.10166  1.000 52.96220  ?  362 HOH   C O     1 
HETATM 5659 O  O     . HOH   M 6 .   ? -28.88023 24.46939  7.40424   1.000 48.07231  ?  363 HOH   C O     1 
HETATM 5660 O  O     . HOH   M 6 .   ? -37.33997 -1.78561  25.82601  1.000 41.87507  ?  364 HOH   C O     1 
HETATM 5661 O  O     . HOH   M 6 .   ? -25.14398 21.02093  19.22382  1.000 40.00469  ?  365 HOH   C O     1 
HETATM 5662 O  O     . HOH   M 6 .   ? -36.27651 2.48401   14.34559  1.000 50.14345  ?  366 HOH   C O     1 
HETATM 5663 O  O     . HOH   M 6 .   ? -53.12120 12.70161  12.76302  1.000 35.53349  ?  367 HOH   C O     1 
HETATM 5664 O  O     . HOH   M 6 .   ? -52.27812 24.57625  20.76998  1.000 41.39745  ?  368 HOH   C O     1 
HETATM 5665 O  O     . HOH   M 6 .   ? -50.248   0.050     32.122    1.000 41.87527  ?  369 HOH   C O     1 
HETATM 5666 O  O     . HOH   M 6 .   ? -60.68427 15.03008  26.21632  1.000 42.11169  ?  370 HOH   C O     1 
HETATM 5667 O  O     . HOH   M 6 .   ? -46.619   -0.670    38.925    1.000 36.51289  ?  371 HOH   C O     1 
HETATM 5668 O  O     . HOH   M 6 .   ? -44.97868 0.50053   33.15663  1.000 30.84022  ?  372 HOH   C O     1 
HETATM 5669 O  O     . HOH   M 6 .   ? -49.96343 28.89987  40.98120  1.000 46.26123  ?  373 HOH   C O     1 
HETATM 5670 O  O     . HOH   M 6 .   ? -40.28460 3.53168   41.06725  1.000 45.27063  ?  374 HOH   C O     1 
HETATM 5671 O  O     . HOH   M 6 .   ? -29.47312 26.10684  16.86641  1.000 43.96501  ?  375 HOH   C O     1 
HETATM 5672 O  O     . HOH   M 6 .   ? -51.61634 13.64382  10.24774  1.000 48.62292  ?  376 HOH   C O     1 
HETATM 5673 O  O     . HOH   M 6 .   ? -51.02424 27.25447  23.07786  1.000 40.57262  ?  377 HOH   C O     1 
HETATM 5674 O  O     . HOH   M 6 .   ? -38.322   4.158     11.685    1.000 38.38646  ?  378 HOH   C O     1 
HETATM 5675 O  O     . HOH   M 6 .   ? -44.371   -1.047    40.741    1.000 35.40989  ?  379 HOH   C O     1 
HETATM 5676 O  O     . HOH   M 6 .   ? -45.99756 8.37957   11.12858  1.000 33.32524  ?  380 HOH   C O     1 
HETATM 5677 O  O     . HOH   M 6 .   ? -22.66420 20.62478  20.35073  1.000 40.70015  ?  381 HOH   C O     1 
HETATM 5678 O  O     . HOH   M 6 .   ? -30.26394 25.74634  23.88807  1.000 48.95201  ?  382 HOH   C O     1 
HETATM 5679 O  O     . HOH   M 6 .   ? -60.62686 12.69249  26.93829  1.000 49.30689  ?  383 HOH   C O     1 
HETATM 5680 O  O     . HOH   M 6 .   ? -39.61987 18.12351  3.95208   1.000 45.48097  ?  384 HOH   C O     1 
HETATM 5681 O  O     . HOH   M 6 .   ? -34.28529 26.45637  23.15191  1.000 46.08849  ?  385 HOH   C O     1 
HETATM 5682 O  O     . HOH   M 6 .   ? -32.33765 26.88091  24.80991  1.000 52.86295  ?  386 HOH   C O     1 
HETATM 5683 O  O     . HOH   M 6 .   ? -33.74186 15.20996  9.28008   1.000 38.63739  ?  387 HOH   C O     1 
HETATM 5684 O  O     . HOH   N 6 .   ? -18.74659 52.63362  15.07166  1.000 44.70894  ?  301 HOH   D O     1 
HETATM 5685 O  O     . HOH   N 6 .   ? -16.27231 38.41024  8.40829   1.000 28.27994  ?  302 HOH   D O     1 
HETATM 5686 O  O     . HOH   N 6 .   ? 3.35394   31.36693  21.24177  1.000 47.56732  ?  303 HOH   D O     1 
HETATM 5687 O  O     . HOH   N 6 .   ? -10.38027 38.23023  25.87647  1.000 38.58594  ?  304 HOH   D O     1 
HETATM 5688 O  O     . HOH   N 6 .   ? -7.04099  55.23241  4.76510   1.000 35.26484  ?  305 HOH   D O     1 
HETATM 5689 O  O     . HOH   N 6 .   ? -17.75382 40.52047  25.57627  1.000 30.01615  ?  306 HOH   D O     1 
HETATM 5690 O  O     . HOH   N 6 .   ? 2.94946   42.57666  17.78571  1.000 36.56508  ?  307 HOH   D O     1 
HETATM 5691 O  O     . HOH   N 6 .   ? -8.67963  48.03097  -6.24387  1.000 49.60605  ?  308 HOH   D O     1 
HETATM 5692 O  O     . HOH   N 6 .   ? -24.39538 40.57302  14.77081  1.000 36.42032  ?  309 HOH   D O     1 
HETATM 5693 O  O     . HOH   N 6 .   ? 1.35619   27.03448  -5.39580  1.000 36.07038  ?  310 HOH   D O     1 
HETATM 5694 O  O     . HOH   N 6 .   ? -22.07005 40.05331  3.36832   1.000 35.83258  ?  311 HOH   D O     1 
HETATM 5695 O  O     . HOH   N 6 .   ? -14.10406 26.54534  13.76065  1.000 32.57932  ?  312 HOH   D O     1 
HETATM 5696 O  O     . HOH   N 6 .   ? -2.18199  31.11720  22.97713  1.000 34.93059  ?  313 HOH   D O     1 
HETATM 5697 O  O     . HOH   N 6 .   ? -20.05249 38.48613  -5.83092  1.000 42.37956  ?  314 HOH   D O     1 
HETATM 5698 O  O     . HOH   N 6 .   ? -21.06643 48.34034  15.99925  1.000 35.12836  ?  315 HOH   D O     1 
HETATM 5699 O  O     . HOH   N 6 .   ? -16.48336 27.91585  13.73644  1.000 32.71207  ?  316 HOH   D O     1 
HETATM 5700 O  O     . HOH   N 6 .   ? -3.53895  31.40558  -6.12426  1.000 33.96346  ?  317 HOH   D O     1 
HETATM 5701 O  O     . HOH   N 6 .   ? -24.54869 35.47303  8.12538   1.000 47.32764  ?  318 HOH   D O     1 
HETATM 5702 O  O     . HOH   N 6 .   ? -19.24692 31.02062  23.67066  1.000 32.18056  ?  319 HOH   D O     1 
HETATM 5703 O  O     . HOH   N 6 .   ? -2.01107  30.81119  0.90224   1.000 24.65165  ?  320 HOH   D O     1 
HETATM 5704 O  O     . HOH   N 6 .   ? -14.84879 45.38325  -2.96976  1.000 30.08987  ?  321 HOH   D O     1 
HETATM 5705 O  O     . HOH   N 6 .   ? 3.70667   30.13729  -0.77185  1.000 43.08409  ?  322 HOH   D O     1 
HETATM 5706 O  O     . HOH   N 6 .   ? -8.11726  34.06565  2.67533   1.000 28.18054  ?  323 HOH   D O     1 
HETATM 5707 O  O     . HOH   N 6 .   ? -9.66370  29.39755  -8.20794  1.000 36.70325  ?  324 HOH   D O     1 
HETATM 5708 O  O     . HOH   N 6 .   ? -10.224   45.462    27.368    1.000 36.90519  ?  325 HOH   D O     1 
HETATM 5709 O  O     . HOH   N 6 .   ? -17.82146 24.46220  20.55955  1.000 38.60037  ?  326 HOH   D O     1 
HETATM 5710 O  O     . HOH   N 6 .   ? 12.338    35.395    8.228     1.000 41.00452  ?  327 HOH   D O     1 
HETATM 5711 O  O     . HOH   N 6 .   ? -1.65028  33.32450  3.67852   1.000 24.94000  ?  328 HOH   D O     1 
HETATM 5712 O  O     . HOH   N 6 .   ? -21.73470 31.86558  -3.06999  1.000 50.19016  ?  329 HOH   D O     1 
HETATM 5713 O  O     . HOH   N 6 .   ? -13.43183 50.60291  22.22794  1.000 29.29432  ?  330 HOH   D O     1 
HETATM 5714 O  O     . HOH   N 6 .   ? -21.60633 50.78726  4.17884   1.000 42.22472  ?  331 HOH   D O     1 
HETATM 5715 O  O     . HOH   N 6 .   ? -14.37624 38.32997  25.80757  1.000 35.67384  ?  332 HOH   D O     1 
HETATM 5716 O  O     . HOH   N 6 .   ? -17.32317 30.84796  -2.60004  1.000 39.96671  ?  333 HOH   D O     1 
HETATM 5717 O  O     . HOH   N 6 .   ? -5.96790  40.61258  1.60353   1.000 27.16542  ?  334 HOH   D O     1 
HETATM 5718 O  O     . HOH   N 6 .   ? -12.83758 44.35434  26.18998  1.000 32.53775  ?  335 HOH   D O     1 
HETATM 5719 O  O     . HOH   N 6 .   ? -5.07576  35.49620  -8.62279  1.000 33.07338  ?  336 HOH   D O     1 
HETATM 5720 O  O     . HOH   N 6 .   ? -19.67422 28.51945  21.40911  1.000 31.38221  ?  337 HOH   D O     1 
HETATM 5721 O  O     . HOH   N 6 .   ? -2.24166  26.92501  9.01993   1.000 26.31950  ?  338 HOH   D O     1 
HETATM 5722 O  O     . HOH   N 6 .   ? -1.76856  24.88976  -2.52999  1.000 34.60795  ?  339 HOH   D O     1 
HETATM 5723 O  O     . HOH   N 6 .   ? 6.31494   35.57628  15.44973  1.000 31.70753  ?  340 HOH   D O     1 
HETATM 5724 O  O     . HOH   N 6 .   ? -13.40637 55.84192  13.22681  1.000 39.87742  ?  341 HOH   D O     1 
HETATM 5725 O  O     . HOH   N 6 .   ? -19.35836 30.05625  14.76123  1.000 31.15083  ?  342 HOH   D O     1 
HETATM 5726 O  O     . HOH   N 6 .   ? -21.01353 43.03403  1.38077   1.000 31.56627  ?  343 HOH   D O     1 
HETATM 5727 O  O     . HOH   N 6 .   ? -12.75364 28.32522  8.13067   1.000 27.02225  ?  344 HOH   D O     1 
HETATM 5728 O  O     . HOH   N 6 .   ? 7.93446   44.08107  0.17802   1.000 33.39721  ?  345 HOH   D O     1 
HETATM 5729 O  O     . HOH   N 6 .   ? 3.80125   39.46772  21.91766  1.000 41.70878  ?  346 HOH   D O     1 
HETATM 5730 O  O     . HOH   N 6 .   ? -12.82580 37.71377  -7.82274  1.000 40.62306  ?  347 HOH   D O     1 
HETATM 5731 O  O     . HOH   N 6 .   ? 4.53742   49.14504  -1.37765  1.000 37.34892  ?  348 HOH   D O     1 
HETATM 5732 O  O     . HOH   N 6 .   ? 4.23879   34.81271  8.13948   1.000 26.86184  ?  349 HOH   D O     1 
HETATM 5733 O  O     . HOH   N 6 .   ? -17.01347 34.50253  7.89448   1.000 26.60295  ?  350 HOH   D O     1 
HETATM 5734 O  O     . HOH   N 6 .   ? -13.14777 29.11140  -0.63642  1.000 40.64708  ?  351 HOH   D O     1 
HETATM 5735 O  O     . HOH   N 6 .   ? 4.10525   28.68493  2.96086   1.000 37.08365  ?  352 HOH   D O     1 
HETATM 5736 O  O     . HOH   N 6 .   ? -18.96266 52.21633  4.68664   1.000 45.81213  ?  353 HOH   D O     1 
HETATM 5737 O  O     . HOH   N 6 .   ? -20.43828 34.51044  14.72714  1.000 26.69018  ?  354 HOH   D O     1 
HETATM 5738 O  O     . HOH   N 6 .   ? -25.682   48.043    20.855    1.000 38.25083  ?  355 HOH   D O     1 
HETATM 5739 O  O     . HOH   N 6 .   ? 3.82357   37.43347  6.33303   1.000 25.15595  ?  356 HOH   D O     1 
HETATM 5740 O  O     . HOH   N 6 .   ? -2.44740  37.11748  24.61651  1.000 35.75313  ?  357 HOH   D O     1 
HETATM 5741 O  O     . HOH   N 6 .   ? -17.53471 45.74020  2.39190   1.000 33.11768  ?  358 HOH   D O     1 
HETATM 5742 O  O     . HOH   N 6 .   ? -0.69638  37.21882  -0.06379  1.000 23.96664  ?  359 HOH   D O     1 
HETATM 5743 O  O     . HOH   N 6 .   ? 1.11307   29.46948  2.50581   1.000 29.22072  ?  360 HOH   D O     1 
HETATM 5744 O  O     . HOH   N 6 .   ? 1.29852   42.72589  19.63020  1.000 35.29163  ?  361 HOH   D O     1 
HETATM 5745 O  O     . HOH   N 6 .   ? -20.29071 46.07541  -2.08801  1.000 35.94546  ?  362 HOH   D O     1 
HETATM 5746 O  O     . HOH   N 6 .   ? -3.22849  45.31216  -6.37965  1.000 35.63239  ?  363 HOH   D O     1 
HETATM 5747 O  O     . HOH   N 6 .   ? -22.80563 33.98649  24.53867  1.000 38.29715  ?  364 HOH   D O     1 
HETATM 5748 O  O     . HOH   N 6 .   ? 1.13467   36.29152  23.23803  1.000 37.62850  ?  365 HOH   D O     1 
HETATM 5749 O  O     . HOH   N 6 .   ? -23.07149 31.83718  15.97552  1.000 40.70333  ?  366 HOH   D O     1 
HETATM 5750 O  O     . HOH   N 6 .   ? -1.67788  48.54627  -1.50523  1.000 31.71633  ?  367 HOH   D O     1 
HETATM 5751 O  O     . HOH   N 6 .   ? 4.38926   39.93286  5.16529   1.000 26.61294  ?  368 HOH   D O     1 
HETATM 5752 O  O     . HOH   N 6 .   ? -4.82727  41.95639  23.55064  1.000 38.93477  ?  369 HOH   D O     1 
HETATM 5753 O  O     . HOH   N 6 .   ? -3.83605  49.48162  -0.59569  1.000 40.62863  ?  370 HOH   D O     1 
HETATM 5754 O  O     . HOH   N 6 .   ? -12.48212 42.61918  -8.37141  1.000 43.41719  ?  371 HOH   D O     1 
HETATM 5755 O  O     . HOH   N 6 .   ? -19.99383 35.25143  7.17880   1.000 33.36723  ?  372 HOH   D O     1 
HETATM 5756 O  O     . HOH   N 6 .   ? -8.66317  52.00718  20.91773  1.000 39.53401  ?  373 HOH   D O     1 
HETATM 5757 O  O     . HOH   N 6 .   ? -19.29578 50.67490  16.13737  1.000 38.21981  ?  374 HOH   D O     1 
HETATM 5758 O  O     . HOH   N 6 .   ? -25.54720 40.90903  7.77002   1.000 38.92050  ?  375 HOH   D O     1 
HETATM 5759 O  O     . HOH   N 6 .   ? -2.20155  45.93685  17.45143  1.000 36.60878  ?  376 HOH   D O     1 
HETATM 5760 O  O     . HOH   N 6 .   ? -11.13817 33.14010  1.65371   1.000 25.60919  ?  377 HOH   D O     1 
HETATM 5761 O  O     . HOH   N 6 .   ? 7.48299   40.96003  11.96896  1.000 28.99589  ?  378 HOH   D O     1 
HETATM 5762 O  O     . HOH   N 6 .   ? -15.08712 53.52125  2.67350   1.000 28.86590  ?  379 HOH   D O     1 
HETATM 5763 O  O     . HOH   N 6 .   ? -8.22549  31.76501  -8.32497  1.000 26.72794  ?  380 HOH   D O     1 
HETATM 5764 O  O     . HOH   N 6 .   ? -22.07592 39.23147  0.61314   1.000 43.19921  ?  381 HOH   D O     1 
HETATM 5765 O  O     . HOH   N 6 .   ? -14.84214 25.86504  24.97057  1.000 31.38204  ?  382 HOH   D O     1 
HETATM 5766 O  O     . HOH   N 6 .   ? -25.07323 43.45120  11.89558  1.000 37.02275  ?  383 HOH   D O     1 
HETATM 5767 O  O     . HOH   N 6 .   ? -10.82498 31.66403  -2.02116  1.000 39.91328  ?  384 HOH   D O     1 
HETATM 5768 O  O     . HOH   N 6 .   ? 9.44179   32.71723  8.91534   1.000 47.13038  ?  385 HOH   D O     1 
HETATM 5769 O  O     . HOH   N 6 .   ? -8.40632  49.11746  22.73782  1.000 34.41879  ?  386 HOH   D O     1 
HETATM 5770 O  O     . HOH   N 6 .   ? 6.96980   41.32778  -1.90653  1.000 33.27578  ?  387 HOH   D O     1 
HETATM 5771 O  O     . HOH   N 6 .   ? -10.63836 35.42018  26.50185  1.000 29.04199  ?  388 HOH   D O     1 
HETATM 5772 O  O     . HOH   N 6 .   ? -18.40175 48.30376  2.76456   1.000 40.97722  ?  389 HOH   D O     1 
HETATM 5773 O  O     . HOH   N 6 .   ? -6.47697  49.46231  20.48843  1.000 31.48317  ?  390 HOH   D O     1 
HETATM 5774 O  O     . HOH   N 6 .   ? 0.45024   36.88764  16.49983  1.000 25.63105  ?  391 HOH   D O     1 
HETATM 5775 O  O     . HOH   N 6 .   ? -2.98650  27.61861  -5.70028  1.000 35.45005  ?  392 HOH   D O     1 
HETATM 5776 O  O     . HOH   N 6 .   ? -3.28656  22.81917  -0.46019  1.000 38.83916  ?  393 HOH   D O     1 
HETATM 5777 O  O     . HOH   N 6 .   ? -5.52207  51.78569  -4.35943  1.000 59.39590  ?  394 HOH   D O     1 
HETATM 5778 O  O     . HOH   N 6 .   ? -8.31581  28.96068  0.80515   1.000 41.85860  ?  395 HOH   D O     1 
HETATM 5779 O  O     . HOH   N 6 .   ? 2.69860   54.50889  6.61462   1.000 37.54786  ?  396 HOH   D O     1 
HETATM 5780 O  O     . HOH   N 6 .   ? 10.13024  35.38889  18.68538  1.000 42.84784  ?  397 HOH   D O     1 
HETATM 5781 O  O     . HOH   N 6 .   ? -23.14892 44.04194  21.73624  1.000 33.00433  ?  398 HOH   D O     1 
HETATM 5782 O  O     . HOH   N 6 .   ? -17.32463 31.57769  26.81858  1.000 35.62316  ?  399 HOH   D O     1 
HETATM 5783 O  O     . HOH   N 6 .   ? -16.25234 57.07173  9.80797   1.000 48.08111  ?  400 HOH   D O     1 
HETATM 5784 O  O     . HOH   N 6 .   ? -5.85972  54.20039  -0.55593  1.000 33.44713  ?  401 HOH   D O     1 
HETATM 5785 O  O     . HOH   N 6 .   ? -24.28151 26.83904  4.76039   1.000 39.59219  ?  402 HOH   D O     1 
HETATM 5786 O  O     . HOH   N 6 .   ? -14.00282 21.39000  21.88990  1.000 38.81927  ?  403 HOH   D O     1 
HETATM 5787 O  O     . HOH   N 6 .   ? -20.64998 40.85973  -0.55153  1.000 34.12617  ?  404 HOH   D O     1 
HETATM 5788 O  O     . HOH   N 6 .   ? -3.69226  26.41898  6.41459   1.000 31.84196  ?  405 HOH   D O     1 
HETATM 5789 O  O     . HOH   N 6 .   ? -15.79791 23.76404  21.65042  1.000 40.98159  ?  406 HOH   D O     1 
HETATM 5790 O  O     . HOH   N 6 .   ? -6.84133  46.54841  24.75925  1.000 50.76230  ?  407 HOH   D O     1 
HETATM 5791 O  O     . HOH   N 6 .   ? -20.18379 49.67098  1.38614   1.000 49.91947  ?  408 HOH   D O     1 
HETATM 5792 O  O     . HOH   N 6 .   ? -19.90076 44.79951  0.40970   1.000 34.41719  ?  409 HOH   D O     1 
HETATM 5793 O  O     . HOH   N 6 .   ? -14.93039 57.04020  7.43730   1.000 46.65100  ?  410 HOH   D O     1 
HETATM 5794 O  O     . HOH   N 6 .   ? 6.61917   47.04527  -1.86298  1.000 44.86664  ?  411 HOH   D O     1 
HETATM 5795 O  O     . HOH   N 6 .   ? -9.42734  52.00737  23.55733  1.000 40.48052  ?  412 HOH   D O     1 
HETATM 5796 O  O     . HOH   N 6 .   ? -13.88185 41.94563  27.13561  1.000 33.81800  ?  413 HOH   D O     1 
HETATM 5797 O  O     . HOH   N 6 .   ? -13.94677 35.36408  -8.56771  1.000 44.31763  ?  414 HOH   D O     1 
HETATM 5798 O  O     . HOH   N 6 .   ? -9.97338  31.04299  0.36633   1.000 36.95611  ?  415 HOH   D O     1 
HETATM 5799 O  O     . HOH   N 6 .   ? -19.20197 25.86184  22.44982  1.000 45.58821  ?  416 HOH   D O     1 
HETATM 5800 O  O     . HOH   N 6 .   ? 9.17875   30.72834  7.93365   1.000 47.83111  ?  417 HOH   D O     1 
HETATM 5801 O  O     . HOH   N 6 .   ? -22.27331 27.75258  21.13847  1.000 42.76361  ?  418 HOH   D O     1 
HETATM 5802 O  O     . HOH   N 6 .   ? 11.80106  32.74996  7.25304   1.000 39.22698  ?  419 HOH   D O     1 
HETATM 5803 O  O     . HOH   N 6 .   ? -4.46405  46.10788  23.94547  1.000 46.17705  ?  420 HOH   D O     1 
HETATM 5804 O  O     . HOH   N 6 .   ? -20.59415 31.55727  10.29239  1.000 36.24947  ?  421 HOH   D O     1 
HETATM 5805 O  O     . HOH   N 6 .   ? 12.786    37.636    7.229     1.000 37.75162  ?  422 HOH   D O     1 
HETATM 5806 O  O     . HOH   N 6 .   ? -4.04989  52.29449  -0.85918  1.000 36.56823  ?  423 HOH   D O     1 
HETATM 5807 O  O     . HOH   N 6 .   ? -20.28582 29.87433  25.74692  1.000 33.45816  ?  424 HOH   D O     1 
HETATM 5808 O  O     . HOH   N 6 .   ? 8.49227   36.04310  16.75125  1.000 46.21234  ?  425 HOH   D O     1 
HETATM 5809 O  O     . HOH   N 6 .   ? 2.23190   44.67977  15.78395  1.000 51.71190  ?  426 HOH   D O     1 
HETATM 5810 O  O     . HOH   N 6 .   ? 4.98827   46.89607  11.50380  1.000 47.78462  ?  427 HOH   D O     1 
HETATM 5811 O  O     . HOH   N 6 .   ? -17.94657 21.21197  20.89710  1.000 49.50154  ?  428 HOH   D O     1 
HETATM 5812 O  O     . HOH   N 6 .   ? 5.46752   47.39375  8.75436   1.000 50.22795  ?  429 HOH   D O     1 
HETATM 5813 O  O     . HOH   N 6 .   ? 4.21750   24.78552  17.35337  1.000 38.78723  ?  430 HOH   D O     1 
HETATM 5814 O  O     . HOH   N 6 .   ? -25.18446 43.05818  9.28104   1.000 40.91635  ?  431 HOH   D O     1 
HETATM 5815 O  O     . HOH   N 6 .   ? 0.19870   50.11954  -2.88767  1.000 48.14785  ?  432 HOH   D O     1 
HETATM 5816 O  O     . HOH   N 6 .   ? 3.22055   49.79944  -3.78830  1.000 49.41918  ?  433 HOH   D O     1 
HETATM 5817 O  O     . HOH   N 6 .   ? 4.59206   37.49064  23.48252  1.000 44.78082  ?  434 HOH   D O     1 
HETATM 5818 O  O     . HOH   N 6 .   ? 9.29787   40.19418  13.60779  1.000 43.55263  ?  435 HOH   D O     1 
HETATM 5819 O  O     . HOH   N 6 .   ? -15.35128 59.43988  10.60230  1.000 51.01824  ?  436 HOH   D O     1 
HETATM 5820 O  O     . HOH   N 6 .   ? -23.86385 28.06419  22.93465  1.000 45.83172  ?  437 HOH   D O     1 
HETATM 5821 O  O     . HOH   N 6 .   ? -23.31355 48.86637  14.25685  1.000 36.18446  ?  438 HOH   D O     1 
HETATM 5822 O  O     . HOH   N 6 .   ? 9.10205   37.75938  15.34222  1.000 41.77570  ?  439 HOH   D O     1 
HETATM 5823 O  O     . HOH   N 6 .   ? -6.85882  53.23933  24.45844  1.000 43.93582  ?  440 HOH   D O     1 
# 
